data_9FD8
# 
_entry.id   9FD8 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   9FD8         pdb_00009fd8 10.2210/pdb9fd8/pdb 
WWPDB D_1292137772 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FD8 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              g.j.poelarends@rug.nl 
_pdbx_contact_author.name_first         Gerrit 
_pdbx_contact_author.name_last          Poelarends 
_pdbx_contact_author.name_mi            J. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6917-6368 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Thunnissen, A.M.W.H.' 1 0000-0002-1915-9850 
'Zhou, H.'             2 ?                   
'Frietema, H.O.T.'     3 ?                   
'Poelarends, G.J.'     4 0000-0002-6917-6368 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Angew.Chem.Int.Ed.Engl. 
_citation.journal_id_ASTM           ACIEAY 
_citation.journal_id_CSD            0179 
_citation.journal_id_ISSN           1521-3773 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            64 
_citation.language                  ? 
_citation.page_first                e202503054 
_citation.page_last                 e202503054 
_citation.title                     
'Engineering 2-Deoxy-D-ribose-5-phosphate Aldolase for anti- and syn-Selective Epoxidations of alpha , beta-Unsaturated Aldehydes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202503054 
_citation.pdbx_database_id_PubMed   39993220 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhou, H.'           1 ?                   
primary 'Kunzendorf, A.'     2 ?                   
primary 'Xu, G.'             3 ?                   
primary 'Frietema, H.O.T.'   4 ?                   
primary 'Thunnissen, A.W.H.' 5 ?                   
primary 'Poelarends, G.J.'   6 0000-0002-6917-6368 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Deoxyribose-phosphate aldolase'     28715.734 2   4.1.2.4 
'T18S, L20S, D22G, D24Y, C47S, I48V, F52S, K172R, T197S, P202V, A203T, R207S, G236S, S239G' ? ? 
2 non-polymer syn '(2E)-3-(4-chlorophenyl)prop-2-enal' 168.620   2   ?       ? ? ? 
3 non-polymer syn GLYCEROL                             92.094    1   ?       ? ? ? 
4 water       nat water                                18.015    238 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'DERA,2-deoxy-D-ribose 5-phosphate aldolase,Phosphodeoxyriboaldolase,Deoxyriboaldolase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MTDLKASSLRALKLMDLSTLNGDYTDEKVIALCHQAKTPVGNTAAISVYPRSIPIARKTLKEQGTPEIRIATVTNFPHGN
DDIEIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIK
AGADFIKTSTGRVAVNATPESARIMMEVIRDMGVEKSVGFKVTGGVSTAEDAQKYLAIADELFGADWADARHYRFSASGL
LASLLKALGHGDGKSASSYLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTDLKASSLRALKLMDLSTLNGDYTDEKVIALCHQAKTPVGNTAAISVYPRSIPIARKTLKEQGTPEIRIATVTNFPHGN
DDIEIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIK
AGADFIKTSTGRVAVNATPESARIMMEVIRDMGVEKSVGFKVTGGVSTAEDAQKYLAIADELFGADWADARHYRFSASGL
LASLLKALGHGDGKSASSYLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '(2E)-3-(4-chlorophenyl)prop-2-enal' A1ICA 
3 GLYCEROL                             GOL   
4 water                                HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   MET n 
1 2   THR n 
1 3   ASP n 
1 4   LEU n 
1 5   LYS n 
1 6   ALA n 
1 7   SER n 
1 8   SER n 
1 9   LEU n 
1 10  ARG n 
1 11  ALA n 
1 12  LEU n 
1 13  LYS n 
1 14  LEU n 
1 15  MET n 
1 16  ASP n 
1 17  LEU n 
1 18  SER n 
1 19  THR n 
1 20  LEU n 
1 21  ASN n 
1 22  GLY n 
1 23  ASP n 
1 24  TYR n 
1 25  THR n 
1 26  ASP n 
1 27  GLU n 
1 28  LYS n 
1 29  VAL n 
1 30  ILE n 
1 31  ALA n 
1 32  LEU n 
1 33  CYS n 
1 34  HIS n 
1 35  GLN n 
1 36  ALA n 
1 37  LYS n 
1 38  THR n 
1 39  PRO n 
1 40  VAL n 
1 41  GLY n 
1 42  ASN n 
1 43  THR n 
1 44  ALA n 
1 45  ALA n 
1 46  ILE n 
1 47  SER n 
1 48  VAL n 
1 49  TYR n 
1 50  PRO n 
1 51  ARG n 
1 52  SER n 
1 53  ILE n 
1 54  PRO n 
1 55  ILE n 
1 56  ALA n 
1 57  ARG n 
1 58  LYS n 
1 59  THR n 
1 60  LEU n 
1 61  LYS n 
1 62  GLU n 
1 63  GLN n 
1 64  GLY n 
1 65  THR n 
1 66  PRO n 
1 67  GLU n 
1 68  ILE n 
1 69  ARG n 
1 70  ILE n 
1 71  ALA n 
1 72  THR n 
1 73  VAL n 
1 74  THR n 
1 75  ASN n 
1 76  PHE n 
1 77  PRO n 
1 78  HIS n 
1 79  GLY n 
1 80  ASN n 
1 81  ASP n 
1 82  ASP n 
1 83  ILE n 
1 84  GLU n 
1 85  ILE n 
1 86  ALA n 
1 87  LEU n 
1 88  ALA n 
1 89  GLU n 
1 90  THR n 
1 91  ARG n 
1 92  ALA n 
1 93  ALA n 
1 94  ILE n 
1 95  ALA n 
1 96  TYR n 
1 97  GLY n 
1 98  ALA n 
1 99  ASP n 
1 100 GLU n 
1 101 VAL n 
1 102 ASP n 
1 103 VAL n 
1 104 VAL n 
1 105 PHE n 
1 106 PRO n 
1 107 TYR n 
1 108 ARG n 
1 109 ALA n 
1 110 LEU n 
1 111 MET n 
1 112 ALA n 
1 113 GLY n 
1 114 ASN n 
1 115 GLU n 
1 116 GLN n 
1 117 VAL n 
1 118 GLY n 
1 119 PHE n 
1 120 ASP n 
1 121 LEU n 
1 122 VAL n 
1 123 LYS n 
1 124 ALA n 
1 125 CYS n 
1 126 LYS n 
1 127 GLU n 
1 128 ALA n 
1 129 CYS n 
1 130 ALA n 
1 131 ALA n 
1 132 ALA n 
1 133 ASN n 
1 134 VAL n 
1 135 LEU n 
1 136 LEU n 
1 137 LYS n 
1 138 VAL n 
1 139 ILE n 
1 140 ILE n 
1 141 GLU n 
1 142 THR n 
1 143 GLY n 
1 144 GLU n 
1 145 LEU n 
1 146 LYS n 
1 147 ASP n 
1 148 GLU n 
1 149 ALA n 
1 150 LEU n 
1 151 ILE n 
1 152 ARG n 
1 153 LYS n 
1 154 ALA n 
1 155 SER n 
1 156 GLU n 
1 157 ILE n 
1 158 SER n 
1 159 ILE n 
1 160 LYS n 
1 161 ALA n 
1 162 GLY n 
1 163 ALA n 
1 164 ASP n 
1 165 PHE n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 SER n 
1 170 THR n 
1 171 GLY n 
1 172 ARG n 
1 173 VAL n 
1 174 ALA n 
1 175 VAL n 
1 176 ASN n 
1 177 ALA n 
1 178 THR n 
1 179 PRO n 
1 180 GLU n 
1 181 SER n 
1 182 ALA n 
1 183 ARG n 
1 184 ILE n 
1 185 MET n 
1 186 MET n 
1 187 GLU n 
1 188 VAL n 
1 189 ILE n 
1 190 ARG n 
1 191 ASP n 
1 192 MET n 
1 193 GLY n 
1 194 VAL n 
1 195 GLU n 
1 196 LYS n 
1 197 SER n 
1 198 VAL n 
1 199 GLY n 
1 200 PHE n 
1 201 LYS n 
1 202 VAL n 
1 203 THR n 
1 204 GLY n 
1 205 GLY n 
1 206 VAL n 
1 207 SER n 
1 208 THR n 
1 209 ALA n 
1 210 GLU n 
1 211 ASP n 
1 212 ALA n 
1 213 GLN n 
1 214 LYS n 
1 215 TYR n 
1 216 LEU n 
1 217 ALA n 
1 218 ILE n 
1 219 ALA n 
1 220 ASP n 
1 221 GLU n 
1 222 LEU n 
1 223 PHE n 
1 224 GLY n 
1 225 ALA n 
1 226 ASP n 
1 227 TRP n 
1 228 ALA n 
1 229 ASP n 
1 230 ALA n 
1 231 ARG n 
1 232 HIS n 
1 233 TYR n 
1 234 ARG n 
1 235 PHE n 
1 236 SER n 
1 237 ALA n 
1 238 SER n 
1 239 GLY n 
1 240 LEU n 
1 241 LEU n 
1 242 ALA n 
1 243 SER n 
1 244 LEU n 
1 245 LEU n 
1 246 LYS n 
1 247 ALA n 
1 248 LEU n 
1 249 GLY n 
1 250 HIS n 
1 251 GLY n 
1 252 ASP n 
1 253 GLY n 
1 254 LYS n 
1 255 SER n 
1 256 ALA n 
1 257 SER n 
1 258 SER n 
1 259 TYR n 
1 260 LEU n 
1 261 GLU n 
1 262 HIS n 
1 263 HIS n 
1 264 HIS n 
1 265 HIS n 
1 266 HIS n 
1 267 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   267 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'deoC, EcolC_3675' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ICA non-polymer         . '(2E)-3-(4-chlorophenyl)prop-2-enal' '(~{E})-3-(4-chlorophenyl)prop-2-en-1-ol' 'C9 H9 Cl O'     
168.620 
ALA   'L-peptide linking' y ALANINE                              ?                                         'C3 H7 N O2'     89.093 
ARG   'L-peptide linking' y ARGININE                             ?                                         'C6 H15 N4 O2 1' 
175.209 
ASN   'L-peptide linking' y ASPARAGINE                           ?                                         'C4 H8 N2 O3'    
132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID'                      ?                                         'C4 H7 N O4'     
133.103 
CYS   'L-peptide linking' y CYSTEINE                             ?                                         'C3 H7 N O2 S'   
121.158 
GLN   'L-peptide linking' y GLUTAMINE                            ?                                         'C5 H10 N2 O3'   
146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID'                      ?                                         'C5 H9 N O4'     
147.129 
GLY   'peptide linking'   y GLYCINE                              ?                                         'C2 H5 N O2'     75.067 
GOL   non-polymer         . GLYCEROL                             'GLYCERIN; PROPANE-1,2,3-TRIOL'           'C3 H8 O3'       92.094 
HIS   'L-peptide linking' y HISTIDINE                            ?                                         'C6 H10 N3 O2 1' 
156.162 
HOH   non-polymer         . WATER                                ?                                         'H2 O'           18.015 
ILE   'L-peptide linking' y ISOLEUCINE                           ?                                         'C6 H13 N O2'    
131.173 
LEU   'L-peptide linking' y LEUCINE                              ?                                         'C6 H13 N O2'    
131.173 
LYS   'L-peptide linking' y LYSINE                               ?                                         'C6 H15 N2 O2 1' 
147.195 
MET   'L-peptide linking' y METHIONINE                           ?                                         'C5 H11 N O2 S'  
149.211 
PHE   'L-peptide linking' y PHENYLALANINE                        ?                                         'C9 H11 N O2'    
165.189 
PRO   'L-peptide linking' y PROLINE                              ?                                         'C5 H9 N O2'     
115.130 
SER   'L-peptide linking' y SERINE                               ?                                         'C3 H7 N O3'     
105.093 
THR   'L-peptide linking' y THREONINE                            ?                                         'C4 H9 N O3'     
119.119 
TRP   'L-peptide linking' y TRYPTOPHAN                           ?                                         'C11 H12 N2 O2'  
204.225 
TYR   'L-peptide linking' y TYROSINE                             ?                                         'C9 H11 N O3'    
181.189 
VAL   'L-peptide linking' y VALINE                               ?                                         'C5 H11 N O2'    
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   ASP 3   3   ?   ?   ?   A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  MET 15  15  15  MET MET A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  THR 19  19  19  THR THR A . n 
A 1 20  LEU 20  20  ?   ?   ?   A . n 
A 1 21  ASN 21  21  ?   ?   ?   A . n 
A 1 22  GLY 22  22  ?   ?   ?   A . n 
A 1 23  ASP 23  23  ?   ?   ?   A . n 
A 1 24  TYR 24  24  ?   ?   ?   A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  CYS 33  33  33  CYS CYS A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  THR 38  38  38  THR THR A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  ASN 42  42  42  ASN ASN A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  PRO 50  50  50  PRO PRO A . n 
A 1 51  ARG 51  51  51  ARG ARG A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  ARG 57  57  57  ARG ARG A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  PRO 77  77  77  PRO PRO A A n 
A 1 78  HIS 78  78  78  HIS HIS A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  ASN 80  80  80  ASN ASN A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 PHE 105 105 105 PHE PHE A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 MET 111 111 111 MET MET A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 CYS 125 125 125 CYS CYS A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 CYS 129 129 129 CYS CYS A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 MET 186 186 186 MET MET A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 MET 192 192 192 MET MET A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 GLN 213 213 213 GLN GLN A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 TYR 215 215 215 TYR TYR A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 TRP 227 227 227 TRP TRP A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 HIS 232 232 232 HIS HIS A . n 
A 1 233 TYR 233 233 233 TYR TYR A . n 
A 1 234 ARG 234 234 234 ARG ARG A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 LYS 246 246 246 LYS LYS A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 GLY 249 249 249 GLY GLY A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 GLY 251 251 ?   ?   ?   A . n 
A 1 252 ASP 252 252 ?   ?   ?   A . n 
A 1 253 GLY 253 253 ?   ?   ?   A . n 
A 1 254 LYS 254 254 ?   ?   ?   A . n 
A 1 255 SER 255 255 ?   ?   ?   A . n 
A 1 256 ALA 256 256 ?   ?   ?   A . n 
A 1 257 SER 257 257 ?   ?   ?   A . n 
A 1 258 SER 258 258 ?   ?   ?   A . n 
A 1 259 TYR 259 259 ?   ?   ?   A . n 
A 1 260 LEU 260 260 ?   ?   ?   A . n 
A 1 261 GLU 261 261 ?   ?   ?   A . n 
A 1 262 HIS 262 262 ?   ?   ?   A . n 
A 1 263 HIS 263 263 ?   ?   ?   A . n 
A 1 264 HIS 264 264 ?   ?   ?   A . n 
A 1 265 HIS 265 265 ?   ?   ?   A . n 
A 1 266 HIS 266 266 ?   ?   ?   A . n 
A 1 267 HIS 267 267 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   ASP 3   3   3   ASP ASP B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  LYS 13  13  13  LYS LYS B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  MET 15  15  15  MET MET B . n 
B 1 16  ASP 16  16  16  ASP ASP B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  SER 18  18  18  SER SER B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  LEU 20  20  ?   ?   ?   B . n 
B 1 21  ASN 21  21  ?   ?   ?   B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  ASP 23  23  23  ASP ASP B . n 
B 1 24  TYR 24  24  24  TYR TYR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  ASP 26  26  26  ASP ASP B . n 
B 1 27  GLU 27  27  27  GLU GLU B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ALA 31  31  31  ALA ALA B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  CYS 33  33  33  CYS CYS B . n 
B 1 34  HIS 34  34  34  HIS HIS B . n 
B 1 35  GLN 35  35  35  GLN GLN B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  LYS 37  37  37  LYS LYS B . n 
B 1 38  THR 38  38  38  THR THR B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  VAL 40  40  40  VAL VAL B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  ASN 42  42  42  ASN ASN B . n 
B 1 43  THR 43  43  43  THR THR B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  TYR 49  49  49  TYR TYR B . n 
B 1 50  PRO 50  50  50  PRO PRO B . n 
B 1 51  ARG 51  51  51  ARG ARG B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  PRO 54  54  54  PRO PRO B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  ARG 57  57  57  ARG ARG B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  THR 59  59  59  THR THR B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  GLN 63  63  63  GLN GLN B . n 
B 1 64  GLY 64  64  64  GLY GLY B . n 
B 1 65  THR 65  65  65  THR THR B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  ILE 68  68  68  ILE ILE B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  ILE 70  70  70  ILE ILE B . n 
B 1 71  ALA 71  71  71  ALA ALA B . n 
B 1 72  THR 72  72  72  THR THR B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  THR 74  74  74  THR THR B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  PRO 77  77  77  PRO PRO B . n 
B 1 78  HIS 78  78  78  HIS HIS B . n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  ASN 80  80  80  ASN ASN B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  ILE 85  85  85  ILE ILE B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  ALA 88  88  88  ALA ALA B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  TYR 96  96  96  TYR TYR B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  ALA 98  98  98  ALA ALA B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 VAL 101 101 101 VAL VAL B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 PHE 105 105 105 PHE PHE B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 TYR 107 107 107 TYR TYR B . n 
B 1 108 ARG 108 108 108 ARG ARG B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 MET 111 111 111 MET MET B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 GLY 113 113 113 GLY GLY B . n 
B 1 114 ASN 114 114 114 ASN ASN B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 GLN 116 116 116 GLN GLN B . n 
B 1 117 VAL 117 117 117 VAL VAL B . n 
B 1 118 GLY 118 118 118 GLY GLY B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 LEU 121 121 121 LEU LEU B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 LYS 123 123 123 LYS LYS B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 CYS 125 125 125 CYS CYS B . n 
B 1 126 LYS 126 126 126 LYS LYS B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 ALA 128 128 128 ALA ALA B . n 
B 1 129 CYS 129 129 129 CYS CYS B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 VAL 138 138 138 VAL VAL B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 ILE 140 140 140 ILE ILE B . n 
B 1 141 GLU 141 141 141 GLU GLU B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 GLU 144 144 144 GLU GLU B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 LYS 146 146 146 LYS LYS B . n 
B 1 147 ASP 147 147 147 ASP ASP B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 ALA 149 149 149 ALA ALA B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ARG 152 152 152 ARG ARG B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 GLU 156 156 156 GLU GLU B . n 
B 1 157 ILE 157 157 157 ILE ILE B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 ILE 159 159 159 ILE ILE B . n 
B 1 160 LYS 160 160 160 LYS LYS B . n 
B 1 161 ALA 161 161 161 ALA ALA B . n 
B 1 162 GLY 162 162 162 GLY GLY B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 PHE 165 165 165 PHE PHE B . n 
B 1 166 ILE 166 166 166 ILE ILE B . n 
B 1 167 LYS 167 167 167 LYS LYS B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 THR 170 170 170 THR THR B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 ARG 172 172 172 ARG ARG B . n 
B 1 173 VAL 173 173 173 VAL VAL B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 VAL 175 175 175 VAL VAL B . n 
B 1 176 ASN 176 176 176 ASN ASN B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 THR 178 178 178 THR THR B . n 
B 1 179 PRO 179 179 179 PRO PRO B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 SER 181 181 181 SER SER B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 ARG 183 183 183 ARG ARG B . n 
B 1 184 ILE 184 184 184 ILE ILE B . n 
B 1 185 MET 185 185 185 MET MET B . n 
B 1 186 MET 186 186 186 MET MET B . n 
B 1 187 GLU 187 187 187 GLU GLU B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 ILE 189 189 189 ILE ILE B . n 
B 1 190 ARG 190 190 190 ARG ARG B . n 
B 1 191 ASP 191 191 191 ASP ASP B . n 
B 1 192 MET 192 192 192 MET MET B . n 
B 1 193 GLY 193 193 193 GLY GLY B . n 
B 1 194 VAL 194 194 194 VAL VAL B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 LYS 196 196 196 LYS LYS B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 VAL 198 198 198 VAL VAL B . n 
B 1 199 GLY 199 199 199 GLY GLY B . n 
B 1 200 PHE 200 200 200 PHE PHE B . n 
B 1 201 LYS 201 201 201 LYS LYS B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 THR 203 203 203 THR THR B . n 
B 1 204 GLY 204 204 204 GLY GLY B . n 
B 1 205 GLY 205 205 205 GLY GLY B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 SER 207 207 207 SER SER B . n 
B 1 208 THR 208 208 208 THR THR B . n 
B 1 209 ALA 209 209 209 ALA ALA B . n 
B 1 210 GLU 210 210 210 GLU GLU B . n 
B 1 211 ASP 211 211 211 ASP ASP B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 GLN 213 213 213 GLN GLN B . n 
B 1 214 LYS 214 214 214 LYS LYS B . n 
B 1 215 TYR 215 215 215 TYR TYR B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 ALA 217 217 217 ALA ALA B . n 
B 1 218 ILE 218 218 218 ILE ILE B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 GLU 221 221 221 GLU GLU B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 ASP 226 226 226 ASP ASP B . n 
B 1 227 TRP 227 227 227 TRP TRP B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 ARG 231 231 231 ARG ARG B . n 
B 1 232 HIS 232 232 232 HIS HIS B . n 
B 1 233 TYR 233 233 233 TYR TYR B . n 
B 1 234 ARG 234 234 234 ARG ARG B . n 
B 1 235 PHE 235 235 235 PHE PHE B . n 
B 1 236 SER 236 236 236 SER SER B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 GLY 239 239 239 GLY GLY B . n 
B 1 240 LEU 240 240 240 LEU LEU B . n 
B 1 241 LEU 241 241 241 LEU LEU B . n 
B 1 242 ALA 242 242 242 ALA ALA B . n 
B 1 243 SER 243 243 243 SER SER B . n 
B 1 244 LEU 244 244 244 LEU LEU B . n 
B 1 245 LEU 245 245 245 LEU LEU B . n 
B 1 246 LYS 246 246 246 LYS LYS B . n 
B 1 247 ALA 247 247 247 ALA ALA B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 GLY 249 249 249 GLY GLY B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 GLY 251 251 ?   ?   ?   B . n 
B 1 252 ASP 252 252 ?   ?   ?   B . n 
B 1 253 GLY 253 253 ?   ?   ?   B . n 
B 1 254 LYS 254 254 ?   ?   ?   B . n 
B 1 255 SER 255 255 ?   ?   ?   B . n 
B 1 256 ALA 256 256 ?   ?   ?   B . n 
B 1 257 SER 257 257 ?   ?   ?   B . n 
B 1 258 SER 258 258 ?   ?   ?   B . n 
B 1 259 TYR 259 259 ?   ?   ?   B . n 
B 1 260 LEU 260 260 ?   ?   ?   B . n 
B 1 261 GLU 261 261 ?   ?   ?   B . n 
B 1 262 HIS 262 262 ?   ?   ?   B . n 
B 1 263 HIS 263 263 ?   ?   ?   B . n 
B 1 264 HIS 264 264 ?   ?   ?   B . n 
B 1 265 HIS 265 265 ?   ?   ?   B . n 
B 1 266 HIS 266 266 ?   ?   ?   B . n 
B 1 267 HIS 267 267 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ICA 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ICA 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1ICA 1   301 301 A1ICA PCC A . 
D 2 A1ICA 1   301 301 A1ICA PCC B . 
E 3 GOL   1   302 302 GOL   GOL B . 
F 4 HOH   1   401 178 HOH   HOH A . 
F 4 HOH   2   402 145 HOH   HOH A . 
F 4 HOH   3   403 218 HOH   HOH A . 
F 4 HOH   4   404 96  HOH   HOH A . 
F 4 HOH   5   405 86  HOH   HOH A . 
F 4 HOH   6   406 71  HOH   HOH A . 
F 4 HOH   7   407 149 HOH   HOH A . 
F 4 HOH   8   408 228 HOH   HOH A . 
F 4 HOH   9   409 223 HOH   HOH A . 
F 4 HOH   10  410 99  HOH   HOH A . 
F 4 HOH   11  411 72  HOH   HOH A . 
F 4 HOH   12  412 221 HOH   HOH A . 
F 4 HOH   13  413 75  HOH   HOH A . 
F 4 HOH   14  414 23  HOH   HOH A . 
F 4 HOH   15  415 133 HOH   HOH A . 
F 4 HOH   16  416 229 HOH   HOH A . 
F 4 HOH   17  417 100 HOH   HOH A . 
F 4 HOH   18  418 14  HOH   HOH A . 
F 4 HOH   19  419 88  HOH   HOH A . 
F 4 HOH   20  420 9   HOH   HOH A . 
F 4 HOH   21  421 42  HOH   HOH A . 
F 4 HOH   22  422 109 HOH   HOH A . 
F 4 HOH   23  423 168 HOH   HOH A . 
F 4 HOH   24  424 37  HOH   HOH A . 
F 4 HOH   25  425 152 HOH   HOH A . 
F 4 HOH   26  426 236 HOH   HOH A . 
F 4 HOH   27  427 150 HOH   HOH A . 
F 4 HOH   28  428 89  HOH   HOH A . 
F 4 HOH   29  429 230 HOH   HOH A . 
F 4 HOH   30  430 3   HOH   HOH A . 
F 4 HOH   31  431 18  HOH   HOH A . 
F 4 HOH   32  432 64  HOH   HOH A . 
F 4 HOH   33  433 194 HOH   HOH A . 
F 4 HOH   34  434 30  HOH   HOH A . 
F 4 HOH   35  435 39  HOH   HOH A . 
F 4 HOH   36  436 173 HOH   HOH A . 
F 4 HOH   37  437 122 HOH   HOH A . 
F 4 HOH   38  438 217 HOH   HOH A . 
F 4 HOH   39  439 54  HOH   HOH A . 
F 4 HOH   40  440 56  HOH   HOH A . 
F 4 HOH   41  441 15  HOH   HOH A . 
F 4 HOH   42  442 76  HOH   HOH A . 
F 4 HOH   43  443 44  HOH   HOH A . 
F 4 HOH   44  444 47  HOH   HOH A . 
F 4 HOH   45  445 144 HOH   HOH A . 
F 4 HOH   46  446 224 HOH   HOH A . 
F 4 HOH   47  447 119 HOH   HOH A . 
F 4 HOH   48  448 41  HOH   HOH A . 
F 4 HOH   49  449 11  HOH   HOH A . 
F 4 HOH   50  450 188 HOH   HOH A . 
F 4 HOH   51  451 177 HOH   HOH A . 
F 4 HOH   52  452 22  HOH   HOH A . 
F 4 HOH   53  453 137 HOH   HOH A . 
F 4 HOH   54  454 162 HOH   HOH A . 
F 4 HOH   55  455 60  HOH   HOH A . 
F 4 HOH   56  456 104 HOH   HOH A . 
F 4 HOH   57  457 97  HOH   HOH A . 
F 4 HOH   58  458 155 HOH   HOH A . 
F 4 HOH   59  459 50  HOH   HOH A . 
F 4 HOH   60  460 180 HOH   HOH A . 
F 4 HOH   61  461 215 HOH   HOH A . 
F 4 HOH   62  462 159 HOH   HOH A . 
F 4 HOH   63  463 238 HOH   HOH A . 
F 4 HOH   64  464 16  HOH   HOH A . 
F 4 HOH   65  465 8   HOH   HOH A . 
F 4 HOH   66  466 110 HOH   HOH A . 
F 4 HOH   67  467 210 HOH   HOH A . 
F 4 HOH   68  468 165 HOH   HOH A . 
F 4 HOH   69  469 185 HOH   HOH A . 
F 4 HOH   70  470 186 HOH   HOH A . 
F 4 HOH   71  471 57  HOH   HOH A . 
F 4 HOH   72  472 19  HOH   HOH A . 
F 4 HOH   73  473 68  HOH   HOH A . 
F 4 HOH   74  474 220 HOH   HOH A . 
F 4 HOH   75  475 29  HOH   HOH A . 
F 4 HOH   76  476 164 HOH   HOH A . 
F 4 HOH   77  477 34  HOH   HOH A . 
F 4 HOH   78  478 32  HOH   HOH A . 
F 4 HOH   79  479 33  HOH   HOH A . 
F 4 HOH   80  480 231 HOH   HOH A . 
F 4 HOH   81  481 235 HOH   HOH A . 
F 4 HOH   82  482 38  HOH   HOH A . 
F 4 HOH   83  483 187 HOH   HOH A . 
F 4 HOH   84  484 12  HOH   HOH A . 
F 4 HOH   85  485 141 HOH   HOH A . 
F 4 HOH   86  486 107 HOH   HOH A . 
F 4 HOH   87  487 106 HOH   HOH A . 
F 4 HOH   88  488 184 HOH   HOH A . 
F 4 HOH   89  489 125 HOH   HOH A . 
F 4 HOH   90  490 85  HOH   HOH A . 
F 4 HOH   91  491 43  HOH   HOH A . 
F 4 HOH   92  492 157 HOH   HOH A . 
F 4 HOH   93  493 55  HOH   HOH A . 
F 4 HOH   94  494 69  HOH   HOH A . 
F 4 HOH   95  495 93  HOH   HOH A . 
F 4 HOH   96  496 176 HOH   HOH A . 
F 4 HOH   97  497 169 HOH   HOH A . 
F 4 HOH   98  498 115 HOH   HOH A . 
F 4 HOH   99  499 219 HOH   HOH A . 
F 4 HOH   100 500 212 HOH   HOH A . 
F 4 HOH   101 501 183 HOH   HOH A . 
F 4 HOH   102 502 79  HOH   HOH A . 
F 4 HOH   103 503 227 HOH   HOH A . 
F 4 HOH   104 504 127 HOH   HOH A . 
F 4 HOH   105 505 13  HOH   HOH A . 
F 4 HOH   106 506 232 HOH   HOH A . 
F 4 HOH   107 507 21  HOH   HOH A . 
F 4 HOH   108 508 74  HOH   HOH A . 
F 4 HOH   109 509 160 HOH   HOH A . 
F 4 HOH   110 510 108 HOH   HOH A . 
F 4 HOH   111 511 128 HOH   HOH A . 
F 4 HOH   112 512 120 HOH   HOH A . 
F 4 HOH   113 513 182 HOH   HOH A . 
F 4 HOH   114 514 129 HOH   HOH A . 
F 4 HOH   115 515 90  HOH   HOH A . 
F 4 HOH   116 516 226 HOH   HOH A . 
F 4 HOH   117 517 213 HOH   HOH A . 
F 4 HOH   118 518 174 HOH   HOH A . 
F 4 HOH   119 519 166 HOH   HOH A . 
F 4 HOH   120 520 198 HOH   HOH A . 
F 4 HOH   121 521 167 HOH   HOH A . 
F 4 HOH   122 522 135 HOH   HOH A . 
F 4 HOH   123 523 146 HOH   HOH A . 
F 4 HOH   124 524 197 HOH   HOH A . 
F 4 HOH   125 525 234 HOH   HOH A . 
F 4 HOH   126 526 179 HOH   HOH A . 
F 4 HOH   127 527 123 HOH   HOH A . 
G 4 HOH   1   401 151 HOH   HOH B . 
G 4 HOH   2   402 204 HOH   HOH B . 
G 4 HOH   3   403 140 HOH   HOH B . 
G 4 HOH   4   404 83  HOH   HOH B . 
G 4 HOH   5   405 207 HOH   HOH B . 
G 4 HOH   6   406 154 HOH   HOH B . 
G 4 HOH   7   407 28  HOH   HOH B . 
G 4 HOH   8   408 175 HOH   HOH B . 
G 4 HOH   9   409 161 HOH   HOH B . 
G 4 HOH   10  410 17  HOH   HOH B . 
G 4 HOH   11  411 61  HOH   HOH B . 
G 4 HOH   12  412 67  HOH   HOH B . 
G 4 HOH   13  413 111 HOH   HOH B . 
G 4 HOH   14  414 7   HOH   HOH B . 
G 4 HOH   15  415 214 HOH   HOH B . 
G 4 HOH   16  416 48  HOH   HOH B . 
G 4 HOH   17  417 65  HOH   HOH B . 
G 4 HOH   18  418 4   HOH   HOH B . 
G 4 HOH   19  419 112 HOH   HOH B . 
G 4 HOH   20  420 118 HOH   HOH B . 
G 4 HOH   21  421 126 HOH   HOH B . 
G 4 HOH   22  422 58  HOH   HOH B . 
G 4 HOH   23  423 131 HOH   HOH B . 
G 4 HOH   24  424 49  HOH   HOH B . 
G 4 HOH   25  425 84  HOH   HOH B . 
G 4 HOH   26  426 26  HOH   HOH B . 
G 4 HOH   27  427 95  HOH   HOH B . 
G 4 HOH   28  428 202 HOH   HOH B . 
G 4 HOH   29  429 20  HOH   HOH B . 
G 4 HOH   30  430 201 HOH   HOH B . 
G 4 HOH   31  431 200 HOH   HOH B . 
G 4 HOH   32  432 5   HOH   HOH B . 
G 4 HOH   33  433 102 HOH   HOH B . 
G 4 HOH   34  434 192 HOH   HOH B . 
G 4 HOH   35  435 205 HOH   HOH B . 
G 4 HOH   36  436 172 HOH   HOH B . 
G 4 HOH   37  437 103 HOH   HOH B . 
G 4 HOH   38  438 117 HOH   HOH B . 
G 4 HOH   39  439 203 HOH   HOH B . 
G 4 HOH   40  440 24  HOH   HOH B . 
G 4 HOH   41  441 199 HOH   HOH B . 
G 4 HOH   42  442 105 HOH   HOH B . 
G 4 HOH   43  443 91  HOH   HOH B . 
G 4 HOH   44  444 6   HOH   HOH B . 
G 4 HOH   45  445 92  HOH   HOH B . 
G 4 HOH   46  446 1   HOH   HOH B . 
G 4 HOH   47  447 142 HOH   HOH B . 
G 4 HOH   48  448 63  HOH   HOH B . 
G 4 HOH   49  449 53  HOH   HOH B . 
G 4 HOH   50  450 143 HOH   HOH B . 
G 4 HOH   51  451 139 HOH   HOH B . 
G 4 HOH   52  452 132 HOH   HOH B . 
G 4 HOH   53  453 113 HOH   HOH B . 
G 4 HOH   54  454 191 HOH   HOH B . 
G 4 HOH   55  455 31  HOH   HOH B . 
G 4 HOH   56  456 195 HOH   HOH B . 
G 4 HOH   57  457 225 HOH   HOH B . 
G 4 HOH   58  458 121 HOH   HOH B . 
G 4 HOH   59  459 10  HOH   HOH B . 
G 4 HOH   60  460 51  HOH   HOH B . 
G 4 HOH   61  461 208 HOH   HOH B . 
G 4 HOH   62  462 40  HOH   HOH B . 
G 4 HOH   63  463 70  HOH   HOH B . 
G 4 HOH   64  464 130 HOH   HOH B . 
G 4 HOH   65  465 237 HOH   HOH B . 
G 4 HOH   66  466 62  HOH   HOH B . 
G 4 HOH   67  467 25  HOH   HOH B . 
G 4 HOH   68  468 46  HOH   HOH B . 
G 4 HOH   69  469 211 HOH   HOH B . 
G 4 HOH   70  470 27  HOH   HOH B . 
G 4 HOH   71  471 82  HOH   HOH B . 
G 4 HOH   72  472 209 HOH   HOH B . 
G 4 HOH   73  473 52  HOH   HOH B . 
G 4 HOH   74  474 77  HOH   HOH B . 
G 4 HOH   75  475 2   HOH   HOH B . 
G 4 HOH   76  476 78  HOH   HOH B . 
G 4 HOH   77  477 73  HOH   HOH B . 
G 4 HOH   78  478 94  HOH   HOH B . 
G 4 HOH   79  479 80  HOH   HOH B . 
G 4 HOH   80  480 87  HOH   HOH B . 
G 4 HOH   81  481 124 HOH   HOH B . 
G 4 HOH   82  482 138 HOH   HOH B . 
G 4 HOH   83  483 45  HOH   HOH B . 
G 4 HOH   84  484 36  HOH   HOH B . 
G 4 HOH   85  485 114 HOH   HOH B . 
G 4 HOH   86  486 59  HOH   HOH B . 
G 4 HOH   87  487 181 HOH   HOH B . 
G 4 HOH   88  488 153 HOH   HOH B . 
G 4 HOH   89  489 158 HOH   HOH B . 
G 4 HOH   90  490 136 HOH   HOH B . 
G 4 HOH   91  491 35  HOH   HOH B . 
G 4 HOH   92  492 147 HOH   HOH B . 
G 4 HOH   93  493 98  HOH   HOH B . 
G 4 HOH   94  494 101 HOH   HOH B . 
G 4 HOH   95  495 66  HOH   HOH B . 
G 4 HOH   96  496 81  HOH   HOH B . 
G 4 HOH   97  497 206 HOH   HOH B . 
G 4 HOH   98  498 222 HOH   HOH B . 
G 4 HOH   99  499 216 HOH   HOH B . 
G 4 HOH   100 500 148 HOH   HOH B . 
G 4 HOH   101 501 170 HOH   HOH B . 
G 4 HOH   102 502 233 HOH   HOH B . 
G 4 HOH   103 503 116 HOH   HOH B . 
G 4 HOH   104 504 171 HOH   HOH B . 
G 4 HOH   105 505 193 HOH   HOH B . 
G 4 HOH   106 506 163 HOH   HOH B . 
G 4 HOH   107 507 189 HOH   HOH B . 
G 4 HOH   108 508 196 HOH   HOH B . 
G 4 HOH   109 509 134 HOH   HOH B . 
G 4 HOH   110 510 190 HOH   HOH B . 
G 4 HOH   111 511 156 HOH   HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        2 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .        3 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.20 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FD8 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.084 
_cell.length_a_esd                 ? 
_cell.length_b                     72.470 
_cell.length_b_esd                 ? 
_cell.length_c                     70.885 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         9FD8 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9FD8 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.14 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.47 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Protein was concentrated to 8 mg/mL in 20 mM potassium phosphate, pH 7. Crystallization conditions: 0-4% 2-propanol, 22-24% PEG 3350 in 0.1 M HEPES, pH 7.5. The Schiff-base complex was obtained by brief soaking (about 30 seconds) in saturated ligand solution prepared with crystallization solution plus 25% glycerol
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9655 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9655 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FD8 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.58 
_reflns.d_resolution_low                               48 
_reflns.details                                        ? 
_reflns.limit_h_max                                    ? 
_reflns.limit_h_min                                    ? 
_reflns.limit_k_max                                    ? 
_reflns.limit_k_min                                    ? 
_reflns.limit_l_max                                    ? 
_reflns.limit_l_min                                    ? 
_reflns.number_all                                     ? 
_reflns.number_obs                                     65329 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           98.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.2 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.49 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.101 
_reflns.pdbx_Rpim_I_all                                0.055 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.996 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.084 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.58 
_reflns_shell.d_res_low                                     1.61 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           6512 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             2935 
_reflns_shell.percent_possible_obs                          89.6 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               2.2 
_reflns_shell.pdbx_chi_squared                              0.47 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     1.0 
_reflns_shell.pdbx_Rrim_I_all                               0.862 
_reflns_shell.pdbx_Rpim_I_all                               0.542 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.455 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.664 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            -0.92 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            0.16 
_refine.aniso_B[2][2]                            0.84 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            0.04 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               18.965 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.962 
_refine.correlation_coeff_Fo_to_Fc_free          0.956 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9FD8 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.58 
_refine.ls_d_res_low                             47.85 
_refine.ls_extinction_coef                       ? 
_refine.ls_extinction_coef_esd                   ? 
_refine.ls_extinction_expression                 ? 
_refine.ls_extinction_method                     ? 
_refine.ls_goodness_of_fit_all                   ? 
_refine.ls_goodness_of_fit_all_esd               ? 
_refine.ls_goodness_of_fit_obs                   ? 
_refine.ls_goodness_of_fit_obs_esd               ? 
_refine.ls_hydrogen_treatment                    ? 
_refine.ls_matrix_type                           ? 
_refine.ls_number_constraints                    ? 
_refine.ls_number_parameters                     ? 
_refine.ls_number_reflns_all                     ? 
_refine.ls_number_reflns_obs                     62201 
_refine.ls_number_reflns_R_free                  3107 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.56 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.16514 
_refine.ls_R_factor_R_free                       0.18472 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.16419 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'FOURIER SYNTHESIS' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.077 
_refine.pdbx_overall_ESU_R_Free                  0.075 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             3.711 
_refine.overall_SU_ML                            0.058 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.58 
_refine_hist.d_res_low                        47.85 
_refine_hist.number_atoms_solvent             238 
_refine_hist.number_atoms_total               3922 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3658 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         26 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  0.012  3765 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3722 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.601  1.795  5097 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.545  1.723  8569 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.271  5.000  498  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.214  5.714  28   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.543 10.000 663  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.083  0.200  609  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.007  0.020  4395 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.020  793  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 1.307  1.361  1962 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.299  1.361  1962 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.950  2.432  2449 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.950  2.433  2450 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.854  1.720  1803 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.854  1.720  1804 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.488  2.976  2642 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.574  14.65  4271 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.475  14.05  4223 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.580 
_refine_ls_shell.d_res_low                        1.621 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             192 
_refine_ls_shell.number_reflns_R_work             4178 
_refine_ls_shell.percent_reflns_obs               90.38 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.293 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.321 
# 
_struct.entry_id                     9FD8 
_struct.title                        
'Re-engineered peroxygenase variant of 2-deoxy-D-ribose-5-phosphate aldolase, Schiff-base complex with 4-chloro-cinnamaldehyde' 
_struct.pdbx_model_details           ? 
_struct.pdbx_formula_weight          ? 
_struct.pdbx_formula_weight_method   ? 
_struct.pdbx_model_type_details      ? 
_struct.pdbx_CASP_flag               N 
# 
_struct_keywords.entry_id        9FD8 
_struct_keywords.text            'protein engineering, directed evolution, aldolase, peroxygenase, Schiff base, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 3 ? 
F N N 4 ? 
G N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DEOC_ECOLC 
_struct_ref.pdbx_db_accession          B1IS38 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTDLKASSLRALKLMDLTTLNDDDTDEKVIALCHQAKTPVGNTAAICIYPRFIPIARKTLKEQGTPEIRIATVTNFPHGN
DDIEIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIK
AGADFIKTSTGKVAVNATPESARIMMEVIRDMGVEKTVGFKPAGGVRTAEDAQKYLAIADELFGADWADARHYRFGASSL
LASLLKALGHGDGKSASSY
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9FD8 A 1 ? 259 ? B1IS38 1 ? 259 ? 1 259 
2 1 9FD8 B 1 ? 259 ? B1IS38 1 ? 259 ? 1 259 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9FD8 SER A 18  ? UNP B1IS38 THR 18  'engineered mutation' 18  1  
1 9FD8 GLY A 22  ? UNP B1IS38 ASP 22  'engineered mutation' 22  2  
1 9FD8 TYR A 24  ? UNP B1IS38 ASP 24  'engineered mutation' 24  3  
1 9FD8 SER A 47  ? UNP B1IS38 CYS 47  'engineered mutation' 47  4  
1 9FD8 VAL A 48  ? UNP B1IS38 ILE 48  'engineered mutation' 48  5  
1 9FD8 SER A 52  ? UNP B1IS38 PHE 52  'engineered mutation' 52  6  
1 9FD8 ARG A 172 ? UNP B1IS38 LYS 172 'engineered mutation' 172 7  
1 9FD8 SER A 197 ? UNP B1IS38 THR 197 'engineered mutation' 197 8  
1 9FD8 VAL A 202 ? UNP B1IS38 PRO 202 'engineered mutation' 202 9  
1 9FD8 THR A 203 ? UNP B1IS38 ALA 203 'engineered mutation' 203 10 
1 9FD8 SER A 207 ? UNP B1IS38 ARG 207 'engineered mutation' 207 11 
1 9FD8 SER A 236 ? UNP B1IS38 GLY 236 'engineered mutation' 236 12 
1 9FD8 GLY A 239 ? UNP B1IS38 SER 239 'engineered mutation' 239 13 
1 9FD8 LEU A 260 ? UNP B1IS38 ?   ?   'expression tag'      260 14 
1 9FD8 GLU A 261 ? UNP B1IS38 ?   ?   'expression tag'      261 15 
1 9FD8 HIS A 262 ? UNP B1IS38 ?   ?   'expression tag'      262 16 
1 9FD8 HIS A 263 ? UNP B1IS38 ?   ?   'expression tag'      263 17 
1 9FD8 HIS A 264 ? UNP B1IS38 ?   ?   'expression tag'      264 18 
1 9FD8 HIS A 265 ? UNP B1IS38 ?   ?   'expression tag'      265 19 
1 9FD8 HIS A 266 ? UNP B1IS38 ?   ?   'expression tag'      266 20 
1 9FD8 HIS A 267 ? UNP B1IS38 ?   ?   'expression tag'      267 21 
2 9FD8 SER B 18  ? UNP B1IS38 THR 18  'engineered mutation' 18  22 
2 9FD8 GLY B 22  ? UNP B1IS38 ASP 22  'engineered mutation' 22  23 
2 9FD8 TYR B 24  ? UNP B1IS38 ASP 24  'engineered mutation' 24  24 
2 9FD8 SER B 47  ? UNP B1IS38 CYS 47  'engineered mutation' 47  25 
2 9FD8 VAL B 48  ? UNP B1IS38 ILE 48  'engineered mutation' 48  26 
2 9FD8 SER B 52  ? UNP B1IS38 PHE 52  'engineered mutation' 52  27 
2 9FD8 ARG B 172 ? UNP B1IS38 LYS 172 'engineered mutation' 172 28 
2 9FD8 SER B 197 ? UNP B1IS38 THR 197 'engineered mutation' 197 29 
2 9FD8 VAL B 202 ? UNP B1IS38 PRO 202 'engineered mutation' 202 30 
2 9FD8 THR B 203 ? UNP B1IS38 ALA 203 'engineered mutation' 203 31 
2 9FD8 SER B 207 ? UNP B1IS38 ARG 207 'engineered mutation' 207 32 
2 9FD8 SER B 236 ? UNP B1IS38 GLY 236 'engineered mutation' 236 33 
2 9FD8 GLY B 239 ? UNP B1IS38 SER 239 'engineered mutation' 239 34 
2 9FD8 LEU B 260 ? UNP B1IS38 ?   ?   'expression tag'      260 35 
2 9FD8 GLU B 261 ? UNP B1IS38 ?   ?   'expression tag'      261 36 
2 9FD8 HIS B 262 ? UNP B1IS38 ?   ?   'expression tag'      262 37 
2 9FD8 HIS B 263 ? UNP B1IS38 ?   ?   'expression tag'      263 38 
2 9FD8 HIS B 264 ? UNP B1IS38 ?   ?   'expression tag'      264 39 
2 9FD8 HIS B 265 ? UNP B1IS38 ?   ?   'expression tag'      265 40 
2 9FD8 HIS B 266 ? UNP B1IS38 ?   ?   'expression tag'      266 41 
2 9FD8 HIS B 267 ? UNP B1IS38 ?   ?   'expression tag'      267 42 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,F   
2 1 B,D,E,G 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'gel filtration' ? 
2 2 'gel filtration' ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LEU A 4   ? LYS A 13  ? LEU A 4   LYS A 13  1 ? 10 
HELX_P HELX_P2  AA2 ASP A 26  ? ALA A 36  ? ASP A 26  ALA A 36  1 ? 11 
HELX_P HELX_P3  AA3 TYR A 49  ? ARG A 51  ? TYR A 49  ARG A 51  5 ? 3  
HELX_P HELX_P4  AA4 SER A 52  ? GLN A 63  ? SER A 52  GLN A 63  1 ? 12 
HELX_P HELX_P5  AA5 ASP A 82  ? GLY A 97  ? ASP A 82  GLY A 97  1 ? 16 
HELX_P HELX_P6  AA6 PRO A 106 ? ALA A 112 ? PRO A 106 ALA A 112 1 ? 7  
HELX_P HELX_P7  AA7 GLU A 115 ? ALA A 132 ? GLU A 115 ALA A 132 1 ? 18 
HELX_P HELX_P8  AA8 GLU A 141 ? LYS A 146 ? GLU A 141 LYS A 146 1 ? 6  
HELX_P HELX_P9  AA9 ASP A 147 ? ALA A 161 ? ASP A 147 ALA A 161 1 ? 15 
HELX_P HELX_P10 AB1 THR A 178 ? GLY A 193 ? THR A 178 GLY A 193 1 ? 16 
HELX_P HELX_P11 AB2 THR A 208 ? GLY A 224 ? THR A 208 GLY A 224 1 ? 17 
HELX_P HELX_P12 AB3 GLY A 239 ? LEU A 248 ? GLY A 239 LEU A 248 1 ? 10 
HELX_P HELX_P13 AB4 LEU B 4   ? LYS B 13  ? LEU B 4   LYS B 13  1 ? 10 
HELX_P HELX_P14 AB5 THR B 25  ? ALA B 36  ? THR B 25  ALA B 36  1 ? 12 
HELX_P HELX_P15 AB6 TYR B 49  ? ARG B 51  ? TYR B 49  ARG B 51  5 ? 3  
HELX_P HELX_P16 AB7 SER B 52  ? GLN B 63  ? SER B 52  GLN B 63  1 ? 12 
HELX_P HELX_P17 AB8 ASP B 82  ? GLY B 97  ? ASP B 82  GLY B 97  1 ? 16 
HELX_P HELX_P18 AB9 PRO B 106 ? ALA B 112 ? PRO B 106 ALA B 112 1 ? 7  
HELX_P HELX_P19 AC1 GLU B 115 ? ALA B 132 ? GLU B 115 ALA B 132 1 ? 18 
HELX_P HELX_P20 AC2 GLU B 141 ? LYS B 146 ? GLU B 141 LYS B 146 1 ? 6  
HELX_P HELX_P21 AC3 ASP B 147 ? ALA B 161 ? ASP B 147 ALA B 161 1 ? 15 
HELX_P HELX_P22 AC4 THR B 178 ? GLY B 193 ? THR B 178 GLY B 193 1 ? 16 
HELX_P HELX_P23 AC5 THR B 208 ? GLY B 224 ? THR B 208 GLY B 224 1 ? 17 
HELX_P HELX_P24 AC6 GLY B 239 ? LEU B 248 ? GLY B 239 LEU B 248 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one ? A LYS 167 NZ ? ? ? 1_555 C A1ICA . C1 ? ? A LYS 167 A A1ICA 301 1_555 ? ? ? ? ? ? ? 1.272 ? ? 
covale2 covale one ? B LYS 167 NZ ? ? ? 1_555 D A1ICA . C1 ? ? B LYS 167 B A1ICA 301 1_555 ? ? ? ? ? ? ? 1.271 ? ? 
# 
_struct_conn_type.id          covale 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 A1ICA C . ? LYS A 167 ? A1ICA A 301 ? 1_555 LYS A 167 ? 1_555 C1 NZ LYS 1 A1ICA None 'Covalent chemical modification' 
2 A1ICA D . ? LYS B 167 ? A1ICA B 301 ? 1_555 LYS B 167 ? 1_555 C1 NZ LYS 1 A1ICA None 'Covalent chemical modification' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 76 A . ? PHE 76 A PRO 77 A A PRO 77 A 1 -6.49 
2 PHE 76 B . ? PHE 76 B PRO 77 B ? PRO 77 B 1 -4.73 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 8 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 16  ? LEU A 17  ? ASP A 16  LEU A 17  
AA1 2 ALA A 45  ? SER A 47  ? ALA A 45  SER A 47  
AA1 3 ARG A 69  ? THR A 74  ? ARG A 69  THR A 74  
AA1 4 GLU A 100 ? VAL A 104 ? GLU A 100 VAL A 104 
AA1 5 LEU A 135 ? ILE A 139 ? LEU A 135 ILE A 139 
AA1 6 PHE A 165 ? LYS A 167 ? PHE A 165 LYS A 167 
AA1 7 GLY A 199 ? THR A 203 ? GLY A 199 THR A 203 
AA1 8 TYR A 233 ? SER A 236 ? TYR A 233 SER A 236 
AA2 1 LYS A 37  ? THR A 38  ? LYS A 37  THR A 38  
AA2 2 GLY A 41  ? ASN A 42  ? GLY A 41  ASN A 42  
AA3 1 ASP B 16  ? LEU B 17  ? ASP B 16  LEU B 17  
AA3 2 ALA B 45  ? SER B 47  ? ALA B 45  SER B 47  
AA3 3 ARG B 69  ? THR B 74  ? ARG B 69  THR B 74  
AA3 4 GLU B 100 ? VAL B 104 ? GLU B 100 VAL B 104 
AA3 5 LEU B 135 ? ILE B 139 ? LEU B 135 ILE B 139 
AA3 6 PHE B 165 ? LYS B 167 ? PHE B 165 LYS B 167 
AA3 7 GLY B 199 ? THR B 203 ? GLY B 199 THR B 203 
AA3 8 TYR B 233 ? SER B 236 ? TYR B 233 SER B 236 
AA4 1 LYS B 37  ? THR B 38  ? LYS B 37  THR B 38  
AA4 2 GLY B 41  ? ASN B 42  ? GLY B 41  ASN B 42  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 17  ? N LEU A 17  O ALA A 45  ? O ALA A 45  
AA1 2 3 N ILE A 46  ? N ILE A 46  O ALA A 71  ? O ALA A 71  
AA1 3 4 N THR A 72  ? N THR A 72  O ASP A 102 ? O ASP A 102 
AA1 4 5 N VAL A 103 ? N VAL A 103 O ILE A 139 ? O ILE A 139 
AA1 5 6 N VAL A 138 ? N VAL A 138 O LYS A 167 ? O LYS A 167 
AA1 6 7 N ILE A 166 ? N ILE A 166 O GLY A 199 ? O GLY A 199 
AA1 7 8 N VAL A 202 ? N VAL A 202 O ARG A 234 ? O ARG A 234 
AA2 1 2 N THR A 38  ? N THR A 38  O GLY A 41  ? O GLY A 41  
AA3 1 2 N LEU B 17  ? N LEU B 17  O ALA B 45  ? O ALA B 45  
AA3 2 3 N ILE B 46  ? N ILE B 46  O ALA B 71  ? O ALA B 71  
AA3 3 4 N THR B 72  ? N THR B 72  O ASP B 102 ? O ASP B 102 
AA3 4 5 N VAL B 103 ? N VAL B 103 O ILE B 139 ? O ILE B 139 
AA3 5 6 N VAL B 138 ? N VAL B 138 O LYS B 167 ? O LYS B 167 
AA3 6 7 N ILE B 166 ? N ILE B 166 O GLY B 199 ? O GLY B 199 
AA3 7 8 N VAL B 202 ? N VAL B 202 O ARG B 234 ? O ARG B 234 
AA4 1 2 N THR B 38  ? N THR B 38  O GLY B 41  ? O GLY B 41  
# 
_pdbx_entry_details.entry_id                   9FD8 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              111 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              111 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              111 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                89.26 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            -10.94 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 141 ? ? 63.35   65.80   
2 1 LYS A 146 ? ? 70.10   -50.21  
3 1 ASN A 176 ? ? -109.87 -138.69 
4 1 GLU B 141 ? ? 62.66   65.78   
5 1 LYS B 146 ? ? 71.67   -53.10  
6 1 ASN B 176 ? ? -112.45 -141.52 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG B 172 ? ? 0.077 'SIDE CHAIN' 
2 1 ARG B 234 ? ? 0.073 'SIDE CHAIN' 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1 'X-RAY DIFFRACTION' ? refined -0.9029 -23.2788 -35.7762 0.0200 ? -0.0041 ? 0.0028 ? 0.0213 ? -0.0003 ? 0.0034 ? 0.6117 ? -0.0765 
? -0.0261 ? 0.0253 ? 0.1163 ? 0.8198 ? 0.0201 ? 0.0367  ? 0.0407 ? 0.0033 ? -0.0102 ? -0.0060 ? 0.0316 ? -0.0357 ? -0.0099 ? 
2 'X-RAY DIFFRACTION' ? refined 4.6960  -9.7961  0.0607   0.0242 ? 0.0057  ? 0.0004 ? 0.0189 ? 0.0033  ? 0.0047 ? 0.4889 ? 0.0332  
? -0.1133 ? 0.1253 ? 0.1905 ? 0.3469 ? 0.0025 ? -0.0065 ? 0.0300 ? 0.0033 ? 0.0059  ? 0.0015  ? 0.0095 ? 0.0158  ? -0.0084 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1 'X-RAY DIFFRACTION' 1 ? ? A 4 ? ? ? A 301 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 3 ? ? ? B 302 ? ? ? 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A ASP 3   ? A ASP 3   
4  1 Y 1 A LEU 20  ? A LEU 20  
5  1 Y 1 A ASN 21  ? A ASN 21  
6  1 Y 1 A GLY 22  ? A GLY 22  
7  1 Y 1 A ASP 23  ? A ASP 23  
8  1 Y 1 A TYR 24  ? A TYR 24  
9  1 Y 1 A GLY 251 ? A GLY 251 
10 1 Y 1 A ASP 252 ? A ASP 252 
11 1 Y 1 A GLY 253 ? A GLY 253 
12 1 Y 1 A LYS 254 ? A LYS 254 
13 1 Y 1 A SER 255 ? A SER 255 
14 1 Y 1 A ALA 256 ? A ALA 256 
15 1 Y 1 A SER 257 ? A SER 257 
16 1 Y 1 A SER 258 ? A SER 258 
17 1 Y 1 A TYR 259 ? A TYR 259 
18 1 Y 1 A LEU 260 ? A LEU 260 
19 1 Y 1 A GLU 261 ? A GLU 261 
20 1 Y 1 A HIS 262 ? A HIS 262 
21 1 Y 1 A HIS 263 ? A HIS 263 
22 1 Y 1 A HIS 264 ? A HIS 264 
23 1 Y 1 A HIS 265 ? A HIS 265 
24 1 Y 1 A HIS 266 ? A HIS 266 
25 1 Y 1 A HIS 267 ? A HIS 267 
26 1 Y 1 B MET 1   ? B MET 1   
27 1 Y 1 B THR 2   ? B THR 2   
28 1 Y 1 B LEU 20  ? B LEU 20  
29 1 Y 1 B ASN 21  ? B ASN 21  
30 1 Y 1 B GLY 251 ? B GLY 251 
31 1 Y 1 B ASP 252 ? B ASP 252 
32 1 Y 1 B GLY 253 ? B GLY 253 
33 1 Y 1 B LYS 254 ? B LYS 254 
34 1 Y 1 B SER 255 ? B SER 255 
35 1 Y 1 B ALA 256 ? B ALA 256 
36 1 Y 1 B SER 257 ? B SER 257 
37 1 Y 1 B SER 258 ? B SER 258 
38 1 Y 1 B TYR 259 ? B TYR 259 
39 1 Y 1 B LEU 260 ? B LEU 260 
40 1 Y 1 B GLU 261 ? B GLU 261 
41 1 Y 1 B HIS 262 ? B HIS 262 
42 1 Y 1 B HIS 263 ? B HIS 263 
43 1 Y 1 B HIS 264 ? B HIS 264 
44 1 Y 1 B HIS 265 ? B HIS 265 
45 1 Y 1 B HIS 266 ? B HIS 266 
46 1 Y 1 B HIS 267 ? B HIS 267 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
A1ICA C1   C  N N 1   
A1ICA C2   C  N N 2   
A1ICA C3   C  N N 3   
A1ICA C4   C  Y N 4   
A1ICA C5   C  Y N 5   
A1ICA C6   C  Y N 6   
A1ICA C7   C  Y N 7   
A1ICA CL1  CL N N 8   
A1ICA C8   C  Y N 9   
A1ICA C9   C  Y N 10  
A1ICA O1   O  N N 11  
A1ICA H1   H  N N 12  
A1ICA H2   H  N N 13  
A1ICA H3   H  N N 14  
A1ICA H4   H  N N 15  
A1ICA H5   H  N N 16  
A1ICA H6   H  N N 17  
A1ICA H7   H  N N 18  
A1ICA H8   H  N N 19  
A1ICA H9   H  N N 20  
ALA   N    N  N N 21  
ALA   CA   C  N S 22  
ALA   C    C  N N 23  
ALA   O    O  N N 24  
ALA   CB   C  N N 25  
ALA   OXT  O  N N 26  
ALA   H    H  N N 27  
ALA   H2   H  N N 28  
ALA   HA   H  N N 29  
ALA   HB1  H  N N 30  
ALA   HB2  H  N N 31  
ALA   HB3  H  N N 32  
ALA   HXT  H  N N 33  
ARG   N    N  N N 34  
ARG   CA   C  N S 35  
ARG   C    C  N N 36  
ARG   O    O  N N 37  
ARG   CB   C  N N 38  
ARG   CG   C  N N 39  
ARG   CD   C  N N 40  
ARG   NE   N  N N 41  
ARG   CZ   C  N N 42  
ARG   NH1  N  N N 43  
ARG   NH2  N  N N 44  
ARG   OXT  O  N N 45  
ARG   H    H  N N 46  
ARG   H2   H  N N 47  
ARG   HA   H  N N 48  
ARG   HB2  H  N N 49  
ARG   HB3  H  N N 50  
ARG   HG2  H  N N 51  
ARG   HG3  H  N N 52  
ARG   HD2  H  N N 53  
ARG   HD3  H  N N 54  
ARG   HE   H  N N 55  
ARG   HH11 H  N N 56  
ARG   HH12 H  N N 57  
ARG   HH21 H  N N 58  
ARG   HH22 H  N N 59  
ARG   HXT  H  N N 60  
ASN   N    N  N N 61  
ASN   CA   C  N S 62  
ASN   C    C  N N 63  
ASN   O    O  N N 64  
ASN   CB   C  N N 65  
ASN   CG   C  N N 66  
ASN   OD1  O  N N 67  
ASN   ND2  N  N N 68  
ASN   OXT  O  N N 69  
ASN   H    H  N N 70  
ASN   H2   H  N N 71  
ASN   HA   H  N N 72  
ASN   HB2  H  N N 73  
ASN   HB3  H  N N 74  
ASN   HD21 H  N N 75  
ASN   HD22 H  N N 76  
ASN   HXT  H  N N 77  
ASP   N    N  N N 78  
ASP   CA   C  N S 79  
ASP   C    C  N N 80  
ASP   O    O  N N 81  
ASP   CB   C  N N 82  
ASP   CG   C  N N 83  
ASP   OD1  O  N N 84  
ASP   OD2  O  N N 85  
ASP   OXT  O  N N 86  
ASP   H    H  N N 87  
ASP   H2   H  N N 88  
ASP   HA   H  N N 89  
ASP   HB2  H  N N 90  
ASP   HB3  H  N N 91  
ASP   HD2  H  N N 92  
ASP   HXT  H  N N 93  
CYS   N    N  N N 94  
CYS   CA   C  N R 95  
CYS   C    C  N N 96  
CYS   O    O  N N 97  
CYS   CB   C  N N 98  
CYS   SG   S  N N 99  
CYS   OXT  O  N N 100 
CYS   H    H  N N 101 
CYS   H2   H  N N 102 
CYS   HA   H  N N 103 
CYS   HB2  H  N N 104 
CYS   HB3  H  N N 105 
CYS   HG   H  N N 106 
CYS   HXT  H  N N 107 
GLN   N    N  N N 108 
GLN   CA   C  N S 109 
GLN   C    C  N N 110 
GLN   O    O  N N 111 
GLN   CB   C  N N 112 
GLN   CG   C  N N 113 
GLN   CD   C  N N 114 
GLN   OE1  O  N N 115 
GLN   NE2  N  N N 116 
GLN   OXT  O  N N 117 
GLN   H    H  N N 118 
GLN   H2   H  N N 119 
GLN   HA   H  N N 120 
GLN   HB2  H  N N 121 
GLN   HB3  H  N N 122 
GLN   HG2  H  N N 123 
GLN   HG3  H  N N 124 
GLN   HE21 H  N N 125 
GLN   HE22 H  N N 126 
GLN   HXT  H  N N 127 
GLU   N    N  N N 128 
GLU   CA   C  N S 129 
GLU   C    C  N N 130 
GLU   O    O  N N 131 
GLU   CB   C  N N 132 
GLU   CG   C  N N 133 
GLU   CD   C  N N 134 
GLU   OE1  O  N N 135 
GLU   OE2  O  N N 136 
GLU   OXT  O  N N 137 
GLU   H    H  N N 138 
GLU   H2   H  N N 139 
GLU   HA   H  N N 140 
GLU   HB2  H  N N 141 
GLU   HB3  H  N N 142 
GLU   HG2  H  N N 143 
GLU   HG3  H  N N 144 
GLU   HE2  H  N N 145 
GLU   HXT  H  N N 146 
GLY   N    N  N N 147 
GLY   CA   C  N N 148 
GLY   C    C  N N 149 
GLY   O    O  N N 150 
GLY   OXT  O  N N 151 
GLY   H    H  N N 152 
GLY   H2   H  N N 153 
GLY   HA2  H  N N 154 
GLY   HA3  H  N N 155 
GLY   HXT  H  N N 156 
GOL   C1   C  N N 157 
GOL   O1   O  N N 158 
GOL   C2   C  N N 159 
GOL   O2   O  N N 160 
GOL   C3   C  N N 161 
GOL   O3   O  N N 162 
GOL   H11  H  N N 163 
GOL   H12  H  N N 164 
GOL   HO1  H  N N 165 
GOL   H2   H  N N 166 
GOL   HO2  H  N N 167 
GOL   H31  H  N N 168 
GOL   H32  H  N N 169 
GOL   HO3  H  N N 170 
HIS   N    N  N N 171 
HIS   CA   C  N S 172 
HIS   C    C  N N 173 
HIS   O    O  N N 174 
HIS   CB   C  N N 175 
HIS   CG   C  Y N 176 
HIS   ND1  N  Y N 177 
HIS   CD2  C  Y N 178 
HIS   CE1  C  Y N 179 
HIS   NE2  N  Y N 180 
HIS   OXT  O  N N 181 
HIS   H    H  N N 182 
HIS   H2   H  N N 183 
HIS   HA   H  N N 184 
HIS   HB2  H  N N 185 
HIS   HB3  H  N N 186 
HIS   HD1  H  N N 187 
HIS   HD2  H  N N 188 
HIS   HE1  H  N N 189 
HIS   HE2  H  N N 190 
HIS   HXT  H  N N 191 
HOH   O    O  N N 192 
HOH   H1   H  N N 193 
HOH   H2   H  N N 194 
ILE   N    N  N N 195 
ILE   CA   C  N S 196 
ILE   C    C  N N 197 
ILE   O    O  N N 198 
ILE   CB   C  N S 199 
ILE   CG1  C  N N 200 
ILE   CG2  C  N N 201 
ILE   CD1  C  N N 202 
ILE   OXT  O  N N 203 
ILE   H    H  N N 204 
ILE   H2   H  N N 205 
ILE   HA   H  N N 206 
ILE   HB   H  N N 207 
ILE   HG12 H  N N 208 
ILE   HG13 H  N N 209 
ILE   HG21 H  N N 210 
ILE   HG22 H  N N 211 
ILE   HG23 H  N N 212 
ILE   HD11 H  N N 213 
ILE   HD12 H  N N 214 
ILE   HD13 H  N N 215 
ILE   HXT  H  N N 216 
LEU   N    N  N N 217 
LEU   CA   C  N S 218 
LEU   C    C  N N 219 
LEU   O    O  N N 220 
LEU   CB   C  N N 221 
LEU   CG   C  N N 222 
LEU   CD1  C  N N 223 
LEU   CD2  C  N N 224 
LEU   OXT  O  N N 225 
LEU   H    H  N N 226 
LEU   H2   H  N N 227 
LEU   HA   H  N N 228 
LEU   HB2  H  N N 229 
LEU   HB3  H  N N 230 
LEU   HG   H  N N 231 
LEU   HD11 H  N N 232 
LEU   HD12 H  N N 233 
LEU   HD13 H  N N 234 
LEU   HD21 H  N N 235 
LEU   HD22 H  N N 236 
LEU   HD23 H  N N 237 
LEU   HXT  H  N N 238 
LYS   N    N  N N 239 
LYS   CA   C  N S 240 
LYS   C    C  N N 241 
LYS   O    O  N N 242 
LYS   CB   C  N N 243 
LYS   CG   C  N N 244 
LYS   CD   C  N N 245 
LYS   CE   C  N N 246 
LYS   NZ   N  N N 247 
LYS   OXT  O  N N 248 
LYS   H    H  N N 249 
LYS   H2   H  N N 250 
LYS   HA   H  N N 251 
LYS   HB2  H  N N 252 
LYS   HB3  H  N N 253 
LYS   HG2  H  N N 254 
LYS   HG3  H  N N 255 
LYS   HD2  H  N N 256 
LYS   HD3  H  N N 257 
LYS   HE2  H  N N 258 
LYS   HE3  H  N N 259 
LYS   HZ1  H  N N 260 
LYS   HZ2  H  N N 261 
LYS   HZ3  H  N N 262 
LYS   HXT  H  N N 263 
MET   N    N  N N 264 
MET   CA   C  N S 265 
MET   C    C  N N 266 
MET   O    O  N N 267 
MET   CB   C  N N 268 
MET   CG   C  N N 269 
MET   SD   S  N N 270 
MET   CE   C  N N 271 
MET   OXT  O  N N 272 
MET   H    H  N N 273 
MET   H2   H  N N 274 
MET   HA   H  N N 275 
MET   HB2  H  N N 276 
MET   HB3  H  N N 277 
MET   HG2  H  N N 278 
MET   HG3  H  N N 279 
MET   HE1  H  N N 280 
MET   HE2  H  N N 281 
MET   HE3  H  N N 282 
MET   HXT  H  N N 283 
PHE   N    N  N N 284 
PHE   CA   C  N S 285 
PHE   C    C  N N 286 
PHE   O    O  N N 287 
PHE   CB   C  N N 288 
PHE   CG   C  Y N 289 
PHE   CD1  C  Y N 290 
PHE   CD2  C  Y N 291 
PHE   CE1  C  Y N 292 
PHE   CE2  C  Y N 293 
PHE   CZ   C  Y N 294 
PHE   OXT  O  N N 295 
PHE   H    H  N N 296 
PHE   H2   H  N N 297 
PHE   HA   H  N N 298 
PHE   HB2  H  N N 299 
PHE   HB3  H  N N 300 
PHE   HD1  H  N N 301 
PHE   HD2  H  N N 302 
PHE   HE1  H  N N 303 
PHE   HE2  H  N N 304 
PHE   HZ   H  N N 305 
PHE   HXT  H  N N 306 
PRO   N    N  N N 307 
PRO   CA   C  N S 308 
PRO   C    C  N N 309 
PRO   O    O  N N 310 
PRO   CB   C  N N 311 
PRO   CG   C  N N 312 
PRO   CD   C  N N 313 
PRO   OXT  O  N N 314 
PRO   H    H  N N 315 
PRO   HA   H  N N 316 
PRO   HB2  H  N N 317 
PRO   HB3  H  N N 318 
PRO   HG2  H  N N 319 
PRO   HG3  H  N N 320 
PRO   HD2  H  N N 321 
PRO   HD3  H  N N 322 
PRO   HXT  H  N N 323 
SER   N    N  N N 324 
SER   CA   C  N S 325 
SER   C    C  N N 326 
SER   O    O  N N 327 
SER   CB   C  N N 328 
SER   OG   O  N N 329 
SER   OXT  O  N N 330 
SER   H    H  N N 331 
SER   H2   H  N N 332 
SER   HA   H  N N 333 
SER   HB2  H  N N 334 
SER   HB3  H  N N 335 
SER   HG   H  N N 336 
SER   HXT  H  N N 337 
THR   N    N  N N 338 
THR   CA   C  N S 339 
THR   C    C  N N 340 
THR   O    O  N N 341 
THR   CB   C  N R 342 
THR   OG1  O  N N 343 
THR   CG2  C  N N 344 
THR   OXT  O  N N 345 
THR   H    H  N N 346 
THR   H2   H  N N 347 
THR   HA   H  N N 348 
THR   HB   H  N N 349 
THR   HG1  H  N N 350 
THR   HG21 H  N N 351 
THR   HG22 H  N N 352 
THR   HG23 H  N N 353 
THR   HXT  H  N N 354 
TRP   N    N  N N 355 
TRP   CA   C  N S 356 
TRP   C    C  N N 357 
TRP   O    O  N N 358 
TRP   CB   C  N N 359 
TRP   CG   C  Y N 360 
TRP   CD1  C  Y N 361 
TRP   CD2  C  Y N 362 
TRP   NE1  N  Y N 363 
TRP   CE2  C  Y N 364 
TRP   CE3  C  Y N 365 
TRP   CZ2  C  Y N 366 
TRP   CZ3  C  Y N 367 
TRP   CH2  C  Y N 368 
TRP   OXT  O  N N 369 
TRP   H    H  N N 370 
TRP   H2   H  N N 371 
TRP   HA   H  N N 372 
TRP   HB2  H  N N 373 
TRP   HB3  H  N N 374 
TRP   HD1  H  N N 375 
TRP   HE1  H  N N 376 
TRP   HE3  H  N N 377 
TRP   HZ2  H  N N 378 
TRP   HZ3  H  N N 379 
TRP   HH2  H  N N 380 
TRP   HXT  H  N N 381 
TYR   N    N  N N 382 
TYR   CA   C  N S 383 
TYR   C    C  N N 384 
TYR   O    O  N N 385 
TYR   CB   C  N N 386 
TYR   CG   C  Y N 387 
TYR   CD1  C  Y N 388 
TYR   CD2  C  Y N 389 
TYR   CE1  C  Y N 390 
TYR   CE2  C  Y N 391 
TYR   CZ   C  Y N 392 
TYR   OH   O  N N 393 
TYR   OXT  O  N N 394 
TYR   H    H  N N 395 
TYR   H2   H  N N 396 
TYR   HA   H  N N 397 
TYR   HB2  H  N N 398 
TYR   HB3  H  N N 399 
TYR   HD1  H  N N 400 
TYR   HD2  H  N N 401 
TYR   HE1  H  N N 402 
TYR   HE2  H  N N 403 
TYR   HH   H  N N 404 
TYR   HXT  H  N N 405 
VAL   N    N  N N 406 
VAL   CA   C  N S 407 
VAL   C    C  N N 408 
VAL   O    O  N N 409 
VAL   CB   C  N N 410 
VAL   CG1  C  N N 411 
VAL   CG2  C  N N 412 
VAL   OXT  O  N N 413 
VAL   H    H  N N 414 
VAL   H2   H  N N 415 
VAL   HA   H  N N 416 
VAL   HB   H  N N 417 
VAL   HG11 H  N N 418 
VAL   HG12 H  N N 419 
VAL   HG13 H  N N 420 
VAL   HG21 H  N N 421 
VAL   HG22 H  N N 422 
VAL   HG23 H  N N 423 
VAL   HXT  H  N N 424 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
A1ICA C1  C2   sing N N 1   
A1ICA C2  C3   doub N E 2   
A1ICA C3  C4   sing N N 3   
A1ICA C4  C5   doub Y N 4   
A1ICA C4  C9   sing Y N 5   
A1ICA C5  C6   sing Y N 6   
A1ICA C9  C8   doub Y N 7   
A1ICA C6  C7   doub Y N 8   
A1ICA C8  C7   sing Y N 9   
A1ICA C7  CL1  sing N N 10  
A1ICA C1  O1   sing N N 11  
A1ICA C1  H1   sing N N 12  
A1ICA C1  H2   sing N N 13  
A1ICA C2  H3   sing N N 14  
A1ICA C3  H4   sing N N 15  
A1ICA C5  H5   sing N N 16  
A1ICA C6  H6   sing N N 17  
A1ICA C8  H7   sing N N 18  
A1ICA C9  H8   sing N N 19  
A1ICA O1  H9   sing N N 20  
ALA   N   CA   sing N N 21  
ALA   N   H    sing N N 22  
ALA   N   H2   sing N N 23  
ALA   CA  C    sing N N 24  
ALA   CA  CB   sing N N 25  
ALA   CA  HA   sing N N 26  
ALA   C   O    doub N N 27  
ALA   C   OXT  sing N N 28  
ALA   CB  HB1  sing N N 29  
ALA   CB  HB2  sing N N 30  
ALA   CB  HB3  sing N N 31  
ALA   OXT HXT  sing N N 32  
ARG   N   CA   sing N N 33  
ARG   N   H    sing N N 34  
ARG   N   H2   sing N N 35  
ARG   CA  C    sing N N 36  
ARG   CA  CB   sing N N 37  
ARG   CA  HA   sing N N 38  
ARG   C   O    doub N N 39  
ARG   C   OXT  sing N N 40  
ARG   CB  CG   sing N N 41  
ARG   CB  HB2  sing N N 42  
ARG   CB  HB3  sing N N 43  
ARG   CG  CD   sing N N 44  
ARG   CG  HG2  sing N N 45  
ARG   CG  HG3  sing N N 46  
ARG   CD  NE   sing N N 47  
ARG   CD  HD2  sing N N 48  
ARG   CD  HD3  sing N N 49  
ARG   NE  CZ   sing N N 50  
ARG   NE  HE   sing N N 51  
ARG   CZ  NH1  sing N N 52  
ARG   CZ  NH2  doub N N 53  
ARG   NH1 HH11 sing N N 54  
ARG   NH1 HH12 sing N N 55  
ARG   NH2 HH21 sing N N 56  
ARG   NH2 HH22 sing N N 57  
ARG   OXT HXT  sing N N 58  
ASN   N   CA   sing N N 59  
ASN   N   H    sing N N 60  
ASN   N   H2   sing N N 61  
ASN   CA  C    sing N N 62  
ASN   CA  CB   sing N N 63  
ASN   CA  HA   sing N N 64  
ASN   C   O    doub N N 65  
ASN   C   OXT  sing N N 66  
ASN   CB  CG   sing N N 67  
ASN   CB  HB2  sing N N 68  
ASN   CB  HB3  sing N N 69  
ASN   CG  OD1  doub N N 70  
ASN   CG  ND2  sing N N 71  
ASN   ND2 HD21 sing N N 72  
ASN   ND2 HD22 sing N N 73  
ASN   OXT HXT  sing N N 74  
ASP   N   CA   sing N N 75  
ASP   N   H    sing N N 76  
ASP   N   H2   sing N N 77  
ASP   CA  C    sing N N 78  
ASP   CA  CB   sing N N 79  
ASP   CA  HA   sing N N 80  
ASP   C   O    doub N N 81  
ASP   C   OXT  sing N N 82  
ASP   CB  CG   sing N N 83  
ASP   CB  HB2  sing N N 84  
ASP   CB  HB3  sing N N 85  
ASP   CG  OD1  doub N N 86  
ASP   CG  OD2  sing N N 87  
ASP   OD2 HD2  sing N N 88  
ASP   OXT HXT  sing N N 89  
CYS   N   CA   sing N N 90  
CYS   N   H    sing N N 91  
CYS   N   H2   sing N N 92  
CYS   CA  C    sing N N 93  
CYS   CA  CB   sing N N 94  
CYS   CA  HA   sing N N 95  
CYS   C   O    doub N N 96  
CYS   C   OXT  sing N N 97  
CYS   CB  SG   sing N N 98  
CYS   CB  HB2  sing N N 99  
CYS   CB  HB3  sing N N 100 
CYS   SG  HG   sing N N 101 
CYS   OXT HXT  sing N N 102 
GLN   N   CA   sing N N 103 
GLN   N   H    sing N N 104 
GLN   N   H2   sing N N 105 
GLN   CA  C    sing N N 106 
GLN   CA  CB   sing N N 107 
GLN   CA  HA   sing N N 108 
GLN   C   O    doub N N 109 
GLN   C   OXT  sing N N 110 
GLN   CB  CG   sing N N 111 
GLN   CB  HB2  sing N N 112 
GLN   CB  HB3  sing N N 113 
GLN   CG  CD   sing N N 114 
GLN   CG  HG2  sing N N 115 
GLN   CG  HG3  sing N N 116 
GLN   CD  OE1  doub N N 117 
GLN   CD  NE2  sing N N 118 
GLN   NE2 HE21 sing N N 119 
GLN   NE2 HE22 sing N N 120 
GLN   OXT HXT  sing N N 121 
GLU   N   CA   sing N N 122 
GLU   N   H    sing N N 123 
GLU   N   H2   sing N N 124 
GLU   CA  C    sing N N 125 
GLU   CA  CB   sing N N 126 
GLU   CA  HA   sing N N 127 
GLU   C   O    doub N N 128 
GLU   C   OXT  sing N N 129 
GLU   CB  CG   sing N N 130 
GLU   CB  HB2  sing N N 131 
GLU   CB  HB3  sing N N 132 
GLU   CG  CD   sing N N 133 
GLU   CG  HG2  sing N N 134 
GLU   CG  HG3  sing N N 135 
GLU   CD  OE1  doub N N 136 
GLU   CD  OE2  sing N N 137 
GLU   OE2 HE2  sing N N 138 
GLU   OXT HXT  sing N N 139 
GLY   N   CA   sing N N 140 
GLY   N   H    sing N N 141 
GLY   N   H2   sing N N 142 
GLY   CA  C    sing N N 143 
GLY   CA  HA2  sing N N 144 
GLY   CA  HA3  sing N N 145 
GLY   C   O    doub N N 146 
GLY   C   OXT  sing N N 147 
GLY   OXT HXT  sing N N 148 
GOL   C1  O1   sing N N 149 
GOL   C1  C2   sing N N 150 
GOL   C1  H11  sing N N 151 
GOL   C1  H12  sing N N 152 
GOL   O1  HO1  sing N N 153 
GOL   C2  O2   sing N N 154 
GOL   C2  C3   sing N N 155 
GOL   C2  H2   sing N N 156 
GOL   O2  HO2  sing N N 157 
GOL   C3  O3   sing N N 158 
GOL   C3  H31  sing N N 159 
GOL   C3  H32  sing N N 160 
GOL   O3  HO3  sing N N 161 
HIS   N   CA   sing N N 162 
HIS   N   H    sing N N 163 
HIS   N   H2   sing N N 164 
HIS   CA  C    sing N N 165 
HIS   CA  CB   sing N N 166 
HIS   CA  HA   sing N N 167 
HIS   C   O    doub N N 168 
HIS   C   OXT  sing N N 169 
HIS   CB  CG   sing N N 170 
HIS   CB  HB2  sing N N 171 
HIS   CB  HB3  sing N N 172 
HIS   CG  ND1  sing Y N 173 
HIS   CG  CD2  doub Y N 174 
HIS   ND1 CE1  doub Y N 175 
HIS   ND1 HD1  sing N N 176 
HIS   CD2 NE2  sing Y N 177 
HIS   CD2 HD2  sing N N 178 
HIS   CE1 NE2  sing Y N 179 
HIS   CE1 HE1  sing N N 180 
HIS   NE2 HE2  sing N N 181 
HIS   OXT HXT  sing N N 182 
HOH   O   H1   sing N N 183 
HOH   O   H2   sing N N 184 
ILE   N   CA   sing N N 185 
ILE   N   H    sing N N 186 
ILE   N   H2   sing N N 187 
ILE   CA  C    sing N N 188 
ILE   CA  CB   sing N N 189 
ILE   CA  HA   sing N N 190 
ILE   C   O    doub N N 191 
ILE   C   OXT  sing N N 192 
ILE   CB  CG1  sing N N 193 
ILE   CB  CG2  sing N N 194 
ILE   CB  HB   sing N N 195 
ILE   CG1 CD1  sing N N 196 
ILE   CG1 HG12 sing N N 197 
ILE   CG1 HG13 sing N N 198 
ILE   CG2 HG21 sing N N 199 
ILE   CG2 HG22 sing N N 200 
ILE   CG2 HG23 sing N N 201 
ILE   CD1 HD11 sing N N 202 
ILE   CD1 HD12 sing N N 203 
ILE   CD1 HD13 sing N N 204 
ILE   OXT HXT  sing N N 205 
LEU   N   CA   sing N N 206 
LEU   N   H    sing N N 207 
LEU   N   H2   sing N N 208 
LEU   CA  C    sing N N 209 
LEU   CA  CB   sing N N 210 
LEU   CA  HA   sing N N 211 
LEU   C   O    doub N N 212 
LEU   C   OXT  sing N N 213 
LEU   CB  CG   sing N N 214 
LEU   CB  HB2  sing N N 215 
LEU   CB  HB3  sing N N 216 
LEU   CG  CD1  sing N N 217 
LEU   CG  CD2  sing N N 218 
LEU   CG  HG   sing N N 219 
LEU   CD1 HD11 sing N N 220 
LEU   CD1 HD12 sing N N 221 
LEU   CD1 HD13 sing N N 222 
LEU   CD2 HD21 sing N N 223 
LEU   CD2 HD22 sing N N 224 
LEU   CD2 HD23 sing N N 225 
LEU   OXT HXT  sing N N 226 
LYS   N   CA   sing N N 227 
LYS   N   H    sing N N 228 
LYS   N   H2   sing N N 229 
LYS   CA  C    sing N N 230 
LYS   CA  CB   sing N N 231 
LYS   CA  HA   sing N N 232 
LYS   C   O    doub N N 233 
LYS   C   OXT  sing N N 234 
LYS   CB  CG   sing N N 235 
LYS   CB  HB2  sing N N 236 
LYS   CB  HB3  sing N N 237 
LYS   CG  CD   sing N N 238 
LYS   CG  HG2  sing N N 239 
LYS   CG  HG3  sing N N 240 
LYS   CD  CE   sing N N 241 
LYS   CD  HD2  sing N N 242 
LYS   CD  HD3  sing N N 243 
LYS   CE  NZ   sing N N 244 
LYS   CE  HE2  sing N N 245 
LYS   CE  HE3  sing N N 246 
LYS   NZ  HZ1  sing N N 247 
LYS   NZ  HZ2  sing N N 248 
LYS   NZ  HZ3  sing N N 249 
LYS   OXT HXT  sing N N 250 
MET   N   CA   sing N N 251 
MET   N   H    sing N N 252 
MET   N   H2   sing N N 253 
MET   CA  C    sing N N 254 
MET   CA  CB   sing N N 255 
MET   CA  HA   sing N N 256 
MET   C   O    doub N N 257 
MET   C   OXT  sing N N 258 
MET   CB  CG   sing N N 259 
MET   CB  HB2  sing N N 260 
MET   CB  HB3  sing N N 261 
MET   CG  SD   sing N N 262 
MET   CG  HG2  sing N N 263 
MET   CG  HG3  sing N N 264 
MET   SD  CE   sing N N 265 
MET   CE  HE1  sing N N 266 
MET   CE  HE2  sing N N 267 
MET   CE  HE3  sing N N 268 
MET   OXT HXT  sing N N 269 
PHE   N   CA   sing N N 270 
PHE   N   H    sing N N 271 
PHE   N   H2   sing N N 272 
PHE   CA  C    sing N N 273 
PHE   CA  CB   sing N N 274 
PHE   CA  HA   sing N N 275 
PHE   C   O    doub N N 276 
PHE   C   OXT  sing N N 277 
PHE   CB  CG   sing N N 278 
PHE   CB  HB2  sing N N 279 
PHE   CB  HB3  sing N N 280 
PHE   CG  CD1  doub Y N 281 
PHE   CG  CD2  sing Y N 282 
PHE   CD1 CE1  sing Y N 283 
PHE   CD1 HD1  sing N N 284 
PHE   CD2 CE2  doub Y N 285 
PHE   CD2 HD2  sing N N 286 
PHE   CE1 CZ   doub Y N 287 
PHE   CE1 HE1  sing N N 288 
PHE   CE2 CZ   sing Y N 289 
PHE   CE2 HE2  sing N N 290 
PHE   CZ  HZ   sing N N 291 
PHE   OXT HXT  sing N N 292 
PRO   N   CA   sing N N 293 
PRO   N   CD   sing N N 294 
PRO   N   H    sing N N 295 
PRO   CA  C    sing N N 296 
PRO   CA  CB   sing N N 297 
PRO   CA  HA   sing N N 298 
PRO   C   O    doub N N 299 
PRO   C   OXT  sing N N 300 
PRO   CB  CG   sing N N 301 
PRO   CB  HB2  sing N N 302 
PRO   CB  HB3  sing N N 303 
PRO   CG  CD   sing N N 304 
PRO   CG  HG2  sing N N 305 
PRO   CG  HG3  sing N N 306 
PRO   CD  HD2  sing N N 307 
PRO   CD  HD3  sing N N 308 
PRO   OXT HXT  sing N N 309 
SER   N   CA   sing N N 310 
SER   N   H    sing N N 311 
SER   N   H2   sing N N 312 
SER   CA  C    sing N N 313 
SER   CA  CB   sing N N 314 
SER   CA  HA   sing N N 315 
SER   C   O    doub N N 316 
SER   C   OXT  sing N N 317 
SER   CB  OG   sing N N 318 
SER   CB  HB2  sing N N 319 
SER   CB  HB3  sing N N 320 
SER   OG  HG   sing N N 321 
SER   OXT HXT  sing N N 322 
THR   N   CA   sing N N 323 
THR   N   H    sing N N 324 
THR   N   H2   sing N N 325 
THR   CA  C    sing N N 326 
THR   CA  CB   sing N N 327 
THR   CA  HA   sing N N 328 
THR   C   O    doub N N 329 
THR   C   OXT  sing N N 330 
THR   CB  OG1  sing N N 331 
THR   CB  CG2  sing N N 332 
THR   CB  HB   sing N N 333 
THR   OG1 HG1  sing N N 334 
THR   CG2 HG21 sing N N 335 
THR   CG2 HG22 sing N N 336 
THR   CG2 HG23 sing N N 337 
THR   OXT HXT  sing N N 338 
TRP   N   CA   sing N N 339 
TRP   N   H    sing N N 340 
TRP   N   H2   sing N N 341 
TRP   CA  C    sing N N 342 
TRP   CA  CB   sing N N 343 
TRP   CA  HA   sing N N 344 
TRP   C   O    doub N N 345 
TRP   C   OXT  sing N N 346 
TRP   CB  CG   sing N N 347 
TRP   CB  HB2  sing N N 348 
TRP   CB  HB3  sing N N 349 
TRP   CG  CD1  doub Y N 350 
TRP   CG  CD2  sing Y N 351 
TRP   CD1 NE1  sing Y N 352 
TRP   CD1 HD1  sing N N 353 
TRP   CD2 CE2  doub Y N 354 
TRP   CD2 CE3  sing Y N 355 
TRP   NE1 CE2  sing Y N 356 
TRP   NE1 HE1  sing N N 357 
TRP   CE2 CZ2  sing Y N 358 
TRP   CE3 CZ3  doub Y N 359 
TRP   CE3 HE3  sing N N 360 
TRP   CZ2 CH2  doub Y N 361 
TRP   CZ2 HZ2  sing N N 362 
TRP   CZ3 CH2  sing Y N 363 
TRP   CZ3 HZ3  sing N N 364 
TRP   CH2 HH2  sing N N 365 
TRP   OXT HXT  sing N N 366 
TYR   N   CA   sing N N 367 
TYR   N   H    sing N N 368 
TYR   N   H2   sing N N 369 
TYR   CA  C    sing N N 370 
TYR   CA  CB   sing N N 371 
TYR   CA  HA   sing N N 372 
TYR   C   O    doub N N 373 
TYR   C   OXT  sing N N 374 
TYR   CB  CG   sing N N 375 
TYR   CB  HB2  sing N N 376 
TYR   CB  HB3  sing N N 377 
TYR   CG  CD1  doub Y N 378 
TYR   CG  CD2  sing Y N 379 
TYR   CD1 CE1  sing Y N 380 
TYR   CD1 HD1  sing N N 381 
TYR   CD2 CE2  doub Y N 382 
TYR   CD2 HD2  sing N N 383 
TYR   CE1 CZ   doub Y N 384 
TYR   CE1 HE1  sing N N 385 
TYR   CE2 CZ   sing Y N 386 
TYR   CE2 HE2  sing N N 387 
TYR   CZ  OH   sing N N 388 
TYR   OH  HH   sing N N 389 
TYR   OXT HXT  sing N N 390 
VAL   N   CA   sing N N 391 
VAL   N   H    sing N N 392 
VAL   N   H2   sing N N 393 
VAL   CA  C    sing N N 394 
VAL   CA  CB   sing N N 395 
VAL   CA  HA   sing N N 396 
VAL   C   O    doub N N 397 
VAL   C   OXT  sing N N 398 
VAL   CB  CG1  sing N N 399 
VAL   CB  CG2  sing N N 400 
VAL   CB  HB   sing N N 401 
VAL   CG1 HG11 sing N N 402 
VAL   CG1 HG12 sing N N 403 
VAL   CG1 HG13 sing N N 404 
VAL   CG2 HG21 sing N N 405 
VAL   CG2 HG22 sing N N 406 
VAL   CG2 HG23 sing N N 407 
VAL   OXT HXT  sing N N 408 
# 
_pdbx_audit_support.funding_organization   'Netherlands Organisation for Scientific Research (NWO)' 
_pdbx_audit_support.country                Netherlands 
_pdbx_audit_support.grant_number           724.016.002 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      Other 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          'Crystal structure of the apo enzyme was used as starting model' 
# 
_atom_sites.entry_id                    9FD8 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.020797 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002259 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013799 
_atom_sites.fract_transf_matrix[2][3]   0.000000 
_atom_sites.fract_transf_matrix[3][1]   0.000000 
_atom_sites.fract_transf_matrix[3][2]   0.000000 
_atom_sites.fract_transf_matrix[3][3]   0.014190 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
CL 
N  
O  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . LEU   A 1 4   ? -16.475 -21.499 -53.659 1.00 35.32 ? 4   LEU   A N   1 
ATOM   2    C  CA  . LEU   A 1 4   ? -15.876 -20.427 -52.822 1.00 35.00 ? 4   LEU   A CA  1 
ATOM   3    C  C   . LEU   A 1 4   ? -16.639 -20.339 -51.506 1.00 35.11 ? 4   LEU   A C   1 
ATOM   4    O  O   . LEU   A 1 4   ? -16.016 -20.178 -50.451 1.00 29.91 ? 4   LEU   A O   1 
ATOM   5    C  CB  . LEU   A 1 4   ? -15.809 -19.064 -53.499 1.00 35.97 ? 4   LEU   A CB  1 
ATOM   6    C  CG  . LEU   A 1 4   ? -15.015 -18.007 -52.727 1.00 37.80 ? 4   LEU   A CG  1 
ATOM   7    C  CD1 . LEU   A 1 4   ? -13.555 -18.443 -52.621 1.00 40.80 ? 4   LEU   A CD1 1 
ATOM   8    C  CD2 . LEU   A 1 4   ? -15.094 -16.601 -53.309 1.00 40.26 ? 4   LEU   A CD2 1 
ATOM   9    N  N   . LYS   A 1 5   ? -17.978 -20.439 -51.555 1.00 31.68 ? 5   LYS   A N   1 
ATOM   10   C  CA  . LYS   A 1 5   ? -18.758 -20.472 -50.325 1.00 33.87 ? 5   LYS   A CA  1 
ATOM   11   C  C   . LYS   A 1 5   ? -18.421 -21.732 -49.526 1.00 31.66 ? 5   LYS   A C   1 
ATOM   12   O  O   . LYS   A 1 5   ? -18.211 -21.665 -48.306 1.00 27.52 ? 5   LYS   A O   1 
ATOM   13   C  CB  . LYS   A 1 5   ? -20.262 -20.331 -50.594 1.00 36.87 ? 5   LYS   A CB  1 
ATOM   14   C  CG  . LYS   A 1 5   ? -20.630 -18.923 -51.046 1.00 43.36 ? 5   LYS   A CG  1 
ATOM   15   C  CD  . LYS   A 1 5   ? -22.108 -18.576 -50.981 1.00 52.22 ? 5   LYS   A CD  1 
ATOM   16   C  CE  . LYS   A 1 5   ? -22.356 -17.127 -51.255 1.00 55.12 ? 5   LYS   A CE  1 
ATOM   17   N  NZ  . LYS   A 1 5   ? -23.796 -16.883 -51.366 1.00 58.83 ? 5   LYS   A NZ  1 
ATOM   18   N  N   . ALA   A 1 6   ? -18.341 -22.870 -50.220 1.00 29.12 ? 6   ALA   A N   1 
ATOM   19   C  CA  . ALA   A 1 6   ? -18.025 -24.136 -49.576 1.00 29.52 ? 6   ALA   A CA  1 
ATOM   20   C  C   . ALA   A 1 6   ? -16.617 -24.102 -48.976 1.00 28.33 ? 6   ALA   A C   1 
ATOM   21   O  O   . ALA   A 1 6   ? -16.410 -24.594 -47.854 1.00 25.26 ? 6   ALA   A O   1 
ATOM   22   C  CB  . ALA   A 1 6   ? -18.172 -25.282 -50.547 1.00 30.92 ? 6   ALA   A CB  1 
ATOM   23   N  N   . SER   A 1 7   ? -15.651 -23.530 -49.721 1.00 25.27 ? 7   SER   A N   1 
ATOM   24   C  CA  . SER   A 1 7   ? -14.287 -23.480 -49.219 1.00 24.89 ? 7   SER   A CA  1 
ATOM   25   C  C   . SER   A 1 7   ? -14.213 -22.507 -48.042 1.00 24.04 ? 7   SER   A C   1 
ATOM   26   O  O   . SER   A 1 7   ? -13.461 -22.759 -47.098 1.00 23.97 ? 7   SER   A O   1 
ATOM   27   C  CB  . SER   A 1 7   ? -13.250 -23.172 -50.281 1.00 28.36 ? 7   SER   A CB  1 
ATOM   28   O  OG  . SER   A 1 7   ? -13.460 -21.899 -50.867 1.00 32.30 ? 7   SER   A OG  1 
ATOM   29   N  N   . SER   A 1 8   ? -14.965 -21.403 -48.104 1.00 21.76 ? 8   SER   A N   1 
ATOM   30   C  CA  . SER   A 1 8   ? -14.930 -20.400 -47.056 1.00 21.73 ? 8   SER   A CA  1 
ATOM   31   C  C   . SER   A 1 8   ? -15.486 -20.945 -45.740 1.00 21.91 ? 8   SER   A C   1 
ATOM   32   O  O   . SER   A 1 8   ? -14.943 -20.662 -44.675 1.00 21.02 ? 8   SER   A O   1 
ATOM   33   C  CB  . SER   A 1 8   ? -15.632 -19.155 -47.475 1.00 22.79 ? 8   SER   A CB  1 
ATOM   34   O  OG  . SER   A 1 8   ? -14.971 -18.588 -48.597 1.00 24.13 ? 8   SER   A OG  1 
ATOM   35   N  N   . LEU   A 1 9   ? -16.587 -21.690 -45.809 1.00 22.60 ? 9   LEU   A N   1 
ATOM   36   C  CA  . LEU   A 1 9   ? -17.165 -22.288 -44.621 1.00 22.66 ? 9   LEU   A CA  1 
ATOM   37   C  C   . LEU   A 1 9   ? -16.172 -23.280 -44.018 1.00 21.93 ? 9   LEU   A C   1 
ATOM   38   O  O   . LEU   A 1 9   ? -15.981 -23.339 -42.808 1.00 19.43 ? 9   LEU   A O   1 
ATOM   39   C  CB  . LEU   A 1 9   ? -18.470 -22.983 -44.978 1.00 25.39 ? 9   LEU   A CB  1 
ATOM   40   C  CG  . LEU   A 1 9   ? -19.254 -23.565 -43.802 1.00 29.51 ? 9   LEU   A CG  1 
ATOM   41   C  CD1 . LEU   A 1 9   ? -19.650 -22.480 -42.838 1.00 31.21 ? 9   LEU   A CD1 1 
ATOM   42   C  CD2 . LEU   A 1 9   ? -20.485 -24.257 -44.377 1.00 30.84 ? 9   LEU   A CD2 1 
ATOM   43   N  N   . ARG   A 1 10  ? -15.532 -24.052 -44.894 1.00 20.18 ? 10  ARG   A N   1 
ATOM   44   C  CA  . ARG   A 1 10  ? -14.575 -25.032 -44.447 1.00 21.42 ? 10  ARG   A CA  1 
ATOM   45   C  C   . ARG   A 1 10  ? -13.399 -24.349 -43.736 1.00 18.34 ? 10  ARG   A C   1 
ATOM   46   O  O   . ARG   A 1 10  ? -13.003 -24.742 -42.634 1.00 18.30 ? 10  ARG   A O   1 
ATOM   47   C  CB  . ARG   A 1 10  ? -14.182 -25.795 -45.709 1.00 24.10 ? 10  ARG   A CB  1 
ATOM   48   C  CG  . ARG   A 1 10  ? -13.523 -27.121 -45.434 1.00 27.19 ? 10  ARG   A CG  1 
ATOM   49   C  CD  . ARG   A 1 10  ? -13.257 -27.700 -46.814 1.00 30.66 ? 10  ARG   A CD  1 
ATOM   50   N  NE  . ARG   A 1 10  ? -12.185 -28.642 -46.613 1.00 31.75 ? 10  ARG   A NE  1 
ATOM   51   C  CZ  . ARG   A 1 10  ? -11.426 -29.103 -47.591 1.00 29.56 ? 10  ARG   A CZ  1 
ATOM   52   N  NH1 . ARG   A 1 10  ? -11.400 -28.511 -48.775 1.00 34.17 ? 10  ARG   A NH1 1 
ATOM   53   N  NH2 . ARG   A 1 10  ? -10.656 -30.133 -47.341 1.00 31.09 ? 10  ARG   A NH2 1 
ATOM   54   N  N   . ALA   A 1 11  ? -12.861 -23.289 -44.342 1.00 16.92 ? 11  ALA   A N   1 
ATOM   55   C  CA  . ALA   A 1 11  ? -11.731 -22.558 -43.781 1.00 17.16 ? 11  ALA   A CA  1 
ATOM   56   C  C   . ALA   A 1 11  ? -12.097 -21.920 -42.449 1.00 16.05 ? 11  ALA   A C   1 
ATOM   57   O  O   . ALA   A 1 11  ? -11.293 -21.905 -41.522 1.00 15.59 ? 11  ALA   A O   1 
ATOM   58   C  CB  . ALA   A 1 11  ? -11.275 -21.480 -44.753 1.00 17.89 ? 11  ALA   A CB  1 
ATOM   59   N  N   . LEU   A 1 12  ? -13.315 -21.363 -42.366 1.00 15.91 ? 12  LEU   A N   1 
ATOM   60   C  CA  . LEU   A 1 12  ? -13.730 -20.687 -41.141 1.00 15.68 ? 12  LEU   A CA  1 
ATOM   61   C  C   . LEU   A 1 12  ? -13.653 -21.667 -39.974 1.00 16.13 ? 12  LEU   A C   1 
ATOM   62   O  O   . LEU   A 1 12  ? -13.182 -21.326 -38.883 1.00 15.67 ? 12  LEU   A O   1 
ATOM   63   C  CB  . LEU   A 1 12  ? -15.126 -20.109 -41.346 1.00 17.29 ? 12  LEU   A CB  1 
ATOM   64   C  CG  . LEU   A 1 12  ? -15.697 -19.336 -40.150 1.00 18.04 ? 12  LEU   A CG  1 
ATOM   65   C  CD1 . LEU   A 1 12  ? -16.646 -18.246 -40.651 1.00 20.05 ? 12  LEU   A CD1 1 
ATOM   66   C  CD2 . LEU   A 1 12  ? -16.393 -20.249 -39.149 1.00 18.77 ? 12  LEU   A CD2 1 
ATOM   67   N  N   . LYS   A 1 13  ? -14.112 -22.903 -40.206 1.00 16.56 ? 13  LYS   A N   1 
ATOM   68   C  CA  . LYS   A 1 13  ? -14.181 -23.890 -39.133 1.00 16.08 ? 13  LYS   A CA  1 
ATOM   69   C  C   . LYS   A 1 13  ? -12.804 -24.470 -38.826 1.00 15.99 ? 13  LYS   A C   1 
ATOM   70   O  O   . LYS   A 1 13  ? -12.670 -25.275 -37.906 1.00 15.32 ? 13  LYS   A O   1 
ATOM   71   C  CB  . LYS   A 1 13  ? -15.163 -25.008 -39.499 1.00 18.51 ? 13  LYS   A CB  1 
ATOM   72   C  CG  . LYS   A 1 13  ? -16.606 -24.524 -39.558 1.00 21.80 ? 13  LYS   A CG  1 
ATOM   73   C  CD  . LYS   A 1 13  ? -17.601 -25.610 -39.962 1.00 26.83 ? 13  LYS   A CD  1 
ATOM   74   C  CE  . LYS   A 1 13  ? -18.944 -25.019 -40.138 1.00 31.56 ? 13  LYS   A CE  1 
ATOM   75   N  NZ  . LYS   A 1 13  ? -19.911 -26.063 -40.453 1.00 35.73 ? 13  LYS   A NZ  1 
ATOM   76   N  N   . LEU   A 1 14  ? -11.783 -24.079 -39.614 1.00 14.41 ? 14  LEU   A N   1 
ATOM   77   C  CA  . LEU   A 1 14  ? -10.401 -24.491 -39.363 1.00 13.32 ? 14  LEU   A CA  1 
ATOM   78   C  C   . LEU   A 1 14  ? -9.560  -23.343 -38.812 1.00 13.85 ? 14  LEU   A C   1 
ATOM   79   O  O   . LEU   A 1 14  ? -8.334  -23.487 -38.689 1.00 12.74 ? 14  LEU   A O   1 
ATOM   80   C  CB  . LEU   A 1 14  ? -9.792  -25.001 -40.668 1.00 13.88 ? 14  LEU   A CB  1 
ATOM   81   C  CG  . LEU   A 1 14  ? -10.484 -26.229 -41.260 1.00 13.93 ? 14  LEU   A CG  1 
ATOM   82   C  CD1 . LEU   A 1 14  ? -9.965  -26.518 -42.658 1.00 14.57 ? 14  LEU   A CD1 1 
ATOM   83   C  CD2 . LEU   A 1 14  ? -10.310 -27.427 -40.363 1.00 14.27 ? 14  LEU   A CD2 1 
ATOM   84   N  N   . MET   A 1 15  ? -10.190 -22.219 -38.453 1.00 13.82 ? 15  MET   A N   1 
ATOM   85   C  CA  . MET   A 1 15  ? -9.421  -21.053 -38.022 1.00 13.84 ? 15  MET   A CA  1 
ATOM   86   C  C   . MET   A 1 15  ? -9.022  -21.162 -36.551 1.00 13.37 ? 15  MET   A C   1 
ATOM   87   O  O   . MET   A 1 15  ? -9.821  -21.604 -35.719 1.00 12.59 ? 15  MET   A O   1 
ATOM   88   C  CB  . MET   A 1 15  ? -10.188 -19.739 -38.204 1.00 16.27 ? 15  MET   A CB  1 
ATOM   89   C  CG  . MET   A 1 15  ? -10.173 -19.222 -39.618 1.00 21.98 ? 15  MET   A CG  1 
ATOM   90   S  SD  . MET   A 1 15  ? -10.710 -17.498 -39.665 1.00 28.02 ? 15  MET   A SD  1 
ATOM   91   C  CE  . MET   A 1 15  ? -9.190  -16.748 -39.049 1.00 31.29 ? 15  MET   A CE  1 
ATOM   92   N  N   . ASP   A 1 16  ? -7.766  -20.759 -36.266 1.00 13.81 ? 16  ASP   A N   1 
ATOM   93   C  CA  . ASP   A 1 16  ? -7.354  -20.382 -34.919 1.00 13.60 ? 16  ASP   A CA  1 
ATOM   94   C  C   . ASP   A 1 16  ? -7.455  -18.865 -34.870 1.00 14.67 ? 16  ASP   A C   1 
ATOM   95   O  O   . ASP   A 1 16  ? -6.611  -18.174 -35.445 1.00 15.23 ? 16  ASP   A O   1 
ATOM   96   C  CB  . ASP   A 1 16  ? -5.935  -20.804 -34.605 1.00 14.05 ? 16  ASP   A CB  1 
ATOM   97   C  CG  . ASP   A 1 16  ? -5.676  -22.288 -34.429 1.00 15.97 ? 16  ASP   A CG  1 
ATOM   98   O  OD1 . ASP   A 1 16  ? -6.630  -23.067 -34.580 1.00 16.63 ? 16  ASP   A OD1 1 
ATOM   99   O  OD2 . ASP   A 1 16  ? -4.511  -22.657 -34.104 1.00 18.32 ? 16  ASP   A OD2 1 
ATOM   100  N  N   . LEU   A 1 17  ? -8.537  -18.343 -34.278 1.00 14.16 ? 17  LEU   A N   1 
ATOM   101  C  CA  . LEU   A 1 17  ? -8.804  -16.912 -34.377 1.00 15.77 ? 17  LEU   A CA  1 
ATOM   102  C  C   . LEU   A 1 17  ? -8.000  -16.155 -33.319 1.00 18.45 ? 17  LEU   A C   1 
ATOM   103  O  O   . LEU   A 1 17  ? -8.089  -16.488 -32.165 1.00 17.55 ? 17  LEU   A O   1 
ATOM   104  C  CB  . LEU   A 1 17  ? -10.307 -16.697 -34.212 1.00 16.49 ? 17  LEU   A CB  1 
ATOM   105  C  CG  . LEU   A 1 17  ? -10.806 -15.273 -34.450 1.00 18.01 ? 17  LEU   A CG  1 
ATOM   106  C  CD1 . LEU   A 1 17  ? -10.608 -14.936 -35.913 1.00 19.61 ? 17  LEU   A CD1 1 
ATOM   107  C  CD2 . LEU   A 1 17  ? -12.284 -15.144 -34.038 1.00 20.15 ? 17  LEU   A CD2 1 
ATOM   108  N  N   . SER   A 1 18  ? -7.230  -15.139 -33.704 1.00 22.15 ? 18  SER   A N   1 
ATOM   109  C  CA  A SER   A 1 18  ? -6.551  -14.264 -32.752 0.50 25.79 ? 18  SER   A CA  1 
ATOM   110  C  CA  B SER   A 1 18  ? -6.541  -14.261 -32.761 0.50 27.32 ? 18  SER   A CA  1 
ATOM   111  C  C   . SER   A 1 18  ? -7.077  -12.835 -32.891 1.00 28.73 ? 18  SER   A C   1 
ATOM   112  O  O   . SER   A 1 18  ? -7.746  -12.515 -33.861 1.00 34.37 ? 18  SER   A O   1 
ATOM   113  C  CB  A SER   A 1 18  ? -5.065  -14.324 -32.941 0.50 26.50 ? 18  SER   A CB  1 
ATOM   114  C  CB  B SER   A 1 18  ? -5.055  -14.279 -32.982 0.50 30.11 ? 18  SER   A CB  1 
ATOM   115  O  OG  A SER   A 1 18  ? -4.715  -14.085 -34.298 0.50 24.71 ? 18  SER   A OG  1 
ATOM   116  O  OG  B SER   A 1 18  ? -4.549  -15.601 -33.075 0.50 32.05 ? 18  SER   A OG  1 
ATOM   117  N  N   . THR   A 1 19  ? -6.842  -11.992 -31.871 1.00 38.16 ? 19  THR   A N   1 
ATOM   118  C  CA  . THR   A 1 19  ? -7.276  -10.597 -31.944 1.00 41.73 ? 19  THR   A CA  1 
ATOM   119  C  C   . THR   A 1 19  ? -6.500  -9.925  -33.053 1.00 41.08 ? 19  THR   A C   1 
ATOM   120  O  O   . THR   A 1 19  ? -5.263  -10.092 -32.996 1.00 42.75 ? 19  THR   A O   1 
ATOM   121  C  CB  . THR   A 1 19  ? -7.041  -9.852  -30.629 1.00 44.75 ? 19  THR   A CB  1 
ATOM   122  O  OG1 . THR   A 1 19  ? -5.645  -10.005 -30.377 1.00 43.92 ? 19  THR   A OG1 1 
ATOM   123  C  CG2 . THR   A 1 19  ? -7.856  -10.403 -29.469 1.00 44.92 ? 19  THR   A CG2 1 
ATOM   124  N  N   . THR   A 1 25  ? -6.083  -6.612  -23.484 1.00 36.22 ? 25  THR   A N   1 
ATOM   125  C  CA  . THR   A 1 25  ? -7.057  -6.427  -22.385 1.00 33.61 ? 25  THR   A CA  1 
ATOM   126  C  C   . THR   A 1 25  ? -8.026  -7.609  -22.359 1.00 30.23 ? 25  THR   A C   1 
ATOM   127  O  O   . THR   A 1 25  ? -8.272  -8.244  -23.371 1.00 26.66 ? 25  THR   A O   1 
ATOM   128  C  CB  . THR   A 1 25  ? -7.801  -5.096  -22.539 1.00 38.21 ? 25  THR   A CB  1 
ATOM   129  O  OG1 . THR   A 1 25  ? -8.599  -5.208  -23.717 1.00 35.16 ? 25  THR   A OG1 1 
ATOM   130  C  CG2 . THR   A 1 25  ? -6.862  -3.906  -22.614 1.00 38.97 ? 25  THR   A CG2 1 
ATOM   131  N  N   . ASP   A 1 26  ? -8.598  -7.868  -21.185 1.00 28.84 ? 26  ASP   A N   1 
ATOM   132  C  CA  . ASP   A 1 26  ? -9.614  -8.885  -21.010 1.00 27.95 ? 26  ASP   A CA  1 
ATOM   133  C  C   . ASP   A 1 26  ? -10.811 -8.611  -21.922 1.00 26.47 ? 26  ASP   A C   1 
ATOM   134  O  O   . ASP   A 1 26  ? -11.391 -9.529  -22.505 1.00 23.65 ? 26  ASP   A O   1 
ATOM   135  C  CB  . ASP   A 1 26  ? -10.057 -8.915  -19.559 1.00 29.80 ? 26  ASP   A CB  1 
ATOM   136  C  CG  . ASP   A 1 26  ? -9.086  -9.555  -18.586 1.00 31.67 ? 26  ASP   A CG  1 
ATOM   137  O  OD1 . ASP   A 1 26  ? -8.061  -10.093 -19.031 1.00 29.44 ? 26  ASP   A OD1 1 
ATOM   138  O  OD2 . ASP   A 1 26  ? -9.394  -9.506  -17.395 1.00 38.94 ? 26  ASP   A OD2 1 
ATOM   139  N  N   . GLU   A 1 27  ? -11.157 -7.333  -22.073 1.00 26.68 ? 27  GLU   A N   1 
ATOM   140  C  CA  . GLU   A 1 27  ? -12.278 -6.945  -22.918 1.00 28.14 ? 27  GLU   A CA  1 
ATOM   141  C  C   . GLU   A 1 27  ? -12.065 -7.426  -24.359 1.00 26.50 ? 27  GLU   A C   1 
ATOM   142  O  O   . GLU   A 1 27  ? -12.979 -7.913  -25.016 1.00 25.42 ? 27  GLU   A O   1 
ATOM   143  C  CB  . GLU   A 1 27  ? -12.461 -5.434  -22.816 1.00 33.53 ? 27  GLU   A CB  1 
ATOM   144  C  CG  . GLU   A 1 27  ? -13.040 -4.994  -21.473 1.00 41.27 ? 27  GLU   A CG  1 
ATOM   145  C  CD  . GLU   A 1 27  ? -12.109 -4.976  -20.262 1.00 47.93 ? 27  GLU   A CD  1 
ATOM   146  O  OE1 . GLU   A 1 27  ? -10.860 -5.015  -20.363 1.00 43.38 ? 27  GLU   A OE1 1 
ATOM   147  O  OE2 . GLU   A 1 27  ? -12.699 -4.937  -19.161 1.00 59.42 ? 27  GLU   A OE2 1 
ATOM   148  N  N   . LYS   A 1 28  ? -10.860 -7.258  -24.874 1.00 25.20 ? 28  LYS   A N   1 
ATOM   149  C  CA  . LYS   A 1 28  ? -10.546 -7.684  -26.230 1.00 26.43 ? 28  LYS   A CA  1 
ATOM   150  C  C   . LYS   A 1 28  ? -10.554 -9.208  -26.337 1.00 24.37 ? 28  LYS   A C   1 
ATOM   151  O  O   . LYS   A 1 28  ? -10.889 -9.728  -27.385 1.00 24.38 ? 28  LYS   A O   1 
ATOM   152  C  CB  . LYS   A 1 28  ? -9.154  -7.212  -26.672 1.00 28.26 ? 28  LYS   A CB  1 
ATOM   153  C  CG  . LYS   A 1 28  ? -8.998  -5.711  -26.733 1.00 35.30 ? 28  LYS   A CG  1 
ATOM   154  C  CD  . LYS   A 1 28  ? -9.671  -5.080  -27.945 1.00 42.21 ? 28  LYS   A CD  1 
ATOM   155  C  CE  . LYS   A 1 28  ? -9.722  -3.581  -27.867 1.00 44.90 ? 28  LYS   A CE  1 
ATOM   156  N  NZ  . LYS   A 1 28  ? -10.933 -3.148  -28.565 1.00 46.43 ? 28  LYS   A NZ  1 
ATOM   157  N  N   . VAL   A 1 29  ? -10.142 -9.926  -25.280 1.00 21.58 ? 29  VAL   A N   1 
ATOM   158  C  CA  . VAL   A 1 29  ? -10.152 -11.378 -25.309 1.00 21.84 ? 29  VAL   A CA  1 
ATOM   159  C  C   . VAL   A 1 29  ? -11.596 -11.869 -25.333 1.00 21.09 ? 29  VAL   A C   1 
ATOM   160  O  O   . VAL   A 1 29  ? -11.938 -12.804 -26.047 1.00 18.62 ? 29  VAL   A O   1 
ATOM   161  C  CB  . VAL   A 1 29  ? -9.357  -11.959 -24.117 1.00 22.26 ? 29  VAL   A CB  1 
ATOM   162  C  CG1 . VAL   A 1 29  ? -9.632  -13.445 -23.877 1.00 20.95 ? 29  VAL   A CG1 1 
ATOM   163  C  CG2 . VAL   A 1 29  ? -7.858  -11.706 -24.292 1.00 23.61 ? 29  VAL   A CG2 1 
ATOM   164  N  N   . ILE   A 1 30  ? -12.429 -11.273 -24.479 1.00 20.92 ? 30  ILE   A N   1 
ATOM   165  C  CA  . ILE   A 1 30  ? -13.834 -11.625 -24.412 1.00 20.89 ? 30  ILE   A CA  1 
ATOM   166  C  C   . ILE   A 1 30  ? -14.465 -11.397 -25.784 1.00 20.52 ? 30  ILE   A C   1 
ATOM   167  O  O   . ILE   A 1 30  ? -15.207 -12.246 -26.248 1.00 21.62 ? 30  ILE   A O   1 
ATOM   168  C  CB  . ILE   A 1 30  ? -14.533 -10.821 -23.297 1.00 22.12 ? 30  ILE   A CB  1 
ATOM   169  C  CG1 . ILE   A 1 30  ? -14.033 -11.234 -21.925 1.00 23.20 ? 30  ILE   A CG1 1 
ATOM   170  C  CG2 . ILE   A 1 30  ? -16.059 -10.907 -23.413 1.00 23.00 ? 30  ILE   A CG2 1 
ATOM   171  C  CD1 . ILE   A 1 30  ? -14.409 -10.264 -20.816 1.00 25.09 ? 30  ILE   A CD1 1 
ATOM   172  N  N   . ALA   A 1 31  ? -14.169 -10.262 -26.424 1.00 21.26 ? 31  ALA   A N   1 
ATOM   173  C  CA  . ALA   A 1 31  ? -14.695 -9.957  -27.748 1.00 21.35 ? 31  ALA   A CA  1 
ATOM   174  C  C   . ALA   A 1 31  ? -14.224 -10.977 -28.786 1.00 21.74 ? 31  ALA   A C   1 
ATOM   175  O  O   . ALA   A 1 31  ? -14.976 -11.336 -29.674 1.00 20.26 ? 31  ALA   A O   1 
ATOM   176  C  CB  . ALA   A 1 31  ? -14.286 -8.572  -28.182 1.00 22.79 ? 31  ALA   A CB  1 
ATOM   177  N  N   . LEU   A 1 32  ? -12.964 -11.413 -28.674 1.00 19.30 ? 32  LEU   A N   1 
ATOM   178  C  CA  . LEU   A 1 32  ? -12.426 -12.448 -29.531 1.00 18.89 ? 32  LEU   A CA  1 
ATOM   179  C  C   . LEU   A 1 32  ? -13.276 -13.698 -29.406 1.00 18.24 ? 32  LEU   A C   1 
ATOM   180  O  O   . LEU   A 1 32  ? -13.584 -14.354 -30.409 1.00 18.65 ? 32  LEU   A O   1 
ATOM   181  C  CB  . LEU   A 1 32  ? -10.974 -12.724 -29.155 1.00 18.75 ? 32  LEU   A CB  1 
ATOM   182  C  CG  . LEU   A 1 32  ? -10.310 -13.899 -29.876 1.00 19.77 ? 32  LEU   A CG  1 
ATOM   183  C  CD1 . LEU   A 1 32  ? -10.215 -13.575 -31.350 1.00 20.77 ? 32  LEU   A CD1 1 
ATOM   184  C  CD2 . LEU   A 1 32  ? -8.918  -14.209 -29.342 1.00 19.80 ? 32  LEU   A CD2 1 
ATOM   185  N  N   . CYS   A 1 33  ? -13.545 -14.092 -28.163 1.00 17.47 ? 33  CYS   A N   1 
ATOM   186  C  CA  . CYS   A 1 33  ? -14.339 -15.281 -27.920 1.00 18.74 ? 33  CYS   A CA  1 
ATOM   187  C  C   . CYS   A 1 33  ? -15.705 -15.142 -28.582 1.00 18.43 ? 33  CYS   A C   1 
ATOM   188  O  O   . CYS   A 1 33  ? -16.185 -16.082 -29.216 1.00 17.86 ? 33  CYS   A O   1 
ATOM   189  C  CB  . CYS   A 1 33  ? -14.514 -15.517 -26.437 1.00 19.39 ? 33  CYS   A CB  1 
ATOM   190  S  SG  . CYS   A 1 33  ? -12.958 -15.981 -25.653 1.00 21.91 ? 33  CYS   A SG  1 
ATOM   191  N  N   . HIS   A 1 34  ? -16.335 -13.972 -28.416 1.00 19.29 ? 34  HIS   A N   1 
ATOM   192  C  CA  . HIS   A 1 34  ? -17.615 -13.697 -29.074 1.00 21.41 ? 34  HIS   A CA  1 
ATOM   193  C  C   . HIS   A 1 34  ? -17.520 -13.833 -30.594 1.00 20.77 ? 34  HIS   A C   1 
ATOM   194  O  O   . HIS   A 1 34  ? -18.392 -14.428 -31.228 1.00 21.02 ? 34  HIS   A O   1 
ATOM   195  C  CB  . HIS   A 1 34  ? -18.144 -12.310 -28.690 1.00 22.61 ? 34  HIS   A CB  1 
ATOM   196  C  CG  . HIS   A 1 34  ? -18.473 -12.215 -27.252 1.00 24.58 ? 34  HIS   A CG  1 
ATOM   197  N  ND1 . HIS   A 1 34  ? -18.639 -11.011 -26.601 1.00 27.85 ? 34  HIS   A ND1 1 
ATOM   198  C  CD2 . HIS   A 1 34  ? -18.669 -13.159 -26.348 1.00 23.71 ? 34  HIS   A CD2 1 
ATOM   199  C  CE1 . HIS   A 1 34  ? -18.918 -11.245 -25.333 1.00 26.87 ? 34  HIS   A CE1 1 
ATOM   200  N  NE2 . HIS   A 1 34  ? -18.937 -12.543 -25.149 1.00 25.64 ? 34  HIS   A NE2 1 
ATOM   201  N  N   . GLN   A 1 35  ? -16.454 -13.307 -31.179 1.00 20.66 ? 35  GLN   A N   1 
ATOM   202  C  CA  . GLN   A 1 35  ? -16.296 -13.323 -32.625 1.00 22.36 ? 35  GLN   A CA  1 
ATOM   203  C  C   . GLN   A 1 35  ? -16.083 -14.735 -33.173 1.00 19.52 ? 35  GLN   A C   1 
ATOM   204  O  O   . GLN   A 1 35  ? -16.431 -15.016 -34.318 1.00 20.45 ? 35  GLN   A O   1 
ATOM   205  C  CB  . GLN   A 1 35  ? -15.100 -12.470 -33.006 1.00 25.88 ? 35  GLN   A CB  1 
ATOM   206  C  CG  . GLN   A 1 35  ? -15.304 -10.990 -32.731 1.00 31.70 ? 35  GLN   A CG  1 
ATOM   207  C  CD  . GLN   A 1 35  ? -14.022 -10.216 -32.910 1.00 40.84 ? 35  GLN   A CD  1 
ATOM   208  O  OE1 . GLN   A 1 35  ? -12.968 -10.783 -33.233 1.00 50.80 ? 35  GLN   A OE1 1 
ATOM   209  N  NE2 . GLN   A 1 35  ? -14.107 -8.910  -32.719 1.00 47.78 ? 35  GLN   A NE2 1 
ATOM   210  N  N   . ALA   A 1 36  ? -15.519 -15.626 -32.358 1.00 18.09 ? 36  ALA   A N   1 
ATOM   211  C  CA  . ALA   A 1 36  ? -15.263 -17.003 -32.770 1.00 17.23 ? 36  ALA   A CA  1 
ATOM   212  C  C   . ALA   A 1 36  ? -16.567 -17.786 -32.943 1.00 18.31 ? 36  ALA   A C   1 
ATOM   213  O  O   . ALA   A 1 36  ? -16.599 -18.810 -33.625 1.00 16.35 ? 36  ALA   A O   1 
ATOM   214  C  CB  . ALA   A 1 36  ? -14.374 -17.689 -31.751 1.00 16.13 ? 36  ALA   A CB  1 
ATOM   215  N  N   . LYS   A 1 37  ? -17.644 -17.330 -32.272 1.00 18.14 ? 37  LYS   A N   1 
ATOM   216  C  CA  . LYS   A 1 37  ? -18.956 -17.944 -32.420 1.00 18.92 ? 37  LYS   A CA  1 
ATOM   217  C  C   . LYS   A 1 37  ? -19.695 -17.183 -33.524 1.00 19.86 ? 37  LYS   A C   1 
ATOM   218  O  O   . LYS   A 1 37  ? -20.339 -16.170 -33.278 1.00 20.25 ? 37  LYS   A O   1 
ATOM   219  C  CB  . LYS   A 1 37  ? -19.678 -17.909 -31.076 1.00 20.18 ? 37  LYS   A CB  1 
ATOM   220  C  CG  . LYS   A 1 37  ? -21.092 -18.484 -31.072 1.00 19.90 ? 37  LYS   A CG  1 
ATOM   221  C  CD  . LYS   A 1 37  ? -21.752 -18.223 -29.717 1.00 20.42 ? 37  LYS   A CD  1 
ATOM   222  C  CE  . LYS   A 1 37  ? -23.081 -18.923 -29.636 1.00 22.45 ? 37  LYS   A CE  1 
ATOM   223  N  NZ  . LYS   A 1 37  ? -23.722 -18.579 -28.360 1.00 23.59 ? 37  LYS   A NZ  1 
ATOM   224  N  N   . THR   A 1 38  ? -19.489 -17.611 -34.766 1.00 18.94 ? 38  THR   A N   1 
ATOM   225  C  CA  . THR   A 1 38  ? -19.937 -16.835 -35.903 1.00 18.83 ? 38  THR   A CA  1 
ATOM   226  C  C   . THR   A 1 38  ? -21.320 -17.314 -36.316 1.00 18.50 ? 38  THR   A C   1 
ATOM   227  O  O   . THR   A 1 38  ? -21.743 -18.412 -35.980 1.00 18.26 ? 38  THR   A O   1 
ATOM   228  C  CB  . THR   A 1 38  ? -18.975 -16.932 -37.102 1.00 19.19 ? 38  THR   A CB  1 
ATOM   229  O  OG1 . THR   A 1 38  ? -19.412 -17.986 -37.964 1.00 18.21 ? 38  THR   A OG1 1 
ATOM   230  C  CG2 . THR   A 1 38  ? -17.504 -17.069 -36.695 1.00 19.07 ? 38  THR   A CG2 1 
ATOM   231  N  N   . PRO   A 1 39  ? -22.041 -16.529 -37.138 1.00 20.47 ? 39  PRO   A N   1 
ATOM   232  C  CA  . PRO   A 1 39  ? -23.358 -16.957 -37.626 1.00 20.72 ? 39  PRO   A CA  1 
ATOM   233  C  C   . PRO   A 1 39  ? -23.385 -18.253 -38.437 1.00 19.88 ? 39  PRO   A C   1 
ATOM   234  O  O   . PRO   A 1 39  ? -24.462 -18.804 -38.666 1.00 18.64 ? 39  PRO   A O   1 
ATOM   235  C  CB  . PRO   A 1 39  ? -23.819 -15.743 -38.444 1.00 22.17 ? 39  PRO   A CB  1 
ATOM   236  C  CG  . PRO   A 1 39  ? -23.035 -14.578 -37.899 1.00 23.59 ? 39  PRO   A CG  1 
ATOM   237  C  CD  . PRO   A 1 39  ? -21.691 -15.156 -37.532 1.00 22.17 ? 39  PRO   A CD  1 
ATOM   238  N  N   . VAL   A 1 40  ? -22.223 -18.687 -38.970 1.00 18.25 ? 40  VAL   A N   1 
ATOM   239  C  CA  . VAL   A 1 40  ? -22.168 -19.869 -39.814 1.00 18.11 ? 40  VAL   A CA  1 
ATOM   240  C  C   . VAL   A 1 40  ? -21.427 -21.012 -39.133 1.00 18.22 ? 40  VAL   A C   1 
ATOM   241  O  O   . VAL   A 1 40  ? -21.236 -22.042 -39.747 1.00 18.24 ? 40  VAL   A O   1 
ATOM   242  C  CB  . VAL   A 1 40  ? -21.559 -19.539 -41.190 1.00 20.43 ? 40  VAL   A CB  1 
ATOM   243  C  CG1 . VAL   A 1 40  ? -22.354 -18.418 -41.854 1.00 21.79 ? 40  VAL   A CG1 1 
ATOM   244  C  CG2 . VAL   A 1 40  ? -20.083 -19.183 -41.069 1.00 19.75 ? 40  VAL   A CG2 1 
ATOM   245  N  N   . GLY   A 1 41  ? -21.034 -20.832 -37.865 1.00 17.07 ? 41  GLY   A N   1 
ATOM   246  C  CA  . GLY   A 1 41  ? -20.347 -21.854 -37.114 1.00 16.63 ? 41  GLY   A CA  1 
ATOM   247  C  C   . GLY   A 1 41  ? -19.187 -21.270 -36.299 1.00 16.03 ? 41  GLY   A C   1 
ATOM   248  O  O   . GLY   A 1 41  ? -18.911 -20.076 -36.328 1.00 16.07 ? 41  GLY   A O   1 
ATOM   249  N  N   . ASN   A 1 42  ? -18.578 -22.153 -35.519 1.00 15.89 ? 42  ASN   A N   1 
ATOM   250  C  CA  . ASN   A 1 42  ? -17.503 -21.805 -34.617 1.00 16.49 ? 42  ASN   A CA  1 
ATOM   251  C  C   . ASN   A 1 42  ? -16.176 -22.007 -35.331 1.00 16.88 ? 42  ASN   A C   1 
ATOM   252  O  O   . ASN   A 1 42  ? -16.017 -22.948 -36.116 1.00 15.51 ? 42  ASN   A O   1 
ATOM   253  C  CB  . ASN   A 1 42  ? -17.553 -22.675 -33.378 1.00 16.85 ? 42  ASN   A CB  1 
ATOM   254  C  CG  . ASN   A 1 42  ? -18.806 -22.455 -32.555 1.00 18.49 ? 42  ASN   A CG  1 
ATOM   255  O  OD1 . ASN   A 1 42  ? -19.401 -21.385 -32.624 1.00 17.74 ? 42  ASN   A OD1 1 
ATOM   256  N  ND2 . ASN   A 1 42  ? -19.150 -23.415 -31.716 1.00 20.81 ? 42  ASN   A ND2 1 
ATOM   257  N  N   . THR   A 1 43  ? -15.210 -21.123 -35.052 1.00 16.29 ? 43  THR   A N   1 
ATOM   258  C  CA  . THR   A 1 43  ? -13.840 -21.403 -35.459 1.00 15.21 ? 43  THR   A CA  1 
ATOM   259  C  C   . THR   A 1 43  ? -13.354 -22.631 -34.693 1.00 15.07 ? 43  THR   A C   1 
ATOM   260  O  O   . THR   A 1 43  ? -13.993 -23.056 -33.720 1.00 15.04 ? 43  THR   A O   1 
ATOM   261  C  CB  . THR   A 1 43  ? -12.937 -20.191 -35.237 1.00 15.24 ? 43  THR   A CB  1 
ATOM   262  O  OG1 . THR   A 1 43  ? -12.886 -19.825 -33.865 1.00 15.73 ? 43  THR   A OG1 1 
ATOM   263  C  CG2 . THR   A 1 43  ? -13.400 -18.981 -36.022 1.00 16.18 ? 43  THR   A CG2 1 
ATOM   264  N  N   . ALA   A 1 44  ? -12.238 -23.225 -35.141 1.00 13.39 ? 44  ALA   A N   1 
ATOM   265  C  CA  . ALA   A 1 44  ? -11.672 -24.375 -34.453 1.00 13.29 ? 44  ALA   A CA  1 
ATOM   266  C  C   . ALA   A 1 44  ? -11.155 -23.983 -33.074 1.00 12.93 ? 44  ALA   A C   1 
ATOM   267  O  O   . ALA   A 1 44  ? -11.284 -24.753 -32.110 1.00 13.98 ? 44  ALA   A O   1 
ATOM   268  C  CB  . ALA   A 1 44  ? -10.548 -24.975 -35.292 1.00 12.85 ? 44  ALA   A CB  1 
