data_9FD9
# 
_entry.id   9FD9 
# 
_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   9FD9         pdb_00009fd9 10.2210/pdb9fd9/pdb 
WWPDB D_1292137941 ?            ?                   
# 
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                        9FD9 
_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 4-nitro-cinnamaldehyde           179.173   2   ?       ? ? ? 
3 non-polymer syn GLYCEROL                         92.094    1   ?       ? ? ? 
4 water       nat water                            18.015    246 ?       ? ? ? 
# 
_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 4-nitro-cinnamaldehyde A1IB9 
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 
A1IB9 non-polymer         . 4-nitro-cinnamaldehyde '(~{E})-3-(4-nitrophenyl)prop-2-en-1-ol' 'C9 H9 N O3'     179.173 
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   3   ASP ASP 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  ?   ?   ?   B . n 
B 1 23  ASP 23  23  ?   ?   ?   B . n 
B 1 24  TYR 24  24  ?   ?   ?   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        A1IB9 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1IB9 
_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 A1IB9 1   301 301 A1IB9 PNC A . 
D 3 GOL   1   302 302 GOL   GOL A . 
E 2 A1IB9 1   301 301 A1IB9 PNC B . 
F 4 HOH   1   401 221 HOH   HOH A . 
F 4 HOH   2   402 65  HOH   HOH A . 
F 4 HOH   3   403 132 HOH   HOH A . 
F 4 HOH   4   404 118 HOH   HOH A . 
F 4 HOH   5   405 226 HOH   HOH A . 
F 4 HOH   6   406 97  HOH   HOH A . 
F 4 HOH   7   407 199 HOH   HOH A . 
F 4 HOH   8   408 13  HOH   HOH A . 
F 4 HOH   9   409 72  HOH   HOH A . 
F 4 HOH   10  410 83  HOH   HOH A . 
F 4 HOH   11  411 33  HOH   HOH A . 
F 4 HOH   12  412 54  HOH   HOH A . 
F 4 HOH   13  413 75  HOH   HOH A . 
F 4 HOH   14  414 115 HOH   HOH A . 
F 4 HOH   15  415 44  HOH   HOH A . 
F 4 HOH   16  416 161 HOH   HOH A . 
F 4 HOH   17  417 174 HOH   HOH A . 
F 4 HOH   18  418 164 HOH   HOH A . 
F 4 HOH   19  419 9   HOH   HOH A . 
F 4 HOH   20  420 131 HOH   HOH A . 
F 4 HOH   21  421 10  HOH   HOH A . 
F 4 HOH   22  422 241 HOH   HOH A . 
F 4 HOH   23  423 23  HOH   HOH A . 
F 4 HOH   24  424 48  HOH   HOH A . 
F 4 HOH   25  425 20  HOH   HOH A . 
F 4 HOH   26  426 129 HOH   HOH A . 
F 4 HOH   27  427 113 HOH   HOH A . 
F 4 HOH   28  428 86  HOH   HOH A . 
F 4 HOH   29  429 58  HOH   HOH A . 
F 4 HOH   30  430 182 HOH   HOH A . 
F 4 HOH   31  431 233 HOH   HOH A . 
F 4 HOH   32  432 138 HOH   HOH A . 
F 4 HOH   33  433 154 HOH   HOH A . 
F 4 HOH   34  434 123 HOH   HOH A . 
F 4 HOH   35  435 29  HOH   HOH A . 
F 4 HOH   36  436 171 HOH   HOH A . 
F 4 HOH   37  437 3   HOH   HOH A . 
F 4 HOH   38  438 62  HOH   HOH A . 
F 4 HOH   39  439 30  HOH   HOH A . 
F 4 HOH   40  440 104 HOH   HOH A . 
F 4 HOH   41  441 103 HOH   HOH A . 
F 4 HOH   42  442 6   HOH   HOH A . 
F 4 HOH   43  443 234 HOH   HOH A . 
F 4 HOH   44  444 112 HOH   HOH A . 
F 4 HOH   45  445 169 HOH   HOH A . 
F 4 HOH   46  446 49  HOH   HOH A . 
F 4 HOH   47  447 2   HOH   HOH A . 
F 4 HOH   48  448 243 HOH   HOH A . 
F 4 HOH   49  449 50  HOH   HOH A . 
F 4 HOH   50  450 80  HOH   HOH A . 
F 4 HOH   51  451 64  HOH   HOH A . 
F 4 HOH   52  452 32  HOH   HOH A . 
F 4 HOH   53  453 214 HOH   HOH A . 
F 4 HOH   54  454 34  HOH   HOH A . 
F 4 HOH   55  455 207 HOH   HOH A . 
F 4 HOH   56  456 176 HOH   HOH A . 
F 4 HOH   57  457 160 HOH   HOH A . 
F 4 HOH   58  458 135 HOH   HOH A . 
F 4 HOH   59  459 116 HOH   HOH A . 
F 4 HOH   60  460 158 HOH   HOH A . 
F 4 HOH   61  461 70  HOH   HOH A . 
F 4 HOH   62  462 147 HOH   HOH A . 
F 4 HOH   63  463 122 HOH   HOH A . 
F 4 HOH   64  464 35  HOH   HOH A . 
F 4 HOH   65  465 228 HOH   HOH A . 
F 4 HOH   66  466 190 HOH   HOH A . 
F 4 HOH   67  467 142 HOH   HOH A . 
F 4 HOH   68  468 210 HOH   HOH A . 
F 4 HOH   69  469 198 HOH   HOH A . 
F 4 HOH   70  470 157 HOH   HOH A . 
F 4 HOH   71  471 63  HOH   HOH A . 
F 4 HOH   72  472 203 HOH   HOH A . 
F 4 HOH   73  473 195 HOH   HOH A . 
F 4 HOH   74  474 114 HOH   HOH A . 
F 4 HOH   75  475 145 HOH   HOH A . 
F 4 HOH   76  476 127 HOH   HOH A . 
F 4 HOH   77  477 220 HOH   HOH A . 
F 4 HOH   78  478 200 HOH   HOH A . 
F 4 HOH   79  479 107 HOH   HOH A . 
F 4 HOH   80  480 148 HOH   HOH A . 
F 4 HOH   81  481 87  HOH   HOH A . 
F 4 HOH   82  482 159 HOH   HOH A . 
F 4 HOH   83  483 124 HOH   HOH A . 
F 4 HOH   84  484 183 HOH   HOH A . 
F 4 HOH   85  485 11  HOH   HOH A . 
F 4 HOH   86  486 18  HOH   HOH A . 
F 4 HOH   87  487 85  HOH   HOH A . 
F 4 HOH   88  488 168 HOH   HOH A . 
F 4 HOH   89  489 155 HOH   HOH A . 
F 4 HOH   90  490 181 HOH   HOH A . 
F 4 HOH   91  491 56  HOH   HOH A . 
F 4 HOH   92  492 59  HOH   HOH A . 
F 4 HOH   93  493 150 HOH   HOH A . 
F 4 HOH   94  494 76  HOH   HOH A . 
F 4 HOH   95  495 105 HOH   HOH A . 
F 4 HOH   96  496 217 HOH   HOH A . 
F 4 HOH   97  497 73  HOH   HOH A . 
F 4 HOH   98  498 163 HOH   HOH A . 
F 4 HOH   99  499 134 HOH   HOH A . 
F 4 HOH   100 500 96  HOH   HOH A . 
F 4 HOH   101 501 205 HOH   HOH A . 
F 4 HOH   102 502 218 HOH   HOH A . 
F 4 HOH   103 503 109 HOH   HOH A . 
F 4 HOH   104 504 106 HOH   HOH A . 
F 4 HOH   105 505 89  HOH   HOH A . 
F 4 HOH   106 506 46  HOH   HOH A . 
F 4 HOH   107 507 1   HOH   HOH A . 
F 4 HOH   108 508 42  HOH   HOH A . 
F 4 HOH   109 509 211 HOH   HOH A . 
F 4 HOH   110 510 208 HOH   HOH A . 
F 4 HOH   111 511 193 HOH   HOH A . 
F 4 HOH   112 512 167 HOH   HOH A . 
F 4 HOH   113 513 55  HOH   HOH A . 
F 4 HOH   114 514 125 HOH   HOH A . 
F 4 HOH   115 515 165 HOH   HOH A . 
F 4 HOH   116 516 92  HOH   HOH A . 
G 4 HOH   1   401 240 HOH   HOH B . 
G 4 HOH   2   402 232 HOH   HOH B . 
G 4 HOH   3   403 245 HOH   HOH B . 
G 4 HOH   4   404 225 HOH   HOH B . 
G 4 HOH   5   405 238 HOH   HOH B . 
G 4 HOH   6   406 236 HOH   HOH B . 
G 4 HOH   7   407 77  HOH   HOH B . 
G 4 HOH   8   408 74  HOH   HOH B . 
G 4 HOH   9   409 196 HOH   HOH B . 
G 4 HOH   10  410 98  HOH   HOH B . 
G 4 HOH   11  411 133 HOH   HOH B . 
G 4 HOH   12  412 201 HOH   HOH B . 
G 4 HOH   13  413 21  HOH   HOH B . 
G 4 HOH   14  414 51  HOH   HOH B . 
G 4 HOH   15  415 140 HOH   HOH B . 
G 4 HOH   16  416 25  HOH   HOH B . 
G 4 HOH   17  417 173 HOH   HOH B . 
G 4 HOH   18  418 81  HOH   HOH B . 
G 4 HOH   19  419 7   HOH   HOH B . 
G 4 HOH   20  420 45  HOH   HOH B . 
G 4 HOH   21  421 5   HOH   HOH B . 
G 4 HOH   22  422 179 HOH   HOH B . 
G 4 HOH   23  423 235 HOH   HOH B . 
G 4 HOH   24  424 137 HOH   HOH B . 
G 4 HOH   25  425 170 HOH   HOH B . 
G 4 HOH   26  426 192 HOH   HOH B . 
G 4 HOH   27  427 17  HOH   HOH B . 
G 4 HOH   28  428 79  HOH   HOH B . 
G 4 HOH   29  429 101 HOH   HOH B . 
G 4 HOH   30  430 141 HOH   HOH B . 
G 4 HOH   31  431 19  HOH   HOH B . 
G 4 HOH   32  432 153 HOH   HOH B . 
G 4 HOH   33  433 90  HOH   HOH B . 
G 4 HOH   34  434 184 HOH   HOH B . 
G 4 HOH   35  435 121 HOH   HOH B . 
G 4 HOH   36  436 53  HOH   HOH B . 
G 4 HOH   37  437 144 HOH   HOH B . 
G 4 HOH   38  438 188 HOH   HOH B . 
G 4 HOH   39  439 26  HOH   HOH B . 
G 4 HOH   40  440 52  HOH   HOH B . 
G 4 HOH   41  441 202 HOH   HOH B . 
G 4 HOH   42  442 166 HOH   HOH B . 
G 4 HOH   43  443 36  HOH   HOH B . 
G 4 HOH   44  444 175 HOH   HOH B . 
G 4 HOH   45  445 14  HOH   HOH B . 
G 4 HOH   46  446 130 HOH   HOH B . 
G 4 HOH   47  447 60  HOH   HOH B . 
G 4 HOH   48  448 27  HOH   HOH B . 
G 4 HOH   49  449 227 HOH   HOH B . 
G 4 HOH   50  450 39  HOH   HOH B . 
G 4 HOH   51  451 177 HOH   HOH B . 
G 4 HOH   52  452 4   HOH   HOH B . 
G 4 HOH   53  453 117 HOH   HOH B . 
G 4 HOH   54  454 172 HOH   HOH B . 
G 4 HOH   55  455 41  HOH   HOH B . 
G 4 HOH   56  456 40  HOH   HOH B . 
G 4 HOH   57  457 15  HOH   HOH B . 
G 4 HOH   58  458 67  HOH   HOH B . 
G 4 HOH   59  459 120 HOH   HOH B . 
G 4 HOH   60  460 224 HOH   HOH B . 
G 4 HOH   61  461 146 HOH   HOH B . 
G 4 HOH   62  462 93  HOH   HOH B . 
G 4 HOH   63  463 43  HOH   HOH B . 
G 4 HOH   64  464 47  HOH   HOH B . 
G 4 HOH   65  465 111 HOH   HOH B . 
G 4 HOH   66  466 152 HOH   HOH B . 
G 4 HOH   67  467 149 HOH   HOH B . 
G 4 HOH   68  468 139 HOH   HOH B . 
G 4 HOH   69  469 119 HOH   HOH B . 
G 4 HOH   70  470 95  HOH   HOH B . 
G 4 HOH   71  471 219 HOH   HOH B . 
G 4 HOH   72  472 222 HOH   HOH B . 
G 4 HOH   73  473 237 HOH   HOH B . 
G 4 HOH   74  474 31  HOH   HOH B . 
G 4 HOH   75  475 94  HOH   HOH B . 
G 4 HOH   76  476 69  HOH   HOH B . 
G 4 HOH   77  477 22  HOH   HOH B . 
G 4 HOH   78  478 246 HOH   HOH B . 
G 4 HOH   79  479 102 HOH   HOH B . 
G 4 HOH   80  480 244 HOH   HOH B . 
G 4 HOH   81  481 24  HOH   HOH B . 
G 4 HOH   82  482 230 HOH   HOH B . 
G 4 HOH   83  483 126 HOH   HOH B . 
G 4 HOH   84  484 143 HOH   HOH B . 
G 4 HOH   85  485 66  HOH   HOH B . 
G 4 HOH   86  486 16  HOH   HOH B . 
G 4 HOH   87  487 38  HOH   HOH B . 
G 4 HOH   88  488 186 HOH   HOH B . 
G 4 HOH   89  489 28  HOH   HOH B . 
G 4 HOH   90  490 78  HOH   HOH B . 
G 4 HOH   91  491 57  HOH   HOH B . 
G 4 HOH   92  492 191 HOH   HOH B . 
G 4 HOH   93  493 61  HOH   HOH B . 
G 4 HOH   94  494 128 HOH   HOH B . 
G 4 HOH   95  495 151 HOH   HOH B . 
G 4 HOH   96  496 8   HOH   HOH B . 
G 4 HOH   97  497 215 HOH   HOH B . 
G 4 HOH   98  498 99  HOH   HOH B . 
G 4 HOH   99  499 197 HOH   HOH B . 
G 4 HOH   100 500 91  HOH   HOH B . 
G 4 HOH   101 501 180 HOH   HOH B . 
G 4 HOH   102 502 185 HOH   HOH B . 
G 4 HOH   103 503 223 HOH   HOH B . 
G 4 HOH   104 504 110 HOH   HOH B . 
G 4 HOH   105 505 216 HOH   HOH B . 
G 4 HOH   106 506 71  HOH   HOH B . 
G 4 HOH   107 507 37  HOH   HOH B . 
G 4 HOH   108 508 136 HOH   HOH B . 
G 4 HOH   109 509 194 HOH   HOH B . 
G 4 HOH   110 510 187 HOH   HOH B . 
G 4 HOH   111 511 204 HOH   HOH B . 
G 4 HOH   112 512 242 HOH   HOH B . 
G 4 HOH   113 513 209 HOH   HOH B . 
G 4 HOH   114 514 239 HOH   HOH B . 
G 4 HOH   115 515 88  HOH   HOH B . 
G 4 HOH   116 516 162 HOH   HOH B . 
G 4 HOH   117 517 108 HOH   HOH B . 
G 4 HOH   118 518 156 HOH   HOH B . 
G 4 HOH   119 519 12  HOH   HOH B . 
G 4 HOH   120 520 212 HOH   HOH B . 
G 4 HOH   121 521 231 HOH   HOH B . 
G 4 HOH   122 522 178 HOH   HOH B . 
G 4 HOH   123 523 84  HOH   HOH B . 
G 4 HOH   124 524 213 HOH   HOH B . 
G 4 HOH   125 525 100 HOH   HOH B . 
G 4 HOH   126 526 68  HOH   HOH B . 
G 4 HOH   127 527 82  HOH   HOH B . 
G 4 HOH   128 528 229 HOH   HOH B . 
G 4 HOH   129 529 206 HOH   HOH B . 
G 4 HOH   130 530 189 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 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.27 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FD9 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.095 
_cell.length_a_esd                 ? 
_cell.length_b                     72.531 
_cell.length_b_esd                 ? 
_cell.length_c                     70.688 
_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                         9FD9 
_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                   9FD9 
_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             2.13 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.36 
_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 PILATUS 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   0.965459 
_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        0.965459 
_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                                       9FD9 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.52 
_reflns.d_resolution_low                               47.81 
_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                                     70796 
_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                           95.5 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                2.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               1.07 
_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                                0.115 
_reflns.pdbx_Rpim_I_all                                0.072 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       164586 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.988 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.090 
_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                                    1.52 
_reflns_shell.d_res_low                                     1.55 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           8355 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3451 
_reflns_shell.percent_possible_obs                          93.6 
_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                               2.4 
_reflns_shell.pdbx_chi_squared                              1.04 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     0.8 
_reflns_shell.pdbx_Rrim_I_all                               1.471 
_reflns_shell.pdbx_Rpim_I_all                               0.900 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.312 
_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                                  1.155 
_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]                            -0.35 
_refine.aniso_B[1][2]                            -0.00 
_refine.aniso_B[1][3]                            0.04 
_refine.aniso_B[2][2]                            0.69 
_refine.aniso_B[2][3]                            0.00 
_refine.aniso_B[3][3]                            -0.34 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               20.473 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.963 
_refine.correlation_coeff_Fo_to_Fc_free          0.949 
_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                                 9FD9 
_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                            1.52 
_refine.ls_d_res_low                             41.73 
_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                     67356 
_refine.ls_number_reflns_R_free                  3406 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.28 
_refine.ls_percent_reflns_R_free                 4.8 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.18777 
_refine.ls_R_factor_R_free                       0.21755 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.18633 
_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                       0.082 
_refine.pdbx_overall_ESU_R_Free                  0.083 
_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                             4.870 
_refine.overall_SU_ML                            0.077 
_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                       1.52 
_refine_hist.d_res_low                        41.73 
_refine_hist.number_atoms_solvent             246 
_refine_hist.number_atoms_total               3918 
_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        3642 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_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' ? 0.009  0.012  3802 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3770 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.782  1.786  5149 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.597  1.727  8683 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.542  5.000  506  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 9.532  5.968  31   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 12.214 10.000 680  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.091  0.200  611  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.009  0.019  4469 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.018  803  ? 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' ? 1.362  1.400  1982 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 1.331  1.399  1982 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 1.991  2.496  2484 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 1.991  2.497  2485 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 2.605  1.718  1820 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 2.605  1.718  1821 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 4.068  2.997  2660 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 5.270  15.12  4407 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 5.212  14.52  4359 ? 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                       1.520 
_refine_ls_shell.d_res_low                        1.559 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             259 
_refine_ls_shell.number_reflns_R_work             4930 
_refine_ls_shell.percent_reflns_obs               94.05 
_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                  0.334 
_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                  0.349 
# 
_struct.entry_id                     9FD9 
_struct.title                        
'Re-engineered peroxygenase variant of 2-deoxy-D-ribose-5-phosphate aldolase, Schiff-base complex with 4-nitro-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        9FD9 
_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 3 ? 
E N N 2 ? 
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 9FD9 A 1 ? 259 ? B1IS38 1 ? 259 ? 1 259 
2 1 9FD9 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 9FD9 SER A 18  ? UNP B1IS38 THR 18  'engineered mutation' 18  1  
1 9FD9 GLY A 22  ? UNP B1IS38 ASP 22  'engineered mutation' 22  2  
1 9FD9 TYR A 24  ? UNP B1IS38 ASP 24  'engineered mutation' 24  3  
1 9FD9 SER A 47  ? UNP B1IS38 CYS 47  'engineered mutation' 47  4  
1 9FD9 VAL A 48  ? UNP B1IS38 ILE 48  'engineered mutation' 48  5  
1 9FD9 SER A 52  ? UNP B1IS38 PHE 52  'engineered mutation' 52  6  
1 9FD9 ARG A 172 ? UNP B1IS38 LYS 172 'engineered mutation' 172 7  
1 9FD9 SER A 197 ? UNP B1IS38 THR 197 'engineered mutation' 197 8  
1 9FD9 VAL A 202 ? UNP B1IS38 PRO 202 'engineered mutation' 202 9  
1 9FD9 THR A 203 ? UNP B1IS38 ALA 203 'engineered mutation' 203 10 
1 9FD9 SER A 207 ? UNP B1IS38 ARG 207 'engineered mutation' 207 11 
1 9FD9 SER A 236 ? UNP B1IS38 GLY 236 'engineered mutation' 236 12 
1 9FD9 GLY A 239 ? UNP B1IS38 SER 239 'engineered mutation' 239 13 
1 9FD9 LEU A 260 ? UNP B1IS38 ?   ?   'expression tag'      260 14 
1 9FD9 GLU A 261 ? UNP B1IS38 ?   ?   'expression tag'      261 15 
1 9FD9 HIS A 262 ? UNP B1IS38 ?   ?   'expression tag'      262 16 
1 9FD9 HIS A 263 ? UNP B1IS38 ?   ?   'expression tag'      263 17 
1 9FD9 HIS A 264 ? UNP B1IS38 ?   ?   'expression tag'      264 18 
1 9FD9 HIS A 265 ? UNP B1IS38 ?   ?   'expression tag'      265 19 
1 9FD9 HIS A 266 ? UNP B1IS38 ?   ?   'expression tag'      266 20 
1 9FD9 HIS A 267 ? UNP B1IS38 ?   ?   'expression tag'      267 21 
2 9FD9 SER B 18  ? UNP B1IS38 THR 18  'engineered mutation' 18  22 
2 9FD9 GLY B 22  ? UNP B1IS38 ASP 22  'engineered mutation' 22  23 
2 9FD9 TYR B 24  ? UNP B1IS38 ASP 24  'engineered mutation' 24  24 
2 9FD9 SER B 47  ? UNP B1IS38 CYS 47  'engineered mutation' 47  25 
2 9FD9 VAL B 48  ? UNP B1IS38 ILE 48  'engineered mutation' 48  26 
2 9FD9 SER B 52  ? UNP B1IS38 PHE 52  'engineered mutation' 52  27 
2 9FD9 ARG B 172 ? UNP B1IS38 LYS 172 'engineered mutation' 172 28 
2 9FD9 SER B 197 ? UNP B1IS38 THR 197 'engineered mutation' 197 29 
2 9FD9 VAL B 202 ? UNP B1IS38 PRO 202 'engineered mutation' 202 30 
2 9FD9 THR B 203 ? UNP B1IS38 ALA 203 'engineered mutation' 203 31 
2 9FD9 SER B 207 ? UNP B1IS38 ARG 207 'engineered mutation' 207 32 
2 9FD9 SER B 236 ? UNP B1IS38 GLY 236 'engineered mutation' 236 33 
2 9FD9 GLY B 239 ? UNP B1IS38 SER 239 'engineered mutation' 239 34 
2 9FD9 LEU B 260 ? UNP B1IS38 ?   ?   'expression tag'      260 35 
2 9FD9 GLU B 261 ? UNP B1IS38 ?   ?   'expression tag'      261 36 
2 9FD9 HIS B 262 ? UNP B1IS38 ?   ?   'expression tag'      262 37 
2 9FD9 HIS B 263 ? UNP B1IS38 ?   ?   'expression tag'      263 38 
2 9FD9 HIS B 264 ? UNP B1IS38 ?   ?   'expression tag'      264 39 
2 9FD9 HIS B 265 ? UNP B1IS38 ?   ?   'expression tag'      265 40 
2 9FD9 HIS B 266 ? UNP B1IS38 ?   ?   'expression tag'      266 41 
2 9FD9 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,D,F 
2 1 B,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 ASP A 3   ? LYS A 13  ? ASP A 3   LYS A 13  1 ? 11 
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 ASN A 114 ? ALA A 132 ? ASN A 114 ALA A 132 1 ? 19 
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 ASP B 26  ? ALA B 36  ? ASP B 26  ALA B 36  1 ? 11 
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 ? MET B 192 ? THR B 178 MET B 192 1 ? 15 
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 A1IB9 . C1 ? ? A LYS 167 A A1IB9 301 1_555 ? ? ? ? ? ? ? 1.265 ? ? 
covale2 covale one ? B LYS 167 NZ ? ? ? 1_555 E A1IB9 . C1 ? ? B LYS 167 B A1IB9 301 1_555 ? ? ? ? ? ? ? 1.258 ? ? 
# 
_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 A1IB9 C . ? LYS A 167 ? A1IB9 A 301 ? 1_555 LYS A 167 ? 1_555 C1 NZ LYS 1 A1IB9 None 'Covalent chemical modification' 
2 A1IB9 E . ? LYS B 167 ? A1IB9 B 301 ? 1_555 LYS B 167 ? 1_555 C1 NZ LYS 1 A1IB9 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 -5.51 
2 PHE 76 B . ? PHE 76 B PRO 77 B ? PRO 77 B 1 -6.49 
# 
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  ? SER A 18  ? ASP A 16  SER A 18  
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  ? SER B 18  ? ASP B 16  SER B 18  
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 SER A 47  ? O SER A 47  
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                   9FD9 
_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 
# 
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 ? ? 61.04   67.76   
2 1 LYS A 146 ? ? 74.19   -54.21  
3 1 ASN A 176 ? ? -110.66 -141.60 
4 1 GLU B 141 ? ? 64.73   63.24   
5 1 LYS B 146 ? ? 67.93   -57.07  
6 1 ASN B 176 ? ? -106.78 -135.59 
# 
_pdbx_validate_peptide_omega.id               1 
_pdbx_validate_peptide_omega.PDB_model_num    1 
_pdbx_validate_peptide_omega.auth_comp_id_1   THR 
_pdbx_validate_peptide_omega.auth_asym_id_1   B 
_pdbx_validate_peptide_omega.auth_seq_id_1    168 
_pdbx_validate_peptide_omega.PDB_ins_code_1   ? 
_pdbx_validate_peptide_omega.label_alt_id_1   ? 
_pdbx_validate_peptide_omega.auth_comp_id_2   SER 
_pdbx_validate_peptide_omega.auth_asym_id_2   B 
_pdbx_validate_peptide_omega.auth_seq_id_2    169 
_pdbx_validate_peptide_omega.PDB_ins_code_2   ? 
_pdbx_validate_peptide_omega.label_alt_id_2   ? 
_pdbx_validate_peptide_omega.omega            -148.81 
# 
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 A 234 ? ? 0.081 'SIDE CHAIN' 
2 1 ARG B 108 ? ? 0.076 'SIDE CHAIN' 
3 1 ARG B 234 ? ? 0.077 '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 4.5746  -8.0205  0.2682   0.0204 ? 0.0048  ? 0.0036 ? 0.0844 ? 0.0033  ? 0.0044 ? 0.4265 ? 0.0440  
? -0.1053 ? 0.1604 ? 0.1894 ? 0.2864 ? 0.0113 ? -0.0010 ? 0.0243 ? 0.0055 ? -0.0012 ? -0.0007 ? 0.0069 ? 0.0131  ? -0.0101 ? 
2 'X-RAY DIFFRACTION' ? refined -1.0033 -21.3769 -35.7459 0.0133 ? -0.0042 ? 0.0035 ? 0.0920 ? -0.0013 ? 0.0044 ? 0.6457 ? -0.0843 
? -0.1113 ? 0.0255 ? 0.1112 ? 0.6691 ? 0.0121 ? 0.0455  ? 0.0488 ? 0.0059 ? -0.0082 ? -0.0056 ? 0.0414 ? -0.0337 ? -0.0039 ? 
# 
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 3 ? ? ? A 302 ? ? ? 
2 'X-RAY DIFFRACTION' 2 ? ? B 3 ? ? ? B 301 ? ? ? 