ATOM   269  N  N   . ALA   A 1 45  ? -10.559 -22.783 -33.003 1.00 12.43 ? 45  ALA   A N   1 
ATOM   270  C  CA  . ALA   A 1 45  ? -9.854  -22.342 -31.812 1.00 12.97 ? 45  ALA   A CA  1 
ATOM   271  C  C   . ALA   A 1 45  ? -9.844  -20.837 -31.753 1.00 12.53 ? 45  ALA   A C   1 
ATOM   272  O  O   . ALA   A 1 45  ? -10.105 -20.154 -32.751 1.00 11.62 ? 45  ALA   A O   1 
ATOM   273  C  CB  . ALA   A 1 45  ? -8.432  -22.878 -31.800 1.00 12.50 ? 45  ALA   A CB  1 
ATOM   274  N  N   . ILE   A 1 46  ? -9.492  -20.348 -30.562 1.00 12.14 ? 46  ILE   A N   1 
ATOM   275  C  CA  . ILE   A 1 46  ? -9.009  -19.000 -30.397 1.00 13.81 ? 46  ILE   A CA  1 
ATOM   276  C  C   . ILE   A 1 46  ? -7.556  -19.128 -29.939 1.00 13.71 ? 46  ILE   A C   1 
ATOM   277  O  O   . ILE   A 1 46  ? -7.193  -20.128 -29.306 1.00 14.15 ? 46  ILE   A O   1 
ATOM   278  C  CB  . ILE   A 1 46  ? -9.878  -18.196 -29.421 1.00 15.93 ? 46  ILE   A CB  1 
ATOM   279  C  CG1 . ILE   A 1 46  ? -9.953  -18.838 -28.034 1.00 18.99 ? 46  ILE   A CG1 1 
ATOM   280  C  CG2 . ILE   A 1 46  ? -11.275 -18.001 -30.005 1.00 16.90 ? 46  ILE   A CG2 1 
ATOM   281  C  CD1 . ILE   A 1 46  ? -9.037  -18.169 -27.038 1.00 23.48 ? 46  ILE   A CD1 1 
ATOM   282  N  N   . SER   A 1 47  ? -6.791  -18.097 -30.251 1.00 12.93 ? 47  SER   A N   1 
ATOM   283  C  CA  A SER   A 1 47  ? -5.364  -18.046 -29.969 0.50 13.24 ? 47  SER   A CA  1 
ATOM   284  C  CA  B SER   A 1 47  ? -5.368  -18.065 -29.948 0.50 14.10 ? 47  SER   A CA  1 
ATOM   285  C  C   . SER   A 1 47  ? -5.078  -16.793 -29.162 1.00 13.57 ? 47  SER   A C   1 
ATOM   286  O  O   . SER   A 1 47  ? -5.334  -15.689 -29.635 1.00 13.89 ? 47  SER   A O   1 
ATOM   287  C  CB  A SER   A 1 47  ? -4.561  -18.030 -31.244 0.50 13.61 ? 47  SER   A CB  1 
ATOM   288  C  CB  B SER   A 1 47  ? -4.502  -18.161 -31.200 0.50 15.63 ? 47  SER   A CB  1 
ATOM   289  O  OG  A SER   A 1 47  ? -4.438  -19.343 -31.738 0.50 13.48 ? 47  SER   A OG  1 
ATOM   290  O  OG  B SER   A 1 47  ? -3.161  -18.474 -30.827 0.50 18.59 ? 47  SER   A OG  1 
ATOM   291  N  N   . VAL   A 1 48  ? -4.547  -16.973 -27.948 1.00 13.76 ? 48  VAL   A N   1 
ATOM   292  C  CA  . VAL   A 1 48  ? -4.325  -15.875 -27.029 1.00 13.37 ? 48  VAL   A CA  1 
ATOM   293  C  C   . VAL   A 1 48  ? -2.988  -16.112 -26.358 1.00 13.73 ? 48  VAL   A C   1 
ATOM   294  O  O   . VAL   A 1 48  ? -2.461  -17.215 -26.391 1.00 13.79 ? 48  VAL   A O   1 
ATOM   295  C  CB  . VAL   A 1 48  ? -5.444  -15.746 -25.971 1.00 14.74 ? 48  VAL   A CB  1 
ATOM   296  C  CG1 . VAL   A 1 48  ? -6.783  -15.405 -26.627 1.00 15.05 ? 48  VAL   A CG1 1 
ATOM   297  C  CG2 . VAL   A 1 48  ? -5.546  -17.000 -25.113 1.00 15.39 ? 48  VAL   A CG2 1 
ATOM   298  N  N   . TYR   A 1 49  ? -2.448  -15.067 -25.746 1.00 13.05 ? 49  TYR   A N   1 
ATOM   299  C  CA  . TYR   A 1 49  ? -1.291  -15.239 -24.887 1.00 14.47 ? 49  TYR   A CA  1 
ATOM   300  C  C   . TYR   A 1 49  ? -1.668  -16.028 -23.628 1.00 13.33 ? 49  TYR   A C   1 
ATOM   301  O  O   . TYR   A 1 49  ? -2.813  -16.038 -23.199 1.00 13.55 ? 49  TYR   A O   1 
ATOM   302  C  CB  . TYR   A 1 49  ? -0.704  -13.886 -24.464 1.00 16.95 ? 49  TYR   A CB  1 
ATOM   303  C  CG  . TYR   A 1 49  ? 0.076   -13.188 -25.576 1.00 21.01 ? 49  TYR   A CG  1 
ATOM   304  C  CD1 . TYR   A 1 49  ? 0.972   -13.869 -26.372 1.00 26.03 ? 49  TYR   A CD1 1 
ATOM   305  C  CD2 . TYR   A 1 49  ? -0.156  -11.861 -25.875 1.00 30.61 ? 49  TYR   A CD2 1 
ATOM   306  C  CE1 . TYR   A 1 49  ? 1.675   -13.238 -27.388 1.00 27.89 ? 49  TYR   A CE1 1 
ATOM   307  C  CE2 . TYR   A 1 49  ? 0.530   -11.213 -26.893 1.00 31.65 ? 49  TYR   A CE2 1 
ATOM   308  C  CZ  . TYR   A 1 49  ? 1.453   -11.909 -27.654 1.00 32.97 ? 49  TYR   A CZ  1 
ATOM   309  O  OH  . TYR   A 1 49  ? 2.181   -11.325 -28.662 1.00 40.36 ? 49  TYR   A OH  1 
ATOM   310  N  N   . PRO   A 1 50  ? -0.697  -16.744 -23.014 1.00 13.28 ? 50  PRO   A N   1 
ATOM   311  C  CA  . PRO   A 1 50  ? -1.012  -17.660 -21.916 1.00 12.80 ? 50  PRO   A CA  1 
ATOM   312  C  C   . PRO   A 1 50  ? -1.842  -17.047 -20.798 1.00 13.07 ? 50  PRO   A C   1 
ATOM   313  O  O   . PRO   A 1 50  ? -2.796  -17.654 -20.327 1.00 11.78 ? 50  PRO   A O   1 
ATOM   314  C  CB  . PRO   A 1 50  ? 0.385   -18.081 -21.466 1.00 12.81 ? 50  PRO   A CB  1 
ATOM   315  C  CG  . PRO   A 1 50  ? 1.205   -18.083 -22.733 1.00 13.18 ? 50  PRO   A CG  1 
ATOM   316  C  CD  . PRO   A 1 50  ? 0.696   -16.848 -23.449 1.00 13.02 ? 50  PRO   A CD  1 
ATOM   317  N  N   . ARG   A 1 51  ? -1.497  -15.820 -20.417 1.00 13.30 ? 51  ARG   A N   1 
ATOM   318  C  CA  . ARG   A 1 51  ? -2.164  -15.189 -19.293 1.00 14.64 ? 51  ARG   A CA  1 
ATOM   319  C  C   . ARG   A 1 51  ? -3.667  -14.977 -19.531 1.00 14.43 ? 51  ARG   A C   1 
ATOM   320  O  O   . ARG   A 1 51  ? -4.419  -14.765 -18.558 1.00 14.01 ? 51  ARG   A O   1 
ATOM   321  C  CB  . ARG   A 1 51  ? -1.482  -13.859 -18.970 1.00 17.54 ? 51  ARG   A CB  1 
ATOM   322  C  CG  . ARG   A 1 51  ? -1.599  -12.799 -20.053 1.00 22.40 ? 51  ARG   A CG  1 
ATOM   323  C  CD  . ARG   A 1 51  ? -0.923  -11.498 -19.636 1.00 27.35 ? 51  ARG   A CD  1 
ATOM   324  N  NE  . ARG   A 1 51  ? -0.617  -10.629 -20.761 1.00 36.36 ? 51  ARG   A NE  1 
ATOM   325  C  CZ  . ARG   A 1 51  ? 0.396   -10.797 -21.624 1.00 41.18 ? 51  ARG   A CZ  1 
ATOM   326  N  NH1 . ARG   A 1 51  ? 1.301   -11.762 -21.489 1.00 39.17 ? 51  ARG   A NH1 1 
ATOM   327  N  NH2 . ARG   A 1 51  ? 0.519   -9.958  -22.634 1.00 49.54 ? 51  ARG   A NH2 1 
ATOM   328  N  N   . SER   A 1 52  ? -4.108  -15.013 -20.800 1.00 14.10 ? 52  SER   A N   1 
ATOM   329  C  CA  . SER   A 1 52  ? -5.476  -14.752 -21.190 1.00 14.06 ? 52  SER   A CA  1 
ATOM   330  C  C   . SER   A 1 52  ? -6.312  -16.021 -21.233 1.00 13.17 ? 52  SER   A C   1 
ATOM   331  O  O   . SER   A 1 52  ? -7.516  -15.948 -21.436 1.00 13.62 ? 52  SER   A O   1 
ATOM   332  C  CB  . SER   A 1 52  ? -5.511  -14.054 -22.534 1.00 15.93 ? 52  SER   A CB  1 
ATOM   333  O  OG  . SER   A 1 52  ? -4.887  -12.789 -22.452 1.00 16.75 ? 52  SER   A OG  1 
ATOM   334  N  N   . ILE   A 1 53  ? -5.700  -17.182 -21.001 1.00 12.37 ? 53  ILE   A N   1 
ATOM   335  C  CA  . ILE   A 1 53  ? -6.415  -18.427 -21.176 1.00 13.09 ? 53  ILE   A CA  1 
ATOM   336  C  C   . ILE   A 1 53  ? -7.564  -18.531 -20.173 1.00 12.72 ? 53  ILE   A C   1 
ATOM   337  O  O   . ILE   A 1 53  ? -8.657  -18.915 -20.544 1.00 12.30 ? 53  ILE   A O   1 
ATOM   338  C  CB  . ILE   A 1 53  ? -5.452  -19.626 -21.107 1.00 13.33 ? 53  ILE   A CB  1 
ATOM   339  C  CG1 . ILE   A 1 53  ? -4.496  -19.619 -22.328 1.00 13.74 ? 53  ILE   A CG1 1 
ATOM   340  C  CG2 . ILE   A 1 53  ? -6.222  -20.945 -20.986 1.00 14.17 ? 53  ILE   A CG2 1 
ATOM   341  C  CD1 . ILE   A 1 53  ? -3.366  -20.611 -22.189 1.00 14.23 ? 53  ILE   A CD1 1 
ATOM   342  N  N   . PRO   A 1 54  ? -7.392  -18.230 -18.870 1.00 13.62 ? 54  PRO   A N   1 
ATOM   343  C  CA  . PRO   A 1 54  ? -8.506  -18.410 -17.936 1.00 13.72 ? 54  PRO   A CA  1 
ATOM   344  C  C   . PRO   A 1 54  ? -9.753  -17.588 -18.260 1.00 14.72 ? 54  PRO   A C   1 
ATOM   345  O  O   . PRO   A 1 54  ? -10.866 -18.109 -18.257 1.00 14.72 ? 54  PRO   A O   1 
ATOM   346  C  CB  . PRO   A 1 54  ? -7.885  -18.013 -16.580 1.00 14.30 ? 54  PRO   A CB  1 
ATOM   347  C  CG  . PRO   A 1 54  ? -6.423  -18.362 -16.765 1.00 14.26 ? 54  PRO   A CG  1 
ATOM   348  C  CD  . PRO   A 1 54  ? -6.120  -17.931 -18.193 1.00 13.95 ? 54  PRO   A CD  1 
ATOM   349  N  N   . ILE   A 1 55  ? -9.565  -16.314 -18.613 1.00 14.56 ? 55  ILE   A N   1 
ATOM   350  C  CA  . ILE   A 1 55  ? -10.726 -15.503 -18.934 1.00 16.50 ? 55  ILE   A CA  1 
ATOM   351  C  C   . ILE   A 1 55  ? -11.330 -15.920 -20.274 1.00 15.48 ? 55  ILE   A C   1 
ATOM   352  O  O   . ILE   A 1 55  ? -12.559 -15.862 -20.439 1.00 15.46 ? 55  ILE   A O   1 
ATOM   353  C  CB  . ILE   A 1 55  ? -10.424 -14.001 -18.876 1.00 18.85 ? 55  ILE   A CB  1 
ATOM   354  C  CG1 . ILE   A 1 55  ? -11.739 -13.175 -18.828 1.00 21.81 ? 55  ILE   A CG1 1 
ATOM   355  C  CG2 . ILE   A 1 55  ? -9.565  -13.554 -20.034 1.00 18.41 ? 55  ILE   A CG2 1 
ATOM   356  C  CD1 . ILE   A 1 55  ? -12.691 -13.589 -17.727 1.00 23.50 ? 55  ILE   A CD1 1 
ATOM   357  N  N   . ALA   A 1 56  ? -10.504 -16.386 -21.211 1.00 13.79 ? 56  ALA   A N   1 
ATOM   358  C  CA  . ALA   A 1 56  ? -11.045 -16.951 -22.441 1.00 14.36 ? 56  ALA   A CA  1 
ATOM   359  C  C   . ALA   A 1 56  ? -11.919 -18.170 -22.178 1.00 13.89 ? 56  ALA   A C   1 
ATOM   360  O  O   . ALA   A 1 56  ? -13.006 -18.287 -22.741 1.00 14.73 ? 56  ALA   A O   1 
ATOM   361  C  CB  . ALA   A 1 56  ? -9.910  -17.295 -23.393 1.00 15.80 ? 56  ALA   A CB  1 
ATOM   362  N  N   . ARG   A 1 57  ? -11.452 -19.073 -21.301 1.00 14.34 ? 57  ARG   A N   1 
ATOM   363  C  CA  . ARG   A 1 57  ? -12.162 -20.303 -21.031 1.00 15.61 ? 57  ARG   A CA  1 
ATOM   364  C  C   . ARG   A 1 57  ? -13.515 -19.970 -20.396 1.00 16.32 ? 57  ARG   A C   1 
ATOM   365  O  O   . ARG   A 1 57  ? -14.533 -20.540 -20.772 1.00 17.45 ? 57  ARG   A O   1 
ATOM   366  C  CB  . ARG   A 1 57  ? -11.348 -21.227 -20.127 1.00 15.80 ? 57  ARG   A CB  1 
ATOM   367  C  CG  . ARG   A 1 57  ? -12.044 -22.536 -19.788 1.00 19.19 ? 57  ARG   A CG  1 
ATOM   368  C  CD  . ARG   A 1 57  ? -12.022 -23.500 -20.932 1.00 22.27 ? 57  ARG   A CD  1 
ATOM   369  N  NE  . ARG   A 1 57  ? -10.666 -24.046 -21.095 1.00 21.48 ? 57  ARG   A NE  1 
ATOM   370  C  CZ  . ARG   A 1 57  ? -10.240 -24.677 -22.178 1.00 21.91 ? 57  ARG   A CZ  1 
ATOM   371  N  NH1 . ARG   A 1 57  ? -11.016 -24.815 -23.251 1.00 21.54 ? 57  ARG   A NH1 1 
ATOM   372  N  NH2 . ARG   A 1 57  ? -9.013  -25.164 -22.191 1.00 19.89 ? 57  ARG   A NH2 1 
ATOM   373  N  N   . LYS   A 1 58  ? -13.499 -19.018 -19.463 1.00 16.25 ? 58  LYS   A N   1 
ATOM   374  C  CA  . LYS   A 1 58  ? -14.731 -18.615 -18.804 1.00 17.54 ? 58  LYS   A CA  1 
ATOM   375  C  C   . LYS   A 1 58  ? -15.736 -18.098 -19.828 1.00 17.50 ? 58  LYS   A C   1 
ATOM   376  O  O   . LYS   A 1 58  ? -16.908 -18.503 -19.815 1.00 17.76 ? 58  LYS   A O   1 
ATOM   377  C  CB  . LYS   A 1 58  ? -14.436 -17.576 -17.726 1.00 18.44 ? 58  LYS   A CB  1 
ATOM   378  C  CG  . LYS   A 1 58  ? -15.643 -17.197 -16.880 1.00 19.56 ? 58  LYS   A CG  1 
ATOM   379  C  CD  . LYS   A 1 58  ? -15.271 -16.139 -15.838 1.00 21.25 ? 58  LYS   A CD  1 
ATOM   380  C  CE  . LYS   A 1 58  ? -16.393 -15.851 -14.867 1.00 25.01 ? 58  LYS   A CE  1 
ATOM   381  N  NZ  . LYS   A 1 58  ? -15.923 -15.034 -13.740 1.00 24.86 ? 58  LYS   A NZ  1 
ATOM   382  N  N   . THR   A 1 59  ? -15.249 -17.263 -20.760 1.00 16.10 ? 59  THR   A N   1 
ATOM   383  C  CA  . THR   A 1 59  ? -16.115 -16.651 -21.742 1.00 17.72 ? 59  THR   A CA  1 
ATOM   384  C  C   . THR   A 1 59  ? -16.682 -17.710 -22.691 1.00 19.74 ? 59  THR   A C   1 
ATOM   385  O  O   . THR   A 1 59  ? -17.879 -17.691 -23.004 1.00 20.40 ? 59  THR   A O   1 
ATOM   386  C  CB  . THR   A 1 59  ? -15.346 -15.561 -22.466 1.00 18.74 ? 59  THR   A CB  1 
ATOM   387  O  OG1 . THR   A 1 59  ? -14.796 -14.667 -21.511 1.00 19.20 ? 59  THR   A OG1 1 
ATOM   388  C  CG2 . THR   A 1 59  ? -16.247 -14.782 -23.398 1.00 19.70 ? 59  THR   A CG2 1 
ATOM   389  N  N   . LEU   A 1 60  ? -15.827 -18.614 -23.199 1.00 17.71 ? 60  LEU   A N   1 
ATOM   390  C  CA  . LEU   A 1 60  ? -16.308 -19.653 -24.098 1.00 18.23 ? 60  LEU   A CA  1 
ATOM   391  C  C   . LEU   A 1 60  ? -17.372 -20.524 -23.425 1.00 19.74 ? 60  LEU   A C   1 
ATOM   392  O  O   . LEU   A 1 60  ? -18.345 -20.928 -24.061 1.00 20.32 ? 60  LEU   A O   1 
ATOM   393  C  CB  . LEU   A 1 60  ? -15.121 -20.486 -24.587 1.00 17.39 ? 60  LEU   A CB  1 
ATOM   394  C  CG  . LEU   A 1 60  ? -14.126 -19.734 -25.481 1.00 17.02 ? 60  LEU   A CG  1 
ATOM   395  C  CD1 . LEU   A 1 60  ? -12.868 -20.587 -25.705 1.00 16.73 ? 60  LEU   A CD1 1 
ATOM   396  C  CD2 . LEU   A 1 60  ? -14.720 -19.349 -26.793 1.00 17.03 ? 60  LEU   A CD2 1 
ATOM   397  N  N   . LYS   A 1 61  ? -17.173 -20.858 -22.152 1.00 21.74 ? 61  LYS   A N   1 
ATOM   398  C  CA  . LYS   A 1 61  ? -18.155 -21.646 -21.418 1.00 23.18 ? 61  LYS   A CA  1 
ATOM   399  C  C   . LYS   A 1 61  ? -19.462 -20.870 -21.264 1.00 23.03 ? 61  LYS   A C   1 
ATOM   400  O  O   . LYS   A 1 61  ? -20.528 -21.428 -21.512 1.00 23.26 ? 61  LYS   A O   1 
ATOM   401  C  CB  . LYS   A 1 61  ? -17.636 -22.049 -20.036 1.00 24.94 ? 61  LYS   A CB  1 
ATOM   402  C  CG  . LYS   A 1 61  ? -16.520 -23.088 -20.052 1.00 28.93 ? 61  LYS   A CG  1 
ATOM   403  C  CD  . LYS   A 1 61  ? -15.986 -23.345 -18.644 1.00 35.64 ? 61  LYS   A CD  1 
ATOM   404  C  CE  . LYS   A 1 61  ? -14.939 -24.409 -18.597 1.00 41.75 ? 61  LYS   A CE  1 
ATOM   405  N  NZ  . LYS   A 1 61  ? -14.196 -24.388 -17.331 1.00 45.08 ? 61  LYS   A NZ  1 
ATOM   406  N  N   . GLU   A 1 62  ? -19.378 -19.574 -20.928 1.00 21.71 ? 62  GLU   A N   1 
ATOM   407  C  CA  . GLU   A 1 62  ? -20.575 -18.787 -20.669 1.00 24.66 ? 62  GLU   A CA  1 
ATOM   408  C  C   . GLU   A 1 62  ? -21.412 -18.617 -21.933 1.00 23.81 ? 62  GLU   A C   1 
ATOM   409  O  O   . GLU   A 1 62  ? -22.628 -18.572 -21.841 1.00 23.59 ? 62  GLU   A O   1 
ATOM   410  C  CB  . GLU   A 1 62  ? -20.289 -17.395 -20.117 1.00 28.56 ? 62  GLU   A CB  1 
ATOM   411  C  CG  . GLU   A 1 62  ? -19.918 -17.460 -18.643 1.00 36.28 ? 62  GLU   A CG  1 
ATOM   412  C  CD  . GLU   A 1 62  ? -19.597 -16.121 -17.996 1.00 41.45 ? 62  GLU   A CD  1 
ATOM   413  O  OE1 . GLU   A 1 62  ? -19.659 -15.063 -18.652 1.00 46.40 ? 62  GLU   A OE1 1 
ATOM   414  O  OE2 . GLU   A 1 62  ? -19.258 -16.178 -16.805 1.00 46.54 ? 62  GLU   A OE2 1 
ATOM   415  N  N   . GLN   A 1 63  ? -20.777 -18.533 -23.114 1.00 21.79 ? 63  GLN   A N   1 
ATOM   416  C  CA  . GLN   A 1 63  ? -21.537 -18.380 -24.343 1.00 21.34 ? 63  GLN   A CA  1 
ATOM   417  C  C   . GLN   A 1 63  ? -21.929 -19.720 -24.969 1.00 20.38 ? 63  GLN   A C   1 
ATOM   418  O  O   . GLN   A 1 63  ? -22.469 -19.740 -26.060 1.00 23.41 ? 63  GLN   A O   1 
ATOM   419  C  CB  . GLN   A 1 63  ? -20.760 -17.528 -25.343 1.00 21.02 ? 63  GLN   A CB  1 
ATOM   420  C  CG  . GLN   A 1 63  ? -19.532 -18.224 -25.929 1.00 20.15 ? 63  GLN   A CG  1 
ATOM   421  C  CD  . GLN   A 1 63  ? -18.811 -17.331 -26.906 1.00 21.12 ? 63  GLN   A CD  1 
ATOM   422  O  OE1 . GLN   A 1 63  ? -19.016 -16.118 -26.941 1.00 22.25 ? 63  GLN   A OE1 1 
ATOM   423  N  NE2 . GLN   A 1 63  ? -17.955 -17.924 -27.731 1.00 19.57 ? 63  GLN   A NE2 1 
ATOM   424  N  N   . GLY   A 1 64  ? -21.687 -20.827 -24.286 1.00 21.62 ? 64  GLY   A N   1 
ATOM   425  C  CA  . GLY   A 1 64  ? -22.124 -22.127 -24.748 1.00 23.75 ? 64  GLY   A CA  1 
ATOM   426  C  C   . GLY   A 1 64  ? -21.293 -22.664 -25.915 1.00 23.85 ? 64  GLY   A C   1 
ATOM   427  O  O   . GLY   A 1 64  ? -21.797 -23.464 -26.692 1.00 24.65 ? 64  GLY   A O   1 
ATOM   428  N  N   . THR   A 1 65  ? -20.000 -22.287 -26.002 1.00 22.30 ? 65  THR   A N   1 
ATOM   429  C  CA  . THR   A 1 65  ? -19.120 -22.865 -27.012 1.00 20.42 ? 65  THR   A CA  1 
ATOM   430  C  C   . THR   A 1 65  ? -17.884 -23.439 -26.338 1.00 20.70 ? 65  THR   A C   1 
ATOM   431  O  O   . THR   A 1 65  ? -16.755 -23.089 -26.702 1.00 19.37 ? 65  THR   A O   1 
ATOM   432  C  CB  . THR   A 1 65  ? -18.733 -21.837 -28.078 1.00 19.84 ? 65  THR   A CB  1 
ATOM   433  O  OG1 . THR   A 1 65  ? -17.946 -20.843 -27.428 1.00 18.79 ? 65  THR   A OG1 1 
ATOM   434  C  CG2 . THR   A 1 65  ? -19.957 -21.288 -28.798 1.00 20.51 ? 65  THR   A CG2 1 
ATOM   435  N  N   . PRO   A 1 66  ? -18.052 -24.408 -25.426 1.00 22.77 ? 66  PRO   A N   1 
ATOM   436  C  CA  . PRO   A 1 66  ? -16.920 -24.988 -24.713 1.00 23.36 ? 66  PRO   A CA  1 
ATOM   437  C  C   . PRO   A 1 66  ? -16.003 -25.867 -25.566 1.00 23.38 ? 66  PRO   A C   1 
ATOM   438  O  O   . PRO   A 1 66  ? -14.895 -26.177 -25.127 1.00 25.50 ? 66  PRO   A O   1 
ATOM   439  C  CB  . PRO   A 1 66  ? -17.633 -25.777 -23.586 1.00 24.74 ? 66  PRO   A CB  1 
ATOM   440  C  CG  . PRO   A 1 66  ? -18.923 -26.214 -24.221 1.00 24.61 ? 66  PRO   A CG  1 
ATOM   441  C  CD  . PRO   A 1 66  ? -19.347 -24.993 -25.002 1.00 25.41 ? 66  PRO   A CD  1 
ATOM   442  N  N   . GLU   A 1 67  ? -16.428 -26.224 -26.779 1.00 21.32 ? 67  GLU   A N   1 
ATOM   443  C  CA  . GLU   A 1 67  ? -15.614 -27.054 -27.648 1.00 22.67 ? 67  GLU   A CA  1 
ATOM   444  C  C   . GLU   A 1 67  ? -14.701 -26.203 -28.535 1.00 22.28 ? 67  GLU   A C   1 
ATOM   445  O  O   . GLU   A 1 67  ? -13.901 -26.767 -29.276 1.00 25.01 ? 67  GLU   A O   1 
ATOM   446  C  CB  . GLU   A 1 67  ? -16.462 -27.999 -28.505 1.00 28.77 ? 67  GLU   A CB  1 
ATOM   447  C  CG  . GLU   A 1 67  ? -17.247 -29.011 -27.671 1.00 36.63 ? 67  GLU   A CG  1 
ATOM   448  C  CD  . GLU   A 1 67  ? -18.026 -30.085 -28.441 1.00 49.00 ? 67  GLU   A CD  1 
ATOM   449  O  OE1 . GLU   A 1 67  ? -17.761 -30.342 -29.645 1.00 54.88 ? 67  GLU   A OE1 1 
ATOM   450  O  OE2 . GLU   A 1 67  ? -18.935 -30.690 -27.816 1.00 59.57 ? 67  GLU   A OE2 1 
ATOM   451  N  N   . ILE   A 1 68  ? -14.817 -24.864 -28.512 1.00 18.69 ? 68  ILE   A N   1 
ATOM   452  C  CA  . ILE   A 1 68  ? -13.822 -24.043 -29.186 1.00 17.28 ? 68  ILE   A CA  1 
ATOM   453  C  C   . ILE   A 1 68  ? -12.518 -24.188 -28.402 1.00 16.13 ? 68  ILE   A C   1 
ATOM   454  O  O   . ILE   A 1 68  ? -12.496 -23.974 -27.208 1.00 16.77 ? 68  ILE   A O   1 
ATOM   455  C  CB  . ILE   A 1 68  ? -14.255 -22.574 -29.325 1.00 16.22 ? 68  ILE   A CB  1 
ATOM   456  C  CG1 . ILE   A 1 68  ? -15.521 -22.435 -30.204 1.00 15.91 ? 68  ILE   A CG1 1 
ATOM   457  C  CG2 . ILE   A 1 68  ? -13.116 -21.716 -29.863 1.00 17.07 ? 68  ILE   A CG2 1 
ATOM   458  C  CD1 . ILE   A 1 68  ? -15.970 -20.988 -30.383 1.00 16.66 ? 68  ILE   A CD1 1 
ATOM   459  N  N   . ARG   A 1 69  ? -11.438 -24.589 -29.078 1.00 14.64 ? 69  ARG   A N   1 
ATOM   460  C  CA  . ARG   A 1 69  ? -10.187 -24.889 -28.402 1.00 14.76 ? 69  ARG   A CA  1 
ATOM   461  C  C   . ARG   A 1 69  ? -9.483  -23.584 -28.053 1.00 14.42 ? 69  ARG   A C   1 
ATOM   462  O  O   . ARG   A 1 69  ? -9.689  -22.547 -28.710 1.00 14.03 ? 69  ARG   A O   1 
ATOM   463  C  CB  . ARG   A 1 69  ? -9.271  -25.763 -29.263 1.00 16.41 ? 69  ARG   A CB  1 
ATOM   464  C  CG  . ARG   A 1 69  ? -9.905  -27.076 -29.719 1.00 21.18 ? 69  ARG   A CG  1 
ATOM   465  C  CD  . ARG   A 1 69  ? -9.310  -27.430 -31.087 1.00 29.61 ? 69  ARG   A CD  1 
ATOM   466  N  NE  . ARG   A 1 69  ? -9.828  -28.628 -31.760 1.00 36.55 ? 69  ARG   A NE  1 
ATOM   467  C  CZ  . ARG   A 1 69  ? -10.925 -28.669 -32.510 1.00 39.66 ? 69  ARG   A CZ  1 
ATOM   468  N  NH1 . ARG   A 1 69  ? -11.646 -27.572 -32.712 1.00 36.88 ? 69  ARG   A NH1 1 
ATOM   469  N  NH2 . ARG   A 1 69  ? -11.315 -29.827 -33.023 1.00 41.58 ? 69  ARG   A NH2 1 
ATOM   470  N  N   . ILE   A 1 70  ? -8.654  -23.657 -27.004 1.00 12.16 ? 70  ILE   A N   1 
ATOM   471  C  CA  . ILE   A 1 70  ? -7.830  -22.517 -26.659 1.00 12.83 ? 70  ILE   A CA  1 
ATOM   472  C  C   . ILE   A 1 70  ? -6.375  -22.855 -26.969 1.00 11.93 ? 70  ILE   A C   1 
ATOM   473  O  O   . ILE   A 1 70  ? -5.780  -23.739 -26.354 1.00 12.11 ? 70  ILE   A O   1 
ATOM   474  C  CB  . ILE   A 1 70  ? -8.011  -22.045 -25.207 1.00 14.31 ? 70  ILE   A CB  1 
ATOM   475  C  CG1 . ILE   A 1 70  ? -9.441  -21.640 -24.926 1.00 14.22 ? 70  ILE   A CG1 1 
ATOM   476  C  CG2 . ILE   A 1 70  ? -7.059  -20.870 -24.949 1.00 14.86 ? 70  ILE   A CG2 1 
ATOM   477  C  CD1 . ILE   A 1 70  ? -9.683  -21.347 -23.451 1.00 15.15 ? 70  ILE   A CD1 1 
ATOM   478  N  N   . ALA   A 1 71  ? -5.823  -22.145 -27.951 1.00 11.12 ? 71  ALA   A N   1 
ATOM   479  C  CA  . ALA   A 1 71  ? -4.429  -22.297 -28.316 1.00 11.14 ? 71  ALA   A CA  1 
ATOM   480  C  C   . ALA   A 1 71  ? -3.646  -21.098 -27.804 1.00 11.07 ? 71  ALA   A C   1 
ATOM   481  O  O   . ALA   A 1 71  ? -4.198  -20.000 -27.646 1.00 12.49 ? 71  ALA   A O   1 
ATOM   482  C  CB  . ALA   A 1 71  ? -4.263  -22.428 -29.806 1.00 12.79 ? 71  ALA   A CB  1 
ATOM   483  N  N   . THR   A 1 72  ? -2.356  -21.309 -27.524 1.00 10.17 ? 72  THR   A N   1 
ATOM   484  C  CA  . THR   A 1 72  ? -1.508  -20.203 -27.133 1.00 10.30 ? 72  THR   A CA  1 
ATOM   485  C  C   . THR   A 1 72  ? -0.125  -20.410 -27.745 1.00 11.01 ? 72  THR   A C   1 
ATOM   486  O  O   . THR   A 1 72  ? 0.058   -21.277 -28.586 1.00 12.04 ? 72  THR   A O   1 
ATOM   487  C  CB  . THR   A 1 72  ? -1.491  -20.147 -25.597 1.00 10.43 ? 72  THR   A CB  1 
ATOM   488  O  OG1 . THR   A 1 72  ? -0.856  -18.948 -25.209 1.00 9.96  ? 72  THR   A OG1 1 
ATOM   489  C  CG2 . THR   A 1 72  ? -0.749  -21.308 -24.970 1.00 11.36 ? 72  THR   A CG2 1 
ATOM   490  N  N   . VAL   A 1 73  ? 0.824   -19.547 -27.383 1.00 11.68 ? 73  VAL   A N   1 
ATOM   491  C  CA  . VAL   A 1 73  ? 2.138   -19.517 -27.999 1.00 11.79 ? 73  VAL   A CA  1 
ATOM   492  C  C   . VAL   A 1 73  ? 3.195   -19.528 -26.897 1.00 11.17 ? 73  VAL   A C   1 
ATOM   493  O  O   . VAL   A 1 73  ? 3.017   -18.867 -25.864 1.00 11.64 ? 73  VAL   A O   1 
ATOM   494  C  CB  . VAL   A 1 73  ? 2.342   -18.292 -28.901 1.00 13.28 ? 73  VAL   A CB  1 
ATOM   495  C  CG1 . VAL   A 1 73  ? 1.621   -18.450 -30.247 1.00 12.81 ? 73  VAL   A CG1 1 
ATOM   496  C  CG2 . VAL   A 1 73  ? 1.942   -16.994 -28.211 1.00 14.19 ? 73  VAL   A CG2 1 
ATOM   497  N  N   . THR   A 1 74  ? 4.292   -20.259 -27.147 1.00 10.30 ? 74  THR   A N   1 
ATOM   498  C  CA  . THR   A 1 74  ? 5.452   -20.225 -26.274 1.00 10.34 ? 74  THR   A CA  1 
ATOM   499  C  C   . THR   A 1 74  ? 6.744   -20.143 -27.095 1.00 10.20 ? 74  THR   A C   1 
ATOM   500  O  O   . THR   A 1 74  ? 6.756   -20.369 -28.310 1.00 10.28 ? 74  THR   A O   1 
ATOM   501  C  CB  . THR   A 1 74  ? 5.475   -21.426 -25.332 1.00 10.53 ? 74  THR   A CB  1 
ATOM   502  O  OG1 . THR   A 1 74  ? 5.635   -22.611 -26.116 1.00 11.66 ? 74  THR   A OG1 1 
ATOM   503  C  CG2 . THR   A 1 74  ? 4.226   -21.524 -24.473 1.00 10.84 ? 74  THR   A CG2 1 
ATOM   504  N  N   . ASN   A 1 75  ? 7.844   -19.808 -26.394 1.00 11.15 ? 75  ASN   A N   1 
ATOM   505  C  CA  . ASN   A 1 75  ? 9.125   -19.513 -27.024 1.00 11.19 ? 75  ASN   A CA  1 
ATOM   506  C  C   . ASN   A 1 75  ? 8.964   -18.473 -28.128 1.00 11.80 ? 75  ASN   A C   1 
ATOM   507  O  O   . ASN   A 1 75  ? 9.623   -18.530 -29.171 1.00 12.89 ? 75  ASN   A O   1 
ATOM   508  C  CB  . ASN   A 1 75  ? 9.766   -20.776 -27.567 1.00 11.50 ? 75  ASN   A CB  1 
ATOM   509  C  CG  . ASN   A 1 75  ? 11.272  -20.663 -27.639 1.00 12.73 ? 75  ASN   A CG  1 
ATOM   510  O  OD1 . ASN   A 1 75  ? 11.884  -20.051 -26.749 1.00 12.94 ? 75  ASN   A OD1 1 
ATOM   511  N  ND2 . ASN   A 1 75  ? 11.860  -21.289 -28.654 1.00 11.38 ? 75  ASN   A ND2 1 
ATOM   512  N  N   . PHE   A 1 76  ? 8.045   -17.515 -27.911 1.00 12.15 ? 76  PHE   A N   1 
ATOM   513  C  CA  . PHE   A 1 76  ? 7.464   -16.750 -28.997 1.00 12.63 ? 76  PHE   A CA  1 
ATOM   514  C  C   . PHE   A 1 76  ? 7.683   -15.258 -28.836 1.00 14.71 ? 76  PHE   A C   1 
ATOM   515  O  O   . PHE   A 1 76  ? 7.550   -14.743 -27.724 1.00 15.29 ? 76  PHE   A O   1 
ATOM   516  C  CB  . PHE   A 1 76  ? 5.959   -17.050 -28.969 1.00 12.60 ? 76  PHE   A CB  1 
ATOM   517  C  CG  . PHE   A 1 76  ? 5.142   -16.291 -30.002 1.00 12.82 ? 76  PHE   A CG  1 
ATOM   518  C  CD1 . PHE   A 1 76  ? 4.681   -14.998 -29.741 1.00 13.76 ? 76  PHE   A CD1 1 
ATOM   519  C  CD2 . PHE   A 1 76  ? 4.788   -16.898 -31.194 1.00 14.09 ? 76  PHE   A CD2 1 
ATOM   520  C  CE1 . PHE   A 1 76  ? 3.942   -14.321 -30.700 1.00 14.15 ? 76  PHE   A CE1 1 
ATOM   521  C  CE2 . PHE   A 1 76  ? 4.022   -16.213 -32.135 1.00 14.11 ? 76  PHE   A CE2 1 
ATOM   522  C  CZ  . PHE   A 1 76  ? 3.639   -14.928 -31.880 1.00 13.67 ? 76  PHE   A CZ  1 
ATOM   523  N  N   . PRO   A 1 77  A 7.881   -14.481 -29.927 1.00 14.90 ? 77  PRO   A N   1 
ATOM   524  C  CA  . PRO   A 1 77  A 8.037   -14.994 -31.285 1.00 15.80 ? 77  PRO   A CA  1 
ATOM   525  C  C   . PRO   A 1 77  A 9.461   -15.351 -31.700 1.00 14.79 ? 77  PRO   A C   1 
ATOM   526  O  O   . PRO   A 1 77  A 9.674   -15.814 -32.821 1.00 13.68 ? 77  PRO   A O   1 
ATOM   527  C  CB  . PRO   A 1 77  A 7.538   -13.793 -32.080 1.00 17.09 ? 77  PRO   A CB  1 
ATOM   528  C  CG  . PRO   A 1 77  A 8.092   -12.604 -31.325 1.00 16.67 ? 77  PRO   A CG  1 
ATOM   529  C  CD  . PRO   A 1 77  A 7.886   -13.005 -29.880 1.00 17.21 ? 77  PRO   A CD  1 
ATOM   530  N  N   . HIS   A 1 78  ? 10.399  -15.282 -30.739 1.00 13.67 ? 78  HIS   A N   1 
ATOM   531  C  CA  . HIS   A 1 78  ? 11.829  -15.282 -31.014 1.00 14.32 ? 78  HIS   A CA  1 
ATOM   532  C  C   . HIS   A 1 78  ? 12.375  -16.625 -31.470 1.00 13.50 ? 78  HIS   A C   1 
ATOM   533  O  O   . HIS   A 1 78  ? 13.328  -16.652 -32.233 1.00 14.62 ? 78  HIS   A O   1 
ATOM   534  C  CB  . HIS   A 1 78  ? 12.594  -14.802 -29.779 1.00 14.82 ? 78  HIS   A CB  1 
ATOM   535  C  CG  . HIS   A 1 78  ? 12.092  -15.419 -28.524 1.00 15.06 ? 78  HIS   A CG  1 
ATOM   536  N  ND1 . HIS   A 1 78  ? 12.346  -16.715 -28.136 1.00 15.18 ? 78  HIS   A ND1 1 
ATOM   537  C  CD2 . HIS   A 1 78  ? 11.327  -14.864 -27.534 1.00 16.00 ? 78  HIS   A CD2 1 
ATOM   538  C  CE1 . HIS   A 1 78  ? 11.751  -16.946 -26.981 1.00 15.59 ? 78  HIS   A CE1 1 
ATOM   539  N  NE2 . HIS   A 1 78  ? 11.138  -15.830 -26.579 1.00 16.16 ? 78  HIS   A NE2 1 
ATOM   540  N  N   . GLY   A 1 79  ? 11.812  -17.743 -31.010 1.00 12.66 ? 79  GLY   A N   1 
ATOM   541  C  CA  . GLY   A 1 79  ? 12.398  -19.041 -31.330 1.00 12.53 ? 79  GLY   A CA  1 
ATOM   542  C  C   . GLY   A 1 79  ? 13.840  -19.154 -30.826 1.00 14.56 ? 79  GLY   A C   1 
ATOM   543  O  O   . GLY   A 1 79  ? 14.711  -19.760 -31.462 1.00 13.73 ? 79  GLY   A O   1 
ATOM   544  N  N   . ASN   A 1 80  ? 14.072  -18.642 -29.612 1.00 14.00 ? 80  ASN   A N   1 
ATOM   545  C  CA  . ASN   A 1 80  ? 15.353  -18.819 -28.962 1.00 14.92 ? 80  ASN   A CA  1 
ATOM   546  C  C   . ASN   A 1 80  ? 15.633  -20.300 -28.709 1.00 15.08 ? 80  ASN   A C   1 
ATOM   547  O  O   . ASN   A 1 80  ? 14.734  -21.135 -28.746 1.00 13.88 ? 80  ASN   A O   1 
ATOM   548  C  CB  . ASN   A 1 80  ? 15.395  -18.061 -27.631 1.00 15.24 ? 80  ASN   A CB  1 
ATOM   549  C  CG  . ASN   A 1 80  ? 15.451  -16.569 -27.796 1.00 16.58 ? 80  ASN   A CG  1 
ATOM   550  O  OD1 . ASN   A 1 80  ? 15.749  -16.057 -28.886 1.00 19.96 ? 80  ASN   A OD1 1 
ATOM   551  N  ND2 . ASN   A 1 80  ? 15.179  -15.844 -26.710 1.00 18.22 ? 80  ASN   A ND2 1 
ATOM   552  N  N   . ASP   A 1 81  ? 16.893  -20.618 -28.398 1.00 16.05 ? 81  ASP   A N   1 
ATOM   553  C  CA  . ASP   A 1 81  ? 17.299  -22.008 -28.265 1.00 16.86 ? 81  ASP   A CA  1 
ATOM   554  C  C   . ASP   A 1 81  ? 17.592  -22.384 -26.809 1.00 17.63 ? 81  ASP   A C   1 
ATOM   555  O  O   . ASP   A 1 81  ? 18.330  -23.342 -26.560 1.00 17.47 ? 81  ASP   A O   1 
ATOM   556  C  CB  . ASP   A 1 81  ? 18.499  -22.311 -29.153 1.00 18.40 ? 81  ASP   A CB  1 
ATOM   557  C  CG  . ASP   A 1 81  ? 19.742  -21.499 -28.817 1.00 20.79 ? 81  ASP   A CG  1 
ATOM   558  O  OD1 . ASP   A 1 81  ? 19.673  -20.650 -27.916 1.00 23.52 ? 81  ASP   A OD1 1 
ATOM   559  O  OD2 . ASP   A 1 81  ? 20.760  -21.683 -29.489 1.00 26.33 ? 81  ASP   A OD2 1 
ATOM   560  N  N   . ASP   A 1 82  ? 16.930  -21.705 -25.853 1.00 16.15 ? 82  ASP   A N   1 
ATOM   561  C  CA  . ASP   A 1 82  ? 17.010  -22.097 -24.458 1.00 16.16 ? 82  ASP   A CA  1 
ATOM   562  C  C   . ASP   A 1 82  ? 15.850  -23.034 -24.136 1.00 14.91 ? 82  ASP   A C   1 
ATOM   563  O  O   . ASP   A 1 82  ? 14.700  -22.600 -24.035 1.00 14.40 ? 82  ASP   A O   1 
ATOM   564  C  CB  . ASP   A 1 82  ? 17.073  -20.877 -23.554 1.00 17.25 ? 82  ASP   A CB  1 
ATOM   565  C  CG  . ASP   A 1 82  ? 17.286  -21.206 -22.081 1.00 19.49 ? 82  ASP   A CG  1 
ATOM   566  O  OD1 . ASP   A 1 82  ? 16.678  -22.195 -21.611 1.00 18.61 ? 82  ASP   A OD1 1 
ATOM   567  O  OD2 . ASP   A 1 82  ? 18.004  -20.438 -21.409 1.00 21.33 ? 82  ASP   A OD2 1 
ATOM   568  N  N   . ILE   A 1 83  ? 16.158  -24.318 -24.025 1.00 14.57 ? 83  ILE   A N   1 
ATOM   569  C  CA  . ILE   A 1 83  ? 15.142  -25.338 -23.869 1.00 15.00 ? 83  ILE   A CA  1 
ATOM   570  C  C   . ILE   A 1 83  ? 14.426  -25.161 -22.535 1.00 15.49 ? 83  ILE   A C   1 
ATOM   571  O  O   . ILE   A 1 83  ? 13.210  -25.338 -22.473 1.00 15.39 ? 83  ILE   A O   1 
ATOM   572  C  CB  . ILE   A 1 83  ? 15.749  -26.742 -23.973 1.00 16.38 ? 83  ILE   A CB  1 
ATOM   573  C  CG1 . ILE   A 1 83  ? 16.327  -27.001 -25.362 1.00 18.56 ? 83  ILE   A CG1 1 
ATOM   574  C  CG2 . ILE   A 1 83  ? 14.724  -27.799 -23.589 1.00 16.07 ? 83  ILE   A CG2 1 
ATOM   575  C  CD1 . ILE   A 1 83  ? 17.149  -28.269 -25.440 1.00 20.25 ? 83  ILE   A CD1 1 
ATOM   576  N  N   . GLU   A 1 84  ? 15.183  -24.866 -21.462 1.00 17.03 ? 84  GLU   A N   1 
ATOM   577  C  CA  . GLU   A 1 84  ? 14.569  -24.708 -20.146 1.00 17.79 ? 84  GLU   A CA  1 
ATOM   578  C  C   . GLU   A 1 84  ? 13.552  -23.575 -20.139 1.00 14.95 ? 84  GLU   A C   1 
ATOM   579  O  O   . GLU   A 1 84  ? 12.485  -23.724 -19.540 1.00 15.42 ? 84  GLU   A O   1 
ATOM   580  C  CB  . GLU   A 1 84  ? 15.625  -24.550 -19.053 1.00 20.95 ? 84  GLU   A CB  1 
ATOM   581  C  CG  . GLU   A 1 84  ? 16.388  -25.850 -18.814 1.00 26.14 ? 84  GLU   A CG  1 
ATOM   582  C  CD  . GLU   A 1 84  ? 15.529  -27.062 -18.475 1.00 35.83 ? 84  GLU   A CD  1 
ATOM   583  O  OE1 . GLU   A 1 84  ? 14.633  -26.913 -17.618 1.00 41.39 ? 84  GLU   A OE1 1 
ATOM   584  O  OE2 . GLU   A 1 84  ? 15.735  -28.158 -19.064 1.00 46.04 ? 84  GLU   A OE2 1 
ATOM   585  N  N   . ILE   A 1 85  ? 13.833  -22.466 -20.809 1.00 14.15 ? 85  ILE   A N   1 
ATOM   586  C  CA  . ILE   A 1 85  ? 12.864  -21.393 -20.880 1.00 14.49 ? 85  ILE   A CA  1 
ATOM   587  C  C   . ILE   A 1 85  ? 11.633  -21.809 -21.690 1.00 13.74 ? 85  ILE   A C   1 
ATOM   588  O  O   . ILE   A 1 85  ? 10.503  -21.564 -21.280 1.00 13.91 ? 85  ILE   A O   1 
ATOM   589  C  CB  . ILE   A 1 85  ? 13.509  -20.098 -21.378 1.00 15.56 ? 85  ILE   A CB  1 
ATOM   590  C  CG1 . ILE   A 1 85  ? 14.523  -19.571 -20.334 1.00 17.14 ? 85  ILE   A CG1 1 
ATOM   591  C  CG2 . ILE   A 1 85  ? 12.468  -19.047 -21.733 1.00 16.17 ? 85  ILE   A CG2 1 
ATOM   592  C  CD1 . ILE   A 1 85  ? 15.126  -18.230 -20.689 1.00 18.82 ? 85  ILE   A CD1 1 
ATOM   593  N  N   . ALA   A 1 86  ? 11.836  -22.408 -22.869 1.00 13.42 ? 86  ALA   A N   1 
ATOM   594  C  CA  . ALA   A 1 86  ? 10.705  -22.821 -23.676 1.00 13.14 ? 86  ALA   A CA  1 
ATOM   595  C  C   . ALA   A 1 86  ? 9.831   -23.835 -22.943 1.00 12.45 ? 86  ALA   A C   1 
ATOM   596  O  O   . ALA   A 1 86  ? 8.592   -23.756 -22.980 1.00 11.74 ? 86  ALA   A O   1 
ATOM   597  C  CB  . ALA   A 1 86  ? 11.190  -23.384 -24.996 1.00 13.36 ? 86  ALA   A CB  1 
ATOM   598  N  N   . LEU   A 1 87  ? 10.467  -24.758 -22.214 1.00 13.39 ? 87  LEU   A N   1 
ATOM   599  C  CA  . LEU   A 1 87  ? 9.734   -25.749 -21.458 1.00 13.01 ? 87  LEU   A CA  1 
ATOM   600  C  C   . LEU   A 1 87  ? 8.939   -25.107 -20.316 1.00 12.95 ? 87  LEU   A C   1 
ATOM   601  O  O   . LEU   A 1 87  ? 7.798   -25.479 -20.091 1.00 12.88 ? 87  LEU   A O   1 
ATOM   602  C  CB  . LEU   A 1 87  ? 10.744  -26.769 -20.936 1.00 14.14 ? 87  LEU   A CB  1 
ATOM   603  C  CG  . LEU   A 1 87  ? 10.161  -27.898 -20.089 1.00 14.68 ? 87  LEU   A CG  1 
ATOM   604  C  CD1 . LEU   A 1 87  ? 9.054   -28.680 -20.764 1.00 14.81 ? 87  LEU   A CD1 1 
ATOM   605  C  CD2 . LEU   A 1 87  ? 11.315  -28.795 -19.650 1.00 15.48 ? 87  LEU   A CD2 1 
ATOM   606  N  N   . ALA   A 1 88  ? 9.556   -24.177 -19.568 1.00 12.58 ? 88  ALA   A N   1 
ATOM   607  C  CA  . ALA   A 1 88  ? 8.879   -23.483 -18.492 1.00 13.22 ? 88  ALA   A CA  1 
ATOM   608  C  C   . ALA   A 1 88  ? 7.626   -22.771 -19.002 1.00 12.14 ? 88  ALA   A C   1 
ATOM   609  O  O   . ALA   A 1 88  ? 6.546   -22.853 -18.423 1.00 11.50 ? 88  ALA   A O   1 
ATOM   610  C  CB  . ALA   A 1 88  ? 9.830   -22.510 -17.835 1.00 13.39 ? 88  ALA   A CB  1 
ATOM   611  N  N   . GLU   A 1 89  ? 7.760   -22.084 -20.134 1.00 12.46 ? 89  GLU   A N   1 
ATOM   612  C  CA  . GLU   A 1 89  ? 6.660   -21.362 -20.743 1.00 11.47 ? 89  GLU   A CA  1 
ATOM   613  C  C   . GLU   A 1 89  ? 5.558   -22.339 -21.160 1.00 11.36 ? 89  GLU   A C   1 
ATOM   614  O  O   . GLU   A 1 89  ? 4.371   -22.066 -20.983 1.00 11.33 ? 89  GLU   A O   1 
ATOM   615  C  CB  . GLU   A 1 89  ? 7.134   -20.506 -21.913 1.00 12.02 ? 89  GLU   A CB  1 
ATOM   616  C  CG  . GLU   A 1 89  ? 8.039   -19.354 -21.498 1.00 13.42 ? 89  GLU   A CG  1 
ATOM   617  C  CD  . GLU   A 1 89  ? 8.425   -18.434 -22.639 1.00 15.70 ? 89  GLU   A CD  1 
ATOM   618  O  OE1 . GLU   A 1 89  ? 8.215   -18.880 -23.814 1.00 18.24 ? 89  GLU   A OE1 1 
ATOM   619  O  OE2 . GLU   A 1 89  ? 8.910   -17.307 -22.378 1.00 16.52 ? 89  GLU   A OE2 1 
ATOM   620  N  N   . THR   A 1 90  ? 5.950   -23.490 -21.735 1.00 10.83 ? 90  THR   A N   1 
ATOM   621  C  CA  . THR   A 1 90  ? 4.999   -24.490 -22.172 1.00 11.07 ? 90  THR   A CA  1 
ATOM   622  C  C   . THR   A 1 90  ? 4.256   -25.096 -20.970 1.00 10.63 ? 90  THR   A C   1 
ATOM   623  O  O   . THR   A 1 90  ? 3.026   -25.275 -20.996 1.00 11.16 ? 90  THR   A O   1 
ATOM   624  C  CB  . THR   A 1 90  ? 5.741   -25.541 -23.001 1.00 11.78 ? 90  THR   A CB  1 
ATOM   625  O  OG1 . THR   A 1 90  ? 6.250   -24.910 -24.184 1.00 13.08 ? 90  THR   A OG1 1 
ATOM   626  C  CG2 . THR   A 1 90  ? 4.839   -26.679 -23.445 1.00 11.69 ? 90  THR   A CG2 1 
ATOM   627  N  N   . ARG   A 1 91  ? 4.985   -25.390 -19.896 1.00 11.57 ? 91  ARG   A N   1 
ATOM   628  C  CA  . ARG   A 1 91  ? 4.354   -25.909 -18.685 1.00 11.92 ? 91  ARG   A CA  1 
ATOM   629  C  C   . ARG   A 1 91  ? 3.364   -24.895 -18.115 1.00 11.60 ? 91  ARG   A C   1 
ATOM   630  O  O   . ARG   A 1 91  ? 2.286   -25.247 -17.669 1.00 11.02 ? 91  ARG   A O   1 
ATOM   631  C  CB  . ARG   A 1 91  ? 5.423   -26.281 -17.650 1.00 12.90 ? 91  ARG   A CB  1 
ATOM   632  C  CG  . ARG   A 1 91  ? 6.187   -27.549 -18.011 1.00 14.50 ? 91  ARG   A CG  1 
ATOM   633  C  CD  . ARG   A 1 91  ? 7.275   -27.838 -17.008 1.00 17.50 ? 91  ARG   A CD  1 
ATOM   634  N  NE  . ARG   A 1 91  ? 7.861   -29.139 -17.253 1.00 20.92 ? 91  ARG   A NE  1 
ATOM   635  C  CZ  . ARG   A 1 91  ? 9.022   -29.543 -16.746 1.00 27.09 ? 91  ARG   A CZ  1 
ATOM   636  N  NH1 . ARG   A 1 91  ? 9.825   -28.690 -16.139 1.00 30.41 ? 91  ARG   A NH1 1 
ATOM   637  N  NH2 . ARG   A 1 91  ? 9.408   -30.789 -16.936 1.00 31.10 ? 91  ARG   A NH2 1 
ATOM   638  N  N   . ALA   A 1 92  ? 3.723   -23.608 -18.165 1.00 11.74 ? 92  ALA   A N   1 
ATOM   639  C  CA  . ALA   A 1 92  ? 2.833   -22.566 -17.672 1.00 11.87 ? 92  ALA   A CA  1 
ATOM   640  C  C   . ALA   A 1 92  ? 1.583   -22.476 -18.541 1.00 11.49 ? 92  ALA   A C   1 
ATOM   641  O  O   . ALA   A 1 92  ? 0.484   -22.374 -18.032 1.00 10.90 ? 92  ALA   A O   1 
ATOM   642  C  CB  . ALA   A 1 92  ? 3.543   -21.226 -17.629 1.00 12.12 ? 92  ALA   A CB  1 
ATOM   643  N  N   . ALA   A 1 93  ? 1.756   -22.528 -19.870 1.00 10.48 ? 93  ALA   A N   1 
ATOM   644  C  CA  . ALA   A 1 93  ? 0.612   -22.545 -20.766 1.00 11.07 ? 93  ALA   A CA  1 
ATOM   645  C  C   . ALA   A 1 93  ? -0.355  -23.686 -20.432 1.00 11.79 ? 93  ALA   A C   1 
ATOM   646  O  O   . ALA   A 1 93  ? -1.574  -23.504 -20.407 1.00 12.43 ? 93  ALA   A O   1 
ATOM   647  C  CB  . ALA   A 1 93  ? 1.074   -22.660 -22.214 1.00 11.23 ? 93  ALA   A CB  1 
ATOM   648  N  N   . ILE   A 1 94  ? 0.212   -24.868 -20.195 1.00 11.45 ? 94  ILE   A N   1 
ATOM   649  C  CA  . ILE   A 1 94  ? -0.588  -26.034 -19.826 1.00 12.40 ? 94  ILE   A CA  1 
ATOM   650  C  C   . ILE   A 1 94  ? -1.344  -25.759 -18.520 1.00 12.96 ? 94  ILE   A C   1 
ATOM   651  O  O   . ILE   A 1 94  ? -2.556  -26.020 -18.417 1.00 13.07 ? 94  ILE   A O   1 
ATOM   652  C  CB  . ILE   A 1 94  ? 0.297   -27.278 -19.723 1.00 12.47 ? 94  ILE   A CB  1 
ATOM   653  C  CG1 . ILE   A 1 94  ? 0.835   -27.706 -21.090 1.00 12.11 ? 94  ILE   A CG1 1 
ATOM   654  C  CG2 . ILE   A 1 94  ? -0.471  -28.425 -19.059 1.00 13.47 ? 94  ILE   A CG2 1 
ATOM   655  C  CD1 . ILE   A 1 94  ? 2.024   -28.637 -21.009 1.00 12.85 ? 94  ILE   A CD1 1 
ATOM   656  N  N   . ALA   A 1 95  ? -0.629  -25.210 -17.538 1.00 12.16 ? 95  ALA   A N   1 
ATOM   657  C  CA  . ALA   A 1 95  ? -1.191  -24.940 -16.235 1.00 12.01 ? 95  ALA   A CA  1 
ATOM   658  C  C   . ALA   A 1 95  ? -2.291  -23.902 -16.292 1.00 12.04 ? 95  ALA   A C   1 
ATOM   659  O  O   . ALA   A 1 95  ? -3.244  -23.947 -15.511 1.00 12.40 ? 95  ALA   A O   1 
ATOM   660  C  CB  . ALA   A 1 95  ? -0.110  -24.505 -15.265 1.00 12.25 ? 95  ALA   A CB  1 
ATOM   661  N  N   . TYR   A 1 96  ? -2.157  -22.914 -17.161 1.00 12.55 ? 96  TYR   A N   1 
ATOM   662  C  CA  . TYR   A 1 96  ? -3.202  -21.922 -17.325 1.00 12.24 ? 96  TYR   A CA  1 
ATOM   663  C  C   . TYR   A 1 96  ? -4.496  -22.544 -17.882 1.00 14.18 ? 96  TYR   A C   1 
ATOM   664  O  O   . TYR   A 1 96  ? -5.574  -21.966 -17.708 1.00 14.37 ? 96  TYR   A O   1 
ATOM   665  C  CB  . TYR   A 1 96  ? -2.805  -20.811 -18.282 1.00 11.71 ? 96  TYR   A CB  1 
ATOM   666  C  CG  . TYR   A 1 96  ? -1.965  -19.669 -17.743 1.00 11.30 ? 96  TYR   A CG  1 
ATOM   667  C  CD1 . TYR   A 1 96  ? -2.484  -18.795 -16.790 1.00 11.32 ? 96  TYR   A CD1 1 
ATOM   668  C  CD2 . TYR   A 1 96  ? -0.701  -19.381 -18.253 1.00 11.62 ? 96  TYR   A CD2 1 
ATOM   669  C  CE1 . TYR   A 1 96  ? -1.779  -17.694 -16.380 1.00 11.04 ? 96  TYR   A CE1 1 
ATOM   670  C  CE2 . TYR   A 1 96  ? 0.025   -18.274 -17.851 1.00 11.30 ? 96  TYR   A CE2 1 
ATOM   671  C  CZ  . TYR   A 1 96  ? -0.502  -17.452 -16.871 1.00 11.79 ? 96  TYR   A CZ  1 
ATOM   672  O  OH  . TYR   A 1 96  ? 0.179   -16.353 -16.434 1.00 12.83 ? 96  TYR   A OH  1 
ATOM   673  N  N   . GLY   A 1 97  ? -4.366  -23.650 -18.630 1.00 13.35 ? 97  GLY   A N   1 
ATOM   674  C  CA  . GLY   A 1 97  ? -5.509  -24.386 -19.168 1.00 13.78 ? 97  GLY   A CA  1 
ATOM   675  C  C   . GLY   A 1 97  ? -5.517  -24.491 -20.699 1.00 14.22 ? 97  GLY   A C   1 
ATOM   676  O  O   . GLY   A 1 97  ? -6.553  -24.795 -21.274 1.00 13.27 ? 97  GLY   A O   1 
ATOM   677  N  N   . ALA   A 1 98  ? -4.371  -24.303 -21.368 1.00 12.76 ? 98  ALA   A N   1 
ATOM   678  C  CA  . ALA   A 1 98  ? -4.357  -24.396 -22.827 1.00 11.81 ? 98  ALA   A CA  1 
ATOM   679  C  C   . ALA   A 1 98  ? -4.833  -25.769 -23.301 1.00 11.42 ? 98  ALA   A C   1 
ATOM   680  O  O   . ALA   A 1 98  ? -4.507  -26.781 -22.691 1.00 12.37 ? 98  ALA   A O   1 
ATOM   681  C  CB  . ALA   A 1 98  ? -2.954  -24.139 -23.349 1.00 11.68 ? 98  ALA   A CB  1 
ATOM   682  N  N   . ASP   A 1 99  ? -5.519  -25.809 -24.446 1.00 11.72 ? 99  ASP   A N   1 
ATOM   683  C  CA  . ASP   A 1 99  ? -5.769  -27.049 -25.156 1.00 11.92 ? 99  ASP   A CA  1 
ATOM   684  C  C   . ASP   A 1 99  ? -4.631  -27.360 -26.124 1.00 12.13 ? 99  ASP   A C   1 
ATOM   685  O  O   . ASP   A 1 99  ? -4.393  -28.524 -26.454 1.00 11.46 ? 99  ASP   A O   1 
ATOM   686  C  CB  . ASP   A 1 99  ? -7.069  -26.979 -25.943 1.00 13.15 ? 99  ASP   A CB  1 
ATOM   687  C  CG  . ASP   A 1 99  ? -8.296  -26.765 -25.077 1.00 14.13 ? 99  ASP   A CG  1 
ATOM   688  O  OD1 . ASP   A 1 99  ? -8.376  -27.456 -24.059 1.00 14.50 ? 99  ASP   A OD1 1 
ATOM   689  O  OD2 . ASP   A 1 99  ? -9.074  -25.842 -25.346 1.00 15.03 ? 99  ASP   A OD2 1 
ATOM   690  N  N   . GLU   A 1 100 ? -3.992  -26.300 -26.619 1.00 11.17 ? 100 GLU   A N   1 
ATOM   691  C  CA  . GLU   A 1 100 ? -2.935  -26.430 -27.622 1.00 11.88 ? 100 GLU   A CA  1 
ATOM   692  C  C   . GLU   A 1 100 ? -1.876  -25.371 -27.358 1.00 11.21 ? 100 GLU   A C   1 
ATOM   693  O  O   . GLU   A 1 100 ? -2.210  -24.237 -26.984 1.00 11.49 ? 100 GLU   A O   1 
ATOM   694  C  CB  . GLU   A 1 100 ? -3.477  -26.183 -29.033 1.00 12.92 ? 100 GLU   A CB  1 
ATOM   695  C  CG  . GLU   A 1 100 ? -4.720  -27.018 -29.334 1.00 14.12 ? 100 GLU   A CG  1 
ATOM   696  C  CD  . GLU   A 1 100 ? -5.287  -26.878 -30.746 1.00 16.13 ? 100 GLU   A CD  1 
ATOM   697  O  OE1 . GLU   A 1 100 ? -4.939  -25.912 -31.454 1.00 14.81 ? 100 GLU   A OE1 1 
ATOM   698  O  OE2 . GLU   A 1 100 ? -6.125  -27.751 -31.082 1.00 16.80 ? 100 GLU   A OE2 1 
ATOM   699  N  N   . VAL   A 1 101 ? -0.619  -25.755 -27.582 1.00 11.46 ? 101 VAL   A N   1 
ATOM   700  C  CA  . VAL   A 1 101 ? 0.500   -24.841 -27.480 1.00 10.93 ? 101 VAL   A CA  1 
ATOM   701  C  C   . VAL   A 1 101 ? 1.232   -24.816 -28.807 1.00 11.00 ? 101 VAL   A C   1 
ATOM   702  O  O   . VAL   A 1 101 ? 1.535   -25.890 -29.327 1.00 11.43 ? 101 VAL   A O   1 
ATOM   703  C  CB  . VAL   A 1 101 ? 1.446   -25.305 -26.368 1.00 12.19 ? 101 VAL   A CB  1 
ATOM   704  C  CG1 . VAL   A 1 101 ? 2.747   -24.502 -26.347 1.00 13.04 ? 101 VAL   A CG1 1 
ATOM   705  C  CG2 . VAL   A 1 101 ? 0.726   -25.210 -25.035 1.00 12.46 ? 101 VAL   A CG2 1 
ATOM   706  N  N   . ASP   A 1 102 ? 1.437   -23.601 -29.322 1.00 10.96 ? 102 ASP   A N   1 
ATOM   707  C  CA  . ASP   A 1 102 ? 2.204   -23.404 -30.547 1.00 11.33 ? 102 ASP   A CA  1 
ATOM   708  C  C   . ASP   A 1 102 ? 3.576   -22.863 -30.112 1.00 11.28 ? 102 ASP   A C   1 
ATOM   709  O  O   . ASP   A 1 102 ? 3.717   -21.690 -29.713 1.00 11.57 ? 102 ASP   A O   1 
ATOM   710  C  CB  . ASP   A 1 102 ? 1.484   -22.453 -31.495 1.00 12.13 ? 102 ASP   A CB  1 
ATOM   711  C  CG  . ASP   A 1 102 ? 0.073   -22.843 -31.967 1.00 14.06 ? 102 ASP   A CG  1 
ATOM   712  O  OD1 . ASP   A 1 102 ? -0.496  -23.856 -31.473 1.00 13.76 ? 102 ASP   A OD1 1 
ATOM   713  O  OD2 . ASP   A 1 102 ? -0.496  -22.048 -32.771 1.00 17.00 ? 102 ASP   A OD2 1 
ATOM   714  N  N   . VAL   A 1 103 ? 4.593   -23.721 -30.172 1.00 10.78 ? 103 VAL   A N   1 
ATOM   715  C  CA  . VAL   A 1 103 ? 5.936   -23.339 -29.758 1.00 11.14 ? 103 VAL   A CA  1 
ATOM   716  C  C   . VAL   A 1 103 ? 6.745   -22.924 -30.990 1.00 11.05 ? 103 VAL   A C   1 
ATOM   717  O  O   . VAL   A 1 103 ? 6.669   -23.572 -32.045 1.00 10.68 ? 103 VAL   A O   1 
ATOM   718  C  CB  . VAL   A 1 103 ? 6.619   -24.473 -28.975 1.00 11.32 ? 103 VAL   A CB  1 
ATOM   719  C  CG1 . VAL   A 1 103 ? 6.898   -25.716 -29.824 1.00 11.76 ? 103 VAL   A CG1 1 
ATOM   720  C  CG2 . VAL   A 1 103 ? 7.887   -24.003 -28.314 1.00 12.48 ? 103 VAL   A CG2 1 
ATOM   721  N  N   . VAL   A 1 104 ? 7.617   -21.923 -30.827 1.00 11.27 ? 104 VAL   A N   1 
ATOM   722  C  CA  . VAL   A 1 104 ? 8.489   -21.543 -31.931 1.00 11.08 ? 104 VAL   A CA  1 
ATOM   723  C  C   . VAL   A 1 104 ? 9.752   -22.404 -31.904 1.00 11.26 ? 104 VAL   A C   1 
ATOM   724  O  O   . VAL   A 1 104 ? 10.467  -22.464 -30.892 1.00 11.27 ? 104 VAL   A O   1 
ATOM   725  C  CB  . VAL   A 1 104 ? 8.836   -20.053 -31.930 1.00 11.17 ? 104 VAL   A CB  1 
ATOM   726  C  CG1 . VAL   A 1 104 ? 9.588   -19.714 -33.202 1.00 10.93 ? 104 VAL   A CG1 1 
ATOM   727  C  CG2 . VAL   A 1 104 ? 7.600   -19.189 -31.841 1.00 11.32 ? 104 VAL   A CG2 1 
ATOM   728  N  N   . PHE   A 1 105 ? 10.006  -23.097 -33.025 1.00 11.27 ? 105 PHE   A N   1 
ATOM   729  C  CA  . PHE   A 1 105 ? 11.209  -23.884 -33.218 1.00 11.76 ? 105 PHE   A CA  1 
ATOM   730  C  C   . PHE   A 1 105 ? 12.428  -22.978 -33.191 1.00 11.41 ? 105 PHE   A C   1 
ATOM   731  O  O   . PHE   A 1 105 ? 12.350  -21.827 -33.643 1.00 11.47 ? 105 PHE   A O   1 
ATOM   732  C  CB  . PHE   A 1 105 ? 11.095  -24.496 -34.617 1.00 11.85 ? 105 PHE   A CB  1 
ATOM   733  C  CG  . PHE   A 1 105 ? 12.191  -25.481 -34.976 1.00 12.55 ? 105 PHE   A CG  1 
ATOM   734  C  CD1 . PHE   A 1 105 ? 12.044  -26.821 -34.707 1.00 13.54 ? 105 PHE   A CD1 1 
ATOM   735  C  CD2 . PHE   A 1 105 ? 13.335  -25.068 -35.651 1.00 14.34 ? 105 PHE   A CD2 1 
ATOM   736  C  CE1 . PHE   A 1 105 ? 13.027  -27.736 -35.079 1.00 14.22 ? 105 PHE   A CE1 1 
ATOM   737  C  CE2 . PHE   A 1 105 ? 14.330  -25.972 -35.989 1.00 14.71 ? 105 PHE   A CE2 1 
ATOM   738  C  CZ  . PHE   A 1 105 ? 14.171  -27.304 -35.714 1.00 14.21 ? 105 PHE   A CZ  1 
ATOM   739  N  N   . PRO   A 1 106 ? 13.587  -23.471 -32.701 1.00 12.78 ? 106 PRO   A N   1 
ATOM   740  C  CA  . PRO   A 1 106 ? 14.811  -22.668 -32.709 1.00 12.82 ? 106 PRO   A CA  1 
ATOM   741  C  C   . PRO   A 1 106 ? 15.421  -22.653 -34.104 1.00 13.52 ? 106 PRO   A C   1 
ATOM   742  O  O   . PRO   A 1 106 ? 16.392  -23.349 -34.383 1.00 14.65 ? 106 PRO   A O   1 
ATOM   743  C  CB  . PRO   A 1 106 ? 15.710  -23.323 -31.655 1.00 12.89 ? 106 PRO   A CB  1 
ATOM   744  C  CG  . PRO   A 1 106 ? 15.246  -24.759 -31.604 1.00 13.28 ? 106 PRO   A CG  1 
ATOM   745  C  CD  . PRO   A 1 106 ? 13.752  -24.736 -31.971 1.00 12.38 ? 106 PRO   A CD  1 
ATOM   746  N  N   . TYR   A 1 107 ? 14.820  -21.831 -34.967 1.00 12.45 ? 107 TYR   A N   1 
ATOM   747  C  CA  . TYR   A 1 107 ? 15.177  -21.824 -36.380 1.00 13.30 ? 107 TYR   A CA  1 
ATOM   748  C  C   . TYR   A 1 107 ? 16.554  -21.186 -36.614 1.00 13.71 ? 107 TYR   A C   1 
ATOM   749  O  O   . TYR   A 1 107 ? 17.299  -21.614 -37.502 1.00 14.27 ? 107 TYR   A O   1 
ATOM   750  C  CB  . TYR   A 1 107 ? 14.061  -21.166 -37.182 1.00 13.13 ? 107 TYR   A CB  1 
ATOM   751  C  CG  . TYR   A 1 107 ? 13.736  -19.717 -36.860 1.00 13.62 ? 107 TYR   A CG  1 
ATOM   752  C  CD1 . TYR   A 1 107 ? 14.473  -18.688 -37.422 1.00 14.44 ? 107 TYR   A CD1 1 
ATOM   753  C  CD2 . TYR   A 1 107 ? 12.688  -19.383 -36.020 1.00 13.46 ? 107 TYR   A CD2 1 
ATOM   754  C  CE1 . TYR   A 1 107 ? 14.171  -17.374 -37.171 1.00 15.41 ? 107 TYR   A CE1 1 
ATOM   755  C  CE2 . TYR   A 1 107 ? 12.393  -18.065 -35.727 1.00 14.22 ? 107 TYR   A CE2 1 
ATOM   756  C  CZ  . TYR   A 1 107 ? 13.140  -17.056 -36.315 1.00 15.32 ? 107 TYR   A CZ  1 
ATOM   757  O  OH  . TYR   A 1 107 ? 12.872  -15.741 -36.077 1.00 14.75 ? 107 TYR   A OH  1 
ATOM   758  N  N   . ARG   A 1 108 ? 16.927  -20.190 -35.804 1.00 14.44 ? 108 ARG   A N   1 
ATOM   759  C  CA  . ARG   A 1 108 ? 18.240  -19.582 -35.942 1.00 15.44 ? 108 ARG   A CA  1 
ATOM   760  C  C   . ARG   A 1 108 ? 19.327  -20.594 -35.598 1.00 15.98 ? 108 ARG   A C   1 
ATOM   761  O  O   . ARG   A 1 108 ? 20.379  -20.614 -36.239 1.00 16.55 ? 108 ARG   A O   1 
ATOM   762  C  CB  . ARG   A 1 108 ? 18.348  -18.314 -35.104 1.00 15.63 ? 108 ARG   A CB  1 
ATOM   763  C  CG  . ARG   A 1 108 ? 17.624  -17.123 -35.697 1.00 18.14 ? 108 ARG   A CG  1 
ATOM   764  C  CD  . ARG   A 1 108 ? 17.951  -15.836 -34.958 1.00 20.86 ? 108 ARG   A CD  1 
ATOM   765  N  NE  . ARG   A 1 108 ? 17.625  -15.953 -33.541 1.00 24.30 ? 108 ARG   A NE  1 
ATOM   766  C  CZ  . ARG   A 1 108 ? 16.403  -15.905 -33.045 1.00 25.63 ? 108 ARG   A CZ  1 
ATOM   767  N  NH1 . ARG   A 1 108 ? 15.400  -15.507 -33.822 1.00 30.25 ? 108 ARG   A NH1 1 
ATOM   768  N  NH2 . ARG   A 1 108 ? 16.187  -16.198 -31.763 1.00 22.94 ? 108 ARG   A NH2 1 
ATOM   769  N  N   . ALA   A 1 109 ? 19.072  -21.455 -34.607 1.00 15.14 ? 109 ALA   A N   1 
ATOM   770  C  CA  . ALA   A 1 109 ? 20.026  -22.479 -34.250 1.00 15.66 ? 109 ALA   A CA  1 
ATOM   771  C  C   . ALA   A 1 109 ? 20.174  -23.470 -35.382 1.00 15.76 ? 109 ALA   A C   1 
ATOM   772  O  O   . ALA   A 1 109 ? 21.281  -23.879 -35.694 1.00 15.49 ? 109 ALA   A O   1 
ATOM   773  C  CB  . ALA   A 1 109 ? 19.626  -23.186 -32.973 1.00 15.11 ? 109 ALA   A CB  1 
ATOM   774  N  N   . LEU   A 1 110 ? 19.057  -23.812 -36.051 1.00 14.93 ? 110 LEU   A N   1 
ATOM   775  C  CA  . LEU   A 1 110 ? 19.140  -24.702 -37.204 1.00 15.11 ? 110 LEU   A CA  1 
ATOM   776  C  C   . LEU   A 1 110 ? 19.951  -24.064 -38.330 1.00 14.94 ? 110 LEU   A C   1 
ATOM   777  O  O   . LEU   A 1 110 ? 20.743  -24.747 -39.002 1.00 15.32 ? 110 LEU   A O   1 
ATOM   778  C  CB  . LEU   A 1 110 ? 17.754  -25.090 -37.700 1.00 14.79 ? 110 LEU   A CB  1 
ATOM   779  C  CG  . LEU   A 1 110 ? 17.739  -25.950 -38.959 1.00 15.65 ? 110 LEU   A CG  1 
ATOM   780  C  CD1 . LEU   A 1 110 ? 18.338  -27.319 -38.652 1.00 16.64 ? 110 LEU   A CD1 1 
ATOM   781  C  CD2 . LEU   A 1 110 ? 16.307  -26.101 -39.449 1.00 16.71 ? 110 LEU   A CD2 1 
ATOM   782  N  N   . MET   A 1 111 ? 19.744  -22.766 -38.564 1.00 14.95 ? 111 MET   A N   1 
ATOM   783  C  CA  . MET   A 1 111 ? 20.462  -22.079 -39.627 1.00 17.07 ? 111 MET   A CA  1 
ATOM   784  C  C   . MET   A 1 111 ? 21.963  -22.010 -39.292 1.00 17.58 ? 111 MET   A C   1 
ATOM   785  O  O   . MET   A 1 111 ? 22.779  -21.882 -40.205 1.00 18.31 ? 111 MET   A O   1 
ATOM   786  C  CB  . MET   A 1 111 ? 19.862  -20.693 -39.868 1.00 18.51 ? 111 MET   A CB  1 
ATOM   787  C  CG  . MET   A 1 111 ? 18.469  -20.792 -40.489 1.00 23.16 ? 111 MET   A CG  1 
ATOM   788  S  SD  . MET   A 1 111 ? 17.565  -19.229 -40.432 1.00 30.00 ? 111 MET   A SD  1 
ATOM   789  C  CE  . MET   A 1 111 ? 18.342  -18.675 -41.942 1.00 30.40 ? 111 MET   A CE  1 
ATOM   790  N  N   . ALA   A 1 112 ? 22.304  -22.133 -38.009 1.00 17.95 ? 112 ALA   A N   1 
ATOM   791  C  CA  . ALA   A 1 112 ? 23.693  -22.175 -37.558 1.00 19.51 ? 112 ALA   A CA  1 
ATOM   792  C  C   . ALA   A 1 112 ? 24.202  -23.607 -37.432 1.00 20.08 ? 112 ALA   A C   1 
ATOM   793  O  O   . ALA   A 1 112 ? 25.251  -23.843 -36.826 1.00 20.61 ? 112 ALA   A O   1 
ATOM   794  C  CB  . ALA   A 1 112 ? 23.815  -21.440 -36.238 1.00 20.19 ? 112 ALA   A CB  1 
ATOM   795  N  N   . GLY   A 1 113 ? 23.449  -24.575 -37.957 1.00 19.78 ? 113 GLY   A N   1 
ATOM   796  C  CA  . GLY   A 1 113 ? 23.939  -25.936 -38.084 1.00 20.23 ? 113 GLY   A CA  1 
ATOM   797  C  C   . GLY   A 1 113 ? 23.588  -26.828 -36.907 1.00 20.66 ? 113 GLY   A C   1 
ATOM   798  O  O   . GLY   A 1 113 ? 24.052  -27.958 -36.851 1.00 22.54 ? 113 GLY   A O   1 
ATOM   799  N  N   . ASN   A 1 114 ? 22.809  -26.331 -35.938 1.00 19.36 ? 114 ASN   A N   1 
ATOM   800  C  CA  . ASN   A 1 114 ? 22.480  -27.120 -34.769 1.00 18.13 ? 114 ASN   A CA  1 
ATOM   801  C  C   . ASN   A 1 114 ? 21.075  -27.690 -34.928 1.00 18.99 ? 114 ASN   A C   1 
ATOM   802  O  O   . ASN   A 1 114 ? 20.095  -27.014 -34.619 1.00 20.05 ? 114 ASN   A O   1 
ATOM   803  C  CB  . ASN   A 1 114 ? 22.603  -26.281 -33.507 1.00 18.87 ? 114 ASN   A CB  1 
ATOM   804  C  CG  . ASN   A 1 114 ? 22.454  -27.109 -32.256 1.00 19.70 ? 114 ASN   A CG  1 
ATOM   805  O  OD1 . ASN   A 1 114 ? 21.937  -28.231 -32.281 1.00 18.96 ? 114 ASN   A OD1 1 
ATOM   806  N  ND2 . ASN   A 1 114 ? 22.849  -26.515 -31.148 1.00 22.45 ? 114 ASN   A ND2 1 
ATOM   807  N  N   . GLU   A 1 115 ? 21.003  -28.946 -35.367 1.00 18.81 ? 115 GLU   A N   1 
ATOM   808  C  CA  . GLU   A 1 115 ? 19.758  -29.665 -35.524 1.00 19.25 ? 115 GLU   A CA  1 
ATOM   809  C  C   . GLU   A 1 115 ? 19.289  -30.221 -34.193 1.00 18.62 ? 115 GLU   A C   1 
ATOM   810  O  O   . GLU   A 1 115 ? 18.083  -30.315 -33.957 1.00 17.96 ? 115 GLU   A O   1 
ATOM   811  C  CB  . GLU   A 1 115 ? 19.955  -30.806 -36.516 1.00 21.05 ? 115 GLU   A CB  1 
ATOM   812  C  CG  . GLU   A 1 115 ? 20.209  -30.301 -37.929 1.00 21.89 ? 115 GLU   A CG  1 
ATOM   813  C  CD  . GLU   A 1 115 ? 20.347  -31.448 -38.911 1.00 26.68 ? 115 GLU   A CD  1 
ATOM   814  O  OE1 . GLU   A 1 115 ? 20.081  -32.620 -38.569 1.00 29.19 ? 115 GLU   A OE1 1 
ATOM   815  O  OE2 . GLU   A 1 115 ? 20.748  -31.146 -40.039 1.00 27.27 ? 115 GLU   A OE2 1 
ATOM   816  N  N   . GLN   A 1 116 ? 20.252  -30.594 -33.331 1.00 19.35 ? 116 GLN   A N   1 
ATOM   817  C  CA  . GLN   A 1 116 ? 19.928  -31.327 -32.130 1.00 19.57 ? 116 GLN   A CA  1 
ATOM   818  C  C   . GLN   A 1 116 ? 19.081  -30.479 -31.189 1.00 17.70 ? 116 GLN   A C   1 
ATOM   819  O  O   . GLN   A 1 116 ? 18.184  -31.007 -30.535 1.00 18.35 ? 116 GLN   A O   1 
ATOM   820  C  CB  . GLN   A 1 116 ? 21.195  -31.793 -31.401 1.00 21.59 ? 116 GLN   A CB  1 
ATOM   821  C  CG  . GLN   A 1 116 ? 20.913  -32.788 -30.279 1.00 22.66 ? 116 GLN   A CG  1 
ATOM   822  C  CD  . GLN   A 1 116 ? 20.250  -34.059 -30.758 1.00 25.96 ? 116 GLN   A CD  1 
ATOM   823  O  OE1 . GLN   A 1 116 ? 20.649  -34.680 -31.751 1.00 29.61 ? 116 GLN   A OE1 1 
ATOM   824  N  NE2 . GLN   A 1 116 ? 19.237  -34.498 -30.038 1.00 27.94 ? 116 GLN   A NE2 1 
ATOM   825  N  N   . VAL   A 1 117 ? 19.383  -29.187 -31.066 1.00 15.70 ? 117 VAL   A N   1 
ATOM   826  C  CA  . VAL   A 1 117 ? 18.685  -28.389 -30.080 1.00 16.29 ? 117 VAL   A CA  1 
ATOM   827  C  C   . VAL   A 1 117 ? 17.200  -28.266 -30.460 1.00 15.81 ? 117 VAL   A C   1 
ATOM   828  O  O   . VAL   A 1 117 ? 16.343  -28.227 -29.578 1.00 16.44 ? 117 VAL   A O   1 
ATOM   829  C  CB  . VAL   A 1 117 ? 19.329  -27.021 -29.822 1.00 16.67 ? 117 VAL   A CB  1 
ATOM   830  C  CG1 . VAL   A 1 117 ? 19.262  -26.088 -31.019 1.00 17.14 ? 117 VAL   A CG1 1 
ATOM   831  C  CG2 . VAL   A 1 117 ? 18.718  -26.332 -28.602 1.00 17.99 ? 117 VAL   A CG2 1 
ATOM   832  N  N   . GLY   A 1 118 ? 16.905  -28.160 -31.754 1.00 15.90 ? 118 GLY   A N   1 
ATOM   833  C  CA  . GLY   A 1 118 ? 15.519  -28.131 -32.216 1.00 15.06 ? 118 GLY   A CA  1 
ATOM   834  C  C   . GLY   A 1 118 ? 14.767  -29.404 -31.840 1.00 15.05 ? 118 GLY   A C   1 
ATOM   835  O  O   . GLY   A 1 118 ? 13.625  -29.375 -31.385 1.00 14.61 ? 118 GLY   A O   1 
ATOM   836  N  N   . PHE   A 1 119 ? 15.422  -30.545 -32.045 1.00 14.76 ? 119 PHE   A N   1 
ATOM   837  C  CA  . PHE   A 1 119 ? 14.849  -31.827 -31.694 1.00 14.75 ? 119 PHE   A CA  1 
ATOM   838  C  C   . PHE   A 1 119 ? 14.565  -31.849 -30.193 1.00 14.68 ? 119 PHE   A C   1 
ATOM   839  O  O   . PHE   A 1 119 ? 13.455  -32.209 -29.755 1.00 14.43 ? 119 PHE   A O   1 
ATOM   840  C  CB  . PHE   A 1 119 ? 15.783  -32.977 -32.093 1.00 15.28 ? 119 PHE   A CB  1 
ATOM   841  C  CG  . PHE   A 1 119 ? 15.208  -34.329 -31.718 1.00 16.44 ? 119 PHE   A CG  1 
ATOM   842  C  CD1 . PHE   A 1 119 ? 14.402  -35.024 -32.607 1.00 17.73 ? 119 PHE   A CD1 1 
ATOM   843  C  CD2 . PHE   A 1 119 ? 15.426  -34.876 -30.455 1.00 17.32 ? 119 PHE   A CD2 1 
ATOM   844  C  CE1 . PHE   A 1 119 ? 13.817  -36.234 -32.240 1.00 18.37 ? 119 PHE   A CE1 1 
ATOM   845  C  CE2 . PHE   A 1 119 ? 14.864  -36.088 -30.115 1.00 17.98 ? 119 PHE   A CE2 1 
ATOM   846  C  CZ  . PHE   A 1 119 ? 14.057  -36.767 -31.022 1.00 19.00 ? 119 PHE   A CZ  1 
ATOM   847  N  N   . ASP   A 1 120 ? 15.570  -31.458 -29.400 1.00 14.31 ? 120 ASP   A N   1 
ATOM   848  C  CA  . ASP   A 1 120 ? 15.469  -31.540 -27.961 1.00 15.02 ? 120 ASP   A CA  1 
ATOM   849  C  C   . ASP   A 1 120 ? 14.399  -30.579 -27.433 1.00 14.31 ? 120 ASP   A C   1 
ATOM   850  O  O   . ASP   A 1 120 ? 13.659  -30.931 -26.494 1.00 14.30 ? 120 ASP   A O   1 
ATOM   851  C  CB  . ASP   A 1 120 ? 16.817  -31.305 -27.303 1.00 17.29 ? 120 ASP   A CB  1 
ATOM   852  C  CG  . ASP   A 1 120 ? 17.828  -32.429 -27.506 1.00 20.46 ? 120 ASP   A CG  1 
ATOM   853  O  OD1 . ASP   A 1 120 ? 17.427  -33.528 -27.936 1.00 21.96 ? 120 ASP   A OD1 1 
ATOM   854  O  OD2 . ASP   A 1 120 ? 19.014  -32.166 -27.285 1.00 24.36 ? 120 ASP   A OD2 1 
ATOM   855  N  N   . LEU   A 1 121 ? 14.345  -29.373 -28.013 1.00 13.25 ? 121 LEU   A N   1 
ATOM   856  C  CA  . LEU   A 1 121 ? 13.375  -28.376 -27.563 1.00 13.37 ? 121 LEU   A CA  1 
ATOM   857  C  C   . LEU   A 1 121 ? 11.954  -28.865 -27.864 1.00 12.98 ? 121 LEU   A C   1 
ATOM   858  O  O   . LEU   A 1 121 ? 11.065  -28.853 -26.998 1.00 13.24 ? 121 LEU   A O   1 
ATOM   859  C  CB  . LEU   A 1 121 ? 13.677  -27.026 -28.199 1.00 13.35 ? 121 LEU   A CB  1 
ATOM   860  C  CG  . LEU   A 1 121 ? 12.921  -25.841 -27.594 1.00 13.68 ? 121 LEU   A CG  1 
ATOM   861  C  CD1 . LEU   A 1 121 ? 13.752  -24.601 -27.734 1.00 13.67 ? 121 LEU   A CD1 1 
ATOM   862  C  CD2 . LEU   A 1 121 ? 11.547  -25.634 -28.239 1.00 14.17 ? 121 LEU   A CD2 1 
ATOM   863  N  N   . VAL   A 1 122 ? 11.713  -29.320 -29.095 1.00 11.54 ? 122 VAL   A N   1 
ATOM   864  C  CA  . VAL   A 1 122 ? 10.379  -29.783 -29.451 1.00 12.69 ? 122 VAL   A CA  1 
ATOM   865  C  C   . VAL   A 1 122 ? 10.008  -30.973 -28.578 1.00 13.64 ? 122 VAL   A C   1 
ATOM   866  O  O   . VAL   A 1 122 ? 8.883   -31.062 -28.080 1.00 13.94 ? 122 VAL   A O   1 
ATOM   867  C  CB  . VAL   A 1 122 ? 10.244  -30.107 -30.945 1.00 13.05 ? 122 VAL   A CB  1 
ATOM   868  C  CG1 . VAL   A 1 122 ? 8.931   -30.807 -31.245 1.00 13.21 ? 122 VAL   A CG1 1 
ATOM   869  C  CG2 . VAL   A 1 122 ? 10.407  -28.835 -31.762 1.00 12.88 ? 122 VAL   A CG2 1 
ATOM   870  N  N   . LYS   A 1 123 ? 10.952  -31.900 -28.408 1.00 14.36 ? 123 LYS   A N   1 
ATOM   871  C  CA  . LYS   A 1 123 ? 10.640  -33.116 -27.685 1.00 15.58 ? 123 LYS   A CA  1 
ATOM   872  C  C   . LYS   A 1 123 ? 10.275  -32.804 -26.233 1.00 14.46 ? 123 LYS   A C   1 
ATOM   873  O  O   . LYS   A 1 123 ? 9.342   -33.405 -25.692 1.00 14.51 ? 123 LYS   A O   1 
ATOM   874  C  CB  . LYS   A 1 123 ? 11.836  -34.060 -27.747 1.00 19.40 ? 123 LYS   A CB  1 
ATOM   875  C  CG  . LYS   A 1 123 ? 11.582  -35.363 -26.987 1.00 23.56 ? 123 LYS   A CG  1 
ATOM   876  C  CD  . LYS   A 1 123 ? 12.642  -36.399 -27.314 1.00 31.12 ? 123 LYS   A CD  1 
ATOM   877  C  CE  . LYS   A 1 123 ? 14.013  -35.993 -26.844 1.00 41.46 ? 123 LYS   A CE  1 
ATOM   878  N  NZ  . LYS   A 1 123 ? 14.930  -37.144 -26.709 1.00 49.78 ? 123 LYS   A NZ  1 
ATOM   879  N  N   . ALA   A 1 124 ? 11.035  -31.915 -25.587 1.00 14.02 ? 124 ALA   A N   1 
ATOM   880  C  CA  . ALA   A 1 124 ? 10.765  -31.560 -24.203 1.00 14.89 ? 124 ALA   A CA  1 
ATOM   881  C  C   . ALA   A 1 124 ? 9.353   -30.965 -24.075 1.00 14.54 ? 124 ALA   A C   1 
ATOM   882  O  O   . ALA   A 1 124 ? 8.591   -31.316 -23.164 1.00 14.04 ? 124 ALA   A O   1 
ATOM   883  C  CB  . ALA   A 1 124 ? 11.796  -30.569 -23.703 1.00 16.10 ? 124 ALA   A CB  1 
ATOM   884  N  N   . CYS   A 1 125 ? 9.017   -30.041 -24.991 1.00 13.06 ? 125 CYS   A N   1 
ATOM   885  C  CA  . CYS   A 1 125 ? 7.698   -29.424 -24.993 1.00 13.70 ? 125 CYS   A CA  1 
ATOM   886  C  C   . CYS   A 1 125 ? 6.605   -30.458 -25.276 1.00 13.89 ? 125 CYS   A C   1 
ATOM   887  O  O   . CYS   A 1 125 ? 5.534   -30.422 -24.674 1.00 13.61 ? 125 CYS   A O   1 
ATOM   888  C  CB  . CYS   A 1 125 ? 7.663   -28.257 -25.975 1.00 13.85 ? 125 CYS   A CB  1 
ATOM   889  S  SG  . CYS   A 1 125 ? 8.697   -26.887 -25.416 1.00 15.72 ? 125 CYS   A SG  1 
ATOM   890  N  N   . LYS   A 1 126 ? 6.840   -31.364 -26.233 1.00 13.91 ? 126 LYS   A N   1 
ATOM   891  C  CA  . LYS   A 1 126 ? 5.868   -32.389 -26.553 1.00 14.82 ? 126 LYS   A CA  1 
ATOM   892  C  C   . LYS   A 1 126 ? 5.624   -33.307 -25.353 1.00 15.24 ? 126 LYS   A C   1 
ATOM   893  O  O   . LYS   A 1 126 ? 4.487   -33.690 -25.088 1.00 15.67 ? 126 LYS   A O   1 
ATOM   894  C  CB  . LYS   A 1 126 ? 6.345   -33.282 -27.704 1.00 15.92 ? 126 LYS   A CB  1 
ATOM   895  C  CG  . LYS   A 1 126 ? 5.427   -34.464 -28.032 1.00 16.94 ? 126 LYS   A CG  1 
ATOM   896  C  CD  . LYS   A 1 126 ? 3.985   -34.095 -28.377 1.00 19.15 ? 126 LYS   A CD  1 
ATOM   897  C  CE  . LYS   A 1 126 ? 3.093   -35.298 -28.554 1.00 21.87 ? 126 LYS   A CE  1 
ATOM   898  N  NZ  . LYS   A 1 126 ? 3.238   -35.844 -29.895 1.00 26.05 ? 126 LYS   A NZ  1 
ATOM   899  N  N   . GLU   A 1 127 ? 6.686   -33.665 -24.622 1.00 16.69 ? 127 GLU   A N   1 
ATOM   900  C  CA  . GLU   A 1 127 ? 6.510   -34.551 -23.480 1.00 18.71 ? 127 GLU   A CA  1 
ATOM   901  C  C   . GLU   A 1 127 ? 5.569   -33.920 -22.457 1.00 16.69 ? 127 GLU   A C   1 
ATOM   902  O  O   . GLU   A 1 127 ? 4.672   -34.583 -21.924 1.00 17.15 ? 127 GLU   A O   1 
ATOM   903  C  CB  . GLU   A 1 127 ? 7.867   -34.892 -22.873 1.00 21.69 ? 127 GLU   A CB  1 
ATOM   904  C  CG  . GLU   A 1 127 ? 8.611   -35.908 -23.733 1.00 26.29 ? 127 GLU   A CG  1 
ATOM   905  C  CD  . GLU   A 1 127 ? 10.042  -36.184 -23.298 1.00 33.41 ? 127 GLU   A CD  1 
ATOM   906  O  OE1 . GLU   A 1 127 ? 10.574  -35.459 -22.407 1.00 34.38 ? 127 GLU   A OE1 1 
ATOM   907  O  OE2 . GLU   A 1 127 ? 10.617  -37.125 -23.899 1.00 37.68 ? 127 GLU   A OE2 1 
ATOM   908  N  N   . ALA   A 1 128 ? 5.755   -32.621 -22.214 1.00 14.97 ? 128 ALA   A N   1 
ATOM   909  C  CA  . ALA   A 1 128 ? 4.925   -31.911 -21.267 1.00 13.83 ? 128 ALA   A CA  1 
ATOM   910  C  C   . ALA   A 1 128 ? 3.491   -31.858 -21.767 1.00 13.24 ? 128 ALA   A C   1 
ATOM   911  O  O   . ALA   A 1 128 ? 2.550   -32.105 -21.035 1.00 14.83 ? 128 ALA   A O   1 
ATOM   912  C  CB  . ALA   A 1 128 ? 5.485   -30.516 -21.043 1.00 13.86 ? 128 ALA   A CB  1 
ATOM   913  N  N   . CYS   A 1 129 ? 3.314   -31.503 -23.038 1.00 12.94 ? 129 CYS   A N   1 
ATOM   914  C  CA  . CYS   A 1 129 ? 1.994   -31.406 -23.621 1.00 14.02 ? 129 CYS   A CA  1 
ATOM   915  C  C   . CYS   A 1 129 ? 1.264   -32.757 -23.573 1.00 14.80 ? 129 CYS   A C   1 
ATOM   916  O  O   . CYS   A 1 129 ? 0.092   -32.836 -23.192 1.00 14.47 ? 129 CYS   A O   1 
ATOM   917  C  CB  . CYS   A 1 129 ? 2.077   -30.845 -25.036 1.00 14.64 ? 129 CYS   A CB  1 
ATOM   918  S  SG  . CYS   A 1 129 ? 2.444   -29.070 -25.048 1.00 14.68 ? 129 CYS   A SG  1 
ATOM   919  N  N   . ALA   A 1 130 ? 1.956   -33.808 -23.996 1.00 15.00 ? 130 ALA   A N   1 
ATOM   920  C  CA  . ALA   A 1 130 ? 1.328   -35.116 -24.113 1.00 16.65 ? 130 ALA   A CA  1 
ATOM   921  C  C   . ALA   A 1 130 ? 0.837   -35.600 -22.752 1.00 16.76 ? 130 ALA   A C   1 
ATOM   922  O  O   . ALA   A 1 130 ? -0.228  -36.199 -22.658 1.00 17.93 ? 130 ALA   A O   1 
ATOM   923  C  CB  . ALA   A 1 130 ? 2.296   -36.112 -24.702 1.00 18.18 ? 130 ALA   A CB  1 
ATOM   924  N  N   . ALA   A 1 131 ? 1.605   -35.310 -21.707 1.00 16.25 ? 131 ALA   A N   1 
ATOM   925  C  CA  . ALA   A 1 131 ? 1.238   -35.688 -20.351 1.00 17.04 ? 131 ALA   A CA  1 
ATOM   926  C  C   . ALA   A 1 131 ? -0.098  -35.055 -19.942 1.00 16.75 ? 131 ALA   A C   1 
ATOM   927  O  O   . ALA   A 1 131 ? -0.781  -35.603 -19.076 1.00 18.09 ? 131 ALA   A O   1 
ATOM   928  C  CB  . ALA   A 1 131 ? 2.321   -35.258 -19.395 1.00 17.12 ? 131 ALA   A CB  1 
ATOM   929  N  N   . ALA   A 1 132 ? -0.446  -33.893 -20.523 1.00 15.76 ? 132 ALA   A N   1 
ATOM   930  C  CA  . ALA   A 1 132 ? -1.642  -33.156 -20.163 1.00 16.44 ? 132 ALA   A CA  1 
ATOM   931  C  C   . ALA   A 1 132 ? -2.709  -33.240 -21.252 1.00 16.03 ? 132 ALA   A C   1 
ATOM   932  O  O   . ALA   A 1 132 ? -3.680  -32.495 -21.192 1.00 16.68 ? 132 ALA   A O   1 
ATOM   933  C  CB  . ALA   A 1 132 ? -1.272  -31.698 -19.890 1.00 17.38 ? 132 ALA   A CB  1 
ATOM   934  N  N   . ASN   A 1 133 ? -2.518  -34.092 -22.266 1.00 16.66 ? 133 ASN   A N   1 
ATOM   935  C  CA  . ASN   A 1 133 ? -3.426  -34.218 -23.396 1.00 19.34 ? 133 ASN   A CA  1 
ATOM   936  C  C   . ASN   A 1 133 ? -3.595  -32.895 -24.139 1.00 16.97 ? 133 ASN   A C   1 
ATOM   937  O  O   . ASN   A 1 133 ? -4.689  -32.532 -24.577 1.00 17.48 ? 133 ASN   A O   1 
ATOM   938  C  CB  . ASN   A 1 133 ? -4.775  -34.803 -22.970 1.00 25.12 ? 133 ASN   A CB  1 
ATOM   939  C  CG  . ASN   A 1 133 ? -4.612  -36.239 -22.524 1.00 31.59 ? 133 ASN   A CG  1 
ATOM   940  O  OD1 . ASN   A 1 133 ? -4.818  -36.584 -21.354 1.00 46.28 ? 133 ASN   A OD1 1 
ATOM   941  N  ND2 . ASN   A 1 133 ? -4.216  -37.093 -23.450 1.00 36.68 ? 133 ASN   A ND2 1 
ATOM   942  N  N   . VAL   A 1 134 ? -2.483  -32.183 -24.302 1.00 14.78 ? 134 VAL   A N   1 
ATOM   943  C  CA  . VAL   A 1 134 ? -2.453  -30.906 -24.995 1.00 13.85 ? 134 VAL   A CA  1 
ATOM   944  C  C   . VAL   A 1 134 ? -1.726  -31.117 -26.314 1.00 13.70 ? 134 VAL   A C   1 
ATOM   945  O  O   . VAL   A 1 134 ? -0.719  -31.787 -26.349 1.00 13.62 ? 134 VAL   A O   1 
ATOM   946  C  CB  . VAL   A 1 134 ? -1.738  -29.888 -24.082 1.00 13.60 ? 134 VAL   A CB  1 
ATOM   947  C  CG1 . VAL   A 1 134 ? -1.277  -28.624 -24.814 1.00 13.33 ? 134 VAL   A CG1 1 
ATOM   948  C  CG2 . VAL   A 1 134 ? -2.643  -29.513 -22.911 1.00 15.57 ? 134 VAL   A CG2 1 
ATOM   949  N  N   . LEU   A 1 135 ? -2.256  -30.530 -27.389 1.00 14.83 ? 135 LEU   A N   1 
ATOM   950  C  CA  . LEU   A 1 135 ? -1.636  -30.645 -28.694 1.00 15.38 ? 135 LEU   A CA  1 
ATOM   951  C  C   . LEU   A 1 135 ? -0.495  -29.643 -28.807 1.00 13.68 ? 135 LEU   A C   1 
ATOM   952  O  O   . LEU   A 1 135 ? -0.635  -28.509 -28.368 1.00 13.27 ? 135 LEU   A O   1 
ATOM   953  C  CB  . LEU   A 1 135 ? -2.669  -30.365 -29.782 1.00 18.80 ? 135 LEU   A CB  1 
ATOM   954  C  CG  . LEU   A 1 135 ? -3.008  -31.531 -30.717 1.00 30.81 ? 135 LEU   A CG  1 
ATOM   955  C  CD1 . LEU   A 1 135 ? -3.424  -32.797 -29.974 1.00 31.27 ? 135 LEU   A CD1 1 
ATOM   956  C  CD2 . LEU   A 1 135 ? -4.059  -31.134 -31.726 1.00 30.75 ? 135 LEU   A CD2 1 
ATOM   957  N  N   . LEU   A 1 136 ? 0.591   -30.066 -29.451 1.00 12.40 ? 136 LEU   A N   1 
ATOM   958  C  CA  . LEU   A 1 136 ? 1.723   -29.191 -29.711 1.00 11.83 ? 136 LEU   A CA  1 
ATOM   959  C  C   . LEU   A 1 136 ? 1.855   -28.897 -31.205 1.00 12.16 ? 136 LEU   A C   1 
ATOM   960  O  O   . LEU   A 1 136 ? 2.061   -29.800 -32.018 1.00 13.29 ? 136 LEU   A O   1 
ATOM   961  C  CB  . LEU   A 1 136 ? 3.024   -29.825 -29.212 1.00 12.43 ? 136 LEU   A CB  1 
ATOM   962  C  CG  . LEU   A 1 136 ? 4.266   -28.929 -29.343 1.00 13.45 ? 136 LEU   A CG  1 
ATOM   963  C  CD1 . LEU   A 1 136 ? 4.258   -27.801 -28.340 1.00 13.90 ? 136 LEU   A CD1 1 
ATOM   964  C  CD2 . LEU   A 1 136 ? 5.523   -29.771 -29.229 1.00 14.66 ? 136 LEU   A CD2 1 
ATOM   965  N  N   . LYS   A 1 137 ? 1.808   -27.614 -31.531 1.00 11.30 ? 137 LYS   A N   1 
ATOM   966  C  CA  . LYS   A 1 137 ? 2.103   -27.153 -32.867 1.00 10.90 ? 137 LYS   A CA  1 
ATOM   967  C  C   . LYS   A 1 137 ? 3.507   -26.564 -32.812 1.00 11.74 ? 137 LYS   A C   1 
ATOM   968  O  O   . LYS   A 1 137 ? 3.888   -25.908 -31.840 1.00 11.67 ? 137 LYS   A O   1 
ATOM   969  C  CB  . LYS   A 1 137 ? 1.143   -26.073 -33.379 1.00 11.76 ? 137 LYS   A CB  1 
ATOM   970  C  CG  . LYS   A 1 137 ? -0.323  -26.361 -33.195 1.00 12.41 ? 137 LYS   A CG  1 
ATOM   971  C  CD  . LYS   A 1 137 ? -1.223  -25.550 -34.124 1.00 12.41 ? 137 LYS   A CD  1 
ATOM   972  C  CE  . LYS   A 1 137 ? -2.674  -25.510 -33.735 1.00 13.89 ? 137 LYS   A CE  1 
ATOM   973  N  NZ  . LYS   A 1 137 ? -2.956  -24.572 -32.622 1.00 13.67 ? 137 LYS   A NZ  1 
ATOM   974  N  N   . VAL   A 1 138 ? 4.274   -26.772 -33.877 1.00 10.86 ? 138 VAL   A N   1 
ATOM   975  C  CA  . VAL   A 1 138 ? 5.616   -26.190 -33.908 1.00 10.31 ? 138 VAL   A CA  1 
ATOM   976  C  C   . VAL   A 1 138 ? 5.713   -25.207 -35.066 1.00 10.62 ? 138 VAL   A C   1 
ATOM   977  O  O   . VAL   A 1 138 ? 5.538   -25.593 -36.223 1.00 10.84 ? 138 VAL   A O   1 
ATOM   978  C  CB  . VAL   A 1 138 ? 6.701   -27.275 -34.024 1.00 10.92 ? 138 VAL   A CB  1 
ATOM   979  C  CG1 . VAL   A 1 138 ? 8.081   -26.644 -34.172 1.00 11.95 ? 138 VAL   A CG1 1 
ATOM   980  C  CG2 . VAL   A 1 138 ? 6.624   -28.266 -32.866 1.00 11.18 ? 138 VAL   A CG2 1 
ATOM   981  N  N   . ILE   A 1 139 ? 6.031   -23.967 -34.745 1.00 9.86  ? 139 ILE   A N   1 
ATOM   982  C  CA  . ILE   A 1 139 ? 6.240   -22.904 -35.714 1.00 10.56 ? 139 ILE   A CA  1 
ATOM   983  C  C   . ILE   A 1 139 ? 7.681   -22.938 -36.208 1.00 11.22 ? 139 ILE   A C   1 
ATOM   984  O  O   . ILE   A 1 139 ? 8.599   -22.726 -35.409 1.00 10.65 ? 139 ILE   A O   1 
ATOM   985  C  CB  . ILE   A 1 139 ? 5.941   -21.525 -35.090 1.00 10.40 ? 139 ILE   A CB  1 
ATOM   986  C  CG1 . ILE   A 1 139 ? 4.520   -21.421 -34.543 1.00 10.93 ? 139 ILE   A CG1 1 
ATOM   987  C  CG2 . ILE   A 1 139 ? 6.257   -20.442 -36.115 1.00 10.88 ? 139 ILE   A CG2 1 
ATOM   988  C  CD1 . ILE   A 1 139 ? 4.344   -20.324 -33.509 1.00 10.83 ? 139 ILE   A CD1 1 
ATOM   989  N  N   . ILE   A 1 140 ? 7.914   -23.155 -37.516 1.00 11.15 ? 140 ILE   A N   1 
ATOM   990  C  CA  . ILE   A 1 140 ? 9.284   -23.245 -37.996 1.00 11.68 ? 140 ILE   A CA  1 
ATOM   991  C  C   . ILE   A 1 140 ? 9.798   -21.938 -38.598 1.00 12.09 ? 140 ILE   A C   1 
ATOM   992  O  O   . ILE   A 1 140 ? 11.000  -21.819 -38.793 1.00 11.88 ? 140 ILE   A O   1 
ATOM   993  C  CB  . ILE   A 1 140 ? 9.466   -24.435 -38.956 1.00 12.88 ? 140 ILE   A CB  1 
ATOM   994  C  CG1 . ILE   A 1 140 ? 8.630   -24.264 -40.208 1.00 14.09 ? 140 ILE   A CG1 1 
ATOM   995  C  CG2 . ILE   A 1 140 ? 9.164   -25.776 -38.259 1.00 12.14 ? 140 ILE   A CG2 1 
ATOM   996  C  CD1 . ILE   A 1 140 ? 9.033   -25.218 -41.312 1.00 14.93 ? 140 ILE   A CD1 1 
ATOM   997  N  N   . GLU   A 1 141 ? 8.911   -20.962 -38.846 1.00 12.18 ? 141 GLU   A N   1 
ATOM   998  C  CA  . GLU   A 1 141 ? 9.270   -19.643 -39.373 1.00 11.64 ? 141 GLU   A CA  1 
ATOM   999  C  C   . GLU   A 1 141 ? 9.880   -19.738 -40.782 1.00 12.75 ? 141 GLU   A C   1 
ATOM   1000 O  O   . GLU   A 1 141 ? 11.043  -19.371 -41.030 1.00 12.79 ? 141 GLU   A O   1 
ATOM   1001 C  CB  . GLU   A 1 141 ? 10.145  -18.864 -38.397 1.00 12.38 ? 141 GLU   A CB  1 
ATOM   1002 C  CG  . GLU   A 1 141 ? 9.992   -17.360 -38.583 1.00 13.12 ? 141 GLU   A CG  1 
ATOM   1003 C  CD  . GLU   A 1 141 ? 8.689   -16.782 -38.092 1.00 13.73 ? 141 GLU   A CD  1 
ATOM   1004 O  OE1 . GLU   A 1 141 ? 7.624   -17.018 -38.758 1.00 13.22 ? 141 GLU   A OE1 1 
ATOM   1005 O  OE2 . GLU   A 1 141 ? 8.719   -16.052 -37.048 1.00 14.51 ? 141 GLU   A OE2 1 
ATOM   1006 N  N   . THR   A 1 142 ? 9.035   -20.168 -41.712 1.00 12.64 ? 142 THR   A N   1 
ATOM   1007 C  CA  . THR   A 1 142 ? 9.479   -20.436 -43.079 1.00 13.33 ? 142 THR   A CA  1 
ATOM   1008 C  C   . THR   A 1 142 ? 10.025  -19.158 -43.729 1.00 14.31 ? 142 THR   A C   1 
ATOM   1009 O  O   . THR   A 1 142 ? 10.899  -19.234 -44.585 1.00 14.96 ? 142 THR   A O   1 
ATOM   1010 C  CB  . THR   A 1 142 ? 8.323   -21.002 -43.902 1.00 12.69 ? 142 THR   A CB  1 
ATOM   1011 O  OG1 . THR   A 1 142 ? 7.246   -20.085 -43.794 1.00 13.48 ? 142 THR   A OG1 1 
ATOM   1012 C  CG2 . THR   A 1 142 ? 7.855   -22.376 -43.460 1.00 12.86 ? 142 THR   A CG2 1 
ATOM   1013 N  N   . GLY   A 1 143 ? 9.500   -17.999 -43.332 1.00 14.55 ? 143 GLY   A N   1 
ATOM   1014 C  CA  . GLY   A 1 143 ? 9.908   -16.716 -43.884 1.00 16.07 ? 143 GLY   A CA  1 
ATOM   1015 C  C   . GLY   A 1 143 ? 11.318  -16.298 -43.457 1.00 17.90 ? 143 GLY   A C   1 
ATOM   1016 O  O   . GLY   A 1 143 ? 11.941  -15.477 -44.134 1.00 20.77 ? 143 GLY   A O   1 
ATOM   1017 N  N   . GLU   A 1 144 ? 11.850  -16.904 -42.387 1.00 16.82 ? 144 GLU   A N   1 
ATOM   1018 C  CA  . GLU   A 1 144 ? 13.234  -16.682 -41.968 1.00 17.11 ? 144 GLU   A CA  1 
ATOM   1019 C  C   . GLU   A 1 144 ? 14.146  -17.791 -42.489 1.00 17.33 ? 144 GLU   A C   1 
ATOM   1020 O  O   . GLU   A 1 144 ? 15.289  -17.528 -42.850 1.00 19.27 ? 144 GLU   A O   1 
ATOM   1021 C  CB  . GLU   A 1 144 ? 13.316  -16.531 -40.445 1.00 17.82 ? 144 GLU   A CB  1 
ATOM   1022 C  CG  . GLU   A 1 144 ? 12.636  -15.270 -39.913 1.00 19.16 ? 144 GLU   A CG  1 
ATOM   1023 C  CD  . GLU   A 1 144 ? 13.235  -13.976 -40.422 1.00 23.97 ? 144 GLU   A CD  1 
ATOM   1024 O  OE1 . GLU   A 1 144 ? 14.474  -13.933 -40.507 1.00 24.19 ? 144 GLU   A OE1 1 
ATOM   1025 O  OE2 . GLU   A 1 144 ? 12.480  -13.053 -40.774 1.00 26.33 ? 144 GLU   A OE2 1 
ATOM   1026 N  N   . LEU   A 1 145 ? 13.674  -19.041 -42.525 1.00 15.24 ? 145 LEU   A N   1 
ATOM   1027 C  CA  . LEU   A 1 145 ? 14.421  -20.137 -43.100 1.00 16.80 ? 145 LEU   A CA  1 
ATOM   1028 C  C   . LEU   A 1 145 ? 14.674  -19.903 -44.596 1.00 18.63 ? 145 LEU   A C   1 
ATOM   1029 O  O   . LEU   A 1 145 ? 15.797  -20.140 -45.048 1.00 18.22 ? 145 LEU   A O   1 
ATOM   1030 C  CB  . LEU   A 1 145 ? 13.751  -21.480 -42.893 1.00 16.98 ? 145 LEU   A CB  1 
ATOM   1031 C  CG  . LEU   A 1 145 ? 13.611  -21.924 -41.435 1.00 17.31 ? 145 LEU   A CG  1 
ATOM   1032 C  CD1 . LEU   A 1 145 ? 12.706  -23.121 -41.335 1.00 17.60 ? 145 LEU   A CD1 1 
ATOM   1033 C  CD2 . LEU   A 1 145 ? 14.959  -22.222 -40.794 1.00 18.39 ? 145 LEU   A CD2 1 
ATOM   1034 N  N   . LYS   A 1 146 ? 13.609  -19.524 -45.325 1.00 18.77 ? 146 LYS   A N   1 
ATOM   1035 C  CA  . LYS   A 1 146 ? 13.634  -19.137 -46.737 1.00 23.84 ? 146 LYS   A CA  1 
ATOM   1036 C  C   . LYS   A 1 146 ? 13.909  -20.322 -47.670 1.00 24.58 ? 146 LYS   A C   1 
ATOM   1037 O  O   . LYS   A 1 146 ? 13.153  -20.593 -48.594 1.00 33.64 ? 146 LYS   A O   1 
ATOM   1038 C  CB  . LYS   A 1 146 ? 14.626  -17.994 -46.948 1.00 29.51 ? 146 LYS   A CB  1 
ATOM   1039 C  CG  . LYS   A 1 146 ? 14.193  -16.690 -46.302 1.00 33.80 ? 146 LYS   A CG  1 
ATOM   1040 C  CD  . LYS   A 1 146 ? 15.305  -15.654 -46.159 1.00 40.87 ? 146 LYS   A CD  1 
ATOM   1041 C  CE  . LYS   A 1 146 ? 14.831  -14.461 -45.360 1.00 44.44 ? 146 LYS   A CE  1 
ATOM   1042 N  NZ  . LYS   A 1 146 ? 15.931  -13.530 -45.086 1.00 47.93 ? 146 LYS   A NZ  1 
ATOM   1043 N  N   . ASP   A 1 147 ? 14.941  -21.079 -47.380 1.00 23.26 ? 147 ASP   A N   1 
ATOM   1044 C  CA  . ASP   A 1 147 ? 15.406  -22.145 -48.222 1.00 23.46 ? 147 ASP   A CA  1 
ATOM   1045 C  C   . ASP   A 1 147 ? 14.540  -23.381 -48.072 1.00 21.25 ? 147 ASP   A C   1 
ATOM   1046 O  O   . ASP   A 1 147 ? 14.266  -23.825 -46.947 1.00 18.74 ? 147 ASP   A O   1 
ATOM   1047 C  CB  . ASP   A 1 147 ? 16.850  -22.414 -47.849 1.00 26.73 ? 147 ASP   A CB  1 
ATOM   1048 C  CG  . ASP   A 1 147 ? 17.416  -23.645 -48.495 1.00 31.59 ? 147 ASP   A CG  1 
ATOM   1049 O  OD1 . ASP   A 1 147 ? 17.728  -23.553 -49.676 1.00 37.03 ? 147 ASP   A OD1 1 
ATOM   1050 O  OD2 . ASP   A 1 147 ? 17.419  -24.691 -47.828 1.00 35.88 ? 147 ASP   A OD2 1 
ATOM   1051 N  N   . GLU   A 1 148 ? 14.185  -23.983 -49.212 1.00 18.87 ? 148 GLU   A N   1 
ATOM   1052 C  CA  . GLU   A 1 148 ? 13.393  -25.203 -49.241 1.00 18.93 ? 148 GLU   A CA  1 
ATOM   1053 C  C   . GLU   A 1 148 ? 14.016  -26.298 -48.370 1.00 19.18 ? 148 GLU   A C   1 
ATOM   1054 O  O   . GLU   A 1 148 ? 13.315  -26.979 -47.608 1.00 18.19 ? 148 GLU   A O   1 
ATOM   1055 C  CB  . GLU   A 1 148 ? 13.208  -25.706 -50.680 1.00 21.50 ? 148 GLU   A CB  1 
ATOM   1056 C  CG  . GLU   A 1 148 ? 12.563  -27.085 -50.720 1.00 24.65 ? 148 GLU   A CG  1 
ATOM   1057 C  CD  . GLU   A 1 148 ? 12.159  -27.637 -52.076 1.00 31.14 ? 148 GLU   A CD  1 
ATOM   1058 O  OE1 . GLU   A 1 148 ? 12.409  -26.924 -53.052 1.00 31.76 ? 148 GLU   A OE1 1 
ATOM   1059 O  OE2 . GLU   A 1 148 ? 11.593  -28.760 -52.136 1.00 34.63 ? 148 GLU   A OE2 1 
ATOM   1060 N  N   . ALA   A 1 149 ? 15.337  -26.509 -48.492 1.00 18.94 ? 149 ALA   A N   1 
ATOM   1061 C  CA  . ALA   A 1 149 ? 16.006  -27.569 -47.758 1.00 19.72 ? 149 ALA   A CA  1 
ATOM   1062 C  C   . ALA   A 1 149 ? 15.871  -27.343 -46.248 1.00 16.96 ? 149 ALA   A C   1 
ATOM   1063 O  O   . ALA   A 1 149 ? 15.665  -28.291 -45.481 1.00 17.16 ? 149 ALA   A O   1 
ATOM   1064 C  CB  . ALA   A 1 149 ? 17.465  -27.703 -48.209 1.00 20.57 ? 149 ALA   A CB  1 
ATOM   1065 N  N   . LEU   A 1 150 ? 16.031  -26.095 -45.811 1.00 16.42 ? 150 LEU   A N   1 
ATOM   1066 C  CA  . LEU   A 1 150 ? 15.906  -25.790 -44.389 1.00 16.69 ? 150 LEU   A CA  1 
ATOM   1067 C  C   . LEU   A 1 150 ? 14.457  -25.912 -43.915 1.00 15.23 ? 150 LEU   A C   1 
ATOM   1068 O  O   . LEU   A 1 150 ? 14.212  -26.328 -42.792 1.00 14.88 ? 150 LEU   A O   1 
ATOM   1069 C  CB  . LEU   A 1 150 ? 16.428  -24.389 -44.101 1.00 17.31 ? 150 LEU   A CB  1 
ATOM   1070 C  CG  . LEU   A 1 150 ? 17.951  -24.211 -44.058 1.00 19.57 ? 150 LEU   A CG  1 
ATOM   1071 C  CD1 . LEU   A 1 150 ? 18.253  -22.730 -44.051 1.00 20.26 ? 150 LEU   A CD1 1 
ATOM   1072 C  CD2 . LEU   A 1 150 ? 18.475  -24.864 -42.803 1.00 21.42 ? 150 LEU   A CD2 1 
ATOM   1073 N  N   . ILE   A 1 151 ? 13.485  -25.562 -44.753 1.00 15.18 ? 151 ILE   A N   1 
ATOM   1074 C  CA  . ILE   A 1 151 ? 12.089  -25.718 -44.360 1.00 14.06 ? 151 ILE   A CA  1 
ATOM   1075 C  C   . ILE   A 1 151 ? 11.773  -27.204 -44.191 1.00 13.57 ? 151 ILE   A C   1 
ATOM   1076 O  O   . ILE   A 1 151 ? 11.127  -27.615 -43.233 1.00 13.64 ? 151 ILE   A O   1 
ATOM   1077 C  CB  . ILE   A 1 151 ? 11.199  -25.031 -45.399 1.00 13.82 ? 151 ILE   A CB  1 
ATOM   1078 C  CG1 . ILE   A 1 151 ? 11.409  -23.540 -45.362 1.00 13.74 ? 151 ILE   A CG1 1 
ATOM   1079 C  CG2 . ILE   A 1 151 ? 9.746   -25.465 -45.262 1.00 13.75 ? 151 ILE   A CG2 1 
ATOM   1080 C  CD1 . ILE   A 1 151 ? 10.735  -22.794 -46.493 1.00 15.29 ? 151 ILE   A CD1 1 
ATOM   1081 N  N   . ARG   A 1 152 ? 12.270  -28.041 -45.115 1.00 14.00 ? 152 ARG   A N   1 
ATOM   1082 C  CA  . ARG   A 1 152 ? 12.070  -29.480 -44.979 1.00 14.86 ? 152 ARG   A CA  1 
ATOM   1083 C  C   . ARG   A 1 152 ? 12.725  -30.008 -43.717 1.00 14.38 ? 152 ARG   A C   1 
ATOM   1084 O  O   . ARG   A 1 152 ? 12.145  -30.852 -43.027 1.00 15.08 ? 152 ARG   A O   1 
ATOM   1085 C  CB  . ARG   A 1 152 ? 12.624  -30.247 -46.185 1.00 16.04 ? 152 ARG   A CB  1 
ATOM   1086 C  CG  . ARG   A 1 152 ? 11.803  -30.057 -47.446 1.00 17.90 ? 152 ARG   A CG  1 
ATOM   1087 C  CD  . ARG   A 1 152 ? 12.214  -31.040 -48.557 1.00 20.18 ? 152 ARG   A CD  1 
ATOM   1088 N  NE  . ARG   A 1 152 ? 11.564  -30.609 -49.794 1.00 24.79 ? 152 ARG   A NE  1 
ATOM   1089 C  CZ  . ARG   A 1 152 ? 10.309  -30.885 -50.146 1.00 27.15 ? 152 ARG   A CZ  1 
ATOM   1090 N  NH1 . ARG   A 1 152 ? 9.577   -31.754 -49.460 1.00 28.87 ? 152 ARG   A NH1 1 
ATOM   1091 N  NH2 . ARG   A 1 152 ? 9.803   -30.297 -51.218 1.00 30.26 ? 152 ARG   A NH2 1 
ATOM   1092 N  N   . LYS   A 1 153 ? 13.943  -29.550 -43.451 1.00 15.26 ? 153 LYS   A N   1 
ATOM   1093 C  CA  . LYS   A 1 153 ? 14.715  -30.068 -42.331 1.00 16.66 ? 153 LYS   A CA  1 
ATOM   1094 C  C   . LYS   A 1 153 ? 14.022  -29.700 -41.015 1.00 14.24 ? 153 LYS   A C   1 
ATOM   1095 O  O   . LYS   A 1 153 ? 13.893  -30.536 -40.131 1.00 14.61 ? 153 LYS   A O   1 
ATOM   1096 C  CB  . LYS   A 1 153 ? 16.147  -29.531 -42.310 1.00 18.43 ? 153 LYS   A CB  1 
ATOM   1097 C  CG  . LYS   A 1 153 ? 17.027  -30.125 -41.223 1.00 21.89 ? 153 LYS   A CG  1 
ATOM   1098 C  CD  . LYS   A 1 153 ? 17.063  -31.643 -41.201 1.00 25.27 ? 153 LYS   A CD  1 
ATOM   1099 C  CE  . LYS   A 1 153 ? 17.733  -32.166 -42.425 1.00 30.21 ? 153 LYS   A CE  1 
ATOM   1100 N  NZ  . LYS   A 1 153 ? 17.815  -33.634 -42.350 1.00 32.02 ? 153 LYS   A NZ  1 
ATOM   1101 N  N   . ALA   A 1 154 ? 13.584  -28.439 -40.887 1.00 14.14 ? 154 ALA   A N   1 
ATOM   1102 C  CA  . ALA   A 1 154 ? 12.903  -28.028 -39.660 1.00 13.02 ? 154 ALA   A CA  1 
ATOM   1103 C  C   . ALA   A 1 154 ? 11.615  -28.838 -39.450 1.00 12.94 ? 154 ALA   A C   1 
ATOM   1104 O  O   . ALA   A 1 154 ? 11.269  -29.223 -38.330 1.00 13.01 ? 154 ALA   A O   1 
ATOM   1105 C  CB  . ALA   A 1 154 ? 12.637  -26.541 -39.701 1.00 12.12 ? 154 ALA   A CB  1 
ATOM   1106 N  N   . SER   A 1 155 ? 10.884  -29.055 -40.556 1.00 12.97 ? 155 SER   A N   1 
ATOM   1107 C  CA  . SER   A 1 155 ? 9.657   -29.841 -40.552 1.00 13.12 ? 155 SER   A CA  1 
ATOM   1108 C  C   . SER   A 1 155 ? 9.950   -31.274 -40.111 1.00 13.99 ? 155 SER   A C   1 
ATOM   1109 O  O   . SER   A 1 155 ? 9.278   -31.802 -39.224 1.00 14.00 ? 155 SER   A O   1 
ATOM   1110 C  CB  . SER   A 1 155 ? 8.973   -29.802 -41.903 1.00 13.21 ? 155 SER   A CB  1 
ATOM   1111 O  OG  . SER   A 1 155 ? 8.623   -28.482 -42.287 1.00 12.53 ? 155 SER   A OG  1 
ATOM   1112 N  N   . GLU   A 1 156 ? 10.994  -31.883 -40.691 1.00 13.99 ? 156 GLU   A N   1 
ATOM   1113 C  CA  . GLU   A 1 156 ? 11.367  -33.255 -40.357 1.00 16.07 ? 156 GLU   A CA  1 
ATOM   1114 C  C   . GLU   A 1 156 ? 11.747  -33.411 -38.885 1.00 14.99 ? 156 GLU   A C   1 
ATOM   1115 O  O   . GLU   A 1 156 ? 11.323  -34.351 -38.209 1.00 15.79 ? 156 GLU   A O   1 
ATOM   1116 C  CB  . GLU   A 1 156 ? 12.566  -33.625 -41.232 1.00 19.16 ? 156 GLU   A CB  1 
ATOM   1117 C  CG  . GLU   A 1 156 ? 13.179  -34.989 -40.952 1.00 26.55 ? 156 GLU   A CG  1 
ATOM   1118 C  CD  . GLU   A 1 156 ? 14.475  -35.177 -41.750 1.00 33.52 ? 156 GLU   A CD  1 
ATOM   1119 O  OE1 . GLU   A 1 156 ? 14.909  -34.243 -42.507 1.00 32.30 ? 156 GLU   A OE1 1 
ATOM   1120 O  OE2 . GLU   A 1 156 ? 15.050  -36.288 -41.621 1.00 39.38 ? 156 GLU   A OE2 1 
ATOM   1121 N  N   . ILE   A 1 157 ? 12.590  -32.505 -38.402 1.00 14.55 ? 157 ILE   A N   1 
ATOM   1122 C  CA  . ILE   A 1 157 ? 13.054  -32.561 -37.022 1.00 14.99 ? 157 ILE   A CA  1 
ATOM   1123 C  C   . ILE   A 1 157 ? 11.854  -32.439 -36.087 1.00 14.90 ? 157 ILE   A C   1 
ATOM   1124 O  O   . ILE   A 1 157 ? 11.732  -33.191 -35.120 1.00 14.16 ? 157 ILE   A O   1 
ATOM   1125 C  CB  . ILE   A 1 157 ? 14.094  -31.469 -36.754 1.00 15.28 ? 157 ILE   A CB  1 
ATOM   1126 C  CG1 . ILE   A 1 157 ? 15.406  -31.750 -37.508 1.00 15.33 ? 157 ILE   A CG1 1 
ATOM   1127 C  CG2 . ILE   A 1 157 ? 14.330  -31.290 -35.249 1.00 15.49 ? 157 ILE   A CG2 1 
ATOM   1128 C  CD1 . ILE   A 1 157 ? 16.322  -30.549 -37.594 1.00 15.76 ? 157 ILE   A CD1 1 
ATOM   1129 N  N   . SER   A 1 158 ? 10.987  -31.465 -36.360 1.00 14.02 ? 158 SER   A N   1 
ATOM   1130 C  CA  . SER   A 1 158 ? 9.804   -31.235 -35.546 1.00 13.31 ? 158 SER   A CA  1 
ATOM   1131 C  C   . SER   A 1 158 ? 8.929   -32.476 -35.481 1.00 13.51 ? 158 SER   A C   1 
ATOM   1132 O  O   . SER   A 1 158 ? 8.465   -32.860 -34.417 1.00 13.26 ? 158 SER   A O   1 
ATOM   1133 C  CB  . SER   A 1 158 ? 9.035   -30.044 -36.061 1.00 13.20 ? 158 SER   A CB  1 
ATOM   1134 O  OG  . SER   A 1 158 ? 9.841   -28.872 -35.980 1.00 13.10 ? 158 SER   A OG  1 
ATOM   1135 N  N   . ILE   A 1 159 ? 8.683   -33.100 -36.625 1.00 13.87 ? 159 ILE   A N   1 
ATOM   1136 C  CA  . ILE   A 1 159 ? 7.874   -34.300 -36.663 1.00 14.37 ? 159 ILE   A CA  1 
ATOM   1137 C  C   . ILE   A 1 159 ? 8.545   -35.438 -35.888 1.00 14.62 ? 159 ILE   A C   1 
ATOM   1138 O  O   . ILE   A 1 159 ? 7.866   -36.143 -35.128 1.00 14.78 ? 159 ILE   A O   1 
ATOM   1139 C  CB  . ILE   A 1 159 ? 7.609   -34.674 -38.128 1.00 14.63 ? 159 ILE   A CB  1 
ATOM   1140 C  CG1 . ILE   A 1 159 ? 6.613   -33.685 -38.742 1.00 14.71 ? 159 ILE   A CG1 1 
ATOM   1141 C  CG2 . ILE   A 1 159 ? 7.123   -36.121 -38.231 1.00 14.84 ? 159 ILE   A CG2 1 
ATOM   1142 C  CD1 . ILE   A 1 159 ? 6.552   -33.754 -40.266 1.00 16.18 ? 159 ILE   A CD1 1 
ATOM   1143 N  N   . LYS   A 1 160 ? 9.845   -35.641 -36.120 1.00 15.01 ? 160 LYS   A N   1 
ATOM   1144 C  CA  . LYS   A 1 160 ? 10.570  -36.689 -35.401 1.00 16.37 ? 160 LYS   A CA  1 
ATOM   1145 C  C   . LYS   A 1 160 ? 10.499  -36.482 -33.894 1.00 16.88 ? 160 LYS   A C   1 
ATOM   1146 O  O   . LYS   A 1 160 ? 10.458  -37.449 -33.130 1.00 16.25 ? 160 LYS   A O   1 
ATOM   1147 C  CB  . LYS   A 1 160 ? 12.035  -36.760 -35.832 1.00 18.42 ? 160 LYS   A CB  1 
ATOM   1148 C  CG  . LYS   A 1 160 ? 12.158  -37.400 -37.199 1.00 21.48 ? 160 LYS   A CG  1 
ATOM   1149 C  CD  . LYS   A 1 160 ? 13.604  -37.452 -37.664 1.00 25.61 ? 160 LYS   A CD  1 
ATOM   1150 C  CE  . LYS   A 1 160 ? 13.741  -38.301 -38.905 1.00 31.68 ? 160 LYS   A CE  1 
ATOM   1151 N  NZ  . LYS   A 1 160 ? 15.038  -38.063 -39.554 1.00 35.51 ? 160 LYS   A NZ  1 
ATOM   1152 N  N   . ALA   A 1 161 ? 10.528  -35.217 -33.462 1.00 15.97 ? 161 ALA   A N   1 
ATOM   1153 C  CA  . ALA   A 1 161 ? 10.468  -34.924 -32.032 1.00 16.78 ? 161 ALA   A CA  1 
ATOM   1154 C  C   . ALA   A 1 161 ? 9.060   -35.020 -31.433 1.00 18.94 ? 161 ALA   A C   1 
ATOM   1155 O  O   . ALA   A 1 161 ? 8.900   -34.871 -30.201 1.00 17.63 ? 161 ALA   A O   1 
ATOM   1156 C  CB  . ALA   A 1 161 ? 11.059  -33.569 -31.779 1.00 16.30 ? 161 ALA   A CB  1 
ATOM   1157 N  N   . GLY   A 1 162 ? 8.034   -35.181 -32.283 1.00 16.17 ? 162 GLY   A N   1 
ATOM   1158 C  CA  . GLY   A 1 162 ? 6.681   -35.482 -31.838 1.00 16.68 ? 162 GLY   A CA  1 
ATOM   1159 C  C   . GLY   A 1 162 ? 5.698   -34.328 -32.040 1.00 15.42 ? 162 GLY   A C   1 
ATOM   1160 O  O   . GLY   A 1 162 ? 4.611   -34.357 -31.477 1.00 16.27 ? 162 GLY   A O   1 
ATOM   1161 N  N   . ALA   A 1 163 ? 6.018   -33.337 -32.870 1.00 14.76 ? 163 ALA   A N   1 
ATOM   1162 C  CA  . ALA   A 1 163 ? 5.031   -32.310 -33.198 1.00 13.89 ? 163 ALA   A CA  1 
ATOM   1163 C  C   . ALA   A 1 163 ? 3.694   -32.909 -33.637 1.00 13.92 ? 163 ALA   A C   1 
ATOM   1164 O  O   . ALA   A 1 163 ? 3.655   -33.820 -34.469 1.00 14.57 ? 163 ALA   A O   1 
ATOM   1165 C  CB  . ALA   A 1 163 ? 5.552   -31.423 -34.293 1.00 14.17 ? 163 ALA   A CB  1 
ATOM   1166 N  N   . ASP   A 1 164 ? 2.586   -32.339 -33.144 1.00 13.12 ? 164 ASP   A N   1 
ATOM   1167 C  CA  . ASP   A 1 164 ? 1.264   -32.748 -33.584 1.00 13.80 ? 164 ASP   A CA  1 
ATOM   1168 C  C   . ASP   A 1 164 ? 0.817   -31.943 -34.804 1.00 12.73 ? 164 ASP   A C   1 
ATOM   1169 O  O   . ASP   A 1 164 ? -0.102  -32.352 -35.525 1.00 13.97 ? 164 ASP   A O   1 
ATOM   1170 C  CB  . ASP   A 1 164 ? 0.264   -32.582 -32.454 1.00 13.72 ? 164 ASP   A CB  1 
ATOM   1171 C  CG  . ASP   A 1 164 ? 0.625   -33.404 -31.225 1.00 15.19 ? 164 ASP   A CG  1 
ATOM   1172 O  OD1 . ASP   A 1 164 ? 0.899   -34.630 -31.409 1.00 16.20 ? 164 ASP   A OD1 1 
ATOM   1173 O  OD2 . ASP   A 1 164 ? 0.661   -32.806 -30.099 1.00 15.66 ? 164 ASP   A OD2 1 
ATOM   1174 N  N   . PHE   A 1 165 ? 1.411   -30.766 -34.966 1.00 12.32 ? 165 PHE   A N   1 
ATOM   1175 C  CA  . PHE   A 1 165 ? 1.233   -29.893 -36.118 1.00 12.46 ? 165 PHE   A CA  1 
ATOM   1176 C  C   . PHE   A 1 165 ? 2.548   -29.193 -36.441 1.00 11.65 ? 165 PHE   A C   1 
ATOM   1177 O  O   . PHE   A 1 165 ? 3.351   -28.932 -35.543 1.00 10.70 ? 165 PHE   A O   1 
ATOM   1178 C  CB  . PHE   A 1 165 ? 0.303   -28.712 -35.819 1.00 12.46 ? 165 PHE   A CB  1 
ATOM   1179 C  CG  . PHE   A 1 165 ? -1.178  -28.897 -36.117 1.00 13.77 ? 165 PHE   A CG  1 
ATOM   1180 C  CD1 . PHE   A 1 165 ? -2.004  -29.567 -35.246 1.00 16.47 ? 165 PHE   A CD1 1 
ATOM   1181 C  CD2 . PHE   A 1 165 ? -1.742  -28.311 -37.242 1.00 14.41 ? 165 PHE   A CD2 1 
ATOM   1182 C  CE1 . PHE   A 1 165 ? -3.368  -29.664 -35.508 1.00 16.59 ? 165 PHE   A CE1 1 
ATOM   1183 C  CE2 . PHE   A 1 165 ? -3.093  -28.454 -37.514 1.00 16.30 ? 165 PHE   A CE2 1 
ATOM   1184 C  CZ  . PHE   A 1 165 ? -3.896  -29.137 -36.650 1.00 16.37 ? 165 PHE   A CZ  1 
ATOM   1185 N  N   . ILE   A 1 166 ? 2.757   -28.917 -37.729 1.00 11.33 ? 166 ILE   A N   1 
ATOM   1186 C  CA  . ILE   A 1 166 ? 3.808   -27.994 -38.119 1.00 11.56 ? 166 ILE   A CA  1 
ATOM   1187 C  C   . ILE   A 1 166 ? 3.125   -26.764 -38.717 1.00 12.27 ? 166 ILE   A C   1 
ATOM   1188 O  O   . ILE   A 1 166 ? 2.119   -26.872 -39.443 1.00 11.71 ? 166 ILE   A O   1 
ATOM   1189 C  CB  . ILE   A 1 166 ? 4.858   -28.664 -39.023 1.00 12.22 ? 166 ILE   A CB  1 
ATOM   1190 C  CG1 . ILE   A 1 166 ? 4.239   -29.305 -40.255 1.00 12.90 ? 166 ILE   A CG1 1 
ATOM   1191 C  CG2 . ILE   A 1 166 ? 5.674   -29.665 -38.210 1.00 13.67 ? 166 ILE   A CG2 1 
ATOM   1192 C  CD1 . ILE   A 1 166 ? 5.261   -29.805 -41.268 1.00 13.35 ? 166 ILE   A CD1 1 
ATOM   1193 N  N   . LYS   A 1 167 ? 3.641   -25.604 -38.300 1.00 11.39 ? 167 LYS   A N   1 
ATOM   1194 C  CA  . LYS   A 1 167 ? 3.006   -24.328 -38.558 1.00 11.86 ? 167 LYS   A CA  1 
ATOM   1195 C  C   . LYS   A 1 167 ? 4.010   -23.433 -39.276 1.00 11.56 ? 167 LYS   A C   1 
ATOM   1196 O  O   . LYS   A 1 167 ? 5.183   -23.374 -38.899 1.00 11.44 ? 167 LYS   A O   1 
ATOM   1197 C  CB  . LYS   A 1 167 ? 2.556   -23.802 -37.187 1.00 12.46 ? 167 LYS   A CB  1 
ATOM   1198 C  CG  . LYS   A 1 167 ? 2.070   -22.368 -37.146 1.00 13.73 ? 167 LYS   A CG  1 
ATOM   1199 C  CD  . LYS   A 1 167 ? 1.455   -22.017 -35.801 1.00 14.32 ? 167 LYS   A CD  1 
ATOM   1200 C  CE  . LYS   A 1 167 ? 1.275   -20.576 -35.769 1.00 15.51 ? 167 LYS   A CE  1 
ATOM   1201 N  NZ  . LYS   A 1 167 ? 0.617   -20.068 -34.560 1.00 17.52 ? 167 LYS   A NZ  1 
ATOM   1202 N  N   . THR   A 1 168 ? 3.551   -22.641 -40.257 1.00 11.75 ? 168 THR   A N   1 
ATOM   1203 C  CA  . THR   A 1 168 ? 4.515   -21.907 -41.075 1.00 11.76 ? 168 THR   A CA  1 
ATOM   1204 C  C   . THR   A 1 168 ? 5.254   -20.840 -40.273 1.00 11.34 ? 168 THR   A C   1 
ATOM   1205 O  O   . THR   A 1 168 ? 6.463   -20.657 -40.444 1.00 12.20 ? 168 THR   A O   1 
ATOM   1206 C  CB  . THR   A 1 168 ? 3.840   -21.273 -42.292 1.00 11.85 ? 168 THR   A CB  1 
ATOM   1207 O  OG1 . THR   A 1 168 ? 2.898   -20.281 -41.888 1.00 11.61 ? 168 THR   A OG1 1 
ATOM   1208 C  CG2 . THR   A 1 168 ? 3.193   -22.325 -43.170 1.00 11.60 ? 168 THR   A CG2 1 
ATOM   1209 N  N   . SER   A 1 169 ? 4.523   -20.037 -39.492 1.00 11.89 ? 169 SER   A N   1 
ATOM   1210 C  CA  . SER   A 1 169 ? 4.993   -18.709 -39.172 1.00 11.33 ? 169 SER   A CA  1 
ATOM   1211 C  C   . SER   A 1 169 ? 4.473   -18.214 -37.824 1.00 12.40 ? 169 SER   A C   1 
ATOM   1212 O  O   . SER   A 1 169 ? 3.407   -18.631 -37.373 1.00 12.69 ? 169 SER   A O   1 
ATOM   1213 C  CB  . SER   A 1 169 ? 4.565   -17.723 -40.259 1.00 12.35 ? 169 SER   A CB  1 
ATOM   1214 O  OG  . SER   A 1 169 ? 4.887   -18.219 -41.546 1.00 11.82 ? 169 SER   A OG  1 
ATOM   1215 N  N   . THR   A 1 170 ? 5.169   -17.202 -37.278 1.00 12.52 ? 170 THR   A N   1 
ATOM   1216 C  CA  . THR   A 1 170 ? 4.675   -16.512 -36.096 1.00 12.50 ? 170 THR   A CA  1 
ATOM   1217 C  C   . THR   A 1 170 ? 3.660   -15.425 -36.441 1.00 14.54 ? 170 THR   A C   1 
ATOM   1218 O  O   . THR   A 1 170 ? 2.901   -14.984 -35.574 1.00 14.89 ? 170 THR   A O   1 
ATOM   1219 C  CB  . THR   A 1 170 ? 5.829   -15.878 -35.335 1.00 12.83 ? 170 THR   A CB  1 
ATOM   1220 O  OG1 . THR   A 1 170 ? 6.501   -14.960 -36.204 1.00 12.92 ? 170 THR   A OG1 1 
ATOM   1221 C  CG2 . THR   A 1 170 ? 6.789   -16.903 -34.771 1.00 12.58 ? 170 THR   A CG2 1 
ATOM   1222 N  N   . GLY   A 1 171 ? 3.700   -14.913 -37.677 1.00 14.62 ? 171 GLY   A N   1 
ATOM   1223 C  CA  . GLY   A 1 171 ? 2.956   -13.715 -38.003 1.00 16.83 ? 171 GLY   A CA  1 
ATOM   1224 C  C   . GLY   A 1 171 ? 3.687   -12.452 -37.568 1.00 19.25 ? 171 GLY   A C   1 
ATOM   1225 O  O   . GLY   A 1 171 ? 3.126   -11.359 -37.740 1.00 21.95 ? 171 GLY   A O   1 
ATOM   1226 N  N   . ARG   A 1 172 ? 4.921   -12.584 -37.029 1.00 17.62 ? 172 ARG   A N   1 
ATOM   1227 C  CA  . ARG   A 1 172 ? 5.605   -11.437 -36.449 1.00 21.40 ? 172 ARG   A CA  1 
ATOM   1228 C  C   . ARG   A 1 172 ? 6.852   -11.042 -37.232 1.00 21.97 ? 172 ARG   A C   1 
ATOM   1229 O  O   . ARG   A 1 172 ? 7.592   -10.170 -36.787 1.00 22.67 ? 172 ARG   A O   1 
ATOM   1230 C  CB  . ARG   A 1 172 ? 5.982   -11.703 -34.990 1.00 22.07 ? 172 ARG   A CB  1 
ATOM   1231 C  CG  . ARG   A 1 172 ? 4.791   -11.922 -34.086 1.00 23.57 ? 172 ARG   A CG  1 
ATOM   1232 C  CD  . ARG   A 1 172 ? 3.998   -10.643 -33.957 1.00 29.92 ? 172 ARG   A CD  1 
ATOM   1233 N  NE  . ARG   A 1 172 ? 2.858   -10.853 -33.093 1.00 35.95 ? 172 ARG   A NE  1 
ATOM   1234 C  CZ  . ARG   A 1 172 ? 2.893   -10.786 -31.765 1.00 43.83 ? 172 ARG   A CZ  1 
ATOM   1235 N  NH1 . ARG   A 1 172 ? 3.988   -10.396 -31.127 1.00 43.84 ? 172 ARG   A NH1 1 
ATOM   1236 N  NH2 . ARG   A 1 172 ? 1.806   -11.069 -31.070 1.00 46.30 ? 172 ARG   A NH2 1 
ATOM   1237 N  N   . VAL   A 1 173 ? 7.100   -11.690 -38.370 1.00 18.97 ? 173 VAL   A N   1 
ATOM   1238 C  CA  . VAL   A 1 173 ? 8.237   -11.365 -39.219 1.00 20.11 ? 173 VAL   A CA  1 
ATOM   1239 C  C   . VAL   A 1 173 ? 7.706   -10.868 -40.560 1.00 20.61 ? 173 VAL   A C   1 
ATOM   1240 O  O   . VAL   A 1 173 ? 6.506   -10.930 -40.794 1.00 20.04 ? 173 VAL   A O   1 
ATOM   1241 C  CB  . VAL   A 1 173 ? 9.179   -12.557 -39.395 1.00 19.02 ? 173 VAL   A CB  1 
ATOM   1242 C  CG1 . VAL   A 1 173 ? 9.855   -12.887 -38.060 1.00 20.30 ? 173 VAL   A CG1 1 
ATOM   1243 C  CG2 . VAL   A 1 173 ? 8.474   -13.773 -39.973 1.00 17.77 ? 173 VAL   A CG2 1 
ATOM   1244 N  N   . ALA   A 1 174 ? 8.610   -10.384 -41.417 1.00 20.90 ? 174 ALA   A N   1 
ATOM   1245 C  CA  . ALA   A 1 174 ? 8.218   -9.738  -42.662 1.00 21.59 ? 174 ALA   A CA  1 
ATOM   1246 C  C   . ALA   A 1 174 ? 7.482   -10.701 -43.586 1.00 20.03 ? 174 ALA   A C   1 
ATOM   1247 O  O   . ALA   A 1 174 ? 6.512   -10.315 -44.245 1.00 19.13 ? 174 ALA   A O   1 
ATOM   1248 C  CB  . ALA   A 1 174 ? 9.441   -9.156  -43.363 1.00 22.07 ? 174 ALA   A CB  1 
ATOM   1249 N  N   . VAL   A 1 175 ? 7.947   -11.959 -43.638 1.00 17.24 ? 175 VAL   A N   1 
ATOM   1250 C  CA  . VAL   A 1 175 ? 7.411   -12.913 -44.580 1.00 16.55 ? 175 VAL   A CA  1 
ATOM   1251 C  C   . VAL   A 1 175 ? 6.839   -14.075 -43.774 1.00 15.67 ? 175 VAL   A C   1 
ATOM   1252 O  O   . VAL   A 1 175 ? 7.559   -14.675 -42.998 1.00 15.15 ? 175 VAL   A O   1 
ATOM   1253 C  CB  . VAL   A 1 175 ? 8.447   -13.399 -45.609 1.00 19.43 ? 175 VAL   A CB  1 
ATOM   1254 C  CG1 . VAL   A 1 175 ? 7.864   -14.435 -46.549 1.00 18.75 ? 175 VAL   A CG1 1 
ATOM   1255 C  CG2 . VAL   A 1 175 ? 9.031   -12.239 -46.417 1.00 20.88 ? 175 VAL   A CG2 1 
ATOM   1256 N  N   . ASN   A 1 176 ? 5.559   -14.359 -43.980 1.00 15.30 ? 176 ASN   A N   1 
ATOM   1257 C  CA  . ASN   A 1 176 ? 4.874   -15.447 -43.288 1.00 15.22 ? 176 ASN   A CA  1 
ATOM   1258 C  C   . ASN   A 1 176 ? 4.604   -16.527 -44.334 1.00 14.69 ? 176 ASN   A C   1 
ATOM   1259 O  O   . ASN   A 1 176 ? 5.487   -16.781 -45.143 1.00 15.41 ? 176 ASN   A O   1 
ATOM   1260 C  CB  . ASN   A 1 176 ? 3.720   -14.902 -42.468 1.00 16.45 ? 176 ASN   A CB  1 
ATOM   1261 C  CG  . ASN   A 1 176 ? 4.271   -13.956 -41.424 1.00 19.65 ? 176 ASN   A CG  1 
ATOM   1262 O  OD1 . ASN   A 1 176 ? 4.860   -14.394 -40.424 1.00 19.11 ? 176 ASN   A OD1 1 
ATOM   1263 N  ND2 . ASN   A 1 176 ? 4.142   -12.672 -41.686 1.00 21.77 ? 176 ASN   A ND2 1 
ATOM   1264 N  N   . ALA   A 1 177 ? 3.429   -17.157 -44.328 1.00 12.75 ? 177 ALA   A N   1 
ATOM   1265 C  CA  . ALA   A 1 177 ? 3.198   -18.283 -45.210 1.00 12.92 ? 177 ALA   A CA  1 
ATOM   1266 C  C   . ALA   A 1 177 ? 3.258   -17.813 -46.662 1.00 12.71 ? 177 ALA   A C   1 
ATOM   1267 O  O   . ALA   A 1 177 ? 2.866   -16.679 -46.968 1.00 13.71 ? 177 ALA   A O   1 
ATOM   1268 C  CB  . ALA   A 1 177 ? 1.886   -18.938 -44.944 1.00 12.37 ? 177 ALA   A CB  1 
ATOM   1269 N  N   . THR   A 1 178 ? 3.704   -18.740 -47.519 1.00 13.27 ? 178 THR   A N   1 
ATOM   1270 C  CA  . THR   A 1 178 ? 3.439   -18.661 -48.947 1.00 14.23 ? 178 THR   A CA  1 
ATOM   1271 C  C   . THR   A 1 178 ? 2.882   -19.999 -49.380 1.00 13.39 ? 178 THR   A C   1 
ATOM   1272 O  O   . THR   A 1 178 ? 3.045   -20.992 -48.686 1.00 13.70 ? 178 THR   A O   1 
ATOM   1273 C  CB  . THR   A 1 178 ? 4.712   -18.341 -49.742 1.00 15.03 ? 178 THR   A CB  1 
ATOM   1274 O  OG1 . THR   A 1 178 ? 5.566   -19.489 -49.706 1.00 14.56 ? 178 THR   A OG1 1 
ATOM   1275 C  CG2 . THR   A 1 178 ? 5.433   -17.119 -49.206 1.00 16.62 ? 178 THR   A CG2 1 
ATOM   1276 N  N   . PRO   A 1 179 ? 2.242   -20.069 -50.566 1.00 14.01 ? 179 PRO   A N   1 
ATOM   1277 C  CA  . PRO   A 1 179 ? 1.775   -21.351 -51.072 1.00 14.32 ? 179 PRO   A CA  1 
ATOM   1278 C  C   . PRO   A 1 179 ? 2.908   -22.357 -51.218 1.00 14.25 ? 179 PRO   A C   1 
ATOM   1279 O  O   . PRO   A 1 179 ? 2.693   -23.556 -50.991 1.00 14.62 ? 179 PRO   A O   1 
ATOM   1280 C  CB  . PRO   A 1 179 ? 1.115   -20.999 -52.412 1.00 15.19 ? 179 PRO   A CB  1 
ATOM   1281 C  CG  . PRO   A 1 179 ? 0.744   -19.558 -52.252 1.00 16.56 ? 179 PRO   A CG  1 
ATOM   1282 C  CD  . PRO   A 1 179 ? 1.808   -18.920 -51.381 1.00 14.86 ? 179 PRO   A CD  1 
ATOM   1283 N  N   . GLU   A 1 180 ? 4.089   -21.890 -51.637 1.00 14.12 ? 180 GLU   A N   1 
ATOM   1284 C  CA  A GLU   A 1 180 ? 5.200   -22.809 -51.832 0.50 14.72 ? 180 GLU   A CA  1 
ATOM   1285 C  CA  B GLU   A 1 180 ? 5.238   -22.756 -51.820 0.50 14.48 ? 180 GLU   A CA  1 
ATOM   1286 C  C   . GLU   A 1 180 ? 5.670   -23.350 -50.478 1.00 14.20 ? 180 GLU   A C   1 
ATOM   1287 O  O   . GLU   A 1 180 ? 5.920   -24.547 -50.369 1.00 14.08 ? 180 GLU   A O   1 
ATOM   1288 C  CB  A GLU   A 1 180 ? 6.317   -22.242 -52.711 0.50 16.26 ? 180 GLU   A CB  1 
ATOM   1289 C  CB  B GLU   A 1 180 ? 6.383   -21.962 -52.448 0.50 15.63 ? 180 GLU   A CB  1 
ATOM   1290 C  CG  A GLU   A 1 180 ? 5.824   -21.909 -54.118 0.50 18.03 ? 180 GLU   A CG  1 
ATOM   1291 C  CG  B GLU   A 1 180 ? 7.595   -22.833 -52.724 0.50 16.54 ? 180 GLU   A CG  1 
ATOM   1292 C  CD  A GLU   A 1 180 ? 5.165   -23.030 -54.926 0.50 19.76 ? 180 GLU   A CD  1 
ATOM   1293 C  CD  B GLU   A 1 180 ? 7.365   -23.843 -53.837 0.50 17.99 ? 180 GLU   A CD  1 
ATOM   1294 O  OE1 A GLU   A 1 180 ? 5.705   -24.146 -54.971 0.50 21.28 ? 180 GLU   A OE1 1 
ATOM   1295 O  OE1 B GLU   A 1 180 ? 6.247   -24.023 -54.333 0.50 18.91 ? 180 GLU   A OE1 1 
ATOM   1296 O  OE2 A GLU   A 1 180 ? 4.089   -22.783 -55.503 0.50 20.80 ? 180 GLU   A OE2 1 
ATOM   1297 O  OE2 B GLU   A 1 180 ? 8.357   -24.498 -54.182 0.50 18.67 ? 180 GLU   A OE2 1 
ATOM   1298 N  N   . SER   A 1 181 ? 5.757   -22.512 -49.442 1.00 14.36 ? 181 SER   A N   1 
ATOM   1299 C  CA  . SER   A 1 181 ? 6.209   -23.064 -48.175 1.00 14.57 ? 181 SER   A CA  1 
ATOM   1300 C  C   . SER   A 1 181 ? 5.155   -24.008 -47.584 1.00 13.69 ? 181 SER   A C   1 
ATOM   1301 O  O   . SER   A 1 181 ? 5.508   -25.038 -47.010 1.00 13.67 ? 181 SER   A O   1 
ATOM   1302 C  CB  . SER   A 1 181 ? 6.703   -22.010 -47.222 1.00 15.90 ? 181 SER   A CB  1 
ATOM   1303 O  OG  . SER   A 1 181 ? 5.703   -21.069 -46.928 1.00 20.13 ? 181 SER   A OG  1 
ATOM   1304 N  N   . ALA   A 1 182 ? 3.874   -23.740 -47.825 1.00 13.76 ? 182 ALA   A N   1 
ATOM   1305 C  CA  . ALA   A 1 182 ? 2.798   -24.644 -47.426 1.00 13.81 ? 182 ALA   A CA  1 
ATOM   1306 C  C   . ALA   A 1 182 ? 2.949   -25.996 -48.126 1.00 14.43 ? 182 ALA   A C   1 
ATOM   1307 O  O   . ALA   A 1 182 ? 2.863   -27.030 -47.477 1.00 14.32 ? 182 ALA   A O   1 