# 
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 LEU 20  ? A LEU 20  
4  1 Y 1 A ASN 21  ? A ASN 21  
5  1 Y 1 A GLY 22  ? A GLY 22  
6  1 Y 1 A ASP 23  ? A ASP 23  
7  1 Y 1 A TYR 24  ? A TYR 24  
8  1 Y 1 A GLY 251 ? A GLY 251 
9  1 Y 1 A ASP 252 ? A ASP 252 
10 1 Y 1 A GLY 253 ? A GLY 253 
11 1 Y 1 A LYS 254 ? A LYS 254 
12 1 Y 1 A SER 255 ? A SER 255 
13 1 Y 1 A ALA 256 ? A ALA 256 
14 1 Y 1 A SER 257 ? A SER 257 
15 1 Y 1 A SER 258 ? A SER 258 
16 1 Y 1 A TYR 259 ? A TYR 259 
17 1 Y 1 A LEU 260 ? A LEU 260 
18 1 Y 1 A GLU 261 ? A GLU 261 
19 1 Y 1 A HIS 262 ? A HIS 262 
20 1 Y 1 A HIS 263 ? A HIS 263 
21 1 Y 1 A HIS 264 ? A HIS 264 
22 1 Y 1 A HIS 265 ? A HIS 265 
23 1 Y 1 A HIS 266 ? A HIS 266 
24 1 Y 1 A HIS 267 ? A HIS 267 
25 1 Y 1 B MET 1   ? B MET 1   
26 1 Y 1 B THR 2   ? B THR 2   
27 1 Y 1 B LEU 20  ? B LEU 20  
28 1 Y 1 B ASN 21  ? B ASN 21  
29 1 Y 1 B GLY 22  ? B GLY 22  
30 1 Y 1 B ASP 23  ? B ASP 23  
31 1 Y 1 B TYR 24  ? B TYR 24  
32 1 Y 1 B GLY 251 ? B GLY 251 
33 1 Y 1 B ASP 252 ? B ASP 252 
34 1 Y 1 B GLY 253 ? B GLY 253 
35 1 Y 1 B LYS 254 ? B LYS 254 
36 1 Y 1 B SER 255 ? B SER 255 
37 1 Y 1 B ALA 256 ? B ALA 256 
38 1 Y 1 B SER 257 ? B SER 257 
39 1 Y 1 B SER 258 ? B SER 258 
40 1 Y 1 B TYR 259 ? B TYR 259 
41 1 Y 1 B LEU 260 ? B LEU 260 
42 1 Y 1 B GLU 261 ? B GLU 261 
43 1 Y 1 B HIS 262 ? B HIS 262 
44 1 Y 1 B HIS 263 ? B HIS 263 
45 1 Y 1 B HIS 264 ? B HIS 264 
46 1 Y 1 B HIS 265 ? B HIS 265 
47 1 Y 1 B HIS 266 ? B HIS 266 
48 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 
A1IB9 C1   C N N 1   
A1IB9 C2   C N N 2   
A1IB9 C3   C N N 3   
A1IB9 C4   C Y N 4   
A1IB9 C5   C Y N 5   
A1IB9 C6   C Y N 6   
A1IB9 C7   C Y N 7   
A1IB9 C8   C Y N 8   
A1IB9 C9   C Y N 9   
A1IB9 N1   N N N 10  
A1IB9 O2   O N N 11  
A1IB9 O3   O N N 12  
A1IB9 O1   O N N 13  
A1IB9 H1   H N N 14  
A1IB9 H2   H N N 15  
A1IB9 H3   H N N 16  
A1IB9 H4   H N N 17  
A1IB9 H5   H N N 18  
A1IB9 H6   H N N 19  
A1IB9 H7   H N N 20  
A1IB9 H8   H N N 21  
A1IB9 H9   H N N 22  
ALA   N    N N N 23  
ALA   CA   C N S 24  
ALA   C    C N N 25  
ALA   O    O N N 26  
ALA   CB   C N N 27  
ALA   OXT  O N N 28  
ALA   H    H N N 29  
ALA   H2   H N N 30  
ALA   HA   H N N 31  
ALA   HB1  H N N 32  
ALA   HB2  H N N 33  
ALA   HB3  H N N 34  
ALA   HXT  H N N 35  
ARG   N    N N N 36  
ARG   CA   C N S 37  
ARG   C    C N N 38  
ARG   O    O N N 39  
ARG   CB   C N N 40  
ARG   CG   C N N 41  
ARG   CD   C N N 42  
ARG   NE   N N N 43  
ARG   CZ   C N N 44  
ARG   NH1  N N N 45  
ARG   NH2  N N N 46  
ARG   OXT  O N N 47  
ARG   H    H N N 48  
ARG   H2   H N N 49  
ARG   HA   H N N 50  
ARG   HB2  H N N 51  
ARG   HB3  H N N 52  
ARG   HG2  H N N 53  
ARG   HG3  H N N 54  
ARG   HD2  H N N 55  
ARG   HD3  H N N 56  
ARG   HE   H N N 57  
ARG   HH11 H N N 58  
ARG   HH12 H N N 59  
ARG   HH21 H N N 60  
ARG   HH22 H N N 61  
ARG   HXT  H N N 62  
ASN   N    N N N 63  
ASN   CA   C N S 64  
ASN   C    C N N 65  
ASN   O    O N N 66  
ASN   CB   C N N 67  
ASN   CG   C N N 68  
ASN   OD1  O N N 69  
ASN   ND2  N N N 70  
ASN   OXT  O N N 71  
ASN   H    H N N 72  
ASN   H2   H N N 73  
ASN   HA   H N N 74  
ASN   HB2  H N N 75  
ASN   HB3  H N N 76  
ASN   HD21 H N N 77  
ASN   HD22 H N N 78  
ASN   HXT  H N N 79  
ASP   N    N N N 80  
ASP   CA   C N S 81  
ASP   C    C N N 82  
ASP   O    O N N 83  
ASP   CB   C N N 84  
ASP   CG   C N N 85  
ASP   OD1  O N N 86  
ASP   OD2  O N N 87  
ASP   OXT  O N N 88  
ASP   H    H N N 89  
ASP   H2   H N N 90  
ASP   HA   H N N 91  
ASP   HB2  H N N 92  
ASP   HB3  H N N 93  
ASP   HD2  H N N 94  
ASP   HXT  H N N 95  
CYS   N    N N N 96  
CYS   CA   C N R 97  
CYS   C    C N N 98  
CYS   O    O N N 99  
CYS   CB   C N N 100 
CYS   SG   S N N 101 
CYS   OXT  O N N 102 
CYS   H    H N N 103 
CYS   H2   H N N 104 
CYS   HA   H N N 105 
CYS   HB2  H N N 106 
CYS   HB3  H N N 107 
CYS   HG   H N N 108 
CYS   HXT  H N N 109 
GLN   N    N N N 110 
GLN   CA   C N S 111 
GLN   C    C N N 112 
GLN   O    O N N 113 
GLN   CB   C N N 114 
GLN   CG   C N N 115 
GLN   CD   C N N 116 
GLN   OE1  O N N 117 
GLN   NE2  N N N 118 
GLN   OXT  O N N 119 
GLN   H    H N N 120 
GLN   H2   H N N 121 
GLN   HA   H N N 122 
GLN   HB2  H N N 123 
GLN   HB3  H N N 124 
GLN   HG2  H N N 125 
GLN   HG3  H N N 126 
GLN   HE21 H N N 127 
GLN   HE22 H N N 128 
GLN   HXT  H N N 129 
GLU   N    N N N 130 
GLU   CA   C N S 131 
GLU   C    C N N 132 
GLU   O    O N N 133 
GLU   CB   C N N 134 
GLU   CG   C N N 135 
GLU   CD   C N N 136 
GLU   OE1  O N N 137 
GLU   OE2  O N N 138 
GLU   OXT  O N N 139 
GLU   H    H N N 140 
GLU   H2   H N N 141 
GLU   HA   H N N 142 
GLU   HB2  H N N 143 
GLU   HB3  H N N 144 
GLU   HG2  H N N 145 
GLU   HG3  H N N 146 
GLU   HE2  H N N 147 
GLU   HXT  H N N 148 
GLY   N    N N N 149 
GLY   CA   C N N 150 
GLY   C    C N N 151 
GLY   O    O N N 152 
GLY   OXT  O N N 153 
GLY   H    H N N 154 
GLY   H2   H N N 155 
GLY   HA2  H N N 156 
GLY   HA3  H N N 157 
GLY   HXT  H N N 158 
GOL   C1   C N N 159 
GOL   O1   O N N 160 
GOL   C2   C N N 161 
GOL   O2   O N N 162 
GOL   C3   C N N 163 
GOL   O3   O N N 164 
GOL   H11  H N N 165 
GOL   H12  H N N 166 
GOL   HO1  H N N 167 
GOL   H2   H N N 168 
GOL   HO2  H N N 169 
GOL   H31  H N N 170 
GOL   H32  H N N 171 
GOL   HO3  H N N 172 
HIS   N    N N N 173 
HIS   CA   C N S 174 
HIS   C    C N N 175 
HIS   O    O N N 176 
HIS   CB   C N N 177 
HIS   CG   C Y N 178 
HIS   ND1  N Y N 179 
HIS   CD2  C Y N 180 
HIS   CE1  C Y N 181 
HIS   NE2  N Y N 182 
HIS   OXT  O N N 183 
HIS   H    H N N 184 
HIS   H2   H N N 185 
HIS   HA   H N N 186 
HIS   HB2  H N N 187 
HIS   HB3  H N N 188 
HIS   HD1  H N N 189 
HIS   HD2  H N N 190 
HIS   HE1  H N N 191 
HIS   HE2  H N N 192 
HIS   HXT  H N N 193 
HOH   O    O N N 194 
HOH   H1   H N N 195 
HOH   H2   H N N 196 
ILE   N    N N N 197 
ILE   CA   C N S 198 
ILE   C    C N N 199 
ILE   O    O N N 200 
ILE   CB   C N S 201 
ILE   CG1  C N N 202 
ILE   CG2  C N N 203 
ILE   CD1  C N N 204 
ILE   OXT  O N N 205 
ILE   H    H N N 206 
ILE   H2   H N N 207 
ILE   HA   H N N 208 
ILE   HB   H N N 209 
ILE   HG12 H N N 210 
ILE   HG13 H N N 211 
ILE   HG21 H N N 212 
ILE   HG22 H N N 213 
ILE   HG23 H N N 214 
ILE   HD11 H N N 215 
ILE   HD12 H N N 216 
ILE   HD13 H N N 217 
ILE   HXT  H N N 218 
LEU   N    N N N 219 
LEU   CA   C N S 220 
LEU   C    C N N 221 
LEU   O    O N N 222 
LEU   CB   C N N 223 
LEU   CG   C N N 224 
LEU   CD1  C N N 225 
LEU   CD2  C N N 226 
LEU   OXT  O N N 227 
LEU   H    H N N 228 
LEU   H2   H N N 229 
LEU   HA   H N N 230 
LEU   HB2  H N N 231 
LEU   HB3  H N N 232 
LEU   HG   H N N 233 
LEU   HD11 H N N 234 
LEU   HD12 H N N 235 
LEU   HD13 H N N 236 
LEU   HD21 H N N 237 
LEU   HD22 H N N 238 
LEU   HD23 H N N 239 
LEU   HXT  H N N 240 
LYS   N    N N N 241 
LYS   CA   C N S 242 
LYS   C    C N N 243 
LYS   O    O N N 244 
LYS   CB   C N N 245 
LYS   CG   C N N 246 
LYS   CD   C N N 247 
LYS   CE   C N N 248 
LYS   NZ   N N N 249 
LYS   OXT  O N N 250 
LYS   H    H N N 251 
LYS   H2   H N N 252 
LYS   HA   H N N 253 
LYS   HB2  H N N 254 
LYS   HB3  H N N 255 
LYS   HG2  H N N 256 
LYS   HG3  H N N 257 
LYS   HD2  H N N 258 
LYS   HD3  H N N 259 
LYS   HE2  H N N 260 
LYS   HE3  H N N 261 
LYS   HZ1  H N N 262 
LYS   HZ2  H N N 263 
LYS   HZ3  H N N 264 
LYS   HXT  H N N 265 
MET   N    N N N 266 
MET   CA   C N S 267 
MET   C    C N N 268 
MET   O    O N N 269 
MET   CB   C N N 270 
MET   CG   C N N 271 
MET   SD   S N N 272 
MET   CE   C N N 273 
MET   OXT  O N N 274 
MET   H    H N N 275 
MET   H2   H N N 276 
MET   HA   H N N 277 
MET   HB2  H N N 278 
MET   HB3  H N N 279 
MET   HG2  H N N 280 
MET   HG3  H N N 281 
MET   HE1  H N N 282 
MET   HE2  H N N 283 
MET   HE3  H N N 284 
MET   HXT  H N N 285 
PHE   N    N N N 286 
PHE   CA   C N S 287 
PHE   C    C N N 288 
PHE   O    O N N 289 
PHE   CB   C N N 290 
PHE   CG   C Y N 291 
PHE   CD1  C Y N 292 
PHE   CD2  C Y N 293 
PHE   CE1  C Y N 294 
PHE   CE2  C Y N 295 
PHE   CZ   C Y N 296 
PHE   OXT  O N N 297 
PHE   H    H N N 298 
PHE   H2   H N N 299 
PHE   HA   H N N 300 
PHE   HB2  H N N 301 
PHE   HB3  H N N 302 
PHE   HD1  H N N 303 
PHE   HD2  H N N 304 
PHE   HE1  H N N 305 
PHE   HE2  H N N 306 
PHE   HZ   H N N 307 
PHE   HXT  H N N 308 
PRO   N    N N N 309 
PRO   CA   C N S 310 
PRO   C    C N N 311 
PRO   O    O N N 312 
PRO   CB   C N N 313 
PRO   CG   C N N 314 
PRO   CD   C N N 315 
PRO   OXT  O N N 316 
PRO   H    H N N 317 
PRO   HA   H N N 318 
PRO   HB2  H N N 319 
PRO   HB3  H N N 320 
PRO   HG2  H N N 321 
PRO   HG3  H N N 322 
PRO   HD2  H N N 323 
PRO   HD3  H N N 324 
PRO   HXT  H N N 325 
SER   N    N N N 326 
SER   CA   C N S 327 
SER   C    C N N 328 
SER   O    O N N 329 
SER   CB   C N N 330 
SER   OG   O N N 331 
SER   OXT  O N N 332 
SER   H    H N N 333 
SER   H2   H N N 334 
SER   HA   H N N 335 
SER   HB2  H N N 336 
SER   HB3  H N N 337 
SER   HG   H N N 338 
SER   HXT  H N N 339 
THR   N    N N N 340 
THR   CA   C N S 341 
THR   C    C N N 342 
THR   O    O N N 343 
THR   CB   C N R 344 
THR   OG1  O N N 345 
THR   CG2  C N N 346 
THR   OXT  O N N 347 
THR   H    H N N 348 
THR   H2   H N N 349 
THR   HA   H N N 350 
THR   HB   H N N 351 
THR   HG1  H N N 352 
THR   HG21 H N N 353 
THR   HG22 H N N 354 
THR   HG23 H N N 355 
THR   HXT  H N N 356 
TRP   N    N N N 357 
TRP   CA   C N S 358 
TRP   C    C N N 359 
TRP   O    O N N 360 
TRP   CB   C N N 361 
TRP   CG   C Y N 362 
TRP   CD1  C Y N 363 
TRP   CD2  C Y N 364 
TRP   NE1  N Y N 365 
TRP   CE2  C Y N 366 
TRP   CE3  C Y N 367 
TRP   CZ2  C Y N 368 
TRP   CZ3  C Y N 369 
TRP   CH2  C Y N 370 
TRP   OXT  O N N 371 
TRP   H    H N N 372 
TRP   H2   H N N 373 
TRP   HA   H N N 374 
TRP   HB2  H N N 375 
TRP   HB3  H N N 376 
TRP   HD1  H N N 377 
TRP   HE1  H N N 378 
TRP   HE3  H N N 379 
TRP   HZ2  H N N 380 
TRP   HZ3  H N N 381 
TRP   HH2  H N N 382 
TRP   HXT  H N N 383 
TYR   N    N N N 384 
TYR   CA   C N S 385 
TYR   C    C N N 386 
TYR   O    O N N 387 
TYR   CB   C N N 388 
TYR   CG   C Y N 389 
TYR   CD1  C Y N 390 
TYR   CD2  C Y N 391 
TYR   CE1  C Y N 392 
TYR   CE2  C Y N 393 
TYR   CZ   C Y N 394 
TYR   OH   O N N 395 
TYR   OXT  O N N 396 
TYR   H    H N N 397 
TYR   H2   H N N 398 
TYR   HA   H N N 399 
TYR   HB2  H N N 400 
TYR   HB3  H N N 401 
TYR   HD1  H N N 402 
TYR   HD2  H N N 403 
TYR   HE1  H N N 404 
TYR   HE2  H N N 405 
TYR   HH   H N N 406 
TYR   HXT  H N N 407 
VAL   N    N N N 408 
VAL   CA   C N S 409 
VAL   C    C N N 410 
VAL   O    O N N 411 
VAL   CB   C N N 412 
VAL   CG1  C N N 413 
VAL   CG2  C N N 414 
VAL   OXT  O N N 415 
VAL   H    H N N 416 
VAL   H2   H N N 417 
VAL   HA   H N N 418 
VAL   HB   H N N 419 
VAL   HG11 H N N 420 
VAL   HG12 H N N 421 
VAL   HG13 H N N 422 
VAL   HG21 H N N 423 
VAL   HG22 H N N 424 
VAL   HG23 H N N 425 
VAL   HXT  H N N 426 
# 
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 
A1IB9 O3  N1   doub N N 1   
A1IB9 O2  N1   doub N N 2   
A1IB9 N1  C7   sing N N 3   
A1IB9 C7  C6   doub Y N 4   
A1IB9 C7  C8   sing Y N 5   
A1IB9 C6  C5   sing Y N 6   
A1IB9 C8  C9   doub Y N 7   
A1IB9 C5  C4   doub Y N 8   
A1IB9 C9  C4   sing Y N 9   
A1IB9 C4  C3   sing N N 10  
A1IB9 C3  C2   doub N E 11  
A1IB9 C2  C1   sing N N 12  
A1IB9 C1  O1   sing N N 13  
A1IB9 C1  H1   sing N N 14  
A1IB9 C1  H2   sing N N 15  
A1IB9 C2  H3   sing N N 16  
A1IB9 C3  H4   sing N N 17  
A1IB9 C5  H5   sing N N 18  
A1IB9 C6  H6   sing N N 19  
A1IB9 C8  H7   sing N N 20  
A1IB9 C9  H8   sing N N 21  
A1IB9 O1  H9   sing N N 22  
ALA   N   CA   sing N N 23  
ALA   N   H    sing N N 24  
ALA   N   H2   sing N N 25  
ALA   CA  C    sing N N 26  
ALA   CA  CB   sing N N 27  
ALA   CA  HA   sing N N 28  
ALA   C   O    doub N N 29  
ALA   C   OXT  sing N N 30  
ALA   CB  HB1  sing N N 31  
ALA   CB  HB2  sing N N 32  
ALA   CB  HB3  sing N N 33  
ALA   OXT HXT  sing N N 34  
ARG   N   CA   sing N N 35  
ARG   N   H    sing N N 36  
ARG   N   H2   sing N N 37  
ARG   CA  C    sing N N 38  
ARG   CA  CB   sing N N 39  
ARG   CA  HA   sing N N 40  
ARG   C   O    doub N N 41  
ARG   C   OXT  sing N N 42  
ARG   CB  CG   sing N N 43  
ARG   CB  HB2  sing N N 44  
ARG   CB  HB3  sing N N 45  
ARG   CG  CD   sing N N 46  
ARG   CG  HG2  sing N N 47  
ARG   CG  HG3  sing N N 48  
ARG   CD  NE   sing N N 49  
ARG   CD  HD2  sing N N 50  
ARG   CD  HD3  sing N N 51  
ARG   NE  CZ   sing N N 52  
ARG   NE  HE   sing N N 53  
ARG   CZ  NH1  sing N N 54  
ARG   CZ  NH2  doub N N 55  
ARG   NH1 HH11 sing N N 56  
ARG   NH1 HH12 sing N N 57  
ARG   NH2 HH21 sing N N 58  
ARG   NH2 HH22 sing N N 59  
ARG   OXT HXT  sing N N 60  
ASN   N   CA   sing N N 61  
ASN   N   H    sing N N 62  
ASN   N   H2   sing N N 63  
ASN   CA  C    sing N N 64  
ASN   CA  CB   sing N N 65  
ASN   CA  HA   sing N N 66  
ASN   C   O    doub N N 67  
ASN   C   OXT  sing N N 68  
ASN   CB  CG   sing N N 69  
ASN   CB  HB2  sing N N 70  
ASN   CB  HB3  sing N N 71  
ASN   CG  OD1  doub N N 72  
ASN   CG  ND2  sing N N 73  
ASN   ND2 HD21 sing N N 74  
ASN   ND2 HD22 sing N N 75  
ASN   OXT HXT  sing N N 76  
ASP   N   CA   sing N N 77  
ASP   N   H    sing N N 78  
ASP   N   H2   sing N N 79  
ASP   CA  C    sing N N 80  
ASP   CA  CB   sing N N 81  
ASP   CA  HA   sing N N 82  
ASP   C   O    doub N N 83  
ASP   C   OXT  sing N N 84  
ASP   CB  CG   sing N N 85  
ASP   CB  HB2  sing N N 86  
ASP   CB  HB3  sing N N 87  
ASP   CG  OD1  doub N N 88  
ASP   CG  OD2  sing N N 89  
ASP   OD2 HD2  sing N N 90  
ASP   OXT HXT  sing N N 91  
CYS   N   CA   sing N N 92  
CYS   N   H    sing N N 93  
CYS   N   H2   sing N N 94  
CYS   CA  C    sing N N 95  
CYS   CA  CB   sing N N 96  
CYS   CA  HA   sing N N 97  
CYS   C   O    doub N N 98  
CYS   C   OXT  sing N N 99  
CYS   CB  SG   sing N N 100 
CYS   CB  HB2  sing N N 101 
CYS   CB  HB3  sing N N 102 
CYS   SG  HG   sing N N 103 
CYS   OXT HXT  sing N N 104 
GLN   N   CA   sing N N 105 
GLN   N   H    sing N N 106 
GLN   N   H2   sing N N 107 
GLN   CA  C    sing N N 108 
GLN   CA  CB   sing N N 109 
GLN   CA  HA   sing N N 110 
GLN   C   O    doub N N 111 
GLN   C   OXT  sing N N 112 
GLN   CB  CG   sing N N 113 
GLN   CB  HB2  sing N N 114 
GLN   CB  HB3  sing N N 115 
GLN   CG  CD   sing N N 116 
GLN   CG  HG2  sing N N 117 
GLN   CG  HG3  sing N N 118 
GLN   CD  OE1  doub N N 119 
GLN   CD  NE2  sing N N 120 
GLN   NE2 HE21 sing N N 121 
GLN   NE2 HE22 sing N N 122 
GLN   OXT HXT  sing N N 123 
GLU   N   CA   sing N N 124 
GLU   N   H    sing N N 125 
GLU   N   H2   sing N N 126 
GLU   CA  C    sing N N 127 
GLU   CA  CB   sing N N 128 
GLU   CA  HA   sing N N 129 
GLU   C   O    doub N N 130 
GLU   C   OXT  sing N N 131 
GLU   CB  CG   sing N N 132 
GLU   CB  HB2  sing N N 133 
GLU   CB  HB3  sing N N 134 
GLU   CG  CD   sing N N 135 
GLU   CG  HG2  sing N N 136 
GLU   CG  HG3  sing N N 137 
GLU   CD  OE1  doub N N 138 
GLU   CD  OE2  sing N N 139 
GLU   OE2 HE2  sing N N 140 
GLU   OXT HXT  sing N N 141 
GLY   N   CA   sing N N 142 
GLY   N   H    sing N N 143 
GLY   N   H2   sing N N 144 
GLY   CA  C    sing N N 145 
GLY   CA  HA2  sing N N 146 
GLY   CA  HA3  sing N N 147 
GLY   C   O    doub N N 148 
GLY   C   OXT  sing N N 149 
GLY   OXT HXT  sing N N 150 
GOL   C1  O1   sing N N 151 
GOL   C1  C2   sing N N 152 
GOL   C1  H11  sing N N 153 
GOL   C1  H12  sing N N 154 
GOL   O1  HO1  sing N N 155 
GOL   C2  O2   sing N N 156 
GOL   C2  C3   sing N N 157 
GOL   C2  H2   sing N N 158 
GOL   O2  HO2  sing N N 159 
GOL   C3  O3   sing N N 160 
GOL   C3  H31  sing N N 161 
GOL   C3  H32  sing N N 162 
GOL   O3  HO3  sing N N 163 
HIS   N   CA   sing N N 164 
HIS   N   H    sing N N 165 
HIS   N   H2   sing N N 166 
HIS   CA  C    sing N N 167 
HIS   CA  CB   sing N N 168 
HIS   CA  HA   sing N N 169 
HIS   C   O    doub N N 170 
HIS   C   OXT  sing N N 171 
HIS   CB  CG   sing N N 172 
HIS   CB  HB2  sing N N 173 
HIS   CB  HB3  sing N N 174 
HIS   CG  ND1  sing Y N 175 
HIS   CG  CD2  doub Y N 176 
HIS   ND1 CE1  doub Y N 177 
HIS   ND1 HD1  sing N N 178 
HIS   CD2 NE2  sing Y N 179 
HIS   CD2 HD2  sing N N 180 
HIS   CE1 NE2  sing Y N 181 
HIS   CE1 HE1  sing N N 182 
HIS   NE2 HE2  sing N N 183 
HIS   OXT HXT  sing N N 184 
HOH   O   H1   sing N N 185 
HOH   O   H2   sing N N 186 
ILE   N   CA   sing N N 187 
ILE   N   H    sing N N 188 
ILE   N   H2   sing N N 189 
ILE   CA  C    sing N N 190 
ILE   CA  CB   sing N N 191 
ILE   CA  HA   sing N N 192 
ILE   C   O    doub N N 193 
ILE   C   OXT  sing N N 194 
ILE   CB  CG1  sing N N 195 
ILE   CB  CG2  sing N N 196 
ILE   CB  HB   sing N N 197 
ILE   CG1 CD1  sing N N 198 
ILE   CG1 HG12 sing N N 199 
ILE   CG1 HG13 sing N N 200 
ILE   CG2 HG21 sing N N 201 
ILE   CG2 HG22 sing N N 202 
ILE   CG2 HG23 sing N N 203 
ILE   CD1 HD11 sing N N 204 
ILE   CD1 HD12 sing N N 205 
ILE   CD1 HD13 sing N N 206 
ILE   OXT HXT  sing N N 207 
LEU   N   CA   sing N N 208 
LEU   N   H    sing N N 209 
LEU   N   H2   sing N N 210 
LEU   CA  C    sing N N 211 
LEU   CA  CB   sing N N 212 
LEU   CA  HA   sing N N 213 
LEU   C   O    doub N N 214 
LEU   C   OXT  sing N N 215 
LEU   CB  CG   sing N N 216 
LEU   CB  HB2  sing N N 217 
LEU   CB  HB3  sing N N 218 
LEU   CG  CD1  sing N N 219 
LEU   CG  CD2  sing N N 220 
LEU   CG  HG   sing N N 221 
LEU   CD1 HD11 sing N N 222 
LEU   CD1 HD12 sing N N 223 
LEU   CD1 HD13 sing N N 224 
LEU   CD2 HD21 sing N N 225 
LEU   CD2 HD22 sing N N 226 
LEU   CD2 HD23 sing N N 227 
LEU   OXT HXT  sing N N 228 
LYS   N   CA   sing N N 229 
LYS   N   H    sing N N 230 
LYS   N   H2   sing N N 231 
LYS   CA  C    sing N N 232 
LYS   CA  CB   sing N N 233 
LYS   CA  HA   sing N N 234 
LYS   C   O    doub N N 235 
LYS   C   OXT  sing N N 236 
LYS   CB  CG   sing N N 237 
LYS   CB  HB2  sing N N 238 
LYS   CB  HB3  sing N N 239 
LYS   CG  CD   sing N N 240 
LYS   CG  HG2  sing N N 241 
LYS   CG  HG3  sing N N 242 
LYS   CD  CE   sing N N 243 
LYS   CD  HD2  sing N N 244 
LYS   CD  HD3  sing N N 245 
LYS   CE  NZ   sing N N 246 
LYS   CE  HE2  sing N N 247 
LYS   CE  HE3  sing N N 248 
LYS   NZ  HZ1  sing N N 249 
LYS   NZ  HZ2  sing N N 250 
LYS   NZ  HZ3  sing N N 251 
LYS   OXT HXT  sing N N 252 
MET   N   CA   sing N N 253 
MET   N   H    sing N N 254 
MET   N   H2   sing N N 255 
MET   CA  C    sing N N 256 
MET   CA  CB   sing N N 257 
MET   CA  HA   sing N N 258 
MET   C   O    doub N N 259 
MET   C   OXT  sing N N 260 
MET   CB  CG   sing N N 261 
MET   CB  HB2  sing N N 262 
MET   CB  HB3  sing N N 263 
MET   CG  SD   sing N N 264 
MET   CG  HG2  sing N N 265 
MET   CG  HG3  sing N N 266 
MET   SD  CE   sing N N 267 
MET   CE  HE1  sing N N 268 
MET   CE  HE2  sing N N 269 
MET   CE  HE3  sing N N 270 
MET   OXT HXT  sing N N 271 
PHE   N   CA   sing N N 272 
PHE   N   H    sing N N 273 
PHE   N   H2   sing N N 274 
PHE   CA  C    sing N N 275 
PHE   CA  CB   sing N N 276 
PHE   CA  HA   sing N N 277 
PHE   C   O    doub N N 278 
PHE   C   OXT  sing N N 279 
PHE   CB  CG   sing N N 280 
PHE   CB  HB2  sing N N 281 
PHE   CB  HB3  sing N N 282 
PHE   CG  CD1  doub Y N 283 
PHE   CG  CD2  sing Y N 284 
PHE   CD1 CE1  sing Y N 285 
PHE   CD1 HD1  sing N N 286 
PHE   CD2 CE2  doub Y N 287 
PHE   CD2 HD2  sing N N 288 
PHE   CE1 CZ   doub Y N 289 
PHE   CE1 HE1  sing N N 290 
PHE   CE2 CZ   sing Y N 291 
PHE   CE2 HE2  sing N N 292 
PHE   CZ  HZ   sing N N 293 
PHE   OXT HXT  sing N N 294 
PRO   N   CA   sing N N 295 
PRO   N   CD   sing N N 296 
PRO   N   H    sing N N 297 
PRO   CA  C    sing N N 298 
PRO   CA  CB   sing N N 299 
PRO   CA  HA   sing N N 300 
PRO   C   O    doub N N 301 
PRO   C   OXT  sing N N 302 
PRO   CB  CG   sing N N 303 
PRO   CB  HB2  sing N N 304 
PRO   CB  HB3  sing N N 305 
PRO   CG  CD   sing N N 306 
PRO   CG  HG2  sing N N 307 
PRO   CG  HG3  sing N N 308 
PRO   CD  HD2  sing N N 309 
PRO   CD  HD3  sing N N 310 
PRO   OXT HXT  sing N N 311 
SER   N   CA   sing N N 312 
SER   N   H    sing N N 313 
SER   N   H2   sing N N 314 
SER   CA  C    sing N N 315 
SER   CA  CB   sing N N 316 
SER   CA  HA   sing N N 317 
SER   C   O    doub N N 318 
SER   C   OXT  sing N N 319 
SER   CB  OG   sing N N 320 
SER   CB  HB2  sing N N 321 
SER   CB  HB3  sing N N 322 
SER   OG  HG   sing N N 323 
SER   OXT HXT  sing N N 324 
THR   N   CA   sing N N 325 
THR   N   H    sing N N 326 
THR   N   H2   sing N N 327 
THR   CA  C    sing N N 328 
THR   CA  CB   sing N N 329 
THR   CA  HA   sing N N 330 
THR   C   O    doub N N 331 