ATOM   1308 C  CB  . ALA   A 1 182 ? 1.452   -24.023 -47.703 1.00 14.14 ? 182 ALA   A CB  1 
ATOM   1309 N  N   . ARG   A 1 183 ? 3.194   -25.976 -49.441 1.00 14.46 ? 183 ARG   A N   1 
ATOM   1310 C  CA  . ARG   A 1 183 ? 3.347   -27.198 -50.210 1.00 15.60 ? 183 ARG   A CA  1 
ATOM   1311 C  C   . ARG   A 1 183 ? 4.526   -28.016 -49.694 1.00 14.64 ? 183 ARG   A C   1 
ATOM   1312 O  O   . ARG   A 1 183 ? 4.417   -29.234 -49.493 1.00 14.52 ? 183 ARG   A O   1 
ATOM   1313 C  CB  . ARG   A 1 183 ? 3.527   -26.918 -51.708 1.00 18.58 ? 183 ARG   A CB  1 
ATOM   1314 C  CG  . ARG   A 1 183 ? 3.782   -28.158 -52.545 1.00 22.85 ? 183 ARG   A CG  1 
ATOM   1315 C  CD  . ARG   A 1 183 ? 4.162   -27.820 -53.981 1.00 28.16 ? 183 ARG   A CD  1 
ATOM   1316 N  NE  . ARG   A 1 183 ? 5.397   -27.024 -54.049 1.00 37.07 ? 183 ARG   A NE  1 
ATOM   1317 C  CZ  . ARG   A 1 183 ? 6.647   -27.492 -53.981 1.00 39.90 ? 183 ARG   A CZ  1 
ATOM   1318 N  NH1 . ARG   A 1 183 ? 6.886   -28.784 -53.863 1.00 43.71 ? 183 ARG   A NH1 1 
ATOM   1319 N  NH2 . ARG   A 1 183 ? 7.678   -26.671 -54.069 1.00 41.00 ? 183 ARG   A NH2 1 
ATOM   1320 N  N   . ILE   A 1 184 ? 5.653   -27.340 -49.452 1.00 14.64 ? 184 ILE   A N   1 
ATOM   1321 C  CA  . ILE   A 1 184 ? 6.847   -28.038 -48.993 1.00 13.96 ? 184 ILE   A CA  1 
ATOM   1322 C  C   . ILE   A 1 184 ? 6.550   -28.728 -47.671 1.00 13.73 ? 184 ILE   A C   1 
ATOM   1323 O  O   . ILE   A 1 184 ? 6.890   -29.892 -47.473 1.00 13.78 ? 184 ILE   A O   1 
ATOM   1324 C  CB  . ILE   A 1 184 ? 8.039   -27.071 -48.883 1.00 14.38 ? 184 ILE   A CB  1 
ATOM   1325 C  CG1 . ILE   A 1 184 ? 8.450   -26.545 -50.245 1.00 15.46 ? 184 ILE   A CG1 1 
ATOM   1326 C  CG2 . ILE   A 1 184 ? 9.195   -27.722 -48.143 1.00 14.87 ? 184 ILE   A CG2 1 
ATOM   1327 C  CD1 . ILE   A 1 184 ? 9.228   -25.244 -50.202 1.00 15.40 ? 184 ILE   A CD1 1 
ATOM   1328 N  N   . MET   A 1 185 ? 5.920   -27.994 -46.736 1.00 13.30 ? 185 MET   A N   1 
ATOM   1329 C  CA  . MET   A 1 185 ? 5.693   -28.590 -45.425 1.00 12.79 ? 185 MET   A CA  1 
ATOM   1330 C  C   . MET   A 1 185 ? 4.725   -29.767 -45.511 1.00 12.73 ? 185 MET   A C   1 
ATOM   1331 O  O   . MET   A 1 185 ? 4.907   -30.772 -44.816 1.00 12.84 ? 185 MET   A O   1 
ATOM   1332 C  CB  . MET   A 1 185 ? 5.209   -27.537 -44.426 1.00 12.46 ? 185 MET   A CB  1 
ATOM   1333 C  CG  . MET   A 1 185 ? 6.275   -26.519 -44.126 1.00 12.15 ? 185 MET   A CG  1 
ATOM   1334 S  SD  . MET   A 1 185 ? 5.720   -25.149 -43.079 1.00 13.11 ? 185 MET   A SD  1 
ATOM   1335 C  CE  . MET   A 1 185 ? 5.386   -25.974 -41.517 1.00 11.96 ? 185 MET   A CE  1 
ATOM   1336 N  N   . MET   A 1 186 ? 3.677   -29.648 -46.324 1.00 12.86 ? 186 MET   A N   1 
ATOM   1337 C  CA  . MET   A 1 186 ? 2.725   -30.753 -46.429 1.00 13.49 ? 186 MET   A CA  1 
ATOM   1338 C  C   . MET   A 1 186 ? 3.365   -31.940 -47.164 1.00 14.50 ? 186 MET   A C   1 
ATOM   1339 O  O   . MET   A 1 186 ? 3.102   -33.089 -46.833 1.00 15.30 ? 186 MET   A O   1 
ATOM   1340 C  CB  . MET   A 1 186 ? 1.434   -30.273 -47.072 1.00 13.54 ? 186 MET   A CB  1 
ATOM   1341 C  CG  . MET   A 1 186 ? 0.541   -29.525 -46.097 1.00 14.85 ? 186 MET   A CG  1 
ATOM   1342 S  SD  . MET   A 1 186 ? -1.076  -29.111 -46.779 1.00 17.28 ? 186 MET   A SD  1 
ATOM   1343 C  CE  . MET   A 1 186 ? -0.674  -27.527 -47.531 1.00 17.13 ? 186 MET   A CE  1 
ATOM   1344 N  N   . GLU   A 1 187 ? 4.267   -31.667 -48.095 1.00 15.62 ? 187 GLU   A N   1 
ATOM   1345 C  CA  . GLU   A 1 187 ? 5.011   -32.751 -48.734 1.00 16.71 ? 187 GLU   A CA  1 
ATOM   1346 C  C   . GLU   A 1 187 ? 5.841   -33.505 -47.707 1.00 16.43 ? 187 GLU   A C   1 
ATOM   1347 O  O   . GLU   A 1 187 ? 5.966   -34.725 -47.800 1.00 16.20 ? 187 GLU   A O   1 
ATOM   1348 C  CB  . GLU   A 1 187 ? 5.900   -32.271 -49.889 1.00 18.82 ? 187 GLU   A CB  1 
ATOM   1349 C  CG  . GLU   A 1 187 ? 5.112   -31.881 -51.130 1.00 22.07 ? 187 GLU   A CG  1 
ATOM   1350 C  CD  . GLU   A 1 187 ? 6.015   -31.376 -52.253 1.00 26.84 ? 187 GLU   A CD  1 
ATOM   1351 O  OE1 . GLU   A 1 187 ? 7.245   -31.282 -52.085 1.00 31.00 ? 187 GLU   A OE1 1 
ATOM   1352 O  OE2 . GLU   A 1 187 ? 5.444   -31.056 -53.315 1.00 27.61 ? 187 GLU   A OE2 1 
ATOM   1353 N  N   . VAL   A 1 188 ? 6.432   -32.796 -46.739 1.00 15.12 ? 188 VAL   A N   1 
ATOM   1354 C  CA  . VAL   A 1 188 ? 7.186   -33.499 -45.705 1.00 15.54 ? 188 VAL   A CA  1 
ATOM   1355 C  C   . VAL   A 1 188 ? 6.274   -34.448 -44.936 1.00 15.49 ? 188 VAL   A C   1 
ATOM   1356 O  O   . VAL   A 1 188 ? 6.616   -35.598 -44.659 1.00 15.61 ? 188 VAL   A O   1 
ATOM   1357 C  CB  . VAL   A 1 188 ? 7.924   -32.535 -44.748 1.00 16.18 ? 188 VAL   A CB  1 
ATOM   1358 C  CG1 . VAL   A 1 188 ? 8.598   -33.294 -43.617 1.00 16.33 ? 188 VAL   A CG1 1 
ATOM   1359 C  CG2 . VAL   A 1 188 ? 8.966   -31.707 -45.486 1.00 15.33 ? 188 VAL   A CG2 1 
ATOM   1360 N  N   . ILE   A 1 189 ? 5.108   -33.951 -44.524 1.00 14.29 ? 189 ILE   A N   1 
ATOM   1361 C  CA  . ILE   A 1 189 ? 4.139   -34.779 -43.810 1.00 14.26 ? 189 ILE   A CA  1 
ATOM   1362 C  C   . ILE   A 1 189 ? 3.833   -36.038 -44.617 1.00 15.76 ? 189 ILE   A C   1 
ATOM   1363 O  O   . ILE   A 1 189 ? 3.869   -37.153 -44.089 1.00 15.99 ? 189 ILE   A O   1 
ATOM   1364 C  CB  . ILE   A 1 189 ? 2.851   -33.985 -43.508 1.00 14.31 ? 189 ILE   A CB  1 
ATOM   1365 C  CG1 . ILE   A 1 189 ? 3.149   -32.892 -42.489 1.00 13.99 ? 189 ILE   A CG1 1 
ATOM   1366 C  CG2 . ILE   A 1 189 ? 1.720   -34.891 -43.020 1.00 16.55 ? 189 ILE   A CG2 1 
ATOM   1367 C  CD1 . ILE   A 1 189 ? 1.988   -31.946 -42.271 1.00 14.13 ? 189 ILE   A CD1 1 
ATOM   1368 N  N   . ARG   A 1 190 ? 3.546   -35.837 -45.909 1.00 17.17 ? 190 ARG   A N   1 
ATOM   1369 C  CA  . ARG   A 1 190 ? 3.241   -36.943 -46.792 1.00 18.24 ? 190 ARG   A CA  1 
ATOM   1370 C  C   . ARG   A 1 190 ? 4.432   -37.897 -46.897 1.00 19.39 ? 190 ARG   A C   1 
ATOM   1371 O  O   . ARG   A 1 190 ? 4.251   -39.108 -46.731 1.00 20.71 ? 190 ARG   A O   1 
ATOM   1372 C  CB  . ARG   A 1 190 ? 2.858   -36.418 -48.180 1.00 18.85 ? 190 ARG   A CB  1 
ATOM   1373 C  CG  . ARG   A 1 190 ? 2.340   -37.509 -49.114 1.00 19.74 ? 190 ARG   A CG  1 
ATOM   1374 C  CD  . ARG   A 1 190 ? 2.405   -37.043 -50.557 1.00 22.80 ? 190 ARG   A CD  1 
ATOM   1375 N  NE  . ARG   A 1 190 ? 3.788   -36.744 -50.915 1.00 26.57 ? 190 ARG   A NE  1 
ATOM   1376 C  CZ  . ARG   A 1 190 ? 4.142   -36.126 -52.030 1.00 28.58 ? 190 ARG   A CZ  1 
ATOM   1377 N  NH1 . ARG   A 1 190 ? 3.225   -35.894 -52.943 1.00 26.47 ? 190 ARG   A NH1 1 
ATOM   1378 N  NH2 . ARG   A 1 190 ? 5.390   -35.737 -52.221 1.00 29.06 ? 190 ARG   A NH2 1 
ATOM   1379 N  N   . ASP   A 1 191 ? 5.620   -37.349 -47.210 1.00 20.06 ? 191 ASP   A N   1 
ATOM   1380 C  CA  . ASP   A 1 191 ? 6.807   -38.155 -47.495 1.00 21.12 ? 191 ASP   A CA  1 
ATOM   1381 C  C   . ASP   A 1 191 ? 7.200   -38.965 -46.262 1.00 21.07 ? 191 ASP   A C   1 
ATOM   1382 O  O   . ASP   A 1 191 ? 7.725   -40.059 -46.387 1.00 21.14 ? 191 ASP   A O   1 
ATOM   1383 C  CB  . ASP   A 1 191 ? 7.979   -37.307 -47.958 1.00 22.80 ? 191 ASP   A CB  1 
ATOM   1384 C  CG  . ASP   A 1 191 ? 7.810   -36.695 -49.339 1.00 25.14 ? 191 ASP   A CG  1 
ATOM   1385 O  OD1 . ASP   A 1 191 ? 6.831   -37.088 -50.022 1.00 25.38 ? 191 ASP   A OD1 1 
ATOM   1386 O  OD2 . ASP   A 1 191 ? 8.573   -35.750 -49.658 1.00 26.53 ? 191 ASP   A OD2 1 
ATOM   1387 N  N   . MET   A 1 192 ? 6.943   -38.416 -45.064 1.00 18.85 ? 192 MET   A N   1 
ATOM   1388 C  CA  . MET   A 1 192 ? 7.320   -39.099 -43.848 1.00 19.67 ? 192 MET   A CA  1 
ATOM   1389 C  C   . MET   A 1 192 ? 6.273   -40.119 -43.427 1.00 21.42 ? 192 MET   A C   1 
ATOM   1390 O  O   . MET   A 1 192 ? 6.514   -40.881 -42.501 1.00 21.58 ? 192 MET   A O   1 
ATOM   1391 C  CB  . MET   A 1 192 ? 7.566   -38.074 -42.736 1.00 19.18 ? 192 MET   A CB  1 
ATOM   1392 C  CG  . MET   A 1 192 ? 8.856   -37.319 -42.963 1.00 18.98 ? 192 MET   A CG  1 
ATOM   1393 S  SD  . MET   A 1 192 ? 9.224   -36.196 -41.595 1.00 19.95 ? 192 MET   A SD  1 
ATOM   1394 C  CE  . MET   A 1 192 ? 9.790   -37.343 -40.336 1.00 22.30 ? 192 MET   A CE  1 
ATOM   1395 N  N   . GLY   A 1 193 ? 5.094   -40.101 -44.066 1.00 20.13 ? 193 GLY   A N   1 
ATOM   1396 C  CA  . GLY   A 1 193 ? 4.074   -41.084 -43.762 1.00 21.65 ? 193 GLY   A CA  1 
ATOM   1397 C  C   . GLY   A 1 193 ? 3.290   -40.752 -42.496 1.00 21.00 ? 193 GLY   A C   1 
ATOM   1398 O  O   . GLY   A 1 193 ? 2.698   -41.657 -41.899 1.00 21.19 ? 193 GLY   A O   1 
ATOM   1399 N  N   . VAL   A 1 194 ? 3.268   -39.458 -42.107 1.00 19.13 ? 194 VAL   A N   1 
ATOM   1400 C  CA  . VAL   A 1 194 ? 2.727   -39.085 -40.804 1.00 17.77 ? 194 VAL   A CA  1 
ATOM   1401 C  C   . VAL   A 1 194 ? 1.435   -38.277 -40.942 1.00 17.57 ? 194 VAL   A C   1 
ATOM   1402 O  O   . VAL   A 1 194 ? 1.036   -37.604 -40.002 1.00 18.36 ? 194 VAL   A O   1 
ATOM   1403 C  CB  . VAL   A 1 194 ? 3.776   -38.338 -39.955 1.00 17.37 ? 194 VAL   A CB  1 
ATOM   1404 C  CG1 . VAL   A 1 194 ? 4.991   -39.204 -39.667 1.00 18.06 ? 194 VAL   A CG1 1 
ATOM   1405 C  CG2 . VAL   A 1 194 ? 4.203   -37.017 -40.550 1.00 17.69 ? 194 VAL   A CG2 1 
ATOM   1406 N  N   . GLU   A 1 195 ? 0.733   -38.391 -42.078 1.00 18.58 ? 195 GLU   A N   1 
ATOM   1407 C  CA  . GLU   A 1 195 ? -0.450  -37.580 -42.329 1.00 19.31 ? 195 GLU   A CA  1 
ATOM   1408 C  C   . GLU   A 1 195 ? -1.568  -37.913 -41.347 1.00 19.25 ? 195 GLU   A C   1 
ATOM   1409 O  O   . GLU   A 1 195 ? -2.419  -37.070 -41.083 1.00 19.97 ? 195 GLU   A O   1 
ATOM   1410 C  CB  . GLU   A 1 195 ? -0.907  -37.710 -43.787 1.00 21.93 ? 195 GLU   A CB  1 
ATOM   1411 C  CG  . GLU   A 1 195 ? -1.517  -39.063 -44.143 1.00 25.21 ? 195 GLU   A CG  1 
ATOM   1412 C  CD  . GLU   A 1 195 ? -0.560  -40.222 -44.331 1.00 29.39 ? 195 GLU   A CD  1 
ATOM   1413 O  OE1 . GLU   A 1 195 ? 0.684   -40.067 -44.389 1.00 27.97 ? 195 GLU   A OE1 1 
ATOM   1414 O  OE2 . GLU   A 1 195 ? -1.142  -41.319 -44.425 1.00 36.92 ? 195 GLU   A OE2 1 
ATOM   1415 N  N   . LYS   A 1 196 ? -1.545  -39.101 -40.741 1.00 20.04 ? 196 LYS   A N   1 
ATOM   1416 C  CA  . LYS   A 1 196 ? -2.558  -39.428 -39.751 1.00 23.01 ? 196 LYS   A CA  1 
ATOM   1417 C  C   . LYS   A 1 196 ? -2.360  -38.617 -38.475 1.00 21.23 ? 196 LYS   A C   1 
ATOM   1418 O  O   . LYS   A 1 196 ? -3.335  -38.189 -37.872 1.00 21.97 ? 196 LYS   A O   1 
ATOM   1419 C  CB  . LYS   A 1 196 ? -2.590  -40.918 -39.422 1.00 26.73 ? 196 LYS   A CB  1 
ATOM   1420 C  CG  . LYS   A 1 196 ? -3.145  -41.753 -40.531 1.00 36.63 ? 196 LYS   A CG  1 
ATOM   1421 C  CD  . LYS   A 1 196 ? -2.910  -43.244 -40.299 1.00 42.00 ? 196 LYS   A CD  1 
ATOM   1422 C  CE  . LYS   A 1 196 ? -3.286  -44.036 -41.499 1.00 46.07 ? 196 LYS   A CE  1 
ATOM   1423 N  NZ  . LYS   A 1 196 ? -4.682  -43.760 -41.852 1.00 50.67 ? 196 LYS   A NZ  1 
ATOM   1424 N  N   . SER   A 1 197 ? -1.106  -38.354 -38.102 1.00 20.18 ? 197 SER   A N   1 
ATOM   1425 C  CA  . SER   A 1 197 ? -0.773  -37.851 -36.775 1.00 19.83 ? 197 SER   A CA  1 
ATOM   1426 C  C   . SER   A 1 197 ? -0.299  -36.410 -36.780 1.00 17.77 ? 197 SER   A C   1 
ATOM   1427 O  O   . SER   A 1 197 ? -0.191  -35.821 -35.707 1.00 17.89 ? 197 SER   A O   1 
ATOM   1428 C  CB  . SER   A 1 197 ? 0.249   -38.752 -36.118 1.00 21.65 ? 197 SER   A CB  1 
ATOM   1429 O  OG  . SER   A 1 197 ? 1.449   -38.818 -36.881 1.00 22.97 ? 197 SER   A OG  1 
ATOM   1430 N  N   . VAL   A 1 198 ? 0.018   -35.831 -37.953 1.00 17.22 ? 198 VAL   A N   1 
ATOM   1431 C  CA  . VAL   A 1 198 ? 0.594   -34.495 -37.986 1.00 15.78 ? 198 VAL   A CA  1 
ATOM   1432 C  C   . VAL   A 1 198 ? -0.244  -33.591 -38.880 1.00 14.18 ? 198 VAL   A C   1 
ATOM   1433 O  O   . VAL   A 1 198 ? -0.501  -33.911 -40.046 1.00 14.10 ? 198 VAL   A O   1 
ATOM   1434 C  CB  . VAL   A 1 198 ? 2.058   -34.533 -38.458 1.00 16.09 ? 198 VAL   A CB  1 
ATOM   1435 C  CG1 . VAL   A 1 198 ? 2.650   -33.133 -38.549 1.00 16.00 ? 198 VAL   A CG1 1 
ATOM   1436 C  CG2 . VAL   A 1 198 ? 2.894   -35.416 -37.539 1.00 16.47 ? 198 VAL   A CG2 1 
ATOM   1437 N  N   . GLY   A 1 199 ? -0.651  -32.445 -38.334 1.00 12.15 ? 199 GLY   A N   1 
ATOM   1438 C  CA  . GLY   A 1 199 ? -1.380  -31.448 -39.086 1.00 11.88 ? 199 GLY   A CA  1 
ATOM   1439 C  C   . GLY   A 1 199 ? -0.470  -30.331 -39.591 1.00 11.85 ? 199 GLY   A C   1 
ATOM   1440 O  O   . GLY   A 1 199 ? 0.703   -30.250 -39.242 1.00 11.34 ? 199 GLY   A O   1 
ATOM   1441 N  N   . PHE   A 1 200 ? -1.067  -29.468 -40.407 1.00 11.55 ? 200 PHE   A N   1 
ATOM   1442 C  CA  . PHE   A 1 200 ? -0.434  -28.303 -40.976 1.00 11.94 ? 200 PHE   A CA  1 
ATOM   1443 C  C   . PHE   A 1 200 ? -1.230  -27.055 -40.637 1.00 11.99 ? 200 PHE   A C   1 
ATOM   1444 O  O   . PHE   A 1 200 ? -2.458  -27.046 -40.775 1.00 13.20 ? 200 PHE   A O   1 
ATOM   1445 C  CB  . PHE   A 1 200 ? -0.367  -28.528 -42.480 1.00 12.19 ? 200 PHE   A CB  1 
ATOM   1446 C  CG  . PHE   A 1 200 ? 0.113   -27.268 -43.184 1.00 12.18 ? 200 PHE   A CG  1 
ATOM   1447 C  CD1 . PHE   A 1 200 ? 1.430   -26.844 -43.023 1.00 12.62 ? 200 PHE   A CD1 1 
ATOM   1448 C  CD2 . PHE   A 1 200 ? -0.756  -26.463 -43.883 1.00 13.35 ? 200 PHE   A CD2 1 
ATOM   1449 C  CE1 . PHE   A 1 200 ? 1.871   -25.681 -43.598 1.00 11.92 ? 200 PHE   A CE1 1 
ATOM   1450 C  CE2 . PHE   A 1 200 ? -0.289  -25.311 -44.494 1.00 14.04 ? 200 PHE   A CE2 1 
ATOM   1451 C  CZ  . PHE   A 1 200 ? 1.015   -24.920 -44.340 1.00 13.39 ? 200 PHE   A CZ  1 
ATOM   1452 N  N   . LYS   A 1 201 ? -0.520  -25.993 -40.219 1.00 11.60 ? 201 LYS   A N   1 
ATOM   1453 C  CA  . LYS   A 1 201 ? -1.158  -24.721 -39.983 1.00 11.77 ? 201 LYS   A CA  1 
ATOM   1454 C  C   . LYS   A 1 201 ? -0.488  -23.628 -40.800 1.00 12.28 ? 201 LYS   A C   1 
ATOM   1455 O  O   . LYS   A 1 201 ? 0.732   -23.431 -40.719 1.00 11.30 ? 201 LYS   A O   1 
ATOM   1456 C  CB  . LYS   A 1 201 ? -1.194  -24.347 -38.502 1.00 11.86 ? 201 LYS   A CB  1 
ATOM   1457 C  CG  . LYS   A 1 201 ? -1.729  -22.959 -38.209 1.00 13.53 ? 201 LYS   A CG  1 
ATOM   1458 C  CD  . LYS   A 1 201 ? -2.072  -22.759 -36.734 1.00 15.33 ? 201 LYS   A CD  1 
ATOM   1459 C  CE  . LYS   A 1 201 ? -2.396  -21.310 -36.403 1.00 18.33 ? 201 LYS   A CE  1 
ATOM   1460 N  NZ  . LYS   A 1 201 ? -2.509  -21.156 -34.946 1.00 19.55 ? 201 LYS   A NZ  1 
ATOM   1461 N  N   . VAL   A 1 202 ? -1.331  -22.889 -41.524 1.00 12.13 ? 202 VAL   A N   1 
ATOM   1462 C  CA  . VAL   A 1 202 ? -0.905  -21.719 -42.287 1.00 14.23 ? 202 VAL   A CA  1 
ATOM   1463 C  C   . VAL   A 1 202 ? -1.129  -20.460 -41.457 1.00 13.66 ? 202 VAL   A C   1 
ATOM   1464 O  O   . VAL   A 1 202 ? -2.236  -20.194 -40.992 1.00 15.25 ? 202 VAL   A O   1 
ATOM   1465 C  CB  . VAL   A 1 202 ? -1.599  -21.621 -43.664 1.00 17.49 ? 202 VAL   A CB  1 
ATOM   1466 C  CG1 . VAL   A 1 202 ? -3.075  -21.777 -43.595 1.00 18.91 ? 202 VAL   A CG1 1 
ATOM   1467 C  CG2 . VAL   A 1 202 ? -1.301  -20.301 -44.367 1.00 18.71 ? 202 VAL   A CG2 1 
ATOM   1468 N  N   . THR   A 1 203 ? -0.064  -19.687 -41.242 1.00 13.38 ? 203 THR   A N   1 
ATOM   1469 C  CA  . THR   A 1 203 ? -0.152  -18.420 -40.555 1.00 14.12 ? 203 THR   A CA  1 
ATOM   1470 C  C   . THR   A 1 203 ? 0.361   -17.318 -41.477 1.00 15.13 ? 203 THR   A C   1 
ATOM   1471 O  O   . THR   A 1 203 ? 1.482   -17.383 -41.978 1.00 13.03 ? 203 THR   A O   1 
ATOM   1472 C  CB  . THR   A 1 203 ? 0.662   -18.487 -39.266 1.00 16.56 ? 203 THR   A CB  1 
ATOM   1473 O  OG1 . THR   A 1 203 ? 0.016   -19.465 -38.450 1.00 18.31 ? 203 THR   A OG1 1 
ATOM   1474 C  CG2 . THR   A 1 203 ? 0.641   -17.175 -38.504 1.00 16.53 ? 203 THR   A CG2 1 
ATOM   1475 N  N   . GLY   A 1 204 ? -0.478  -16.305 -41.642 1.00 15.54 ? 204 GLY   A N   1 
ATOM   1476 C  CA  . GLY   A 1 204 ? -0.199  -15.194 -42.528 1.00 17.47 ? 204 GLY   A CA  1 
ATOM   1477 C  C   . GLY   A 1 204 ? -0.326  -15.614 -43.992 1.00 20.48 ? 204 GLY   A C   1 
ATOM   1478 O  O   . GLY   A 1 204 ? -0.604  -16.767 -44.299 1.00 20.76 ? 204 GLY   A O   1 
ATOM   1479 N  N   . GLY   A 1 205 ? -0.204  -14.640 -44.899 1.00 25.72 ? 205 GLY   A N   1 
ATOM   1480 C  CA  . GLY   A 1 205 ? -0.273  -14.888 -46.333 1.00 27.82 ? 205 GLY   A CA  1 
ATOM   1481 C  C   . GLY   A 1 205 ? -1.646  -15.376 -46.816 1.00 33.92 ? 205 GLY   A C   1 
ATOM   1482 O  O   . GLY   A 1 205 ? -1.754  -15.864 -47.940 1.00 38.73 ? 205 GLY   A O   1 
ATOM   1483 N  N   . VAL   A 1 206 ? -2.705  -15.256 -45.996 1.00 33.97 ? 206 VAL   A N   1 
ATOM   1484 C  CA  . VAL   A 1 206 ? -4.026  -15.736 -46.374 1.00 33.19 ? 206 VAL   A CA  1 
ATOM   1485 C  C   . VAL   A 1 206 ? -5.051  -14.658 -46.028 1.00 36.68 ? 206 VAL   A C   1 
ATOM   1486 O  O   . VAL   A 1 206 ? -5.784  -14.775 -45.046 1.00 40.08 ? 206 VAL   A O   1 
ATOM   1487 C  CB  . VAL   A 1 206 ? -4.424  -17.069 -45.715 1.00 35.10 ? 206 VAL   A CB  1 
ATOM   1488 C  CG1 . VAL   A 1 206 ? -5.655  -17.674 -46.371 1.00 36.13 ? 206 VAL   A CG1 1 
ATOM   1489 C  CG2 . VAL   A 1 206 ? -3.291  -18.068 -45.746 1.00 36.80 ? 206 VAL   A CG2 1 
ATOM   1490 N  N   . SER   A 1 207 ? -5.111  -13.631 -46.870 1.00 35.71 ? 207 SER   A N   1 
ATOM   1491 C  CA  . SER   A 1 207 ? -5.909  -12.434 -46.630 1.00 41.93 ? 207 SER   A CA  1 
ATOM   1492 C  C   . SER   A 1 207 ? -7.382  -12.675 -46.940 1.00 37.94 ? 207 SER   A C   1 
ATOM   1493 O  O   . SER   A 1 207 ? -8.245  -12.149 -46.246 1.00 43.08 ? 207 SER   A O   1 
ATOM   1494 C  CB  . SER   A 1 207 ? -5.427  -11.281 -47.458 1.00 39.95 ? 207 SER   A CB  1 
ATOM   1495 O  OG  . SER   A 1 207 ? -4.038  -11.094 -47.284 1.00 48.39 ? 207 SER   A OG  1 
ATOM   1496 N  N   . THR   A 1 208 ? -7.644  -13.465 -47.989 1.00 31.50 ? 208 THR   A N   1 
ATOM   1497 C  CA  . THR   A 1 208 ? -8.951  -13.534 -48.602 1.00 30.10 ? 208 THR   A CA  1 
ATOM   1498 C  C   . THR   A 1 208 ? -9.437  -14.975 -48.620 1.00 29.47 ? 208 THR   A C   1 
ATOM   1499 O  O   . THR   A 1 208 ? -8.661  -15.938 -48.527 1.00 27.86 ? 208 THR   A O   1 
ATOM   1500 C  CB  . THR   A 1 208 ? -8.903  -12.988 -50.031 1.00 30.78 ? 208 THR   A CB  1 
ATOM   1501 O  OG1 . THR   A 1 208 ? -8.180  -13.918 -50.847 1.00 28.85 ? 208 THR   A OG1 1 
ATOM   1502 C  CG2 . THR   A 1 208 ? -8.297  -11.600 -50.111 1.00 32.99 ? 208 THR   A CG2 1 
ATOM   1503 N  N   . ALA   A 1 209 ? -10.744 -15.084 -48.822 1.00 28.01 ? 209 ALA   A N   1 
ATOM   1504 C  CA  . ALA   A 1 209 ? -11.405 -16.346 -49.085 1.00 27.37 ? 209 ALA   A CA  1 
ATOM   1505 C  C   . ALA   A 1 209 ? -10.735 -17.084 -50.244 1.00 26.02 ? 209 ALA   A C   1 
ATOM   1506 O  O   . ALA   A 1 209 ? -10.590 -18.304 -50.199 1.00 24.03 ? 209 ALA   A O   1 
ATOM   1507 C  CB  . ALA   A 1 209 ? -12.874 -16.080 -49.386 1.00 27.69 ? 209 ALA   A CB  1 
ATOM   1508 N  N   . GLU   A 1 210 ? -10.384 -16.358 -51.314 1.00 25.36 ? 210 GLU   A N   1 
ATOM   1509 C  CA  . GLU   A 1 210 ? -9.748  -16.982 -52.470 1.00 26.47 ? 210 GLU   A CA  1 
ATOM   1510 C  C   . GLU   A 1 210 ? -8.387  -17.585 -52.088 1.00 23.63 ? 210 GLU   A C   1 
ATOM   1511 O  O   . GLU   A 1 210 ? -8.019  -18.680 -52.519 1.00 22.71 ? 210 GLU   A O   1 
ATOM   1512 C  CB  . GLU   A 1 210 ? -9.554  -15.967 -53.600 1.00 28.29 ? 210 GLU   A CB  1 
ATOM   1513 C  CG  . GLU   A 1 210 ? -10.871 -15.482 -54.212 1.00 32.39 ? 210 GLU   A CG  1 
ATOM   1514 C  CD  . GLU   A 1 210 ? -11.629 -14.387 -53.470 1.00 34.50 ? 210 GLU   A CD  1 
ATOM   1515 O  OE1 . GLU   A 1 210 ? -11.250 -13.910 -52.376 1.00 34.24 ? 210 GLU   A OE1 1 
ATOM   1516 O  OE2 . GLU   A 1 210 ? -12.690 -14.014 -54.013 1.00 42.75 ? 210 GLU   A OE2 1 
ATOM   1517 N  N   . ASP   A 1 211 ? -7.629  -16.857 -51.285 1.00 23.36 ? 211 ASP   A N   1 
ATOM   1518 C  CA  . ASP   A 1 211 ? -6.380  -17.392 -50.765 1.00 23.61 ? 211 ASP   A CA  1 
ATOM   1519 C  C   . ASP   A 1 211 ? -6.630  -18.666 -49.965 1.00 22.74 ? 211 ASP   A C   1 
ATOM   1520 O  O   . ASP   A 1 211 ? -5.923  -19.653 -50.125 1.00 19.15 ? 211 ASP   A O   1 
ATOM   1521 C  CB  . ASP   A 1 211 ? -5.678  -16.397 -49.866 1.00 23.69 ? 211 ASP   A CB  1 
ATOM   1522 C  CG  . ASP   A 1 211 ? -5.244  -15.108 -50.544 1.00 27.17 ? 211 ASP   A CG  1 
ATOM   1523 O  OD1 . ASP   A 1 211 ? -4.894  -15.175 -51.737 1.00 27.99 ? 211 ASP   A OD1 1 
ATOM   1524 O  OD2 . ASP   A 1 211 ? -5.245  -14.075 -49.861 1.00 28.98 ? 211 ASP   A OD2 1 
ATOM   1525 N  N   . ALA   A 1 212 ? -7.637  -18.645 -49.082 1.00 21.31 ? 212 ALA   A N   1 
ATOM   1526 C  CA  . ALA   A 1 212 ? -7.879  -19.824 -48.249 1.00 20.58 ? 212 ALA   A CA  1 
ATOM   1527 C  C   . ALA   A 1 212 ? -8.202  -21.038 -49.120 1.00 20.61 ? 212 ALA   A C   1 
ATOM   1528 O  O   . ALA   A 1 212 ? -7.749  -22.144 -48.842 1.00 19.37 ? 212 ALA   A O   1 
ATOM   1529 C  CB  . ALA   A 1 212 ? -8.983  -19.555 -47.250 1.00 21.47 ? 212 ALA   A CB  1 
ATOM   1530 N  N   . GLN   A 1 213 ? -8.988  -20.835 -50.177 1.00 20.45 ? 213 GLN   A N   1 
ATOM   1531 C  CA  . GLN   A 1 213 ? -9.328  -21.913 -51.084 1.00 22.25 ? 213 GLN   A CA  1 
ATOM   1532 C  C   . GLN   A 1 213 ? -8.063  -22.518 -51.702 1.00 20.62 ? 213 GLN   A C   1 
ATOM   1533 O  O   . GLN   A 1 213 ? -7.964  -23.726 -51.854 1.00 21.57 ? 213 GLN   A O   1 
ATOM   1534 C  CB  . GLN   A 1 213 ? -10.269 -21.342 -52.145 1.00 25.53 ? 213 GLN   A CB  1 
ATOM   1535 C  CG  . GLN   A 1 213 ? -10.781 -22.385 -53.119 1.00 29.54 ? 213 GLN   A CG  1 
ATOM   1536 C  CD  . GLN   A 1 213 ? -11.740 -21.767 -54.118 1.00 35.25 ? 213 GLN   A CD  1 
ATOM   1537 O  OE1 . GLN   A 1 213 ? -11.442 -20.736 -54.738 1.00 38.04 ? 213 GLN   A OE1 1 
ATOM   1538 N  NE2 . GLN   A 1 213 ? -12.910 -22.363 -54.242 1.00 33.19 ? 213 GLN   A NE2 1 
ATOM   1539 N  N   . LYS   A 1 214 ? -7.095  -21.681 -52.080 1.00 21.44 ? 214 LYS   A N   1 
ATOM   1540 C  CA  . LYS   A 1 214 ? -5.871  -22.155 -52.718 1.00 22.52 ? 214 LYS   A CA  1 
ATOM   1541 C  C   . LYS   A 1 214 ? -5.074  -23.011 -51.734 1.00 19.81 ? 214 LYS   A C   1 
ATOM   1542 O  O   . LYS   A 1 214 ? -4.589  -24.085 -52.070 1.00 21.07 ? 214 LYS   A O   1 
ATOM   1543 C  CB  . LYS   A 1 214 ? -5.049  -20.953 -53.201 1.00 26.75 ? 214 LYS   A CB  1 
ATOM   1544 C  CG  . LYS   A 1 214 ? -3.775  -21.343 -53.902 1.00 36.12 ? 214 LYS   A CG  1 
ATOM   1545 C  CD  . LYS   A 1 214 ? -3.150  -20.250 -54.760 1.00 42.75 ? 214 LYS   A CD  1 
ATOM   1546 C  CE  . LYS   A 1 214 ? -2.490  -19.145 -53.973 1.00 43.91 ? 214 LYS   A CE  1 
ATOM   1547 N  NZ  . LYS   A 1 214 ? -1.706  -18.307 -54.892 1.00 43.51 ? 214 LYS   A NZ  1 
ATOM   1548 N  N   . TYR   A 1 215 ? -4.967  -22.540 -50.476 1.00 17.64 ? 215 TYR   A N   1 
ATOM   1549 C  CA  . TYR   A 1 215 ? -4.220  -23.294 -49.485 1.00 15.84 ? 215 TYR   A CA  1 
ATOM   1550 C  C   . TYR   A 1 215 ? -4.905  -24.619 -49.176 1.00 16.07 ? 215 TYR   A C   1 
ATOM   1551 O  O   . TYR   A 1 215 ? -4.231  -25.618 -48.986 1.00 17.57 ? 215 TYR   A O   1 
ATOM   1552 C  CB  . TYR   A 1 215 ? -4.029  -22.485 -48.203 1.00 16.19 ? 215 TYR   A CB  1 
ATOM   1553 C  CG  . TYR   A 1 215 ? -2.897  -21.465 -48.267 1.00 16.47 ? 215 TYR   A CG  1 
ATOM   1554 C  CD1 . TYR   A 1 215 ? -1.573  -21.822 -48.020 1.00 15.73 ? 215 TYR   A CD1 1 
ATOM   1555 C  CD2 . TYR   A 1 215 ? -3.148  -20.138 -48.604 1.00 19.67 ? 215 TYR   A CD2 1 
ATOM   1556 C  CE1 . TYR   A 1 215 ? -0.548  -20.889 -48.058 1.00 15.72 ? 215 TYR   A CE1 1 
ATOM   1557 C  CE2 . TYR   A 1 215 ? -2.122  -19.205 -48.697 1.00 19.66 ? 215 TYR   A CE2 1 
ATOM   1558 C  CZ  . TYR   A 1 215 ? -0.820  -19.572 -48.390 1.00 17.61 ? 215 TYR   A CZ  1 
ATOM   1559 O  OH  . TYR   A 1 215 ? 0.203   -18.661 -48.439 1.00 17.42 ? 215 TYR   A OH  1 
ATOM   1560 N  N   . LEU   A 1 216 ? -6.234  -24.649 -49.100 1.00 17.30 ? 216 LEU   A N   1 
ATOM   1561 C  CA  . LEU   A 1 216 ? -6.934  -25.915 -48.895 1.00 18.02 ? 216 LEU   A CA  1 
ATOM   1562 C  C   . LEU   A 1 216 ? -6.752  -26.853 -50.075 1.00 18.42 ? 216 LEU   A C   1 
ATOM   1563 O  O   . LEU   A 1 216 ? -6.710  -28.067 -49.883 1.00 18.43 ? 216 LEU   A O   1 
ATOM   1564 C  CB  . LEU   A 1 216 ? -8.420  -25.712 -48.621 1.00 19.27 ? 216 LEU   A CB  1 
ATOM   1565 C  CG  . LEU   A 1 216 ? -8.702  -25.331 -47.174 1.00 20.67 ? 216 LEU   A CG  1 
ATOM   1566 C  CD1 . LEU   A 1 216 ? -10.124 -24.814 -47.016 1.00 23.16 ? 216 LEU   A CD1 1 
ATOM   1567 C  CD2 . LEU   A 1 216 ? -8.423  -26.547 -46.301 1.00 20.37 ? 216 LEU   A CD2 1 
ATOM   1568 N  N   . ALA   A 1 217 ? -6.725  -26.291 -51.291 1.00 18.77 ? 217 ALA   A N   1 
ATOM   1569 C  CA  . ALA   A 1 217 ? -6.590  -27.113 -52.490 1.00 18.65 ? 217 ALA   A CA  1 
ATOM   1570 C  C   . ALA   A 1 217 ? -5.264  -27.869 -52.469 1.00 19.03 ? 217 ALA   A C   1 
ATOM   1571 O  O   . ALA   A 1 217 ? -5.196  -29.003 -52.931 1.00 20.46 ? 217 ALA   A O   1 
ATOM   1572 C  CB  . ALA   A 1 217 ? -6.755  -26.259 -53.733 1.00 18.82 ? 217 ALA   A CB  1 
ATOM   1573 N  N   . ILE   A 1 218 ? -4.209  -27.279 -51.887 1.00 17.70 ? 218 ILE   A N   1 
ATOM   1574 C  CA  . ILE   A 1 218 ? -2.934  -27.971 -51.810 1.00 17.87 ? 218 ILE   A CA  1 
ATOM   1575 C  C   . ILE   A 1 218 ? -3.087  -29.240 -50.977 1.00 18.33 ? 218 ILE   A C   1 
ATOM   1576 O  O   . ILE   A 1 218 ? -2.626  -30.310 -51.370 1.00 18.59 ? 218 ILE   A O   1 
ATOM   1577 C  CB  . ILE   A 1 218 ? -1.834  -27.042 -51.274 1.00 19.07 ? 218 ILE   A CB  1 
ATOM   1578 C  CG1 . ILE   A 1 218 ? -1.617  -25.820 -52.180 1.00 18.94 ? 218 ILE   A CG1 1 
ATOM   1579 C  CG2 . ILE   A 1 218 ? -0.556  -27.835 -51.035 1.00 19.97 ? 218 ILE   A CG2 1 
ATOM   1580 C  CD1 . ILE   A 1 218 ? -0.904  -24.668 -51.497 1.00 19.92 ? 218 ILE   A CD1 1 
ATOM   1581 N  N   . ALA   A 1 219 ? -3.729  -29.117 -49.816 1.00 17.58 ? 219 ALA   A N   1 
ATOM   1582 C  CA  . ALA   A 1 219 ? -3.960  -30.267 -48.952 1.00 17.21 ? 219 ALA   A CA  1 
ATOM   1583 C  C   . ALA   A 1 219 ? -4.808  -31.312 -49.682 1.00 18.02 ? 219 ALA   A C   1 
ATOM   1584 O  O   . ALA   A 1 219 ? -4.527  -32.502 -49.651 1.00 17.24 ? 219 ALA   A O   1 
ATOM   1585 C  CB  . ALA   A 1 219 ? -4.644  -29.804 -47.679 1.00 18.02 ? 219 ALA   A CB  1 
ATOM   1586 N  N   . ASP   A 1 220 ? -5.887  -30.858 -50.307 1.00 18.34 ? 220 ASP   A N   1 
ATOM   1587 C  CA  . ASP   A 1 220 ? -6.784  -31.765 -51.025 1.00 19.39 ? 220 ASP   A CA  1 
ATOM   1588 C  C   . ASP   A 1 220 ? -6.040  -32.541 -52.113 1.00 19.48 ? 220 ASP   A C   1 
ATOM   1589 O  O   . ASP   A 1 220 ? -6.228  -33.751 -52.239 1.00 21.95 ? 220 ASP   A O   1 
ATOM   1590 C  CB  . ASP   A 1 220 ? -7.977  -31.006 -51.580 1.00 20.74 ? 220 ASP   A CB  1 
ATOM   1591 C  CG  . ASP   A 1 220 ? -8.949  -30.440 -50.557 1.00 23.77 ? 220 ASP   A CG  1 
ATOM   1592 O  OD1 . ASP   A 1 220 ? -8.816  -30.751 -49.337 1.00 24.53 ? 220 ASP   A OD1 1 
ATOM   1593 O  OD2 . ASP   A 1 220 ? -9.831  -29.663 -50.974 1.00 25.50 ? 220 ASP   A OD2 1 
ATOM   1594 N  N   . GLU   A 1 221 ? -5.170  -31.867 -52.860 1.00 20.89 ? 221 GLU   A N   1 
ATOM   1595 C  CA  . GLU   A 1 221 ? -4.404  -32.527 -53.915 1.00 24.40 ? 221 GLU   A CA  1 
ATOM   1596 C  C   . GLU   A 1 221 ? -3.372  -33.516 -53.357 1.00 22.24 ? 221 GLU   A C   1 
ATOM   1597 O  O   . GLU   A 1 221 ? -3.118  -34.556 -53.961 1.00 21.92 ? 221 GLU   A O   1 
ATOM   1598 C  CB  . GLU   A 1 221 ? -3.727  -31.493 -54.821 1.00 29.91 ? 221 GLU   A CB  1 
ATOM   1599 C  CG  . GLU   A 1 221 ? -2.906  -32.111 -55.957 1.00 38.56 ? 221 GLU   A CG  1 
ATOM   1600 C  CD  . GLU   A 1 221 ? -3.626  -32.930 -57.042 1.00 48.49 ? 221 GLU   A CD  1 
ATOM   1601 O  OE1 . GLU   A 1 221 ? -4.863  -32.750 -57.226 1.00 52.45 ? 221 GLU   A OE1 1 
ATOM   1602 O  OE2 . GLU   A 1 221 ? -2.960  -33.773 -57.714 1.00 47.96 ? 221 GLU   A OE2 1 
ATOM   1603 N  N   . LEU   A 1 222 ? -2.745  -33.201 -52.216 1.00 19.12 ? 222 LEU   A N   1 
ATOM   1604 C  CA  . LEU   A 1 222 ? -1.716  -34.062 -51.676 1.00 18.53 ? 222 LEU   A CA  1 
ATOM   1605 C  C   . LEU   A 1 222 ? -2.312  -35.267 -50.961 1.00 18.82 ? 222 LEU   A C   1 
ATOM   1606 O  O   . LEU   A 1 222 ? -1.753  -36.360 -51.062 1.00 19.85 ? 222 LEU   A O   1 
ATOM   1607 C  CB  . LEU   A 1 222 ? -0.813  -33.283 -50.723 1.00 20.30 ? 222 LEU   A CB  1 
ATOM   1608 C  CG  . LEU   A 1 222 ? 0.178   -32.316 -51.374 1.00 21.82 ? 222 LEU   A CG  1 
ATOM   1609 C  CD1 . LEU   A 1 222 ? 0.862   -31.570 -50.245 1.00 21.37 ? 222 LEU   A CD1 1 
ATOM   1610 C  CD2 . LEU   A 1 222 ? 1.218   -33.012 -52.228 1.00 23.56 ? 222 LEU   A CD2 1 
ATOM   1611 N  N   . PHE   A 1 223 ? -3.397  -35.062 -50.202 1.00 17.99 ? 223 PHE   A N   1 
ATOM   1612 C  CA  . PHE   A 1 223 ? -3.844  -36.082 -49.277 1.00 19.39 ? 223 PHE   A CA  1 
ATOM   1613 C  C   . PHE   A 1 223 ? -5.227  -36.633 -49.615 1.00 20.14 ? 223 PHE   A C   1 
ATOM   1614 O  O   . PHE   A 1 223 ? -5.567  -37.702 -49.111 1.00 21.63 ? 223 PHE   A O   1 
ATOM   1615 C  CB  . PHE   A 1 223 ? -3.912  -35.517 -47.857 1.00 18.82 ? 223 PHE   A CB  1 
ATOM   1616 C  CG  . PHE   A 1 223 ? -2.554  -35.083 -47.341 1.00 17.81 ? 223 PHE   A CG  1 
ATOM   1617 C  CD1 . PHE   A 1 223 ? -1.584  -36.029 -47.101 1.00 19.76 ? 223 PHE   A CD1 1 
ATOM   1618 C  CD2 . PHE   A 1 223 ? -2.252  -33.746 -47.111 1.00 18.51 ? 223 PHE   A CD2 1 
ATOM   1619 C  CE1 . PHE   A 1 223 ? -0.333  -35.653 -46.626 1.00 20.07 ? 223 PHE   A CE1 1 
ATOM   1620 C  CE2 . PHE   A 1 223 ? -0.988  -33.379 -46.680 1.00 17.75 ? 223 PHE   A CE2 1 
ATOM   1621 C  CZ  . PHE   A 1 223 ? -0.045  -34.333 -46.396 1.00 18.72 ? 223 PHE   A CZ  1 
ATOM   1622 N  N   . GLY   A 1 224 ? -5.991  -35.911 -50.424 1.00 21.93 ? 224 GLY   A N   1 
ATOM   1623 C  CA  . GLY   A 1 224 ? -7.405  -36.173 -50.588 1.00 21.72 ? 224 GLY   A CA  1 
ATOM   1624 C  C   . GLY   A 1 224 ? -8.223  -35.164 -49.792 1.00 23.43 ? 224 GLY   A C   1 
ATOM   1625 O  O   . GLY   A 1 224 ? -7.771  -34.657 -48.757 1.00 21.97 ? 224 GLY   A O   1 
ATOM   1626 N  N   . ALA   A 1 225 ? -9.472  -34.967 -50.227 1.00 22.34 ? 225 ALA   A N   1 
ATOM   1627 C  CA  . ALA   A 1 225 ? -10.285 -33.860 -49.757 1.00 23.70 ? 225 ALA   A CA  1 
ATOM   1628 C  C   . ALA   A 1 225 ? -10.787 -34.054 -48.331 1.00 22.55 ? 225 ALA   A C   1 
ATOM   1629 O  O   . ALA   A 1 225 ? -11.240 -33.086 -47.726 1.00 26.88 ? 225 ALA   A O   1 
ATOM   1630 C  CB  . ALA   A 1 225 ? -11.442 -33.653 -50.717 1.00 25.71 ? 225 ALA   A CB  1 
ATOM   1631 N  N   . ASP   A 1 226 ? -10.702 -35.256 -47.765 1.00 22.82 ? 226 ASP   A N   1 
ATOM   1632 C  CA  . ASP   A 1 226 ? -11.187 -35.488 -46.405 1.00 24.90 ? 226 ASP   A CA  1 
ATOM   1633 C  C   . ASP   A 1 226 ? -10.113 -35.253 -45.341 1.00 23.53 ? 226 ASP   A C   1 
ATOM   1634 O  O   . ASP   A 1 226 ? -10.393 -35.329 -44.140 1.00 22.68 ? 226 ASP   A O   1 
ATOM   1635 C  CB  . ASP   A 1 226 ? -11.735 -36.898 -46.244 1.00 30.53 ? 226 ASP   A CB  1 
ATOM   1636 C  CG  . ASP   A 1 226 ? -13.028 -37.150 -47.005 1.00 37.07 ? 226 ASP   A CG  1 
ATOM   1637 O  OD1 . ASP   A 1 226 ? -13.866 -36.217 -47.063 1.00 44.65 ? 226 ASP   A OD1 1 
ATOM   1638 O  OD2 . ASP   A 1 226 ? -13.191 -38.272 -47.511 1.00 44.88 ? 226 ASP   A OD2 1 
ATOM   1639 N  N   . TRP   A 1 227 ? -8.859  -35.069 -45.752 1.00 20.34 ? 227 TRP   A N   1 
ATOM   1640 C  CA  . TRP   A 1 227 ? -7.771  -35.014 -44.791 1.00 19.53 ? 227 TRP   A CA  1 
ATOM   1641 C  C   . TRP   A 1 227 ? -7.855  -33.780 -43.883 1.00 17.91 ? 227 TRP   A C   1 
ATOM   1642 O  O   . TRP   A 1 227 ? -7.622  -33.913 -42.682 1.00 19.04 ? 227 TRP   A O   1 
ATOM   1643 C  CB  . TRP   A 1 227 ? -6.430  -35.071 -45.516 1.00 19.31 ? 227 TRP   A CB  1 
ATOM   1644 C  CG  . TRP   A 1 227 ? -5.255  -35.022 -44.598 1.00 18.35 ? 227 TRP   A CG  1 
ATOM   1645 C  CD1 . TRP   A 1 227 ? -4.754  -36.055 -43.871 1.00 19.59 ? 227 TRP   A CD1 1 
ATOM   1646 C  CD2 . TRP   A 1 227 ? -4.434  -33.877 -44.309 1.00 17.67 ? 227 TRP   A CD2 1 
ATOM   1647 N  NE1 . TRP   A 1 227 ? -3.673  -35.636 -43.149 1.00 19.38 ? 227 TRP   A NE1 1 
ATOM   1648 C  CE2 . TRP   A 1 227 ? -3.441  -34.311 -43.400 1.00 17.44 ? 227 TRP   A CE2 1 
ATOM   1649 C  CE3 . TRP   A 1 227 ? -4.423  -32.545 -44.724 1.00 16.94 ? 227 TRP   A CE3 1 
ATOM   1650 C  CZ2 . TRP   A 1 227 ? -2.461  -33.448 -42.892 1.00 16.27 ? 227 TRP   A CZ2 1 
ATOM   1651 C  CZ3 . TRP   A 1 227 ? -3.449  -31.694 -44.232 1.00 16.59 ? 227 TRP   A CZ3 1 
ATOM   1652 C  CH2 . TRP   A 1 227 ? -2.451  -32.156 -43.376 1.00 16.68 ? 227 TRP   A CH2 1 
ATOM   1653 N  N   . ALA   A 1 228 ? -8.170  -32.618 -44.458 1.00 16.92 ? 228 ALA   A N   1 
ATOM   1654 C  CA  . ALA   A 1 228 ? -8.048  -31.333 -43.766 1.00 17.02 ? 228 ALA   A CA  1 
ATOM   1655 C  C   . ALA   A 1 228 ? -9.234  -31.055 -42.846 1.00 17.99 ? 228 ALA   A C   1 
ATOM   1656 O  O   . ALA   A 1 228 ? -9.992  -30.115 -43.053 1.00 18.95 ? 228 ALA   A O   1 
ATOM   1657 C  CB  . ALA   A 1 228 ? -7.870  -30.192 -44.739 1.00 17.82 ? 228 ALA   A CB  1 
ATOM   1658 N  N   . ASP   A 1 229 ? -9.350  -31.858 -41.798 1.00 17.64 ? 229 ASP   A N   1 
ATOM   1659 C  CA  . ASP   A 1 229 ? -10.245 -31.569 -40.685 1.00 17.78 ? 229 ASP   A CA  1 
ATOM   1660 C  C   . ASP   A 1 229 ? -9.472  -30.747 -39.649 1.00 17.00 ? 229 ASP   A C   1 
ATOM   1661 O  O   . ASP   A 1 229 ? -8.293  -30.399 -39.845 1.00 15.63 ? 229 ASP   A O   1 
ATOM   1662 C  CB  . ASP   A 1 229 ? -10.818 -32.856 -40.138 1.00 18.70 ? 229 ASP   A CB  1 
ATOM   1663 C  CG  . ASP   A 1 229 ? -9.811  -33.807 -39.491 1.00 22.56 ? 229 ASP   A CG  1 
ATOM   1664 O  OD1 . ASP   A 1 229 ? -8.632  -33.407 -39.252 1.00 19.13 ? 229 ASP   A OD1 1 
ATOM   1665 O  OD2 . ASP   A 1 229 ? -10.211 -34.942 -39.180 1.00 26.17 ? 229 ASP   A OD2 1 
ATOM   1666 N  N   . ALA   A 1 230 ? -10.137 -30.454 -38.529 1.00 14.90 ? 230 ALA   A N   1 
ATOM   1667 C  CA  . ALA   A 1 230 ? -9.535  -29.539 -37.556 1.00 16.81 ? 230 ALA   A CA  1 
ATOM   1668 C  C   . ALA   A 1 230 ? -8.329  -30.162 -36.854 1.00 15.31 ? 230 ALA   A C   1 
ATOM   1669 O  O   . ALA   A 1 230 ? -7.522  -29.444 -36.287 1.00 15.27 ? 230 ALA   A O   1 
ATOM   1670 C  CB  . ALA   A 1 230 ? -10.553 -29.073 -36.551 1.00 18.46 ? 230 ALA   A CB  1 
ATOM   1671 N  N   . ARG   A 1 231 ? -8.191  -31.488 -36.878 1.00 14.84 ? 231 ARG   A N   1 
ATOM   1672 C  CA  . ARG   A 1 231 ? -7.015  -32.118 -36.296 1.00 15.54 ? 231 ARG   A CA  1 
ATOM   1673 C  C   . ARG   A 1 231 ? -5.813  -32.023 -37.244 1.00 15.66 ? 231 ARG   A C   1 
ATOM   1674 O  O   . ARG   A 1 231 ? -4.675  -32.301 -36.825 1.00 15.61 ? 231 ARG   A O   1 
ATOM   1675 C  CB  . ARG   A 1 231 ? -7.341  -33.562 -35.929 1.00 15.75 ? 231 ARG   A CB  1 
ATOM   1676 C  CG  . ARG   A 1 231 ? -6.184  -34.367 -35.359 1.00 17.73 ? 231 ARG   A CG  1 
ATOM   1677 C  CD  . ARG   A 1 231 ? -5.487  -33.786 -34.134 1.00 16.47 ? 231 ARG   A CD  1 
ATOM   1678 N  NE  . ARG   A 1 231 ? -4.330  -34.569 -33.738 1.00 17.18 ? 231 ARG   A NE  1 
ATOM   1679 C  CZ  . ARG   A 1 231 ? -3.084  -34.465 -34.216 1.00 17.19 ? 231 ARG   A CZ  1 
ATOM   1680 N  NH1 . ARG   A 1 231 ? -2.790  -33.588 -35.166 1.00 16.91 ? 231 ARG   A NH1 1 
ATOM   1681 N  NH2 . ARG   A 1 231 ? -2.109  -35.212 -33.719 1.00 16.65 ? 231 ARG   A NH2 1 
ATOM   1682 N  N   . HIS   A 1 232 ? -6.059  -31.718 -38.535 1.00 13.99 ? 232 HIS   A N   1 
ATOM   1683 C  CA  . HIS   A 1 232 ? -4.998  -31.763 -39.521 1.00 13.91 ? 232 HIS   A CA  1 
ATOM   1684 C  C   . HIS   A 1 232 ? -4.718  -30.446 -40.225 1.00 12.65 ? 232 HIS   A C   1 
ATOM   1685 O  O   . HIS   A 1 232 ? -3.735  -30.369 -40.937 1.00 12.63 ? 232 HIS   A O   1 
ATOM   1686 C  CB  . HIS   A 1 232 ? -5.272  -32.879 -40.527 1.00 14.89 ? 232 HIS   A CB  1 
ATOM   1687 C  CG  . HIS   A 1 232 ? -5.244  -34.203 -39.850 1.00 15.16 ? 232 HIS   A CG  1 
ATOM   1688 N  ND1 . HIS   A 1 232 ? -6.328  -34.772 -39.237 1.00 17.72 ? 232 HIS   A ND1 1 
ATOM   1689 C  CD2 . HIS   A 1 232 ? -4.249  -35.051 -39.684 1.00 16.94 ? 232 HIS   A CD2 1 
ATOM   1690 C  CE1 . HIS   A 1 232 ? -5.981  -35.952 -38.748 1.00 17.71 ? 232 HIS   A CE1 1 
ATOM   1691 N  NE2 . HIS   A 1 232 ? -4.710  -36.122 -38.953 1.00 17.22 ? 232 HIS   A NE2 1 
ATOM   1692 N  N   . TYR   A 1 233 ? -5.575  -29.434 -40.092 1.00 12.74 ? 233 TYR   A N   1 
ATOM   1693 C  CA  . TYR   A 1 233 ? -5.371  -28.199 -40.822 1.00 12.27 ? 233 TYR   A CA  1 
ATOM   1694 C  C   . TYR   A 1 233 ? -5.943  -27.038 -40.021 1.00 12.30 ? 233 TYR   A C   1 
ATOM   1695 O  O   . TYR   A 1 233 ? -7.043  -27.151 -39.469 1.00 12.21 ? 233 TYR   A O   1 
ATOM   1696 C  CB  . TYR   A 1 233 ? -6.097  -28.281 -42.165 1.00 11.94 ? 233 TYR   A CB  1 
ATOM   1697 C  CG  . TYR   A 1 233 ? -5.519  -27.371 -43.218 1.00 12.33 ? 233 TYR   A CG  1 
ATOM   1698 C  CD1 . TYR   A 1 233 ? -5.764  -26.006 -43.227 1.00 13.28 ? 233 TYR   A CD1 1 
ATOM   1699 C  CD2 . TYR   A 1 233 ? -4.751  -27.914 -44.231 1.00 13.88 ? 233 TYR   A CD2 1 
ATOM   1700 C  CE1 . TYR   A 1 233 ? -5.155  -25.182 -44.171 1.00 14.97 ? 233 TYR   A CE1 1 
ATOM   1701 C  CE2 . TYR   A 1 233 ? -4.182  -27.109 -45.207 1.00 14.81 ? 233 TYR   A CE2 1 
ATOM   1702 C  CZ  . TYR   A 1 233 ? -4.402  -25.754 -45.175 1.00 15.67 ? 233 TYR   A CZ  1 
ATOM   1703 O  OH  . TYR   A 1 233 ? -3.772  -25.031 -46.161 1.00 18.27 ? 233 TYR   A OH  1 
ATOM   1704 N  N   . ARG   A 1 234 ? -5.196  -25.936 -39.996 1.00 11.61 ? 234 ARG   A N   1 
ATOM   1705 C  CA  . ARG   A 1 234 ? -5.658  -24.703 -39.394 1.00 11.47 ? 234 ARG   A CA  1 
ATOM   1706 C  C   . ARG   A 1 234 ? -5.169  -23.506 -40.201 1.00 11.78 ? 234 ARG   A C   1 
ATOM   1707 O  O   . ARG   A 1 234 ? -4.138  -23.547 -40.891 1.00 11.62 ? 234 ARG   A O   1 
ATOM   1708 C  CB  . ARG   A 1 234 ? -5.134  -24.542 -37.962 1.00 11.76 ? 234 ARG   A CB  1 
ATOM   1709 C  CG  . ARG   A 1 234 ? -5.546  -25.643 -37.000 1.00 11.78 ? 234 ARG   A CG  1 
ATOM   1710 C  CD  . ARG   A 1 234 ? -7.004  -25.572 -36.613 1.00 11.92 ? 234 ARG   A CD  1 
ATOM   1711 N  NE  . ARG   A 1 234 ? -7.281  -26.698 -35.724 1.00 12.53 ? 234 ARG   A NE  1 
ATOM   1712 C  CZ  . ARG   A 1 234 ? -6.888  -26.771 -34.458 1.00 13.80 ? 234 ARG   A CZ  1 
ATOM   1713 N  NH1 . ARG   A 1 234 ? -6.502  -25.698 -33.797 1.00 14.34 ? 234 ARG   A NH1 1 
ATOM   1714 N  NH2 . ARG   A 1 234 ? -6.941  -27.925 -33.821 1.00 15.73 ? 234 ARG   A NH2 1 
ATOM   1715 N  N   . PHE   A 1 235 ? -5.898  -22.392 -40.024 1.00 12.18 ? 235 PHE   A N   1 
ATOM   1716 C  CA  . PHE   A 1 235 ? -5.545  -21.111 -40.585 1.00 13.50 ? 235 PHE   A CA  1 
ATOM   1717 C  C   . PHE   A 1 235 ? -5.497  -20.073 -39.483 1.00 15.36 ? 235 PHE   A C   1 
ATOM   1718 O  O   . PHE   A 1 235 ? -6.377  -20.068 -38.607 1.00 14.73 ? 235 PHE   A O   1 
ATOM   1719 C  CB  . PHE   A 1 235 ? -6.633  -20.556 -41.514 1.00 14.47 ? 235 PHE   A CB  1 
ATOM   1720 C  CG  . PHE   A 1 235 ? -6.792  -21.248 -42.854 1.00 14.95 ? 235 PHE   A CG  1 
ATOM   1721 C  CD1 . PHE   A 1 235 ? -6.016  -20.830 -43.911 1.00 16.55 ? 235 PHE   A CD1 1 
ATOM   1722 C  CD2 . PHE   A 1 235 ? -7.713  -22.271 -43.055 1.00 17.33 ? 235 PHE   A CD2 1 
ATOM   1723 C  CE1 . PHE   A 1 235 ? -6.150  -21.418 -45.167 1.00 17.78 ? 235 PHE   A CE1 1 
ATOM   1724 C  CE2 . PHE   A 1 235 ? -7.827  -22.868 -44.308 1.00 18.08 ? 235 PHE   A CE2 1 
ATOM   1725 C  CZ  . PHE   A 1 235 ? -7.052  -22.434 -45.353 1.00 17.24 ? 235 PHE   A CZ  1 
ATOM   1726 N  N   . SER   A 1 236 ? -4.533  -19.150 -39.573 1.00 16.83 ? 236 SER   A N   1 
ATOM   1727 C  CA  . SER   A 1 236 ? -4.653  -17.878 -38.866 1.00 19.11 ? 236 SER   A CA  1 
ATOM   1728 C  C   . SER   A 1 236 ? -4.072  -16.751 -39.728 1.00 19.33 ? 236 SER   A C   1 
ATOM   1729 O  O   . SER   A 1 236 ? -3.015  -16.880 -40.327 1.00 19.28 ? 236 SER   A O   1 
ATOM   1730 C  CB  . SER   A 1 236 ? -4.007  -17.947 -37.508 1.00 23.24 ? 236 SER   A CB  1 
ATOM   1731 O  OG  . SER   A 1 236 ? -2.597  -18.031 -37.656 1.00 29.13 ? 236 SER   A OG  1 
ATOM   1732 N  N   . ALA   A 1 237 ? -4.784  -15.638 -39.813 1.00 20.69 ? 237 ALA   A N   1 
ATOM   1733 C  CA  . ALA   A 1 237 ? -4.325  -14.473 -40.553 1.00 22.78 ? 237 ALA   A CA  1 
ATOM   1734 C  C   . ALA   A 1 237 ? -5.224  -13.285 -40.204 1.00 26.30 ? 237 ALA   A C   1 
ATOM   1735 O  O   . ALA   A 1 237 ? -6.442  -13.445 -40.121 1.00 25.07 ? 237 ALA   A O   1 
ATOM   1736 C  CB  . ALA   A 1 237 ? -4.370  -14.749 -42.038 1.00 24.08 ? 237 ALA   A CB  1 
ATOM   1737 N  N   . SER   A 1 238 ? -4.617  -12.106 -40.051 1.00 30.38 ? 238 SER   A N   1 
ATOM   1738 C  CA  . SER   A 1 238 ? -5.336  -10.840 -39.965 1.00 35.37 ? 238 SER   A CA  1 
ATOM   1739 C  C   . SER   A 1 238 ? -6.297  -10.681 -41.133 1.00 32.25 ? 238 SER   A C   1 
ATOM   1740 O  O   . SER   A 1 238 ? -5.894  -10.832 -42.283 1.00 33.49 ? 238 SER   A O   1 
ATOM   1741 C  CB  . SER   A 1 238 ? -4.390  -9.650  -39.997 1.00 37.98 ? 238 SER   A CB  1 
ATOM   1742 O  OG  . SER   A 1 238 ? -3.542  -9.648  -38.863 1.00 45.12 ? 238 SER   A OG  1 
ATOM   1743 N  N   . GLY   A 1 239 ? -7.562  -10.356 -40.823 1.00 33.46 ? 239 GLY   A N   1 
ATOM   1744 C  CA  . GLY   A 1 239 ? -8.520  -9.991  -41.849 1.00 31.77 ? 239 GLY   A CA  1 
ATOM   1745 C  C   . GLY   A 1 239 ? -9.218  -11.202 -42.472 1.00 31.48 ? 239 GLY   A C   1 
ATOM   1746 O  O   . GLY   A 1 239 ? -10.192 -11.036 -43.204 1.00 30.11 ? 239 GLY   A O   1 
ATOM   1747 N  N   . LEU   A 1 240 ? -8.748  -12.430 -42.188 1.00 25.26 ? 240 LEU   A N   1 
ATOM   1748 C  CA  . LEU   A 1 240 ? -9.275  -13.566 -42.923 1.00 22.73 ? 240 LEU   A CA  1 
ATOM   1749 C  C   . LEU   A 1 240 ? -10.734 -13.833 -42.531 1.00 21.42 ? 240 LEU   A C   1 
ATOM   1750 O  O   . LEU   A 1 240 ? -11.543 -14.134 -43.385 1.00 23.23 ? 240 LEU   A O   1 
ATOM   1751 C  CB  . LEU   A 1 240 ? -8.413  -14.808 -42.725 1.00 22.44 ? 240 LEU   A CB  1 
ATOM   1752 C  CG  . LEU   A 1 240 ? -8.933  -16.067 -43.424 1.00 21.33 ? 240 LEU   A CG  1 
ATOM   1753 C  CD1 . LEU   A 1 240 ? -9.082  -15.859 -44.912 1.00 23.11 ? 240 LEU   A CD1 1 
ATOM   1754 C  CD2 . LEU   A 1 240 ? -8.004  -17.244 -43.135 1.00 21.70 ? 240 LEU   A CD2 1 
ATOM   1755 N  N   . LEU   A 1 241 ? -11.066 -13.789 -41.242 1.00 22.29 ? 241 LEU   A N   1 
ATOM   1756 C  CA  . LEU   A 1 241 ? -12.411 -14.154 -40.812 1.00 22.89 ? 241 LEU   A CA  1 
ATOM   1757 C  C   . LEU   A 1 241 ? -13.425 -13.231 -41.494 1.00 23.60 ? 241 LEU   A C   1 
ATOM   1758 O  O   . LEU   A 1 241 ? -14.453 -13.693 -41.970 1.00 23.16 ? 241 LEU   A O   1 
ATOM   1759 C  CB  . LEU   A 1 241 ? -12.556 -14.082 -39.297 1.00 22.97 ? 241 LEU   A CB  1 
ATOM   1760 C  CG  . LEU   A 1 241 ? -13.964 -14.349 -38.757 1.00 23.51 ? 241 LEU   A CG  1 
ATOM   1761 C  CD1 . LEU   A 1 241 ? -14.435 -15.733 -39.168 1.00 24.17 ? 241 LEU   A CD1 1 
ATOM   1762 C  CD2 . LEU   A 1 241 ? -14.065 -14.170 -37.247 1.00 24.37 ? 241 LEU   A CD2 1 
ATOM   1763 N  N   . ALA   A 1 242 ? -13.132 -11.931 -41.499 1.00 25.87 ? 242 ALA   A N   1 
ATOM   1764 C  CA  . ALA   A 1 242 ? -14.002 -10.947 -42.138 1.00 28.20 ? 242 ALA   A CA  1 
ATOM   1765 C  C   . ALA   A 1 242 ? -14.178 -11.270 -43.618 1.00 27.74 ? 242 ALA   A C   1 
ATOM   1766 O  O   . ALA   A 1 242 ? -15.292 -11.222 -44.144 1.00 27.41 ? 242 ALA   A O   1 
ATOM   1767 C  CB  . ALA   A 1 242 ? -13.459 -9.547  -41.923 1.00 29.04 ? 242 ALA   A CB  1 
ATOM   1768 N  N   . SER   A 1 243 ? -13.099 -11.670 -44.293 1.00 26.62 ? 243 SER   A N   1 
ATOM   1769 C  CA  . SER   A 1 243 ? -13.199 -12.010 -45.706 1.00 25.85 ? 243 SER   A CA  1 
ATOM   1770 C  C   . SER   A 1 243 ? -14.046 -13.269 -45.906 1.00 24.58 ? 243 SER   A C   1 
ATOM   1771 O  O   . SER   A 1 243 ? -14.845 -13.357 -46.842 1.00 25.44 ? 243 SER   A O   1 
ATOM   1772 C  CB  . SER   A 1 243 ? -11.813 -12.145 -46.338 1.00 25.94 ? 243 SER   A CB  1 
ATOM   1773 O  OG  . SER   A 1 243 ? -11.938 -12.559 -47.691 1.00 27.35 ? 243 SER   A OG  1 
ATOM   1774 N  N   . LEU   A 1 244 ? -13.870 -14.273 -45.036 1.00 21.30 ? 244 LEU   A N   1 
ATOM   1775 C  CA  . LEU   A 1 244 ? -14.662 -15.494 -45.147 1.00 22.58 ? 244 LEU   A CA  1 
ATOM   1776 C  C   . LEU   A 1 244 ? -16.146 -15.197 -44.909 1.00 23.93 ? 244 LEU   A C   1 
ATOM   1777 O  O   . LEU   A 1 244 ? -17.001 -15.738 -45.599 1.00 24.43 ? 244 LEU   A O   1 
ATOM   1778 C  CB  . LEU   A 1 244 ? -14.177 -16.563 -44.168 1.00 20.67 ? 244 LEU   A CB  1 
ATOM   1779 C  CG  . LEU   A 1 244 ? -12.728 -17.038 -44.375 1.00 20.91 ? 244 LEU   A CG  1 
ATOM   1780 C  CD1 . LEU   A 1 244 ? -12.286 -17.961 -43.241 1.00 21.04 ? 244 LEU   A CD1 1 
ATOM   1781 C  CD2 . LEU   A 1 244 ? -12.600 -17.782 -45.670 1.00 21.51 ? 244 LEU   A CD2 1 
ATOM   1782 N  N   . LEU   A 1 245 ? -16.439 -14.372 -43.904 1.00 23.49 ? 245 LEU   A N   1 
ATOM   1783 C  CA  . LEU   A 1 245 ? -17.822 -14.070 -43.584 1.00 24.72 ? 245 LEU   A CA  1 
ATOM   1784 C  C   . LEU   A 1 245 ? -18.473 -13.285 -44.724 1.00 25.91 ? 245 LEU   A C   1 
ATOM   1785 O  O   . LEU   A 1 245 ? -19.631 -13.527 -45.028 1.00 26.79 ? 245 LEU   A O   1 
ATOM   1786 C  CB  . LEU   A 1 245 ? -17.931 -13.333 -42.258 1.00 24.37 ? 245 LEU   A CB  1 
ATOM   1787 C  CG  . LEU   A 1 245 ? -17.743 -14.227 -41.028 1.00 24.61 ? 245 LEU   A CG  1 
ATOM   1788 C  CD1 . LEU   A 1 245 ? -17.684 -13.378 -39.784 1.00 26.58 ? 245 LEU   A CD1 1 
ATOM   1789 C  CD2 . LEU   A 1 245 ? -18.865 -15.267 -40.944 1.00 24.11 ? 245 LEU   A CD2 1 
ATOM   1790 N  N   . LYS   A 1 246 ? -17.707 -12.388 -45.341 1.00 29.44 ? 246 LYS   A N   1 
ATOM   1791 C  CA  . LYS   A 1 246 ? -18.188 -11.614 -46.476 1.00 33.25 ? 246 LYS   A CA  1 
ATOM   1792 C  C   . LYS   A 1 246 ? -18.554 -12.559 -47.614 1.00 32.28 ? 246 LYS   A C   1 
ATOM   1793 O  O   . LYS   A 1 246 ? -19.622 -12.426 -48.200 1.00 34.39 ? 246 LYS   A O   1 
ATOM   1794 C  CB  . LYS   A 1 246 ? -17.168 -10.601 -47.002 1.00 39.32 ? 246 LYS   A CB  1 
ATOM   1795 C  CG  . LYS   A 1 246 ? -16.718 -9.478  -46.080 1.00 46.31 ? 246 LYS   A CG  1 
ATOM   1796 C  CD  . LYS   A 1 246 ? -16.527 -8.173  -46.853 1.00 54.70 ? 246 LYS   A CD  1 
ATOM   1797 C  CE  . LYS   A 1 246 ? -16.150 -7.032  -45.961 1.00 59.49 ? 246 LYS   A CE  1 
ATOM   1798 N  NZ  . LYS   A 1 246 ? -14.834 -7.247  -45.343 1.00 60.53 ? 246 LYS   A NZ  1 
ATOM   1799 N  N   . ALA   A 1 247 ? -17.658 -13.505 -47.930 1.00 29.93 ? 247 ALA   A N   1 
ATOM   1800 C  CA  . ALA   A 1 247 ? -17.928 -14.484 -48.966 1.00 30.78 ? 247 ALA   A CA  1 
ATOM   1801 C  C   . ALA   A 1 247 ? -19.180 -15.291 -48.649 1.00 32.92 ? 247 ALA   A C   1 
ATOM   1802 O  O   . ALA   A 1 247 ? -19.829 -15.780 -49.558 1.00 34.65 ? 247 ALA   A O   1 
ATOM   1803 C  CB  . ALA   A 1 247 ? -16.742 -15.396 -49.180 1.00 30.68 ? 247 ALA   A CB  1 
ATOM   1804 N  N   . LEU   A 1 248 ? -19.510 -15.458 -47.361 1.00 31.01 ? 248 LEU   A N   1 
ATOM   1805 C  CA  . LEU   A 1 248 ? -20.634 -16.294 -46.983 1.00 32.54 ? 248 LEU   A CA  1 
ATOM   1806 C  C   . LEU   A 1 248 ? -21.914 -15.476 -46.823 1.00 33.72 ? 248 LEU   A C   1 
ATOM   1807 O  O   . LEU   A 1 248 ? -22.943 -16.037 -46.474 1.00 33.74 ? 248 LEU   A O   1 
ATOM   1808 C  CB  . LEU   A 1 248 ? -20.268 -17.040 -45.701 1.00 30.73 ? 248 LEU   A CB  1 
ATOM   1809 C  CG  . LEU   A 1 248 ? -19.258 -18.177 -45.903 1.00 29.53 ? 248 LEU   A CG  1 
ATOM   1810 C  CD1 . LEU   A 1 248 ? -18.654 -18.686 -44.608 1.00 28.21 ? 248 LEU   A CD1 1 
ATOM   1811 C  CD2 . LEU   A 1 248 ? -19.923 -19.320 -46.655 1.00 31.17 ? 248 LEU   A CD2 1 
ATOM   1812 N  N   . GLY   A 1 249 ? -21.835 -14.159 -47.024 1.00 36.39 ? 249 GLY   A N   1 
ATOM   1813 C  CA  . GLY   A 1 249 ? -23.020 -13.312 -46.998 1.00 37.75 ? 249 GLY   A CA  1 
ATOM   1814 C  C   . GLY   A 1 249 ? -23.209 -12.581 -45.673 1.00 39.90 ? 249 GLY   A C   1 
ATOM   1815 O  O   . GLY   A 1 249 ? -24.258 -11.995 -45.448 1.00 40.64 ? 249 GLY   A O   1 
ATOM   1816 N  N   . HIS   A 1 250 ? -22.201 -12.582 -44.793 1.00 38.36 ? 250 HIS   A N   1 
ATOM   1817 C  CA  . HIS   A 1 250 ? -22.290 -11.794 -43.580 1.00 40.51 ? 250 HIS   A CA  1 
ATOM   1818 C  C   . HIS   A 1 250 ? -21.407 -10.556 -43.741 1.00 45.71 ? 250 HIS   A C   1 
ATOM   1819 O  O   . HIS   A 1 250 ? -20.475 -10.517 -42.943 1.00 57.49 ? 250 HIS   A O   1 
ATOM   1820 C  CB  . HIS   A 1 250 ? -22.027 -12.687 -42.363 1.00 39.31 ? 250 HIS   A CB  1 
ATOM   1821 C  CG  . HIS   A 1 250 ? -23.123 -13.693 -42.188 1.00 38.44 ? 250 HIS   A CG  1 
ATOM   1822 N  ND1 . HIS   A 1 250 ? -23.138 -14.898 -42.865 1.00 37.92 ? 250 HIS   A ND1 1 
ATOM   1823 C  CD2 . HIS   A 1 250 ? -24.273 -13.640 -41.484 1.00 38.72 ? 250 HIS   A CD2 1 
ATOM   1824 C  CE1 . HIS   A 1 250 ? -24.231 -15.574 -42.522 1.00 38.84 ? 250 HIS   A CE1 1 
ATOM   1825 N  NE2 . HIS   A 1 250 ? -24.947 -14.823 -41.701 1.00 38.65 ? 250 HIS   A NE2 1 
ATOM   1826 N  N   . ASP   B 1 3   ? 19.781  2.238   15.938  1.00 43.86 ? 3   ASP   B N   1 
ATOM   1827 C  CA  . ASP   B 1 3   ? 20.881  2.245   14.937  1.00 40.26 ? 3   ASP   B CA  1 
ATOM   1828 C  C   . ASP   B 1 3   ? 20.263  2.109   13.543  1.00 35.16 ? 3   ASP   B C   1 
ATOM   1829 O  O   . ASP   B 1 3   ? 19.821  1.032   13.126  1.00 29.02 ? 3   ASP   B O   1 
ATOM   1830 C  CB  . ASP   B 1 3   ? 21.915  1.174   15.252  1.00 44.97 ? 3   ASP   B CB  1 
ATOM   1831 C  CG  . ASP   B 1 3   ? 23.043  1.032   14.238  1.00 48.66 ? 3   ASP   B CG  1 
ATOM   1832 O  OD1 . ASP   B 1 3   ? 23.051  1.797   13.253  1.00 47.78 ? 3   ASP   B OD1 1 
ATOM   1833 O  OD2 . ASP   B 1 3   ? 23.902  0.150   14.436  1.00 55.42 ? 3   ASP   B OD2 1 
ATOM   1834 N  N   . LEU   B 1 4   ? 20.253  3.224   12.823  1.00 30.51 ? 4   LEU   B N   1 
ATOM   1835 C  CA  . LEU   B 1 4   ? 19.614  3.268   11.521  1.00 31.07 ? 4   LEU   B CA  1 
ATOM   1836 C  C   . LEU   B 1 4   ? 20.365  2.415   10.494  1.00 29.80 ? 4   LEU   B C   1 
ATOM   1837 O  O   . LEU   B 1 4   ? 19.752  1.839   9.593   1.00 25.38 ? 4   LEU   B O   1 
ATOM   1838 C  CB  . LEU   B 1 4   ? 19.548  4.733   11.105  1.00 32.56 ? 4   LEU   B CB  1 
ATOM   1839 C  CG  . LEU   B 1 4   ? 18.725  5.027   9.856   1.00 34.45 ? 4   LEU   B CG  1 
ATOM   1840 C  CD1 . LEU   B 1 4   ? 17.281  4.548   10.040  1.00 34.90 ? 4   LEU   B CD1 1 
ATOM   1841 C  CD2 . LEU   B 1 4   ? 18.760  6.509   9.494   1.00 35.71 ? 4   LEU   B CD2 1 
ATOM   1842 N  N   . LYS   B 1 5   ? 21.702  2.359   10.590  1.00 27.94 ? 5   LYS   B N   1 
ATOM   1843 C  CA  . LYS   B 1 5   ? 22.466  1.538   9.656   1.00 28.88 ? 5   LYS   B CA  1 
ATOM   1844 C  C   . LYS   B 1 5   ? 22.123  0.063   9.843   1.00 25.16 ? 5   LYS   B C   1 
ATOM   1845 O  O   . LYS   B 1 5   ? 21.925  -0.660  8.863   1.00 23.80 ? 5   LYS   B O   1 
ATOM   1846 C  CB  . LYS   B 1 5   ? 23.982  1.773   9.789   1.00 31.93 ? 5   LYS   B CB  1 
ATOM   1847 C  CG  . LYS   B 1 5   ? 24.391  3.128   9.227   1.00 36.95 ? 5   LYS   B CG  1 
ATOM   1848 C  CD  . LYS   B 1 5   ? 25.867  3.324   8.909   1.00 42.94 ? 5   LYS   B CD  1 
ATOM   1849 C  CE  . LYS   B 1 5   ? 26.080  4.678   8.308   1.00 48.31 ? 5   LYS   B CE  1 
ATOM   1850 N  NZ  . LYS   B 1 5   ? 27.356  4.750   7.591   1.00 56.32 ? 5   LYS   B NZ  1 
ATOM   1851 N  N   . ALA   B 1 6   ? 22.020  -0.373  11.103  1.00 24.51 ? 6   ALA   B N   1 
ATOM   1852 C  CA  . ALA   B 1 6   ? 21.731  -1.768  11.395  1.00 24.50 ? 6   ALA   B CA  1 
ATOM   1853 C  C   . ALA   B 1 6   ? 20.322  -2.120  10.921  1.00 22.48 ? 6   ALA   B C   1 
ATOM   1854 O  O   . ALA   B 1 6   ? 20.122  -3.194  10.350  1.00 22.08 ? 6   ALA   B O   1 
ATOM   1855 C  CB  . ALA   B 1 6   ? 21.908  -2.059  12.866  1.00 25.90 ? 6   ALA   B CB  1 
ATOM   1856 N  N   . SER   B 1 7   ? 19.353  -1.213  11.157  1.00 21.14 ? 7   SER   B N   1 
ATOM   1857 C  CA  . SER   B 1 7   ? 17.994  -1.481  10.699  1.00 21.97 ? 7   SER   B CA  1 
ATOM   1858 C  C   . SER   B 1 7   ? 17.932  -1.484  9.172   1.00 19.13 ? 7   SER   B C   1 
ATOM   1859 O  O   . SER   B 1 7   ? 17.175  -2.263  8.599   1.00 17.94 ? 7   SER   B O   1 
ATOM   1860 C  CB  . SER   B 1 7   ? 16.953  -0.575  11.327  1.00 25.20 ? 7   SER   B CB  1 
ATOM   1861 O  OG  . SER   B 1 7   ? 17.193  0.775   10.999  1.00 31.69 ? 7   SER   B OG  1 
ATOM   1862 N  N   . SER   B 1 8   ? 18.686  -0.595  8.522   1.00 18.46 ? 8   SER   B N   1 
ATOM   1863 C  CA  . SER   B 1 8   ? 18.666  -0.496  7.072   1.00 17.71 ? 8   SER   B CA  1 
ATOM   1864 C  C   . SER   B 1 8   ? 19.223  -1.750  6.403   1.00 16.37 ? 8   SER   B C   1 
ATOM   1865 O  O   . SER   B 1 8   ? 18.668  -2.223  5.411   1.00 15.33 ? 8   SER   B O   1 
ATOM   1866 C  CB  . SER   B 1 8   ? 19.377  0.740   6.607   1.00 19.65 ? 8   SER   B CB  1 
ATOM   1867 O  OG  . SER   B 1 8   ? 18.728  1.880   7.152   1.00 19.95 ? 8   SER   B OG  1 
ATOM   1868 N  N   . LEU   B 1 9   ? 20.313  -2.294  6.943   1.00 17.50 ? 9   LEU   B N   1 
ATOM   1869 C  CA  . LEU   B 1 9   ? 20.874  -3.520  6.414   1.00 18.78 ? 9   LEU   B CA  1 
ATOM   1870 C  C   . LEU   B 1 9   ? 19.880  -4.664  6.572   1.00 18.00 ? 9   LEU   B C   1 
ATOM   1871 O  O   . LEU   B 1 9   ? 19.684  -5.502  5.695   1.00 17.09 ? 9   LEU   B O   1 
ATOM   1872 C  CB  . LEU   B 1 9   ? 22.183  -3.858  7.129   1.00 22.35 ? 9   LEU   B CB  1 
ATOM   1873 C  CG  . LEU   B 1 9   ? 22.942  -5.045  6.546   1.00 26.03 ? 9   LEU   B CG  1 
ATOM   1874 C  CD1 . LEU   B 1 9   ? 23.339  -4.751  5.087   1.00 27.50 ? 9   LEU   B CD1 1 
ATOM   1875 C  CD2 . LEU   B 1 9   ? 24.148  -5.370  7.408   1.00 28.46 ? 9   LEU   B CD2 1 
ATOM   1876 N  N   . ARG   B 1 10  ? 19.247  -4.700  7.728   1.00 17.17 ? 10  ARG   B N   1 
ATOM   1877 C  CA  . ARG   B 1 10  ? 18.274  -5.721  8.016   1.00 16.71 ? 10  ARG   B CA  1 
ATOM   1878 C  C   . ARG   B 1 10  ? 17.114  -5.641  7.025   1.00 14.38 ? 10  ARG   B C   1 
ATOM   1879 O  O   . ARG   B 1 10  ? 16.730  -6.660  6.432   1.00 14.21 ? 10  ARG   B O   1 
ATOM   1880 C  CB  . ARG   B 1 10  ? 17.875  -5.465  9.463   1.00 20.01 ? 10  ARG   B CB  1 
ATOM   1881 C  CG  . ARG   B 1 10  ? 17.157  -6.593  10.146  1.00 22.59 ? 10  ARG   B CG  1 
ATOM   1882 C  CD  . ARG   B 1 10  ? 16.897  -6.070  11.559  1.00 23.20 ? 10  ARG   B CD  1 
ATOM   1883 N  NE  . ARG   B 1 10  ? 15.890  -6.960  12.049  1.00 23.72 ? 10  ARG   B NE  1 
ATOM   1884 C  CZ  . ARG   B 1 10  ? 15.092  -6.705  13.064  1.00 21.94 ? 10  ARG   B CZ  1 
ATOM   1885 N  NH1 . ARG   B 1 10  ? 15.046  -5.500  13.590  1.00 24.05 ? 10  ARG   B NH1 1 
ATOM   1886 N  NH2 . ARG   B 1 10  ? 14.330  -7.667  13.504  1.00 22.60 ? 10  ARG   B NH2 1 
ATOM   1887 N  N   . ALA   B 1 11  ? 16.570  -4.426  6.815   1.00 13.21 ? 11  ALA   B N   1 
ATOM   1888 C  CA  . ALA   B 1 11  ? 15.442  -4.223  5.914   1.00 12.93 ? 11  ALA   B CA  1 
ATOM   1889 C  C   . ALA   B 1 11  ? 15.815  -4.588  4.474   1.00 12.73 ? 11  ALA   B C   1 
ATOM   1890 O  O   . ALA   B 1 11  ? 15.006  -5.177  3.761   1.00 13.06 ? 11  ALA   B O   1 
ATOM   1891 C  CB  . ALA   B 1 11  ? 14.959  -2.796  5.959   1.00 13.86 ? 11  ALA   B CB  1 
ATOM   1892 N  N   . LEU   B 1 12  ? 17.039  -4.238  4.053   1.00 12.93 ? 12  LEU   B N   1 
ATOM   1893 C  CA  . LEU   B 1 12  ? 17.445  -4.513  2.688   1.00 13.13 ? 12  LEU   B CA  1 
ATOM   1894 C  C   . LEU   B 1 12  ? 17.382  -6.008  2.414   1.00 13.38 ? 12  LEU   B C   1 
ATOM   1895 O  O   . LEU   B 1 12  ? 16.910  -6.446  1.350   1.00 12.81 ? 12  LEU   B O   1 
ATOM   1896 C  CB  . LEU   B 1 12  ? 18.838  -3.920  2.477   1.00 14.12 ? 12  LEU   B CB  1 
ATOM   1897 C  CG  . LEU   B 1 12  ? 19.411  -4.089  1.067   1.00 14.56 ? 12  LEU   B CG  1 
ATOM   1898 C  CD1 . LEU   B 1 12  ? 20.367  -2.934  0.772   1.00 17.01 ? 12  LEU   B CD1 1 
ATOM   1899 C  CD2 . LEU   B 1 12  ? 20.126  -5.401  0.919   1.00 15.55 ? 12  LEU   B CD2 1 
ATOM   1900 N  N   . LYS   B 1 13  ? 17.824  -6.807  3.383   1.00 12.77 ? 13  LYS   B N   1 
ATOM   1901 C  CA  . LYS   B 1 13  ? 17.905  -8.254  3.196   1.00 13.84 ? 13  LYS   B CA  1 
ATOM   1902 C  C   . LYS   B 1 13  ? 16.533  -8.902  3.341   1.00 13.56 ? 13  LYS   B C   1 
ATOM   1903 O  O   . LYS   B 1 13  ? 16.404  -10.115 3.151   1.00 12.95 ? 13  LYS   B O   1 
ATOM   1904 C  CB  . LYS   B 1 13  ? 18.877  -8.879  4.196   1.00 16.06 ? 13  LYS   B CB  1 
ATOM   1905 C  CG  . LYS   B 1 13  ? 20.327  -8.437  3.949   1.00 17.89 ? 13  LYS   B CG  1 
ATOM   1906 C  CD  . LYS   B 1 13  ? 21.308  -8.917  5.021   1.00 20.81 ? 13  LYS   B CD  1 
ATOM   1907 C  CE  . LYS   B 1 13  ? 22.667  -8.446  4.586   1.00 23.56 ? 13  LYS   B CE  1 
ATOM   1908 N  NZ  . LYS   B 1 13  ? 23.685  -8.954  5.502   1.00 26.82 ? 13  LYS   B NZ  1 
ATOM   1909 N  N   . LEU   B 1 14  ? 15.510  -8.094  3.692   1.00 12.20 ? 14  LEU   B N   1 
ATOM   1910 C  CA  . LEU   B 1 14  ? 14.127  -8.551  3.751   1.00 12.54 ? 14  LEU   B CA  1 
ATOM   1911 C  C   . LEU   B 1 14  ? 13.295  -8.025  2.581   1.00 11.67 ? 14  LEU   B C   1 
ATOM   1912 O  O   . LEU   B 1 14  ? 12.064  -8.199  2.568   1.00 11.36 ? 14  LEU   B O   1 
ATOM   1913 C  CB  . LEU   B 1 14  ? 13.518  -8.113  5.088   1.00 12.34 ? 14  LEU   B CB  1 
ATOM   1914 C  CG  . LEU   B 1 14  ? 14.191  -8.688  6.333   1.00 13.56 ? 14  LEU   B CG  1 
ATOM   1915 C  CD1 . LEU   B 1 14  ? 13.622  -8.023  7.558   1.00 13.90 ? 14  LEU   B CD1 1 
ATOM   1916 C  CD2 . LEU   B 1 14  ? 14.038  -10.197 6.407   1.00 12.98 ? 14  LEU   B CD2 1 
ATOM   1917 N  N   . MET   B 1 15  ? 13.934  -7.397  1.590   1.00 11.49 ? 15  MET   B N   1 
ATOM   1918 C  CA  . MET   B 1 15  ? 13.171  -6.781  0.508   1.00 12.64 ? 15  MET   B CA  1 
ATOM   1919 C  C   . MET   B 1 15  ? 12.764  -7.789  -0.572  1.00 12.32 ? 15  MET   B C   1 
ATOM   1920 O  O   . MET   B 1 15  ? 13.541  -8.653  -0.926  1.00 12.87 ? 15  MET   B O   1 
ATOM   1921 C  CB  . MET   B 1 15  ? 13.936  -5.645  -0.182  1.00 14.24 ? 15  MET   B CB  1 
ATOM   1922 C  CG  . MET   B 1 15  ? 13.854  -4.329  0.604   1.00 18.15 ? 15  MET   B CG  1 
ATOM   1923 S  SD  . MET   B 1 15  ? 14.414  -2.980  -0.469  1.00 23.03 ? 15  MET   B SD  1 
ATOM   1924 C  CE  . MET   B 1 15  ? 12.910  -2.829  -1.440  1.00 25.80 ? 15  MET   B CE  1 
ATOM   1925 N  N   . ASP   B 1 16  ? 11.520  -7.665  -1.045  1.00 11.53 ? 16  ASP   B N   1 
ATOM   1926 C  CA  . ASP   B 1 16  ? 11.088  -8.240  -2.309  1.00 12.58 ? 16  ASP   B CA  1 
ATOM   1927 C  C   . ASP   B 1 16  ? 11.186  -7.101  -3.314  1.00 12.21 ? 16  ASP   B C   1 
ATOM   1928 O  O   . ASP   B 1 16  ? 10.347  -6.204  -3.316  1.00 13.30 ? 16  ASP   B O   1 
ATOM   1929 C  CB  . ASP   B 1 16  ? 9.672   -8.778  -2.272  1.00 12.99 ? 16  ASP   B CB  1 
ATOM   1930 C  CG  . ASP   B 1 16  ? 9.418   -10.008 -1.426  1.00 14.34 ? 16  ASP   B CG  1 
ATOM   1931 O  OD1 . ASP   B 1 16  ? 10.400  -10.519 -0.856  1.00 14.08 ? 16  ASP   B OD1 1 
ATOM   1932 O  OD2 . ASP   B 1 16  ? 8.243   -10.513 -1.456  1.00 15.92 ? 16  ASP   B OD2 1 
ATOM   1933 N  N   . LEU   B 1 17  ? 12.257  -7.069  -4.093  1.00 12.13 ? 17  LEU   B N   1 
ATOM   1934 C  CA  . LEU   B 1 17  ? 12.528  -5.915  -4.931  1.00 13.29 ? 17  LEU   B CA  1 
ATOM   1935 C  C   . LEU   B 1 17  ? 11.724  -5.992  -6.227  1.00 15.27 ? 17  LEU   B C   1 
ATOM   1936 O  O   . LEU   B 1 17  ? 11.776  -7.016  -6.898  1.00 14.76 ? 17  LEU   B O   1 
ATOM   1937 C  CB  . LEU   B 1 17  ? 14.034  -5.884  -5.210  1.00 13.55 ? 17  LEU   B CB  1 
ATOM   1938 C  CG  . LEU   B 1 17  ? 14.516  -4.629  -5.937  1.00 14.65 ? 17  LEU   B CG  1 
ATOM   1939 C  CD1 . LEU   B 1 17  ? 14.345  -3.444  -4.991  1.00 15.96 ? 17  LEU   B CD1 1 
ATOM   1940 C  CD2 . LEU   B 1 17  ? 15.949  -4.772  -6.359  1.00 15.29 ? 17  LEU   B CD2 1 
ATOM   1941 N  N   . SER   B 1 18  ? 10.976  -4.937  -6.594  1.00 19.91 ? 18  SER   B N   1 
ATOM   1942 C  CA  A SER   B 1 18  ? 10.256  -4.929  -7.866  0.50 23.48 ? 18  SER   B CA  1 
ATOM   1943 C  CA  B SER   B 1 18  ? 10.291  -4.946  -7.880  0.50 24.52 ? 18  SER   B CA  1 
ATOM   1944 C  C   . SER   B 1 18  ? 10.725  -3.740  -8.706  1.00 28.13 ? 18  SER   B C   1 
ATOM   1945 O  O   . SER   B 1 18  ? 11.335  -2.814  -8.166  1.00 26.36 ? 18  SER   B O   1 
ATOM   1946 C  CB  A SER   B 1 18  ? 8.755   -4.920  -7.675  0.50 24.72 ? 18  SER   B CB  1 
ATOM   1947 C  CB  B SER   B 1 18  ? 8.785   -5.014  -7.745  0.50 27.29 ? 18  SER   B CB  1 
ATOM   1948 O  OG  A SER   B 1 18  ? 8.380   -3.845  -6.836  0.50 24.04 ? 18  SER   B OG  1 
ATOM   1949 O  OG  B SER   B 1 18  ? 8.220   -5.442  -8.983  0.50 29.02 ? 18  SER   B OG  1 
ATOM   1950 N  N   . THR   B 1 19  ? 10.471  -3.800  -10.030 1.00 32.62 ? 19  THR   B N   1 
ATOM   1951 C  CA  . THR   B 1 19  ? 10.899  -2.740  -10.938 1.00 38.31 ? 19  THR   B CA  1 
ATOM   1952 C  C   . THR   B 1 19  ? 10.145  -1.479  -10.592 1.00 43.15 ? 19  THR   B C   1 
ATOM   1953 O  O   . THR   B 1 19  ? 8.907   -1.612  -10.521 1.00 43.77 ? 19  THR   B O   1 
ATOM   1954 C  CB  . THR   B 1 19  ? 10.640  -3.090  -12.405 1.00 41.10 ? 19  THR   B CB  1 
ATOM   1955 O  OG1 . THR   B 1 19  ? 9.242   -3.371  -12.467 1.00 47.31 ? 19  THR   B OG1 1 
ATOM   1956 C  CG2 . THR   B 1 19  ? 11.420  -4.284  -12.905 1.00 42.30 ? 19  THR   B CG2 1 
ATOM   1957 N  N   . GLY   B 1 22  ? 6.587   -1.782  -13.534 1.00 39.88 ? 22  GLY   B N   1 
ATOM   1958 C  CA  . GLY   B 1 22  ? 6.458   -3.221  -13.826 1.00 33.86 ? 22  GLY   B CA  1 
ATOM   1959 C  C   . GLY   B 1 22  ? 7.432   -3.638  -14.929 1.00 37.89 ? 22  GLY   B C   1 
ATOM   1960 O  O   . GLY   B 1 22  ? 7.934   -2.809  -15.691 1.00 38.96 ? 22  GLY   B O   1 
ATOM   1961 N  N   . ASP   B 1 23  ? 7.660   -4.954  -15.008 1.00 31.12 ? 23  ASP   B N   1 
ATOM   1962 C  CA  . ASP   B 1 23  ? 8.564   -5.584  -15.957 1.00 29.43 ? 23  ASP   B CA  1 
ATOM   1963 C  C   . ASP   B 1 23  ? 7.811   -5.980  -17.235 1.00 32.69 ? 23  ASP   B C   1 
ATOM   1964 O  O   . ASP   B 1 23  ? 7.014   -6.909  -17.222 1.00 33.54 ? 23  ASP   B O   1 
ATOM   1965 C  CB  . ASP   B 1 23  ? 9.152   -6.830  -15.301 1.00 28.29 ? 23  ASP   B CB  1 
ATOM   1966 C  CG  . ASP   B 1 23  ? 8.154   -7.625  -14.460 1.00 28.33 ? 23  ASP   B CG  1 
ATOM   1967 O  OD1 . ASP   B 1 23  ? 7.623   -7.049  -13.498 1.00 31.28 ? 23  ASP   B OD1 1 
ATOM   1968 O  OD2 . ASP   B 1 23  ? 7.865   -8.791  -14.778 1.00 23.10 ? 23  ASP   B OD2 1 
ATOM   1969 N  N   . TYR   B 1 24  ? 8.085   -5.308  -18.354 1.00 30.79 ? 24  TYR   B N   1 
ATOM   1970 C  CA  . TYR   B 1 24  ? 7.464   -5.644  -19.628 1.00 33.36 ? 24  TYR   B CA  1 
ATOM   1971 C  C   . TYR   B 1 24  ? 8.518   -5.970  -20.680 1.00 32.40 ? 24  TYR   B C   1 
ATOM   1972 O  O   . TYR   B 1 24  ? 8.203   -6.258  -21.849 1.00 31.51 ? 24  TYR   B O   1 
ATOM   1973 C  CB  . TYR   B 1 24  ? 6.669   -4.416  -20.085 1.00 35.91 ? 24  TYR   B CB  1 
ATOM   1974 C  CG  . TYR   B 1 24  ? 5.384   -4.236  -19.299 1.00 34.77 ? 24  TYR   B CG  1 
ATOM   1975 C  CD1 . TYR   B 1 24  ? 5.406   -3.679  -18.021 1.00 35.79 ? 24  TYR   B CD1 1 
ATOM   1976 C  CD2 . TYR   B 1 24  ? 4.157   -4.626  -19.832 1.00 35.60 ? 24  TYR   B CD2 1 
ATOM   1977 C  CE1 . TYR   B 1 24  ? 4.237   -3.504  -17.299 1.00 36.04 ? 24  TYR   B CE1 1 
ATOM   1978 C  CE2 . TYR   B 1 24  ? 2.981   -4.455  -19.116 1.00 38.26 ? 24  TYR   B CE2 1 
ATOM   1979 C  CZ  . TYR   B 1 24  ? 3.026   -3.895  -17.848 1.00 40.01 ? 24  TYR   B CZ  1 
ATOM   1980 O  OH  . TYR   B 1 24  ? 1.878   -3.730  -17.130 1.00 42.59 ? 24  TYR   B OH  1 
ATOM   1981 N  N   . THR   B 1 25  ? 9.776   -5.780  -20.287 1.00 25.83 ? 25  THR   B N   1 
ATOM   1982 C  CA  . THR   B 1 25  ? 10.870  -6.075  -21.179 1.00 25.88 ? 25  THR   B CA  1 
ATOM   1983 C  C   . THR   B 1 25  ? 11.888  -6.882  -20.390 1.00 23.02 ? 25  THR   B C   1 
ATOM   1984 O  O   . THR   B 1 25  ? 12.034  -6.727  -19.183 1.00 19.93 ? 25  THR   B O   1 
ATOM   1985 C  CB  . THR   B 1 25  ? 11.460  -4.795  -21.763 1.00 25.01 ? 25  THR   B CB  1 
ATOM   1986 O  OG1 . THR   B 1 25  ? 12.122  -4.085  -20.713 1.00 22.44 ? 25  THR   B OG1 1 
ATOM   1987 C  CG2 . THR   B 1 25  ? 10.393  -3.924  -22.417 1.00 24.17 ? 25  THR   B CG2 1 
ATOM   1988 N  N   . ASP   B 1 26  ? 12.624  -7.704  -21.131 1.00 25.46 ? 26  ASP   B N   1 
ATOM   1989 C  CA  . ASP   B 1 26  ? 13.690  -8.501  -20.565 1.00 24.27 ? 26  ASP   B CA  1 
ATOM   1990 C  C   . ASP   B 1 26  ? 14.718  -7.566  -19.939 1.00 23.13 ? 26  ASP   B C   1 
ATOM   1991 O  O   . ASP   B 1 26  ? 15.270  -7.843  -18.881 1.00 20.47 ? 26  ASP   B O   1 
ATOM   1992 C  CB  . ASP   B 1 26  ? 14.299  -9.391  -21.627 1.00 28.16 ? 26  ASP   B CB  1 
ATOM   1993 C  CG  . ASP   B 1 26  ? 13.396  -10.527 -22.098 1.00 30.73 ? 26  ASP   B CG  1 
ATOM   1994 O  OD1 . ASP   B 1 26  ? 12.374  -10.805 -21.427 1.00 28.79 ? 26  ASP   B OD1 1 
ATOM   1995 O  OD2 . ASP   B 1 26  ? 13.741  -11.116 -23.135 1.00 37.22 ? 26  ASP   B OD2 1 
ATOM   1996 N  N   . GLU   B 1 27  ? 14.993  -6.439  -20.612 1.00 20.68 ? 27  GLU   B N   1 
ATOM   1997 C  CA  . GLU   B 1 27  ? 15.980  -5.501  -20.118 1.00 21.60 ? 27  GLU   B CA  1 
ATOM   1998 C  C   . GLU   B 1 27  ? 15.640  -5.037  -18.695 1.00 20.11 ? 27  GLU   B C   1 
ATOM   1999 O  O   . GLU   B 1 27  ? 16.527  -4.945  -17.838 1.00 20.92 ? 27  GLU   B O   1 
ATOM   2000 C  CB  . GLU   B 1 27  ? 16.072  -4.328  -21.091 1.00 25.45 ? 27  GLU   B CB  1 
ATOM   2001 C  CG  . GLU   B 1 27  ? 17.165  -3.355  -20.671 1.00 30.52 ? 27  GLU   B CG  1 
ATOM   2002 C  CD  . GLU   B 1 27  ? 17.315  -2.114  -21.544 1.00 36.23 ? 27  GLU   B CD  1 
ATOM   2003 O  OE1 . GLU   B 1 27  ? 16.636  -1.879  -22.598 1.00 38.15 ? 27  GLU   B OE1 1 
ATOM   2004 O  OE2 . GLU   B 1 27  ? 18.183  -1.355  -21.079 1.00 37.57 ? 27  GLU   B OE2 1 
ATOM   2005 N  N   . LYS   B 1 28  ? 14.364  -4.740  -18.445 1.00 18.50 ? 28  LYS   B N   1 
ATOM   2006 C  CA  . LYS   B 1 28  ? 13.952  -4.288  -17.126 1.00 19.72 ? 28  LYS   B CA  1 
ATOM   2007 C  C   . LYS   B 1 28  ? 14.096  -5.412  -16.097 1.00 17.67 ? 28  LYS   B C   1 
ATOM   2008 O  O   . LYS   B 1 28  ? 14.446  -5.145  -14.951 1.00 16.31 ? 28  LYS   B O   1 
ATOM   2009 C  CB  . LYS   B 1 28  ? 12.492  -3.825  -17.104 1.00 22.05 ? 28  LYS   B CB  1 
ATOM   2010 C  CG  . LYS   B 1 28  ? 12.270  -2.516  -17.823 1.00 26.00 ? 28  LYS   B CG  1 
ATOM   2011 C  CD  . LYS   B 1 28  ? 12.627  -1.309  -16.985 1.00 28.26 ? 28  LYS   B CD  1 
ATOM   2012 C  CE  . LYS   B 1 28  ? 11.614  -1.150  -15.881 1.00 32.33 ? 28  LYS   B CE  1 
ATOM   2013 N  NZ  . LYS   B 1 28  ? 12.019  -0.151  -14.888 1.00 33.50 ? 28  LYS   B NZ  1 
ATOM   2014 N  N   . VAL   B 1 29  ? 13.774  -6.650  -16.503 1.00 16.05 ? 29  VAL   B N   1 
ATOM   2015 C  CA  . VAL   B 1 29  ? 13.861  -7.770  -15.564 1.00 15.85 ? 29  VAL   B CA  1 
ATOM   2016 C  C   . VAL   B 1 29  ? 15.337  -8.029  -15.202 1.00 15.98 ? 29  VAL   B C   1 
ATOM   2017 O  O   . VAL   B 1 29  ? 15.706  -8.268  -14.043 1.00 15.17 ? 29  VAL   B O   1 
ATOM   2018 C  CB  . VAL   B 1 29  ? 13.227  -9.041  -16.166 1.00 16.59 ? 29  VAL   B CB  1 
ATOM   2019 C  CG1 . VAL   B 1 29  ? 13.482  -10.250 -15.285 1.00 16.48 ? 29  VAL   B CG1 1 
ATOM   2020 C  CG2 . VAL   B 1 29  ? 11.745  -8.895  -16.441 1.00 17.92 ? 29  VAL   B CG2 1 
ATOM   2021 N  N   . ILE   B 1 30  ? 16.190  -8.011  -16.224 1.00 15.10 ? 30  ILE   B N   1 
ATOM   2022 C  CA  . ILE   B 1 30  ? 17.605  -8.252  -16.036 1.00 16.64 ? 30  ILE   B CA  1 
ATOM   2023 C  C   . ILE   B 1 30  ? 18.189  -7.179  -15.124 1.00 16.82 ? 30  ILE   B C   1 
ATOM   2024 O  O   . ILE   B 1 30  ? 18.913  -7.508  -14.202 1.00 19.28 ? 30  ILE   B O   1 
ATOM   2025 C  CB  . ILE   B 1 30  ? 18.325  -8.332  -17.401 1.00 17.90 ? 30  ILE   B CB  1 
ATOM   2026 C  CG1 . ILE   B 1 30  ? 17.867  -9.576  -18.161 1.00 18.39 ? 30  ILE   B CG1 1 
ATOM   2027 C  CG2 . ILE   B 1 30  ? 19.844  -8.281  -17.220 1.00 19.36 ? 30  ILE   B CG2 1 
ATOM   2028 C  CD1 . ILE   B 1 30  ? 18.238  -9.543  -19.644 1.00 20.09 ? 30  ILE   B CD1 1 
ATOM   2029 N  N   . ALA   B 1 31  ? 17.812  -5.909  -15.339 1.00 16.52 ? 31  ALA   B N   1 
ATOM   2030 C  CA  . ALA   B 1 31  ? 18.281  -4.810  -14.516 1.00 17.06 ? 31  ALA   B CA  1 
ATOM   2031 C  C   . ALA   B 1 31  ? 17.820  -4.977  -13.066 1.00 16.45 ? 31  ALA   B C   1 
ATOM   2032 O  O   . ALA   B 1 31  ? 18.564  -4.655  -12.140 1.00 16.53 ? 31  ALA   B O   1 
ATOM   2033 C  CB  . ALA   B 1 31  ? 17.786  -3.476  -15.043 1.00 17.77 ? 31  ALA   B CB  1 
ATOM   2034 N  N   . LEU   B 1 32  ? 16.578  -5.428  -12.886 1.00 16.12 ? 32  LEU   B N   1 
ATOM   2035 C  CA  . LEU   B 1 32  ? 16.053  -5.681  -11.555 1.00 14.37 ? 32  LEU   B CA  1 
ATOM   2036 C  C   . LEU   B 1 32  ? 16.922  -6.716  -10.841 1.00 13.96 ? 32  LEU   B C   1 
ATOM   2037 O  O   . LEU   B 1 32  ? 17.235  -6.580  -9.655  1.00 13.57 ? 32  LEU   B O   1 
ATOM   2038 C  CB  . LEU   B 1 32  ? 14.615  -6.190  -11.644 1.00 14.17 ? 32  LEU   B CB  1 
ATOM   2039 C  CG  . LEU   B 1 32  ? 13.968  -6.587  -10.316 1.00 14.33 ? 32  LEU   B CG  1 
ATOM   2040 C  CD1 . LEU   B 1 32  ? 13.845  -5.378  -9.444  1.00 15.41 ? 32  LEU   B CD1 1 
ATOM   2041 C  CD2 . LEU   B 1 32  ? 12.574  -7.200  -10.550 1.00 14.45 ? 32  LEU   B CD2 1 
ATOM   2042 N  N   . CYS   B 1 33  ? 17.220  -7.813  -11.539 1.00 14.05 ? 33  CYS   B N   1 
ATOM   2043 C  CA  . CYS   B 1 33  ? 18.058  -8.845  -10.956 1.00 15.00 ? 33  CYS   B CA  1 
ATOM   2044 C  C   . CYS   B 1 33  ? 19.409  -8.261  -10.537 1.00 15.71 ? 33  CYS   B C   1 
ATOM   2045 O  O   . CYS   B 1 33  ? 19.907  -8.551  -9.454  1.00 14.61 ? 33  CYS   B O   1 
ATOM   2046 C  CB  . CYS   B 1 33  ? 18.296  -9.969  -11.947 1.00 14.76 ? 33  CYS   B CB  1 
ATOM   2047 S  SG  . CYS   B 1 33  ? 16.805  -10.889 -12.343 1.00 17.33 ? 33  CYS   B SG  1 
ATOM   2048 N  N   . HIS   B 1 34  ? 20.020  -7.440  -11.414 1.00 15.59 ? 34  HIS   B N   1 
ATOM   2049 C  CA  . HIS   B 1 34  ? 21.279  -6.793  -11.069 1.00 17.11 ? 34  HIS   B CA  1 
ATOM   2050 C  C   . HIS   B 1 34  ? 21.155  -5.915  -9.822  1.00 16.95 ? 34  HIS   B C   1 
ATOM   2051 O  O   . HIS   B 1 34  ? 22.048  -5.898  -8.983  1.00 16.10 ? 34  HIS   B O   1 
ATOM   2052 C  CB  . HIS   B 1 34  ? 21.794  -5.958  -12.248 1.00 18.49 ? 34  HIS   B CB  1 
ATOM   2053 C  CG  . HIS   B 1 34  ? 22.167  -6.812  -13.403 1.00 20.03 ? 34  HIS   B CG  1 
ATOM   2054 N  ND1 . HIS   B 1 34  ? 22.411  -6.289  -14.655 1.00 23.35 ? 34  HIS   B ND1 1 
ATOM   2055 C  CD2 . HIS   B 1 34  ? 22.313  -8.124  -13.511 1.00 19.71 ? 34  HIS   B CD2 1 
ATOM   2056 C  CE1 . HIS   B 1 34  ? 22.697  -7.289  -15.484 1.00 22.24 ? 34  HIS   B CE1 1 
ATOM   2057 N  NE2 . HIS   B 1 34  ? 22.641  -8.409  -14.827 1.00 22.91 ? 34  HIS   B NE2 1 
ATOM   2058 N  N   . GLN   B 1 35  ? 20.063  -5.169  -9.719  1.00 15.69 ? 35  GLN   B N   1 
ATOM   2059 C  CA  . GLN   B 1 35  ? 19.860  -4.253  -8.619  1.00 16.09 ? 35  GLN   B CA  1 
ATOM   2060 C  C   . GLN   B 1 35  ? 19.722  -4.977  -7.282  1.00 14.48 ? 35  GLN   B C   1 
ATOM   2061 O  O   . GLN   B 1 35  ? 20.074  -4.421  -6.230  1.00 14.31 ? 35  GLN   B O   1 
ATOM   2062 C  CB  . GLN   B 1 35  ? 18.616  -3.459  -8.977  1.00 20.67 ? 35  GLN   B CB  1 
ATOM   2063 C  CG  . GLN   B 1 35  ? 18.268  -2.334  -8.026  1.00 28.42 ? 35  GLN   B CG  1 
ATOM   2064 C  CD  . GLN   B 1 35  ? 17.000  -1.626  -8.470  1.00 40.07 ? 35  GLN   B CD  1 
ATOM   2065 O  OE1 . GLN   B 1 35  ? 16.302  -2.056  -9.403  1.00 46.04 ? 35  GLN   B OE1 1 
ATOM   2066 N  NE2 . GLN   B 1 35  ? 16.688  -0.529  -7.798  1.00 42.27 ? 35  GLN   B NE2 1 
ATOM   2067 N  N   . ALA   B 1 36  ? 19.169  -6.182  -7.328  1.00 12.72 ? 36  ALA   B N   1 
ATOM   2068 C  CA  . ALA   B 1 36  ? 18.935  -6.987  -6.135  1.00 13.11 ? 36  ALA   B CA  1 
ATOM   2069 C  C   . ALA   B 1 36  ? 20.259  -7.450  -5.522  1.00 13.63 ? 36  ALA   B C   1 
ATOM   2070 O  O   . ALA   B 1 36  ? 20.284  -7.808  -4.364  1.00 13.73 ? 36  ALA   B O   1 
ATOM   2071 C  CB  . ALA   B 1 36  ? 18.058  -8.185  -6.465  1.00 13.34 ? 36  ALA   B CB  1 
ATOM   2072 N  N   . LYS   B 1 37  ? 21.329  -7.524  -6.318  1.00 13.84 ? 37  LYS   B N   1 
ATOM   2073 C  CA  . LYS   B 1 37  ? 22.650  -7.897  -5.829  1.00 14.52 ? 37  LYS   B CA  1 
ATOM   2074 C  C   . LYS   B 1 37  ? 23.371  -6.607  -5.460  1.00 14.34 ? 37  LYS   B C   1 
ATOM   2075 O  O   . LYS   B 1 37  ? 24.065  -6.002  -6.280  1.00 15.82 ? 37  LYS   B O   1 
ATOM   2076 C  CB  . LYS   B 1 37  ? 23.364  -8.719  -6.914  1.00 15.80 ? 37  LYS   B CB  1 
ATOM   2077 C  CG  . LYS   B 1 37  ? 24.772  -9.180  -6.536  1.00 16.14 ? 37  LYS   B CG  1 
ATOM   2078 C  CD  . LYS   B 1 37  ? 25.468  -9.806  -7.751  1.00 18.67 ? 37  LYS   B CD  1 
ATOM   2079 C  CE  . LYS   B 1 37  ? 26.789  -10.408 -7.378  1.00 20.57 ? 37  LYS   B CE  1 
ATOM   2080 N  NZ  . LYS   B 1 37  ? 27.411  -10.940 -8.600  1.00 22.19 ? 37  LYS   B NZ  1 
ATOM   2081 N  N   . THR   B 1 38  ? 23.151  -6.143  -4.241  1.00 14.61 ? 38  THR   B N   1 
ATOM   2082 C  CA  . THR   B 1 38  ? 23.612  -4.822  -3.867  1.00 15.40 ? 38  THR   B CA  1 
ATOM   2083 C  C   . THR   B 1 38  ? 25.007  -4.930  -3.256  1.00 15.58 ? 38  THR   B C   1 
ATOM   2084 O  O   . THR   B 1 38  ? 25.440  -6.001  -2.820  1.00 14.73 ? 38  THR   B O   1 
ATOM   2085 C  CB  . THR   B 1 38  ? 22.656  -4.142  -2.874  1.00 15.97 ? 38  THR   B CB  1 
ATOM   2086 O  OG1 . THR   B 1 38  ? 23.081  -4.411  -1.540  1.00 14.50 ? 38  THR   B OG1 1 
ATOM   2087 C  CG2 . THR   B 1 38  ? 21.195  -4.541  -3.031  1.00 16.56 ? 38  THR   B CG2 1 
ATOM   2088 N  N   . PRO   B 1 39  ? 25.704  -3.789  -3.104  1.00 17.69 ? 39  PRO   B N   1 
ATOM   2089 C  CA  . PRO   B 1 39  ? 27.022  -3.804  -2.476  1.00 17.31 ? 39  PRO   B CA  1 
ATOM   2090 C  C   . PRO   B 1 39  ? 27.085  -4.285  -1.038  1.00 16.80 ? 39  PRO   B C   1 
ATOM   2091 O  O   . PRO   B 1 39  ? 28.176  -4.590  -0.558  1.00 17.05 ? 39  PRO   B O   1 
ATOM   2092 C  CB  . PRO   B 1 39  ? 27.497  -2.338  -2.612  1.00 19.80 ? 39  PRO   B CB  1 
ATOM   2093 C  CG  . PRO   B 1 39  ? 26.676  -1.776  -3.747  1.00 19.95 ? 39  PRO   B CG  1 
ATOM   2094 C  CD  . PRO   B 1 39  ? 25.334  -2.467  -3.644  1.00 18.26 ? 39  PRO   B CD  1 
ATOM   2095 N  N   . VAL   B 1 40  ? 25.936  -4.302  -0.331  1.00 15.23 ? 40  VAL   B N   1 
ATOM   2096 C  CA  . VAL   B 1 40  ? 25.915  -4.650  1.064   1.00 15.69 ? 40  VAL   B CA  1 
ATOM   2097 C  C   . VAL   B 1 40  ? 25.151  -5.945  1.286   1.00 14.79 ? 40  VAL   B C   1 
ATOM   2098 O  O   . VAL   B 1 40  ? 24.988  -6.357  2.436   1.00 15.57 ? 40  VAL   B O   1 
ATOM   2099 C  CB  . VAL   B 1 40  ? 25.319  -3.510  1.917   1.00 17.86 ? 40  VAL   B CB  1 
ATOM   2100 C  CG1 . VAL   B 1 40  ? 26.124  -2.239  1.758   1.00 19.74 ? 40  VAL   B CG1 1 
ATOM   2101 C  CG2 . VAL   B 1 40  ? 23.835  -3.274  1.602   1.00 19.59 ? 40  VAL   B CG2 1 
ATOM   2102 N  N   . GLY   B 1 41  ? 24.758  -6.624  0.210   1.00 14.60 ? 41  GLY   B N   1 
ATOM   2103 C  CA  . GLY   B 1 41  ? 24.054  -7.891  0.325   1.00 14.61 ? 41  GLY   B CA  1 
ATOM   2104 C  C   . GLY   B 1 41  ? 22.914  -7.975  -0.686  1.00 13.38 ? 41  GLY   B C   1 
ATOM   2105 O  O   . GLY   B 1 41  ? 22.643  -7.032  -1.422  1.00 13.57 ? 41  GLY   B O   1 
ATOM   2106 N  N   . ASN   B 1 42  ? 22.304  -9.148  -0.715  1.00 13.88 ? 42  ASN   B N   1 
ATOM   2107 C  CA  . ASN   B 1 42  ? 21.222  -9.434  -1.636  1.00 14.18 ? 42  ASN   B CA  1 
ATOM   2108 C  C   . ASN   B 1 42  ? 19.899  -9.134  -0.951  1.00 12.45 ? 42  ASN   B C   1 
ATOM   2109 O  O   . ASN   B 1 42  ? 19.739  -9.357  0.248   1.00 12.84 ? 42  ASN   B O   1 
ATOM   2110 C  CB  . ASN   B 1 42  ? 21.243  -10.887 -2.085  1.00 13.70 ? 42  ASN   B CB  1 
ATOM   2111 C  CG  . ASN   B 1 42  ? 22.512  -11.226 -2.855  1.00 16.21 ? 42  ASN   B CG  1 
ATOM   2112 O  OD1 . ASN   B 1 42  ? 23.127  -10.352 -3.469  1.00 16.74 ? 42  ASN   B OD1 1 
ATOM   2113 N  ND2 . ASN   B 1 42  ? 22.901  -12.484 -2.861  1.00 16.40 ? 42  ASN   B ND2 1 
ATOM   2114 N  N   . THR   B 1 43  ? 18.920  -8.665  -1.740  1.00 12.25 ? 43  THR   B N   1 
ATOM   2115 C  CA  . THR   B 1 43  ? 17.552  -8.619  -1.250  1.00 11.90 ? 43  THR   B CA  1 
ATOM   2116 C  C   . THR   B 1 43  ? 17.083  -10.062 -1.044  1.00 11.27 ? 43  THR   B C   1 
ATOM   2117 O  O   . THR   B 1 43  ? 17.710  -10.996 -1.551  1.00 11.53 ? 43  THR   B O   1 
ATOM   2118 C  CB  . THR   B 1 43  ? 16.656  -7.821  -2.200  1.00 12.34 ? 43  THR   B CB  1 
ATOM   2119 O  OG1 . THR   B 1 43  ? 16.593  -8.476  -3.466  1.00 11.98 ? 43  THR   B OG1 1 
ATOM   2120 C  CG2 . THR   B 1 43  ? 17.136  -6.382  -2.367  1.00 12.80 ? 43  THR   B CG2 1 
ATOM   2121 N  N   . ALA   B 1 44  ? 15.960  -10.237 -0.337  1.00 10.83 ? 44  ALA   B N   1 
ATOM   2122 C  CA  . ALA   B 1 44  ? 15.411  -11.569 -0.108  1.00 11.26 ? 44  ALA   B CA  1 
ATOM   2123 C  C   . ALA   B 1 44  ? 14.918  -12.175 -1.415  1.00 10.99 ? 44  ALA   B C   1 
ATOM   2124 O  O   . ALA   B 1 44  ? 15.022  -13.389 -1.644  1.00 10.75 ? 44  ALA   B O   1 
ATOM   2125 C  CB  . ALA   B 1 44  ? 14.297  -11.501 0.924   1.00 11.51 ? 44  ALA   B CB  1 
ATOM   2126 N  N   . ALA   B 1 45  ? 14.294  -11.317 -2.239  1.00 10.91 ? 45  ALA   B N   1 
ATOM   2127 C  CA  . ALA   B 1 45  ? 13.586  -11.761 -3.424  1.00 10.65 ? 45  ALA   B CA  1 
ATOM   2128 C  C   . ALA   B 1 45  ? 13.575  -10.635 -4.445  1.00 11.40 ? 45  ALA   B C   1 
ATOM   2129 O  O   . ALA   B 1 45  ? 13.856  -9.480  -4.133  1.00 10.52 ? 45  ALA   B O   1 
ATOM   2130 C  CB  . ALA   B 1 45  ? 12.164  -12.180 -3.082  1.00 10.72 ? 45  ALA   B CB  1 
ATOM   2131 N  N   . ILE   B 1 46  ? 13.223  -11.015 -5.659  1.00 12.09 ? 46  ILE   B N   1 
ATOM   2132 C  CA  . ILE   B 1 46  ? 12.717  -10.075 -6.644  1.00 12.95 ? 46  ILE   B CA  1 
ATOM   2133 C  C   . ILE   B 1 46  ? 11.281  -10.494 -6.933  1.00 12.62 ? 46  ILE   B C   1 
ATOM   2134 O  O   . ILE   B 1 46  ? 10.915  -11.652 -6.739  1.00 12.94 ? 46  ILE   B O   1 
ATOM   2135 C  CB  . ILE   B 1 46  ? 13.576  -10.080 -7.914  1.00 14.33 ? 46  ILE   B CB  1 
ATOM   2136 C  CG1 . ILE   B 1 46  ? 13.661  -11.459 -8.518  1.00 15.97 ? 46  ILE   B CG1 1 
ATOM   2137 C  CG2 . ILE   B 1 46  ? 14.963  -9.511  -7.617  1.00 14.60 ? 46  ILE   B CG2 1 
ATOM   2138 C  CD1 . ILE   B 1 46  ? 14.338  -11.492 -9.865  1.00 19.23 ? 46  ILE   B CD1 1 
ATOM   2139 N  N   . SER   B 1 47  ? 10.504  -9.507  -7.355  1.00 12.36 ? 47  SER   B N   1 
ATOM   2140 C  CA  A SER   B 1 47  ? 9.090   -9.673  -7.642  0.50 12.11 ? 47  SER   B CA  1 
ATOM   2141 C  CA  B SER   B 1 47  ? 9.094   -9.689  -7.639  0.50 13.54 ? 47  SER   B CA  1 
ATOM   2142 C  C   . SER   B 1 47  ? 8.846   -9.261  -9.081  1.00 11.85 ? 47  SER   B C   1 
ATOM   2143 O  O   . SER   B 1 47  ? 9.147   -8.130  -9.441  1.00 12.37 ? 47  SER   B O   1 
ATOM   2144 C  CB  A SER   B 1 47  ? 8.252   -8.834  -6.717  0.50 12.36 ? 47  SER   B CB  1 
ATOM   2145 C  CB  B SER   B 1 47  ? 8.269   -8.898  -6.643  0.50 15.85 ? 47  SER   B CB  1 
ATOM   2146 O  OG  A SER   B 1 47  ? 8.208   -9.398  -5.424  0.50 11.58 ? 47  SER   B OG  1 
ATOM   2147 O  OG  B SER   B 1 47  ? 6.900   -9.274  -6.689  0.50 19.69 ? 47  SER   B OG  1 
ATOM   2148 N  N   . VAL   B 1 48  ? 8.305   -10.201 -9.879  1.00 11.86 ? 48  VAL   B N   1 
ATOM   2149 C  CA  . VAL   B 1 48  ? 8.109   -9.987  -11.302 1.00 12.71 ? 48  VAL   B CA  1 
ATOM   2150 C  C   . VAL   B 1 48  ? 6.772   -10.592 -11.688 1.00 12.49 ? 48  VAL   B C   1 
ATOM   2151 O  O   . VAL   B 1 48  ? 6.223   -11.411 -10.961 1.00 12.14 ? 48  VAL   B O   1 
ATOM   2152 C  CB  . VAL   B 1 48  ? 9.238   -10.592 -12.160 1.00 13.24 ? 48  VAL   B CB  1 
ATOM   2153 C  CG1 . VAL   B 1 48  ? 10.566  -9.928  -11.884 1.00 13.70 ? 48  VAL   B CG1 1 
ATOM   2154 C  CG2 . VAL   B 1 48  ? 9.332   -12.099 -11.986 1.00 13.64 ? 48  VAL   B CG2 1 
ATOM   2155 N  N   . TYR   B 1 49  ? 6.303   -10.256 -12.888 1.00 12.37 ? 49  TYR   B N   1 
ATOM   2156 C  CA  . TYR   B 1 49  ? 5.118   -10.909 -13.428 1.00 12.94 ? 49  TYR   B CA  1 
ATOM   2157 C  C   . TYR   B 1 49  ? 5.476   -12.331 -13.840 1.00 12.51 ? 49  TYR   B C   1 
ATOM   2158 O  O   . TYR   B 1 49  ? 6.621   -12.652 -14.126 1.00 12.31 ? 49  TYR   B O   1 
ATOM   2159 C  CB  . TYR   B 1 49  ? 4.572   -10.153 -14.644 1.00 15.39 ? 49  TYR   B CB  1 
ATOM   2160 C  CG  . TYR   B 1 49  ? 3.877   -8.848  -14.306 1.00 17.58 ? 49  TYR   B CG  1 
ATOM   2161 C  CD1 . TYR   B 1 49  ? 2.831   -8.834  -13.413 1.00 20.39 ? 49  TYR   B CD1 1 
ATOM   2162 C  CD2 . TYR   B 1 49  ? 4.304   -7.628  -14.823 1.00 22.43 ? 49  TYR   B CD2 1 
ATOM   2163 C  CE1 . TYR   B 1 49  ? 2.162   -7.661  -13.092 1.00 23.99 ? 49  TYR   B CE1 1 
ATOM   2164 C  CE2 . TYR   B 1 49  ? 3.683   -6.433  -14.464 1.00 25.40 ? 49  TYR   B CE2 1 
ATOM   2165 C  CZ  . TYR   B 1 49  ? 2.595   -6.454  -13.607 1.00 29.08 ? 49  TYR   B CZ  1 
ATOM   2166 O  OH  . TYR   B 1 49  ? 1.898   -5.328  -13.226 1.00 33.28 ? 49  TYR   B OH  1 
ATOM   2167 N  N   . PRO   B 1 50  ? 4.502   -13.261 -13.827 1.00 13.02 ? 50  PRO   B N   1 
ATOM   2168 C  CA  . PRO   B 1 50  ? 4.825   -14.671 -14.046 1.00 12.73 ? 50  PRO   B CA  1 
ATOM   2169 C  C   . PRO   B 1 50  ? 5.644   -14.941 -15.301 1.00 12.58 ? 50  PRO   B C   1 
ATOM   2170 O  O   . PRO   B 1 50  ? 6.574   -15.732 -15.270 1.00 12.05 ? 50  PRO   B O   1 
ATOM   2171 C  CB  . PRO   B 1 50  ? 3.410   -15.305 -14.093 1.00 12.87 ? 50  PRO   B CB  1 
ATOM   2172 C  CG  . PRO   B 1 50  ? 2.615   -14.448 -13.127 1.00 11.89 ? 50  PRO   B CG  1 
ATOM   2173 C  CD  . PRO   B 1 50  ? 3.091   -13.040 -13.461 1.00 11.87 ? 50  PRO   B CD  1 
ATOM   2174 N  N   . ARG   B 1 51  ? 5.303   -14.276 -16.404 1.00 12.68 ? 51  ARG   B N   1 
ATOM   2175 C  CA  . ARG   B 1 51  ? 5.978   -14.549 -17.664 1.00 14.39 ? 51  ARG   B CA  1 
ATOM   2176 C  C   . ARG   B 1 51  ? 7.475   -14.204 -17.630 1.00 14.37 ? 51  ARG   B C   1 
ATOM   2177 O  O   . ARG   B 1 51  ? 8.222   -14.665 -18.495 1.00 12.80 ? 51  ARG   B O   1 
ATOM   2178 C  CB  . ARG   B 1 51  ? 5.314   -13.765 -18.806 1.00 16.66 ? 51  ARG   B CB  1 
ATOM   2179 C  CG  . ARG   B 1 51  ? 5.354   -12.255 -18.640 1.00 20.32 ? 51  ARG   B CG  1 
ATOM   2180 C  CD  . ARG   B 1 51  ? 4.674   -11.560 -19.818 1.00 27.63 ? 51  ARG   B CD  1 
ATOM   2181 N  NE  . ARG   B 1 51  ? 4.485   -10.146 -19.534 1.00 34.34 ? 51  ARG   B NE  1 
ATOM   2182 C  CZ  . ARG   B 1 51  ? 3.535   -9.610  -18.762 1.00 46.32 ? 51  ARG   B CZ  1 
ATOM   2183 N  NH1 . ARG   B 1 51  ? 2.532   -10.335 -18.271 1.00 44.79 ? 51  ARG   B NH1 1 
ATOM   2184 N  NH2 . ARG   B 1 51  ? 3.587   -8.309  -18.513 1.00 51.91 ? 51  ARG   B NH2 1 
ATOM   2185 N  N   . SER   B 1 52  ? 7.915   -13.414 -16.638 1.00 12.87 ? 52  SER   B N   1 
ATOM   2186 C  CA  . SER   B 1 52  ? 9.277   -12.945 -16.506 1.00 12.78 ? 52  SER   B CA  1 
ATOM   2187 C  C   . SER   B 1 52  ? 10.115  -13.893 -15.661 1.00 11.83 ? 52  SER   B C   1 
ATOM   2188 O  O   . SER   B 1 52  ? 11.327  -13.707 -15.553 1.00 11.95 ? 52  SER   B O   1 
ATOM   2189 C  CB  . SER   B 1 52  ? 9.289   -11.567 -15.852 1.00 13.42 ? 52  SER   B CB  1 
ATOM   2190 O  OG  . SER   B 1 52  ? 8.640   -10.639 -16.698 1.00 15.79 ? 52  SER   B OG  1 
ATOM   2191 N  N   . ILE   B 1 53  ? 9.485   -14.911 -15.066 1.00 11.90 ? 53  ILE   B N   1 
ATOM   2192 C  CA  . ILE   B 1 53  ? 10.192  -15.757 -14.135 1.00 11.78 ? 53  ILE   B CA  1 
ATOM   2193 C  C   . ILE   B 1 53  ? 11.349  -16.476 -14.825 1.00 12.34 ? 53  ILE   B C   1 
ATOM   2194 O  O   . ILE   B 1 53  ? 12.450  -16.520 -14.281 1.00 11.80 ? 53  ILE   B O   1 
ATOM   2195 C  CB  . ILE   B 1 53  ? 9.235   -16.688 -13.383 1.00 11.79 ? 53  ILE   B CB  1 
ATOM   2196 C  CG1 . ILE   B 1 53  ? 8.319   -15.882 -12.437 1.00 12.07 ? 53  ILE   B CG1 1 
ATOM   2197 C  CG2 . ILE   B 1 53  ? 9.992   -17.735 -12.590 1.00 12.20 ? 53  ILE   B CG2 1 
ATOM   2198 C  CD1 . ILE   B 1 53  ? 7.151   -16.686 -11.882 1.00 12.14 ? 53  ILE   B CD1 1 
ATOM   2199 N  N   . PRO   B 1 54  ? 11.168  -17.109 -16.006 1.00 13.06 ? 54  PRO   B N   1 
ATOM   2200 C  CA  . PRO   B 1 54  ? 12.291  -17.847 -16.594 1.00 13.68 ? 54  PRO   B CA  1 
ATOM   2201 C  C   . PRO   B 1 54  ? 13.539  -17.019 -16.878 1.00 13.03 ? 54  PRO   B C   1 
ATOM   2202 O  O   . PRO   B 1 54  ? 14.664  -17.422 -16.516 1.00 14.53 ? 54  PRO   B O   1 
ATOM   2203 C  CB  . PRO   B 1 54  ? 11.666  -18.436 -17.858 1.00 14.02 ? 54  PRO   B CB  1 
ATOM   2204 C  CG  . PRO   B 1 54  ? 10.204  -18.569 -17.494 1.00 14.00 ? 54  PRO   B CG  1 
ATOM   2205 C  CD  . PRO   B 1 54  ? 9.890   -17.311 -16.715 1.00 12.98 ? 54  PRO   B CD  1 
ATOM   2206 N  N   . ILE   B 1 55  ? 13.366  -15.828 -17.451 1.00 13.15 ? 55  ILE   B N   1 
ATOM   2207 C  CA  . ILE   B 1 55  ? 14.532  -14.997 -17.724 1.00 14.47 ? 55  ILE   B CA  1 
ATOM   2208 C  C   . ILE   B 1 55  ? 15.130  -14.433 -16.441 1.00 13.40 ? 55  ILE   B C   1 
ATOM   2209 O  O   . ILE   B 1 55  ? 16.338  -14.291 -16.345 1.00 14.58 ? 55  ILE   B O   1 
ATOM   2210 C  CB  . ILE   B 1 55  ? 14.269  -13.888 -18.757 1.00 17.73 ? 55  ILE   B CB  1 
ATOM   2211 C  CG1 . ILE   B 1 55  ? 15.580  -13.387 -19.343 1.00 21.43 ? 55  ILE   B CG1 1 
ATOM   2212 C  CG2 . ILE   B 1 55  ? 13.437  -12.749 -18.167 1.00 18.14 ? 55  ILE   B CG2 1 
ATOM   2213 C  CD1 . ILE   B 1 55  ? 16.191  -14.357 -20.328 1.00 25.27 ? 55  ILE   B CD1 1 
ATOM   2214 N  N   . ALA   B 1 56  ? 14.304  -14.180 -15.437 1.00 12.61 ? 56  ALA   B N   1 
ATOM   2215 C  CA  . ALA   B 1 56  ? 14.834  -13.754 -14.147 1.00 12.87 ? 56  ALA   B CA  1 
ATOM   2216 C  C   . ALA   B 1 56  ? 15.689  -14.859 -13.516 1.00 12.26 ? 56  ALA   B C   1 
ATOM   2217 O  O   . ALA   B 1 56  ? 16.753  -14.585 -12.983 1.00 12.74 ? 56  ALA   B O   1 
ATOM   2218 C  CB  . ALA   B 1 56  ? 13.704  -13.369 -13.206 1.00 13.02 ? 56  ALA   B CB  1 
ATOM   2219 N  N   . ARG   B 1 57  ? 15.231  -16.109 -13.568 1.00 12.18 ? 57  ARG   B N   1 
ATOM   2220 C  CA  . ARG   B 1 57  ? 15.958  -17.207 -12.970 1.00 13.39 ? 57  ARG   B CA  1 
ATOM   2221 C  C   . ARG   B 1 57  ? 17.310  -17.367 -13.674 1.00 14.16 ? 57  ARG   B C   1 
ATOM   2222 O  O   . ARG   B 1 57  ? 18.341  -17.564 -13.034 1.00 13.87 ? 57  ARG   B O   1 
ATOM   2223 C  CB  . ARG   B 1 57  ? 15.178  -18.512 -13.065 1.00 14.14 ? 57  ARG   B CB  1 
ATOM   2224 C  CG  . ARG   B 1 57  ? 15.878  -19.695 -12.423 1.00 16.29 ? 57  ARG   B CG  1 
ATOM   2225 C  CD  . ARG   B 1 57  ? 15.857  -19.643 -10.916 1.00 18.39 ? 57  ARG   B CD  1 
ATOM   2226 N  NE  . ARG   B 1 57  ? 14.498  -19.964 -10.461 1.00 18.01 ? 57  ARG   B NE  1 
ATOM   2227 C  CZ  . ARG   B 1 57  ? 14.032  -19.754 -9.243  1.00 18.00 ? 57  ARG   B CZ  1 
ATOM   2228 N  NH1 . ARG   B 1 57  ? 14.777  -19.145 -8.332  1.00 17.20 ? 57  ARG   B NH1 1 
ATOM   2229 N  NH2 . ARG   B 1 57  ? 12.788  -20.085 -8.956  1.00 17.19 ? 57  ARG   B NH2 1 
ATOM   2230 N  N   . LYS   B 1 58  ? 17.295  -17.279 -14.997 1.00 14.09 ? 58  LYS   B N   1 
ATOM   2231 C  CA  . LYS   B 1 58  ? 18.535  -17.394 -15.752 1.00 15.78 ? 58  LYS   B CA  1 
ATOM   2232 C  C   . LYS   B 1 58  ? 19.520  -16.309 -15.319 1.00 16.08 ? 58  LYS   B C   1 
ATOM   2233 O  O   . LYS   B 1 58  ? 20.698  -16.608 -15.087 1.00 16.90 ? 58  LYS   B O   1 
ATOM   2234 C  CB  . LYS   B 1 58  ? 18.239  -17.322 -17.253 1.00 16.39 ? 58  LYS   B CB  1 
ATOM   2235 C  CG  . LYS   B 1 58  ? 19.446  -17.574 -18.143 1.00 18.45 ? 58  LYS   B CG  1 
ATOM   2236 C  CD  . LYS   B 1 58  ? 19.051  -17.649 -19.614 1.00 19.62 ? 58  LYS   B CD  1 
ATOM   2237 C  CE  . LYS   B 1 58  ? 20.175  -17.942 -20.566 1.00 23.73 ? 58  LYS   B CE  1 
ATOM   2238 N  NZ  . LYS   B 1 58  ? 19.579  -18.219 -21.897 1.00 24.73 ? 58  LYS   B NZ  1 
ATOM   2239 N  N   . THR   B 1 59  ? 19.017  -15.075 -15.168 1.00 14.57 ? 59  THR   B N   1 
ATOM   2240 C  CA  . THR   B 1 59  ? 19.850  -13.950 -14.831 1.00 14.63 ? 59  THR   B CA  1 
ATOM   2241 C  C   . THR   B 1 59  ? 20.410  -14.117 -13.418 1.00 14.62 ? 59  THR   B C   1 
ATOM   2242 O  O   . THR   B 1 59  ? 21.598  -13.866 -13.178 1.00 13.80 ? 59  THR   B O   1 
ATOM   2243 C  CB  . THR   B 1 59  ? 19.085  -12.640 -15.006 1.00 14.59 ? 59  THR   B CB  1 
ATOM   2244 O  OG1 . THR   B 1 59  ? 18.552  -12.607 -16.333 1.00 15.07 ? 59  THR   B OG1 1 
ATOM   2245 C  CG2 . THR   B 1 59  ? 19.982  -11.432 -14.830 1.00 15.19 ? 59  THR   B CG2 1 
ATOM   2246 N  N   . LEU   B 1 60  ? 19.554  -14.467 -12.449 1.00 14.21 ? 60  LEU   B N   1 
ATOM   2247 C  CA  . LEU   B 1 60  ? 20.041  -14.676 -11.093 1.00 14.70 ? 60  LEU   B CA  1 
ATOM   2248 C  C   . LEU   B 1 60  ? 21.135  -15.753 -11.030 1.00 15.67 ? 60  LEU   B C   1 
ATOM   2249 O  O   . LEU   B 1 60  ? 22.113  -15.602 -10.287 1.00 15.94 ? 60  LEU   B O   1 
ATOM   2250 C  CB  . LEU   B 1 60  ? 18.872  -15.020 -10.181 1.00 14.16 ? 60  LEU   B CB  1 
ATOM   2251 C  CG  . LEU   B 1 60  ? 17.842  -13.901 -9.986  1.00 14.24 ? 60  LEU   B CG  1 
ATOM   2252 C  CD1 . LEU   B 1 60  ? 16.657  -14.426 -9.222  1.00 13.59 ? 60  LEU   B CD1 1 
ATOM   2253 C  CD2 . LEU   B 1 60  ? 18.447  -12.733 -9.245  1.00 14.19 ? 60  LEU   B CD2 1 
ATOM   2254 N  N   . LYS   B 1 61  ? 20.952  -16.855 -11.757 1.00 16.19 ? 61  LYS   B N   1 
ATOM   2255 C  CA  . LYS   B 1 61  ? 21.960  -17.901 -11.824 1.00 18.73 ? 61  LYS   B CA  1 
ATOM   2256 C  C   . LYS   B 1 61  ? 23.258  -17.366 -12.428 1.00 19.18 ? 61  LYS   B C   1 
ATOM   2257 O  O   . LYS   B 1 61  ? 24.335  -17.577 -11.864 1.00 19.83 ? 61  LYS   B O   1 
ATOM   2258 C  CB  . LYS   B 1 61  ? 21.457  -19.123 -12.596 1.00 21.91 ? 61  LYS   B CB  1 
ATOM   2259 C  CG  . LYS   B 1 61  ? 20.371  -19.925 -11.858 1.00 28.27 ? 61  LYS   B CG  1 
ATOM   2260 C  CD  . LYS   B 1 61  ? 19.826  -21.059 -12.725 1.00 34.97 ? 61  LYS   B CD  1 
ATOM   2261 C  CE  . LYS   B 1 61  ? 18.784  -21.857 -12.023 1.00 41.76 ? 61  LYS   B CE  1 
ATOM   2262 N  NZ  . LYS   B 1 61  ? 18.047  -22.717 -12.961 1.00 44.32 ? 61  LYS   B NZ  1 
ATOM   2263 N  N   . GLU   B 1 62  ? 23.157  -16.642 -13.541 1.00 18.86 ? 62  GLU   B N   1 
ATOM   2264 C  CA  . GLU   B 1 62  ? 24.337  -16.162 -14.253 1.00 22.90 ? 62  GLU   B CA  1 
ATOM   2265 C  C   . GLU   B 1 62  ? 25.151  -15.181 -13.414 1.00 21.08 ? 62  GLU   B C   1 
ATOM   2266 O  O   . GLU   B 1 62  ? 26.372  -15.164 -13.515 1.00 20.19 ? 62  GLU   B O   1 
ATOM   2267 C  CB  . GLU   B 1 62  ? 24.041  -15.513 -15.600 1.00 25.71 ? 62  GLU   B CB  1 
ATOM   2268 C  CG  . GLU   B 1 62  ? 23.689  -16.573 -16.640 1.00 33.20 ? 62  GLU   B CG  1 
ATOM   2269 C  CD  . GLU   B 1 62  ? 23.498  -16.069 -18.057 1.00 37.95 ? 62  GLU   B CD  1 
ATOM   2270 O  OE1 . GLU   B 1 62  ? 23.811  -14.890 -18.339 1.00 43.99 ? 62  GLU   B OE1 1 
ATOM   2271 O  OE2 . GLU   B 1 62  ? 23.033  -16.882 -18.876 1.00 43.52 ? 62  GLU   B OE2 1 
ATOM   2272 N  N   . GLN   B 1 63  ? 24.509  -14.370 -12.576 1.00 16.85 ? 63  GLN   B N   1 
ATOM   2273 C  CA  . GLN   B 1 63  ? 25.244  -13.420 -11.754 1.00 18.14 ? 63  GLN   B CA  1 
ATOM   2274 C  C   . GLN   B 1 63  ? 25.650  -14.013 -10.401 1.00 18.31 ? 63  GLN   B C   1 
ATOM   2275 O  O   . GLN   B 1 63  ? 26.153  -13.291 -9.553  1.00 19.48 ? 63  GLN   B O   1 
ATOM   2276 C  CB  . GLN   B 1 63  ? 24.432  -12.145 -11.577 1.00 17.90 ? 63  GLN   B CB  1 
ATOM   2277 C  CG  . GLN   B 1 63  ? 23.209  -12.315 -10.683 1.00 17.59 ? 63  GLN   B CG  1 
ATOM   2278 C  CD  . GLN   B 1 63  ? 22.492  -11.005 -10.466 1.00 17.96 ? 63  GLN   B CD  1 
ATOM   2279 O  OE1 . GLN   B 1 63  ? 22.712  -10.022 -11.178 1.00 20.65 ? 63  GLN   B OE1 1 
ATOM   2280 N  NE2 . GLN   B 1 63  ? 21.656  -10.953 -9.446  1.00 16.71 ? 63  GLN   B NE2 1 
ATOM   2281 N  N   . GLY   B 1 64  ? 25.431  -15.302 -10.186 1.00 18.62 ? 64  GLY   B N   1 
ATOM   2282 C  CA  . GLY   B 1 64  ? 25.910  -15.970 -8.990  1.00 19.84 ? 64  GLY   B CA  1 
ATOM   2283 C  C   . GLY   B 1 64  ? 25.059  -15.675 -7.757  1.00 20.12 ? 64  GLY   B C   1 
ATOM   2284 O  O   . GLY   B 1 64  ? 25.572  -15.780 -6.653  1.00 20.35 ? 64  GLY   B O   1 
ATOM   2285 N  N   . THR   B 1 65  ? 23.762  -15.354 -7.926  1.00 17.25 ? 65  THR   B N   1 
ATOM   2286 C  CA  . THR   B 1 65  ? 22.869  -15.151 -6.789  1.00 16.40 ? 65  THR   B CA  1 
ATOM   2287 C  C   . THR   B 1 65  ? 21.642  -16.055 -6.916  1.00 17.38 ? 65  THR   B C   1 
ATOM   2288 O  O   . THR   B 1 65  ? 20.499  -15.592 -6.888  1.00 15.19 ? 65  THR   B O   1 
ATOM   2289 C  CB  . THR   B 1 65  ? 22.469  -13.690 -6.646  1.00 16.09 ? 65  THR   B CB  1 
ATOM   2290 O  OG1 . THR   B 1 65  ? 21.691  -13.371 -7.804  1.00 16.44 ? 65  THR   B OG1 1 
ATOM   2291 C  CG2 . THR   B 1 65  ? 23.670  -12.781 -6.444  1.00 17.53 ? 65  THR   B CG2 1 
ATOM   2292 N  N   . PRO   B 1 66  ? 21.838  -17.392 -6.985  1.00 20.10 ? 66  PRO   B N   1 
ATOM   2293 C  CA  . PRO   B 1 66  ? 20.735  -18.341 -7.122  1.00 20.83 ? 66  PRO   B CA  1 
ATOM   2294 C  C   . PRO   B 1 66  ? 19.806  -18.451 -5.918  1.00 22.24 ? 66  PRO   B C   1 
ATOM   2295 O  O   . PRO   B 1 66  ? 18.718  -18.996 -6.036  1.00 21.98 ? 66  PRO   B O   1 
ATOM   2296 C  CB  . PRO   B 1 66  ? 21.465  -19.662 -7.390  1.00 23.23 ? 66  PRO   B CB  1 
ATOM   2297 C  CG  . PRO   B 1 66  ? 22.762  -19.514 -6.642  1.00 22.18 ? 66  PRO   B CG  1 
ATOM   2298 C  CD  . PRO   B 1 66  ? 23.153  -18.074 -6.915  1.00 22.24 ? 66  PRO   B CD  1 
ATOM   2299 N  N   . GLU   B 1 67  ? 20.230  -17.916 -4.771  1.00 19.86 ? 67  GLU   B N   1 
ATOM   2300 C  CA  . GLU   B 1 67  ? 19.441  -17.970 -3.560  1.00 21.70 ? 67  GLU   B CA  1 
ATOM   2301 C  C   . GLU   B 1 67  ? 18.486  -16.789 -3.449  1.00 18.68 ? 67  GLU   B C   1 
ATOM   2302 O  O   . GLU   B 1 67  ? 17.666  -16.780 -2.531  1.00 17.58 ? 67  GLU   B O   1 
ATOM   2303 C  CB  . GLU   B 1 67  ? 20.345  -18.120 -2.330  1.00 27.20 ? 67  GLU   B CB  1 
ATOM   2304 C  CG  . GLU   B 1 67  ? 21.086  -19.460 -2.390  1.00 35.09 ? 67  GLU   B CG  1 
ATOM   2305 C  CD  . GLU   B 1 67  ? 21.807  -19.975 -1.149  1.00 45.13 ? 67  GLU   B CD  1 
ATOM   2306 O  OE1 . GLU   B 1 67  ? 21.550  -19.499 -0.025  1.00 51.24 ? 67  GLU   B OE1 1 
ATOM   2307 O  OE2 . GLU   B 1 67  ? 22.651  -20.882 -1.347  1.00 58.11 ? 67  GLU   B OE2 1 
ATOM   2308 N  N   . ILE   B 1 68  ? 18.587  -15.779 -4.324  1.00 14.85 ? 68  ILE   B N   1 
ATOM   2309 C  CA  . ILE   B 1 68  ? 17.567  -14.735 -4.333  1.00 13.62 ? 68  ILE   B CA  1 
ATOM   2310 C  C   . ILE   B 1 68  ? 16.270  -15.377 -4.837  1.00 13.14 ? 68  ILE   B C   1 
ATOM   2311 O  O   . ILE   B 1 68  ? 16.268  -15.990 -5.902  1.00 13.14 ? 68  ILE   B O   1 
ATOM   2312 C  CB  . ILE   B 1 68  ? 17.990  -13.539 -5.202  1.00 13.32 ? 68  ILE   B CB  1 
ATOM   2313 C  CG1 . ILE   B 1 68  ? 19.248  -12.841 -4.634  1.00 12.54 ? 68  ILE   B CG1 1 
ATOM   2314 C  CG2 . ILE   B 1 68  ? 16.832  -12.559 -5.385  1.00 14.03 ? 68  ILE   B CG2 1 
ATOM   2315 C  CD1 . ILE   B 1 68  ? 19.689  -11.617 -5.414  1.00 12.93 ? 68  ILE   B CD1 1 
ATOM   2316 N  N   . ARG   B 1 69  ? 15.182  -15.218 -4.083  1.00 12.70 ? 69  ARG   B N   1 
ATOM   2317 C  CA  . ARG   B 1 69  ? 13.925  -15.868 -4.405  1.00 13.90 ? 69  ARG   B CA  1 
ATOM   2318 C  C   . ARG   B 1 69  ? 13.226  -15.095 -5.514  1.00 12.69 ? 69  ARG   B C   1 
ATOM   2319 O  O   . ARG   B 1 69  ? 13.398  -13.886 -5.644  1.00 12.43 ? 69  ARG   B O   1 
ATOM   2320 C  CB  . ARG   B 1 69  ? 13.035  -15.978 -3.163  1.00 15.75 ? 69  ARG   B CB  1 
ATOM   2321 C  CG  . ARG   B 1 69  ? 13.680  -16.705 -1.977  1.00 19.48 ? 69  ARG   B CG  1 
ATOM   2322 C  CD  . ARG   B 1 69  ? 13.074  -16.117 -0.700  1.00 26.22 ? 69  ARG   B CD  1 
ATOM   2323 N  NE  . ARG   B 1 69  ? 13.594  -16.565 0.596   1.00 32.84 ? 69  ARG   B NE  1 
ATOM   2324 C  CZ  . ARG   B 1 69  ? 14.718  -16.134 1.173   1.00 35.03 ? 69  ARG   B CZ  1 
ATOM   2325 N  NH1 . ARG   B 1 69  ? 15.412  -15.132 0.653   1.00 33.15 ? 69  ARG   B NH1 1 
ATOM   2326 N  NH2 . ARG   B 1 69  ? 15.128  -16.700 2.296   1.00 36.37 ? 69  ARG   B NH2 1 
ATOM   2327 N  N   . ILE   B 1 70  ? 12.425  -15.817 -6.301  1.00 11.32 ? 70  ILE   B N   1 
ATOM   2328 C  CA  . ILE   B 1 70  ? 11.585  -15.175 -7.288  1.00 11.02 ? 70  ILE   B CA  1 
ATOM   2329 C  C   . ILE   B 1 70  ? 10.126  -15.252 -6.813  1.00 10.77 ? 70  ILE   B C   1 
ATOM   2330 O  O   . ILE   B 1 70  ? 9.556   -16.337 -6.692  1.00 10.30 ? 70  ILE   B O   1 
ATOM   2331 C  CB  . ILE   B 1 70  ? 11.768  -15.772 -8.681  1.00 12.43 ? 70  ILE   B CB  1 
ATOM   2332 C  CG1 . ILE   B 1 70  ? 13.218  -15.671 -9.167  1.00 12.90 ? 70  ILE   B CG1 1 
ATOM   2333 C  CG2 . ILE   B 1 70  ? 10.816  -15.055 -9.645  1.00 12.53 ? 70  ILE   B CG2 1 
ATOM   2334 C  CD1 . ILE   B 1 70  ? 13.463  -16.393 -10.467 1.00 13.03 ? 70  ILE   B CD1 1 
ATOM   2335 N  N   . ALA   B 1 71  ? 9.566   -14.083 -6.479  1.00 10.30 ? 71  ALA   B N   1 
ATOM   2336 C  CA  . ALA   B 1 71  ? 8.160   -13.962 -6.127  1.00 10.71 ? 71  ALA   B CA  1 
ATOM   2337 C  C   . ALA   B 1 71  ? 7.377   -13.389 -7.305  1.00 11.74 ? 71  ALA   B C   1 
ATOM   2338 O  O   . ALA   B 1 71  ? 7.919   -12.652 -8.135  1.00 12.38 ? 71  ALA   B O   1 
ATOM   2339 C  CB  . ALA   B 1 71  ? 7.987   -13.050 -4.928  1.00 10.88 ? 71  ALA   B CB  1 
ATOM   2340 N  N   . THR   B 1 72  ? 6.096   -13.742 -7.400  1.00 10.67 ? 72  THR   B N   1 
ATOM   2341 C  CA  . THR   B 1 72  ? 5.244   -13.202 -8.422  1.00 10.62 ? 72  THR   B CA  1 
ATOM   2342 C  C   . THR   B 1 72  ? 3.863   -12.957 -7.822  1.00 11.88 ? 72  THR   B C   1 
ATOM   2343 O  O   . THR   B 1 72  ? 3.675   -13.075 -6.599  1.00 11.74 ? 72  THR   B O   1 
ATOM   2344 C  CB  . THR   B 1 72  ? 5.239   -14.149 -9.617  1.00 10.80 ? 72  THR   B CB  1 
ATOM   2345 O  OG1 . THR   B 1 72  ? 4.651   -13.446 -10.711 1.00 11.21 ? 72  THR   B OG1 1 
ATOM   2346 C  CG2 . THR   B 1 72  ? 4.456   -15.421 -9.346  1.00 11.14 ? 72  THR   B CG2 1 