THR   C   OXT  sing N N 332 
THR   CB  OG1  sing N N 333 
THR   CB  CG2  sing N N 334 
THR   CB  HB   sing N N 335 
THR   OG1 HG1  sing N N 336 
THR   CG2 HG21 sing N N 337 
THR   CG2 HG22 sing N N 338 
THR   CG2 HG23 sing N N 339 
THR   OXT HXT  sing N N 340 
TRP   N   CA   sing N N 341 
TRP   N   H    sing N N 342 
TRP   N   H2   sing N N 343 
TRP   CA  C    sing N N 344 
TRP   CA  CB   sing N N 345 
TRP   CA  HA   sing N N 346 
TRP   C   O    doub N N 347 
TRP   C   OXT  sing N N 348 
TRP   CB  CG   sing N N 349 
TRP   CB  HB2  sing N N 350 
TRP   CB  HB3  sing N N 351 
TRP   CG  CD1  doub Y N 352 
TRP   CG  CD2  sing Y N 353 
TRP   CD1 NE1  sing Y N 354 
TRP   CD1 HD1  sing N N 355 
TRP   CD2 CE2  doub Y N 356 
TRP   CD2 CE3  sing Y N 357 
TRP   NE1 CE2  sing Y N 358 
TRP   NE1 HE1  sing N N 359 
TRP   CE2 CZ2  sing Y N 360 
TRP   CE3 CZ3  doub Y N 361 
TRP   CE3 HE3  sing N N 362 
TRP   CZ2 CH2  doub Y N 363 
TRP   CZ2 HZ2  sing N N 364 
TRP   CZ3 CH2  sing Y N 365 
TRP   CZ3 HZ3  sing N N 366 
TRP   CH2 HH2  sing N N 367 
TRP   OXT HXT  sing N N 368 
TYR   N   CA   sing N N 369 
TYR   N   H    sing N N 370 
TYR   N   H2   sing N N 371 
TYR   CA  C    sing N N 372 
TYR   CA  CB   sing N N 373 
TYR   CA  HA   sing N N 374 
TYR   C   O    doub N N 375 
TYR   C   OXT  sing N N 376 
TYR   CB  CG   sing N N 377 
TYR   CB  HB2  sing N N 378 
TYR   CB  HB3  sing N N 379 
TYR   CG  CD1  doub Y N 380 
TYR   CG  CD2  sing Y N 381 
TYR   CD1 CE1  sing Y N 382 
TYR   CD1 HD1  sing N N 383 
TYR   CD2 CE2  doub Y N 384 
TYR   CD2 HD2  sing N N 385 
TYR   CE1 CZ   doub Y N 386 
TYR   CE1 HE1  sing N N 387 
TYR   CE2 CZ   sing Y N 388 
TYR   CE2 HE2  sing N N 389 
TYR   CZ  OH   sing N N 390 
TYR   OH  HH   sing N N 391 
TYR   OXT HXT  sing N N 392 
VAL   N   CA   sing N N 393 
VAL   N   H    sing N N 394 
VAL   N   H2   sing N N 395 
VAL   CA  C    sing N N 396 
VAL   CA  CB   sing N N 397 
VAL   CA  HA   sing N N 398 
VAL   C   O    doub N N 399 
VAL   C   OXT  sing N N 400 
VAL   CB  CG1  sing N N 401 
VAL   CB  CG2  sing N N 402 
VAL   CB  HB   sing N N 403 
VAL   CG1 HG11 sing N N 404 
VAL   CG1 HG12 sing N N 405 
VAL   CG1 HG13 sing N N 406 
VAL   CG2 HG21 sing N N 407 
VAL   CG2 HG22 sing N N 408 
VAL   CG2 HG23 sing N N 409 
VAL   OXT HXT  sing N N 410 
# 
_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 initial model' 
# 
_atom_sites.entry_id                    9FD9 
_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]   0.020792 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002284 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013787 
_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]   0.014232 
_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 
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   . ASP   A 1 3   ? 19.669  4.238   15.821  1.00 45.73 ?  3   ASP   A N   1 
ATOM   2    C CA  . ASP   A 1 3   ? 20.809  4.127   14.870  1.00 41.96 ?  3   ASP   A CA  1 
ATOM   3    C C   . ASP   A 1 3   ? 20.226  3.956   13.468  1.00 34.47 ?  3   ASP   A C   1 
ATOM   4    O O   . ASP   A 1 3   ? 19.835  2.858   13.046  1.00 28.95 ?  3   ASP   A O   1 
ATOM   5    C CB  . ASP   A 1 3   ? 21.790  3.055   15.318  1.00 44.95 ?  3   ASP   A CB  1 
ATOM   6    C CG  . ASP   A 1 3   ? 22.937  2.749   14.361  1.00 48.83 ?  3   ASP   A CG  1 
ATOM   7    O OD1 . ASP   A 1 3   ? 22.936  3.261   13.214  1.00 47.53 ?  3   ASP   A OD1 1 
ATOM   8    O OD2 . ASP   A 1 3   ? 23.834  1.993   14.770  1.00 53.86 ?  3   ASP   A OD2 1 
ATOM   9    N N   . LEU   A 1 4   ? 20.145  5.082   12.766  1.00 31.41 ?  4   LEU   A N   1 
ATOM   10   C CA  . LEU   A 1 4   ? 19.541  5.116   11.445  1.00 32.21 ?  4   LEU   A CA  1 
ATOM   11   C C   . LEU   A 1 4   ? 20.308  4.252   10.446  1.00 29.92 ?  4   LEU   A C   1 
ATOM   12   O O   . LEU   A 1 4   ? 19.719  3.658   9.545   1.00 28.48 ?  4   LEU   A O   1 
ATOM   13   C CB  . LEU   A 1 4   ? 19.454  6.560   10.962  1.00 34.31 ?  4   LEU   A CB  1 
ATOM   14   C CG  . LEU   A 1 4   ? 18.543  6.813   9.763   1.00 33.82 ?  4   LEU   A CG  1 
ATOM   15   C CD1 . LEU   A 1 4   ? 17.158  6.191   9.949   1.00 31.82 ?  4   LEU   A CD1 1 
ATOM   16   C CD2 . LEU   A 1 4   ? 18.428  8.312   9.513   1.00 36.11 ?  4   LEU   A CD2 1 
ATOM   17   N N   . LYS   A 1 5   ? 21.637  4.192   10.559  1.00 29.19 ?  5   LYS   A N   1 
ATOM   18   C CA  . LYS   A 1 5   ? 22.401  3.401   9.609   1.00 27.15 ?  5   LYS   A CA  1 
ATOM   19   C C   . LYS   A 1 5   ? 22.076  1.924   9.788   1.00 26.46 ?  5   LYS   A C   1 
ATOM   20   O O   . LYS   A 1 5   ? 21.883  1.200   8.808   1.00 24.38 ?  5   LYS   A O   1 
ATOM   21   C CB  . LYS   A 1 5   ? 23.910  3.621   9.753   1.00 32.72 ?  5   LYS   A CB  1 
ATOM   22   C CG  . LYS   A 1 5   ? 24.410  4.896   9.058   1.00 37.67 ?  5   LYS   A CG  1 
ATOM   23   C CD  . LYS   A 1 5   ? 25.902  5.127   9.254   1.00 43.08 ?  5   LYS   A CD  1 
ATOM   24   C CE  . LYS   A 1 5   ? 26.316  6.533   8.986   1.00 48.71 ?  5   LYS   A CE  1 
ATOM   25   N NZ  . LYS   A 1 5   ? 26.503  6.760   7.553   1.00 52.60 ?  5   LYS   A NZ  1 
ATOM   26   N N   . ALA   A 1 6   ? 21.991  1.501   11.048  1.00 25.72 ?  6   ALA   A N   1 
ATOM   27   C CA  . ALA   A 1 6   ? 21.722  0.114   11.370  1.00 24.72 ?  6   ALA   A CA  1 
ATOM   28   C C   . ALA   A 1 6   ? 20.315  -0.285  10.907  1.00 23.84 ?  6   ALA   A C   1 
ATOM   29   O O   . ALA   A 1 6   ? 20.121  -1.399  10.421  1.00 23.34 ?  6   ALA   A O   1 
ATOM   30   C CB  . ALA   A 1 6   ? 21.915  -0.065  12.857  1.00 28.10 ?  6   ALA   A CB  1 
ATOM   31   N N   . SER   A 1 7   ? 19.326  0.611   11.092  1.00 22.62 ?  7   SER   A N   1 
ATOM   32   C CA  . SER   A 1 7   ? 17.975  0.287   10.656  1.00 24.27 ?  7   SER   A CA  1 
ATOM   33   C C   . SER   A 1 7   ? 17.887  0.298   9.138   1.00 21.30 ?  7   SER   A C   1 
ATOM   34   O O   . SER   A 1 7   ? 17.134  -0.498  8.598   1.00 20.08 ?  7   SER   A O   1 
ATOM   35   C CB  . SER   A 1 7   ? 16.918  1.148   11.236  1.00 24.47 ?  7   SER   A CB  1 
ATOM   36   O OG  . SER   A 1 7   ? 17.267  2.506   11.137  1.00 29.77 ?  7   SER   A OG  1 
ATOM   37   N N   . SER   A 1 8   ? 18.629  1.193   8.496   1.00 20.94 ?  8   SER   A N   1 
ATOM   38   C CA  . SER   A 1 8   ? 18.578  1.302   7.049   1.00 19.16 ?  8   SER   A CA  1 
ATOM   39   C C   . SER   A 1 8   ? 19.144  0.065   6.364   1.00 18.89 ?  8   SER   A C   1 
ATOM   40   O O   . SER   A 1 8   ? 18.614  -0.417  5.360   1.00 18.07 ?  8   SER   A O   1 
ATOM   41   C CB  . SER   A 1 8   ? 19.292  2.531   6.615   1.00 20.86 ?  8   SER   A CB  1 
ATOM   42   O OG  . SER   A 1 8   ? 18.627  3.669   7.143   1.00 24.08 ?  8   SER   A OG  1 
ATOM   43   N N   . LEU   A 1 9   ? 20.272  -0.424  6.866   1.00 18.99 ?  9   LEU   A N   1 
ATOM   44   C CA  . LEU   A 1 9   ? 20.817  -1.671  6.386   1.00 19.99 ?  9   LEU   A CA  1 
ATOM   45   C C   . LEU   A 1 9   ? 19.840  -2.819  6.583   1.00 18.51 ?  9   LEU   A C   1 
ATOM   46   O O   . LEU   A 1 9   ? 19.658  -3.648  5.700   1.00 18.14 ?  9   LEU   A O   1 
ATOM   47   C CB  . LEU   A 1 9   ? 22.126  -1.965  7.117   1.00 22.63 ?  9   LEU   A CB  1 
ATOM   48   C CG  . LEU   A 1 9   ? 22.896  -3.169  6.583   1.00 24.65 ?  9   LEU   A CG  1 
ATOM   49   C CD1 . LEU   A 1 9   ? 23.213  -3.054  5.093   1.00 25.00 ?  9   LEU   A CD1 1 
ATOM   50   C CD2 . LEU   A 1 9   ? 24.190  -3.297  7.372   1.00 29.18 ?  9   LEU   A CD2 1 
ATOM   51   N N   A ARG   A 1 10  ? 19.206  -2.909  7.762   0.50 18.25 ?  10  ARG   A N   1 
ATOM   52   N N   B ARG   A 1 10  ? 19.218  -2.855  7.756   0.50 18.50 ?  10  ARG   A N   1 
ATOM   53   C CA  A ARG   A 1 10  ? 18.249  -3.985  7.978   0.50 16.99 ?  10  ARG   A CA  1 
ATOM   54   C CA  B ARG   A 1 10  ? 18.259  -3.894  8.066   0.50 17.39 ?  10  ARG   A CA  1 
ATOM   55   C C   A ARG   A 1 10  ? 17.088  -3.857  6.988   0.50 15.96 ?  10  ARG   A C   1 
ATOM   56   C C   B ARG   A 1 10  ? 17.099  -3.840  7.059   0.50 16.15 ?  10  ARG   A C   1 
ATOM   57   O O   A ARG   A 1 10  ? 16.643  -4.860  6.428   0.50 15.53 ?  10  ARG   A O   1 
ATOM   58   O O   B ARG   A 1 10  ? 16.695  -4.872  6.520   0.50 15.62 ?  10  ARG   A O   1 
ATOM   59   C CB  A ARG   A 1 10  ? 17.678  -4.046  9.403   0.50 17.21 ?  10  ARG   A CB  1 
ATOM   60   C CB  B ARG   A 1 10  ? 17.838  -3.705  9.528   0.50 17.95 ?  10  ARG   A CB  1 
ATOM   61   C CG  A ARG   A 1 10  ? 16.462  -4.962  9.516   0.50 17.02 ?  10  ARG   A CG  1 
ATOM   62   C CG  B ARG   A 1 10  ? 17.324  -4.965  10.209  0.50 17.90 ?  10  ARG   A CG  1 
ATOM   63   C CD  A ARG   A 1 10  ? 16.090  -5.544  10.891  0.50 17.53 ?  10  ARG   A CD  1 
ATOM   64   C CD  B ARG   A 1 10  ? 16.603  -4.737  11.537  0.50 18.08 ?  10  ARG   A CD  1 
ATOM   65   N NE  A ARG   A 1 10  ? 15.907  -4.501  11.888  0.50 16.29 ?  10  ARG   A NE  1 
ATOM   66   N NE  B ARG   A 1 10  ? 15.928  -5.991  11.868  0.50 18.19 ?  10  ARG   A NE  1 
ATOM   67   C CZ  A ARG   A 1 10  ? 15.020  -4.515  12.885  0.50 15.65 ?  10  ARG   A CZ  1 
ATOM   68   C CZ  B ARG   A 1 10  ? 15.190  -6.210  12.947  0.50 19.19 ?  10  ARG   A CZ  1 
ATOM   69   N NH1 A ARG   A 1 10  ? 14.364  -5.620  13.204  0.50 15.15 ?  10  ARG   A NH1 1 
ATOM   70   N NH1 B ARG   A 1 10  ? 14.750  -5.194  13.664  0.50 19.76 ?  10  ARG   A NH1 1 
ATOM   71   N NH2 A ARG   A 1 10  ? 14.810  -3.412  13.570  0.50 14.64 ?  10  ARG   A NH2 1 
ATOM   72   N NH2 B ARG   A 1 10  ? 14.867  -7.454  13.279  0.50 18.43 ?  10  ARG   A NH2 1 
ATOM   73   N N   . ALA   A 1 11  ? 16.568  -2.630  6.800   1.00 15.26 ?  11  ALA   A N   1 
ATOM   74   C CA  . ALA   A 1 11  ? 15.415  -2.437  5.929   1.00 14.33 ?  11  ALA   A CA  1 
ATOM   75   C C   . ALA   A 1 11  ? 15.763  -2.790  4.486   1.00 13.77 ?  11  ALA   A C   1 
ATOM   76   O O   . ALA   A 1 11  ? 14.953  -3.407  3.806   1.00 13.44 ?  11  ALA   A O   1 
ATOM   77   C CB  . ALA   A 1 11  ? 14.867  -1.026  6.032   1.00 14.35 ?  11  ALA   A CB  1 
ATOM   78   N N   . LEU   A 1 12  ? 16.971  -2.415  4.053   1.00 14.53 ?  12  LEU   A N   1 
ATOM   79   C CA  . LEU   A 1 12  ? 17.398  -2.688  2.705   1.00 15.04 ?  12  LEU   A CA  1 
ATOM   80   C C   . LEU   A 1 12  ? 17.323  -4.181  2.401   1.00 15.13 ?  12  LEU   A C   1 
ATOM   81   O O   . LEU   A 1 12  ? 16.843  -4.573  1.332   1.00 14.01 ?  12  LEU   A O   1 
ATOM   82   C CB  . LEU   A 1 12  ? 18.787  -2.097  2.453   1.00 16.42 ?  12  LEU   A CB  1 
ATOM   83   C CG  . LEU   A 1 12  ? 19.344  -2.280  1.036   1.00 16.26 ?  12  LEU   A CG  1 
ATOM   84   C CD1 . LEU   A 1 12  ? 20.316  -1.159  0.734   1.00 17.43 ?  12  LEU   A CD1 1 
ATOM   85   C CD2 . LEU   A 1 12  ? 20.059  -3.624  0.877   1.00 16.96 ?  12  LEU   A CD2 1 
ATOM   86   N N   . LYS   A 1 13  ? 17.778  -5.008  3.354   1.00 15.07 ?  13  LYS   A N   1 
ATOM   87   C CA  . LYS   A 1 13  ? 17.845  -6.447  3.186   1.00 15.39 ?  13  LYS   A CA  1 
ATOM   88   C C   . LYS   A 1 13  ? 16.467  -7.089  3.338   1.00 14.36 ?  13  LYS   A C   1 
ATOM   89   O O   . LYS   A 1 13  ? 16.376  -8.298  3.185   1.00 14.73 ?  13  LYS   A O   1 
ATOM   90   C CB  . LYS   A 1 13  ? 18.808  -7.054  4.207   1.00 16.29 ?  13  LYS   A CB  1 
ATOM   91   C CG  . LYS   A 1 13  ? 20.259  -6.735  3.912   1.00 18.39 ?  13  LYS   A CG  1 
ATOM   92   C CD  . LYS   A 1 13  ? 21.268  -7.163  4.982   1.00 21.83 ?  13  LYS   A CD  1 
ATOM   93   C CE  . LYS   A 1 13  ? 22.576  -6.627  4.532   1.00 23.46 ?  13  LYS   A CE  1 
ATOM   94   N NZ  . LYS   A 1 13  ? 23.588  -6.989  5.522   1.00 26.94 ?  13  LYS   A NZ  1 
ATOM   95   N N   . LEU   A 1 14  ? 15.458  -6.271  3.677   1.00 13.75 ?  14  LEU   A N   1 
ATOM   96   C CA  . LEU   A 1 14  ? 14.063  -6.688  3.763   1.00 14.49 ?  14  LEU   A CA  1 
ATOM   97   C C   . LEU   A 1 14  ? 13.246  -6.169  2.578   1.00 14.50 ?  14  LEU   A C   1 
ATOM   98   O O   . LEU   A 1 14  ? 12.022  -6.335  2.555   1.00 13.32 ?  14  LEU   A O   1 
ATOM   99   C CB  . LEU   A 1 14  ? 13.415  -6.255  5.076   1.00 14.41 ?  14  LEU   A CB  1 
ATOM   100  C CG  . LEU   A 1 14  ? 14.124  -6.801  6.327   1.00 15.40 ?  14  LEU   A CG  1 
ATOM   101  C CD1 . LEU   A 1 14  ? 13.545  -6.166  7.575   1.00 14.88 ?  14  LEU   A CD1 1 
ATOM   102  C CD2 . LEU   A 1 14  ? 14.042  -8.338  6.404   1.00 15.34 ?  14  LEU   A CD2 1 
ATOM   103  N N   . MET   A 1 15  ? 13.877  -5.573  1.586   1.00 15.10 ?  15  MET   A N   1 
ATOM   104  C CA  . MET   A 1 15  ? 13.076  -5.015  0.498   1.00 15.15 ?  15  MET   A CA  1 
ATOM   105  C C   . MET   A 1 15  ? 12.692  -6.073  -0.532  1.00 14.64 ?  15  MET   A C   1 
ATOM   106  O O   . MET   A 1 15  ? 13.472  -6.931  -0.914  1.00 15.20 ?  15  MET   A O   1 
ATOM   107  C CB  . MET   A 1 15  ? 13.786  -3.892  -0.269  1.00 16.41 ?  15  MET   A CB  1 
ATOM   108  C CG  . MET   A 1 15  ? 13.753  -2.610  0.523   1.00 18.60 ?  15  MET   A CG  1 
ATOM   109  S SD  . MET   A 1 15  ? 14.304  -1.209  -0.460  1.00 20.46 ?  15  MET   A SD  1 
ATOM   110  C CE  . MET   A 1 15  ? 12.907  -0.959  -1.576  1.00 21.04 ?  15  MET   A CE  1 
ATOM   111  N N   . ASP   A 1 16  ? 11.453  -5.953  -1.005  1.00 14.07 ?  16  ASP   A N   1 
ATOM   112  C CA  . ASP   A 1 16  ? 11.024  -6.484  -2.287  1.00 15.50 ?  16  ASP   A CA  1 
ATOM   113  C C   . ASP   A 1 16  ? 11.095  -5.354  -3.294  1.00 15.92 ?  16  ASP   A C   1 
ATOM   114  O O   . ASP   A 1 16  ? 10.189  -4.537  -3.370  1.00 14.91 ?  16  ASP   A O   1 
ATOM   115  C CB  . ASP   A 1 16  ? 9.600   -7.013  -2.193  1.00 16.22 ?  16  ASP   A CB  1 
ATOM   116  C CG  . ASP   A 1 16  ? 9.378   -8.298  -1.425  1.00 16.10 ?  16  ASP   A CG  1 
ATOM   117  O OD1 . ASP   A 1 16  ? 10.296  -8.756  -0.752  1.00 15.91 ?  16  ASP   A OD1 1 
ATOM   118  O OD2 . ASP   A 1 16  ? 8.237   -8.802  -1.492  1.00 16.84 ?  16  ASP   A OD2 1 
ATOM   119  N N   . LEU   A 1 17  ? 12.212  -5.280  -4.038  1.00 14.04 ?  17  LEU   A N   1 
ATOM   120  C CA  . LEU   A 1 17  ? 12.455  -4.115  -4.861  1.00 15.67 ?  17  LEU   A CA  1 
ATOM   121  C C   . LEU   A 1 17  ? 11.641  -4.229  -6.153  1.00 15.97 ?  17  LEU   A C   1 
ATOM   122  O O   . LEU   A 1 17  ? 11.610  -5.283  -6.791  1.00 16.25 ?  17  LEU   A O   1 
ATOM   123  C CB  . LEU   A 1 17  ? 13.947  -4.043  -5.186  1.00 15.77 ?  17  LEU   A CB  1 
ATOM   124  C CG  . LEU   A 1 17  ? 14.354  -2.746  -5.878  1.00 17.40 ?  17  LEU   A CG  1 
ATOM   125  C CD1 . LEU   A 1 17  ? 14.241  -1.614  -4.862  1.00 17.00 ?  17  LEU   A CD1 1 
ATOM   126  C CD2 . LEU   A 1 17  ? 15.788  -2.873  -6.429  1.00 17.91 ?  17  LEU   A CD2 1 
ATOM   127  N N   . SER   A 1 18  ? 10.938  -3.162  -6.490  1.00 19.24 ?  18  SER   A N   1 
ATOM   128  C CA  . SER   A 1 18  ? 10.102  -3.198  -7.686  1.00 27.83 ?  18  SER   A CA  1 
ATOM   129  C C   . SER   A 1 18  ? 10.321  -1.910  -8.463  1.00 33.73 ?  18  SER   A C   1 
ATOM   130  O O   . SER   A 1 18  ? 10.718  -0.926  -7.853  1.00 34.20 ?  18  SER   A O   1 
ATOM   131  C CB  . SER   A 1 18  ? 8.639   -3.375  -7.355  1.00 32.90 ?  18  SER   A CB  1 
ATOM   132  O OG  . SER   A 1 18  ? 8.198   -2.228  -6.660  1.00 39.05 ?  18  SER   A OG  1 
ATOM   133  N N   . THR   A 1 19  ? 10.068  -1.927  -9.782  1.00 38.28 ?  19  THR   A N   1 
ATOM   134  C CA  . THR   A 1 19  ? 10.326  -0.765  -10.625 1.00 43.53 ?  19  THR   A CA  1 
ATOM   135  C C   . THR   A 1 19  ? 9.513   0.423   -10.143 1.00 47.96 ?  19  THR   A C   1 
ATOM   136  O O   . THR   A 1 19  ? 8.345   0.201   -9.762  1.00 48.74 ?  19  THR   A O   1 
ATOM   137  C CB  . THR   A 1 19  ? 10.020  -1.071  -12.092 1.00 47.73 ?  19  THR   A CB  1 
ATOM   138  O OG1 . THR   A 1 19  ? 8.787   -1.784  -12.135 1.00 49.66 ?  19  THR   A OG1 1 
ATOM   139  C CG2 . THR   A 1 19  ? 11.092  -1.921  -12.740 1.00 44.16 ?  19  THR   A CG2 1 
ATOM   140  N N   . THR   A 1 25  ? 9.543   -3.803  -19.908 1.00 31.88 ?  25  THR   A N   1 
ATOM   141  C CA  . THR   A 1 25  ? 10.522  -4.195  -20.932 1.00 31.10 ?  25  THR   A CA  1 
ATOM   142  C C   . THR   A 1 25  ? 11.598  -5.002  -20.230 1.00 30.27 ?  25  THR   A C   1 
ATOM   143  O O   . THR   A 1 25  ? 11.789  -4.875  -19.021 1.00 25.23 ?  25  THR   A O   1 
ATOM   144  C CB  . THR   A 1 25  ? 11.160  -2.992  -21.625 1.00 31.32 ?  25  THR   A CB  1 
ATOM   145  O OG1 . THR   A 1 25  ? 11.944  -2.272  -20.661 1.00 29.73 ?  25  THR   A OG1 1 
ATOM   146  C CG2 . THR   A 1 25  ? 10.129  -2.096  -22.286 1.00 30.92 ?  25  THR   A CG2 1 
ATOM   147  N N   . ASP   A 1 26  ? 12.338  -5.756  -21.035 1.00 31.87 ?  26  ASP   A N   1 
ATOM   148  C CA  . ASP   A 1 26  ? 13.415  -6.577  -20.528 1.00 30.17 ?  26  ASP   A CA  1 
ATOM   149  C C   . ASP   A 1 26  ? 14.476  -5.682  -19.905 1.00 30.13 ?  26  ASP   A C   1 
ATOM   150  O O   . ASP   A 1 26  ? 15.000  -6.006  -18.846 1.00 23.30 ?  26  ASP   A O   1 
ATOM   151  C CB  . ASP   A 1 26  ? 13.852  -7.533  -21.615 1.00 31.15 ?  26  ASP   A CB  1 
ATOM   152  C CG  . ASP   A 1 26  ? 12.865  -8.670  -21.844 1.00 30.61 ?  26  ASP   A CG  1 
ATOM   153  O OD1 . ASP   A 1 26  ? 11.913  -8.824  -21.046 1.00 30.39 ?  26  ASP   A OD1 1 
ATOM   154  O OD2 . ASP   A 1 26  ? 13.030  -9.374  -22.839 1.00 37.68 ?  26  ASP   A OD2 1 
ATOM   155  N N   . GLU   A 1 27  ? 14.782  -4.558  -20.570 1.00 26.81 ?  27  GLU   A N   1 
ATOM   156  C CA  . GLU   A 1 27  ? 15.795  -3.640  -20.086 1.00 26.57 ?  27  GLU   A CA  1 
ATOM   157  C C   . GLU   A 1 27  ? 15.448  -3.184  -18.661 1.00 24.95 ?  27  GLU   A C   1 
ATOM   158  O O   . GLU   A 1 27  ? 16.319  -3.044  -17.804 1.00 26.06 ?  27  GLU   A O   1 
ATOM   159  C CB  . GLU   A 1 27  ? 15.917  -2.437  -21.023 1.00 31.17 ?  27  GLU   A CB  1 
ATOM   160  C CG  . GLU   A 1 27  ? 16.828  -1.359  -20.443 1.00 35.66 ?  27  GLU   A CG  1 
ATOM   161  C CD  . GLU   A 1 27  ? 17.344  -0.298  -21.409 1.00 37.99 ?  27  GLU   A CD  1 
ATOM   162  O OE1 . GLU   A 1 27  ? 16.828  -0.046  -22.532 1.00 39.52 ?  27  GLU   A OE1 1 
ATOM   163  O OE2 . GLU   A 1 27  ? 18.350  0.264   -20.963 1.00 37.58 ?  27  GLU   A OE2 1 
ATOM   164  N N   . LYS   A 1 28  ? 14.174  -2.914  -18.400 1.00 23.11 ?  28  LYS   A N   1 
ATOM   165  C CA  . LYS   A 1 28  ? 13.787  -2.473  -17.061 1.00 24.02 ?  28  LYS   A CA  1 
ATOM   166  C C   . LYS   A 1 28  ? 13.916  -3.590  -16.027 1.00 22.87 ?  28  LYS   A C   1 
ATOM   167  O O   . LYS   A 1 28  ? 14.242  -3.302  -14.867 1.00 20.89 ?  28  LYS   A O   1 
ATOM   168  C CB  . LYS   A 1 28  ? 12.352  -1.962  -16.985 1.00 24.18 ?  28  LYS   A CB  1 
ATOM   169  C CG  . LYS   A 1 28  ? 12.150  -0.708  -17.793 1.00 27.28 ?  28  LYS   A CG  1 
ATOM   170  C CD  . LYS   A 1 28  ? 12.463  0.563   -17.032 1.00 29.72 ?  28  LYS   A CD  1 
ATOM   171  C CE  . LYS   A 1 28  ? 11.418  0.783   -15.961 1.00 33.46 ?  28  LYS   A CE  1 
ATOM   172  N NZ  . LYS   A 1 28  ? 11.970  1.656   -14.915 1.00 34.03 ?  28  LYS   A NZ  1 
ATOM   173  N N   . VAL   A 1 29  ? 13.570  -4.830  -16.419 1.00 20.29 ?  29  VAL   A N   1 
ATOM   174  C CA  . VAL   A 1 29  ? 13.658  -5.951  -15.489 1.00 18.98 ?  29  VAL   A CA  1 
ATOM   175  C C   . VAL   A 1 29  ? 15.124  -6.170  -15.147 1.00 18.45 ?  29  VAL   A C   1 
ATOM   176  O O   . VAL   A 1 29  ? 15.527  -6.370  -14.005 1.00 15.99 ?  29  VAL   A O   1 
ATOM   177  C CB  . VAL   A 1 29  ? 13.067  -7.236  -16.084 1.00 19.93 ?  29  VAL   A CB  1 
ATOM   178  C CG1 . VAL   A 1 29  ? 13.379  -8.475  -15.249 1.00 19.29 ?  29  VAL   A CG1 1 
ATOM   179  C CG2 . VAL   A 1 29  ? 11.573  -7.114  -16.329 1.00 20.69 ?  29  VAL   A CG2 1 
ATOM   180  N N   . ILE   A 1 30  ? 15.952  -6.157  -16.199 1.00 16.93 ?  30  ILE   A N   1 
ATOM   181  C CA  . ILE   A 1 30  ? 17.371  -6.419  -16.026 1.00 18.01 ?  30  ILE   A CA  1 
ATOM   182  C C   . ILE   A 1 30  ? 17.970  -5.341  -15.130 1.00 18.04 ?  30  ILE   A C   1 
ATOM   183  O O   . ILE   A 1 30  ? 18.714  -5.662  -14.226 1.00 18.78 ?  30  ILE   A O   1 
ATOM   184  C CB  . ILE   A 1 30  ? 18.063  -6.526  -17.404 1.00 19.76 ?  30  ILE   A CB  1 
ATOM   185  C CG1 . ILE   A 1 30  ? 17.715  -7.843  -18.129 1.00 20.46 ?  30  ILE   A CG1 1 
ATOM   186  C CG2 . ILE   A 1 30  ? 19.581  -6.398  -17.257 1.00 20.60 ?  30  ILE   A CG2 1 
ATOM   187  C CD1 . ILE   A 1 30  ? 18.098  -7.801  -19.608 1.00 21.49 ?  30  ILE   A CD1 1 
ATOM   188  N N   . ALA   A 1 31  ? 17.585  -4.068  -15.331 1.00 18.23 ?  31  ALA   A N   1 
ATOM   189  C CA  . ALA   A 1 31  ? 18.086  -2.996  -14.498 1.00 18.93 ?  31  ALA   A CA  1 
ATOM   190  C C   . ALA   A 1 31  ? 17.614  -3.174  -13.046 1.00 18.26 ?  31  ALA   A C   1 
ATOM   191  O O   . ALA   A 1 31  ? 18.366  -2.949  -12.100 1.00 17.56 ?  31  ALA   A O   1 
ATOM   192  C CB  . ALA   A 1 31  ? 17.628  -1.675  -15.081 1.00 19.85 ?  31  ALA   A CB  1 
ATOM   193  N N   . LEU   A 1 32  ? 16.349  -3.571  -12.846 1.00 17.90 ?  32  LEU   A N   1 
ATOM   194  C CA  . LEU   A 1 32  ? 15.865  -3.826  -11.486 1.00 16.44 ?  32  LEU   A CA  1 
ATOM   195  C C   . LEU   A 1 32  ? 16.755  -4.852  -10.782 1.00 17.07 ?  32  LEU   A C   1 
ATOM   196  O O   . LEU   A 1 32  ? 17.136  -4.709  -9.607  1.00 17.57 ?  32  LEU   A O   1 
ATOM   197  C CB  . LEU   A 1 32  ? 14.424  -4.344  -11.561 1.00 15.79 ?  32  LEU   A CB  1 
ATOM   198  C CG  . LEU   A 1 32  ? 13.748  -4.692  -10.229 1.00 16.42 ?  32  LEU   A CG  1 
ATOM   199  C CD1 . LEU   A 1 32  ? 13.559  -3.414  -9.439  1.00 16.90 ?  32  LEU   A CD1 1 
ATOM   200  C CD2 . LEU   A 1 32  ? 12.392  -5.405  -10.493 1.00 15.94 ?  32  LEU   A CD2 1 
ATOM   201  N N   . CYS   A 1 33  ? 17.013  -5.961  -11.473 1.00 17.18 ?  33  CYS   A N   1 
ATOM   202  C CA  . CYS   A 1 33  ? 17.856  -6.988  -10.885 1.00 18.66 ?  33  CYS   A CA  1 
ATOM   203  C C   . CYS   A 1 33  ? 19.217  -6.427  -10.480 1.00 18.38 ?  33  CYS   A C   1 
ATOM   204  O O   . CYS   A 1 33  ? 19.724  -6.739  -9.410  1.00 15.99 ?  33  CYS   A O   1 
ATOM   205  C CB  . CYS   A 1 33  ? 18.116  -8.124  -11.853 1.00 17.06 ?  33  CYS   A CB  1 
ATOM   206  S SG  . CYS   A 1 33  ? 16.630  -9.038  -12.301 1.00 19.37 ?  33  CYS   A SG  1 
ATOM   207  N N   . HIS   A 1 34  ? 19.853  -5.647  -11.373 1.00 19.07 ?  34  HIS   A N   1 
ATOM   208  C CA  . HIS   A 1 34  ? 21.115  -5.004  -11.046 1.00 18.79 ?  34  HIS   A CA  1 
ATOM   209  C C   . HIS   A 1 34  ? 21.006  -4.143  -9.782  1.00 18.82 ?  34  HIS   A C   1 
ATOM   210  O O   . HIS   A 1 34  ? 21.929  -4.125  -8.973  1.00 17.75 ?  34  HIS   A O   1 
ATOM   211  C CB  . HIS   A 1 34  ? 21.597  -4.174  -12.237 1.00 20.53 ?  34  HIS   A CB  1 
ATOM   212  C CG  . HIS   A 1 34  ? 21.974  -5.010  -13.410 1.00 20.17 ?  34  HIS   A CG  1 
ATOM   213  N ND1 . HIS   A 1 34  ? 22.235  -4.458  -14.648 1.00 22.26 ?  34  HIS   A ND1 1 
ATOM   214  C CD2 . HIS   A 1 34  ? 22.115  -6.323  -13.544 1.00 20.50 ?  34  HIS   A CD2 1 
ATOM   215  C CE1 . HIS   A 1 34  ? 22.508  -5.435  -15.495 1.00 21.98 ?  34  HIS   A CE1 1 
ATOM   216  N NE2 . HIS   A 1 34  ? 22.495  -6.566  -14.850 1.00 21.26 ?  34  HIS   A NE2 1 
ATOM   217  N N   . GLN   A 1 35  ? 19.945  -3.345  -9.688  1.00 17.88 ?  35  GLN   A N   1 
ATOM   218  C CA  . GLN   A 1 35  ? 19.747  -2.438  -8.577  1.00 18.70 ?  35  GLN   A CA  1 
ATOM   219  C C   . GLN   A 1 35  ? 19.584  -3.169  -7.255  1.00 17.64 ?  35  GLN   A C   1 
ATOM   220  O O   . GLN   A 1 35  ? 19.945  -2.603  -6.210  1.00 17.08 ?  35  GLN   A O   1 
ATOM   221  C CB  . GLN   A 1 35  ? 18.520  -1.570  -8.817  1.00 22.31 ?  35  GLN   A CB  1 
ATOM   222  C CG  . GLN   A 1 35  ? 18.792  -0.532  -9.897  1.00 29.50 ?  35  GLN   A CG  1 
ATOM   223  C CD  . GLN   A 1 35  ? 17.547  0.061   -10.503 1.00 37.87 ?  35  GLN   A CD  1 
ATOM   224  O OE1 . GLN   A 1 35  ? 17.578  0.569   -11.631 1.00 46.76 ?  35  GLN   A OE1 1 
ATOM   225  N NE2 . GLN   A 1 35  ? 16.446  -0.011  -9.766  1.00 41.88 ?  35  GLN   A NE2 1 
ATOM   226  N N   . ALA   A 1 36  ? 19.012  -4.385  -7.308  1.00 16.13 ?  36  ALA   A N   1 
ATOM   227  C CA  . ALA   A 1 36  ? 18.806  -5.229  -6.145  1.00 15.77 ?  36  ALA   A CA  1 
ATOM   228  C C   . ALA   A 1 36  ? 20.136  -5.674  -5.540  1.00 16.54 ?  36  ALA   A C   1 
ATOM   229  O O   . ALA   A 1 36  ? 20.204  -5.984  -4.368  1.00 16.29 ?  36  ALA   A O   1 
ATOM   230  C CB  . ALA   A 1 36  ? 17.953  -6.441  -6.480  1.00 15.60 ?  36  ALA   A CB  1 
ATOM   231  N N   . LYS   A 1 37  ? 21.196  -5.732  -6.352  1.00 16.73 ?  37  LYS   A N   1 
ATOM   232  C CA  . LYS   A 1 37  ? 22.529  -6.085  -5.868  1.00 18.02 ?  37  LYS   A CA  1 
ATOM   233  C C   . LYS   A 1 37  ? 23.262  -4.806  -5.480  1.00 17.69 ?  37  LYS   A C   1 
ATOM   234  O O   . LYS   A 1 37  ? 23.894  -4.145  -6.305  1.00 19.08 ?  37  LYS   A O   1 
ATOM   235  C CB  . LYS   A 1 37  ? 23.302  -6.788  -6.983  1.00 18.38 ?  37  LYS   A CB  1 
ATOM   236  C CG  . LYS   A 1 37  ? 24.643  -7.323  -6.588  1.00 18.60 ?  37  LYS   A CG  1 
ATOM   237  C CD  . LYS   A 1 37  ? 25.319  -7.957  -7.814  1.00 20.08 ?  37  LYS   A CD  1 
ATOM   238  C CE  . LYS   A 1 37  ? 26.556  -8.682  -7.391  1.00 21.82 ?  37  LYS   A CE  1 
ATOM   239  N NZ  . LYS   A 1 37  ? 27.297  -9.166  -8.569  1.00 23.72 ?  37  LYS   A NZ  1 
ATOM   240  N N   . THR   A 1 38  ? 23.140  -4.394  -4.227  1.00 17.45 ?  38  THR   A N   1 
ATOM   241  C CA  . THR   A 1 38  ? 23.587  -3.070  -3.875  1.00 16.46 ?  38  THR   A CA  1 
ATOM   242  C C   . THR   A 1 38  ? 24.973  -3.177  -3.260  1.00 16.40 ?  38  THR   A C   1 
ATOM   243  O O   . THR   A 1 38  ? 25.427  -4.266  -2.905  1.00 15.49 ?  38  THR   A O   1 
ATOM   244  C CB  . THR   A 1 38  ? 22.642  -2.337  -2.911  1.00 16.64 ?  38  THR   A CB  1 
ATOM   245  O OG1 . THR   A 1 38  ? 23.014  -2.526  -1.542  1.00 15.62 ?  38  THR   A OG1 1 
ATOM   246  C CG2 . THR   A 1 38  ? 21.205  -2.741  -3.068  1.00 17.45 ?  38  THR   A CG2 1 
ATOM   247  N N   . PRO   A 1 39  ? 25.646  -2.023  -3.127  1.00 17.89 ?  39  PRO   A N   1 
ATOM   248  C CA  . PRO   A 1 39  ? 26.973  -1.997  -2.539  1.00 19.02 ?  39  PRO   A CA  1 
ATOM   249  C C   . PRO   A 1 39  ? 27.039  -2.409  -1.075  1.00 19.01 ?  39  PRO   A C   1 
ATOM   250  O O   . PRO   A 1 39  ? 28.142  -2.713  -0.603  1.00 21.17 ?  39  PRO   A O   1 
ATOM   251  C CB  . PRO   A 1 39  ? 27.435  -0.525  -2.743  1.00 20.37 ?  39  PRO   A CB  1 
ATOM   252  C CG  . PRO   A 1 39  ? 26.523  0.020   -3.791  1.00 20.80 ?  39  PRO   A CG  1 
ATOM   253  C CD  . PRO   A 1 39  ? 25.203  -0.684  -3.559  1.00 18.89 ?  39  PRO   A CD  1 
ATOM   254  N N   . VAL   A 1 40  ? 25.900  -2.385  -0.355  1.00 18.10 ?  40  VAL   A N   1 
ATOM   255  C CA  . VAL   A 1 40  ? 25.873  -2.781  1.042   1.00 17.23 ?  40  VAL   A CA  1 
ATOM   256  C C   . VAL   A 1 40  ? 25.156  -4.119  1.261   1.00 16.90 ?  40  VAL   A C   1 
ATOM   257  O O   . VAL   A 1 40  ? 24.938  -4.515  2.393   1.00 16.94 ?  40  VAL   A O   1 
ATOM   258  C CB  . VAL   A 1 40  ? 25.285  -1.647  1.892   1.00 19.23 ?  40  VAL   A CB  1 
ATOM   259  C CG1 . VAL   A 1 40  ? 26.058  -0.355  1.723   1.00 21.41 ?  40  VAL   A CG1 1 
ATOM   260  C CG2 . VAL   A 1 40  ? 23.801  -1.428  1.610   1.00 19.85 ?  40  VAL   A CG2 1 
ATOM   261  N N   . GLY   A 1 41  ? 24.712  -4.764  0.186   1.00 16.06 ?  41  GLY   A N   1 
ATOM   262  C CA  . GLY   A 1 41  ? 24.006  -6.026  0.271   1.00 15.33 ?  41  GLY   A CA  1 
ATOM   263  C C   . GLY   A 1 41  ? 22.861  -6.090  -0.742  1.00 15.18 ?  41  GLY   A C   1 
ATOM   264  O O   . GLY   A 1 41  ? 22.528  -5.114  -1.400  1.00 16.45 ?  41  GLY   A O   1 
ATOM   265  N N   . ASN   A 1 42  ? 22.263  -7.274  -0.772  1.00 14.67 ?  42  ASN   A N   1 
ATOM   266  C CA  . ASN   A 1 42  ? 21.156  -7.579  -1.640  1.00 14.66 ?  42  ASN   A CA  1 
ATOM   267  C C   . ASN   A 1 42  ? 19.845  -7.318  -0.920  1.00 14.24 ?  42  ASN   A C   1 
ATOM   268  O O   . ASN   A 1 42  ? 19.705  -7.564  0.267   1.00 14.26 ?  42  ASN   A O   1 
ATOM   269  C CB  . ASN   A 1 42  ? 21.229  -9.042  -2.036  1.00 15.20 ?  42  ASN   A CB  1 
ATOM   270  C CG  . ASN   A 1 42  ? 22.457  -9.351  -2.870  1.00 17.68 ?  42  ASN   A CG  1 
ATOM   271  O OD1 . ASN   A 1 42  ? 23.071  -8.448  -3.438  1.00 18.35 ?  42  ASN   A OD1 1 
ATOM   272  N ND2 . ASN   A 1 42  ? 22.843  -10.618 -2.938  1.00 18.92 ?  42  ASN   A ND2 1 
ATOM   273  N N   . THR   A 1 43  ? 18.846  -6.882  -1.697  1.00 13.98 ?  43  THR   A N   1 
ATOM   274  C CA  . THR   A 1 43  ? 17.499  -6.825  -1.203  1.00 13.69 ?  43  THR   A CA  1 
ATOM   275  C C   . THR   A 1 43  ? 17.048  -8.267  -1.017  1.00 14.37 ?  43  THR   A C   1 
ATOM   276  O O   . THR   A 1 43  ? 17.705  -9.185  -1.481  1.00 14.90 ?  43  THR   A O   1 
ATOM   277  C CB  . THR   A 1 43  ? 16.569  -6.036  -2.127  1.00 14.22 ?  43  THR   A CB  1 
ATOM   278  O OG1 . THR   A 1 43  ? 16.464  -6.672  -3.389  1.00 14.01 ?  43  THR   A OG1 1 
ATOM   279  C CG2 . THR   A 1 43  ? 16.994  -4.595  -2.266  1.00 14.19 ?  43  THR   A CG2 1 
ATOM   280  N N   . ALA   A 1 44  ? 15.952  -8.471  -0.266  1.00 13.21 ?  44  ALA   A N   1 
ATOM   281  C CA  . ALA   A 1 44  ? 15.424  -9.812  -0.058  1.00 12.60 ?  44  ALA   A CA  1 
ATOM   282  C C   . ALA   A 1 44  ? 14.919  -10.420 -1.366  1.00 12.30 ?  44  ALA   A C   1 
ATOM   283  O O   . ALA   A 1 44  ? 14.984  -11.637 -1.636  1.00 13.36 ?  44  ALA   A O   1 
ATOM   284  C CB  . ALA   A 1 44  ? 14.311  -9.738  0.943   1.00 12.83 ?  44  ALA   A CB  1 
ATOM   285  N N   . ALA   A 1 45  ? 14.299  -9.560  -2.159  1.00 12.34 ?  45  ALA   A N   1 
ATOM   286  C CA  . ALA   A 1 45  ? 13.595  -10.000 -3.356  1.00 12.23 ?  45  ALA   A CA  1 
ATOM   287  C C   . ALA   A 1 45  ? 13.570  -8.882  -4.379  1.00 12.96 ?  45  ALA   A C   1 
ATOM   288  O O   . ALA   A 1 45  ? 13.798  -7.717  -4.069  1.00 12.93 ?  45  ALA   A O   1 
ATOM   289  C CB  . ALA   A 1 45  ? 12.169  -10.425 -2.987  1.00 12.18 ?  45  ALA   A CB  1 
ATOM   290  N N   . ILE   A 1 46  ? 13.191  -9.249  -5.609  1.00 13.71 ?  46  ILE   A N   1 
ATOM   291  C CA  . ILE   A 1 46  ? 12.631  -8.294  -6.564  1.00 15.46 ?  46  ILE   A CA  1 
ATOM   292  C C   . ILE   A 1 46  ? 11.166  -8.674  -6.819  1.00 14.62 ?  46  ILE   A C   1 
ATOM   293  O O   . ILE   A 1 46  ? 10.795  -9.831  -6.668  1.00 14.45 ?  46  ILE   A O   1 
ATOM   294  C CB  . ILE   A 1 46  ? 13.435  -8.286  -7.874  1.00 17.64 ?  46  ILE   A CB  1 
ATOM   295  C CG1 . ILE   A 1 46  ? 13.482  -9.669  -8.467  1.00 18.83 ?  46  ILE   A CG1 1 
ATOM   296  C CG2 . ILE   A 1 46  ? 14.833  -7.708  -7.621  1.00 17.75 ?  46  ILE   A CG2 1 
ATOM   297  C CD1 . ILE   A 1 46  ? 14.003  -9.739  -9.868  1.00 21.33 ?  46  ILE   A CD1 1 
ATOM   298  N N   A SER   A 1 47  ? 10.371  -7.684  -7.224  0.50 15.45 ?  47  SER   A N   1 
ATOM   299  N N   B SER   A 1 47  ? 10.366  -7.703  -7.251  0.50 14.48 ?  47  SER   A N   1 
ATOM   300  C CA  A SER   A 1 47  ? 8.984   -7.902  -7.594  0.50 16.26 ?  47  SER   A CA  1 
ATOM   301  C CA  B SER   A 1 47  ? 8.967   -7.942  -7.562  0.50 14.58 ?  47  SER   A CA  1 
ATOM   302  C C   A SER   A 1 47  ? 8.801   -7.532  -9.051  0.50 15.18 ?  47  SER   A C   1 
ATOM   303  C C   B SER   A 1 47  ? 8.734   -7.518  -9.006  0.50 14.32 ?  47  SER   A C   1 
ATOM   304  O O   A SER   A 1 47  ? 9.146   -6.419  -9.431  0.50 14.51 ?  47  SER   A O   1 
ATOM   305  O O   B SER   A 1 47  ? 9.061   -6.390  -9.361  0.50 13.62 ?  47  SER   A O   1 
ATOM   306  C CB  A SER   A 1 47  ? 8.036   -7.112  -6.729  0.50 18.57 ?  47  SER   A CB  1 
ATOM   307  C CB  B SER   A 1 47  ? 8.062   -7.238  -6.543  0.50 15.30 ?  47  SER   A CB  1 
ATOM   308  O OG  A SER   A 1 47  ? 7.910   -7.702  -5.449  0.50 20.64 ?  47  SER   A OG  1 
ATOM   309  O OG  B SER   A 1 47  ? 6.674   -7.330  -6.844  0.50 15.22 ?  47  SER   A OG  1 
ATOM   310  N N   . VAL   A 1 48  ? 8.176   -8.455  -9.806  1.00 13.56 ?  48  VAL   A N   1 
ATOM   311  C CA  . VAL   A 1 48  ? 7.980   -8.250  -11.235 1.00 14.77 ?  48  VAL   A CA  1 
ATOM   312  C C   . VAL   A 1 48  ? 6.638   -8.846  -11.621 1.00 14.54 ?  48  VAL   A C   1 
ATOM   313  O O   . VAL   A 1 48  ? 6.121   -9.706  -10.916 1.00 15.30 ?  48  VAL   A O   1 
ATOM   314  C CB  . VAL   A 1 48  ? 9.098   -8.848  -12.118 1.00 13.92 ?  48  VAL   A CB  1 
ATOM   315  C CG1 . VAL   A 1 48  ? 10.426  -8.141  -11.918 1.00 15.12 ?  48  VAL   A CG1 1 
ATOM   316  C CG2 . VAL   A 1 48  ? 9.255   -10.361 -11.918 1.00 13.82 ?  48  VAL   A CG2 1 
ATOM   317  N N   . TYR   A 1 49  ? 6.144   -8.483  -12.806 1.00 14.99 ?  49  TYR   A N   1 
ATOM   318  C CA  . TYR   A 1 49  ? 4.981   -9.173  -13.330 1.00 14.57 ?  49  TYR   A CA  1 
ATOM   319  C C   . TYR   A 1 49  ? 5.344   -10.592 -13.725 1.00 13.54 ?  49  TYR   A C   1 
ATOM   320  O O   . TYR   A 1 49  ? 6.484   -10.906 -14.000 1.00 13.76 ?  49  TYR   A O   1 
ATOM   321  C CB  . TYR   A 1 49  ? 4.390   -8.471  -14.539 1.00 16.05 ?  49  TYR   A CB  1 
ATOM   322  C CG  . TYR   A 1 49  ? 3.713   -7.169  -14.200 1.00 19.61 ?  49  TYR   A CG  1 
ATOM   323  C CD1 . TYR   A 1 49  ? 2.661   -7.166  -13.307 1.00 22.22 ?  49  TYR   A CD1 1 
ATOM   324  C CD2 . TYR   A 1 49  ? 4.181   -5.950  -14.652 1.00 23.06 ?  49  TYR   A CD2 1 
ATOM   325  C CE1 . TYR   A 1 49  ? 2.001   -5.996  -12.983 1.00 25.69 ?  49  TYR   A CE1 1 
ATOM   326  C CE2 . TYR   A 1 49  ? 3.536   -4.764  -14.332 1.00 28.35 ?  49  TYR   A CE2 1 
ATOM   327  C CZ  . TYR   A 1 49  ? 2.430   -4.791  -13.496 1.00 29.60 ?  49  TYR   A CZ  1 
ATOM   328  O OH  . TYR   A 1 49  ? 1.736   -3.674  -13.110 1.00 35.40 ?  49  TYR   A OH  1 
ATOM   329  N N   . PRO   A 1 50  ? 4.374   -11.513 -13.739 1.00 14.14 ?  50  PRO   A N   1 
ATOM   330  C CA  . PRO   A 1 50  ? 4.688   -12.927 -13.954 1.00 14.08 ?  50  PRO   A CA  1 
ATOM   331  C C   . PRO   A 1 50  ? 5.512   -13.186 -15.214 1.00 14.20 ?  50  PRO   A C   1 
ATOM   332  O O   . PRO   A 1 50  ? 6.453   -13.977 -15.157 1.00 15.29 ?  50  PRO   A O   1 
ATOM   333  C CB  . PRO   A 1 50  ? 3.307   -13.559 -14.004 1.00 14.35 ?  50  PRO   A CB  1 
ATOM   334  C CG  . PRO   A 1 50  ? 2.531   -12.716 -13.054 1.00 13.79 ?  50  PRO   A CG  1 
ATOM   335  C CD  . PRO   A 1 50  ? 2.974   -11.298 -13.330 1.00 13.62 ?  50  PRO   A CD  1 
ATOM   336  N N   . ARG   A 1 51  ? 5.164   -12.487 -16.292 1.00 14.42 ?  51  ARG   A N   1 
ATOM   337  C CA  . ARG   A 1 51  ? 5.811   -12.751 -17.567 1.00 15.47 ?  51  ARG   A CA  1 
ATOM   338  C C   . ARG   A 1 51  ? 7.310   -12.442 -17.543 1.00 15.28 ?  51  ARG   A C   1 
ATOM   339  O O   . ARG   A 1 51  ? 8.043   -12.942 -18.382 1.00 14.63 ?  51  ARG   A O   1 
ATOM   340  C CB  . ARG   A 1 51  ? 5.152   -11.964 -18.697 1.00 17.04 ?  51  ARG   A CB  1 
ATOM   341  C CG  . ARG   A 1 51  ? 5.201   -10.447 -18.556 1.00 19.30 ?  51  ARG   A CG  1 
ATOM   342  C CD  . ARG   A 1 51  ? 4.469   -9.810  -19.734 1.00 24.81 ?  51  ARG   A CD  1 
ATOM   343  N NE  . ARG   A 1 51  ? 4.192   -8.417  -19.407 1.00 33.80 ?  51  ARG   A NE  1 
ATOM   344  C CZ  . ARG   A 1 51  ? 3.160   -7.978  -18.669 1.00 40.93 ?  51  ARG   A CZ  1 
ATOM   345  N NH1 . ARG   A 1 51  ? 2.252   -8.818  -18.186 1.00 39.09 ?  51  ARG   A NH1 1 
ATOM   346  N NH2 . ARG   A 1 51  ? 3.035   -6.683  -18.431 1.00 48.09 ?  51  ARG   A NH2 1 
ATOM   347  N N   . SER   A 1 52  ? 7.765   -11.627 -16.582 1.00 15.70 ?  52  SER   A N   1 
ATOM   348  C CA  . SER   A 1 52  ? 9.140   -11.192 -16.472 1.00 15.26 ?  52  SER   A CA  1 
ATOM   349  C C   . SER   A 1 52  ? 9.979   -12.123 -15.599 1.00 15.33 ?  52  SER   A C   1 
ATOM   350  O O   . SER   A 1 52  ? 11.181  -11.884 -15.482 1.00 14.64 ?  52  SER   A O   1 
ATOM   351  C CB  . SER   A 1 52  ? 9.199   -9.797  -15.860 1.00 16.41 ?  52  SER   A CB  1 
ATOM   352  O OG  . SER   A 1 52  ? 8.467   -8.879  -16.658 1.00 17.63 ?  52  SER   A OG  1 
ATOM   353  N N   . ILE   A 1 53  ? 9.372   -13.143 -14.971 1.00 15.28 ?  53  ILE   A N   1 
ATOM   354  C CA  . ILE   A 1 53  ? 10.086  -14.009 -14.049 1.00 14.75 ?  53  ILE   A CA  1 
ATOM   355  C C   . ILE   A 1 53  ? 11.248  -14.734 -14.730 1.00 15.39 ?  53  ILE   A C   1 
ATOM   356  O O   . ILE   A 1 53  ? 12.369  -14.703 -14.218 1.00 14.30 ?  53  ILE   A O   1 
ATOM   357  C CB  . ILE   A 1 53  ? 9.131   -14.956 -13.293 1.00 16.35 ?  53  ILE   A CB  1 
ATOM   358  C CG1 . ILE   A 1 53  ? 8.208   -14.161 -12.364 1.00 15.74 ?  53  ILE   A CG1 1 
ATOM   359  C CG2 . ILE   A 1 53  ? 9.914   -16.028 -12.535 1.00 16.25 ?  53  ILE   A CG2 1 
ATOM   360  C CD1 . ILE   A 1 53  ? 7.028   -14.936 -11.806 1.00 15.59 ?  53  ILE   A CD1 1 
ATOM   361  N N   . PRO   A 1 54  ? 11.077  -15.377 -15.903 1.00 15.26 ?  54  PRO   A N   1 
ATOM   362  C CA  . PRO   A 1 54  ? 12.212  -16.082 -16.528 1.00 15.53 ?  54  PRO   A CA  1 
ATOM   363  C C   . PRO   A 1 54  ? 13.465  -15.238 -16.790 1.00 16.63 ?  54  PRO   A C   1 
ATOM   364  O O   . PRO   A 1 54  ? 14.606  -15.623 -16.430 1.00 17.38 ?  54  PRO   A O   1 
ATOM   365  C CB  . PRO   A 1 54  ? 11.559  -16.591 -17.818 1.00 15.82 ?  54  PRO   A CB  1 
ATOM   366  C CG  . PRO   A 1 54  ? 10.124  -16.778 -17.419 1.00 15.76 ?  54  PRO   A CG  1 
ATOM   367  C CD  . PRO   A 1 54  ? 9.813   -15.526 -16.632 1.00 15.26 ?  54  PRO   A CD  1 
ATOM   368  N N   . ILE   A 1 55  ? 13.263  -14.040 -17.362 1.00 15.17 ?  55  ILE   A N   1 
ATOM   369  C CA  . ILE   A 1 55  ? 14.396  -13.166 -17.660 1.00 17.29 ?  55  ILE   A CA  1 
ATOM   370  C C   . ILE   A 1 55  ? 15.007  -12.611 -16.375 1.00 15.99 ?  55  ILE   A C   1 
ATOM   371  O O   . ILE   A 1 55  ? 16.228  -12.443 -16.261 1.00 16.13 ?  55  ILE   A O   1 
ATOM   372  C CB  . ILE   A 1 55  ? 14.083  -12.034 -18.653 1.00 20.39 ?  55  ILE   A CB  1 
ATOM   373  C CG1 . ILE   A 1 55  ? 15.375  -11.490 -19.265 1.00 22.18 ?  55  ILE   A CG1 1 
ATOM   374  C CG2 . ILE   A 1 55  ? 13.292  -10.929 -17.955 1.00 22.17 ?  55  ILE   A CG2 1 
ATOM   375  C CD1 . ILE   A 1 55  ? 16.103  -12.475 -20.156 1.00 25.01 ?  55  ILE   A CD1 1 
ATOM   376  N N   . ALA   A 1 56  ? 14.177  -12.381 -15.371 1.00 15.27 ?  56  ALA   A N   1 
ATOM   377  C CA  . ALA   A 1 56  ? 14.731  -11.953 -14.086 1.00 15.22 ?  56  ALA   A CA  1 
ATOM   378  C C   . ALA   A 1 56  ? 15.582  -13.055 -13.460 1.00 15.39 ?  56  ALA   A C   1 
ATOM   379  O O   . ALA   A 1 56  ? 16.649  -12.780 -12.903 1.00 15.47 ?  56  ALA   A O   1 
ATOM   380  C CB  . ALA   A 1 56  ? 13.602  -11.546 -13.176 1.00 15.37 ?  56  ALA   A CB  1 
ATOM   381  N N   . ARG   A 1 57  ? 15.128  -14.313 -13.529 1.00 15.21 ?  57  ARG   A N   1 
ATOM   382  C CA  . ARG   A 1 57  ? 15.873  -15.402 -12.945 1.00 15.36 ?  57  ARG   A CA  1 
ATOM   383  C C   . ARG   A 1 57  ? 17.239  -15.529 -13.620 1.00 16.38 ?  57  ARG   A C   1 
ATOM   384  O O   . ARG   A 1 57  ? 18.268  -15.693 -12.956 1.00 16.80 ?  57  ARG   A O   1 
ATOM   385  C CB  . ARG   A 1 57  ? 15.135  -16.727 -13.060 1.00 16.13 ?  57  ARG   A CB  1 
ATOM   386  C CG  . ARG   A 1 57  ? 15.838  -17.865 -12.356 1.00 17.81 ?  57  ARG   A CG  1 
ATOM   387  C CD  . ARG   A 1 57  ? 15.769  -17.827 -10.855 1.00 18.55 ?  57  ARG   A CD  1 
ATOM   388  N NE  . ARG   A 1 57  ? 14.408  -18.200 -10.400 1.00 19.66 ?  57  ARG   A NE  1 
ATOM   389  C CZ  . ARG   A 1 57  ? 13.915  -17.959 -9.176  1.00 19.64 ?  57  ARG   A CZ  1 
ATOM   390  N NH1 . ARG   A 1 57  ? 14.675  -17.371 -8.265  1.00 19.87 ?  57  ARG   A NH1 1 
ATOM   391  N NH2 . ARG   A 1 57  ? 12.666  -18.303 -8.875  1.00 17.97 ?  57  ARG   A NH2 1 
ATOM   392  N N   A LYS   A 1 58  ? 17.237  -15.442 -14.946 0.50 16.31 ?  58  LYS   A N   1 
ATOM   393  N N   B LYS   A 1 58  ? 17.227  -15.467 -14.948 0.50 15.77 ?  58  LYS   A N   1 
ATOM   394  C CA  A LYS   A 1 58  ? 18.470  -15.553 -15.696 0.50 16.84 ?  58  LYS   A CA  1 
ATOM   395  C CA  B LYS   A 1 58  ? 18.445  -15.525 -15.729 0.50 15.89 ?  58  LYS   A CA  1 
ATOM   396  C C   A LYS   A 1 58  ? 19.415  -14.430 -15.280 0.50 16.38 ?  58  LYS   A C   1 
ATOM   397  C C   B LYS   A 1 58  ? 19.403  -14.432 -15.273 0.50 15.85 ?  58  LYS   A C   1 
ATOM   398  O O   A LYS   A 1 58  ? 20.600  -14.666 -15.079 0.50 17.82 ?  58  LYS   A O   1 
ATOM   399  O O   B LYS   A 1 58  ? 20.581  -14.688 -15.057 0.50 17.28 ?  58  LYS   A O   1 
ATOM   400  C CB  A LYS   A 1 58  ? 18.157  -15.575 -17.196 0.50 17.29 ?  58  LYS   A CB  1 
ATOM   401  C CB  B LYS   A 1 58  ? 18.087  -15.394 -17.214 0.50 15.60 ?  58  LYS   A CB  1 
ATOM   402  C CG  A LYS   A 1 58  ? 19.313  -16.055 -18.067 0.50 18.43 ?  58  LYS   A CG  1 
ATOM   403  C CG  B LYS   A 1 58  ? 19.265  -15.199 -18.169 0.50 15.83 ?  58  LYS   A CG  1 
ATOM   404  C CD  A LYS   A 1 58  ? 18.961  -16.175 -19.546 0.50 18.63 ?  58  LYS   A CD  1 
ATOM   405  C CD  B LYS   A 1 58  ? 18.825  -15.300 -19.629 0.50 15.52 ?  58  LYS   A CD  1 
ATOM   406  C CE  A LYS   A 1 58  ? 20.125  -16.597 -20.374 0.50 20.34 ?  58  LYS   A CE  1 
ATOM   407  C CE  B LYS   A 1 58  ? 19.943  -15.674 -20.557 0.50 16.18 ?  58  LYS   A CE  1 
ATOM   408  N NZ  A LYS   A 1 58  ? 21.166  -15.575 -20.249 0.50 20.82 ?  58  LYS   A NZ  1 
ATOM   409  N NZ  B LYS   A 1 58  ? 19.471  -16.339 -21.778 0.50 16.00 ?  58  LYS   A NZ  1 
ATOM   410  N N   . THR   A 1 59  ? 18.902  -13.203 -15.163 1.00 15.41 ?  59  THR   A N   1 
ATOM   411  C CA  . THR   A 1 59  ? 19.727  -12.074 -14.820 1.00 15.42 ?  59  THR   A CA  1 
ATOM   412  C C   . THR   A 1 59  ? 20.297  -12.226 -13.410 1.00 15.67 ?  59  THR   A C   1 
ATOM   413  O O   . THR   A 1 59  ? 21.480  -11.928 -13.161 1.00 15.48 ?  59  THR   A O   1 