ATOM   2347 N  N   . VAL   B 1 73  ? 2.925   -12.550 -8.676  1.00 11.11 ? 73  VAL   B N   1 
ATOM   2348 C  CA  . VAL   B 1 73  ? 1.620   -12.090 -8.212  1.00 12.28 ? 73  VAL   B CA  1 
ATOM   2349 C  C   . VAL   B 1 73  ? 0.561   -12.821 -9.058  1.00 11.30 ? 73  VAL   B C   1 
ATOM   2350 O  O   . VAL   B 1 73  ? 0.771   -13.023 -10.246 1.00 11.00 ? 73  VAL   B O   1 
ATOM   2351 C  CB  . VAL   B 1 73  ? 1.404   -10.573 -8.348  1.00 12.41 ? 73  VAL   B CB  1 
ATOM   2352 C  CG1 . VAL   B 1 73  ? 2.104   -9.811  -7.242  1.00 12.95 ? 73  VAL   B CG1 1 
ATOM   2353 C  CG2 . VAL   B 1 73  ? 1.809   -10.039 -9.727  1.00 13.74 ? 73  VAL   B CG2 1 
ATOM   2354 N  N   . THR   B 1 74  ? -0.546  -13.214 -8.411  1.00 10.39 ? 74  THR   B N   1 
ATOM   2355 C  CA  . THR   B 1 74  ? -1.709  -13.756 -9.079  1.00 10.47 ? 74  THR   B CA  1 
ATOM   2356 C  C   . THR   B 1 74  ? -2.996  -13.165 -8.483  1.00 10.91 ? 74  THR   B C   1 
ATOM   2357 O  O   . THR   B 1 74  ? -2.997  -12.501 -7.435  1.00 9.41  ? 74  THR   B O   1 
ATOM   2358 C  CB  . THR   B 1 74  ? -1.712  -15.282 -9.030  1.00 11.35 ? 74  THR   B CB  1 
ATOM   2359 O  OG1 . THR   B 1 74  ? -1.906  -15.675 -7.665  1.00 11.34 ? 74  THR   B OG1 1 
ATOM   2360 C  CG2 . THR   B 1 74  ? -0.456  -15.905 -9.582  1.00 11.37 ? 74  THR   B CG2 1 
ATOM   2361 N  N   . ASN   B 1 75  ? -4.087  -13.333 -9.255  1.00 11.00 ? 75  ASN   B N   1 
ATOM   2362 C  CA  . ASN   B 1 75  ? -5.363  -12.691 -8.971  1.00 11.01 ? 75  ASN   B CA  1 
ATOM   2363 C  C   . ASN   B 1 75  ? -5.190  -11.185 -8.814  1.00 11.38 ? 75  ASN   B C   1 
ATOM   2364 O  O   . ASN   B 1 75  ? -5.884  -10.541 -8.020  1.00 10.80 ? 75  ASN   B O   1 
ATOM   2365 C  CB  . ASN   B 1 75  ? -6.027  -13.295 -7.744  1.00 10.66 ? 75  ASN   B CB  1 
ATOM   2366 C  CG  . ASN   B 1 75  ? -7.530  -13.152 -7.802  1.00 11.45 ? 75  ASN   B CG  1 
ATOM   2367 O  OD1 . ASN   B 1 75  ? -8.131  -13.249 -8.892  1.00 11.64 ? 75  ASN   B OD1 1 
ATOM   2368 N  ND2 . ASN   B 1 75  ? -8.146  -12.964 -6.649  1.00 11.22 ? 75  ASN   B ND2 1 
ATOM   2369 N  N   . PHE   B 1 76  ? -4.291  -10.608 -9.627  1.00 11.59 ? 76  PHE   B N   1 
ATOM   2370 C  CA  . PHE   B 1 76  ? -3.696  -9.322  -9.298  1.00 12.34 ? 76  PHE   B CA  1 
ATOM   2371 C  C   . PHE   B 1 76  ? -3.904  -8.283  -10.395 1.00 13.05 ? 76  PHE   B C   1 
ATOM   2372 O  O   . PHE   B 1 76  ? -3.770  -8.613  -11.579 1.00 13.76 ? 76  PHE   B O   1 
ATOM   2373 C  CB  . PHE   B 1 76  ? -2.199  -9.568  -9.134  1.00 12.61 ? 76  PHE   B CB  1 
ATOM   2374 C  CG  . PHE   B 1 76  ? -1.379  -8.320  -8.834  1.00 13.67 ? 76  PHE   B CG  1 
ATOM   2375 C  CD1 . PHE   B 1 76  ? -0.929  -7.493  -9.872  1.00 14.51 ? 76  PHE   B CD1 1 
ATOM   2376 C  CD2 . PHE   B 1 76  ? -1.057  -7.993  -7.534  1.00 14.11 ? 76  PHE   B CD2 1 
ATOM   2377 C  CE1 . PHE   B 1 76  ? -0.186  -6.360  -9.588  1.00 15.06 ? 76  PHE   B CE1 1 
ATOM   2378 C  CE2 . PHE   B 1 76  ? -0.327  -6.840  -7.260  1.00 15.19 ? 76  PHE   B CE2 1 
ATOM   2379 C  CZ  . PHE   B 1 76  ? 0.092   -6.027  -8.289  1.00 14.68 ? 76  PHE   B CZ  1 
ATOM   2380 N  N   . PRO   B 1 77  ? -4.122  -6.991  -10.070 1.00 13.28 ? 77  PRO   B N   1 
ATOM   2381 C  CA  . PRO   B 1 77  ? -4.275  -6.510  -8.692  1.00 13.93 ? 77  PRO   B CA  1 
ATOM   2382 C  C   . PRO   B 1 77  ? -5.696  -6.502  -8.133  1.00 12.83 ? 77  PRO   B C   1 
ATOM   2383 O  O   . PRO   B 1 77  ? -5.925  -6.061  -6.995  1.00 12.87 ? 77  PRO   B O   1 
ATOM   2384 C  CB  . PRO   B 1 77  ? -3.767  -5.070  -8.867  1.00 15.30 ? 77  PRO   B CB  1 
ATOM   2385 C  CG  . PRO   B 1 77  ? -4.332  -4.654  -10.197 1.00 14.95 ? 77  PRO   B CG  1 
ATOM   2386 C  CD  . PRO   B 1 77  ? -4.170  -5.899  -11.063 1.00 15.52 ? 77  PRO   B CD  1 
ATOM   2387 N  N   . HIS   B 1 78  ? -6.643  -7.051  -8.906  1.00 11.75 ? 78  HIS   B N   1 
ATOM   2388 C  CA  . HIS   B 1 78  ? -8.062  -6.838  -8.709  1.00 12.78 ? 78  HIS   B CA  1 
ATOM   2389 C  C   . HIS   B 1 78  ? -8.640  -7.570  -7.491  1.00 12.20 ? 78  HIS   B C   1 
ATOM   2390 O  O   . HIS   B 1 78  ? -9.616  -7.102  -6.903  1.00 12.48 ? 78  HIS   B O   1 
ATOM   2391 C  CB  . HIS   B 1 78  ? -8.838  -7.277  -9.951  1.00 13.57 ? 78  HIS   B CB  1 
ATOM   2392 C  CG  . HIS   B 1 78  ? -8.348  -8.583  -10.504 1.00 13.96 ? 78  HIS   B CG  1 
ATOM   2393 N  ND1 . HIS   B 1 78  ? -8.592  -9.822  -9.944  1.00 13.47 ? 78  HIS   B ND1 1 
ATOM   2394 C  CD2 . HIS   B 1 78  ? -7.555  -8.811  -11.579 1.00 15.10 ? 78  HIS   B CD2 1 
ATOM   2395 C  CE1 . HIS   B 1 78  ? -8.002  -10.754 -10.678 1.00 14.81 ? 78  HIS   B CE1 1 
ATOM   2396 N  NE2 . HIS   B 1 78  ? -7.386  -10.168 -11.703 1.00 15.29 ? 78  HIS   B NE2 1 
ATOM   2397 N  N   . GLY   B 1 79  ? -8.067  -8.719  -7.105  1.00 11.21 ? 79  GLY   B N   1 
ATOM   2398 C  CA  . GLY   B 1 79  ? -8.664  -9.506  -6.032  1.00 11.51 ? 79  GLY   B CA  1 
ATOM   2399 C  C   . GLY   B 1 79  ? -10.103 -9.928  -6.366  1.00 12.28 ? 79  GLY   B C   1 
ATOM   2400 O  O   . GLY   B 1 79  ? -10.990 -9.971  -5.511  1.00 12.24 ? 79  GLY   B O   1 
ATOM   2401 N  N   . ASN   B 1 80  ? -10.325 -10.345 -7.612  1.00 12.26 ? 80  ASN   B N   1 
ATOM   2402 C  CA  . ASN   B 1 80  ? -11.613 -10.893 -8.011  1.00 12.66 ? 80  ASN   B CA  1 
ATOM   2403 C  C   . ASN   B 1 80  ? -11.890 -12.192 -7.260  1.00 12.45 ? 80  ASN   B C   1 
ATOM   2404 O  O   . ASN   B 1 80  ? -11.008 -12.804 -6.638  1.00 11.29 ? 80  ASN   B O   1 
ATOM   2405 C  CB  . ASN   B 1 80  ? -11.636 -11.142 -9.513  1.00 14.01 ? 80  ASN   B CB  1 
ATOM   2406 C  CG  . ASN   B 1 80  ? -11.686 -9.874  -10.331 1.00 15.50 ? 80  ASN   B CG  1 
ATOM   2407 O  OD1 . ASN   B 1 80  ? -11.970 -8.778  -9.831  1.00 16.89 ? 80  ASN   B OD1 1 
ATOM   2408 N  ND2 . ASN   B 1 80  ? -11.405 -10.014 -11.622 1.00 17.50 ? 80  ASN   B ND2 1 
ATOM   2409 N  N   . ASP   B 1 81  ? -13.160 -12.622 -7.282  1.00 12.97 ? 81  ASP   B N   1 
ATOM   2410 C  CA  . ASP   B 1 81  ? -13.567 -13.768 -6.491  1.00 13.97 ? 81  ASP   B CA  1 
ATOM   2411 C  C   . ASP   B 1 81  ? -13.835 -14.997 -7.348  1.00 13.80 ? 81  ASP   B C   1 
ATOM   2412 O  O   . ASP   B 1 81  ? -14.580 -15.874 -6.923  1.00 15.61 ? 81  ASP   B O   1 
ATOM   2413 C  CB  . ASP   B 1 81  ? -14.770 -13.444 -5.619  1.00 16.30 ? 81  ASP   B CB  1 
ATOM   2414 C  CG  . ASP   B 1 81  ? -15.997 -12.991 -6.393  1.00 20.86 ? 81  ASP   B CG  1 
ATOM   2415 O  OD1 . ASP   B 1 81  ? -15.937 -12.964 -7.635  1.00 22.45 ? 81  ASP   B OD1 1 
ATOM   2416 O  OD2 . ASP   B 1 81  ? -16.984 -12.656 -5.726  1.00 26.62 ? 81  ASP   B OD2 1 
ATOM   2417 N  N   . ASP   B 1 82  ? -13.162 -15.100 -8.496  1.00 13.21 ? 82  ASP   B N   1 
ATOM   2418 C  CA  . ASP   B 1 82  ? -13.232 -16.294 -9.319  1.00 14.42 ? 82  ASP   B CA  1 
ATOM   2419 C  C   . ASP   B 1 82  ? -12.072 -17.213 -8.972  1.00 13.33 ? 82  ASP   B C   1 
ATOM   2420 O  O   . ASP   B 1 82  ? -10.927 -16.950 -9.327  1.00 12.74 ? 82  ASP   B O   1 
ATOM   2421 C  CB  . ASP   B 1 82  ? -13.232 -15.953 -10.807 1.00 15.39 ? 82  ASP   B CB  1 
ATOM   2422 C  CG  . ASP   B 1 82  ? -13.507 -17.154 -11.705 1.00 17.79 ? 82  ASP   B CG  1 
ATOM   2423 O  OD1 . ASP   B 1 82  ? -12.896 -18.199 -11.484 1.00 17.12 ? 82  ASP   B OD1 1 
ATOM   2424 O  OD2 . ASP   B 1 82  ? -14.346 -17.019 -12.634 1.00 21.76 ? 82  ASP   B OD2 1 
ATOM   2425 N  N   . ILE   B 1 83  ? -12.388 -18.275 -8.225  1.00 13.01 ? 83  ILE   B N   1 
ATOM   2426 C  CA  . ILE   B 1 83  ? -11.372 -19.155 -7.686  1.00 13.18 ? 83  ILE   B CA  1 
ATOM   2427 C  C   . ILE   B 1 83  ? -10.635 -19.865 -8.813  1.00 13.13 ? 83  ILE   B C   1 
ATOM   2428 O  O   . ILE   B 1 83  ? -9.426  -20.024 -8.742  1.00 14.14 ? 83  ILE   B O   1 
ATOM   2429 C  CB  . ILE   B 1 83  ? -12.001 -20.165 -6.715  1.00 14.14 ? 83  ILE   B CB  1 
ATOM   2430 C  CG1 . ILE   B 1 83  ? -12.561 -19.467 -5.505  1.00 16.08 ? 83  ILE   B CG1 1 
ATOM   2431 C  CG2 . ILE   B 1 83  ? -10.985 -21.234 -6.326  1.00 15.26 ? 83  ILE   B CG2 1 
ATOM   2432 C  CD1 . ILE   B 1 83  ? -13.377 -20.374 -4.597  1.00 16.71 ? 83  ILE   B CD1 1 
ATOM   2433 N  N   . GLU   B 1 84  ? -11.361 -20.311 -9.839  1.00 14.62 ? 84  GLU   B N   1 
ATOM   2434 C  CA  . GLU   B 1 84  ? -10.741 -21.067 -10.919 1.00 16.07 ? 84  GLU   B CA  1 
ATOM   2435 C  C   . GLU   B 1 84  ? -9.717  -20.207 -11.645 1.00 14.42 ? 84  GLU   B C   1 
ATOM   2436 O  O   . GLU   B 1 84  ? -8.667  -20.710 -12.015 1.00 14.10 ? 84  GLU   B O   1 
ATOM   2437 C  CB  . GLU   B 1 84  ? -11.800 -21.607 -11.874 1.00 19.17 ? 84  GLU   B CB  1 
ATOM   2438 C  CG  . GLU   B 1 84  ? -12.669 -22.684 -11.247 1.00 26.29 ? 84  GLU   B CG  1 
ATOM   2439 C  CD  . GLU   B 1 84  ? -12.058 -24.072 -11.219 1.00 39.78 ? 84  GLU   B CD  1 
ATOM   2440 O  OE1 . GLU   B 1 84  ? -10.920 -24.294 -11.732 1.00 49.15 ? 84  GLU   B OE1 1 
ATOM   2441 O  OE2 . GLU   B 1 84  ? -12.779 -24.960 -10.703 1.00 48.29 ? 84  GLU   B OE2 1 
ATOM   2442 N  N   . ILE   B 1 85  ? -10.003 -18.918 -11.841 1.00 13.41 ? 85  ILE   B N   1 
ATOM   2443 C  CA  . ILE   B 1 85  ? -9.021  -18.062 -12.478 1.00 12.41 ? 85  ILE   B CA  1 
ATOM   2444 C  C   . ILE   B 1 85  ? -7.804  -17.849 -11.585 1.00 12.36 ? 85  ILE   B C   1 
ATOM   2445 O  O   . ILE   B 1 85  ? -6.671  -17.933 -12.042 1.00 11.84 ? 85  ILE   B O   1 
ATOM   2446 C  CB  . ILE   B 1 85  ? -9.676  -16.761 -12.950 1.00 13.68 ? 85  ILE   B CB  1 
ATOM   2447 C  CG1 . ILE   B 1 85  ? -10.652 -17.053 -14.123 1.00 14.12 ? 85  ILE   B CG1 1 
ATOM   2448 C  CG2 . ILE   B 1 85  ? -8.638  -15.705 -13.318 1.00 14.53 ? 85  ILE   B CG2 1 
ATOM   2449 C  CD1 . ILE   B 1 85  ? -11.308 -15.817 -14.693 1.00 15.20 ? 85  ILE   B CD1 1 
ATOM   2450 N  N   . ALA   B 1 86  ? -8.027  -17.507 -10.303 1.00 12.03 ? 86  ALA   B N   1 
ATOM   2451 C  CA  . ALA   B 1 86  ? -6.912  -17.328 -9.397  1.00 11.95 ? 86  ALA   B CA  1 
ATOM   2452 C  C   . ALA   B 1 86  ? -6.048  -18.583 -9.325  1.00 11.96 ? 86  ALA   B C   1 
ATOM   2453 O  O   . ALA   B 1 86  ? -4.814  -18.514 -9.316  1.00 11.20 ? 86  ALA   B O   1 
ATOM   2454 C  CB  . ALA   B 1 86  ? -7.417  -16.929 -8.037  1.00 12.09 ? 86  ALA   B CB  1 
ATOM   2455 N  N   . LEU   B 1 87  ? -6.683  -19.756 -9.273  1.00 11.52 ? 87  LEU   B N   1 
ATOM   2456 C  CA  . LEU   B 1 87  ? -5.944  -20.998 -9.177  1.00 12.06 ? 87  LEU   B CA  1 
ATOM   2457 C  C   . LEU   B 1 87  ? -5.151  -21.291 -10.452 1.00 11.77 ? 87  LEU   B C   1 
ATOM   2458 O  O   . LEU   B 1 87  ? -4.003  -21.714 -10.360 1.00 11.48 ? 87  LEU   B O   1 
ATOM   2459 C  CB  . LEU   B 1 87  ? -6.958  -22.104 -8.926  1.00 12.94 ? 87  LEU   B CB  1 
ATOM   2460 C  CG  . LEU   B 1 87  ? -6.384  -23.514 -8.805  1.00 13.80 ? 87  LEU   B CG  1 
ATOM   2461 C  CD1 . LEU   B 1 87  ? -5.296  -23.702 -7.791  1.00 13.35 ? 87  LEU   B CD1 1 
ATOM   2462 C  CD2 . LEU   B 1 87  ? -7.504  -24.509 -8.591  1.00 15.10 ? 87  LEU   B CD2 1 
ATOM   2463 N  N   . ALA   B 1 88  ? -5.766  -21.064 -11.619 1.00 12.13 ? 88  ALA   B N   1 
ATOM   2464 C  CA  . ALA   B 1 88  ? -5.070  -21.281 -12.879 1.00 12.14 ? 88  ALA   B CA  1 
ATOM   2465 C  C   . ALA   B 1 88  ? -3.814  -20.400 -12.959 1.00 12.33 ? 88  ALA   B C   1 
ATOM   2466 O  O   . ALA   B 1 88  ? -2.743  -20.833 -13.367 1.00 12.34 ? 88  ALA   B O   1 
ATOM   2467 C  CB  . ALA   B 1 88  ? -6.030  -21.015 -14.031 1.00 12.40 ? 88  ALA   B CB  1 
ATOM   2468 N  N   . GLU   B 1 89  ? -3.953  -19.131 -12.583 1.00 11.86 ? 89  GLU   B N   1 
ATOM   2469 C  CA  . GLU   B 1 89  ? -2.844  -18.198 -12.575 1.00 12.15 ? 89  GLU   B CA  1 
ATOM   2470 C  C   . GLU   B 1 89  ? -1.759  -18.657 -11.597 1.00 11.58 ? 89  GLU   B C   1 
ATOM   2471 O  O   . GLU   B 1 89  ? -0.573  -18.566 -11.904 1.00 11.22 ? 89  GLU   B O   1 
ATOM   2472 C  CB  . GLU   B 1 89  ? -3.334  -16.789 -12.233 1.00 12.73 ? 89  GLU   B CB  1 
ATOM   2473 C  CG  . GLU   B 1 89  ? -4.234  -16.169 -13.302 1.00 14.21 ? 89  GLU   B CG  1 
ATOM   2474 C  CD  . GLU   B 1 89  ? -4.578  -14.717 -13.033 1.00 17.07 ? 89  GLU   B CD  1 
ATOM   2475 O  OE1 . GLU   B 1 89  ? -4.366  -14.263 -11.892 1.00 17.86 ? 89  GLU   B OE1 1 
ATOM   2476 O  OE2 . GLU   B 1 89  ? -5.054  -13.986 -13.925 1.00 16.15 ? 89  GLU   B OE2 1 
ATOM   2477 N  N   . THR   B 1 90  ? -2.165  -19.164 -10.430 1.00 10.39 ? 90  THR   B N   1 
ATOM   2478 C  CA  . THR   B 1 90  ? -1.216  -19.625 -9.431  1.00 10.39 ? 90  THR   B CA  1 
ATOM   2479 C  C   . THR   B 1 90  ? -0.471  -20.867 -9.939  1.00 10.16 ? 90  THR   B C   1 
ATOM   2480 O  O   . THR   B 1 90  ? 0.748   -20.970 -9.821  1.00 9.26  ? 90  THR   B O   1 
ATOM   2481 C  CB  . THR   B 1 90  ? -1.949  -19.859 -8.110  1.00 11.01 ? 90  THR   B CB  1 
ATOM   2482 O  OG1 . THR   B 1 90  ? -2.531  -18.635 -7.633  1.00 11.03 ? 90  THR   B OG1 1 
ATOM   2483 C  CG2 . THR   B 1 90  ? -1.046  -20.457 -7.053  1.00 10.98 ? 90  THR   B CG2 1 
ATOM   2484 N  N   . ARG   B 1 91  ? -1.195  -21.807 -10.554 1.00 11.03 ? 91  ARG   B N   1 
ATOM   2485 C  CA  . ARG   B 1 91  ? -0.566  -22.976 -11.150 1.00 11.59 ? 91  ARG   B CA  1 
ATOM   2486 C  C   . ARG   B 1 91  ? 0.443   -22.583 -12.220 1.00 11.16 ? 91  ARG   B C   1 
ATOM   2487 O  O   . ARG   B 1 91  ? 1.531   -23.160 -12.306 1.00 11.09 ? 91  ARG   B O   1 
ATOM   2488 C  CB  . ARG   B 1 91  ? -1.638  -23.918 -11.699 1.00 12.41 ? 91  ARG   B CB  1 
ATOM   2489 C  CG  . ARG   B 1 91  ? -2.396  -24.687 -10.620 1.00 13.77 ? 91  ARG   B CG  1 
ATOM   2490 C  CD  . ARG   B 1 91  ? -3.488  -25.508 -11.268 1.00 18.53 ? 91  ARG   B CD  1 
ATOM   2491 N  NE  . ARG   B 1 91  ? -4.215  -26.296 -10.268 1.00 21.03 ? 91  ARG   B NE  1 
ATOM   2492 C  CZ  . ARG   B 1 91  ? -5.386  -26.887 -10.496 1.00 25.04 ? 91  ARG   B CZ  1 
ATOM   2493 N  NH1 . ARG   B 1 91  ? -6.066  -26.635 -11.599 1.00 26.67 ? 91  ARG   B NH1 1 
ATOM   2494 N  NH2 . ARG   B 1 91  ? -5.882  -27.715 -9.607  1.00 24.92 ? 91  ARG   B NH2 1 
ATOM   2495 N  N   . ALA   B 1 92  ? 0.087   -21.590 -13.046 1.00 11.34 ? 92  ALA   B N   1 
ATOM   2496 C  CA  . ALA   B 1 92  ? 0.980   -21.144 -14.099 1.00 11.01 ? 92  ALA   B CA  1 
ATOM   2497 C  C   . ALA   B 1 92  ? 2.232   -20.521 -13.485 1.00 10.84 ? 92  ALA   B C   1 
ATOM   2498 O  O   . ALA   B 1 92  ? 3.337   -20.782 -13.931 1.00 10.58 ? 92  ALA   B O   1 
ATOM   2499 C  CB  . ALA   B 1 92  ? 0.286   -20.138 -14.995 1.00 11.65 ? 92  ALA   B CB  1 
ATOM   2500 N  N   . ALA   B 1 93  ? 2.044   -19.675 -12.460 1.00 10.46 ? 93  ALA   B N   1 
ATOM   2501 C  CA  . ALA   B 1 93  ? 3.188   -19.080 -11.781 1.00 10.26 ? 93  ALA   B CA  1 
ATOM   2502 C  C   . ALA   B 1 93  ? 4.157   -20.149 -11.277 1.00 11.06 ? 93  ALA   B C   1 
ATOM   2503 O  O   . ALA   B 1 93  ? 5.378   -20.001 -11.389 1.00 10.93 ? 93  ALA   B O   1 
ATOM   2504 C  CB  . ALA   B 1 93  ? 2.717   -18.240 -10.627 1.00 9.79  ? 93  ALA   B CB  1 
ATOM   2505 N  N   . ILE   B 1 94  ? 3.595   -21.194 -10.667 1.00 10.96 ? 94  ILE   B N   1 
ATOM   2506 C  CA  . ILE   B 1 94  ? 4.386   -22.312 -10.182 1.00 11.02 ? 94  ILE   B CA  1 
ATOM   2507 C  C   . ILE   B 1 94  ? 5.149   -22.972 -11.338 1.00 11.50 ? 94  ILE   B C   1 
ATOM   2508 O  O   . ILE   B 1 94  ? 6.349   -23.250 -11.241 1.00 11.67 ? 94  ILE   B O   1 
ATOM   2509 C  CB  . ILE   B 1 94  ? 3.474   -23.302 -9.446  1.00 11.45 ? 94  ILE   B CB  1 
ATOM   2510 C  CG1 . ILE   B 1 94  ? 2.934   -22.696 -8.143  1.00 11.95 ? 94  ILE   B CG1 1 
ATOM   2511 C  CG2 . ILE   B 1 94  ? 4.223   -24.604 -9.179  1.00 12.11 ? 94  ILE   B CG2 1 
ATOM   2512 C  CD1 . ILE   B 1 94  ? 1.735   -23.434 -7.597  1.00 12.11 ? 94  ILE   B CD1 1 
ATOM   2513 N  N   . ALA   B 1 95  ? 4.443   -23.210 -12.434 1.00 10.87 ? 95  ALA   B N   1 
ATOM   2514 C  CA  . ALA   B 1 95  ? 5.017   -23.889 -13.589 1.00 11.11 ? 95  ALA   B CA  1 
ATOM   2515 C  C   . ALA   B 1 95  ? 6.122   -23.055 -14.231 1.00 12.03 ? 95  ALA   B C   1 
ATOM   2516 O  O   . ALA   B 1 95  ? 7.098   -23.595 -14.748 1.00 11.75 ? 95  ALA   B O   1 
ATOM   2517 C  CB  . ALA   B 1 95  ? 3.956   -24.224 -14.588 1.00 11.01 ? 95  ALA   B CB  1 
ATOM   2518 N  N   . TYR   B 1 96  ? 5.983   -21.743 -14.204 1.00 11.69 ? 96  TYR   B N   1 
ATOM   2519 C  CA  . TYR   B 1 96  ? 7.021   -20.882 -14.732 1.00 12.06 ? 96  TYR   B CA  1 
ATOM   2520 C  C   . TYR   B 1 96  ? 8.305   -20.959 -13.890 1.00 12.70 ? 96  TYR   B C   1 
ATOM   2521 O  O   . TYR   B 1 96  ? 9.365   -20.615 -14.399 1.00 13.55 ? 96  TYR   B O   1 
ATOM   2522 C  CB  . TYR   B 1 96  ? 6.585   -19.432 -14.745 1.00 11.93 ? 96  TYR   B CB  1 
ATOM   2523 C  CG  . TYR   B 1 96  ? 5.756   -18.932 -15.911 1.00 11.49 ? 96  TYR   B CG  1 
ATOM   2524 C  CD1 . TYR   B 1 96  ? 6.289   -18.895 -17.192 1.00 11.86 ? 96  TYR   B CD1 1 
ATOM   2525 C  CD2 . TYR   B 1 96  ? 4.486   -18.391 -15.715 1.00 11.32 ? 96  TYR   B CD2 1 
ATOM   2526 C  CE1 . TYR   B 1 96  ? 5.549   -18.413 -18.255 1.00 11.59 ? 96  TYR   B CE1 1 
ATOM   2527 C  CE2 . TYR   B 1 96  ? 3.768   -17.839 -16.750 1.00 12.13 ? 96  TYR   B CE2 1 
ATOM   2528 C  CZ  . TYR   B 1 96  ? 4.312   -17.848 -18.026 1.00 12.35 ? 96  TYR   B CZ  1 
ATOM   2529 O  OH  . TYR   B 1 96  ? 3.619   -17.302 -19.083 1.00 13.29 ? 96  TYR   B OH  1 
ATOM   2530 N  N   . GLY   B 1 97  ? 8.179   -21.331 -12.608 1.00 12.45 ? 97  GLY   B N   1 
ATOM   2531 C  CA  . GLY   B 1 97  ? 9.297   -21.533 -11.697 1.00 13.13 ? 97  GLY   B CA  1 
ATOM   2532 C  C   . GLY   B 1 97  ? 9.284   -20.596 -10.485 1.00 11.98 ? 97  GLY   B C   1 
ATOM   2533 O  O   . GLY   B 1 97  ? 10.335  -20.421 -9.866  1.00 12.61 ? 97  GLY   B O   1 
ATOM   2534 N  N   . ALA   B 1 98  ? 8.124   -20.042 -10.104 1.00 11.04 ? 98  ALA   B N   1 
ATOM   2535 C  CA  . ALA   B 1 98  ? 8.102   -19.150 -8.944  1.00 10.75 ? 98  ALA   B CA  1 
ATOM   2536 C  C   . ALA   B 1 98  ? 8.593   -19.871 -7.695  1.00 10.84 ? 98  ALA   B C   1 
ATOM   2537 O  O   . ALA   B 1 98  ? 8.270   -21.041 -7.502  1.00 10.58 ? 98  ALA   B O   1 
ATOM   2538 C  CB  . ALA   B 1 98  ? 6.699   -18.612 -8.699  1.00 11.63 ? 98  ALA   B CB  1 
ATOM   2539 N  N   . ASP   B 1 99  ? 9.295   -19.137 -6.806  1.00 10.33 ? 99  ASP   B N   1 
ATOM   2540 C  CA  . ASP   B 1 99  ? 9.541   -19.608 -5.450  1.00 10.38 ? 99  ASP   B CA  1 
ATOM   2541 C  C   . ASP   B 1 99  ? 8.400   -19.234 -4.518  1.00 10.44 ? 99  ASP   B C   1 
ATOM   2542 O  O   . ASP   B 1 99  ? 8.161   -19.929 -3.537  1.00 10.83 ? 99  ASP   B O   1 
ATOM   2543 C  CB  . ASP   B 1 99  ? 10.831  -19.023 -4.919  1.00 10.75 ? 99  ASP   B CB  1 
ATOM   2544 C  CG  . ASP   B 1 99  ? 12.062  -19.456 -5.693  1.00 12.22 ? 99  ASP   B CG  1 
ATOM   2545 O  OD1 . ASP   B 1 99  ? 12.159  -20.682 -5.948  1.00 13.29 ? 99  ASP   B OD1 1 
ATOM   2546 O  OD2 . ASP   B 1 99  ? 12.827  -18.567 -6.123  1.00 13.40 ? 99  ASP   B OD2 1 
ATOM   2547 N  N   . GLU   B 1 100 ? 7.730   -18.117 -4.836  1.00 10.15 ? 100 GLU   B N   1 
ATOM   2548 C  CA  . GLU   B 1 100 ? 6.681   -17.555 -4.005  1.00 10.43 ? 100 GLU   B CA  1 
ATOM   2549 C  C   . GLU   B 1 100 ? 5.624   -16.929 -4.889  1.00 10.25 ? 100 GLU   B C   1 
ATOM   2550 O  O   . GLU   B 1 100 ? 5.956   -16.332 -5.931  1.00 10.07 ? 100 GLU   B O   1 
ATOM   2551 C  CB  . GLU   B 1 100 ? 7.238   -16.465 -3.086  1.00 11.93 ? 100 GLU   B CB  1 
ATOM   2552 C  CG  . GLU   B 1 100 ? 8.400   -16.966 -2.242  1.00 13.87 ? 100 GLU   B CG  1 
ATOM   2553 C  CD  . GLU   B 1 100 ? 9.024   -15.941 -1.313  1.00 15.73 ? 100 GLU   B CD  1 
ATOM   2554 O  OE1 . GLU   B 1 100 ? 8.680   -14.737 -1.391  1.00 14.74 ? 100 GLU   B OE1 1 
ATOM   2555 O  OE2 . GLU   B 1 100 ? 9.889   -16.403 -0.517  1.00 15.72 ? 100 GLU   B OE2 1 
ATOM   2556 N  N   . VAL   B 1 101 ? 4.370   -17.071 -4.467  1.00 9.59  ? 101 VAL   B N   1 
ATOM   2557 C  CA  . VAL   B 1 101 ? 3.247   -16.462 -5.140  1.00 10.02 ? 101 VAL   B CA  1 
ATOM   2558 C  C   . VAL   B 1 101 ? 2.519   -15.569 -4.157  1.00 10.45 ? 101 VAL   B C   1 
ATOM   2559 O  O   . VAL   B 1 101 ? 2.163   -16.048 -3.101  1.00 11.05 ? 101 VAL   B O   1 
ATOM   2560 C  CB  . VAL   B 1 101 ? 2.283   -17.525 -5.689  1.00 11.12 ? 101 VAL   B CB  1 
ATOM   2561 C  CG1 . VAL   B 1 101 ? 0.992   -16.900 -6.247  1.00 11.97 ? 101 VAL   B CG1 1 
ATOM   2562 C  CG2 . VAL   B 1 101 ? 3.003   -18.367 -6.739  1.00 11.02 ? 101 VAL   B CG2 1 
ATOM   2563 N  N   . ASP   B 1 102 ? 2.324   -14.302 -4.539  1.00 10.70 ? 102 ASP   B N   1 
ATOM   2564 C  CA  . ASP   B 1 102 ? 1.540   -13.363 -3.763  1.00 11.32 ? 102 ASP   B CA  1 
ATOM   2565 C  C   . ASP   B 1 102 ? 0.167   -13.249 -4.450  1.00 10.80 ? 102 ASP   B C   1 
ATOM   2566 O  O   . ASP   B 1 102 ? 0.042   -12.618 -5.502  1.00 11.59 ? 102 ASP   B O   1 
ATOM   2567 C  CB  . ASP   B 1 102 ? 2.244   -12.012 -3.662  1.00 11.74 ? 102 ASP   B CB  1 
ATOM   2568 C  CG  . ASP   B 1 102 ? 3.650   -11.986 -3.042  1.00 13.68 ? 102 ASP   B CG  1 
ATOM   2569 O  OD1 . ASP   B 1 102 ? 4.222   -13.055 -2.733  1.00 14.42 ? 102 ASP   B OD1 1 
ATOM   2570 O  OD2 . ASP   B 1 102 ? 4.197   -10.866 -2.890  1.00 16.15 ? 102 ASP   B OD2 1 
ATOM   2571 N  N   . VAL   B 1 103 ? -0.861  -13.856 -3.847  1.00 10.61 ? 103 VAL   B N   1 
ATOM   2572 C  CA  . VAL   B 1 103 ? -2.201  -13.825 -4.415  1.00 10.22 ? 103 VAL   B CA  1 
ATOM   2573 C  C   . VAL   B 1 103 ? -3.045  -12.724 -3.747  1.00 10.77 ? 103 VAL   B C   1 
ATOM   2574 O  O   . VAL   B 1 103 ? -2.970  -12.517 -2.541  1.00 10.91 ? 103 VAL   B O   1 
ATOM   2575 C  CB  . VAL   B 1 103 ? -2.884  -15.198 -4.272  1.00 11.11 ? 103 VAL   B CB  1 
ATOM   2576 C  CG1 . VAL   B 1 103 ? -3.152  -15.580 -2.837  1.00 11.26 ? 103 VAL   B CG1 1 
ATOM   2577 C  CG2 . VAL   B 1 103 ? -4.165  -15.283 -5.093  1.00 11.24 ? 103 VAL   B CG2 1 
ATOM   2578 N  N   . VAL   B 1 104 ? -3.911  -12.064 -4.513  1.00 10.08 ? 104 VAL   B N   1 
ATOM   2579 C  CA  . VAL   B 1 104 ? -4.773  -11.052 -3.932  1.00 10.34 ? 104 VAL   B CA  1 
ATOM   2580 C  C   . VAL   B 1 104 ? -6.051  -11.742 -3.412  1.00 10.59 ? 104 VAL   B C   1 
ATOM   2581 O  O   . VAL   B 1 104 ? -6.772  -12.442 -4.142  1.00 11.07 ? 104 VAL   B O   1 
ATOM   2582 C  CB  . VAL   B 1 104 ? -5.109  -9.910  -4.903  1.00 10.08 ? 104 VAL   B CB  1 
ATOM   2583 C  CG1 . VAL   B 1 104 ? -5.863  -8.838  -4.164  1.00 10.40 ? 104 VAL   B CG1 1 
ATOM   2584 C  CG2 . VAL   B 1 104 ? -3.871  -9.316  -5.550  1.00 10.64 ? 104 VAL   B CG2 1 
ATOM   2585 N  N   . PHE   B 1 105 ? -6.309  -11.544 -2.110  1.00 10.50 ? 105 PHE   B N   1 
ATOM   2586 C  CA  . PHE   B 1 105 ? -7.510  -11.993 -1.465  1.00 10.76 ? 105 PHE   B CA  1 
ATOM   2587 C  C   . PHE   B 1 105 ? -8.729  -11.308 -2.064  1.00 10.44 ? 105 PHE   B C   1 
ATOM   2588 O  O   . PHE   B 1 105 ? -8.646  -10.137 -2.479  1.00 10.08 ? 105 PHE   B O   1 
ATOM   2589 C  CB  . PHE   B 1 105 ? -7.382  -11.570 -0.006  1.00 10.67 ? 105 PHE   B CB  1 
ATOM   2590 C  CG  . PHE   B 1 105 ? -8.480  -12.055 0.917   1.00 11.23 ? 105 PHE   B CG  1 
ATOM   2591 C  CD1 . PHE   B 1 105 ? -8.351  -13.262 1.563   1.00 12.12 ? 105 PHE   B CD1 1 
ATOM   2592 C  CD2 . PHE   B 1 105 ? -9.628  -11.289 1.140   1.00 12.05 ? 105 PHE   B CD2 1 
ATOM   2593 C  CE1 . PHE   B 1 105 ? -9.339  -13.702 2.420   1.00 13.04 ? 105 PHE   B CE1 1 
ATOM   2594 C  CE2 . PHE   B 1 105 ? -10.629 -11.760 1.971   1.00 13.84 ? 105 PHE   B CE2 1 
ATOM   2595 C  CZ  . PHE   B 1 105 ? -10.479 -12.953 2.616   1.00 12.73 ? 105 PHE   B CZ  1 
ATOM   2596 N  N   . PRO   B 1 106 ? -9.885  -12.002 -2.134  1.00 10.88 ? 106 PRO   B N   1 
ATOM   2597 C  CA  . PRO   B 1 106 ? -11.086 -11.369 -2.660  1.00 10.88 ? 106 PRO   B CA  1 
ATOM   2598 C  C   . PRO   B 1 106 ? -11.688 -10.462 -1.592  1.00 11.33 ? 106 PRO   B C   1 
ATOM   2599 O  O   . PRO   B 1 106 ? -12.672 -10.801 -0.950  1.00 12.32 ? 106 PRO   B O   1 
ATOM   2600 C  CB  . PRO   B 1 106 ? -11.955 -12.571 -3.050  1.00 11.75 ? 106 PRO   B CB  1 
ATOM   2601 C  CG  . PRO   B 1 106 ? -11.572 -13.640 -2.075  1.00 11.39 ? 106 PRO   B CG  1 
ATOM   2602 C  CD  . PRO   B 1 106 ? -10.073 -13.436 -1.869  1.00 11.25 ? 106 PRO   B CD  1 
ATOM   2603 N  N   . TYR   B 1 107 ? -11.118 -9.270  -1.486  1.00 11.01 ? 107 TYR   B N   1 
ATOM   2604 C  CA  . TYR   B 1 107 ? -11.451 -8.349  -0.424  1.00 11.49 ? 107 TYR   B CA  1 
ATOM   2605 C  C   . TYR   B 1 107 ? -12.830 -7.723  -0.651  1.00 11.48 ? 107 TYR   B C   1 
ATOM   2606 O  O   . TYR   B 1 107 ? -13.577 -7.508  0.324   1.00 12.02 ? 107 TYR   B O   1 
ATOM   2607 C  CB  . TYR   B 1 107 ? -10.342 -7.326  -0.192  1.00 12.08 ? 107 TYR   B CB  1 
ATOM   2608 C  CG  . TYR   B 1 107 ? -10.007 -6.427  -1.360  1.00 11.90 ? 107 TYR   B CG  1 
ATOM   2609 C  CD1 . TYR   B 1 107 ? -10.737 -5.282  -1.605  1.00 12.54 ? 107 TYR   B CD1 1 
ATOM   2610 C  CD2 . TYR   B 1 107 ? -8.966  -6.742  -2.233  1.00 12.28 ? 107 TYR   B CD2 1 
ATOM   2611 C  CE1 . TYR   B 1 107 ? -10.441 -4.476  -2.695  1.00 12.80 ? 107 TYR   B CE1 1 
ATOM   2612 C  CE2 . TYR   B 1 107 ? -8.658  -5.946  -3.329  1.00 11.98 ? 107 TYR   B CE2 1 
ATOM   2613 C  CZ  . TYR   B 1 107 ? -9.415  -4.812  -3.554  1.00 12.71 ? 107 TYR   B CZ  1 
ATOM   2614 O  OH  . TYR   B 1 107 ? -9.142  -3.978  -4.583  1.00 13.89 ? 107 TYR   B OH  1 
ATOM   2615 N  N   . ARG   B 1 108 ? -13.205 -7.466  -1.906  1.00 11.96 ? 108 ARG   B N   1 
ATOM   2616 C  CA  . ARG   B 1 108 ? -14.514 -6.912  -2.185  1.00 12.11 ? 108 ARG   B CA  1 
ATOM   2617 C  C   . ARG   B 1 108 ? -15.596 -7.911  -1.799  1.00 12.52 ? 108 ARG   B C   1 
ATOM   2618 O  O   . ARG   B 1 108 ? -16.650 -7.512  -1.288  1.00 13.11 ? 108 ARG   B O   1 
ATOM   2619 C  CB  . ARG   B 1 108 ? -14.635 -6.458  -3.633  1.00 13.38 ? 108 ARG   B CB  1 
ATOM   2620 C  CG  . ARG   B 1 108 ? -13.878 -5.181  -3.960  1.00 14.80 ? 108 ARG   B CG  1 
ATOM   2621 C  CD  . ARG   B 1 108 ? -14.224 -4.691  -5.352  1.00 16.74 ? 108 ARG   B CD  1 
ATOM   2622 N  NE  . ARG   B 1 108 ? -13.911 -5.743  -6.288  1.00 19.61 ? 108 ARG   B NE  1 
ATOM   2623 C  CZ  . ARG   B 1 108 ? -12.704 -6.053  -6.728  1.00 21.40 ? 108 ARG   B CZ  1 
ATOM   2624 N  NH1 . ARG   B 1 108 ? -11.692 -5.244  -6.458  1.00 26.03 ? 108 ARG   B NH1 1 
ATOM   2625 N  NH2 . ARG   B 1 108 ? -12.526 -7.121  -7.497  1.00 19.31 ? 108 ARG   B NH2 1 
ATOM   2626 N  N   . ALA   B 1 109 ? -15.344 -9.209  -2.018  1.00 12.36 ? 109 ALA   B N   1 
ATOM   2627 C  CA  . ALA   B 1 109 ? -16.297 -10.228 -1.626  1.00 13.35 ? 109 ALA   B CA  1 
ATOM   2628 C  C   . ALA   B 1 109 ? -16.470 -10.251 -0.112  1.00 13.17 ? 109 ALA   B C   1 
ATOM   2629 O  O   . ALA   B 1 109 ? -17.575 -10.359 0.403   1.00 13.62 ? 109 ALA   B O   1 
ATOM   2630 C  CB  . ALA   B 1 109 ? -15.902 -11.574 -2.154  1.00 13.25 ? 109 ALA   B CB  1 
ATOM   2631 N  N   . LEU   B 1 110 ? -15.369 -10.080 0.620   1.00 13.27 ? 110 LEU   B N   1 
ATOM   2632 C  CA  . LEU   B 1 110 ? -15.448 -10.031 2.077   1.00 12.50 ? 110 LEU   B CA  1 
ATOM   2633 C  C   . LEU   B 1 110 ? -16.230 -8.803  2.536   1.00 12.63 ? 110 LEU   B C   1 
ATOM   2634 O  O   . LEU   B 1 110 ? -17.028 -8.899  3.486   1.00 13.84 ? 110 LEU   B O   1 
ATOM   2635 C  CB  . LEU   B 1 110 ? -14.063 -10.056 2.727   1.00 12.64 ? 110 LEU   B CB  1 
ATOM   2636 C  CG  . LEU   B 1 110 ? -14.062 -9.855  4.245   1.00 13.46 ? 110 LEU   B CG  1 
ATOM   2637 C  CD1 . LEU   B 1 110 ? -14.674 -11.117 4.871   1.00 13.75 ? 110 LEU   B CD1 1 
ATOM   2638 C  CD2 . LEU   B 1 110 ? -12.631 -9.652  4.707   1.00 13.89 ? 110 LEU   B CD2 1 
ATOM   2639 N  N   . MET   B 1 111 ? -16.028 -7.662  1.880   1.00 12.94 ? 111 MET   B N   1 
ATOM   2640 C  CA  . MET   B 1 111 ? -16.748 -6.451  2.242   1.00 14.34 ? 111 MET   B CA  1 
ATOM   2641 C  C   . MET   B 1 111 ? -18.250 -6.608  1.947   1.00 14.07 ? 111 MET   B C   1 
ATOM   2642 O  O   . MET   B 1 111 ? -19.067 -5.941  2.559   1.00 13.93 ? 111 MET   B O   1 
ATOM   2643 C  CB  . MET   B 1 111 ? -16.147 -5.240  1.516   1.00 16.33 ? 111 MET   B CB  1 
ATOM   2644 C  CG  . MET   B 1 111 ? -14.701 -4.906  1.988   1.00 19.35 ? 111 MET   B CG  1 
ATOM   2645 S  SD  . MET   B 1 111 ? -13.775 -3.806  0.888   1.00 25.73 ? 111 MET   B SD  1 
ATOM   2646 C  CE  . MET   B 1 111 ? -14.559 -2.396  1.676   1.00 26.93 ? 111 MET   B CE  1 
ATOM   2647 N  N   . ALA   B 1 112 ? -18.594 -7.523  1.047   1.00 13.17 ? 112 ALA   B N   1 
ATOM   2648 C  CA  . ALA   B 1 112 ? -19.978 -7.863  0.727   1.00 14.19 ? 112 ALA   B CA  1 
ATOM   2649 C  C   . ALA   B 1 112 ? -20.483 -9.036  1.579   1.00 15.52 ? 112 ALA   B C   1 
ATOM   2650 O  O   . ALA   B 1 112 ? -21.534 -9.604  1.272   1.00 17.28 ? 112 ALA   B O   1 
ATOM   2651 C  CB  . ALA   B 1 112 ? -20.096 -8.169  -0.755  1.00 14.04 ? 112 ALA   B CB  1 
ATOM   2652 N  N   . GLY   B 1 113 ? -19.713 -9.430  2.601   1.00 15.23 ? 113 GLY   B N   1 
ATOM   2653 C  CA  . GLY   B 1 113 ? -20.149 -10.398 3.590   1.00 16.16 ? 113 GLY   B CA  1 
ATOM   2654 C  C   . GLY   B 1 113 ? -19.869 -11.845 3.217   1.00 17.28 ? 113 GLY   B C   1 
ATOM   2655 O  O   . GLY   B 1 113 ? -20.318 -12.744 3.920   1.00 20.20 ? 113 GLY   B O   1 
ATOM   2656 N  N   . ASN   B 1 114 ? -19.097 -12.098 2.147   1.00 16.17 ? 114 ASN   B N   1 
ATOM   2657 C  CA  . ASN   B 1 114 ? -18.762 -13.457 1.769   1.00 15.77 ? 114 ASN   B CA  1 
ATOM   2658 C  C   . ASN   B 1 114 ? -17.353 -13.786 2.269   1.00 16.67 ? 114 ASN   B C   1 
ATOM   2659 O  O   . ASN   B 1 114 ? -16.367 -13.442 1.622   1.00 15.90 ? 114 ASN   B O   1 
ATOM   2660 C  CB  . ASN   B 1 114 ? -18.888 -13.630 0.278   1.00 16.27 ? 114 ASN   B CB  1 
ATOM   2661 C  CG  . ASN   B 1 114 ? -18.722 -15.063 -0.158  1.00 16.38 ? 114 ASN   B CG  1 
ATOM   2662 O  OD1 . ASN   B 1 114 ? -18.220 -15.908 0.596   1.00 17.07 ? 114 ASN   B OD1 1 
ATOM   2663 N  ND2 . ASN   B 1 114 ? -19.137 -15.348 -1.375  1.00 19.38 ? 114 ASN   B ND2 1 
ATOM   2664 N  N   . GLU   B 1 115 ? -17.291 -14.449 3.419   1.00 15.99 ? 115 GLU   B N   1 
ATOM   2665 C  CA  . GLU   B 1 115 ? -16.042 -14.890 4.007   1.00 16.98 ? 115 GLU   B CA  1 
ATOM   2666 C  C   . GLU   B 1 115 ? -15.590 -16.183 3.334   1.00 16.24 ? 115 GLU   B C   1 
ATOM   2667 O  O   . GLU   B 1 115 ? -14.403 -16.454 3.257   1.00 16.64 ? 115 GLU   B O   1 
ATOM   2668 C  CB  . GLU   B 1 115 ? -16.236 -15.151 5.498   1.00 18.64 ? 115 GLU   B CB  1 
ATOM   2669 C  CG  . GLU   B 1 115 ? -16.532 -13.885 6.280   1.00 18.87 ? 115 GLU   B CG  1 
ATOM   2670 C  CD  . GLU   B 1 115 ? -16.615 -14.168 7.774   1.00 22.62 ? 115 GLU   B CD  1 
ATOM   2671 O  OE1 . GLU   B 1 115 ? -16.324 -15.311 8.189   1.00 23.56 ? 115 GLU   B OE1 1 
ATOM   2672 O  OE2 . GLU   B 1 115 ? -16.954 -13.220 8.488   1.00 23.34 ? 115 GLU   B OE2 1 
ATOM   2673 N  N   . GLN   B 1 116 ? -16.543 -16.989 2.880   1.00 15.51 ? 116 GLN   B N   1 
ATOM   2674 C  CA  . GLN   B 1 116 ? -16.247 -18.353 2.468   1.00 16.86 ? 116 GLN   B CA  1 
ATOM   2675 C  C   . GLN   B 1 116 ? -15.396 -18.330 1.202   1.00 15.11 ? 116 GLN   B C   1 
ATOM   2676 O  O   . GLN   B 1 116 ? -14.488 -19.159 1.054   1.00 15.40 ? 116 GLN   B O   1 
ATOM   2677 C  CB  . GLN   B 1 116 ? -17.513 -19.183 2.224   1.00 18.39 ? 116 GLN   B CB  1 
ATOM   2678 C  CG  . GLN   B 1 116 ? -17.254 -20.674 1.997   1.00 22.33 ? 116 GLN   B CG  1 
ATOM   2679 C  CD  . GLN   B 1 116 ? -16.567 -21.357 3.170   1.00 25.70 ? 116 GLN   B CD  1 
ATOM   2680 O  OE1 . GLN   B 1 116 ? -16.949 -21.177 4.324   1.00 27.59 ? 116 GLN   B OE1 1 
ATOM   2681 N  NE2 . GLN   B 1 116 ? -15.502 -22.107 2.933   1.00 28.62 ? 116 GLN   B NE2 1 
ATOM   2682 N  N   . VAL   B 1 117 ? -15.675 -17.412 0.284   1.00 13.64 ? 117 VAL   B N   1 
ATOM   2683 C  CA  . VAL   B 1 117 ? -14.968 -17.450 -0.978  1.00 13.55 ? 117 VAL   B CA  1 
ATOM   2684 C  C   . VAL   B 1 117 ? -13.482 -17.105 -0.751  1.00 13.94 ? 117 VAL   B C   1 
ATOM   2685 O  O   . VAL   B 1 117 ? -12.615 -17.628 -1.445  1.00 13.95 ? 117 VAL   B O   1 
ATOM   2686 C  CB  . VAL   B 1 117 ? -15.597 -16.571 -2.079  1.00 15.19 ? 117 VAL   B CB  1 
ATOM   2687 C  CG1 . VAL   B 1 117 ? -15.529 -15.073 -1.770  1.00 15.80 ? 117 VAL   B CG1 1 
ATOM   2688 C  CG2 . VAL   B 1 117 ? -14.980 -16.878 -3.439  1.00 16.48 ? 117 VAL   B CG2 1 
ATOM   2689 N  N   . GLY   B 1 118 ? -13.198 -16.184 0.177   1.00 12.65 ? 118 GLY   B N   1 
ATOM   2690 C  CA  . GLY   B 1 118 ? -11.819 -15.854 0.538   1.00 12.40 ? 118 GLY   B CA  1 
ATOM   2691 C  C   . GLY   B 1 118 ? -11.073 -17.069 1.067   1.00 12.12 ? 118 GLY   B C   1 
ATOM   2692 O  O   . GLY   B 1 118 ? -9.932  -17.355 0.696   1.00 13.14 ? 118 GLY   B O   1 
ATOM   2693 N  N   . PHE   B 1 119 ? -11.757 -17.819 1.942   1.00 12.35 ? 119 PHE   B N   1 
ATOM   2694 C  CA  . PHE   B 1 119 ? -11.179 -19.021 2.504   1.00 12.59 ? 119 PHE   B CA  1 
ATOM   2695 C  C   . PHE   B 1 119 ? -10.869 -19.998 1.367   1.00 12.48 ? 119 PHE   B C   1 
ATOM   2696 O  O   . PHE   B 1 119 ? -9.779  -20.568 1.288   1.00 11.95 ? 119 PHE   B O   1 
ATOM   2697 C  CB  . PHE   B 1 119 ? -12.113 -19.624 3.546   1.00 13.63 ? 119 PHE   B CB  1 
ATOM   2698 C  CG  . PHE   B 1 119 ? -11.561 -20.913 4.125   1.00 14.64 ? 119 PHE   B CG  1 
ATOM   2699 C  CD1 . PHE   B 1 119 ? -10.716 -20.899 5.229   1.00 15.30 ? 119 PHE   B CD1 1 
ATOM   2700 C  CD2 . PHE   B 1 119 ? -11.827 -22.128 3.522   1.00 15.34 ? 119 PHE   B CD2 1 
ATOM   2701 C  CE1 . PHE   B 1 119 ? -10.147 -22.070 5.697   1.00 16.14 ? 119 PHE   B CE1 1 
ATOM   2702 C  CE2 . PHE   B 1 119 ? -11.276 -23.305 4.008   1.00 17.58 ? 119 PHE   B CE2 1 
ATOM   2703 C  CZ  . PHE   B 1 119 ? -10.468 -23.271 5.119   1.00 17.60 ? 119 PHE   B CZ  1 
ATOM   2704 N  N   . ASP   B 1 120 ? -11.872 -20.239 0.524   1.00 12.54 ? 120 ASP   B N   1 
ATOM   2705 C  CA  . ASP   B 1 120 ? -11.754 -21.231 -0.525  1.00 12.80 ? 120 ASP   B CA  1 
ATOM   2706 C  C   . ASP   B 1 120 ? -10.677 -20.830 -1.540  1.00 12.70 ? 120 ASP   B C   1 
ATOM   2707 O  O   . ASP   B 1 120 ? -9.945  -21.692 -2.036  1.00 12.50 ? 120 ASP   B O   1 
ATOM   2708 C  CB  . ASP   B 1 120 ? -13.095 -21.464 -1.191  1.00 14.96 ? 120 ASP   B CB  1 
ATOM   2709 C  CG  . ASP   B 1 120 ? -14.121 -22.173 -0.324  1.00 18.78 ? 120 ASP   B CG  1 
ATOM   2710 O  OD1 . ASP   B 1 120 ? -13.702 -22.838 0.632   1.00 22.36 ? 120 ASP   B OD1 1 
ATOM   2711 O  OD2 . ASP   B 1 120 ? -15.319 -22.087 -0.659  1.00 21.33 ? 120 ASP   B OD2 1 
ATOM   2712 N  N   . LEU   B 1 121 ? -10.628 -19.549 -1.882  1.00 11.88 ? 121 LEU   B N   1 
ATOM   2713 C  CA  . LEU   B 1 121 ? -9.666  -19.087 -2.875  1.00 11.58 ? 121 LEU   B CA  1 
ATOM   2714 C  C   . LEU   B 1 121 ? -8.249  -19.267 -2.341  1.00 10.75 ? 121 LEU   B C   1 
ATOM   2715 O  O   . LEU   B 1 121 ? -7.371  -19.825 -3.018  1.00 11.11 ? 121 LEU   B O   1 
ATOM   2716 C  CB  . LEU   B 1 121 ? -9.973  -17.645 -3.284  1.00 11.32 ? 121 LEU   B CB  1 
ATOM   2717 C  CG  . LEU   B 1 121 ? -9.186  -17.129 -4.485  1.00 11.54 ? 121 LEU   B CG  1 
ATOM   2718 C  CD1 . LEU   B 1 121 ? -10.022 -16.102 -5.184  1.00 12.85 ? 121 LEU   B CD1 1 
ATOM   2719 C  CD2 . LEU   B 1 121 ? -7.837  -16.537 -4.079  1.00 11.86 ? 121 LEU   B CD2 1 
ATOM   2720 N  N   . VAL   B 1 122 ? -8.003  -18.810 -1.105  1.00 10.70 ? 122 VAL   B N   1 
ATOM   2721 C  CA  . VAL   B 1 122 ? -6.681  -18.918 -0.527  1.00 10.97 ? 122 VAL   B CA  1 
ATOM   2722 C  C   . VAL   B 1 122 ? -6.313  -20.384 -0.409  1.00 11.82 ? 122 VAL   B C   1 
ATOM   2723 O  O   . VAL   B 1 122 ? -5.185  -20.754 -0.694  1.00 11.85 ? 122 VAL   B O   1 
ATOM   2724 C  CB  . VAL   B 1 122 ? -6.566  -18.201 0.824   1.00 10.88 ? 122 VAL   B CB  1 
ATOM   2725 C  CG1 . VAL   B 1 122 ? -5.264  -18.523 1.550   1.00 11.06 ? 122 VAL   B CG1 1 
ATOM   2726 C  CG2 . VAL   B 1 122 ? -6.725  -16.718 0.624   1.00 11.34 ? 122 VAL   B CG2 1 
ATOM   2727 N  N   . LYS   B 1 123 ? -7.255  -21.215 0.055   1.00 12.83 ? 123 LYS   B N   1 
ATOM   2728 C  CA  . LYS   B 1 123 ? -6.925  -22.606 0.299   1.00 14.28 ? 123 LYS   B CA  1 
ATOM   2729 C  C   . LYS   B 1 123 ? -6.553  -23.299 -1.012  1.00 13.71 ? 123 LYS   B C   1 
ATOM   2730 O  O   . LYS   B 1 123 ? -5.602  -24.079 -1.048  1.00 13.96 ? 123 LYS   B O   1 
ATOM   2731 C  CB  . LYS   B 1 123 ? -8.131  -23.282 0.949   1.00 16.76 ? 123 LYS   B CB  1 
ATOM   2732 C  CG  . LYS   B 1 123 ? -7.886  -24.750 1.251   1.00 20.72 ? 123 LYS   B CG  1 
ATOM   2733 C  CD  . LYS   B 1 123 ? -8.973  -25.315 2.145   1.00 25.30 ? 123 LYS   B CD  1 
ATOM   2734 C  CE  . LYS   B 1 123 ? -8.866  -26.767 2.486   1.00 31.42 ? 123 LYS   B CE  1 
ATOM   2735 N  NZ  . LYS   B 1 123 ? -9.007  -27.594 1.296   1.00 35.42 ? 123 LYS   B NZ  1 
ATOM   2736 N  N   . ALA   B 1 124 ? -7.306  -23.019 -2.077  1.00 13.08 ? 124 ALA   B N   1 
ATOM   2737 C  CA  . ALA   B 1 124 ? -7.011  -23.640 -3.361  1.00 12.50 ? 124 ALA   B CA  1 
ATOM   2738 C  C   . ALA   B 1 124 ? -5.592  -23.265 -3.812  1.00 12.20 ? 124 ALA   B C   1 
ATOM   2739 O  O   . ALA   B 1 124 ? -4.820  -24.106 -4.260  1.00 12.43 ? 124 ALA   B O   1 
ATOM   2740 C  CB  . ALA   B 1 124 ? -8.031  -23.221 -4.366  1.00 12.27 ? 124 ALA   B CB  1 
ATOM   2741 N  N   . CYS   B 1 125 ? -5.259  -21.975 -3.719  1.00 11.47 ? 125 CYS   B N   1 
ATOM   2742 C  CA  . CYS   B 1 125 ? -3.945  -21.498 -4.115  1.00 11.85 ? 125 CYS   B CA  1 
ATOM   2743 C  C   . CYS   B 1 125 ? -2.845  -22.061 -3.220  1.00 11.59 ? 125 CYS   B C   1 
ATOM   2744 O  O   . CYS   B 1 125 ? -1.762  -22.400 -3.703  1.00 11.91 ? 125 CYS   B O   1 
ATOM   2745 C  CB  . CYS   B 1 125 ? -3.919  -19.988 -4.166  1.00 12.54 ? 125 CYS   B CB  1 
ATOM   2746 S  SG  . CYS   B 1 125 ? -4.983  -19.305 -5.472  1.00 14.02 ? 125 CYS   B SG  1 
ATOM   2747 N  N   . LYS   B 1 126 ? -3.103  -22.141 -1.907  1.00 11.66 ? 126 LYS   B N   1 
ATOM   2748 C  CA  . LYS   B 1 126 ? -2.149  -22.714 -0.979  1.00 12.62 ? 126 LYS   B CA  1 
ATOM   2749 C  C   . LYS   B 1 126 ? -1.867  -24.173 -1.330  1.00 12.87 ? 126 LYS   B C   1 
ATOM   2750 O  O   . LYS   B 1 126 ? -0.712  -24.598 -1.313  1.00 12.64 ? 126 LYS   B O   1 
ATOM   2751 C  CB  . LYS   B 1 126 ? -2.610  -22.619 0.480   1.00 13.51 ? 126 LYS   B CB  1 
ATOM   2752 C  CG  . LYS   B 1 126 ? -1.708  -23.367 1.470   1.00 14.26 ? 126 LYS   B CG  1 
ATOM   2753 C  CD  . LYS   B 1 126 ? -0.264  -22.902 1.515   1.00 15.94 ? 126 LYS   B CD  1 
ATOM   2754 C  CE  . LYS   B 1 126 ? 0.615   -23.750 2.445   1.00 18.08 ? 126 LYS   B CE  1 
ATOM   2755 N  NZ  . LYS   B 1 126 ? 0.504   -23.264 3.798   1.00 22.16 ? 126 LYS   B NZ  1 
ATOM   2756 N  N   . GLU   B 1 127 ? -2.903  -24.925 -1.667  1.00 13.83 ? 127 GLU   B N   1 
ATOM   2757 C  CA  . GLU   B 1 127 ? -2.729  -26.334 -1.949  1.00 16.30 ? 127 GLU   B CA  1 
ATOM   2758 C  C   . GLU   B 1 127 ? -1.807  -26.497 -3.145  1.00 14.77 ? 127 GLU   B C   1 
ATOM   2759 O  O   . GLU   B 1 127 ? -0.954  -27.374 -3.143  1.00 14.50 ? 127 GLU   B O   1 
ATOM   2760 C  CB  . GLU   B 1 127 ? -4.081  -27.025 -2.080  1.00 18.75 ? 127 GLU   B CB  1 
ATOM   2761 C  CG  . GLU   B 1 127 ? -4.665  -27.178 -0.676  1.00 24.81 ? 127 GLU   B CG  1 
ATOM   2762 C  CD  . GLU   B 1 127 ? -6.046  -27.762 -0.533  1.00 34.85 ? 127 GLU   B CD  1 
ATOM   2763 O  OE1 . GLU   B 1 127 ? -6.730  -27.938 -1.546  1.00 48.08 ? 127 GLU   B OE1 1 
ATOM   2764 O  OE2 . GLU   B 1 127 ? -6.431  -28.017 0.628   1.00 42.73 ? 127 GLU   B OE2 1 
ATOM   2765 N  N   . ALA   B 1 128 ? -2.005  -25.654 -4.168  1.00 14.01 ? 128 ALA   B N   1 
ATOM   2766 C  CA  . ALA   B 1 128 ? -1.185  -25.747 -5.360  1.00 13.64 ? 128 ALA   B CA  1 
ATOM   2767 C  C   . ALA   B 1 128 ? 0.260   -25.400 -5.014  1.00 12.81 ? 128 ALA   B C   1 
ATOM   2768 O  O   . ALA   B 1 128 ? 1.194   -26.099 -5.405  1.00 12.81 ? 128 ALA   B O   1 
ATOM   2769 C  CB  . ALA   B 1 128 ? -1.747  -24.863 -6.444  1.00 13.56 ? 128 ALA   B CB  1 
ATOM   2770 N  N   . CYS   B 1 129 ? 0.448   -24.310 -4.269  1.00 11.45 ? 129 CYS   B N   1 
ATOM   2771 C  CA  . CYS   B 1 129 ? 1.768   -23.874 -3.867  1.00 11.53 ? 129 CYS   B CA  1 
ATOM   2772 C  C   . CYS   B 1 129 ? 2.473   -24.934 -3.009  1.00 12.39 ? 129 CYS   B C   1 
ATOM   2773 O  O   . CYS   B 1 129 ? 3.655   -25.262 -3.233  1.00 13.70 ? 129 CYS   B O   1 
ATOM   2774 C  CB  . CYS   B 1 129 ? 1.691   -22.549 -3.132  1.00 11.95 ? 129 CYS   B CB  1 
ATOM   2775 S  SG  . CYS   B 1 129 ? 1.354   -21.173 -4.244  1.00 12.66 ? 129 CYS   B SG  1 
ATOM   2776 N  N   . ALA   B 1 130 ? 1.754   -25.465 -2.016  1.00 13.08 ? 130 ALA   B N   1 
ATOM   2777 C  CA  . ALA   B 1 130 ? 2.345   -26.406 -1.078  1.00 14.30 ? 130 ALA   B CA  1 
ATOM   2778 C  C   . ALA   B 1 130 ? 2.865   -27.646 -1.808  1.00 16.20 ? 130 ALA   B C   1 
ATOM   2779 O  O   . ALA   B 1 130 ? 3.930   -28.163 -1.469  1.00 15.17 ? 130 ALA   B O   1 
ATOM   2780 C  CB  . ALA   B 1 130 ? 1.371   -26.810 -0.002  1.00 15.07 ? 130 ALA   B CB  1 
ATOM   2781 N  N   . ALA   B 1 131 ? 2.098   -28.101 -2.795  1.00 16.22 ? 131 ALA   B N   1 
ATOM   2782 C  CA  . ALA   B 1 131 ? 2.477   -29.258 -3.594  1.00 18.57 ? 131 ALA   B CA  1 
ATOM   2783 C  C   . ALA   B 1 131 ? 3.807   -29.048 -4.314  1.00 18.27 ? 131 ALA   B C   1 
ATOM   2784 O  O   . ALA   B 1 131 ? 4.456   -30.022 -4.670  1.00 18.94 ? 131 ALA   B O   1 
ATOM   2785 C  CB  . ALA   B 1 131 ? 1.383   -29.562 -4.587  1.00 19.56 ? 131 ALA   B CB  1 
ATOM   2786 N  N   . ALA   B 1 132 ? 4.197   -27.795 -4.575  1.00 16.27 ? 132 ALA   B N   1 
ATOM   2787 C  CA  . ALA   B 1 132 ? 5.419   -27.480 -5.294  1.00 16.03 ? 132 ALA   B CA  1 
ATOM   2788 C  C   . ALA   B 1 132 ? 6.500   -26.887 -4.395  1.00 16.19 ? 132 ALA   B C   1 
ATOM   2789 O  O   . ALA   B 1 132 ? 7.481   -26.330 -4.908  1.00 16.66 ? 132 ALA   B O   1 
ATOM   2790 C  CB  . ALA   B 1 132 ? 5.061   -26.469 -6.394  1.00 16.50 ? 132 ALA   B CB  1 
ATOM   2791 N  N   . ASN   B 1 133 ? 6.283   -26.890 -3.066  1.00 15.34 ? 133 ASN   B N   1 
ATOM   2792 C  CA  . ASN   B 1 133 ? 7.178   -26.243 -2.111  1.00 16.77 ? 133 ASN   B CA  1 
ATOM   2793 C  C   . ASN   B 1 133 ? 7.362   -24.750 -2.417  1.00 15.95 ? 133 ASN   B C   1 
ATOM   2794 O  O   . ASN   B 1 133 ? 8.459   -24.190 -2.308  1.00 16.42 ? 133 ASN   B O   1 
ATOM   2795 C  CB  . ASN   B 1 133 ? 8.528   -26.943 -2.039  1.00 20.20 ? 133 ASN   B CB  1 
ATOM   2796 C  CG  . ASN   B 1 133 ? 8.414   -28.348 -1.494  1.00 26.15 ? 133 ASN   B CG  1 
ATOM   2797 O  OD1 . ASN   B 1 133 ? 8.723   -29.315 -2.198  1.00 36.13 ? 133 ASN   B OD1 1 
ATOM   2798 N  ND2 . ASN   B 1 133 ? 7.956   -28.489 -0.265  1.00 29.28 ? 133 ASN   B ND2 1 
ATOM   2799 N  N   . VAL   B 1 134 ? 6.262   -24.099 -2.776  1.00 12.30 ? 134 VAL   B N   1 
ATOM   2800 C  CA  . VAL   B 1 134 ? 6.246   -22.665 -3.055  1.00 12.14 ? 134 VAL   B CA  1 
ATOM   2801 C  C   . VAL   B 1 134 ? 5.498   -21.993 -1.915  1.00 12.43 ? 134 VAL   B C   1 
ATOM   2802 O  O   . VAL   B 1 134 ? 4.479   -22.508 -1.433  1.00 12.63 ? 134 VAL   B O   1 
ATOM   2803 C  CB  . VAL   B 1 134 ? 5.539   -22.464 -4.409  1.00 11.55 ? 134 VAL   B CB  1 
ATOM   2804 C  CG1 . VAL   B 1 134 ? 5.031   -21.062 -4.672  1.00 11.01 ? 134 VAL   B CG1 1 
ATOM   2805 C  CG2 . VAL   B 1 134 ? 6.393   -22.971 -5.561  1.00 12.80 ? 134 VAL   B CG2 1 
ATOM   2806 N  N   . LEU   B 1 135 ? 6.011   -20.841 -1.484  1.00 12.91 ? 135 LEU   B N   1 
ATOM   2807 C  CA  . LEU   B 1 135 ? 5.352   -20.100 -0.431  1.00 13.26 ? 135 LEU   B CA  1 
ATOM   2808 C  C   . LEU   B 1 135 ? 4.210   -19.272 -1.017  1.00 12.26 ? 135 LEU   B C   1 
ATOM   2809 O  O   . LEU   B 1 135 ? 4.368   -18.666 -2.082  1.00 12.41 ? 135 LEU   B O   1 
ATOM   2810 C  CB  . LEU   B 1 135 ? 6.339   -19.185 0.279   1.00 17.44 ? 135 LEU   B CB  1 
ATOM   2811 C  CG  . LEU   B 1 135 ? 7.349   -19.813 1.247   1.00 22.46 ? 135 LEU   B CG  1 
ATOM   2812 C  CD1 . LEU   B 1 135 ? 7.790   -18.626 2.101   1.00 22.80 ? 135 LEU   B CD1 1 
ATOM   2813 C  CD2 . LEU   B 1 135 ? 6.850   -20.939 2.132   1.00 24.08 ? 135 LEU   B CD2 1 
ATOM   2814 N  N   . LEU   B 1 136 ? 3.123   -19.176 -0.253  1.00 11.03 ? 136 LEU   B N   1 
ATOM   2815 C  CA  . LEU   B 1 136 ? 1.991   -18.346 -0.631  1.00 11.04 ? 136 LEU   B CA  1 
ATOM   2816 C  C   . LEU   B 1 136 ? 1.890   -17.146 0.307   1.00 10.30 ? 136 LEU   B C   1 
ATOM   2817 O  O   . LEU   B 1 136 ? 1.656   -17.305 1.507   1.00 11.34 ? 136 LEU   B O   1 
ATOM   2818 C  CB  . LEU   B 1 136 ? 0.681   -19.117 -0.667  1.00 11.69 ? 136 LEU   B CB  1 
ATOM   2819 C  CG  . LEU   B 1 136 ? -0.547  -18.310 -1.099  1.00 12.54 ? 136 LEU   B CG  1 
ATOM   2820 C  CD1 . LEU   B 1 136 ? -0.541  -18.083 -2.594  1.00 13.42 ? 136 LEU   B CD1 1 
ATOM   2821 C  CD2 . LEU   B 1 136 ? -1.815  -18.986 -0.642  1.00 14.01 ? 136 LEU   B CD2 1 
ATOM   2822 N  N   . LYS   B 1 137 ? 1.941   -15.956 -0.281  1.00 9.65  ? 137 LYS   B N   1 
ATOM   2823 C  CA  . LYS   B 1 137 ? 1.605   -14.745 0.438   1.00 10.06 ? 137 LYS   B CA  1 
ATOM   2824 C  C   . LYS   B 1 137 ? 0.203   -14.353 -0.003  1.00 10.56 ? 137 LYS   B C   1 
ATOM   2825 O  O   . LYS   B 1 137 ? -0.161  -14.490 -1.169  1.00 11.51 ? 137 LYS   B O   1 
ATOM   2826 C  CB  . LYS   B 1 137 ? 2.537   -13.559 0.124   1.00 11.11 ? 137 LYS   B CB  1 
ATOM   2827 C  CG  . LYS   B 1 137 ? 4.023   -13.893 0.200   1.00 11.58 ? 137 LYS   B CG  1 
ATOM   2828 C  CD  . LYS   B 1 137 ? 4.919   -12.674 0.391   1.00 12.39 ? 137 LYS   B CD  1 
ATOM   2829 C  CE  . LYS   B 1 137 ? 6.366   -12.965 0.083   1.00 13.84 ? 137 LYS   B CE  1 
ATOM   2830 N  NZ  . LYS   B 1 137 ? 6.670   -12.910 -1.376  1.00 13.92 ? 137 LYS   B NZ  1 
ATOM   2831 N  N   . VAL   B 1 138 ? -0.561  -13.793 0.931   1.00 9.29  ? 138 VAL   B N   1 
ATOM   2832 C  CA  . VAL   B 1 138 ? -1.902  -13.357 0.615   1.00 9.71  ? 138 VAL   B CA  1 
ATOM   2833 C  C   . VAL   B 1 138 ? -1.996  -11.859 0.844   1.00 9.37  ? 138 VAL   B C   1 
ATOM   2834 O  O   . VAL   B 1 138 ? -1.814  -11.380 1.968   1.00 9.43  ? 138 VAL   B O   1 
ATOM   2835 C  CB  . VAL   B 1 138 ? -2.991  -14.085 1.421   1.00 9.47  ? 138 VAL   B CB  1 
ATOM   2836 C  CG1 . VAL   B 1 138 ? -4.361  -13.548 1.067   1.00 9.77  ? 138 VAL   B CG1 1 
ATOM   2837 C  CG2 . VAL   B 1 138 ? -2.923  -15.579 1.177   1.00 9.44  ? 138 VAL   B CG2 1 
ATOM   2838 N  N   . ILE   B 1 139 ? -2.301  -11.141 -0.246  1.00 9.17  ? 139 ILE   B N   1 
ATOM   2839 C  CA  . ILE   B 1 139 ? -2.506  -9.707  -0.174  1.00 9.99  ? 139 ILE   B CA  1 
ATOM   2840 C  C   . ILE   B 1 139 ? -3.950  -9.414  0.226   1.00 10.32 ? 139 ILE   B C   1 
ATOM   2841 O  O   . ILE   B 1 139 ? -4.854  -9.704  -0.544  1.00 10.98 ? 139 ILE   B O   1 
ATOM   2842 C  CB  . ILE   B 1 139 ? -2.185  -9.045  -1.523  1.00 10.69 ? 139 ILE   B CB  1 
ATOM   2843 C  CG1 . ILE   B 1 139 ? -0.768  -9.315  -1.978  1.00 11.65 ? 139 ILE   B CG1 1 
ATOM   2844 C  CG2 . ILE   B 1 139 ? -2.482  -7.540  -1.439  1.00 10.45 ? 139 ILE   B CG2 1 
ATOM   2845 C  CD1 . ILE   B 1 139 ? -0.583  -9.110  -3.477  1.00 11.62 ? 139 ILE   B CD1 1 
ATOM   2846 N  N   . ILE   B 1 140 ? -4.170  -8.728  1.359   1.00 10.24 ? 140 ILE   B N   1 
ATOM   2847 C  CA  . ILE   B 1 140 ? -5.536  -8.485  1.798   1.00 10.67 ? 140 ILE   B CA  1 
ATOM   2848 C  C   . ILE   B 1 140 ? -6.055  -7.107  1.394   1.00 10.32 ? 140 ILE   B C   1 
ATOM   2849 O  O   . ILE   B 1 140 ? -7.277  -6.910  1.443   1.00 11.26 ? 140 ILE   B O   1 
ATOM   2850 C  CB  . ILE   B 1 140 ? -5.718  -8.732  3.303   1.00 10.83 ? 140 ILE   B CB  1 
ATOM   2851 C  CG1 . ILE   B 1 140 ? -4.897  -7.759  4.121   1.00 11.25 ? 140 ILE   B CG1 1 
ATOM   2852 C  CG2 . ILE   B 1 140 ? -5.432  -10.186 3.664   1.00 11.87 ? 140 ILE   B CG2 1 
ATOM   2853 C  CD1 . ILE   B 1 140 ? -5.285  -7.790  5.587   1.00 12.50 ? 140 ILE   B CD1 1 
ATOM   2854 N  N   . GLU   B 1 141 ? -5.167  -6.202  0.956   1.00 9.56  ? 141 GLU   B N   1 
ATOM   2855 C  CA  . GLU   B 1 141 ? -5.522  -4.859  0.524   1.00 10.60 ? 141 GLU   B CA  1 
ATOM   2856 C  C   . GLU   B 1 141 ? -6.133  -4.044  1.662   1.00 10.41 ? 141 GLU   B C   1 
ATOM   2857 O  O   . GLU   B 1 141 ? -7.284  -3.591  1.593   1.00 10.84 ? 141 GLU   B O   1 
ATOM   2858 C  CB  . GLU   B 1 141 ? -6.406  -4.890  -0.730  1.00 11.85 ? 141 GLU   B CB  1 
ATOM   2859 C  CG  . GLU   B 1 141 ? -6.276  -3.620  -1.565  1.00 12.75 ? 141 GLU   B CG  1 
ATOM   2860 C  CD  . GLU   B 1 141 ? -4.953  -3.458  -2.305  1.00 12.46 ? 141 GLU   B CD  1 
ATOM   2861 O  OE1 . GLU   B 1 141 ? -3.885  -3.253  -1.637  1.00 12.35 ? 141 GLU   B OE1 1 
ATOM   2862 O  OE2 . GLU   B 1 141 ? -4.960  -3.620  -3.543  1.00 13.40 ? 141 GLU   B OE2 1 
ATOM   2863 N  N   . THR   B 1 142 ? -5.304  -3.777  2.665   1.00 10.16 ? 142 THR   B N   1 
ATOM   2864 C  CA  . THR   B 1 142 ? -5.726  -3.055  3.852   1.00 11.41 ? 142 THR   B CA  1 
ATOM   2865 C  C   . THR   B 1 142 ? -6.294  -1.682  3.492   1.00 11.60 ? 142 THR   B C   1 
ATOM   2866 O  O   . THR   B 1 142 ? -7.194  -1.205  4.172   1.00 12.59 ? 142 THR   B O   1 
ATOM   2867 C  CB  . THR   B 1 142 ? -4.567  -2.913  4.850   1.00 11.33 ? 142 THR   B CB  1 
ATOM   2868 O  OG1 . THR   B 1 142 ? -3.498  -2.296  4.168   1.00 11.40 ? 142 THR   B OG1 1 
ATOM   2869 C  CG2 . THR   B 1 142 ? -4.154  -4.243  5.439   1.00 11.72 ? 142 THR   B CG2 1 
ATOM   2870 N  N   . GLY   B 1 143 ? -5.752  -1.050  2.460   1.00 12.62 ? 143 GLY   B N   1 
ATOM   2871 C  CA  . GLY   B 1 143 ? -6.176  0.285   2.086   1.00 13.06 ? 143 GLY   B CA  1 
ATOM   2872 C  C   . GLY   B 1 143 ? -7.558  0.326   1.439   1.00 14.59 ? 143 GLY   B C   1 
ATOM   2873 O  O   . GLY   B 1 143 ? -8.146  1.402   1.381   1.00 15.71 ? 143 GLY   B O   1 
ATOM   2874 N  N   . GLU   B 1 144 ? -8.080  -0.832  0.993   1.00 13.14 ? 144 GLU   B N   1 
ATOM   2875 C  CA  . GLU   B 1 144 ? -9.460  -0.926  0.544   1.00 13.22 ? 144 GLU   B CA  1 
ATOM   2876 C  C   . GLU   B 1 144 ? -10.388 -1.408  1.655   1.00 13.74 ? 144 GLU   B C   1 
ATOM   2877 O  O   . GLU   B 1 144 ? -11.500 -0.908  1.761   1.00 14.95 ? 144 GLU   B O   1 
ATOM   2878 C  CB  . GLU   B 1 144 ? -9.562  -1.769  -0.724  1.00 14.73 ? 144 GLU   B CB  1 
ATOM   2879 C  CG  . GLU   B 1 144 ? -8.909  -1.138  -1.943  1.00 15.55 ? 144 GLU   B CG  1 
ATOM   2880 C  CD  . GLU   B 1 144 ? -9.544  0.182   -2.360  1.00 18.58 ? 144 GLU   B CD  1 
ATOM   2881 O  OE1 . GLU   B 1 144 ? -10.787 0.253   -2.367  1.00 20.94 ? 144 GLU   B OE1 1 
ATOM   2882 O  OE2 . GLU   B 1 144 ? -8.786  1.101   -2.703  1.00 18.74 ? 144 GLU   B OE2 1 
ATOM   2883 N  N   . LEU   B 1 145 ? -9.937  -2.359  2.482   1.00 13.14 ? 145 LEU   B N   1 
ATOM   2884 C  CA  . LEU   B 1 145 ? -10.739 -2.831  3.614   1.00 13.59 ? 145 LEU   B CA  1 
ATOM   2885 C  C   . LEU   B 1 145 ? -10.987 -1.710  4.621   1.00 14.21 ? 145 LEU   B C   1 
ATOM   2886 O  O   . LEU   B 1 145 ? -12.100 -1.589  5.125   1.00 16.47 ? 145 LEU   B O   1 
ATOM   2887 C  CB  . LEU   B 1 145 ? -10.017 -3.988  4.300   1.00 12.98 ? 145 LEU   B CB  1 
ATOM   2888 C  CG  . LEU   B 1 145 ? -9.891  -5.272  3.476   1.00 13.62 ? 145 LEU   B CG  1 
ATOM   2889 C  CD1 . LEU   B 1 145 ? -9.027  -6.259  4.209   1.00 13.63 ? 145 LEU   B CD1 1 
ATOM   2890 C  CD2 . LEU   B 1 145 ? -11.260 -5.859  3.147   1.00 14.39 ? 145 LEU   B CD2 1 
ATOM   2891 N  N   . LYS   B 1 146 ? -9.916  -0.977  4.965   1.00 16.02 ? 146 LYS   B N   1 
ATOM   2892 C  CA  . LYS   B 1 146 ? -9.941  0.241   5.785   1.00 18.78 ? 146 LYS   B CA  1 
ATOM   2893 C  C   . LYS   B 1 146 ? -10.238 -0.019  7.262   1.00 18.89 ? 146 LYS   B C   1 
ATOM   2894 O  O   . LYS   B 1 146 ? -9.451  0.363   8.135   1.00 20.30 ? 146 LYS   B O   1 
ATOM   2895 C  CB  . LYS   B 1 146 ? -10.914 1.274   5.214   1.00 22.38 ? 146 LYS   B CB  1 
ATOM   2896 C  CG  . LYS   B 1 146 ? -10.376 1.850   3.906   1.00 28.55 ? 146 LYS   B CG  1 
ATOM   2897 C  CD  . LYS   B 1 146 ? -11.399 2.710   3.165   1.00 35.60 ? 146 LYS   B CD  1 
ATOM   2898 C  CE  . LYS   B 1 146 ? -10.903 3.106   1.792   1.00 39.80 ? 146 LYS   B CE  1 
ATOM   2899 N  NZ  . LYS   B 1 146 ? -9.698  3.935   1.920   1.00 42.02 ? 146 LYS   B NZ  1 
ATOM   2900 N  N   . ASP   B 1 147 ? -11.329 -0.722  7.519   1.00 18.26 ? 147 ASP   B N   1 
ATOM   2901 C  CA  . ASP   B 1 147 ? -11.807 -0.959  8.862   1.00 18.71 ? 147 ASP   B CA  1 
ATOM   2902 C  C   . ASP   B 1 147 ? -10.944 -2.009  9.554   1.00 16.67 ? 147 ASP   B C   1 
ATOM   2903 O  O   . ASP   B 1 147 ? -10.644 -3.066  8.988   1.00 14.90 ? 147 ASP   B O   1 
ATOM   2904 C  CB  . ASP   B 1 147 ? -13.251 -1.400  8.773   1.00 22.41 ? 147 ASP   B CB  1 
ATOM   2905 C  CG  . ASP   B 1 147 ? -13.796 -1.936  10.072  1.00 30.66 ? 147 ASP   B CG  1 
ATOM   2906 O  OD1 . ASP   B 1 147 ? -14.119 -1.105  10.934  1.00 40.77 ? 147 ASP   B OD1 1 
ATOM   2907 O  OD2 . ASP   B 1 147 ? -13.798 -3.173  10.226  1.00 41.99 ? 147 ASP   B OD2 1 
ATOM   2908 N  N   . GLU   B 1 148 ? -10.590 -1.726  10.817  1.00 17.28 ? 148 GLU   B N   1 
ATOM   2909 C  CA  . GLU   B 1 148 ? -9.781  -2.634  11.613  1.00 17.51 ? 148 GLU   B CA  1 
ATOM   2910 C  C   . GLU   B 1 148 ? -10.387 -4.040  11.655  1.00 16.13 ? 148 GLU   B C   1 
ATOM   2911 O  O   . GLU   B 1 148 ? -9.659  -5.023  11.487  1.00 14.47 ? 148 GLU   B O   1 
ATOM   2912 C  CB  . GLU   B 1 148 ? -9.567  -2.079  13.024  1.00 19.41 ? 148 GLU   B CB  1 
ATOM   2913 C  CG  . GLU   B 1 148 ? -8.865  -3.088  13.919  1.00 22.10 ? 148 GLU   B CG  1 
ATOM   2914 C  CD  . GLU   B 1 148 ? -8.335  -2.558  15.241  1.00 28.57 ? 148 GLU   B CD  1 
ATOM   2915 O  OE1 . GLU   B 1 148 ? -8.396  -1.335  15.457  1.00 29.20 ? 148 GLU   B OE1 1 
ATOM   2916 O  OE2 . GLU   B 1 148 ? -7.811  -3.396  15.996  1.00 32.97 ? 148 GLU   B OE2 1 
ATOM   2917 N  N   . ALA   B 1 149 ? -11.699 -4.138  11.911  1.00 15.98 ? 149 ALA   B N   1 
ATOM   2918 C  CA  . ALA   B 1 149 ? -12.371 -5.425  11.988  1.00 16.61 ? 149 ALA   B CA  1 
ATOM   2919 C  C   . ALA   B 1 149 ? -12.237 -6.210  10.675  1.00 15.24 ? 149 ALA   B C   1 
ATOM   2920 O  O   . ALA   B 1 149 ? -12.015 -7.424  10.712  1.00 14.01 ? 149 ALA   B O   1 
ATOM   2921 C  CB  . ALA   B 1 149 ? -13.841 -5.275  12.412  1.00 18.28 ? 149 ALA   B CB  1 
ATOM   2922 N  N   . LEU   B 1 150 ? -12.354 -5.522  9.535   1.00 14.13 ? 150 LEU   B N   1 
ATOM   2923 C  CA  . LEU   B 1 150 ? -12.233 -6.208  8.248   1.00 14.04 ? 150 LEU   B CA  1 
ATOM   2924 C  C   . LEU   B 1 150 ? -10.793 -6.630  7.975   1.00 12.94 ? 150 LEU   B C   1 
ATOM   2925 O  O   . LEU   B 1 150 ? -10.568 -7.695  7.417   1.00 11.94 ? 150 LEU   B O   1 
ATOM   2926 C  CB  . LEU   B 1 150 ? -12.748 -5.358  7.098   1.00 15.59 ? 150 LEU   B CB  1 
ATOM   2927 C  CG  . LEU   B 1 150 ? -14.272 -5.245  6.986   1.00 18.22 ? 150 LEU   B CG  1 
ATOM   2928 C  CD1 . LEU   B 1 150 ? -14.612 -4.155  6.008   1.00 18.88 ? 150 LEU   B CD1 1 
ATOM   2929 C  CD2 . LEU   B 1 150 ? -14.871 -6.554  6.533   1.00 20.72 ? 150 LEU   B CD2 1 
ATOM   2930 N  N   . ILE   B 1 151 ? -9.822  -5.824  8.372   1.00 12.69 ? 151 ILE   B N   1 
ATOM   2931 C  CA  . ILE   B 1 151 ? -8.424  -6.209  8.211   1.00 12.40 ? 151 ILE   B CA  1 
ATOM   2932 C  C   . ILE   B 1 151 ? -8.134  -7.447  9.063   1.00 12.29 ? 151 ILE   B C   1 
ATOM   2933 O  O   . ILE   B 1 151 ? -7.473  -8.395  8.621   1.00 12.28 ? 151 ILE   B O   1 
ATOM   2934 C  CB  . ILE   B 1 151 ? -7.536  -5.012  8.583   1.00 13.09 ? 151 ILE   B CB  1 
ATOM   2935 C  CG1 . ILE   B 1 151 ? -7.729  -3.879  7.578   1.00 13.83 ? 151 ILE   B CG1 1 
ATOM   2936 C  CG2 . ILE   B 1 151 ? -6.074  -5.437  8.725   1.00 13.10 ? 151 ILE   B CG2 1 
ATOM   2937 C  CD1 . ILE   B 1 151 ? -7.026  -2.605  7.979   1.00 13.67 ? 151 ILE   B CD1 1 
ATOM   2938 N  N   . ARG   B 1 152 ? -8.637  -7.479  10.295  1.00 12.13 ? 152 ARG   B N   1 
ATOM   2939 C  CA  . ARG   B 1 152 ? -8.433  -8.658  11.135  1.00 12.95 ? 152 ARG   B CA  1 
ATOM   2940 C  C   . ARG   B 1 152 ? -9.080  -9.897  10.529  1.00 13.34 ? 152 ARG   B C   1 
ATOM   2941 O  O   . ARG   B 1 152 ? -8.476  -10.981 10.537  1.00 13.63 ? 152 ARG   B O   1 
ATOM   2942 C  CB  . ARG   B 1 152 ? -8.946  -8.485  12.566  1.00 13.74 ? 152 ARG   B CB  1 
ATOM   2943 C  CG  . ARG   B 1 152 ? -8.146  -7.462  13.356  1.00 15.70 ? 152 ARG   B CG  1 
ATOM   2944 C  CD  . ARG   B 1 152 ? -8.575  -7.425  14.835  1.00 18.30 ? 152 ARG   B CD  1 
ATOM   2945 N  NE  . ARG   B 1 152 ? -7.904  -6.327  15.501  1.00 21.74 ? 152 ARG   B NE  1 
ATOM   2946 C  CZ  . ARG   B 1 152 ? -6.636  -6.325  15.933  1.00 24.25 ? 152 ARG   B CZ  1 
ATOM   2947 N  NH1 . ARG   B 1 152 ? -5.941  -7.440  16.032  1.00 24.83 ? 152 ARG   B NH1 1 
ATOM   2948 N  NH2 . ARG   B 1 152 ? -6.100  -5.203  16.362  1.00 26.03 ? 152 ARG   B NH2 1 
ATOM   2949 N  N   . LYS   B 1 153 ? -10.311 -9.726  10.032  1.00 13.47 ? 153 LYS   B N   1 
ATOM   2950 C  CA  . LYS   B 1 153 ? -11.049 -10.844 9.496   1.00 13.17 ? 153 LYS   B CA  1 
ATOM   2951 C  C   . LYS   B 1 153 ? -10.350 -11.411 8.257   1.00 12.09 ? 153 LYS   B C   1 
ATOM   2952 O  O   . LYS   B 1 153 ? -10.225 -12.618 8.106   1.00 12.49 ? 153 LYS   B O   1 
ATOM   2953 C  CB  . LYS   B 1 153 ? -12.494 -10.480 9.164   1.00 14.79 ? 153 LYS   B CB  1 
ATOM   2954 C  CG  . LYS   B 1 153 ? -13.319 -11.659 8.689   1.00 17.78 ? 153 LYS   B CG  1 
ATOM   2955 C  CD  . LYS   B 1 153 ? -13.356 -12.805 9.683   1.00 21.73 ? 153 LYS   B CD  1 
ATOM   2956 C  CE  . LYS   B 1 153 ? -13.994 -12.391 10.999  1.00 24.30 ? 153 LYS   B CE  1 
ATOM   2957 N  NZ  . LYS   B 1 153 ? -14.159 -13.596 11.807  1.00 28.23 ? 153 LYS   B NZ  1 
ATOM   2958 N  N   . ALA   B 1 154 ? -9.932  -10.542 7.346   1.00 11.84 ? 154 ALA   B N   1 
ATOM   2959 C  CA  . ALA   B 1 154 ? -9.256  -11.009 6.144   1.00 11.33 ? 154 ALA   B CA  1 
ATOM   2960 C  C   . ALA   B 1 154 ? -7.959  -11.742 6.499   1.00 10.70 ? 154 ALA   B C   1 
ATOM   2961 O  O   . ALA   B 1 154 ? -7.599  -12.755 5.865   1.00 10.12 ? 154 ALA   B O   1 
ATOM   2962 C  CB  . ALA   B 1 154 ? -8.976  -9.836  5.209   1.00 11.91 ? 154 ALA   B CB  1 
ATOM   2963 N  N   . SER   B 1 155 ? -7.243  -11.183 7.462   1.00 10.62 ? 155 SER   B N   1 
ATOM   2964 C  CA  . SER   B 1 155 ? -6.009  -11.788 7.972   1.00 11.02 ? 155 SER   B CA  1 
ATOM   2965 C  C   . SER   B 1 155 ? -6.302  -13.177 8.538   1.00 11.44 ? 155 SER   B C   1 
ATOM   2966 O  O   . SER   B 1 155 ? -5.621  -14.150 8.191   1.00 11.65 ? 155 SER   B O   1 
ATOM   2967 C  CB  . SER   B 1 155 ? -5.306  -10.905 8.999   1.00 10.74 ? 155 SER   B CB  1 
ATOM   2968 O  OG  . SER   B 1 155 ? -4.952  -9.651  8.435   1.00 10.52 ? 155 SER   B OG  1 
ATOM   2969 N  N   . GLU   B 1 156 ? -7.345  -13.267 9.375   1.00 11.64 ? 156 GLU   B N   1 
ATOM   2970 C  CA  . GLU   B 1 156 ? -7.701  -14.524 10.013  1.00 13.35 ? 156 GLU   B CA  1 
ATOM   2971 C  C   . GLU   B 1 156 ? -8.084  -15.600 8.996   1.00 12.71 ? 156 GLU   B C   1 
ATOM   2972 O  O   . GLU   B 1 156 ? -7.632  -16.748 9.062   1.00 12.72 ? 156 GLU   B O   1 
ATOM   2973 C  CB  . GLU   B 1 156 ? -8.870  -14.263 10.973  1.00 16.79 ? 156 GLU   B CB  1 
ATOM   2974 C  CG  . GLU   B 1 156 ? -9.339  -15.541 11.651  1.00 22.15 ? 156 GLU   B CG  1 
ATOM   2975 C  CD  . GLU   B 1 156 ? -10.626 -15.400 12.453  1.00 32.57 ? 156 GLU   B CD  1 
ATOM   2976 O  OE1 . GLU   B 1 156 ? -11.405 -14.471 12.169  1.00 35.42 ? 156 GLU   B OE1 1 
ATOM   2977 O  OE2 . GLU   B 1 156 ? -10.808 -16.231 13.371  1.00 42.04 ? 156 GLU   B OE2 1 
ATOM   2978 N  N   . ILE   B 1 157 ? -8.944  -15.221 8.040   1.00 12.01 ? 157 ILE   B N   1 
ATOM   2979 C  CA  . ILE   B 1 157 ? -9.387  -16.162 7.019   1.00 11.40 ? 157 ILE   B CA  1 
ATOM   2980 C  C   . ILE   B 1 157 ? -8.178  -16.673 6.238   1.00 11.24 ? 157 ILE   B C   1 
ATOM   2981 O  O   . ILE   B 1 157 ? -8.047  -17.862 5.987   1.00 11.97 ? 157 ILE   B O   1 
ATOM   2982 C  CB  . ILE   B 1 157 ? -10.409 -15.477 6.091   1.00 11.43 ? 157 ILE   B CB  1 
ATOM   2983 C  CG1 . ILE   B 1 157 ? -11.748 -15.195 6.839   1.00 12.07 ? 157 ILE   B CG1 1 
ATOM   2984 C  CG2 . ILE   B 1 157 ? -10.651 -16.333 4.852   1.00 11.79 ? 157 ILE   B CG2 1 
ATOM   2985 C  CD1 . ILE   B 1 157 ? -12.622 -14.191 6.130   1.00 12.40 ? 157 ILE   B CD1 1 
ATOM   2986 N  N   . SER   B 1 158 ? -7.313  -15.749 5.814   1.00 10.94 ? 158 SER   B N   1 
ATOM   2987 C  CA  . SER   B 1 158 ? -6.123  -16.101 5.061   1.00 10.41 ? 158 SER   B CA  1 
ATOM   2988 C  C   . SER   B 1 158 ? -5.243  -17.091 5.820   1.00 11.03 ? 158 SER   B C   1 
ATOM   2989 O  O   . SER   B 1 158 ? -4.764  -18.073 5.279   1.00 11.33 ? 158 SER   B O   1 
ATOM   2990 C  CB  . SER   B 1 158 ? -5.359  -14.882 4.699   1.00 10.51 ? 158 SER   B CB  1 
ATOM   2991 O  OG  . SER   B 1 158 ? -6.109  -14.004 3.873   1.00 10.75 ? 158 SER   B OG  1 
ATOM   2992 N  N   . ILE   B 1 159 ? -5.044  -16.843 7.117   1.00 11.95 ? 159 ILE   B N   1 
ATOM   2993 C  CA  . ILE   B 1 159 ? -4.227  -17.715 7.931   1.00 11.72 ? 159 ILE   B CA  1 
ATOM   2994 C  C   . ILE   B 1 159 ? -4.897  -19.081 8.072   1.00 12.66 ? 159 ILE   B C   1 
ATOM   2995 O  O   . ILE   B 1 159 ? -4.222  -20.098 7.939   1.00 12.22 ? 159 ILE   B O   1 
ATOM   2996 C  CB  . ILE   B 1 159 ? -3.975  -17.044 9.286   1.00 13.11 ? 159 ILE   B CB  1 
ATOM   2997 C  CG1 . ILE   B 1 159 ? -2.993  -15.883 9.109   1.00 12.58 ? 159 ILE   B CG1 1 
ATOM   2998 C  CG2 . ILE   B 1 159 ? -3.494  -18.081 10.320  1.00 13.60 ? 159 ILE   B CG2 1 
ATOM   2999 C  CD1 . ILE   B 1 159 ? -2.860  -14.958 10.290  1.00 12.77 ? 159 ILE   B CD1 1 
ATOM   3000 N  N   . LYS   B 1 160 ? -6.203  -19.100 8.363   1.00 12.20 ? 160 LYS   B N   1 
ATOM   3001 C  CA  . LYS   B 1 160 ? -6.917  -20.358 8.489   1.00 13.89 ? 160 LYS   B CA  1 
ATOM   3002 C  C   . LYS   B 1 160 ? -6.847  -21.177 7.209   1.00 14.11 ? 160 LYS   B C   1 
ATOM   3003 O  O   . LYS   B 1 160 ? -6.795  -22.406 7.261   1.00 13.52 ? 160 LYS   B O   1 
ATOM   3004 C  CB  . LYS   B 1 160 ? -8.395  -20.133 8.834   1.00 17.17 ? 160 LYS   B CB  1 
ATOM   3005 C  CG  . LYS   B 1 160 ? -8.582  -19.705 10.251  1.00 23.17 ? 160 LYS   B CG  1 
ATOM   3006 C  CD  . LYS   B 1 160 ? -10.066 -19.472 10.543  1.00 28.57 ? 160 LYS   B CD  1 
ATOM   3007 C  CE  . LYS   B 1 160 ? -10.322 -19.146 11.978  1.00 32.66 ? 160 LYS   B CE  1 
ATOM   3008 N  NZ  . LYS   B 1 160 ? -11.750 -18.881 12.163  1.00 38.30 ? 160 LYS   B NZ  1 
ATOM   3009 N  N   . ALA   B 1 161 ? -6.852  -20.498 6.064   1.00 12.11 ? 161 ALA   B N   1 
ATOM   3010 C  CA  . ALA   B 1 161 ? -6.778  -21.190 4.782   1.00 13.70 ? 161 ALA   B CA  1 
ATOM   3011 C  C   . ALA   B 1 161 ? -5.367  -21.641 4.393   1.00 14.30 ? 161 ALA   B C   1 
ATOM   3012 O  O   . ALA   B 1 161 ? -5.212  -22.307 3.363   1.00 15.09 ? 161 ALA   B O   1 
ATOM   3013 C  CB  . ALA   B 1 161 ? -7.349  -20.298 3.711   1.00 13.96 ? 161 ALA   B CB  1 
ATOM   3014 N  N   . GLY   B 1 162 ? -4.350  -21.251 5.171   1.00 13.47 ? 162 GLY   B N   1 
ATOM   3015 C  CA  . GLY   B 1 162 ? -3.006  -21.767 5.018   1.00 13.59 ? 162 GLY   B CA  1 
ATOM   3016 C  C   . GLY   B 1 162 ? -1.992  -20.743 4.481   1.00 12.88 ? 162 GLY   B C   1 
ATOM   3017 O  O   . GLY   B 1 162 ? -0.894  -21.155 4.107   1.00 13.98 ? 162 GLY   B O   1 
ATOM   3018 N  N   . ALA   B 1 163 ? -2.310  -19.446 4.462   1.00 11.82 ? 163 ALA   B N   1 
ATOM   3019 C  CA  . ALA   B 1 163 ? -1.326  -18.458 4.026   1.00 11.43 ? 163 ALA   B CA  1 
ATOM   3020 C  C   . ALA   B 1 163 ? 0.003   -18.632 4.769   1.00 11.09 ? 163 ALA   B C   1 
ATOM   3021 O  O   . ALA   B 1 163 ? 0.022   -18.758 6.012   1.00 12.01 ? 163 ALA   B O   1 
ATOM   3022 C  CB  . ALA   B 1 163 ? -1.846  -17.082 4.270   1.00 11.16 ? 163 ALA   B CB  1 
ATOM   3023 N  N   . ASP   B 1 164 ? 1.112   -18.503 4.029   1.00 10.91 ? 164 ASP   B N   1 
ATOM   3024 C  CA  . ASP   B 1 164 ? 2.438   -18.520 4.625   1.00 11.25 ? 164 ASP   B CA  1 
ATOM   3025 C  C   . ASP   B 1 164 ? 2.882   -17.127 5.053   1.00 10.83 ? 164 ASP   B C   1 
ATOM   3026 O  O   . ASP   B 1 164 ? 3.782   -16.972 5.865   1.00 11.25 ? 164 ASP   B O   1 
ATOM   3027 C  CB  . ASP   B 1 164 ? 3.432   -19.151 3.664   1.00 11.08 ? 164 ASP   B CB  1 
ATOM   3028 C  CG  . ASP   B 1 164 ? 3.066   -20.563 3.255   1.00 13.00 ? 164 ASP   B CG  1 
ATOM   3029 O  OD1 . ASP   B 1 164 ? 2.807   -21.377 4.175   1.00 13.54 ? 164 ASP   B OD1 1 
ATOM   3030 O  OD2 . ASP   B 1 164 ? 3.083   -20.871 2.031   1.00 13.09 ? 164 ASP   B OD2 1 
ATOM   3031 N  N   . PHE   B 1 165 ? 2.309   -16.121 4.393   1.00 10.53 ? 165 PHE   B N   1 
ATOM   3032 C  CA  . PHE   B 1 165 ? 2.487   -14.719 4.708   1.00 10.46 ? 165 PHE   B CA  1 
ATOM   3033 C  C   . PHE   B 1 165 ? 1.155   -14.011 4.504   1.00 9.98  ? 165 PHE   B C   1 
ATOM   3034 O  O   . PHE   B 1 165 ? 0.368   -14.397 3.638   1.00 10.55 ? 165 PHE   B O   1 
ATOM   3035 C  CB  . PHE   B 1 165 ? 3.418   -13.996 3.732   1.00 10.57 ? 165 PHE   B CB  1 
ATOM   3036 C  CG  . PHE   B 1 165 ? 4.902   -13.978 4.066   1.00 11.55 ? 165 PHE   B CG  1 
ATOM   3037 C  CD1 . PHE   B 1 165 ? 5.703   -15.076 3.846   1.00 14.32 ? 165 PHE   B CD1 1 
ATOM   3038 C  CD2 . PHE   B 1 165 ? 5.480   -12.829 4.566   1.00 13.48 ? 165 PHE   B CD2 1 
ATOM   3039 C  CE1 . PHE   B 1 165 ? 7.087   -15.000 4.069   1.00 15.64 ? 165 PHE   B CE1 1 
ATOM   3040 C  CE2 . PHE   B 1 165 ? 6.823   -12.792 4.883   1.00 14.72 ? 165 PHE   B CE2 1 
ATOM   3041 C  CZ  . PHE   B 1 165 ? 7.624   -13.867 4.613   1.00 15.44 ? 165 PHE   B CZ  1 
ATOM   3042 N  N   . ILE   B 1 166 ? 0.924   -12.974 5.305   1.00 9.82  ? 166 ILE   B N   1 
ATOM   3043 C  CA  . ILE   B 1 166 ? -0.111  -12.011 4.986   1.00 9.95  ? 166 ILE   B CA  1 
ATOM   3044 C  C   . ILE   B 1 166 ? 0.595   -10.698 4.644   1.00 11.04 ? 166 ILE   B C   1 
ATOM   3045 O  O   . ILE   B 1 166 ? 1.573   -10.304 5.289   1.00 10.79 ? 166 ILE   B O   1 
ATOM   3046 C  CB  . ILE   B 1 166 ? -1.154  -11.928 6.116   1.00 10.88 ? 166 ILE   B CB  1 
ATOM   3047 C  CG1 . ILE   B 1 166 ? -0.554  -11.636 7.469   1.00 10.78 ? 166 ILE   B CG1 1 
ATOM   3048 C  CG2 . ILE   B 1 166 ? -1.961  -13.236 6.119   1.00 11.37 ? 166 ILE   B CG2 1 
ATOM   3049 C  CD1 . ILE   B 1 166 ? -1.601  -11.336 8.561   1.00 11.28 ? 166 ILE   B CD1 1 
ATOM   3050 N  N   . LYS   B 1 167 ? 0.076   -10.042 3.600   1.00 10.66 ? 167 LYS   B N   1 
ATOM   3051 C  CA  . LYS   B 1 167 ? 0.730   -8.917  2.948   1.00 11.02 ? 167 LYS   B CA  1 
ATOM   3052 C  C   . LYS   B 1 167 ? -0.283  -7.786  2.907   1.00 10.63 ? 167 LYS   B C   1 
ATOM   3053 O  O   . LYS   B 1 167 ? -1.455  -8.015  2.578   1.00 9.56  ? 167 LYS   B O   1 
ATOM   3054 C  CB  . LYS   B 1 167 ? 1.149   -9.397  1.562   1.00 11.53 ? 167 LYS   B CB  1 
ATOM   3055 C  CG  . LYS   B 1 167 ? 1.665   -8.328  0.604   1.00 13.21 ? 167 LYS   B CG  1 
ATOM   3056 C  CD  . LYS   B 1 167 ? 2.288   -8.907  -0.637  1.00 13.63 ? 167 LYS   B CD  1 
ATOM   3057 C  CE  . LYS   B 1 167 ? 2.466   -7.819  -1.610  1.00 15.87 ? 167 LYS   B CE  1 
ATOM   3058 N  NZ  . LYS   B 1 167 ? 3.120   -8.202  -2.847  1.00 18.62 ? 167 LYS   B NZ  1 
ATOM   3059 N  N   . THR   B 1 168 ? 0.149   -6.550  3.174   1.00 10.24 ? 168 THR   B N   1 
ATOM   3060 C  CA  . THR   B 1 168 ? -0.796  -5.473  3.299   1.00 10.68 ? 168 THR   B CA  1 
ATOM   3061 C  C   . THR   B 1 168 ? -1.523  -5.166  1.987   1.00 10.62 ? 168 THR   B C   1 
ATOM   3062 O  O   . THR   B 1 168 ? -2.725  -4.944  1.995   1.00 10.78 ? 168 THR   B O   1 
ATOM   3063 C  CB  . THR   B 1 168 ? -0.124  -4.198  3.826   1.00 11.28 ? 168 THR   B CB  1 
ATOM   3064 O  OG1 . THR   B 1 168 ? 0.835   -3.730  2.879   1.00 10.99 ? 168 THR   B OG1 1 
ATOM   3065 C  CG2 . THR   B 1 168 ? 0.506   -4.437  5.180   1.00 10.86 ? 168 THR   B CG2 1 
ATOM   3066 N  N   . SER   B 1 169 ? -0.789  -5.054  0.872   1.00 10.50 ? 169 SER   B N   1 
ATOM   3067 C  CA  . SER   B 1 169 ? -1.244  -4.225  -0.233  1.00 10.93 ? 169 SER   B CA  1 
ATOM   3068 C  C   . SER   B 1 169 ? -0.713  -4.728  -1.575  1.00 11.18 ? 169 SER   B C   1 
ATOM   3069 O  O   . SER   B 1 169 ? 0.361   -5.345  -1.635  1.00 12.24 ? 169 SER   B O   1 
ATOM   3070 C  CB  . SER   B 1 169 ? -0.795  -2.804  -0.032  1.00 11.41 ? 169 SER   B CB  1 
ATOM   3071 O  OG  . SER   B 1 169 ? -1.169  -2.332  1.266   1.00 12.29 ? 169 SER   B OG  1 
ATOM   3072 N  N   . THR   B 1 170 ? -1.427  -4.335  -2.643  1.00 11.75 ? 170 THR   B N   1 
ATOM   3073 C  CA  . THR   B 1 170 ? -0.939  -4.579  -3.988  1.00 11.77 ? 170 THR   B CA  1 
ATOM   3074 C  C   . THR   B 1 170 ? 0.093   -3.531  -4.409  1.00 13.25 ? 170 THR   B C   1 
ATOM   3075 O  O   . THR   B 1 170 ? 0.827   -3.780  -5.369  1.00 13.80 ? 170 THR   B O   1 
ATOM   3076 C  CB  . THR   B 1 170 ? -2.097  -4.578  -4.979  1.00 12.02 ? 170 THR   B CB  1 
ATOM   3077 O  OG1 . THR   B 1 170 ? -2.737  -3.304  -4.945  1.00 11.63 ? 170 THR   B OG1 1 
ATOM   3078 C  CG2 . THR   B 1 170 ? -3.071  -5.716  -4.764  1.00 11.84 ? 170 THR   B CG2 1 
ATOM   3079 N  N   . GLY   B 1 171 ? 0.037   -2.339  -3.830  1.00 12.70 ? 171 GLY   B N   1 
ATOM   3080 C  CA  . GLY   B 1 171 ? 0.785   -1.212  -4.362  1.00 15.02 ? 171 GLY   B CA  1 
ATOM   3081 C  C   . GLY   B 1 171 ? 0.050   -0.518  -5.500  1.00 16.96 ? 171 GLY   B C   1 
ATOM   3082 O  O   . GLY   B 1 171 ? 0.602   0.419   -6.075  1.00 19.74 ? 171 GLY   B O   1 
ATOM   3083 N  N   . ARG   B 1 172 ? -1.176  -0.961  -5.840  1.00 15.61 ? 172 ARG   B N   1 
ATOM   3084 C  CA  . ARG   B 1 172 ? -1.862  -0.440  -7.019  1.00 17.48 ? 172 ARG   B CA  1 
ATOM   3085 C  C   . ARG   B 1 172 ? -3.112  0.364   -6.664  1.00 18.88 ? 172 ARG   B C   1 
ATOM   3086 O  O   . ARG   B 1 172 ? -3.852  0.773   -7.542  1.00 22.08 ? 172 ARG   B O   1 
ATOM   3087 C  CB  . ARG   B 1 172 ? -2.248  -1.597  -7.949  1.00 19.51 ? 172 ARG   B CB  1 
ATOM   3088 C  CG  . ARG   B 1 172 ? -1.048  -2.356  -8.489  1.00 21.28 ? 172 ARG   B CG  1 
ATOM   3089 C  CD  . ARG   B 1 172 ? -0.159  -1.531  -9.401  1.00 25.84 ? 172 ARG   B CD  1 
ATOM   3090 N  NE  . ARG   B 1 172 ? -0.438  -2.026  -10.732 1.00 37.09 ? 172 ARG   B NE  1 
ATOM   3091 C  CZ  . ARG   B 1 172 ? 0.260   -2.983  -11.330 1.00 37.10 ? 172 ARG   B CZ  1 
ATOM   3092 N  NH1 . ARG   B 1 172 ? 1.445   -3.354  -10.863 1.00 39.85 ? 172 ARG   B NH1 1 
ATOM   3093 N  NH2 . ARG   B 1 172 ? -0.253  -3.574  -12.384 1.00 41.04 ? 172 ARG   B NH2 1 
ATOM   3094 N  N   . VAL   B 1 173 ? -3.355  0.608   -5.370  1.00 16.32 ? 173 VAL   B N   1 
ATOM   3095 C  CA  . VAL   B 1 173 ? -4.476  1.409   -4.915  1.00 16.61 ? 173 VAL   B CA  1 
ATOM   3096 C  C   . VAL   B 1 173 ? -3.900  2.623   -4.195  1.00 16.63 ? 173 VAL   B C   1 
ATOM   3097 O  O   . VAL   B 1 173 ? -2.710  2.681   -3.942  1.00 17.41 ? 173 VAL   B O   1 
ATOM   3098 C  CB  . VAL   B 1 173 ? -5.446  0.598   -4.036  1.00 17.76 ? 173 VAL   B CB  1 
ATOM   3099 C  CG1 . VAL   B 1 173 ? -6.091  -0.520  -4.866  1.00 18.68 ? 173 VAL   B CG1 1 
ATOM   3100 C  CG2 . VAL   B 1 173 ? -4.780  0.018   -2.799  1.00 17.52 ? 173 VAL   B CG2 1 
ATOM   3101 N  N   . ALA   B 1 174 ? -4.761  3.562   -3.849  1.00 17.80 ? 174 ALA   B N   1 
ATOM   3102 C  CA  . ALA   B 1 174 ? -4.342  4.831   -3.283  1.00 19.11 ? 174 ALA   B CA  1 
ATOM   3103 C  C   . ALA   B 1 174 ? -3.681  4.647   -1.912  1.00 17.14 ? 174 ALA   B C   1 
ATOM   3104 O  O   . ALA   B 1 174 ? -2.725  5.340   -1.589  1.00 16.85 ? 174 ALA   B O   1 
ATOM   3105 C  CB  . ALA   B 1 174 ? -5.561  5.730   -3.177  1.00 19.71 ? 174 ALA   B CB  1 
ATOM   3106 N  N   . VAL   B 1 175 ? -4.202  3.717   -1.116  1.00 15.83 ? 175 VAL   B N   1 
ATOM   3107 C  CA  . VAL   B 1 175 ? -3.747  3.532   0.249   1.00 16.11 ? 175 VAL   B CA  1 
ATOM   3108 C  C   . VAL   B 1 175 ? -3.089  2.167   0.355   1.00 14.62 ? 175 VAL   B C   1 
ATOM   3109 O  O   . VAL   B 1 175 ? -3.756  1.166   0.120   1.00 13.78 ? 175 VAL   B O   1 
ATOM   3110 C  CB  . VAL   B 1 175 ? -4.881  3.707   1.274   1.00 15.56 ? 175 VAL   B CB  1 
ATOM   3111 C  CG1 . VAL   B 1 175 ? -4.423  3.444   2.711   1.00 15.69 ? 175 VAL   B CG1 1 
ATOM   3112 C  CG2 . VAL   B 1 175 ? -5.468  5.126   1.199   1.00 16.95 ? 175 VAL   B CG2 1 
ATOM   3113 N  N   . ASN   B 1 176 ? -1.814  2.151   0.752   1.00 14.48 ? 176 ASN   B N   1 
ATOM   3114 C  CA  . ASN   B 1 176 ? -1.089  0.890   0.890   1.00 14.75 ? 176 ASN   B CA  1 
ATOM   3115 C  C   . ASN   B 1 176 ? -0.826  0.715   2.378   1.00 13.41 ? 176 ASN   B C   1 
ATOM   3116 O  O   . ASN   B 1 176 ? -1.687  1.072   3.155   1.00 14.62 ? 176 ASN   B O   1 
ATOM   3117 C  CB  . ASN   B 1 176 ? 0.077   0.816   -0.080  1.00 15.77 ? 176 ASN   B CB  1 
ATOM   3118 C  CG  . ASN   B 1 176 ? -0.443  0.848   -1.499  1.00 17.93 ? 176 ASN   B CG  1 
ATOM   3119 O  OD1 . ASN   B 1 176 ? -0.980  -0.139  -2.011  1.00 17.35 ? 176 ASN   B OD1 1 
ATOM   3120 N  ND2 . ASN   B 1 176 ? -0.386  2.025   -2.099  1.00 20.74 ? 176 ASN   B ND2 1 
ATOM   3121 N  N   . ALA   B 1 177 ? 0.342   0.205   2.766   1.00 12.23 ? 177 ALA   B N   1 
ATOM   3122 C  CA  . ALA   B 1 177 ? 0.579   -0.077  4.172   1.00 12.32 ? 177 ALA   B CA  1 
ATOM   3123 C  C   . ALA   B 1 177 ? 0.577   1.219   4.966   1.00 12.41 ? 177 ALA   B C   1 
ATOM   3124 O  O   . ALA   B 1 177 ? 0.991   2.260   4.476   1.00 13.39 ? 177 ALA   B O   1 
ATOM   3125 C  CB  . ALA   B 1 177 ? 1.875   -0.788  4.385   1.00 12.19 ? 177 ALA   B CB  1 
ATOM   3126 N  N   . THR   B 1 178 ? 0.198   1.092   6.232   1.00 13.09 ? 178 THR   B N   1 
ATOM   3127 C  CA  . THR   B 1 178 ? 0.478   2.092   7.249   1.00 14.41 ? 178 THR   B CA  1 
ATOM   3128 C  C   . THR   B 1 178 ? 1.003   1.355   8.469   1.00 14.38 ? 178 THR   B C   1 
ATOM   3129 O  O   . THR   B 1 178 ? 0.783   0.155   8.599   1.00 12.43 ? 178 THR   B O   1 
ATOM   3130 C  CB  . THR   B 1 178 ? -0.771  2.885   7.623   1.00 15.39 ? 178 THR   B CB  1 
ATOM   3131 O  OG1 . THR   B 1 178 ? -1.675  2.009   8.297   1.00 15.91 ? 178 THR   B OG1 1 
ATOM   3132 C  CG2 . THR   B 1 178 ? -1.487  3.460   6.418   1.00 16.38 ? 178 THR   B CG2 1 
ATOM   3133 N  N   . PRO   B 1 179 ? 1.663   2.064   9.416   1.00 15.34 ? 179 PRO   B N   1 
ATOM   3134 C  CA  . PRO   B 1 179 ? 2.072   1.438   10.671  1.00 15.13 ? 179 PRO   B CA  1 
ATOM   3135 C  C   . PRO   B 1 179 ? 0.902   0.784   11.380  1.00 14.35 ? 179 PRO   B C   1 
ATOM   3136 O  O   . PRO   B 1 179 ? 1.071   -0.281  11.949  1.00 15.16 ? 179 PRO   B O   1 
ATOM   3137 C  CB  . PRO   B 1 179 ? 2.713   2.571   11.478  1.00 15.98 ? 179 PRO   B CB  1 
ATOM   3138 C  CG  . PRO   B 1 179 ? 3.249   3.466   10.347  1.00 16.84 ? 179 PRO   B CG  1 
ATOM   3139 C  CD  . PRO   B 1 179 ? 2.158   3.448   9.284   1.00 16.47 ? 179 PRO   B CD  1 
ATOM   3140 N  N   . GLU   B 1 180 ? -0.269  1.430   11.353  1.00 15.71 ? 180 GLU   B N   1 
ATOM   3141 C  CA  . GLU   B 1 180 ? -1.449  0.900   12.032  1.00 17.32 ? 180 GLU   B CA  1 
ATOM   3142 C  C   . GLU   B 1 180 ? -1.915  -0.402  11.386  1.00 15.05 ? 180 GLU   B C   1 
ATOM   3143 O  O   . GLU   B 1 180 ? -2.186  -1.393  12.059  1.00 14.01 ? 180 GLU   B O   1 
ATOM   3144 C  CB  . GLU   B 1 180 ? -2.572  1.939   12.004  1.00 21.36 ? 180 GLU   B CB  1 
ATOM   3145 C  CG  . GLU   B 1 180 ? -2.161  3.274   12.634  1.00 27.91 ? 180 GLU   B CG  1 
ATOM   3146 C  CD  . GLU   B 1 180 ? -1.176  4.253   11.964  1.00 35.74 ? 180 GLU   B CD  1 
ATOM   3147 O  OE1 . GLU   B 1 180 ? -0.835  4.211   10.749  1.00 30.93 ? 180 GLU   B OE1 1 
ATOM   3148 O  OE2 . GLU   B 1 180 ? -0.676  5.113   12.754  1.00 50.58 ? 180 GLU   B OE2 1 
ATOM   3149 N  N   . SER   B 1 181 ? -1.984  -0.440  10.057  1.00 14.16 ? 181 SER   B N   1 
ATOM   3150 C  CA  . SER   B 1 181 ? -2.456  -1.682  9.452   1.00 14.23 ? 181 SER   B CA  1 
ATOM   3151 C  C   . SER   B 1 181 ? -1.427  -2.794  9.628   1.00 13.29 ? 181 SER   B C   1 
ATOM   3152 O  O   . SER   B 1 181 ? -1.793  -3.933  9.823   1.00 12.82 ? 181 SER   B O   1 
ATOM   3153 C  CB  . SER   B 1 181 ? -2.919  -1.488  7.994   1.00 15.71 ? 181 SER   B CB  1 
ATOM   3154 O  OG  . SER   B 1 181 ? -1.875  -1.011  7.182   1.00 17.78 ? 181 SER   B OG  1 
ATOM   3155 N  N   . ALA   B 1 182 ? -0.141  -2.463  9.623   1.00 12.51 ? 182 ALA   B N   1 
ATOM   3156 C  CA  . ALA   B 1 182 ? 0.910   -3.434  9.901   1.00 12.47 ? 182 ALA   B CA  1 
ATOM   3157 C  C   . ALA   B 1 182 ? 0.762   -4.002  11.303  1.00 12.21 ? 182 ALA   B C   1 
ATOM   3158 O  O   . ALA   B 1 182 ? 0.833   -5.213  11.506  1.00 13.04 ? 182 ALA   B O   1 
ATOM   3159 C  CB  . ALA   B 1 182 ? 2.252   -2.800  9.694   1.00 13.08 ? 182 ALA   B CB  1 
ATOM   3160 N  N   . ARG   B 1 183 ? 0.552   -3.113  12.295  1.00 12.47 ? 183 ARG   B N   1 
ATOM   3161 C  CA  . ARG   B 1 183 ? 0.356   -3.547  13.667  1.00 13.73 ? 183 ARG   B CA  1 
ATOM   3162 C  C   . ARG   B 1 183 ? -0.844  -4.489  13.776  1.00 12.97 ? 183 ARG   B C   1 
ATOM   3163 O  O   . ARG   B 1 183 ? -0.757  -5.545  14.388  1.00 12.52 ? 183 ARG   B O   1 
ATOM   3164 C  CB  . ARG   B 1 183 ? 0.204   -2.333  14.591  1.00 14.61 ? 183 ARG   B CB  1 
ATOM   3165 C  CG  . ARG   B 1 183 ? -0.075  -2.711  16.037  1.00 17.57 ? 183 ARG   B CG  1 
ATOM   3166 C  CD  . ARG   B 1 183 ? -0.463  -1.501  16.877  1.00 20.09 ? 183 ARG   B CD  1 
ATOM   3167 N  NE  . ARG   B 1 183 ? -1.642  -0.772  16.393  1.00 23.46 ? 183 ARG   B NE  1 
ATOM   3168 C  CZ  . ARG   B 1 183 ? -2.909  -1.146  16.541  1.00 25.36 ? 183 ARG   B CZ  1 
ATOM   3169 N  NH1 . ARG   B 1 183 ? -3.223  -2.274  17.136  1.00 29.10 ? 183 ARG   B NH1 1 
ATOM   3170 N  NH2 . ARG   B 1 183 ? -3.881  -0.364  16.120  1.00 29.77 ? 183 ARG   B NH2 1 
ATOM   3171 N  N   . ILE   B 1 184 ? -1.978  -4.092  13.182  1.00 12.02 ? 184 ILE   B N   1 
ATOM   3172 C  CA  . ILE   B 1 184 ? -3.179  -4.909  13.250  1.00 11.84 ? 184 ILE   B CA  1 
ATOM   3173 C  C   . ILE   B 1 184 ? -2.896  -6.301  12.715  1.00 11.03 ? 184 ILE   B C   1 
ATOM   3174 O  O   . ILE   B 1 184 ? -3.282  -7.309  13.297  1.00 11.53 ? 184 ILE   B O   1 
ATOM   3175 C  CB  . ILE   B 1 184 ? -4.350  -4.220  12.534  1.00 12.51 ? 184 ILE   B CB  1 
ATOM   3176 C  CG1 . ILE   B 1 184 ? -4.732  -2.928  13.274  1.00 13.82 ? 184 ILE   B CG1 1 
ATOM   3177 C  CG2 . ILE   B 1 184 ? -5.535  -5.173  12.389  1.00 13.07 ? 184 ILE   B CG2 1 
ATOM   3178 C  CD1 . ILE   B 1 184 ? -5.534  -1.943  12.454  1.00 15.08 ? 184 ILE   B CD1 1 
ATOM   3179 N  N   . MET   B 1 185 ? -2.305  -6.369  11.522  1.00 10.74 ? 185 MET   B N   1 
ATOM   3180 C  CA  . MET   B 1 185 ? -2.027  -7.664  10.930  1.00 10.76 ? 185 MET   B CA  1 
ATOM   3181 C  C   . MET   B 1 185 ? -1.100  -8.533  11.774  1.00 11.18 ? 185 MET   B C   1 
ATOM   3182 O  O   . MET   B 1 185 ? -1.328  -9.745  11.913  1.00 11.56 ? 185 MET   B O   1 
ATOM   3183 C  CB  . MET   B 1 185 ? -1.472  -7.465  9.510   1.00 11.16 ? 185 MET   B CB  1 
ATOM   3184 C  CG  . MET   B 1 185 ? -2.547  -6.959  8.595   1.00 11.23 ? 185 MET   B CG  1 
ATOM   3185 S  SD  . MET   B 1 185 ? -2.006  -6.609  6.909   1.00 11.82 ? 185 MET   B SD  1 
ATOM   3186 C  CE  . MET   B 1 185 ? -1.677  -8.259  6.287   1.00 12.44 ? 185 MET   B CE  1 
ATOM   3187 N  N   . MET   B 1 186 ? -0.037  -7.945  12.321  1.00 11.98 ? 186 MET   B N   1 
ATOM   3188 C  CA  . MET   B 1 186 ? 0.884   -8.724  13.134  1.00 11.92 ? 186 MET   B CA  1 
ATOM   3189 C  C   . MET   B 1 186 ? 0.205   -9.125  14.450  1.00 12.35 ? 186 MET   B C   1 
ATOM   3190 O  O   . MET   B 1 186 ? 0.458   -10.208 14.961  1.00 11.68 ? 186 MET   B O   1 
ATOM   3191 C  CB  . MET   B 1 186 ? 2.197   -7.982  13.357  1.00 13.00 ? 186 MET   B CB  1 
ATOM   3192 C  CG  . MET   B 1 186 ? 3.105   -8.016  12.133  1.00 14.93 ? 186 MET   B CG  1 
ATOM   3193 S  SD  . MET   B 1 186 ? 4.693   -7.210  12.417  1.00 16.67 ? 186 MET   B SD  1 
ATOM   3194 C  CE  . MET   B 1 186 ? 4.302   -5.538  11.911  1.00 16.69 ? 186 MET   B CE  1 
ATOM   3195 N  N   . GLU   B 1 187 ? -0.691  -8.282  14.972  1.00 12.61 ? 187 GLU   B N   1 
ATOM   3196 C  CA  . GLU   B 1 187 ? -1.451  -8.684  16.152  1.00 14.04 ? 187 GLU   B CA  1 
ATOM   3197 C  C   . GLU   B 1 187 ? -2.305  -9.914  15.855  1.00 13.80 ? 187 GLU   B C   1 
ATOM   3198 O  O   . GLU   B 1 187 ? -2.490  -10.773 16.713  1.00 14.68 ? 187 GLU   B O   1 
ATOM   3199 C  CB  . GLU   B 1 187 ? -2.319  -7.548  16.689  1.00 15.01 ? 187 GLU   B CB  1 
ATOM   3200 C  CG  . GLU   B 1 187 ? -1.509  -6.440  17.361  1.00 16.96 ? 187 GLU   B CG  1 
ATOM   3201 C  CD  . GLU   B 1 187 ? -2.388  -5.288  17.855  1.00 22.05 ? 187 GLU   B CD  1 
ATOM   3202 O  OE1 . GLU   B 1 187 ? -3.599  -5.308  17.562  1.00 25.35 ? 187 GLU   B OE1 1 
ATOM   3203 O  OE2 . GLU   B 1 187 ? -1.877  -4.326  18.456  1.00 21.41 ? 187 GLU   B OE2 1 
ATOM   3204 N  N   . VAL   B 1 188 ? -2.871  -10.006 14.658  1.00 12.58 ? 188 VAL   B N   1 
ATOM   3205 C  CA  . VAL   B 1 188 ? -3.643  -11.191 14.313  1.00 12.89 ? 188 VAL   B CA  1 
ATOM   3206 C  C   . VAL   B 1 188 ? -2.744  -12.432 14.357  1.00 12.90 ? 188 VAL   B C   1 
ATOM   3207 O  O   . VAL   B 1 188 ? -3.120  -13.479 14.889  1.00 12.68 ? 188 VAL   B O   1 
ATOM   3208 C  CB  . VAL   B 1 188 ? -4.363  -11.087 12.964  1.00 13.19 ? 188 VAL   B CB  1 
ATOM   3209 C  CG1 . VAL   B 1 188 ? -5.062  -12.392 12.598  1.00 13.52 ? 188 VAL   B CG1 1 
ATOM   3210 C  CG2 . VAL   B 1 188 ? -5.379  -9.964  12.964  1.00 13.90 ? 188 VAL   B CG2 1 
ATOM   3211 N  N   . ILE   B 1 189 ? -1.568  -12.326 13.754  1.00 12.67 ? 189 ILE   B N   1 
ATOM   3212 C  CA  . ILE   B 1 189 ? -0.612  -13.428 13.777  1.00 12.44 ? 189 ILE   B CA  1 
ATOM   3213 C  C   . ILE   B 1 189 ? -0.372  -13.847 15.233  1.00 13.27 ? 189 ILE   B C   1 
ATOM   3214 O  O   . ILE   B 1 189 ? -0.394  -15.037 15.563  1.00 13.62 ? 189 ILE   B O   1 
ATOM   3215 C  CB  . ILE   B 1 189 ? 0.694   -13.039 13.061  1.00 12.89 ? 189 ILE   B CB  1 
ATOM   3216 C  CG1 . ILE   B 1 189 ? 0.466   -12.866 11.566  1.00 11.94 ? 189 ILE   B CG1 1 
ATOM   3217 C  CG2 . ILE   B 1 189 ? 1.796   -14.062 13.322  1.00 13.10 ? 189 ILE   B CG2 1 
ATOM   3218 C  CD1 . ILE   B 1 189 ? 1.653   -12.324 10.790  1.00 12.50 ? 189 ILE   B CD1 1 
ATOM   3219 N  N   . ARG   B 1 190 ? -0.097  -12.860 16.085  1.00 13.52 ? 190 ARG   B N   1 
ATOM   3220 C  CA  . ARG   B 1 190 ? 0.177   -13.150 17.483  1.00 14.82 ? 190 ARG   B CA  1 
ATOM   3221 C  C   . ARG   B 1 190 ? -1.047  -13.773 18.163  1.00 14.07 ? 190 ARG   B C   1 
ATOM   3222 O  O   . ARG   B 1 190 ? -0.915  -14.757 18.892  1.00 14.84 ? 190 ARG   B O   1 
ATOM   3223 C  CB  . ARG   B 1 190 ? 0.570   -11.869 18.213  1.00 16.89 ? 190 ARG   B CB  1 
ATOM   3224 C  CG  . ARG   B 1 190 ? 1.078   -12.115 19.630  1.00 20.87 ? 190 ARG   B CG  1 
ATOM   3225 C  CD  . ARG   B 1 190 ? 0.898   -10.889 20.518  1.00 25.52 ? 190 ARG   B CD  1 
ATOM   3226 N  NE  . ARG   B 1 190 ? -0.447  -10.336 20.426  1.00 27.46 ? 190 ARG   B NE  1 
ATOM   3227 C  CZ  . ARG   B 1 190 ? -0.753  -9.123  20.830  1.00 31.89 ? 190 ARG   B CZ  1 
ATOM   3228 N  NH1 . ARG   B 1 190 ? 0.135   -8.480  21.572  1.00 36.13 ? 190 ARG   B NH1 1 
ATOM   3229 N  NH2 . ARG   B 1 190 ? -1.932  -8.598  20.543  1.00 31.20 ? 190 ARG   B NH2 1 
ATOM   3230 N  N   . ASP   B 1 191 ? -2.220  -13.159 17.992  1.00 13.26 ? 191 ASP   B N   1 
ATOM   3231 C  CA  . ASP   B 1 191 ? -3.439  -13.584 18.666  1.00 13.84 ? 191 ASP   B CA  1 
ATOM   3232 C  C   . ASP   B 1 191 ? -3.836  -14.990 18.221  1.00 14.14 ? 191 ASP   B C   1 
ATOM   3233 O  O   . ASP   B 1 191 ? -4.426  -15.737 18.993  1.00 14.70 ? 191 ASP   B O   1 
ATOM   3234 C  CB  . ASP   B 1 191 ? -4.576  -12.610 18.427  1.00 15.29 ? 191 ASP   B CB  1 
ATOM   3235 C  CG  . ASP   B 1 191 ? -4.439  -11.262 19.124  1.00 18.42 ? 191 ASP   B CG  1 
ATOM   3236 O  OD1 . ASP   B 1 191 ? -3.479  -11.082 19.925  1.00 20.44 ? 191 ASP   B OD1 1 
ATOM   3237 O  OD2 . ASP   B 1 191 ? -5.209  -10.371 18.750  1.00 21.39 ? 191 ASP   B OD2 1 
ATOM   3238 N  N   . MET   B 1 192 ? -3.517  -15.359 16.969  1.00 13.68 ? 192 MET   B N   1 
ATOM   3239 C  CA  . MET   B 1 192 ? -3.854  -16.678 16.467  1.00 14.36 ? 192 MET   B CA  1 
ATOM   3240 C  C   . MET   B 1 192 ? -2.818  -17.714 16.906  1.00 13.91 ? 192 MET   B C   1 
ATOM   3241 O  O   . MET   B 1 192 ? -3.062  -18.910 16.833  1.00 14.62 ? 192 MET   B O   1 
ATOM   3242 C  CB  . MET   B 1 192 ? -4.021  -16.633 14.954  1.00 15.36 ? 192 MET   B CB  1 
ATOM   3243 C  CG  . MET   B 1 192 ? -5.326  -15.929 14.560  1.00 16.54 ? 192 MET   B CG  1 
ATOM   3244 S  SD  . MET   B 1 192 ? -5.545  -15.978 12.763  1.00 19.42 ? 192 MET   B SD  1 
ATOM   3245 C  CE  . MET   B 1 192 ? -6.203  -17.653 12.611  1.00 18.78 ? 192 MET   B CE  1 
ATOM   3246 N  N   . GLY   B 1 193 ? -1.657  -17.247 17.343  1.00 13.68 ? 193 GLY   B N   1 
ATOM   3247 C  CA  . GLY   B 1 193 ? -0.586  -18.108 17.809  1.00 13.94 ? 193 GLY   B CA  1 
ATOM   3248 C  C   . GLY   B 1 193 ? 0.209   -18.723 16.667  1.00 13.80 ? 193 GLY   B C   1 
ATOM   3249 O  O   . GLY   B 1 193 ? 0.816   -19.773 16.863  1.00 14.50 ? 193 GLY   B O   1 
ATOM   3250 N  N   . VAL   B 1 194 ? 0.260   -18.047 15.507  1.00 12.66 ? 194 VAL   B N   1 
ATOM   3251 C  CA  . VAL   B 1 194 ? 0.802   -18.678 14.304  1.00 13.68 ? 194 VAL   B CA  1 
ATOM   3252 C  C   . VAL   B 1 194 ? 2.129   -18.040 13.858  1.00 14.35 ? 194 VAL   B C   1 
ATOM   3253 O  O   . VAL   B 1 194 ? 2.550   -18.219 12.720  1.00 13.81 ? 194 VAL   B O   1 
ATOM   3254 C  CB  . VAL   B 1 194 ? -0.223  -18.688 13.155  1.00 13.91 ? 194 VAL   B CB  1 
ATOM   3255 C  CG1 . VAL   B 1 194 ? -1.459  -19.505 13.516  1.00 15.74 ? 194 VAL   B CG1 1 
ATOM   3256 C  CG2 . VAL   B 1 194 ? -0.617  -17.291 12.715  1.00 13.41 ? 194 VAL   B CG2 1 
ATOM   3257 N  N   . GLU   B 1 195 ? 2.811   -17.317 14.755  1.00 15.19 ? 195 GLU   B N   1 
ATOM   3258 C  CA  . GLU   B 1 195 ? 4.016   -16.576 14.402  1.00 16.44 ? 195 GLU   B CA  1 
ATOM   3259 C  C   . GLU   B 1 195 ? 5.146   -17.487 13.909  1.00 16.09 ? 195 GLU   B C   1 
ATOM   3260 O  O   . GLU   B 1 195 ? 6.005   -17.049 13.158  1.00 15.81 ? 195 GLU   B O   1 
ATOM   3261 C  CB  . GLU   B 1 195 ? 4.498   -15.696 15.549  1.00 18.76 ? 195 GLU   B CB  1 
ATOM   3262 C  CG  . GLU   B 1 195 ? 5.000   -16.461 16.765  1.00 20.48 ? 195 GLU   B CG  1 
ATOM   3263 C  CD  . GLU   B 1 195 ? 3.885   -16.875 17.714  1.00 25.37 ? 195 GLU   B CD  1 
ATOM   3264 O  OE1 . GLU   B 1 195 ? 2.666   -16.631 17.519  1.00 23.92 ? 195 GLU   B OE1 1 
ATOM   3265 O  OE2 . GLU   B 1 195 ? 4.301   -17.446 18.732  1.00 31.61 ? 195 GLU   B OE2 1 
ATOM   3266 N  N   . LYS   B 1 196 ? 5.138   -18.758 14.274  1.00 16.56 ? 196 LYS   B N   1 
ATOM   3267 C  CA  . LYS   B 1 196 ? 6.138   -19.680 13.751  1.00 18.57 ? 196 LYS   B CA  1 
ATOM   3268 C  C   . LYS   B 1 196 ? 5.975   -19.901 12.244  1.00 17.65 ? 196 LYS   B C   1 
ATOM   3269 O  O   . LYS   B 1 196 ? 6.986   -19.985 11.536  1.00 19.18 ? 196 LYS   B O   1 
ATOM   3270 C  CB  . LYS   B 1 196 ? 6.065   -21.022 14.492  1.00 22.21 ? 196 LYS   B CB  1 
ATOM   3271 C  CG  . LYS   B 1 196 ? 6.980   -22.073 13.907  1.00 29.93 ? 196 LYS   B CG  1 
ATOM   3272 C  CD  . LYS   B 1 196 ? 6.793   -23.473 14.487  1.00 37.22 ? 196 LYS   B CD  1 
ATOM   3273 C  CE  . LYS   B 1 196 ? 7.127   -24.525 13.491  1.00 45.71 ? 196 LYS   B CE  1 
ATOM   3274 N  NZ  . LYS   B 1 196 ? 6.821   -25.847 14.041  1.00 56.62 ? 196 LYS   B NZ  1 
ATOM   3275 N  N   . SER   B 1 197 ? 4.727   -19.906 11.740  1.00 14.62 ? 197 SER   B N   1 
ATOM   3276 C  CA  . SER   B 1 197 ? 4.430   -20.395 10.404  1.00 15.27 ? 197 SER   B CA  1 
ATOM   3277 C  C   . SER   B 1 197 ? 3.990   -19.270 9.463   1.00 14.98 ? 197 SER   B C   1 
ATOM   3278 O  O   . SER   B 1 197 ? 3.861   -19.500 8.257   1.00 17.25 ? 197 SER   B O   1 
ATOM   3279 C  CB  . SER   B 1 197 ? 3.420   -21.503 10.431  1.00 16.37 ? 197 SER   B CB  1 
ATOM   3280 O  OG  . SER   B 1 197 ? 2.190   -21.076 10.996  1.00 17.36 ? 197 SER   B OG  1 
ATOM   3281 N  N   . VAL   B 1 198 ? 3.662   -18.098 9.999   1.00 12.47 ? 198 VAL   B N   1 
ATOM   3282 C  CA  . VAL   B 1 198 ? 3.078   -17.053 9.178   1.00 12.01 ? 198 VAL   B CA  1 
ATOM   3283 C  C   . VAL   B 1 198 ? 3.924   -15.794 9.280   1.00 13.01 ? 198 VAL   B C   1 
ATOM   3284 O  O   . VAL   B 1 198 ? 4.151   -15.275 10.372  1.00 13.62 ? 198 VAL   B O   1 
ATOM   3285 C  CB  . VAL   B 1 198 ? 1.617   -16.760 9.569   1.00 11.90 ? 198 VAL   B CB  1 
ATOM   3286 C  CG1 . VAL   B 1 198 ? 1.037   -15.645 8.710   1.00 11.58 ? 198 VAL   B CG1 1 
ATOM   3287 C  CG2 . VAL   B 1 198 ? 0.775   -18.009 9.440   1.00 12.28 ? 198 VAL   B CG2 1 
ATOM   3288 N  N   . GLY   B 1 199 ? 4.318   -15.267 8.123   1.00 11.62 ? 199 GLY   B N   1 
ATOM   3289 C  CA  . GLY   B 1 199 ? 5.072   -14.046 8.013   1.00 11.26 ? 199 GLY   B CA  1 
ATOM   3290 C  C   . GLY   B 1 199 ? 4.164   -12.863 7.662   1.00 11.16 ? 199 GLY   B C   1 
ATOM   3291 O  O   . GLY   B 1 199 ? 2.983   -13.014 7.335   1.00 10.61 ? 199 GLY   B O   1 
ATOM   3292 N  N   . PHE   B 1 200 ? 4.775   -11.676 7.730   1.00 10.97 ? 200 PHE   B N   1 
ATOM   3293 C  CA  . PHE   B 1 200 ? 4.137   -10.415 7.414   1.00 10.78 ? 200 PHE   B CA  1 
ATOM   3294 C  C   . PHE   B 1 200 ? 4.936   -9.680  6.355   1.00 11.00 ? 200 PHE   B C   1 
ATOM   3295 O  O   . PHE   B 1 200 ? 6.167   -9.571  6.473   1.00 11.36 ? 200 PHE   B O   1 
ATOM   3296 C  CB  . PHE   B 1 200 ? 4.045   -9.626  8.710   1.00 11.10 ? 200 PHE   B CB  1 
ATOM   3297 C  CG  . PHE   B 1 200 ? 3.532   -8.233  8.441   1.00 11.22 ? 200 PHE   B CG  1 
ATOM   3298 C  CD1 . PHE   B 1 200 ? 2.235   -8.027  7.994   1.00 11.98 ? 200 PHE   B CD1 1 
ATOM   3299 C  CD2 . PHE   B 1 200 ? 4.389   -7.159  8.480   1.00 12.77 ? 200 PHE   B CD2 1 
ATOM   3300 C  CE1 . PHE   B 1 200 ? 1.795   -6.754  7.667   1.00 11.99 ? 200 PHE   B CE1 1 
ATOM   3301 C  CE2 . PHE   B 1 200 ? 3.933   -5.890  8.163   1.00 13.53 ? 200 PHE   B CE2 1 
ATOM   3302 C  CZ  . PHE   B 1 200 ? 2.645   -5.696  7.743   1.00 12.63 ? 200 PHE   B CZ  1 
ATOM   3303 N  N   . LYS   B 1 201 ? 4.233   -9.137  5.356   1.00 10.50 ? 201 LYS   B N   1 
ATOM   3304 C  CA  . LYS   B 1 201 ? 4.876   -8.311  4.357   1.00 10.86 ? 201 LYS   B CA  1 
ATOM   3305 C  C   . LYS   B 1 201 ? 4.203   -6.948  4.245   1.00 11.20 ? 201 LYS   B C   1 
ATOM   3306 O  O   . LYS   B 1 201 ? 2.994   -6.843  4.044   1.00 10.70 ? 201 LYS   B O   1 
ATOM   3307 C  CB  . LYS   B 1 201 ? 4.934   -8.999  2.992   1.00 10.97 ? 201 LYS   B CB  1 
ATOM   3308 C  CG  . LYS   B 1 201 ? 5.448   -8.124  1.850   1.00 12.09 ? 201 LYS   B CG  1 
ATOM   3309 C  CD  . LYS   B 1 201 ? 5.786   -8.935  0.607   1.00 14.16 ? 201 LYS   B CD  1 
ATOM   3310 C  CE  . LYS   B 1 201 ? 6.143   -8.032  -0.563  1.00 16.59 ? 201 LYS   B CE  1 
ATOM   3311 N  NZ  . LYS   B 1 201 ? 6.256   -8.852  -1.798  1.00 19.66 ? 201 LYS   B NZ  1 
ATOM   3312 N  N   . VAL   B 1 202 ? 5.048   -5.923  4.301   1.00 11.52 ? 202 VAL   B N   1 
ATOM   3313 C  CA  A VAL   B 1 202 ? 4.688   -4.518  4.146   0.50 12.29 ? 202 VAL   B CA  1 
ATOM   3314 C  CA  B VAL   B 1 202 ? 4.573   -4.558  4.131   0.50 12.18 ? 202 VAL   B CA  1 
ATOM   3315 C  C   . VAL   B 1 202 ? 4.861   -4.120  2.693   1.00 12.59 ? 202 VAL   B C   1 
ATOM   3316 O  O   . VAL   B 1 202 ? 5.976   -4.210  2.200   1.00 14.25 ? 202 VAL   B O   1 
ATOM   3317 C  CB  A VAL   B 1 202 ? 5.664   -3.639  4.961   0.50 13.05 ? 202 VAL   B CB  1 
ATOM   3318 C  CB  B VAL   B 1 202 ? 5.164   -3.609  5.207   0.50 12.87 ? 202 VAL   B CB  1 
ATOM   3319 C  CG1 A VAL   B 1 202 ? 5.527   -2.152  4.635   0.50 13.18 ? 202 VAL   B CG1 1 
ATOM   3320 C  CG1 B VAL   B 1 202 ? 6.679   -3.568  5.185   0.50 12.90 ? 202 VAL   B CG1 1 
ATOM   3321 C  CG2 A VAL   B 1 202 ? 5.559   -3.877  6.454   0.50 13.31 ? 202 VAL   B CG2 1 
ATOM   3322 C  CG2 B VAL   B 1 202 ? 4.631   -2.183  5.136   0.50 12.81 ? 202 VAL   B CG2 1 
ATOM   3323 N  N   . THR   B 1 203 ? 3.800   -3.660  2.033   1.00 12.63 ? 203 THR   B N   1 
ATOM   3324 C  CA  . THR   B 1 203 ? 3.897   -3.143  0.681   1.00 13.90 ? 203 THR   B CA  1 
ATOM   3325 C  C   . THR   B 1 203 ? 3.385   -1.725  0.656   1.00 13.87 ? 203 THR   B C   1 
ATOM   3326 O  O   . THR   B 1 203 ? 2.266   -1.448  1.084   1.00 12.44 ? 203 THR   B O   1 
ATOM   3327 C  CB  . THR   B 1 203 ? 3.099   -4.021  -0.270  1.00 16.29 ? 203 THR   B CB  1 
ATOM   3328 O  OG1 . THR   B 1 203 ? 3.784   -5.259  -0.279  1.00 19.70 ? 203 THR   B OG1 1 
ATOM   3329 C  CG2 . THR   B 1 203 ? 3.125   -3.516  -1.697  1.00 16.00 ? 203 THR   B CG2 1 
ATOM   3330 N  N   . GLY   B 1 204 ? 4.261   -0.855  0.158   1.00 14.75 ? 204 GLY   B N   1 
ATOM   3331 C  CA  . GLY   B 1 204 ? 4.006   0.571   0.119   1.00 17.66 ? 204 GLY   B CA  1 
ATOM   3332 C  C   . GLY   B 1 204 ? 4.105   1.152   1.516   1.00 19.35 ? 204 GLY   B C   1 
ATOM   3333 O  O   . GLY   B 1 204 ? 4.367   0.441   2.493   1.00 19.93 ? 204 GLY   B O   1 
ATOM   3334 N  N   . GLY   B 1 205 ? 3.984   2.467   1.578   1.00 21.73 ? 205 GLY   B N   1 
ATOM   3335 C  CA  . GLY   B 1 205 ? 4.041   3.193   2.833   1.00 22.81 ? 205 GLY   B CA  1 
ATOM   3336 C  C   . GLY   B 1 205 ? 5.389   3.094   3.548   1.00 24.57 ? 205 GLY   B C   1 
ATOM   3337 O  O   . GLY   B 1 205 ? 5.483   3.455   4.704   1.00 25.60 ? 205 GLY   B O   1 
ATOM   3338 N  N   . VAL   B 1 206 ? 6.456   2.664   2.867   1.00 22.09 ? 206 VAL   B N   1 
ATOM   3339 C  CA  A VAL   B 1 206 ? 7.768   2.542   3.481   0.50 22.35 ? 206 VAL   B CA  1 
ATOM   3340 C  CA  B VAL   B 1 206 ? 7.758   2.559   3.491   0.50 21.85 ? 206 VAL   B CA  1 
ATOM   3341 C  C   . VAL   B 1 206 ? 8.787   3.129   2.509   1.00 23.67 ? 206 VAL   B C   1 
ATOM   3342 O  O   . VAL   B 1 206 ? 9.502   2.400   1.846   1.00 23.12 ? 206 VAL   B O   1 
ATOM   3343 C  CB  A VAL   B 1 206 ? 8.177   1.103   3.838   0.50 22.13 ? 206 VAL   B CB  1 
ATOM   3344 C  CB  B VAL   B 1 206 ? 8.019   1.103   3.938   0.50 20.94 ? 206 VAL   B CB  1 
ATOM   3345 C  CG1 A VAL   B 1 206 ? 9.399   1.106   4.750   0.50 23.33 ? 206 VAL   B CG1 1 
ATOM   3346 C  CG1 B VAL   B 1 206 ? 7.854   0.084   2.816   0.50 20.99 ? 206 VAL   B CG1 1 
ATOM   3347 C  CG2 A VAL   B 1 206 ? 7.034   0.304   4.435   0.50 23.05 ? 206 VAL   B CG2 1 
ATOM   3348 C  CG2 B VAL   B 1 206 ? 9.367   0.944   4.622   0.50 22.04 ? 206 VAL   B CG2 1 
ATOM   3349 N  N   . SER   B 1 207 ? 8.854   4.458   2.463   1.00 24.17 ? 207 SER   B N   1 
ATOM   3350 C  CA  . SER   B 1 207 ? 9.666   5.190   1.514   1.00 27.85 ? 207 SER   B CA  1 
ATOM   3351 C  C   . SER   B 1 207 ? 11.121  5.254   1.941   1.00 26.15 ? 207 SER   B C   1 
ATOM   3352 O  O   . SER   B 1 207 ? 11.983  5.250   1.078   1.00 29.95 ? 207 SER   B O   1 
ATOM   3353 C  CB  . SER   B 1 207 ? 9.123   6.577   1.329   1.00 29.75 ? 207 SER   B CB  1 
ATOM   3354 O  OG  . SER   B 1 207 ? 7.961   6.432   0.534   1.00 35.47 ? 207 SER   B OG  1 
ATOM   3355 N  N   . THR   B 1 208 ? 11.368  5.320   3.245   1.00 21.20 ? 208 THR   B N   1 
ATOM   3356 C  CA  . THR   B 1 208 ? 12.662  5.706   3.778   1.00 21.44 ? 208 THR   B CA  1 
ATOM   3357 C  C   . THR   B 1 208 ? 13.165  4.646   4.743   1.00 20.55 ? 208 THR   B C   1 
ATOM   3358 O  O   . THR   B 1 208 ? 12.399  3.854   5.294   1.00 19.32 ? 208 THR   B O   1 
ATOM   3359 C  CB  . THR   B 1 208 ? 12.627  7.062   4.491   1.00 22.22 ? 208 THR   B CB  1 
ATOM   3360 O  OG1 . THR   B 1 208 ? 11.915  6.869   5.710   1.00 21.47 ? 208 THR   B OG1 1 
ATOM   3361 C  CG2 . THR   B 1 208 ? 12.015  8.162   3.636   1.00 23.62 ? 208 THR   B CG2 1 
ATOM   3362 N  N   . ALA   B 1 209 ? 14.474  4.696   4.970   1.00 21.32 ? 209 ALA   B N   1 
ATOM   3363 C  CA  . ALA   B 1 209 ? 15.129  3.899   5.990   1.00 22.01 ? 209 ALA   B CA  1 
ATOM   3364 C  C   . ALA   B 1 209 ? 14.461  4.087   7.356   1.00 21.42 ? 209 ALA   B C   1 
ATOM   3365 O  O   . ALA   B 1 209 ? 14.331  3.133   8.123   1.00 19.41 ? 209 ALA   B O   1 
ATOM   3366 C  CB  . ALA   B 1 209 ? 16.600  4.284   6.046   1.00 22.96 ? 209 ALA   B CB  1 
ATOM   3367 N  N   . GLU   B 1 210 ? 14.117  5.340   7.689   1.00 20.73 ? 210 GLU   B N   1 
ATOM   3368 C  CA  . GLU   B 1 210 ? 13.464  5.645   8.952   1.00 21.02 ? 210 GLU   B CA  1 
ATOM   3369 C  C   . GLU   B 1 210 ? 12.111  4.915   9.070   1.00 20.21 ? 210 GLU   B C   1 
ATOM   3370 O  O   . GLU   B 1 210 ? 11.753  4.345   10.119  1.00 19.51 ? 210 GLU   B O   1 
ATOM   3371 C  CB  . GLU   B 1 210 ? 13.261  7.155   9.089   1.00 24.43 ? 210 GLU   B CB  1 
ATOM   3372 C  CG  . GLU   B 1 210 ? 14.561  7.939   9.275   1.00 28.45 ? 210 GLU   B CG  1 
ATOM   3373 C  CD  . GLU   B 1 210 ? 15.373  8.251   8.021   1.00 32.95 ? 210 GLU   B CD  1 
ATOM   3374 O  OE1 . GLU   B 1 210 ? 15.041  7.866   6.862   1.00 29.60 ? 210 GLU   B OE1 1 
ATOM   3375 O  OE2 . GLU   B 1 210 ? 16.421  8.929   8.243   1.00 38.49 ? 210 GLU   B OE2 1 
ATOM   3376 N  N   . ASP   B 1 211 ? 11.352  4.944   7.984   1.00 18.41 ? 211 ASP   B N   1 
ATOM   3377 C  CA  . ASP   B 1 211 ? 10.112  4.197   7.924   1.00 18.52 ? 211 ASP   B CA  1 
ATOM   3378 C  C   . ASP   B 1 211 ? 10.352  2.713   8.160   1.00 17.71 ? 211 ASP   B C   1 
ATOM   3379 O  O   . ASP   B 1 211 ? 9.634   2.064   8.920   1.00 16.11 ? 211 ASP   B O   1 
ATOM   3380 C  CB  . ASP   B 1 211 ? 9.412   4.364   6.591   1.00 19.22 ? 211 ASP   B CB  1 
ATOM   3381 C  CG  . ASP   B 1 211 ? 8.979   5.776   6.247   1.00 21.41 ? 211 ASP   B CG  1 
ATOM   3382 O  OD1 . ASP   B 1 211 ? 8.635   6.525   7.199   1.00 23.00 ? 211 ASP   B OD1 1 
ATOM   3383 O  OD2 . ASP   B 1 211 ? 8.974   6.084   5.040   1.00 20.83 ? 211 ASP   B OD2 1 
ATOM   3384 N  N   . ALA   B 1 212 ? 11.347  2.143   7.469   1.00 16.13 ? 212 ALA   B N   1 
ATOM   3385 C  CA  . ALA   B 1 212 ? 11.601  0.715   7.610   1.00 15.18 ? 212 ALA   B CA  1 
ATOM   3386 C  C   . ALA   B 1 212 ? 11.929  0.334   9.045   1.00 15.86 ? 212 ALA   B C   1 
ATOM   3387 O  O   . ALA   B 1 212 ? 11.437  -0.680  9.538   1.00 15.63 ? 212 ALA   B O   1 
ATOM   3388 C  CB  . ALA   B 1 212 ? 12.695  0.261   6.659   1.00 15.19 ? 212 ALA   B CB  1 
ATOM   3389 N  N   . GLN   B 1 213 ? 12.696  1.177   9.730   1.00 16.17 ? 213 GLN   B N   1 
ATOM   3390 C  CA  . GLN   B 1 213 ? 13.018  0.939   11.122  1.00 18.09 ? 213 GLN   B CA  1 
ATOM   3391 C  C   . GLN   B 1 213 ? 11.743  0.875   11.979  1.00 17.30 ? 213 GLN   B C   1 
ATOM   3392 O  O   . GLN   B 1 213 ? 11.656  0.041   12.874  1.00 18.55 ? 213 GLN   B O   1 
ATOM   3393 C  CB  . GLN   B 1 213 ? 13.963  2.048   11.565  1.00 20.27 ? 213 GLN   B CB  1 
ATOM   3394 C  CG  . GLN   B 1 213 ? 14.447  1.913   12.996  1.00 25.24 ? 213 GLN   B CG  1 
ATOM   3395 C  CD  . GLN   B 1 213 ? 15.449  3.006   13.308  1.00 32.50 ? 213 GLN   B CD  1 
ATOM   3396 O  OE1 . GLN   B 1 213 ? 15.185  4.200   13.095  1.00 33.68 ? 213 GLN   B OE1 1 
ATOM   3397 N  NE2 . GLN   B 1 213 ? 16.624  2.599   13.754  1.00 34.50 ? 213 GLN   B NE2 1 
ATOM   3398 N  N   . LYS   B 1 214 ? 10.772  1.760   11.718  1.00 17.32 ? 214 LYS   B N   1 
ATOM   3399 C  CA  . LYS   B 1 214 ? 9.531   1.806   12.494  1.00 19.58 ? 214 LYS   B CA  1 
ATOM   3400 C  C   . LYS   B 1 214 ? 8.747   0.503   12.317  1.00 17.57 ? 214 LYS   B C   1 
ATOM   3401 O  O   . LYS   B 1 214 ? 8.235   -0.107  13.258  1.00 16.90 ? 214 LYS   B O   1 
ATOM   3402 C  CB  . LYS   B 1 214 ? 8.710   3.021   12.071  1.00 22.24 ? 214 LYS   B CB  1 
ATOM   3403 C  CG  . LYS   B 1 214 ? 7.369   3.143   12.797  1.00 27.85 ? 214 LYS   B CG  1 
ATOM   3404 C  CD  . LYS   B 1 214 ? 6.713   4.499   12.615  1.00 36.64 ? 214 LYS   B CD  1 
ATOM   3405 C  CE  . LYS   B 1 214 ? 6.055   4.905   13.910  1.00 45.73 ? 214 LYS   B CE  1 
ATOM   3406 N  NZ  . LYS   B 1 214 ? 5.152   6.043   13.723  1.00 49.67 ? 214 LYS   B NZ  1 
ATOM   3407 N  N   . TYR   B 1 215 ? 8.660   0.036   11.063  1.00 16.40 ? 215 TYR   B N   1 
ATOM   3408 C  CA  . TYR   B 1 215 ? 7.914   -1.186  10.791  1.00 15.29 ? 215 TYR   B CA  1 
ATOM   3409 C  C   . TYR   B 1 215 ? 8.592   -2.387  11.424  1.00 13.68 ? 215 TYR   B C   1 
ATOM   3410 O  O   . TYR   B 1 215 ? 7.916   -3.284  11.935  1.00 15.04 ? 215 TYR   B O   1 
ATOM   3411 C  CB  . TYR   B 1 215 ? 7.771   -1.417  9.278   1.00 15.96 ? 215 TYR   B CB  1 
ATOM   3412 C  CG  . TYR   B 1 215 ? 6.671   -0.574  8.658   1.00 16.91 ? 215 TYR   B CG  1 
ATOM   3413 C  CD1 . TYR   B 1 215 ? 5.349   -1.001  8.665   1.00 15.17 ? 215 TYR   B CD1 1 
ATOM   3414 C  CD2 . TYR   B 1 215 ? 6.954   0.619   8.019   1.00 19.45 ? 215 TYR   B CD2 1 
ATOM   3415 C  CE1 . TYR   B 1 215 ? 4.346   -0.261  8.069   1.00 14.91 ? 215 TYR   B CE1 1 
ATOM   3416 C  CE2 . TYR   B 1 215 ? 5.960   1.360   7.394   1.00 20.76 ? 215 TYR   B CE2 1 
ATOM   3417 C  CZ  . TYR   B 1 215 ? 4.651   0.918   7.419   1.00 18.57 ? 215 TYR   B CZ  1 
ATOM   3418 O  OH  . TYR   B 1 215 ? 3.665   1.652   6.809   1.00 16.79 ? 215 TYR   B OH  1 
ATOM   3419 N  N   . LEU   B 1 216 ? 9.922   -2.433  11.393  1.00 13.49 ? 216 LEU   B N   1 
ATOM   3420 C  CA  . LEU   B 1 216 ? 10.603  -3.535  12.051  1.00 13.99 ? 216 LEU   B CA  1 
ATOM   3421 C  C   . LEU   B 1 216 ? 10.410  -3.458  13.570  1.00 15.10 ? 216 LEU   B C   1 
ATOM   3422 O  O   . LEU   B 1 216 ? 10.379  -4.500  14.211  1.00 16.25 ? 216 LEU   B O   1 
ATOM   3423 C  CB  . LEU   B 1 216 ? 12.086  -3.544  11.707  1.00 16.44 ? 216 LEU   B CB  1 
ATOM   3424 C  CG  . LEU   B 1 216 ? 12.377  -4.142  10.334  1.00 17.52 ? 216 LEU   B CG  1 
ATOM   3425 C  CD1 . LEU   B 1 216 ? 13.781  -3.813  9.851   1.00 19.74 ? 216 LEU   B CD1 1 
ATOM   3426 C  CD2 . LEU   B 1 216 ? 12.106  -5.650  10.375  1.00 17.68 ? 216 LEU   B CD2 1 
ATOM   3427 N  N   . ALA   B 1 217 ? 10.389  -2.248  14.139  1.00 14.90 ? 217 ALA   B N   1 
ATOM   3428 C  CA  . ALA   B 1 217 ? 10.212  -2.095  15.574  1.00 16.03 ? 217 ALA   B CA  1 
ATOM   3429 C  C   . ALA   B 1 217 ? 8.894   -2.723  16.043  1.00 16.52 ? 217 ALA   B C   1 
ATOM   3430 O  O   . ALA   B 1 217 ? 8.830   -3.301  17.124  1.00 16.25 ? 217 ALA   B O   1 
ATOM   3431 C  CB  . ALA   B 1 217 ? 10.319  -0.634  15.981  1.00 16.32 ? 217 ALA   B CB  1 
ATOM   3432 N  N   . ILE   B 1 218 ? 7.833   -2.616  15.236  1.00 16.17 ? 218 ILE   B N   1 
ATOM   3433 C  CA  . ILE   B 1 218 ? 6.556   -3.215  15.606  1.00 16.06 ? 218 ILE   B CA  1 
ATOM   3434 C  C   . ILE   B 1 218 ? 6.727   -4.728  15.739  1.00 16.04 ? 218 ILE   B C   1 
ATOM   3435 O  O   . ILE   B 1 218 ? 6.257   -5.330  16.697  1.00 16.97 ? 218 ILE   B O   1 
ATOM   3436 C  CB  . ILE   B 1 218 ? 5.479   -2.835  14.575  1.00 17.35 ? 218 ILE   B CB  1 
ATOM   3437 C  CG1 . ILE   B 1 218 ? 5.236   -1.323  14.568  1.00 18.38 ? 218 ILE   B CG1 1 
ATOM   3438 C  CG2 . ILE   B 1 218 ? 4.203   -3.631  14.835  1.00 17.20 ? 218 ILE   B CG2 1 
ATOM   3439 C  CD1 . ILE   B 1 218 ? 4.541   -0.786  13.336  1.00 19.37 ? 218 ILE   B CD1 1 
ATOM   3440 N  N   . ALA   B 1 219 ? 7.392   -5.364  14.764  1.00 14.81 ? 219 ALA   B N   1 
ATOM   3441 C  CA  . ALA   B 1 219 ? 7.621   -6.800  14.802  1.00 15.57 ? 219 ALA   B CA  1 
ATOM   3442 C  C   . ALA   B 1 219 ? 8.461   -7.163  16.028  1.00 16.53 ? 219 ALA   B C   1 
ATOM   3443 O  O   . ALA   B 1 219 ? 8.172   -8.140  16.722  1.00 16.83 ? 219 ALA   B O   1 
ATOM   3444 C  CB  . ALA   B 1 219 ? 8.312   -7.243  13.519  1.00 15.60 ? 219 ALA   B CB  1 
ATOM   3445 N  N   . ASP   B 1 220 ? 9.535   -6.389  16.259  1.00 15.65 ? 220 ASP   B N   1 
ATOM   3446 C  CA  . ASP   B 1 220 ? 10.428  -6.666  17.371  1.00 18.16 ? 220 ASP   B CA  1 
ATOM   3447 C  C   . ASP   B 1 220 ? 9.670   -6.603  18.709  1.00 18.71 ? 220 ASP   B C   1 
ATOM   3448 O  O   . ASP   B 1 220 ? 9.868   -7.464  19.578  1.00 18.91 ? 220 ASP   B O   1 
ATOM   3449 C  CB  . ASP   B 1 220 ? 11.614  -5.720  17.352  1.00 18.42 ? 220 ASP   B CB  1 
ATOM   3450 C  CG  . ASP   B 1 220 ? 12.591  -5.920  16.202  1.00 20.13 ? 220 ASP   B CG  1 
ATOM   3451 O  OD1 . ASP   B 1 220 ? 12.463  -6.923  15.442  1.00 21.35 ? 220 ASP   B OD1 1 
ATOM   3452 O  OD2 . ASP   B 1 220 ? 13.476  -5.040  16.036  1.00 22.55 ? 220 ASP   B OD2 1 
ATOM   3453 N  N   . GLU   B 1 221 ? 8.800   -5.611  18.864  1.00 19.49 ? 221 GLU   B N   1 
ATOM   3454 C  CA  . GLU   B 1 221 ? 8.016   -5.459  20.091  1.00 20.74 ? 221 GLU   B CA  1 
ATOM   3455 C  C   . GLU   B 1 221 ? 6.976   -6.572  20.261  1.00 20.63 ? 221 GLU   B C   1 
ATOM   3456 O  O   . GLU   B 1 221 ? 6.717   -7.024  21.383  1.00 20.97 ? 221 GLU   B O   1 
ATOM   3457 C  CB  . GLU   B 1 221 ? 7.342   -4.090  20.102  1.00 23.31 ? 221 GLU   B CB  1 
ATOM   3458 C  CG  . GLU   B 1 221 ? 8.371   -2.965  20.173  1.00 31.55 ? 221 GLU   B CG  1 
ATOM   3459 C  CD  . GLU   B 1 221 ? 7.959   -1.566  19.729  1.00 43.87 ? 221 GLU   B CD  1 
ATOM   3460 O  OE1 . GLU   B 1 221 ? 6.786   -1.346  19.340  1.00 55.74 ? 221 GLU   B OE1 1 
ATOM   3461 O  OE2 . GLU   B 1 221 ? 8.855   -0.681  19.757  1.00 50.73 ? 221 GLU   B OE2 1 
ATOM   3462 N  N   . LEU   B 1 222 ? 6.364   -7.040  19.169  1.00 16.79 ? 222 LEU   B N   1 
ATOM   3463 C  CA  . LEU   B 1 222 ? 5.373   -8.084  19.287  1.00 17.38 ? 222 LEU   B CA  1 
ATOM   3464 C  C   . LEU   B 1 222 ? 5.999   -9.461  19.484  1.00 17.86 ? 222 LEU   B C   1 
ATOM   3465 O  O   . LEU   B 1 222 ? 5.417   -10.264 20.191  1.00 19.92 ? 222 LEU   B O   1 
ATOM   3466 C  CB  . LEU   B 1 222 ? 4.450   -8.078  18.065  1.00 16.22 ? 222 LEU   B CB  1 
ATOM   3467 C  CG  . LEU   B 1 222 ? 3.429   -6.945  18.029  1.00 19.25 ? 222 LEU   B CG  1 
ATOM   3468 C  CD1 . LEU   B 1 222 ? 2.737   -6.935  16.667  1.00 18.39 ? 222 LEU   B CD1 1 
ATOM   3469 C  CD2 . LEU   B 1 222 ? 2.384   -7.098  19.117  1.00 21.36 ? 222 LEU   B CD2 1 
ATOM   3470 N  N   . PHE   B 1 223 ? 7.084   -9.785  18.777  1.00 17.33 ? 223 PHE   B N   1 
ATOM   3471 C  CA  . PHE   B 1 223 ? 7.536   -11.161 18.673  1.00 18.18 ? 223 PHE   B CA  1 
ATOM   3472 C  C   . PHE   B 1 223 ? 8.963   -11.373 19.167  1.00 20.40 ? 223 PHE   B C   1 
ATOM   3473 O  O   . PHE   B 1 223 ? 9.453   -12.506 19.143  1.00 22.78 ? 223 PHE   B O   1 
ATOM   3474 C  CB  . PHE   B 1 223 ? 7.523   -11.605 17.215  1.00 17.49 ? 223 PHE   B CB  1 
ATOM   3475 C  CG  . PHE   B 1 223 ? 6.128   -11.611 16.608  1.00 17.87 ? 223 PHE   B CG  1 
ATOM   3476 C  CD1 . PHE   B 1 223 ? 5.114   -12.407 17.151  1.00 18.46 ? 223 PHE   B CD1 1 
ATOM   3477 C  CD2 . PHE   B 1 223 ? 5.815   -10.739 15.577  1.00 17.00 ? 223 PHE   B CD2 1 
ATOM   3478 C  CE1 . PHE   B 1 223 ? 3.833   -12.377 16.617  1.00 19.70 ? 223 PHE   B CE1 1 
ATOM   3479 C  CE2 . PHE   B 1 223 ? 4.536   -10.715 15.047  1.00 18.09 ? 223 PHE   B CE2 1 
ATOM   3480 C  CZ  . PHE   B 1 223 ? 3.547   -11.524 15.595  1.00 17.14 ? 223 PHE   B CZ  1 
ATOM   3481 N  N   . GLY   B 1 224 ? 9.663   -10.285 19.493  1.00 20.95 ? 224 GLY   B N   1 
ATOM   3482 C  CA  . GLY   B 1 224 ? 11.088  -10.326 19.783  1.00 22.05 ? 224 GLY   B CA  1 
ATOM   3483 C  C   . GLY   B 1 224 ? 11.916  -10.050 18.532  1.00 23.33 ? 224 GLY   B C   1 
ATOM   3484 O  O   . GLY   B 1 224 ? 11.485  -10.311 17.418  1.00 22.03 ? 224 GLY   B O   1 
ATOM   3485 N  N   . ALA   B 1 225 ? 13.150  -9.621  18.741  1.00 25.37 ? 225 ALA   B N   1 
ATOM   3486 C  CA  . ALA   B 1 225 ? 13.985  -9.063  17.689  1.00 25.03 ? 225 ALA   B CA  1 
ATOM   3487 C  C   . ALA   B 1 225 ? 14.512  -10.129 16.733  1.00 23.22 ? 225 ALA   B C   1 
ATOM   3488 O  O   . ALA   B 1 225 ? 14.983  -9.773  15.661  1.00 24.86 ? 225 ALA   B O   1 
ATOM   3489 C  CB  . ALA   B 1 225 ? 15.116  -8.286  18.330  1.00 26.49 ? 225 ALA   B CB  1 
ATOM   3490 N  N   . ASP   B 1 226 ? 14.431  -11.416 17.092  1.00 22.00 ? 226 ASP   B N   1 
ATOM   3491 C  CA  . ASP   B 1 226 ? 14.885  -12.491 16.218  1.00 24.90 ? 226 ASP   B CA  1 
ATOM   3492 C  C   . ASP   B 1 226 ? 13.797  -12.978 15.256  1.00 22.96 ? 226 ASP   B C   1 
ATOM   3493 O  O   . ASP   B 1 226 ? 14.074  -13.750 14.360  1.00 22.97 ? 226 ASP   B O   1 
ATOM   3494 C  CB  . ASP   B 1 226 ? 15.415  -13.680 17.001  1.00 30.42 ? 226 ASP   B CB  1 
ATOM   3495 C  CG  . ASP   B 1 226 ? 16.722  -13.400 17.733  1.00 40.69 ? 226 ASP   B CG  1 
ATOM   3496 O  OD1 . ASP   B 1 226 ? 17.566  -12.653 17.171  1.00 42.79 ? 226 ASP   B OD1 1 
ATOM   3497 O  OD2 . ASP   B 1 226 ? 16.889  -13.923 18.859  1.00 50.63 ? 226 ASP   B OD2 1 
ATOM   3498 N  N   . TRP   B 1 227 ? 12.551  -12.555 15.438  1.00 19.63 ? 227 TRP   B N   1 
ATOM   3499 C  CA  . TRP   B 1 227 ? 11.459  -13.117 14.663  1.00 18.10 ? 227 TRP   B CA  1 
ATOM   3500 C  C   . TRP   B 1 227 ? 11.537  -12.767 13.167  1.00 17.05 ? 227 TRP   B C   1 
ATOM   3501 O  O   . TRP   B 1 227 ? 11.295  -13.636 12.328  1.00 15.72 ? 227 TRP   B O   1 
ATOM   3502 C  CB  . TRP   B 1 227 ? 10.117  -12.675 15.241  1.00 16.61 ? 227 TRP   B CB  1 
ATOM   3503 C  CG  . TRP   B 1 227 ? 8.949   -13.267 14.521  1.00 16.26 ? 227 TRP   B CG  1 
ATOM   3504 C  CD1 . TRP   B 1 227 ? 8.465   -14.544 14.601  1.00 15.14 ? 227 TRP   B CD1 1 
ATOM   3505 C  CD2 . TRP   B 1 227 ? 8.108   -12.568 13.575  1.00 15.70 ? 227 TRP   B CD2 1 
ATOM   3506 N  NE1 . TRP   B 1 227 ? 7.366   -14.679 13.808  1.00 15.38 ? 227 TRP   B NE1 1 
ATOM   3507 C  CE2 . TRP   B 1 227 ? 7.139   -13.495 13.139  1.00 14.40 ? 227 TRP   B CE2 1 
ATOM   3508 C  CE3 . TRP   B 1 227 ? 8.096   -11.269 13.052  1.00 15.01 ? 227 TRP   B CE3 1 
ATOM   3509 C  CZ2 . TRP   B 1 227 ? 6.163   -13.141 12.221  1.00 14.38 ? 227 TRP   B CZ2 1 
ATOM   3510 C  CZ3 . TRP   B 1 227 ? 7.116   -10.919 12.168  1.00 14.57 ? 227 TRP   B CZ3 1 
ATOM   3511 C  CH2 . TRP   B 1 227 ? 6.150   -11.843 11.762  1.00 15.01 ? 227 TRP   B CH2 1 
ATOM   3512 N  N   . ALA   B 1 228 ? 11.862  -11.524 12.853  1.00 17.55 ? 228 ALA   B N   1 
ATOM   3513 C  CA  . ALA   B 1 228 ? 11.730  -10.999 11.494  1.00 16.12 ? 228 ALA   B CA  1 
ATOM   3514 C  C   . ALA   B 1 228 ? 12.918  -11.380 10.614  1.00 17.07 ? 228 ALA   B C   1 
ATOM   3515 O  O   . ALA   B 1 228 ? 13.645  -10.513 10.152  1.00 18.74 ? 228 ALA   B O   1 
ATOM   3516 C  CB  . ALA   B 1 228 ? 11.548  -9.495  11.518  1.00 16.28 ? 228 ALA   B CB  1 
ATOM   3517 N  N   . ASP   B 1 229 ? 13.076  -12.677 10.347  1.00 15.66 ? 229 ASP   B N   1 
ATOM   3518 C  CA  . ASP   B 1 229 ? 13.940  -13.155 9.287   1.00 15.29 ? 229 ASP   B CA  1 
ATOM   3519 C  C   . ASP   B 1 229 ? 13.145  -13.189 7.974   1.00 14.49 ? 229 ASP   B C   1 
ATOM   3520 O  O   . ASP   B 1 229 ? 11.965  -12.807 7.914   1.00 12.94 ? 229 ASP   B O   1 
ATOM   3521 C  CB  . ASP   B 1 229 ? 14.503  -14.511 9.657   1.00 17.20 ? 229 ASP   B CB  1 
ATOM   3522 C  CG  . ASP   B 1 229 ? 13.500  -15.649 9.803   1.00 18.83 ? 229 ASP   B CG  1 
ATOM   3523 O  OD1 . ASP   B 1 229 ? 12.312  -15.495 9.386   1.00 17.04 ? 229 ASP   B OD1 1 
ATOM   3524 O  OD2 . ASP   B 1 229 ? 13.897  -16.694 10.367  1.00 20.70 ? 229 ASP   B OD2 1 
ATOM   3525 N  N   . ALA   B 1 230 ? 13.789  -13.665 6.928   1.00 14.57 ? 230 ALA   B N   1 
ATOM   3526 C  CA  . ALA   B 1 230 ? 13.206  -13.589 5.597   1.00 14.21 ? 230 ALA   B CA  1 
ATOM   3527 C  C   . ALA   B 1 230 ? 12.027  -14.549 5.443   1.00 12.87 ? 230 ALA   B C   1 
ATOM   3528 O  O   . ALA   B 1 230 ? 11.205  -14.345 4.558   1.00 12.73 ? 230 ALA   B O   1 
ATOM   3529 C  CB  . ALA   B 1 230 ? 14.242  -13.853 4.533   1.00 14.54 ? 230 ALA   B CB  1 
ATOM   3530 N  N   . ARG   B 1 231 ? 11.890  -15.561 6.297   1.00 12.34 ? 231 ARG   B N   1 
ATOM   3531 C  CA  . ARG   B 1 231 ? 10.688  -16.385 6.255   1.00 12.62 ? 231 ARG   B CA  1 
ATOM   3532 C  C   . ARG   B 1 231 ? 9.504   -15.702 6.956   1.00 12.88 ? 231 ARG   B C   1 
ATOM   3533 O  O   . ARG   B 1 231 ? 8.370   -16.167 6.811   1.00 13.28 ? 231 ARG   B O   1 
ATOM   3534 C  CB  . ARG   B 1 231 ? 11.003  -17.743 6.895   1.00 13.53 ? 231 ARG   B CB  1 
ATOM   3535 C  CG  . ARG   B 1 231 ? 9.829   -18.705 7.036   1.00 13.74 ? 231 ARG   B CG  1 
ATOM   3536 C  CD  . ARG   B 1 231 ? 9.147   -19.062 5.729   1.00 14.30 ? 231 ARG   B CD  1 
ATOM   3537 N  NE  . ARG   B 1 231 ? 7.972   -19.891 5.900   1.00 14.67 ? 231 ARG   B NE  1 
ATOM   3538 C  CZ  . ARG   B 1 231 ? 6.736   -19.488 6.227   1.00 13.70 ? 231 ARG   B CZ  1 
ATOM   3539 N  NH1 . ARG   B 1 231 ? 6.454   -18.210 6.375   1.00 13.67 ? 231 ARG   B NH1 1 
ATOM   3540 N  NH2 . ARG   B 1 231 ? 5.769   -20.381 6.328   1.00 14.37 ? 231 ARG   B NH2 1 
ATOM   3541 N  N   . HIS   B 1 232 ? 9.741   -14.640 7.746   1.00 12.38 ? 232 HIS   B N   1 
ATOM   3542 C  CA  . HIS   B 1 232 ? 8.687   -14.032 8.525   1.00 12.36 ? 232 HIS   B CA  1 
ATOM   3543 C  C   . HIS   B 1 232 ? 8.401   -12.566 8.208   1.00 11.83 ? 232 HIS   B C   1 
ATOM   3544 O  O   . HIS   B 1 232 ? 7.409   -12.041 8.724   1.00 11.38 ? 232 HIS   B O   1 
ATOM   3545 C  CB  . HIS   B 1 232 ? 8.964   -14.226 10.027  1.00 13.32 ? 232 HIS   B CB  1 
ATOM   3546 C  CG  . HIS   B 1 232 ? 8.913   -15.670 10.354  1.00 14.57 ? 232 HIS   B CG  1 
ATOM   3547 N  ND1 . HIS   B 1 232 ? 10.001  -16.519 10.237  1.00 15.97 ? 232 HIS   B ND1 1 
ATOM   3548 C  CD2 . HIS   B 1 232 ? 7.876   -16.422 10.765  1.00 14.84 ? 232 HIS   B CD2 1 
ATOM   3549 C  CE1 . HIS   B 1 232 ? 9.622   -17.747 10.605  1.00 17.21 ? 232 HIS   B CE1 1 
ATOM   3550 N  NE2 . HIS   B 1 232 ? 8.333   -17.714 10.932  1.00 16.66 ? 232 HIS   B NE2 1 
ATOM   3551 N  N   . TYR   B 1 233 ? 9.271   -11.881 7.452   1.00 11.00 ? 233 TYR   B N   1 
ATOM   3552 C  CA  . TYR   B 1 233 ? 9.078   -10.460 7.235   1.00 11.08 ? 233 TYR   B CA  1 
ATOM   3553 C  C   . TYR   B 1 233 ? 9.647   -10.078 5.877   1.00 11.23 ? 233 TYR   B C   1 
ATOM   3554 O  O   . TYR   B 1 233 ? 10.749  -10.503 5.537   1.00 12.11 ? 233 TYR   B O   1 
ATOM   3555 C  CB  . TYR   B 1 233 ? 9.768   -9.659  8.344   1.00 11.88 ? 233 TYR   B CB  1 
ATOM   3556 C  CG  . TYR   B 1 233 ? 9.182   -8.292  8.571   1.00 13.04 ? 233 TYR   B CG  1 
ATOM   3557 C  CD1 . TYR   B 1 233 ? 9.426   -7.241  7.694   1.00 14.94 ? 233 TYR   B CD1 1 
ATOM   3558 C  CD2 . TYR   B 1 233 ? 8.345   -8.071  9.650   1.00 14.76 ? 233 TYR   B CD2 1 
ATOM   3559 C  CE1 . TYR   B 1 233 ? 8.828   -6.010  7.882   1.00 16.24 ? 233 TYR   B CE1 1 
ATOM   3560 C  CE2 . TYR   B 1 233 ? 7.793   -6.816  9.884   1.00 16.31 ? 233 TYR   B CE2 1 
ATOM   3561 C  CZ  . TYR   B 1 233 ? 8.037   -5.788  8.994   1.00 17.78 ? 233 TYR   B CZ  1 
ATOM   3562 O  OH  . TYR   B 1 233 ? 7.422   -4.594  9.235   1.00 20.27 ? 233 TYR   B OH  1 
ATOM   3563 N  N   . ARG   B 1 234 ? 8.889   -9.278  5.135   1.00 10.10 ? 234 ARG   B N   1 
ATOM   3564 C  CA  . ARG   B 1 234 ? 9.371   -8.689  3.904   1.00 9.89  ? 234 ARG   B CA  1 
ATOM   3565 C  C   . ARG   B 1 234 ? 8.890   -7.269  3.752   1.00 10.31 ? 234 ARG   B C   1 
ATOM   3566 O  O   . ARG   B 1 234 ? 7.846   -6.869  4.276   1.00 9.89  ? 234 ARG   B O   1 
ATOM   3567 C  CB  . ARG   B 1 234 ? 8.881   -9.475  2.680   1.00 10.15 ? 234 ARG   B CB  1 
ATOM   3568 C  CG  . ARG   B 1 234 ? 9.286   -10.933 2.639   1.00 10.64 ? 234 ARG   B CG  1 
ATOM   3569 C  CD  . ARG   B 1 234 ? 10.746  -11.144 2.336   1.00 10.42 ? 234 ARG   B CD  1 
ATOM   3570 N  NE  . ARG   B 1 234 ? 11.002  -12.568 2.360   1.00 10.80 ? 234 ARG   B NE  1 
ATOM   3571 C  CZ  . ARG   B 1 234 ? 10.597  -13.445 1.434   1.00 12.86 ? 234 ARG   B CZ  1 
ATOM   3572 N  NH1 . ARG   B 1 234 ? 10.206  -13.042 0.239   1.00 12.66 ? 234 ARG   B NH1 1 
ATOM   3573 N  NH2 . ARG   B 1 234 ? 10.630  -14.743 1.685   1.00 13.06 ? 234 ARG   B NH2 1 
ATOM   3574 N  N   . PHE   B 1 235 ? 9.641   -6.531  2.938   1.00 11.46 ? 235 PHE   B N   1 
ATOM   3575 C  CA  . PHE   B 1 235 ? 9.312   -5.175  2.523   1.00 11.99 ? 235 PHE   B CA  1 
ATOM   3576 C  C   . PHE   B 1 235 ? 9.282   -5.051  1.014   1.00 13.11 ? 235 PHE   B C   1 
ATOM   3577 O  O   . PHE   B 1 235 ? 10.117  -5.641  0.335   1.00 12.36 ? 235 PHE   B O   1 
ATOM   3578 C  CB  . PHE   B 1 235 ? 10.411  -4.185  2.902   1.00 12.61 ? 235 PHE   B CB  1 
ATOM   3579 C  CG  . PHE   B 1 235 ? 10.527  -3.845  4.369   1.00 14.31 ? 235 PHE   B CG  1 
ATOM   3580 C  CD1 . PHE   B 1 235 ? 9.717   -2.863  4.907   1.00 16.79 ? 235 PHE   B CD1 1 
ATOM   3581 C  CD2 . PHE   B 1 235 ? 11.424  -4.504  5.195   1.00 14.97 ? 235 PHE   B CD2 1 
ATOM   3582 C  CE1 . PHE   B 1 235 ? 9.845   -2.516  6.251   1.00 17.17 ? 235 PHE   B CE1 1 
ATOM   3583 C  CE2 . PHE   B 1 235 ? 11.537  -4.137  6.525   1.00 16.99 ? 235 PHE   B CE2 1 
ATOM   3584 C  CZ  . PHE   B 1 235 ? 10.750  -3.148  7.040   1.00 16.15 ? 235 PHE   B CZ  1 
ATOM   3585 N  N   . SER   B 1 236 ? 8.320   -4.275  0.501   1.00 15.02 ? 236 SER   B N   1 
ATOM   3586 C  CA  . SER   B 1 236 ? 8.421   -3.795  -0.871  1.00 16.54 ? 236 SER   B CA  1 
ATOM   3587 C  C   . SER   B 1 236 ? 7.850   -2.389  -0.962  1.00 16.08 ? 236 SER   B C   1 
ATOM   3588 O  O   . SER   B 1 236 ? 6.795   -2.099  -0.417  1.00 15.33 ? 236 SER   B O   1 
ATOM   3589 C  CB  . SER   B 1 236 ? 7.782   -4.740  -1.866  1.00 20.92 ? 236 SER   B CB  1 
ATOM   3590 O  OG  . SER   B 1 236 ? 6.379   -4.669  -1.729  1.00 29.72 ? 236 SER   B OG  1 
ATOM   3591 N  N   . ALA   B 1 237 ? 8.603   -1.492  -1.600  1.00 16.72 ? 237 ALA   B N   1 
ATOM   3592 C  CA  . ALA   B 1 237 ? 8.147   -0.146  -1.831  1.00 18.63 ? 237 ALA   B CA  1 
ATOM   3593 C  C   . ALA   B 1 237 ? 9.091   0.508   -2.826  1.00 20.95 ? 237 ALA   B C   1 
ATOM   3594 O  O   . ALA   B 1 237 ? 10.309  0.358   -2.732  1.00 18.34 ? 237 ALA   B O   1 
ATOM   3595 C  CB  . ALA   B 1 237 ? 8.125   0.634   -0.547  1.00 20.33 ? 237 ALA   B CB  1 
ATOM   3596 N  N   . SER   B 1 238 ? 8.529   1.280   -3.739  1.00 21.83 ? 238 SER   B N   1 
ATOM   3597 C  CA  . SER   B 1 238 ? 9.359   2.014   -4.679  1.00 24.73 ? 238 SER   B CA  1 
ATOM   3598 C  C   . SER   B 1 238 ? 10.191  3.040   -3.912  1.00 23.33 ? 238 SER   B C   1 
ATOM   3599 O  O   . SER   B 1 238 ? 9.706   3.701   -2.993  1.00 23.45 ? 238 SER   B O   1 
ATOM   3600 C  CB  . SER   B 1 238 ? 8.531   2.672   -5.750  1.00 31.14 ? 238 SER   B CB  1 
ATOM   3601 O  OG  . SER   B 1 238 ? 7.664   3.588   -5.117  1.00 37.37 ? 238 SER   B OG  1 
ATOM   3602 N  N   . GLY   B 1 239 ? 11.475  3.132   -4.270  1.00 21.43 ? 239 GLY   B N   1 
ATOM   3603 C  CA  . GLY   B 1 239 ? 12.358  4.110   -3.666  1.00 21.27 ? 239 GLY   B CA  1 
ATOM   3604 C  C   . GLY   B 1 239 ? 13.040  3.603   -2.408  1.00 20.20 ? 239 GLY   B C   1 
ATOM   3605 O  O   . GLY   B 1 239 ? 13.999  4.212   -1.944  1.00 19.52 ? 239 GLY   B O   1 
ATOM   3606 N  N   . LEU   B 1 240 ? 12.532  2.512   -1.805  1.00 17.48 ? 240 LEU   B N   1 
ATOM   3607 C  CA  . LEU   B 1 240 ? 13.071  2.104   -0.523  1.00 15.65 ? 240 LEU   B CA  1 
ATOM   3608 C  C   . LEU   B 1 240 ? 14.524  1.639   -0.641  1.00 15.38 ? 240 LEU   B C   1 
ATOM   3609 O  O   . LEU   B 1 240 ? 15.332  1.934   0.217   1.00 15.63 ? 240 LEU   B O   1 
ATOM   3610 C  CB  . LEU   B 1 240 ? 12.194  1.039   0.123   1.00 16.01 ? 240 LEU   B CB  1 
ATOM   3611 C  CG  . LEU   B 1 240 ? 12.705  0.495   1.452   1.00 15.82 ? 240 LEU   B CG  1 
ATOM   3612 C  CD1 . LEU   B 1 240 ? 12.848  1.601   2.461   1.00 17.34 ? 240 LEU   B CD1 1 
ATOM   3613 C  CD2 . LEU   B 1 240 ? 11.798  -0.621  2.002   1.00 16.91 ? 240 LEU   B CD2 1 
ATOM   3614 N  N   . LEU   B 1 241 ? 14.847  0.855   -1.652  1.00 15.09 ? 241 LEU   B N   1 
ATOM   3615 C  CA  . LEU   B 1 241 ? 16.196  0.311   -1.742  1.00 15.62 ? 241 LEU   B CA  1 
ATOM   3616 C  C   . LEU   B 1 241 ? 17.225  1.451   -1.784  1.00 16.75 ? 241 LEU   B C   1 
ATOM   3617 O  O   . LEU   B 1 241 ? 18.236  1.415   -1.091  1.00 16.36 ? 241 LEU   B O   1 
ATOM   3618 C  CB  . LEU   B 1 241 ? 16.322  -0.605  -2.949  1.00 15.99 ? 241 LEU   B CB  1 
ATOM   3619 C  CG  . LEU   B 1 241 ? 17.726  -1.190  -3.136  1.00 17.89 ? 241 LEU   B CG  1 
ATOM   3620 C  CD1 . LEU   B 1 241 ? 18.240  -1.930  -1.953  1.00 18.03 ? 241 LEU   B CD1 1 
ATOM   3621 C  CD2 . LEU   B 1 241 ? 17.809  -2.119  -4.324  1.00 19.70 ? 241 LEU   B CD2 1 
ATOM   3622 N  N   . ALA   B 1 242 ? 16.949  2.457   -2.612  1.00 19.08 ? 242 ALA   B N   1 
ATOM   3623 C  CA  . ALA   B 1 242 ? 17.816  3.629   -2.735  1.00 21.17 ? 242 ALA   B CA  1 
ATOM   3624 C  C   . ALA   B 1 242 ? 17.971  4.321   -1.391  1.00 21.00 ? 242 ALA   B C   1 
ATOM   3625 O  O   . ALA   B 1 242 ? 19.067  4.715   -1.005  1.00 21.16 ? 242 ALA   B O   1 
ATOM   3626 C  CB  . ALA   B 1 242 ? 17.283  4.581   -3.791  1.00 22.17 ? 242 ALA   B CB  1 
ATOM   3627 N  N   . SER   B 1 243 ? 16.878  4.419   -0.624  1.00 20.33 ? 243 SER   B N   1 
ATOM   3628 C  CA  . SER   B 1 243 ? 16.951  5.065   0.675   1.00 20.30 ? 243 SER   B CA  1 
ATOM   3629 C  C   . SER   B 1 243 ? 17.807  4.249   1.649   1.00 19.02 ? 243 SER   B C   1 
ATOM   3630 O  O   . SER   B 1 243 ? 18.591  4.793   2.437   1.00 19.79 ? 243 SER   B O   1 
ATOM   3631 C  CB  . SER   B 1 243 ? 15.553  5.318   1.217   1.00 19.28 ? 243 SER   B CB  1 
ATOM   3632 O  OG  . SER   B 1 243 ? 15.649  5.922   2.496   1.00 21.41 ? 243 SER   B OG  1 
ATOM   3633 N  N   . LEU   B 1 244 ? 17.652  2.926   1.623   1.00 17.72 ? 244 LEU   B N   1 
ATOM   3634 C  CA  . LEU   B 1 244 ? 18.418  2.063   2.510   1.00 17.83 ? 244 LEU   B CA  1 
ATOM   3635 C  C   . LEU   B 1 244 ? 19.898  2.140   2.157   1.00 18.73 ? 244 LEU   B C   1 
ATOM   3636 O  O   . LEU   B 1 244 ? 20.752  2.168   3.037   1.00 19.39 ? 244 LEU   B O   1 
ATOM   3637 C  CB  . LEU   B 1 244 ? 17.930  0.613   2.415   1.00 17.89 ? 244 LEU   B CB  1 
ATOM   3638 C  CG  . LEU   B 1 244 ? 16.483  0.363   2.861   1.00 18.01 ? 244 LEU   B CG  1 
ATOM   3639 C  CD1 . LEU   B 1 244 ? 16.044  -1.049  2.602   1.00 18.17 ? 244 LEU   B CD1 1 
ATOM   3640 C  CD2 . LEU   B 1 244 ? 16.318  0.643   4.324   1.00 18.11 ? 244 LEU   B CD2 1 
ATOM   3641 N  N   . LEU   B 1 245 ? 20.198  2.111   0.864   1.00 18.86 ? 245 LEU   B N   1 
ATOM   3642 C  CA  . LEU   B 1 245 ? 21.589  2.148   0.420   1.00 21.09 ? 245 LEU   B CA  1 
ATOM   3643 C  C   . LEU   B 1 245 ? 22.248  3.469   0.810   1.00 22.94 ? 245 LEU   B C   1 
ATOM   3644 O  O   . LEU   B 1 245 ? 23.404  3.492   1.227   1.00 22.58 ? 245 LEU   B O   1 
ATOM   3645 C  CB  . LEU   B 1 245 ? 21.655  1.910   -1.077  1.00 19.63 ? 245 LEU   B CB  1 
ATOM   3646 C  CG  . LEU   B 1 245 ? 21.474  0.458   -1.516  1.00 19.44 ? 245 LEU   B CG  1 
ATOM   3647 C  CD1 . LEU   B 1 245 ? 21.423  0.359   -3.010  1.00 18.33 ? 245 LEU   B CD1 1 
ATOM   3648 C  CD2 . LEU   B 1 245 ? 22.537  -0.421  -0.911  1.00 20.79 ? 245 LEU   B CD2 1 
ATOM   3649 N  N   . LYS   B 1 246 ? 21.479  4.549   0.708   1.00 25.21 ? 246 LYS   B N   1 
ATOM   3650 C  CA  . LYS   B 1 246 ? 21.954  5.870   1.086   1.00 29.61 ? 246 LYS   B CA  1 
ATOM   3651 C  C   . LYS   B 1 246 ? 22.264  5.904   2.573   1.00 27.91 ? 246 LYS   B C   1 
ATOM   3652 O  O   . LYS   B 1 246 ? 23.282  6.448   2.978   1.00 29.08 ? 246 LYS   B O   1 
ATOM   3653 C  CB  . LYS   B 1 246 ? 20.936  6.944   0.697   1.00 32.08 ? 246 LYS   B CB  1 
ATOM   3654 C  CG  . LYS   B 1 246 ? 21.312  8.349   1.123   1.00 38.46 ? 246 LYS   B CG  1 
ATOM   3655 C  CD  . LYS   B 1 246 ? 20.705  9.401   0.199   1.00 46.10 ? 246 LYS   B CD  1 
ATOM   3656 C  CE  . LYS   B 1 246 ? 21.328  10.755  0.414   1.00 51.66 ? 246 LYS   B CE  1 
ATOM   3657 N  NZ  . LYS   B 1 246 ? 21.046  11.239  1.767   1.00 51.99 ? 246 LYS   B NZ  1 
ATOM   3658 N  N   . ALA   B 1 247 ? 21.369  5.349   3.402   1.00 25.84 ? 247 ALA   B N   1 
ATOM   3659 C  CA  . ALA   B 1 247 ? 21.632  5.267   4.828   1.00 25.57 ? 247 ALA   B CA  1 
ATOM   3660 C  C   . ALA   B 1 247 ? 22.902  4.475   5.114   1.00 26.81 ? 247 ALA   B C   1 
ATOM   3661 O  O   . ALA   B 1 247 ? 23.550  4.684   6.135   1.00 27.03 ? 247 ALA   B O   1 
ATOM   3662 C  CB  . ALA   B 1 247 ? 20.445  4.705   5.563   1.00 24.71 ? 247 ALA   B CB  1 
ATOM   3663 N  N   . LEU   B 1 248 ? 23.249  3.531   4.241   1.00 26.70 ? 248 LEU   B N   1 
ATOM   3664 C  CA  . LEU   B 1 248 ? 24.391  2.671   4.485   1.00 26.74 ? 248 LEU   B CA  1 
ATOM   3665 C  C   . LEU   B 1 248 ? 25.665  3.248   3.852   1.00 28.36 ? 248 LEU   B C   1 
ATOM   3666 O  O   . LEU   B 1 248 ? 26.699  2.600   3.930   1.00 29.17 ? 248 LEU   B O   1 
ATOM   3667 C  CB  . LEU   B 1 248 ? 24.054  1.277   3.967   1.00 26.77 ? 248 LEU   B CB  1 
ATOM   3668 C  CG  . LEU   B 1 248 ? 23.042  0.503   4.817   1.00 26.56 ? 248 LEU   B CG  1 
ATOM   3669 C  CD1 . LEU   B 1 248 ? 22.444  -0.711  4.124   1.00 26.07 ? 248 LEU   B CD1 1 
ATOM   3670 C  CD2 . LEU   B 1 248 ? 23.703  0.066   6.117   1.00 27.24 ? 248 LEU   B CD2 1 
ATOM   3671 N  N   . GLY   B 1 249 ? 25.565  4.402   3.177   1.00 30.99 ? 249 GLY   B N   1 
ATOM   3672 C  CA  . GLY   B 1 249 ? 26.712  5.079   2.587   1.00 33.22 ? 249 GLY   B CA  1 
ATOM   3673 C  C   . GLY   B 1 249 ? 26.942  4.752   1.111   1.00 35.21 ? 249 GLY   B C   1 
ATOM   3674 O  O   . GLY   B 1 249 ? 28.008  5.030   0.568   1.00 36.88 ? 249 GLY   B O   1 
ATOM   3675 N  N   . HIS   B 1 250 ? 25.958  4.172   0.432   1.00 34.41 ? 250 HIS   B N   1 
ATOM   3676 C  CA  . HIS   B 1 250 ? 26.051  3.976   -1.002  1.00 36.15 ? 250 HIS   B CA  1 
ATOM   3677 C  C   . HIS   B 1 250 ? 25.126  4.996   -1.664  1.00 39.03 ? 250 HIS   B C   1 
ATOM   3678 O  O   . HIS   B 1 250 ? 24.231  4.462   -2.323  1.00 45.46 ? 250 HIS   B O   1 
ATOM   3679 C  CB  . HIS   B 1 250 ? 25.806  2.505   -1.359  1.00 37.34 ? 250 HIS   B CB  1 
ATOM   3680 C  CG  . HIS   B 1 250 ? 26.889  1.621   -0.829  1.00 37.07 ? 250 HIS   B CG  1 
ATOM   3681 N  ND1 . HIS   B 1 250 ? 26.937  1.164   0.470   1.00 39.35 ? 250 HIS   B ND1 1 
ATOM   3682 C  CD2 . HIS   B 1 250 ? 28.002  1.164   -1.419  1.00 34.62 ? 250 HIS   B CD2 1 
ATOM   3683 C  CE1 . HIS   B 1 250 ? 28.027  0.417   0.634   1.00 35.21 ? 250 HIS   B CE1 1 
ATOM   3684 N  NE2 . HIS   B 1 250 ? 28.684  0.414   -0.498  1.00 32.70 ? 250 HIS   B NE2 1 
HETATM 3685 C  C1  . A1ICA C 2 .   ? 0.734   -18.805 -34.461 0.60 18.12 ? 301 A1ICA A C1  1 
HETATM 3686 C  C2  . A1ICA C 2 .   ? 0.108   -18.076 -33.435 0.60 18.40 ? 301 A1ICA A C2  1 
HETATM 3687 C  C3  . A1ICA C 2 .   ? 0.274   -16.770 -33.333 0.60 19.25 ? 301 A1ICA A C3  1 
HETATM 3688 C  C4  . A1ICA C 2 .   ? -0.281  -15.934 -32.277 0.60 20.59 ? 301 A1ICA A C4  1 
HETATM 3689 C  C5  . A1ICA C 2 .   ? 0.087   -14.604 -32.064 0.60 22.49 ? 301 A1ICA A C5  1 
HETATM 3690 C  C6  . A1ICA C 2 .   ? -0.475  -13.867 -31.032 0.60 25.42 ? 301 A1ICA A C6  1 
HETATM 3691 C  C7  . A1ICA C 2 .   ? -1.364  -14.477 -30.177 0.60 23.07 ? 301 A1ICA A C7  1 
HETATM 3692 CL CL1 . A1ICA C 2 .   ? -2.068  -13.570 -28.885 0.60 29.19 ? 301 A1ICA A CL1 1 
HETATM 3693 C  C8  . A1ICA C 2 .   ? -1.708  -15.796 -30.323 0.60 22.27 ? 301 A1ICA A C8  1 
HETATM 3694 C  C9  . A1ICA C 2 .   ? -1.183  -16.509 -31.381 0.60 20.04 ? 301 A1ICA A C9  1 
HETATM 3695 C  C1  . A1ICA D 2 .   ? 2.875   -7.390  -3.794  0.60 19.37 ? 301 A1ICA B C1  1 
HETATM 3696 C  C2  . A1ICA D 2 .   ? 3.580   -7.466  -5.025  0.60 19.02 ? 301 A1ICA B C2  1 
HETATM 3697 C  C3  . A1ICA D 2 .   ? 3.455   -6.516  -5.943  0.60 19.75 ? 301 A1ICA B C3  1 
HETATM 3698 C  C4  . A1ICA D 2 .   ? 3.972   -6.602  -7.302  0.60 18.47 ? 301 A1ICA B C4  1 
HETATM 3699 C  C5  . A1ICA D 2 .   ? 4.824   -7.664  -7.598  0.60 18.30 ? 301 A1ICA B C5  1 
HETATM 3700 C  C6  . A1ICA D 2 .   ? 5.347   -7.838  -8.860  0.60 18.42 ? 301 A1ICA B C6  1 
HETATM 3701 C  C7  . A1ICA D 2 .   ? 4.999   -6.949  -9.838  0.60 18.97 ? 301 A1ICA B C7  1 
HETATM 3702 CL CL1 . A1ICA D 2 .   ? 5.684   -7.164  -11.406 0.60 20.78 ? 301 A1ICA B CL1 1 
HETATM 3703 C  C8  . A1ICA D 2 .   ? 4.151   -5.892  -9.597  0.60 19.88 ? 301 A1ICA B C8  1 
HETATM 3704 C  C9  . A1ICA D 2 .   ? 3.619   -5.734  -8.332  0.60 18.50 ? 301 A1ICA B C9  1 
HETATM 3705 C  C1  . GOL   E 3 .   ? 0.956   6.562   0.014   0.60 24.24 ? 302 GOL   B C1  1 
HETATM 3706 O  O1  . GOL   E 3 .   ? 2.135   5.900   -0.415  0.60 27.59 ? 302 GOL   B O1  1 
HETATM 3707 C  C2  . GOL   E 3 .   ? 0.055   5.533   0.642   0.60 21.23 ? 302 GOL   B C2  1 
HETATM 3708 O  O2  . GOL   E 3 .   ? -0.269  4.574   -0.360  0.60 19.36 ? 302 GOL   B O2  1 
HETATM 3709 C  C3  . GOL   E 3 .   ? 0.723   4.839   1.809   0.60 21.86 ? 302 GOL   B C3  1 
HETATM 3710 O  O3  . GOL   E 3 .   ? -0.106  3.823   2.342   0.60 18.82 ? 302 GOL   B O3  1 
HETATM 3711 O  O   . HOH   F 4 .   ? -0.295  -16.513 -49.710 1.00 30.98 ? 401 HOH   A O   1 
HETATM 3712 O  O   . HOH   F 4 .   ? 17.039  -25.560 -50.803 1.00 35.80 ? 402 HOH   A O   1 
HETATM 3713 O  O   . HOH   F 4 .   ? -11.495 -31.649 -45.656 1.00 37.43 ? 403 HOH   A O   1 
HETATM 3714 O  O   . HOH   F 4 .   ? -0.108  -19.988 -55.631 1.00 28.83 ? 404 HOH   A O   1 
HETATM 3715 O  O   . HOH   F 4 .   ? -9.029  -36.489 -37.690 1.00 30.79 ? 405 HOH   A O   1 
HETATM 3716 O  O   . HOH   F 4 .   ? 21.908  -29.067 -40.695 1.00 42.96 ? 406 HOH   A O   1 
HETATM 3717 O  O   . HOH   F 4 .   ? 9.835   -33.991 -48.393 1.00 40.59 ? 407 HOH   A O   1 
HETATM 3718 O  O   . HOH   F 4 .   ? -10.016 -3.176  -24.273 1.00 47.40 ? 408 HOH   A O   1 
HETATM 3719 O  O   . HOH   F 4 .   ? 16.295  -13.580 -29.105 1.00 46.54 ? 409 HOH   A O   1 
HETATM 3720 O  O   . HOH   F 4 .   ? -12.326 -19.879 -49.170 1.00 26.78 ? 410 HOH   A O   1 
HETATM 3721 O  O   . HOH   F 4 .   ? 9.516   -15.699 -24.296 1.00 28.26 ? 411 HOH   A O   1 
HETATM 3722 O  O   . HOH   F 4 .   ? 2.110   -40.556 -46.770 1.00 38.12 ? 412 HOH   A O   1 
HETATM 3723 O  O   . HOH   F 4 .   ? -17.903 -26.362 -46.695 1.00 34.30 ? 413 HOH   A O   1 
HETATM 3724 O  O   . HOH   F 4 .   ? 10.431  -15.240 -35.276 1.00 15.76 ? 414 HOH   A O   1 
HETATM 3725 O  O   . HOH   F 4 .   ? -12.485 -29.502 -43.523 1.00 36.50 ? 415 HOH   A O   1 
HETATM 3726 O  O   . HOH   F 4 .   ? 22.185  -21.254 -42.668 1.00 42.21 ? 416 HOH   A O   1 
HETATM 3727 O  O   . HOH   F 4 .   ? 2.314   -24.509 -54.675 1.00 49.08 ? 417 HOH   A O   1 
HETATM 3728 O  O   . HOH   F 4 .   ? -26.699 -18.421 -37.347 1.00 18.19 ? 418 HOH   A O   1 
HETATM 3729 O  O   . HOH   F 4 .   ? -1.189  -14.636 -14.985 1.00 22.65 ? 419 HOH   A O   1 
HETATM 3730 O  O   . HOH   F 4 .   ? 1.197   -14.351 -21.032 1.00 19.18 ? 420 HOH   A O   1 
HETATM 3731 O  O   . HOH   F 4 .   ? -14.998 -25.249 -32.656 1.00 24.05 ? 421 HOH   A O   1 
HETATM 3732 O  O   . HOH   F 4 .   ? -9.879  -28.094 -53.093 1.00 39.35 ? 422 HOH   A O   1 
HETATM 3733 O  O   . HOH   F 4 .   ? 19.223  -34.543 -40.160 1.00 36.15 ? 423 HOH   A O   1 
HETATM 3734 O  O   . HOH   F 4 .   ? 7.341   -15.832 -20.843 1.00 16.87 ? 424 HOH   A O   1 
HETATM 3735 O  O   . HOH   F 4 .   ? 4.769   -37.229 -21.912 1.00 34.99 ? 425 HOH   A O   1 
HETATM 3736 O  O   . HOH   F 4 .   ? -5.429  -13.043 -29.529 1.00 37.25 ? 426 HOH   A O   1 
HETATM 3737 O  O   . HOH   F 4 .   ? -17.464 -23.575 -54.976 1.00 42.26 ? 427 HOH   A O   1 
HETATM 3738 O  O   . HOH   F 4 .   ? 0.252   -41.430 -40.904 1.00 22.27 ? 428 HOH   A O   1 
HETATM 3739 O  O   . HOH   F 4 .   ? 8.401   -36.944 -28.607 1.00 42.23 ? 429 HOH   A O   1 
HETATM 3740 O  O   . HOH   F 4 .   ? 14.170  -20.243 -25.387 1.00 14.08 ? 430 HOH   A O   1 
HETATM 3741 O  O   . HOH   F 4 .   ? -3.999  -27.508 -20.100 1.00 16.25 ? 431 HOH   A O   1 
HETATM 3742 O  O   . HOH   F 4 .   ? -7.303  -29.676 -29.649 1.00 30.38 ? 432 HOH   A O   1 
HETATM 3743 O  O   . HOH   F 4 .   ? 2.944   -20.372 -55.339 1.00 25.62 ? 433 HOH   A O   1 
HETATM 3744 O  O   . HOH   F 4 .   ? -7.642  -32.348 -47.409 1.00 18.93 ? 434 HOH   A O   1 
HETATM 3745 O  O   . HOH   F 4 .   ? -8.254  -22.125 -17.636 1.00 21.08 ? 435 HOH   A O   1 
HETATM 3746 O  O   . HOH   F 4 .   ? -9.017  -19.240 -54.950 1.00 37.73 ? 436 HOH   A O   1 
HETATM 3747 O  O   . HOH   F 4 .   ? 0.429   -33.903 -27.554 1.00 27.81 ? 437 HOH   A O   1 
HETATM 3748 O  O   . HOH   F 4 .   ? -23.643 -16.011 -27.551 1.00 42.98 ? 438 HOH   A O   1 
HETATM 3749 O  O   . HOH   F 4 .   ? 1.277   -36.586 -33.222 1.00 24.22 ? 439 HOH   A O   1 
HETATM 3750 O  O   . HOH   F 4 .   ? -21.562 -20.370 -34.132 1.00 18.94 ? 440 HOH   A O   1 
HETATM 3751 O  O   . HOH   F 4 .   ? 7.527   -17.146 -41.452 1.00 12.52 ? 441 HOH   A O   1 
HETATM 3752 O  O   . HOH   F 4 .   ? 10.751  -12.743 -42.824 1.00 22.77 ? 442 HOH   A O   1 
HETATM 3753 O  O   . HOH   F 4 .   ? -7.756  -36.395 -41.615 1.00 29.57 ? 443 HOH   A O   1 
HETATM 3754 O  O   . HOH   F 4 .   ? 9.531   -32.317 -20.831 1.00 24.50 ? 444 HOH   A O   1 
HETATM 3755 O  O   . HOH   F 4 .   ? -20.835 -24.083 -21.965 1.00 40.71 ? 445 HOH   A O   1 
HETATM 3756 O  O   . HOH   F 4 .   ? 8.447   -34.220 -51.895 1.00 39.04 ? 446 HOH   A O   1 
HETATM 3757 O  O   . HOH   F 4 .   ? 20.431  -29.852 -27.384 1.00 42.17 ? 447 HOH   A O   1 
HETATM 3758 O  O   . HOH   F 4 .   ? 5.157   -36.147 -34.875 1.00 17.36 ? 448 HOH   A O   1 
HETATM 3759 O  O   . HOH   F 4 .   ? 4.431   -17.554 -23.945 1.00 23.27 ? 449 HOH   A O   1 
HETATM 3760 O  O   . HOH   F 4 .   ? 1.162   -13.033 -34.812 1.00 39.59 ? 450 HOH   A O   1 
HETATM 3761 O  O   . HOH   F 4 .   ? 21.380  -26.629 -40.870 1.00 35.65 ? 451 HOH   A O   1 
HETATM 3762 O  O   . HOH   F 4 .   ? 7.142   -18.699 -46.163 1.00 15.92 ? 452 HOH   A O   1 
HETATM 3763 O  O   . HOH   F 4 .   ? 3.981   -38.327 -35.919 1.00 29.67 ? 453 HOH   A O   1 
HETATM 3764 O  O   . HOH   F 4 .   ? 16.305  -15.000 -38.748 1.00 34.87 ? 454 HOH   A O   1 
HETATM 3765 O  O   . HOH   F 4 .   ? 1.330   -41.275 -38.130 1.00 27.87 ? 455 HOH   A O   1 
HETATM 3766 O  O   . HOH   F 4 .   ? 12.256  -25.519 -17.449 1.00 24.95 ? 456 HOH   A O   1 
HETATM 3767 O  O   . HOH   F 4 .   ? -9.021  -13.261 -39.150 1.00 27.88 ? 457 HOH   A O   1 
HETATM 3768 O  O   . HOH   F 4 .   ? -13.381 -23.968 -24.451 1.00 25.23 ? 458 HOH   A O   1 
HETATM 3769 O  O   . HOH   F 4 .   ? 17.414  -26.408 -34.330 1.00 16.91 ? 459 HOH   A O   1 
HETATM 3770 O  O   . HOH   F 4 .   ? -19.417 -12.650 -22.429 1.00 42.35 ? 460 HOH   A O   1 
HETATM 3771 O  O   . HOH   F 4 .   ? -18.019 -13.415 -35.928 1.00 35.11 ? 461 HOH   A O   1 
HETATM 3772 O  O   . HOH   F 4 .   ? -14.550 -26.139 -36.060 1.00 30.50 ? 462 HOH   A O   1 
HETATM 3773 O  O   . HOH   F 4 .   ? -0.059  -16.364 -13.671 1.00 34.50 ? 463 HOH   A O   1 
HETATM 3774 O  O   . HOH   F 4 .   ? 8.329   -19.246 -49.609 1.00 25.26 ? 464 HOH   A O   1 
HETATM 3775 O  O   . HOH   F 4 .   ? 15.249  -18.750 -33.992 1.00 13.26 ? 465 HOH   A O   1 
HETATM 3776 O  O   . HOH   F 4 .   ? -6.035  -30.671 -27.095 1.00 33.24 ? 466 HOH   A O   1 
HETATM 3777 O  O   . HOH   F 4 .   ? 3.340   -14.095 -46.064 1.00 32.66 ? 467 HOH   A O   1 
HETATM 3778 O  O   . HOH   F 4 .   ? -6.957  -12.968 -53.156 1.00 55.28 ? 468 HOH   A O   1 
HETATM 3779 O  O   . HOH   F 4 .   ? 17.512  -20.787 -18.690 1.00 36.61 ? 469 HOH   A O   1 
HETATM 3780 O  O   . HOH   F 4 .   ? -21.107 -14.214 -30.610 1.00 33.64 ? 470 HOH   A O   1 
HETATM 3781 O  O   . HOH   F 4 .   ? 2.545   -31.679 -18.275 1.00 25.01 ? 471 HOH   A O   1 
HETATM 3782 O  O   . HOH   F 4 .   ? -5.578  -24.743 -14.160 1.00 35.67 ? 472 HOH   A O   1 
HETATM 3783 O  O   . HOH   F 4 .   ? -9.061  -24.174 -18.781 1.00 27.22 ? 473 HOH   A O   1 
HETATM 3784 O  O   . HOH   F 4 .   ? -13.774 -27.909 -34.532 1.00 41.13 ? 474 HOH   A O   1 
HETATM 3785 O  O   . HOH   F 4 .   ? 2.195   -27.674 -16.228 1.00 29.74 ? 475 HOH   A O   1 
HETATM 3786 O  O   . HOH   F 4 .   ? 18.374  -19.012 -45.389 1.00 37.70 ? 476 HOH   A O   1 
HETATM 3787 O  O   . HOH   F 4 .   ? -3.074  -18.441 -34.282 1.00 23.78 ? 477 HOH   A O   1 
HETATM 3788 O  O   . HOH   F 4 .   ? -12.980 -30.685 -38.451 1.00 25.58 ? 478 HOH   A O   1 
HETATM 3789 O  O   . HOH   F 4 .   ? 17.349  -20.487 -32.278 1.00 14.21 ? 479 HOH   A O   1 
HETATM 3790 O  O   . HOH   F 4 .   ? -19.637 -20.539 -53.888 1.00 43.88 ? 480 HOH   A O   1 
HETATM 3791 O  O   A HOH   F 4 .   ? -1.749  -20.233 -30.938 0.50 14.06 ? 481 HOH   A O   1 
HETATM 3792 O  O   B HOH   F 4 .   ? -2.863  -20.760 -32.681 0.50 21.92 ? 481 HOH   A O   1 
HETATM 3793 O  O   . HOH   F 4 .   ? 6.674   -16.930 -25.265 1.00 15.59 ? 482 HOH   A O   1 
HETATM 3794 O  O   . HOH   F 4 .   ? 14.384  -33.093 -24.736 1.00 33.82 ? 483 HOH   A O   1 
HETATM 3795 O  O   . HOH   F 4 .   ? -7.250  -14.630 -17.926 1.00 16.43 ? 484 HOH   A O   1 
HETATM 3796 O  O   . HOH   F 4 .   ? -17.320 -25.667 -31.474 1.00 29.07 ? 485 HOH   A O   1 
HETATM 3797 O  O   . HOH   F 4 .   ? 18.207  -24.654 -21.246 1.00 34.84 ? 486 HOH   A O   1 
HETATM 3798 O  O   . HOH   F 4 .   ? -13.894 -27.445 -41.985 1.00 25.81 ? 487 HOH   A O   1 
HETATM 3799 O  O   . HOH   F 4 .   ? -15.190 -12.624 -15.230 1.00 45.62 ? 488 HOH   A O   1 
HETATM 3800 O  O   . HOH   F 4 .   ? -21.353 -14.668 -27.963 1.00 39.36 ? 489 HOH   A O   1 
HETATM 3801 O  O   . HOH   F 4 .   ? 14.875  -22.875 -51.844 1.00 32.13 ? 490 HOH   A O   1 
HETATM 3802 O  O   . HOH   F 4 .   ? 19.023  -24.983 -23.822 1.00 28.40 ? 491 HOH   A O   1 
HETATM 3803 O  O   . HOH   F 4 .   ? 0.378   -36.703 -53.080 1.00 32.78 ? 492 HOH   A O   1 
HETATM 3804 O  O   . HOH   F 4 .   ? -11.625 -20.053 -16.153 1.00 26.32 ? 493 HOH   A O   1 
HETATM 3805 O  O   . HOH   F 4 .   ? -10.157 -36.343 -52.766 1.00 33.59 ? 494 HOH   A O   1 
HETATM 3806 O  O   . HOH   F 4 .   ? 11.192  -22.040 -50.303 1.00 43.02 ? 495 HOH   A O   1 
HETATM 3807 O  O   . HOH   F 4 .   ? 15.001  -12.880 -26.426 1.00 37.24 ? 496 HOH   A O   1 
HETATM 3808 O  O   . HOH   F 4 .   ? -8.160  -30.871 -32.803 1.00 48.90 ? 497 HOH   A O   1 
HETATM 3809 O  O   . HOH   F 4 .   ? 9.494   -18.437 -47.096 1.00 37.05 ? 498 HOH   A O   1 
HETATM 3810 O  O   . HOH   F 4 .   ? 23.098  -30.873 -34.365 1.00 29.99 ? 499 HOH   A O   1 
HETATM 3811 O  O   . HOH   F 4 .   ? -7.541  -5.933  -19.117 1.00 42.64 ? 500 HOH   A O   1 
HETATM 3812 O  O   . HOH   F 4 .   ? 18.601  -17.892 -28.574 1.00 40.65 ? 501 HOH   A O   1 
HETATM 3813 O  O   . HOH   F 4 .   ? -10.849 -10.857 -39.815 1.00 33.52 ? 502 HOH   A O   1 
HETATM 3814 O  O   . HOH   F 4 .   ? 1.752   -12.409 -44.087 1.00 45.11 ? 503 HOH   A O   1 
HETATM 3815 O  O   . HOH   F 4 .   ? 15.256  -13.858 -36.563 1.00 42.32 ? 504 HOH   A O   1 
HETATM 3816 O  O   . HOH   F 4 .   ? -7.815  -12.359 -16.944 1.00 31.78 ? 505 HOH   A O   1 
HETATM 3817 O  O   . HOH   F 4 .   ? 20.383  -20.996 -24.927 1.00 46.93 ? 506 HOH   A O   1 
HETATM 3818 O  O   . HOH   F 4 .   ? 14.658  -17.731 -24.311 1.00 21.72 ? 507 HOH   A O   1 
HETATM 3819 O  O   . HOH   F 4 .   ? -6.510  -15.501 -37.013 1.00 30.29 ? 508 HOH   A O   1 
HETATM 3820 O  O   . HOH   F 4 .   ? 19.856  -19.468 -31.481 1.00 31.28 ? 509 HOH   A O   1 
HETATM 3821 O  O   . HOH   F 4 .   ? -21.342 -24.385 -29.645 1.00 34.33 ? 510 HOH   A O   1 
HETATM 3822 O  O   . HOH   F 4 .   ? -1.232  -16.401 -52.407 1.00 42.50 ? 511 HOH   A O   1 
HETATM 3823 O  O   . HOH   F 4 .   ? -13.690 -12.893 -13.015 1.00 36.84 ? 512 HOH   A O   1 
HETATM 3824 O  O   . HOH   F 4 .   ? 9.361   -10.528 -34.153 1.00 46.18 ? 513 HOH   A O   1 
HETATM 3825 O  O   . HOH   F 4 .   ? -19.421 -23.005 -53.268 1.00 38.91 ? 514 HOH   A O   1 
HETATM 3826 O  O   . HOH   F 4 .   ? -1.964  -38.526 -19.885 1.00 50.75 ? 515 HOH   A O   1 
HETATM 3827 O  O   . HOH   F 4 .   ? 3.343   -37.334 -32.872 1.00 46.68 ? 516 HOH   A O   1 
HETATM 3828 O  O   . HOH   F 4 .   ? -18.035 -8.231  -28.372 1.00 42.22 ? 517 HOH   A O   1 
HETATM 3829 O  O   . HOH   F 4 .   ? 22.512  -28.710 -28.586 1.00 40.50 ? 518 HOH   A O   1 
HETATM 3830 O  O   . HOH   F 4 .   ? 7.578   -32.940 -19.016 1.00 42.52 ? 519 HOH   A O   1 
HETATM 3831 O  O   . HOH   F 4 .   ? -19.977 -10.239 -22.687 1.00 47.86 ? 520 HOH   A O   1 
HETATM 3832 O  O   . HOH   F 4 .   ? 13.451  -21.666 -16.802 1.00 32.80 ? 521 HOH   A O   1 
HETATM 3833 O  O   . HOH   F 4 .   ? 3.442   -14.377 -22.653 1.00 32.92 ? 522 HOH   A O   1 
HETATM 3834 O  O   . HOH   F 4 .   ? 10.789  -12.523 -34.431 1.00 36.05 ? 523 HOH   A O   1 
HETATM 3835 O  O   . HOH   F 4 .   ? -16.919 -12.615 -17.561 1.00 53.71 ? 524 HOH   A O   1 
HETATM 3836 O  O   . HOH   F 4 .   ? 15.320  -12.393 -31.411 1.00 42.62 ? 525 HOH   A O   1 
HETATM 3837 O  O   . HOH   F 4 .   ? 13.850  -11.847 -37.237 1.00 57.55 ? 526 HOH   A O   1 
HETATM 3838 O  O   . HOH   F 4 .   ? -1.067  -35.969 -27.287 1.00 43.53 ? 527 HOH   A O   1 
HETATM 3839 O  O   . HOH   G 4 .   ? 16.289  8.021   4.701   1.00 38.66 ? 401 HOH   B O   1 
HETATM 3840 O  O   . HOH   G 4 .   ? 3.266   -23.242 0.650   1.00 22.05 ? 402 HOH   B O   1 
HETATM 3841 O  O   . HOH   G 4 .   ? 14.457  6.663   -2.340  1.00 32.48 ? 403 HOH   B O   1 
HETATM 3842 O  O   . HOH   G 4 .   ? -6.028  -11.672 -13.597 1.00 27.23 ? 404 HOH   B O   1 
HETATM 3843 O  O   . HOH   G 4 .   ? 12.621  -18.913 10.155  1.00 31.59 ? 405 HOH   B O   1 
HETATM 3844 O  O   . HOH   G 4 .   ? -16.975 -23.886 0.204   1.00 37.86 ? 406 HOH   B O   1 
HETATM 3845 O  O   . HOH   G 4 .   ? -6.722  -4.065  -5.518  1.00 14.16 ? 407 HOH   B O   1 
HETATM 3846 O  O   . HOH   G 4 .   ? 10.885  -18.822 -0.385  1.00 35.16 ? 408 HOH   B O   1 
HETATM 3847 O  O   . HOH   G 4 .   ? 23.099  -10.441 -16.418 1.00 37.62 ? 409 HOH   B O   1 
HETATM 3848 O  O   . HOH   G 4 .   ? 30.355  -5.135  -1.915  1.00 14.81 ? 410 HOH   B O   1 
HETATM 3849 O  O   . HOH   G 4 .   ? 4.969   -16.994 -21.322 1.00 23.60 ? 411 HOH   B O   1 
HETATM 3850 O  O   . HOH   G 4 .   ? -12.722 1.079   0.539   1.00 35.97 ? 412 HOH   B O   1 
HETATM 3851 O  O   . HOH   G 4 .   ? -12.560 -1.518  -3.204  1.00 31.45 ? 413 HOH   B O   1 
HETATM 3852 O  O   . HOH   G 4 .   ? 25.194  -8.623  -3.053  1.00 15.35 ? 414 HOH   B O   1 
HETATM 3853 O  O   . HOH   G 4 .   ? -12.716 -6.452  -10.847 1.00 42.29 ? 415 HOH   B O   1 
HETATM 3854 O  O   . HOH   G 4 .   ? 1.292   -27.609 -7.577  1.00 25.03 ? 416 HOH   B O   1 
HETATM 3855 O  O   . HOH   G 4 .   ? -3.528  -13.995 -16.088 1.00 19.21 ? 417 HOH   B O   1 
HETATM 3856 O  O   . HOH   G 4 .   ? 7.850   -23.258 -8.909  1.00 12.14 ? 418 HOH   B O   1 
HETATM 3857 O  O   . HOH   G 4 .   ? 24.421  -19.320 -9.855  1.00 30.35 ? 419 HOH   B O   1 
HETATM 3858 O  O   . HOH   G 4 .   ? 21.608  -2.247  -6.015  1.00 35.18 ? 420 HOH   B O   1 
HETATM 3859 O  O   . HOH   G 4 .   ? -1.107  -5.751  -13.675 1.00 42.34 ? 421 HOH   B O   1 
HETATM 3860 O  O   . HOH   G 4 .   ? 12.505  5.197   12.542  1.00 29.13 ? 422 HOH   B O   1 
HETATM 3861 O  O   . HOH   G 4 .   ? 16.094  1.150   8.506   1.00 22.06 ? 423 HOH   B O   1 
HETATM 3862 O  O   . HOH   G 4 .   ? -7.097  2.683   -1.335  1.00 21.60 ? 424 HOH   B O   1 
HETATM 3863 O  O   . HOH   G 4 .   ? 12.051  -20.740 -14.457 1.00 26.05 ? 425 HOH   B O   1 
HETATM 3864 O  O   . HOH   G 4 .   ? -16.620 -14.438 -9.784  1.00 47.63 ? 426 HOH   B O   1 
HETATM 3865 O  O   A HOH   G 4 .   ? 8.937   -6.157  -11.269 1.00 28.14 ? 427 HOH   B O   1 
HETATM 3866 O  O   . HOH   G 4 .   ? 11.274  -9.277  14.859  1.00 16.87 ? 428 HOH   B O   1 
HETATM 3867 O  O   . HOH   G 4 .   ? -5.661  -15.190 21.337  1.00 17.09 ? 429 HOH   B O   1 
HETATM 3868 O  O   . HOH   G 4 .   ? -3.371  0.279   5.119   1.00 14.94 ? 430 HOH   B O   1 
HETATM 3869 O  O   . HOH   G 4 .   ? -3.763  -1.520  0.471   1.00 12.08 ? 431 HOH   B O   1 
HETATM 3870 O  O   . HOH   G 4 .   ? -10.475 -14.314 -9.758  1.00 13.77 ? 432 HOH   B O   1 
HETATM 3871 O  O   . HOH   G 4 .   ? 15.648  8.470   1.572   1.00 36.19 ? 433 HOH   B O   1 
HETATM 3872 O  O   . HOH   G 4 .   ? 2.164   -21.946 13.569  1.00 25.11 ? 434 HOH   B O   1 
HETATM 3873 O  O   . HOH   G 4 .   ? -1.511  -20.245 7.784   1.00 14.57 ? 435 HOH   B O   1 
HETATM 3874 O  O   . HOH   G 4 .   ? 27.305  -9.396  -10.838 1.00 37.48 ? 436 HOH   B O   1 
HETATM 3875 O  O   . HOH   G 4 .   ? 21.105  5.160   -2.755  1.00 32.80 ? 437 HOH   B O   1 
HETATM 3876 O  O   . HOH   G 4 .   ? 17.220  -17.772 -7.956  1.00 23.05 ? 438 HOH   B O   1 
HETATM 3877 O  O   . HOH   G 4 .   ? -13.715 -13.216 1.019   1.00 13.70 ? 439 HOH   B O   1 
HETATM 3878 O  O   . HOH   G 4 .   ? -11.505 -7.597  -4.260  1.00 12.43 ? 440 HOH   B O   1 
HETATM 3879 O  O   . HOH   G 4 .   ? -12.319 -25.079 -0.106  1.00 41.30 ? 441 HOH   B O   1 
HETATM 3880 O  O   . HOH   G 4 .   ? -16.627 -20.277 -2.251  1.00 32.84 ? 442 HOH   B O   1 
HETATM 3881 O  O   . HOH   G 4 .   ? -4.393  2.353   8.505   1.00 40.82 ? 443 HOH   B O   1 
HETATM 3882 O  O   . HOH   G 4 .   ? 1.888   -15.279 -18.387 1.00 15.12 ? 444 HOH   B O   1 
HETATM 3883 O  O   . HOH   G 4 .   ? 16.731  -18.482 -0.577  1.00 45.40 ? 445 HOH   B O   1 
HETATM 3884 O  O   . HOH   G 4 .   ? -2.911  -11.920 -12.055 1.00 15.69 ? 446 HOH   B O   1 
HETATM 3885 O  O   . HOH   G 4 .   ? 14.561  -2.779  -13.512 1.00 36.50 ? 447 HOH   B O   1 
HETATM 3886 O  O   . HOH   G 4 .   ? 18.724  -13.506 -0.925  1.00 21.03 ? 448 HOH   B O   1 
HETATM 3887 O  O   . HOH   G 4 .   ? 1.576   -25.903 -11.789 1.00 21.37 ? 449 HOH   B O   1 
HETATM 3888 O  O   . HOH   G 4 .   ? 8.104   8.738   5.012   1.00 44.69 ? 450 HOH   B O   1 
HETATM 3889 O  O   . HOH   G 4 .   ? -7.255  3.686   -5.105  1.00 36.15 ? 451 HOH   B O   1 
HETATM 3890 O  O   . HOH   G 4 .   ? 1.811   4.773   5.386   1.00 33.41 ? 452 HOH   B O   1 
HETATM 3891 O  O   . HOH   G 4 .   ? -13.919 -19.247 -14.272 1.00 31.80 ? 453 HOH   B O   1 
HETATM 3892 O  O   . HOH   G 4 .   ? 3.349   -20.428 15.867  1.00 20.21 ? 454 HOH   B O   1 
HETATM 3893 O  O   . HOH   G 4 .   ? 12.892  -0.201  -3.658  1.00 19.64 ? 455 HOH   B O   1 
HETATM 3894 O  O   . HOH   G 4 .   ? -8.939  -26.437 -2.398  1.00 27.69 ? 456 HOH   B O   1 
HETATM 3895 O  O   . HOH   G 4 .   ? -6.783  1.243   8.067   1.00 45.73 ? 457 HOH   B O   1 
HETATM 3896 O  O   . HOH   G 4 .   ? 9.922   -21.094 -1.682  1.00 38.70 ? 458 HOH   B O   1 
HETATM 3897 O  O   . HOH   G 4 .   ? 8.768   7.073   9.955   1.00 35.18 ? 459 HOH   B O   1 
HETATM 3898 O  O   . HOH   G 4 .   ? -5.700  -26.532 -5.383  1.00 28.76 ? 460 HOH   B O   1 
HETATM 3899 O  O   . HOH   G 4 .   ? 11.532  -16.331 13.113  1.00 26.63 ? 461 HOH   B O   1 
HETATM 3900 O  O   . HOH   G 4 .   ? -10.844 -24.362 -2.179  1.00 24.66 ? 462 HOH   B O   1 
HETATM 3901 O  O   . HOH   G 4 .   ? 24.805  -6.240  -9.493  1.00 30.40 ? 463 HOH   B O   1 
HETATM 3902 O  O   . HOH   G 4 .   ? 7.249   1.044   17.890  1.00 50.62 ? 464 HOH   B O   1 
HETATM 3903 O  O   . HOH   G 4 .   ? 1.370   -16.034 19.990  1.00 20.71 ? 465 HOH   B O   1 
HETATM 3904 O  O   . HOH   G 4 .   ? -8.837  4.756   -0.659  1.00 35.73 ? 466 HOH   B O   1 
HETATM 3905 O  O   . HOH   G 4 .   ? 11.036  -14.904 -18.929 1.00 15.99 ? 467 HOH   B O   1 
HETATM 3906 O  O   . HOH   G 4 .   ? -11.324 -7.930  -13.584 1.00 34.17 ? 468 HOH   B O   1 
HETATM 3907 O  O   . HOH   G 4 .   ? -0.640  -13.200 -12.747 1.00 25.56 ? 469 HOH   B O   1 
HETATM 3908 O  O   . HOH   G 4 .   ? 10.590  9.173   6.828   1.00 34.90 ? 470 HOH   B O   1 
HETATM 3909 O  O   A HOH   G 4 .   ? 5.529   -10.750 -5.449  0.50 11.58 ? 471 HOH   B O   1 
HETATM 3910 O  O   B HOH   G 4 .   ? 6.432   -9.968  -3.887  0.50 28.54 ? 471 HOH   B O   1 
HETATM 3911 O  O   . HOH   G 4 .   ? 17.480  -9.138  7.722   1.00 26.24 ? 472 HOH   B O   1 
HETATM 3912 O  O   . HOH   G 4 .   ? 12.909  -21.789 -12.049 1.00 25.69 ? 473 HOH   B O   1 
HETATM 3913 O  O   . HOH   G 4 .   ? 18.567  7.400   3.703   1.00 34.31 ? 474 HOH   B O   1 
HETATM 3914 O  O   . HOH   G 4 .   ? -13.672 -10.035 -4.389  1.00 13.74 ? 475 HOH   B O   1 
HETATM 3915 O  O   . HOH   G 4 .   ? 15.254  -20.261 -16.815 1.00 27.06 ? 476 HOH   B O   1 
HETATM 3916 O  O   . HOH   G 4 .   ? 6.854   -7.152  -4.100  1.00 23.38 ? 477 HOH   B O   1 
HETATM 3917 O  O   . HOH   G 4 .   ? -11.090 0.933   11.929  1.00 27.47 ? 478 HOH   B O   1 
HETATM 3918 O  O   . HOH   G 4 .   ? 21.981  -3.413  -14.980 1.00 42.62 ? 479 HOH   B O   1 
HETATM 3919 O  O   . HOH   G 4 .   ? -15.207 -18.974 -7.811  1.00 26.65 ? 480 HOH   B O   1 
HETATM 3920 O  O   . HOH   G 4 .   ? 28.465  -15.878 -6.058  1.00 53.40 ? 481 HOH   B O   1 
HETATM 3921 O  O   . HOH   G 4 .   ? 20.190  -13.389 -18.677 1.00 43.79 ? 482 HOH   B O   1 
HETATM 3922 O  O   . HOH   G 4 .   ? 2.587   -12.941 -16.854 1.00 18.13 ? 483 HOH   B O   1 
HETATM 3923 O  O   . HOH   G 4 .   ? 25.141  -8.331  -11.416 1.00 32.59 ? 484 HOH   B O   1 
HETATM 3924 O  O   . HOH   G 4 .   ? -14.359 -20.424 -10.001 1.00 35.33 ? 485 HOH   B O   1 
HETATM 3925 O  O   . HOH   G 4 .   ? -10.945 -12.917 -12.288 1.00 18.90 ? 486 HOH   B O   1 
HETATM 3926 O  O   . HOH   G 4 .   ? -14.840 -9.052  -7.298  1.00 37.57 ? 487 HOH   B O   1 
HETATM 3927 O  O   . HOH   G 4 .   ? 8.140   -25.891 -7.863  1.00 37.89 ? 488 HOH   B O   1 
HETATM 3928 O  O   . HOH   G 4 .   ? 25.022  -14.531 -3.708  1.00 32.54 ? 489 HOH   B O   1 
HETATM 3929 O  O   . HOH   G 4 .   ? -16.268 -9.680  -5.427  1.00 31.61 ? 490 HOH   B O   1 
HETATM 3930 O  O   . HOH   G 4 .   ? -11.645 -2.320  -5.483  1.00 34.90 ? 491 HOH   B O   1 
HETATM 3931 O  O   . HOH   G 4 .   ? 20.733  6.067   13.935  1.00 41.65 ? 492 HOH   B O   1 
HETATM 3932 O  O   . HOH   G 4 .   ? 17.335  -17.051 -23.681 1.00 39.31 ? 493 HOH   B O   1 
HETATM 3933 O  O   . HOH   G 4 .   ? -4.031  -27.350 -7.131  1.00 40.05 ? 494 HOH   B O   1 
HETATM 3934 O  O   . HOH   G 4 .   ? 14.836  2.135   -4.883  1.00 26.96 ? 495 HOH   B O   1 
HETATM 3935 O  O   . HOH   G 4 .   ? 10.485  -3.053  -3.559  1.00 28.24 ? 496 HOH   B O   1 
HETATM 3936 O  O   . HOH   G 4 .   ? 14.553  -17.118 6.922   1.00 30.08 ? 497 HOH   B O   1 
HETATM 3937 O  O   . HOH   G 4 .   ? 9.925   -9.835  -19.700 1.00 48.44 ? 498 HOH   B O   1 
HETATM 3938 O  O   . HOH   G 4 .   ? 6.325   3.860   -0.271  1.00 35.88 ? 499 HOH   B O   1 
HETATM 3939 O  O   . HOH   G 4 .   ? -18.914 -18.475 -1.935  1.00 40.34 ? 500 HOH   B O   1 
HETATM 3940 O  O   . HOH   G 4 .   ? 3.881   -2.213  18.211  1.00 43.50 ? 501 HOH   B O   1 
HETATM 3941 O  O   . HOH   G 4 .   ? -5.811  1.370   5.650   1.00 23.82 ? 502 HOH   B O   1 
HETATM 3942 O  O   . HOH   G 4 .   ? -9.559  -21.216 -15.441 1.00 36.15 ? 503 HOH   B O   1 
HETATM 3943 O  O   . HOH   G 4 .   ? 17.675  -20.738 -15.925 1.00 51.82 ? 504 HOH   B O   1 
HETATM 3944 O  O   . HOH   G 4 .   ? -18.227 -8.489  -4.471  1.00 32.97 ? 505 HOH   B O   1 
HETATM 3945 O  O   . HOH   G 4 .   ? -7.387  -2.629  -7.904  1.00 37.58 ? 506 HOH   B O   1 
HETATM 3946 O  O   . HOH   G 4 .   ? 0.183   -11.762 -15.578 1.00 45.16 ? 507 HOH   B O   1 
HETATM 3947 O  O   . HOH   G 4 .   ? -8.035  -3.742  -10.302 1.00 38.15 ? 508 HOH   B O   1 
HETATM 3948 O  O   . HOH   G 4 .   ? 3.723   -27.107 -11.990 1.00 38.45 ? 509 HOH   B O   1 
HETATM 3949 O  O   . HOH   G 4 .   ? -10.102 0.401   -6.762  1.00 53.71 ? 510 HOH   B O   1 
HETATM 3950 O  O   . HOH   G 4 .   ? 23.585  -21.572 -10.195 1.00 44.87 ? 511 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N  N   . LEU   A 4   ? 0.3976 0.5643 0.3800 0.0223  0.0041  0.0046  4   LEU   A N   
2    C  CA  . LEU   A 4   ? 0.3978 0.5512 0.3808 0.0253  0.0047  0.0091  4   LEU   A CA  
3    C  C   . LEU   A 4   ? 0.4000 0.5506 0.3833 0.0238  0.0045  0.0071  4   LEU   A C   
4    O  O   . LEU   A 4   ? 0.3384 0.4759 0.3222 0.0222  0.0046  0.0076  4   LEU   A O   
5    C  CB  . LEU   A 4   ? 0.4094 0.5648 0.3923 0.0326  0.0053  0.0153  4   LEU   A CB  
6    C  CG  . LEU   A 4   ? 0.4376 0.5776 0.4211 0.0348  0.0060  0.0197  4   LEU   A CG  
7    C  CD1 . LEU   A 4   ? 0.4793 0.6077 0.4631 0.0309  0.0061  0.0197  4   LEU   A CD1 
8    C  CD2 . LEU   A 4   ? 0.4687 0.6093 0.4517 0.0421  0.0068  0.0260  4   LEU   A CD2 
9    N  N   . LYS   A 5   ? 0.3521 0.5162 0.3353 0.0244  0.0042  0.0048  5   LYS   A N   
10   C  CA  . LYS   A 5   ? 0.3799 0.5436 0.3634 0.0225  0.0041  0.0024  5   LYS   A CA  
11   C  C   . LYS   A 5   ? 0.3545 0.5106 0.3377 0.0143  0.0038  -0.0019 5   LYS   A C   
12   O  O   . LYS   A 5   ? 0.3053 0.4517 0.2888 0.0124  0.0038  -0.0021 5   LYS   A O   
13   C  CB  . LYS   A 5   ? 0.4119 0.5934 0.3953 0.0248  0.0039  0.0007  5   LYS   A CB  
14   C  CG  . LYS   A 5   ? 0.4927 0.6789 0.4760 0.0339  0.0042  0.0055  5   LYS   A CG  
15   C  CD  . LYS   A 5   ? 0.5996 0.8019 0.5828 0.0374  0.0039  0.0041  5   LYS   A CD  
16   C  CE  . LYS   A 5   ? 0.6361 0.8393 0.6187 0.0471  0.0042  0.0093  5   LYS   A CE  
17   N  NZ  . LYS   A 5   ? 0.6772 0.8986 0.6595 0.0511  0.0038  0.0076  5   LYS   A NZ  
18   N  N   . ALA   A 6   ? 0.3212 0.4816 0.3036 0.0098  0.0035  -0.0053 6   ALA   A N   
19   C  CA  . ALA   A 6   ? 0.3292 0.4818 0.3107 0.0023  0.0032  -0.0093 6   ALA   A CA  
20   C  C   . ALA   A 6   ? 0.3200 0.4551 0.3015 0.0018  0.0033  -0.0072 6   ALA   A C   
21   O  O   . ALA   A 6   ? 0.2844 0.4102 0.2653 -0.0023 0.0032  -0.0086 6   ALA   A O   
22   C  CB  . ALA   A 6   ? 0.3448 0.5046 0.3253 -0.0018 0.0029  -0.0134 6   ALA   A CB  
23   N  N   . SER   A 7   ? 0.2823 0.4137 0.2642 0.0058  0.0034  -0.0038 7   SER   A N   
24   C  CA  . SER   A 7   ? 0.2824 0.3990 0.2644 0.0054  0.0035  -0.0020 7   SER   A CA  
25   C  C   . SER   A 7   ? 0.2738 0.3826 0.2568 0.0074  0.0039  0.0006  7   SER   A C   
26   O  O   . SER   A 7   ? 0.2768 0.3742 0.2596 0.0050  0.0038  0.0003  7   SER   A O   
27   C  CB  . SER   A 7   ? 0.3266 0.4421 0.3088 0.0084  0.0037  0.0008  7   SER   A CB  
28   O  OG  . SER   A 7   ? 0.3745 0.4952 0.3575 0.0143  0.0043  0.0053  7   SER   A OG  
29   N  N   . SER   A 8   ? 0.2427 0.3576 0.2266 0.0123  0.0042  0.0031  8   SER   A N   
30   C  CA  . SER   A 8   ? 0.2444 0.3521 0.2292 0.0148  0.0045  0.0052  8   SER   A CA  
31   C  C   . SER   A 8   ? 0.2472 0.3533 0.2319 0.0107  0.0042  0.0019  8   SER   A C   
32   O  O   . SER   A 8   ? 0.2391 0.3352 0.2243 0.0101  0.0042  0.0024  8   SER   A O   
33   C  CB  . SER   A 8   ? 0.2555 0.3697 0.2409 0.0214  0.0048  0.0084  8   SER   A CB  
34   O  OG  . SER   A 8   ? 0.2725 0.3864 0.2578 0.0250  0.0053  0.0123  8   SER   A OG  
35   N  N   . LEU   A 9   ? 0.2526 0.3694 0.2366 0.0078  0.0039  -0.0014 9   LEU   A N   
36   C  CA  . LEU   A 9   ? 0.2536 0.3701 0.2371 0.0032  0.0037  -0.0044 9   LEU   A CA  
37   C  C   . LEU   A 9   ? 0.2488 0.3530 0.2312 -0.0021 0.0036  -0.0057 9   LEU   A C   
38   O  O   . LEU   A 9   ? 0.2196 0.3168 0.2019 -0.0041 0.0036  -0.0060 9   LEU   A O   
39   C  CB  . LEU   A 9   ? 0.2836 0.4145 0.2664 0.0003  0.0036  -0.0078 9   LEU   A CB  
40   C  CG  . LEU   A 9   ? 0.3353 0.4685 0.3176 -0.0048 0.0035  -0.0107 9   LEU   A CG  
41   C  CD1 . LEU   A 9   ? 0.3562 0.4899 0.3397 -0.0006 0.0036  -0.0092 9   LEU   A CD1 
42   C  CD2 . LEU   A 9   ? 0.3471 0.4958 0.3288 -0.0081 0.0035  -0.0141 9   LEU   A CD2 
43   N  N   . ARG   A 10  ? 0.2277 0.3299 0.2092 -0.0041 0.0034  -0.0065 10  ARG   A N   
44   C  CA  . ARG   A 10  ? 0.2476 0.3385 0.2276 -0.0083 0.0032  -0.0077 10  ARG   A CA  
45   C  C   . ARG   A 10  ? 0.2123 0.2913 0.1931 -0.0059 0.0033  -0.0049 10  ARG   A C   
46   O  O   . ARG   A 10  ? 0.2147 0.2855 0.1949 -0.0085 0.0032  -0.0055 10  ARG   A O   
47   C  CB  . ARG   A 10  ? 0.2812 0.3741 0.2602 -0.0093 0.0029  -0.0091 10  ARG   A CB  
48   C  CG  . ARG   A 10  ? 0.3243 0.4079 0.3009 -0.0143 0.0026  -0.0117 10  ARG   A CG  
49   C  CD  . ARG   A 10  ? 0.3671 0.4549 0.3430 -0.0142 0.0022  -0.0134 10  ARG   A CD  
50   N  NE  . ARG   A 10  ? 0.3854 0.4616 0.3594 -0.0164 0.0018  -0.0147 10  ARG   A NE  
51   C  CZ  . ARG   A 10  ? 0.3581 0.4336 0.3314 -0.0155 0.0015  -0.0158 10  ARG   A CZ  
52   N  NH1 . ARG   A 10  ? 0.4130 0.4977 0.3878 -0.0118 0.0015  -0.0146 10  ARG   A NH1 
53   N  NH2 . ARG   A 10  ? 0.3817 0.4471 0.3525 -0.0179 0.0010  -0.0178 10  ARG   A NH2 
54   N  N   . ALA   A 11  ? 0.1939 0.2725 0.1763 -0.0009 0.0036  -0.0017 11  ALA   A N   
55   C  CA  . ALA   A 11  ? 0.2001 0.2684 0.1836 0.0012  0.0038  0.0008  11  ALA   A CA  
56   C  C   . ALA   A 11  ? 0.1866 0.2520 0.1710 0.0016  0.0040  0.0009  11  ALA   A C   
57   O  O   . ALA   A 11  ? 0.1838 0.2403 0.1683 0.0006  0.0039  0.0010  11  ALA   A O   
58   C  CB  . ALA   A 11  ? 0.2085 0.2780 0.1933 0.0060  0.0043  0.0044  11  ALA   A CB  
59   N  N   . LEU   A 12  ? 0.1818 0.2557 0.1669 0.0037  0.0041  0.0007  12  LEU   A N   
60   C  CA  . LEU   A 12  ? 0.1792 0.2515 0.1651 0.0048  0.0041  0.0006  12  LEU   A CA  
61   C  C   . LEU   A 12  ? 0.1866 0.2549 0.1714 -0.0004 0.0039  -0.0019 12  LEU   A C   
62   O  O   . LEU   A 12  ? 0.1828 0.2445 0.1682 -0.0004 0.0039  -0.0018 12  LEU   A O   
63   C  CB  . LEU   A 12  ? 0.1956 0.2795 0.1820 0.0079  0.0041  0.0003  12  LEU   A CB  
64   C  CG  . LEU   A 12  ? 0.2046 0.2888 0.1919 0.0099  0.0041  -0.0003 12  LEU   A CG  
65   C  CD1 . LEU   A 12  ? 0.2271 0.3196 0.2151 0.0162  0.0042  0.0010  12  LEU   A CD1 
66   C  CD2 . LEU   A 12  ? 0.2128 0.3012 0.1992 0.0049  0.0039  -0.0034 12  LEU   A CD2 
67   N  N   . LYS   A 13  ? 0.1914 0.2636 0.1743 -0.0050 0.0036  -0.0041 13  LYS   A N   
68   C  CA  . LYS   A 13  ? 0.1870 0.2556 0.1682 -0.0102 0.0035  -0.0061 13  LYS   A CA  
69   C  C   . LYS   A 13  ? 0.1903 0.2468 0.1704 -0.0119 0.0033  -0.0056 13  LYS   A C   
70   O  O   . LYS   A 13  ? 0.1840 0.2358 0.1623 -0.0156 0.0032  -0.0066 13  LYS   A O   
71   C  CB  . LYS   A 13  ? 0.2160 0.2921 0.1953 -0.0151 0.0034  -0.0086 13  LYS   A CB  
72   C  CG  . LYS   A 13  ? 0.2528 0.3426 0.2331 -0.0140 0.0036  -0.0096 13  LYS   A CG  
73   C  CD  . LYS   A 13  ? 0.3140 0.4126 0.2927 -0.0195 0.0036  -0.0125 13  LYS   A CD  
74   C  CE  . LYS   A 13  ? 0.3685 0.4822 0.3484 -0.0175 0.0037  -0.0134 13  LYS   A CE  
75   N  NZ  . LYS   A 13  ? 0.4187 0.5417 0.3971 -0.0235 0.0039  -0.0165 13  LYS   A NZ  
76   N  N   . LEU   A 14  ? 0.1715 0.2237 0.1524 -0.0090 0.0033  -0.0039 14  LEU   A N   
77   C  CA  . LEU   A 14  ? 0.1612 0.2034 0.1413 -0.0096 0.0031  -0.0034 14  LEU   A CA  
78   C  C   . LEU   A 14  ? 0.1690 0.2060 0.1513 -0.0063 0.0034  -0.0015 14  LEU   A C   
79   O  O   . LEU   A 14  ? 0.1572 0.1873 0.1394 -0.0062 0.0033  -0.0010 14  LEU   A O   
80   C  CB  . LEU   A 14  ? 0.1687 0.2106 0.1480 -0.0093 0.0029  -0.0035 14  LEU   A CB  
81   C  CG  . LEU   A 14  ? 0.1688 0.2146 0.1458 -0.0130 0.0027  -0.0060 14  LEU   A CG  
82   C  CD1 . LEU   A 14  ? 0.1764 0.2240 0.1531 -0.0117 0.0025  -0.0063 14  LEU   A CD1 
83   C  CD2 . LEU   A 14  ? 0.1765 0.2150 0.1506 -0.0173 0.0024  -0.0077 14  LEU   A CD2 
84   N  N   . MET   A 15  ? 0.1667 0.2072 0.1510 -0.0036 0.0037  -0.0008 15  MET   A N   
85   C  CA  . MET   A 15  ? 0.1680 0.2033 0.1545 -0.0007 0.0040  0.0008  15  MET   A CA  
86   C  C   . MET   A 15  ? 0.1637 0.1940 0.1502 -0.0023 0.0039  -0.0004 15  MET   A C   
87   O  O   . MET   A 15  ? 0.1532 0.1865 0.1387 -0.0043 0.0037  -0.0020 15  MET   A O   
88   C  CB  . MET   A 15  ? 0.1968 0.2362 0.1852 0.0035  0.0044  0.0020  15  MET   A CB  
89   C  CG  . MET   A 15  ? 0.2680 0.3102 0.2568 0.0065  0.0047  0.0043  15  MET   A CG  
90   S  SD  . MET   A 15  ? 0.3438 0.3865 0.3344 0.0122  0.0053  0.0065  15  MET   A SD  
91   C  CE  . MET   A 15  ? 0.3886 0.4194 0.3809 0.0120  0.0058  0.0075  15  MET   A CE  
92   N  N   . ASP   A 16  ? 0.1712 0.1948 0.1587 -0.0016 0.0040  0.0003  16  ASP   A N   
93   C  CA  . ASP   A 16  ? 0.1695 0.1893 0.1578 -0.0019 0.0040  -0.0007 16  ASP   A CA  
94   C  C   . ASP   A 16  ? 0.1824 0.2017 0.1735 0.0015  0.0045  0.0000  16  ASP   A C   
95   O  O   . ASP   A 16  ? 0.1903 0.2056 0.1827 0.0029  0.0049  0.0015  16  ASP   A O   
96   C  CB  . ASP   A 16  ? 0.1774 0.1912 0.1652 -0.0031 0.0038  -0.0007 16  ASP   A CB  
97   C  CG  . ASP   A 16  ? 0.2033 0.2155 0.1880 -0.0059 0.0033  -0.0015 16  ASP   A CG  
98   O  OD1 . ASP   A 16  ? 0.2112 0.2266 0.1940 -0.0077 0.0031  -0.0021 16  ASP   A OD1 
99   O  OD2 . ASP   A 16  ? 0.2347 0.2425 0.2187 -0.0062 0.0031  -0.0016 16  ASP   A OD2 
100  N  N   . LEU   A 17  ? 0.1742 0.1976 0.1660 0.0030  0.0044  -0.0011 17  LEU   A N   
101  C  CA  . LEU   A 17  ? 0.1943 0.2168 0.1881 0.0069  0.0049  -0.0004 17  LEU   A CA  
102  C  C   . LEU   A 17  ? 0.2297 0.2462 0.2253 0.0071  0.0050  -0.0017 17  LEU   A C   
103  O  O   . LEU   A 17  ? 0.2179 0.2356 0.2133 0.0056  0.0047  -0.0039 17  LEU   A O   
104  C  CB  . LEU   A 17  ? 0.2008 0.2311 0.1944 0.0089  0.0047  -0.0014 17  LEU   A CB  
105  C  CG  . LEU   A 17  ? 0.2197 0.2497 0.2148 0.0140  0.0050  -0.0006 17  LEU   A CG  
106  C  CD1 . LEU   A 17  ? 0.2404 0.2693 0.2353 0.0161  0.0054  0.0026  17  LEU   A CD1 
107  C  CD2 . LEU   A 17  ? 0.2439 0.2830 0.2387 0.0161  0.0046  -0.0024 17  LEU   A CD2 
108  N  N   . SER   A 18  ? 0.2780 0.2885 0.2752 0.0087  0.0056  -0.0004 18  SER   A N   
109  C  CA  A SER   A 18  ? 0.3252 0.3302 0.3244 0.0089  0.0059  -0.0021 18  SER   A CA  
110  C  CA  B SER   A 18  ? 0.3446 0.3496 0.3438 0.0089  0.0059  -0.0021 18  SER   A CA  
111  C  C   . SER   A 18  ? 0.3629 0.3650 0.3635 0.0129  0.0063  -0.0017 18  SER   A C   
112  O  O   . SER   A 18  ? 0.4341 0.4378 0.4341 0.0157  0.0066  0.0006  18  SER   A O   
113  C  CB  A SER   A 18  ? 0.3358 0.3356 0.3357 0.0065  0.0062  -0.0013 18  SER   A CB  
114  C  CB  B SER   A 18  ? 0.3815 0.3811 0.3814 0.0066  0.0063  -0.0012 18  SER   A CB  
115  O  OG  A SER   A 18  ? 0.3137 0.3117 0.3134 0.0072  0.0068  0.0019  18  SER   A OG  
116  O  OG  B SER   A 18  ? 0.4060 0.4077 0.4041 0.0039  0.0058  -0.0012 18  SER   A OG  
117  N  N   . THR   A 19  ? 0.4832 0.4814 0.4854 0.0135  0.0064  -0.0042 19  THR   A N   
118  C  CA  . THR   A 19  ? 0.5295 0.5231 0.5328 0.0175  0.0069  -0.0042 19  THR   A CA  
119  C  C   . THR   A 19  ? 0.5237 0.5098 0.5272 0.0177  0.0079  -0.0006 19  THR   A C   
120  O  O   . THR   A 19  ? 0.5457 0.5283 0.5502 0.0140  0.0083  -0.0006 19  THR   A O   
121  C  CB  . THR   A 19  ? 0.5684 0.5585 0.5735 0.0177  0.0068  -0.0082 19  THR   A CB  
122  O  OG1 . THR   A 19  ? 0.5589 0.5447 0.5651 0.0136  0.0072  -0.0087 19  THR   A OG1 
123  C  CG2 . THR   A 19  ? 0.5680 0.5662 0.5728 0.0178  0.0059  -0.0116 19  THR   A CG2 
124  N  N   . THR   A 25  ? 0.4582 0.4450 0.4730 0.0181  0.0054  -0.0353 25  THR   A N   
125  C  CA  . THR   A 25  ? 0.4226 0.4167 0.4377 0.0213  0.0045  -0.0397 25  THR   A CA  
126  C  C   . THR   A 25  ? 0.3766 0.3822 0.3896 0.0216  0.0039  -0.0376 25  THR   A C   
127  O  O   . THR   A 25  ? 0.3319 0.3380 0.3432 0.0212  0.0040  -0.0331 25  THR   A O   
128  C  CB  . THR   A 25  ? 0.4829 0.4705 0.4984 0.0267  0.0046  -0.0415 25  THR   A CB  
129  O  OG1 . THR   A 25  ? 0.4450 0.4322 0.4586 0.0296  0.0048  -0.0367 25  THR   A OG1 
130  C  CG2 . THR   A 25  ? 0.4963 0.4709 0.5136 0.0258  0.0055  -0.0433 25  THR   A CG2 
131  N  N   . ASP   A 26  ? 0.3558 0.3709 0.3689 0.0223  0.0031  -0.0412 26  ASP   A N   
132  C  CA  . ASP   A 26  ? 0.3414 0.3680 0.3526 0.0224  0.0025  -0.0399 26  ASP   A CA  
133  C  C   . ASP   A 26  ? 0.3226 0.3504 0.3326 0.0265  0.0025  -0.0377 26  ASP   A C   
134  O  O   . ASP   A 26  ? 0.2857 0.3192 0.2938 0.0254  0.0024  -0.0344 26  ASP   A O   
135  C  CB  . ASP   A 26  ? 0.3614 0.3978 0.3731 0.0231  0.0019  -0.0445 26  ASP   A CB  
136  C  CG  . ASP   A 26  ? 0.3839 0.4235 0.3960 0.0189  0.0018  -0.0459 26  ASP   A CG  
137  O  OD1 . ASP   A 26  ? 0.3575 0.3920 0.3691 0.0154  0.0022  -0.0432 26  ASP   A OD1 
138  O  OD2 . ASP   A 26  ? 0.4730 0.5208 0.4856 0.0196  0.0013  -0.0497 26  ASP   A OD2 
139  N  N   . GLU   A 27  ? 0.3269 0.3490 0.3379 0.0314  0.0025  -0.0397 27  GLU   A N   
140  C  CA  . GLU   A 27  ? 0.3454 0.3687 0.3551 0.0364  0.0024  -0.0378 27  GLU   A CA  
141  C  C   . GLU   A 27  ? 0.3265 0.3457 0.3348 0.0348  0.0031  -0.0320 27  GLU   A C   
142  O  O   . GLU   A 27  ? 0.3110 0.3371 0.3177 0.0362  0.0029  -0.0296 27  GLU   A O   
143  C  CB  . GLU   A 27  ? 0.4160 0.4311 0.4268 0.0420  0.0025  -0.0408 27  GLU   A CB  
144  C  CG  . GLU   A 27  ? 0.5114 0.5336 0.5232 0.0450  0.0016  -0.0469 27  GLU   A CG  
145  C  CD  . GLU   A 27  ? 0.5951 0.6169 0.6089 0.0413  0.0015  -0.0513 27  GLU   A CD  
146  O  OE1 . GLU   A 27  ? 0.5399 0.5537 0.5548 0.0369  0.0022  -0.0505 27  GLU   A OE1 
147  O  OE2 . GLU   A 27  ? 0.7373 0.7688 0.7517 0.0431  0.0008  -0.0558 27  GLU   A OE2 
148  N  N   . LYS   A 28  ? 0.3132 0.3219 0.3222 0.0320  0.0038  -0.0301 28  LYS   A N   
149  C  CA  . LYS   A 28  ? 0.3304 0.3355 0.3382 0.0305  0.0044  -0.0248 28  LYS   A CA  
150  C  C   . LYS   A 28  ? 0.3020 0.3154 0.3084 0.0260  0.0041  -0.0228 28  LYS   A C   
151  O  O   . LYS   A 28  ? 0.3020 0.3173 0.3068 0.0259  0.0043  -0.0193 28  LYS   A O   
152  C  CB  . LYS   A 28  ? 0.3573 0.3504 0.3661 0.0277  0.0053  -0.0233 28  LYS   A CB  
153  C  CG  . LYS   A 28  ? 0.4498 0.4319 0.4597 0.0311  0.0058  -0.0246 28  LYS   A CG  
154  C  CD  . LYS   A 28  ? 0.5392 0.5170 0.5476 0.0360  0.0062  -0.0206 28  LYS   A CD  
155  C  CE  . LYS   A 28  ? 0.5769 0.5435 0.5856 0.0402  0.0066  -0.0221 28  LYS   A CE  
156  N  NZ  . LYS   A 28  ? 0.5964 0.5647 0.6032 0.0470  0.0064  -0.0199 28  LYS   A NZ  
157  N  N   . VAL   A 29  ? 0.2652 0.2829 0.2718 0.0224  0.0038  -0.0251 29  VAL   A N   
158  C  CA  . VAL   A 29  ? 0.2670 0.2912 0.2718 0.0183  0.0035  -0.0232 29  VAL   A CA  
159  C  C   . VAL   A 29  ? 0.2544 0.2892 0.2576 0.0197  0.0031  -0.0231 29  VAL   A C   
160  O  O   . VAL   A 29  ? 0.2226 0.2610 0.2240 0.0176  0.0031  -0.0204 29  VAL   A O   
161  C  CB  . VAL   A 29  ? 0.2716 0.2976 0.2767 0.0146  0.0033  -0.0254 29  VAL   A CB  
162  C  CG1 . VAL   A 29  ? 0.2534 0.2866 0.2560 0.0110  0.0030  -0.0239 29  VAL   A CG1 
163  C  CG2 . VAL   A 29  ? 0.2912 0.3083 0.2976 0.0125  0.0038  -0.0250 29  VAL   A CG2 
164  N  N   . ILE   A 30  ? 0.2500 0.2906 0.2540 0.0229  0.0027  -0.0265 30  ILE   A N   
165  C  CA  . ILE   A 30  ? 0.2462 0.2985 0.2490 0.0244  0.0023  -0.0269 30  ILE   A CA  
166  C  C   . ILE   A 30  ? 0.2418 0.2940 0.2438 0.0273  0.0025  -0.0240 30  ILE   A C   
167  O  O   . ILE   A 30  ? 0.2536 0.3138 0.2540 0.0257  0.0024  -0.0224 30  ILE   A O   
168  C  CB  . ILE   A 30  ? 0.2594 0.3177 0.2634 0.0283  0.0017  -0.0314 30  ILE   A CB  
169  C  CG1 . ILE   A 30  ? 0.2718 0.3334 0.2763 0.0250  0.0015  -0.0341 30  ILE   A CG1 
170  C  CG2 . ILE   A 30  ? 0.2667 0.3375 0.2697 0.0312  0.0013  -0.0320 30  ILE   A CG2 
171  C  CD1 . ILE   A 30  ? 0.2939 0.3593 0.3001 0.0290  0.0010  -0.0392 30  ILE   A CD1 
172  N  N   . ALA   A 31  ? 0.2539 0.2970 0.2568 0.0315  0.0028  -0.0233 31  ALA   A N   
173  C  CA  . ALA   A 31  ? 0.2556 0.2981 0.2575 0.0349  0.0030  -0.0201 31  ALA   A CA  
174  C  C   . ALA   A 31  ? 0.2612 0.3028 0.2619 0.0306  0.0034  -0.0163 31  ALA   A C   
175  O  O   . ALA   A 31  ? 0.2409 0.2887 0.2403 0.0316  0.0034  -0.0143 31  ALA   A O   
176  C  CB  . ALA   A 31  ? 0.2774 0.3083 0.2802 0.0397  0.0034  -0.0195 31  ALA   A CB  
177  N  N   . LEU   A 32  ? 0.2326 0.2669 0.2337 0.0261  0.0037  -0.0155 32  LEU   A N   
178  C  CA  . LEU   A 32  ? 0.2282 0.2616 0.2281 0.0220  0.0040  -0.0125 32  LEU   A CA  
179  C  C   . LEU   A 32  ? 0.2170 0.2610 0.2151 0.0189  0.0036  -0.0127 32  LEU   A C   
180  O  O   . LEU   A 32  ? 0.2216 0.2688 0.2183 0.0178  0.0037  -0.0106 32  LEU   A O   
181  C  CB  . LEU   A 32  ? 0.2288 0.2543 0.2293 0.0181  0.0042  -0.0125 32  LEU   A CB  
182  C  CG  . LEU   A 32  ? 0.2425 0.2670 0.2415 0.0139  0.0044  -0.0099 32  LEU   A CG  
183  C  CD1 . LEU   A 32  ? 0.2563 0.2778 0.2551 0.0157  0.0048  -0.0066 32  LEU   A CD1 
184  C  CD2 . LEU   A 32  ? 0.2448 0.2633 0.2444 0.0105  0.0045  -0.0104 32  LEU   A CD2 
185  N  N   . CYS   A 33  ? 0.2056 0.2547 0.2036 0.0170  0.0032  -0.0154 33  CYS   A N   
186  C  CA  . CYS   A 33  ? 0.2190 0.2778 0.2152 0.0133  0.0030  -0.0156 33  CYS   A CA  
187  C  C   . CYS   A 33  ? 0.2121 0.2806 0.2077 0.0160  0.0029  -0.0155 33  CYS   A C   
188  O  O   . CYS   A 33  ? 0.2036 0.2775 0.1976 0.0130  0.0030  -0.0142 33  CYS   A O   
189  C  CB  . CYS   A 33  ? 0.2257 0.2894 0.2219 0.0116  0.0027  -0.0183 33  CYS   A CB  
190  S  SG  . CYS   A 33  ? 0.2604 0.3153 0.2566 0.0079  0.0028  -0.0182 33  CYS   A SG  
191  N  N   . HIS   A 34  ? 0.2217 0.2928 0.2186 0.0218  0.0027  -0.0170 34  HIS   A N   
192  C  CA  . HIS   A 34  ? 0.2454 0.3263 0.2418 0.0256  0.0025  -0.0169 34  HIS   A CA  
193  C  C   . HIS   A 34  ? 0.2382 0.3170 0.2338 0.0262  0.0028  -0.0136 34  HIS   A C   
194  O  O   . HIS   A 34  ? 0.2385 0.3271 0.2329 0.0253  0.0028  -0.0132 34  HIS   A O   
195  C  CB  . HIS   A 34  ? 0.2599 0.3416 0.2575 0.0329  0.0022  -0.0190 34  HIS   A CB  
196  C  CG  . HIS   A 34  ? 0.2827 0.3700 0.2810 0.0328  0.0018  -0.0228 34  HIS   A CG  
197  N  ND1 . HIS   A 34  ? 0.3243 0.4098 0.3239 0.0385  0.0014  -0.0256 34  HIS   A ND1 
198  C  CD2 . HIS   A 34  ? 0.2695 0.3641 0.2672 0.0277  0.0017  -0.0242 34  HIS   A CD2 
199  C  CE1 . HIS   A 34  ? 0.3093 0.4020 0.3094 0.0369  0.0011  -0.0289 34  HIS   A CE1 
200  N  NE2 . HIS   A 34  ? 0.2923 0.3907 0.2912 0.0303  0.0012  -0.0278 34  HIS   A NE2 
201  N  N   . GLN   A 35  ? 0.2407 0.3074 0.2368 0.0274  0.0032  -0.0114 35  GLN   A N   
202  C  CA  . GLN   A 35  ? 0.2632 0.3279 0.2586 0.0285  0.0036  -0.0081 35  GLN   A CA  
203  C  C   . GLN   A 35  ? 0.2267 0.2942 0.2208 0.0224  0.0037  -0.0071 35  GLN   A C   
204  O  O   . GLN   A 35  ? 0.2374 0.3092 0.2306 0.0229  0.0038  -0.0053 35  GLN   A O   
205  C  CB  . GLN   A 35  ? 0.3119 0.3630 0.3083 0.0302  0.0041  -0.0060 35  GLN   A CB  
206  C  CG  . GLN   A 35  ? 0.3870 0.4332 0.3844 0.0365  0.0042  -0.0065 35  GLN   A CG  
207  C  CD  . GLN   A 35  ? 0.5071 0.5391 0.5055 0.0366  0.0048  -0.0048 35  GLN   A CD  
208  O  OE1 . GLN   A 35  ? 0.6349 0.6617 0.6334 0.0321  0.0052  -0.0033 35  GLN   A OE1 
209  N  NE2 . GLN   A 35  ? 0.5969 0.6224 0.5959 0.0417  0.0050  -0.0052 35  GLN   A NE2 
210  N  N   . ALA   A 36  ? 0.2096 0.2746 0.2033 0.0170  0.0036  -0.0083 36  ALA   A N   
211  C  CA  . ALA   A 36  ? 0.1989 0.2647 0.1909 0.0113  0.0036  -0.0075 36  ALA   A CA  
212  C  C   . ALA   A 36  ? 0.2088 0.2873 0.1994 0.0091  0.0035  -0.0087 36  ALA   A C   
213  O  O   . ALA   A 36  ? 0.1839 0.2642 0.1731 0.0052  0.0035  -0.0082 36  ALA   A O   
214  C  CB  . ALA   A 36  ? 0.1871 0.2469 0.1787 0.0069  0.0036  -0.0084 36  ALA   A CB  
215  N  N   . LYS   A 37  ? 0.2034 0.2912 0.1946 0.0114  0.0032  -0.0107 37  LYS   A N   
216  C  CA  . LYS   A 37  ? 0.2090 0.3106 0.1991 0.0095  0.0032  -0.0120 37  LYS   A CA  
217  C  C   . LYS   A 37  ? 0.2185 0.3269 0.2090 0.0152  0.0031  -0.0112 37  LYS   A C   
218  O  O   . LYS   A 37  ? 0.2216 0.3348 0.2130 0.0211  0.0029  -0.0120 37  LYS   A O   
219  C  CB  . LYS   A 37  ? 0.2224 0.3316 0.2127 0.0088  0.0030  -0.0146 37  LYS   A CB  
220  C  CG  . LYS   A 37  ? 0.2138 0.3391 0.2031 0.0064  0.0029  -0.0163 37  LYS   A CG  
221  C  CD  . LYS   A 37  ? 0.2175 0.3508 0.2073 0.0068  0.0027  -0.0187 37  LYS   A CD  
222  C  CE  . LYS   A 37  ? 0.2382 0.3879 0.2269 0.0031  0.0029  -0.0204 37  LYS   A CE  
223  N  NZ  . LYS   A 37  ? 0.2495 0.4081 0.2387 0.0041  0.0027  -0.0228 37  LYS   A NZ  
224  N  N   . THR   A 38  ? 0.2073 0.3152 0.1971 0.0143  0.0033  -0.0095 38  THR   A N   
225  C  CA  . THR   A 38  ? 0.2043 0.3167 0.1944 0.0202  0.0033  -0.0079 38  THR   A CA  
226  C  C   . THR   A 38  ? 0.1948 0.3241 0.1841 0.0195  0.0031  -0.0096 38  THR   A C   
227  O  O   . THR   A 38  ? 0.1900 0.3254 0.1784 0.0130  0.0032  -0.0116 38  THR   A O   
228  C  CB  . THR   A 38  ? 0.2117 0.3160 0.2015 0.0202  0.0036  -0.0050 38  THR   A CB  
229  O  OG1 . THR   A 38  ? 0.1969 0.3094 0.1855 0.0162  0.0036  -0.0056 38  THR   A OG1 
230  C  CG2 . THR   A 38  ? 0.2151 0.3044 0.2052 0.0174  0.0038  -0.0040 38  THR   A CG2 
231  N  N   . PRO   A 39  ? 0.2170 0.3543 0.2064 0.0259  0.0030  -0.0087 39  PRO   A N   
232  C  CA  . PRO   A 39  ? 0.2145 0.3697 0.2032 0.0255  0.0028  -0.0105 39  PRO   A CA  
233  C  C   . PRO   A 39  ? 0.2026 0.3624 0.1903 0.0186  0.0031  -0.0112 39  PRO   A C   
234  O  O   . PRO   A 39  ? 0.1821 0.3569 0.1693 0.0162  0.0030  -0.0135 39  PRO   A O   
235  C  CB  . PRO   A 39  ? 0.2313 0.3910 0.2202 0.0350  0.0027  -0.0086 39  PRO   A CB  
236  C  CG  . PRO   A 39  ? 0.2538 0.3989 0.2434 0.0402  0.0027  -0.0068 39  PRO   A CG  
237  C  CD  . PRO   A 39  ? 0.2407 0.3708 0.2307 0.0340  0.0030  -0.0061 39  PRO   A CD  
238  N  N   . VAL   A 40  ? 0.1862 0.3337 0.1735 0.0159  0.0033  -0.0093 40  VAL   A N   
239  C  CA  . VAL   A 40  ? 0.1837 0.3342 0.1700 0.0101  0.0034  -0.0102 40  VAL   A CA  
240  C  C   . VAL   A 40  ? 0.1887 0.3293 0.1741 0.0021  0.0036  -0.0113 40  VAL   A C   
241  O  O   . VAL   A 40  ? 0.1895 0.3297 0.1737 -0.0029 0.0037  -0.0122 40  VAL   A O   
242  C  CB  . VAL   A 40  ? 0.2142 0.3615 0.2004 0.0138  0.0035  -0.0075 40  VAL   A CB  
243  C  CG1 . VAL   A 40  ? 0.2280 0.3854 0.2147 0.0220  0.0034  -0.0059 40  VAL   A CG1 
244  C  CG2 . VAL   A 40  ? 0.2113 0.3412 0.1980 0.0147  0.0037  -0.0047 40  VAL   A CG2 
245  N  N   . GLY   A 41  ? 0.1768 0.3096 0.1624 0.0013  0.0036  -0.0113 41  GLY   A N   
246  C  CA  . GLY   A 41  ? 0.1746 0.2981 0.1590 -0.0053 0.0037  -0.0119 41  GLY   A CA  
247  C  C   . GLY   A 41  ? 0.1714 0.2810 0.1566 -0.0031 0.0036  -0.0103 41  GLY   A C   
248  O  O   . GLY   A 41  ? 0.1724 0.2790 0.1592 0.0030  0.0036  -0.0088 41  GLY   A O   
249  N  N   . ASN   A 42  ? 0.1727 0.2746 0.1566 -0.0085 0.0037  -0.0107 42  ASN   A N   
250  C  CA  . ASN   A 42  ? 0.1839 0.2742 0.1683 -0.0075 0.0037  -0.0097 42  ASN   A CA  
251  C  C   . ASN   A 42  ? 0.1928 0.2717 0.1770 -0.0074 0.0037  -0.0079 42  ASN   A C   
252  O  O   . ASN   A 42  ? 0.1762 0.2542 0.1588 -0.0106 0.0037  -0.0080 42  ASN   A O   
253  C  CB  . ASN   A 42  ? 0.1895 0.2785 0.1723 -0.0130 0.0037  -0.0107 42  ASN   A CB  
254  C  CG  . ASN   A 42  ? 0.2061 0.3071 0.1893 -0.0133 0.0038  -0.0125 42  ASN   A CG  
255  O  OD1 . ASN   A 42  ? 0.1937 0.3016 0.1788 -0.0079 0.0036  -0.0130 42  ASN   A OD1 
256  N  ND2 . ASN   A 42  ? 0.2354 0.3385 0.2167 -0.0193 0.0040  -0.0133 42  ASN   A ND2 
257  N  N   . THR   A 43  ? 0.1876 0.2581 0.1733 -0.0037 0.0037  -0.0065 43  THR   A N   
258  C  CA  . THR   A 43  ? 0.1775 0.2375 0.1629 -0.0043 0.0037  -0.0051 43  THR   A CA  
259  C  C   . THR   A 43  ? 0.1782 0.2329 0.1614 -0.0096 0.0035  -0.0059 43  THR   A C   
260  O  O   . THR   A 43  ? 0.1770 0.2352 0.1592 -0.0124 0.0035  -0.0072 43  THR   A O   
261  C  CB  . THR   A 43  ? 0.1796 0.2324 0.1671 -0.0001 0.0038  -0.0037 43  THR   A CB  
262  O  OG1 . THR   A 43  ? 0.1861 0.2372 0.1744 0.0000  0.0037  -0.0049 43  THR   A OG1 
263  C  CG2 . THR   A 43  ? 0.1897 0.2461 0.1789 0.0053  0.0040  -0.0024 43  THR   A CG2 
264  N  N   . ALA   A 44  ? 0.1600 0.2066 0.1420 -0.0108 0.0034  -0.0051 44  ALA   A N   
265  C  CA  . ALA   A 44  ? 0.1617 0.2020 0.1412 -0.0148 0.0033  -0.0056 44  ALA   A CA  
266  C  C   . ALA   A 44  ? 0.1583 0.1947 0.1384 -0.0142 0.0033  -0.0055 44  ALA   A C   
267  O  O   . ALA   A 44  ? 0.1726 0.2079 0.1506 -0.0175 0.0032  -0.0059 44  ALA   A O   
268  C  CB  . ALA   A 44  ? 0.1589 0.1921 0.1371 -0.0150 0.0031  -0.0049 44  ALA   A CB  
269  N  N   . ALA   A 45  ? 0.1517 0.1860 0.1345 -0.0102 0.0033  -0.0049 45  ALA   A N   
270  C  CA  . ALA   A 45  ? 0.1596 0.1899 0.1434 -0.0094 0.0033  -0.0052 45  ALA   A CA  
271  C  C   . ALA   A 45  ? 0.1527 0.1837 0.1397 -0.0052 0.0035  -0.0053 45  ALA   A C   
272  O  O   . ALA   A 45  ? 0.1402 0.1727 0.1285 -0.0025 0.0037  -0.0043 45  ALA   A O   
273  C  CB  . ALA   A 45  ? 0.1567 0.1789 0.1394 -0.0101 0.0031  -0.0045 45  ALA   A CB  
274  N  N   . ILE   A 46  ? 0.1478 0.1773 0.1359 -0.0046 0.0034  -0.0064 46  ILE   A N   
275  C  CA  . ILE   A 46  ? 0.1690 0.1955 0.1600 -0.0012 0.0037  -0.0067 46  ILE   A CA  
276  C  C   . ILE   A 46  ? 0.1699 0.1898 0.1611 -0.0022 0.0036  -0.0067 46  ILE   A C   
277  O  O   . ILE   A 46  ? 0.1764 0.1957 0.1656 -0.0047 0.0033  -0.0070 46  ILE   A O   
278  C  CB  . ILE   A 46  ? 0.1938 0.2253 0.1862 0.0008  0.0036  -0.0088 46  ILE   A CB  
279  C  CG1 . ILE   A 46  ? 0.2321 0.2663 0.2233 -0.0018 0.0033  -0.0103 46  ILE   A CG1 
280  C  CG2 . ILE   A 46  ? 0.2035 0.2426 0.1958 0.0025  0.0036  -0.0087 46  ILE   A CG2 
281  C  CD1 . ILE   A 46  ? 0.2895 0.3200 0.2825 -0.0008 0.0033  -0.0119 46  ILE   A CD1 
282  N  N   . SER   A 47  ? 0.1607 0.1762 0.1542 -0.0001 0.0040  -0.0065 47  SER   A N   
283  C  CA  A SER   A 47  ? 0.1662 0.1766 0.1604 -0.0009 0.0041  -0.0066 47  SER   A CA  
284  C  CA  B SER   A 47  ? 0.1770 0.1875 0.1712 -0.0010 0.0041  -0.0067 47  SER   A CA  
285  C  C   . SER   A 47  ? 0.1699 0.1786 0.1669 0.0006  0.0043  -0.0086 47  SER   A C   
286  O  O   . SER   A 47  ? 0.1740 0.1808 0.1728 0.0029  0.0048  -0.0083 47  SER   A O   
287  C  CB  A SER   A 47  ? 0.1720 0.1789 0.1663 -0.0008 0.0044  -0.0045 47  SER   A CB  
288  C  CB  B SER   A 47  ? 0.1977 0.2046 0.1918 -0.0010 0.0043  -0.0046 47  SER   A CB  
289  O  OG  A SER   A 47  ? 0.1710 0.1785 0.1626 -0.0025 0.0040  -0.0036 47  SER   A OG  
290  O  OG  B SER   A 47  ? 0.2361 0.2400 0.2301 -0.0023 0.0043  -0.0050 47  SER   A OG  
291  N  N   . VAL   A 48  ? 0.1721 0.1814 0.1693 -0.0006 0.0041  -0.0106 48  VAL   A N   
292  C  CA  . VAL   A 48  ? 0.1666 0.1751 0.1663 0.0005  0.0042  -0.0133 48  VAL   A CA  
293  C  C   . VAL   A 48  ? 0.1715 0.1787 0.1716 -0.0012 0.0041  -0.0145 48  VAL   A C   
294  O  O   . VAL   A 48  ? 0.1728 0.1806 0.1707 -0.0027 0.0038  -0.0133 48  VAL   A O   
295  C  CB  . VAL   A 48  ? 0.1820 0.1963 0.1818 0.0015  0.0038  -0.0156 48  VAL   A CB  
296  C  CG1 . VAL   A 48  ? 0.1851 0.2019 0.1847 0.0037  0.0039  -0.0148 48  VAL   A CG1 
297  C  CG2 . VAL   A 48  ? 0.1895 0.2084 0.1867 -0.0008 0.0033  -0.0157 48  VAL   A CG2 
298  N  N   . TYR   A 49  ? 0.1624 0.1680 0.1653 -0.0008 0.0044  -0.0171 49  TYR   A N   
299  C  CA  . TYR   A 49  ? 0.1800 0.1866 0.1833 -0.0024 0.0043  -0.0191 49  TYR   A CA  
300  C  C   . TYR   A 49  ? 0.1640 0.1767 0.1656 -0.0026 0.0036  -0.0204 49  TYR   A C   
301  O  O   . TYR   A 49  ? 0.1658 0.1821 0.1669 -0.0017 0.0034  -0.0210 49  TYR   A O   
302  C  CB  . TYR   A 49  ? 0.2111 0.2151 0.2179 -0.0024 0.0048  -0.0222 49  TYR   A CB  
303  C  CG  . TYR   A 49  ? 0.2640 0.2619 0.2724 -0.0032 0.0056  -0.0206 49  TYR   A CG  
304  C  CD1 . TYR   A 49  ? 0.3282 0.3255 0.3354 -0.0046 0.0058  -0.0181 49  TYR   A CD1 
305  C  CD2 . TYR   A 49  ? 0.3867 0.3791 0.3973 -0.0023 0.0063  -0.0213 49  TYR   A CD2 
306  C  CE1 . TYR   A 49  ? 0.3528 0.3456 0.3614 -0.0056 0.0066  -0.0164 49  TYR   A CE1 
307  C  CE2 . TYR   A 49  ? 0.4014 0.3879 0.4131 -0.0034 0.0073  -0.0193 49  TYR   A CE2 
308  C  CZ  . TYR   A 49  ? 0.4182 0.4055 0.4289 -0.0052 0.0074  -0.0168 49  TYR   A CZ  
309  O  OH  . TYR   A 49  ? 0.5130 0.4959 0.5248 -0.0067 0.0084  -0.0146 49  TYR   A OH  
310  N  N   . PRO   A 50  ? 0.1631 0.1779 0.1635 -0.0038 0.0033  -0.0208 50  PRO   A N   
311  C  CA  . PRO   A 50  ? 0.1561 0.1763 0.1541 -0.0040 0.0027  -0.0210 50  PRO   A CA  
312  C  C   . PRO   A 50  ? 0.1573 0.1827 0.1566 -0.0032 0.0026  -0.0240 50  PRO   A C   
313  O  O   . PRO   A 50  ? 0.1403 0.1699 0.1375 -0.0033 0.0023  -0.0232 50  PRO   A O   
314  C  CB  . PRO   A 50  ? 0.1560 0.1773 0.1534 -0.0046 0.0025  -0.0215 50  PRO   A CB  
315  C  CG  . PRO   A 50  ? 0.1623 0.1785 0.1600 -0.0049 0.0028  -0.0197 50  PRO   A CG  
316  C  CD  . PRO   A 50  ? 0.1605 0.1731 0.1613 -0.0047 0.0035  -0.0203 50  PRO   A CD  
317  N  N   . ARG   A 51  ? 0.1591 0.1843 0.1620 -0.0025 0.0028  -0.0275 51  ARG   A N   
318  C  CA  . ARG   A 51  ? 0.1738 0.2043 0.1782 -0.0014 0.0026  -0.0311 51  ARG   A CA  
319  C  C   . ARG   A 51  ? 0.1707 0.2026 0.1748 0.0002  0.0025  -0.0307 51  ARG   A C   
320  O  O   . ARG   A 51  ? 0.1632 0.2016 0.1676 0.0012  0.0022  -0.0332 51  ARG   A O   
321  C  CB  . ARG   A 51  ? 0.2100 0.2384 0.2182 -0.0011 0.0029  -0.0354 51  ARG   A CB  
322  C  CG  . ARG   A 51  ? 0.2735 0.2936 0.2838 -0.0004 0.0035  -0.0351 51  ARG   A CG  
323  C  CD  . ARG   A 51  ? 0.3361 0.3532 0.3500 -0.0007 0.0039  -0.0396 51  ARG   A CD  
324  N  NE  . ARG   A 51  ? 0.4527 0.4605 0.4681 -0.0010 0.0048  -0.0384 51  ARG   A NE  
325  C  CZ  . ARG   A 51  ? 0.5151 0.5189 0.5305 -0.0032 0.0053  -0.0359 51  ARG   A CZ  
326  N  NH1 . ARG   A 51  ? 0.4887 0.4968 0.5029 -0.0051 0.0051  -0.0348 51  ARG   A NH1 
327  N  NH2 . ARG   A 51  ? 0.6234 0.6191 0.6399 -0.0034 0.0062  -0.0343 51  ARG   A NH2 
328  N  N   . SER   A 52  ? 0.1684 0.1954 0.1718 0.0005  0.0028  -0.0277 52  SER   A N   
329  C  CA  . SER   A 52  ? 0.1674 0.1963 0.1706 0.0023  0.0028  -0.0272 52  SER   A CA  
330  C  C   . SER   A 52  ? 0.1556 0.1895 0.1554 0.0008  0.0026  -0.0245 52  SER   A C   
331  O  O   . SER   A 52  ? 0.1602 0.1979 0.1595 0.0019  0.0025  -0.0243 52  SER   A O   
332  C  CB  . SER   A 52  ? 0.1930 0.2148 0.1973 0.0037  0.0033  -0.0255 52  SER   A CB  
333  O  OG  . SER   A 52  ? 0.2042 0.2207 0.2114 0.0048  0.0037  -0.0281 52  SER   A OG  
334  N  N   . ILE   A 53  ? 0.1462 0.1803 0.1435 -0.0016 0.0024  -0.0226 53  ILE   A N   
335  C  CA  . ILE   A 53  ? 0.1557 0.1923 0.1493 -0.0036 0.0023  -0.0197 53  ILE   A CA  
336  C  C   . ILE   A 53  ? 0.1482 0.1938 0.1412 -0.0038 0.0022  -0.0210 53  ILE   A C   
337  O  O   . ILE   A 53  ? 0.1422 0.1912 0.1338 -0.0046 0.0022  -0.0198 53  ILE   A O   
338  C  CB  . ILE   A 53  ? 0.1607 0.1942 0.1514 -0.0057 0.0022  -0.0174 53  ILE   A CB  
339  C  CG1 . ILE   A 53  ? 0.1684 0.1943 0.1594 -0.0055 0.0024  -0.0159 53  ILE   A CG1 
340  C  CG2 . ILE   A 53  ? 0.1720 0.2078 0.1585 -0.0083 0.0022  -0.0148 53  ILE   A CG2 
341  C  CD1 . ILE   A 53  ? 0.1764 0.1994 0.1648 -0.0065 0.0021  -0.0144 53  ILE   A CD1 
342  N  N   . PRO   A 54  ? 0.1576 0.2084 0.1514 -0.0032 0.0019  -0.0236 54  PRO   A N   
343  C  CA  . PRO   A 54  ? 0.1559 0.2165 0.1488 -0.0035 0.0018  -0.0246 54  PRO   A CA  
344  C  C   . PRO   A 54  ? 0.1665 0.2315 0.1613 -0.0013 0.0018  -0.0264 54  PRO   A C   
345  O  O   . PRO   A 54  ? 0.1649 0.2364 0.1579 -0.0025 0.0019  -0.0254 54  PRO   A O   
346  C  CB  . PRO   A 54  ? 0.1614 0.2265 0.1556 -0.0026 0.0015  -0.0277 54  PRO   A CB  
347  C  CG  . PRO   A 54  ? 0.1633 0.2214 0.1570 -0.0034 0.0016  -0.0265 54  PRO   A CG  
348  C  CD  . PRO   A 54  ? 0.1619 0.2111 0.1570 -0.0028 0.0018  -0.0255 54  PRO   A CD  
349  N  N   . ILE   A 55  ? 0.1646 0.2258 0.1627 0.0021  0.0018  -0.0290 55  ILE   A N   
350  C  CA  . ILE   A 55  ? 0.1875 0.2524 0.1869 0.0052  0.0017  -0.0306 55  ILE   A CA  
351  C  C   . ILE   A 55  ? 0.1758 0.2386 0.1738 0.0047  0.0019  -0.0273 55  ILE   A C   
352  O  O   . ILE   A 55  ? 0.1733 0.2433 0.1709 0.0058  0.0019  -0.0276 55  ILE   A O   
353  C  CB  . ILE   A 55  ? 0.2176 0.2781 0.2204 0.0092  0.0016  -0.0343 55  ILE   A CB  
354  C  CG1 . ILE   A 55  ? 0.2527 0.3193 0.2566 0.0134  0.0013  -0.0368 55  ILE   A CG1 
355  C  CG2 . ILE   A 55  ? 0.2156 0.2645 0.2195 0.0096  0.0020  -0.0326 55  ILE   A CG2 
356  C  CD1 . ILE   A 55  ? 0.2701 0.3500 0.2730 0.0131  0.0009  -0.0386 55  ILE   A CD1 
357  N  N   . ALA   A 56  ? 0.1574 0.2118 0.1545 0.0029  0.0022  -0.0244 56  ALA   A N   
358  C  CA  . ALA   A 56  ? 0.1655 0.2191 0.1611 0.0019  0.0024  -0.0214 56  ALA   A CA  
359  C  C   . ALA   A 56  ? 0.1580 0.2190 0.1506 -0.0017 0.0024  -0.0200 56  ALA   A C   
360  O  O   . ALA   A 56  ? 0.1670 0.2335 0.1590 -0.0016 0.0025  -0.0195 56  ALA   A O   
361  C  CB  . ALA   A 56  ? 0.1871 0.2311 0.1822 0.0006  0.0027  -0.0189 56  ALA   A CB  
362  N  N   . ARG   A 57  ? 0.1643 0.2258 0.1547 -0.0049 0.0024  -0.0193 57  ARG   A N   
363  C  CA  . ARG   A 57  ? 0.1798 0.2465 0.1669 -0.0091 0.0026  -0.0174 57  ARG   A CA  
364  C  C   . ARG   A 57  ? 0.1845 0.2634 0.1722 -0.0085 0.0026  -0.0194 57  ARG   A C   
365  O  O   . ARG   A 57  ? 0.1973 0.2821 0.1834 -0.0109 0.0028  -0.0184 57  ARG   A O   
366  C  CB  . ARG   A 57  ? 0.1838 0.2481 0.1683 -0.0119 0.0026  -0.0160 57  ARG   A CB  
367  C  CG  . ARG   A 57  ? 0.2268 0.2950 0.2073 -0.0166 0.0030  -0.0136 57  ARG   A CG  
368  C  CD  . ARG   A 57  ? 0.2689 0.3304 0.2468 -0.0195 0.0032  -0.0109 57  ARG   A CD  
369  N  NE  . ARG   A 57  ? 0.2628 0.3140 0.2391 -0.0196 0.0031  -0.0092 57  ARG   A NE  
370  C  CZ  . ARG   A 57  ? 0.2714 0.3148 0.2462 -0.0206 0.0031  -0.0076 57  ARG   A CZ  
371  N  NH1 . ARG   A 57  ? 0.2665 0.3108 0.2413 -0.0218 0.0033  -0.0074 57  ARG   A NH1 
372  N  NH2 . ARG   A 57  ? 0.2490 0.2843 0.2222 -0.0202 0.0029  -0.0063 57  ARG   A NH2 
373  N  N   . LYS   A 58  ? 0.1814 0.2646 0.1714 -0.0053 0.0023  -0.0225 58  LYS   A N   
374  C  CA  . LYS   A 58  ? 0.1934 0.2890 0.1842 -0.0039 0.0021  -0.0249 58  LYS   A CA  
375  C  C   . LYS   A 58  ? 0.1913 0.2903 0.1832 -0.0014 0.0021  -0.0254 58  LYS   A C   
376  O  O   . LYS   A 58  ? 0.1916 0.3010 0.1823 -0.0030 0.0022  -0.0253 58  LYS   A O   
377  C  CB  . LYS   A 58  ? 0.2029 0.3014 0.1963 -0.0002 0.0017  -0.0289 58  LYS   A CB  
378  C  CG  . LYS   A 58  ? 0.2122 0.3247 0.2062 0.0015  0.0014  -0.0318 58  LYS   A CG  
379  C  CD  . LYS   A 58  ? 0.2320 0.3466 0.2287 0.0055  0.0009  -0.0363 58  LYS   A CD  
380  C  CE  . LYS   A 58  ? 0.2745 0.4042 0.2716 0.0071  0.0006  -0.0394 58  LYS   A CE  
381  N  NZ  . LYS   A 58  ? 0.2710 0.4031 0.2703 0.0102  0.0002  -0.0438 58  LYS   A NZ  
382  N  N   . THR   A 59  ? 0.1758 0.2663 0.1696 0.0022  0.0020  -0.0256 59  THR   A N   
383  C  CA  . THR   A 59  ? 0.1951 0.2883 0.1898 0.0057  0.0019  -0.0258 59  THR   A CA  
384  C  C   . THR   A 59  ? 0.2207 0.3164 0.2130 0.0018  0.0023  -0.0229 59  THR   A C   
385  O  O   . THR   A 59  ? 0.2257 0.3314 0.2178 0.0025  0.0023  -0.0235 59  THR   A O   
386  C  CB  . THR   A 59  ? 0.2109 0.2932 0.2078 0.0100  0.0019  -0.0260 59  THR   A CB  
387  O  OG1 . THR   A 59  ? 0.2170 0.2967 0.2159 0.0127  0.0016  -0.0291 59  THR   A OG1 
388  C  CG2 . THR   A 59  ? 0.2220 0.3070 0.2196 0.0147  0.0018  -0.0262 59  THR   A CG2 
389  N  N   . LEU   A 60  ? 0.1983 0.2854 0.1889 -0.0021 0.0026  -0.0202 60  LEU   A N   
390  C  CA  . LEU   A 60  ? 0.2053 0.2939 0.1936 -0.0061 0.0029  -0.0180 60  LEU   A CA  
391  C  C   . LEU   A 60  ? 0.2213 0.3212 0.2075 -0.0106 0.0031  -0.0182 60  LEU   A C   
392  O  O   . LEU   A 60  ? 0.2266 0.3337 0.2119 -0.0125 0.0033  -0.0180 60  LEU   A O   
393  C  CB  . LEU   A 60  ? 0.1990 0.2761 0.1856 -0.0092 0.0031  -0.0154 60  LEU   A CB  
394  C  CG  . LEU   A 60  ? 0.1970 0.2642 0.1855 -0.0056 0.0030  -0.0148 60  LEU   A CG  
395  C  CD1 . LEU   A 60  ? 0.1972 0.2544 0.1840 -0.0084 0.0031  -0.0128 60  LEU   A CD1 
396  C  CD2 . LEU   A 60  ? 0.1962 0.2653 0.1854 -0.0033 0.0030  -0.0142 60  LEU   A CD2 
397  N  N   . LYS   A 61  ? 0.2463 0.3481 0.2316 -0.0127 0.0032  -0.0185 61  LYS   A N   
398  C  CA  . LYS   A 61  ? 0.2617 0.3744 0.2448 -0.0173 0.0035  -0.0184 61  LYS   A CA  
399  C  C   . LYS   A 61  ? 0.2543 0.3814 0.2392 -0.0143 0.0033  -0.0212 61  LYS   A C   
400  O  O   . LYS   A 61  ? 0.2544 0.3913 0.2380 -0.0176 0.0037  -0.0210 61  LYS   A O   
401  C  CB  . LYS   A 61  ? 0.2844 0.3969 0.2661 -0.0195 0.0036  -0.0180 61  LYS   A CB  
402  C  CG  . LYS   A 61  ? 0.3400 0.4404 0.3189 -0.0231 0.0039  -0.0148 61  LYS   A CG  
403  C  CD  . LYS   A 61  ? 0.4251 0.5262 0.4026 -0.0241 0.0039  -0.0144 61  LYS   A CD  
404  C  CE  . LYS   A 61  ? 0.5074 0.5973 0.4815 -0.0271 0.0041  -0.0111 61  LYS   A CE  
405  N  NZ  . LYS   A 61  ? 0.5497 0.6398 0.5232 -0.0262 0.0039  -0.0110 61  LYS   A NZ  
406  N  N   . GLU   A 62  ? 0.2362 0.3646 0.2241 -0.0078 0.0028  -0.0239 62  GLU   A N   
407  C  CA  . GLU   A 62  ? 0.2684 0.4105 0.2579 -0.0038 0.0024  -0.0269 62  GLU   A CA  
408  C  C   . GLU   A 62  ? 0.2562 0.4027 0.2459 -0.0021 0.0024  -0.0267 62  GLU   A C   
409  O  O   . GLU   A 62  ? 0.2485 0.4094 0.2382 -0.0017 0.0024  -0.0283 62  GLU   A O   
410  C  CB  . GLU   A 62  ? 0.3173 0.4581 0.3097 0.0033  0.0018  -0.0302 62  GLU   A CB  
411  C  CG  . GLU   A 62  ? 0.4142 0.5578 0.4065 0.0021  0.0017  -0.0317 62  GLU   A CG  
412  C  CD  . GLU   A 62  ? 0.4792 0.6215 0.4744 0.0086  0.0010  -0.0357 62  GLU   A CD  
413  O  OE1 . GLU   A 62  ? 0.5426 0.6806 0.5397 0.0144  0.0007  -0.0372 62  GLU   A OE1 
414  O  OE2 . GLU   A 62  ? 0.5426 0.6879 0.5379 0.0077  0.0009  -0.0372 62  GLU   A OE2 
415  N  N   . GLN   A 63  ? 0.2341 0.3696 0.2241 -0.0009 0.0025  -0.0249 63  GLN   A N   
416  C  CA  . GLN   A 63  ? 0.2268 0.3671 0.2169 0.0010  0.0025  -0.0246 63  GLN   A CA  
417  C  C   . GLN   A 63  ? 0.2143 0.3579 0.2020 -0.0062 0.0031  -0.0227 63  GLN   A C   
418  O  O   . GLN   A 63  ? 0.2515 0.3990 0.2391 -0.0054 0.0031  -0.0224 63  GLN   A O   
419  C  CB  . GLN   A 63  ? 0.2262 0.3547 0.2178 0.0062  0.0023  -0.0235 63  GLN   A CB  
420  C  CG  . GLN   A 63  ? 0.2202 0.3348 0.2108 0.0024  0.0026  -0.0206 63  GLN   A CG  
421  C  CD  . GLN   A 63  ? 0.2354 0.3397 0.2274 0.0074  0.0025  -0.0195 63  GLN   A CD  
422  O  OE1 . GLN   A 63  ? 0.2491 0.3535 0.2429 0.0137  0.0022  -0.0207 63  GLN   A OE1 
423  N  NE2 . GLN   A 63  ? 0.2191 0.3142 0.2102 0.0047  0.0028  -0.0170 63  GLN   A NE2 
424  N  N   . GLY   A 64  ? 0.2313 0.3733 0.2168 -0.0130 0.0035  -0.0215 64  GLY   A N   
425  C  CA  . GLY   A 64  ? 0.2583 0.4030 0.2411 -0.0204 0.0041  -0.0201 64  GLY   A CA  
426  C  C   . GLY   A 64  ? 0.2641 0.3960 0.2459 -0.0220 0.0042  -0.0180 64  GLY   A C   
427  O  O   . GLY   A 64  ? 0.2738 0.4088 0.2540 -0.0263 0.0046  -0.0177 64  GLY   A O   
428  N  N   . THR   A 65  ? 0.2489 0.3670 0.2315 -0.0189 0.0039  -0.0169 65  THR   A N   
429  C  CA  . THR   A 65  ? 0.2293 0.3358 0.2108 -0.0205 0.0040  -0.0150 65  THR   A CA  
430  C  C   . THR   A 65  ? 0.2375 0.3318 0.2174 -0.0228 0.0041  -0.0134 65  THR   A C   
431  O  O   . THR   A 65  ? 0.2238 0.3076 0.2046 -0.0200 0.0038  -0.0125 65  THR   A O   
432  C  CB  . THR   A 65  ? 0.2225 0.3250 0.2064 -0.0143 0.0037  -0.0148 65  THR   A CB  
433  O  OG1 . THR   A 65  ? 0.2107 0.3069 0.1965 -0.0096 0.0034  -0.0151 65  THR   A OG1 
434  C  CG2 . THR   A 65  ? 0.2265 0.3413 0.2115 -0.0113 0.0036  -0.0161 65  THR   A CG2 
435  N  N   . PRO   A 66  ? 0.2642 0.3597 0.2414 -0.0283 0.0044  -0.0127 66  PRO   A N   
436  C  CA  . PRO   A 66  ? 0.2758 0.3608 0.2511 -0.0300 0.0045  -0.0109 66  PRO   A CA  
437  C  C   . PRO   A 66  ? 0.2809 0.3535 0.2539 -0.0320 0.0045  -0.0091 66  PRO   A C   
438  O  O   . PRO   A 66  ? 0.3113 0.3745 0.2830 -0.0318 0.0043  -0.0078 66  PRO   A O   
439  C  CB  . PRO   A 66  ? 0.2918 0.3836 0.2644 -0.0353 0.0050  -0.0104 66  PRO   A CB  
440  C  CG  . PRO   A 66  ? 0.2872 0.3886 0.2591 -0.0392 0.0054  -0.0112 66  PRO   A CG  
441  C  CD  . PRO   A 66  ? 0.2940 0.4018 0.2696 -0.0331 0.0049  -0.0133 66  PRO   A CD  
442  N  N   . GLU   A 67  ? 0.2547 0.3279 0.2274 -0.0335 0.0046  -0.0093 67  GLU   A N   
443  C  CA  . GLU   A 67  ? 0.2762 0.3385 0.2467 -0.0352 0.0045  -0.0081 67  GLU   A CA  
444  C  C   . GLU   A 67  ? 0.2722 0.3290 0.2454 -0.0296 0.0041  -0.0081 67  GLU   A C   
445  O  O   . GLU   A 67  ? 0.3100 0.3584 0.2819 -0.0300 0.0039  -0.0073 67  GLU   A O   
446  C  CB  . GLU   A 67  ? 0.3531 0.4186 0.3216 -0.0403 0.0049  -0.0087 67  GLU   A CB  
447  C  CG  . GLU   A 67  ? 0.4526 0.5214 0.4177 -0.0472 0.0056  -0.0082 67  GLU   A CG  
448  C  CD  . GLU   A 67  ? 0.6095 0.6801 0.5721 -0.0536 0.0061  -0.0090 67  GLU   A CD  
449  O  OE1 . GLU   A 67  ? 0.6853 0.7518 0.6479 -0.0532 0.0058  -0.0098 67  GLU   A OE1 
450  O  OE2 . GLU   A 67  ? 0.7421 0.8189 0.7026 -0.0594 0.0068  -0.0090 67  GLU   A OE2 
451  N  N   . ILE   A 68  ? 0.2240 0.2855 0.2008 -0.0244 0.0039  -0.0090 68  ILE   A N   
452  C  CA  . ILE   A 68  ? 0.2076 0.2625 0.1866 -0.0196 0.0036  -0.0086 68  ILE   A CA  
453  C  C   . ILE   A 68  ? 0.1963 0.2421 0.1747 -0.0193 0.0034  -0.0078 68  ILE   A C   
454  O  O   . ILE   A 68  ? 0.2037 0.2512 0.1823 -0.0192 0.0034  -0.0083 68  ILE   A O   
455  C  CB  . ILE   A 68  ? 0.1911 0.2515 0.1736 -0.0142 0.0035  -0.0095 68  ILE   A CB  
456  C  CG1 . ILE   A 68  ? 0.1837 0.2541 0.1666 -0.0137 0.0036  -0.0102 68  ILE   A CG1 
457  C  CG2 . ILE   A 68  ? 0.2039 0.2562 0.1885 -0.0101 0.0034  -0.0087 68  ILE   A CG2 
458  C  CD1 . ILE   A 68  ? 0.1907 0.2659 0.1765 -0.0075 0.0035  -0.0109 68  ILE   A CD1 
459  N  N   . ARG   A 69  ? 0.1805 0.2177 0.1581 -0.0191 0.0033  -0.0067 69  ARG   A N   
460  C  CA  . ARG   A 69  ? 0.1850 0.2144 0.1614 -0.0189 0.0031  -0.0059 69  ARG   A CA  
461  C  C   . ARG   A 69  ? 0.1797 0.2084 0.1597 -0.0147 0.0030  -0.0066 69  ARG   A C   
462  O  O   . ARG   A 69  ? 0.1732 0.2039 0.1561 -0.0117 0.0031  -0.0071 69  ARG   A O   
463  C  CB  . ARG   A 69  ? 0.2092 0.2306 0.1835 -0.0197 0.0029  -0.0049 69  ARG   A CB  
464  C  CG  . ARG   A 69  ? 0.2712 0.2917 0.2418 -0.0241 0.0030  -0.0046 69  ARG   A CG  
465  C  CD  . ARG   A 69  ? 0.3796 0.3955 0.3498 -0.0233 0.0027  -0.0045 69  ARG   A CD  
466  N  NE  . ARG   A 69  ? 0.4691 0.4836 0.4361 -0.0271 0.0028  -0.0050 69  ARG   A NE  
467  C  CZ  . ARG   A 69  ? 0.5060 0.5273 0.4735 -0.0290 0.0030  -0.0060 69  ARG   A CZ  
468  N  NH1 . ARG   A 69  ? 0.4668 0.4969 0.4376 -0.0267 0.0032  -0.0065 69  ARG   A NH1 
469  N  NH2 . ARG   A 69  ? 0.5321 0.5513 0.4965 -0.0331 0.0031  -0.0068 69  ARG   A NH2 
470  N  N   . ILE   A 70  ? 0.1523 0.1780 0.1319 -0.0146 0.0028  -0.0067 70  ILE   A N   
471  C  CA  . ILE   A 70  ? 0.1602 0.1844 0.1429 -0.0113 0.0028  -0.0078 70  ILE   A CA  
472  C  C   . ILE   A 70  ? 0.1514 0.1684 0.1334 -0.0109 0.0026  -0.0069 70  ILE   A C   
473  O  O   . ILE   A 70  ? 0.1554 0.1699 0.1348 -0.0122 0.0024  -0.0063 70  ILE   A O   
474  C  CB  . ILE   A 70  ? 0.1771 0.2057 0.1608 -0.0108 0.0027  -0.0094 70  ILE   A CB  
475  C  CG1 . ILE   A 70  ? 0.1730 0.2099 0.1575 -0.0107 0.0028  -0.0106 70  ILE   A CG1 
476  C  CG2 . ILE   A 70  ? 0.1837 0.2100 0.1708 -0.0079 0.0027  -0.0110 70  ILE   A CG2 
477  C  CD1 . ILE   A 70  ? 0.1827 0.2253 0.1678 -0.0105 0.0027  -0.0123 70  ILE   A CD1 
478  N  N   . ALA   A 71  ? 0.1412 0.1557 0.1255 -0.0089 0.0028  -0.0067 71  ALA   A N   
479  C  CA  . ALA   A 71  ? 0.1433 0.1526 0.1275 -0.0082 0.0026  -0.0061 71  ALA   A CA  
480  C  C   . ALA   A 71  ? 0.1413 0.1502 0.1289 -0.0064 0.0028  -0.0075 71  ALA   A C   
481  O  O   . ALA   A 71  ? 0.1578 0.1687 0.1481 -0.0051 0.0031  -0.0086 71  ALA   A O   
482  C  CB  . ALA   A 71  ? 0.1649 0.1721 0.1491 -0.0078 0.0027  -0.0048 71  ALA   A CB  
483  N  N   . THR   A 72  ? 0.1308 0.1373 0.1182 -0.0063 0.0027  -0.0077 72  THR   A N   
484  C  CA  . THR   A 72  ? 0.1315 0.1378 0.1221 -0.0053 0.0030  -0.0093 72  THR   A CA  
485  C  C   . THR   A 72  ? 0.1414 0.1450 0.1320 -0.0052 0.0030  -0.0086 72  THR   A C   
486  O  O   . THR   A 72  ? 0.1558 0.1577 0.1441 -0.0053 0.0027  -0.0070 72  THR   A O   
487  C  CB  . THR   A 72  ? 0.1320 0.1416 0.1228 -0.0055 0.0027  -0.0113 72  THR   A CB  
488  O  OG1 . THR   A 72  ? 0.1248 0.1346 0.1191 -0.0048 0.0030  -0.0135 72  THR   A OG1 
489  C  CG2 . THR   A 72  ? 0.1448 0.1545 0.1324 -0.0060 0.0022  -0.0107 72  THR   A CG2 