ATOM   414  C CB  . THR   A 1 59  ? 18.920  -10.795 -14.927 1.00 15.72 ?  59  THR   A CB  1 
ATOM   415  O OG1 . THR   A 1 59  ? 18.314  -10.665 -16.204 1.00 16.27 ?  59  THR   A OG1 1 
ATOM   416  C CG2 . THR   A 1 59  ? 19.787  -9.570  -14.778 1.00 15.91 ?  59  THR   A CG2 1 
ATOM   417  N N   . LEU   A 1 60  ? 19.434  -12.612 -12.465 1.00 14.37 ?  60  LEU   A N   1 
ATOM   418  C CA  . LEU   A 1 60  ? 19.915  -12.769 -11.089 1.00 15.63 ?  60  LEU   A CA  1 
ATOM   419  C C   . LEU   A 1 60  ? 21.047  -13.812 -11.014 1.00 17.75 ?  60  LEU   A C   1 
ATOM   420  O O   . LEU   A 1 60  ? 22.030  -13.653 -10.243 1.00 17.40 ?  60  LEU   A O   1 
ATOM   421  C CB  . LEU   A 1 60  ? 18.781  -13.164 -10.137 1.00 16.59 ?  60  LEU   A CB  1 
ATOM   422  C CG  . LEU   A 1 60  ? 17.707  -12.085 -9.898  1.00 17.41 ?  60  LEU   A CG  1 
ATOM   423  C CD1 . LEU   A 1 60  ? 16.574  -12.699 -9.089  1.00 16.95 ?  60  LEU   A CD1 1 
ATOM   424  C CD2 . LEU   A 1 60  ? 18.238  -10.812 -9.232  1.00 17.92 ?  60  LEU   A CD2 1 
ATOM   425  N N   . LYS   A 1 61  ? 20.854  -14.927 -11.724 1.00 18.40 ?  61  LYS   A N   1 
ATOM   426  C CA  . LYS   A 1 61  ? 21.864  -15.973 -11.811 1.00 20.44 ?  61  LYS   A CA  1 
ATOM   427  C C   . LYS   A 1 61  ? 23.162  -15.452 -12.409 1.00 20.71 ?  61  LYS   A C   1 
ATOM   428  O O   . LYS   A 1 61  ? 24.224  -15.701 -11.847 1.00 19.54 ?  61  LYS   A O   1 
ATOM   429  C CB  . LYS   A 1 61  ? 21.348  -17.182 -12.599 1.00 24.61 ?  61  LYS   A CB  1 
ATOM   430  C CG  . LYS   A 1 61  ? 20.356  -18.008 -11.796 1.00 29.33 ?  61  LYS   A CG  1 
ATOM   431  C CD  . LYS   A 1 61  ? 19.658  -19.034 -12.682 1.00 34.97 ?  61  LYS   A CD  1 
ATOM   432  C CE  . LYS   A 1 61  ? 18.761  -19.941 -11.924 1.00 38.82 ?  61  LYS   A CE  1 
ATOM   433  N NZ  . LYS   A 1 61  ? 17.930  -20.673 -12.887 1.00 40.04 ?  61  LYS   A NZ  1 
ATOM   434  N N   . GLU   A 1 62  ? 23.062  -14.768 -13.553 1.00 21.09 ?  62  GLU   A N   1 
ATOM   435  C CA  . GLU   A 1 62  ? 24.233  -14.264 -14.268 1.00 22.91 ?  62  GLU   A CA  1 
ATOM   436  C C   . GLU   A 1 62  ? 25.018  -13.270 -13.411 1.00 22.46 ?  62  GLU   A C   1 
ATOM   437  O O   . GLU   A 1 62  ? 26.235  -13.184 -13.552 1.00 21.82 ?  62  GLU   A O   1 
ATOM   438  C CB  . GLU   A 1 62  ? 23.878  -13.639 -15.613 1.00 24.82 ?  62  GLU   A CB  1 
ATOM   439  C CG  . GLU   A 1 62  ? 23.506  -14.708 -16.634 1.00 30.18 ?  62  GLU   A CG  1 
ATOM   440  C CD  . GLU   A 1 62  ? 23.286  -14.222 -18.047 1.00 33.67 ?  62  GLU   A CD  1 
ATOM   441  O OE1 . GLU   A 1 62  ? 23.509  -13.029 -18.307 1.00 43.43 ?  62  GLU   A OE1 1 
ATOM   442  O OE2 . GLU   A 1 62  ? 22.877  -15.039 -18.876 1.00 36.46 ?  62  GLU   A OE2 1 
ATOM   443  N N   . GLN   A 1 63  ? 24.374  -12.549 -12.496 1.00 18.79 ?  63  GLN   A N   1 
ATOM   444  C CA  . GLN   A 1 63  ? 25.097  -11.572 -11.693 1.00 19.58 ?  63  GLN   A CA  1 
ATOM   445  C C   . GLN   A 1 63  ? 25.553  -12.143 -10.347 1.00 19.92 ?  63  GLN   A C   1 
ATOM   446  O O   . GLN   A 1 63  ? 26.069  -11.408 -9.504  1.00 18.21 ?  63  GLN   A O   1 
ATOM   447  C CB  . GLN   A 1 63  ? 24.303  -10.302 -11.492 1.00 20.69 ?  63  GLN   A CB  1 
ATOM   448  C CG  . GLN   A 1 63  ? 23.042  -10.467 -10.646 1.00 19.69 ?  63  GLN   A CG  1 
ATOM   449  C CD  . GLN   A 1 63  ? 22.386  -9.123  -10.398 1.00 19.76 ?  63  GLN   A CD  1 
ATOM   450  O OE1 . GLN   A 1 63  ? 22.578  -8.168  -11.147 1.00 21.87 ?  63  GLN   A OE1 1 
ATOM   451  N NE2 . GLN   A 1 63  ? 21.509  -9.054  -9.405  1.00 16.46 ?  63  GLN   A NE2 1 
ATOM   452  N N   . GLY   A 1 64  ? 25.447  -13.464 -10.182 1.00 20.42 ?  64  GLY   A N   1 
ATOM   453  C CA  . GLY   A 1 64  ? 25.861  -14.090 -8.948  1.00 20.93 ?  64  GLY   A CA  1 
ATOM   454  C C   . GLY   A 1 64  ? 24.969  -13.727 -7.762  1.00 20.89 ?  64  GLY   A C   1 
ATOM   455  O O   . GLY   A 1 64  ? 25.458  -13.784 -6.635  1.00 21.18 ?  64  GLY   A O   1 
ATOM   456  N N   . THR   A 1 65  ? 23.667  -13.452 -7.966  1.00 18.81 ?  65  THR   A N   1 
ATOM   457  C CA  . THR   A 1 65  ? 22.777  -13.282 -6.813  1.00 17.28 ?  65  THR   A CA  1 
ATOM   458  C C   . THR   A 1 65  ? 21.575  -14.210 -6.901  1.00 20.41 ?  65  THR   A C   1 
ATOM   459  O O   . THR   A 1 65  ? 20.431  -13.774 -6.866  1.00 18.65 ?  65  THR   A O   1 
ATOM   460  C CB  . THR   A 1 65  ? 22.360  -11.841 -6.594  1.00 17.74 ?  65  THR   A CB  1 
ATOM   461  O OG1 . THR   A 1 65  ? 21.575  -11.438 -7.716  1.00 18.42 ?  65  THR   A OG1 1 
ATOM   462  C CG2 . THR   A 1 65  ? 23.527  -10.886 -6.440  1.00 18.78 ?  65  THR   A CG2 1 
ATOM   463  N N   . PRO   A 1 66  ? 21.802  -15.537 -6.901  1.00 22.49 ?  66  PRO   A N   1 
ATOM   464  C CA  . PRO   A 1 66  ? 20.723  -16.497 -7.073  1.00 22.44 ?  66  PRO   A CA  1 
ATOM   465  C C   . PRO   A 1 66  ? 19.785  -16.602 -5.883  1.00 24.54 ?  66  PRO   A C   1 
ATOM   466  O O   . PRO   A 1 66  ? 18.722  -17.198 -6.027  1.00 23.29 ?  66  PRO   A O   1 
ATOM   467  C CB  . PRO   A 1 66  ? 21.443  -17.821 -7.311  1.00 24.17 ?  66  PRO   A CB  1 
ATOM   468  C CG  . PRO   A 1 66  ? 22.756  -17.657 -6.572  1.00 23.49 ?  66  PRO   A CG  1 
ATOM   469  C CD  . PRO   A 1 66  ? 23.129  -16.188 -6.831  1.00 22.77 ?  66  PRO   A CD  1 
ATOM   470  N N   . GLU   A 1 67  ? 20.206  -16.066 -4.728  1.00 22.55 ?  67  GLU   A N   1 
ATOM   471  C CA  . GLU   A 1 67  ? 19.404  -16.109 -3.527  1.00 22.26 ?  67  GLU   A CA  1 
ATOM   472  C C   . GLU   A 1 67  ? 18.456  -14.917 -3.425  1.00 19.70 ?  67  GLU   A C   1 
ATOM   473  O O   . GLU   A 1 67  ? 17.669  -14.853 -2.481  1.00 18.40 ?  67  GLU   A O   1 
ATOM   474  C CB  . GLU   A 1 67  ? 20.283  -16.166 -2.276  1.00 27.12 ?  67  GLU   A CB  1 
ATOM   475  C CG  . GLU   A 1 67  ? 21.013  -17.504 -2.163  1.00 33.86 ?  67  GLU   A CG  1 
ATOM   476  C CD  . GLU   A 1 67  ? 21.557  -17.914 -0.787  1.00 41.77 ?  67  GLU   A CD  1 
ATOM   477  O OE1 . GLU   A 1 67  ? 20.954  -17.628 0.270   1.00 50.63 ?  67  GLU   A OE1 1 
ATOM   478  O OE2 . GLU   A 1 67  ? 22.612  -18.580 -0.774  1.00 50.81 ?  67  GLU   A OE2 1 
ATOM   479  N N   . ILE   A 1 68  ? 18.530  -13.935 -4.318  1.00 17.20 ?  68  ILE   A N   1 
ATOM   480  C CA  . ILE   A 1 68  ? 17.510  -12.895 -4.315  1.00 15.80 ?  68  ILE   A CA  1 
ATOM   481  C C   . ILE   A 1 68  ? 16.215  -13.547 -4.801  1.00 15.74 ?  68  ILE   A C   1 
ATOM   482  O O   . ILE   A 1 68  ? 16.194  -14.202 -5.832  1.00 14.69 ?  68  ILE   A O   1 
ATOM   483  C CB  . ILE   A 1 68  ? 17.889  -11.669 -5.163  1.00 16.03 ?  68  ILE   A CB  1 
ATOM   484  C CG1 . ILE   A 1 68  ? 19.155  -10.965 -4.593  1.00 15.69 ?  68  ILE   A CG1 1 
ATOM   485  C CG2 . ILE   A 1 68  ? 16.713  -10.685 -5.313  1.00 15.99 ?  68  ILE   A CG2 1 
ATOM   486  C CD1 . ILE   A 1 68  ? 19.595  -9.745  -5.383  1.00 15.43 ?  68  ILE   A CD1 1 
ATOM   487  N N   . ARG   A 1 69  ? 15.133  -13.382 -4.031  1.00 14.47 ?  69  ARG   A N   1 
ATOM   488  C CA  . ARG   A 1 69  ? 13.894  -14.062 -4.340  1.00 15.05 ?  69  ARG   A CA  1 
ATOM   489  C C   . ARG   A 1 69  ? 13.195  -13.317 -5.473  1.00 13.54 ?  69  ARG   A C   1 
ATOM   490  O O   . ARG   A 1 69  ? 13.315  -12.093 -5.618  1.00 12.81 ?  69  ARG   A O   1 
ATOM   491  C CB  . ARG   A 1 69  ? 13.001  -14.170 -3.103  1.00 16.10 ?  69  ARG   A CB  1 
ATOM   492  C CG  . ARG   A 1 69  ? 13.695  -14.814 -1.898  1.00 18.99 ?  69  ARG   A CG  1 
ATOM   493  C CD  . ARG   A 1 69  ? 13.057  -14.268 -0.633  1.00 24.10 ?  69  ARG   A CD  1 
ATOM   494  N NE  . ARG   A 1 69  ? 13.583  -14.690 0.670   1.00 30.73 ?  69  ARG   A NE  1 
ATOM   495  C CZ  . ARG   A 1 69  ? 14.734  -14.281 1.214   1.00 30.27 ?  69  ARG   A CZ  1 
ATOM   496  N NH1 . ARG   A 1 69  ? 15.424  -13.293 0.674   1.00 29.06 ?  69  ARG   A NH1 1 
ATOM   497  N NH2 . ARG   A 1 69  ? 15.181  -14.863 2.311   1.00 34.92 ?  69  ARG   A NH2 1 
ATOM   498  N N   . ILE   A 1 70  ? 12.347  -14.054 -6.193  1.00 13.20 ?  70  ILE   A N   1 
ATOM   499  C CA  . ILE   A 1 70  ? 11.508  -13.436 -7.193  1.00 12.93 ?  70  ILE   A CA  1 
ATOM   500  C C   . ILE   A 1 70  ? 10.049  -13.522 -6.725  1.00 12.55 ?  70  ILE   A C   1 
ATOM   501  O O   . ILE   A 1 70  ? 9.479   -14.636 -6.624  1.00 12.06 ?  70  ILE   A O   1 
ATOM   502  C CB  . ILE   A 1 70  ? 11.666  -14.087 -8.573  1.00 13.57 ?  70  ILE   A CB  1 
ATOM   503  C CG1 . ILE   A 1 70  ? 13.127  -14.061 -9.043  1.00 13.36 ?  70  ILE   A CG1 1 
ATOM   504  C CG2 . ILE   A 1 70  ? 10.721  -13.404 -9.548  1.00 13.78 ?  70  ILE   A CG2 1 
ATOM   505  C CD1 . ILE   A 1 70  ? 13.365  -14.693 -10.395 1.00 13.75 ?  70  ILE   A CD1 1 
ATOM   506  N N   . ALA   A 1 71  ? 9.514   -12.346 -6.443  1.00 11.99 ?  71  ALA   A N   1 
ATOM   507  C CA  . ALA   A 1 71  ? 8.110   -12.216 -6.096  1.00 12.49 ?  71  ALA   A CA  1 
ATOM   508  C C   . ALA   A 1 71  ? 7.348   -11.617 -7.268  1.00 13.47 ?  71  ALA   A C   1 
ATOM   509  O O   . ALA   A 1 71  ? 7.913   -10.878 -8.099  1.00 13.30 ?  71  ALA   A O   1 
ATOM   510  C CB  . ALA   A 1 71  ? 7.946   -11.343 -4.853  1.00 13.41 ?  71  ALA   A CB  1 
ATOM   511  N N   . THR   A 1 72  ? 6.048   -11.952 -7.344  1.00 12.37 ?  72  THR   A N   1 
ATOM   512  C CA  . THR   A 1 72  ? 5.186   -11.436 -8.380  1.00 13.58 ?  72  THR   A CA  1 
ATOM   513  C C   . THR   A 1 72  ? 3.818   -11.132 -7.767  1.00 13.99 ?  72  THR   A C   1 
ATOM   514  O O   . THR   A 1 72  ? 3.627   -11.234 -6.552  1.00 15.22 ?  72  THR   A O   1 
ATOM   515  C CB  . THR   A 1 72  ? 5.120   -12.408 -9.551  1.00 14.59 ?  72  THR   A CB  1 
ATOM   516  O OG1 . THR   A 1 72  ? 4.540   -11.695 -10.655 1.00 14.67 ?  72  THR   A OG1 1 
ATOM   517  C CG2 . THR   A 1 72  ? 4.415   -13.716 -9.200  1.00 14.35 ?  72  THR   A CG2 1 
ATOM   518  N N   . VAL   A 1 73  ? 2.868   -10.762 -8.626  1.00 12.77 ?  73  VAL   A N   1 
ATOM   519  C CA  . VAL   A 1 73  ? 1.555   -10.325 -8.170  1.00 13.30 ?  73  VAL   A CA  1 
ATOM   520  C C   . VAL   A 1 73  ? 0.510   -11.039 -9.015  1.00 13.72 ?  73  VAL   A C   1 
ATOM   521  O O   . VAL   A 1 73  ? 0.730   -11.265 -10.199 1.00 12.99 ?  73  VAL   A O   1 
ATOM   522  C CB  . VAL   A 1 73  ? 1.403   -8.801  -8.280  1.00 13.51 ?  73  VAL   A CB  1 
ATOM   523  C CG1 . VAL   A 1 73  ? 2.252   -8.101  -7.221  1.00 14.99 ?  73  VAL   A CG1 1 
ATOM   524  C CG2 . VAL   A 1 73  ? 1.764   -8.288  -9.671  1.00 15.32 ?  73  VAL   A CG2 1 
ATOM   525  N N   . THR   A 1 74  ? -0.600  -11.415 -8.377  1.00 13.83 ?  74  THR   A N   1 
ATOM   526  C CA  . THR   A 1 74  ? -1.750  -11.999 -9.060  1.00 12.79 ?  74  THR   A CA  1 
ATOM   527  C C   . THR   A 1 74  ? -3.011  -11.383 -8.457  1.00 13.51 ?  74  THR   A C   1 
ATOM   528  O O   . THR   A 1 74  ? -2.958  -10.646 -7.452  1.00 12.90 ?  74  THR   A O   1 
ATOM   529  C CB  . THR   A 1 74  ? -1.764  -13.531 -8.947  1.00 12.10 ?  74  THR   A CB  1 
ATOM   530  O OG1 . THR   A 1 74  ? -1.965  -13.887 -7.555  1.00 12.88 ?  74  THR   A OG1 1 
ATOM   531  C CG2 . THR   A 1 74  ? -0.525  -14.136 -9.571  1.00 12.92 ?  74  THR   A CG2 1 
ATOM   532  N N   . ASN   A 1 75  ? -4.121  -11.574 -9.203  1.00 12.96 ?  75  ASN   A N   1 
ATOM   533  C CA  . ASN   A 1 75  ? -5.399  -10.926 -8.962  1.00 12.72 ?  75  ASN   A CA  1 
ATOM   534  C C   . ASN   A 1 75  ? -5.231  -9.420  -8.806  1.00 12.93 ?  75  ASN   A C   1 
ATOM   535  O O   . ASN   A 1 75  ? -5.904  -8.798  -7.986  1.00 12.50 ?  75  ASN   A O   1 
ATOM   536  C CB  . ASN   A 1 75  ? -6.082  -11.519 -7.737  1.00 12.41 ?  75  ASN   A CB  1 
ATOM   537  C CG  . ASN   A 1 75  ? -7.575  -11.349 -7.770  1.00 12.55 ?  75  ASN   A CG  1 
ATOM   538  O OD1 . ASN   A 1 75  ? -8.192  -11.457 -8.853  1.00 13.24 ?  75  ASN   A OD1 1 
ATOM   539  N ND2 . ASN   A 1 75  ? -8.196  -11.185 -6.597  1.00 12.28 ?  75  ASN   A ND2 1 
ATOM   540  N N   . PHE   A 1 76  ? -4.309  -8.858  -9.594  1.00 13.58 ?  76  PHE   A N   1 
ATOM   541  C CA  . PHE   A 1 76  ? -3.740  -7.566  -9.312  1.00 13.94 ?  76  PHE   A CA  1 
ATOM   542  C C   . PHE   A 1 76  ? -3.940  -6.567  -10.437 1.00 15.81 ?  76  PHE   A C   1 
ATOM   543  O O   . PHE   A 1 76  ? -3.859  -6.942  -11.609 1.00 15.30 ?  76  PHE   A O   1 
ATOM   544  C CB  . PHE   A 1 76  ? -2.246  -7.831  -9.209  1.00 14.31 ?  76  PHE   A CB  1 
ATOM   545  C CG  . PHE   A 1 76  ? -1.446  -6.572  -8.908  1.00 15.56 ?  76  PHE   A CG  1 
ATOM   546  C CD1 . PHE   A 1 76  ? -0.997  -5.753  -9.941  1.00 15.67 ?  76  PHE   A CD1 1 
ATOM   547  C CD2 . PHE   A 1 76  ? -1.090  -6.266  -7.599  1.00 15.59 ?  76  PHE   A CD2 1 
ATOM   548  C CE1 . PHE   A 1 76  ? -0.232  -4.634  -9.667  1.00 16.45 ?  76  PHE   A CE1 1 
ATOM   549  C CE2 . PHE   A 1 76  ? -0.338  -5.114  -7.319  1.00 17.13 ?  76  PHE   A CE2 1 
ATOM   550  C CZ  . PHE   A 1 76  ? 0.084   -4.304  -8.350  1.00 15.88 ?  76  PHE   A CZ  1 
ATOM   551  N N   . PRO   A 1 77  A -4.141  -5.270  -10.136 1.00 15.64 ?  77  PRO   A N   1 
ATOM   552  C CA  . PRO   A 1 77  A -4.296  -4.771  -8.757  1.00 15.41 ?  77  PRO   A CA  1 
ATOM   553  C C   . PRO   A 1 77  A -5.705  -4.733  -8.173  1.00 15.05 ?  77  PRO   A C   1 
ATOM   554  O O   . PRO   A 1 77  A -5.899  -4.261  -7.048  1.00 16.20 ?  77  PRO   A O   1 
ATOM   555  C CB  . PRO   A 1 77  A -3.828  -3.322  -8.967  1.00 17.04 ?  77  PRO   A CB  1 
ATOM   556  C CG  . PRO   A 1 77  A -4.399  -2.974  -10.315 1.00 16.65 ?  77  PRO   A CG  1 
ATOM   557  C CD  . PRO   A 1 77  A -4.255  -4.236  -11.182 1.00 16.55 ?  77  PRO   A CD  1 
ATOM   558  N N   . HIS   A 1 78  ? -6.671  -5.246  -8.950  1.00 14.46 ?  78  HIS   A N   1 
ATOM   559  C CA  . HIS   A 1 78  ? -8.098  -5.045  -8.712  1.00 15.58 ?  78  HIS   A CA  1 
ATOM   560  C C   . HIS   A 1 78  ? -8.646  -5.739  -7.464  1.00 14.85 ?  78  HIS   A C   1 
ATOM   561  O O   . HIS   A 1 78  ? -9.593  -5.244  -6.840  1.00 15.29 ?  78  HIS   A O   1 
ATOM   562  C CB  . HIS   A 1 78  ? -8.872  -5.511  -9.956  1.00 15.37 ?  78  HIS   A CB  1 
ATOM   563  C CG  . HIS   A 1 78  ? -8.403  -6.829  -10.496 1.00 15.90 ?  78  HIS   A CG  1 
ATOM   564  N ND1 . HIS   A 1 78  ? -8.706  -8.064  -9.955  1.00 15.26 ?  78  HIS   A ND1 1 
ATOM   565  C CD2 . HIS   A 1 78  ? -7.606  -7.081  -11.581 1.00 15.47 ?  78  HIS   A CD2 1 
ATOM   566  C CE1 . HIS   A 1 78  ? -8.157  -9.016  -10.702 1.00 16.22 ?  78  HIS   A CE1 1 
ATOM   567  N NE2 . HIS   A 1 78  ? -7.467  -8.439  -11.705 1.00 15.35 ?  78  HIS   A NE2 1 
ATOM   568  N N   . GLY   A 1 79  ? -8.119  -6.914  -7.122  1.00 14.08 ?  79  GLY   A N   1 
ATOM   569  C CA  . GLY   A 1 79  ? -8.687  -7.726  -6.050  1.00 13.79 ?  79  GLY   A CA  1 
ATOM   570  C C   . GLY   A 1 79  ? -10.119 -8.142  -6.369  1.00 15.03 ?  79  GLY   A C   1 
ATOM   571  O O   . GLY   A 1 79  ? -10.996 -8.078  -5.508  1.00 13.97 ?  79  GLY   A O   1 
ATOM   572  N N   . ASN   A 1 80  ? -10.342 -8.589  -7.612  1.00 14.86 ?  80  ASN   A N   1 
ATOM   573  C CA  . ASN   A 1 80  ? -11.639 -9.095  -8.008  1.00 15.45 ?  80  ASN   A CA  1 
ATOM   574  C C   . ASN   A 1 80  ? -11.928 -10.385 -7.242  1.00 15.93 ?  80  ASN   A C   1 
ATOM   575  O O   . ASN   A 1 80  ? -11.020 -10.972 -6.634  1.00 15.22 ?  80  ASN   A O   1 
ATOM   576  C CB  . ASN   A 1 80  ? -11.666 -9.325  -9.519  1.00 16.06 ?  80  ASN   A CB  1 
ATOM   577  C CG  . ASN   A 1 80  ? -11.670 -8.047  -10.318 1.00 17.77 ?  80  ASN   A CG  1 
ATOM   578  O OD1 . ASN   A 1 80  ? -11.956 -6.969  -9.789  1.00 16.89 ?  80  ASN   A OD1 1 
ATOM   579  N ND2 . ASN   A 1 80  ? -11.342 -8.154  -11.613 1.00 19.55 ?  80  ASN   A ND2 1 
ATOM   580  N N   . ASP   A 1 81  ? -13.209 -10.797 -7.240  1.00 16.99 ?  81  ASP   A N   1 
ATOM   581  C CA  . ASP   A 1 81  ? -13.634 -11.955 -6.479  1.00 17.12 ?  81  ASP   A CA  1 
ATOM   582  C C   . ASP   A 1 81  ? -13.863 -13.193 -7.335  1.00 16.06 ?  81  ASP   A C   1 
ATOM   583  O O   . ASP   A 1 81  ? -14.562 -14.112 -6.906  1.00 16.60 ?  81  ASP   A O   1 
ATOM   584  C CB  . ASP   A 1 81  ? -14.870 -11.659 -5.648  1.00 18.44 ?  81  ASP   A CB  1 
ATOM   585  C CG  . ASP   A 1 81  ? -16.062 -11.166 -6.453  1.00 22.79 ?  81  ASP   A CG  1 
ATOM   586  O OD1 . ASP   A 1 81  ? -15.963 -11.134 -7.667  1.00 21.34 ?  81  ASP   A OD1 1 
ATOM   587  O OD2 . ASP   A 1 81  ? -17.047 -10.759 -5.829  1.00 26.40 ?  81  ASP   A OD2 1 
ATOM   588  N N   . ASP   A 1 82  ? -13.207 -13.268 -8.496  1.00 15.55 ?  82  ASP   A N   1 
ATOM   589  C CA  . ASP   A 1 82  ? -13.285 -14.463 -9.312  1.00 16.87 ?  82  ASP   A CA  1 
ATOM   590  C C   . ASP   A 1 82  ? -12.129 -15.372 -8.934  1.00 16.15 ?  82  ASP   A C   1 
ATOM   591  O O   . ASP   A 1 82  ? -10.996 -15.122 -9.356  1.00 14.64 ?  82  ASP   A O   1 
ATOM   592  C CB  . ASP   A 1 82  ? -13.255 -14.156 -10.805 1.00 16.18 ?  82  ASP   A CB  1 
ATOM   593  C CG  . ASP   A 1 82  ? -13.484 -15.387 -11.660 1.00 18.18 ?  82  ASP   A CG  1 
ATOM   594  O OD1 . ASP   A 1 82  ? -12.869 -16.431 -11.395 1.00 18.18 ?  82  ASP   A OD1 1 
ATOM   595  O OD2 . ASP   A 1 82  ? -14.287 -15.274 -12.608 1.00 21.64 ?  82  ASP   A OD2 1 
ATOM   596  N N   . ILE   A 1 83  ? -12.445 -16.396 -8.132  1.00 16.00 ?  83  ILE   A N   1 
ATOM   597  C CA  . ILE   A 1 83  ? -11.455 -17.336 -7.627  1.00 16.12 ?  83  ILE   A CA  1 
ATOM   598  C C   . ILE   A 1 83  ? -10.728 -18.041 -8.766  1.00 16.63 ?  83  ILE   A C   1 
ATOM   599  O O   . ILE   A 1 83  ? -9.525  -18.212 -8.688  1.00 16.34 ?  83  ILE   A O   1 
ATOM   600  C CB  . ILE   A 1 83  ? -12.067 -18.366 -6.670  1.00 17.21 ?  83  ILE   A CB  1 
ATOM   601  C CG1 . ILE   A 1 83  ? -12.619 -17.706 -5.441  1.00 18.75 ?  83  ILE   A CG1 1 
ATOM   602  C CG2 . ILE   A 1 83  ? -11.030 -19.434 -6.295  1.00 17.45 ?  83  ILE   A CG2 1 
ATOM   603  C CD1 . ILE   A 1 83  ? -13.476 -18.607 -4.584  1.00 19.24 ?  83  ILE   A CD1 1 
ATOM   604  N N   . GLU   A 1 84  ? -11.453 -18.491 -9.785  1.00 16.50 ?  84  GLU   A N   1 
ATOM   605  C CA  . GLU   A 1 84  ? -10.843 -19.226 -10.876 1.00 18.71 ?  84  GLU   A CA  1 
ATOM   606  C C   . GLU   A 1 84  ? -9.792  -18.379 -11.582 1.00 15.62 ?  84  GLU   A C   1 
ATOM   607  O O   . GLU   A 1 84  ? -8.739  -18.905 -11.955 1.00 16.10 ?  84  GLU   A O   1 
ATOM   608  C CB  . GLU   A 1 84  ? -11.923 -19.726 -11.829 1.00 22.42 ?  84  GLU   A CB  1 
ATOM   609  C CG  . GLU   A 1 84  ? -12.787 -20.842 -11.256 1.00 28.09 ?  84  GLU   A CG  1 
ATOM   610  C CD  . GLU   A 1 84  ? -12.082 -22.191 -11.172 1.00 41.84 ?  84  GLU   A CD  1 
ATOM   611  O OE1 . GLU   A 1 84  ? -10.871 -22.283 -11.535 1.00 48.10 ?  84  GLU   A OE1 1 
ATOM   612  O OE2 . GLU   A 1 84  ? -12.753 -23.174 -10.756 1.00 53.81 ?  84  GLU   A OE2 1 
ATOM   613  N N   . ILE   A 1 85  ? -10.076 -17.091 -11.837 1.00 14.53 ?  85  ILE   A N   1 
ATOM   614  C CA  . ILE   A 1 85  ? -9.079  -16.243 -12.462 1.00 13.47 ?  85  ILE   A CA  1 
ATOM   615  C C   . ILE   A 1 85  ? -7.873  -16.068 -11.532 1.00 13.04 ?  85  ILE   A C   1 
ATOM   616  O O   . ILE   A 1 85  ? -6.730  -16.173 -11.952 1.00 12.97 ?  85  ILE   A O   1 
ATOM   617  C CB  . ILE   A 1 85  ? -9.670  -14.900 -12.899 1.00 14.50 ?  85  ILE   A CB  1 
ATOM   618  C CG1 . ILE   A 1 85  ? -10.674 -15.152 -14.078 1.00 15.35 ?  85  ILE   A CG1 1 
ATOM   619  C CG2 . ILE   A 1 85  ? -8.590  -13.887 -13.311 1.00 14.45 ?  85  ILE   A CG2 1 
ATOM   620  C CD1 . ILE   A 1 85  ? -11.400 -13.910 -14.573 1.00 15.86 ?  85  ILE   A CD1 1 
ATOM   621  N N   . ALA   A 1 86  ? -8.112  -15.729 -10.266 1.00 13.44 ?  86  ALA   A N   1 
ATOM   622  C CA  . ALA   A 1 86  ? -7.013  -15.519 -9.330  1.00 12.96 ?  86  ALA   A CA  1 
ATOM   623  C C   . ALA   A 1 86  ? -6.143  -16.762 -9.236  1.00 13.61 ?  86  ALA   A C   1 
ATOM   624  O O   . ALA   A 1 86  ? -4.898  -16.679 -9.233  1.00 13.56 ?  86  ALA   A O   1 
ATOM   625  C CB  . ALA   A 1 86  ? -7.545  -15.111 -7.993  1.00 13.78 ?  86  ALA   A CB  1 
ATOM   626  N N   . LEU   A 1 87  ? -6.772  -17.934 -9.211  1.00 13.20 ?  87  LEU   A N   1 
ATOM   627  C CA  . LEU   A 1 87  ? -6.045  -19.199 -9.110  1.00 13.33 ?  87  LEU   A CA  1 
ATOM   628  C C   . LEU   A 1 87  ? -5.223  -19.474 -10.374 1.00 13.28 ?  87  LEU   A C   1 
ATOM   629  O O   . LEU   A 1 87  ? -4.081  -19.893 -10.287 1.00 13.54 ?  87  LEU   A O   1 
ATOM   630  C CB  . LEU   A 1 87  ? -7.033  -20.323 -8.847  1.00 14.14 ?  87  LEU   A CB  1 
ATOM   631  C CG  . LEU   A 1 87  ? -6.434  -21.725 -8.781  1.00 15.14 ?  87  LEU   A CG  1 
ATOM   632  C CD1 . LEU   A 1 87  ? -5.331  -21.853 -7.751  1.00 15.63 ?  87  LEU   A CD1 1 
ATOM   633  C CD2 . LEU   A 1 87  ? -7.551  -22.756 -8.520  1.00 16.13 ?  87  LEU   A CD2 1 
ATOM   634  N N   . ALA   A 1 88  ? -5.814  -19.228 -11.542 1.00 13.51 ?  88  ALA   A N   1 