490  N  N   . VAL   A 73  ? 0.1489 0.1528 0.1422 -0.0050 0.0033  -0.0102 73  VAL   A N   
491  C  CA  . VAL   A 73  ? 0.1504 0.1532 0.1443 -0.0050 0.0034  -0.0098 73  VAL   A CA  
492  C  C   . VAL   A 73  ? 0.1415 0.1471 0.1359 -0.0052 0.0032  -0.0119 73  VAL   A C   
493  O  O   . VAL   A 73  ? 0.1461 0.1538 0.1423 -0.0054 0.0033  -0.0142 73  VAL   A O   
494  C  CB  . VAL   A 73  ? 0.1688 0.1696 0.1660 -0.0053 0.0043  -0.0094 73  VAL   A CB  
495  C  CG1 . VAL   A 73  ? 0.1638 0.1629 0.1600 -0.0047 0.0045  -0.0067 73  VAL   A CG1 
496  C  CG2 . VAL   A 73  ? 0.1796 0.1798 0.1799 -0.0054 0.0048  -0.0114 73  VAL   A CG2 
497  N  N   . THR   A 74  ? 0.1307 0.1372 0.1235 -0.0047 0.0028  -0.0114 74  THR   A N   
498  C  CA  . THR   A 74  ? 0.1297 0.1401 0.1230 -0.0046 0.0026  -0.0134 74  THR   A CA  
499  C  C   . THR   A 74  ? 0.1272 0.1389 0.1214 -0.0046 0.0029  -0.0133 74  THR   A C   
500  O  O   . THR   A 74  ? 0.1292 0.1387 0.1228 -0.0044 0.0030  -0.0113 74  THR   A O   
501  C  CB  . THR   A 74  ? 0.1329 0.1450 0.1223 -0.0032 0.0018  -0.0132 74  THR   A CB  
502  O  OG1 . THR   A 74  ? 0.1494 0.1585 0.1350 -0.0019 0.0013  -0.0109 74  THR   A OG1 
503  C  CG2 . THR   A 74  ? 0.1371 0.1491 0.1255 -0.0035 0.0017  -0.0132 74  THR   A CG2 
504  N  N   . ASN   A 75  ? 0.1371 0.1536 0.1328 -0.0050 0.0029  -0.0156 75  ASN   A N   
505  C  CA  . ASN   A 75  ? 0.1360 0.1558 0.1334 -0.0057 0.0033  -0.0161 75  ASN   A CA  
506  C  C   . ASN   A 75  ? 0.1439 0.1603 0.1442 -0.0078 0.0044  -0.0150 75  ASN   A C   
507  O  O   . ASN   A 75  ? 0.1573 0.1747 0.1578 -0.0081 0.0047  -0.0137 75  ASN   A O   
508  C  CB  . ASN   A 75  ? 0.1408 0.1619 0.1344 -0.0032 0.0025  -0.0146 75  ASN   A CB  
509  C  CG  . ASN   A 75  ? 0.1536 0.1815 0.1484 -0.0031 0.0025  -0.0161 75  ASN   A CG  
510  O  OD1 . ASN   A 75  ? 0.1538 0.1868 0.1509 -0.0044 0.0028  -0.0188 75  ASN   A OD1 
511  N  ND2 . ASN   A 75  ? 0.1368 0.1657 0.1299 -0.0016 0.0022  -0.0147 75  ASN   A ND2 
512  N  N   . PHE   A 76  ? 0.1488 0.1614 0.1514 -0.0090 0.0050  -0.0155 76  PHE   A N   
513  C  CA  . PHE   A 76  ? 0.1560 0.1637 0.1600 -0.0099 0.0058  -0.0134 76  PHE   A CA  
514  C  C   . PHE   A 76  ? 0.1818 0.1874 0.1897 -0.0125 0.0070  -0.0150 76  PHE   A C   
515  O  O   . PHE   A 76  ? 0.1884 0.1946 0.1978 -0.0130 0.0069  -0.0180 76  PHE   A O   
516  C  CB  . PHE   A 76  ? 0.1575 0.1617 0.1598 -0.0083 0.0054  -0.0121 76  PHE   A CB  
517  C  CG  . PHE   A 76  ? 0.1614 0.1611 0.1648 -0.0083 0.0062  -0.0098 76  PHE   A CG  
518  C  CD1 . PHE   A 76  ? 0.1734 0.1698 0.1795 -0.0090 0.0069  -0.0108 76  PHE   A CD1 
519  C  CD2 . PHE   A 76  ? 0.1783 0.1773 0.1797 -0.0073 0.0061  -0.0069 76  PHE   A CD2 
520  C  CE1 . PHE   A 76  ? 0.1796 0.1718 0.1862 -0.0083 0.0076  -0.0083 76  PHE   A CE1 
521  C  CE2 . PHE   A 76  ? 0.1793 0.1753 0.1815 -0.0069 0.0067  -0.0047 76  PHE   A CE2 
522  C  CZ  . PHE   A 76  ? 0.1741 0.1666 0.1788 -0.0072 0.0075  -0.0052 76  PHE   A CZ  
523  N  N   . PRO   A 77  A 0.1847 0.1871 0.1941 -0.0140 0.0080  -0.0129 77  PRO   A N   
524  C  CA  . PRO   A 77  A 0.1966 0.1994 0.2045 -0.0133 0.0081  -0.0094 77  PRO   A CA  
525  C  C   . PRO   A 77  A 0.1819 0.1904 0.1898 -0.0145 0.0082  -0.0095 77  PRO   A C   
526  O  O   . PRO   A 77  A 0.1677 0.1776 0.1743 -0.0138 0.0083  -0.0070 77  PRO   A O   
527  C  CB  . PRO   A 77  A 0.2143 0.2112 0.2239 -0.0144 0.0094  -0.0072 77  PRO   A CB  
528  C  CG  . PRO   A 77  A 0.2086 0.2036 0.2214 -0.0173 0.0103  -0.0100 77  PRO   A CG  
529  C  CD  . PRO   A 77  A 0.2145 0.2123 0.2271 -0.0164 0.0093  -0.0138 77  PRO   A CD  
530  N  N   . HIS   A 78  ? 0.1657 0.1789 0.1748 -0.0158 0.0081  -0.0128 78  HIS   A N   
531  C  CA  . HIS   A 78  ? 0.1714 0.1913 0.1815 -0.0177 0.0085  -0.0135 78  HIS   A CA  
532  C  C   . HIS   A 78  ? 0.1601 0.1855 0.1672 -0.0148 0.0074  -0.0126 78  HIS   A C   
533  O  O   . HIS   A 78  ? 0.1726 0.2029 0.1800 -0.0157 0.0078  -0.0120 78  HIS   A O   
534  C  CB  . HIS   A 78  ? 0.1755 0.1998 0.1879 -0.0198 0.0086  -0.0178 78  HIS   A CB  
535  C  CG  . HIS   A 78  ? 0.1787 0.2040 0.1896 -0.0173 0.0075  -0.0200 78  HIS   A CG  
536  N  ND1 . HIS   A 78  ? 0.1796 0.2097 0.1873 -0.0139 0.0061  -0.0201 78  HIS   A ND1 
537  C  CD2 . HIS   A 78  ? 0.1913 0.2135 0.2034 -0.0176 0.0074  -0.0221 78  HIS   A CD2 
538  C  CE1 . HIS   A 78  ? 0.1853 0.2151 0.1921 -0.0125 0.0055  -0.0217 78  HIS   A CE1 
539  N  NE2 . HIS   A 78  ? 0.1928 0.2186 0.2024 -0.0147 0.0062  -0.0232 78  HIS   A NE2 
540  N  N   . GLY   A 79  ? 0.1509 0.1754 0.1546 -0.0113 0.0061  -0.0127 79  GLY   A N   
541  C  CA  . GLY   A 79  ? 0.1490 0.1777 0.1493 -0.0082 0.0050  -0.0123 79  GLY   A CA  
542  C  C   . GLY   A 79  ? 0.1715 0.2091 0.1725 -0.0082 0.0048  -0.0148 79  GLY   A C   
543  O  O   . GLY   A 79  ? 0.1597 0.2027 0.1594 -0.0066 0.0044  -0.0145 79  GLY   A O   
544  N  N   . ASN   A 80  ? 0.1630 0.2031 0.1659 -0.0096 0.0050  -0.0176 80  ASN   A N   
545  C  CA  . ASN   A 80  ? 0.1713 0.2210 0.1745 -0.0093 0.0046  -0.0204 80  ASN   A CA  
546  C  C   . ASN   A 80  ? 0.1741 0.2265 0.1725 -0.0040 0.0031  -0.0200 80  ASN   A C   
547  O  O   . ASN   A 80  ? 0.1621 0.2080 0.1572 -0.0013 0.0023  -0.0181 80  ASN   A O   
548  C  CB  . ASN   A 80  ? 0.1738 0.2257 0.1796 -0.0115 0.0049  -0.0237 80  ASN   A CB  
549  C  CG  . ASN   A 80  ? 0.1898 0.2398 0.2002 -0.0168 0.0065  -0.0249 80  ASN   A CG  
550  O  OD1 . ASN   A 80  ? 0.2324 0.2814 0.2443 -0.0193 0.0075  -0.0232 80  ASN   A OD1 
551  N  ND2 . ASN   A 80  ? 0.2101 0.2595 0.2228 -0.0187 0.0068  -0.0280 80  ASN   A ND2 
552  N  N   . ASP   A 81  ? 0.1831 0.2454 0.1812 -0.0026 0.0026  -0.0221 81  ASP   A N   
553  C  CA  . ASP   A 81  ? 0.1942 0.2590 0.1875 0.0031  0.0012  -0.0216 81  ASP   A CA  
554  C  C   . ASP   A 81  ? 0.2028 0.2723 0.1946 0.0055  0.0004  -0.0236 81  ASP   A C   
555  O  O   . ASP   A 81  ? 0.2003 0.2750 0.1886 0.0102  -0.0007 -0.0239 81  ASP   A O   
556  C  CB  . ASP   A 81  ? 0.2111 0.2841 0.2040 0.0045  0.0010  -0.0220 81  ASP   A CB  
557  C  CG  . ASP   A 81  ? 0.2359 0.3212 0.2326 0.0017  0.0017  -0.0250 81  ASP   A CG  
558  O  OD1 . ASP   A 81  ? 0.2691 0.3558 0.2689 -0.0018 0.0024  -0.0271 81  ASP   A OD1 
559  O  OD2 . ASP   A 81  ? 0.3033 0.3972 0.3000 0.0025  0.0017  -0.0256 81  ASP   A OD2 
560  N  N   . ASP   A 82  ? 0.1842 0.2514 0.1781 0.0029  0.0008  -0.0248 82  ASP   A N   
561  C  CA  . ASP   A 82  ? 0.1835 0.2548 0.1756 0.0053  0.0001  -0.0262 82  ASP   A CA  
562  C  C   . ASP   A 82  ? 0.1723 0.2343 0.1599 0.0082  -0.0007 -0.0234 82  ASP   A C   
563  O  O   . ASP   A 82  ? 0.1677 0.2227 0.1565 0.0057  -0.0002 -0.0226 82  ASP   A O   
564  C  CB  . ASP   A 82  ? 0.1942 0.2702 0.1910 0.0011  0.0009  -0.0297 82  ASP   A CB  
565  C  CG  . ASP   A 82  ? 0.2207 0.3035 0.2161 0.0035  0.0002  -0.0317 82  ASP   A CG  
566  O  OD1 . ASP   A 82  ? 0.2125 0.2912 0.2034 0.0074  -0.0007 -0.0293 82  ASP   A OD1 
567  O  OD2 . ASP   A 82  ? 0.2398 0.3320 0.2387 0.0012  0.0006  -0.0356 82  ASP   A OD2 
568  N  N   . ILE   A 83  ? 0.1698 0.2317 0.1522 0.0133  -0.0019 -0.0218 83  ILE   A N   
569  C  CA  . ILE   A 83  ? 0.1801 0.2324 0.1576 0.0157  -0.0025 -0.0187 83  ILE   A CA  
570  C  C   . ILE   A 83  ? 0.1863 0.2385 0.1637 0.0149  -0.0025 -0.0190 83  ILE   A C   
571  O  O   . ILE   A 83  ? 0.1881 0.2323 0.1643 0.0136  -0.0023 -0.0171 83  ILE   A O   
572  C  CB  . ILE   A 83  ? 0.1997 0.2514 0.1712 0.0216  -0.0037 -0.0171 83  ILE   A CB  
573  C  CG1 . ILE   A 83  ? 0.2275 0.2789 0.1987 0.0228  -0.0039 -0.0169 83  ILE   A CG1 
574  C  CG2 . ILE   A 83  ? 0.2010 0.2424 0.1671 0.0235  -0.0043 -0.0140 83  ILE   A CG2 
575  C  CD1 . ILE   A 83  ? 0.2505 0.3029 0.2161 0.0293  -0.0052 -0.0163 83  ILE   A CD1 
576  N  N   . GLU   A 84  ? 0.2021 0.2642 0.1806 0.0157  -0.0026 -0.0215 84  GLU   A N   
577  C  CA  . GLU   A 84  ? 0.2112 0.2750 0.1896 0.0152  -0.0026 -0.0220 84  GLU   A CA  
578  C  C   . GLU   A 84  ? 0.1749 0.2351 0.1579 0.0102  -0.0016 -0.0233 84  GLU   A C   
579  O  O   . GLU   A 84  ? 0.1827 0.2389 0.1644 0.0098  -0.0016 -0.0221 84  GLU   A O   
580  C  CB  . GLU   A 84  ? 0.2467 0.3233 0.2258 0.0171  -0.0030 -0.0249 84  GLU   A CB  
581  C  CG  . GLU   A 84  ? 0.3136 0.3928 0.2867 0.0234  -0.0041 -0.0228 84  GLU   A CG  
582  C  CD  . GLU   A 84  ? 0.4417 0.5115 0.4084 0.0265  -0.0047 -0.0184 84  GLU   A CD  
583  O  OE1 . GLU   A 84  ? 0.5126 0.5808 0.4791 0.0249  -0.0045 -0.0178 84  GLU   A OE1 
584  O  OE2 . GLU   A 84  ? 0.5747 0.6383 0.5362 0.0305  -0.0054 -0.0156 84  GLU   A OE2 
585  N  N   . ILE   A 85  ? 0.1627 0.2241 0.1508 0.0066  -0.0008 -0.0255 85  ILE   A N   
586  C  CA  . ILE   A 85  ? 0.1672 0.2240 0.1592 0.0025  0.0001  -0.0265 85  ILE   A CA  
587  C  C   . ILE   A 85  ? 0.1620 0.2080 0.1519 0.0024  0.0002  -0.0230 85  ILE   A C   
588  O  O   . ILE   A 85  ? 0.1653 0.2077 0.1556 0.0013  0.0004  -0.0227 85  ILE   A O   
589  C  CB  . ILE   A 85  ? 0.1780 0.2377 0.1755 -0.0014 0.0011  -0.0295 85  ILE   A CB  
590  C  CG1 . ILE   A 85  ? 0.1934 0.2645 0.1934 -0.0022 0.0012  -0.0339 85  ILE   A CG1 
591  C  CG2 . ILE   A 85  ? 0.1870 0.2394 0.1879 -0.0049 0.0021  -0.0297 85  ILE   A CG2 
592  C  CD1 . ILE   A 85  ? 0.2120 0.2855 0.2175 -0.0070 0.0024  -0.0373 85  ILE   A CD1 
593  N  N   . ALA   A 86  ? 0.1600 0.2019 0.1480 0.0035  0.0000  -0.0206 86  ALA   A N   
594  C  CA  . ALA   A 86  ? 0.1602 0.1930 0.1463 0.0032  0.0001  -0.0176 86  ALA   A CA  
595  C  C   . ALA   A 86  ? 0.1541 0.1833 0.1357 0.0049  -0.0006 -0.0156 86  ALA   A C   
596  O  O   . ALA   A 86  ? 0.1467 0.1710 0.1282 0.0034  -0.0003 -0.0145 86  ALA   A O   
597  C  CB  . ALA   A 86  ? 0.1642 0.1946 0.1487 0.0044  -0.0001 -0.0159 86  ALA   A CB  
598  N  N   . LEU   A 87  ? 0.1663 0.1985 0.1440 0.0082  -0.0014 -0.0151 87  LEU   A N   
599  C  CA  . LEU   A 87  ? 0.1643 0.1929 0.1372 0.0097  -0.0019 -0.0127 87  LEU   A CA  
600  C  C   . LEU   A 87  ? 0.1618 0.1937 0.1367 0.0077  -0.0015 -0.0139 87  LEU   A C   
601  O  O   . LEU   A 87  ? 0.1629 0.1904 0.1358 0.0067  -0.0014 -0.0121 87  LEU   A O   
602  C  CB  . LEU   A 87  ? 0.1792 0.2107 0.1475 0.0141  -0.0027 -0.0119 87  LEU   A CB  
603  C  CG  . LEU   A 87  ? 0.1893 0.2166 0.1517 0.0160  -0.0032 -0.0088 87  LEU   A CG  
604  C  CD1 . LEU   A 87  ? 0.1957 0.2121 0.1547 0.0147  -0.0031 -0.0058 87  LEU   A CD1 
605  C  CD2 . LEU   A 87  ? 0.1999 0.2304 0.1579 0.0213  -0.0041 -0.0080 87  LEU   A CD2 
606  N  N   . ALA   A 88  ? 0.1530 0.1933 0.1317 0.0071  -0.0013 -0.0174 88  ALA   A N   
607  C  CA  . ALA   A 88  ? 0.1589 0.2033 0.1399 0.0055  -0.0010 -0.0193 88  ALA   A CA  
608  C  C   . ALA   A 88  ? 0.1462 0.1853 0.1299 0.0025  -0.0003 -0.0194 88  ALA   A C   
609  O  O   . ALA   A 88  ? 0.1385 0.1770 0.1213 0.0018  -0.0003 -0.0187 88  ALA   A O   
610  C  CB  . ALA   A 88  ? 0.1566 0.2104 0.1418 0.0050  -0.0008 -0.0237 88  ALA   A CB  
611  N  N   . GLU   A 89  ? 0.1503 0.1858 0.1371 0.0009  0.0002  -0.0200 89  GLU   A N   
612  C  CA  . GLU   A 89  ? 0.1386 0.1692 0.1279 -0.0012 0.0008  -0.0198 89  GLU   A CA  
613  C  C   . GLU   A 89  ? 0.1405 0.1652 0.1258 -0.0010 0.0005  -0.0163 89  GLU   A C   
614  O  O   . GLU   A 89  ? 0.1404 0.1640 0.1262 -0.0021 0.0008  -0.0162 89  GLU   A O   
615  C  CB  . GLU   A 89  ? 0.1453 0.1733 0.1381 -0.0027 0.0014  -0.0205 89  GLU   A CB  
616  C  CG  . GLU   A 89  ? 0.1598 0.1929 0.1570 -0.0042 0.0019  -0.0244 89  GLU   A CG  
617  C  CD  . GLU   A 89  ? 0.1887 0.2186 0.1893 -0.0063 0.0028  -0.0246 89  GLU   A CD  
618  O  OE1 . GLU   A 89  ? 0.2230 0.2481 0.2220 -0.0059 0.0028  -0.0215 89  GLU   A OE1 
619  O  OE2 . GLU   A 89  ? 0.1970 0.2290 0.2015 -0.0085 0.0034  -0.0278 89  GLU   A OE2 
620  N  N   . THR   A 90  ? 0.1364 0.1576 0.1176 0.0005  0.0001  -0.0137 90  THR   A N   
621  C  CA  . THR   A 90  ? 0.1427 0.1578 0.1199 0.0003  -0.0001 -0.0107 90  THR   A CA  
622  C  C   . THR   A 90  ? 0.1378 0.1543 0.1119 0.0001  -0.0003 -0.0096 90  THR   A C   
623  O  O   . THR   A 90  ? 0.1455 0.1598 0.1187 -0.0017 0.0000  -0.0084 90  THR   A O   
624  C  CB  . THR   A 90  ? 0.1543 0.1652 0.1279 0.0022  -0.0006 -0.0088 90  THR   A CB  
625  O  OG1 . THR   A 90  ? 0.1698 0.1804 0.1466 0.0018  -0.0003 -0.0096 90  THR   A OG1 
626  C  CG2 . THR   A 90  ? 0.1571 0.1610 0.1262 0.0017  -0.0008 -0.0060 90  THR   A CG2 
627  N  N   . ARG   A 91  ? 0.1486 0.1698 0.1212 0.0020  -0.0007 -0.0099 91  ARG   A N   
628  C  CA  . ARG   A 91  ? 0.1533 0.1769 0.1228 0.0019  -0.0008 -0.0087 91  ARG   A CA  
629  C  C   . ARG   A 91  ? 0.1463 0.1747 0.1197 -0.0002 -0.0003 -0.0109 91  ARG   A C   
630  O  O   . ARG   A 91  ? 0.1395 0.1679 0.1110 -0.0016 -0.0001 -0.0094 91  ARG   A O   
631  C  CB  . ARG   A 91  ? 0.1645 0.1937 0.1320 0.0048  -0.0013 -0.0088 91  ARG   A CB  
632  C  CG  . ARG   A 91  ? 0.1883 0.2123 0.1504 0.0077  -0.0019 -0.0059 91  ARG   A CG  
633  C  CD  . ARG   A 91  ? 0.2247 0.2554 0.1848 0.0113  -0.0024 -0.0062 91  ARG   A CD  
634  N  NE  . ARG   A 91  ? 0.2720 0.2969 0.2260 0.0147  -0.0030 -0.0030 91  ARG   A NE  
635  C  CZ  . ARG   A 91  ? 0.3494 0.3789 0.3010 0.0190  -0.0036 -0.0029 91  ARG   A CZ  
636  N  NH1 . ARG   A 91  ? 0.3864 0.4271 0.3419 0.0199  -0.0037 -0.0064 91  ARG   A NH1 
637  N  NH2 . ARG   A 91  ? 0.4045 0.4273 0.3498 0.0226  -0.0042 0.0003  91  ARG   A NH2 
638  N  N   . ALA   A 92  ? 0.1451 0.1773 0.1239 -0.0005 0.0000  -0.0145 92  ALA   A N   
639  C  CA  . ALA   A 92  ? 0.1442 0.1803 0.1267 -0.0019 0.0003  -0.0172 92  ALA   A CA  
640  C  C   . ALA   A 92  ? 0.1409 0.1720 0.1236 -0.0035 0.0007  -0.0158 92  ALA   A C   
641  O  O   . ALA   A 92  ? 0.1326 0.1664 0.1152 -0.0044 0.0008  -0.0159 92  ALA   A O   
642  C  CB  . ALA   A 92  ? 0.1445 0.1838 0.1323 -0.0020 0.0006  -0.0214 92  ALA   A CB  
643  N  N   . ALA   A 93  ? 0.1301 0.1551 0.1131 -0.0038 0.0008  -0.0146 93  ALA   A N   
644  C  CA  . ALA   A 93  ? 0.1388 0.1599 0.1217 -0.0051 0.0011  -0.0131 93  ALA   A CA  
645  C  C   . ALA   A 93  ? 0.1497 0.1702 0.1281 -0.0063 0.0010  -0.0105 93  ALA   A C   
646  O  O   . ALA   A 93  ? 0.1571 0.1794 0.1359 -0.0076 0.0013  -0.0105 93  ALA   A O   
647  C  CB  . ALA   A 93  ? 0.1428 0.1581 0.1258 -0.0049 0.0012  -0.0118 93  ALA   A CB  
648  N  N   . ILE   A 94  ? 0.1478 0.1657 0.1217 -0.0058 0.0007  -0.0082 94  ILE   A N   
649  C  CA  . ILE   A 94  ? 0.1620 0.1782 0.1311 -0.0074 0.0007  -0.0053 94  ILE   A CA  
650  C  C   . ILE   A 94  ? 0.1665 0.1901 0.1359 -0.0083 0.0009  -0.0060 94  ILE   A C   
651  O  O   . ILE   A 94  ? 0.1679 0.1928 0.1361 -0.0107 0.0012  -0.0050 94  ILE   A O   
652  C  CB  . ILE   A 94  ? 0.1662 0.1774 0.1301 -0.0060 0.0002  -0.0027 94  ILE   A CB  
653  C  CG1 . ILE   A 94  ? 0.1644 0.1683 0.1274 -0.0053 0.0000  -0.0021 94  ILE   A CG1 
654  C  CG2 . ILE   A 94  ? 0.1814 0.1905 0.1400 -0.0079 0.0004  0.0004  94  ILE   A CG2 
655  C  CD1 . ILE   A 94  ? 0.1764 0.1765 0.1354 -0.0025 -0.0006 -0.0006 94  ILE   A CD1 
656  N  N   . ALA   A 95  ? 0.1538 0.1833 0.1250 -0.0065 0.0006  -0.0080 95  ALA   A N   
657  C  CA  . ALA   A 95  ? 0.1490 0.1867 0.1205 -0.0068 0.0007  -0.0090 95  ALA   A CA  
658  C  C   . ALA   A 95  ? 0.1466 0.1886 0.1221 -0.0078 0.0010  -0.0117 95  ALA   A C   
659  O  O   . ALA   A 95  ? 0.1495 0.1975 0.1243 -0.0089 0.0012  -0.0117 95  ALA   A O   
660  C  CB  . ALA   A 95  ? 0.1496 0.1933 0.1225 -0.0045 0.0004  -0.0113 95  ALA   A CB  
661  N  N   . TYR   A 96  ? 0.1525 0.1922 0.1322 -0.0071 0.0011  -0.0140 96  TYR   A N   
662  C  CA  . TYR   A 96  ? 0.1464 0.1890 0.1295 -0.0073 0.0014  -0.0164 96  TYR   A CA  
663  C  C   . TYR   A 96  ? 0.1720 0.2138 0.1529 -0.0094 0.0016  -0.0139 96  TYR   A C   
664  O  O   . TYR   A 96  ? 0.1721 0.2191 0.1547 -0.0095 0.0018  -0.0155 96  TYR   A O   
665  C  CB  . TYR   A 96  ? 0.1397 0.1783 0.1270 -0.0061 0.0015  -0.0185 96  TYR   A CB  
666  C  CG  . TYR   A 96  ? 0.1324 0.1733 0.1237 -0.0046 0.0015  -0.0225 96  TYR   A CG  
667  C  CD1 . TYR   A 96  ? 0.1297 0.1770 0.1236 -0.0038 0.0014  -0.0261 96  TYR   A CD1 
668  C  CD2 . TYR   A 96  ? 0.1373 0.1741 0.1301 -0.0043 0.0015  -0.0230 96  TYR   A CD2 
669  C  CE1 . TYR   A 96  ? 0.1245 0.1730 0.1221 -0.0028 0.0014  -0.0302 96  TYR   A CE1 
670  C  CE2 . TYR   A 96  ? 0.1313 0.1699 0.1280 -0.0038 0.0016  -0.0270 96  TYR   A CE2 
671  C  CZ  . TYR   A 96  ? 0.1350 0.1792 0.1340 -0.0031 0.0016  -0.0307 96  TYR   A CZ  
672  O  OH  . TYR   A 96  ? 0.1464 0.1920 0.1492 -0.0029 0.0017  -0.0351 96  TYR   A OH  
673  N  N   . GLY   A 97  ? 0.1649 0.2002 0.1421 -0.0108 0.0017  -0.0106 97  GLY   A N   
674  C  CA  . GLY   A 97  ? 0.1715 0.2059 0.1461 -0.0135 0.0019  -0.0084 97  GLY   A CA  
675  C  C   . GLY   A 97  ? 0.1792 0.2070 0.1541 -0.0138 0.0020  -0.0075 97  GLY   A C   
676  O  O   . GLY   A 97  ? 0.1673 0.1958 0.1413 -0.0158 0.0023  -0.0068 97  GLY   A O   
677  N  N   . ALA   A 98  ? 0.1621 0.1845 0.1381 -0.0120 0.0018  -0.0077 98  ALA   A N   
678  C  CA  . ALA   A 98  ? 0.1517 0.1689 0.1280 -0.0121 0.0019  -0.0069 98  ALA   A CA  
679  C  C   . ALA   A 98  ? 0.1497 0.1628 0.1213 -0.0147 0.0019  -0.0044 98  ALA   A C   
680  O  O   . ALA   A 98  ? 0.1640 0.1744 0.1316 -0.0157 0.0018  -0.0027 98  ALA   A O   
681  C  CB  . ALA   A 98  ? 0.1511 0.1640 0.1286 -0.0100 0.0017  -0.0072 98  ALA   A CB  
682  N  N   . ASP   A 99  ? 0.1537 0.1659 0.1257 -0.0158 0.0021  -0.0042 99  ASP   A N   
683  C  CA  . ASP   A 99  ? 0.1592 0.1664 0.1272 -0.0182 0.0021  -0.0026 99  ASP   A CA  
684  C  C   . ASP   A 99  ? 0.1643 0.1648 0.1317 -0.0164 0.0017  -0.0022 99  ASP   A C   
685  O  O   . ASP   A 99  ? 0.1592 0.1538 0.1226 -0.0175 0.0015  -0.0010 99  ASP   A O   
686  C  CB  . ASP   A 99  ? 0.1733 0.1843 0.1421 -0.0203 0.0024  -0.0030 99  ASP   A CB  
687  C  CG  . ASP   A 99  ? 0.1829 0.2018 0.1520 -0.0223 0.0028  -0.0035 99  ASP   A CG  
688  O  OD1 . ASP   A 99  ? 0.1886 0.2075 0.1548 -0.0243 0.0029  -0.0024 99  ASP   A OD1 
689  O  OD2 . ASP   A 99  ? 0.1912 0.2165 0.1635 -0.0212 0.0029  -0.0049 99  ASP   A OD2 
690  N  N   . GLU   A 100 ? 0.1504 0.1521 0.1218 -0.0137 0.0017  -0.0033 100 GLU   A N   
691  C  CA  . GLU   A 100 ? 0.1609 0.1582 0.1323 -0.0119 0.0014  -0.0031 100 GLU   A CA  
692  C  C   . GLU   A 100 ? 0.1507 0.1496 0.1257 -0.0094 0.0014  -0.0042 100 GLU   A C   
693  O  O   . GLU   A 100 ? 0.1518 0.1546 0.1303 -0.0089 0.0018  -0.0054 100 GLU   A O   
694  C  CB  . GLU   A 100 ? 0.1734 0.1713 0.1463 -0.0122 0.0016  -0.0032 100 GLU   A CB  
695  C  CG  . GLU   A 100 ? 0.1892 0.1877 0.1595 -0.0152 0.0017  -0.0028 100 GLU   A CG  
696  C  CD  . GLU   A 100 ? 0.2138 0.2140 0.1852 -0.0154 0.0019  -0.0031 100 GLU   A CD  
697  O  OE1 . GLU   A 100 ? 0.1953 0.1973 0.1699 -0.0130 0.0020  -0.0032 100 GLU   A OE1 
698  O  OE2 . GLU   A 100 ? 0.2231 0.2233 0.1920 -0.0183 0.0019  -0.0032 100 GLU   A OE2 
699  N  N   . VAL   A 101 ? 0.1552 0.1510 0.1291 -0.0078 0.0011  -0.0040 101 VAL   A N   
700  C  CA  . VAL   A 101 ? 0.1468 0.1445 0.1239 -0.0060 0.0012  -0.0051 101 VAL   A CA  
701  C  C   . VAL   A 101 ? 0.1481 0.1440 0.1259 -0.0050 0.0012  -0.0047 101 VAL   A C   
702  O  O   . VAL   A 101 ? 0.1558 0.1485 0.1302 -0.0045 0.0007  -0.0039 101 VAL   A O   
703  C  CB  . VAL   A 101 ? 0.1633 0.1615 0.1385 -0.0049 0.0007  -0.0054 101 VAL   A CB  
704  C  CG1 . VAL   A 101 ? 0.1721 0.1729 0.1504 -0.0033 0.0008  -0.0068 101 VAL   A CG1 
705  C  CG2 . VAL   A 101 ? 0.1657 0.1670 0.1406 -0.0058 0.0008  -0.0057 101 VAL   A CG2 
706  N  N   . ASP   A 102 ? 0.1455 0.1434 0.1274 -0.0047 0.0017  -0.0052 102 ASP   A N   
707  C  CA  . ASP   A 102 ? 0.1500 0.1475 0.1329 -0.0039 0.0019  -0.0047 102 ASP   A CA  
708  C  C   . ASP   A 102 ? 0.1481 0.1476 0.1329 -0.0032 0.0020  -0.0058 102 ASP   A C   
709  O  O   . ASP   A 102 ? 0.1500 0.1512 0.1384 -0.0038 0.0026  -0.0068 102 ASP   A O   
710  C  CB  . ASP   A 102 ? 0.1590 0.1573 0.1447 -0.0043 0.0025  -0.0039 102 ASP   A CB  
711  C  CG  . ASP   A 102 ? 0.1839 0.1822 0.1682 -0.0050 0.0025  -0.0031 102 ASP   A CG  
712  O  OD1 . ASP   A 102 ? 0.1815 0.1788 0.1627 -0.0059 0.0021  -0.0033 102 ASP   A OD1 
713  O  OD2 . ASP   A 102 ? 0.2200 0.2195 0.2064 -0.0046 0.0030  -0.0024 102 ASP   A OD2 
714  N  N   . VAL   A 103 ? 0.1425 0.1421 0.1250 -0.0019 0.0014  -0.0058 103 VAL   A N   
715  C  CA  . VAL   A 103 ? 0.1454 0.1485 0.1294 -0.0011 0.0014  -0.0071 103 VAL   A CA  
716  C  C   . VAL   A 103 ? 0.1430 0.1479 0.1289 -0.0011 0.0018  -0.0067 103 VAL   A C   
717  O  O   . VAL   A 103 ? 0.1394 0.1429 0.1234 -0.0002 0.0015  -0.0056 103 VAL   A O   
718  C  CB  . VAL   A 103 ? 0.1488 0.1522 0.1290 0.0009  0.0005  -0.0075 103 VAL   A CB  
719  C  CG1 . VAL   A 103 ? 0.1568 0.1571 0.1329 0.0029  -0.0002 -0.0064 103 VAL   A CG1 
720  C  CG2 . VAL   A 103 ? 0.1611 0.1700 0.1431 0.0016  0.0005  -0.0092 103 VAL   A CG2 
721  N  N   . VAL   A 104 ? 0.1435 0.1519 0.1328 -0.0021 0.0024  -0.0078 104 VAL   A N   
722  C  CA  . VAL   A 104 ? 0.1397 0.1508 0.1306 -0.0024 0.0029  -0.0072 104 VAL   A CA  
723  C  C   . VAL   A 104 ? 0.1412 0.1566 0.1300 -0.0003 0.0022  -0.0081 104 VAL   A C   
724  O  O   . VAL   A 104 ? 0.1402 0.1589 0.1289 0.0003  0.0019  -0.0099 104 VAL   A O   
725  C  CB  . VAL   A 104 ? 0.1388 0.1514 0.1343 -0.0050 0.0041  -0.0077 104 VAL   A CB  
726  C  CG1 . VAL   A 104 ? 0.1345 0.1497 0.1312 -0.0058 0.0048  -0.0063 104 VAL   A CG1 
727  C  CG2 . VAL   A 104 ? 0.1416 0.1497 0.1388 -0.0062 0.0048  -0.0070 104 VAL   A CG2 
728  N  N   . PHE   A 105 ? 0.1419 0.1576 0.1287 0.0013  0.0018  -0.0071 105 PHE   A N   
729  C  CA  . PHE   A 105 ? 0.1473 0.1674 0.1320 0.0039  0.0010  -0.0080 105 PHE   A CA  
730  C  C   . PHE   A 105 ? 0.1392 0.1668 0.1274 0.0024  0.0018  -0.0091 105 PHE   A C   
731  O  O   . PHE   A 105 ? 0.1386 0.1669 0.1305 -0.0007 0.0030  -0.0084 105 PHE   A O   
732  C  CB  . PHE   A 105 ? 0.1494 0.1687 0.1323 0.0053  0.0008  -0.0069 105 PHE   A CB  
733  C  CG  . PHE   A 105 ? 0.1579 0.1811 0.1379 0.0089  -0.0002 -0.0080 105 PHE   A CG  
734  C  CD1 . PHE   A 105 ? 0.1735 0.1922 0.1487 0.0123  -0.0015 -0.0084 105 PHE   A CD1 
735  C  CD2 . PHE   A 105 ? 0.1772 0.2085 0.1592 0.0090  0.0001  -0.0084 105 PHE   A CD2 
736  C  CE1 . PHE   A 105 ? 0.1822 0.2038 0.1543 0.0163  -0.0025 -0.0096 105 PHE   A CE1 
737  C  CE2 . PHE   A 105 ? 0.1813 0.2171 0.1605 0.0129  -0.0009 -0.0097 105 PHE   A CE2 
738  C  CZ  . PHE   A 105 ? 0.1783 0.2090 0.1526 0.0169  -0.0022 -0.0104 105 PHE   A CZ  
739  N  N   . PRO   A 106 ? 0.1550 0.1885 0.1420 0.0046  0.0011  -0.0109 106 PRO   A N   
740  C  CA  . PRO   A 106 ? 0.1515 0.1938 0.1418 0.0028  0.0018  -0.0123 106 PRO   A CA  
741  C  C   . PRO   A 106 ? 0.1587 0.2055 0.1495 0.0029  0.0021  -0.0114 106 PRO   A C   
742  O  O   . PRO   A 106 ? 0.1715 0.2247 0.1605 0.0059  0.0014  -0.0124 106 PRO   A O   
743  C  CB  . PRO   A 106 ? 0.1512 0.1991 0.1394 0.0059  0.0008  -0.0145 106 PRO   A CB  
744  C  CG  . PRO   A 106 ? 0.1599 0.2019 0.1426 0.0105  -0.0006 -0.0136 106 PRO   A CG  
745  C  CD  . PRO   A 106 ? 0.1518 0.1842 0.1342 0.0087  -0.0003 -0.0116 106 PRO   A CD  
746  N  N   . TYR   A 107 ? 0.1454 0.1892 0.1386 -0.0002 0.0032  -0.0093 107 TYR   A N   
747  C  CA  . TYR   A 107 ? 0.1548 0.2024 0.1482 -0.0002 0.0036  -0.0078 107 TYR   A CA  
748  C  C   . TYR   A 107 ? 0.1557 0.2135 0.1518 -0.0023 0.0044  -0.0087 107 TYR   A C   
749  O  O   . TYR   A 107 ? 0.1607 0.2255 0.1559 -0.0007 0.0042  -0.0086 107 TYR   A O   
750  C  CB  . TYR   A 107 ? 0.1541 0.1957 0.1489 -0.0024 0.0046  -0.0050 107 TYR   A CB  
751  C  CG  . TYR   A 107 ? 0.1601 0.1987 0.1587 -0.0068 0.0061  -0.0041 107 TYR   A CG  
752  C  CD1 . TYR   A 107 ? 0.1681 0.2109 0.1697 -0.0103 0.0075  -0.0030 107 TYR   A CD1 
753  C  CD2 . TYR   A 107 ? 0.1604 0.1916 0.1593 -0.0074 0.0061  -0.0043 107 TYR   A CD2 
754  C  CE1 . TYR   A 107 ? 0.1808 0.2193 0.1855 -0.0142 0.0089  -0.0022 107 TYR   A CE1 
755  C  CE2 . TYR   A 107 ? 0.1701 0.1979 0.1723 -0.0108 0.0074  -0.0038 107 TYR   A CE2 
756  C  CZ  . TYR   A 107 ? 0.1821 0.2128 0.1871 -0.0143 0.0088  -0.0027 107 TYR   A CZ  
757  O  OH  . TYR   A 107 ? 0.1755 0.2014 0.1834 -0.0177 0.0102  -0.0022 107 TYR   A OH  
758  N  N   . ARG   A 108 ? 0.1632 0.2228 0.1625 -0.0061 0.0054  -0.0099 108 ARG   A N   
759  C  CA  . ARG   A 108 ? 0.1717 0.2415 0.1736 -0.0089 0.0063  -0.0111 108 ARG   A CA  
760  C  C   . ARG   A 108 ? 0.1761 0.2554 0.1757 -0.0048 0.0049  -0.0137 108 ARG   A C   
761  O  O   . ARG   A 108 ? 0.1797 0.2692 0.1799 -0.0050 0.0052  -0.0142 108 ARG   A O   
762  C  CB  . ARG   A 108 ? 0.1731 0.2419 0.1790 -0.0142 0.0076  -0.0123 108 ARG   A CB  
763  C  CG  . ARG   A 108 ? 0.2065 0.2678 0.2149 -0.0185 0.0092  -0.0095 108 ARG   A CG  
764  C  CD  . ARG   A 108 ? 0.2399 0.3005 0.2521 -0.0240 0.0107  -0.0112 108 ARG   A CD  
765  N  NE  . ARG   A 108 ? 0.2842 0.3425 0.2964 -0.0230 0.0099  -0.0144 108 ARG   A NE  
766  C  CZ  . ARG   A 108 ? 0.3044 0.3533 0.3159 -0.0216 0.0095  -0.0139 108 ARG   A CZ  
767  N  NH1 . ARG   A 108 ? 0.3658 0.4063 0.3772 -0.0219 0.0101  -0.0106 108 ARG   A NH1 
768  N  NH2 . ARG   A 108 ? 0.2706 0.3193 0.2816 -0.0200 0.0086  -0.0167 108 ARG   A NH2 
769  N  N   . ALA   A 109 ? 0.1674 0.2438 0.1642 -0.0008 0.0035  -0.0152 109 ALA   A N   
770  C  CA  . ALA   A 109 ? 0.1723 0.2566 0.1661 0.0041  0.0022  -0.0174 109 ALA   A CA  
771  C  C   . ALA   A 109 ? 0.1743 0.2597 0.1648 0.0085  0.0012  -0.0165 109 ALA   A C   
772  O  O   . ALA   A 109 ? 0.1678 0.2635 0.1574 0.0111  0.0007  -0.0180 109 ALA   A O   
773  C  CB  . ALA   A 109 ? 0.1679 0.2474 0.1588 0.0075  0.0010  -0.0185 109 ALA   A CB  
774  N  N   . LEU   A 110 ? 0.1676 0.2432 0.1564 0.0092  0.0010  -0.0143 110 LEU   A N   
775  C  CA  . LEU   A 110 ? 0.1705 0.2471 0.1564 0.0130  0.0002  -0.0138 110 LEU   A CA  
776  C  C   . LEU   A 110 ? 0.1640 0.2510 0.1527 0.0106  0.0012  -0.0133 110 LEU   A C   
777  O  O   . LEU   A 110 ? 0.1668 0.2616 0.1537 0.0143  0.0004  -0.0144 110 LEU   A O   
778  C  CB  . LEU   A 110 ? 0.1708 0.2360 0.1549 0.0133  0.0000  -0.0119 110 LEU   A CB  
779  C  CG  . LEU   A 110 ? 0.1824 0.2485 0.1638 0.0167  -0.0008 -0.0118 110 LEU   A CG  
780  C  CD1 . LEU   A 110 ? 0.1963 0.2630 0.1728 0.0231  -0.0026 -0.0141 110 LEU   A CD1 
781  C  CD2 . LEU   A 110 ? 0.1994 0.2554 0.1799 0.0157  -0.0007 -0.0100 110 LEU   A CD2 
782  N  N   . MET   A 111 ? 0.1627 0.2496 0.1557 0.0046  0.0030  -0.0115 111 MET   A N   
783  C  CA  . MET   A 111 ? 0.1857 0.2817 0.1812 0.0015  0.0042  -0.0103 111 MET   A CA  
784  C  C   . MET   A 111 ? 0.1872 0.2971 0.1838 0.0014  0.0043  -0.0129 111 MET   A C   
785  O  O   . MET   A 111 ? 0.1926 0.3131 0.1901 0.0007  0.0047  -0.0127 111 MET   A O   
786  C  CB  . MET   A 111 ? 0.2044 0.2953 0.2036 -0.0048 0.0062  -0.0074 111 MET   A CB  
787  C  CG  . MET   A 111 ? 0.2672 0.3476 0.2652 -0.0040 0.0062  -0.0046 111 MET   A CG  
788  S  SD  . MET   A 111 ? 0.3556 0.4272 0.3572 -0.0100 0.0082  -0.0015 111 MET   A SD  
789  C  CE  . MET   A 111 ? 0.3570 0.4381 0.3601 -0.0126 0.0096  0.0014  111 MET   A CE  
790  N  N   . ALA   A 112 ? 0.1915 0.3024 0.1880 0.0023  0.0037  -0.0155 112 ALA   A N   
791  C  CA  . ALA   A 112 ? 0.2063 0.3312 0.2035 0.0029  0.0035  -0.0185 112 ALA   A CA  
792  C  C   . ALA   A 112 ? 0.2137 0.3430 0.2062 0.0111  0.0013  -0.0206 112 ALA   A C   
793  O  O   . ALA   A 112 ? 0.2169 0.3570 0.2090 0.0133  0.0008  -0.0234 112 ALA   A O   
794  C  CB  . ALA   A 112 ? 0.2141 0.3389 0.2139 -0.0008 0.0041  -0.0203 112 ALA   A CB  
795  N  N   . GLY   A 113 ? 0.2142 0.3346 0.2028 0.0158  0.0002  -0.0195 113 GLY   A N   
796  C  CA  . GLY   A 113 ? 0.2204 0.3439 0.2042 0.0237  -0.0018 -0.0214 113 GLY   A CA  
797  C  C   . GLY   A 113 ? 0.2300 0.3452 0.2097 0.0285  -0.0032 -0.0223 113 GLY   A C   
798  O  O   . GLY   A 113 ? 0.2547 0.3715 0.2300 0.0355  -0.0049 -0.0239 113 GLY   A O   
799  N  N   . ASN   A 114 ? 0.2160 0.3227 0.1971 0.0251  -0.0026 -0.0214 114 ASN   A N   
800  C  CA  . ASN   A 114 ? 0.2040 0.3037 0.1813 0.0292  -0.0038 -0.0218 114 ASN   A CA  
801  C  C   . ASN   A 114 ? 0.2210 0.3049 0.1955 0.0297  -0.0042 -0.0197 114 ASN   A C   
802  O  O   . ASN   A 114 ? 0.2362 0.3126 0.2130 0.0251  -0.0033 -0.0182 114 ASN   A O   
803  C  CB  . ASN   A 114 ? 0.2114 0.3139 0.1917 0.0255  -0.0031 -0.0227 114 ASN   A CB  
804  C  CG  . ASN   A 114 ? 0.2246 0.3229 0.2009 0.0302  -0.0043 -0.0232 114 ASN   A CG  
805  O  OD1 . ASN   A 114 ? 0.2201 0.3090 0.1913 0.0351  -0.0055 -0.0221 114 ASN   A OD1 
806  N  ND2 . ASN   A 114 ? 0.2566 0.3611 0.2351 0.0282  -0.0039 -0.0247 114 ASN   A ND2 
807  N  N   . GLU   A 115 ? 0.2221 0.3011 0.1914 0.0356  -0.0057 -0.0199 115 GLU   A N   
808  C  CA  . GLU   A 115 ? 0.2337 0.2982 0.1997 0.0363  -0.0061 -0.0184 115 GLU   A CA  
809  C  C   . GLU   A 115 ? 0.2295 0.2857 0.1921 0.0382  -0.0068 -0.0178 115 GLU   A C   
810  O  O   . GLU   A 115 ? 0.2251 0.2703 0.1870 0.0358  -0.0065 -0.0161 115 GLU   A O   
811  C  CB  . GLU   A 115 ? 0.2584 0.3213 0.2201 0.0417  -0.0074 -0.0193 115 GLU   A CB  
812  C  CG  . GLU   A 115 ? 0.2654 0.3359 0.2302 0.0397  -0.0068 -0.0195 115 GLU   A CG  
813  C  CD  . GLU   A 115 ? 0.3282 0.3970 0.2887 0.0452  -0.0081 -0.0210 115 GLU   A CD  
814  O  OE1 . GLU   A 115 ? 0.3649 0.4242 0.3200 0.0500  -0.0094 -0.0217 115 GLU   A OE1 
815  O  OE2 . GLU   A 115 ? 0.3320 0.4094 0.2946 0.0446  -0.0078 -0.0216 115 GLU   A OE2 
816  N  N   . GLN   A 116 ? 0.2374 0.2999 0.1980 0.0425  -0.0076 -0.0191 116 GLN   A N   
817  C  CA  . GLN   A 116 ? 0.2440 0.2991 0.2003 0.0455  -0.0084 -0.0183 116 GLN   A CA  
818  C  C   . GLN   A 116 ? 0.2204 0.2722 0.1799 0.0399  -0.0073 -0.0170 116 GLN   A C   
819  O  O   . GLN   A 116 ? 0.2331 0.2745 0.1895 0.0402  -0.0075 -0.0154 116 GLN   A O   
820  C  CB  . GLN   A 116 ? 0.2674 0.3319 0.2211 0.0516  -0.0094 -0.0199 116 GLN   A CB  
821  C  CG  . GLN   A 116 ? 0.2858 0.3416 0.2334 0.0563  -0.0104 -0.0184 116 GLN   A CG  
822  C  CD  . GLN   A 116 ? 0.3346 0.3757 0.2760 0.0599  -0.0113 -0.0171 116 GLN   A CD  
823  O  OE1 . GLN   A 116 ? 0.3816 0.4224 0.3208 0.0637  -0.0121 -0.0183 116 GLN   A OE1 
824  N  NE2 . GLN   A 116 ? 0.3647 0.3936 0.3031 0.0588  -0.0113 -0.0147 116 GLN   A NE2 
825  N  N   . VAL   A 117 ? 0.1903 0.2508 0.1557 0.0350  -0.0060 -0.0180 117 VAL   A N   
826  C  CA  . VAL   A 117 ? 0.1975 0.2556 0.1657 0.0304  -0.0051 -0.0175 117 VAL   A CA  
827  C  C   . VAL   A 117 ? 0.1953 0.2414 0.1639 0.0268  -0.0046 -0.0154 117 VAL   A C   
828  O  O   . VAL   A 117 ? 0.2055 0.2457 0.1736 0.0253  -0.0044 -0.0144 117 VAL   A O   
829  C  CB  . VAL   A 117 ? 0.1967 0.2657 0.1711 0.0258  -0.0040 -0.0194 117 VAL   A CB  
830  C  CG1 . VAL   A 117 ? 0.2005 0.2712 0.1794 0.0209  -0.0027 -0.0191 117 VAL   A CG1 
831  C  CG2 . VAL   A 117 ? 0.2133 0.2805 0.1899 0.0223  -0.0033 -0.0196 117 VAL   A CG2 
832  N  N   . GLY   A 118 ? 0.1968 0.2408 0.1665 0.0253  -0.0042 -0.0147 118 GLY   A N   
833  C  CA  . GLY   A 118 ? 0.1896 0.2235 0.1593 0.0224  -0.0038 -0.0129 118 GLY   A CA  
834  C  C   . GLY   A 118 ? 0.1948 0.2183 0.1588 0.0253  -0.0048 -0.0118 118 GLY   A C   
835  O  O   . GLY   A 118 ? 0.1918 0.2081 0.1554 0.0228  -0.0044 -0.0105 118 GLY   A O   
836  N  N   . PHE   A 119 ? 0.1930 0.2157 0.1522 0.0307  -0.0060 -0.0124 119 PHE   A N   
837  C  CA  . PHE   A 119 ? 0.1985 0.2103 0.1516 0.0337  -0.0069 -0.0113 119 PHE   A CA  
838  C  C   . PHE   A 119 ? 0.1988 0.2085 0.1505 0.0334  -0.0069 -0.0102 119 PHE   A C   
839  O  O   . PHE   A 119 ? 0.1992 0.2000 0.1489 0.0314  -0.0067 -0.0085 119 PHE   A O   
840  C  CB  . PHE   A 119 ? 0.2069 0.2185 0.1549 0.0403  -0.0083 -0.0124 119 PHE   A CB  
841  C  CG  . PHE   A 119 ? 0.2284 0.2269 0.1694 0.0433  -0.0092 -0.0111 119 PHE   A CG  
842  C  CD1 . PHE   A 119 ? 0.2488 0.2376 0.1873 0.0425  -0.0094 -0.0111 119 PHE   A CD1 
843  C  CD2 . PHE   A 119 ? 0.2417 0.2375 0.1787 0.0464  -0.0097 -0.0099 119 PHE   A CD2 
844  C  CE1 . PHE   A 119 ? 0.2633 0.2390 0.1955 0.0442  -0.0100 -0.0099 119 PHE   A CE1 
845  C  CE2 . PHE   A 119 ? 0.2566 0.2394 0.1870 0.0485  -0.0103 -0.0082 119 PHE   A CE2 
846  C  CZ  . PHE   A 119 ? 0.2738 0.2461 0.2019 0.0472  -0.0104 -0.0083 119 PHE   A CZ  
847  N  N   . ASP   A 120 ? 0.1905 0.2096 0.1435 0.0352  -0.0070 -0.0112 120 ASP   A N   
848  C  CA  . ASP   A 120 ? 0.2000 0.2192 0.1515 0.0359  -0.0070 -0.0104 120 ASP   A CA  
849  C  C   . ASP   A 120 ? 0.1901 0.2079 0.1456 0.0299  -0.0059 -0.0098 120 ASP   A C   
850  O  O   . ASP   A 120 ? 0.1925 0.2051 0.1456 0.0294  -0.0059 -0.0082 120 ASP   A O   
851  C  CB  . ASP   A 120 ? 0.2244 0.2557 0.1767 0.0392  -0.0074 -0.0122 120 ASP   A CB  
852  C  CG  . ASP   A 120 ? 0.2661 0.2985 0.2129 0.0466  -0.0088 -0.0125 120 ASP   A CG  
853  O  OD1 . ASP   A 120 ? 0.2905 0.3119 0.2319 0.0496  -0.0095 -0.0111 120 ASP   A OD1 
854  O  OD2 . ASP   A 120 ? 0.3111 0.3555 0.2591 0.0493  -0.0091 -0.0144 120 ASP   A OD2 
855  N  N   . LEU   A 121 ? 0.1730 0.1959 0.1346 0.0256  -0.0049 -0.0111 121 LEU   A N   
856  C  CA  . LEU   A 121 ? 0.1735 0.1953 0.1391 0.0205  -0.0039 -0.0109 121 LEU   A CA  
857  C  C   . LEU   A 121 ? 0.1728 0.1841 0.1362 0.0187  -0.0038 -0.0088 121 LEU   A C   
858  O  O   . LEU   A 121 ? 0.1774 0.1854 0.1402 0.0169  -0.0035 -0.0079 121 LEU   A O   
859  C  CB  . LEU   A 121 ? 0.1691 0.1972 0.1410 0.0167  -0.0028 -0.0124 121 LEU   A CB  
860  C  CG  . LEU   A 121 ? 0.1718 0.2000 0.1481 0.0122  -0.0018 -0.0129 121 LEU   A CG  
861  C  CD1 . LEU   A 121 ? 0.1671 0.2034 0.1487 0.0095  -0.0009 -0.0150 121 LEU   A CD1 
862  C  CD2 . LEU   A 121 ? 0.1803 0.2007 0.1573 0.0094  -0.0013 -0.0112 121 LEU   A CD2 
863  N  N   . VAL   A 122 ? 0.1565 0.1632 0.1187 0.0189  -0.0039 -0.0083 122 VAL   A N   
864  C  CA  . VAL   A 122 ? 0.1746 0.1725 0.1349 0.0168  -0.0038 -0.0068 122 VAL   A CA  
865  C  C   . VAL   A 122 ? 0.1911 0.1818 0.1454 0.0187  -0.0045 -0.0053 122 VAL   A C   
866  O  O   . VAL   A 122 ? 0.1966 0.1827 0.1502 0.0159  -0.0041 -0.0041 122 VAL   A O   
867  C  CB  . VAL   A 122 ? 0.1802 0.1754 0.1401 0.0170  -0.0039 -0.0069 122 VAL   A CB  
868  C  CG1 . VAL   A 122 ? 0.1862 0.1726 0.1433 0.0150  -0.0039 -0.0058 122 VAL   A CG1 
869  C  CG2 . VAL   A 122 ? 0.1740 0.1758 0.1397 0.0144  -0.0030 -0.0076 122 VAL   A CG2 
870  N  N   . LYS   A 123 ? 0.2019 0.1918 0.1519 0.0236  -0.0054 -0.0053 123 LYS   A N   
871  C  CA  . LYS   A 123 ? 0.2223 0.2037 0.1658 0.0257  -0.0060 -0.0034 123 LYS   A CA  
872  C  C   . LYS   A 123 ? 0.2074 0.1910 0.1511 0.0243  -0.0056 -0.0022 123 LYS   A C   
873  O  O   . LYS   A 123 ? 0.2115 0.1879 0.1518 0.0227  -0.0055 -0.0002 123 LYS   A O   
874  C  CB  . LYS   A 123 ? 0.2725 0.2533 0.2113 0.0321  -0.0072 -0.0037 123 LYS   A CB  
875  C  CG  . LYS   A 123 ? 0.3311 0.3017 0.2624 0.0348  -0.0078 -0.0013 123 LYS   A CG  
876  C  CD  . LYS   A 123 ? 0.4296 0.3973 0.3555 0.0417  -0.0090 -0.0017 123 LYS   A CD  
877  C  CE  . LYS   A 123 ? 0.5561 0.5358 0.4835 0.0463  -0.0095 -0.0030 123 LYS   A CE  
878  N  NZ  . LYS   A 123 ? 0.6648 0.6411 0.5855 0.0540  -0.0108 -0.0026 123 LYS   A NZ  
879  N  N   . ALA   A 124 ? 0.1971 0.1910 0.1446 0.0249  -0.0054 -0.0037 124 ALA   A N   
880  C  CA  . ALA   A 124 ? 0.2067 0.2044 0.1547 0.0238  -0.0051 -0.0031 124 ALA   A CA  
881  C  C   . ALA   A 124 ? 0.2022 0.1974 0.1530 0.0184  -0.0042 -0.0026 124 ALA   A C   
882  O  O   . ALA   A 124 ? 0.1975 0.1900 0.1458 0.0173  -0.0040 -0.0008 124 ALA   A O   
883  C  CB  . ALA   A 124 ? 0.2165 0.2263 0.1690 0.0246  -0.0050 -0.0056 124 ALA   A CB  
884  N  N   . CYS   A 125 ? 0.1811 0.1780 0.1370 0.0153  -0.0036 -0.0041 125 CYS   A N   
885  C  CA  . CYS   A 125 ? 0.1888 0.1842 0.1474 0.0108  -0.0028 -0.0038 125 CYS   A CA  
886  C  C   . CYS   A 125 ? 0.1958 0.1820 0.1499 0.0094  -0.0029 -0.0017 125 CYS   A C   
887  O  O   . CYS   A 125 ? 0.1928 0.1778 0.1466 0.0066  -0.0024 -0.0007 125 CYS   A O   
888  C  CB  . CYS   A 125 ? 0.1878 0.1864 0.1521 0.0086  -0.0022 -0.0055 125 CYS   A CB  
889  S  SG  . CYS   A 125 ? 0.2062 0.2150 0.1761 0.0084  -0.0018 -0.0082 125 CYS   A SG  
890  N  N   . LYS   A 126 ? 0.1992 0.1793 0.1500 0.0111  -0.0034 -0.0012 126 LYS   A N   
891  C  CA  . LYS   A 126 ? 0.2152 0.1861 0.1616 0.0093  -0.0034 0.0004  126 LYS   A CA  
892  C  C   . LYS   A 126 ? 0.2240 0.1902 0.1649 0.0099  -0.0036 0.0028  126 LYS   A C   
893  O  O   . LYS   A 126 ? 0.2315 0.1933 0.1705 0.0063  -0.0031 0.0043  126 LYS   A O   
894  C  CB  . LYS   A 126 ? 0.2322 0.1972 0.1754 0.0117  -0.0041 0.0000  126 LYS   A CB  
895  C  CG  . LYS   A 126 ? 0.2504 0.2048 0.1885 0.0098  -0.0041 0.0012  126 LYS   A CG  
896  C  CD  . LYS   A 126 ? 0.2775 0.2319 0.2180 0.0043  -0.0033 0.0012  126 LYS   A CD  
897  C  CE  . LYS   A 126 ? 0.3170 0.2616 0.2523 0.0017  -0.0033 0.0022  126 LYS   A CE  
898  N  NZ  . LYS   A 126 ? 0.3718 0.3120 0.3059 0.0025  -0.0037 0.0005  126 LYS   A NZ  
899  N  N   . GLU   A 127 ? 0.2427 0.2104 0.1810 0.0142  -0.0042 0.0034  127 GLU   A N   
900  C  CA  . GLU   A 127 ? 0.2717 0.2348 0.2043 0.0152  -0.0043 0.0062  127 GLU   A CA  
901  C  C   . GLU   A 127 ? 0.2437 0.2118 0.1786 0.0113  -0.0035 0.0069  127 GLU   A C   
902  O  O   . GLU   A 127 ? 0.2526 0.2154 0.1836 0.0088  -0.0031 0.0094  127 GLU   A O   
903  C  CB  . GLU   A 127 ? 0.3094 0.2754 0.2392 0.0212  -0.0051 0.0065  127 GLU   A CB  
904  C  CG  . GLU   A 127 ? 0.3717 0.3302 0.2969 0.0256  -0.0060 0.0065  127 GLU   A CG  
905  C  CD  . GLU   A 127 ? 0.4612 0.4241 0.3841 0.0323  -0.0069 0.0063  127 GLU   A CD  
906  O  OE1 . GLU   A 127 ? 0.4689 0.4425 0.3946 0.0334  -0.0068 0.0057  127 GLU   A OE1 
907  O  OE2 . GLU   A 127 ? 0.5192 0.4753 0.4374 0.0366  -0.0077 0.0065  127 GLU   A OE2 
908  N  N   . ALA   A 128 ? 0.2164 0.1947 0.1575 0.0106  -0.0032 0.0046  128 ALA   A N   
909  C  CA  . ALA   A 128 ? 0.1991 0.1833 0.1430 0.0075  -0.0025 0.0045  128 ALA   A CA  
910  C  C   . ALA   A 128 ? 0.1925 0.1733 0.1373 0.0027  -0.0019 0.0049  128 ALA   A C   
911  O  O   . ALA   A 128 ? 0.2133 0.1939 0.1563 0.0000  -0.0014 0.0065  128 ALA   A O   
912  C  CB  . ALA   A 128 ? 0.1939 0.1885 0.1443 0.0079  -0.0024 0.0013  128 ALA   A CB  
913  N  N   . CYS   A 129 ? 0.1882 0.1674 0.1359 0.0015  -0.0018 0.0033  129 CYS   A N   
914  C  CA  . CYS   A 129 ? 0.2022 0.1795 0.1509 -0.0026 -0.0012 0.0034  129 CYS   A CA  
915  C  C   . CYS   A 129 ? 0.2170 0.1857 0.1596 -0.0048 -0.0011 0.0059  129 CYS   A C   
916  O  O   . CYS   A 129 ? 0.2127 0.1821 0.1548 -0.0087 -0.0005 0.0068  129 CYS   A O   
917  C  CB  . CYS   A 129 ? 0.2088 0.1863 0.1612 -0.0028 -0.0012 0.0015  129 CYS   A CB  
918  S  SG  . CYS   A 129 ? 0.2036 0.1905 0.1636 -0.0023 -0.0008 -0.0011 129 CYS   A SG  
919  N  N   . ALA   A 130 ? 0.2239 0.1844 0.1617 -0.0024 -0.0017 0.0069  130 ALA   A N   
920  C  CA  . ALA   A 130 ? 0.2502 0.2006 0.1819 -0.0046 -0.0016 0.0090  130 ALA   A CA  
921  C  C   . ALA   A 130 ? 0.2532 0.2027 0.1811 -0.0063 -0.0011 0.0120  130 ALA   A C   
922  O  O   . ALA   A 130 ? 0.2703 0.2155 0.1954 -0.0109 -0.0005 0.0136  130 ALA   A O   
923  C  CB  . ALA   A 130 ? 0.2741 0.2156 0.2012 -0.0007 -0.0024 0.0093  130 ALA   A CB  
924  N  N   . ALA   A 131 ? 0.2449 0.1995 0.1728 -0.0029 -0.0014 0.0128  131 ALA   A N   
925  C  CA  . ALA   A 131 ? 0.2558 0.2113 0.1802 -0.0039 -0.0010 0.0158  131 ALA   A CA  
926  C  C   . ALA   A 131 ? 0.2488 0.2113 0.1764 -0.0092 -0.0001 0.0154  131 ALA   A C   
927  O  O   . ALA   A 131 ? 0.2672 0.2288 0.1912 -0.0120 0.0005  0.0183  131 ALA   A O   
928  C  CB  . ALA   A 131 ? 0.2541 0.2169 0.1793 0.0009  -0.0015 0.0157  131 ALA   A CB  
929  N  N   . ALA   A 132 ? 0.2315 0.2013 0.1658 -0.0104 0.0000  0.0121  132 ALA   A N   
930  C  CA  . ALA   A 132 ? 0.2363 0.2140 0.1741 -0.0142 0.0007  0.0112  132 ALA   A CA  
931  C  C   . ALA   A 132 ? 0.2316 0.2070 0.1705 -0.0183 0.0011  0.0103  132 ALA   A C   
932  O  O   . ALA   A 132 ? 0.2362 0.2189 0.1787 -0.0209 0.0016  0.0090  132 ALA   A O   
933  C  CB  . ALA   A 132 ? 0.2426 0.2308 0.1871 -0.0120 0.0006  0.0081  132 ALA   A CB  
934  N  N   . ASN   A 133 ? 0.2438 0.2097 0.1797 -0.0186 0.0009  0.0107  133 ASN   A N   
935  C  CA  . ASN   A 133 ? 0.2780 0.2421 0.2148 -0.0222 0.0012  0.0094  133 ASN   A CA  
936  C  C   . ASN   A 133 ? 0.2430 0.2153 0.1866 -0.0213 0.0012  0.0064  133 ASN   A C   
937  O  O   . ASN   A 133 ? 0.2472 0.2240 0.1932 -0.0244 0.0016  0.0053  133 ASN   A O   
938  C  CB  . ASN   A 133 ? 0.3520 0.3162 0.2861 -0.0281 0.0021  0.0110  133 ASN   A CB  
939  C  CG  . ASN   A 133 ? 0.4402 0.3932 0.3667 -0.0295 0.0022  0.0143  133 ASN   A CG  
940  O  OD1 . ASN   A 133 ? 0.6271 0.5807 0.5505 -0.0308 0.0027  0.0171  133 ASN   A OD1 
941  N  ND2 . ASN   A 133 ? 0.5093 0.4518 0.4326 -0.0290 0.0019  0.0140  133 ASN   A ND2 
942  N  N   . VAL   A 134 ? 0.2135 0.1877 0.1602 -0.0169 0.0007  0.0051  134 VAL   A N   
943  C  CA  . VAL   A 134 ? 0.1977 0.1782 0.1504 -0.0156 0.0007  0.0027  134 VAL   A CA  
944  C  C   . VAL   A 134 ? 0.1972 0.1731 0.1500 -0.0137 0.0002  0.0019  134 VAL   A C   
945  O  O   . VAL   A 134 ? 0.1989 0.1696 0.1488 -0.0111 -0.0003 0.0025  134 VAL   A O   
946  C  CB  . VAL   A 134 ? 0.1913 0.1781 0.1475 -0.0128 0.0006  0.0017  134 VAL   A CB  
947  C  CG1 . VAL   A 134 ? 0.1847 0.1754 0.1465 -0.0108 0.0006  -0.0005 134 VAL   A CG1 
948  C  CG2 . VAL   A 134 ? 0.2138 0.2070 0.1707 -0.0148 0.0010  0.0019  134 VAL   A CG2 
949  N  N   . LEU   A 135 ? 0.2096 0.1883 0.1657 -0.0145 0.0005  0.0006  135 LEU   A N   
950  C  CA  . LEU   A 135 ? 0.2173 0.1933 0.1739 -0.0128 0.0001  -0.0002 135 LEU   A CA  
951  C  C   . LEU   A 135 ? 0.1933 0.1728 0.1537 -0.0093 -0.0001 -0.0011 135 LEU   A C   
952  O  O   . LEU   A 135 ? 0.1849 0.1700 0.1493 -0.0091 0.0003  -0.0017 135 LEU   A O   
953  C  CB  . LEU   A 135 ? 0.2590 0.2378 0.2176 -0.0150 0.0005  -0.0011 135 LEU   A CB  
954  C  CG  . LEU   A 135 ? 0.4141 0.3874 0.3690 -0.0169 0.0003  -0.0014 135 LEU   A CG  
955  C  CD1 . LEU   A 135 ? 0.4239 0.3906 0.3734 -0.0198 0.0003  -0.0003 135 LEU   A CD1 
956  C  CD2 . LEU   A 135 ? 0.4108 0.3893 0.3682 -0.0189 0.0006  -0.0025 135 LEU   A CD2 
957  N  N   . LEU   A 136 ? 0.1785 0.1550 0.1377 -0.0067 -0.0006 -0.0013 136 LEU   A N   
958  C  CA  . LEU   A 136 ? 0.1688 0.1492 0.1315 -0.0040 -0.0007 -0.0022 136 LEU   A CA  
959  C  C   . LEU   A 136 ? 0.1720 0.1534 0.1366 -0.0035 -0.0006 -0.0028 136 LEU   A C   
960  O  O   . LEU   A 136 ? 0.1885 0.1662 0.1502 -0.0028 -0.0011 -0.0030 136 LEU   A O   
961  C  CB  . LEU   A 136 ? 0.1780 0.1563 0.1378 -0.0008 -0.0013 -0.0020 136 LEU   A CB  
962  C  CG  . LEU   A 136 ? 0.1880 0.1717 0.1514 0.0015  -0.0013 -0.0032 136 LEU   A CG  
963  C  CD1 . LEU   A 136 ? 0.1905 0.1797 0.1577 0.0007  -0.0008 -0.0038 136 LEU   A CD1 
964  C  CD2 . LEU   A 136 ? 0.2050 0.1871 0.1649 0.0052  -0.0022 -0.0032 136 LEU   A CD2 
965  N  N   . LYS   A 137 ? 0.1578 0.1442 0.1272 -0.0036 0.0000  -0.0031 137 LYS   A N   
966  C  CA  . LYS   A 137 ? 0.1513 0.1399 0.1229 -0.0029 0.0002  -0.0031 137 LYS   A CA  
967  C  C   . LYS   A 137 ? 0.1603 0.1516 0.1340 -0.0009 0.0002  -0.0035 137 LYS   A C   
968  O  O   . LYS   A 137 ? 0.1582 0.1515 0.1338 -0.0009 0.0004  -0.0040 137 LYS   A O   
969  C  CB  . LYS   A 137 ? 0.1599 0.1519 0.1351 -0.0042 0.0009  -0.0027 137 LYS   A CB  
970  C  CG  . LYS   A 137 ? 0.1684 0.1604 0.1426 -0.0064 0.0011  -0.0026 137 LYS   A CG  
971  C  CD  . LYS   A 137 ? 0.1663 0.1621 0.1431 -0.0067 0.0016  -0.0022 137 LYS   A CD  
972  C  CE  . LYS   A 137 ? 0.1843 0.1824 0.1610 -0.0085 0.0018  -0.0024 137 LYS   A CE  
973  N  NZ  . LYS   A 137 ? 0.1800 0.1801 0.1591 -0.0083 0.0022  -0.0026 137 LYS   A NZ  
974  N  N   . VAL   A 138 ? 0.1489 0.1412 0.1224 0.0006  0.0000  -0.0036 138 VAL   A N   
975  C  CA  . VAL   A 138 ? 0.1398 0.1362 0.1155 0.0020  0.0001  -0.0041 138 VAL   A CA  
976  C  C   . VAL   A 138 ? 0.1414 0.1415 0.1207 0.0013  0.0009  -0.0033 138 VAL   A C   
977  O  O   . VAL   A 138 ? 0.1444 0.1448 0.1227 0.0019  0.0008  -0.0029 138 VAL   A O   
978  C  CB  . VAL   A 138 ? 0.1489 0.1446 0.1211 0.0049  -0.0008 -0.0049 138 VAL   A CB  
979  C  CG1 . VAL   A 138 ? 0.1592 0.1610 0.1339 0.0061  -0.0006 -0.0055 138 VAL   A CG1 
980  C  CG2 . VAL   A 138 ? 0.1551 0.1463 0.1232 0.0059  -0.0015 -0.0050 138 VAL   A CG2 
981  N  N   . ILE   A 139 ? 0.1296 0.1322 0.1127 0.0002  0.0017  -0.0031 139 ILE   A N   
982  C  CA  . ILE   A 139 ? 0.1365 0.1420 0.1228 -0.0006 0.0027  -0.0019 139 ILE   A CA  
983  C  C   . ILE   A 139 ? 0.1432 0.1532 0.1300 0.0002  0.0026  -0.0022 139 ILE   A C   
984  O  O   . ILE   A 139 ? 0.1349 0.1471 0.1226 0.0001  0.0026  -0.0035 139 ILE   A O   
985  C  CB  . ILE   A 139 ? 0.1333 0.1383 0.1233 -0.0024 0.0036  -0.0017 139 ILE   A CB  
986  C  CG1 . ILE   A 139 ? 0.1412 0.1431 0.1309 -0.0029 0.0036  -0.0016 139 ILE   A CG1 
987  C  CG2 . ILE   A 139 ? 0.1380 0.1447 0.1308 -0.0034 0.0047  0.0001  139 ILE   A CG2 
988  C  CD1 . ILE   A 139 ? 0.1393 0.1405 0.1318 -0.0040 0.0042  -0.0026 139 ILE   A CD1 
989  N  N   . ILE   A 140 ? 0.1415 0.1541 0.1279 0.0010  0.0027  -0.0013 140 ILE   A N   
990  C  CA  . ILE   A 140 ? 0.1463 0.1645 0.1329 0.0019  0.0026  -0.0018 140 ILE   A CA  
991  C  C   . ILE   A 140 ? 0.1488 0.1711 0.1393 -0.0003 0.0040  -0.0001 140 ILE   A C   
992  O  O   . ILE   A 140 ? 0.1441 0.1720 0.1354 -0.0004 0.0042  -0.0007 140 ILE   A O   
993  C  CB  . ILE   A 140 ? 0.1621 0.1817 0.1455 0.0046  0.0017  -0.0024 140 ILE   A CB  
994  C  CG1 . ILE   A 140 ? 0.1771 0.1973 0.1609 0.0042  0.0021  -0.0007 140 ILE   A CG1 
995  C  CG2 . ILE   A 140 ? 0.1559 0.1703 0.1350 0.0067  0.0004  -0.0040 140 ILE   A CG2 
996  C  CD1 . ILE   A 140 ? 0.1874 0.2110 0.1688 0.0066  0.0013  -0.0016 140 ILE   A CD1 
997  N  N   . GLU   A 141 ? 0.1503 0.1696 0.1428 -0.0021 0.0050  0.0019  141 GLU   A N   
998  C  CA  . GLU   A 141 ? 0.1418 0.1629 0.1376 -0.0045 0.0065  0.0040  141 GLU   A CA  
999  C  C   . GLU   A 141 ? 0.1539 0.1810 0.1495 -0.0040 0.0068  0.0057  141 GLU   A C   
1000 O  O   . GLU   A 141 ? 0.1522 0.1846 0.1492 -0.0054 0.0074  0.0059  141 GLU   A O   
1001 C  CB  . GLU   A 141 ? 0.1502 0.1719 0.1485 -0.0068 0.0071  0.0026  141 GLU   A CB  
1002 C  CG  . GLU   A 141 ? 0.1594 0.1782 0.1608 -0.0098 0.0087  0.0046  141 GLU   A CG  
1003 C  CD  . GLU   A 141 ? 0.1693 0.1811 0.1712 -0.0097 0.0089  0.0051  141 GLU   A CD  
1004 O  OE1 . GLU   A 141 ? 0.1639 0.1739 0.1644 -0.0078 0.0087  0.0070  141 GLU   A OE1 
1005 O  OE2 . GLU   A 141 ? 0.1797 0.1883 0.1834 -0.0113 0.0093  0.0035  141 GLU   A OE2 
1006 N  N   . THR   A 142 ? 0.1530 0.1800 0.1471 -0.0024 0.0065  0.0070  142 THR   A N   
1007 C  CA  . THR   A 142 ? 0.1599 0.1933 0.1533 -0.0014 0.0066  0.0083  142 THR   A CA  
1008 C  C   . THR   A 142 ? 0.1704 0.2069 0.1665 -0.0039 0.0083  0.0116  142 THR   A C   
1009 O  O   . THR   A 142 ? 0.1762 0.2200 0.1724 -0.0039 0.0086  0.0124  142 THR   A O   
1010 C  CB  . THR   A 142 ? 0.1525 0.1855 0.1440 0.0005  0.0061  0.0090  142 THR   A CB  
1011 O  OG1 . THR   A 142 ? 0.1635 0.1921 0.1564 -0.0005 0.0069  0.0112  142 THR   A OG1 
1012 C  CG2 . THR   A 142 ? 0.1567 0.1868 0.1451 0.0024  0.0045  0.0059  142 THR   A CG2 
1013 N  N   . GLY   A 143 ? 0.1745 0.2055 0.1727 -0.0059 0.0094  0.0135  143 GLY   A N   
1014 C  CA  . GLY   A 143 ? 0.1930 0.2244 0.1933 -0.0086 0.0112  0.0170  143 GLY   A CA  
1015 C  C   . GLY   A 143 ? 0.2143 0.2492 0.2165 -0.0118 0.0119  0.0159  143 GLY   A C   
1016 O  O   . GLY   A 143 ? 0.2492 0.2869 0.2528 -0.0144 0.0134  0.0187  143 GLY   A O   
1017 N  N   . GLU   A 144 ? 0.2005 0.2362 0.2026 -0.0115 0.0109  0.0120  144 GLU   A N   
1018 C  CA  . GLU   A 144 ? 0.2018 0.2430 0.2054 -0.0141 0.0113  0.0102  144 GLU   A CA  
1019 C  C   . GLU   A 144 ? 0.2019 0.2527 0.2038 -0.0117 0.0103  0.0086  144 GLU   A C   
1020 O  O   . GLU   A 144 ? 0.2234 0.2822 0.2265 -0.0137 0.0110  0.0087  144 GLU   A O   
1021 C  CB  . GLU   A 144 ? 0.2117 0.2490 0.2164 -0.0151 0.0110  0.0069  144 GLU   A CB  
1022 C  CG  . GLU   A 144 ? 0.2309 0.2595 0.2377 -0.0179 0.0122  0.0080  144 GLU   A CG  
1023 C  CD  . GLU   A 144 ? 0.2910 0.3195 0.3003 -0.0224 0.0142  0.0105  144 GLU   A CD  
1024 O  OE1 . GLU   A 144 ? 0.2909 0.3269 0.3013 -0.0249 0.0147  0.0095  144 GLU   A OE1 
1025 O  OE2 . GLU   A 144 ? 0.3230 0.3443 0.3329 -0.0233 0.0153  0.0135  144 GLU   A OE2 
1026 N  N   . LEU   A 145 ? 0.1765 0.2269 0.1754 -0.0075 0.0086  0.0069  145 LEU   A N   
1027 C  CA  . LEU   A 145 ? 0.1944 0.2527 0.1911 -0.0044 0.0075  0.0052  145 LEU   A CA  
1028 C  C   . LEU   A 145 ? 0.2151 0.2804 0.2122 -0.0047 0.0083  0.0079  145 LEU   A C   
1029 O  O   . LEU   A 145 ? 0.2067 0.2816 0.2038 -0.0044 0.0082  0.0071  145 LEU   A O   
1030 C  CB  . LEU   A 145 ? 0.1992 0.2535 0.1924 -0.0001 0.0057  0.0030  145 LEU   A CB  
1031 C  CG  . LEU   A 145 ? 0.2057 0.2543 0.1978 0.0007  0.0048  0.0004  145 LEU   A CG  
1032 C  CD1 . LEU   A 145 ? 0.2124 0.2552 0.2009 0.0039  0.0033  -0.0008 145 LEU   A CD1 
1033 C  CD2 . LEU   A 145 ? 0.2172 0.2724 0.2093 0.0016  0.0043  -0.0022 145 LEU   A CD2 
1034 N  N   . LYS   A 146 ? 0.2183 0.2797 0.2153 -0.0048 0.0089  0.0110  146 LYS   A N   
1035 C  CA  . LYS   A 146 ? 0.2804 0.3477 0.2778 -0.0052 0.0098  0.0144  146 LYS   A CA  
1036 C  C   . LYS   A 146 ? 0.2879 0.3632 0.2828 -0.0014 0.0085  0.0126  146 LYS   A C   
1037 O  O   . LYS   A 146 ? 0.4027 0.4790 0.3965 0.0004  0.0083  0.0139  146 LYS   A O   
1038 C  CB  . LYS   A 146 ? 0.3498 0.4218 0.3498 -0.0096 0.0117  0.0169  146 LYS   A CB  
1039 C  CG  . LYS   A 146 ? 0.4063 0.4692 0.4086 -0.0134 0.0132  0.0192  146 LYS   A CG  
1040 C  CD  . LYS   A 146 ? 0.4940 0.5601 0.4989 -0.0186 0.0149  0.0204  146 LYS   A CD  
1041 C  CE  . LYS   A 146 ? 0.5422 0.5975 0.5490 -0.0220 0.0162  0.0216  146 LYS   A CE  
1042 N  NZ  . LYS   A 146 ? 0.5847 0.6424 0.5940 -0.0276 0.0178  0.0219  146 LYS   A NZ  
1043 N  N   . ASP   A 147 ? 0.2695 0.3506 0.2636 0.0003  0.0075  0.0093  147 ASP   A N   
1044 C  CA  . ASP   A 147 ? 0.2701 0.3593 0.2619 0.0041  0.0063  0.0071  147 ASP   A CA  
1045 C  C   . ASP   A 147 ? 0.2453 0.3281 0.2338 0.0080  0.0045  0.0042  147 ASP   A C   
1046 O  O   . ASP   A 147 ? 0.2167 0.2915 0.2040 0.0088  0.0037  0.0021  147 ASP   A O   
1047 C  CB  . ASP   A 147 ? 0.3087 0.4062 0.3007 0.0047  0.0059  0.0046  147 ASP   A CB  
1048 C  CG  . ASP   A 147 ? 0.3687 0.4738 0.3578 0.0097  0.0043  0.0013  147 ASP   A CG  
1049 O  OD1 . ASP   A 147 ? 0.4343 0.5488 0.4237 0.0099  0.0047  0.0026  147 ASP   A OD1 
1050 O  OD2 . ASP   A 147 ? 0.4254 0.5262 0.4118 0.0134  0.0026  -0.0023 147 ASP   A OD2 
1051 N  N   . GLU   A 148 ? 0.2144 0.3014 0.2013 0.0105  0.0039  0.0038  148 GLU   A N   
1052 C  CA  . GLU   A 148 ? 0.2180 0.2995 0.2016 0.0138  0.0023  0.0007  148 GLU   A CA  
1053 C  C   . GLU   A 148 ? 0.2232 0.3015 0.2041 0.0169  0.0007  -0.0035 148 GLU   A C   
1054 O  O   . GLU   A 148 ? 0.2146 0.2831 0.1932 0.0178  -0.0002 -0.0052 148 GLU   A O   
1055 C  CB  . GLU   A 148 ? 0.2485 0.3375 0.2309 0.0160  0.0019  0.0002  148 GLU   A CB  
1056 C  CG  . GLU   A 148 ? 0.2914 0.3750 0.2701 0.0193  0.0001  -0.0040 148 GLU   A CG  
1057 C  CD  . GLU   A 148 ? 0.3719 0.4619 0.3494 0.0213  -0.0004 -0.0053 148 GLU   A CD  
1058 O  OE1 . GLU   A 148 ? 0.3757 0.4757 0.3552 0.0205  0.0006  -0.0026 148 GLU   A OE1 
1059 O  OE2 . GLU   A 148 ? 0.4188 0.5038 0.3933 0.0234  -0.0018 -0.0091 148 GLU   A OE2 
1060 N  N   . ALA   A 149 ? 0.2173 0.3043 0.1980 0.0188  0.0003  -0.0050 149 ALA   A N   
1061 C  CA  . ALA   A 149 ? 0.2288 0.3139 0.2065 0.0228  -0.0013 -0.0089 149 ALA   A CA  
1062 C  C   . ALA   A 149 ? 0.1966 0.2731 0.1746 0.0212  -0.0011 -0.0086 149 ALA   A C   
1063 O  O   . ALA   A 149 ? 0.2029 0.2716 0.1776 0.0239  -0.0024 -0.0109 149 ALA   A O   
1064 C  CB  . ALA   A 149 ? 0.2352 0.3334 0.2130 0.0252  -0.0015 -0.0104 149 ALA   A CB  
1065 N  N   . LEU   A 150 ? 0.1880 0.2661 0.1697 0.0168  0.0004  -0.0060 150 LEU   A N   
1066 C  CA  . LEU   A 150 ? 0.1936 0.2647 0.1760 0.0151  0.0006  -0.0060 150 LEU   A CA  
1067 C  C   . LEU   A 150 ? 0.1793 0.2385 0.1607 0.0141  0.0005  -0.0052 150 LEU   A C   
1068 O  O   . LEU   A 150 ? 0.1777 0.2300 0.1575 0.0148  -0.0002 -0.0064 150 LEU   A O   
1069 C  CB  . LEU   A 150 ? 0.1984 0.2740 0.1851 0.0104  0.0023  -0.0039 150 LEU   A CB  
1070 C  CG  . LEU   A 150 ? 0.2229 0.3101 0.2107 0.0105  0.0025  -0.0052 150 LEU   A CG  
1071 C  CD1 . LEU   A 150 ? 0.2290 0.3196 0.2212 0.0046  0.0045  -0.0025 150 LEU   A CD1 
1072 C  CD2 . LEU   A 150 ? 0.2473 0.3331 0.2333 0.0132  0.0013  -0.0082 150 LEU   A CD2 
1073 N  N   . ILE   A 151 ? 0.1789 0.2365 0.1612 0.0125  0.0011  -0.0032 151 ILE   A N   
1074 C  CA  . ILE   A 151 ? 0.1682 0.2162 0.1496 0.0116  0.0009  -0.0027 151 ILE   A CA  
1075 C  C   . ILE   A 151 ? 0.1654 0.2079 0.1423 0.0149  -0.0007 -0.0057 151 ILE   A C   
1076 O  O   . ILE   A 151 ? 0.1696 0.2038 0.1448 0.0147  -0.0012 -0.0064 151 ILE   A O   
1077 C  CB  . ILE   A 151 ? 0.1642 0.2137 0.1473 0.0098  0.0019  0.0000  151 ILE   A CB  
1078 C  CG1 . ILE   A 151 ? 0.1612 0.2128 0.1481 0.0063  0.0037  0.0033  151 ILE   A CG1 
1079 C  CG2 . ILE   A 151 ? 0.1663 0.2083 0.1478 0.0096  0.0015  -0.0002 151 ILE   A CG2 
1080 C  CD1 . ILE   A 151 ? 0.1794 0.2337 0.1677 0.0052  0.0048  0.0067  151 ILE   A CD1 
1081 N  N   . ARG   A 152 ? 0.1700 0.2172 0.1447 0.0181  -0.0016 -0.0077 152 ARG   A N   
1082 C  CA  . ARG   A 152 ? 0.1846 0.2254 0.1546 0.0214  -0.0032 -0.0108 152 ARG   A CA  
1083 C  C   . ARG   A 152 ? 0.1808 0.2172 0.1486 0.0235  -0.0040 -0.0122 152 ARG   A C   
1084 O  O   . ARG   A 152 ? 0.1939 0.2208 0.1584 0.0243  -0.0048 -0.0132 152 ARG   A O   
1085 C  CB  . ARG   A 152 ? 0.1980 0.2451 0.1661 0.0250  -0.0041 -0.0133 152 ARG   A CB  
1086 C  CG  . ARG   A 152 ? 0.2200 0.2708 0.1892 0.0236  -0.0037 -0.0126 152 ARG   A CG  
1087 C  CD  . ARG   A 152 ? 0.2482 0.3039 0.2148 0.0276  -0.0049 -0.0160 152 ARG   A CD  
1088 N  NE  . ARG   A 152 ? 0.3037 0.3660 0.2721 0.0260  -0.0042 -0.0148 152 ARG   A NE  
1089 C  CZ  . ARG   A 152 ? 0.3353 0.3933 0.3030 0.0245  -0.0042 -0.0153 152 ARG   A CZ  
1090 N  NH1 . ARG   A 152 ? 0.3618 0.4087 0.3265 0.0242  -0.0050 -0.0174 152 ARG   A NH1 
1091 N  NH2 . ARG   A 152 ? 0.3714 0.4372 0.3412 0.0232  -0.0034 -0.0136 152 ARG   A NH2 
1092 N  N   . LYS   A 153 ? 0.1888 0.2327 0.1582 0.0244  -0.0038 -0.0122 153 LYS   A N   
1093 C  CA  . LYS   A 153 ? 0.2079 0.2501 0.1751 0.0272  -0.0046 -0.0136 153 LYS   A CA  
1094 C  C   . LYS   A 153 ? 0.1796 0.2140 0.1474 0.0244  -0.0041 -0.0122 153 LYS   A C   
1095 O  O   . LYS   A 153 ? 0.1880 0.2150 0.1521 0.0266  -0.0050 -0.0131 153 LYS   A O   
1096 C  CB  . LYS   A 153 ? 0.2256 0.2795 0.1949 0.0282  -0.0044 -0.0140 153 LYS   A CB  
1097 C  CG  . LYS   A 153 ? 0.2703 0.3244 0.2371 0.0320  -0.0054 -0.0158 153 LYS   A CG  
1098 C  CD  . LYS   A 153 ? 0.3173 0.3647 0.2780 0.0379  -0.0072 -0.0181 153 LYS   A CD  
1099 C  CE  . LYS   A 153 ? 0.3779 0.4326 0.3374 0.0417  -0.0079 -0.0203 153 LYS   A CE  
1100 N  NZ  . LYS   A 153 ? 0.4053 0.4524 0.3587 0.0478  -0.0097 -0.0229 153 LYS   A NZ  
1101 N  N   . ALA   A 154 ? 0.1764 0.2122 0.1485 0.0198  -0.0027 -0.0099 154 ALA   A N   
1102 C  CA  . ALA   A 154 ? 0.1641 0.1936 0.1371 0.0173  -0.0023 -0.0089 154 ALA   A CA  
1103 C  C   . ALA   A 154 ? 0.1675 0.1868 0.1373 0.0172  -0.0028 -0.0089 154 ALA   A C   
1104 O  O   . ALA   A 154 ? 0.1711 0.1842 0.1389 0.0173  -0.0032 -0.0090 154 ALA   A O   
1105 C  CB  . ALA   A 154 ? 0.1501 0.1823 0.1280 0.0128  -0.0007 -0.0068 154 ALA   A CB  
1106 N  N   . SER   A 155 ? 0.1683 0.1868 0.1378 0.0166  -0.0028 -0.0088 155 SER   A N   
1107 C  CA  . SER   A 155 ? 0.1740 0.1841 0.1405 0.0160  -0.0032 -0.0091 155 SER   A CA  
1108 C  C   . SER   A 155 ? 0.1889 0.1925 0.1501 0.0194  -0.0046 -0.0111 155 SER   A C   
1109 O  O   . SER   A 155 ? 0.1926 0.1880 0.1512 0.0185  -0.0048 -0.0109 155 SER   A O   
1110 C  CB  . SER   A 155 ? 0.1739 0.1866 0.1412 0.0150  -0.0030 -0.0090 155 SER   A CB  
1111 O  OG  . SER   A 155 ? 0.1622 0.1799 0.1340 0.0122  -0.0017 -0.0066 155 SER   A OG  
1112 N  N   . GLU   A 156 ? 0.1885 0.1956 0.1476 0.0234  -0.0055 -0.0130 156 GLU   A N   
1113 C  CA  . GLU   A 156 ? 0.2189 0.2192 0.1725 0.0276  -0.0069 -0.0149 156 GLU   A CA  
1114 C  C   . GLU   A 156 ? 0.2072 0.2036 0.1589 0.0288  -0.0071 -0.0141 156 GLU   A C   
1115 O  O   . GLU   A 156 ? 0.2220 0.2085 0.1693 0.0297  -0.0077 -0.0141 156 GLU   A O   
1116 C  CB  . GLU   A 156 ? 0.2559 0.2634 0.2086 0.0322  -0.0077 -0.0171 156 GLU   A CB  
1117 C  CG  . GLU   A 156 ? 0.3536 0.3549 0.3003 0.0378  -0.0092 -0.0194 156 GLU   A CG  
1118 C  CD  . GLU   A 156 ? 0.4387 0.4497 0.3850 0.0428  -0.0100 -0.0216 156 GLU   A CD  
1119 O  OE1 . GLU   A 156 ? 0.4177 0.4407 0.3686 0.0413  -0.0093 -0.0212 156 GLU   A OE1 
1120 O  OE2 . GLU   A 156 ? 0.5161 0.5227 0.4574 0.0484  -0.0114 -0.0238 156 GLU   A OE2 
1121 N  N   . ILE   A 157 ? 0.1978 0.2024 0.1529 0.0288  -0.0066 -0.0134 157 ILE   A N   
1122 C  CA  . ILE   A 157 ? 0.2041 0.2075 0.1579 0.0302  -0.0068 -0.0129 157 ILE   A CA  
1123 C  C   . ILE   A 157 ? 0.2056 0.2012 0.1593 0.0264  -0.0062 -0.0111 157 ILE   A C   
1124 O  O   . ILE   A 157 ? 0.1999 0.1887 0.1495 0.0280  -0.0068 -0.0107 157 ILE   A O   
1125 C  CB  . ILE   A 157 ? 0.2024 0.2173 0.1607 0.0297  -0.0062 -0.0129 157 ILE   A CB  
1126 C  CG1 . ILE   A 157 ? 0.2003 0.2240 0.1580 0.0340  -0.0069 -0.0148 157 ILE   A CG1 
1127 C  CG2 . ILE   A 157 ? 0.2054 0.2199 0.1634 0.0298  -0.0061 -0.0124 157 ILE   A CG2 
1128 C  CD1 . ILE   A 157 ? 0.1998 0.2361 0.1627 0.0320  -0.0059 -0.0148 157 ILE   A CD1 
1129 N  N   . SER   A 158 ? 0.1926 0.1897 0.1505 0.0217  -0.0051 -0.0100 158 SER   A N   
1130 C  CA  . SER   A 158 ? 0.1852 0.1768 0.1435 0.0181  -0.0045 -0.0086 158 SER   A CA  
1131 C  C   . SER   A 158 ? 0.1928 0.1742 0.1460 0.0181  -0.0051 -0.0086 158 SER   A C   
1132 O  O   . SER   A 158 ? 0.1925 0.1682 0.1432 0.0174  -0.0052 -0.0076 158 SER   A O   
1133 C  CB  . SER   A 158 ? 0.1811 0.1763 0.1444 0.0140  -0.0033 -0.0076 158 SER   A CB  
1134 O  OG  . SER   A 158 ? 0.1756 0.1787 0.1434 0.0134  -0.0026 -0.0074 158 SER   A OG  
1135 N  N   . ILE   A 159 ? 0.1988 0.1779 0.1503 0.0187  -0.0055 -0.0098 159 ILE   A N   
1136 C  CA  . ILE   A 159 ? 0.2102 0.1792 0.1568 0.0182  -0.0060 -0.0103 159 ILE   A CA  
1137 C  C   . ILE   A 159 ? 0.2176 0.1793 0.1584 0.0222  -0.0070 -0.0104 159 ILE   A C   
1138 O  O   . ILE   A 159 ? 0.2239 0.1767 0.1609 0.0208  -0.0071 -0.0093 159 ILE   A O   
1139 C  CB  . ILE   A 159 ? 0.2133 0.1829 0.1596 0.0182  -0.0063 -0.0122 159 ILE   A CB  
1140 C  CG1 . ILE   A 159 ? 0.2109 0.1860 0.1620 0.0138  -0.0053 -0.0114 159 ILE   A CG1 
1141 C  CG2 . ILE   A 159 ? 0.2216 0.1801 0.1620 0.0186  -0.0071 -0.0136 159 ILE   A CG2 
1142 C  CD1 . ILE   A 159 ? 0.2276 0.2073 0.1797 0.0143  -0.0054 -0.0131 159 ILE   A CD1 
1143 N  N   . LYS   A 160 ? 0.2216 0.1874 0.1614 0.0273  -0.0078 -0.0117 160 LYS   A N   
1144 C  CA  . LYS   A 160 ? 0.2428 0.2022 0.1768 0.0323  -0.0089 -0.0117 160 LYS   A CA  
1145 C  C   . LYS   A 160 ? 0.2500 0.2081 0.1834 0.0316  -0.0085 -0.0093 160 LYS   A C   
1146 O  O   . LYS   A 160 ? 0.2468 0.1958 0.1746 0.0337  -0.0090 -0.0082 160 LYS   A O   
1147 C  CB  . LYS   A 160 ? 0.2664 0.2332 0.2001 0.0382  -0.0098 -0.0135 160 LYS   A CB  
1148 C  CG  . LYS   A 160 ? 0.3060 0.2718 0.2382 0.0403  -0.0105 -0.0161 160 LYS   A CG  
1149 C  CD  . LYS   A 160 ? 0.3554 0.3301 0.2874 0.0463  -0.0114 -0.0181 160 LYS   A CD  
1150 C  CE  . LYS   A 160 ? 0.4340 0.4064 0.3633 0.0494  -0.0124 -0.0212 160 LYS   A CE  
1151 N  NZ  . LYS   A 160 ? 0.4778 0.4627 0.4087 0.0541  -0.0129 -0.0231 160 LYS   A NZ  
1152 N  N   . ALA   A 161 ? 0.2335 0.2006 0.1725 0.0289  -0.0076 -0.0085 161 ALA   A N   
1153 C  CA  . ALA   A 161 ? 0.2437 0.2113 0.1827 0.0282  -0.0073 -0.0067 161 ALA   A CA  
1154 C  C   . ALA   A 161 ? 0.2735 0.2342 0.2117 0.0234  -0.0066 -0.0049 161 ALA   A C   
1155 O  O   . ALA   A 161 ? 0.2571 0.2179 0.1947 0.0227  -0.0063 -0.0034 161 ALA   A O   
1156 C  CB  . ALA   A 161 ? 0.2316 0.2110 0.1767 0.0271  -0.0067 -0.0072 161 ALA   A CB  
1157 N  N   . GLY   A 162 ? 0.2398 0.1962 0.1782 0.0198  -0.0063 -0.0053 162 GLY   A N   
1158 C  CA  . GLY   A 162 ? 0.2489 0.1989 0.1858 0.0153  -0.0057 -0.0039 162 GLY   A CA  
1159 C  C   . GLY   A 162 ? 0.2291 0.1852 0.1718 0.0104  -0.0046 -0.0038 162 GLY   A C   
1160 O  O   . GLY   A 162 ? 0.2408 0.1943 0.1830 0.0067  -0.0041 -0.0027 162 GLY   A O   
1161 N  N   . ALA   A 163 ? 0.2163 0.1803 0.1640 0.0104  -0.0043 -0.0049 163 ALA   A N   
1162 C  CA  . ALA   A 163 ? 0.2022 0.1708 0.1546 0.0064  -0.0034 -0.0047 163 ALA   A CA  
1163 C  C   . ALA   A 163 ? 0.2049 0.1685 0.1554 0.0030  -0.0032 -0.0047 163 ALA   A C   
1164 O  O   . ALA   A 163 ? 0.2157 0.1747 0.1632 0.0035  -0.0037 -0.0059 163 ALA   A O   
1165 C  CB  . ALA   A 163 ? 0.2019 0.1777 0.1588 0.0072  -0.0031 -0.0056 163 ALA   A CB  
1166 N  N   . ASP   A 164 ? 0.1934 0.1589 0.1461 -0.0006 -0.0024 -0.0039 164 ASP   A N   
1167 C  CA  . ASP   A 164 ? 0.2031 0.1665 0.1547 -0.0044 -0.0021 -0.0041 164 ASP   A CA  
1168 C  C   . ASP   A 164 ? 0.1861 0.1559 0.1418 -0.0052 -0.0017 -0.0050 164 ASP   A C   
1169 O  O   . ASP   A 164 ? 0.2022 0.1716 0.1571 -0.0076 -0.0016 -0.0058 164 ASP   A O   
1170 C  CB  . ASP   A 164 ? 0.2021 0.1656 0.1537 -0.0077 -0.0015 -0.0029 164 ASP   A CB  
1171 C  CG  . ASP   A 164 ? 0.2243 0.1817 0.1713 -0.0070 -0.0018 -0.0015 164 ASP   A CG  
1172 O  OD1 . ASP   A 164 ? 0.2416 0.1907 0.1834 -0.0063 -0.0023 -0.0015 164 ASP   A OD1 
1173 O  OD2 . ASP   A 164 ? 0.2286 0.1895 0.1771 -0.0070 -0.0015 -0.0005 164 ASP   A OD2 
1174 N  N   . PHE   A 165 ? 0.1773 0.1534 0.1374 -0.0035 -0.0014 -0.0046 165 PHE   A N   
1175 C  CA  . PHE   A 165 ? 0.1757 0.1579 0.1397 -0.0034 -0.0010 -0.0047 165 PHE   A CA  
1176 C  C   . PHE   A 165 ? 0.1634 0.1494 0.1299 -0.0005 -0.0010 -0.0045 165 PHE   A C   
1177 O  O   . PHE   A 165 ? 0.1512 0.1371 0.1181 0.0006  -0.0010 -0.0043 165 PHE   A O   
1178 C  CB  . PHE   A 165 ? 0.1729 0.1598 0.1407 -0.0052 -0.0001 -0.0038 165 PHE   A CB  
1179 C  CG  . PHE   A 165 ? 0.1892 0.1774 0.1566 -0.0080 0.0002  -0.0040 165 PHE   A CG  
1180 C  CD1 . PHE   A 165 ? 0.2252 0.2104 0.1900 -0.0106 0.0001  -0.0042 165 PHE   A CD1 
1181 C  CD2 . PHE   A 165 ? 0.1947 0.1884 0.1645 -0.0079 0.0005  -0.0039 165 PHE   A CD2 
1182 C  CE1 . PHE   A 165 ? 0.2258 0.2140 0.1906 -0.0135 0.0005  -0.0046 165 PHE   A CE1 
1183 C  CE2 . PHE   A 165 ? 0.2178 0.2143 0.1873 -0.0103 0.0008  -0.0044 165 PHE   A CE2 
1184 C  CZ  . PHE   A 165 ? 0.2203 0.2143 0.1874 -0.0133 0.0007  -0.0049 165 PHE   A CZ  
1185 N  N   . ILE   A 166 ? 0.1575 0.1475 0.1255 0.0003  -0.0009 -0.0047 166 ILE   A N   
1186 C  CA  . ILE   A 166 ? 0.1576 0.1527 0.1288 0.0020  -0.0005 -0.0040 166 ILE   A CA  
1187 C  C   . ILE   A 166 ? 0.1638 0.1634 0.1389 0.0007  0.0005  -0.0025 166 ILE   A C   
1188 O  O   . ILE   A 166 ? 0.1563 0.1572 0.1313 -0.0002 0.0006  -0.0024 166 ILE   A O   
1189 C  CB  . ILE   A 166 ? 0.1660 0.1626 0.1355 0.0046  -0.0012 -0.0052 166 ILE   A CB  
1190 C  CG1 . ILE   A 166 ? 0.1750 0.1722 0.1430 0.0045  -0.0015 -0.0061 166 ILE   A CG1 
1191 C  CG2 . ILE   A 166 ? 0.1872 0.1792 0.1530 0.0068  -0.0021 -0.0063 166 ILE   A CG2 
1192 C  CD1 . ILE   A 166 ? 0.1800 0.1804 0.1469 0.0074  -0.0021 -0.0075 166 ILE   A CD1 
1193 N  N   . LYS   A 167 ? 0.1509 0.1527 0.1294 0.0006  0.0012  -0.0014 167 LYS   A N   
1194 C  CA  . LYS   A 167 ? 0.1549 0.1590 0.1368 -0.0003 0.0022  0.0002  167 LYS   A CA  
1195 C  C   . LYS   A 167 ? 0.1490 0.1569 0.1335 0.0002  0.0029  0.0016  167 LYS   A C   
1196 O  O   . LYS   A 167 ? 0.1470 0.1557 0.1320 0.0005  0.0028  0.0010  167 LYS   A O   
1197 C  CB  . LYS   A 167 ? 0.1629 0.1645 0.1459 -0.0015 0.0024  0.0000  167 LYS   A CB  
1198 C  CG  . LYS   A 167 ? 0.1775 0.1802 0.1641 -0.0019 0.0034  0.0013  167 LYS   A CG  
1199 C  CD  . LYS   A 167 ? 0.1854 0.1862 0.1725 -0.0028 0.0034  0.0003  167 LYS   A CD  
1200 C  CE  . LYS   A 167 ? 0.1993 0.2003 0.1898 -0.0027 0.0043  0.0012  167 LYS   A CE  
1201 N  NZ  . LYS   A 167 ? 0.2248 0.2246 0.2163 -0.0031 0.0044  0.0000  167 LYS   A NZ  
1202 N  N   . THR   A 168 ? 0.1498 0.1604 0.1361 0.0002  0.0037  0.0036  168 THR   A N   
1203 C  CA  . THR   A 168 ? 0.1480 0.1624 0.1363 0.0004  0.0044  0.0053  168 THR   A CA  
1204 C  C   . THR   A 168 ? 0.1423 0.1553 0.1333 -0.0010 0.0052  0.0057  168 THR   A C   
1205 O  O   . THR   A 168 ? 0.1519 0.1677 0.1438 -0.0014 0.0055  0.0057  168 THR   A O   
1206 C  CB  . THR   A 168 ? 0.1478 0.1654 0.1372 0.0008  0.0052  0.0079  168 THR   A CB  
1207 O  OG1 . THR   A 168 ? 0.1452 0.1600 0.1361 0.0004  0.0059  0.0093  168 THR   A OG1 
1208 C  CG2 . THR   A 168 ? 0.1445 0.1648 0.1313 0.0019  0.0044  0.0070  168 THR   A CG2 
1209 N  N   . SER   A 169 ? 0.1499 0.1593 0.1425 -0.0018 0.0057  0.0060  169 SER   A N   
1210 C  CA  . SER   A 169 ? 0.1423 0.1502 0.1379 -0.0033 0.0068  0.0070  169 SER   A CA  
1211 C  C   . SER   A 169 ? 0.1569 0.1606 0.1535 -0.0039 0.0068  0.0054  169 SER   A C   
1212 O  O   . SER   A 169 ? 0.1615 0.1638 0.1568 -0.0031 0.0062  0.0046  169 SER   A O   
1213 C  CB  . SER   A 169 ? 0.1548 0.1628 0.1516 -0.0031 0.0079  0.0104  169 SER   A CB  
1214 O  OG  . SER   A 169 ? 0.1468 0.1599 0.1425 -0.0022 0.0079  0.0119  169 SER   A OG  
1215 N  N   . THR   A 170 ? 0.1581 0.1602 0.1572 -0.0056 0.0077  0.0050  170 THR   A N   
1216 C  CA  . THR   A 170 ? 0.1586 0.1570 0.1592 -0.0061 0.0078  0.0033  170 THR   A CA  
1217 C  C   . THR   A 170 ? 0.1853 0.1800 0.1871 -0.0054 0.0086  0.0053  170 THR   A C   
1218 O  O   . THR   A 170 ? 0.1904 0.1824 0.1928 -0.0048 0.0085  0.0038  170 THR   A O   
1219 C  CB  . THR   A 170 ? 0.1620 0.1604 0.1649 -0.0084 0.0083  0.0015  170 THR   A CB  
1220 O  OG1 . THR   A 170 ? 0.1627 0.1607 0.1674 -0.0101 0.0096  0.0037  170 THR   A OG1 
1221 C  CG2 . THR   A 170 ? 0.1579 0.1607 0.1595 -0.0084 0.0074  -0.0007 170 THR   A CG2 
1222 N  N   . GLY   A 171 ? 0.1862 0.1809 0.1883 -0.0051 0.0095  0.0086  171 GLY   A N   
1223 C  CA  . GLY   A 171 ? 0.2153 0.2056 0.2184 -0.0041 0.0104  0.0108  171 GLY   A CA  
1224 C  C   . GLY   A 171 ? 0.2469 0.2320 0.2524 -0.0064 0.0116  0.0106  171 GLY   A C   
1225 O  O   . GLY   A 171 ? 0.2827 0.2624 0.2889 -0.0054 0.0124  0.0124  171 GLY   A O   
1226 N  N   . ARG   A 172 ? 0.2254 0.2121 0.2321 -0.0092 0.0117  0.0085  172 ARG   A N   
1227 C  CA  . ARG   A 172 ? 0.2739 0.2561 0.2831 -0.0121 0.0128  0.0073  172 ARG   A CA  
1228 C  C   . ARG   A 172 ? 0.2802 0.2640 0.2904 -0.0154 0.0140  0.0093  172 ARG   A C   
1229 O  O   . ARG   A 172 ? 0.2894 0.2702 0.3016 -0.0187 0.0150  0.0081  172 ARG   A O   
1230 C  CB  . ARG   A 172 ? 0.2816 0.2652 0.2917 -0.0133 0.0120  0.0025  172 ARG   A CB  
1231 C  CG  . ARG   A 172 ? 0.3013 0.2836 0.3107 -0.0107 0.0110  0.0004  172 ARG   A CG  
1232 C  CD  . ARG   A 172 ? 0.3837 0.3589 0.3944 -0.0098 0.0118  0.0007  172 ARG   A CD  
1233 N  NE  . ARG   A 172 ? 0.4601 0.4355 0.4701 -0.0071 0.0108  -0.0015 172 ARG   A NE  
1234 C  CZ  . ARG   A 172 ? 0.5594 0.5355 0.5705 -0.0077 0.0103  -0.0057 172 ARG   A CZ  
1235 N  NH1 . ARG   A 172 ? 0.5589 0.5348 0.5719 -0.0107 0.0108  -0.0083 172 ARG   A NH1 
1236 N  NH2 . ARG   A 172 ? 0.5903 0.5680 0.6006 -0.0053 0.0095  -0.0073 172 ARG   A NH2 
1237 N  N   . VAL   A 173 ? 0.2410 0.2300 0.2497 -0.0146 0.0139  0.0121  173 VAL   A N   
1238 C  CA  . VAL   A 173 ? 0.2542 0.2462 0.2637 -0.0175 0.0151  0.0144  173 VAL   A CA  
1239 C  C   . VAL   A 173 ? 0.2615 0.2517 0.2700 -0.0162 0.0160  0.0196  173 VAL   A C   
1240 O  O   . VAL   A 173 ? 0.2554 0.2433 0.2626 -0.0128 0.0155  0.0210  173 VAL   A O   
1241 C  CB  . VAL   A 173 ? 0.2375 0.2389 0.2462 -0.0176 0.0141  0.0128  173 VAL   A CB  
1242 C  CG1 . VAL   A 173 ? 0.2527 0.2561 0.2624 -0.0190 0.0134  0.0080  173 VAL   A CG1 
1243 C  CG2 . VAL   A 173 ? 0.2213 0.2264 0.2273 -0.0137 0.0128  0.0134  173 VAL   A CG2 
1244 N  N   . ALA   A 174 ? 0.2642 0.2566 0.2733 -0.0191 0.0174  0.0226  174 ALA   A N   
1245 C  CA  . ALA   A 174 ? 0.2740 0.2643 0.2820 -0.0182 0.0186  0.0282  174 ALA   A CA  
1246 C  C   . ALA   A 174 ? 0.2528 0.2494 0.2586 -0.0140 0.0175  0.0299  174 ALA   A C   
1247 O  O   . ALA   A 174 ? 0.2427 0.2368 0.2473 -0.0112 0.0178  0.0333  174 ALA   A O   
1248 C  CB  . ALA   A 174 ? 0.2789 0.2719 0.2879 -0.0227 0.0203  0.0310  174 ALA   A CB  
1249 N  N   . VAL   A 175 ? 0.2149 0.2199 0.2200 -0.0134 0.0162  0.0272  175 VAL   A N   
1250 C  CA  . VAL   A 175 ? 0.2049 0.2162 0.2079 -0.0100 0.0153  0.0282  175 VAL   A CA  
1251 C  C   . VAL   A 175 ? 0.1938 0.2058 0.1956 -0.0078 0.0134  0.0238  175 VAL   A C   
1252 O  O   . VAL   A 175 ? 0.1866 0.2003 0.1887 -0.0089 0.0127  0.0203  175 VAL   A O   
1253 C  CB  . VAL   A 175 ? 0.2383 0.2590 0.2409 -0.0109 0.0155  0.0295  175 VAL   A CB  
1254 C  CG1 . VAL   A 175 ? 0.2282 0.2556 0.2286 -0.0073 0.0144  0.0297  175 VAL   A CG1 
1255 C  CG2 . VAL   A 175 ? 0.2564 0.2769 0.2599 -0.0137 0.0175  0.0344  175 VAL   A CG2 
1256 N  N   . ASN   A 176 ? 0.1899 0.2010 0.1903 -0.0048 0.0127  0.0242  176 ASN   A N   
1257 C  CA  . ASN   A 176 ? 0.1892 0.2007 0.1883 -0.0031 0.0111  0.0205  176 ASN   A CA  
1258 C  C   . ASN   A 176 ? 0.1810 0.1993 0.1780 -0.0011 0.0103  0.0206  176 ASN   A C   
1259 O  O   . ASN   A 176 ? 0.1883 0.2120 0.1851 -0.0015 0.0105  0.0215  176 ASN   A O   
1260 C  CB  . ASN   A 176 ? 0.2067 0.2122 0.2062 -0.0021 0.0111  0.0200  176 ASN   A CB  
1261 C  CG  . ASN   A 176 ? 0.2485 0.2480 0.2501 -0.0044 0.0118  0.0189  176 ASN   A CG  
1262 O  OD1 . ASN   A 176 ? 0.2415 0.2410 0.2436 -0.0058 0.0112  0.0155  176 ASN   A OD1 
1263 N  ND2 . ASN   A 176 ? 0.2766 0.2712 0.2794 -0.0047 0.0132  0.0218  176 ASN   A ND2 
1264 N  N   . ALA   A 177 ? 0.1567 0.1754 0.1522 0.0008  0.0094  0.0195  177 ALA   A N   
1265 C  CA  . ALA   A 177 ? 0.1576 0.1824 0.1510 0.0022  0.0085  0.0186  177 ALA   A CA  
1266 C  C   . ALA   A 177 ? 0.1530 0.1835 0.1465 0.0033  0.0093  0.0223  177 ALA   A C   
1267 O  O   . ALA   A 177 ? 0.1659 0.1946 0.1603 0.0038  0.0105  0.0259  177 ALA   A O   
1268 C  CB  . ALA   A 177 ? 0.1512 0.1757 0.1432 0.0033  0.0076  0.0167  177 ALA   A CB  
1269 N  N   . THR   A 178 ? 0.1583 0.1955 0.1505 0.0040  0.0087  0.0213  178 THR   A N   
1270 C  CA  . THR   A 178 ? 0.1682 0.2127 0.1598 0.0056  0.0091  0.0239  178 THR   A CA  
1271 C  C   . THR   A 178 ? 0.1567 0.2059 0.1461 0.0070  0.0077  0.0204  178 THR   A C   
1272 O  O   . THR   A 178 ? 0.1619 0.2084 0.1503 0.0064  0.0066  0.0164  178 THR   A O   
1273 C  CB  . THR   A 178 ? 0.1763 0.2261 0.1686 0.0048  0.0099  0.0262  178 THR   A CB  
1274 O  OG1 . THR   A 178 ? 0.1695 0.2228 0.1608 0.0048  0.0088  0.0223  178 THR   A OG1 
1275 C  CG2 . THR   A 178 ? 0.1976 0.2421 0.1919 0.0024  0.0113  0.0289  178 THR   A CG2 
1276 N  N   . PRO   A 179 ? 0.1624 0.2188 0.1511 0.0087  0.0077  0.0218  179 PRO   A N   
1277 C  CA  . PRO   A 179 ? 0.1653 0.2267 0.1520 0.0096  0.0065  0.0180  179 PRO   A CA  
1278 C  C   . PRO   A 179 ? 0.1642 0.2274 0.1499 0.0094  0.0056  0.0148  179 PRO   A C   
1279 O  O   . PRO   A 179 ? 0.1700 0.2318 0.1538 0.0094  0.0043  0.0104  179 PRO   A O   
1280 C  CB  . PRO   A 179 ? 0.1733 0.2438 0.1599 0.0116  0.0070  0.0207  179 PRO   A CB  
1281 C  CG  . PRO   A 179 ? 0.1913 0.2586 0.1793 0.0121  0.0083  0.0257  179 PRO   A CG  
1282 C  CD  . PRO   A 179 ? 0.1718 0.2314 0.1613 0.0101  0.0090  0.0269  179 PRO   A CD  
1283 N  N   . GLU   A 180 ? 0.1611 0.2277 0.1477 0.0094  0.0063  0.0169  180 GLU   A N   
1284 C  CA  A GLU   A 180 ? 0.1679 0.2378 0.1535 0.0099  0.0054  0.0138  180 GLU   A CA  
1285 C  CA  B GLU   A 180 ? 0.1649 0.2347 0.1506 0.0099  0.0055  0.0140  180 GLU   A CA  
1286 C  C   . GLU   A 180 ? 0.1644 0.2259 0.1494 0.0090  0.0046  0.0107  180 GLU   A C   
1287 O  O   . GLU   A 180 ? 0.1638 0.2246 0.1467 0.0100  0.0033  0.0066  180 GLU   A O   
1288 C  CB  A GLU   A 180 ? 0.1844 0.2624 0.1712 0.0101  0.0063  0.0166  180 GLU   A CB  
1289 C  CB  B GLU   A 180 ? 0.1768 0.2528 0.1641 0.0095  0.0066  0.0174  180 GLU   A CB  
1290 C  CG  A GLU   A 180 ? 0.2036 0.2909 0.1903 0.0115  0.0069  0.0195  180 GLU   A CG  
1291 C  CG  B GLU   A 180 ? 0.1869 0.2683 0.1732 0.0105  0.0057  0.0142  180 GLU   A CG  
1292 C  CD  A GLU   A 180 ? 0.2243 0.3176 0.2090 0.0136  0.0056  0.0158  180 GLU   A CD  
1293 C  CD  B GLU   A 180 ? 0.2033 0.2926 0.1876 0.0130  0.0047  0.0114  180 GLU   A CD  
1294 O  OE1 A GLU   A 180 ? 0.2436 0.3383 0.2268 0.0145  0.0044  0.0112  180 GLU   A OE1 
1295 O  OE1 B GLU   A 180 ? 0.2148 0.3053 0.1984 0.0137  0.0044  0.0112  180 GLU   A OE1 
1296 O  OE2 A GLU   A 180 ? 0.2363 0.3330 0.2209 0.0144  0.0059  0.0173  180 GLU   A OE2 
1297 O  OE2 B GLU   A 180 ? 0.2105 0.3051 0.1939 0.0145  0.0039  0.0089  180 GLU   A OE2 
1298 N  N   . SER   A 181 ? 0.1680 0.2231 0.1547 0.0072  0.0054  0.0124  181 SER   A N   
1299 C  CA  . SER   A 181 ? 0.1730 0.2215 0.1589 0.0066  0.0046  0.0094  181 SER   A CA  
1300 C  C   . SER   A 181 ? 0.1645 0.2074 0.1483 0.0068  0.0035  0.0065  181 SER   A C   
1301 O  O   . SER   A 181 ? 0.1662 0.2055 0.1478 0.0073  0.0024  0.0032  181 SER   A O   
1302 C  CB  . SER   A 181 ? 0.1905 0.2348 0.1788 0.0046  0.0056  0.0113  181 SER   A CB  
1303 O  OG  . SER   A 181 ? 0.2450 0.2851 0.2346 0.0036  0.0064  0.0137  181 SER   A OG  
1304 N  N   . ALA   A 182 ? 0.1654 0.2081 0.1494 0.0065  0.0038  0.0075  182 ALA   A N   
1305 C  CA  . ALA   A 182 ? 0.1679 0.2070 0.1498 0.0060  0.0029  0.0047  182 ALA   A CA  
1306 C  C   . ALA   A 182 ? 0.1758 0.2173 0.1550 0.0071  0.0017  0.0012  182 ALA   A C   
1307 O  O   . ALA   A 182 ? 0.1773 0.2130 0.1540 0.0066  0.0008  -0.0019 182 ALA   A O   
1308 C  CB  . ALA   A 182 ? 0.1711 0.2122 0.1540 0.0057  0.0035  0.0065  182 ALA   A CB  
1309 N  N   . ARG   A 183 ? 0.1734 0.2232 0.1528 0.0085  0.0018  0.0016  183 ARG   A N   
1310 C  CA  . ARG   A 183 ? 0.1876 0.2404 0.1645 0.0098  0.0007  -0.0021 183 ARG   A CA  
1311 C  C   . ARG   A 183 ? 0.1775 0.2261 0.1525 0.0110  -0.0002 -0.0048 183 ARG   A C   
1312 O  O   . ARG   A 183 ? 0.1787 0.2224 0.1506 0.0114  -0.0014 -0.0086 183 ARG   A O   
1313 C  CB  . ARG   A 183 ? 0.2214 0.2854 0.1992 0.0115  0.0010  -0.0010 183 ARG   A CB  
1314 C  CG  . ARG   A 183 ? 0.2750 0.3429 0.2503 0.0131  -0.0002 -0.0055 183 ARG   A CG  
1315 C  CD  . ARG   A 183 ? 0.3378 0.4181 0.3140 0.0150  0.0002  -0.0042 183 ARG   A CD  
1316 N  NE  . ARG   A 183 ? 0.4488 0.5328 0.4268 0.0157  0.0009  -0.0010 183 ARG   A NE  
1317 C  CZ  . ARG   A 183 ? 0.4846 0.5696 0.4618 0.0172  0.0003  -0.0029 183 ARG   A CZ  
1318 N  NH1 . ARG   A 183 ? 0.5350 0.6166 0.5093 0.0189  -0.0012 -0.0080 183 ARG   A NH1 
1319 N  NH2 . ARG   A 183 ? 0.4963 0.5859 0.4754 0.0172  0.0012  0.0003  183 ARG   A NH2 
1320 N  N   . ILE   A 184 ? 0.1764 0.2267 0.1531 0.0116  0.0003  -0.0027 184 ILE   A N   
1321 C  CA  . ILE   A 184 ? 0.1690 0.2173 0.1440 0.0133  -0.0006 -0.0051 184 ILE   A CA  
1322 C  C   . ILE   A 184 ? 0.1704 0.2080 0.1432 0.0127  -0.0013 -0.0070 184 ILE   A C   
1323 O  O   . ILE   A 184 ? 0.1736 0.2069 0.1430 0.0145  -0.0025 -0.0102 184 ILE   A O   
1324 C  CB  . ILE   A 184 ? 0.1720 0.2250 0.1495 0.0133  0.0003  -0.0025 184 ILE   A CB  
1325 C  CG1 . ILE   A 184 ? 0.1815 0.2455 0.1606 0.0140  0.0010  -0.0006 184 ILE   A CG1 
1326 C  CG2 . ILE   A 184 ? 0.1794 0.2303 0.1553 0.0151  -0.0006 -0.0049 184 ILE   A CG2 
1327 C  CD1 . ILE   A 184 ? 0.1783 0.2465 0.1605 0.0123  0.0025  0.0034  184 ILE   A CD1 
1328 N  N   . MET   A 185 ? 0.1659 0.1989 0.1403 0.0103  -0.0005 -0.0048 185 MET   A N   
1329 C  CA  . MET   A 185 ? 0.1633 0.1871 0.1356 0.0096  -0.0011 -0.0061 185 MET   A CA  
1330 C  C   . MET   A 185 ? 0.1654 0.1841 0.1344 0.0090  -0.0019 -0.0088 185 MET   A C   
1331 O  O   . MET   A 185 ? 0.1703 0.1817 0.1359 0.0096  -0.0028 -0.0109 185 MET   A O   
1332 C  CB  . MET   A 185 ? 0.1591 0.1802 0.1341 0.0073  -0.0001 -0.0036 185 MET   A CB  
1333 C  CG  . MET   A 185 ? 0.1532 0.1774 0.1309 0.0073  0.0006  -0.0017 185 MET   A CG  
1334 S  SD  . MET   A 185 ? 0.1653 0.1863 0.1463 0.0048  0.0018  0.0009  185 MET   A SD  
1335 C  CE  . MET   A 185 ? 0.1543 0.1673 0.1327 0.0043  0.0010  -0.0012 185 MET   A CE  
1336 N  N   . MET   A 186 ? 0.1656 0.1879 0.1352 0.0077  -0.0016 -0.0088 186 MET   A N   
1337 C  CA  . MET   A 186 ? 0.1759 0.1940 0.1425 0.0063  -0.0023 -0.0117 186 MET   A CA  
1338 C  C   . MET   A 186 ? 0.1900 0.2076 0.1535 0.0086  -0.0034 -0.0153 186 MET   A C   
1339 O  O   . MET   A 186 ? 0.2039 0.2136 0.1636 0.0081  -0.0042 -0.0181 186 MET   A O   
1340 C  CB  . MET   A 186 ? 0.1742 0.1978 0.1426 0.0043  -0.0017 -0.0109 186 MET   A CB  
1341 C  CG  . MET   A 186 ? 0.1910 0.2121 0.1610 0.0019  -0.0009 -0.0086 186 MET   A CG  
1342 S  SD  . MET   A 186 ? 0.2190 0.2472 0.1905 0.0001  -0.0003 -0.0082 186 MET   A SD  
1343 C  CE  . MET   A 186 ? 0.2130 0.2494 0.1883 0.0026  0.0007  -0.0039 186 MET   A CE  
1344 N  N   . GLU   A 187 ? 0.2012 0.2266 0.1658 0.0113  -0.0035 -0.0153 187 GLU   A N   
1345 C  CA  . GLU   A 187 ? 0.2160 0.2414 0.1776 0.0143  -0.0047 -0.0190 187 GLU   A CA  
1346 C  C   . GLU   A 187 ? 0.2165 0.2329 0.1750 0.0163  -0.0056 -0.0203 187 GLU   A C   
1347 O  O   . GLU   A 187 ? 0.2170 0.2273 0.1714 0.0179  -0.0067 -0.0238 187 GLU   A O   
1348 C  CB  . GLU   A 187 ? 0.2381 0.2752 0.2017 0.0170  -0.0046 -0.0186 187 GLU   A CB  
1349 C  CG  . GLU   A 187 ? 0.2756 0.3220 0.2411 0.0161  -0.0041 -0.0182 187 GLU   A CG  
1350 C  CD  . GLU   A 187 ? 0.3314 0.3899 0.2987 0.0186  -0.0038 -0.0172 187 GLU   A CD  
1351 O  OE1 . GLU   A 187 ? 0.3833 0.4437 0.3507 0.0208  -0.0040 -0.0169 187 GLU   A OE1 
1352 O  OE2 . GLU   A 187 ? 0.3377 0.4048 0.3063 0.0183  -0.0034 -0.0166 187 GLU   A OE2 
1353 N  N   . VAL   A 188 ? 0.1996 0.2150 0.1597 0.0164  -0.0050 -0.0175 188 VAL   A N   
1354 C  CA  . VAL   A 188 ? 0.2086 0.2162 0.1655 0.0185  -0.0058 -0.0184 188 VAL   A CA  
1355 C  C   . VAL   A 188 ? 0.2132 0.2090 0.1664 0.0166  -0.0063 -0.0196 188 VAL   A C   
1356 O  O   . VAL   A 188 ? 0.2189 0.2067 0.1675 0.0188  -0.0073 -0.0219 188 VAL   A O   
1357 C  CB  . VAL   A 188 ? 0.2151 0.2249 0.1747 0.0186  -0.0052 -0.0155 188 VAL   A CB  
1358 C  CG1 . VAL   A 188 ? 0.2208 0.2230 0.1768 0.0210  -0.0060 -0.0164 188 VAL   A CG1 
1359 C  CG2 . VAL   A 188 ? 0.1996 0.2206 0.1624 0.0201  -0.0047 -0.0146 188 VAL   A CG2 
1360 N  N   . ILE   A 189 ? 0.1979 0.1922 0.1528 0.0124  -0.0054 -0.0178 189 ILE   A N   
1361 C  CA  . ILE   A 189 ? 0.2020 0.1863 0.1535 0.0096  -0.0055 -0.0186 189 ILE   A CA  
1362 C  C   . ILE   A 189 ? 0.2237 0.2037 0.1714 0.0098  -0.0064 -0.0225 189 ILE   A C   
1363 O  O   . ILE   A 189 ? 0.2318 0.2009 0.1747 0.0101  -0.0071 -0.0241 189 ILE   A O   
1364 C  CB  . ILE   A 189 ? 0.2009 0.1875 0.1553 0.0051  -0.0045 -0.0166 189 ILE   A CB  
1365 C  CG1 . ILE   A 189 ? 0.1953 0.1836 0.1528 0.0050  -0.0037 -0.0133 189 ILE   A CG1 
1366 C  CG2 . ILE   A 189 ? 0.2331 0.2115 0.1842 0.0014  -0.0045 -0.0178 189 ILE   A CG2 
1367 C  CD1 . ILE   A 189 ? 0.1948 0.1866 0.1555 0.0016  -0.0027 -0.0114 189 ILE   A CD1 
1368 N  N   . ARG   A 190 ? 0.2381 0.2264 0.1878 0.0096  -0.0063 -0.0240 190 ARG   A N   
1369 C  CA  . ARG   A 190 ? 0.2536 0.2394 0.2001 0.0096  -0.0071 -0.0283 190 ARG   A CA  
1370 C  C   . ARG   A 190 ? 0.2712 0.2517 0.2137 0.0146  -0.0084 -0.0310 190 ARG   A C   
1371 O  O   . ARG   A 190 ? 0.2932 0.2629 0.2309 0.0145  -0.0092 -0.0339 190 ARG   A O   
1372 C  CB  . ARG   A 190 ? 0.2561 0.2543 0.2058 0.0093  -0.0068 -0.0293 190 ARG   A CB  
1373 C  CG  . ARG   A 190 ? 0.2688 0.2656 0.2157 0.0085  -0.0076 -0.0343 190 ARG   A CG  
1374 C  CD  . ARG   A 190 ? 0.3019 0.3126 0.2516 0.0101  -0.0075 -0.0354 190 ARG   A CD  
1375 N  NE  . ARG   A 190 ? 0.3476 0.3639 0.2982 0.0151  -0.0080 -0.0347 190 ARG   A NE  
1376 C  CZ  . ARG   A 190 ? 0.3677 0.3970 0.3211 0.0170  -0.0078 -0.0343 190 ARG   A CZ  
1377 N  NH1 . ARG   A 190 ? 0.3377 0.3753 0.2928 0.0150  -0.0074 -0.0351 190 ARG   A NH1 
1378 N  NH2 . ARG   A 190 ? 0.3715 0.4066 0.3260 0.0209  -0.0079 -0.0331 190 ARG   A NH2 
1379 N  N   . ASP   A 191 ? 0.2765 0.2649 0.2210 0.0188  -0.0086 -0.0302 191 ASP   A N   
1380 C  CA  . ASP   A 191 ? 0.2915 0.2782 0.2328 0.0243  -0.0099 -0.0330 191 ASP   A CA  
1381 C  C   . ASP   A 191 ? 0.2968 0.2703 0.2334 0.0261  -0.0105 -0.0328 191 ASP   A C   
1382 O  O   . ASP   A 191 ? 0.3017 0.2681 0.2335 0.0299  -0.0117 -0.0360 191 ASP   A O   
1383 C  CB  . ASP   A 191 ? 0.3075 0.3068 0.2521 0.0279  -0.0098 -0.0317 191 ASP   A CB  
1384 C  CG  . ASP   A 191 ? 0.3315 0.3440 0.2797 0.0274  -0.0094 -0.0321 191 ASP   A CG  
1385 O  OD1 . ASP   A 191 ? 0.3349 0.3470 0.2825 0.0250  -0.0094 -0.0343 191 ASP   A OD1 
1386 O  OD2 . ASP   A 191 ? 0.3443 0.3677 0.2960 0.0287  -0.0088 -0.0298 191 ASP   A OD2 
1387 N  N   . MET   A 192 ? 0.2695 0.2397 0.2072 0.0237  -0.0097 -0.0291 192 MET   A N   
1388 C  CA  . MET   A 192 ? 0.2851 0.2440 0.2184 0.0255  -0.0102 -0.0283 192 MET   A CA  
1389 C  C   . MET   A 192 ? 0.3133 0.2585 0.2421 0.0220  -0.0103 -0.0292 192 MET   A C   
1390 O  O   . MET   A 192 ? 0.3206 0.2547 0.2447 0.0235  -0.0107 -0.0286 192 MET   A O   
1391 C  CB  . MET   A 192 ? 0.2766 0.2391 0.2130 0.0245  -0.0094 -0.0241 192 MET   A CB  
1392 C  CG  . MET   A 192 ? 0.2694 0.2429 0.2089 0.0285  -0.0095 -0.0236 192 MET   A CG  
1393 S  SD  . MET   A 192 ? 0.2794 0.2563 0.2222 0.0273  -0.0086 -0.0196 192 MET   A SD  
1394 C  CE  . MET   A 192 ? 0.3151 0.2806 0.2515 0.0312  -0.0096 -0.0197 192 MET   A CE  
1395 N  N   . GLY   A 193 ? 0.2960 0.2426 0.2262 0.0170  -0.0097 -0.0304 193 GLY   A N   
1396 C  CA  . GLY   A 193 ? 0.3208 0.2552 0.2468 0.0128  -0.0096 -0.0317 193 GLY   A CA  
1397 C  C   . GLY   A 193 ? 0.3137 0.2440 0.2400 0.0083  -0.0086 -0.0279 193 GLY   A C   
1398 O  O   . GLY   A 193 ? 0.3217 0.2400 0.2435 0.0054  -0.0085 -0.0281 193 GLY   A O   
1399 N  N   . VAL   A 194 ? 0.2851 0.2252 0.2167 0.0075  -0.0078 -0.0247 194 VAL   A N   
1400 C  CA  . VAL   A 194 ? 0.2687 0.2058 0.2006 0.0043  -0.0069 -0.0212 194 VAL   A CA  
1401 C  C   . VAL   A 194 ? 0.2623 0.2067 0.1984 -0.0011 -0.0058 -0.0203 194 VAL   A C   
1402 O  O   . VAL   A 194 ? 0.2711 0.2172 0.2091 -0.0031 -0.0051 -0.0174 194 VAL   A O   
1403 C  CB  . VAL   A 194 ? 0.2618 0.2026 0.1955 0.0081  -0.0070 -0.0184 194 VAL   A CB  
1404 C  CG1 . VAL   A 194 ? 0.2744 0.2083 0.2034 0.0138  -0.0081 -0.0192 194 VAL   A CG1 
1405 C  CG2 . VAL   A 194 ? 0.2594 0.2136 0.1992 0.0093  -0.0065 -0.0177 194 VAL   A CG2 
1406 N  N   . GLU   A 195 ? 0.2733 0.2220 0.2105 -0.0033 -0.0058 -0.0229 195 GLU   A N   
1407 C  CA  . GLU   A 195 ? 0.2784 0.2357 0.2196 -0.0075 -0.0048 -0.0221 195 GLU   A CA  
1408 C  C   . GLU   A 195 ? 0.2800 0.2318 0.2194 -0.0129 -0.0041 -0.0211 195 GLU   A C   
1409 O  O   . GLU   A 195 ? 0.2857 0.2446 0.2285 -0.0156 -0.0033 -0.0194 195 GLU   A O   
1410 C  CB  . GLU   A 195 ? 0.3089 0.2731 0.2513 -0.0083 -0.0050 -0.0254 195 GLU   A CB  
1411 C  CG  . GLU   A 195 ? 0.3546 0.3107 0.2925 -0.0115 -0.0054 -0.0293 195 GLU   A CG  
1412 C  CD  . GLU   A 195 ? 0.4126 0.3584 0.3456 -0.0080 -0.0065 -0.0320 195 GLU   A CD  
1413 O  OE1 . GLU   A 195 ? 0.3945 0.3409 0.3275 -0.0024 -0.0072 -0.0314 195 GLU   A OE1 
1414 O  OE2 . GLU   A 195 ? 0.5122 0.4492 0.4411 -0.0114 -0.0067 -0.0349 195 GLU   A OE2 
1415 N  N   . LYS   A 196 ? 0.2961 0.2353 0.2300 -0.0142 -0.0045 -0.0217 196 LYS   A N   
1416 C  CA  . LYS   A 196 ? 0.3361 0.2702 0.2680 -0.0196 -0.0037 -0.0202 196 LYS   A CA  
1417 C  C   . LYS   A 196 ? 0.3123 0.2484 0.2461 -0.0186 -0.0032 -0.0163 196 LYS   A C   
1418 O  O   . LYS   A 196 ? 0.3199 0.2597 0.2552 -0.0226 -0.0024 -0.0148 196 LYS   A O   
1419 C  CB  . LYS   A 196 ? 0.3905 0.3096 0.3156 -0.0215 -0.0040 -0.0215 196 LYS   A CB  
1420 C  CG  . LYS   A 196 ? 0.5172 0.4340 0.4405 -0.0245 -0.0042 -0.0259 196 LYS   A CG  
1421 C  CD  . LYS   A 196 ? 0.5934 0.4932 0.5094 -0.0252 -0.0047 -0.0274 196 LYS   A CD  
1422 C  CE  . LYS   A 196 ? 0.6461 0.5438 0.5605 -0.0274 -0.0051 -0.0326 196 LYS   A CE  
1423 N  NZ  . LYS   A 196 ? 0.7004 0.6069 0.6177 -0.0344 -0.0041 -0.0339 196 LYS   A NZ  
1424 N  N   . SER   A 197 ? 0.2993 0.2342 0.2331 -0.0133 -0.0038 -0.0149 197 SER   A N   
1425 C  CA  . SER   A 197 ? 0.2948 0.2295 0.2291 -0.0122 -0.0035 -0.0116 197 SER   A CA  
1426 C  C   . SER   A 197 ? 0.2631 0.2088 0.2033 -0.0095 -0.0032 -0.0104 197 SER   A C   
1427 O  O   . SER   A 197 ? 0.2637 0.2110 0.2052 -0.0093 -0.0029 -0.0081 197 SER   A O   
1428 C  CB  . SER   A 197 ? 0.3231 0.2473 0.2521 -0.0085 -0.0042 -0.0108 197 SER   A CB  
1429 O  OG  . SER   A 197 ? 0.3395 0.2648 0.2685 -0.0030 -0.0051 -0.0125 197 SER   A OG  
1430 N  N   . VAL   A 198 ? 0.2525 0.2055 0.1961 -0.0076 -0.0034 -0.0118 198 VAL   A N   
1431 C  CA  . VAL   A 198 ? 0.2297 0.1916 0.1783 -0.0051 -0.0031 -0.0104 198 VAL   A CA  
1432 C  C   . VAL   A 198 ? 0.2050 0.1759 0.1580 -0.0069 -0.0025 -0.0106 198 VAL   A C   
1433 O  O   . VAL   A 198 ? 0.2031 0.1765 0.1560 -0.0072 -0.0027 -0.0124 198 VAL   A O   
1434 C  CB  . VAL   A 198 ? 0.2334 0.1962 0.1819 -0.0001 -0.0038 -0.0111 198 VAL   A CB  
1435 C  CG1 . VAL   A 198 ? 0.2274 0.1993 0.1812 0.0015  -0.0033 -0.0096 198 VAL   A CG1 
1436 C  CG2 . VAL   A 198 ? 0.2424 0.1969 0.1863 0.0025  -0.0045 -0.0108 198 VAL   A CG2 
1437 N  N   . GLY   A 199 ? 0.1762 0.1525 0.1330 -0.0078 -0.0017 -0.0087 199 GLY   A N   
1438 C  CA  . GLY   A 199 ? 0.1685 0.1533 0.1294 -0.0086 -0.0011 -0.0083 199 GLY   A CA  
1439 C  C   . GLY   A 199 ? 0.1651 0.1555 0.1297 -0.0054 -0.0009 -0.0070 199 GLY   A C   
1440 O  O   . GLY   A 199 ? 0.1592 0.1479 0.1238 -0.0030 -0.0011 -0.0067 199 GLY   A O   
1441 N  N   . PHE   A 200 ? 0.1579 0.1554 0.1257 -0.0056 -0.0003 -0.0063 200 PHE   A N   
1442 C  CA  . PHE   A 200 ? 0.1598 0.1627 0.1312 -0.0033 0.0002  -0.0046 200 PHE   A CA  
1443 C  C   . PHE   A 200 ? 0.1581 0.1645 0.1328 -0.0039 0.0011  -0.0027 200 PHE   A C   
1444 O  O   . PHE   A 200 ? 0.1726 0.1816 0.1473 -0.0054 0.0012  -0.0030 200 PHE   A O   
1445 C  CB  . PHE   A 200 ? 0.1614 0.1693 0.1327 -0.0022 0.0000  -0.0053 200 PHE   A CB  
1446 C  CG  . PHE   A 200 ? 0.1579 0.1720 0.1328 -0.0003 0.0008  -0.0029 200 PHE   A CG  
1447 C  CD1 . PHE   A 200 ? 0.1633 0.1770 0.1393 0.0013  0.0009  -0.0020 200 PHE   A CD1 
1448 C  CD2 . PHE   A 200 ? 0.1701 0.1901 0.1471 -0.0003 0.0014  -0.0013 200 PHE   A CD2 
1449 C  CE1 . PHE   A 200 ? 0.1517 0.1703 0.1308 0.0022  0.0017  0.0005  200 PHE   A CE1 
1450 C  CE2 . PHE   A 200 ? 0.1765 0.2008 0.1562 0.0013  0.0022  0.0014  200 PHE   A CE2 
1451 C  CZ  . PHE   A 200 ? 0.1682 0.1914 0.1490 0.0023  0.0024  0.0024  200 PHE   A CZ  
1452 N  N   . LYS   A 201 ? 0.1523 0.1589 0.1296 -0.0027 0.0016  -0.0011 201 LYS   A N   
1453 C  CA  . LYS   A 201 ? 0.1526 0.1617 0.1330 -0.0026 0.0024  0.0006  201 LYS   A CA  
1454 C  C   . LYS   A 201 ? 0.1572 0.1692 0.1403 -0.0009 0.0031  0.0028  201 LYS   A C   
1455 O  O   . LYS   A 201 ? 0.1448 0.1558 0.1286 -0.0004 0.0032  0.0031  201 LYS   A O   
1456 C  CB  . LYS   A 201 ? 0.1546 0.1602 0.1357 -0.0034 0.0025  0.0004  201 LYS   A CB  
1457 C  CG  . LYS   A 201 ? 0.1742 0.1815 0.1584 -0.0028 0.0033  0.0017  201 LYS   A CG  
1458 C  CD  . LYS   A 201 ? 0.1976 0.2027 0.1821 -0.0037 0.0032  0.0008  201 LYS   A CD  
1459 C  CE  . LYS   A 201 ? 0.2343 0.2401 0.2220 -0.0026 0.0039  0.0016  201 LYS   A CE  
1460 N  NZ  . LYS   A 201 ? 0.2501 0.2544 0.2382 -0.0033 0.0038  0.0001  201 LYS   A NZ  
1461 N  N   . VAL   A 202 ? 0.1534 0.1695 0.1380 -0.0001 0.0036  0.0044  202 VAL   A N   
1462 C  CA  . VAL   A 202 ? 0.1785 0.1969 0.1654 0.0014  0.0045  0.0072  202 VAL   A CA  
1463 C  C   . VAL   A 202 ? 0.1715 0.1868 0.1607 0.0016  0.0053  0.0085  202 VAL   A C   
1464 O  O   . VAL   A 202 ? 0.1915 0.2071 0.1809 0.0019  0.0053  0.0082  202 VAL   A O   
1465 C  CB  . VAL   A 202 ? 0.2177 0.2424 0.2044 0.0027  0.0048  0.0087  202 VAL   A CB  
1466 C  CG1 . VAL   A 202 ? 0.2349 0.2625 0.2210 0.0027  0.0046  0.0079  202 VAL   A CG1 
1467 C  CG2 . VAL   A 202 ? 0.2319 0.2583 0.2208 0.0044  0.0059  0.0124  202 VAL   A CG2 
1468 N  N   . THR   A 203 ? 0.1683 0.1810 0.1593 0.0014  0.0059  0.0096  203 THR   A N   
1469 C  CA  . THR   A 203 ? 0.1780 0.1871 0.1713 0.0015  0.0067  0.0106  203 THR   A CA  
1470 C  C   . THR   A 203 ? 0.1903 0.1994 0.1851 0.0022  0.0078  0.0140  203 THR   A C   
1471 O  O   . THR   A 203 ? 0.1632 0.1735 0.1583 0.0013  0.0081  0.0147  203 THR   A O   
1472 C  CB  . THR   A 203 ? 0.2100 0.2153 0.2039 -0.0001 0.0065  0.0084  203 THR   A CB  
1473 O  OG1 . THR   A 203 ? 0.2328 0.2380 0.2248 -0.0005 0.0055  0.0060  203 THR   A OG1 
1474 C  CG2 . THR   A 203 ? 0.2101 0.2114 0.2064 -0.0002 0.0072  0.0086  203 THR   A CG2 
1475 N  N   . GLY   A 204 ? 0.1957 0.2035 0.1913 0.0039  0.0085  0.0160  204 GLY   A N   
1476 C  CA  . GLY   A 204 ? 0.2201 0.2269 0.2167 0.0048  0.0097  0.0199  204 GLY   A CA  
1477 C  C   . GLY   A 204 ? 0.2565 0.2699 0.2518 0.0061  0.0098  0.0223  204 GLY   A C   
1478 O  O   . GLY   A 204 ? 0.2588 0.2773 0.2526 0.0062  0.0088  0.0203  204 GLY   A O   
1479 N  N   . GLY   A 205 ? 0.3228 0.3361 0.3185 0.0073  0.0109  0.0265  205 GLY   A N   
1480 C  CA  . GLY   A 205 ? 0.3473 0.3679 0.3419 0.0088  0.0111  0.0292  205 GLY   A CA  
1481 C  C   . GLY   A 205 ? 0.4230 0.4496 0.4161 0.0115  0.0104  0.0287  205 GLY   A C   
1482 O  O   . GLY   A 205 ? 0.4818 0.5160 0.4738 0.0126  0.0102  0.0297  205 GLY   A O   
1483 N  N   . VAL   A 206 ? 0.4243 0.4489 0.4174 0.0126  0.0099  0.0270  206 VAL   A N   
1484 C  CA  . VAL   A 206 ? 0.4126 0.4440 0.4044 0.0148  0.0093  0.0260  206 VAL   A CA  
1485 C  C   . VAL   A 206 ? 0.4574 0.4867 0.4496 0.0180  0.0097  0.0276  206 VAL   A C   
1486 O  O   . VAL   A 206 ? 0.5008 0.5289 0.4931 0.0180  0.0091  0.0248  206 VAL   A O   
1487 C  CB  . VAL   A 206 ? 0.4363 0.4700 0.4273 0.0126  0.0080  0.0212  206 VAL   A CB  
1488 C  CG1 . VAL   A 206 ? 0.4468 0.4895 0.4365 0.0139  0.0074  0.0201  206 VAL   A CG1 
1489 C  CG2 . VAL   A 206 ? 0.4583 0.4913 0.4488 0.0098  0.0075  0.0191  206 VAL   A CG2 
1490 N  N   . SER   A 207 ? 0.4453 0.4743 0.4372 0.0209  0.0107  0.0323  207 SER   A N   
1491 C  CA  . SER   A 207 ? 0.5254 0.5505 0.5173 0.0248  0.0112  0.0346  207 SER   A CA  
1492 C  C   . SER   A 207 ? 0.4722 0.5063 0.4629 0.0284  0.0106  0.0338  207 SER   A C   
1493 O  O   . SER   A 207 ? 0.5379 0.5704 0.5287 0.0309  0.0104  0.0329  207 SER   A O   
1494 C  CB  . SER   A 207 ? 0.5018 0.5228 0.4934 0.0268  0.0126  0.0403  207 SER   A CB  
1495 O  OG  . SER   A 207 ? 0.6105 0.6249 0.6032 0.0228  0.0134  0.0409  207 SER   A OG  
1496 N  N   . THR   A 208 ? 0.3876 0.4319 0.3773 0.0286  0.0102  0.0340  208 THR   A N   
1497 C  CA  . THR   A 208 ? 0.3668 0.4215 0.3553 0.0324  0.0098  0.0342  208 THR   A CA  
1498 C  C   . THR   A 208 ? 0.3560 0.4197 0.3441 0.0294  0.0087  0.0294  208 THR   A C   
1499 O  O   . THR   A 208 ? 0.3359 0.3984 0.3242 0.0252  0.0083  0.0269  208 THR   A O   
1500 C  CB  . THR   A 208 ? 0.3742 0.4340 0.3615 0.0359  0.0106  0.0395  208 THR   A CB  
1501 O  OG1 . THR   A 208 ? 0.3478 0.4132 0.3350 0.0330  0.0104  0.0388  208 THR   A OG1 
1502 C  CG2 . THR   A 208 ? 0.4055 0.4551 0.3928 0.0381  0.0120  0.0448  208 THR   A CG2 
1503 N  N   . ALA   A 209 ? 0.3346 0.4077 0.3220 0.0320  0.0082  0.0283  209 ALA   A N   
1504 C  CA  . ALA   A 209 ? 0.3232 0.4068 0.3100 0.0294  0.0073  0.0242  209 ALA   A CA  
1505 C  C   . ALA   A 209 ? 0.3047 0.3932 0.2909 0.0278  0.0073  0.0244  209 ALA   A C   
1506 O  O   . ALA   A 209 ? 0.2789 0.3694 0.2647 0.0237  0.0066  0.0203  209 ALA   A O   
1507 C  CB  . ALA   A 209 ? 0.3237 0.4185 0.3098 0.0333  0.0071  0.0240  209 ALA   A CB  
1508 N  N   . GLU   A 210 ? 0.2956 0.3864 0.2814 0.0313  0.0080  0.0291  210 GLU   A N   
1509 C  CA  . GLU   A 210 ? 0.3079 0.4048 0.2931 0.0302  0.0080  0.0294  210 GLU   A CA  
1510 C  C   . GLU   A 210 ? 0.2744 0.3629 0.2603 0.0258  0.0079  0.0277  210 GLU   A C   
1511 O  O   . GLU   A 210 ? 0.2616 0.3541 0.2470 0.0232  0.0073  0.0246  210 GLU   A O   
1512 C  CB  . GLU   A 210 ? 0.3300 0.4303 0.3146 0.0348  0.0090  0.0356  210 GLU   A CB  
1513 C  CG  . GLU   A 210 ? 0.3787 0.4898 0.3623 0.0400  0.0091  0.0374  210 GLU   A CG  
1514 C  CD  . GLU   A 210 ? 0.4071 0.5131 0.3906 0.0439  0.0094  0.0395  210 GLU   A CD  
1515 O  OE1 . GLU   A 210 ? 0.4077 0.5012 0.3921 0.0427  0.0096  0.0394  210 GLU   A OE1 
1516 O  OE2 . GLU   A 210 ? 0.5086 0.6244 0.4911 0.0488  0.0093  0.0410  210 GLU   A OE2 
1517 N  N   . ASP   A 211 ? 0.2746 0.3516 0.2614 0.0253  0.0085  0.0297  211 ASP   A N   
1518 C  CA  . ASP   A 211 ? 0.2801 0.3497 0.2675 0.0214  0.0083  0.0278  211 ASP   A CA  
1519 C  C   . ASP   A 211 ? 0.2694 0.3382 0.2564 0.0178  0.0072  0.0221  211 ASP   A C   
1520 O  O   . ASP   A 211 ? 0.2241 0.2929 0.2105 0.0153  0.0066  0.0195  211 ASP   A O   
1521 C  CB  . ASP   A 211 ? 0.2845 0.3426 0.2731 0.0210  0.0091  0.0301  211 ASP   A CB  
1522 C  CG  . ASP   A 211 ? 0.3291 0.3850 0.3180 0.0236  0.0105  0.0360  211 ASP   A CG  
1523 O  OD1 . ASP   A 211 ? 0.3376 0.4001 0.3258 0.0245  0.0108  0.0385  211 ASP   A OD1 
1524 O  OD2 . ASP   A 211 ? 0.3548 0.4021 0.3443 0.0245  0.0112  0.0380  211 ASP   A OD2 
1525 N  N   . ALA   A 212 ? 0.2515 0.3195 0.2385 0.0177  0.0068  0.0201  212 ALA   A N   
1526 C  CA  . ALA   A 212 ? 0.2431 0.3096 0.2294 0.0139  0.0059  0.0152  212 ALA   A CA  
1527 C  C   . ALA   A 212 ? 0.2411 0.3160 0.2261 0.0122  0.0052  0.0121  212 ALA   A C   
1528 O  O   . ALA   A 212 ? 0.2268 0.2984 0.2107 0.0089  0.0045  0.0088  212 ALA   A O   
1529 C  CB  . ALA   A 212 ? 0.2543 0.3206 0.2409 0.0140  0.0057  0.0139  212 ALA   A CB  
1530 N  N   . GLN   A 213 ? 0.2357 0.3211 0.2203 0.0147  0.0053  0.0132  213 GLN   A N   
1531 C  CA  . GLN   A 213 ? 0.2559 0.3503 0.2394 0.0133  0.0047  0.0099  213 GLN   A CA  
1532 C  C   . GLN   A 213 ? 0.2360 0.3283 0.2190 0.0122  0.0045  0.0093  213 GLN   A C   
1533 O  O   . GLN   A 213 ? 0.2483 0.3413 0.2300 0.0094  0.0037  0.0050  213 GLN   A O   
1534 C  CB  . GLN   A 213 ? 0.2932 0.4002 0.2767 0.0170  0.0050  0.0119  213 GLN   A CB  
1535 C  CG  . GLN   A 213 ? 0.3405 0.4589 0.3230 0.0156  0.0044  0.0081  213 GLN   A CG  
1536 C  CD  . GLN   A 213 ? 0.4082 0.5403 0.3907 0.0197  0.0047  0.0102  213 GLN   A CD  
1537 O  OE1 . GLN   A 213 ? 0.4429 0.5768 0.4258 0.0242  0.0054  0.0154  213 GLN   A OE1 
1538 N  NE2 . GLN   A 213 ? 0.3789 0.5210 0.3610 0.0183  0.0042  0.0063  213 GLN   A NE2 
1539 N  N   . LYS   A 214 ? 0.2470 0.3368 0.2308 0.0145  0.0052  0.0135  214 LYS   A N   
1540 C  CA  . LYS   A 214 ? 0.2609 0.3504 0.2443 0.0140  0.0050  0.0132  214 LYS   A CA  
1541 C  C   . LYS   A 214 ? 0.2301 0.3097 0.2129 0.0108  0.0044  0.0098  214 LYS   A C   
1542 O  O   . LYS   A 214 ? 0.2463 0.3266 0.2278 0.0094  0.0036  0.0064  214 LYS   A O   
1543 C  CB  . LYS   A 214 ? 0.3144 0.4032 0.2989 0.0166  0.0062  0.0189  214 LYS   A CB  
1544 C  CG  . LYS   A 214 ? 0.4325 0.5231 0.4169 0.0163  0.0061  0.0189  214 LYS   A CG  
1545 C  CD  . LYS   A 214 ? 0.5151 0.6090 0.5001 0.0186  0.0073  0.0247  214 LYS   A CD  
1546 C  CE  . LYS   A 214 ? 0.5326 0.6166 0.5190 0.0182  0.0084  0.0286  214 LYS   A CE  
1547 N  NZ  . LYS   A 214 ? 0.5264 0.6137 0.5131 0.0195  0.0096  0.0338  214 LYS   A NZ  
1548 N  N   . TYR   A 215 ? 0.2054 0.2759 0.1890 0.0099  0.0046  0.0107  215 TYR   A N   
1549 C  CA  . TYR   A 215 ? 0.1857 0.2473 0.1686 0.0073  0.0041  0.0079  215 TYR   A CA  
1550 C  C   . TYR   A 215 ? 0.1894 0.2507 0.1703 0.0045  0.0031  0.0031  215 TYR   A C   
1551 O  O   . TYR   A 215 ? 0.2104 0.2672 0.1897 0.0030  0.0024  0.0003  215 TYR   A O   
1552 C  CB  . TYR   A 215 ? 0.1926 0.2458 0.1768 0.0069  0.0045  0.0096  215 TYR   A CB  
1553 C  CG  . TYR   A 215 ? 0.1966 0.2467 0.1824 0.0081  0.0054  0.0133  215 TYR   A CG  
1554 C  CD1 . TYR   A 215 ? 0.1885 0.2346 0.1743 0.0071  0.0052  0.0125  215 TYR   A CD1 
1555 C  CD2 . TYR   A 215 ? 0.2362 0.2875 0.2235 0.0103  0.0065  0.0175  215 TYR   A CD2 
1556 C  CE1 . TYR   A 215 ? 0.1886 0.2326 0.1759 0.0074  0.0061  0.0155  215 TYR   A CE1 
1557 C  CE2 . TYR   A 215 ? 0.2368 0.2848 0.2255 0.0107  0.0074  0.0209  215 TYR   A CE2 
1558 C  CZ  . TYR   A 215 ? 0.2118 0.2564 0.2007 0.0089  0.0073  0.0198  215 TYR   A CZ  
1559 O  OH  . TYR   A 215 ? 0.2099 0.2518 0.2001 0.0085  0.0083  0.0228  215 TYR   A OH  
1560 N  N   . LEU   A 216 ? 0.2036 0.2694 0.1844 0.0038  0.0031  0.0022  216 LEU   A N   
1561 C  CA  . LEU   A 216 ? 0.2133 0.2794 0.1920 0.0004  0.0023  -0.0024 216 LEU   A CA  
1562 C  C   . LEU   A 216 ? 0.2170 0.2884 0.1943 0.0001  0.0018  -0.0053 216 LEU   A C   
1563 O  O   . LEU   A 216 ? 0.2193 0.2866 0.1944 -0.0028 0.0011  -0.0093 216 LEU   A O   
1564 C  CB  . LEU   A 216 ? 0.2271 0.2989 0.2061 -0.0005 0.0025  -0.0030 216 LEU   A CB  
1565 C  CG  . LEU   A 216 ? 0.2470 0.3121 0.2265 -0.0017 0.0027  -0.0023 216 LEU   A CG  
1566 C  CD1 . LEU   A 216 ? 0.2755 0.3484 0.2558 -0.0013 0.0030  -0.0021 216 LEU   A CD1 
1567 C  CD2 . LEU   A 216 ? 0.2466 0.3034 0.2239 -0.0058 0.0022  -0.0054 216 LEU   A CD2 
1568 N  N   . ALA   A 217 ? 0.2180 0.2989 0.1964 0.0031  0.0021  -0.0034 217 ALA   A N   
1569 C  CA  . ALA   A 217 ? 0.2145 0.3024 0.1917 0.0031  0.0015  -0.0064 217 ALA   A CA  
1570 C  C   . ALA   A 217 ? 0.2221 0.3029 0.1980 0.0029  0.0009  -0.0082 217 ALA   A C   
1571 O  O   . ALA   A 217 ? 0.2407 0.3221 0.2146 0.0016  0.0001  -0.0127 217 ALA   A O   
1572 C  CB  . ALA   A 217 ? 0.2122 0.3120 0.1908 0.0068  0.0021  -0.0032 217 ALA   A CB  
1573 N  N   . ILE   A 218 ? 0.2073 0.2813 0.1840 0.0042  0.0013  -0.0052 218 ILE   A N   
1574 C  CA  . ILE   A 218 ? 0.2117 0.2801 0.1871 0.0045  0.0006  -0.0069 218 ILE   A CA  
1575 C  C   . ILE   A 218 ? 0.2214 0.2807 0.1941 0.0016  -0.0002 -0.0113 218 ILE   A C   
1576 O  O   . ILE   A 218 ? 0.2261 0.2836 0.1966 0.0015  -0.0011 -0.0150 218 ILE   A O   
1577 C  CB  . ILE   A 218 ? 0.2278 0.2917 0.2049 0.0060  0.0013  -0.0030 218 ILE   A CB  
1578 C  CG1 . ILE   A 218 ? 0.2228 0.2948 0.2021 0.0085  0.0023  0.0017  218 ILE   A CG1 
1579 C  CG2 . ILE   A 218 ? 0.2416 0.3001 0.2171 0.0064  0.0005  -0.0052 218 ILE   A CG2 
1580 C  CD1 . ILE   A 218 ? 0.2362 0.3031 0.2174 0.0089  0.0032  0.0059  218 ILE   A CD1 
1581 N  N   . ALA   A 219 ? 0.2141 0.2672 0.1867 -0.0007 0.0000  -0.0107 219 ALA   A N   
1582 C  CA  . ALA   A 219 ? 0.2132 0.2574 0.1831 -0.0038 -0.0006 -0.0140 219 ALA   A CA  
1583 C  C   . ALA   A 219 ? 0.2230 0.2708 0.1909 -0.0062 -0.0011 -0.0184 219 ALA   A C   
1584 O  O   . ALA   A 219 ? 0.2163 0.2577 0.1812 -0.0076 -0.0019 -0.0221 219 ALA   A O   
1585 C  CB  . ALA   A 219 ? 0.2247 0.2645 0.1952 -0.0058 -0.0001 -0.0122 219 ALA   A CB  
1586 N  N   . ASP   A 220 ? 0.2232 0.2812 0.1926 -0.0067 -0.0007 -0.0182 220 ASP   A N   
1587 C  CA  . ASP   A 220 ? 0.2352 0.2986 0.2031 -0.0095 -0.0011 -0.0227 220 ASP   A CA  
1588 C  C   . ASP   A 220 ? 0.2361 0.3014 0.2026 -0.0080 -0.0019 -0.0261 220 ASP   A C   
1589 O  O   . ASP   A 220 ? 0.2696 0.3308 0.2334 -0.0107 -0.0025 -0.0309 220 ASP   A O   
1590 C  CB  . ASP   A 220 ? 0.2472 0.3235 0.2173 -0.0093 -0.0005 -0.0216 220 ASP   A CB  
1591 C  CG  . ASP   A 220 ? 0.2854 0.3612 0.2565 -0.0111 0.0001  -0.0197 220 ASP   A CG  
1592 O  OD1 . ASP   A 220 ? 0.2990 0.3643 0.2689 -0.0134 0.0001  -0.0195 220 ASP   A OD1 
1593 O  OD2 . ASP   A 220 ? 0.3030 0.3897 0.2760 -0.0098 0.0006  -0.0181 220 ASP   A OD2 
1594 N  N   . GLU   A 221 ? 0.2515 0.3224 0.2197 -0.0037 -0.0018 -0.0236 221 GLU   A N   
1595 C  CA  . GLU   A 221 ? 0.2953 0.3695 0.2623 -0.0017 -0.0025 -0.0268 221 GLU   A CA  
1596 C  C   . GLU   A 221 ? 0.2731 0.3348 0.2372 -0.0016 -0.0034 -0.0293 221 GLU   A C   
1597 O  O   . GLU   A 221 ? 0.2702 0.3309 0.2319 -0.0015 -0.0043 -0.0341 221 GLU   A O   
1598 C  CB  . GLU   A 221 ? 0.3609 0.4451 0.3303 0.0026  -0.0021 -0.0229 221 GLU   A CB  
1599 C  CG  . GLU   A 221 ? 0.4690 0.5588 0.4374 0.0050  -0.0028 -0.0261 221 GLU   A CG  
1600 C  CD  . GLU   A 221 ? 0.5921 0.6907 0.5595 0.0040  -0.0034 -0.0314 221 GLU   A CD  
1601 O  OE1 . GLU   A 221 ? 0.6399 0.7451 0.6081 0.0019  -0.0031 -0.0318 221 GLU   A OE1 
1602 O  OE2 . GLU   A 221 ? 0.5857 0.6852 0.5514 0.0054  -0.0044 -0.0357 221 GLU   A OE2 
1603 N  N   . LEU   A 222 ? 0.2367 0.2889 0.2007 -0.0011 -0.0032 -0.0263 222 LEU   A N   
1604 C  CA  . LEU   A 222 ? 0.2339 0.2752 0.1950 -0.0001 -0.0040 -0.0282 222 LEU   A CA  
1605 C  C   . LEU   A 222 ? 0.2426 0.2726 0.2000 -0.0039 -0.0045 -0.0318 222 LEU   A C   
1606 O  O   . LEU   A 222 ? 0.2591 0.2819 0.2131 -0.0031 -0.0054 -0.0355 222 LEU   A O   
1607 C  CB  . LEU   A 222 ? 0.2574 0.2939 0.2198 0.0018  -0.0036 -0.0239 222 LEU   A CB  
1608 C  CG  . LEU   A 222 ? 0.2730 0.3178 0.2381 0.0055  -0.0032 -0.0208 222 LEU   A CG  
1609 C  CD1 . LEU   A 222 ? 0.2688 0.3081 0.2352 0.0060  -0.0027 -0.0171 222 LEU   A CD1 
1610 C  CD2 . LEU   A 222 ? 0.2947 0.3422 0.2583 0.0086  -0.0042 -0.0238 222 LEU   A CD2 
1611 N  N   . PHE   A 223 ? 0.2325 0.2607 0.1904 -0.0078 -0.0038 -0.0306 223 PHE   A N   
1612 C  CA  . PHE   A 223 ? 0.2554 0.2718 0.2097 -0.0117 -0.0040 -0.0327 223 PHE   A CA  
1613 C  C   . PHE   A 223 ? 0.2639 0.2836 0.2175 -0.0168 -0.0038 -0.0360 223 PHE   A C   
1614 O  O   . PHE   A 223 ? 0.2873 0.2970 0.2373 -0.0206 -0.0040 -0.0387 223 PHE   A O   
1615 C  CB  . PHE   A 223 ? 0.2499 0.2604 0.2049 -0.0127 -0.0034 -0.0286 223 PHE   A CB  
1616 C  CG  . PHE   A 223 ? 0.2384 0.2446 0.1937 -0.0084 -0.0036 -0.0258 223 PHE   A CG  
1617 C  CD1 . PHE   A 223 ? 0.2675 0.2642 0.2192 -0.0065 -0.0045 -0.0276 223 PHE   A CD1 
1618 C  CD2 . PHE   A 223 ? 0.2440 0.2560 0.2032 -0.0063 -0.0029 -0.0216 223 PHE   A CD2 
1619 C  CE1 . PHE   A 223 ? 0.2720 0.2664 0.2241 -0.0025 -0.0047 -0.0253 223 PHE   A CE1 
1620 C  CE2 . PHE   A 223 ? 0.2353 0.2443 0.1949 -0.0030 -0.0031 -0.0196 223 PHE   A CE2 
1621 C  CZ  . PHE   A 223 ? 0.2515 0.2523 0.2076 -0.0012 -0.0040 -0.0214 223 PHE   A CZ  
1622 N  N   . GLY   A 224 ? 0.2811 0.3145 0.2378 -0.0169 -0.0033 -0.0356 224 GLY   A N   
1623 C  CA  . GLY   A 224 ? 0.2765 0.3157 0.2333 -0.0218 -0.0029 -0.0381 224 GLY   A CA  
1624 C  C   . GLY   A 224 ? 0.2959 0.3394 0.2552 -0.0230 -0.0020 -0.0340 224 GLY   A C   
1625 O  O   . GLY   A 224 ? 0.2793 0.3162 0.2391 -0.0217 -0.0018 -0.0303 224 GLY   A O   
1626 N  N   . ALA   A 225 ? 0.2778 0.3325 0.2385 -0.0256 -0.0016 -0.0353 225 ALA   A N   
1627 C  CA  . ALA   A 225 ? 0.2915 0.3539 0.2551 -0.0252 -0.0008 -0.0317 225 ALA   A CA  
1628 C  C   . ALA   A 225 ? 0.2800 0.3344 0.2424 -0.0292 -0.0004 -0.0307 225 ALA   A C   
1629 O  O   . ALA   A 225 ? 0.3327 0.3912 0.2973 -0.0281 0.0002  -0.0274 225 ALA   A O   
1630 C  CB  . ALA   A 225 ? 0.3111 0.3892 0.2763 -0.0262 -0.0006 -0.0337 225 ALA   A CB  
1631 N  N   . ASP   A 226 ? 0.2885 0.3314 0.2472 -0.0336 -0.0006 -0.0333 226 ASP   A N   
1632 C  CA  . ASP   A 226 ? 0.3177 0.3534 0.2749 -0.0376 -0.0001 -0.0321 226 ASP   A CA  
1633 C  C   . ASP   A 226 ? 0.3044 0.3286 0.2609 -0.0348 -0.0003 -0.0285 226 ASP   A C   
1634 O  O   . ASP   A 226 ? 0.2959 0.3145 0.2513 -0.0373 0.0001  -0.0268 226 ASP   A O   
1635 C  CB  . ASP   A 226 ? 0.3927 0.4215 0.3459 -0.0444 -0.0001 -0.0362 226 ASP   A CB  
1636 C  CG  . ASP   A 226 ? 0.4712 0.5123 0.4252 -0.0490 0.0002  -0.0400 226 ASP   A CG  
1637 O  OD1 . ASP   A 226 ? 0.5615 0.6161 0.5187 -0.0482 0.0007  -0.0385 226 ASP   A OD1 
1638 O  OD2 . ASP   A 226 ? 0.5722 0.6096 0.5235 -0.0531 0.0000  -0.0446 226 ASP   A OD2 
1639 N  N   . TRP   A 227 ? 0.2651 0.2857 0.2219 -0.0298 -0.0008 -0.0275 227 TRP   A N   
1640 C  CA  . TRP   A 227 ? 0.2588 0.2687 0.2145 -0.0273 -0.0010 -0.0249 227 TRP   A CA  
1641 C  C   . TRP   A 227 ? 0.2363 0.2493 0.1950 -0.0256 -0.0004 -0.0207 227 TRP   A C   
1642 O  O   . TRP   A 227 ? 0.2536 0.2587 0.2110 -0.0265 -0.0003 -0.0191 227 TRP   A O   
1643 C  CB  . TRP   A 227 ? 0.2568 0.2645 0.2123 -0.0224 -0.0017 -0.0252 227 TRP   A CB  
1644 C  CG  . TRP   A 227 ? 0.2482 0.2464 0.2026 -0.0196 -0.0020 -0.0228 227 TRP   A CG  
1645 C  CD1 . TRP   A 227 ? 0.2695 0.2553 0.2197 -0.0204 -0.0025 -0.0236 227 TRP   A CD1 
1646 C  CD2 . TRP   A 227 ? 0.2376 0.2385 0.1951 -0.0154 -0.0018 -0.0193 227 TRP   A CD2 
1647 N  NE1 . TRP   A 227 ? 0.2680 0.2497 0.2186 -0.0167 -0.0026 -0.0210 227 TRP   A NE1 
1648 C  CE2 . TRP   A 227 ? 0.2389 0.2297 0.1939 -0.0140 -0.0022 -0.0185 227 TRP   A CE2 
1649 C  CE3 . TRP   A 227 ? 0.2239 0.2342 0.1857 -0.0129 -0.0013 -0.0168 227 TRP   A CE3 
1650 C  CZ2 . TRP   A 227 ? 0.2233 0.2145 0.1805 -0.0105 -0.0021 -0.0157 227 TRP   A CZ2 
1651 C  CZ3 . TRP   A 227 ? 0.2192 0.2283 0.1829 -0.0098 -0.0011 -0.0138 227 TRP   A CZ3 
1652 C  CH2 . TRP   A 227 ? 0.2240 0.2243 0.1856 -0.0087 -0.0015 -0.0136 227 TRP   A CH2 
1653 N  N   . ALA   A 228 ? 0.2188 0.2427 0.1814 -0.0229 -0.0001 -0.0191 228 ALA   A N   
1654 C  CA  . ALA   A 228 ? 0.2184 0.2443 0.1839 -0.0202 0.0004  -0.0154 228 ALA   A CA  
1655 C  C   . ALA   A 228 ? 0.2295 0.2584 0.1956 -0.0232 0.0010  -0.0149 228 ALA   A C   
1656 O  O   . ALA   A 228 ? 0.2377 0.2759 0.2064 -0.0219 0.0014  -0.0138 228 ALA   A O   
1657 C  CB  . ALA   A 228 ? 0.2244 0.2592 0.1933 -0.0160 0.0007  -0.0135 228 ALA   A CB  
1658 N  N   . ASP   A 229 ? 0.2286 0.2498 0.1920 -0.0268 0.0010  -0.0155 229 ASP   A N   
1659 C  CA  . ASP   A 229 ? 0.2295 0.2527 0.1932 -0.0293 0.0015  -0.0145 229 ASP   A CA  
1660 C  C   . ASP   A 229 ? 0.2206 0.2394 0.1858 -0.0261 0.0016  -0.0116 229 ASP   A C   
1661 O  O   . ASP   A 229 ? 0.2044 0.2192 0.1704 -0.0224 0.0013  -0.0104 229 ASP   A O   
1662 C  CB  . ASP   A 229 ? 0.2442 0.2621 0.2041 -0.0353 0.0016  -0.0164 229 ASP   A CB  
1663 C  CG  . ASP   A 229 ? 0.2990 0.3029 0.2551 -0.0359 0.0012  -0.0160 229 ASP   A CG  
1664 O  OD1 . ASP   A 229 ? 0.2571 0.2561 0.2137 -0.0314 0.0009  -0.0143 229 ASP   A OD1 
1665 O  OD2 . ASP   A 229 ? 0.3481 0.3459 0.3003 -0.0407 0.0013  -0.0174 229 ASP   A OD2 
1666 N  N   . ALA   A 230 ? 0.1935 0.2138 0.1590 -0.0278 0.0020  -0.0108 230 ALA   A N   
1667 C  CA  . ALA   A 230 ? 0.2177 0.2358 0.1851 -0.0248 0.0020  -0.0086 230 ALA   A CA  
1668 C  C   . ALA   A 230 ? 0.2032 0.2104 0.1681 -0.0244 0.0017  -0.0079 230 ALA   A C   
1669 O  O   . ALA   A 230 ? 0.2028 0.2081 0.1694 -0.0214 0.0016  -0.0064 230 ALA   A O   
1670 C  CB  . ALA   A 230 ? 0.2365 0.2599 0.2048 -0.0264 0.0025  -0.0082 230 ALA   A CB  
1671 N  N   . ARG   A 231 ? 0.2009 0.2012 0.1618 -0.0274 0.0014  -0.0090 231 ARG   A N   
1672 C  CA  . ARG   A 231 ? 0.2140 0.2042 0.1721 -0.0261 0.0010  -0.0083 231 ARG   A CA  
1673 C  C   . ARG   A 231 ? 0.2161 0.2043 0.1748 -0.0220 0.0004  -0.0086 231 ARG   A C   
1674 O  O   . ARG   A 231 ? 0.2180 0.1997 0.1752 -0.0197 0.0000  -0.0080 231 ARG   A O   
1675 C  CB  . ARG   A 231 ? 0.2211 0.2034 0.1740 -0.0305 0.0009  -0.0091 231 ARG   A CB  
1676 C  CG  . ARG   A 231 ? 0.2511 0.2221 0.2002 -0.0288 0.0004  -0.0082 231 ARG   A CG  
1677 C  CD  . ARG   A 231 ? 0.2353 0.2053 0.1853 -0.0261 0.0004  -0.0059 231 ARG   A CD  
1678 N  NE  . ARG   A 231 ? 0.2487 0.2091 0.1948 -0.0237 -0.0002 -0.0052 231 ARG   A NE  
1679 C  CZ  . ARG   A 231 ? 0.2493 0.2079 0.1958 -0.0191 -0.0008 -0.0056 231 ARG   A CZ  
1680 N  NH1 . ARG   A 231 ? 0.2421 0.2075 0.1928 -0.0167 -0.0009 -0.0064 231 ARG   A NH1 
1681 N  NH2 . ARG   A 231 ? 0.2465 0.1970 0.1892 -0.0167 -0.0014 -0.0049 231 ARG   A NH2 
1682 N  N   . HIS   A 232 ? 0.1922 0.1865 0.1528 -0.0211 0.0004  -0.0097 232 HIS   A N   
1683 C  CA  . HIS   A 232 ? 0.1914 0.1849 0.1523 -0.0177 -0.0001 -0.0102 232 HIS   A CA  
1684 C  C   . HIS   A 232 ? 0.1714 0.1727 0.1367 -0.0143 0.0002  -0.0088 232 HIS   A C   
1685 O  O   . HIS   A 232 ? 0.1710 0.1723 0.1367 -0.0115 -0.0001 -0.0088 232 HIS   A O   
1686 C  CB  . HIS   A 232 ? 0.2051 0.1973 0.1632 -0.0196 -0.0005 -0.0131 232 HIS   A CB  
1687 C  CG  . HIS   A 232 ? 0.2138 0.1954 0.1670 -0.0223 -0.0008 -0.0142 232 HIS   A CG  
1688 N  ND1 . HIS   A 232 ? 0.2475 0.2273 0.1986 -0.0274 -0.0004 -0.0146 232 HIS   A ND1 
1689 C  CD2 . HIS   A 232 ? 0.2405 0.2128 0.1902 -0.0206 -0.0015 -0.0146 232 HIS   A CD2 
1690 C  CE1 . HIS   A 232 ? 0.2526 0.2212 0.1989 -0.0289 -0.0007 -0.0151 232 HIS   A CE1 
1691 N  NE2 . HIS   A 232 ? 0.2484 0.2120 0.1937 -0.0244 -0.0014 -0.0151 232 HIS   A NE2 
1692 N  N   . TYR   A 233 ? 0.1693 0.1772 0.1375 -0.0145 0.0008  -0.0076 233 TYR   A N   
1693 C  CA  . TYR   A 233 ? 0.1601 0.1742 0.1319 -0.0113 0.0012  -0.0059 233 TYR   A CA  
1694 C  C   . TYR   A 233 ? 0.1587 0.1755 0.1332 -0.0107 0.0018  -0.0042 233 TYR   A C   
1695 O  O   . TYR   A 233 ? 0.1568 0.1761 0.1309 -0.0129 0.0020  -0.0049 233 TYR   A O   
1696 C  CB  . TYR   A 233 ? 0.1533 0.1750 0.1255 -0.0113 0.0013  -0.0069 233 TYR   A CB  
1697 C  CG  . TYR   A 233 ? 0.1557 0.1824 0.1304 -0.0077 0.0015  -0.0050 233 TYR   A CG  
1698 C  CD1 . TYR   A 233 ? 0.1654 0.1961 0.1431 -0.0054 0.0022  -0.0023 233 TYR   A CD1 
1699 C  CD2 . TYR   A 233 ? 0.1755 0.2027 0.1492 -0.0066 0.0011  -0.0060 233 TYR   A CD2 
1700 C  CE1 . TYR   A 233 ? 0.1851 0.2192 0.1646 -0.0024 0.0026  -0.0001 233 TYR   A CE1 
1701 C  CE2 . TYR   A 233 ? 0.1849 0.2172 0.1607 -0.0036 0.0014  -0.0040 233 TYR   A CE2 
1702 C  CZ  . TYR   A 233 ? 0.1938 0.2293 0.1723 -0.0017 0.0022  -0.0008 233 TYR   A CZ  
1703 O  OH  . TYR   A 233 ? 0.2247 0.2645 0.2048 0.0009  0.0027  0.0015  233 TYR   A OH  
1704 N  N   . ARG   A 234 ? 0.1490 0.1658 0.1262 -0.0078 0.0021  -0.0023 234 ARG   A N   
1705 C  CA  . ARG   A 234 ? 0.1457 0.1645 0.1256 -0.0065 0.0027  -0.0009 234 ARG   A CA  
1706 C  C   . ARG   A 234 ? 0.1481 0.1690 0.1306 -0.0034 0.0032  0.0014  234 ARG   A C   
1707 O  O   . ARG   A 234 ? 0.1464 0.1662 0.1290 -0.0024 0.0032  0.0021  234 ARG   A O   
1708 C  CB  . ARG   A 234 ? 0.1510 0.1646 0.1311 -0.0070 0.0027  -0.0010 234 ARG   A CB  
1709 C  CG  . ARG   A 234 ? 0.1533 0.1640 0.1304 -0.0100 0.0023  -0.0025 234 ARG   A CG  
1710 C  CD  . ARG   A 234 ? 0.1533 0.1691 0.1304 -0.0118 0.0025  -0.0031 234 ARG   A CD  
1711 N  NE  . ARG   A 234 ? 0.1631 0.1757 0.1371 -0.0152 0.0022  -0.0041 234 ARG   A NE  
1712 C  CZ  . ARG   A 234 ? 0.1808 0.1896 0.1541 -0.0157 0.0022  -0.0039 234 ARG   A CZ  
1713 N  NH1 . ARG   A 234 ? 0.1865 0.1959 0.1625 -0.0134 0.0024  -0.0033 234 ARG   A NH1 
1714 N  NH2 . ARG   A 234 ? 0.2078 0.2124 0.1776 -0.0186 0.0020  -0.0042 234 ARG   A NH2 
1715 N  N   . PHE   A 235 ? 0.1515 0.1753 0.1361 -0.0018 0.0038  0.0026  235 PHE   A N   
1716 C  CA  . PHE   A 235 ? 0.1673 0.1915 0.1542 0.0011  0.0045  0.0052  235 PHE   A CA  
1717 C  C   . PHE   A 235 ? 0.1915 0.2119 0.1804 0.0020  0.0048  0.0056  235 PHE   A C   
1718 O  O   . PHE   A 235 ? 0.1832 0.2047 0.1719 0.0016  0.0046  0.0042  235 PHE   A O   
1719 C  CB  . PHE   A 235 ? 0.1770 0.2082 0.1645 0.0034  0.0048  0.0066  235 PHE   A CB  
1720 C  CG  . PHE   A 235 ? 0.1816 0.2186 0.1677 0.0034  0.0046  0.0066  235 PHE   A CG  
1721 C  CD1 . PHE   A 235 ? 0.2013 0.2392 0.1881 0.0052  0.0050  0.0090  235 PHE   A CD1 
1722 C  CD2 . PHE   A 235 ? 0.2106 0.2527 0.1950 0.0014  0.0040  0.0041  235 PHE   A CD2 
1723 C  CE1 . PHE   A 235 ? 0.2152 0.2595 0.2009 0.0055  0.0048  0.0088  235 PHE   A CE1 
1724 C  CE2 . PHE   A 235 ? 0.2186 0.2665 0.2020 0.0014  0.0038  0.0036  235 PHE   A CE2 
1725 C  CZ  . PHE   A 235 ? 0.2072 0.2565 0.1913 0.0037  0.0041  0.0059  235 PHE   A CZ  
1726 N  N   . SER   A 236 ? 0.2108 0.2273 0.2014 0.0032  0.0054  0.0073  236 SER   A N   
1727 C  CA  . SER   A 236 ? 0.2401 0.2533 0.2327 0.0046  0.0060  0.0079  236 SER   A CA  
1728 C  C   . SER   A 236 ? 0.2431 0.2541 0.2372 0.0065  0.0069  0.0110  236 SER   A C   
1729 O  O   . SER   A 236 ? 0.2427 0.2528 0.2369 0.0055  0.0072  0.0122  236 SER   A O   
1730 C  CB  . SER   A 236 ? 0.2937 0.3025 0.2869 0.0029  0.0058  0.0057  236 SER   A CB  
1731 O  OG  . SER   A 236 ? 0.3692 0.3749 0.3628 0.0017  0.0059  0.0061  236 SER   A OG  
1732 N  N   . ALA   A 237 ? 0.2602 0.2706 0.2552 0.0092  0.0075  0.0125  237 ALA   A N   
1733 C  CA  . ALA   A 237 ? 0.2875 0.2944 0.2836 0.0110  0.0085  0.0160  237 ALA   A CA  
1734 C  C   . ALA   A 237 ? 0.3328 0.3371 0.3295 0.0143  0.0089  0.0167  237 ALA   A C   
1735 O  O   . ALA   A 237 ? 0.3157 0.3251 0.3117 0.0165  0.0084  0.0158  237 ALA   A O   
1736 C  CB  . ALA   A 237 ? 0.3025 0.3147 0.2975 0.0121  0.0087  0.0189  237 ALA   A CB  
1737 N  N   . SER   A 238 ? 0.3865 0.3832 0.3845 0.0148  0.0098  0.0183  238 SER   A N   
1738 C  CA  . SER   A 238 ? 0.4511 0.4435 0.4494 0.0187  0.0104  0.0197  238 SER   A CA  
1739 C  C   . SER   A 238 ? 0.4103 0.4082 0.4070 0.0228  0.0105  0.0230  238 SER   A C   
1740 O  O   . SER   A 238 ? 0.4255 0.4257 0.4214 0.0226  0.0110  0.0262  238 SER   A O   
1741 C  CB  . SER   A 238 ? 0.4870 0.4696 0.4865 0.0179  0.0116  0.0218  238 SER   A CB  
1742 O  OG  . SER   A 238 ? 0.5783 0.5564 0.5794 0.0144  0.0115  0.0183  238 SER   A OG  
1743 N  N   . GLY   A 239 ? 0.4249 0.4256 0.4210 0.0267  0.0100  0.0220  239 GLY   A N   
1744 C  CA  . GLY   A 239 ? 0.4022 0.4081 0.3967 0.0316  0.0102  0.0252  239 GLY   A CA  
1745 C  C   . GLY   A 239 ? 0.3948 0.4131 0.3882 0.0311  0.0094  0.0243  239 GLY   A C   
1746 O  O   . GLY   A 239 ? 0.3754 0.4008 0.3676 0.0352  0.0093  0.0260  239 GLY   A O   
1747 N  N   . LEU   A 240 ? 0.3150 0.3362 0.3087 0.0263  0.0088  0.0215  240 LEU   A N   
1748 C  CA  . LEU   A 240 ? 0.2799 0.3115 0.2724 0.0253  0.0081  0.0207  240 LEU   A CA  
1749 C  C   . LEU   A 240 ? 0.2607 0.3007 0.2526 0.0270  0.0074  0.0182  240 LEU   A C   
1750 O  O   . LEU   A 240 ? 0.2808 0.3302 0.2716 0.0288  0.0072  0.0188  240 LEU   A O   
1751 C  CB  . LEU   A 240 ? 0.2764 0.3076 0.2688 0.0200  0.0077  0.0183  240 LEU   A CB  
1752 C  CG  . LEU   A 240 ? 0.2596 0.3002 0.2505 0.0184  0.0070  0.0168  240 LEU   A CG  
1753 C  CD1 . LEU   A 240 ? 0.2803 0.3271 0.2706 0.0211  0.0074  0.0199  240 LEU   A CD1 
1754 C  CD2 . LEU   A 240 ? 0.2653 0.3033 0.2558 0.0138  0.0065  0.0144  240 LEU   A CD2 
1755 N  N   . LEU   A 241 ? 0.2721 0.3101 0.2647 0.0262  0.0070  0.0151  241 LEU   A N   
1756 C  CA  . LEU   A 241 ? 0.2768 0.3240 0.2688 0.0271  0.0063  0.0124  241 LEU   A CA  
1757 C  C   . LEU   A 241 ? 0.2842 0.3370 0.2756 0.0334  0.0065  0.0146  241 LEU   A C   
1758 O  O   . LEU   A 241 ? 0.2751 0.3394 0.2656 0.0344  0.0061  0.0138  241 LEU   A O   
1759 C  CB  . LEU   A 241 ? 0.2786 0.3228 0.2714 0.0258  0.0060  0.0092  241 LEU   A CB  
1760 C  CG  . LEU   A 241 ? 0.2821 0.3367 0.2745 0.0267  0.0054  0.0064  241 LEU   A CG  
1761 C  CD1 . LEU   A 241 ? 0.2879 0.3516 0.2790 0.0225  0.0050  0.0049  241 LEU   A CD1 
1762 C  CD2 . LEU   A 241 ? 0.2935 0.3456 0.2868 0.0259  0.0051  0.0034  241 LEU   A CD2 
1763 N  N   . ALA   A 242 ? 0.3155 0.3602 0.3073 0.0376  0.0071  0.0173  242 ALA   A N   
1764 C  CA  . ALA   A 242 ? 0.3442 0.3922 0.3350 0.0446  0.0074  0.0200  242 ALA   A CA  
1765 C  C   . ALA   A 242 ? 0.3362 0.3922 0.3256 0.0459  0.0076  0.0231  242 ALA   A C   
1766 O  O   . ALA   A 242 ? 0.3287 0.3956 0.3171 0.0499  0.0073  0.0234  242 ALA   A O   
1767 C  CB  . ALA   A 242 ? 0.3590 0.3940 0.3501 0.0481  0.0081  0.0225  242 ALA   A CB  
1768 N  N   . SER   A 243 ? 0.3232 0.3755 0.3127 0.0424  0.0080  0.0250  243 SER   A N   
1769 C  CA  . SER   A 243 ? 0.3110 0.3716 0.2994 0.0435  0.0082  0.0277  243 SER   A CA  
1770 C  C   . SER   A 243 ? 0.2905 0.3648 0.2785 0.0410  0.0073  0.0240  243 SER   A C   
1771 O  O   . SER   A 243 ? 0.2980 0.3836 0.2849 0.0440  0.0072  0.0249  243 SER   A O   
1772 C  CB  . SER   A 243 ? 0.3143 0.3684 0.3029 0.0403  0.0089  0.0303  243 SER   A CB  
1773 O  OG  . SER   A 243 ? 0.3293 0.3930 0.3169 0.0413  0.0090  0.0324  243 SER   A OG  
1774 N  N   . LEU   A 244 ? 0.2490 0.3224 0.2377 0.0353  0.0068  0.0197  244 LEU   A N   
1775 C  CA  . LEU   A 244 ? 0.2617 0.3465 0.2497 0.0320  0.0060  0.0160  244 LEU   A CA  
1776 C  C   . LEU   A 244 ? 0.2754 0.3709 0.2631 0.0356  0.0057  0.0146  244 LEU   A C   
1777 O  O   . LEU   A 244 ? 0.2776 0.3861 0.2646 0.0356  0.0054  0.0134  244 LEU   A O   
1778 C  CB  . LEU   A 244 ? 0.2390 0.3191 0.2274 0.0255  0.0056  0.0123  244 LEU   A CB  
1779 C  CG  . LEU   A 244 ? 0.2450 0.3162 0.2335 0.0220  0.0058  0.0130  244 LEU   A CG  
1780 C  CD1 . LEU   A 244 ? 0.2484 0.3140 0.2369 0.0166  0.0054  0.0097  244 LEU   A CD1 
1781 C  CD2 . LEU   A 244 ? 0.2506 0.3285 0.2381 0.0210  0.0057  0.0133  244 LEU   A CD2 
1782 N  N   . LEU   A 245 ? 0.2710 0.3620 0.2593 0.0383  0.0057  0.0142  245 LEU   A N   
1783 C  CA  . LEU   A 245 ? 0.2831 0.3848 0.2711 0.0420  0.0052  0.0125  245 LEU   A CA  
1784 C  C   . LEU   A 245 ? 0.2960 0.4054 0.2829 0.0491  0.0054  0.0159  245 LEU   A C   
1785 O  O   . LEU   A 245 ? 0.3025 0.4264 0.2888 0.0510  0.0050  0.0143  245 LEU   A O   
1786 C  CB  . LEU   A 245 ? 0.2807 0.3756 0.2695 0.0438  0.0051  0.0111  245 LEU   A CB  
1787 C  CG  . LEU   A 245 ? 0.2842 0.3771 0.2738 0.0372  0.0047  0.0071  245 LEU   A CG  
1788 C  CD1 . LEU   A 245 ? 0.3112 0.3969 0.3018 0.0395  0.0047  0.0060  245 LEU   A CD1 
1789 C  CD2 . LEU   A 245 ? 0.2732 0.3808 0.2622 0.0339  0.0042  0.0037  245 LEU   A CD2 
1790 N  N   . LYS   A 246 ? 0.3440 0.4441 0.3305 0.0528  0.0061  0.0205  246 LYS   A N   
1791 C  CA  . LYS   A 246 ? 0.3909 0.4967 0.3759 0.0598  0.0065  0.0247  246 LYS   A CA  
1792 C  C   . LYS   A 246 ? 0.3740 0.4941 0.3583 0.0580  0.0062  0.0242  246 LYS   A C   
1793 O  O   . LYS   A 246 ? 0.3965 0.5303 0.3799 0.0625  0.0060  0.0243  246 LYS   A O   
1794 C  CB  . LYS   A 246 ? 0.4723 0.5648 0.4568 0.0628  0.0074  0.0303  246 LYS   A CB  
1795 C  CG  . LYS   A 246 ? 0.5659 0.6429 0.5508 0.0651  0.0079  0.0314  246 LYS   A CG  
1796 C  CD  . LYS   A 246 ? 0.6752 0.7449 0.6583 0.0718  0.0088  0.0376  246 LYS   A CD  
1797 C  CE  . LYS   A 246 ? 0.7410 0.7949 0.7244 0.0741  0.0092  0.0382  246 LYS   A CE  
1798 N  NZ  . LYS   A 246 ? 0.7577 0.7993 0.7429 0.0671  0.0097  0.0371  246 LYS   A NZ  
1799 N  N   . ALA   A 247 ? 0.3450 0.4624 0.3299 0.0517  0.0063  0.0233  247 ALA   A N   
1800 C  CA  . ALA   A 247 ? 0.3517 0.4818 0.3360 0.0493  0.0061  0.0219  247 ALA   A CA  
1801 C  C   . ALA   A 247 ? 0.3740 0.5184 0.3583 0.0471  0.0053  0.0169  247 ALA   A C   
1802 O  O   . ALA   A 247 ? 0.3914 0.5500 0.3751 0.0473  0.0051  0.0158  247 ALA   A O   
1803 C  CB  . ALA   A 247 ? 0.3524 0.4760 0.3373 0.0429  0.0061  0.0211  247 ALA   A CB  
1804 N  N   . LEU   A 248 ? 0.3505 0.4919 0.3356 0.0444  0.0050  0.0136  248 LEU   A N   
1805 C  CA  . LEU   A 248 ? 0.3655 0.5202 0.3506 0.0411  0.0044  0.0088  248 LEU   A CA  
1806 C  C   . LEU   A 248 ? 0.3768 0.5427 0.3616 0.0477  0.0042  0.0088  248 LEU   A C   
1807 O  O   . LEU   A 248 ? 0.3728 0.5514 0.3577 0.0454  0.0037  0.0049  248 LEU   A O   
1808 C  CB  . LEU   A 248 ? 0.3451 0.4915 0.3310 0.0341  0.0042  0.0054  248 LEU   A CB  
1809 C  CG  . LEU   A 248 ? 0.3323 0.4715 0.3181 0.0271  0.0043  0.0042  248 LEU   A CG  
1810 C  CD1 . LEU   A 248 ? 0.3194 0.4472 0.3055 0.0217  0.0042  0.0022  248 LEU   A CD1 
1811 C  CD2 . LEU   A 248 ? 0.3490 0.5014 0.3340 0.0228  0.0040  0.0009  248 LEU   A CD2 
1812 N  N   . GLY   A 249 ? 0.4125 0.5734 0.3968 0.0557  0.0044  0.0131  249 GLY   A N   
1813 C  CA  . GLY   A 249 ? 0.4265 0.5979 0.4100 0.0635  0.0042  0.0135  249 GLY   A CA  
1814 C  C   . GLY   A 249 ? 0.4560 0.6199 0.4401 0.0660  0.0040  0.0124  249 GLY   A C   
1815 O  O   . GLY   A 249 ? 0.4624 0.6357 0.4459 0.0720  0.0036  0.0116  249 GLY   A O   
1816 N  N   . HIS   A 250 ? 0.4416 0.5893 0.4267 0.0619  0.0042  0.0121  250 HIS   A N   
1817 C  CA  . HIS   A 250 ? 0.4712 0.6112 0.4569 0.0647  0.0040  0.0111  250 HIS   A CA  
1818 C  C   . HIS   A 250 ? 0.5427 0.6660 0.5280 0.0699  0.0046  0.0157  250 HIS   A C   
1819 O  O   . HIS   A 250 ? 0.6961 0.8058 0.6825 0.0661  0.0049  0.0151  250 HIS   A O   
1820 C  CB  . HIS   A 250 ? 0.4565 0.5934 0.4436 0.0567  0.0038  0.0068  250 HIS   A CB  
1821 C  CG  . HIS   A 250 ? 0.4398 0.5939 0.4268 0.0527  0.0033  0.0027  250 HIS   A CG  
1822 N  ND1 . HIS   A 250 ? 0.4309 0.5923 0.4177 0.0463  0.0034  0.0014  250 HIS   A ND1 
1823 C  CD2 . HIS   A 250 ? 0.4392 0.6055 0.4263 0.0542  0.0028  -0.0006 250 HIS   A CD2 
1824 C  CE1 . HIS   A 250 ? 0.4376 0.6139 0.4243 0.0433  0.0030  -0.0025 250 HIS   A CE1 
1825 N  NE2 . HIS   A 250 ? 0.4337 0.6141 0.4207 0.0481  0.0027  -0.0036 250 HIS   A NE2 
1826 N  N   . ASP   B 3   ? 0.5213 0.6055 0.5396 -0.0086 0.0106  -0.0557 3   ASP   B N   
1827 C  CA  . ASP   B 3   ? 0.4756 0.5592 0.4948 -0.0091 0.0111  -0.0561 3   ASP   B CA  
1828 C  C   . ASP   B 3   ? 0.4152 0.4878 0.4330 -0.0090 0.0114  -0.0513 3   ASP   B C   
1829 O  O   . ASP   B 3   ? 0.3401 0.4089 0.3536 -0.0064 0.0094  -0.0466 3   ASP   B O   
1830 C  CB  . ASP   B 3   ? 0.5338 0.6249 0.5500 -0.0064 0.0087  -0.0561 3   ASP   B CB  
1831 C  CG  . ASP   B 3   ? 0.5803 0.6715 0.5972 -0.0066 0.0090  -0.0566 3   ASP   B CG  
1832 O  OD1 . ASP   B 3   ? 0.5702 0.6555 0.5897 -0.0091 0.0112  -0.0568 3   ASP   B OD1 
1833 O  OD2 . ASP   B 3   ? 0.6645 0.7618 0.6793 -0.0042 0.0070  -0.0567 3   ASP   B OD2 
1834 N  N   . LEU   B 4   ? 0.3566 0.4243 0.3783 -0.0118 0.0140  -0.0525 4   LEU   B N   
1835 C  CA  . LEU   B 4   ? 0.3674 0.4251 0.3881 -0.0119 0.0145  -0.0481 4   LEU   B CA  
1836 C  C   . LEU   B 4   ? 0.3525 0.4094 0.3704 -0.0107 0.0134  -0.0457 4   LEU   B C   
1837 O  O   . LEU   B 4   ? 0.2997 0.3501 0.3147 -0.0094 0.0125  -0.0411 4   LEU   B O   
1838 C  CB  . LEU   B 4   ? 0.3861 0.4395 0.4117 -0.0152 0.0178  -0.0504 4   LEU   B CB  
1839 C  CG  . LEU   B 4   ? 0.4137 0.4567 0.4387 -0.0155 0.0185  -0.0459 4   LEU   B CG  
1840 C  CD1 . LEU   B 4   ? 0.4215 0.4604 0.4441 -0.0133 0.0169  -0.0422 4   LEU   B CD1 
1841 C  CD2 . LEU   B 4   ? 0.4294 0.4681 0.4595 -0.0186 0.0219  -0.0480 4   LEU   B CD2 
1842 N  N   . LYS   B 5   ? 0.3263 0.3900 0.3453 -0.0112 0.0136  -0.0490 5   LYS   B N   
1843 C  CA  . LYS   B 5   ? 0.3390 0.4027 0.3557 -0.0100 0.0125  -0.0472 5   LYS   B CA  
1844 C  C   . LYS   B 5   ? 0.2934 0.3574 0.3053 -0.0061 0.0093  -0.0435 5   LYS   B C   
1845 O  O   . LYS   B 5   ? 0.2786 0.3377 0.2879 -0.0048 0.0084  -0.0398 5   LYS   B O   
1846 C  CB  . LYS   B 5   ? 0.3740 0.4460 0.3933 -0.0112 0.0133  -0.0521 5   LYS   B CB  
1847 C  CG  . LYS   B 5   ? 0.4369 0.5066 0.4605 -0.0154 0.0168  -0.0550 5   LYS   B CG  
1848 C  CD  . LYS   B 5   ? 0.5099 0.5858 0.5357 -0.0171 0.0180  -0.0591 5   LYS   B CD  
1849 C  CE  . LYS   B 5   ? 0.5779 0.6499 0.6078 -0.0215 0.0218  -0.0612 5   LYS   B CE  
1850 N  NZ  . LYS   B 5   ? 0.6778 0.7533 0.7089 -0.0234 0.0231  -0.0637 5   LYS   B NZ  
1851 N  N   . ALA   B 6   ? 0.2836 0.3533 0.2943 -0.0043 0.0078  -0.0445 6   ALA   B N   
1852 C  CA  . ALA   B 6   ? 0.2849 0.3549 0.2910 -0.0007 0.0050  -0.0410 6   ALA   B CA  
1853 C  C   . ALA   B 6   ? 0.2631 0.3242 0.2667 -0.0001 0.0046  -0.0362 6   ALA   B C   
1854 O  O   . ALA   B 6   ? 0.2603 0.3180 0.2607 0.0021  0.0031  -0.0325 6   ALA   B O   
1855 C  CB  . ALA   B 6   ? 0.3002 0.3783 0.3054 0.0008  0.0036  -0.0429 6   ALA   B CB  
1856 N  N   . SER   B 7   ? 0.2467 0.3044 0.2521 -0.0020 0.0061  -0.0365 7   SER   B N   
1857 C  CA  . SER   B 7   ? 0.2605 0.3104 0.2639 -0.0014 0.0058  -0.0324 7   SER   B CA  
1858 C  C   . SER   B 7   ? 0.2268 0.2701 0.2300 -0.0019 0.0064  -0.0298 7   SER   B C   
1859 O  O   . SER   B 7   ? 0.2143 0.2527 0.2147 -0.0005 0.0053  -0.0259 7   SER   B O   
1860 C  CB  . SER   B 7   ? 0.3012 0.3495 0.3068 -0.0029 0.0070  -0.0334 7   SER   B CB  
1861 O  OG  . SER   B 7   ? 0.3823 0.4295 0.3925 -0.0057 0.0094  -0.0362 7   SER   B OG  
1862 N  N   . SER   B 8   ? 0.2172 0.2605 0.2235 -0.0041 0.0082  -0.0319 8   SER   B N   
1863 C  CA  . SER   B 8   ? 0.2098 0.2473 0.2158 -0.0049 0.0090  -0.0295 8   SER   B CA  
1864 C  C   . SER   B 8   ? 0.1936 0.2319 0.1966 -0.0029 0.0073  -0.0275 8   SER   B C   
1865 O  O   . SER   B 8   ? 0.1828 0.2160 0.1838 -0.0023 0.0068  -0.0241 8   SER   B O   
1866 C  CB  . SER   B 8   ? 0.2331 0.2705 0.2428 -0.0080 0.0116  -0.0322 8   SER   B CB  
1867 O  OG  . SER   B 8   ? 0.2366 0.2722 0.2494 -0.0097 0.0132  -0.0337 8   SER   B OG  
1868 N  N   . LEU   B 9   ? 0.2057 0.2508 0.2085 -0.0018 0.0063  -0.0299 9   LEU   B N   
1869 C  CA  . LEU   B 9   ? 0.2224 0.2685 0.2227 0.0005  0.0046  -0.0284 9   LEU   B CA  
1870 C  C   . LEU   B 9   ? 0.2149 0.2574 0.2116 0.0031  0.0027  -0.0245 9   LEU   B C   
1871 O  O   . LEU   B 9   ? 0.2053 0.2443 0.1999 0.0043  0.0019  -0.0219 9   LEU   B O   
1872 C  CB  . LEU   B 9   ? 0.2645 0.3191 0.2655 0.0016  0.0037  -0.0318 9   LEU   B CB  
1873 C  CG  . LEU   B 9   ? 0.3111 0.3674 0.3104 0.0040  0.0020  -0.0309 9   LEU   B CG  
1874 C  CD1 . LEU   B 9   ? 0.3303 0.3838 0.3306 0.0021  0.0034  -0.0308 9   LEU   B CD1 
1875 C  CD2 . LEU   B 9   ? 0.3387 0.4039 0.3386 0.0057  0.0009  -0.0342 9   LEU   B CD2 
1876 N  N   . ARG   B 10  ? 0.2043 0.2480 0.2002 0.0039  0.0021  -0.0245 10  ARG   B N   
1877 C  CA  . ARG   B 10  ? 0.2006 0.2410 0.1931 0.0060  0.0006  -0.0211 10  ARG   B CA  
1878 C  C   . ARG   B 10  ? 0.1739 0.2068 0.1657 0.0051  0.0012  -0.0181 10  ARG   B C   
1879 O  O   . ARG   B 10  ? 0.1737 0.2032 0.1631 0.0066  0.0003  -0.0153 10  ARG   B O   
1880 C  CB  . ARG   B 10  ? 0.2414 0.2853 0.2337 0.0061  0.0004  -0.0223 10  ARG   B CB  
1881 C  CG  . ARG   B 10  ? 0.2757 0.3185 0.2642 0.0084  -0.0012 -0.0194 10  ARG   B CG  
1882 C  CD  . ARG   B 10  ? 0.2817 0.3292 0.2706 0.0079  -0.0011 -0.0214 10  ARG   B CD  
1883 N  NE  . ARG   B 10  ? 0.2905 0.3351 0.2758 0.0093  -0.0020 -0.0182 10  ARG   B NE  
1884 C  CZ  . ARG   B 10  ? 0.2676 0.3136 0.2524 0.0087  -0.0018 -0.0185 10  ARG   B CZ  
1885 N  NH1 . ARG   B 10  ? 0.2921 0.3415 0.2801 0.0066  -0.0006 -0.0219 10  ARG   B NH1 
1886 N  NH2 . ARG   B 10  ? 0.2779 0.3217 0.2590 0.0101  -0.0027 -0.0155 10  ARG   B NH2 
1887 N  N   . ALA   B 11  ? 0.1591 0.1896 0.1534 0.0028  0.0029  -0.0188 11  ALA   B N   
1888 C  CA  . ALA   B 11  ? 0.1578 0.1818 0.1517 0.0022  0.0035  -0.0161 11  ALA   B CA  
1889 C  C   . ALA   B 11  ? 0.1563 0.1778 0.1495 0.0021  0.0035  -0.0145 11  ALA   B C   
1890 O  O   . ALA   B 11  ? 0.1625 0.1799 0.1538 0.0028  0.0030  -0.0117 11  ALA   B O   
1891 C  CB  . ALA   B 11  ? 0.1691 0.1912 0.1662 0.0000  0.0053  -0.0173 11  ALA   B CB  
1892 N  N   . LEU   B 12  ? 0.1574 0.1818 0.1522 0.0011  0.0042  -0.0165 12  LEU   B N   
1893 C  CA  . LEU   B 12  ? 0.1606 0.1833 0.1548 0.0008  0.0045  -0.0154 12  LEU   B CA  
1894 C  C   . LEU   B 12  ? 0.1648 0.1872 0.1562 0.0032  0.0027  -0.0136 12  LEU   B C   
1895 O  O   . LEU   B 12  ? 0.1592 0.1782 0.1493 0.0033  0.0026  -0.0114 12  LEU   B O   
1896 C  CB  . LEU   B 12  ? 0.1711 0.1979 0.1675 -0.0008 0.0056  -0.0184 12  LEU   B CB  
1897 C  CG  . LEU   B 12  ? 0.1770 0.2031 0.1731 -0.0016 0.0061  -0.0177 12  LEU   B CG  
1898 C  CD1 . LEU   B 12  ? 0.2065 0.2346 0.2053 -0.0044 0.0083  -0.0204 12  LEU   B CD1 
1899 C  CD2 . LEU   B 12  ? 0.1889 0.2183 0.1835 0.0006  0.0045  -0.0181 12  LEU   B CD2 
1900 N  N   . LYS   B 13  ? 0.1562 0.1822 0.1466 0.0052  0.0013  -0.0145 13  LYS   B N   
1901 C  CA  . LYS   B 13  ? 0.1707 0.1963 0.1588 0.0076  -0.0003 -0.0130 13  LYS   B CA  
1902 C  C   . LYS   B 13  ? 0.1695 0.1903 0.1553 0.0085  -0.0008 -0.0100 13  LYS   B C   
1903 O  O   . LYS   B 13  ? 0.1629 0.1822 0.1468 0.0104  -0.0019 -0.0085 13  LYS   B O   
1904 C  CB  . LYS   B 13  ? 0.1972 0.2280 0.1850 0.0098  -0.0015 -0.0146 13  LYS   B CB  
1905 C  CG  . LYS   B 13  ? 0.2178 0.2541 0.2079 0.0091  -0.0011 -0.0179 13  LYS   B CG  
1906 C  CD  . LYS   B 13  ? 0.2527 0.2954 0.2427 0.0114  -0.0025 -0.0199 13  LYS   B CD  
1907 C  CE  . LYS   B 13  ? 0.2848 0.3329 0.2775 0.0103  -0.0018 -0.0234 13  LYS   B CE  
1908 N  NZ  . LYS   B 13  ? 0.3237 0.3788 0.3166 0.0128  -0.0033 -0.0255 13  LYS   B NZ  
1909 N  N   . LEU   B 14  ? 0.1528 0.1714 0.1391 0.0072  -0.0001 -0.0095 14  LEU   B N   
1910 C  CA  . LEU   B 14  ? 0.1592 0.1736 0.1437 0.0076  -0.0004 -0.0070 14  LEU   B CA  
1911 C  C   . LEU   B 14  ? 0.1492 0.1597 0.1343 0.0062  0.0005  -0.0057 14  LEU   B C   
1912 O  O   . LEU   B 14  ? 0.1467 0.1542 0.1309 0.0063  0.0005  -0.0040 14  LEU   B O   
1913 C  CB  . LEU   B 14  ? 0.1563 0.1718 0.1409 0.0075  -0.0003 -0.0076 14  LEU   B CB  
1914 C  CG  . LEU   B 14  ? 0.1707 0.1904 0.1541 0.0091  -0.0013 -0.0085 14  LEU   B CG  
1915 C  CD1 . LEU   B 14  ? 0.1742 0.1958 0.1581 0.0083  -0.0010 -0.0096 14  LEU   B CD1 
1916 C  CD2 . LEU   B 14  ? 0.1650 0.1829 0.1453 0.0113  -0.0025 -0.0063 14  LEU   B CD2 
1917 N  N   . MET   B 15  ? 0.1464 0.1572 0.1329 0.0050  0.0013  -0.0062 15  MET   B N   
1918 C  CA  . MET   B 15  ? 0.1619 0.1694 0.1488 0.0038  0.0022  -0.0046 15  MET   B CA  
1919 C  C   . MET   B 15  ? 0.1591 0.1649 0.1442 0.0045  0.0016  -0.0028 15  MET   B C   
1920 O  O   . MET   B 15  ? 0.1658 0.1731 0.1501 0.0053  0.0010  -0.0034 15  MET   B O   
1921 C  CB  . MET   B 15  ? 0.1813 0.1894 0.1702 0.0019  0.0035  -0.0055 15  MET   B CB  
1922 C  CG  . MET   B 15  ? 0.2301 0.2382 0.2214 0.0006  0.0047  -0.0069 15  MET   B CG  
1923 S  SD  . MET   B 15  ? 0.2917 0.2983 0.2850 -0.0018 0.0067  -0.0069 15  MET   B SD  
1924 C  CE  . MET   B 15  ? 0.3289 0.3305 0.3210 -0.0014 0.0066  -0.0032 15  MET   B CE  
1925 N  N   . ASP   B 16  ? 0.1502 0.1530 0.1347 0.0043  0.0016  -0.0010 16  ASP   B N   
1926 C  CA  . ASP   B 16  ? 0.1643 0.1660 0.1477 0.0043  0.0015  0.0004  16  ASP   B CA  
1927 C  C   . ASP   B 16  ? 0.1595 0.1606 0.1438 0.0029  0.0025  0.0012  16  ASP   B C   
1928 O  O   . ASP   B 16  ? 0.1737 0.1729 0.1587 0.0025  0.0029  0.0023  16  ASP   B O   
1929 C  CB  . ASP   B 16  ? 0.1705 0.1701 0.1528 0.0049  0.0010  0.0018  16  ASP   B CB  
1930 C  CG  . ASP   B 16  ? 0.1882 0.1874 0.1691 0.0061  0.0003  0.0015  16  ASP   B CG  
1931 O  OD1 . ASP   B 16  ? 0.1845 0.1852 0.1652 0.0069  -0.0001 0.0005  16  ASP   B OD1 
1932 O  OD2 . ASP   B 16  ? 0.2091 0.2066 0.1891 0.0063  0.0001  0.0024  16  ASP   B OD2 
1933 N  N   . LEU   B 17  ? 0.1578 0.1608 0.1422 0.0022  0.0029  0.0006  17  LEU   B N   
1934 C  CA  . LEU   B 17  ? 0.1724 0.1749 0.1576 0.0006  0.0041  0.0014  17  LEU   B CA  
1935 C  C   . LEU   B 17  ? 0.1983 0.1997 0.1821 0.0005  0.0040  0.0037  17  LEU   B C   
1936 O  O   . LEU   B 17  ? 0.1918 0.1947 0.1743 0.0009  0.0034  0.0036  17  LEU   B O   
1937 C  CB  . LEU   B 17  ? 0.1746 0.1800 0.1604 -0.0004 0.0048  -0.0005 17  LEU   B CB  
1938 C  CG  . LEU   B 17  ? 0.1884 0.1933 0.1751 -0.0025 0.0065  0.0001  17  LEU   B CG  
1939 C  CD1 . LEU   B 17  ? 0.2049 0.2078 0.1936 -0.0032 0.0074  -0.0004 17  LEU   B CD1 
1940 C  CD2 . LEU   B 17  ? 0.1952 0.2036 0.1822 -0.0037 0.0071  -0.0020 17  LEU   B CD2 
1941 N  N   . SER   B 18  ? 0.2578 0.2567 0.2419 0.0000  0.0046  0.0057  18  SER   B N   
1942 C  CA  A SER   B 18  ? 0.3036 0.3023 0.2862 0.0001  0.0045  0.0081  18  SER   B CA  
1943 C  CA  B SER   B 18  ? 0.3167 0.3155 0.2993 0.0001  0.0045  0.0080  18  SER   B CA  
1944 C  C   . SER   B 18  ? 0.3628 0.3605 0.3455 -0.0014 0.0058  0.0097  18  SER   B C   
1945 O  O   . SER   B 18  ? 0.3403 0.3367 0.3247 -0.0024 0.0070  0.0090  18  SER   B O   
1946 C  CB  A SER   B 18  ? 0.3199 0.3169 0.3024 0.0014  0.0037  0.0094  18  SER   B CB  
1947 C  CB  B SER   B 18  ? 0.3525 0.3497 0.3348 0.0014  0.0036  0.0094  18  SER   B CB  
1948 O  OG  A SER   B 18  ? 0.3115 0.3059 0.2959 0.0014  0.0042  0.0096  18  SER   B OG  
1949 O  OG  B SER   B 18  ? 0.3744 0.3731 0.3551 0.0016  0.0031  0.0109  18  SER   B OG  
1950 N  N   . THR   B 19  ? 0.4200 0.4187 0.4008 -0.0016 0.0058  0.0117  19  THR   B N   
1951 C  CA  . THR   B 19  ? 0.4925 0.4902 0.4728 -0.0030 0.0072  0.0138  19  THR   B CA  
1952 C  C   . THR   B 19  ? 0.5549 0.5482 0.5364 -0.0026 0.0077  0.0159  19  THR   B C   
1953 O  O   . THR   B 19  ? 0.5630 0.5557 0.5444 -0.0009 0.0066  0.0171  19  THR   B O   
1954 C  CB  . THR   B 19  ? 0.5278 0.5280 0.5056 -0.0031 0.0068  0.0158  19  THR   B CB  
1955 O  OG1 . THR   B 19  ? 0.6068 0.6067 0.5840 -0.0013 0.0055  0.0172  19  THR   B OG1 
1956 C  CG2 . THR   B 19  ? 0.5419 0.5466 0.5187 -0.0037 0.0065  0.0136  19  THR   B CG2 
1957 N  N   . GLY   B 22  ? 0.5142 0.5107 0.4902 0.0018  0.0044  0.0242  22  GLY   B N   
1958 C  CA  . GLY   B 22  ? 0.4369 0.4380 0.4118 0.0019  0.0033  0.0221  22  GLY   B CA  
1959 C  C   . GLY   B 22  ? 0.4873 0.4920 0.4602 0.0003  0.0039  0.0221  22  GLY   B C   
1960 O  O   . GLY   B 22  ? 0.5015 0.5057 0.4731 -0.0007 0.0049  0.0244  22  GLY   B O   
1961 N  N   . ASP   B 23  ? 0.4004 0.4087 0.3731 0.0001  0.0034  0.0193  23  ASP   B N   
1962 C  CA  . ASP   B 23  ? 0.3782 0.3906 0.3495 -0.0014 0.0038  0.0182  23  ASP   B CA  
1963 C  C   . ASP   B 23  ? 0.4185 0.4355 0.3878 -0.0010 0.0031  0.0194  23  ASP   B C   
1964 O  O   . ASP   B 23  ? 0.4285 0.4477 0.3981 -0.0001 0.0021  0.0179  23  ASP   B O   
1965 C  CB  . ASP   B 23  ? 0.3629 0.3766 0.3356 -0.0015 0.0035  0.0144  23  ASP   B CB  
1966 C  CG  . ASP   B 23  ? 0.3633 0.3760 0.3371 0.0001  0.0024  0.0130  23  ASP   B CG  
1967 O  OD1 . ASP   B 23  ? 0.4016 0.4107 0.3764 0.0009  0.0023  0.0137  23  ASP   B OD1 
1968 O  OD2 . ASP   B 23  ? 0.2962 0.3117 0.2699 0.0003  0.0019  0.0112  23  ASP   B OD2 
1969 N  N   . TYR   B 24  ? 0.3947 0.4135 0.3618 -0.0019 0.0037  0.0221  24  TYR   B N   
1970 C  CA  . TYR   B 24  ? 0.4262 0.4503 0.3911 -0.0016 0.0030  0.0232  24  TYR   B CA  
1971 C  C   . TYR   B 24  ? 0.4130 0.4417 0.3762 -0.0037 0.0039  0.0224  24  TYR   B C   
1972 O  O   . TYR   B 24  ? 0.4006 0.4348 0.3618 -0.0039 0.0036  0.0231  24  TYR   B O   
1973 C  CB  . TYR   B 24  ? 0.4597 0.4820 0.4229 -0.0004 0.0028  0.0279  24  TYR   B CB  
1974 C  CG  . TYR   B 24  ? 0.4456 0.4652 0.4104 0.0019  0.0016  0.0284  24  TYR   B CG  
1975 C  CD1 . TYR   B 24  ? 0.4596 0.4733 0.4269 0.0024  0.0019  0.0280  24  TYR   B CD1 
1976 C  CD2 . TYR   B 24  ? 0.4549 0.4786 0.4191 0.0035  0.0002  0.0288  24  TYR   B CD2 
1977 C  CE1 . TYR   B 24  ? 0.4630 0.4747 0.4318 0.0043  0.0009  0.0282  24  TYR   B CE1 
1978 C  CE2 . TYR   B 24  ? 0.4888 0.5105 0.4545 0.0055  -0.0008 0.0289  24  TYR   B CE2 
1979 C  CZ  . TYR   B 24  ? 0.5121 0.5278 0.4802 0.0059  -0.0004 0.0286  24  TYR   B CZ  
1980 O  OH  . TYR   B 24  ? 0.5447 0.5589 0.5146 0.0078  -0.0014 0.0284  24  TYR   B OH  
1981 N  N   . THR   B 25  ? 0.3302 0.3570 0.2942 -0.0053 0.0052  0.0211  25  THR   B N   
1982 C  CA  . THR   B 25  ? 0.3297 0.3610 0.2927 -0.0074 0.0062  0.0199  25  THR   B CA  
1983 C  C   . THR   B 25  ? 0.2926 0.3238 0.2582 -0.0080 0.0065  0.0155  25  THR   B C   
1984 O  O   . THR   B 25  ? 0.2544 0.2811 0.2219 -0.0074 0.0065  0.0146  25  THR   B O   
1985 C  CB  . THR   B 25  ? 0.3199 0.3496 0.2807 -0.0090 0.0077  0.0234  25  THR   B CB  
1986 O  OG1 . THR   B 25  ? 0.2886 0.3127 0.2514 -0.0096 0.0088  0.0231  25  THR   B OG1 
1987 C  CG2 . THR   B 25  ? 0.3104 0.3392 0.2687 -0.0078 0.0073  0.0283  25  THR   B CG2 
1988 N  N   . ASP   B 26  ? 0.3218 0.3583 0.2871 -0.0093 0.0068  0.0129  26  ASP   B N   
1989 C  CA  . ASP   B 26  ? 0.3056 0.3430 0.2734 -0.0098 0.0071  0.0087  26  ASP   B CA  
1990 C  C   . ASP   B 26  ? 0.2920 0.3261 0.2605 -0.0109 0.0084  0.0090  26  ASP   B C   
1991 O  O   . ASP   B 26  ? 0.2582 0.2903 0.2291 -0.0104 0.0083  0.0066  26  ASP   B O   
1992 C  CB  . ASP   B 26  ? 0.3528 0.3969 0.3203 -0.0111 0.0074  0.0059  26  ASP   B CB  
1993 C  CG  . ASP   B 26  ? 0.3841 0.4317 0.3518 -0.0100 0.0063  0.0043  26  ASP   B CG  
1994 O  OD1 . ASP   B 26  ? 0.3603 0.4049 0.3288 -0.0082 0.0053  0.0047  26  ASP   B OD1 
1995 O  OD2 . ASP   B 26  ? 0.4644 0.5182 0.4317 -0.0112 0.0067  0.0023  26  ASP   B OD2 
1996 N  N   . GLU   B 27  ? 0.2618 0.2956 0.2283 -0.0127 0.0097  0.0120  27  GLU   B N   
1997 C  CA  . GLU   B 27  ? 0.2741 0.3050 0.2414 -0.0143 0.0113  0.0121  27  GLU   B CA  
1998 C  C   . GLU   B 27  ? 0.2566 0.2815 0.2259 -0.0128 0.0109  0.0123  27  GLU   B C   
1999 O  O   . GLU   B 27  ? 0.2664 0.2903 0.2379 -0.0133 0.0115  0.0098  27  GLU   B O   
2000 C  CB  . GLU   B 27  ? 0.3240 0.3545 0.2884 -0.0162 0.0129  0.0160  27  GLU   B CB  
2001 C  CG  . GLU   B 27  ? 0.3889 0.4166 0.3542 -0.0185 0.0150  0.0158  27  GLU   B CG  
2002 C  CD  . GLU   B 27  ? 0.4627 0.4887 0.4252 -0.0207 0.0169  0.0200  27  GLU   B CD  
2003 O  OE1 . GLU   B 27  ? 0.4877 0.5149 0.4469 -0.0205 0.0168  0.0237  27  GLU   B OE1 
2004 O  OE2 . GLU   B 27  ? 0.4801 0.5035 0.4439 -0.0226 0.0188  0.0192  27  GLU   B OE2 
2005 N  N   . LYS   B 28  ? 0.2375 0.2590 0.2063 -0.0110 0.0099  0.0150  28  LYS   B N   
2006 C  CA  . LYS   B 28  ? 0.2541 0.2704 0.2249 -0.0096 0.0096  0.0151  28  LYS   B CA  
2007 C  C   . LYS   B 28  ? 0.2271 0.2442 0.2002 -0.0083 0.0084  0.0114  28  LYS   B C   
2008 O  O   . LYS   B 28  ? 0.2101 0.2245 0.1852 -0.0080 0.0086  0.0100  28  LYS   B O   
2009 C  CB  . LYS   B 28  ? 0.2848 0.2980 0.2549 -0.0078 0.0086  0.0184  28  LYS   B CB  
2010 C  CG  . LYS   B 28  ? 0.3363 0.3470 0.3046 -0.0085 0.0097  0.0227  28  LYS   B CG  
2011 C  CD  . LYS   B 28  ? 0.3662 0.3713 0.3362 -0.0092 0.0112  0.0235  28  LYS   B CD  
2012 C  CE  . LYS   B 28  ? 0.4184 0.4197 0.3904 -0.0070 0.0101  0.0235  28  LYS   B CE  
2013 N  NZ  . LYS   B 28  ? 0.4339 0.4305 0.4084 -0.0077 0.0114  0.0230  28  LYS   B NZ  
2014 N  N   . VAL   B 29  ? 0.2055 0.2260 0.1782 -0.0074 0.0072  0.0098  29  VAL   B N   
2015 C  CA  . VAL   B 29  ? 0.2023 0.2229 0.1769 -0.0059 0.0062  0.0067  29  VAL   B CA  
2016 C  C   . VAL   B 29  ? 0.2028 0.2253 0.1790 -0.0068 0.0068  0.0036  29  VAL   B C   
2017 O  O   . VAL   B 29  ? 0.1924 0.2135 0.1703 -0.0058 0.0064  0.0018  29  VAL   B O   
2018 C  CB  . VAL   B 29  ? 0.2109 0.2345 0.1850 -0.0050 0.0052  0.0055  29  VAL   B CB  
2019 C  CG1 . VAL   B 29  ? 0.2089 0.2323 0.1850 -0.0036 0.0044  0.0024  29  VAL   B CG1 
2020 C  CG2 . VAL   B 29  ? 0.2285 0.2511 0.2014 -0.0040 0.0044  0.0080  29  VAL   B CG2 
2021 N  N   . ILE   B 30  ? 0.1906 0.2171 0.1661 -0.0086 0.0078  0.0028  30  ILE   B N   
2022 C  CA  . ILE   B 30  ? 0.2086 0.2380 0.1857 -0.0095 0.0084  -0.0004 30  ILE   B CA  
2023 C  C   . ILE   B 30  ? 0.2114 0.2380 0.1896 -0.0103 0.0094  -0.0004 30  ILE   B C   
2024 O  O   . ILE   B 30  ? 0.2417 0.2690 0.2220 -0.0095 0.0091  -0.0031 30  ILE   B O   
2025 C  CB  . ILE   B 30  ? 0.2232 0.2578 0.1992 -0.0116 0.0095  -0.0012 30  ILE   B CB  
2026 C  CG1 . ILE   B 30  ? 0.2284 0.2665 0.2040 -0.0107 0.0085  -0.0025 30  ILE   B CG1 
2027 C  CG2 . ILE   B 30  ? 0.2401 0.2777 0.2178 -0.0130 0.0105  -0.0045 30  ILE   B CG2 
2028 C  CD1 . ILE   B 30  ? 0.2487 0.2921 0.2226 -0.0129 0.0095  -0.0025 30  ILE   B CD1 
2029 N  N   . ALA   B 31  ? 0.2090 0.2325 0.1861 -0.0115 0.0106  0.0028  31  ALA   B N   
2030 C  CA  . ALA   B 31  ? 0.2164 0.2369 0.1949 -0.0126 0.0118  0.0027  31  ALA   B CA  
2031 C  C   . ALA   B 31  ? 0.2090 0.2266 0.1893 -0.0105 0.0106  0.0018  31  ALA   B C   
2032 O  O   . ALA   B 31  ? 0.2094 0.2271 0.1917 -0.0108 0.0111  -0.0004 31  ALA   B O   
2033 C  CB  . ALA   B 31  ? 0.2271 0.2439 0.2042 -0.0140 0.0132  0.0066  31  ALA   B CB  
2034 N  N   . LEU   B 32  ? 0.2057 0.2213 0.1853 -0.0085 0.0092  0.0035  32  LEU   B N   
2035 C  CA  . LEU   B 32  ? 0.1839 0.1971 0.1648 -0.0065 0.0081  0.0028  32  LEU   B CA  
2036 C  C   . LEU   B 32  ? 0.1774 0.1935 0.1597 -0.0055 0.0072  -0.0007 32  LEU   B C   
2037 O  O   . LEU   B 32  ? 0.1720 0.1876 0.1558 -0.0049 0.0071  -0.0022 32  LEU   B O   
2038 C  CB  . LEU   B 32  ? 0.1825 0.1938 0.1622 -0.0048 0.0067  0.0047  32  LEU   B CB  
2039 C  CG  . LEU   B 32  ? 0.1848 0.1939 0.1656 -0.0029 0.0056  0.0040  32  LEU   B CG  
2040 C  CD1 . LEU   B 32  ? 0.1992 0.2052 0.1813 -0.0033 0.0064  0.0046  32  LEU   B CD1 
2041 C  CD2 . LEU   B 32  ? 0.1871 0.1952 0.1667 -0.0015 0.0045  0.0055  32  LEU   B CD2 
2042 N  N   . CYS   B 33  ? 0.1775 0.1969 0.1593 -0.0051 0.0066  -0.0020 33  CYS   B N   
2043 C  CA  . CYS   B 33  ? 0.1883 0.2103 0.1714 -0.0037 0.0058  -0.0051 33  CYS   B CA  
2044 C  C   . CYS   B 33  ? 0.1959 0.2204 0.1807 -0.0049 0.0067  -0.0075 33  CYS   B C   
2045 O  O   . CYS   B 33  ? 0.1812 0.2066 0.1674 -0.0036 0.0061  -0.0094 33  CYS   B O   
2046 C  CB  . CYS   B 33  ? 0.1842 0.2095 0.1670 -0.0035 0.0054  -0.0064 33  CYS   B CB  
2047 S  SG  . CYS   B 33  ? 0.2179 0.2411 0.1993 -0.0021 0.0043  -0.0047 33  CYS   B SG  
2048 N  N   . HIS   B 34  ? 0.1939 0.2201 0.1784 -0.0075 0.0084  -0.0074 34  HIS   B N   
2049 C  CA  . HIS   B 34  ? 0.2117 0.2405 0.1980 -0.0091 0.0096  -0.0099 34  HIS   B CA  
2050 C  C   . HIS   B 34  ? 0.2101 0.2362 0.1977 -0.0091 0.0100  -0.0099 34  HIS   B C   
2051 O  O   . HIS   B 34  ? 0.1977 0.2266 0.1873 -0.0089 0.0100  -0.0129 34  HIS   B O   
2052 C  CB  . HIS   B 34  ? 0.2290 0.2591 0.2145 -0.0123 0.0117  -0.0093 34  HIS   B CB  
2053 C  CG  . HIS   B 34  ? 0.2473 0.2816 0.2319 -0.0126 0.0115  -0.0103 34  HIS   B CG  
2054 N  ND1 . HIS   B 34  ? 0.2894 0.3253 0.2725 -0.0153 0.0131  -0.0091 34  HIS   B ND1 
2055 C  CD2 . HIS   B 34  ? 0.2421 0.2794 0.2273 -0.0107 0.0100  -0.0123 34  HIS   B CD2 
2056 C  CE1 . HIS   B 34  ? 0.2740 0.3142 0.2567 -0.0150 0.0125  -0.0107 34  HIS   B CE1 
2057 N  NE2 . HIS   B 34  ? 0.2818 0.3228 0.2660 -0.0122 0.0107  -0.0127 34  HIS   B NE2 
2058 N  N   . GLN   B 35  ? 0.1960 0.2173 0.1828 -0.0092 0.0103  -0.0069 35  GLN   B N   
2059 C  CA  . GLN   B 35  ? 0.2014 0.2201 0.1897 -0.0094 0.0108  -0.0070 35  GLN   B CA  
2060 C  C   . GLN   B 35  ? 0.1805 0.1999 0.1697 -0.0069 0.0091  -0.0086 35  GLN   B C   
2061 O  O   . GLN   B 35  ? 0.1776 0.1976 0.1686 -0.0072 0.0095  -0.0104 35  GLN   B O   
2062 C  CB  . GLN   B 35  ? 0.2616 0.2750 0.2487 -0.0097 0.0113  -0.0032 35  GLN   B CB  
2063 C  CG  . GLN   B 35  ? 0.3603 0.3703 0.3492 -0.0102 0.0122  -0.0030 35  GLN   B CG  
2064 C  CD  . GLN   B 35  ? 0.5099 0.5148 0.4977 -0.0101 0.0124  0.0008  35  GLN   B CD  
2065 O  OE1 . GLN   B 35  ? 0.5864 0.5907 0.5720 -0.0093 0.0117  0.0033  35  GLN   B OE1 
2066 N  NE2 . GLN   B 35  ? 0.5382 0.5397 0.5279 -0.0107 0.0135  0.0011  35  GLN   B NE2 
2067 N  N   . ALA   B 36  ? 0.1586 0.1780 0.1465 -0.0047 0.0074  -0.0079 36  ALA   B N   
2068 C  CA  . ALA   B 36  ? 0.1635 0.1831 0.1516 -0.0022 0.0057  -0.0088 36  ALA   B CA  
2069 C  C   . ALA   B 36  ? 0.1680 0.1924 0.1576 -0.0014 0.0053  -0.0122 36  ALA   B C   
2070 O  O   . ALA   B 36  ? 0.1689 0.1940 0.1589 0.0003  0.0042  -0.0131 36  ALA   B O   
2071 C  CB  . ALA   B 36  ? 0.1675 0.1855 0.1539 -0.0003 0.0043  -0.0072 36  ALA   B CB  
2072 N  N   . LYS   B 37  ? 0.1692 0.1973 0.1595 -0.0026 0.0060  -0.0141 37  LYS   B N   
2073 C  CA  . LYS   B 37  ? 0.1754 0.2089 0.1674 -0.0019 0.0056  -0.0176 37  LYS   B CA  
2074 C  C   . LYS   B 37  ? 0.1718 0.2073 0.1657 -0.0044 0.0073  -0.0196 37  LYS   B C   
2075 O  O   . LYS   B 37  ? 0.1897 0.2269 0.1842 -0.0070 0.0090  -0.0206 37  LYS   B O   
2076 C  CB  . LYS   B 37  ? 0.1905 0.2273 0.1825 -0.0018 0.0054  -0.0190 37  LYS   B CB  
2077 C  CG  . LYS   B 37  ? 0.1921 0.2351 0.1861 -0.0008 0.0049  -0.0229 37  LYS   B CG  
2078 C  CD  . LYS   B 37  ? 0.2228 0.2692 0.2172 -0.0013 0.0052  -0.0245 37  LYS   B CD  
2079 C  CE  . LYS   B 37  ? 0.2440 0.2967 0.2407 0.0003  0.0044  -0.0285 37  LYS   B CE  
2080 N  NZ  . LYS   B 37  ? 0.2633 0.3194 0.2605 -0.0005 0.0048  -0.0302 37  LYS   B NZ  
2081 N  N   . THR   B 38  ? 0.1751 0.2100 0.1698 -0.0039 0.0072  -0.0200 38  THR   B N   
2082 C  CA  . THR   B 38  ? 0.1841 0.2200 0.1809 -0.0065 0.0091  -0.0218 38  THR   B CA  
2083 C  C   . THR   B 38  ? 0.1833 0.2263 0.1823 -0.0064 0.0090  -0.0262 38  THR   B C   
2084 O  O   . THR   B 38  ? 0.1715 0.2180 0.1703 -0.0036 0.0071  -0.0275 38  THR   B O   
2085 C  CB  . THR   B 38  ? 0.1925 0.2248 0.1896 -0.0063 0.0092  -0.0206 38  THR   B CB  
2086 O  OG1 . THR   B 38  ? 0.1722 0.2085 0.1704 -0.0047 0.0081  -0.0231 38  THR   B OG1 
2087 C  CG2 . THR   B 38  ? 0.2026 0.2293 0.1974 -0.0048 0.0081  -0.0167 38  THR   B CG2 
2088 N  N   . PRO   B 39  ? 0.2086 0.2537 0.2099 -0.0093 0.0112  -0.0288 39  PRO   B N   
2089 C  CA  . PRO   B 39  ? 0.2004 0.2530 0.2041 -0.0094 0.0112  -0.0335 39  PRO   B CA  
2090 C  C   . PRO   B 39  ? 0.1926 0.2489 0.1968 -0.0064 0.0092  -0.0350 39  PRO   B C   
2091 O  O   . PRO   B 39  ? 0.1929 0.2563 0.1987 -0.0055 0.0086  -0.0387 39  PRO   B O   
2092 C  CB  . PRO   B 39  ? 0.2312 0.2839 0.2373 -0.0136 0.0143  -0.0355 39  PRO   B CB  
2093 C  CG  . PRO   B 39  ? 0.2359 0.2815 0.2403 -0.0157 0.0159  -0.0315 39  PRO   B CG  
2094 C  CD  . PRO   B 39  ? 0.2171 0.2576 0.2189 -0.0127 0.0138  -0.0274 39  PRO   B CD  
2095 N  N   . VAL   B 40  ? 0.1746 0.2264 0.1775 -0.0050 0.0083  -0.0324 40  VAL   B N   
2096 C  CA  . VAL   B 40  ? 0.1793 0.2345 0.1823 -0.0026 0.0067  -0.0336 40  VAL   B CA  
2097 C  C   . VAL   B 40  ? 0.1698 0.2223 0.1698 0.0011  0.0042  -0.0303 40  VAL   B C   
2098 O  O   . VAL   B 40  ? 0.1792 0.2337 0.1787 0.0034  0.0026  -0.0304 40  VAL   B O   
2099 C  CB  . VAL   B 40  ? 0.2069 0.2605 0.2113 -0.0044 0.0080  -0.0340 40  VAL   B CB  
2100 C  CG1 . VAL   B 40  ? 0.2287 0.2847 0.2364 -0.0082 0.0107  -0.0376 40  VAL   B CG1 
2101 C  CG2 . VAL   B 40  ? 0.2322 0.2774 0.2348 -0.0047 0.0083  -0.0298 40  VAL   B CG2 
2102 N  N   . GLY   B 41  ? 0.1693 0.2179 0.1677 0.0016  0.0038  -0.0277 41  GLY   B N   
2103 C  CA  . GLY   B 41  ? 0.1712 0.2169 0.1670 0.0048  0.0017  -0.0249 41  GLY   B CA  
2104 C  C   . GLY   B 41  ? 0.1584 0.1974 0.1525 0.0039  0.0022  -0.0214 41  GLY   B C   
2105 O  O   . GLY   B 41  ? 0.1615 0.1980 0.1561 0.0012  0.0040  -0.0208 41  GLY   B O   
2106 N  N   . ASN   B 42  ? 0.1664 0.2027 0.1584 0.0064  0.0007  -0.0192 42  ASN   B N   
2107 C  CA  . ASN   B 42  ? 0.1725 0.2034 0.1629 0.0060  0.0009  -0.0162 42  ASN   B CA  
2108 C  C   . ASN   B 42  ? 0.1524 0.1789 0.1416 0.0060  0.0008  -0.0139 42  ASN   B C   
2109 O  O   . ASN   B 42  ? 0.1573 0.1845 0.1461 0.0076  -0.0001 -0.0140 42  ASN   B O   
2110 C  CB  . ASN   B 42  ? 0.1669 0.1973 0.1562 0.0084  -0.0004 -0.0156 42  ASN   B CB  
2111 C  CG  . ASN   B 42  ? 0.1968 0.2317 0.1875 0.0083  -0.0004 -0.0182 42  ASN   B CG  
2112 O  OD1 . ASN   B 42  ? 0.2022 0.2395 0.1943 0.0058  0.0011  -0.0197 42  ASN   B OD1 
2113 N  ND2 . ASN   B 42  ? 0.1988 0.2348 0.1895 0.0110  -0.0017 -0.0187 42  ASN   B ND2 
2114 N  N   . THR   B 43  ? 0.1516 0.1739 0.1401 0.0045  0.0017  -0.0117 43  THR   B N   
2115 C  CA  . THR   B 43  ? 0.1488 0.1670 0.1362 0.0049  0.0014  -0.0094 43  THR   B CA  
2116 C  C   . THR   B 43  ? 0.1420 0.1587 0.1274 0.0073  -0.0001 -0.0082 43  THR   B C   
2117 O  O   . THR   B 43  ? 0.1450 0.1631 0.1302 0.0084  -0.0007 -0.0088 43  THR   B O   
2118 C  CB  . THR   B 43  ? 0.1556 0.1702 0.1429 0.0031  0.0025  -0.0075 43  THR   B CB  
2119 O  OG1 . THR   B 43  ? 0.1517 0.1657 0.1379 0.0031  0.0024  -0.0065 43  THR   B OG1 
2120 C  CG2 . THR   B 43  ? 0.1606 0.1758 0.1498 0.0007  0.0042  -0.0085 43  THR   B CG2 
2121 N  N   . ALA   B 44  ? 0.1377 0.1516 0.1220 0.0079  -0.0005 -0.0065 44  ALA   B N   
2122 C  CA  . ALA   B 44  ? 0.1446 0.1563 0.1270 0.0099  -0.0015 -0.0052 44  ALA   B CA  
2123 C  C   . ALA   B 44  ? 0.1421 0.1515 0.1239 0.0095  -0.0013 -0.0041 44  ALA   B C   
2124 O  O   . ALA   B 44  ? 0.1396 0.1483 0.1207 0.0110  -0.0019 -0.0040 44  ALA   B O   
2125 C  CB  . ALA   B 44  ? 0.1489 0.1583 0.1302 0.0101  -0.0016 -0.0039 44  ALA   B CB  
2126 N  N   . ALA   B 45  ? 0.1413 0.1495 0.1236 0.0077  -0.0004 -0.0033 45  ALA   B N   
2127 C  CA  . ALA   B 45  ? 0.1389 0.1454 0.1205 0.0072  -0.0002 -0.0022 45  ALA   B CA  
2128 C  C   . ALA   B 45  ? 0.1479 0.1549 0.1302 0.0053  0.0008  -0.0018 45  ALA   B C   
2129 O  O   . ALA   B 45  ? 0.1364 0.1437 0.1196 0.0042  0.0014  -0.0020 45  ALA   B O   
2130 C  CB  . ALA   B 45  ? 0.1413 0.1446 0.1216 0.0076  -0.0004 -0.0006 45  ALA   B CB  
2131 N  N   . ILE   B 46  ? 0.1570 0.1639 0.1386 0.0048  0.0009  -0.0011 46  ILE   B N   
2132 C  CA  . ILE   B 46  ? 0.1680 0.1745 0.1494 0.0033  0.0017  0.0003  46  ILE   B CA  
2133 C  C   . ILE   B 46  ? 0.1648 0.1694 0.1452 0.0037  0.0013  0.0018  46  ILE   B C   
2134 O  O   . ILE   B 46  ? 0.1692 0.1733 0.1491 0.0047  0.0007  0.0013  46  ILE   B O   
2135 C  CB  . ILE   B 46  ? 0.1846 0.1939 0.1660 0.0022  0.0022  -0.0003 46  ILE   B CB  
2136 C  CG1 . ILE   B 46  ? 0.2050 0.2158 0.1860 0.0030  0.0017  -0.0013 46  ILE   B CG1 
2137 C  CG2 . ILE   B 46  ? 0.1868 0.1983 0.1695 0.0015  0.0028  -0.0020 46  ILE   B CG2 
2138 C  CD1 . ILE   B 46  ? 0.2452 0.2593 0.2261 0.0018  0.0022  -0.0020 46  ILE   B CD1 
2139 N  N   . SER   B 47  ? 0.1619 0.1654 0.1422 0.0030  0.0016  0.0036  47  SER   B N   
2140 C  CA  A SER   B 47  ? 0.1593 0.1617 0.1389 0.0034  0.0013  0.0049  47  SER   B CA  
2141 C  CA  B SER   B 47  ? 0.1774 0.1798 0.1570 0.0034  0.0013  0.0048  47  SER   B CA  
2142 C  C   . SER   B 47  ? 0.1558 0.1598 0.1347 0.0026  0.0016  0.0062  47  SER   B C   
2143 O  O   . SER   B 47  ? 0.1624 0.1661 0.1415 0.0018  0.0022  0.0075  47  SER   B O   
2144 C  CB  A SER   B 47  ? 0.1630 0.1631 0.1434 0.0036  0.0013  0.0057  47  SER   B CB  
2145 C  CB  B SER   B 47  ? 0.2072 0.2073 0.1876 0.0037  0.0013  0.0056  47  SER   B CB  
2146 O  OG  A SER   B 47  ? 0.1534 0.1526 0.1339 0.0044  0.0009  0.0046  47  SER   B OG  
2147 O  OG  B SER   B 47  ? 0.2563 0.2557 0.2362 0.0042  0.0008  0.0063  47  SER   B OG  
2148 N  N   . VAL   B 48  ? 0.1557 0.1614 0.1338 0.0028  0.0012  0.0060  48  VAL   B N   
2149 C  CA  . VAL   B 48  ? 0.1658 0.1741 0.1429 0.0021  0.0013  0.0070  48  VAL   B CA  
2150 C  C   . VAL   B 48  ? 0.1629 0.1722 0.1396 0.0026  0.0008  0.0072  48  VAL   B C   
2151 O  O   . VAL   B 48  ? 0.1586 0.1667 0.1358 0.0032  0.0005  0.0060  48  VAL   B O   
2152 C  CB  . VAL   B 48  ? 0.1715 0.1831 0.1484 0.0013  0.0017  0.0056  48  VAL   B CB  
2153 C  CG1 . VAL   B 48  ? 0.1772 0.1886 0.1547 0.0005  0.0024  0.0052  48  VAL   B CG1 
2154 C  CG2 . VAL   B 48  ? 0.1762 0.1885 0.1536 0.0019  0.0014  0.0031  48  VAL   B CG2 
2155 N  N   . TYR   B 49  ? 0.1608 0.1729 0.1365 0.0023  0.0007  0.0085  49  TYR   B N   
2156 C  CA  . TYR   B 49  ? 0.1673 0.1817 0.1427 0.0026  0.0002  0.0081  49  TYR   B CA  
2157 C  C   . TYR   B 49  ? 0.1609 0.1778 0.1365 0.0021  0.0004  0.0053  49  TYR   B C   
2158 O  O   . TYR   B 49  ? 0.1580 0.1759 0.1337 0.0015  0.0008  0.0042  49  TYR   B O   
2159 C  CB  . TYR   B 49  ? 0.1977 0.2152 0.1717 0.0026  -0.0001 0.0103  49  TYR   B CB  
2160 C  CG  . TYR   B 49  ? 0.2262 0.2412 0.2004 0.0036  -0.0004 0.0130  49  TYR   B CG  
2161 C  CD1 . TYR   B 49  ? 0.2622 0.2752 0.2374 0.0046  -0.0008 0.0127  49  TYR   B CD1 
2162 C  CD2 . TYR   B 49  ? 0.2883 0.3025 0.2615 0.0035  0.0000  0.0158  49  TYR   B CD2 
2163 C  CE1 . TYR   B 49  ? 0.3083 0.3192 0.2840 0.0056  -0.0011 0.0149  49  TYR   B CE1 
2164 C  CE2 . TYR   B 49  ? 0.3267 0.3379 0.3004 0.0045  -0.0002 0.0182  49  TYR   B CE2 
2165 C  CZ  . TYR   B 49  ? 0.3733 0.3831 0.3485 0.0057  -0.0008 0.0177  49  TYR   B CZ  
2166 O  OH  . TYR   B 49  ? 0.4270 0.4341 0.4032 0.0070  -0.0010 0.0196  49  TYR   B OH  
2167 N  N   . PRO   B 50  ? 0.1670 0.1847 0.1430 0.0023  0.0002  0.0038  50  PRO   B N   
2168 C  CA  . PRO   B 50  ? 0.1626 0.1815 0.1394 0.0018  0.0006  0.0009  50  PRO   B CA  
2169 C  C   . PRO   B 50  ? 0.1593 0.1827 0.1359 0.0009  0.0009  -0.0001 50  PRO   B C   
2170 O  O   . PRO   B 50  ? 0.1524 0.1757 0.1299 0.0007  0.0014  -0.0021 50  PRO   B O   
2171 C  CB  . PRO   B 50  ? 0.1639 0.1839 0.1411 0.0018  0.0006  -0.0001 50  PRO   B CB  
2172 C  CG  . PRO   B 50  ? 0.1526 0.1696 0.1297 0.0026  0.0002  0.0018  50  PRO   B CG  
2173 C  CD  . PRO   B 50  ? 0.1526 0.1698 0.1288 0.0029  -0.0002 0.0045  50  PRO   B CD  
2174 N  N   . ARG   B 51  ? 0.1596 0.1871 0.1350 0.0005  0.0007  0.0012  51  ARG   B N   
2175 C  CA  . ARG   B 51  ? 0.1797 0.2124 0.1546 -0.0006 0.0011  0.0001  51  ARG   B CA  
2176 C  C   . ARG   B 51  ? 0.1797 0.2116 0.1545 -0.0011 0.0016  0.0002  51  ARG   B C   
2177 O  O   . ARG   B 51  ? 0.1585 0.1944 0.1334 -0.0021 0.0020  -0.0016 51  ARG   B O   
2178 C  CB  . ARG   B 51  ? 0.2076 0.2449 0.1806 -0.0008 0.0007  0.0023  51  ARG   B CB  
2179 C  CG  . ARG   B 51  ? 0.2552 0.2900 0.2268 -0.0003 0.0004  0.0062  51  ARG   B CG  
2180 C  CD  . ARG   B 51  ? 0.3470 0.3863 0.3164 -0.0002 0.0000  0.0087  51  ARG   B CD  
2181 N  NE  . ARG   B 51  ? 0.4335 0.4694 0.4019 0.0007  -0.0003 0.0127  51  ARG   B NE  
2182 C  CZ  . ARG   B 51  ? 0.5862 0.6186 0.5553 0.0022  -0.0009 0.0141  51  ARG   B CZ  
2183 N  NH1 . ARG   B 51  ? 0.5662 0.5990 0.5367 0.0028  -0.0014 0.0121  51  ARG   B NH1 
2184 N  NH2 . ARG   B 51  ? 0.6583 0.6871 0.6269 0.0028  -0.0008 0.0174  51  ARG   B NH2 
2185 N  N   . SER   B 52  ? 0.1623 0.1896 0.1371 -0.0005 0.0015  0.0019  52  SER   B N   
2186 C  CA  . SER   B 52  ? 0.1613 0.1880 0.1362 -0.0011 0.0020  0.0019  52  SER   B CA  
2187 C  C   . SER   B 52  ? 0.1493 0.1742 0.1260 -0.0005 0.0021  -0.0008 52  SER   B C   
2188 O  O   . SER   B 52  ? 0.1506 0.1758 0.1277 -0.0009 0.0025  -0.0015 52  SER   B O   
2189 C  CB  . SER   B 52  ? 0.1709 0.1939 0.1452 -0.0009 0.0021  0.0048  52  SER   B CB  
2190 O  OG  . SER   B 52  ? 0.2010 0.2255 0.1737 -0.0012 0.0021  0.0076  52  SER   B OG  
2191 N  N   . ILE   B 53  ? 0.1505 0.1734 0.1282 0.0004  0.0018  -0.0021 53  ILE   B N   
2192 C  CA  . ILE   B 53  ? 0.1493 0.1697 0.1284 0.0014  0.0017  -0.0040 53  ILE   B CA  
2193 C  C   . ILE   B 53  ? 0.1550 0.1787 0.1352 0.0010  0.0021  -0.0067 53  ILE   B C   
2194 O  O   . ILE   B 53  ? 0.1481 0.1711 0.1291 0.0016  0.0021  -0.0076 53  ILE   B O   
2195 C  CB  . ILE   B 53  ? 0.1505 0.1676 0.1301 0.0023  0.0016  -0.0046 53  ILE   B CB  
2196 C  CG1 . ILE   B 53  ? 0.1553 0.1691 0.1341 0.0027  0.0012  -0.0022 53  ILE   B CG1 
2197 C  CG2 . ILE   B 53  ? 0.1560 0.1706 0.1368 0.0035  0.0016  -0.0063 53  ILE   B CG2 
2198 C  CD1 . ILE   B 53  ? 0.1569 0.1683 0.1359 0.0031  0.0012  -0.0026 53  ILE   B CD1 
2199 N  N   . PRO   B 54  ? 0.1627 0.1905 0.1432 0.0001  0.0025  -0.0084 54  PRO   B N   
2200 C  CA  . PRO   B 54  ? 0.1688 0.2000 0.1509 -0.0001 0.0029  -0.0115 54  PRO   B CA  
2201 C  C   . PRO   B 54  ? 0.1598 0.1935 0.1416 -0.0009 0.0031  -0.0113 54  PRO   B C   
2202 O  O   . PRO   B 54  ? 0.1783 0.2121 0.1616 -0.0002 0.0031  -0.0133 54  PRO   B O   
2203 C  CB  . PRO   B 54  ? 0.1715 0.2073 0.1537 -0.0013 0.0033  -0.0131 54  PRO   B CB  
2204 C  CG  . PRO   B 54  ? 0.1724 0.2056 0.1541 -0.0009 0.0031  -0.0119 54  PRO   B CG  
2205 C  CD  . PRO   B 54  ? 0.1611 0.1910 0.1410 -0.0005 0.0025  -0.0082 54  PRO   B CD  
2206 N  N   . ILE   B 55  ? 0.1615 0.1968 0.1413 -0.0023 0.0034  -0.0088 55  ILE   B N   
2207 C  CA  . ILE   B 55  ? 0.1776 0.2151 0.1570 -0.0034 0.0040  -0.0087 55  ILE   B CA  
2208 C  C   . ILE   B 55  ? 0.1652 0.1986 0.1452 -0.0025 0.0038  -0.0079 55  ILE   B C   
2209 O  O   . ILE   B 55  ? 0.1793 0.2144 0.1602 -0.0029 0.0041  -0.0095 55  ILE   B O   
2210 C  CB  . ILE   B 55  ? 0.2189 0.2590 0.1958 -0.0052 0.0045  -0.0060 55  ILE   B CB  
2211 C  CG1 . ILE   B 55  ? 0.2646 0.3083 0.2413 -0.0070 0.0055  -0.0069 55  ILE   B CG1 
2212 C  CG2 . ILE   B 55  ? 0.2261 0.2618 0.2015 -0.0048 0.0043  -0.0022 55  ILE   B CG2 
2213 C  CD1 . ILE   B 55  ? 0.3108 0.3605 0.2887 -0.0078 0.0059  -0.0105 55  ILE   B CD1 
2214 N  N   . ALA   B 56  ? 0.1569 0.1857 0.1366 -0.0014 0.0032  -0.0060 56  ALA   B N   
2215 C  CA  . ALA   B 56  ? 0.1610 0.1865 0.1413 -0.0005 0.0030  -0.0058 56  ALA   B CA  
2216 C  C   . ALA   B 56  ? 0.1526 0.1783 0.1349 0.0011  0.0025  -0.0086 56  ALA   B C   
2217 O  O   . ALA   B 56  ? 0.1581 0.1846 0.1413 0.0014  0.0025  -0.0097 56  ALA   B O   
2218 C  CB  . ALA   B 56  ? 0.1647 0.1857 0.1444 0.0004  0.0025  -0.0035 56  ALA   B CB  
2219 N  N   . ARG   B 57  ? 0.1516 0.1766 0.1345 0.0022  0.0021  -0.0099 57  ARG   B N   
2220 C  CA  . ARG   B 57  ? 0.1665 0.1910 0.1513 0.0041  0.0016  -0.0122 57  ARG   B CA  
2221 C  C   . ARG   B 57  ? 0.1742 0.2035 0.1605 0.0036  0.0020  -0.0150 57  ARG   B C   
2222 O  O   . ARG   B 57  ? 0.1698 0.1998 0.1575 0.0049  0.0016  -0.0165 57  ARG   B O   
2223 C  CB  . ARG   B 57  ? 0.1764 0.1990 0.1619 0.0051  0.0015  -0.0131 57  ARG   B CB  
2224 C  CG  . ARG   B 57  ? 0.2036 0.2246 0.1909 0.0073  0.0011  -0.0151 57  ARG   B CG  
2225 C  CD  . ARG   B 57  ? 0.2318 0.2485 0.2185 0.0092  0.0003  -0.0134 57  ARG   B CD  
2226 N  NE  . ARG   B 57  ? 0.2288 0.2411 0.2143 0.0093  0.0004  -0.0116 57  ARG   B NE  
2227 C  CZ  . ARG   B 57  ? 0.2303 0.2389 0.2146 0.0102  0.0000  -0.0096 57  ARG   B CZ  
2228 N  NH1 . ARG   B 57  ? 0.2203 0.2291 0.2043 0.0111  -0.0006 -0.0090 57  ARG   B NH1 
2229 N  NH2 . ARG   B 57  ? 0.2215 0.2267 0.2048 0.0099  0.0003  -0.0083 57  ARG   B NH2 
2230 N  N   . LYS   B 58  ? 0.1720 0.2054 0.1580 0.0017  0.0027  -0.0158 58  LYS   B N   
2231 C  CA  . LYS   B 58  ? 0.1912 0.2299 0.1786 0.0009  0.0032  -0.0186 58  LYS   B CA  
2232 C  C   . LYS   B 58  ? 0.1946 0.2344 0.1818 0.0002  0.0035  -0.0183 58  LYS   B C   
2233 O  O   . LYS   B 58  ? 0.2035 0.2459 0.1927 0.0009  0.0034  -0.0209 58  LYS   B O   
2234 C  CB  . LYS   B 58  ? 0.1976 0.2409 0.1842 -0.0014 0.0040  -0.0191 58  LYS   B CB  
2235 C  CG  . LYS   B 58  ? 0.2211 0.2705 0.2092 -0.0025 0.0047  -0.0224 58  LYS   B CG  
2236 C  CD  . LYS   B 58  ? 0.2346 0.2890 0.2217 -0.0046 0.0055  -0.0230 58  LYS   B CD  
2237 C  CE  . LYS   B 58  ? 0.2839 0.3450 0.2725 -0.0060 0.0063  -0.0266 58  LYS   B CE  
2238 N  NZ  . LYS   B 58  ? 0.2953 0.3612 0.2830 -0.0078 0.0069  -0.0273 58  LYS   B NZ  
2239 N  N   . THR   B 59  ? 0.1769 0.2147 0.1621 -0.0012 0.0039  -0.0152 59  THR   B N   
2240 C  CA  . THR   B 59  ? 0.1774 0.2160 0.1625 -0.0023 0.0045  -0.0149 59  THR   B CA  
2241 C  C   . THR   B 59  ? 0.1774 0.2142 0.1641 -0.0003 0.0037  -0.0159 59  THR   B C   
2242 O  O   . THR   B 59  ? 0.1655 0.2054 0.1536 -0.0005 0.0040  -0.0180 59  THR   B O   
2243 C  CB  . THR   B 59  ? 0.1784 0.2146 0.1614 -0.0040 0.0052  -0.0113 59  THR   B CB  
2244 O  OG1 . THR   B 59  ? 0.1843 0.2228 0.1656 -0.0056 0.0058  -0.0102 59  THR   B OG1 
2245 C  CG2 . THR   B 59  ? 0.1856 0.2226 0.1687 -0.0058 0.0064  -0.0112 59  THR   B CG2 
2246 N  N   . LEU   B 60  ? 0.1738 0.2060 0.1601 0.0017  0.0027  -0.0143 60  LEU   B N   
2247 C  CA  . LEU   B 60  ? 0.1801 0.2110 0.1674 0.0038  0.0019  -0.0151 60  LEU   B CA  
2248 C  C   . LEU   B 60  ? 0.1907 0.2247 0.1801 0.0057  0.0012  -0.0183 60  LEU   B C   
2249 O  O   . LEU   B 60  ? 0.1929 0.2290 0.1836 0.0067  0.0008  -0.0199 60  LEU   B O   
2250 C  CB  . LEU   B 60  ? 0.1753 0.2011 0.1615 0.0054  0.0010  -0.0128 60  LEU   B CB  
2251 C  CG  . LEU   B 60  ? 0.1779 0.2007 0.1625 0.0040  0.0015  -0.0099 60  LEU   B CG  
2252 C  CD1 . LEU   B 60  ? 0.1715 0.1899 0.1552 0.0055  0.0008  -0.0082 60  LEU   B CD1 
2253 C  CD2 . LEU   B 60  ? 0.1769 0.2002 0.1620 0.0033  0.0019  -0.0099 60  LEU   B CD2 
2254 N  N   . LYS   B 61  ? 0.1968 0.2313 0.1869 0.0063  0.0010  -0.0195 61  LYS   B N   
2255 C  CA  . LYS   B 61  ? 0.2272 0.2646 0.2198 0.0082  0.0005  -0.0228 61  LYS   B CA  
2256 C  C   . LYS   B 61  ? 0.2304 0.2740 0.2244 0.0067  0.0012  -0.0255 61  LYS   B C   
2257 O  O   . LYS   B 61  ? 0.2371 0.2835 0.2330 0.0083  0.0006  -0.0278 61  LYS   B O   
2258 C  CB  . LYS   B 61  ? 0.2674 0.3041 0.2608 0.0088  0.0006  -0.0238 61  LYS   B CB  
2259 C  CG  . LYS   B 61  ? 0.3503 0.3809 0.3429 0.0107  -0.0001 -0.0219 61  LYS   B CG  
2260 C  CD  . LYS   B 61  ? 0.4350 0.4651 0.4287 0.0107  0.0004  -0.0233 61  LYS   B CD  
2261 C  CE  . LYS   B 61  ? 0.5232 0.5472 0.5163 0.0122  0.0001  -0.0216 61  LYS   B CE  
2262 N  NZ  . LYS   B 61  ? 0.5554 0.5792 0.5494 0.0113  0.0009  -0.0230 61  LYS   B NZ  
2263 N  N   . GLU   B 62  ? 0.2258 0.2719 0.2187 0.0036  0.0025  -0.0252 62  GLU   B N   
2264 C  CA  . GLU   B 62  ? 0.2746 0.3268 0.2687 0.0016  0.0035  -0.0279 62  GLU   B CA  
2265 C  C   . GLU   B 62  ? 0.2510 0.3044 0.2455 0.0011  0.0037  -0.0282 62  GLU   B C   
2266 O  O   . GLU   B 62  ? 0.2374 0.2959 0.2339 0.0008  0.0040  -0.0315 62  GLU   B O   
2267 C  CB  . GLU   B 62  ? 0.3101 0.3645 0.3024 -0.0019 0.0050  -0.0270 62  GLU   B CB  
2268 C  CG  . GLU   B 62  ? 0.4041 0.4605 0.3970 -0.0018 0.0049  -0.0285 62  GLU   B CG  
2269 C  CD  . GLU   B 62  ? 0.4635 0.5237 0.4546 -0.0051 0.0063  -0.0280 62  GLU   B CD  
2270 O  OE1 . GLU   B 62  ? 0.5401 0.6016 0.5297 -0.0076 0.0075  -0.0266 62  GLU   B OE1 
2271 O  OE2 . GLU   B 62  ? 0.5335 0.5953 0.5249 -0.0051 0.0063  -0.0291 62  GLU   B OE2 
2272 N  N   . GLN   B 63  ? 0.1994 0.2485 0.1923 0.0009  0.0037  -0.0253 63  GLN   B N   
2273 C  CA  . GLN   B 63  ? 0.2151 0.2655 0.2087 0.0003  0.0040  -0.0260 63  GLN   B CA  
2274 C  C   . GLN   B 63  ? 0.2168 0.2671 0.2118 0.0037  0.0024  -0.0272 63  GLN   B C   
2275 O  O   . GLN   B 63  ? 0.2309 0.2825 0.2265 0.0035  0.0025  -0.0278 63  GLN   B O   
2276 C  CB  . GLN   B 63  ? 0.2140 0.2604 0.2056 -0.0018 0.0051  -0.0227 63  GLN   B CB  
2277 C  CG  . GLN   B 63  ? 0.2124 0.2531 0.2027 0.0001  0.0039  -0.0197 63  GLN   B CG  
2278 C  CD  . GLN   B 63  ? 0.2188 0.2559 0.2077 -0.0018 0.0049  -0.0169 63  GLN   B CD  
2279 O  OE1 . GLN   B 63  ? 0.2528 0.2907 0.2412 -0.0046 0.0065  -0.0164 63  GLN   B OE1 
2280 N  NE2 . GLN   B 63  ? 0.2046 0.2376 0.1929 -0.0003 0.0041  -0.0151 63  GLN   B NE2 
2281 N  N   . GLY   B 64  ? 0.2210 0.2699 0.2165 0.0068  0.0010  -0.0274 64  GLY   B N   
2282 C  CA  . GLY   B 64  ? 0.2360 0.2852 0.2327 0.0103  -0.0006 -0.0284 64  GLY   B CA  
2283 C  C   . GLY   B 64  ? 0.2417 0.2861 0.2366 0.0115  -0.0013 -0.0254 64  GLY   B C   
2284 O  O   . GLY   B 64  ? 0.2439 0.2897 0.2395 0.0137  -0.0024 -0.0261 64  GLY   B O   
2285 N  N   . THR   B 65  ? 0.2078 0.2471 0.2006 0.0101  -0.0008 -0.0222 65  THR   B N   
2286 C  CA  . THR   B 65  ? 0.1991 0.2340 0.1902 0.0111  -0.0014 -0.0196 65  THR   B CA  
2287 C  C   . THR   B 65  ? 0.2136 0.2433 0.2033 0.0122  -0.0018 -0.0173 65  THR   B C   
2288 O  O   . THR   B 65  ? 0.1877 0.2137 0.1758 0.0109  -0.0013 -0.0148 65  THR   B O   
2289 C  CB  . THR   B 65  ? 0.1956 0.2296 0.1860 0.0084  -0.0002 -0.0182 65  THR   B CB  
2290 O  OG1 . THR   B 65  ? 0.2010 0.2331 0.1903 0.0061  0.0008  -0.0166 65  THR   B OG1 
2291 C  CG2 . THR   B 65  ? 0.2117 0.2506 0.2037 0.0070  0.0005  -0.0208 65  THR   B CG2 
2292 N  N   . PRO   B 66  ? 0.2480 0.2772 0.2386 0.0146  -0.0026 -0.0182 66  PRO   B N   
2293 C  CA  . PRO   B 66  ? 0.2592 0.2834 0.2487 0.0155  -0.0027 -0.0165 66  PRO   B CA  
2294 C  C   . PRO   B 66  ? 0.2793 0.2987 0.2670 0.0167  -0.0033 -0.0137 66  PRO   B C   
2295 O  O   . PRO   B 66  ? 0.2778 0.2931 0.2644 0.0166  -0.0030 -0.0121 66  PRO   B O   
2296 C  CB  . PRO   B 66  ? 0.2886 0.3139 0.2801 0.0179  -0.0034 -0.0187 66  PRO   B CB  
2297 C  CG  . PRO   B 66  ? 0.2735 0.3029 0.2663 0.0198  -0.0043 -0.0204 66  PRO   B CG  
2298 C  CD  . PRO   B 66  ? 0.2730 0.3063 0.2657 0.0168  -0.0034 -0.0211 66  PRO   B CD  
2299 N  N   . GLU   B 67  ? 0.2489 0.2694 0.2362 0.0176  -0.0039 -0.0134 67  GLU   B N   
2300 C  CA  . GLU   B 67  ? 0.2740 0.2909 0.2594 0.0187  -0.0044 -0.0110 67  GLU   B CA  
2301 C  C   . GLU   B 67  ? 0.2367 0.2521 0.2209 0.0161  -0.0036 -0.0094 67  GLU   B C   
2302 O  O   . GLU   B 67  ? 0.2243 0.2367 0.2069 0.0166  -0.0038 -0.0075 67  GLU   B O   
2303 C  CB  . GLU   B 67  ? 0.3429 0.3621 0.3284 0.0213  -0.0057 -0.0115 67  GLU   B CB  
2304 C  CG  . GLU   B 67  ? 0.4424 0.4619 0.4290 0.0245  -0.0066 -0.0125 67  GLU   B CG  
2305 C  CD  . GLU   B 67  ? 0.5692 0.5900 0.5554 0.0281  -0.0082 -0.0122 67  GLU   B CD  
2306 O  OE1 . GLU   B 67  ? 0.6472 0.6681 0.6318 0.0283  -0.0086 -0.0107 67  GLU   B OE1 
2307 O  OE2 . GLU   B 67  ? 0.7327 0.7548 0.7204 0.0307  -0.0090 -0.0136 67  GLU   B OE2 
2308 N  N   . ILE   B 68  ? 0.1873 0.2048 0.1722 0.0136  -0.0026 -0.0101 68  ILE   B N   
2309 C  CA  . ILE   B 68  ? 0.1727 0.1880 0.1566 0.0114  -0.0019 -0.0083 68  ILE   B CA  
2310 C  C   . ILE   B 68  ? 0.1684 0.1798 0.1511 0.0112  -0.0017 -0.0066 68  ILE   B C   
2311 O  O   . ILE   B 68  ? 0.1681 0.1800 0.1512 0.0109  -0.0014 -0.0073 68  ILE   B O   
2312 C  CB  . ILE   B 68  ? 0.1678 0.1857 0.1526 0.0089  -0.0007 -0.0090 68  ILE   B CB  
2313 C  CG1 . ILE   B 68  ? 0.1561 0.1780 0.1423 0.0087  -0.0006 -0.0111 68  ILE   B CG1 
2314 C  CG2 . ILE   B 68  ? 0.1781 0.1931 0.1619 0.0071  0.0000  -0.0069 68  ILE   B CG2 
2315 C  CD1 . ILE   B 68  ? 0.1600 0.1840 0.1471 0.0059  0.0008  -0.0118 68  ILE   B CD1 
2316 N  N   . ARG   B 69  ? 0.1642 0.1724 0.1457 0.0112  -0.0017 -0.0048 69  ARG   B N   
2317 C  CA  . ARG   B 69  ? 0.1810 0.1858 0.1615 0.0110  -0.0015 -0.0035 69  ARG   B CA  
2318 C  C   . ARG   B 69  ? 0.1654 0.1707 0.1459 0.0089  -0.0008 -0.0029 69  ARG   B C   
2319 O  O   . ARG   B 69  ? 0.1616 0.1682 0.1424 0.0077  -0.0004 -0.0026 69  ARG   B O   
2320 C  CB  . ARG   B 69  ? 0.2059 0.2077 0.1850 0.0117  -0.0018 -0.0019 69  ARG   B CB  
2321 C  CG  . ARG   B 69  ? 0.2534 0.2549 0.2320 0.0140  -0.0026 -0.0019 69  ARG   B CG  
2322 C  CD  . ARG   B 69  ? 0.3394 0.3399 0.3168 0.0139  -0.0027 -0.0007 69  ARG   B CD  
2323 N  NE  . ARG   B 69  ? 0.4235 0.4243 0.3998 0.0158  -0.0035 -0.0004 69  ARG   B NE  
2324 C  CZ  . ARG   B 69  ? 0.4497 0.4544 0.4267 0.0168  -0.0041 -0.0016 69  ARG   B CZ  
2325 N  NH1 . ARG   B 69  ? 0.4242 0.4323 0.4030 0.0155  -0.0038 -0.0033 69  ARG   B NH1 
2326 N  NH2 . ARG   B 69  ? 0.4669 0.4721 0.4427 0.0189  -0.0050 -0.0010 69  ARG   B NH2 
2327 N  N   . ILE   B 70  ? 0.1486 0.1528 0.1288 0.0086  -0.0005 -0.0027 70  ILE   B N   
2328 C  CA  . ILE   B 70  ? 0.1446 0.1496 0.1245 0.0070  0.0000  -0.0019 70  ILE   B CA  
2329 C  C   . ILE   B 70  ? 0.1428 0.1448 0.1218 0.0069  0.0000  -0.0005 70  ILE   B C   
2330 O  O   . ILE   B 70  ? 0.1374 0.1378 0.1162 0.0074  0.0000  -0.0008 70  ILE   B O   
2331 C  CB  . ILE   B 70  ? 0.1616 0.1690 0.1419 0.0063  0.0003  -0.0031 70  ILE   B CB  
2332 C  CG1 . ILE   B 70  ? 0.1660 0.1768 0.1473 0.0062  0.0004  -0.0047 70  ILE   B CG1 
2333 C  CG2 . ILE   B 70  ? 0.1626 0.1711 0.1422 0.0048  0.0007  -0.0018 70  ILE   B CG2 
2334 C  CD1 . ILE   B 70  ? 0.1666 0.1802 0.1485 0.0056  0.0007  -0.0064 70  ILE   B CD1 
2335 N  N   . ALA   B 71  ? 0.1370 0.1386 0.1158 0.0063  0.0001  0.0008  71  ALA   B N   
2336 C  CA  . ALA   B 71  ? 0.1430 0.1427 0.1213 0.0061  0.0001  0.0019  71  ALA   B CA  
2337 C  C   . ALA   B 71  ? 0.1556 0.1568 0.1338 0.0051  0.0003  0.0026  71  ALA   B C   
2338 O  O   . ALA   B 71  ? 0.1629 0.1660 0.1413 0.0045  0.0004  0.0031  71  ALA   B O   
2339 C  CB  . ALA   B 71  ? 0.1455 0.1439 0.1239 0.0062  0.0000  0.0026  71  ALA   B CB  
2340 N  N   . THR   B 72  ? 0.1422 0.1430 0.1202 0.0050  0.0003  0.0029  72  THR   B N   
2341 C  CA  . THR   B 72  ? 0.1410 0.1437 0.1189 0.0044  0.0003  0.0037  72  THR   B CA  
2342 C  C   . THR   B 72  ? 0.1573 0.1589 0.1353 0.0046  0.0001  0.0042  72  THR   B C   
2343 O  O   . THR   B 72  ? 0.1563 0.1555 0.1344 0.0049  0.0002  0.0040  72  THR   B O   
2344 C  CB  . THR   B 72  ? 0.1424 0.1478 0.1202 0.0040  0.0004  0.0024  72  THR   B CB  
2345 O  OG1 . THR   B 72  ? 0.1467 0.1550 0.1241 0.0035  0.0003  0.0035  72  THR   B OG1 
2346 C  CG2 . THR   B 72  ? 0.1470 0.1513 0.1249 0.0039  0.0007  0.0010  72  THR   B CG2 
2347 N  N   . VAL   B 73  ? 0.1468 0.1504 0.1248 0.0044  -0.0001 0.0048  73  VAL   B N   
2348 C  CA  . VAL   B 73  ? 0.1616 0.1648 0.1400 0.0047  -0.0003 0.0053  73  VAL   B CA  
2349 C  C   . VAL   B 73  ? 0.1482 0.1544 0.1266 0.0044  -0.0003 0.0043  73  VAL   B C   
2350 O  O   . VAL   B 73  ? 0.1436 0.1528 0.1216 0.0041  -0.0004 0.0041  73  VAL   B O   
2351 C  CB  . VAL   B 73  ? 0.1631 0.1663 0.1421 0.0053  -0.0006 0.0072  73  VAL   B CB  
2352 C  CG1 . VAL   B 73  ? 0.1706 0.1710 0.1503 0.0054  -0.0004 0.0075  73  VAL   B CG1 
2353 C  CG2 . VAL   B 73  ? 0.1793 0.1850 0.1577 0.0052  -0.0007 0.0086  73  VAL   B CG2 
2354 N  N   . THR   B 74  ? 0.1367 0.1424 0.1155 0.0042  -0.0001 0.0033  74  THR   B N   
2355 C  CA  . THR   B 74  ? 0.1366 0.1456 0.1158 0.0038  -0.0001 0.0021  74  THR   B CA  
2356 C  C   . THR   B 74  ? 0.1418 0.1511 0.1218 0.0042  -0.0003 0.0021  74  THR   B C   
2357 O  O   . THR   B 74  ? 0.1234 0.1302 0.1038 0.0046  -0.0004 0.0028  74  THR   B O   
2358 C  CB  . THR   B 74  ? 0.1479 0.1563 0.1270 0.0027  0.0009  -0.0002 74  THR   B CB  
2359 O  OG1 . THR   B 74  ? 0.1491 0.1536 0.1280 0.0025  0.0014  -0.0005 74  THR   B OG1 
2360 C  CG2 . THR   B 74  ? 0.1484 0.1565 0.1271 0.0025  0.0011  -0.0006 74  THR   B CG2 
2361 N  N   . ASN   B 75  ? 0.1413 0.1548 0.1218 0.0041  -0.0006 0.0011  75  ASN   B N   
2362 C  CA  . ASN   B 75  ? 0.1404 0.1557 0.1221 0.0048  -0.0010 0.0010  75  ASN   B CA  
2363 C  C   . ASN   B 75  ? 0.1453 0.1594 0.1274 0.0063  -0.0019 0.0034  75  ASN   B C   
2364 O  O   . ASN   B 75  ? 0.1379 0.1512 0.1212 0.0069  -0.0021 0.0034  75  ASN   B O   
2365 C  CB  . ASN   B 75  ? 0.1365 0.1498 0.1186 0.0038  -0.0002 -0.0008 75  ASN   B CB  
2366 C  CG  . ASN   B 75  ? 0.1448 0.1618 0.1282 0.0038  -0.0004 -0.0022 75  ASN   B CG  
2367 O  OD1 . ASN   B 75  ? 0.1455 0.1675 0.1294 0.0041  -0.0008 -0.0030 75  ASN   B OD1 
2368 N  ND2 . ASN   B 75  ? 0.1421 0.1577 0.1264 0.0036  0.0000  -0.0029 75  ASN   B ND2 
2369 N  N   . PHE   B 76  ? 0.1483 0.1624 0.1295 0.0069  -0.0023 0.0054  76  PHE   B N   
2370 C  CA  . PHE   B 76  ? 0.1587 0.1699 0.1403 0.0079  -0.0025 0.0077  76  PHE   B CA  
2371 C  C   . PHE   B 76  ? 0.1671 0.1804 0.1485 0.0093  -0.0034 0.0101  76  PHE   B C   
2372 O  O   . PHE   B 76  ? 0.1754 0.1921 0.1555 0.0092  -0.0036 0.0106  76  PHE   B O   
2373 C  CB  . PHE   B 76  ? 0.1633 0.1718 0.1440 0.0070  -0.0019 0.0080  76  PHE   B CB  
2374 C  CG  . PHE   B 76  ? 0.1777 0.1831 0.1587 0.0075  -0.0018 0.0099  76  PHE   B CG  
2375 C  CD1 . PHE   B 76  ? 0.1883 0.1944 0.1687 0.0079  -0.0020 0.0122  76  PHE   B CD1 
2376 C  CD2 . PHE   B 76  ? 0.1840 0.1862 0.1660 0.0073  -0.0014 0.0094  76  PHE   B CD2 
2377 C  CE1 . PHE   B 76  ? 0.1961 0.1992 0.1771 0.0081  -0.0016 0.0138  76  PHE   B CE1 
2378 C  CE2 . PHE   B 76  ? 0.1982 0.1979 0.1809 0.0075  -0.0011 0.0107  76  PHE   B CE2 
2379 C  CZ  . PHE   B 76  ? 0.1918 0.1917 0.1741 0.0078  -0.0011 0.0128  76  PHE   B CZ  
2380 N  N   . PRO   B 77  ? 0.1702 0.1814 0.1528 0.0106  -0.0037 0.0119  77  PRO   B N   
2381 C  CA  . PRO   B 77  ? 0.1791 0.1868 0.1635 0.0107  -0.0033 0.0111  77  PRO   B CA  
2382 C  C   . PRO   B 77  ? 0.1640 0.1735 0.1501 0.0114  -0.0037 0.0096  77  PRO   B C   
2383 O  O   . PRO   B 77  ? 0.1646 0.1719 0.1524 0.0114  -0.0034 0.0087  77  PRO   B O   
2384 C  CB  . PRO   B 77  ? 0.1971 0.2020 0.1822 0.0117  -0.0033 0.0138  77  PRO   B CB  
2385 C  CG  . PRO   B 77  ? 0.1918 0.1998 0.1762 0.0132  -0.0042 0.0160  77  PRO   B CG  
2386 C  CD  . PRO   B 77  ? 0.1985 0.2105 0.1808 0.0121  -0.0043 0.0149  77  PRO   B CD  
2387 N  N   . HIS   B 78  ? 0.1488 0.1630 0.1347 0.0118  -0.0043 0.0088  78  HIS   B N   
2388 C  CA  . HIS   B 78  ? 0.1602 0.1774 0.1479 0.0128  -0.0050 0.0076  78  HIS   B CA  
2389 C  C   . HIS   B 78  ? 0.1527 0.1695 0.1414 0.0114  -0.0042 0.0045  78  HIS   B C   
2390 O  O   . HIS   B 78  ? 0.1552 0.1731 0.1459 0.0122  -0.0044 0.0034  78  HIS   B O   
2391 C  CB  . HIS   B 78  ? 0.1685 0.1916 0.1556 0.0135  -0.0058 0.0073  78  HIS   B CB  
2392 C  CG  . HIS   B 78  ? 0.1735 0.1984 0.1587 0.0116  -0.0052 0.0059  78  HIS   B CG  
2393 N  ND1 . HIS   B 78  ? 0.1671 0.1923 0.1524 0.0096  -0.0042 0.0029  78  HIS   B ND1 
2394 C  CD2 . HIS   B 78  ? 0.1880 0.2142 0.1714 0.0113  -0.0052 0.0072  78  HIS   B CD2 
2395 C  CE1 . HIS   B 78  ? 0.1841 0.2105 0.1679 0.0083  -0.0037 0.0022  78  HIS   B CE1 
2396 N  NE2 . HIS   B 78  ? 0.1902 0.2178 0.1729 0.0093  -0.0044 0.0046  78  HIS   B NE2 
2397 N  N   . GLY   B 79  ? 0.1411 0.1565 0.1283 0.0094  -0.0032 0.0032  79  GLY   B N   
2398 C  CA  . GLY   B 79  ? 0.1449 0.1600 0.1325 0.0079  -0.0023 0.0006  79  GLY   B CA  
2399 C  C   . GLY   B 79  ? 0.1526 0.1727 0.1413 0.0078  -0.0024 -0.0016 79  GLY   B C   
2400 O  O   . GLY   B 79  ? 0.1513 0.1722 0.1413 0.0072  -0.0020 -0.0035 79  GLY   B O   
2401 N  N   . ASN   B 80  ? 0.1512 0.1754 0.1394 0.0080  -0.0029 -0.0017 80  ASN   B N   
2402 C  CA  . ASN   B 80  ? 0.1540 0.1837 0.1432 0.0076  -0.0029 -0.0044 80  ASN   B CA  
2403 C  C   . ASN   B 80  ? 0.1519 0.1806 0.1407 0.0049  -0.0012 -0.0072 80  ASN   B C   
2404 O  O   . ASN   B 80  ? 0.1393 0.1632 0.1267 0.0035  -0.0002 -0.0068 80  ASN   B O   
2405 C  CB  . ASN   B 80  ? 0.1698 0.2044 0.1582 0.0082  -0.0037 -0.0041 80  ASN   B CB  
2406 C  CG  . ASN   B 80  ? 0.1879 0.2245 0.1765 0.0110  -0.0054 -0.0012 80  ASN   B CG  
2407 O  OD1 . ASN   B 80  ? 0.2056 0.2406 0.1956 0.0128  -0.0060 0.0001  80  ASN   B OD1 
2408 N  ND2 . ASN   B 80  ? 0.2124 0.2526 0.1998 0.0115  -0.0060 -0.0002 80  ASN   B ND2 
2409 N  N   . ASP   B 81  ? 0.1564 0.1897 0.1466 0.0041  -0.0009 -0.0101 81  ASP   B N   
2410 C  CA  . ASP   B 81  ? 0.1695 0.2016 0.1596 0.0013  0.0010  -0.0128 81  ASP   B CA  
2411 C  C   . ASP   B 81  ? 0.1664 0.2018 0.1563 -0.0005 0.0020  -0.0152 81  ASP   B C   
2412 O  O   . ASP   B 81  ? 0.1888 0.2250 0.1792 -0.0028 0.0035  -0.0181 81  ASP   B O   
2413 C  CB  . ASP   B 81  ? 0.1977 0.2320 0.1897 0.0010  0.0013  -0.0149 81  ASP   B CB  
2414 C  CG  . ASP   B 81  ? 0.2522 0.2940 0.2464 0.0024  0.0001  -0.0167 81  ASP   B CG  
2415 O  OD1 . ASP   B 81  ? 0.2711 0.3168 0.2652 0.0036  -0.0009 -0.0162 81  ASP   B OD1 
2416 O  OD2 . ASP   B 81  ? 0.3238 0.3679 0.3198 0.0024  0.0002  -0.0186 81  ASP   B OD2 
2417 N  N   . ASP   B 82  ? 0.1587 0.1954 0.1478 0.0002  0.0013  -0.0142 82  ASP   B N   
2418 C  CA  . ASP   B 82  ? 0.1732 0.2127 0.1622 -0.0016 0.0024  -0.0167 82  ASP   B CA  
2419 C  C   . ASP   B 82  ? 0.1620 0.1951 0.1494 -0.0031 0.0037  -0.0160 82  ASP   B C   
2420 O  O   . ASP   B 82  ? 0.1557 0.1863 0.1419 -0.0020 0.0030  -0.0136 82  ASP   B O   
2421 C  CB  . ASP   B 82  ? 0.1832 0.2290 0.1724 -0.0001 0.0009  -0.0163 82  ASP   B CB  
2422 C  CG  . ASP   B 82  ? 0.2119 0.2622 0.2016 -0.0021 0.0021  -0.0198 82  ASP   B CG  
2423 O  OD1 . ASP   B 82  ? 0.2050 0.2511 0.1942 -0.0041 0.0038  -0.0208 82  ASP   B OD1 
2424 O  OD2 . ASP   B 82  ? 0.2592 0.3175 0.2500 -0.0015 0.0013  -0.0215 82  ASP   B OD2 
2425 N  N   . ILE   B 83  ? 0.1588 0.1891 0.1463 -0.0055 0.0058  -0.0181 83  ILE   B N   
2426 C  CA  . ILE   B 83  ? 0.1637 0.1872 0.1497 -0.0066 0.0071  -0.0173 83  ILE   B CA  
2427 C  C   . ILE   B 83  ? 0.1628 0.1873 0.1488 -0.0069 0.0073  -0.0180 83  ILE   B C   
2428 O  O   . ILE   B 83  ? 0.1774 0.1975 0.1622 -0.0063 0.0072  -0.0161 83  ILE   B O   
2429 C  CB  . ILE   B 83  ? 0.1769 0.1973 0.1630 -0.0092 0.0094  -0.0193 83  ILE   B CB  
2430 C  CG1 . ILE   B 83  ? 0.2020 0.2212 0.1878 -0.0091 0.0092  -0.0185 83  ILE   B CG1 
2431 C  CG2 . ILE   B 83  ? 0.1939 0.2075 0.1785 -0.0102 0.0108  -0.0185 83  ILE   B CG2 
2432 C  CD1 . ILE   B 83  ? 0.2106 0.2279 0.1963 -0.0119 0.0116  -0.0206 83  ILE   B CD1 
2433 N  N   . GLU   B 84  ? 0.1791 0.2097 0.1666 -0.0078 0.0077  -0.0210 84  GLU   B N   
2434 C  CA  . GLU   B 84  ? 0.1968 0.2291 0.1846 -0.0084 0.0081  -0.0224 84  GLU   B CA  
2435 C  C   . GLU   B 84  ? 0.1759 0.2093 0.1626 -0.0062 0.0062  -0.0195 84  GLU   B C   
2436 O  O   . GLU   B 84  ? 0.1727 0.2039 0.1590 -0.0063 0.0065  -0.0192 84  GLU   B O   
2437 C  CB  . GLU   B 84  ? 0.2328 0.2729 0.2227 -0.0100 0.0088  -0.0265 84  GLU   B CB  
2438 C  CG  . GLU   B 84  ? 0.3231 0.3616 0.3142 -0.0129 0.0114  -0.0300 84  GLU   B CG  
2439 C  CD  . GLU   B 84  ? 0.4955 0.5289 0.4870 -0.0150 0.0137  -0.0316 84  GLU   B CD  
2440 O  OE1 . GLU   B 84  ? 0.6150 0.6465 0.6061 -0.0141 0.0133  -0.0306 84  GLU   B OE1 
2441 O  OE2 . GLU   B 84  ? 0.6036 0.6351 0.5961 -0.0175 0.0160  -0.0343 84  GLU   B OE2 
2442 N  N   . ILE   B 85  ? 0.1622 0.1987 0.1485 -0.0041 0.0043  -0.0174 85  ILE   B N   
2443 C  CA  . ILE   B 85  ? 0.1498 0.1867 0.1349 -0.0022 0.0027  -0.0143 85  ILE   B CA  
2444 C  C   . ILE   B 85  ? 0.1522 0.1816 0.1360 -0.0016 0.0028  -0.0116 85  ILE   B C   
2445 O  O   . ILE   B 85  ? 0.1463 0.1744 0.1293 -0.0013 0.0026  -0.0106 85  ILE   B O   
2446 C  CB  . ILE   B 85  ? 0.1643 0.2061 0.1494 -0.0001 0.0008  -0.0126 85  ILE   B CB  
2447 C  CG1 . ILE   B 85  ? 0.1664 0.2172 0.1527 -0.0004 0.0006  -0.0153 85  ILE   B CG1 
2448 C  CG2 . ILE   B 85  ? 0.1760 0.2163 0.1597 0.0018  -0.0005 -0.0087 85  ILE   B CG2 
2449 C  CD1 . ILE   B 85  ? 0.1784 0.2345 0.1645 0.0021  -0.0015 -0.0134 85  ILE   B CD1 
2450 N  N   . ALA   B 86  ? 0.1494 0.1745 0.1331 -0.0015 0.0029  -0.0106 86  ALA   B N   
2451 C  CA  . ALA   B 86  ? 0.1510 0.1697 0.1334 -0.0009 0.0030  -0.0084 86  ALA   B CA  
2452 C  C   . ALA   B 86  ? 0.1524 0.1675 0.1344 -0.0021 0.0042  -0.0094 86  ALA   B C   
2453 O  O   . ALA   B 86  ? 0.1440 0.1564 0.1252 -0.0013 0.0039  -0.0078 86  ALA   B O   
2454 C  CB  . ALA   B 86  ? 0.1537 0.1693 0.1362 -0.0009 0.0031  -0.0078 86  ALA   B CB  
2455 N  N   . LEU   B 87  ? 0.1466 0.1616 0.1294 -0.0039 0.0058  -0.0121 87  LEU   B N   
2456 C  CA  . LEU   B 87  ? 0.1548 0.1658 0.1375 -0.0048 0.0072  -0.0131 87  LEU   B CA  
2457 C  C   . LEU   B 87  ? 0.1499 0.1639 0.1332 -0.0046 0.0069  -0.0139 87  LEU   B C   
2458 O  O   . LEU   B 87  ? 0.1476 0.1580 0.1305 -0.0041 0.0071  -0.0133 87  LEU   B O   
2459 C  CB  . LEU   B 87  ? 0.1659 0.1764 0.1496 -0.0071 0.0092  -0.0160 87  LEU   B CB  
2460 C  CG  . LEU   B 87  ? 0.1782 0.1839 0.1622 -0.0082 0.0110  -0.0173 87  LEU   B CG  
2461 C  CD1 . LEU   B 87  ? 0.1753 0.1740 0.1578 -0.0071 0.0110  -0.0146 87  LEU   B CD1 
2462 C  CD2 . LEU   B 87  ? 0.1944 0.1997 0.1796 -0.0108 0.0132  -0.0202 87  LEU   B CD2 
2463 N  N   . ALA   B 88  ? 0.1519 0.1727 0.1361 -0.0049 0.0065  -0.0155 88  ALA   B N   
2464 C  CA  . ALA   B 88  ? 0.1506 0.1753 0.1352 -0.0049 0.0062  -0.0165 88  ALA   B CA  
2465 C  C   . ALA   B 88  ? 0.1541 0.1773 0.1372 -0.0031 0.0048  -0.0133 88  ALA   B C   
2466 O  O   . ALA   B 88  ? 0.1544 0.1768 0.1376 -0.0031 0.0050  -0.0137 88  ALA   B O   
2467 C  CB  . ALA   B 88  ? 0.1509 0.1840 0.1363 -0.0052 0.0057  -0.0182 88  ALA   B CB  
2468 N  N   . GLU   B 89  ? 0.1485 0.1715 0.1306 -0.0018 0.0035  -0.0105 89  GLU   B N   
2469 C  CA  . GLU   B 89  ? 0.1531 0.1745 0.1340 -0.0004 0.0025  -0.0076 89  GLU   B CA  
2470 C  C   . GLU   B 89  ? 0.1481 0.1633 0.1287 -0.0002 0.0030  -0.0070 89  GLU   B C   
2471 O  O   . GLU   B 89  ? 0.1438 0.1585 0.1240 0.0002  0.0027  -0.0063 89  GLU   B O   
2472 C  CB  . GLU   B 89  ? 0.1605 0.1822 0.1408 0.0009  0.0013  -0.0050 89  GLU   B CB  
2473 C  CG  . GLU   B 89  ? 0.1771 0.2052 0.1575 0.0014  0.0004  -0.0048 89  GLU   B CG  
2474 C  CD  . GLU   B 89  ? 0.2136 0.2414 0.1936 0.0030  -0.0008 -0.0019 89  GLU   B CD  
2475 O  OE1 . GLU   B 89  ? 0.2252 0.2481 0.2053 0.0034  -0.0008 -0.0007 89  GLU   B OE1 
2476 O  OE2 . GLU   B 89  ? 0.2005 0.2329 0.1802 0.0040  -0.0018 -0.0008 89  GLU   B OE2 
2477 N  N   . THR   B 90  ? 0.1344 0.1453 0.1151 -0.0006 0.0038  -0.0073 90  THR   B N   
2478 C  CA  . THR   B 90  ? 0.1365 0.1418 0.1166 -0.0001 0.0041  -0.0065 90  THR   B CA  
2479 C  C   . THR   B 90  ? 0.1336 0.1380 0.1144 -0.0006 0.0050  -0.0084 90  THR   B C   
2480 O  O   . THR   B 90  ? 0.1229 0.1254 0.1035 0.0004  0.0048  -0.0078 90  THR   B O   
2481 C  CB  . THR   B 90  ? 0.1458 0.1472 0.1254 -0.0005 0.0048  -0.0062 90  THR   B CB  
2482 O  OG1 . THR   B 90  ? 0.1458 0.1482 0.1251 0.0000  0.0039  -0.0047 90  THR   B OG1 
2483 C  CG2 . THR   B 90  ? 0.1475 0.1434 0.1262 0.0000  0.0052  -0.0053 90  THR   B CG2 
2484 N  N   . ARG   B 91  ? 0.1436 0.1499 0.1257 -0.0020 0.0062  -0.0111 91  ARG   B N   
2485 C  CA  . ARG   B 91  ? 0.1503 0.1562 0.1337 -0.0025 0.0072  -0.0135 91  ARG   B CA  
2486 C  C   . ARG   B 91  ? 0.1436 0.1534 0.1272 -0.0019 0.0063  -0.0136 91  ARG   B C   
2487 O  O   . ARG   B 91  ? 0.1430 0.1512 0.1273 -0.0013 0.0065  -0.0142 91  ARG   B O   
2488 C  CB  . ARG   B 91  ? 0.1595 0.1676 0.1445 -0.0044 0.0087  -0.0168 91  ARG   B CB  
2489 C  CG  . ARG   B 91  ? 0.1784 0.1813 0.1635 -0.0054 0.0102  -0.0172 91  ARG   B CG  
2490 C  CD  . ARG   B 91  ? 0.2371 0.2430 0.2240 -0.0076 0.0118  -0.0209 91  ARG   B CD  
2491 N  NE  . ARG   B 91  ? 0.2705 0.2712 0.2574 -0.0090 0.0137  -0.0214 91  ARG   B NE  
2492 C  CZ  . ARG   B 91  ? 0.3201 0.3229 0.3085 -0.0113 0.0153  -0.0244 91  ARG   B CZ  
2493 N  NH1 . ARG   B 91  ? 0.3376 0.3483 0.3274 -0.0121 0.0150  -0.0270 91  ARG   B NH1 
2494 N  NH2 . ARG   B 91  ? 0.3204 0.3176 0.3087 -0.0127 0.0173  -0.0248 91  ARG   B NH2 
2495 N  N   . ALA   B 92  ? 0.1441 0.1595 0.1272 -0.0019 0.0053  -0.0129 92  ALA   B N   
2496 C  CA  . ALA   B 92  ? 0.1387 0.1583 0.1215 -0.0016 0.0046  -0.0127 92  ALA   B CA  
2497 C  C   . ALA   B 92  ? 0.1379 0.1541 0.1198 -0.0003 0.0039  -0.0104 92  ALA   B C   
2498 O  O   . ALA   B 92  ? 0.1343 0.1512 0.1166 -0.0001 0.0039  -0.0111 92  ALA   B O   
2499 C  CB  . ALA   B 92  ? 0.1449 0.1706 0.1270 -0.0017 0.0037  -0.0118 92  ALA   B CB  
2500 N  N   . ALA   B 93  ? 0.1346 0.1476 0.1153 0.0006  0.0032  -0.0078 93  ALA   B N   
2501 C  CA  . ALA   B 93  ? 0.1332 0.1433 0.1133 0.0017  0.0026  -0.0059 93  ALA   B CA  
2502 C  C   . ALA   B 93  ? 0.1443 0.1510 0.1251 0.0022  0.0031  -0.0071 93  ALA   B C   
2503 O  O   . ALA   B 93  ? 0.1424 0.1494 0.1233 0.0029  0.0028  -0.0070 93  ALA   B O   
2504 C  CB  . ALA   B 93  ? 0.1286 0.1357 0.1078 0.0023  0.0022  -0.0037 93  ALA   B CB  
2505 N  N   . ILE   B 94  ? 0.1439 0.1472 0.1252 0.0020  0.0040  -0.0081 94  ILE   B N   
2506 C  CA  . ILE   B 94  ? 0.1458 0.1452 0.1278 0.0028  0.0046  -0.0091 94  ILE   B CA  
2507 C  C   . ILE   B 94  ? 0.1502 0.1526 0.1339 0.0026  0.0049  -0.0116 94  ILE   B C   
2508 O  O   . ILE   B 94  ? 0.1525 0.1540 0.1368 0.0038  0.0047  -0.0119 94  ILE   B O   
2509 C  CB  . ILE   B 94  ? 0.1526 0.1477 0.1347 0.0023  0.0058  -0.0096 94  ILE   B CB  
2510 C  CG1 . ILE   B 94  ? 0.1605 0.1525 0.1408 0.0026  0.0054  -0.0071 94  ILE   B CG1 
2511 C  CG2 . ILE   B 94  ? 0.1620 0.1530 0.1451 0.0031  0.0066  -0.0107 94  ILE   B CG2 
2512 C  CD1 . ILE   B 94  ? 0.1636 0.1528 0.1438 0.0014  0.0067  -0.0077 94  ILE   B CD1 
2513 N  N   . ALA   B 95  ? 0.1406 0.1472 0.1252 0.0011  0.0055  -0.0136 95  ALA   B N   
2514 C  CA  . ALA   B 95  ? 0.1418 0.1522 0.1283 0.0005  0.0061  -0.0166 95  ALA   B CA  
2515 C  C   . ALA   B 95  ? 0.1523 0.1666 0.1383 0.0010  0.0051  -0.0160 95  ALA   B C   
2516 O  O   . ALA   B 95  ? 0.1476 0.1635 0.1351 0.0012  0.0053  -0.0180 95  ALA   B O   
2517 C  CB  . ALA   B 95  ? 0.1386 0.1535 0.1260 -0.0013 0.0069  -0.0190 95  ALA   B CB  
2518 N  N   . TYR   B 96  ? 0.1480 0.1640 0.1322 0.0010  0.0041  -0.0133 96  TYR   B N   
2519 C  CA  . TYR   B 96  ? 0.1519 0.1710 0.1354 0.0011  0.0035  -0.0125 96  TYR   B CA  
2520 C  C   . TYR   B 96  ? 0.1609 0.1767 0.1448 0.0026  0.0032  -0.0121 96  TYR   B C   
2521 O  O   . TYR   B 96  ? 0.1707 0.1893 0.1547 0.0025  0.0030  -0.0126 96  TYR   B O   
2522 C  CB  . TYR   B 96  ? 0.1504 0.1708 0.1319 0.0010  0.0027  -0.0094 96  TYR   B CB  
2523 C  CG  . TYR   B 96  ? 0.1434 0.1692 0.1241 -0.0001 0.0026  -0.0092 96  TYR   B CG  
2524 C  CD1 . TYR   B 96  ? 0.1462 0.1776 0.1268 -0.0010 0.0028  -0.0103 96  TYR   B CD1 
2525 C  CD2 . TYR   B 96  ? 0.1415 0.1672 0.1213 -0.0001 0.0023  -0.0077 96  TYR   B CD2 
2526 C  CE1 . TYR   B 96  ? 0.1412 0.1781 0.1208 -0.0018 0.0026  -0.0098 96  TYR   B CE1 
2527 C  CE2 . TYR   B 96  ? 0.1503 0.1812 0.1292 -0.0006 0.0019  -0.0071 96  TYR   B CE2 
2528 C  CZ  . TYR   B 96  ? 0.1513 0.1879 0.1300 -0.0015 0.0020  -0.0080 96  TYR   B CZ  
2529 O  OH  . TYR   B 96  ? 0.1617 0.2040 0.1391 -0.0019 0.0016  -0.0071 96  TYR   B OH  
2530 N  N   . GLY   B 97  ? 0.1597 0.1700 0.1434 0.0037  0.0031  -0.0112 97  GLY   B N   
2531 C  CA  . GLY   B 97  ? 0.1692 0.1765 0.1532 0.0054  0.0027  -0.0108 97  GLY   B CA  
2532 C  C   . GLY   B 97  ? 0.1561 0.1606 0.1385 0.0062  0.0020  -0.0081 97  GLY   B C   
2533 O  O   . GLY   B 97  ? 0.1643 0.1682 0.1467 0.0074  0.0014  -0.0078 97  GLY   B O   
2534 N  N   . ALA   B 98  ? 0.1449 0.1483 0.1261 0.0056  0.0020  -0.0064 98  ALA   B N   
2535 C  CA  . ALA   B 98  ? 0.1425 0.1435 0.1224 0.0062  0.0014  -0.0042 98  ALA   B CA  
2536 C  C   . ALA   B 98  ? 0.1450 0.1422 0.1248 0.0078  0.0012  -0.0040 98  ALA   B C   
2537 O  O   . ALA   B 98  ? 0.1425 0.1369 0.1226 0.0081  0.0018  -0.0047 98  ALA   B O   
2538 C  CB  . ALA   B 98  ? 0.1541 0.1544 0.1332 0.0054  0.0015  -0.0029 98  ALA   B CB  
2539 N  N   . ASP   B 99  ? 0.1389 0.1357 0.1181 0.0087  0.0006  -0.0028 99  ASP   B N   
2540 C  CA  . ASP   B 99  ? 0.1408 0.1344 0.1193 0.0102  0.0003  -0.0020 99  ASP   B CA  
2541 C  C   . ASP   B 99  ? 0.1427 0.1340 0.1198 0.0097  0.0004  -0.0004 99  ASP   B C   
2542 O  O   . ASP   B 99  ? 0.1491 0.1371 0.1251 0.0105  0.0005  0.0004  99  ASP   B O   
2543 C  CB  . ASP   B 99  ? 0.1447 0.1401 0.1234 0.0114  -0.0005 -0.0020 99  ASP   B CB  
2544 C  CG  . ASP   B 99  ? 0.1621 0.1600 0.1422 0.0121  -0.0007 -0.0038 99  ASP   B CG  
2545 O  OD1 . ASP   B 99  ? 0.1759 0.1723 0.1568 0.0130  -0.0005 -0.0048 99  ASP   B OD1 
2546 O  OD2 . ASP   B 99  ? 0.1757 0.1772 0.1565 0.0115  -0.0009 -0.0045 99  ASP   B OD2 
2547 N  N   . GLU   B 100 ? 0.1385 0.1316 0.1156 0.0084  0.0004  0.0001  100 GLU   B N   
2548 C  CA  . GLU   B 100 ? 0.1427 0.1345 0.1190 0.0078  0.0005  0.0013  100 GLU   B CA  
2549 C  C   . GLU   B 100 ? 0.1398 0.1333 0.1165 0.0065  0.0008  0.0013  100 GLU   B C   
2550 O  O   . GLU   B 100 ? 0.1363 0.1325 0.1137 0.0061  0.0006  0.0011  100 GLU   B O   
2551 C  CB  . GLU   B 100 ? 0.1616 0.1541 0.1376 0.0083  0.0000  0.0021  100 GLU   B CB  
2552 C  CG  . GLU   B 100 ? 0.1864 0.1784 0.1621 0.0099  -0.0005 0.0019  100 GLU   B CG  
2553 C  CD  . GLU   B 100 ? 0.2094 0.2031 0.1852 0.0102  -0.0010 0.0021  100 GLU   B CD  
2554 O  OE1 . GLU   B 100 ? 0.1962 0.1911 0.1727 0.0091  -0.0008 0.0022  100 GLU   B OE1 
2555 O  OE2 . GLU   B 100 ? 0.2095 0.2033 0.1846 0.0117  -0.0015 0.0021  100 GLU   B OE2 
2556 N  N   . VAL   B 101 ? 0.1319 0.1241 0.1082 0.0059  0.0012  0.0016  101 VAL   B N   
2557 C  CA  . VAL   B 101 ? 0.1366 0.1307 0.1133 0.0049  0.0012  0.0016  101 VAL   B CA  
2558 C  C   . VAL   B 101 ? 0.1423 0.1358 0.1189 0.0049  0.0011  0.0024  101 VAL   B C   
2559 O  O   . VAL   B 101 ? 0.1509 0.1422 0.1267 0.0048  0.0014  0.0025  101 VAL   B O   
2560 C  CB  . VAL   B 101 ? 0.1504 0.1446 0.1274 0.0041  0.0020  0.0003  101 VAL   B CB  
2561 C  CG1 . VAL   B 101 ? 0.1601 0.1570 0.1376 0.0033  0.0019  0.0002  101 VAL   B CG1 
2562 C  CG2 . VAL   B 101 ? 0.1486 0.1440 0.1261 0.0040  0.0022  -0.0010 101 VAL   B CG2 
2563 N  N   . ASP   B 102 ? 0.1446 0.1399 0.1220 0.0049  0.0007  0.0031  102 ASP   B N   
2564 C  CA  . ASP   B 102 ? 0.1524 0.1475 0.1303 0.0048  0.0006  0.0036  102 ASP   B CA  
2565 C  C   . ASP   B 102 ? 0.1450 0.1419 0.1235 0.0044  0.0006  0.0033  102 ASP   B C   
2566 O  O   . ASP   B 102 ? 0.1542 0.1532 0.1332 0.0046  0.0002  0.0039  102 ASP   B O   
2567 C  CB  . ASP   B 102 ? 0.1573 0.1527 0.1360 0.0052  0.0002  0.0044  102 ASP   B CB  
2568 C  CG  . ASP   B 102 ? 0.1822 0.1769 0.1607 0.0056  0.0002  0.0043  102 ASP   B CG  
2569 O  OD1 . ASP   B 102 ? 0.1922 0.1861 0.1697 0.0059  0.0002  0.0038  102 ASP   B OD1 
2570 O  OD2 . ASP   B 102 ? 0.2130 0.2080 0.1924 0.0056  0.0002  0.0046  102 ASP   B OD2 
2571 N  N   . VAL   B 103 ? 0.1428 0.1392 0.1211 0.0038  0.0011  0.0024  103 VAL   B N   
2572 C  CA  . VAL   B 103 ? 0.1368 0.1356 0.1159 0.0034  0.0011  0.0017  103 VAL   B CA  
2573 C  C   . VAL   B 103 ? 0.1432 0.1425 0.1234 0.0038  0.0008  0.0019  103 VAL   B C   
2574 O  O   . VAL   B 103 ? 0.1456 0.1433 0.1258 0.0037  0.0010  0.0019  103 VAL   B O   
2575 C  CB  . VAL   B 103 ? 0.1484 0.1467 0.1270 0.0023  0.0021  0.0001  103 VAL   B CB  
2576 C  CG1 . VAL   B 103 ? 0.1516 0.1471 0.1293 0.0017  0.0028  0.0000  103 VAL   B CG1 
2577 C  CG2 . VAL   B 103 ? 0.1485 0.1504 0.1281 0.0017  0.0021  -0.0012 103 VAL   B CG2 
2578 N  N   . VAL   B 104 ? 0.1331 0.1353 0.1146 0.0043  0.0003  0.0019  104 VAL   B N   
2579 C  CA  . VAL   B 104 ? 0.1357 0.1386 0.1187 0.0048  0.0000  0.0019  104 VAL   B CA  
2580 C  C   . VAL   B 104 ? 0.1384 0.1426 0.1216 0.0039  0.0006  -0.0001 104 VAL   B C   
2581 O  O   . VAL   B 104 ? 0.1435 0.1503 0.1268 0.0033  0.0007  -0.0012 104 VAL   B O   
2582 C  CB  . VAL   B 104 ? 0.1313 0.1363 0.1155 0.0062  -0.0010 0.0031  104 VAL   B CB  
2583 C  CG1 . VAL   B 104 ? 0.1346 0.1396 0.1208 0.0071  -0.0012 0.0029  104 VAL   B CG1 
2584 C  CG2 . VAL   B 104 ? 0.1390 0.1427 0.1227 0.0068  -0.0013 0.0051  104 VAL   B CG2 
2585 N  N   . PHE   B 105 ? 0.1374 0.1403 0.1210 0.0034  0.0010  -0.0007 105 PHE   B N   
2586 C  CA  . PHE   B 105 ? 0.1402 0.1444 0.1241 0.0023  0.0017  -0.0025 105 PHE   B CA  
2587 C  C   . PHE   B 105 ? 0.1341 0.1423 0.1203 0.0031  0.0010  -0.0035 105 PHE   B C   
2588 O  O   . PHE   B 105 ? 0.1289 0.1377 0.1164 0.0048  0.0000  -0.0023 105 PHE   B O   
2589 C  CB  . PHE   B 105 ? 0.1396 0.1422 0.1236 0.0020  0.0021  -0.0027 105 PHE   B CB  
2590 C  CG  . PHE   B 105 ? 0.1463 0.1499 0.1303 0.0004  0.0031  -0.0046 105 PHE   B CG  
2591 C  CD1 . PHE   B 105 ? 0.1591 0.1606 0.1407 -0.0012 0.0043  -0.0047 105 PHE   B CD1 
2592 C  CD2 . PHE   B 105 ? 0.1550 0.1617 0.1413 0.0007  0.0029  -0.0061 105 PHE   B CD2 
2593 C  CE1 . PHE   B 105 ? 0.1706 0.1729 0.1519 -0.0029 0.0054  -0.0063 105 PHE   B CE1 
2594 C  CE2 . PHE   B 105 ? 0.1771 0.1852 0.1634 -0.0010 0.0039  -0.0081 105 PHE   B CE2 
2595 C  CZ  . PHE   B 105 ? 0.1646 0.1705 0.1483 -0.0029 0.0053  -0.0081 105 PHE   B CZ  
2596 N  N   . PRO   B 106 ? 0.1387 0.1496 0.1252 0.0020  0.0016  -0.0055 106 PRO   B N   
2597 C  CA  . PRO   B 106 ? 0.1364 0.1519 0.1252 0.0030  0.0009  -0.0067 106 PRO   B CA  
2598 C  C   . PRO   B 106 ? 0.1413 0.1572 0.1320 0.0034  0.0008  -0.0076 106 PRO   B C   
2599 O  O   . PRO   B 106 ? 0.1529 0.1707 0.1443 0.0022  0.0016  -0.0098 106 PRO   B O   
2600 C  CB  . PRO   B 106 ? 0.1465 0.1649 0.1351 0.0012  0.0018  -0.0091 106 PRO   B CB  
2601 C  CG  . PRO   B 106 ? 0.1440 0.1584 0.1305 -0.0010 0.0035  -0.0095 106 PRO   B CG  
2602 C  CD  . PRO   B 106 ? 0.1442 0.1541 0.1291 -0.0002 0.0031  -0.0069 106 PRO   B CD  
2603 N  N   . TYR   B 107 ? 0.1374 0.1516 0.1292 0.0051  0.0000  -0.0059 107 TYR   B N   
2604 C  CA  . TYR   B 107 ? 0.1429 0.1569 0.1368 0.0055  0.0000  -0.0068 107 TYR   B CA  
2605 C  C   . TYR   B 107 ? 0.1403 0.1587 0.1372 0.0068  -0.0007 -0.0085 107 TYR   B C   
2606 O  O   . TYR   B 107 ? 0.1461 0.1660 0.1446 0.0062  -0.0002 -0.0107 107 TYR   B O   
2607 C  CB  . TYR   B 107 ? 0.1513 0.1619 0.1456 0.0067  -0.0004 -0.0048 107 TYR   B CB  
2608 C  CG  . TYR   B 107 ? 0.1488 0.1591 0.1440 0.0088  -0.0015 -0.0026 107 TYR   B CG  
2609 C  CD1 . TYR   B 107 ? 0.1555 0.1672 0.1537 0.0109  -0.0023 -0.0026 107 TYR   B CD1 
2610 C  CD2 . TYR   B 107 ? 0.1550 0.1635 0.1480 0.0089  -0.0017 -0.0005 107 TYR   B CD2 
2611 C  CE1 . TYR   B 107 ? 0.1589 0.1699 0.1574 0.0129  -0.0032 0.0000  107 TYR   B CE1 
2612 C  CE2 . TYR   B 107 ? 0.1512 0.1595 0.1446 0.0106  -0.0025 0.0018  107 TYR   B CE2 
2613 C  CZ  . TYR   B 107 ? 0.1591 0.1686 0.1552 0.0126  -0.0033 0.0022  107 TYR   B CZ  
2614 O  OH  . TYR   B 107 ? 0.1743 0.1831 0.1705 0.0145  -0.0041 0.0048  107 TYR   B OH  
2615 N  N   . ARG   B 108 ? 0.1453 0.1663 0.1428 0.0085  -0.0018 -0.0076 108 ARG   B N   
2616 C  CA  . ARG   B 108 ? 0.1447 0.1704 0.1451 0.0101  -0.0026 -0.0092 108 ARG   B CA  
2617 C  C   . ARG   B 108 ? 0.1485 0.1781 0.1490 0.0080  -0.0017 -0.0126 108 ARG   B C   
2618 O  O   . ARG   B 108 ? 0.1540 0.1869 0.1571 0.0084  -0.0017 -0.0150 108 ARG   B O   
2619 C  CB  . ARG   B 108 ? 0.1599 0.1879 0.1605 0.0126  -0.0042 -0.0073 108 ARG   B CB  
2620 C  CG  . ARG   B 108 ? 0.1788 0.2033 0.1802 0.0150  -0.0050 -0.0041 108 ARG   B CG  
2621 C  CD  . ARG   B 108 ? 0.2023 0.2297 0.2039 0.0176  -0.0066 -0.0021 108 ARG   B CD  
2622 N  NE  . ARG   B 108 ? 0.2389 0.2684 0.2376 0.0164  -0.0065 -0.0017 108 ARG   B NE  
2623 C  CZ  . ARG   B 108 ? 0.2636 0.2899 0.2597 0.0155  -0.0061 0.0004  108 ARG   B CZ  
2624 N  NH1 . ARG   B 108 ? 0.3240 0.3452 0.3200 0.0160  -0.0060 0.0027  108 ARG   B NH1 
2625 N  NH2 . ARG   B 108 ? 0.2369 0.2657 0.2309 0.0142  -0.0059 -0.0001 108 ARG   B NH2 
2626 N  N   . ALA   B 109 ? 0.1475 0.1767 0.1454 0.0057  -0.0007 -0.0130 109 ALA   B N   
2627 C  CA  . ALA   B 109 ? 0.1591 0.1913 0.1570 0.0033  0.0007  -0.0162 109 ALA   B CA  
2628 C  C   . ALA   B 109 ? 0.1573 0.1877 0.1553 0.0015  0.0020  -0.0176 109 ALA   B C   
2629 O  O   . ALA   B 109 ? 0.1612 0.1953 0.1608 0.0004  0.0026  -0.0206 109 ALA   B O   
2630 C  CB  . ALA   B 109 ? 0.1590 0.1901 0.1542 0.0012  0.0017  -0.0163 109 ALA   B CB  
2631 N  N   . LEU   B 110 ? 0.1608 0.1861 0.1571 0.0012  0.0023  -0.0157 110 LEU   B N   
2632 C  CA  . LEU   B 110 ? 0.1516 0.1757 0.1478 -0.0003 0.0034  -0.0168 110 LEU   B CA  
2633 C  C   . LEU   B 110 ? 0.1509 0.1782 0.1508 0.0011  0.0027  -0.0185 110 LEU   B C   
2634 O  O   . LEU   B 110 ? 0.1651 0.1948 0.1659 -0.0004 0.0037  -0.0212 110 LEU   B O   
2635 C  CB  . LEU   B 110 ? 0.1558 0.1748 0.1496 -0.0006 0.0037  -0.0144 110 LEU   B CB  
2636 C  CG  . LEU   B 110 ? 0.1665 0.1849 0.1601 -0.0020 0.0046  -0.0155 110 LEU   B CG  