ATOM   635  C CA  . ALA   A 1 88  ? -5.123  -19.503 -12.791 1.00 13.98 ?  88  ALA   A CA  1 
ATOM   636  C C   . ALA   A 1 88  ? -3.879  -18.618 -12.861 1.00 14.32 ?  88  ALA   A C   1 
ATOM   637  O O   . ALA   A 1 88  ? -2.815  -19.070 -13.272 1.00 14.74 ?  88  ALA   A O   1 
ATOM   638  C CB  . ALA   A 1 88  ? -6.075  -19.244 -13.944 1.00 13.71 ?  88  ALA   A CB  1 
ATOM   639  N N   . GLU   A 1 89  ? -4.041  -17.329 -12.516 1.00 13.58 ?  89  GLU   A N   1 
ATOM   640  C CA  . GLU   A 1 89  ? -2.923  -16.411 -12.497 1.00 13.47 ?  89  GLU   A CA  1 
ATOM   641  C C   . GLU   A 1 89  ? -1.827  -16.901 -11.541 1.00 13.31 ?  89  GLU   A C   1 
ATOM   642  O O   . GLU   A 1 89  ? -0.642  -16.904 -11.872 1.00 13.26 ?  89  GLU   A O   1 
ATOM   643  C CB  . GLU   A 1 89  ? -3.422  -14.992 -12.186 1.00 14.65 ?  89  GLU   A CB  1 
ATOM   644  C CG  . GLU   A 1 89  ? -4.358  -14.410 -13.234 1.00 16.19 ?  89  GLU   A CG  1 
ATOM   645  C CD  . GLU   A 1 89  ? -4.641  -12.932 -13.036 1.00 17.57 ?  89  GLU   A CD  1 
ATOM   646  O OE1 . GLU   A 1 89  ? -4.330  -12.487 -11.939 1.00 19.40 ?  89  GLU   A OE1 1 
ATOM   647  O OE2 . GLU   A 1 89  ? -5.150  -12.191 -13.889 1.00 17.87 ?  89  GLU   A OE2 1 
ATOM   648  N N   . THR   A 1 90  ? -2.215  -17.391 -10.374 1.00 12.84 ?  90  THR   A N   1 
ATOM   649  C CA  . THR   A 1 90  ? -1.278  -17.867 -9.372  1.00 12.68 ?  90  THR   A CA  1 
ATOM   650  C C   . THR   A 1 90  ? -0.553  -19.139 -9.840  1.00 13.09 ?  90  THR   A C   1 
ATOM   651  O O   . THR   A 1 90  ? 0.666   -19.266 -9.741  1.00 11.97 ?  90  THR   A O   1 
ATOM   652  C CB  . THR   A 1 90  ? -2.040  -18.019 -8.038  1.00 12.94 ?  90  THR   A CB  1 
ATOM   653  O OG1 . THR   A 1 90  ? -2.521  -16.739 -7.590  1.00 13.70 ?  90  THR   A OG1 1 
ATOM   654  C CG2 . THR   A 1 90  ? -1.166  -18.634 -6.966  1.00 13.15 ?  90  THR   A CG2 1 
ATOM   655  N N   . ARG   A 1 91  ? -1.274  -20.083 -10.446 1.00 14.47 ?  91  ARG   A N   1 
ATOM   656  C CA  . ARG   A 1 91  ? -0.622  -21.255 -11.019 1.00 15.00 ?  91  ARG   A CA  1 
ATOM   657  C C   . ARG   A 1 91  ? 0.357   -20.830 -12.118 1.00 13.79 ?  91  ARG   A C   1 
ATOM   658  O O   . ARG   A 1 91  ? 1.451   -21.381 -12.209 1.00 13.41 ?  91  ARG   A O   1 
ATOM   659  C CB  . ARG   A 1 91  ? -1.659  -22.224 -11.575 1.00 16.38 ?  91  ARG   A CB  1 
ATOM   660  C CG  . ARG   A 1 91  ? -2.508  -22.878 -10.498 1.00 18.46 ?  91  ARG   A CG  1 
ATOM   661  C CD  . ARG   A 1 91  ? -3.535  -23.691 -11.221 1.00 22.49 ?  91  ARG   A CD  1 
ATOM   662  N NE  . ARG   A 1 91  ? -4.370  -24.374 -10.254 1.00 24.44 ?  91  ARG   A NE  1 
ATOM   663  C CZ  . ARG   A 1 91  ? -5.537  -24.932 -10.530 1.00 26.21 ?  91  ARG   A CZ  1 
ATOM   664  N NH1 . ARG   A 1 91  ? -6.153  -24.674 -11.663 1.00 26.13 ?  91  ARG   A NH1 1 
ATOM   665  N NH2 . ARG   A 1 91  ? -6.078  -25.748 -9.659  1.00 25.67 ?  91  ARG   A NH2 1 
ATOM   666  N N   . ALA   A 1 92  ? -0.007  -19.846 -12.937 1.00 14.05 ?  92  ALA   A N   1 
ATOM   667  C CA  . ALA   A 1 92  ? 0.890   -19.395 -13.998 1.00 14.23 ?  92  ALA   A CA  1 
ATOM   668  C C   . ALA   A 1 92  ? 2.155   -18.766 -13.392 1.00 13.49 ?  92  ALA   A C   1 
ATOM   669  O O   . ALA   A 1 92  ? 3.260   -19.057 -13.831 1.00 12.51 ?  92  ALA   A O   1 
ATOM   670  C CB  . ALA   A 1 92  ? 0.220   -18.408 -14.933 1.00 15.45 ?  92  ALA   A CB  1 
ATOM   671  N N   . ALA   A 1 93  ? 1.966   -17.919 -12.371 1.00 13.32 ?  93  ALA   A N   1 
ATOM   672  C CA  . ALA   A 1 93  ? 3.091   -17.324 -11.655 1.00 13.45 ?  93  ALA   A CA  1 
ATOM   673  C C   . ALA   A 1 93  ? 4.061   -18.395 -11.157 1.00 13.77 ?  93  ALA   A C   1 
ATOM   674  O O   . ALA   A 1 93  ? 5.276   -18.272 -11.291 1.00 12.94 ?  93  ALA   A O   1 
ATOM   675  C CB  . ALA   A 1 93  ? 2.588   -16.522 -10.479 1.00 12.83 ?  93  ALA   A CB  1 
ATOM   676  N N   . ILE   A 1 94  ? 3.491   -19.439 -10.559 1.00 14.01 ?  94  ILE   A N   1 
ATOM   677  C CA  . ILE   A 1 94  ? 4.297   -20.558 -10.090 1.00 14.28 ?  94  ILE   A CA  1 
ATOM   678  C C   . ILE   A 1 94  ? 5.062   -21.194 -11.260 1.00 13.48 ?  94  ILE   A C   1 
ATOM   679  O O   . ILE   A 1 94  ? 6.227   -21.528 -11.142 1.00 14.06 ?  94  ILE   A O   1 
ATOM   680  C CB  . ILE   A 1 94  ? 3.412   -21.570 -9.367  1.00 14.95 ?  94  ILE   A CB  1 
ATOM   681  C CG1 . ILE   A 1 94  ? 2.835   -20.962 -8.077  1.00 14.58 ?  94  ILE   A CG1 1 
ATOM   682  C CG2 . ILE   A 1 94  ? 4.190   -22.859 -9.067  1.00 16.47 ?  94  ILE   A CG2 1 
ATOM   683  C CD1 . ILE   A 1 94  ? 1.685   -21.729 -7.447  1.00 13.55 ?  94  ILE   A CD1 1 
ATOM   684  N N   . ALA   A 1 95  ? 4.386   -21.454 -12.368 1.00 13.35 ?  95  ALA   A N   1 
ATOM   685  C CA  . ALA   A 1 95  ? 4.937   -22.170 -13.500 1.00 13.94 ?  95  ALA   A CA  1 
ATOM   686  C C   . ALA   A 1 95  ? 6.026   -21.339 -14.165 1.00 13.71 ?  95  ALA   A C   1 
ATOM   687  O O   . ALA   A 1 95  ? 7.041   -21.864 -14.653 1.00 13.75 ?  95  ALA   A O   1 
ATOM   688  C CB  . ALA   A 1 95  ? 3.821   -22.515 -14.458 1.00 14.07 ?  95  ALA   A CB  1 
ATOM   689  N N   . TYR   A 1 96  ? 5.886   -20.015 -14.098 1.00 12.99 ?  96  TYR   A N   1 
ATOM   690  C CA  . TYR   A 1 96  ? 6.927   -19.145 -14.628 1.00 13.34 ?  96  TYR   A CA  1 
ATOM   691  C C   . TYR   A 1 96  ? 8.217   -19.257 -13.812 1.00 14.32 ?  96  TYR   A C   1 
ATOM   692  O O   . TYR   A 1 96  ? 9.277   -18.872 -14.310 1.00 14.56 ?  96  TYR   A O   1 
ATOM   693  C CB  . TYR   A 1 96  ? 6.521   -17.681 -14.644 1.00 12.84 ?  96  TYR   A CB  1 
ATOM   694  C CG  . TYR   A 1 96  ? 5.689   -17.167 -15.814 1.00 13.21 ?  96  TYR   A CG  1 
ATOM   695  C CD1 . TYR   A 1 96  ? 6.224   -17.090 -17.093 1.00 13.84 ?  96  TYR   A CD1 1 
ATOM   696  C CD2 . TYR   A 1 96  ? 4.400   -16.659 -15.635 1.00 14.01 ?  96  TYR   A CD2 1 
ATOM   697  C CE1 . TYR   A 1 96  ? 5.472   -16.618 -18.150 1.00 13.65 ?  96  TYR   A CE1 1 
ATOM   698  C CE2 . TYR   A 1 96  ? 3.672   -16.106 -16.667 1.00 13.99 ?  96  TYR   A CE2 1 
ATOM   699  C CZ  . TYR   A 1 96  ? 4.216   -16.081 -17.932 1.00 14.12 ?  96  TYR   A CZ  1 
ATOM   700  O OH  . TYR   A 1 96  ? 3.498   -15.554 -18.989 1.00 14.97 ?  96  TYR   A OH  1 
ATOM   701  N N   . GLY   A 1 97  ? 8.091   -19.647 -12.531 1.00 13.89 ?  97  GLY   A N   1 
ATOM   702  C CA  . GLY   A 1 97  ? 9.234   -19.786 -11.633 1.00 13.68 ?  97  GLY   A CA  1 
ATOM   703  C C   . GLY   A 1 97  ? 9.214   -18.863 -10.417 1.00 13.84 ?  97  GLY   A C   1 
ATOM   704  O O   . GLY   A 1 97  ? 10.251  -18.737 -9.744  1.00 14.03 ?  97  GLY   A O   1 
ATOM   705  N N   . ALA   A 1 98  ? 8.062   -18.276 -10.051 1.00 13.09 ?  98  ALA   A N   1 
ATOM   706  C CA  . ALA   A 1 98  ? 8.035   -17.399 -8.878  1.00 13.37 ?  98  ALA   A CA  1 
ATOM   707  C C   . ALA   A 1 98  ? 8.537   -18.124 -7.628  1.00 13.08 ?  98  ALA   A C   1 
ATOM   708  O O   . ALA   A 1 98  ? 8.212   -19.286 -7.438  1.00 13.87 ?  98  ALA   A O   1 
ATOM   709  C CB  . ALA   A 1 98  ? 6.630   -16.837 -8.611  1.00 12.97 ?  98  ALA   A CB  1 
ATOM   710  N N   . ASP   A 1 99  ? 9.261   -17.392 -6.748  1.00 13.07 ?  99  ASP   A N   1 
ATOM   711  C CA  . ASP   A 1 99  ? 9.501   -17.840 -5.387  1.00 12.42 ?  99  ASP   A CA  1 
ATOM   712  C C   . ASP   A 1 99  ? 8.339   -17.444 -4.487  1.00 12.33 ?  99  ASP   A C   1 
ATOM   713  O O   . ASP   A 1 99  ? 8.104   -18.071 -3.465  1.00 14.02 ?  99  ASP   A O   1 
ATOM   714  C CB  . ASP   A 1 99  ? 10.792  -17.267 -4.855  1.00 13.26 ?  99  ASP   A CB  1 
ATOM   715  C CG  . ASP   A 1 99  ? 12.023  -17.715 -5.630  1.00 13.87 ?  99  ASP   A CG  1 
ATOM   716  O OD1 . ASP   A 1 99  ? 12.174  -18.947 -5.889  1.00 15.09 ?  99  ASP   A OD1 1 
ATOM   717  O OD2 . ASP   A 1 99  ? 12.765  -16.811 -6.026  1.00 15.40 ?  99  ASP   A OD2 1 
ATOM   718  N N   . GLU   A 1 100 ? 7.671   -16.333 -4.825  1.00 12.18 ?  100 GLU   A N   1 
ATOM   719  C CA  . GLU   A 1 100 ? 6.624   -15.813 -3.952  1.00 12.80 ?  100 GLU   A CA  1 
ATOM   720  C C   . GLU   A 1 100 ? 5.544   -15.213 -4.831  1.00 13.20 ?  100 GLU   A C   1 
ATOM   721  O O   . GLU   A 1 100 ? 5.867   -14.632 -5.864  1.00 13.98 ?  100 GLU   A O   1 
ATOM   722  C CB  . GLU   A 1 100 ? 7.194   -14.747 -3.012  1.00 13.13 ?  100 GLU   A CB  1 
ATOM   723  C CG  . GLU   A 1 100 ? 8.334   -15.271 -2.136  1.00 13.74 ?  100 GLU   A CG  1 
ATOM   724  C CD  . GLU   A 1 100 ? 8.901   -14.252 -1.196  1.00 15.13 ?  100 GLU   A CD  1 
ATOM   725  O OE1 . GLU   A 1 100 ? 8.564   -13.061 -1.269  1.00 14.36 ?  100 GLU   A OE1 1 
ATOM   726  O OE2 . GLU   A 1 100 ? 9.733   -14.719 -0.364  1.00 16.12 ?  100 GLU   A OE2 1 
ATOM   727  N N   . VAL   A 1 101 ? 4.293   -15.313 -4.401  1.00 12.05 ?  101 VAL   A N   1 
ATOM   728  C CA  . VAL   A 1 101 ? 3.183   -14.690 -5.085  1.00 13.05 ?  101 VAL   A CA  1 
ATOM   729  C C   . VAL   A 1 101 ? 2.442   -13.793 -4.120  1.00 13.11 ?  101 VAL   A C   1 
ATOM   730  O O   . VAL   A 1 101 ? 2.117   -14.246 -3.046  1.00 13.15 ?  101 VAL   A O   1 
ATOM   731  C CB  . VAL   A 1 101 ? 2.219   -15.732 -5.663  1.00 13.85 ?  101 VAL   A CB  1 
ATOM   732  C CG1 . VAL   A 1 101 ? 0.951   -15.081 -6.231  1.00 14.54 ?  101 VAL   A CG1 1 
ATOM   733  C CG2 . VAL   A 1 101 ? 2.926   -16.588 -6.708  1.00 14.60 ?  101 VAL   A CG2 1 
ATOM   734  N N   . ASP   A 1 102 ? 2.283   -12.522 -4.483  1.00 13.87 ?  102 ASP   A N   1 
ATOM   735  C CA  . ASP   A 1 102 ? 1.522   -11.567 -3.701  1.00 13.43 ?  102 ASP   A CA  1 
ATOM   736  C C   . ASP   A 1 102 ? 0.148   -11.441 -4.390  1.00 13.10 ?  102 ASP   A C   1 
ATOM   737  O O   . ASP   A 1 102 ? 0.046   -10.815 -5.450  1.00 13.63 ?  102 ASP   A O   1 
ATOM   738  C CB  . ASP   A 1 102 ? 2.224   -10.218 -3.659  1.00 13.46 ?  102 ASP   A CB  1 
ATOM   739  C CG  . ASP   A 1 102 ? 3.596   -10.152 -2.976  1.00 14.50 ?  102 ASP   A CG  1 
ATOM   740  O OD1 . ASP   A 1 102 ? 4.154   -11.222 -2.664  1.00 14.42 ?  102 ASP   A OD1 1 
ATOM   741  O OD2 . ASP   A 1 102 ? 4.063   -9.005  -2.751  1.00 16.57 ?  102 ASP   A OD2 1 
ATOM   742  N N   . VAL   A 1 103 ? -0.895  -12.044 -3.797  1.00 12.52 ?  103 VAL   A N   1 
ATOM   743  C CA  . VAL   A 1 103 ? -2.222  -12.053 -4.373  1.00 12.43 ?  103 VAL   A CA  1 
ATOM   744  C C   . VAL   A 1 103 ? -3.051  -10.934 -3.735  1.00 12.67 ?  103 VAL   A C   1 
ATOM   745  O O   . VAL   A 1 103 ? -2.943  -10.699 -2.528  1.00 12.92 ?  103 VAL   A O   1 
ATOM   746  C CB  . VAL   A 1 103 ? -2.911  -13.422 -4.225  1.00 12.48 ?  103 VAL   A CB  1 
ATOM   747  C CG1 . VAL   A 1 103 ? -3.206  -13.773 -2.767  1.00 13.37 ?  103 VAL   A CG1 1 
ATOM   748  C CG2 . VAL   A 1 103 ? -4.217  -13.469 -5.024  1.00 12.55 ?  103 VAL   A CG2 1 
ATOM   749  N N   . VAL   A 1 104 ? -3.929  -10.297 -4.508  1.00 13.01 ?  104 VAL   A N   1 
ATOM   750  C CA  . VAL   A 1 104 ? -4.809  -9.269  -3.935  1.00 13.23 ?  104 VAL   A CA  1 
ATOM   751  C C   . VAL   A 1 104 ? -6.090  -9.922  -3.404  1.00 13.14 ?  104 VAL   A C   1 
ATOM   752  O O   . VAL   A 1 104 ? -6.790  -10.659 -4.112  1.00 12.76 ?  104 VAL   A O   1 
ATOM   753  C CB  . VAL   A 1 104 ? -5.158  -8.125  -4.890  1.00 13.61 ?  104 VAL   A CB  1 
ATOM   754  C CG1 . VAL   A 1 104 ? -5.895  -7.012  -4.141  1.00 14.49 ?  104 VAL   A CG1 1 
ATOM   755  C CG2 . VAL   A 1 104 ? -3.960  -7.575  -5.643  1.00 14.88 ?  104 VAL   A CG2 1 
ATOM   756  N N   . PHE   A 1 105 ? -6.341  -9.691  -2.090  1.00 11.83 ?  105 PHE   A N   1 
ATOM   757  C CA  . PHE   A 1 105 ? -7.530  -10.156 -1.447  1.00 12.47 ?  105 PHE   A CA  1 
ATOM   758  C C   . PHE   A 1 105 ? -8.748  -9.471  -2.060  1.00 12.15 ?  105 PHE   A C   1 
ATOM   759  O O   . PHE   A 1 105 ? -8.674  -8.301  -2.485  1.00 11.79 ?  105 PHE   A O   1 
ATOM   760  C CB  . PHE   A 1 105 ? -7.399  -9.786  0.023   1.00 12.15 ?  105 PHE   A CB  1 
ATOM   761  C CG  . PHE   A 1 105 ? -8.550  -10.217 0.903   1.00 12.34 ?  105 PHE   A CG  1 
ATOM   762  C CD1 . PHE   A 1 105 ? -9.663  -9.419  1.092   1.00 13.19 ?  105 PHE   A CD1 1 
ATOM   763  C CD2 . PHE   A 1 105 ? -8.472  -11.415 1.581   1.00 13.06 ?  105 PHE   A CD2 1 
ATOM   764  C CE1 . PHE   A 1 105 ? -10.680 -9.830  1.942   1.00 14.68 ?  105 PHE   A CE1 1 
ATOM   765  C CE2 . PHE   A 1 105 ? -9.463  -11.826 2.444   1.00 14.00 ?  105 PHE   A CE2 1 
ATOM   766  C CZ  . PHE   A 1 105 ? -10.592 -11.061 2.601   1.00 14.26 ?  105 PHE   A CZ  1 
ATOM   767  N N   . PRO   A 1 106 ? -9.895  -10.179 -2.102  1.00 12.67 ?  106 PRO   A N   1 
ATOM   768  C CA  . PRO   A 1 106 ? -11.123 -9.579  -2.616  1.00 13.97 ?  106 PRO   A CA  1 
ATOM   769  C C   . PRO   A 1 106 ? -11.733 -8.658  -1.566  1.00 13.84 ?  106 PRO   A C   1 
ATOM   770  O O   . PRO   A 1 106 ? -12.745 -8.989  -0.935  1.00 13.24 ?  106 PRO   A O   1 
ATOM   771  C CB  . PRO   A 1 106 ? -12.007 -10.783 -3.035  1.00 13.75 ?  106 PRO   A CB  1 
ATOM   772  C CG  . PRO   A 1 106 ? -11.583 -11.830 -2.070  1.00 13.56 ?  106 PRO   A CG  1 
ATOM   773  C CD  . PRO   A 1 106 ? -10.055 -11.618 -1.877  1.00 12.86 ?  106 PRO   A CD  1 
ATOM   774  N N   . TYR   A 1 107 ? -11.156 -7.461  -1.495  1.00 13.55 ?  107 TYR   A N   1 
ATOM   775  C CA  . TYR   A 1 107 ? -11.497 -6.508  -0.452  1.00 14.75 ?  107 TYR   A CA  1 
ATOM   776  C C   . TYR   A 1 107 ? -12.857 -5.854  -0.711  1.00 14.68 ?  107 TYR   A C   1 
ATOM   777  O O   . TYR   A 1 107 ? -13.615 -5.568  0.255   1.00 15.25 ?  107 TYR   A O   1 
ATOM   778  C CB  . TYR   A 1 107 ? -10.374 -5.477  -0.221  1.00 14.37 ?  107 TYR   A CB  1 
ATOM   779  C CG  . TYR   A 1 107 ? -10.020 -4.607  -1.408  1.00 13.59 ?  107 TYR   A CG  1 
ATOM   780  C CD1 . TYR   A 1 107 ? -10.734 -3.445  -1.647  1.00 14.97 ?  107 TYR   A CD1 1 
ATOM   781  C CD2 . TYR   A 1 107 ? -8.963  -4.913  -2.279  1.00 12.90 ?  107 TYR   A CD2 1 
ATOM   782  C CE1 . TYR   A 1 107 ? -10.423 -2.622  -2.716  1.00 14.84 ?  107 TYR   A CE1 1 
ATOM   783  C CE2 . TYR   A 1 107 ? -8.659  -4.108  -3.372  1.00 13.12 ?  107 TYR   A CE2 1 
ATOM   784  C CZ  . TYR   A 1 107 ? -9.388  -2.950  -3.575  1.00 14.80 ?  107 TYR   A CZ  1 
ATOM   785  O OH  . TYR   A 1 107 ? -9.104  -2.143  -4.640  1.00 15.24 ?  107 TYR   A OH  1 
ATOM   786  N N   . ARG   A 1 108 ? -13.224 -5.609  -1.987  1.00 14.09 ?  108 ARG   A N   1 
ATOM   787  C CA  . ARG   A 1 108 ? -14.549 -5.059  -2.228  1.00 13.65 ?  108 ARG   A CA  1 
ATOM   788  C C   . ARG   A 1 108 ? -15.629 -6.048  -1.836  1.00 13.72 ?  108 ARG   A C   1 
ATOM   789  O O   . ARG   A 1 108 ? -16.694 -5.603  -1.343  1.00 15.33 ?  108 ARG   A O   1 
ATOM   790  C CB  . ARG   A 1 108 ? -14.702 -4.631  -3.696  1.00 14.21 ?  108 ARG   A CB  1 
ATOM   791  C CG  . ARG   A 1 108 ? -13.899 -3.367  -3.975  1.00 16.72 ?  108 ARG   A CG  1 
ATOM   792  C CD  . ARG   A 1 108 ? -14.098 -2.833  -5.373  1.00 20.33 ?  108 ARG   A CD  1 
ATOM   793  N NE  . ARG   A 1 108 ? -13.877 -3.903  -6.317  1.00 24.74 ?  108 ARG   A NE  1 
ATOM   794  C CZ  . ARG   A 1 108 ? -12.712 -4.263  -6.823  1.00 27.59 ?  108 ARG   A CZ  1 
ATOM   795  N NH1 . ARG   A 1 108 ? -11.643 -3.511  -6.627  1.00 32.13 ?  108 ARG   A NH1 1 
ATOM   796  N NH2 . ARG   A 1 108 ? -12.619 -5.379  -7.534  1.00 25.53 ?  108 ARG   A NH2 1 
ATOM   797  N N   . ALA   A 1 109 ? -15.357 -7.360  -2.047  1.00 12.67 ?  109 ALA   A N   1 
ATOM   798  C CA  . ALA   A 1 109 ? -16.289 -8.400  -1.656  1.00 13.47 ?  109 ALA   A CA  1 
ATOM   799  C C   . ALA   A 1 109 ? -16.467 -8.400  -0.150  1.00 13.82 ?  109 ALA   A C   1 
ATOM   800  O O   . ALA   A 1 109 ? -17.576 -8.557  0.336   1.00 14.26 ?  109 ALA   A O   1 
ATOM   801  C CB  . ALA   A 1 109 ? -15.884 -9.784  -2.124  1.00 13.90 ?  109 ALA   A CB  1 
ATOM   802  N N   . LEU   A 1 110 ? -15.367 -8.221  0.598   1.00 13.80 ?  110 LEU   A N   1 
ATOM   803  C CA  . LEU   A 1 110 ? -15.472 -8.184  2.050   1.00 13.00 ?  110 LEU   A CA  1 
ATOM   804  C C   . LEU   A 1 110 ? -16.251 -6.947  2.498   1.00 14.13 ?  110 LEU   A C   1 
ATOM   805  O O   . LEU   A 1 110 ? -17.050 -7.039  3.441   1.00 15.31 ?  110 LEU   A O   1 
ATOM   806  C CB  . LEU   A 1 110 ? -14.091 -8.274  2.677   1.00 13.21 ?  110 LEU   A CB  1 
ATOM   807  C CG  . LEU   A 1 110 ? -14.104 -8.019  4.190   1.00 13.89 ?  110 LEU   A CG  1 
ATOM   808  C CD1 . LEU   A 1 110 ? -14.791 -9.186  4.837   1.00 14.31 ?  110 LEU   A CD1 1 
ATOM   809  C CD2 . LEU   A 1 110 ? -12.662 -7.800  4.697   1.00 14.52 ?  110 LEU   A CD2 1 
ATOM   810  N N   . MET   A 1 111 ? -16.058 -5.801  1.846   1.00 14.32 ?  111 MET   A N   1 
ATOM   811  C CA  . MET   A 1 111 ? -16.791 -4.596  2.180   1.00 15.69 ?  111 MET   A CA  1 
ATOM   812  C C   . MET   A 1 111 ? -18.276 -4.760  1.831   1.00 15.98 ?  111 MET   A C   1 
ATOM   813  O O   . MET   A 1 111 ? -19.118 -4.131  2.444   1.00 15.77 ?  111 MET   A O   1 
ATOM   814  C CB  . MET   A 1 111 ? -16.145 -3.379  1.519   1.00 17.58 ?  111 MET   A CB  1 
ATOM   815  C CG  . MET   A 1 111 ? -14.665 -3.118  1.954   1.00 19.17 ?  111 MET   A CG  1 
ATOM   816  S SD  . MET   A 1 111 ? -13.792 -2.010  0.798   1.00 24.51 ?  111 MET   A SD  1 
ATOM   817  C CE  . MET   A 1 111 ? -14.462 -0.544  1.580   1.00 25.50 ?  111 MET   A CE  1 
ATOM   818  N N   . ALA   A 1 112 ? -18.593 -5.717  0.957   1.00 16.88 ?  112 ALA   A N   1 
ATOM   819  C CA  . ALA   A 1 112 ? -19.983 -6.006  0.661   1.00 17.73 ?  112 ALA   A CA  1 
ATOM   820  C C   . ALA   A 1 112 ? -20.504 -7.153  1.535   1.00 18.97 ?  112 ALA   A C   1 
ATOM   821  O O   . ALA   A 1 112 ? -21.539 -7.741  1.227   1.00 19.35 ?  112 ALA   A O   1 
ATOM   822  C CB  . ALA   A 1 112 ? -20.124 -6.332  -0.817  1.00 17.30 ?  112 ALA   A CB  1 
ATOM   823  N N   . GLY   A 1 113 ? -19.751 -7.538  2.571   1.00 17.43 ?  113 GLY   A N   1 
ATOM   824  C CA  . GLY   A 1 113 ? -20.191 -8.511  3.535   1.00 17.03 ?  113 GLY   A CA  1 
ATOM   825  C C   . GLY   A 1 113 ? -19.897 -9.950  3.148   1.00 18.66 ?  113 GLY   A C   1 
ATOM   826  O O   . GLY   A 1 113 ? -20.273 -10.841 3.895   1.00 20.59 ?  113 GLY   A O   1 
ATOM   827  N N   . ASN   A 1 114 ? -19.122 -10.199 2.079   1.00 17.33 ?  114 ASN   A N   1 
ATOM   828  C CA  . ASN   A 1 114 ? -18.791 -11.568 1.722   1.00 17.14 ?  114 ASN   A CA  1 
ATOM   829  C C   . ASN   A 1 114 ? -17.384 -11.898 2.227   1.00 17.98 ?  114 ASN   A C   1 
ATOM   830  O O   . ASN   A 1 114 ? -16.399 -11.566 1.565   1.00 17.66 ?  114 ASN   A O   1 
ATOM   831  C CB  . ASN   A 1 114 ? -18.922 -11.777 0.225   1.00 17.67 ?  114 ASN   A CB  1 
ATOM   832  C CG  . ASN   A 1 114 ? -18.770 -13.223 -0.182  1.00 17.47 ?  114 ASN   A CG  1 
ATOM   833  O OD1 . ASN   A 1 114 ? -18.250 -14.061 0.543   1.00 18.85 ?  114 ASN   A OD1 1 
ATOM   834  N ND2 . ASN   A 1 114 ? -19.207 -13.529 -1.384  1.00 20.63 ?  114 ASN   A ND2 1 
ATOM   835  N N   . GLU   A 1 115 ? -17.304 -12.516 3.408   1.00 18.32 ?  115 GLU   A N   1 
ATOM   836  C CA  . GLU   A 1 115 ? -16.056 -12.972 4.004   1.00 18.42 ?  115 GLU   A CA  1 
ATOM   837  C C   . GLU   A 1 115 ? -15.631 -14.287 3.348   1.00 18.32 ?  115 GLU   A C   1 
ATOM   838  O O   . GLU   A 1 115 ? -14.448 -14.583 3.247   1.00 16.36 ?  115 GLU   A O   1 
ATOM   839  C CB  . GLU   A 1 115 ? -16.234 -13.252 5.493   1.00 19.79 ?  115 GLU   A CB  1 
ATOM   840  C CG  . GLU   A 1 115 ? -16.643 -12.011 6.262   1.00 21.17 ?  115 GLU   A CG  1 
ATOM   841  C CD  . GLU   A 1 115 ? -16.709 -12.215 7.753   1.00 22.45 ?  115 GLU   A CD  1 
ATOM   842  O OE1 . GLU   A 1 115 ? -16.465 -13.340 8.198   1.00 25.67 ?  115 GLU   A OE1 1 
ATOM   843  O OE2 . GLU   A 1 115 ? -17.015 -11.254 8.425   1.00 22.94 ?  115 GLU   A OE2 1 
ATOM   844  N N   . GLN   A 1 116 ? -16.600 -15.057 2.846   1.00 17.53 ?  116 GLN   A N   1 
ATOM   845  C CA  . GLN   A 1 116 ? -16.335 -16.440 2.468   1.00 18.27 ?  116 GLN   A CA  1 
ATOM   846  C C   . GLN   A 1 116 ? -15.476 -16.487 1.200   1.00 17.05 ?  116 GLN   A C   1 
ATOM   847  O O   . GLN   A 1 116 ? -14.601 -17.337 1.062   1.00 17.49 ?  116 GLN   A O   1 
ATOM   848  C CB  . GLN   A 1 116 ? -17.598 -17.283 2.240   1.00 20.75 ?  116 GLN   A CB  1 
ATOM   849  C CG  . GLN   A 1 116 ? -17.321 -18.763 1.967   1.00 22.96 ?  116 GLN   A CG  1 
ATOM   850  C CD  . GLN   A 1 116 ? -16.701 -19.476 3.150   1.00 28.22 ?  116 GLN   A CD  1 
ATOM   851  O OE1 . GLN   A 1 116 ? -17.159 -19.305 4.274   1.00 28.29 ?  116 GLN   A OE1 1 
ATOM   852  N NE2 . GLN   A 1 116 ? -15.642 -20.257 2.971   1.00 27.71 ?  116 GLN   A NE2 1 
ATOM   853  N N   . VAL   A 1 117 ? -15.699 -15.562 0.278   1.00 16.91 ?  117 VAL   A N   1 
ATOM   854  C CA  . VAL   A 1 117 ? -14.974 -15.611 -0.973  1.00 15.37 ?  117 VAL   A CA  1 
ATOM   855  C C   . VAL   A 1 117 ? -13.499 -15.226 -0.739  1.00 16.88 ?  117 VAL   A C   1 
ATOM   856  O O   . VAL   A 1 117 ? -12.639 -15.786 -1.396  1.00 15.10 ?  117 VAL   A O   1 
ATOM   857  C CB  . VAL   A 1 117 ? -15.601 -14.732 -2.075  1.00 15.99 ?  117 VAL   A CB  1 
ATOM   858  C CG1 . VAL   A 1 117 ? -15.484 -13.234 -1.781  1.00 16.03 ?  117 VAL   A CG1 1 
ATOM   859  C CG2 . VAL   A 1 117 ? -14.992 -15.032 -3.433  1.00 16.23 ?  117 VAL   A CG2 1 
ATOM   860  N N   . GLY   A 1 118 ? -13.211 -14.277 0.177   1.00 15.71 ?  118 GLY   A N   1 
ATOM   861  C CA  . GLY   A 1 118 ? -11.833 -13.970 0.545   1.00 14.75 ?  118 GLY   A CA  1 
ATOM   862  C C   . GLY   A 1 118 ? -11.124 -15.200 1.105   1.00 16.22 ?  118 GLY   A C   1 
ATOM   863  O O   . GLY   A 1 118 ? -9.980  -15.512 0.743   1.00 14.12 ?  118 GLY   A O   1 
ATOM   864  N N   . PHE   A 1 119 ? -11.833 -15.938 1.965   1.00 14.67 ?  119 PHE   A N   1 
ATOM   865  C CA  . PHE   A 1 119 ? -11.280 -17.147 2.531   1.00 15.36 ?  119 PHE   A CA  1 
ATOM   866  C C   . PHE   A 1 119 ? -10.969 -18.137 1.409   1.00 15.24 ?  119 PHE   A C   1 
ATOM   867  O O   . PHE   A 1 119 ? -9.883  -18.708 1.331   1.00 14.59 ?  119 PHE   A O   1 
ATOM   868  C CB  . PHE   A 1 119 ? -12.208 -17.734 3.587   1.00 15.37 ?  119 PHE   A CB  1 
ATOM   869  C CG  . PHE   A 1 119 ? -11.651 -19.018 4.170   1.00 16.29 ?  119 PHE   A CG  1 
ATOM   870  C CD1 . PHE   A 1 119 ? -10.753 -19.001 5.241   1.00 16.25 ?  119 PHE   A CD1 1 
ATOM   871  C CD2 . PHE   A 1 119 ? -11.956 -20.241 3.608   1.00 16.50 ?  119 PHE   A CD2 1 
ATOM   872  C CE1 . PHE   A 1 119 ? -10.220 -20.183 5.729   1.00 17.57 ?  119 PHE   A CE1 1 
ATOM   873  C CE2 . PHE   A 1 119 ? -11.421 -21.417 4.110   1.00 18.63 ?  119 PHE   A CE2 1 
ATOM   874  C CZ  . PHE   A 1 119 ? -10.552 -21.389 5.170   1.00 17.59 ?  119 PHE   A CZ  1 
ATOM   875  N N   . ASP   A 1 120 ? -11.946 -18.350 0.531   1.00 14.98 ?  120 ASP   A N   1 
ATOM   876  C CA  . ASP   A 1 120 ? -11.810 -19.398 -0.450  1.00 15.50 ?  120 ASP   A CA  1 
ATOM   877  C C   . ASP   A 1 120 ? -10.751 -19.018 -1.483  1.00 14.66 ?  120 ASP   A C   1 
ATOM   878  O O   . ASP   A 1 120 ? -10.052 -19.897 -1.969  1.00 14.55 ?  120 ASP   A O   1 
ATOM   879  C CB  . ASP   A 1 120 ? -13.140 -19.662 -1.124  1.00 17.09 ?  120 ASP   A CB  1 
ATOM   880  C CG  . ASP   A 1 120 ? -14.192 -20.332 -0.251  1.00 19.73 ?  120 ASP   A CG  1 
ATOM   881  O OD1 . ASP   A 1 120 ? -13.819 -20.909 0.778   1.00 22.29 ?  120 ASP   A OD1 1 
ATOM   882  O OD2 . ASP   A 1 120 ? -15.379 -20.281 -0.650  1.00 20.89 ?  120 ASP   A OD2 1 
ATOM   883  N N   . LEU   A 1 121 ? -10.670 -17.725 -1.819  1.00 14.13 ?  121 LEU   A N   1 
ATOM   884  C CA  . LEU   A 1 121 ? -9.732  -17.277 -2.835  1.00 13.76 ?  121 LEU   A CA  1 
ATOM   885  C C   . LEU   A 1 121 ? -8.305  -17.466 -2.308  1.00 12.92 ?  121 LEU   A C   1 
ATOM   886  O O   . LEU   A 1 121 ? -7.438  -18.000 -3.026  1.00 13.46 ?  121 LEU   A O   1 
ATOM   887  C CB  . LEU   A 1 121 ? -10.015 -15.830 -3.252  1.00 13.43 ?  121 LEU   A CB  1 
ATOM   888  C CG  . LEU   A 1 121 ? -9.222  -15.306 -4.455  1.00 13.46 ?  121 LEU   A CG  1 
ATOM   889  C CD1 . LEU   A 1 121 ? -10.047 -14.283 -5.179  1.00 14.67 ?  121 LEU   A CD1 1 
ATOM   890  C CD2 . LEU   A 1 121 ? -7.871  -14.687 -4.073  1.00 13.44 ?  121 LEU   A CD2 1 
ATOM   891  N N   . VAL   A 1 122 ? -8.051  -17.010 -1.078  1.00 11.85 ?  122 VAL   A N   1 
ATOM   892  C CA  . VAL   A 1 122 ? -6.726  -17.128 -0.484  1.00 12.44 ?  122 VAL   A CA  1 
ATOM   893  C C   . VAL   A 1 122 ? -6.368  -18.597 -0.347  1.00 13.91 ?  122 VAL   A C   1 
ATOM   894  O O   . VAL   A 1 122 ? -5.257  -18.991 -0.636  1.00 14.01 ?  122 VAL   A O   1 
ATOM   895  C CB  . VAL   A 1 122 ? -6.631  -16.419 0.868   1.00 12.17 ?  122 VAL   A CB  1 
ATOM   896  C CG1 . VAL   A 1 122 ? -5.348  -16.768 1.600   1.00 12.20 ?  122 VAL   A CG1 1 
ATOM   897  C CG2 . VAL   A 1 122 ? -6.744  -14.932 0.613   1.00 12.29 ?  122 VAL   A CG2 1 
ATOM   898  N N   . LYS   A 1 123 ? -7.314  -19.395 0.134   1.00 15.42 ?  123 LYS   A N   1 
ATOM   899  C CA  . LYS   A 1 123 ? -7.030  -20.802 0.352   1.00 16.99 ?  123 LYS   A CA  1 
ATOM   900  C C   . LYS   A 1 123 ? -6.608  -21.495 -0.948  1.00 17.05 ?  123 LYS   A C   1 
ATOM   901  O O   . LYS   A 1 123 ? -5.633  -22.252 -0.961  1.00 17.18 ?  123 LYS   A O   1 
ATOM   902  C CB  . LYS   A 1 123 ? -8.260  -21.447 0.986   1.00 19.77 ?  123 LYS   A CB  1 
ATOM   903  C CG  . LYS   A 1 123 ? -8.047  -22.914 1.219   1.00 23.82 ?  123 LYS   A CG  1 
ATOM   904  C CD  . LYS   A 1 123 ? -9.087  -23.560 2.111   1.00 28.38 ?  123 LYS   A CD  1 
ATOM   905  C CE  . LYS   A 1 123 ? -8.929  -25.040 1.934   1.00 36.78 ?  123 LYS   A CE  1 
ATOM   906  N NZ  . LYS   A 1 123 ? -9.741  -25.827 2.861   1.00 43.83 ?  123 LYS   A NZ  1 
ATOM   907  N N   . ALA   A 1 124 ? -7.396  -21.296 -2.014  1.00 16.02 ?  124 ALA   A N   1 
ATOM   908  C CA  . ALA   A 1 124 ? -7.085  -21.909 -3.296  1.00 15.04 ?  124 ALA   A CA  1 
ATOM   909  C C   . ALA   A 1 124 ? -5.695  -21.501 -3.764  1.00 14.50 ?  124 ALA   A C   1 
ATOM   910  O O   . ALA   A 1 124 ? -4.959  -22.354 -4.193  1.00 14.45 ?  124 ALA   A O   1 
ATOM   911  C CB  . ALA   A 1 124 ? -8.156  -21.550 -4.278  1.00 14.60 ?  124 ALA   A CB  1 
ATOM   912  N N   . CYS   A 1 125 ? -5.334  -20.223 -3.618  1.00 13.02 ?  125 CYS   A N   1 
ATOM   913  C CA  . CYS   A 1 125 ? -4.020  -19.750 -4.036  1.00 12.62 ?  125 CYS   A CA  1 
ATOM   914  C C   . CYS   A 1 125 ? -2.912  -20.280 -3.128  1.00 13.48 ?  125 CYS   A C   1 
ATOM   915  O O   . CYS   A 1 125 ? -1.821  -20.623 -3.616  1.00 13.98 ?  125 CYS   A O   1 
ATOM   916  C CB  . CYS   A 1 125 ? -4.010  -18.234 -4.084  1.00 12.81 ?  125 CYS   A CB  1 
ATOM   917  S SG  . CYS   A 1 125 ? -5.047  -17.543 -5.414  1.00 15.16 ?  125 CYS   A SG  1 
ATOM   918  N N   A LYS   A 1 126 ? -3.157  -20.296 -1.810  0.50 13.89 ?  126 LYS   A N   1 
ATOM   919  N N   B LYS   A 1 126 ? -3.152  -20.316 -1.807  0.50 13.34 ?  126 LYS   A N   1 
ATOM   920  C CA  A LYS   A 1 126 ? -2.204  -20.889 -0.887  0.50 15.43 ?  126 LYS   A CA  1 
ATOM   921  C CA  B LYS   A 1 126 ? -2.164  -20.876 -0.897  0.50 14.31 ?  126 LYS   A CA  1 
ATOM   922  C C   A LYS   A 1 126 ? -1.918  -22.349 -1.232  0.50 15.67 ?  126 LYS   A C   1 
ATOM   923  C C   B LYS   A 1 126 ? -1.918  -22.359 -1.199  0.50 15.00 ?  126 LYS   A C   1 
ATOM   924  O O   A LYS   A 1 126 ? -0.769  -22.790 -1.202  0.50 16.27 ?  126 LYS   A O   1 
ATOM   925  O O   B LYS   A 1 126 ? -0.777  -22.820 -1.154  0.50 15.50 ?  126 LYS   A O   1 
ATOM   926  C CB  A LYS   A 1 126 ? -2.714  -20.904 0.555   0.50 15.79 ?  126 LYS   A CB  1 
ATOM   927  C CB  B LYS   A 1 126 ? -2.557  -20.633 0.567   0.50 13.82 ?  126 LYS   A CB  1 
ATOM   928  C CG  A LYS   A 1 126 ? -1.966  -21.928 1.405   0.50 17.04 ?  126 LYS   A CG  1 
ATOM   929  C CG  B LYS   A 1 126 ? -1.689  -21.371 1.598   0.50 14.26 ?  126 LYS   A CG  1 
ATOM   930  C CD  A LYS   A 1 126 ? -0.576  -21.419 1.766   0.50 17.14 ?  126 LYS   A CD  1 
ATOM   931  C CD  B LYS   A 1 126 ? -0.220  -20.958 1.624   0.50 13.91 ?  126 LYS   A CD  1 
ATOM   932  C CE  A LYS   A 1 126 ? 0.270   -22.324 2.608   0.50 17.43 ?  126 LYS   A CE  1 
ATOM   933  C CE  B LYS   A 1 126 ? 0.608   -21.710 2.642   0.50 13.60 ?  126 LYS   A CE  1 
ATOM   934  N NZ  A LYS   A 1 126 ? 0.990   -21.484 3.564   0.50 17.37 ?  126 LYS   A NZ  1 
ATOM   935  N NZ  B LYS   A 1 126 ? 0.022   -21.617 3.994   0.50 13.34 ?  126 LYS   A NZ  1 
ATOM   936  N N   . GLU   A 1 127 ? -2.961  -23.107 -1.546  1.00 15.69 ?  127 GLU   A N   1 
ATOM   937  C CA  . GLU   A 1 127 ? -2.800  -24.523 -1.830  1.00 18.24 ?  127 GLU   A CA  1 
ATOM   938  C C   . GLU   A 1 127 ? -1.888  -24.701 -3.039  1.00 16.78 ?  127 GLU   A C   1 
ATOM   939  O O   . GLU   A 1 127 ? -0.986  -25.543 -3.039  1.00 17.24 ?  127 GLU   A O   1 
ATOM   940  C CB  . GLU   A 1 127 ? -4.136  -25.216 -2.038  1.00 21.04 ?  127 GLU   A CB  1 
ATOM   941  C CG  . GLU   A 1 127 ? -4.821  -25.434 -0.695  1.00 26.80 ?  127 GLU   A CG  1 
ATOM   942  C CD  . GLU   A 1 127 ? -6.043  -26.312 -0.737  1.00 35.17 ?  127 GLU   A CD  1 
ATOM   943  O OE1 . GLU   A 1 127 ? -6.053  -27.355 -1.448  1.00 48.76 ?  127 GLU   A OE1 1 
ATOM   944  O OE2 . GLU   A 1 127 ? -6.947  -25.972 0.057   1.00 43.66 ?  127 GLU   A OE2 1 
ATOM   945  N N   . ALA   A 1 128 ? -2.114  -23.884 -4.072  1.00 17.03 ?  128 ALA   A N   1 
ATOM   946  C CA  . ALA   A 1 128 ? -1.250  -23.961 -5.254  1.00 15.60 ?  128 ALA   A CA  1 
ATOM   947  C C   . ALA   A 1 128 ? 0.203   -23.654 -4.868  1.00 15.19 ?  128 ALA   A C   1 
ATOM   948  O O   . ALA   A 1 128 ? 1.134   -24.398 -5.242  1.00 16.10 ?  128 ALA   A O   1 
ATOM   949  C CB  . ALA   A 1 128 ? -1.749  -22.998 -6.301  1.00 15.40 ?  128 ALA   A CB  1 
ATOM   950  N N   . CYS   A 1 129 ? 0.382   -22.532 -4.155  1.00 14.12 ?  129 CYS   A N   1 
ATOM   951  C CA  . CYS   A 1 129 ? 1.693   -22.064 -3.729  1.00 14.06 ?  129 CYS   A CA  1 
ATOM   952  C C   . CYS   A 1 129 ? 2.402   -23.132 -2.902  1.00 14.80 ?  129 CYS   A C   1 
ATOM   953  O O   . CYS   A 1 129 ? 3.588   -23.421 -3.125  1.00 15.84 ?  129 CYS   A O   1 
ATOM   954  C CB  . CYS   A 1 129 ? 1.555   -20.726 -3.028  1.00 15.13 ?  129 CYS   A CB  1 
ATOM   955  S SG  . CYS   A 1 129 ? 1.283   -19.370 -4.191  1.00 15.41 ?  129 CYS   A SG  1 
ATOM   956  N N   . ALA   A 1 130 ? 1.702   -23.698 -1.915  1.00 15.57 ?  130 ALA   A N   1 
ATOM   957  C CA  . ALA   A 1 130 ? 2.354   -24.588 -0.947  1.00 16.02 ?  130 ALA   A CA  1 
ATOM   958  C C   . ALA   A 1 130 ? 2.836   -25.878 -1.618  1.00 18.11 ?  130 ALA   A C   1 
ATOM   959  O O   . ALA   A 1 130 ? 3.919   -26.395 -1.316  1.00 18.51 ?  130 ALA   A O   1 
ATOM   960  C CB  . ALA   A 1 130 ? 1.402   -24.880 0.177   1.00 16.97 ?  130 ALA   A CB  1 
ATOM   961  N N   . ALA   A 1 131 ? 2.072   -26.346 -2.613  1.00 17.50 ?  131 ALA   A N   1 
ATOM   962  C CA  . ALA   A 1 131 ? 2.465   -27.533 -3.359  1.00 19.46 ?  131 ALA   A CA  1 
ATOM   963  C C   . ALA   A 1 131 ? 3.739   -27.312 -4.181  1.00 19.45 ?  131 ALA   A C   1 
ATOM   964  O O   . ALA   A 1 131 ? 4.376   -28.278 -4.542  1.00 20.41 ?  131 ALA   A O   1 
ATOM   965  C CB  . ALA   A 1 131 ? 1.339   -27.949 -4.274  1.00 21.58 ?  131 ALA   A CB  1 
ATOM   966  N N   . ALA   A 1 132 ? 4.123   -26.067 -4.442  1.00 17.48 ?  132 ALA   A N   1 
ATOM   967  C CA  . ALA   A 1 132 ? 5.339   -25.742 -5.157  1.00 18.02 ?  132 ALA   A CA  1 
ATOM   968  C C   . ALA   A 1 132 ? 6.398   -25.078 -4.279  1.00 16.74 ?  132 ALA   A C   1 
ATOM   969  O O   . ALA   A 1 132 ? 7.373   -24.528 -4.813  1.00 18.02 ?  132 ALA   A O   1 
ATOM   970  C CB  . ALA   A 1 132 ? 4.965   -24.800 -6.298  1.00 18.95 ?  132 ALA   A CB  1 
ATOM   971  N N   . ASN   A 1 133 ? 6.229   -25.060 -2.941  1.00 16.40 ?  133 ASN   A N   1 
ATOM   972  C CA  . ASN   A 1 133 ? 7.178   -24.418 -2.027  1.00 17.78 ?  133 ASN   A CA  1 
ATOM   973  C C   . ASN   A 1 133 ? 7.330   -22.922 -2.336  1.00 17.23 ?  133 ASN   A C   1 
ATOM   974  O O   . ASN   A 1 133 ? 8.413   -22.345 -2.270  1.00 16.04 ?  133 ASN   A O   1 
ATOM   975  C CB  . ASN   A 1 133 ? 8.524   -25.144 -1.987  1.00 21.66 ?  133 ASN   A CB  1 
ATOM   976  C CG  . ASN   A 1 133 ? 8.395   -26.590 -1.557  1.00 27.28 ?  133 ASN   A CG  1 
ATOM   977  O OD1 . ASN   A 1 133 ? 8.722   -27.506 -2.320  1.00 37.03 ?  133 ASN   A OD1 1 
ATOM   978  N ND2 . ASN   A 1 133 ? 7.939   -26.840 -0.341  1.00 30.02 ?  133 ASN   A ND2 1 
ATOM   979  N N   . VAL   A 1 134 ? 6.230   -22.289 -2.720  1.00 14.08 ?  134 VAL   A N   1 
ATOM   980  C CA  . VAL   A 1 134 ? 6.164   -20.852 -2.985  1.00 14.50 ?  134 VAL   A CA  1 
ATOM   981  C C   . VAL   A 1 134 ? 5.406   -20.221 -1.817  1.00 15.88 ?  134 VAL   A C   1 
ATOM   982  O O   . VAL   A 1 134 ? 4.387   -20.765 -1.372  1.00 15.02 ?  134 VAL   A O   1 
ATOM   983  C CB  . VAL   A 1 134 ? 5.419   -20.682 -4.333  1.00 14.28 ?  134 VAL   A CB  1 
ATOM   984  C CG1 . VAL   A 1 134 ? 4.951   -19.261 -4.589  1.00 13.78 ?  134 VAL   A CG1 1 
ATOM   985  C CG2 . VAL   A 1 134 ? 6.282   -21.182 -5.485  1.00 15.13 ?  134 VAL   A CG2 1 
ATOM   986  N N   . LEU   A 1 135 ? 5.883   -19.078 -1.340  1.00 16.06 ?  135 LEU   A N   1 
ATOM   987  C CA  . LEU   A 1 135 ? 5.191   -18.364 -0.292  1.00 16.68 ?  135 LEU   A CA  1 
ATOM   988  C C   . LEU   A 1 135 ? 4.094   -17.539 -0.933  1.00 15.26 ?  135 LEU   A C   1 
ATOM   989  O O   . LEU   A 1 135 ? 4.270   -16.973 -2.014  1.00 16.10 ?  135 LEU   A O   1 
ATOM   990  C CB  . LEU   A 1 135 ? 6.142   -17.462 0.482   1.00 20.70 ?  135 LEU   A CB  1 
ATOM   991  C CG  . LEU   A 1 135 ? 7.211   -18.162 1.329   1.00 24.29 ?  135 LEU   A CG  1 
ATOM   992  C CD1 . LEU   A 1 135 ? 7.715   -17.007 2.198   1.00 25.20 ?  135 LEU   A CD1 1 
ATOM   993  C CD2 . LEU   A 1 135 ? 6.767   -19.337 2.190   1.00 25.51 ?  135 LEU   A CD2 1 
ATOM   994  N N   . LEU   A 1 136 ? 3.002   -17.409 -0.179  1.00 14.21 ?  136 LEU   A N   1 
ATOM   995  C CA  . LEU   A 1 136 ? 1.896   -16.554 -0.566  1.00 13.29 ?  136 LEU   A CA  1 
ATOM   996  C C   . LEU   A 1 136 ? 1.805   -15.357 0.362   1.00 12.53 ?  136 LEU   A C   1 
ATOM   997  O O   . LEU   A 1 136 ? 1.586   -15.535 1.566   1.00 14.05 ?  136 LEU   A O   1 
ATOM   998  C CB  . LEU   A 1 136 ? 0.577   -17.322 -0.618  1.00 12.90 ?  136 LEU   A CB  1 
ATOM   999  C CG  . LEU   A 1 136 ? -0.595  -16.477 -1.088  1.00 13.53 ?  136 LEU   A CG  1 
ATOM   1000 C CD1 . LEU   A 1 136 ? -0.684  -16.255 -2.593  1.00 13.47 ?  136 LEU   A CD1 1 
ATOM   1001 C CD2 . LEU   A 1 136 ? -1.823  -17.201 -0.649  1.00 15.14 ?  136 LEU   A CD2 1 
ATOM   1002 N N   . LYS   A 1 137 ? 1.905   -14.153 -0.225  1.00 12.40 ?  137 LYS   A N   1 
ATOM   1003 C CA  . LYS   A 1 137 ? 1.546   -12.942 0.473   1.00 12.23 ?  137 LYS   A CA  1 
ATOM   1004 C C   . LYS   A 1 137 ? 0.134   -12.568 0.036   1.00 12.32 ?  137 LYS   A C   1 
ATOM   1005 O O   . LYS   A 1 137 ? -0.204  -12.750 -1.130  1.00 11.95 ?  137 LYS   A O   1 
ATOM   1006 C CB  . LYS   A 1 137 ? 2.470   -11.772 0.177   1.00 12.25 ?  137 LYS   A CB  1 
ATOM   1007 C CG  . LYS   A 1 137 ? 3.988   -12.112 0.285   1.00 12.66 ?  137 LYS   A CG  1 
ATOM   1008 C CD  . LYS   A 1 137 ? 4.873   -10.889 0.443   1.00 13.68 ?  137 LYS   A CD  1 
ATOM   1009 C CE  . LYS   A 1 137 ? 6.361   -11.129 0.167   1.00 13.32 ?  137 LYS   A CE  1 
ATOM   1010 N NZ  . LYS   A 1 137 ? 6.613   -11.138 -1.294  1.00 12.97 ?  137 LYS   A NZ  1 
ATOM   1011 N N   . VAL   A 1 138 ? -0.635  -11.954 0.953   1.00 11.59 ?  138 VAL   A N   1 
ATOM   1012 C CA  . VAL   A 1 138 ? -1.983  -11.505 0.668   1.00 11.28 ?  138 VAL   A CA  1 
ATOM   1013 C C   . VAL   A 1 138 ? -2.078  -9.995  0.903   1.00 11.72 ?  138 VAL   A C   1 
ATOM   1014 O O   . VAL   A 1 138 ? -1.919  -9.488  2.027   1.00 11.62 ?  138 VAL   A O   1 
ATOM   1015 C CB  . VAL   A 1 138 ? -3.045  -12.262 1.471   1.00 10.76 ?  138 VAL   A CB  1 
ATOM   1016 C CG1 . VAL   A 1 138 ? -4.415  -11.691 1.151   1.00 10.98 ?  138 VAL   A CG1 1 
ATOM   1017 C CG2 . VAL   A 1 138 ? -3.028  -13.777 1.255   1.00 11.23 ?  138 VAL   A CG2 1 
ATOM   1018 N N   . ILE   A 1 139 ? -2.377  -9.273  -0.184  1.00 11.90 ?  139 ILE   A N   1 
ATOM   1019 C CA  . ILE   A 1 139 ? -2.553  -7.829  -0.144  1.00 12.48 ?  139 ILE   A CA  1 
ATOM   1020 C C   . ILE   A 1 139 ? -4.015  -7.531  0.178   1.00 13.55 ?  139 ILE   A C   1 
ATOM   1021 O O   . ILE   A 1 139 ? -4.881  -7.782  -0.623  1.00 13.11 ?  139 ILE   A O   1 
ATOM   1022 C CB  . ILE   A 1 139 ? -2.204  -7.207  -1.494  1.00 13.01 ?  139 ILE   A CB  1 
ATOM   1023 C CG1 . ILE   A 1 139 ? -0.798  -7.550  -1.942  1.00 14.07 ?  139 ILE   A CG1 1 
ATOM   1024 C CG2 . ILE   A 1 139 ? -2.497  -5.710  -1.507  1.00 13.46 ?  139 ILE   A CG2 1 
ATOM   1025 C CD1 . ILE   A 1 139 ? -0.637  -7.397  -3.471  1.00 13.89 ?  139 ILE   A CD1 1 
ATOM   1026 N N   . ILE   A 1 140 ? -4.252  -6.936  1.336   1.00 12.88 ?  140 ILE   A N   1 
ATOM   1027 C CA  . ILE   A 1 140 ? -5.607  -6.630  1.758   1.00 12.63 ?  140 ILE   A CA  1 
ATOM   1028 C C   . ILE   A 1 140 ? -6.093  -5.242  1.359   1.00 12.18 ?  140 ILE   A C   1 
ATOM   1029 O O   . ILE   A 1 140 ? -7.306  -5.014  1.433   1.00 12.74 ?  140 ILE   A O   1 
ATOM   1030 C CB  . ILE   A 1 140 ? -5.767  -6.831  3.270   1.00 12.48 ?  140 ILE   A CB  1 
ATOM   1031 C CG1 . ILE   A 1 140 ? -4.975  -5.852  4.119   1.00 12.50 ?  140 ILE   A CG1 1 
ATOM   1032 C CG2 . ILE   A 1 140 ? -5.511  -8.299  3.603   1.00 12.56 ?  140 ILE   A CG2 1 
ATOM   1033 C CD1 . ILE   A 1 140 ? -5.380  -5.908  5.604   1.00 14.09 ?  140 ILE   A CD1 1 
ATOM   1034 N N   . GLU   A 1 141 ? -5.202  -4.355  0.936   1.00 11.99 ?  141 GLU   A N   1 
ATOM   1035 C CA  . GLU   A 1 141 ? -5.560  -3.004  0.500   1.00 12.53 ?  141 GLU   A CA  1 
ATOM   1036 C C   . GLU   A 1 141 ? -6.218  -2.209  1.626   1.00 12.90 ?  141 GLU   A C   1 
ATOM   1037 O O   . GLU   A 1 141 ? -7.323  -1.667  1.495   1.00 13.61 ?  141 GLU   A O   1 
ATOM   1038 C CB  . GLU   A 1 141 ? -6.394  -3.001  -0.798  1.00 12.55 ?  141 GLU   A CB  1 
ATOM   1039 C CG  . GLU   A 1 141 ? -6.224  -1.713  -1.593  1.00 12.91 ?  141 GLU   A CG  1 
ATOM   1040 C CD  . GLU   A 1 141 ? -4.898  -1.668  -2.338  1.00 13.37 ?  141 GLU   A CD  1 
ATOM   1041 O OE1 . GLU   A 1 141 ? -4.948  -1.827  -3.574  1.00 14.28 ?  141 GLU   A OE1 1 
ATOM   1042 O OE2 . GLU   A 1 141 ? -3.867  -1.419  -1.694  1.00 12.22 ?  141 GLU   A OE2 1 
ATOM   1043 N N   . THR   A 1 142 ? -5.376  -1.923  2.632   1.00 13.87 ?  142 THR   A N   1 
ATOM   1044 C CA  . THR   A 1 142 ? -5.762  -1.188  3.809   1.00 14.58 ?  142 THR   A CA  1 
ATOM   1045 C C   . THR   A 1 142 ? -6.303  0.173   3.408   1.00 14.64 ?  142 THR   A C   1 
ATOM   1046 O O   . THR   A 1 142 ? -7.222  0.669   4.043   1.00 14.36 ?  142 THR   A O   1 
ATOM   1047 C CB  . THR   A 1 142 ? -4.588  -1.026  4.774   1.00 14.03 ?  142 THR   A CB  1 
ATOM   1048 O OG1 . THR   A 1 142 ? -3.522  -0.397  4.076   1.00 14.55 ?  142 THR   A OG1 1 
ATOM   1049 C CG2 . THR   A 1 142 ? -4.164  -2.358  5.365   1.00 14.81 ?  142 THR   A CG2 1 
ATOM   1050 N N   . GLY   A 1 143 ? -5.769  0.757   2.358   1.00 15.81 ?  143 GLY   A N   1 
ATOM   1051 C CA  . GLY   A 1 143 ? -6.189  2.100   1.975   1.00 17.12 ?  143 GLY   A CA  1 
ATOM   1052 C C   . GLY   A 1 143 ? -7.577  2.154   1.344   1.00 16.54 ?  143 GLY   A C   1 
ATOM   1053 O O   . GLY   A 1 143 ? -8.181  3.224   1.295   1.00 18.47 ?  143 GLY   A O   1 
ATOM   1054 N N   . GLU   A 1 144 ? -8.112  1.011   0.907   1.00 15.31 ?  144 GLU   A N   1 
ATOM   1055 C CA  . GLU   A 1 144 ? -9.485  0.945   0.434   1.00 15.60 ?  144 GLU   A CA  1 
ATOM   1056 C C   . GLU   A 1 144 ? -10.411 0.450   1.549   1.00 16.49 ?  144 GLU   A C   1 
ATOM   1057 O O   . GLU   A 1 144 ? -11.542 0.911   1.685   1.00 17.33 ?  144 GLU   A O   1 
ATOM   1058 C CB  . GLU   A 1 144 ? -9.593  0.077   -0.820  1.00 16.14 ?  144 GLU   A CB  1 
ATOM   1059 C CG  . GLU   A 1 144 ? -8.919  0.687   -2.040  1.00 16.90 ?  144 GLU   A CG  1 
ATOM   1060 C CD  . GLU   A 1 144 ? -9.577  1.999   -2.444  1.00 18.98 ?  144 GLU   A CD  1 
ATOM   1061 O OE1 . GLU   A 1 144 ? -10.818 2.059   -2.501  1.00 21.16 ?  144 GLU   A OE1 1 
ATOM   1062 O OE2 . GLU   A 1 144 ? -8.881  2.980   -2.711  1.00 21.04 ?  144 GLU   A OE2 1 
ATOM   1063 N N   . LEU   A 1 145 ? -9.946  -0.471  2.389   1.00 15.46 ?  145 LEU   A N   1 
ATOM   1064 C CA  . LEU   A 1 145 ? -10.767 -0.952  3.496   1.00 15.75 ?  145 LEU   A CA  1 
ATOM   1065 C C   . LEU   A 1 145 ? -11.039 0.183   4.462   1.00 15.99 ?  145 LEU   A C   1 
ATOM   1066 O O   . LEU   A 1 145 ? -12.147 0.296   4.977   1.00 16.38 ?  145 LEU   A O   1 
ATOM   1067 C CB  . LEU   A 1 145 ? -10.051 -2.085  4.237   1.00 15.16 ?  145 LEU   A CB  1 
ATOM   1068 C CG  . LEU   A 1 145 ? -9.923  -3.398  3.456   1.00 15.02 ?  145 LEU   A CG  1 
ATOM   1069 C CD1 . LEU   A 1 145 ? -9.073  -4.398  4.137   1.00 15.50 ?  145 LEU   A CD1 1 
ATOM   1070 C CD2 . LEU   A 1 145 ? -11.291 -4.011  3.140   1.00 15.90 ?  145 LEU   A CD2 1 
ATOM   1071 N N   . LYS   A 1 146 ? -9.968  0.886   4.836   1.00 18.04 ?  146 LYS   A N   1 
ATOM   1072 C CA  . LYS   A 1 146 ? -9.995  2.106   5.649   1.00 20.96 ?  146 LYS   A CA  1 
ATOM   1073 C C   . LYS   A 1 146 ? -10.288 1.864   7.127   1.00 20.40 ?  146 LYS   A C   1 
ATOM   1074 O O   . LYS   A 1 146 ? -9.523  2.296   7.998   1.00 21.20 ?  146 LYS   A O   1 
ATOM   1075 C CB  . LYS   A 1 146 ? -10.911 3.174   5.061   1.00 25.46 ?  146 LYS   A CB  1 
ATOM   1076 C CG  . LYS   A 1 146 ? -10.384 3.743   3.748   1.00 27.92 ?  146 LYS   A CG  1 
ATOM   1077 C CD  . LYS   A 1 146 ? -11.402 4.668   3.092   1.00 34.64 ?  146 LYS   A CD  1 