2637 C  CD1 . LEU   B 110 ? 0.1707 0.1896 0.1621 -0.0050 0.0064  -0.0169 110 LEU   B CD1 
2638 C  CD2 . LEU   B 110 ? 0.1739 0.1882 0.1657 -0.0016 0.0045  -0.0131 110 LEU   B CD2 
2639 N  N   . MET   B 111 ? 0.1540 0.1813 0.1562 0.0041  0.0011  -0.0171 111 MET   B N   
2640 C  CA  . MET   B 111 ? 0.1696 0.1993 0.1757 0.0059  0.0004  -0.0187 111 MET   B CA  
2641 C  C   . MET   B 111 ? 0.1633 0.1993 0.1718 0.0061  0.0002  -0.0217 111 MET   B C   
2642 O  O   . MET   B 111 ? 0.1595 0.1984 0.1712 0.0067  0.0001  -0.0242 111 MET   B O   
2643 C  CB  . MET   B 111 ? 0.1950 0.2225 0.2028 0.0091  -0.0011 -0.0161 111 MET   B CB  
2644 C  CG  . MET   B 111 ? 0.2357 0.2577 0.2420 0.0087  -0.0007 -0.0138 111 MET   B CG  
2645 S  SD  . MET   B 111 ? 0.3174 0.3358 0.3244 0.0117  -0.0019 -0.0101 111 MET   B SD  
2646 C  CE  . MET   B 111 ? 0.3305 0.3501 0.3427 0.0134  -0.0021 -0.0123 111 MET   B CE  
2647 N  N   . ALA   B 112 ? 0.1517 0.1900 0.1587 0.0054  0.0002  -0.0219 112 ALA   B N   
2648 C  CA  . ALA   B 112 ? 0.1618 0.2065 0.1707 0.0051  0.0002  -0.0252 112 ALA   B CA  
2649 C  C   . ALA   B 112 ? 0.1788 0.2247 0.1861 0.0011  0.0024  -0.0280 112 ALA   B C   
2650 O  O   . ALA   B 112 ? 0.1991 0.2501 0.2074 0.0000  0.0029  -0.0310 112 ALA   B O   
2651 C  CB  . ALA   B 112 ? 0.1592 0.2066 0.1675 0.0066  -0.0009 -0.0242 112 ALA   B CB  
2652 N  N   . GLY   B 113 ? 0.1775 0.2186 0.1823 -0.0011 0.0038  -0.0271 113 GLY   B N   
2653 C  CA  . GLY   B 113 ? 0.1898 0.2312 0.1930 -0.0048 0.0060  -0.0292 113 GLY   B CA  
2654 C  C   . GLY   B 113 ? 0.2059 0.2450 0.2056 -0.0073 0.0075  -0.0286 113 GLY   B C   
2655 O  O   . GLY   B 113 ? 0.2433 0.2825 0.2415 -0.0106 0.0095  -0.0303 113 GLY   B O   
2656 N  N   . ASN   B 114 ? 0.1931 0.2299 0.1914 -0.0060 0.0066  -0.0262 114 ASN   B N   
2657 C  CA  . ASN   B 114 ? 0.1898 0.2240 0.1853 -0.0083 0.0080  -0.0257 114 ASN   B CA  
2658 C  C   . ASN   B 114 ? 0.2046 0.2319 0.1968 -0.0086 0.0084  -0.0224 114 ASN   B C   
2659 O  O   . ASN   B 114 ? 0.1959 0.2207 0.1875 -0.0065 0.0071  -0.0198 114 ASN   B O   
2660 C  CB  . ASN   B 114 ? 0.1949 0.2321 0.1913 -0.0070 0.0070  -0.0259 114 ASN   B CB  
2661 C  CG  . ASN   B 114 ? 0.1975 0.2330 0.1918 -0.0095 0.0087  -0.0264 114 ASN   B CG  
2662 O  OD1 . ASN   B 114 ? 0.2088 0.2392 0.2005 -0.0118 0.0104  -0.0256 114 ASN   B OD1 
2663 N  ND2 . ASN   B 114 ? 0.2337 0.2735 0.2292 -0.0091 0.0082  -0.0278 114 ASN   B ND2 
2664 N  N   . GLU   B 115 ? 0.1977 0.2222 0.1876 -0.0111 0.0102  -0.0225 115 GLU   B N   
2665 C  CA  . GLU   B 115 ? 0.2134 0.2318 0.2000 -0.0115 0.0107  -0.0195 115 GLU   B CA  
2666 C  C   . GLU   B 115 ? 0.2059 0.2210 0.1903 -0.0126 0.0117  -0.0186 115 GLU   B C   
2667 O  O   . GLU   B 115 ? 0.2131 0.2237 0.1955 -0.0118 0.0114  -0.0159 115 GLU   B O   
2668 C  CB  . GLU   B 115 ? 0.2354 0.2527 0.2202 -0.0137 0.0123  -0.0199 115 GLU   B CB  
2669 C  CG  . GLU   B 115 ? 0.2365 0.2569 0.2235 -0.0127 0.0114  -0.0209 115 GLU   B CG  
2670 C  CD  . GLU   B 115 ? 0.2850 0.3046 0.2698 -0.0150 0.0130  -0.0212 115 GLU   B CD  
2671 O  OE1 . GLU   B 115 ? 0.2993 0.3153 0.2805 -0.0171 0.0146  -0.0198 115 GLU   B OE1 
2672 O  OE2 . GLU   B 115 ? 0.2925 0.3152 0.2793 -0.0146 0.0126  -0.0227 115 GLU   B OE2 
2673 N  N   . GLN   B 116 ? 0.1956 0.2131 0.1807 -0.0147 0.0131  -0.0211 116 GLN   B N   
2674 C  CA  . GLN   B 116 ? 0.2144 0.2284 0.1976 -0.0165 0.0147  -0.0209 116 GLN   B CA  
2675 C  C   . GLN   B 116 ? 0.1925 0.2057 0.1760 -0.0143 0.0132  -0.0195 116 GLN   B C   
2676 O  O   . GLN   B 116 ? 0.1984 0.2068 0.1799 -0.0146 0.0139  -0.0178 116 GLN   B O   
2677 C  CB  . GLN   B 116 ? 0.2324 0.2496 0.2168 -0.0194 0.0167  -0.0246 116 GLN   B CB  
2678 C  CG  . GLN   B 116 ? 0.2844 0.2970 0.2669 -0.0218 0.0190  -0.0245 116 GLN   B CG  
2679 C  CD  . GLN   B 116 ? 0.3307 0.3361 0.3095 -0.0231 0.0206  -0.0218 116 GLN   B CD  
2680 O  OE1 . GLN   B 116 ? 0.3551 0.3603 0.3327 -0.0244 0.0214  -0.0217 116 GLN   B OE1 
2681 N  NE2 . GLN   B 116 ? 0.3703 0.3700 0.3472 -0.0226 0.0208  -0.0194 116 GLN   B NE2 
2682 N  N   . VAL   B 117 ? 0.1713 0.1895 0.1574 -0.0122 0.0113  -0.0201 117 VAL   B N   
2683 C  CA  . VAL   B 117 ? 0.1701 0.1883 0.1563 -0.0105 0.0101  -0.0190 117 VAL   B CA  
2684 C  C   . VAL   B 117 ? 0.1773 0.1905 0.1617 -0.0087 0.0091  -0.0154 117 VAL   B C   
2685 O  O   . VAL   B 117 ? 0.1786 0.1895 0.1620 -0.0083 0.0090  -0.0143 117 VAL   B O   
2686 C  CB  . VAL   B 117 ? 0.1878 0.2126 0.1767 -0.0085 0.0083  -0.0202 117 VAL   B CB  
2687 C  CG1 . VAL   B 117 ? 0.1947 0.2206 0.1849 -0.0058 0.0064  -0.0186 117 VAL   B CG1 
2688 C  CG2 . VAL   B 117 ? 0.2039 0.2295 0.1926 -0.0075 0.0075  -0.0195 117 VAL   B CG2 
2689 N  N   . GLY   B 118 ? 0.1615 0.1735 0.1457 -0.0077 0.0083  -0.0140 118 GLY   B N   
2690 C  CA  . GLY   B 118 ? 0.1603 0.1680 0.1429 -0.0063 0.0076  -0.0111 118 GLY   B CA  
2691 C  C   . GLY   B 118 ? 0.1595 0.1620 0.1392 -0.0076 0.0090  -0.0100 118 GLY   B C   
2692 O  O   . GLY   B 118 ? 0.1737 0.1733 0.1523 -0.0067 0.0085  -0.0082 118 GLY   B O   
2693 N  N   . PHE   B 119 ? 0.1630 0.1645 0.1416 -0.0100 0.0108  -0.0110 119 PHE   B N   
2694 C  CA  . PHE   B 119 ? 0.1688 0.1649 0.1446 -0.0112 0.0123  -0.0097 119 PHE   B CA  
2695 C  C   . PHE   B 119 ? 0.1679 0.1626 0.1439 -0.0115 0.0129  -0.0101 119 PHE   B C   
2696 O  O   . PHE   B 119 ? 0.1630 0.1535 0.1375 -0.0107 0.0128  -0.0083 119 PHE   B O   
2697 C  CB  . PHE   B 119 ? 0.1825 0.1780 0.1571 -0.0140 0.0144  -0.0108 119 PHE   B CB  
2698 C  CG  . PHE   B 119 ? 0.1985 0.1879 0.1699 -0.0152 0.0162  -0.0091 119 PHE   B CG  
2699 C  CD1 . PHE   B 119 ? 0.2090 0.1949 0.1776 -0.0145 0.0160  -0.0063 119 PHE   B CD1 
2700 C  CD2 . PHE   B 119 ? 0.2081 0.1952 0.1795 -0.0169 0.0179  -0.0101 119 PHE   B CD2 
2701 C  CE1 . PHE   B 119 ? 0.2225 0.2026 0.1882 -0.0151 0.0174  -0.0042 119 PHE   B CE1 
2702 C  CE2 . PHE   B 119 ? 0.2395 0.2202 0.2082 -0.0178 0.0196  -0.0082 119 PHE   B CE2 
2703 C  CZ  . PHE   B 119 ? 0.2420 0.2191 0.2077 -0.0167 0.0192  -0.0051 119 PHE   B CZ  
2704 N  N   . ASP   B 120 ? 0.1666 0.1651 0.1446 -0.0127 0.0134  -0.0129 120 ASP   B N   
2705 C  CA  . ASP   B 120 ? 0.1700 0.1680 0.1486 -0.0135 0.0143  -0.0141 120 ASP   B CA  
2706 C  C   . ASP   B 120 ? 0.1683 0.1668 0.1474 -0.0110 0.0124  -0.0128 120 ASP   B C   
2707 O  O   . ASP   B 120 ? 0.1670 0.1626 0.1456 -0.0111 0.0130  -0.0125 120 ASP   B O   
2708 C  CB  . ASP   B 120 ? 0.1947 0.1980 0.1756 -0.0153 0.0152  -0.0178 120 ASP   B CB  
2709 C  CG  . ASP   B 120 ? 0.2436 0.2460 0.2240 -0.0184 0.0177  -0.0197 120 ASP   B CG  
2710 O  OD1 . ASP   B 120 ? 0.2917 0.2882 0.2696 -0.0194 0.0191  -0.0179 120 ASP   B OD1 
2711 O  OD2 . ASP   B 120 ? 0.2733 0.2812 0.2558 -0.0197 0.0182  -0.0229 120 ASP   B OD2 
2712 N  N   . LEU   B 121 ? 0.1563 0.1585 0.1365 -0.0090 0.0104  -0.0121 121 LEU   B N   
2713 C  CA  . LEU   B 121 ? 0.1521 0.1551 0.1326 -0.0070 0.0088  -0.0108 121 LEU   B CA  
2714 C  C   . LEU   B 121 ? 0.1440 0.1417 0.1226 -0.0060 0.0086  -0.0082 121 LEU   B C   
2715 O  O   . LEU   B 121 ? 0.1492 0.1455 0.1276 -0.0055 0.0085  -0.0078 121 LEU   B O   
2716 C  CB  . LEU   B 121 ? 0.1469 0.1544 0.1289 -0.0051 0.0069  -0.0103 121 LEU   B CB  
2717 C  CG  . LEU   B 121 ? 0.1490 0.1583 0.1313 -0.0033 0.0054  -0.0091 121 LEU   B CG  
2718 C  CD1 . LEU   B 121 ? 0.1631 0.1779 0.1472 -0.0021 0.0041  -0.0095 121 LEU   B CD1 
2719 C  CD2 . LEU   B 121 ? 0.1546 0.1602 0.1358 -0.0018 0.0045  -0.0063 121 LEU   B CD2 
2720 N  N   . VAL   B 122 ? 0.1446 0.1400 0.1220 -0.0056 0.0084  -0.0067 122 VAL   B N   
2721 C  CA  . VAL   B 122 ? 0.1500 0.1413 0.1256 -0.0045 0.0080  -0.0044 122 VAL   B CA  
2722 C  C   . VAL   B 122 ? 0.1627 0.1496 0.1369 -0.0054 0.0095  -0.0043 122 VAL   B C   
2723 O  O   . VAL   B 122 ? 0.1640 0.1487 0.1376 -0.0043 0.0091  -0.0032 122 VAL   B O   
2724 C  CB  . VAL   B 122 ? 0.1494 0.1399 0.1240 -0.0041 0.0077  -0.0031 122 VAL   B CB  
2725 C  CG1 . VAL   B 122 ? 0.1536 0.1402 0.1262 -0.0031 0.0075  -0.0010 122 VAL   B CG1 
2726 C  CG2 . VAL   B 122 ? 0.1535 0.1474 0.1299 -0.0028 0.0062  -0.0032 122 VAL   B CG2 
2727 N  N   . LYS   B 123 ? 0.1761 0.1617 0.1498 -0.0075 0.0114  -0.0055 123 LYS   B N   
2728 C  CA  . LYS   B 123 ? 0.1967 0.1771 0.1689 -0.0085 0.0130  -0.0051 123 LYS   B CA  
2729 C  C   . LYS   B 123 ? 0.1888 0.1694 0.1627 -0.0084 0.0133  -0.0065 123 LYS   B C   
2730 O  O   . LYS   B 123 ? 0.1936 0.1701 0.1667 -0.0076 0.0136  -0.0054 123 LYS   B O   
2731 C  CB  . LYS   B 123 ? 0.2286 0.2079 0.2003 -0.0112 0.0152  -0.0063 123 LYS   B CB  
2732 C  CG  . LYS   B 123 ? 0.2813 0.2544 0.2515 -0.0123 0.0174  -0.0057 123 LYS   B CG  
2733 C  CD  . LYS   B 123 ? 0.3404 0.3116 0.3092 -0.0152 0.0197  -0.0063 123 LYS   B CD  
2734 C  CE  . LYS   B 123 ? 0.4207 0.3851 0.3880 -0.0166 0.0222  -0.0055 123 LYS   B CE  
2735 N  NZ  . LYS   B 123 ? 0.4706 0.4348 0.4404 -0.0176 0.0234  -0.0082 123 LYS   B NZ  
2736 N  N   . ALA   B 124 ? 0.1784 0.1642 0.1545 -0.0091 0.0131  -0.0089 124 ALA   B N   
2737 C  CA  . ALA   B 124 ? 0.1701 0.1571 0.1478 -0.0092 0.0133  -0.0106 124 ALA   B CA  
2738 C  C   . ALA   B 124 ? 0.1665 0.1531 0.1440 -0.0068 0.0117  -0.0089 124 ALA   B C   
2739 O  O   . ALA   B 124 ? 0.1701 0.1543 0.1479 -0.0065 0.0122  -0.0092 124 ALA   B O   
2740 C  CB  . ALA   B 124 ? 0.1642 0.1579 0.1440 -0.0100 0.0131  -0.0133 124 ALA   B CB  
2741 N  N   . CYS   B 125 ? 0.1566 0.1456 0.1338 -0.0052 0.0098  -0.0073 125 CYS   B N   
2742 C  CA  . CYS   B 125 ? 0.1613 0.1504 0.1383 -0.0032 0.0083  -0.0058 125 CYS   B CA  
2743 C  C   . CYS   B 125 ? 0.1604 0.1441 0.1358 -0.0022 0.0085  -0.0040 125 CYS   B C   
2744 O  O   . CYS   B 125 ? 0.1646 0.1475 0.1402 -0.0011 0.0080  -0.0038 125 CYS   B O   
2745 C  CB  . CYS   B 125 ? 0.1689 0.1614 0.1462 -0.0020 0.0066  -0.0046 125 CYS   B CB  
2746 S  SG  . CYS   B 125 ? 0.1849 0.1840 0.1640 -0.0023 0.0060  -0.0062 125 CYS   B SG  
2747 N  N   . LYS   B 126 ? 0.1629 0.1436 0.1366 -0.0025 0.0090  -0.0027 126 LYS   B N   
2748 C  CA  . LYS   B 126 ? 0.1773 0.1532 0.1491 -0.0013 0.0091  -0.0007 126 LYS   B CA  
2749 C  C   . LYS   B 126 ? 0.1817 0.1537 0.1537 -0.0016 0.0105  -0.0014 126 LYS   B C   
2750 O  O   . LYS   B 126 ? 0.1797 0.1493 0.1514 0.0001  0.0100  -0.0004 126 LYS   B O   
2751 C  CB  . LYS   B 126 ? 0.1899 0.1637 0.1596 -0.0018 0.0096  0.0008  126 LYS   B CB  
2752 C  CG  . LYS   B 126 ? 0.2018 0.1708 0.1692 -0.0006 0.0098  0.0030  126 LYS   B CG  
2753 C  CD  . LYS   B 126 ? 0.2228 0.1926 0.1901 0.0019  0.0080  0.0043  126 LYS   B CD  
2754 C  CE  . LYS   B 126 ? 0.2522 0.2175 0.2172 0.0035  0.0081  0.0066  126 LYS   B CE  
2755 N  NZ  . LYS   B 126 ? 0.3045 0.2701 0.2672 0.0037  0.0078  0.0083  126 LYS   B NZ  
2756 N  N   . GLU   B 127 ? 0.1936 0.1651 0.1665 -0.0038 0.0123  -0.0033 127 GLU   B N   
2757 C  CA  . GLU   B 127 ? 0.2262 0.1934 0.1997 -0.0044 0.0140  -0.0042 127 GLU   B CA  
2758 C  C   . GLU   B 127 ? 0.2056 0.1746 0.1810 -0.0032 0.0132  -0.0055 127 GLU   B C   
2759 O  O   . GLU   B 127 ? 0.2034 0.1684 0.1790 -0.0021 0.0136  -0.0051 127 GLU   B O   
2760 C  CB  . GLU   B 127 ? 0.2571 0.2239 0.2314 -0.0073 0.0163  -0.0065 127 GLU   B CB  
2761 C  CG  . GLU   B 127 ? 0.3360 0.2990 0.3076 -0.0083 0.0174  -0.0046 127 GLU   B CG  
2762 C  CD  . GLU   B 127 ? 0.4632 0.4257 0.4352 -0.0115 0.0198  -0.0066 127 GLU   B CD  
2763 O  OE1 . GLU   B 127 ? 0.6287 0.5949 0.6033 -0.0131 0.0206  -0.0099 127 GLU   B OE1 
2764 O  OE2 . GLU   B 127 ? 0.5649 0.5239 0.5346 -0.0125 0.0210  -0.0049 127 GLU   B OE2 
2765 N  N   . ALA   B 128 ? 0.1934 0.1685 0.1704 -0.0034 0.0121  -0.0070 128 ALA   B N   
2766 C  CA  . ALA   B 128 ? 0.1872 0.1650 0.1659 -0.0025 0.0115  -0.0084 128 ALA   B CA  
2767 C  C   . ALA   B 128 ? 0.1775 0.1540 0.1554 0.0000  0.0099  -0.0063 128 ALA   B C   
2768 O  O   . ALA   B 128 ? 0.1777 0.1526 0.1565 0.0010  0.0100  -0.0069 128 ALA   B O   
2769 C  CB  . ALA   B 128 ? 0.1835 0.1682 0.1635 -0.0032 0.0106  -0.0099 128 ALA   B CB  
2770 N  N   . CYS   B 129 ? 0.1605 0.1378 0.1368 0.0009  0.0086  -0.0041 129 CYS   B N   
2771 C  CA  . CYS   B 129 ? 0.1618 0.1387 0.1374 0.0031  0.0072  -0.0024 129 CYS   B CA  
2772 C  C   . CYS   B 129 ? 0.1750 0.1463 0.1496 0.0045  0.0077  -0.0011 129 CYS   B C   
2773 O  O   . CYS   B 129 ? 0.1916 0.1623 0.1667 0.0062  0.0070  -0.0012 129 CYS   B O   
2774 C  CB  . CYS   B 129 ? 0.1670 0.1457 0.1413 0.0035  0.0060  -0.0007 129 CYS   B CB  
2775 S  SG  . CYS   B 129 ? 0.1735 0.1583 0.1491 0.0030  0.0049  -0.0015 129 CYS   B SG  
2776 N  N   . ALA   B 130 ? 0.1856 0.1528 0.1584 0.0037  0.0088  0.0000  130 ALA   B N   
2777 C  CA  . ALA   B 130 ? 0.2034 0.1651 0.1747 0.0052  0.0092  0.0019  130 ALA   B CA  
2778 C  C   . ALA   B 130 ? 0.2279 0.1866 0.2010 0.0058  0.0102  0.0005  130 ALA   B C   
2779 O  O   . ALA   B 130 ? 0.2158 0.1718 0.1886 0.0081  0.0096  0.0017  130 ALA   B O   
2780 C  CB  . ALA   B 130 ? 0.2152 0.1731 0.1843 0.0038  0.0107  0.0033  130 ALA   B CB  
2781 N  N   . ALA   B 131 ? 0.2272 0.1868 0.2024 0.0037  0.0116  -0.0022 131 ALA   B N   
2782 C  CA  . ALA   B 131 ? 0.2568 0.2142 0.2344 0.0038  0.0127  -0.0043 131 ALA   B CA  
2783 C  C   . ALA   B 131 ? 0.2516 0.2120 0.2308 0.0059  0.0112  -0.0052 131 ALA   B C   
2784 O  O   . ALA   B 131 ? 0.2603 0.2180 0.2412 0.0070  0.0118  -0.0063 131 ALA   B O   
2785 C  CB  . ALA   B 131 ? 0.2679 0.2277 0.2477 0.0009  0.0144  -0.0076 131 ALA   B CB  
2786 N  N   . ALA   B 132 ? 0.2244 0.1904 0.2033 0.0064  0.0094  -0.0049 132 ALA   B N   
2787 C  CA  . ALA   B 132 ? 0.2197 0.1892 0.2001 0.0080  0.0080  -0.0058 132 ALA   B CA  
2788 C  C   . ALA   B 132 ? 0.2222 0.1917 0.2010 0.0104  0.0063  -0.0034 132 ALA   B C   
2789 O  O   . ALA   B 132 ? 0.2266 0.2001 0.2064 0.0114  0.0051  -0.0042 132 ALA   B O   
2790 C  CB  . ALA   B 132 ? 0.2231 0.1993 0.2043 0.0064  0.0075  -0.0074 132 ALA   B CB  
2791 N  N   . ASN   B 133 ? 0.2136 0.1795 0.1899 0.0111  0.0062  -0.0008 133 ASN   B N   
2792 C  CA  . ASN   B 133 ? 0.2319 0.1986 0.2066 0.0133  0.0046  0.0013  133 ASN   B CA  
2793 C  C   . ASN   B 133 ? 0.2196 0.1922 0.1944 0.0126  0.0034  0.0010  133 ASN   B C   
2794 O  O   . ASN   B 133 ? 0.2245 0.1998 0.1995 0.0141  0.0021  0.0011  133 ASN   B O   
2795 C  CB  . ASN   B 133 ? 0.2756 0.2410 0.2510 0.0161  0.0039  0.0013  133 ASN   B CB  
2796 C  CG  . ASN   B 133 ? 0.3533 0.3120 0.3282 0.0173  0.0050  0.0025  133 ASN   B CG  
2797 O  OD1 . ASN   B 133 ? 0.4796 0.4363 0.4568 0.0178  0.0058  0.0008  133 ASN   B OD1 
2798 N  ND2 . ASN   B 133 ? 0.3951 0.3502 0.3671 0.0176  0.0053  0.0053  133 ASN   B ND2 
2799 N  N   . VAL   B 134 ? 0.1727 0.1471 0.1475 0.0104  0.0039  0.0005  134 VAL   B N   
2800 C  CA  . VAL   B 134 ? 0.1691 0.1481 0.1440 0.0097  0.0029  0.0005  134 VAL   B CA  
2801 C  C   . VAL   B 134 ? 0.1736 0.1520 0.1468 0.0092  0.0029  0.0022  134 VAL   B C   
2802 O  O   . VAL   B 134 ? 0.1774 0.1530 0.1496 0.0081  0.0039  0.0026  134 VAL   B O   
2803 C  CB  . VAL   B 134 ? 0.1601 0.1422 0.1366 0.0078  0.0035  -0.0013 134 VAL   B CB  
2804 C  CG1 . VAL   B 134 ? 0.1520 0.1378 0.1284 0.0068  0.0029  -0.0009 134 VAL   B CG1 
2805 C  CG2 . VAL   B 134 ? 0.1746 0.1587 0.1530 0.0082  0.0035  -0.0032 134 VAL   B CG2 
2806 N  N   . LEU   B 135 ? 0.1789 0.1598 0.1517 0.0097  0.0018  0.0029  135 LEU   B N   
2807 C  CA  . LEU   B 135 ? 0.1838 0.1648 0.1554 0.0092  0.0017  0.0040  135 LEU   B CA  
2808 C  C   . LEU   B 135 ? 0.1701 0.1531 0.1426 0.0074  0.0021  0.0033  135 LEU   B C   
2809 O  O   . LEU   B 135 ? 0.1707 0.1564 0.1445 0.0070  0.0017  0.0026  135 LEU   B O   
2810 C  CB  . LEU   B 135 ? 0.2360 0.2193 0.2074 0.0103  0.0007  0.0045  135 LEU   B CB  
2811 C  CG  . LEU   B 135 ? 0.3004 0.2825 0.2705 0.0124  0.0001  0.0054  135 LEU   B CG  
2812 C  CD1 . LEU   B 135 ? 0.3037 0.2890 0.2736 0.0126  -0.0007 0.0056  135 LEU   B CD1 
2813 C  CD2 . LEU   B 135 ? 0.3230 0.3009 0.2909 0.0128  0.0007  0.0070  135 LEU   B CD2 
2814 N  N   . LEU   B 136 ? 0.1552 0.1372 0.1268 0.0064  0.0026  0.0038  136 LEU   B N   
2815 C  CA  . LEU   B 136 ? 0.1542 0.1384 0.1267 0.0050  0.0028  0.0032  136 LEU   B CA  
2816 C  C   . LEU   B 136 ? 0.1444 0.1300 0.1169 0.0051  0.0023  0.0038  136 LEU   B C   
2817 O  O   . LEU   B 136 ? 0.1585 0.1429 0.1296 0.0050  0.0025  0.0044  136 LEU   B O   
2818 C  CB  . LEU   B 136 ? 0.1630 0.1459 0.1353 0.0035  0.0040  0.0025  136 LEU   B CB  
2819 C  CG  . LEU   B 136 ? 0.1724 0.1582 0.1460 0.0024  0.0040  0.0016  136 LEU   B CG  
2820 C  CD1 . LEU   B 136 ? 0.1821 0.1707 0.1571 0.0024  0.0036  0.0007  136 LEU   B CD1 
2821 C  CD2 . LEU   B 136 ? 0.1915 0.1761 0.1645 0.0008  0.0053  0.0009  136 LEU   B CD2 
2822 N  N   . LYS   B 137 ? 0.1349 0.1231 0.1089 0.0051  0.0017  0.0035  137 LYS   B N   
2823 C  CA  . LYS   B 137 ? 0.1394 0.1289 0.1141 0.0050  0.0014  0.0036  137 LYS   B CA  
2824 C  C   . LYS   B 137 ? 0.1450 0.1357 0.1207 0.0041  0.0017  0.0030  137 LYS   B C   
2825 O  O   . LYS   B 137 ? 0.1564 0.1481 0.1328 0.0038  0.0017  0.0027  137 LYS   B O   
2826 C  CB  . LYS   B 137 ? 0.1516 0.1428 0.1276 0.0055  0.0008  0.0037  137 LYS   B CB  
2827 C  CG  . LYS   B 137 ? 0.1578 0.1490 0.1333 0.0065  0.0004  0.0038  137 LYS   B CG  
2828 C  CD  . LYS   B 137 ? 0.1670 0.1599 0.1437 0.0067  0.0001  0.0035  137 LYS   B CD  
2829 C  CE  . LYS   B 137 ? 0.1851 0.1789 0.1617 0.0074  -0.0003 0.0032  137 LYS   B CE  
2830 N  NZ  . LYS   B 137 ? 0.1856 0.1801 0.1630 0.0071  -0.0002 0.0032  137 LYS   B NZ  
2831 N  N   . VAL   B 138 ? 0.1286 0.1198 0.1046 0.0036  0.0019  0.0027  138 VAL   B N   
2832 C  CA  . VAL   B 138 ? 0.1329 0.1256 0.1102 0.0030  0.0020  0.0019  138 VAL   B CA  
2833 C  C   . VAL   B 138 ? 0.1275 0.1216 0.1068 0.0035  0.0016  0.0019  138 VAL   B C   
2834 O  O   . VAL   B 138 ? 0.1282 0.1224 0.1076 0.0034  0.0017  0.0016  138 VAL   B O   
2835 C  CB  . VAL   B 138 ? 0.1304 0.1227 0.1068 0.0018  0.0030  0.0012  138 VAL   B CB  
2836 C  CG1 . VAL   B 138 ? 0.1327 0.1275 0.1109 0.0013  0.0030  0.0000  138 VAL   B CG1 
2837 C  CG2 . VAL   B 138 ? 0.1313 0.1213 0.1060 0.0012  0.0038  0.0012  138 VAL   B CG2 
2838 N  N   . ILE   B 139 ? 0.1241 0.1196 0.1049 0.0040  0.0011  0.0021  139 ILE   B N   
2839 C  CA  . ILE   B 139 ? 0.1334 0.1297 0.1164 0.0046  0.0007  0.0022  139 ILE   B CA  
2840 C  C   . ILE   B 139 ? 0.1366 0.1345 0.1210 0.0044  0.0008  0.0010  139 ILE   B C   
2841 O  O   . ILE   B 139 ? 0.1444 0.1438 0.1291 0.0045  0.0007  0.0008  139 ILE   B O   
2842 C  CB  . ILE   B 139 ? 0.1419 0.1387 0.1257 0.0055  0.0002  0.0034  139 ILE   B CB  
2843 C  CG1 . ILE   B 139 ? 0.1547 0.1506 0.1373 0.0055  0.0002  0.0043  139 ILE   B CG1 
2844 C  CG2 . ILE   B 139 ? 0.1380 0.1348 0.1242 0.0062  0.0000  0.0038  139 ILE   B CG2 
2845 C  CD1 . ILE   B 139 ? 0.1540 0.1509 0.1365 0.0059  -0.0002 0.0054  139 ILE   B CD1 
2846 N  N   . ILE   B 140 ? 0.1351 0.1331 0.1207 0.0043  0.0011  0.0001  140 ILE   B N   
2847 C  CA  . ILE   B 140 ? 0.1394 0.1393 0.1266 0.0040  0.0013  -0.0014 140 ILE   B CA  
2848 C  C   . ILE   B 140 ? 0.1336 0.1345 0.1239 0.0053  0.0007  -0.0015 140 ILE   B C   
2849 O  O   . ILE   B 140 ? 0.1444 0.1473 0.1362 0.0055  0.0006  -0.0027 140 ILE   B O   
2850 C  CB  . ILE   B 140 ? 0.1416 0.1418 0.1281 0.0029  0.0020  -0.0027 140 ILE   B CB  
2851 C  CG1 . ILE   B 140 ? 0.1466 0.1465 0.1343 0.0031  0.0020  -0.0030 140 ILE   B CG1 
2852 C  CG2 . ILE   B 140 ? 0.1562 0.1552 0.1395 0.0017  0.0026  -0.0023 140 ILE   B CG2 
2853 C  CD1 . ILE   B 140 ? 0.1620 0.1634 0.1497 0.0020  0.0027  -0.0047 140 ILE   B CD1 
2854 N  N   . GLU   B 141 ? 0.1243 0.1235 0.1155 0.0062  0.0004  -0.0001 141 GLU   B N   
2855 C  CA  . GLU   B 141 ? 0.1365 0.1357 0.1307 0.0076  0.0001  0.0003  141 GLU   B CA  
2856 C  C   . GLU   B 141 ? 0.1329 0.1327 0.1299 0.0076  0.0004  -0.0017 141 GLU   B C   
2857 O  O   . GLU   B 141 ? 0.1371 0.1386 0.1363 0.0085  0.0001  -0.0026 141 GLU   B O   
2858 C  CB  . GLU   B 141 ? 0.1517 0.1525 0.1461 0.0088  -0.0008 0.0013  141 GLU   B CB  
2859 C  CG  . GLU   B 141 ? 0.1630 0.1625 0.1591 0.0106  -0.0012 0.0032  141 GLU   B CG  
2860 C  CD  . GLU   B 141 ? 0.1605 0.1577 0.1551 0.0105  -0.0011 0.0054  141 GLU   B CD  
2861 O  OE1 . GLU   B 141 ? 0.1598 0.1550 0.1544 0.0095  -0.0004 0.0050  141 GLU   B OE1 
2862 O  OE2 . GLU   B 141 ? 0.1726 0.1706 0.1659 0.0111  -0.0017 0.0072  141 GLU   B OE2 
2863 N  N   . THR   B 142 ? 0.1299 0.1289 0.1271 0.0068  0.0011  -0.0026 142 THR   B N   
2864 C  CA  . THR   B 142 ? 0.1445 0.1446 0.1443 0.0064  0.0016  -0.0050 142 THR   B CA  
2865 C  C   . THR   B 142 ? 0.1458 0.1452 0.1497 0.0080  0.0015  -0.0052 142 THR   B C   
2866 O  O   . THR   B 142 ? 0.1568 0.1580 0.1635 0.0082  0.0017  -0.0073 142 THR   B O   
2867 C  CB  . THR   B 142 ? 0.1437 0.1435 0.1432 0.0053  0.0023  -0.0059 142 THR   B CB  
2868 O  OG1 . THR   B 142 ? 0.1453 0.1427 0.1453 0.0058  0.0024  -0.0044 142 THR   B OG1 
2869 C  CG2 . THR   B 142 ? 0.1497 0.1503 0.1453 0.0041  0.0024  -0.0058 142 THR   B CG2 
2870 N  N   . GLY   B 143 ? 0.1593 0.1562 0.1637 0.0091  0.0012  -0.0029 143 GLY   B N   
2871 C  CA  . GLY   B 143 ? 0.1643 0.1596 0.1724 0.0108  0.0012  -0.0026 143 GLY   B CA  
2872 C  C   . GLY   B 143 ? 0.1827 0.1798 0.1918 0.0126  0.0002  -0.0022 143 GLY   B C   
2873 O  O   . GLY   B 143 ? 0.1959 0.1923 0.2087 0.0142  0.0001  -0.0025 143 GLY   B O   
2874 N  N   . GLU   B 144 ? 0.1643 0.1641 0.1707 0.0123  -0.0005 -0.0019 144 GLU   B N   
2875 C  CA  . GLU   B 144 ? 0.1639 0.1667 0.1715 0.0136  -0.0014 -0.0025 144 GLU   B CA  
2876 C  C   . GLU   B 144 ? 0.1691 0.1752 0.1776 0.0125  -0.0010 -0.0058 144 GLU   B C   
2877 O  O   . GLU   B 144 ? 0.1827 0.1912 0.1942 0.0137  -0.0014 -0.0074 144 GLU   B O   
2878 C  CB  . GLU   B 144 ? 0.1836 0.1878 0.1882 0.0140  -0.0022 -0.0005 144 GLU   B CB  
2879 C  CG  . GLU   B 144 ? 0.1951 0.1969 0.1990 0.0155  -0.0027 0.0029  144 GLU   B CG  
2880 C  CD  . GLU   B 144 ? 0.2326 0.2336 0.2398 0.0182  -0.0033 0.0040  144 GLU   B CD  
2881 O  OE1 . GLU   B 144 ? 0.2607 0.2650 0.2698 0.0196  -0.0041 0.0027  144 GLU   B OE1 
2882 O  OE2 . GLU   B 144 ? 0.2356 0.2328 0.2435 0.0189  -0.0030 0.0062  144 GLU   B OE2 
2883 N  N   . LEU   B 145 ? 0.1623 0.1687 0.1682 0.0101  -0.0002 -0.0069 145 LEU   B N   
2884 C  CA  . LEU   B 145 ? 0.1668 0.1762 0.1731 0.0086  0.0005  -0.0099 145 LEU   B CA  
2885 C  C   . LEU   B 145 ? 0.1732 0.1831 0.1834 0.0089  0.0010  -0.0123 145 LEU   B C   
2886 O  O   . LEU   B 145 ? 0.2001 0.2133 0.2125 0.0089  0.0011  -0.0148 145 LEU   B O   
2887 C  CB  . LEU   B 145 ? 0.1607 0.1695 0.1631 0.0063  0.0013  -0.0099 145 LEU   B CB  
2888 C  CG  . LEU   B 145 ? 0.1700 0.1785 0.1688 0.0057  0.0011  -0.0083 145 LEU   B CG  
2889 C  CD1 . LEU   B 145 ? 0.1718 0.1788 0.1672 0.0038  0.0019  -0.0079 145 LEU   B CD1 
2890 C  CD2 . LEU   B 145 ? 0.1785 0.1904 0.1777 0.0054  0.0010  -0.0097 145 LEU   B CD2 
2891 N  N   . LYS   B 146 ? 0.1967 0.2039 0.2079 0.0089  0.0014  -0.0118 146 LYS   B N   
2892 C  CA  . LYS   B 146 ? 0.2303 0.2374 0.2457 0.0092  0.0020  -0.0140 146 LYS   B CA  
2893 C  C   . LYS   B 146 ? 0.2306 0.2410 0.2463 0.0072  0.0030  -0.0174 146 LYS   B C   
2894 O  O   . LYS   B 146 ? 0.2482 0.2584 0.2646 0.0061  0.0038  -0.0186 146 LYS   B O   
2895 C  CB  . LYS   B 146 ? 0.2745 0.2816 0.2942 0.0117  0.0014  -0.0143 146 LYS   B CB  
2896 C  CG  . LYS   B 146 ? 0.3540 0.3571 0.3736 0.0137  0.0007  -0.0107 146 LYS   B CG  
2897 C  CD  . LYS   B 146 ? 0.4421 0.4454 0.4652 0.0167  -0.0002 -0.0102 146 LYS   B CD  
2898 C  CE  . LYS   B 146 ? 0.4969 0.4966 0.5189 0.0185  -0.0009 -0.0060 146 LYS   B CE  
2899 N  NZ  . LYS   B 146 ? 0.5262 0.5212 0.5491 0.0180  0.0002  -0.0050 146 LYS   B NZ  
2900 N  N   . ASP   B 147 ? 0.2216 0.2355 0.2367 0.0065  0.0029  -0.0189 147 ASP   B N   
2901 C  CA  . ASP   B 147 ? 0.2259 0.2435 0.2413 0.0046  0.0038  -0.0221 147 ASP   B CA  
2902 C  C   . ASP   B 147 ? 0.2018 0.2193 0.2124 0.0023  0.0045  -0.0212 147 ASP   B C   
2903 O  O   . ASP   B 147 ? 0.1813 0.1972 0.1878 0.0019  0.0042  -0.0188 147 ASP   B O   
2904 C  CB  . ASP   B 147 ? 0.2714 0.2927 0.2875 0.0045  0.0037  -0.0238 147 ASP   B CB  
2905 C  CG  . ASP   B 147 ? 0.3748 0.4001 0.3900 0.0019  0.0048  -0.0267 147 ASP   B CG  
2906 O  OD1 . ASP   B 147 ? 0.5009 0.5287 0.5197 0.0018  0.0053  -0.0298 147 ASP   B OD1 
2907 O  OD2 . ASP   B 147 ? 0.5197 0.5453 0.5305 0.0001  0.0053  -0.0258 147 ASP   B OD2 
2908 N  N   . GLU   B 148 ? 0.2086 0.2281 0.2197 0.0009  0.0053  -0.0234 148 GLU   B N   
2909 C  CA  . GLU   B 148 ? 0.2128 0.2328 0.2195 -0.0009 0.0059  -0.0226 148 GLU   B CA  
2910 C  C   . GLU   B 148 ? 0.1965 0.2172 0.1989 -0.0023 0.0061  -0.0216 148 GLU   B C   
2911 O  O   . GLU   B 148 ? 0.1777 0.1961 0.1758 -0.0028 0.0061  -0.0191 148 GLU   B O   
2912 C  CB  . GLU   B 148 ? 0.2352 0.2587 0.2434 -0.0023 0.0068  -0.0256 148 GLU   B CB  
2913 C  CG  . GLU   B 148 ? 0.2706 0.2954 0.2738 -0.0040 0.0072  -0.0247 148 GLU   B CG  
2914 C  CD  . GLU   B 148 ? 0.3510 0.3796 0.3550 -0.0052 0.0079  -0.0272 148 GLU   B CD  
2915 O  OE1 . GLU   B 148 ? 0.3568 0.3868 0.3658 -0.0048 0.0082  -0.0301 148 GLU   B OE1 
2916 O  OE2 . GLU   B 148 ? 0.4077 0.4378 0.4073 -0.0064 0.0082  -0.0262 148 GLU   B OE2 
2917 N  N   . ALA   B 149 ? 0.1932 0.2170 0.1969 -0.0031 0.0066  -0.0239 149 ALA   B N   
2918 C  CA  . ALA   B 149 ? 0.2021 0.2267 0.2023 -0.0048 0.0072  -0.0234 149 ALA   B CA  
2919 C  C   . ALA   B 149 ? 0.1866 0.2078 0.1846 -0.0039 0.0065  -0.0205 149 ALA   B C   
2920 O  O   . ALA   B 149 ? 0.1730 0.1926 0.1667 -0.0053 0.0070  -0.0188 149 ALA   B O   
2921 C  CB  . ALA   B 149 ? 0.2210 0.2500 0.2236 -0.0058 0.0078  -0.0268 149 ALA   B CB  
2922 N  N   . LEU   B 150 ? 0.1720 0.1921 0.1729 -0.0017 0.0054  -0.0200 150 LEU   B N   
2923 C  CA  . LEU   B 150 ? 0.1723 0.1900 0.1713 -0.0009 0.0048  -0.0175 150 LEU   B CA  
2924 C  C   . LEU   B 150 ? 0.1607 0.1745 0.1566 -0.0007 0.0045  -0.0146 150 LEU   B C   
2925 O  O   . LEU   B 150 ? 0.1496 0.1616 0.1424 -0.0012 0.0046  -0.0129 150 LEU   B O   
2926 C  CB  . LEU   B 150 ? 0.1906 0.2086 0.1931 0.0015  0.0036  -0.0175 150 LEU   B CB  
2927 C  CG  . LEU   B 150 ? 0.2216 0.2438 0.2268 0.0016  0.0036  -0.0201 150 LEU   B CG  
2928 C  CD1 . LEU   B 150 ? 0.2286 0.2510 0.2375 0.0046  0.0022  -0.0197 150 LEU   B CD1 
2929 C  CD2 . LEU   B 150 ? 0.2538 0.2771 0.2562 0.0001  0.0040  -0.0201 150 LEU   B CD2 
2930 N  N   . ILE   B 151 ? 0.1575 0.1702 0.1544 -0.0001 0.0044  -0.0143 151 ILE   B N   
2931 C  CA  . ILE   B 151 ? 0.1557 0.1654 0.1498 0.0001  0.0041  -0.0119 151 ILE   B CA  
2932 C  C   . ILE   B 151 ? 0.1558 0.1655 0.1457 -0.0016 0.0049  -0.0114 151 ILE   B C   
2933 O  O   . ILE   B 151 ? 0.1576 0.1647 0.1443 -0.0016 0.0048  -0.0092 151 ILE   B O   
2934 C  CB  . ILE   B 151 ? 0.1637 0.1732 0.1603 0.0008  0.0040  -0.0125 151 ILE   B CB  
2935 C  CG1 . ILE   B 151 ? 0.1723 0.1806 0.1727 0.0027  0.0034  -0.0122 151 ILE   B CG1 
2936 C  CG2 . ILE   B 151 ? 0.1654 0.1731 0.1592 0.0007  0.0040  -0.0108 151 ILE   B CG2 
2937 C  CD1 . ILE   B 151 ? 0.1693 0.1770 0.1729 0.0032  0.0037  -0.0133 151 ILE   B CD1 
2938 N  N   . ARG   B 152 ? 0.1529 0.1653 0.1426 -0.0031 0.0057  -0.0132 152 ARG   B N   
2939 C  CA  . ARG   B 152 ? 0.1649 0.1770 0.1501 -0.0047 0.0065  -0.0122 152 ARG   B CA  
2940 C  C   . ARG   B 152 ? 0.1712 0.1815 0.1540 -0.0055 0.0070  -0.0111 152 ARG   B C   
2941 O  O   . ARG   B 152 ? 0.1770 0.1846 0.1561 -0.0059 0.0073  -0.0090 152 ARG   B O   
2942 C  CB  . ARG   B 152 ? 0.1737 0.1896 0.1587 -0.0063 0.0075  -0.0144 152 ARG   B CB  
2943 C  CG  . ARG   B 152 ? 0.1972 0.2153 0.1841 -0.0059 0.0072  -0.0157 152 ARG   B CG  
2944 C  CD  . ARG   B 152 ? 0.2289 0.2515 0.2150 -0.0077 0.0082  -0.0178 152 ARG   B CD  
2945 N  NE  . ARG   B 152 ? 0.2707 0.2960 0.2594 -0.0074 0.0080  -0.0197 152 ARG   B NE  
2946 C  CZ  . ARG   B 152 ? 0.3029 0.3285 0.2900 -0.0069 0.0077  -0.0187 152 ARG   B CZ  
2947 N  NH1 . ARG   B 152 ? 0.3126 0.3362 0.2947 -0.0069 0.0075  -0.0158 152 ARG   B NH1 
2948 N  NH2 . ARG   B 152 ? 0.3234 0.3516 0.3139 -0.0066 0.0077  -0.0211 152 ARG   B NH2 
2949 N  N   . LYS   B 153 ? 0.1715 0.1836 0.1566 -0.0058 0.0072  -0.0129 153 LYS   B N   
2950 C  CA  . LYS   B 153 ? 0.1686 0.1798 0.1520 -0.0070 0.0079  -0.0126 153 LYS   B CA  
2951 C  C   . LYS   B 153 ? 0.1564 0.1642 0.1387 -0.0058 0.0073  -0.0104 153 LYS   B C   
2952 O  O   . LYS   B 153 ? 0.1633 0.1686 0.1426 -0.0068 0.0080  -0.0091 153 LYS   B O   
2953 C  CB  . LYS   B 153 ? 0.1868 0.2016 0.1734 -0.0074 0.0081  -0.0154 153 LYS   B CB  
2954 C  CG  . LYS   B 153 ? 0.2253 0.2400 0.2103 -0.0090 0.0092  -0.0157 153 LYS   B CG  
2955 C  CD  . LYS   B 153 ? 0.2772 0.2903 0.2582 -0.0116 0.0109  -0.0152 153 LYS   B CD  
2956 C  CE  . LYS   B 153 ? 0.3083 0.3251 0.2898 -0.0133 0.0119  -0.0173 153 LYS   B CE  
2957 N  NZ  . LYS   B 153 ? 0.3601 0.3753 0.3373 -0.0160 0.0137  -0.0165 153 LYS   B NZ  
2958 N  N   . ALA   B 154 ? 0.1525 0.1601 0.1372 -0.0038 0.0060  -0.0099 154 ALA   B N   
2959 C  CA  . ALA   B 154 ? 0.1472 0.1522 0.1309 -0.0028 0.0053  -0.0080 154 ALA   B CA  
2960 C  C   . ALA   B 154 ? 0.1414 0.1432 0.1219 -0.0028 0.0055  -0.0058 154 ALA   B C   
2961 O  O   . ALA   B 154 ? 0.1355 0.1349 0.1140 -0.0029 0.0057  -0.0046 154 ALA   B O   
2962 C  CB  . ALA   B 154 ? 0.1534 0.1589 0.1401 -0.0007 0.0040  -0.0076 154 ALA   B CB  
2963 N  N   . SER   B 155 ? 0.1404 0.1425 0.1207 -0.0025 0.0053  -0.0057 155 SER   B N   
2964 C  CA  . SER   B 155 ? 0.1471 0.1470 0.1244 -0.0023 0.0053  -0.0039 155 SER   B CA  
2965 C  C   . SER   B 155 ? 0.1542 0.1524 0.1280 -0.0038 0.0064  -0.0030 155 SER   B C   
2966 O  O   . SER   B 155 ? 0.1587 0.1538 0.1301 -0.0034 0.0065  -0.0012 155 SER   B O   
2967 C  CB  . SER   B 155 ? 0.1428 0.1446 0.1207 -0.0019 0.0050  -0.0044 155 SER   B CB  
2968 O  OG  . SER   B 155 ? 0.1386 0.1411 0.1199 -0.0007 0.0042  -0.0051 155 SER   B OG  
2969 N  N   . GLU   B 156 ? 0.1563 0.1564 0.1297 -0.0055 0.0075  -0.0044 156 GLU   B N   
2970 C  CA  . GLU   B 156 ? 0.1796 0.1779 0.1495 -0.0072 0.0089  -0.0035 156 GLU   B CA  
2971 C  C   . GLU   B 156 ? 0.1727 0.1681 0.1420 -0.0078 0.0096  -0.0030 156 GLU   B C   
2972 O  O   . GLU   B 156 ? 0.1751 0.1667 0.1414 -0.0080 0.0103  -0.0012 156 GLU   B O   
2973 C  CB  . GLU   B 156 ? 0.2220 0.2236 0.1922 -0.0092 0.0100  -0.0056 156 GLU   B CB  
2974 C  CG  . GLU   B 156 ? 0.2919 0.2915 0.2583 -0.0114 0.0118  -0.0046 156 GLU   B CG  
2975 C  CD  . GLU   B 156 ? 0.4226 0.4257 0.3894 -0.0138 0.0132  -0.0069 156 GLU   B CD  
2976 O  OE1 . GLU   B 156 ? 0.4561 0.4630 0.4267 -0.0138 0.0128  -0.0097 156 GLU   B OE1 
2977 O  OE2 . GLU   B 156 ? 0.5440 0.5460 0.5072 -0.0157 0.0147  -0.0058 156 GLU   B OE2 
2978 N  N   . ILE   B 157 ? 0.1622 0.1595 0.1344 -0.0079 0.0094  -0.0049 157 ILE   B N   
2979 C  CA  . ILE   B 157 ? 0.1551 0.1508 0.1273 -0.0086 0.0101  -0.0051 157 ILE   B CA  
2980 C  C   . ILE   B 157 ? 0.1545 0.1468 0.1257 -0.0071 0.0094  -0.0031 157 ILE   B C   
2981 O  O   . ILE   B 157 ? 0.1654 0.1545 0.1348 -0.0078 0.0104  -0.0024 157 ILE   B O   
2982 C  CB  . ILE   B 157 ? 0.1530 0.1526 0.1288 -0.0084 0.0096  -0.0075 157 ILE   B CB  
2983 C  CG1 . ILE   B 157 ? 0.1595 0.1627 0.1365 -0.0102 0.0106  -0.0100 157 ILE   B CG1 
2984 C  CG2 . ILE   B 157 ? 0.1577 0.1565 0.1337 -0.0088 0.0100  -0.0079 157 ILE   B CG2 
2985 C  CD1 . ILE   B 157 ? 0.1609 0.1686 0.1418 -0.0092 0.0096  -0.0122 157 ILE   B CD1 
2986 N  N   . SER   B 158 ? 0.1500 0.1431 0.1226 -0.0050 0.0078  -0.0025 158 SER   B N   
2987 C  CA  . SER   B 158 ? 0.1442 0.1349 0.1162 -0.0036 0.0070  -0.0009 158 SER   B CA  
2988 C  C   . SER   B 158 ? 0.1544 0.1414 0.1231 -0.0035 0.0076  0.0010  158 SER   B C   
2989 O  O   . SER   B 158 ? 0.1596 0.1437 0.1273 -0.0032 0.0079  0.0019  158 SER   B O   
2990 C  CB  . SER   B 158 ? 0.1444 0.1367 0.1183 -0.0018 0.0055  -0.0007 158 SER   B CB  
2991 O  OG  . SER   B 158 ? 0.1455 0.1406 0.1222 -0.0015 0.0050  -0.0019 158 SER   B OG  
2992 N  N   . ILE   B 159 ? 0.1664 0.1540 0.1336 -0.0036 0.0076  0.0016  159 ILE   B N   
2993 C  CA  . ILE   B 159 ? 0.1657 0.1502 0.1295 -0.0031 0.0079  0.0038  159 ILE   B CA  
2994 C  C   . ILE   B 159 ? 0.1795 0.1604 0.1411 -0.0048 0.0097  0.0044  159 ILE   B C   
2995 O  O   . ILE   B 159 ? 0.1759 0.1529 0.1357 -0.0041 0.0100  0.0061  159 ILE   B O   
2996 C  CB  . ILE   B 159 ? 0.1828 0.1699 0.1455 -0.0030 0.0076  0.0040  159 ILE   B CB  
2997 C  CG1 . ILE   B 159 ? 0.1745 0.1641 0.1393 -0.0013 0.0060  0.0036  159 ILE   B CG1 
2998 C  CG2 . ILE   B 159 ? 0.1912 0.1756 0.1498 -0.0029 0.0082  0.0064  159 ILE   B CG2 
2999 C  CD1 . ILE   B 159 ? 0.1756 0.1689 0.1406 -0.0014 0.0057  0.0028  159 ILE   B CD1 
3000 N  N   . LYS   B 160 ? 0.1731 0.1555 0.1350 -0.0070 0.0110  0.0029  160 LYS   B N   
3001 C  CA  . LYS   B 160 ? 0.1963 0.1752 0.1563 -0.0091 0.0131  0.0032  160 LYS   B CA  
3002 C  C   . LYS   B 160 ? 0.1996 0.1758 0.1608 -0.0090 0.0135  0.0027  160 LYS   B C   
3003 O  O   . LYS   B 160 ? 0.1942 0.1658 0.1535 -0.0098 0.0150  0.0038  160 LYS   B O   
3004 C  CB  . LYS   B 160 ? 0.2365 0.2184 0.1974 -0.0117 0.0144  0.0008  160 LYS   B CB  
3005 C  CG  . LYS   B 160 ? 0.3125 0.2964 0.2715 -0.0125 0.0147  0.0013  160 LYS   B CG  
3006 C  CD  . LYS   B 160 ? 0.3793 0.3667 0.3396 -0.0151 0.0161  -0.0015 160 LYS   B CD  
3007 C  CE  . LYS   B 160 ? 0.4310 0.4207 0.3892 -0.0163 0.0167  -0.0013 160 LYS   B CE  
3008 N  NZ  . LYS   B 160 ? 0.5006 0.4941 0.4605 -0.0188 0.0180  -0.0044 160 LYS   B NZ  
3009 N  N   . ALA   B 161 ? 0.1722 0.1514 0.1366 -0.0081 0.0123  0.0011  161 ALA   B N   
3010 C  CA  . ALA   B 161 ? 0.1923 0.1701 0.1580 -0.0081 0.0126  0.0003  161 ALA   B CA  
3011 C  C   . ALA   B 161 ? 0.2012 0.1759 0.1663 -0.0060 0.0118  0.0021  161 ALA   B C   
3012 O  O   . ALA   B 161 ? 0.2112 0.1846 0.1774 -0.0060 0.0121  0.0013  161 ALA   B O   
3013 C  CB  . ALA   B 161 ? 0.1930 0.1756 0.1620 -0.0079 0.0116  -0.0020 161 ALA   B CB  
3014 N  N   . GLY   B 162 ? 0.1914 0.1655 0.1548 -0.0042 0.0106  0.0041  162 GLY   B N   
3015 C  CA  . GLY   B 162 ? 0.1941 0.1654 0.1567 -0.0021 0.0099  0.0058  162 GLY   B CA  
3016 C  C   . GLY   B 162 ? 0.1835 0.1579 0.1478 -0.0001 0.0079  0.0056  162 GLY   B C   
3017 O  O   . GLY   B 162 ? 0.1980 0.1709 0.1622 0.0016  0.0072  0.0064  162 GLY   B O   
3018 N  N   . ALA   B 163 ? 0.1682 0.1467 0.1341 -0.0002 0.0070  0.0046  163 ALA   B N   
3019 C  CA  . ALA   B 163 ? 0.1620 0.1430 0.1294 0.0015  0.0054  0.0046  163 ALA   B CA  
3020 C  C   . ALA   B 163 ? 0.1586 0.1385 0.1243 0.0032  0.0047  0.0062  163 ALA   B C   
3021 O  O   . ALA   B 163 ? 0.1711 0.1505 0.1346 0.0032  0.0049  0.0073  163 ALA   B O   
3022 C  CB  . ALA   B 163 ? 0.1568 0.1413 0.1258 0.0011  0.0049  0.0037  163 ALA   B CB  
3023 N  N   . ASP   B 164 ? 0.1559 0.1362 0.1226 0.0047  0.0037  0.0063  164 ASP   B N   
3024 C  CA  . ASP   B 164 ? 0.1604 0.1410 0.1261 0.0065  0.0028  0.0073  164 ASP   B CA  
3025 C  C   . ASP   B 164 ? 0.1535 0.1378 0.1203 0.0068  0.0019  0.0066  164 ASP   B C   
3026 O  O   . ASP   B 164 ? 0.1586 0.1442 0.1245 0.0080  0.0012  0.0071  164 ASP   B O   
3027 C  CB  . ASP   B 164 ? 0.1583 0.1378 0.1248 0.0078  0.0023  0.0072  164 ASP   B CB  
3028 C  CG  . ASP   B 164 ? 0.1842 0.1596 0.1500 0.0075  0.0034  0.0075  164 ASP   B CG  
3029 O  OD1 . ASP   B 164 ? 0.1929 0.1651 0.1563 0.0075  0.0041  0.0090  164 ASP   B OD1 
3030 O  OD2 . ASP   B 164 ? 0.1849 0.1602 0.1523 0.0073  0.0036  0.0064  164 ASP   B OD2 
3031 N  N   . PHE   B 165 ? 0.1483 0.1346 0.1174 0.0059  0.0018  0.0054  165 PHE   B N   
3032 C  CA  . PHE   B 165 ? 0.1458 0.1351 0.1166 0.0058  0.0014  0.0046  165 PHE   B CA  
3033 C  C   . PHE   B 165 ? 0.1389 0.1291 0.1112 0.0045  0.0018  0.0037  165 PHE   B C   
3034 O  O   . PHE   B 165 ? 0.1463 0.1356 0.1191 0.0039  0.0022  0.0035  165 PHE   B O   
3035 C  CB  . PHE   B 165 ? 0.1460 0.1367 0.1188 0.0064  0.0007  0.0041  165 PHE   B CB  
3036 C  CG  . PHE   B 165 ? 0.1581 0.1500 0.1306 0.0077  0.0001  0.0041  165 PHE   B CG  
3037 C  CD1 . PHE   B 165 ? 0.1941 0.1847 0.1653 0.0089  -0.0002 0.0048  165 PHE   B CD1 
3038 C  CD2 . PHE   B 165 ? 0.1812 0.1758 0.1550 0.0077  -0.0002 0.0032  165 PHE   B CD2 
3039 C  CE1 . PHE   B 165 ? 0.2101 0.2026 0.1814 0.0102  -0.0010 0.0045  165 PHE   B CE1 
3040 C  CE2 . PHE   B 165 ? 0.1964 0.1929 0.1702 0.0087  -0.0008 0.0028  165 PHE   B CE2 
3041 C  CZ  . PHE   B 165 ? 0.2062 0.2018 0.1787 0.0101  -0.0012 0.0034  165 PHE   B CZ  
3042 N  N   . ILE   B 166 ? 0.1358 0.1281 0.1092 0.0042  0.0018  0.0029  166 ILE   B N   
3043 C  CA  . ILE   B 166 ? 0.1362 0.1298 0.1120 0.0034  0.0020  0.0018  166 ILE   B CA  
3044 C  C   . ILE   B 166 ? 0.1488 0.1437 0.1271 0.0040  0.0015  0.0013  166 ILE   B C   
3045 O  O   . ILE   B 166 ? 0.1452 0.1411 0.1235 0.0043  0.0013  0.0010  166 ILE   B O   
3046 C  CB  . ILE   B 166 ? 0.1478 0.1424 0.1233 0.0024  0.0026  0.0009  166 ILE   B CB  
3047 C  CG1 . ILE   B 166 ? 0.1462 0.1426 0.1209 0.0024  0.0026  0.0006  166 ILE   B CG1 
3048 C  CG2 . ILE   B 166 ? 0.1553 0.1482 0.1286 0.0015  0.0034  0.0015  166 ILE   B CG2 
3049 C  CD1 . ILE   B 166 ? 0.1517 0.1501 0.1266 0.0012  0.0033  -0.0007 166 ILE   B CD1 
3050 N  N   . LYS   B 167 ? 0.1433 0.1381 0.1235 0.0041  0.0014  0.0013  167 LYS   B N   
3051 C  CA  . LYS   B 167 ? 0.1471 0.1423 0.1294 0.0045  0.0012  0.0014  167 LYS   B CA  
3052 C  C   . LYS   B 167 ? 0.1410 0.1367 0.1259 0.0044  0.0013  0.0007  167 LYS   B C   
3053 O  O   . LYS   B 167 ? 0.1273 0.1233 0.1124 0.0044  0.0013  0.0006  167 LYS   B O   
3054 C  CB  . LYS   B 167 ? 0.1541 0.1484 0.1357 0.0049  0.0009  0.0025  167 LYS   B CB  
3055 C  CG  . LYS   B 167 ? 0.1748 0.1691 0.1580 0.0052  0.0008  0.0031  167 LYS   B CG  
3056 C  CD  . LYS   B 167 ? 0.1806 0.1748 0.1627 0.0054  0.0005  0.0040  167 LYS   B CD  
3057 C  CE  . LYS   B 167 ? 0.2085 0.2027 0.1920 0.0055  0.0006  0.0049  167 LYS   B CE  
3058 N  NZ  . LYS   B 167 ? 0.2434 0.2381 0.2259 0.0054  0.0004  0.0057  167 LYS   B NZ  
3059 N  N   . THR   B 168 ? 0.1353 0.1312 0.1225 0.0045  0.0015  0.0001  168 THR   B N   
3060 C  CA  . THR   B 168 ? 0.1398 0.1360 0.1299 0.0047  0.0017  -0.0008 168 THR   B CA  
3061 C  C   . THR   B 168 ? 0.1391 0.1345 0.1299 0.0055  0.0013  0.0006  168 THR   B C   
3062 O  O   . THR   B 168 ? 0.1404 0.1367 0.1326 0.0059  0.0012  0.0001  168 THR   B O   
3063 C  CB  . THR   B 168 ? 0.1465 0.1427 0.1392 0.0045  0.0023  -0.0019 168 THR   B CB  
3064 O  OG1 . THR   B 168 ? 0.1433 0.1380 0.1364 0.0047  0.0023  -0.0007 168 THR   B OG1 
3065 C  CG2 . THR   B 168 ? 0.1408 0.1390 0.1329 0.0037  0.0026  -0.0035 168 THR   B CG2 
3066 N  N   . SER   B 169 ? 0.1381 0.1324 0.1284 0.0059  0.0011  0.0022  169 SER   B N   
3067 C  CA  . SER   B 169 ? 0.1433 0.1369 0.1350 0.0068  0.0009  0.0036  169 SER   B CA  
3068 C  C   . SER   B 169 ? 0.1472 0.1407 0.1369 0.0070  0.0005  0.0055  169 SER   B C   
3069 O  O   . SER   B 169 ? 0.1612 0.1546 0.1492 0.0064  0.0007  0.0055  169 SER   B O   
3070 C  CB  . SER   B 169 ? 0.1491 0.1410 0.1435 0.0070  0.0015  0.0036  169 SER   B CB  
3071 O  OG  . SER   B 169 ? 0.1593 0.1518 0.1558 0.0066  0.0019  0.0013  169 SER   B OG  
3072 N  N   . THR   B 170 ? 0.1541 0.1480 0.1442 0.0079  0.0000  0.0069  170 THR   B N   
3073 C  CA  . THR   B 170 ? 0.1548 0.1491 0.1432 0.0081  -0.0002 0.0087  170 THR   B CA  
3074 C  C   . THR   B 170 ? 0.1741 0.1663 0.1631 0.0079  0.0003  0.0102  170 THR   B C   
3075 O  O   . THR   B 170 ? 0.1814 0.1740 0.1687 0.0076  0.0004  0.0114  170 THR   B O   
3076 C  CB  . THR   B 170 ? 0.1575 0.1537 0.1457 0.0092  -0.0010 0.0098  170 THR   B CB  
3077 O  OG1 . THR   B 170 ? 0.1520 0.1471 0.1426 0.0105  -0.0012 0.0107  170 THR   B OG1 
3078 C  CG2 . THR   B 170 ? 0.1545 0.1532 0.1421 0.0090  -0.0014 0.0082  170 THR   B CG2 
3079 N  N   . GLY   B 171 ? 0.1669 0.1570 0.1584 0.0082  0.0009  0.0101  171 GLY   B N   
3080 C  CA  . GLY   B 171 ? 0.1968 0.1845 0.1892 0.0081  0.0017  0.0117  171 GLY   B CA  
3081 C  C   . GLY   B 171 ? 0.2217 0.2087 0.2141 0.0096  0.0012  0.0145  171 GLY   B C   
3082 O  O   . GLY   B 171 ? 0.2576 0.2421 0.2504 0.0095  0.0020  0.0164  171 GLY   B O   
3083 N  N   . ARG   B 172 ? 0.2039 0.1932 0.1959 0.0109  0.0001  0.0147  172 ARG   B N   
3084 C  CA  . ARG   B 172 ? 0.2276 0.2173 0.2192 0.0126  -0.0006 0.0175  172 ARG   B CA  
3085 C  C   . ARG   B 172 ? 0.2446 0.2338 0.2390 0.0145  -0.0011 0.0175  172 ARG   B C   
3086 O  O   . ARG   B 172 ? 0.2848 0.2749 0.2792 0.0164  -0.0020 0.0197  172 ARG   B O   
3087 C  CB  . ARG   B 172 ? 0.2528 0.2468 0.2418 0.0127  -0.0016 0.0178  172 ARG   B CB  
3088 C  CG  . ARG   B 172 ? 0.2758 0.2705 0.2622 0.0110  -0.0012 0.0179  172 ARG   B CG  
3089 C  CD  . ARG   B 172 ? 0.3345 0.3275 0.3199 0.0107  -0.0005 0.0206  172 ARG   B CD  
3090 N  NE  . ARG   B 172 ? 0.4766 0.4732 0.4596 0.0112  -0.0013 0.0222  172 ARG   B NE  
3091 C  CZ  . ARG   B 172 ? 0.4765 0.4758 0.4574 0.0099  -0.0012 0.0215  172 ARG   B CZ  
3092 N  NH1 . ARG   B 172 ? 0.5118 0.5098 0.4925 0.0082  -0.0003 0.0200  172 ARG   B NH1 
3093 N  NH2 . ARG   B 172 ? 0.5255 0.5291 0.5046 0.0104  -0.0021 0.0221  172 ARG   B NH2 
3094 N  N   . VAL   B 173 ? 0.2115 0.1998 0.2086 0.0142  -0.0007 0.0149  173 VAL   B N   
3095 C  CA  . VAL   B 173 ? 0.2143 0.2021 0.2146 0.0160  -0.0010 0.0143  173 VAL   B CA  
3096 C  C   . VAL   B 173 ? 0.2149 0.1984 0.2183 0.0156  0.0003  0.0139  173 VAL   B C   
3097 O  O   . VAL   B 173 ? 0.2257 0.2073 0.2285 0.0138  0.0015  0.0135  173 VAL   B O   
3098 C  CB  . VAL   B 173 ? 0.2275 0.2188 0.2285 0.0158  -0.0016 0.0112  173 VAL   B CB  
3099 C  CG1 . VAL   B 173 ? 0.2387 0.2342 0.2371 0.0160  -0.0027 0.0115  173 VAL   B CG1 
3100 C  CG2 . VAL   B 173 ? 0.2245 0.2157 0.2253 0.0135  -0.0007 0.0085  173 VAL   B CG2 
3101 N  N   . ALA   B 174 ? 0.2291 0.2113 0.2360 0.0173  0.0003  0.0135  174 ALA   B N   
3102 C  CA  . ALA   B 174 ? 0.2460 0.2238 0.2565 0.0173  0.0017  0.0130  174 ALA   B CA  
3103 C  C   . ALA   B 174 ? 0.2204 0.1987 0.2322 0.0149  0.0028  0.0093  174 ALA   B C   
3104 O  O   . ALA   B 174 ? 0.2173 0.1925 0.2305 0.0136  0.0043  0.0088  174 ALA   B O   
3105 C  CB  . ALA   B 174 ? 0.2525 0.2296 0.2668 0.0199  0.0011  0.0130  174 ALA   B CB  
3106 N  N   . VAL   B 175 ? 0.2027 0.1849 0.2139 0.0143  0.0022  0.0066  175 VAL   B N   
3107 C  CA  . VAL   B 175 ? 0.2054 0.1888 0.2177 0.0123  0.0031  0.0031  175 VAL   B CA  
3108 C  C   . VAL   B 175 ? 0.1871 0.1730 0.1953 0.0107  0.0028  0.0028  175 VAL   B C   
3109 O  O   . VAL   B 175 ? 0.1763 0.1649 0.1823 0.0110  0.0018  0.0030  175 VAL   B O   
3110 C  CB  . VAL   B 175 ? 0.1967 0.1825 0.2121 0.0129  0.0029  0.0001  175 VAL   B CB  
3111 C  CG1 . VAL   B 175 ? 0.1975 0.1853 0.2135 0.0108  0.0038  -0.0035 175 VAL   B CG1 
3112 C  CG2 . VAL   B 175 ? 0.2137 0.1965 0.2337 0.0147  0.0033  0.0001  175 VAL   B CG2 
3113 N  N   . ASN   B 176 ? 0.1858 0.1711 0.1934 0.0090  0.0037  0.0021  176 ASN   B N   
3114 C  CA  . ASN   B 176 ? 0.1897 0.1771 0.1936 0.0078  0.0034  0.0019  176 ASN   B CA  
3115 C  C   . ASN   B 176 ? 0.1718 0.1613 0.1766 0.0065  0.0040  -0.0013 176 ASN   B C   
3116 O  O   . ASN   B 176 ? 0.1859 0.1764 0.1930 0.0068  0.0041  -0.0032 176 ASN   B O   
3117 C  CB  . ASN   B 176 ? 0.2038 0.1897 0.2057 0.0073  0.0037  0.0040  176 ASN   B CB  
3118 C  CG  . ASN   B 176 ? 0.2319 0.2169 0.2326 0.0086  0.0029  0.0071  176 ASN   B CG  
3119 O  OD1 . ASN   B 176 ? 0.2246 0.2116 0.2229 0.0091  0.0019  0.0078  176 ASN   B OD1 
3120 N  ND2 . ASN   B 176 ? 0.2680 0.2498 0.2704 0.0093  0.0035  0.0088  176 ASN   B ND2 
3121 N  N   . ALA   B 177 ? 0.1570 0.1475 0.1600 0.0053  0.0043  -0.0020 177 ALA   B N   
3122 C  CA  . ALA   B 177 ? 0.1572 0.1505 0.1604 0.0043  0.0046  -0.0047 177 ALA   B CA  
3123 C  C   . ALA   B 177 ? 0.1570 0.1501 0.1645 0.0038  0.0057  -0.0072 177 ALA   B C   
3124 O  O   . ALA   B 177 ? 0.1695 0.1599 0.1795 0.0038  0.0066  -0.0068 177 ALA   B O   
3125 C  CB  . ALA   B 177 ? 0.1560 0.1506 0.1567 0.0034  0.0046  -0.0048 177 ALA   B CB  
3126 N  N   . THR   B 178 ? 0.1643 0.1605 0.1725 0.0032  0.0059  -0.0099 178 THR   B N   
3127 C  CA  . THR   B 178 ? 0.1793 0.1769 0.1913 0.0022  0.0071  -0.0131 178 THR   B CA  
3128 C  C   . THR   B 178 ? 0.1780 0.1802 0.1880 0.0011  0.0070  -0.0151 178 THR   B C   
3129 O  O   . THR   B 178 ? 0.1542 0.1578 0.1604 0.0013  0.0060  -0.0139 178 THR   B O   
3130 C  CB  . THR   B 178 ? 0.1905 0.1880 0.2063 0.0028  0.0074  -0.0148 178 THR   B CB  
3131 O  OG1 . THR   B 178 ? 0.1966 0.1974 0.2106 0.0027  0.0067  -0.0156 178 THR   B OG1 
3132 C  CG2 . THR   B 178 ? 0.2038 0.1972 0.2212 0.0045  0.0071  -0.0124 178 THR   B CG2 
3133 N  N   . PRO   B 179 ? 0.1885 0.1932 0.2011 -0.0001 0.0080  -0.0183 179 PRO   B N   
3134 C  CA  . PRO   B 179 ? 0.1847 0.1947 0.1955 -0.0010 0.0079  -0.0203 179 PRO   B CA  
3135 C  C   . PRO   B 179 ? 0.1746 0.1868 0.1838 -0.0009 0.0073  -0.0206 179 PRO   B C   
3136 O  O   . PRO   B 179 ? 0.1853 0.2001 0.1906 -0.0010 0.0066  -0.0200 179 PRO   B O   
3137 C  CB  . PRO   B 179 ? 0.1932 0.2057 0.2083 -0.0023 0.0093  -0.0243 179 PRO   B CB  
3138 C  CG  . PRO   B 179 ? 0.2049 0.2125 0.2225 -0.0022 0.0102  -0.0232 179 PRO   B CG  
3139 C  CD  . PRO   B 179 ? 0.2019 0.2048 0.2192 -0.0007 0.0095  -0.0201 179 PRO   B CD  
3140 N  N   . GLU   B 180 ? 0.1911 0.2023 0.2034 -0.0006 0.0077  -0.0216 180 GLU   B N   
3141 C  CA  . GLU   B 180 ? 0.2110 0.2248 0.2223 -0.0008 0.0073  -0.0224 180 GLU   B CA  
3142 C  C   . GLU   B 180 ? 0.1844 0.1965 0.1911 -0.0001 0.0062  -0.0191 180 GLU   B C   
3143 O  O   . GLU   B 180 ? 0.1715 0.1860 0.1748 -0.0007 0.0060  -0.0189 180 GLU   B O   
3144 C  CB  . GLU   B 180 ? 0.2608 0.2738 0.2770 -0.0003 0.0079  -0.0244 180 GLU   B CB  
3145 C  CG  . GLU   B 180 ? 0.3416 0.3558 0.3631 -0.0011 0.0093  -0.0281 180 GLU   B CG  
3146 C  CD  . GLU   B 180 ? 0.4410 0.4515 0.4653 -0.0010 0.0101  -0.0279 180 GLU   B CD  
3147 O  OE1 . GLU   B 180 ? 0.3820 0.3880 0.4052 0.0000  0.0097  -0.0246 180 GLU   B OE1 
3148 O  OE2 . GLU   B 180 ? 0.6270 0.6397 0.6550 -0.0022 0.0114  -0.0315 180 GLU   B OE2 
3149 N  N   . SER   B 181 ? 0.1745 0.1825 0.1809 0.0011  0.0057  -0.0164 181 SER   B N   
3150 C  CA  . SER   B 181 ? 0.1770 0.1840 0.1795 0.0015  0.0048  -0.0138 181 SER   B CA  
3151 C  C   . SER   B 181 ? 0.1665 0.1739 0.1646 0.0012  0.0045  -0.0123 181 SER   B C   
3152 O  O   . SER   B 181 ? 0.1616 0.1693 0.1562 0.0010  0.0041  -0.0112 181 SER   B O   
3153 C  CB  . SER   B 181 ? 0.1968 0.2002 0.2000 0.0029  0.0043  -0.0116 181 SER   B CB  
3154 O  OG  . SER   B 181 ? 0.2236 0.2245 0.2273 0.0033  0.0044  -0.0101 181 SER   B OG  
3155 N  N   . ALA   B 182 ? 0.1566 0.1640 0.1549 0.0012  0.0046  -0.0124 182 ALA   B N   
3156 C  CA  . ALA   B 182 ? 0.1569 0.1654 0.1516 0.0011  0.0041  -0.0114 182 ALA   B CA  
3157 C  C   . ALA   B 182 ? 0.1529 0.1652 0.1456 0.0004  0.0042  -0.0126 182 ALA   B C   
3158 O  O   . ALA   B 182 ? 0.1648 0.1771 0.1534 0.0006  0.0037  -0.0108 182 ALA   B O   
3159 C  CB  . ALA   B 182 ? 0.1640 0.1727 0.1601 0.0011  0.0044  -0.0120 182 ALA   B CB  
3160 N  N   . ARG   B 183 ? 0.1542 0.1698 0.1496 -0.0005 0.0049  -0.0156 183 ARG   B N   
3161 C  CA  . ARG   B 183 ? 0.1693 0.1894 0.1628 -0.0013 0.0051  -0.0169 183 ARG   B CA  
3162 C  C   . ARG   B 183 ? 0.1610 0.1802 0.1517 -0.0016 0.0050  -0.0155 183 ARG   B C   
3163 O  O   . ARG   B 183 ? 0.1562 0.1766 0.1428 -0.0018 0.0048  -0.0142 183 ARG   B O   
3164 C  CB  . ARG   B 183 ? 0.1778 0.2018 0.1755 -0.0024 0.0060  -0.0209 183 ARG   B CB  
3165 C  CG  . ARG   B 183 ? 0.2141 0.2435 0.2099 -0.0034 0.0063  -0.0225 183 ARG   B CG  
3166 C  CD  . ARG   B 183 ? 0.2431 0.2767 0.2437 -0.0046 0.0073  -0.0269 183 ARG   B CD  
3167 N  NE  . ARG   B 183 ? 0.2852 0.3164 0.2898 -0.0046 0.0078  -0.0281 183 ARG   B NE  
3168 C  CZ  . ARG   B 183 ? 0.3094 0.3408 0.3133 -0.0050 0.0079  -0.0281 183 ARG   B CZ  
3169 N  NH1 . ARG   B 183 ? 0.3578 0.3910 0.3569 -0.0056 0.0077  -0.0267 183 ARG   B NH1 
3170 N  NH2 . ARG   B 183 ? 0.3644 0.3943 0.3726 -0.0047 0.0083  -0.0295 183 ARG   B NH2 
3171 N  N   . ILE   B 184 ? 0.1488 0.1661 0.1420 -0.0016 0.0052  -0.0159 184 ILE   B N   
3172 C  CA  . ILE   B 184 ? 0.1473 0.1643 0.1384 -0.0021 0.0053  -0.0152 184 ILE   B CA  
3173 C  C   . ILE   B 184 ? 0.1395 0.1536 0.1260 -0.0017 0.0048  -0.0119 184 ILE   B C   
3174 O  O   . ILE   B 184 ? 0.1468 0.1614 0.1298 -0.0025 0.0051  -0.0109 184 ILE   B O   
3175 C  CB  . ILE   B 184 ? 0.1549 0.1707 0.1498 -0.0018 0.0055  -0.0162 184 ILE   B CB  
3176 C  CG1 . ILE   B 184 ? 0.1689 0.1878 0.1684 -0.0023 0.0061  -0.0198 184 ILE   B CG1 
3177 C  CG2 . ILE   B 184 ? 0.1628 0.1783 0.1555 -0.0024 0.0056  -0.0154 184 ILE   B CG2 
3178 C  CD1 . ILE   B 184 ? 0.1838 0.2010 0.1880 -0.0012 0.0061  -0.0207 184 ILE   B CD1 
3179 N  N   . MET   B 185 ? 0.1368 0.1476 0.1235 -0.0005 0.0042  -0.0101 185 MET   B N   
3180 C  CA  . MET   B 185 ? 0.1394 0.1473 0.1223 -0.0001 0.0038  -0.0073 185 MET   B CA  
3181 C  C   . MET   B 185 ? 0.1456 0.1544 0.1248 0.0000  0.0037  -0.0062 185 MET   B C   
3182 O  O   . MET   B 185 ? 0.1522 0.1594 0.1278 -0.0002 0.0038  -0.0044 185 MET   B O   
3183 C  CB  . MET   B 185 ? 0.1449 0.1499 0.1290 0.0011  0.0033  -0.0060 185 MET   B CB  
3184 C  CG  . MET   B 185 ? 0.1454 0.1493 0.1320 0.0012  0.0033  -0.0063 185 MET   B CG  
3185 S  SD  . MET   B 185 ? 0.1535 0.1545 0.1412 0.0025  0.0027  -0.0046 185 MET   B SD  
3186 C  CE  . MET   B 185 ? 0.1633 0.1623 0.1470 0.0026  0.0024  -0.0024 185 MET   B CE  
3187 N  N   . MET   B 186 ? 0.1546 0.1660 0.1346 0.0004  0.0034  -0.0072 186 MET   B N   
3188 C  CA  . MET   B 186 ? 0.1545 0.1675 0.1310 0.0009  0.0030  -0.0061 186 MET   B CA  
3189 C  C   . MET   B 186 ? 0.1598 0.1755 0.1338 -0.0002 0.0036  -0.0064 186 MET   B C   
3190 O  O   . MET   B 186 ? 0.1528 0.1681 0.1227 0.0001  0.0034  -0.0043 186 MET   B O   
3191 C  CB  . MET   B 186 ? 0.1667 0.1825 0.1448 0.0015  0.0026  -0.0074 186 MET   B CB  
3192 C  CG  . MET   B 186 ? 0.1918 0.2048 0.1707 0.0026  0.0021  -0.0063 186 MET   B CG  
3193 S  SD  . MET   B 186 ? 0.2119 0.2288 0.1927 0.0031  0.0018  -0.0083 186 MET   B SD  
3194 C  CE  . MET   B 186 ? 0.2104 0.2268 0.1968 0.0019  0.0028  -0.0108 186 MET   B CE  
3195 N  N   . GLU   B 187 ? 0.1614 0.1798 0.1380 -0.0015 0.0043  -0.0090 187 GLU   B N   
3196 C  CA  . GLU   B 187 ? 0.1793 0.2005 0.1536 -0.0029 0.0050  -0.0094 187 GLU   B CA  
3197 C  C   . GLU   B 187 ? 0.1786 0.1961 0.1496 -0.0034 0.0055  -0.0070 187 GLU   B C   
3198 O  O   . GLU   B 187 ? 0.1909 0.2090 0.1578 -0.0042 0.0059  -0.0056 187 GLU   B O   
3199 C  CB  . GLU   B 187 ? 0.1890 0.2140 0.1672 -0.0043 0.0058  -0.0130 187 GLU   B CB  
3200 C  CG  . GLU   B 187 ? 0.2112 0.2409 0.1924 -0.0043 0.0057  -0.0159 187 GLU   B CG  
3201 C  CD  . GLU   B 187 ? 0.2730 0.3061 0.2587 -0.0056 0.0066  -0.0198 187 GLU   B CD  
3202 O  OE1 . GLU   B 187 ? 0.3149 0.3467 0.3017 -0.0062 0.0071  -0.0202 187 GLU   B OE1 
3203 O  OE2 . GLU   B 187 ? 0.2625 0.2997 0.2512 -0.0059 0.0069  -0.0228 187 GLU   B OE2 
3204 N  N   . VAL   B 188 ? 0.1639 0.1776 0.1365 -0.0033 0.0055  -0.0065 188 VAL   B N   
3205 C  CA  . VAL   B 188 ? 0.1699 0.1802 0.1397 -0.0039 0.0061  -0.0046 188 VAL   B CA  
3206 C  C   . VAL   B 188 ? 0.1725 0.1798 0.1379 -0.0030 0.0058  -0.0014 188 VAL   B C   
3207 O  O   . VAL   B 188 ? 0.1713 0.1772 0.1331 -0.0038 0.0066  0.0003  188 VAL   B O   
3208 C  CB  . VAL   B 188 ? 0.1737 0.1813 0.1460 -0.0038 0.0061  -0.0050 188 VAL   B CB  
3209 C  CG1 . VAL   B 188 ? 0.1799 0.1843 0.1495 -0.0047 0.0069  -0.0034 188 VAL   B CG1 
3210 C  CG2 . VAL   B 188 ? 0.1804 0.1909 0.1570 -0.0045 0.0063  -0.0079 188 VAL   B CG2 
3211 N  N   . ILE   B 189 ? 0.1697 0.1759 0.1357 -0.0012 0.0047  -0.0006 189 ILE   B N   
3212 C  CA  . ILE   B 189 ? 0.1688 0.1725 0.1312 0.0002  0.0042  0.0022  189 ILE   B CA  
3213 C  C   . ILE   B 189 ? 0.1798 0.1860 0.1385 0.0000  0.0044  0.0032  189 ILE   B C   
3214 O  O   . ILE   B 189 ? 0.1864 0.1899 0.1412 0.0002  0.0048  0.0059  189 ILE   B O   
3215 C  CB  . ILE   B 189 ? 0.1740 0.1777 0.1382 0.0021  0.0030  0.0022  189 ILE   B CB  
3216 C  CG1 . ILE   B 189 ? 0.1620 0.1627 0.1288 0.0022  0.0030  0.0019  189 ILE   B CG1 
3217 C  CG2 . ILE   B 189 ? 0.1782 0.1806 0.1390 0.0038  0.0024  0.0046  189 ILE   B CG2 
3218 C  CD1 . ILE   B 189 ? 0.1683 0.1693 0.1371 0.0036  0.0020  0.0016  189 ILE   B CD1 
3219 N  N   . ARG   B 190 ? 0.1806 0.1923 0.1407 -0.0002 0.0041  0.0011  190 ARG   B N   
3220 C  CA  . ARG   B 190 ? 0.1970 0.2124 0.1537 -0.0003 0.0042  0.0018  190 ARG   B CA  
3221 C  C   . ARG   B 190 ? 0.1887 0.2035 0.1425 -0.0024 0.0056  0.0026  190 ARG   B C   
3222 O  O   . ARG   B 190 ? 0.2003 0.2142 0.1493 -0.0022 0.0058  0.0054  190 ARG   B O   
3223 C  CB  . ARG   B 190 ? 0.2201 0.2422 0.1796 -0.0006 0.0039  -0.0014 190 ARG   B CB  
3224 C  CG  . ARG   B 190 ? 0.2700 0.2972 0.2259 -0.0004 0.0036  -0.0008 190 ARG   B CG  
3225 C  CD  . ARG   B 190 ? 0.3256 0.3599 0.2843 -0.0018 0.0040  -0.0048 190 ARG   B CD  
3226 N  NE  . ARG   B 190 ? 0.3493 0.3834 0.3108 -0.0040 0.0052  -0.0071 190 ARG   B NE  
3227 C  CZ  . ARG   B 190 ? 0.4023 0.4413 0.3680 -0.0052 0.0057  -0.0112 190 ARG   B CZ  
3228 N  NH1 . ARG   B 190 ? 0.4538 0.4986 0.4205 -0.0049 0.0052  -0.0132 190 ARG   B NH1 
3229 N  NH2 . ARG   B 190 ? 0.3928 0.4310 0.3617 -0.0066 0.0066  -0.0133 190 ARG   B NH2 
3230 N  N   . ASP   B 191 ? 0.1771 0.1928 0.1338 -0.0043 0.0065  0.0001  191 ASP   B N   
3231 C  CA  . ASP   B 191 ? 0.1850 0.2012 0.1397 -0.0066 0.0080  0.0000  191 ASP   B CA  
3232 C  C   . ASP   B 191 ? 0.1921 0.2021 0.1433 -0.0070 0.0089  0.0032  191 ASP   B C   
3233 O  O   . ASP   B 191 ? 0.2004 0.2100 0.1479 -0.0085 0.0101  0.0046  191 ASP   B O   
3234 C  CB  . ASP   B 191 ? 0.2011 0.2197 0.1603 -0.0082 0.0087  -0.0036 191 ASP   B CB  
3235 C  CG  . ASP   B 191 ? 0.2375 0.2624 0.2001 -0.0085 0.0084  -0.0072 191 ASP   B CG  
3236 O  OD1 . ASP   B 191 ? 0.2624 0.2908 0.2236 -0.0078 0.0078  -0.0070 191 ASP   B OD1 
3237 O  OD2 . ASP   B 191 ? 0.2732 0.2993 0.2403 -0.0092 0.0087  -0.0102 191 ASP   B OD2 
3238 N  N   . MET   B 192 ? 0.1874 0.1926 0.1399 -0.0057 0.0083  0.0042  192 MET   B N   
3239 C  CA  . MET   B 192 ? 0.1988 0.1981 0.1486 -0.0060 0.0093  0.0067  192 MET   B CA  
3240 C  C   . MET   B 192 ? 0.1956 0.1920 0.1410 -0.0043 0.0089  0.0105  192 MET   B C   
3241 O  O   . MET   B 192 ? 0.2073 0.1985 0.1496 -0.0047 0.0100  0.0130  192 MET   B O   
3242 C  CB  . MET   B 192 ? 0.2114 0.2076 0.1646 -0.0055 0.0090  0.0058  192 MET   B CB  
3243 C  CG  . MET   B 192 ? 0.2244 0.2227 0.1811 -0.0074 0.0097  0.0027  192 MET   B CG  
3244 S  SD  . MET   B 192 ? 0.2609 0.2561 0.2210 -0.0067 0.0093  0.0020  192 MET   B SD  
3245 C  CE  . MET   B 192 ? 0.2555 0.2456 0.2123 -0.0084 0.0112  0.0037  192 MET   B CE  
3246 N  N   . GLY   B 193 ? 0.1916 0.1912 0.1368 -0.0022 0.0074  0.0107  193 GLY   B N   
3247 C  CA  . GLY   B 193 ? 0.1969 0.1948 0.1381 0.0000  0.0066  0.0141  193 GLY   B CA  
3248 C  C   . GLY   B 193 ? 0.1964 0.1894 0.1385 0.0022  0.0058  0.0155  193 GLY   B C   
3249 O  O   . GLY   B 193 ? 0.2075 0.1970 0.1463 0.0039  0.0057  0.0187  193 GLY   B O   
3250 N  N   . VAL   B 194 ? 0.1805 0.1735 0.1271 0.0023  0.0053  0.0131  194 VAL   B N   
3251 C  CA  . VAL   B 194 ? 0.1946 0.1830 0.1422 0.0038  0.0049  0.0140  194 VAL   B CA  
3252 C  C   . VAL   B 194 ? 0.2015 0.1925 0.1514 0.0061  0.0031  0.0131  194 VAL   B C   
3253 O  O   . VAL   B 194 ? 0.1948 0.1834 0.1466 0.0070  0.0027  0.0128  194 VAL   B O   
3254 C  CB  . VAL   B 194 ? 0.1974 0.1831 0.1478 0.0020  0.0059  0.0124  194 VAL   B CB  
3255 C  CG1 . VAL   B 194 ? 0.2224 0.2052 0.1705 -0.0003 0.0078  0.0132  194 VAL   B CG1 
3256 C  CG2 . VAL   B 194 ? 0.1884 0.1782 0.1429 0.0012  0.0055  0.0092  194 VAL   B CG2 
3257 N  N   . GLU   B 195 ? 0.2103 0.2067 0.1600 0.0069  0.0022  0.0124  195 GLU   B N   
3258 C  CA  . GLU   B 195 ? 0.2242 0.2238 0.1764 0.0085  0.0008  0.0109  195 GLU   B CA  
3259 C  C   . GLU   B 195 ? 0.2210 0.2180 0.1722 0.0112  -0.0002 0.0128  195 GLU   B C   
3260 O  O   . GLU   B 195 ? 0.2162 0.2145 0.1701 0.0122  -0.0010 0.0115  195 GLU   B O   
3261 C  CB  . GLU   B 195 ? 0.2513 0.2578 0.2036 0.0086  0.0002  0.0094  195 GLU   B CB  
3262 C  CG  . GLU   B 195 ? 0.2741 0.2823 0.2218 0.0101  -0.0003 0.0119  195 GLU   B CG  
3263 C  CD  . GLU   B 195 ? 0.3373 0.3450 0.2817 0.0083  0.0009  0.0133  195 GLU   B CD  
3264 O  OE1 . GLU   B 195 ? 0.3190 0.3252 0.2645 0.0058  0.0023  0.0121  195 GLU   B OE1 
3265 O  OE2 . GLU   B 195 ? 0.4170 0.4264 0.3574 0.0095  0.0005  0.0155  195 GLU   B OE2 
3266 N  N   . LYS   B 196 ? 0.2295 0.2227 0.1771 0.0122  0.0001  0.0159  196 LYS   B N   
3267 C  CA  . LYS   B 196 ? 0.2562 0.2463 0.2031 0.0149  -0.0008 0.0176  196 LYS   B CA  
3268 C  C   . LYS   B 196 ? 0.2450 0.2310 0.1948 0.0145  -0.0003 0.0166  196 LYS   B C   
3269 O  O   . LYS   B 196 ? 0.2637 0.2499 0.2152 0.0163  -0.0013 0.0160  196 LYS   B O   
3270 C  CB  . LYS   B 196 ? 0.3053 0.2911 0.2476 0.0161  -0.0003 0.0214  196 LYS   B CB  
3271 C  CG  . LYS   B 196 ? 0.4044 0.3862 0.3465 0.0190  -0.0010 0.0231  196 LYS   B CG  
3272 C  CD  . LYS   B 196 ? 0.5002 0.4761 0.4380 0.0202  -0.0003 0.0272  196 LYS   B CD  
3273 C  CE  . LYS   B 196 ? 0.6093 0.5790 0.5483 0.0217  0.0000  0.0280  196 LYS   B CE  
3274 N  NZ  . LYS   B 196 ? 0.7511 0.7141 0.6862 0.0224  0.0011  0.0319  196 LYS   B NZ  
3275 N  N   . SER   B 197 ? 0.2072 0.1905 0.1579 0.0119  0.0011  0.0159  197 SER   B N   
3276 C  CA  . SER   B 197 ? 0.2160 0.1953 0.1687 0.0114  0.0017  0.0153  197 SER   B CA  
3277 C  C   . SER   B 197 ? 0.2104 0.1921 0.1668 0.0099  0.0017  0.0125  197 SER   B C   
3278 O  O   . SER   B 197 ? 0.2390 0.2188 0.1974 0.0095  0.0020  0.0117  197 SER   B O   
3279 C  CB  . SER   B 197 ? 0.2325 0.2063 0.1832 0.0101  0.0034  0.0168  197 SER   B CB  
3280 O  OG  . SER   B 197 ? 0.2448 0.2198 0.1949 0.0075  0.0045  0.0162  197 SER   B OG  
3281 N  N   . VAL   B 198 ? 0.1767 0.1627 0.1342 0.0088  0.0016  0.0111  198 VAL   B N   
3282 C  CA  . VAL   B 198 ? 0.1692 0.1569 0.1300 0.0073  0.0018  0.0089  198 VAL   B CA  
3283 C  C   . VAL   B 198 ? 0.1798 0.1719 0.1428 0.0079  0.0008  0.0073  198 VAL   B C   
3284 O  O   . VAL   B 198 ? 0.1865 0.1819 0.1489 0.0080  0.0005  0.0069  198 VAL   B O   
3285 C  CB  . VAL   B 198 ? 0.1678 0.1558 0.1287 0.0051  0.0029  0.0081  198 VAL   B CB  
3286 C  CG1 . VAL   B 198 ? 0.1619 0.1516 0.1263 0.0041  0.0029  0.0060  198 VAL   B CG1 
3287 C  CG2 . VAL   B 198 ? 0.1748 0.1584 0.1336 0.0041  0.0042  0.0094  198 VAL   B CG2 
3288 N  N   . GLY   B 199 ? 0.1611 0.1534 0.1268 0.0081  0.0004  0.0062  199 GLY   B N   
3289 C  CA  . GLY   B 199 ? 0.1546 0.1504 0.1228 0.0083  -0.0001 0.0046  199 GLY   B CA  
3290 C  C   . GLY   B 199 ? 0.1522 0.1488 0.1230 0.0067  0.0004  0.0031  199 GLY   B C   
3291 O  O   . GLY   B 199 ? 0.1458 0.1408 0.1168 0.0057  0.0010  0.0032  199 GLY   B O   
3292 N  N   . PHE   B 200 ? 0.1480 0.1475 0.1212 0.0066  0.0002  0.0016  200 PHE   B N   
3293 C  CA  . PHE   B 200 ? 0.1444 0.1445 0.1206 0.0056  0.0007  0.0002  200 PHE   B CA  
3294 C  C   . PHE   B 200 ? 0.1464 0.1466 0.1249 0.0057  0.0005  -0.0002 200 PHE   B C   
3295 O  O   . PHE   B 200 ? 0.1504 0.1523 0.1291 0.0063  0.0002  -0.0007 200 PHE   B O   
3296 C  CB  . PHE   B 200 ? 0.1470 0.1505 0.1241 0.0049  0.0009  -0.0014 200 PHE   B CB  
3297 C  CG  . PHE   B 200 ? 0.1472 0.1512 0.1280 0.0040  0.0015  -0.0031 200 PHE   B CG  
3298 C  CD1 . PHE   B 200 ? 0.1569 0.1593 0.1388 0.0035  0.0018  -0.0030 200 PHE   B CD1 
3299 C  CD2 . PHE   B 200 ? 0.1653 0.1712 0.1487 0.0039  0.0017  -0.0047 200 PHE   B CD2 
3300 C  CE1 . PHE   B 200 ? 0.1559 0.1583 0.1412 0.0031  0.0022  -0.0042 200 PHE   B CE1 
3301 C  CE2 . PHE   B 200 ? 0.1739 0.1793 0.1608 0.0032  0.0023  -0.0059 200 PHE   B CE2 
3302 C  CZ  . PHE   B 200 ? 0.1628 0.1663 0.1506 0.0030  0.0025  -0.0055 200 PHE   B CZ  
3303 N  N   . LYS   B 201 ? 0.1401 0.1387 0.1203 0.0052  0.0008  0.0000  201 LYS   B N   
3304 C  CA  . LYS   B 201 ? 0.1440 0.1423 0.1261 0.0052  0.0009  -0.0001 201 LYS   B CA  
3305 C  C   . LYS   B 201 ? 0.1474 0.1456 0.1325 0.0045  0.0015  -0.0009 201 LYS   B C   
3306 O  O   . LYS   B 201 ? 0.1412 0.1385 0.1268 0.0044  0.0016  -0.0005 201 LYS   B O   
3307 C  CB  . LYS   B 201 ? 0.1463 0.1429 0.1275 0.0056  0.0006  0.0012  201 LYS   B CB  
3308 C  CG  . LYS   B 201 ? 0.1600 0.1564 0.1429 0.0053  0.0009  0.0014  201 LYS   B CG  
3309 C  CD  . LYS   B 201 ? 0.1869 0.1827 0.1685 0.0056  0.0006  0.0024  201 LYS   B CD  
3310 C  CE  . LYS   B 201 ? 0.2172 0.2129 0.2001 0.0051  0.0009  0.0030  201 LYS   B CE  
3311 N  NZ  . LYS   B 201 ? 0.2565 0.2523 0.2382 0.0053  0.0007  0.0038  201 LYS   B NZ  
3312 N  N   . VAL   B 202 ? 0.1505 0.1495 0.1376 0.0041  0.0019  -0.0020 202 VAL   B N   
3313 C  CA  A VAL   B 202 ? 0.1594 0.1577 0.1498 0.0036  0.0027  -0.0027 202 VAL   B CA  
3314 C  CA  B VAL   B 202 ? 0.1581 0.1563 0.1484 0.0036  0.0027  -0.0026 202 VAL   B CA  
3315 C  C   . VAL   B 202 ? 0.1638 0.1599 0.1547 0.0037  0.0028  -0.0011 202 VAL   B C   
3316 O  O   . VAL   B 202 ? 0.1849 0.1813 0.1753 0.0034  0.0030  -0.0009 202 VAL   B O   
3317 C  CB  A VAL   B 202 ? 0.1676 0.1680 0.1601 0.0028  0.0034  -0.0049 202 VAL   B CB  
3318 C  CB  B VAL   B 202 ? 0.1653 0.1656 0.1580 0.0028  0.0034  -0.0051 202 VAL   B CB  
3319 C  CG1 A VAL   B 202 ? 0.1686 0.1674 0.1648 0.0021  0.0045  -0.0056 202 VAL   B CG1 
3320 C  CG1 B VAL   B 202 ? 0.1651 0.1672 0.1578 0.0025  0.0036  -0.0059 202 VAL   B CG1 
3321 C  CG2 A VAL   B 202 ? 0.1700 0.1735 0.1621 0.0027  0.0033  -0.0068 202 VAL   B CG2 
3322 C  CG2 B VAL   B 202 ? 0.1638 0.1628 0.1603 0.0023  0.0044  -0.0060 202 VAL   B CG2 
3323 N  N   . THR   B 203 ? 0.1646 0.1589 0.1564 0.0040  0.0028  0.0001  203 THR   B N   
3324 C  CA  . THR   B 203 ? 0.1811 0.1735 0.1733 0.0042  0.0030  0.0019  203 THR   B CA  
3325 C  C   . THR   B 203 ? 0.1804 0.1710 0.1757 0.0042  0.0037  0.0019  203 THR   B C   
3326 O  O   . THR   B 203 ? 0.1619 0.1523 0.1585 0.0048  0.0036  0.0014  203 THR   B O   
3327 C  CB  . THR   B 203 ? 0.2122 0.2044 0.2023 0.0049  0.0022  0.0036  203 THR   B CB  
3328 O  OG1 . THR   B 203 ? 0.2558 0.2492 0.2435 0.0048  0.0017  0.0035  203 THR   B OG1 
3329 C  CG2 . THR   B 203 ? 0.2090 0.2000 0.1990 0.0052  0.0022  0.0057  203 THR   B CG2 
3330 N  N   . GLY   B 204 ? 0.1916 0.1807 0.1881 0.0035  0.0047  0.0023  204 GLY   B N   
3331 C  CA  . GLY   B 204 ? 0.2282 0.2148 0.2280 0.0035  0.0057  0.0024  204 GLY   B CA  
3332 C  C   . GLY   B 204 ? 0.2484 0.2359 0.2509 0.0027  0.0065  -0.0008 204 GLY   B C   
3333 O  O   . GLY   B 204 ? 0.2550 0.2456 0.2566 0.0024  0.0061  -0.0027 204 GLY   B O   
3334 N  N   . GLY   B 205 ? 0.2781 0.2632 0.2842 0.0025  0.0077  -0.0013 205 GLY   B N   
3335 C  CA  . GLY   B 205 ? 0.2904 0.2764 0.2999 0.0016  0.0087  -0.0046 205 GLY   B CA  
3336 C  C   . GLY   B 205 ? 0.3117 0.3007 0.3213 0.0000  0.0095  -0.0072 205 GLY   B C   
3337 O  O   . GLY   B 205 ? 0.3231 0.3145 0.3351 -0.0008 0.0101  -0.0104 205 GLY   B O   
3338 N  N   . VAL   B 206 ? 0.2808 0.2701 0.2882 -0.0006 0.0095  -0.0062 206 VAL   B N   
3339 C  CA  A VAL   B 206 ? 0.2829 0.2756 0.2905 -0.0020 0.0101  -0.0087 206 VAL   B CA  
3340 C  CA  B VAL   B 206 ? 0.2766 0.2693 0.2843 -0.0020 0.0101  -0.0088 206 VAL   B CA  
3341 C  C   . VAL   B 206 ? 0.3002 0.2909 0.3083 -0.0032 0.0114  -0.0079 206 VAL   B C   
3342 O  O   . VAL   B 206 ? 0.2937 0.2855 0.2991 -0.0032 0.0109  -0.0068 206 VAL   B O   
3343 C  CB  A VAL   B 206 ? 0.2801 0.2767 0.2840 -0.0013 0.0086  -0.0088 206 VAL   B CB  
3344 C  CB  B VAL   B 206 ? 0.2650 0.2616 0.2690 -0.0012 0.0085  -0.0089 206 VAL   B CB  
3345 C  CG1 A VAL   B 206 ? 0.2935 0.2947 0.2983 -0.0024 0.0091  -0.0120 206 VAL   B CG1 
3346 C  CG1 B VAL   B 206 ? 0.2672 0.2626 0.2677 -0.0001 0.0073  -0.0057 206 VAL   B CG1 
3347 C  CG2 A VAL   B 206 ? 0.2919 0.2895 0.2943 -0.0001 0.0072  -0.0084 206 VAL   B CG2 
3348 C  CG2 B VAL   B 206 ? 0.2774 0.2783 0.2816 -0.0022 0.0089  -0.0116 206 VAL   B CG2 
3349 N  N   . SER   B 207 ? 0.3064 0.2940 0.3180 -0.0043 0.0133  -0.0087 207 SER   B N   
3350 C  CA  . SER   B 207 ? 0.3537 0.3384 0.3660 -0.0057 0.0150  -0.0076 207 SER   B CA  
3351 C  C   . SER   B 207 ? 0.3307 0.3191 0.3439 -0.0078 0.0162  -0.0109 207 SER   B C   
3352 O  O   . SER   B 207 ? 0.3793 0.3672 0.3914 -0.0089 0.0169  -0.0099 207 SER   B O   
3353 C  CB  . SER   B 207 ? 0.3783 0.3577 0.3942 -0.0061 0.0167  -0.0070 207 SER   B CB  
3354 O  OG  . SER   B 207 ? 0.4524 0.4287 0.4667 -0.0040 0.0155  -0.0032 207 SER   B OG  
3355 N  N   . THR   B 208 ? 0.2659 0.2584 0.2813 -0.0084 0.0164  -0.0148 208 THR   B N   
3356 C  CA  . THR   B 208 ? 0.2670 0.2632 0.2845 -0.0105 0.0179  -0.0187 208 THR   B CA  
3357 C  C   . THR   B 208 ? 0.2539 0.2571 0.2696 -0.0098 0.0162  -0.0210 208 THR   B C   
3358 O  O   . THR   B 208 ? 0.2385 0.2432 0.2522 -0.0080 0.0144  -0.0202 208 THR   B O   
3359 C  CB  . THR   B 208 ? 0.2755 0.2706 0.2983 -0.0122 0.0202  -0.0220 208 THR   B CB  
3360 O  OG1 . THR   B 208 ? 0.2645 0.2628 0.2883 -0.0113 0.0192  -0.0242 208 THR   B OG1 
3361 C  CG2 . THR   B 208 ? 0.2951 0.2824 0.3198 -0.0125 0.0219  -0.0194 208 THR   B CG2 
3362 N  N   . ALA   B 209 ? 0.2620 0.2696 0.2786 -0.0113 0.0171  -0.0239 209 ALA   B N   
3363 C  CA  . ALA   B 209 ? 0.2686 0.2836 0.2842 -0.0107 0.0158  -0.0267 209 ALA   B CA  
3364 C  C   . ALA   B 209 ? 0.2596 0.2774 0.2769 -0.0103 0.0155  -0.0291 209 ALA   B C   
3365 O  O   . ALA   B 209 ? 0.2336 0.2556 0.2483 -0.0087 0.0136  -0.0292 209 ALA   B O   
3366 C  CB  . ALA   B 209 ? 0.2785 0.2978 0.2961 -0.0127 0.0172  -0.0303 209 ALA   B CB  
3367 N  N   . GLU   B 210 ? 0.2501 0.2659 0.2717 -0.0119 0.0175  -0.0313 210 GLU   B N   
3368 C  CA  . GLU   B 210 ? 0.2521 0.2707 0.2758 -0.0119 0.0176  -0.0341 210 GLU   B CA  
3369 C  C   . GLU   B 210 ? 0.2434 0.2600 0.2643 -0.0096 0.0156  -0.0310 210 GLU   B C   
3370 O  O   . GLU   B 210 ? 0.2335 0.2546 0.2531 -0.0088 0.0144  -0.0322 210 GLU   B O   
3371 C  CB  . GLU   B 210 ? 0.2944 0.3100 0.3238 -0.0140 0.0203  -0.0368 210 GLU   B CB  
3372 C  CG  . GLU   B 210 ? 0.3431 0.3618 0.3760 -0.0167 0.0226  -0.0411 210 GLU   B CG  
3373 C  CD  . GLU   B 210 ? 0.4016 0.4162 0.4343 -0.0181 0.0240  -0.0394 210 GLU   B CD  
3374 O  OE1 . GLU   B 210 ? 0.3620 0.3713 0.3916 -0.0169 0.0232  -0.0346 210 GLU   B OE1 
3375 O  OE2 . GLU   B 210 ? 0.4696 0.4872 0.5056 -0.0206 0.0262  -0.0435 210 GLU   B OE2 
3376 N  N   . ASP   B 211 ? 0.2232 0.2333 0.2431 -0.0088 0.0154  -0.0270 211 ASP   B N   
3377 C  CA  . ASP   B 211 ? 0.2261 0.2343 0.2432 -0.0067 0.0136  -0.0241 211 ASP   B CA  
3378 C  C   . ASP   B 211 ? 0.2162 0.2281 0.2286 -0.0053 0.0114  -0.0227 211 ASP   B C   
3379 O  O   . ASP   B 211 ? 0.1958 0.2098 0.2064 -0.0043 0.0102  -0.0226 211 ASP   B O   
3380 C  CB  . ASP   B 211 ? 0.2375 0.2390 0.2538 -0.0059 0.0135  -0.0200 211 ASP   B CB  
3381 C  CG  . ASP   B 211 ? 0.2654 0.2619 0.2860 -0.0067 0.0155  -0.0203 211 ASP   B CG  
3382 O  OD1 . ASP   B 211 ? 0.2839 0.2816 0.3083 -0.0074 0.0165  -0.0235 211 ASP   B OD1 
3383 O  OD2 . ASP   B 211 ? 0.2600 0.2516 0.2801 -0.0066 0.0159  -0.0172 211 ASP   B OD2 
3384 N  N   . ALA   B 212 ? 0.1968 0.2093 0.2070 -0.0052 0.0110  -0.0216 212 ALA   B N   
3385 C  CA  . ALA   B 212 ? 0.1852 0.2005 0.1911 -0.0036 0.0090  -0.0202 212 ALA   B CA  
3386 C  C   . ALA   B 212 ? 0.1918 0.2136 0.1973 -0.0033 0.0084  -0.0229 212 ALA   B C   
3387 O  O   . ALA   B 212 ? 0.1896 0.2125 0.1919 -0.0018 0.0069  -0.0214 212 ALA   B O   
3388 C  CB  . ALA   B 212 ? 0.1858 0.2012 0.1902 -0.0035 0.0088  -0.0192 212 ALA   B CB  
3389 N  N   . GLN   B 213 ? 0.1932 0.2191 0.2019 -0.0048 0.0096  -0.0268 213 GLN   B N   
3390 C  CA  . GLN   B 213 ? 0.2154 0.2483 0.2239 -0.0046 0.0091  -0.0297 213 GLN   B CA  
3391 C  C   . GLN   B 213 ? 0.2054 0.2384 0.2135 -0.0043 0.0087  -0.0295 213 GLN   B C   
3392 O  O   . GLN   B 213 ? 0.2209 0.2580 0.2261 -0.0032 0.0074  -0.0293 213 GLN   B O   
3393 C  CB  . GLN   B 213 ? 0.2401 0.2772 0.2530 -0.0068 0.0109  -0.0344 213 GLN   B CB  
3394 C  CG  . GLN   B 213 ? 0.3001 0.3459 0.3132 -0.0068 0.0105  -0.0380 213 GLN   B CG  
3395 C  CD  . GLN   B 213 ? 0.3889 0.4391 0.4066 -0.0092 0.0125  -0.0431 213 GLN   B CD  
3396 O  OE1 . GLN   B 213 ? 0.4035 0.4505 0.4257 -0.0112 0.0147  -0.0450 213 GLN   B OE1 
3397 N  NE2 . GLN   B 213 ? 0.4121 0.4695 0.4291 -0.0088 0.0118  -0.0453 213 GLN   B NE2 
3398 N  N   . LYS   B 214 ? 0.2061 0.2347 0.2171 -0.0051 0.0099  -0.0296 214 LYS   B N   
3399 C  CA  . LYS   B 214 ? 0.2346 0.2634 0.2458 -0.0049 0.0097  -0.0299 214 LYS   B CA  
3400 C  C   . LYS   B 214 ? 0.2114 0.2384 0.2178 -0.0031 0.0079  -0.0260 214 LYS   B C   
3401 O  O   . LYS   B 214 ? 0.2026 0.2327 0.2068 -0.0027 0.0071  -0.0261 214 LYS   B O   
3402 C  CB  . LYS   B 214 ? 0.2684 0.2924 0.2840 -0.0059 0.0113  -0.0306 214 LYS   B CB  
3403 C  CG  . LYS   B 214 ? 0.3390 0.3634 0.3555 -0.0057 0.0112  -0.0314 214 LYS   B CG  
3404 C  CD  . LYS   B 214 ? 0.4498 0.4706 0.4717 -0.0065 0.0129  -0.0331 214 LYS   B CD  
3405 C  CE  . LYS   B 214 ? 0.5626 0.5880 0.5871 -0.0073 0.0134  -0.0369 214 LYS   B CE  
3406 N  NZ  . LYS   B 214 ? 0.6121 0.6336 0.6416 -0.0075 0.0148  -0.0382 214 LYS   B NZ  
3407 N  N   . TYR   B 215 ? 0.1989 0.2207 0.2034 -0.0022 0.0074  -0.0225 215 TYR   B N   
3408 C  CA  . TYR   B 215 ? 0.1869 0.2066 0.1873 -0.0008 0.0059  -0.0191 215 TYR   B CA  
3409 C  C   . TYR   B 215 ? 0.1666 0.1901 0.1630 0.0003  0.0046  -0.0185 215 TYR   B C   
3410 O  O   . TYR   B 215 ? 0.1848 0.2086 0.1781 0.0011  0.0038  -0.0170 215 TYR   B O   
3411 C  CB  . TYR   B 215 ? 0.1976 0.2117 0.1970 -0.0002 0.0057  -0.0159 215 TYR   B CB  
3412 C  CG  . TYR   B 215 ? 0.2103 0.2201 0.2122 -0.0004 0.0064  -0.0153 215 TYR   B CG  
3413 C  CD1 . TYR   B 215 ? 0.1892 0.1973 0.1900 0.0003  0.0058  -0.0138 215 TYR   B CD1 
3414 C  CD2 . TYR   B 215 ? 0.2422 0.2494 0.2476 -0.0013 0.0077  -0.0159 215 TYR   B CD2 
3415 C  CE1 . TYR   B 215 ? 0.1862 0.1909 0.1893 0.0004  0.0063  -0.0132 215 TYR   B CE1 
3416 C  CE2 . TYR   B 215 ? 0.2594 0.2624 0.2670 -0.0010 0.0082  -0.0148 215 TYR   B CE2 
3417 C  CZ  . TYR   B 215 ? 0.2323 0.2344 0.2388 -0.0001 0.0074  -0.0135 215 TYR   B CZ  
3418 O  OH  . TYR   B 215 ? 0.2102 0.2087 0.2189 0.0005  0.0077  -0.0125 215 TYR   B OH  
3419 N  N   . LEU   B 216 ? 0.1632 0.1897 0.1597 0.0004  0.0045  -0.0195 216 LEU   B N   
3420 C  CA  . LEU   B 216 ? 0.1695 0.1999 0.1624 0.0018  0.0031  -0.0190 216 LEU   B CA  
3421 C  C   . LEU   B 216 ? 0.1816 0.2178 0.1742 0.0016  0.0030  -0.0211 216 LEU   B C   
3422 O  O   . LEU   B 216 ? 0.1969 0.2349 0.1856 0.0029  0.0019  -0.0194 216 LEU   B O   
3423 C  CB  . LEU   B 216 ? 0.1993 0.2325 0.1928 0.0021  0.0030  -0.0201 216 LEU   B CB  
3424 C  CG  . LEU   B 216 ? 0.2149 0.2436 0.2071 0.0030  0.0025  -0.0174 216 LEU   B CG  
3425 C  CD1 . LEU   B 216 ? 0.2416 0.2729 0.2354 0.0026  0.0029  -0.0193 216 LEU   B CD1 
3426 C  CD2 . LEU   B 216 ? 0.2189 0.2463 0.2067 0.0050  0.0009  -0.0143 216 LEU   B CD2 
3427 N  N   . ALA   B 217 ? 0.1768 0.2160 0.1734 -0.0002 0.0044  -0.0248 217 ALA   B N   
3428 C  CA  . ALA   B 217 ? 0.1891 0.2345 0.1856 -0.0007 0.0044  -0.0273 217 ALA   B CA  
3429 C  C   . ALA   B 217 ? 0.1966 0.2404 0.1904 -0.0003 0.0040  -0.0252 217 ALA   B C   
3430 O  O   . ALA   B 217 ? 0.1927 0.2411 0.1837 0.0001  0.0033  -0.0252 217 ALA   B O   
3431 C  CB  . ALA   B 217 ? 0.1900 0.2382 0.1920 -0.0028 0.0062  -0.0319 217 ALA   B CB  
3432 N  N   . ILE   B 218 ? 0.1941 0.2317 0.1886 -0.0006 0.0044  -0.0234 218 ILE   B N   
3433 C  CA  . ILE   B 218 ? 0.1940 0.2301 0.1861 -0.0005 0.0041  -0.0217 218 ILE   B CA  
3434 C  C   . ILE   B 218 ? 0.1958 0.2314 0.1822 0.0011  0.0027  -0.0181 218 ILE   B C   
3435 O  O   . ILE   B 218 ? 0.2078 0.2459 0.1913 0.0011  0.0025  -0.0175 218 ILE   B O   
3436 C  CB  . ILE   B 218 ? 0.2117 0.2416 0.2058 -0.0008 0.0046  -0.0205 218 ILE   B CB  
3437 C  CG1 . ILE   B 218 ? 0.2228 0.2528 0.2226 -0.0021 0.0061  -0.0238 218 ILE   B CG1 
3438 C  CG2 . ILE   B 218 ? 0.2113 0.2397 0.2026 -0.0007 0.0043  -0.0186 218 ILE   B CG2 
3439 C  CD1 . ILE   B 218 ? 0.2367 0.2605 0.2388 -0.0019 0.0065  -0.0225 218 ILE   B CD1 
3440 N  N   . ALA   B 219 ? 0.1818 0.2140 0.1667 0.0024  0.0020  -0.0158 219 ALA   B N   
3441 C  CA  . ALA   B 219 ? 0.1935 0.2246 0.1736 0.0041  0.0008  -0.0125 219 ALA   B CA  
3442 C  C   . ALA   B 219 ? 0.2042 0.2417 0.1821 0.0050  0.0001  -0.0132 219 ALA   B C   
3443 O  O   . ALA   B 219 ? 0.2093 0.2472 0.1830 0.0058  -0.0005 -0.0109 219 ALA   B O   
3444 C  CB  . ALA   B 219 ? 0.1953 0.2224 0.1752 0.0052  0.0003  -0.0107 219 ALA   B CB  
3445 N  N   . ASP   B 220 ? 0.1905 0.2329 0.1710 0.0048  0.0001  -0.0162 220 ASP   B N   
3446 C  CA  . ASP   B 220 ? 0.2206 0.2702 0.1993 0.0058  -0.0007 -0.0172 220 ASP   B CA  
3447 C  C   . ASP   B 220 ? 0.2266 0.2806 0.2038 0.0049  -0.0004 -0.0180 220 ASP   B C   
3448 O  O   . ASP   B 220 ? 0.2294 0.2866 0.2023 0.0062  -0.0014 -0.0162 220 ASP   B O   
3449 C  CB  . ASP   B 220 ? 0.2209 0.2755 0.2033 0.0053  -0.0004 -0.0210 220 ASP   B CB  
3450 C  CG  . ASP   B 220 ? 0.2432 0.2952 0.2264 0.0063  -0.0008 -0.0203 220 ASP   B CG  
3451 O  OD1 . ASP   B 220 ? 0.2613 0.3081 0.2419 0.0078  -0.0016 -0.0167 220 ASP   B OD1 
3452 O  OD2 . ASP   B 220 ? 0.2715 0.3269 0.2584 0.0053  -0.0002 -0.0236 220 ASP   B OD2 
3453 N  N   . GLU   B 221 ? 0.2354 0.2894 0.2159 0.0027  0.0009  -0.0206 221 GLU   B N   
3454 C  CA  . GLU   B 221 ? 0.2499 0.3084 0.2296 0.0015  0.0014  -0.0220 221 GLU   B CA  
3455 C  C   . GLU   B 221 ? 0.2514 0.3061 0.2264 0.0019  0.0011  -0.0180 221 GLU   B C   
3456 O  O   . GLU   B 221 ? 0.2554 0.3144 0.2271 0.0018  0.0009  -0.0175 221 GLU   B O   
3457 C  CB  . GLU   B 221 ? 0.2805 0.3395 0.2657 -0.0008 0.0030  -0.0260 221 GLU   B CB  
3458 C  CG  . GLU   B 221 ? 0.3818 0.4454 0.3717 -0.0016 0.0037  -0.0303 221 GLU   B CG  
3459 C  CD  . GLU   B 221 ? 0.5364 0.5979 0.5326 -0.0035 0.0054  -0.0338 221 GLU   B CD  
3460 O  OE1 . GLU   B 221 ? 0.6879 0.7445 0.6854 -0.0040 0.0060  -0.0330 221 GLU   B OE1 
3461 O  OE2 . GLU   B 221 ? 0.6209 0.6856 0.6210 -0.0043 0.0062  -0.0373 221 GLU   B OE2 
3462 N  N   . LEU   B 222 ? 0.2055 0.2524 0.1800 0.0022  0.0012  -0.0153 222 LEU   B N   
3463 C  CA  . LEU   B 222 ? 0.2156 0.2588 0.1860 0.0022  0.0012  -0.0120 222 LEU   B CA  
3464 C  C   . LEU   B 222 ? 0.2238 0.2660 0.1889 0.0044  0.0000  -0.0081 222 LEU   B C   
3465 O  O   . LEU   B 222 ? 0.2513 0.2933 0.2122 0.0043  0.0002  -0.0059 222 LEU   B O   
3466 C  CB  . LEU   B 222 ? 0.2027 0.2387 0.1749 0.0017  0.0018  -0.0109 222 LEU   B CB  
3467 C  CG  . LEU   B 222 ? 0.2395 0.2759 0.2160 -0.0002 0.0030  -0.0140 222 LEU   B CG  
3468 C  CD1 . LEU   B 222 ? 0.2303 0.2601 0.2085 -0.0001 0.0032  -0.0127 222 LEU   B CD1 
3469 C  CD2 . LEU   B 222 ? 0.2658 0.3052 0.2407 -0.0016 0.0037  -0.0147 222 LEU   B CD2 
3470 N  N   . PHE   B 223 ? 0.2175 0.2582 0.1826 0.0063  -0.0009 -0.0070 223 PHE   B N   
3471 C  CA  . PHE   B 223 ? 0.2309 0.2685 0.1915 0.0085  -0.0020 -0.0031 223 PHE   B CA  
3472 C  C   . PHE   B 223 ? 0.2576 0.3005 0.2169 0.0108  -0.0033 -0.0031 223 PHE   B C   
3473 O  O   . PHE   B 223 ? 0.2897 0.3305 0.2455 0.0131  -0.0044 0.0001  223 PHE   B O   
3474 C  CB  . PHE   B 223 ? 0.2242 0.2546 0.1857 0.0091  -0.0020 -0.0014 223 PHE   B CB  
3475 C  CG  . PHE   B 223 ? 0.2305 0.2556 0.1929 0.0073  -0.0008 -0.0009 223 PHE   B CG  
3476 C  CD1 . PHE   B 223 ? 0.2399 0.2628 0.1987 0.0066  -0.0002 0.0012  223 PHE   B CD1 
3477 C  CD2 . PHE   B 223 ? 0.2188 0.2418 0.1854 0.0063  -0.0003 -0.0027 223 PHE   B CD2 
3478 C  CE1 . PHE   B 223 ? 0.2565 0.2755 0.2164 0.0049  0.0009  0.0012  223 PHE   B CE1 
3479 C  CE2 . PHE   B 223 ? 0.2336 0.2526 0.2010 0.0049  0.0006  -0.0024 223 PHE   B CE2 
3480 C  CZ  . PHE   B 223 ? 0.2232 0.2407 0.1874 0.0042  0.0012  -0.0007 223 PHE   B CZ  
3481 N  N   . GLY   B 224 ? 0.2612 0.3106 0.2240 0.0102  -0.0034 -0.0071 224 GLY   B N   
3482 C  CA  . GLY   B 224 ? 0.2733 0.3284 0.2360 0.0122  -0.0046 -0.0080 224 GLY   B CA  
3483 C  C   . GLY   B 224 ? 0.2893 0.3419 0.2553 0.0127  -0.0048 -0.0091 224 GLY   B C   
3484 O  O   . GLY   B 224 ? 0.2750 0.3205 0.2417 0.0125  -0.0044 -0.0075 224 GLY   B O   
3485 N  N   . ALA   B 225 ? 0.3123 0.3713 0.2802 0.0135  -0.0055 -0.0117 225 ALA   B N   
3486 C  CA  . ALA   B 225 ? 0.3070 0.3653 0.2787 0.0133  -0.0052 -0.0139 225 ALA   B CA  
3487 C  C   . ALA   B 225 ? 0.2862 0.3396 0.2562 0.0156  -0.0063 -0.0109 225 ALA   B C   
3488 O  O   . ALA   B 225 ? 0.3067 0.3581 0.2797 0.0152  -0.0059 -0.0120 225 ALA   B O   
3489 C  CB  . ALA   B 225 ? 0.3216 0.3891 0.2959 0.0132  -0.0054 -0.0181 225 ALA   B CB  
3490 N  N   . ASP   B 226 ? 0.2730 0.3245 0.2385 0.0181  -0.0074 -0.0071 226 ASP   B N   
3491 C  CA  . ASP   B 226 ? 0.3118 0.3584 0.2759 0.0204  -0.0083 -0.0044 226 ASP   B CA  
3492 C  C   . ASP   B 226 ? 0.2905 0.3280 0.2541 0.0194  -0.0074 -0.0018 226 ASP   B C   
3493 O  O   . ASP   B 226 ? 0.2921 0.3253 0.2554 0.0208  -0.0078 -0.0002 226 ASP   B O   
3494 C  CB  . ASP   B 226 ? 0.3825 0.4310 0.3424 0.0239  -0.0100 -0.0014 226 ASP   B CB  
3495 C  CG  . ASP   B 226 ? 0.5092 0.5671 0.4696 0.0257  -0.0113 -0.0038 226 ASP   B CG  
3496 O  OD1 . ASP   B 226 ? 0.5333 0.5946 0.4977 0.0250  -0.0112 -0.0074 226 ASP   B OD1 
3497 O  OD2 . ASP   B 226 ? 0.6349 0.6969 0.5918 0.0277  -0.0124 -0.0022 226 ASP   B OD2 
3498 N  N   . TRP   B 227 ? 0.2490 0.2842 0.2127 0.0171  -0.0062 -0.0017 227 TRP   B N   
3499 C  CA  . TRP   B 227 ? 0.2325 0.2599 0.1952 0.0162  -0.0054 0.0007  227 TRP   B CA  
3500 C  C   . TRP   B 227 ? 0.2194 0.2431 0.1854 0.0154  -0.0049 -0.0003 227 TRP   B C   
3501 O  O   . TRP   B 227 ? 0.2046 0.2229 0.1696 0.0161  -0.0049 0.0018  227 TRP   B O   
3502 C  CB  . TRP   B 227 ? 0.2140 0.2408 0.1764 0.0139  -0.0042 0.0005  227 TRP   B CB  
3503 C  CG  . TRP   B 227 ? 0.2123 0.2320 0.1737 0.0130  -0.0034 0.0026  227 TRP   B CG  
3504 C  CD1 . TRP   B 227 ? 0.2008 0.2159 0.1586 0.0138  -0.0034 0.0059  227 TRP   B CD1 
3505 C  CD2 . TRP   B 227 ? 0.2051 0.2218 0.1697 0.0110  -0.0024 0.0014  227 TRP   B CD2 
3506 N  NE1 . TRP   B 227 ? 0.2052 0.2152 0.1638 0.0122  -0.0023 0.0064  227 TRP   B NE1 
3507 C  CE2 . TRP   B 227 ? 0.1912 0.2022 0.1538 0.0107  -0.0018 0.0037  227 TRP   B CE2 
3508 C  CE3 . TRP   B 227 ? 0.1945 0.2125 0.1632 0.0095  -0.0018 -0.0014 227 TRP   B CE3 
3509 C  CZ2 . TRP   B 227 ? 0.1913 0.1990 0.1560 0.0091  -0.0010 0.0032  227 TRP   B CZ2 
3510 C  CZ3 . TRP   B 227 ? 0.1897 0.2038 0.1602 0.0081  -0.0010 -0.0015 227 TRP   B CZ3 
3511 C  CH2 . TRP   B 227 ? 0.1975 0.2070 0.1660 0.0080  -0.0007 0.0007  227 TRP   B CH2 
3512 N  N   . ALA   B 228 ? 0.2236 0.2501 0.1933 0.0139  -0.0043 -0.0034 228 ALA   B N   
3513 C  CA  . ALA   B 228 ? 0.2056 0.2285 0.1782 0.0126  -0.0036 -0.0041 228 ALA   B CA  
3514 C  C   . ALA   B 228 ? 0.2174 0.2405 0.1908 0.0140  -0.0042 -0.0042 228 ALA   B C   
3515 O  O   . ALA   B 228 ? 0.2368 0.2624 0.2131 0.0131  -0.0039 -0.0066 228 ALA   B O   
3516 C  CB  . ALA   B 228 ? 0.2057 0.2309 0.1821 0.0103  -0.0025 -0.0070 228 ALA   B CB  
3517 N  N   . ASP   B 229 ? 0.2013 0.2216 0.1722 0.0160  -0.0051 -0.0018 229 ASP   B N   
3518 C  CA  . ASP   B 229 ? 0.1966 0.2159 0.1685 0.0172  -0.0055 -0.0019 229 ASP   B CA  
3519 C  C   . ASP   B 229 ? 0.1880 0.2019 0.1607 0.0157  -0.0046 -0.0011 229 ASP   B C   
3520 O  O   . ASP   B 229 ? 0.1692 0.1805 0.1420 0.0140  -0.0038 -0.0005 229 ASP   B O   
3521 C  CB  . ASP   B 229 ? 0.2218 0.2407 0.1909 0.0202  -0.0068 0.0000  229 ASP   B CB  
3522 C  CG  . ASP   B 229 ? 0.2454 0.2585 0.2115 0.0208  -0.0066 0.0033  229 ASP   B CG  
3523 O  OD1 . ASP   B 229 ? 0.2241 0.2332 0.1902 0.0188  -0.0055 0.0039  229 ASP   B OD1 
3524 O  OD2 . ASP   B 229 ? 0.2702 0.2828 0.2337 0.0233  -0.0075 0.0052  229 ASP   B OD2 
3525 N  N   . ALA   B 230 ? 0.1891 0.2019 0.1626 0.0165  -0.0048 -0.0011 230 ALA   B N   
3526 C  CA  . ALA   B 230 ? 0.1854 0.1945 0.1600 0.0151  -0.0040 -0.0008 230 ALA   B CA  
3527 C  C   . ALA   B 230 ? 0.1708 0.1748 0.1433 0.0151  -0.0038 0.0015  230 ALA   B C   
3528 O  O   . ALA   B 230 ? 0.1696 0.1711 0.1429 0.0136  -0.0030 0.0017  230 ALA   B O   
3529 C  CB  . ALA   B 230 ? 0.1888 0.1989 0.1648 0.0157  -0.0043 -0.0018 230 ALA   B CB  
3530 N  N   . ARG   B 231 ? 0.1654 0.1680 0.1354 0.0167  -0.0043 0.0031  231 ARG   B N   
3531 C  CA  . ARG   B 231 ? 0.1711 0.1689 0.1393 0.0162  -0.0036 0.0050  231 ARG   B CA  
3532 C  C   . ARG   B 231 ? 0.1747 0.1724 0.1424 0.0144  -0.0029 0.0052  231 ARG   B C   
3533 O  O   . ARG   B 231 ? 0.1812 0.1755 0.1479 0.0134  -0.0022 0.0062  231 ARG   B O   
3534 C  CB  . ARG   B 231 ? 0.1842 0.1799 0.1498 0.0186  -0.0042 0.0070  231 ARG   B CB  
3535 C  CG  . ARG   B 231 ? 0.1894 0.1798 0.1528 0.0180  -0.0033 0.0090  231 ARG   B CG  
3536 C  CD  . ARG   B 231 ? 0.1972 0.1842 0.1620 0.0167  -0.0024 0.0086  231 ARG   B CD  
3537 N  NE  . ARG   B 231 ? 0.2040 0.1864 0.1670 0.0157  -0.0013 0.0100  231 ARG   B NE  
3538 C  CZ  . ARG   B 231 ? 0.1920 0.1739 0.1545 0.0136  -0.0004 0.0101  231 ARG   B CZ  
3539 N  NH1 . ARG   B 231 ? 0.1901 0.1755 0.1539 0.0123  -0.0005 0.0088  231 ARG   B NH1 
3540 N  NH2 . ARG   B 231 ? 0.2023 0.1802 0.1633 0.0127  0.0008  0.0112  231 ARG   B NH2 
3541 N  N   . HIS   B 232 ? 0.1666 0.1684 0.1352 0.0139  -0.0031 0.0038  232 HIS   B N   
3542 C  CA  . HIS   B 232 ? 0.1663 0.1687 0.1346 0.0123  -0.0024 0.0037  232 HIS   B CA  
3543 C  C   . HIS   B 232 ? 0.1579 0.1621 0.1294 0.0105  -0.0018 0.0016  232 HIS   B C   
3544 O  O   . HIS   B 232 ? 0.1520 0.1564 0.1238 0.0092  -0.0012 0.0012  232 HIS   B O   
3545 C  CB  . HIS   B 232 ? 0.1782 0.1836 0.1442 0.0132  -0.0029 0.0041  232 HIS   B CB  
3546 C  CG  . HIS   B 232 ? 0.1963 0.1984 0.1588 0.0148  -0.0032 0.0068  232 HIS   B CG  
3547 N  ND1 . HIS   B 232 ? 0.2144 0.2164 0.1760 0.0173  -0.0042 0.0077  232 HIS   B ND1 
3548 C  CD2 . HIS   B 232 ? 0.2017 0.2004 0.1617 0.0142  -0.0025 0.0087  232 HIS   B CD2 
3549 C  CE1 . HIS   B 232 ? 0.2325 0.2305 0.1910 0.0183  -0.0040 0.0104  232 HIS   B CE1 
3550 N  NE2 . HIS   B 232 ? 0.2266 0.2225 0.1840 0.0163  -0.0029 0.0110  232 HIS   B NE2 
3551 N  N   . TYR   B 233 ? 0.1462 0.1519 0.1200 0.0104  -0.0019 0.0002  233 TYR   B N   
3552 C  CA  . TYR   B 233 ? 0.1458 0.1528 0.1226 0.0088  -0.0012 -0.0015 233 TYR   B CA  
3553 C  C   . TYR   B 233 ? 0.1473 0.1534 0.1259 0.0085  -0.0010 -0.0018 233 TYR   B C   
3554 O  O   . TYR   B 233 ? 0.1581 0.1655 0.1366 0.0094  -0.0015 -0.0021 233 TYR   B O   
3555 C  CB  . TYR   B 233 ? 0.1538 0.1656 0.1318 0.0086  -0.0012 -0.0036 233 TYR   B CB  
3556 C  CG  . TYR   B 233 ? 0.1673 0.1800 0.1481 0.0069  -0.0002 -0.0054 233 TYR   B CG  
3557 C  CD1 . TYR   B 233 ? 0.1907 0.2025 0.1745 0.0058  0.0006  -0.0065 233 TYR   B CD1 
3558 C  CD2 . TYR   B 233 ? 0.1888 0.2028 0.1693 0.0063  0.0001  -0.0060 233 TYR   B CD2 
3559 C  CE1 . TYR   B 233 ? 0.2062 0.2181 0.1929 0.0044  0.0016  -0.0079 233 TYR   B CE1 
3560 C  CE2 . TYR   B 233 ? 0.2071 0.2218 0.1907 0.0048  0.0010  -0.0079 233 TYR   B CE2 
3561 C  CZ  . TYR   B 233 ? 0.2251 0.2385 0.2119 0.0040  0.0018  -0.0088 233 TYR   B CZ  
3562 O  OH  . TYR   B 233 ? 0.2556 0.2691 0.2456 0.0027  0.0028  -0.0106 233 TYR   B OH  
3563 N  N   . ARG   B 234 ? 0.1331 0.1373 0.1134 0.0072  -0.0003 -0.0018 234 ARG   B N   
3564 C  CA  . ARG   B 234 ? 0.1300 0.1336 0.1120 0.0066  0.0001  -0.0019 234 ARG   B CA  
3565 C  C   . ARG   B 234 ? 0.1347 0.1378 0.1193 0.0052  0.0011  -0.0026 234 ARG   B C   
3566 O  O   . ARG   B 234 ? 0.1294 0.1318 0.1146 0.0049  0.0013  -0.0027 234 ARG   B O   
3567 C  CB  . ARG   B 234 ? 0.1347 0.1355 0.1156 0.0069  0.0000  -0.0003 234 ARG   B CB  
3568 C  CG  . ARG   B 234 ? 0.1417 0.1422 0.1205 0.0082  -0.0007 0.0004  234 ARG   B CG  
3569 C  CD  . ARG   B 234 ? 0.1380 0.1407 0.1172 0.0089  -0.0011 -0.0005 234 ARG   B CD  
3570 N  NE  . ARG   B 234 ? 0.1437 0.1455 0.1210 0.0105  -0.0018 0.0002  234 ARG   B NE  
3571 C  CZ  . ARG   B 234 ? 0.1709 0.1702 0.1475 0.0107  -0.0017 0.0011  234 ARG   B CZ  
3572 N  NH1 . ARG   B 234 ? 0.1683 0.1670 0.1458 0.0095  -0.0012 0.0011  234 ARG   B NH1 
3573 N  NH2 . ARG   B 234 ? 0.1745 0.1721 0.1496 0.0121  -0.0021 0.0018  234 ARG   B NH2 
3574 N  N   . PHE   B 235 ? 0.1487 0.1519 0.1349 0.0045  0.0017  -0.0031 235 PHE   B N   
3575 C  CA  . PHE   B 235 ? 0.1550 0.1568 0.1437 0.0033  0.0027  -0.0032 235 PHE   B CA  
3576 C  C   . PHE   B 235 ? 0.1700 0.1697 0.1585 0.0030  0.0030  -0.0015 235 PHE   B C   
3577 O  O   . PHE   B 235 ? 0.1606 0.1612 0.1480 0.0031  0.0027  -0.0013 235 PHE   B O   
3578 C  CB  . PHE   B 235 ? 0.1613 0.1653 0.1524 0.0022  0.0037  -0.0055 235 PHE   B CB  
3579 C  CG  . PHE   B 235 ? 0.1815 0.1884 0.1737 0.0020  0.0038  -0.0079 235 PHE   B CG  
3580 C  CD1 . PHE   B 235 ? 0.2125 0.2185 0.2070 0.0013  0.0046  -0.0087 235 PHE   B CD1 
3581 C  CD2 . PHE   B 235 ? 0.1888 0.1998 0.1800 0.0027  0.0031  -0.0092 235 PHE   B CD2 
3582 C  CE1 . PHE   B 235 ? 0.2156 0.2251 0.2115 0.0009  0.0049  -0.0113 235 PHE   B CE1 
3583 C  CE2 . PHE   B 235 ? 0.2129 0.2274 0.2051 0.0025  0.0033  -0.0115 235 PHE   B CE2 
3584 C  CZ  . PHE   B 235 ? 0.2017 0.2156 0.1962 0.0014  0.0042  -0.0126 235 PHE   B CZ  
3585 N  N   . SER   B 236 ? 0.1947 0.1919 0.1843 0.0027  0.0034  -0.0003 236 SER   B N   
3586 C  CA  . SER   B 236 ? 0.2145 0.2100 0.2041 0.0022  0.0039  0.0014  236 SER   B CA  
3587 C  C   . SER   B 236 ? 0.2086 0.2016 0.2006 0.0017  0.0049  0.0019  236 SER   B C   
3588 O  O   . SER   B 236 ? 0.1991 0.1911 0.1921 0.0023  0.0047  0.0018  236 SER   B O   
3589 C  CB  . SER   B 236 ? 0.2708 0.2659 0.2582 0.0030  0.0030  0.0032  236 SER   B CB  
3590 O  OG  . SER   B 236 ? 0.3826 0.3763 0.3702 0.0037  0.0027  0.0041  236 SER   B OG  
3591 N  N   . ALA   B 237 ? 0.2167 0.2087 0.2098 0.0006  0.0061  0.0022  237 ALA   B N   
3592 C  CA  . ALA   B 237 ? 0.2412 0.2301 0.2366 0.0002  0.0072  0.0031  237 ALA   B CA  
3593 C  C   . ALA   B 237 ? 0.2710 0.2586 0.2665 -0.0012 0.0085  0.0041  237 ALA   B C   
3594 O  O   . ALA   B 237 ? 0.2373 0.2270 0.2327 -0.0024 0.0091  0.0025  237 ALA   B O   
3595 C  CB  . ALA   B 237 ? 0.2617 0.2506 0.2602 -0.0003 0.0080  0.0006  237 ALA   B CB  
3596 N  N   . SER   B 238 ? 0.2831 0.2675 0.2787 -0.0010 0.0090  0.0069  238 SER   B N   
3597 C  CA  . SER   B 238 ? 0.3205 0.3032 0.3160 -0.0025 0.0105  0.0082  238 SER   B CA  
3598 C  C   . SER   B 238 ? 0.3020 0.2837 0.3008 -0.0043 0.0125  0.0057  238 SER   B C   
3599 O  O   . SER   B 238 ? 0.3030 0.2832 0.3046 -0.0041 0.0130  0.0043  238 SER   B O   
3600 C  CB  . SER   B 238 ? 0.4030 0.3823 0.3978 -0.0016 0.0106  0.0120  238 SER   B CB  
3601 O  OG  . SER   B 238 ? 0.4821 0.4581 0.4797 -0.0008 0.0110  0.0120  238 SER   B OG  
3602 N  N   . GLY   B 239 ? 0.2776 0.2606 0.2761 -0.0062 0.0137  0.0047  239 GLY   B N   
3603 C  CA  . GLY   B 239 ? 0.2747 0.2572 0.2764 -0.0084 0.0159  0.0021  239 GLY   B CA  
3604 C  C   . GLY   B 239 ? 0.2591 0.2464 0.2620 -0.0087 0.0155  -0.0022 239 GLY   B C   
3605 O  O   . GLY   B 239 ? 0.2493 0.2379 0.2546 -0.0107 0.0172  -0.0051 239 GLY   B O   
3606 N  N   . LEU   B 240 ? 0.2243 0.2144 0.2257 -0.0068 0.0134  -0.0027 240 LEU   B N   
3607 C  CA  . LEU   B 240 ? 0.1992 0.1938 0.2017 -0.0068 0.0129  -0.0064 240 LEU   B CA  
3608 C  C   . LEU   B 240 ? 0.1945 0.1934 0.1965 -0.0079 0.0132  -0.0085 240 LEU   B C   
3609 O  O   . LEU   B 240 ? 0.1959 0.1981 0.2000 -0.0089 0.0140  -0.0119 240 LEU   B O   
3610 C  CB  . LEU   B 240 ? 0.2039 0.2000 0.2046 -0.0046 0.0108  -0.0060 240 LEU   B CB  
3611 C  CG  . LEU   B 240 ? 0.1996 0.2006 0.2007 -0.0043 0.0101  -0.0092 240 LEU   B CG  
3612 C  CD1 . LEU   B 240 ? 0.2175 0.2192 0.2222 -0.0056 0.0116  -0.0123 240 LEU   B CD1 
3613 C  CD2 . LEU   B 240 ? 0.2139 0.2157 0.2127 -0.0023 0.0081  -0.0082 240 LEU   B CD2 
3614 N  N   . LEU   B 241 ? 0.1914 0.1910 0.1907 -0.0075 0.0125  -0.0067 241 LEU   B N   
3615 C  CA  . LEU   B 241 ? 0.1968 0.2010 0.1957 -0.0082 0.0125  -0.0090 241 LEU   B CA  
3616 C  C   . LEU   B 241 ? 0.2100 0.2147 0.2116 -0.0110 0.0150  -0.0113 241 LEU   B C   
3617 O  O   . LEU   B 241 ? 0.2030 0.2124 0.2062 -0.0117 0.0153  -0.0149 241 LEU   B O   
3618 C  CB  . LEU   B 241 ? 0.2023 0.2069 0.1983 -0.0075 0.0116  -0.0069 241 LEU   B CB  
3619 C  CG  . LEU   B 241 ? 0.2248 0.2344 0.2207 -0.0081 0.0116  -0.0093 241 LEU   B CG  
3620 C  CD1 . LEU   B 241 ? 0.2248 0.2390 0.2212 -0.0067 0.0103  -0.0122 241 LEU   B CD1 
3621 C  CD2 . LEU   B 241 ? 0.2484 0.2586 0.2417 -0.0075 0.0107  -0.0076 241 LEU   B CD2 
3622 N  N   . ALA   B 242 ? 0.2410 0.2409 0.2431 -0.0125 0.0168  -0.0091 242 ALA   B N   
3623 C  CA  . ALA   B 242 ? 0.2667 0.2659 0.2715 -0.0155 0.0196  -0.0109 242 ALA   B CA  
3624 C  C   . ALA   B 242 ? 0.2630 0.2636 0.2715 -0.0163 0.0205  -0.0147 242 ALA   B C   
3625 O  O   . ALA   B 242 ? 0.2630 0.2672 0.2738 -0.0184 0.0221  -0.0184 242 ALA   B O   
3626 C  CB  . ALA   B 242 ? 0.2817 0.2745 0.2861 -0.0166 0.0212  -0.0072 242 ALA   B CB  
3627 N  N   . SER   B 243 ? 0.2548 0.2535 0.2641 -0.0147 0.0196  -0.0142 243 SER   B N   
3628 C  CA  . SER   B 243 ? 0.2526 0.2532 0.2655 -0.0154 0.0205  -0.0181 243 SER   B CA  
3629 C  C   . SER   B 243 ? 0.2338 0.2422 0.2467 -0.0149 0.0193  -0.0219 243 SER   B C   
3630 O  O   . SER   B 243 ? 0.2412 0.2535 0.2571 -0.0166 0.0206  -0.0261 243 SER   B O   
3631 C  CB  . SER   B 243 ? 0.2405 0.2377 0.2542 -0.0138 0.0198  -0.0167 243 SER   B CB  
3632 O  OG  . SER   B 243 ? 0.2655 0.2652 0.2828 -0.0147 0.0207  -0.0209 243 SER   B OG  
3633 N  N   . LEU   B 244 ? 0.2177 0.2285 0.2271 -0.0125 0.0167  -0.0204 244 LEU   B N   
3634 C  CA  . LEU   B 244 ? 0.2168 0.2347 0.2258 -0.0114 0.0152  -0.0233 244 LEU   B CA  
3635 C  C   . LEU   B 244 ? 0.2265 0.2487 0.2364 -0.0132 0.0163  -0.0260 244 LEU   B C   
3636 O  O   . LEU   B 244 ? 0.2322 0.2606 0.2440 -0.0136 0.0164  -0.0301 244 LEU   B O   
3637 C  CB  . LEU   B 244 ? 0.2188 0.2372 0.2239 -0.0085 0.0125  -0.0207 244 LEU   B CB  
3638 C  CG  . LEU   B 244 ? 0.2217 0.2368 0.2256 -0.0068 0.0113  -0.0184 244 LEU   B CG  
3639 C  CD1 . LEU   B 244 ? 0.2250 0.2400 0.2252 -0.0043 0.0090  -0.0158 244 LEU   B CD1 
3640 C  CD2 . LEU   B 244 ? 0.2213 0.2397 0.2270 -0.0067 0.0112  -0.0212 244 LEU   B CD2 
3641 N  N   . LEU   B 245 ? 0.2294 0.2492 0.2381 -0.0141 0.0170  -0.0240 245 LEU   B N   
3642 C  CA  . LEU   B 245 ? 0.2560 0.2800 0.2655 -0.0159 0.0181  -0.0266 245 LEU   B CA  
3643 C  C   . LEU   B 245 ? 0.2777 0.3026 0.2912 -0.0192 0.0211  -0.0303 245 LEU   B C   
3644 O  O   . LEU   B 245 ? 0.2704 0.3018 0.2858 -0.0203 0.0217  -0.0345 245 LEU   B O   
3645 C  CB  . LEU   B 245 ? 0.2392 0.2602 0.2463 -0.0164 0.0185  -0.0234 245 LEU   B CB  
3646 C  CG  . LEU   B 245 ? 0.2374 0.2598 0.2412 -0.0136 0.0158  -0.0214 245 LEU   B CG  
3647 C  CD1 . LEU   B 245 ? 0.2251 0.2446 0.2268 -0.0144 0.0163  -0.0184 245 LEU   B CD1 
3648 C  CD2 . LEU   B 245 ? 0.2520 0.2818 0.2561 -0.0123 0.0144  -0.0248 245 LEU   B CD2 
3649 N  N   . LYS   B 246 ? 0.3081 0.3267 0.3232 -0.0206 0.0229  -0.0288 246 LYS   B N   
3650 C  CA  . LYS   B 246 ? 0.3624 0.3807 0.3818 -0.0238 0.0260  -0.0322 246 LYS   B CA  
3651 C  C   . LYS   B 246 ? 0.3379 0.3627 0.3600 -0.0236 0.0256  -0.0371 246 LYS   B C   
3652 O  O   . LYS   B 246 ? 0.3500 0.3795 0.3753 -0.0260 0.0275  -0.0417 246 LYS   B O   
3653 C  CB  . LYS   B 246 ? 0.3963 0.4058 0.4168 -0.0247 0.0278  -0.0292 246 LYS   B CB  
3654 C  CG  . LYS   B 246 ? 0.4759 0.4839 0.5013 -0.0280 0.0313  -0.0326 246 LYS   B CG  
3655 C  CD  . LYS   B 246 ? 0.5757 0.5742 0.6016 -0.0294 0.0336  -0.0288 246 LYS   B CD  
3656 C  CE  . LYS   B 246 ? 0.6452 0.6419 0.6759 -0.0332 0.0376  -0.0323 246 LYS   B CE  
3657 N  NZ  . LYS   B 246 ? 0.6472 0.6460 0.6821 -0.0333 0.0380  -0.0365 246 LYS   B NZ  
3658 N  N   . ALA   B 247 ? 0.3118 0.3372 0.3328 -0.0208 0.0233  -0.0362 247 ALA   B N   
3659 C  CA  . ALA   B 247 ? 0.3055 0.3378 0.3284 -0.0203 0.0227  -0.0405 247 ALA   B CA  
3660 C  C   . ALA   B 247 ? 0.3184 0.3595 0.3407 -0.0198 0.0215  -0.0435 247 ALA   B C   
3661 O  O   . ALA   B 247 ? 0.3180 0.3662 0.3427 -0.0204 0.0218  -0.0482 247 ALA   B O   
3662 C  CB  . ALA   B 247 ? 0.2955 0.3269 0.3166 -0.0175 0.0204  -0.0385 247 ALA   B CB  
3663 N  N   . LEU   B 248 ? 0.3181 0.3593 0.3371 -0.0184 0.0200  -0.0411 248 LEU   B N   
3664 C  CA  . LEU   B 248 ? 0.3161 0.3655 0.3345 -0.0172 0.0186  -0.0437 248 LEU   B CA  
3665 C  C   . LEU   B 248 ? 0.3348 0.3872 0.3556 -0.0203 0.0210  -0.0469 248 LEU   B C   
3666 O  O   . LEU   B 248 ? 0.3428 0.4022 0.3634 -0.0195 0.0199  -0.0494 248 LEU   B O   
3667 C  CB  . LEU   B 248 ? 0.3184 0.3665 0.3324 -0.0138 0.0157  -0.0397 248 LEU   B CB  
3668 C  CG  . LEU   B 248 ? 0.3167 0.3641 0.3283 -0.0106 0.0132  -0.0374 248 LEU   B CG  
3669 C  CD1 . LEU   B 248 ? 0.3131 0.3567 0.3207 -0.0079 0.0110  -0.0329 248 LEU   B CD1 
3670 C  CD2 . LEU   B 248 ? 0.3223 0.3782 0.3344 -0.0091 0.0118  -0.0409 248 LEU   B CD2 
3671 N  N   . GLY   B 249 ? 0.3693 0.4160 0.3920 -0.0237 0.0241  -0.0466 249 GLY   B N   
3672 C  CA  . GLY   B 249 ? 0.3960 0.4448 0.4211 -0.0273 0.0269  -0.0497 249 GLY   B CA  
3673 C  C   . GLY   B 249 ? 0.4233 0.4687 0.4458 -0.0279 0.0272  -0.0464 249 GLY   B C   
3674 O  O   . GLY   B 249 ? 0.4430 0.4915 0.4668 -0.0306 0.0291  -0.0489 249 GLY   B O   
3675 N  N   . HIS   B 250 ? 0.4164 0.4558 0.4353 -0.0257 0.0255  -0.0410 250 HIS   B N   
3676 C  CA  . HIS   B 250 ? 0.4404 0.4764 0.4568 -0.0265 0.0261  -0.0377 250 HIS   B CA  
3677 C  C   . HIS   B 250 ? 0.4801 0.5067 0.4963 -0.0282 0.0281  -0.0338 250 HIS   B C   
3678 O  O   . HIS   B 250 ? 0.5640 0.5863 0.5770 -0.0261 0.0265  -0.0291 250 HIS   B O   
3679 C  CB  . HIS   B 250 ? 0.4562 0.4937 0.4689 -0.0229 0.0227  -0.0352 250 HIS   B CB  
3680 C  CG  . HIS   B 250 ? 0.4496 0.4961 0.4629 -0.0214 0.0211  -0.0391 250 HIS   B CG  
3681 N  ND1 . HIS   B 250 ? 0.4765 0.5279 0.4905 -0.0190 0.0192  -0.0414 250 HIS   B ND1 
3682 C  CD2 . HIS   B 250 ? 0.4167 0.4684 0.4300 -0.0220 0.0212  -0.0413 250 HIS   B CD2 
3683 C  CE1 . HIS   B 250 ? 0.4215 0.4806 0.4359 -0.0178 0.0180  -0.0445 250 HIS   B CE1 
3684 N  NE2 . HIS   B 250 ? 0.3896 0.4491 0.4038 -0.0196 0.0192  -0.0447 250 HIS   B NE2 
3685 C  C1  . A1ICA C .   ? 0.2318 0.2306 0.2261 -0.0029 0.0052  0.0004  301 A1ICA A C1  
3686 C  C2  . A1ICA C .   ? 0.2351 0.2330 0.2309 -0.0027 0.0053  -0.0010 301 A1ICA A C2  
3687 C  C3  . A1ICA C .   ? 0.2458 0.2414 0.2443 -0.0025 0.0061  -0.0010 301 A1ICA A C3  
3688 C  C4  . A1ICA C .   ? 0.2625 0.2570 0.2627 -0.0020 0.0062  -0.0029 301 A1ICA A C4  
3689 C  C5  . A1ICA C .   ? 0.2870 0.2777 0.2898 -0.0021 0.0070  -0.0035 301 A1ICA A C5  
3690 C  C6  . A1ICA C .   ? 0.3239 0.3136 0.3282 -0.0013 0.0070  -0.0060 301 A1ICA A C6  
3691 C  C7  . A1ICA C .   ? 0.2933 0.2868 0.2963 -0.0006 0.0062  -0.0077 301 A1ICA A C7  
3692 CL CL1 . A1ICA C .   ? 0.3702 0.3639 0.3749 0.0008  0.0061  -0.0112 301 A1ICA A CL1 
3693 C  C8  . A1ICA C .   ? 0.2829 0.2801 0.2832 -0.0011 0.0055  -0.0068 301 A1ICA A C8  
3694 C  C9  . A1ICA C .   ? 0.2551 0.2522 0.2540 -0.0017 0.0055  -0.0046 301 A1ICA A C9  
3695 C  C1  . A1ICA D .   ? 0.2527 0.2475 0.2358 0.0055  0.0004  0.0069  301 A1ICA B C1  
3696 C  C2  . A1ICA D .   ? 0.2482 0.2439 0.2305 0.0053  0.0005  0.0078  301 A1ICA B C2  
3697 C  C3  . A1ICA D .   ? 0.2573 0.2530 0.2400 0.0054  0.0006  0.0094  301 A1ICA B C3  
3698 C  C4  . A1ICA D .   ? 0.2410 0.2381 0.2225 0.0051  0.0006  0.0106  301 A1ICA B C4  
3699 C  C5  . A1ICA D .   ? 0.2388 0.2374 0.2191 0.0046  0.0006  0.0094  301 A1ICA B C5  
3700 C  C6  . A1ICA D .   ? 0.2400 0.2407 0.2193 0.0041  0.0007  0.0100  301 A1ICA B C6  
3701 C  C7  . A1ICA D .   ? 0.2469 0.2481 0.2258 0.0041  0.0008  0.0122  301 A1ICA B C7  
3702 CL CL1 . A1ICA D .   ? 0.2693 0.2738 0.2465 0.0032  0.0011  0.0130  301 A1ICA B CL1 
3703 C  C8  . A1ICA D .   ? 0.2587 0.2580 0.2385 0.0048  0.0007  0.0137  301 A1ICA B C8  
3704 C  C9  . A1ICA D .   ? 0.2415 0.2388 0.2228 0.0054  0.0006  0.0127  301 A1ICA B C9  
3705 C  C1  . GOL   E .   ? 0.3111 0.2823 0.3277 0.0071  0.0094  0.0038  302 GOL   B C1  
3706 O  O1  . GOL   E .   ? 0.3543 0.3266 0.3675 0.0055  0.0096  0.0045  302 GOL   B O1  
3707 C  C2  . GOL   E .   ? 0.2719 0.2476 0.2872 0.0078  0.0078  0.0022  302 GOL   B C2  
3708 O  O2  . GOL   E .   ? 0.2491 0.2261 0.2604 0.0088  0.0062  0.0050  302 GOL   B O2  
3709 C  C3  . GOL   E .   ? 0.2788 0.2582 0.2934 0.0059  0.0080  -0.0011 302 GOL   B C3  
3710 O  O3  . GOL   E .   ? 0.2397 0.2227 0.2526 0.0064  0.0067  -0.0021 302 GOL   B O3  
# 