ATOM   1078 C CE  . LYS   A 1 146 ? -11.115 5.007   1.664   1.00 37.64 ?  146 LYS   A CE  1 
ATOM   1079 N NZ  . LYS   A 1 146 ? -10.002 5.949   1.546   1.00 41.43 ?  146 LYS   A NZ  1 
ATOM   1080 N N   . ASP   A 1 147 ? -11.386 1.185   7.385   1.00 19.71 ?  147 ASP   A N   1 
ATOM   1081 C CA  . ASP   A 1 147 ? -11.865 0.961   8.728   1.00 22.40 ?  147 ASP   A CA  1 
ATOM   1082 C C   . ASP   A 1 147 ? -11.008 -0.066  9.462   1.00 17.99 ?  147 ASP   A C   1 
ATOM   1083 O O   . ASP   A 1 147 ? -10.739 -1.136  8.936   1.00 16.45 ?  147 ASP   A O   1 
ATOM   1084 C CB  . ASP   A 1 147 ? -13.253 0.358   8.630   1.00 27.17 ?  147 ASP   A CB  1 
ATOM   1085 C CG  . ASP   A 1 147 ? -13.885 0.073   9.967   1.00 35.26 ?  147 ASP   A CG  1 
ATOM   1086 O OD1 . ASP   A 1 147 ? -14.408 1.039   10.572  1.00 42.53 ?  147 ASP   A OD1 1 
ATOM   1087 O OD2 . ASP   A 1 147 ? -13.782 -1.092  10.389  1.00 44.09 ?  147 ASP   A OD2 1 
ATOM   1088 N N   . GLU   A 1 148 ? -10.696 0.211   10.724  1.00 18.59 ?  148 GLU   A N   1 
ATOM   1089 C CA  . GLU   A 1 148 ? -9.864  -0.680  11.511  1.00 18.60 ?  148 GLU   A CA  1 
ATOM   1090 C C   . GLU   A 1 148 ? -10.449 -2.094  11.582  1.00 17.15 ?  148 GLU   A C   1 
ATOM   1091 O O   . GLU   A 1 148 ? -9.708  -3.062  11.453  1.00 16.42 ?  148 GLU   A O   1 
ATOM   1092 C CB  . GLU   A 1 148 ? -9.602  -0.123  12.908  1.00 21.68 ?  148 GLU   A CB  1 
ATOM   1093 C CG  . GLU   A 1 148 ? -8.761  -1.084  13.735  1.00 24.21 ?  148 GLU   A CG  1 
ATOM   1094 C CD  . GLU   A 1 148 ? -8.324  -0.599  15.106  1.00 28.92 ?  148 GLU   A CD  1 
ATOM   1095 O OE1 . GLU   A 1 148 ? -8.342  0.621   15.381  1.00 26.29 ?  148 GLU   A OE1 1 
ATOM   1096 O OE2 . GLU   A 1 148 ? -7.950  -1.513  15.866  1.00 28.87 ?  148 GLU   A OE2 1 
ATOM   1097 N N   . ALA   A 1 149 ? -11.748 -2.230  11.875  1.00 17.16 ?  149 ALA   A N   1 
ATOM   1098 C CA  . ALA   A 1 149 ? -12.358 -3.552  11.938  1.00 18.26 ?  149 ALA   A CA  1 
ATOM   1099 C C   . ALA   A 1 149 ? -12.252 -4.319  10.617  1.00 17.02 ?  149 ALA   A C   1 
ATOM   1100 O O   . ALA   A 1 149 ? -12.060 -5.538  10.648  1.00 16.83 ?  149 ALA   A O   1 
ATOM   1101 C CB  . ALA   A 1 149 ? -13.819 -3.446  12.344  1.00 18.77 ?  149 ALA   A CB  1 
ATOM   1102 N N   . LEU   A 1 150 ? -12.378 -3.627  9.465   1.00 17.25 ?  150 LEU   A N   1 
ATOM   1103 C CA  . LEU   A 1 150 ? -12.271 -4.288  8.173   1.00 17.51 ?  150 LEU   A CA  1 
ATOM   1104 C C   . LEU   A 1 150 ? -10.833 -4.719  7.905   1.00 15.35 ?  150 LEU   A C   1 
ATOM   1105 O O   . LEU   A 1 150 ? -10.616 -5.814  7.392   1.00 14.91 ?  150 LEU   A O   1 
ATOM   1106 C CB  . LEU   A 1 150 ? -12.789 -3.432  7.023   1.00 17.17 ?  150 LEU   A CB  1 
ATOM   1107 C CG  . LEU   A 1 150 ? -14.314 -3.281  6.936   1.00 20.15 ?  150 LEU   A CG  1 
ATOM   1108 C CD1 . LEU   A 1 150 ? -14.740 -2.148  6.028   1.00 20.93 ?  150 LEU   A CD1 1 
ATOM   1109 C CD2 . LEU   A 1 150 ? -14.875 -4.588  6.430   1.00 21.96 ?  150 LEU   A CD2 1 
ATOM   1110 N N   . ILE   A 1 151 ? -9.863  -3.885  8.287   1.00 15.77 ?  151 ILE   A N   1 
ATOM   1111 C CA  . ILE   A 1 151 ? -8.461  -4.263  8.179   1.00 14.55 ?  151 ILE   A CA  1 
ATOM   1112 C C   . ILE   A 1 151 ? -8.187  -5.511  9.016   1.00 14.12 ?  151 ILE   A C   1 
ATOM   1113 O O   . ILE   A 1 151 ? -7.527  -6.450  8.556   1.00 14.76 ?  151 ILE   A O   1 
ATOM   1114 C CB  . ILE   A 1 151 ? -7.556  -3.077  8.546   1.00 15.03 ?  151 ILE   A CB  1 
ATOM   1115 C CG1 . ILE   A 1 151 ? -7.719  -1.971  7.527   1.00 16.01 ?  151 ILE   A CG1 1 
ATOM   1116 C CG2 . ILE   A 1 151 ? -6.091  -3.503  8.665   1.00 14.83 ?  151 ILE   A CG2 1 
ATOM   1117 C CD1 . ILE   A 1 151 ? -7.078  -0.670  7.948   1.00 17.27 ?  151 ILE   A CD1 1 
ATOM   1118 N N   . ARG   A 1 152 ? -8.734  -5.572  10.236  1.00 14.43 ?  152 ARG   A N   1 
ATOM   1119 C CA  . ARG   A 1 152 ? -8.487  -6.740  11.066  1.00 15.33 ?  152 ARG   A CA  1 
ATOM   1120 C C   . ARG   A 1 152 ? -9.137  -7.979  10.479  1.00 15.57 ?  152 ARG   A C   1 
ATOM   1121 O O   . ARG   A 1 152 ? -8.556  -9.064  10.548  1.00 15.03 ?  152 ARG   A O   1 
ATOM   1122 C CB  . ARG   A 1 152 ? -8.957  -6.584  12.520  1.00 16.48 ?  152 ARG   A CB  1 
ATOM   1123 C CG  . ARG   A 1 152 ? -8.204  -5.520  13.299  1.00 17.82 ?  152 ARG   A CG  1 
ATOM   1124 C CD  . ARG   A 1 152 ? -8.570  -5.622  14.796  1.00 20.30 ?  152 ARG   A CD  1 
ATOM   1125 N NE  . ARG   A 1 152 ? -7.943  -4.491  15.448  1.00 22.72 ?  152 ARG   A NE  1 
ATOM   1126 C CZ  . ARG   A 1 152 ? -6.676  -4.449  15.888  1.00 26.37 ?  152 ARG   A CZ  1 
ATOM   1127 N NH1 . ARG   A 1 152 ? -5.938  -5.544  15.924  1.00 26.52 ?  152 ARG   A NH1 1 
ATOM   1128 N NH2 . ARG   A 1 152 ? -6.164  -3.309  16.306  1.00 25.89 ?  152 ARG   A NH2 1 
ATOM   1129 N N   . LYS   A 1 153 ? -10.375 -7.837  9.953   1.00 15.71 ?  153 LYS   A N   1 
ATOM   1130 C CA  . LYS   A 1 153 ? -11.106 -8.978  9.463   1.00 15.90 ?  153 LYS   A CA  1 
ATOM   1131 C C   . LYS   A 1 153 ? -10.387 -9.550  8.234   1.00 15.46 ?  153 LYS   A C   1 
ATOM   1132 O O   . LYS   A 1 153 ? -10.280 -10.754 8.074   1.00 15.52 ?  153 LYS   A O   1 
ATOM   1133 C CB  . LYS   A 1 153 ? -12.554 -8.597  9.157   1.00 17.89 ?  153 LYS   A CB  1 
ATOM   1134 C CG  . LYS   A 1 153 ? -13.383 -9.760  8.680   1.00 20.86 ?  153 LYS   A CG  1 
ATOM   1135 C CD  . LYS   A 1 153 ? -13.472 -10.956 9.600   1.00 25.31 ?  153 LYS   A CD  1 
ATOM   1136 C CE  . LYS   A 1 153 ? -14.135 -10.614 10.926  1.00 27.51 ?  153 LYS   A CE  1 
ATOM   1137 N NZ  . LYS   A 1 153 ? -14.112 -11.812 11.762  1.00 29.54 ?  153 LYS   A NZ  1 
ATOM   1138 N N   . ALA   A 1 154 ? -9.986  -8.677  7.321   1.00 14.60 ?  154 ALA   A N   1 
ATOM   1139 C CA  . ALA   A 1 154 ? -9.287  -9.118  6.126   1.00 14.70 ?  154 ALA   A CA  1 
ATOM   1140 C C   . ALA   A 1 154 ? -8.008  -9.843  6.504   1.00 13.04 ?  154 ALA   A C   1 
ATOM   1141 O O   . ALA   A 1 154 ? -7.668  -10.862 5.883   1.00 12.66 ?  154 ALA   A O   1 
ATOM   1142 C CB  . ALA   A 1 154 ? -9.023  -7.948  5.210   1.00 14.02 ?  154 ALA   A CB  1 
ATOM   1143 N N   . SER   A 1 155 ? -7.286  -9.300  7.472   1.00 12.92 ?  155 SER   A N   1 
ATOM   1144 C CA  . SER   A 1 155 ? -6.041  -9.911  7.955   1.00 12.50 ?  155 SER   A CA  1 
ATOM   1145 C C   . SER   A 1 155 ? -6.356  -11.292 8.526   1.00 13.30 ?  155 SER   A C   1 
ATOM   1146 O O   . SER   A 1 155 ? -5.688  -12.286 8.223   1.00 13.80 ?  155 SER   A O   1 
ATOM   1147 C CB  . SER   A 1 155 ? -5.335  -9.033  8.976   1.00 12.24 ?  155 SER   A CB  1 
ATOM   1148 O OG  . SER   A 1 155 ? -5.070  -7.717  8.475   1.00 12.20 ?  155 SER   A OG  1 
ATOM   1149 N N   . GLU   A 1 156 ? -7.427  -11.370 9.329   1.00 12.80 ?  156 GLU   A N   1 
ATOM   1150 C CA  . GLU   A 1 156 ? -7.814  -12.606 9.976   1.00 15.36 ?  156 GLU   A CA  1 
ATOM   1151 C C   . GLU   A 1 156 ? -8.198  -13.697 8.981   1.00 14.21 ?  156 GLU   A C   1 
ATOM   1152 O O   . GLU   A 1 156 ? -7.783  -14.847 9.107   1.00 14.77 ?  156 GLU   A O   1 
ATOM   1153 C CB  . GLU   A 1 156 ? -8.951  -12.299 10.951  1.00 18.31 ?  156 GLU   A CB  1 
ATOM   1154 C CG  . GLU   A 1 156 ? -9.454  -13.561 11.641  1.00 23.80 ?  156 GLU   A CG  1 
ATOM   1155 C CD  . GLU   A 1 156 ? -10.685 -13.291 12.502  1.00 32.47 ?  156 GLU   A CD  1 
ATOM   1156 O OE1 . GLU   A 1 156 ? -11.521 -12.515 12.017  1.00 33.31 ?  156 GLU   A OE1 1 
ATOM   1157 O OE2 . GLU   A 1 156 ? -10.788 -13.869 13.616  1.00 34.25 ?  156 GLU   A OE2 1 
ATOM   1158 N N   . ILE   A 1 157 ? -9.036  -13.334 7.993   1.00 14.26 ?  157 ILE   A N   1 
ATOM   1159 C CA  . ILE   A 1 157 ? -9.468  -14.270 6.981   1.00 14.22 ?  157 ILE   A CA  1 
ATOM   1160 C C   . ILE   A 1 157 ? -8.258  -14.756 6.173   1.00 13.16 ?  157 ILE   A C   1 
ATOM   1161 O O   . ILE   A 1 157 ? -8.116  -15.952 5.973   1.00 13.77 ?  157 ILE   A O   1 
ATOM   1162 C CB  . ILE   A 1 157 ? -10.527 -13.626 6.069   1.00 14.23 ?  157 ILE   A CB  1 
ATOM   1163 C CG1 . ILE   A 1 157 ? -11.789 -13.280 6.859   1.00 15.64 ?  157 ILE   A CG1 1 
ATOM   1164 C CG2 . ILE   A 1 157 ? -10.830 -14.540 4.875   1.00 13.81 ?  157 ILE   A CG2 1 
ATOM   1165 C CD1 . ILE   A 1 157 ? -12.720 -12.371 6.089   1.00 16.16 ?  157 ILE   A CD1 1 
ATOM   1166 N N   . SER   A 1 158 ? -7.341  -13.838 5.833   1.00 12.72 ?  158 SER   A N   1 
ATOM   1167 C CA  . SER   A 1 158 ? -6.155  -14.214 5.082   1.00 13.55 ?  158 SER   A CA  1 
ATOM   1168 C C   . SER   A 1 158 ? -5.300  -15.220 5.859   1.00 14.03 ?  158 SER   A C   1 
ATOM   1169 O O   . SER   A 1 158 ? -4.898  -16.243 5.313   1.00 13.73 ?  158 SER   A O   1 
ATOM   1170 C CB  . SER   A 1 158 ? -5.405  -12.963 4.729   1.00 13.47 ?  158 SER   A CB  1 
ATOM   1171 O OG  . SER   A 1 158 ? -6.206  -12.174 3.873   1.00 13.88 ?  158 SER   A OG  1 
ATOM   1172 N N   . ILE   A 1 159 ? -5.103  -14.977 7.164   1.00 14.34 ?  159 ILE   A N   1 
ATOM   1173 C CA  . ILE   A 1 159 ? -4.290  -15.845 7.997   1.00 14.22 ?  159 ILE   A CA  1 
ATOM   1174 C C   . ILE   A 1 159 ? -4.965  -17.209 8.091   1.00 15.13 ?  159 ILE   A C   1 
ATOM   1175 O O   . ILE   A 1 159 ? -4.334  -18.256 8.007   1.00 14.70 ?  159 ILE   A O   1 
ATOM   1176 C CB  . ILE   A 1 159 ? -4.099  -15.186 9.375   1.00 16.35 ?  159 ILE   A CB  1 
ATOM   1177 C CG1 . ILE   A 1 159 ? -3.127  -13.965 9.238   1.00 17.70 ?  159 ILE   A CG1 1 
ATOM   1178 C CG2 . ILE   A 1 159 ? -3.644  -16.223 10.410  1.00 17.27 ?  159 ILE   A CG2 1 
ATOM   1179 C CD1 . ILE   A 1 159 ? -3.009  -13.047 10.449  1.00 17.93 ?  159 ILE   A CD1 1 
ATOM   1180 N N   . LYS   A 1 160 ? -6.266  -17.204 8.407   1.00 15.47 ?  160 LYS   A N   1 
ATOM   1181 C CA  . LYS   A 1 160 ? -6.979  -18.461 8.521   1.00 17.23 ?  160 LYS   A CA  1 
ATOM   1182 C C   . LYS   A 1 160 ? -6.910  -19.295 7.246   1.00 16.99 ?  160 LYS   A C   1 
ATOM   1183 O O   . LYS   A 1 160 ? -6.879  -20.519 7.310   1.00 16.00 ?  160 LYS   A O   1 
ATOM   1184 C CB  . LYS   A 1 160 ? -8.445  -18.220 8.867   1.00 19.11 ?  160 LYS   A CB  1 
ATOM   1185 C CG  . LYS   A 1 160 ? -8.674  -17.863 10.315  1.00 24.10 ?  160 LYS   A CG  1 
ATOM   1186 C CD  . LYS   A 1 160 ? -10.164 -17.605 10.533  1.00 28.75 ?  160 LYS   A CD  1 
ATOM   1187 C CE  . LYS   A 1 160 ? -10.441 -17.248 11.955  1.00 34.54 ?  160 LYS   A CE  1 
ATOM   1188 N NZ  . LYS   A 1 160 ? -11.865 -16.958 12.136  1.00 37.63 ?  160 LYS   A NZ  1 
ATOM   1189 N N   . ALA   A 1 161 ? -6.921  -18.630 6.098   1.00 15.89 ?  161 ALA   A N   1 
ATOM   1190 C CA  . ALA   A 1 161 ? -6.891  -19.332 4.823   1.00 16.62 ?  161 ALA   A CA  1 
ATOM   1191 C C   . ALA   A 1 161 ? -5.489  -19.806 4.442   1.00 16.12 ?  161 ALA   A C   1 
ATOM   1192 O O   . ALA   A 1 161 ? -5.335  -20.451 3.423   1.00 15.07 ?  161 ALA   A O   1 
ATOM   1193 C CB  . ALA   A 1 161 ? -7.478  -18.436 3.751   1.00 16.70 ?  161 ALA   A CB  1 
ATOM   1194 N N   . GLY   A 1 162 ? -4.471  -19.401 5.212   1.00 15.11 ?  162 GLY   A N   1 
ATOM   1195 C CA  . GLY   A 1 162 ? -3.102  -19.857 5.036   1.00 15.09 ?  162 GLY   A CA  1 
ATOM   1196 C C   . GLY   A 1 162 ? -2.128  -18.805 4.496   1.00 14.05 ?  162 GLY   A C   1 
ATOM   1197 O O   . GLY   A 1 162 ? -1.048  -19.186 4.062   1.00 14.95 ?  162 GLY   A O   1 
ATOM   1198 N N   . ALA   A 1 163 ? -2.421  -17.510 4.537   1.00 13.44 ?  163 ALA   A N   1 
ATOM   1199 C CA  . ALA   A 1 163 ? -1.428  -16.535 4.087   1.00 12.52 ?  163 ALA   A CA  1 
ATOM   1200 C C   . ALA   A 1 163 ? -0.106  -16.750 4.817   1.00 12.82 ?  163 ALA   A C   1 
ATOM   1201 O O   . ALA   A 1 163 ? -0.097  -16.972 6.034   1.00 12.38 ?  163 ALA   A O   1 
ATOM   1202 C CB  . ALA   A 1 163 ? -1.910  -15.140 4.351   1.00 12.09 ?  163 ALA   A CB  1 
ATOM   1203 N N   . ASP   A 1 164 ? 0.995   -16.657 4.082   1.00 12.99 ?  164 ASP   A N   1 
ATOM   1204 C CA  . ASP   A 1 164 ? 2.321   -16.699 4.670   1.00 13.41 ?  164 ASP   A CA  1 
ATOM   1205 C C   . ASP   A 1 164 ? 2.783   -15.292 5.066   1.00 13.08 ?  164 ASP   A C   1 
ATOM   1206 O O   . ASP   A 1 164 ? 3.676   -15.113 5.880   1.00 13.13 ?  164 ASP   A O   1 
ATOM   1207 C CB  . ASP   A 1 164 ? 3.313   -17.341 3.722   1.00 13.56 ?  164 ASP   A CB  1 
ATOM   1208 C CG  . ASP   A 1 164 ? 2.997   -18.772 3.353   1.00 13.76 ?  164 ASP   A CG  1 
ATOM   1209 O OD1 . ASP   A 1 164 ? 2.715   -19.550 4.258   1.00 14.48 ?  164 ASP   A OD1 1 
ATOM   1210 O OD2 . ASP   A 1 164 ? 2.963   -19.078 2.145   1.00 15.59 ?  164 ASP   A OD2 1 
ATOM   1211 N N   . PHE   A 1 165 ? 2.211   -14.303 4.420   1.00 12.48 ?  165 PHE   A N   1 
ATOM   1212 C CA  . PHE   A 1 165 ? 2.379   -12.897 4.718   1.00 11.92 ?  165 PHE   A CA  1 
ATOM   1213 C C   . PHE   A 1 165 ? 1.044   -12.192 4.536   1.00 12.77 ?  165 PHE   A C   1 
ATOM   1214 O O   . PHE   A 1 165 ? 0.258   -12.584 3.661   1.00 12.20 ?  165 PHE   A O   1 
ATOM   1215 C CB  . PHE   A 1 165 ? 3.304   -12.156 3.743   1.00 12.47 ?  165 PHE   A CB  1 
ATOM   1216 C CG  . PHE   A 1 165 ? 4.810   -12.214 4.014   1.00 13.72 ?  165 PHE   A CG  1 
ATOM   1217 C CD1 . PHE   A 1 165 ? 5.546   -13.361 3.821   1.00 15.53 ?  165 PHE   A CD1 1 
ATOM   1218 C CD2 . PHE   A 1 165 ? 5.435   -11.102 4.560   1.00 13.68 ?  165 PHE   A CD2 1 
ATOM   1219 C CE1 . PHE   A 1 165 ? 6.930   -13.373 4.097   1.00 15.91 ?  165 PHE   A CE1 1 
ATOM   1220 C CE2 . PHE   A 1 165 ? 6.773   -11.111 4.874   1.00 14.38 ?  165 PHE   A CE2 1 
ATOM   1221 C CZ  . PHE   A 1 165 ? 7.530   -12.238 4.585   1.00 15.41 ?  165 PHE   A CZ  1 
ATOM   1222 N N   . ILE   A 1 166 ? 0.838   -11.128 5.333   1.00 12.15 ?  166 ILE   A N   1 
ATOM   1223 C CA  . ILE   A 1 166 ? -0.200  -10.178 5.012   1.00 12.38 ?  166 ILE   A CA  1 
ATOM   1224 C C   . ILE   A 1 166 ? 0.480   -8.858  4.706   1.00 13.43 ?  166 ILE   A C   1 
ATOM   1225 O O   . ILE   A 1 166 ? 1.487   -8.491  5.346   1.00 12.65 ?  166 ILE   A O   1 
ATOM   1226 C CB  . ILE   A 1 166 ? -1.265  -10.082 6.106   1.00 12.88 ?  166 ILE   A CB  1 
ATOM   1227 C CG1 . ILE   A 1 166 ? -0.682  -9.742  7.480   1.00 11.87 ?  166 ILE   A CG1 1 
ATOM   1228 C CG2 . ILE   A 1 166 ? -2.089  -11.379 6.121   1.00 13.99 ?  166 ILE   A CG2 1 
ATOM   1229 C CD1 . ILE   A 1 166 ? -1.762  -9.569  8.554   1.00 12.67 ?  166 ILE   A CD1 1 
ATOM   1230 N N   . LYS   A 1 167 ? -0.028  -8.209  3.648   1.00 12.78 ?  167 LYS   A N   1 
ATOM   1231 C CA  . LYS   A 1 167 ? 0.618   -7.072  3.021   1.00 13.69 ?  167 LYS   A CA  1 
ATOM   1232 C C   . LYS   A 1 167 ? -0.378  -5.927  2.986   1.00 12.90 ?  167 LYS   A C   1 
ATOM   1233 O O   . LYS   A 1 167 ? -1.535  -6.142  2.636   1.00 12.41 ?  167 LYS   A O   1 
ATOM   1234 C CB  . LYS   A 1 167 ? 1.037   -7.592  1.637   1.00 14.38 ?  167 LYS   A CB  1 
ATOM   1235 C CG  . LYS   A 1 167 ? 1.549   -6.563  0.671   1.00 17.30 ?  167 LYS   A CG  1 
ATOM   1236 C CD  . LYS   A 1 167 ? 2.272   -7.105  -0.554  1.00 16.50 ?  167 LYS   A CD  1 
ATOM   1237 C CE  . LYS   A 1 167 ? 2.490   -6.021  -1.509  1.00 18.15 ?  167 LYS   A CE  1 
ATOM   1238 N NZ  . LYS   A 1 167 ? 3.174   -6.325  -2.767  1.00 19.82 ?  167 LYS   A NZ  1 
ATOM   1239 N N   . THR   A 1 168 ? 0.058   -4.687  3.224   1.00 11.96 ?  168 THR   A N   1 
ATOM   1240 C CA  . THR   A 1 168 ? -0.884  -3.590  3.303   1.00 12.82 ?  168 THR   A CA  1 
ATOM   1241 C C   . THR   A 1 168 ? -1.587  -3.313  1.978   1.00 12.79 ?  168 THR   A C   1 
ATOM   1242 O O   . THR   A 1 168 ? -2.809  -3.100  1.976   1.00 13.02 ?  168 THR   A O   1 
ATOM   1243 C CB  . THR   A 1 168 ? -0.220  -2.298  3.792   1.00 13.46 ?  168 THR   A CB  1 
ATOM   1244 O OG1 . THR   A 1 168 ? 0.765   -1.872  2.848   1.00 12.52 ?  168 THR   A OG1 1 
ATOM   1245 C CG2 . THR   A 1 168 ? 0.451   -2.469  5.148   1.00 14.36 ?  168 THR   A CG2 1 
ATOM   1246 N N   . SER   A 1 169 ? -0.837  -3.216  0.868   1.00 12.85 ?  169 SER   A N   1 
ATOM   1247 C CA  . SER   A 1 169 ? -1.263  -2.407  -0.259  1.00 12.76 ?  169 SER   A CA  1 
ATOM   1248 C C   . SER   A 1 169 ? -0.704  -2.904  -1.600  1.00 13.09 ?  169 SER   A C   1 
ATOM   1249 O O   . SER   A 1 169 ? 0.349   -3.581  -1.667  1.00 13.95 ?  169 SER   A O   1 
ATOM   1250 C CB  . SER   A 1 169 ? -0.817  -0.943  -0.059  1.00 12.70 ?  169 SER   A CB  1 
ATOM   1251 O OG  . SER   A 1 169 ? -1.205  -0.478  1.236   1.00 14.06 ?  169 SER   A OG  1 
ATOM   1252 N N   . THR   A 1 170 ? -1.429  -2.543  -2.671  1.00 13.11 ?  170 THR   A N   1 
ATOM   1253 C CA  . THR   A 1 170 ? -0.949  -2.814  -4.011  1.00 13.16 ?  170 THR   A CA  1 
ATOM   1254 C C   . THR   A 1 170 ? 0.067   -1.757  -4.441  1.00 15.65 ?  170 THR   A C   1 
ATOM   1255 O O   . THR   A 1 170 ? 0.843   -1.988  -5.377  1.00 16.59 ?  170 THR   A O   1 
ATOM   1256 C CB  . THR   A 1 170 ? -2.108  -2.795  -5.009  1.00 12.81 ?  170 THR   A CB  1 
ATOM   1257 O OG1 . THR   A 1 170 ? -2.703  -1.492  -4.989  1.00 13.80 ?  170 THR   A OG1 1 
ATOM   1258 C CG2 . THR   A 1 170 ? -3.039  -3.967  -4.843  1.00 12.28 ?  170 THR   A CG2 1 
ATOM   1259 N N   . GLY   A 1 171 ? -0.049  -0.544  -3.903  1.00 14.45 ?  171 GLY   A N   1 
ATOM   1260 C CA  . GLY   A 1 171 ? 0.752   0.551   -4.403  1.00 17.00 ?  171 GLY   A CA  1 
ATOM   1261 C C   . GLY   A 1 171 ? 0.050   1.259   -5.563  1.00 19.08 ?  171 GLY   A C   1 
ATOM   1262 O O   . GLY   A 1 171 ? 0.611   2.205   -6.117  1.00 23.37 ?  171 GLY   A O   1 
ATOM   1263 N N   . ARG   A 1 172 ? -1.176  0.852   -5.900  1.00 18.00 ?  172 ARG   A N   1 
ATOM   1264 C CA  . ARG   A 1 172 ? -1.878  1.381   -7.085  1.00 20.96 ?  172 ARG   A CA  1 
ATOM   1265 C C   . ARG   A 1 172 ? -3.136  2.180   -6.747  1.00 21.34 ?  172 ARG   A C   1 
ATOM   1266 O O   . ARG   A 1 172 ? -3.940  2.453   -7.620  1.00 23.61 ?  172 ARG   A O   1 
ATOM   1267 C CB  . ARG   A 1 172 ? -2.310  0.234   -7.992  1.00 23.18 ?  172 ARG   A CB  1 
ATOM   1268 C CG  . ARG   A 1 172 ? -1.156  -0.569  -8.554  1.00 25.63 ?  172 ARG   A CG  1 
ATOM   1269 C CD  . ARG   A 1 172 ? -0.256  0.239   -9.453  1.00 28.83 ?  172 ARG   A CD  1 
ATOM   1270 N NE  . ARG   A 1 172 ? 0.336   -0.657  -10.439 1.00 37.71 ?  172 ARG   A NE  1 
ATOM   1271 C CZ  . ARG   A 1 172 ? -0.310  -1.136  -11.510 1.00 38.82 ?  172 ARG   A CZ  1 
ATOM   1272 N NH1 . ARG   A 1 172 ? -1.540  -0.730  -11.794 1.00 41.09 ?  172 ARG   A NH1 1 
ATOM   1273 N NH2 . ARG   A 1 172 ? 0.280   -2.009  -12.297 1.00 43.68 ?  172 ARG   A NH2 1 
ATOM   1274 N N   . VAL   A 1 173 ? -3.374  2.446   -5.455  1.00 18.79 ?  173 VAL   A N   1 
ATOM   1275 C CA  . VAL   A 1 173 ? -4.503  3.234   -4.988  1.00 18.65 ?  173 VAL   A CA  1 
ATOM   1276 C C   . VAL   A 1 173 ? -3.918  4.422   -4.227  1.00 18.53 ?  173 VAL   A C   1 
ATOM   1277 O O   . VAL   A 1 173 ? -2.726  4.480   -4.002  1.00 18.78 ?  173 VAL   A O   1 
ATOM   1278 C CB  . VAL   A 1 173 ? -5.472  2.392   -4.139  1.00 20.03 ?  173 VAL   A CB  1 
ATOM   1279 C CG1 . VAL   A 1 173 ? -6.005  1.217   -4.948  1.00 22.10 ?  173 VAL   A CG1 1 
ATOM   1280 C CG2 . VAL   A 1 173 ? -4.840  1.848   -2.870  1.00 20.01 ?  173 VAL   A CG2 1 
ATOM   1281 N N   . ALA   A 1 174 ? -4.754  5.385   -3.883  1.00 19.02 ?  174 ALA   A N   1 
ATOM   1282 C CA  . ALA   A 1 174 ? -4.274  6.651   -3.391  1.00 20.36 ?  174 ALA   A CA  1 
ATOM   1283 C C   . ALA   A 1 174 ? -3.654  6.452   -2.006  1.00 17.76 ?  174 ALA   A C   1 
ATOM   1284 O O   . ALA   A 1 174 ? -2.683  7.118   -1.669  1.00 19.83 ?  174 ALA   A O   1 
ATOM   1285 C CB  . ALA   A 1 174 ? -5.445  7.630   -3.389  1.00 21.19 ?  174 ALA   A CB  1 
ATOM   1286 N N   . VAL   A 1 175 ? -4.215  5.540   -1.207  1.00 18.25 ?  175 VAL   A N   1 
ATOM   1287 C CA  . VAL   A 1 175 ? -3.772  5.363   0.177   1.00 17.22 ?  175 VAL   A CA  1 
ATOM   1288 C C   . VAL   A 1 175 ? -3.116  3.996   0.298   1.00 16.73 ?  175 VAL   A C   1 
ATOM   1289 O O   . VAL   A 1 175 ? -3.793  2.972   0.105   1.00 16.77 ?  175 VAL   A O   1 
ATOM   1290 C CB  . VAL   A 1 175 ? -4.914  5.534   1.206   1.00 15.69 ?  175 VAL   A CB  1 
ATOM   1291 C CG1 . VAL   A 1 175 ? -4.471  5.267   2.642   1.00 16.25 ?  175 VAL   A CG1 1 
ATOM   1292 C CG2 . VAL   A 1 175 ? -5.514  6.935   1.118   1.00 16.17 ?  175 VAL   A CG2 1 
ATOM   1293 N N   . ASN   A 1 176 ? -1.816  3.992   0.662   1.00 16.88 ?  176 ASN   A N   1 
ATOM   1294 C CA  . ASN   A 1 176 ? -1.109  2.725   0.834   1.00 16.29 ?  176 ASN   A CA  1 
ATOM   1295 C C   . ASN   A 1 176 ? -0.828  2.556   2.314   1.00 14.27 ?  176 ASN   A C   1 
ATOM   1296 O O   . ASN   A 1 176 ? -1.685  2.929   3.097   1.00 14.40 ?  176 ASN   A O   1 
ATOM   1297 C CB  . ASN   A 1 176 ? 0.031   2.625   -0.171  1.00 17.69 ?  176 ASN   A CB  1 
ATOM   1298 C CG  . ASN   A 1 176 ? -0.541  2.651   -1.569  1.00 19.82 ?  176 ASN   A CG  1 
ATOM   1299 O OD1 . ASN   A 1 176 ? -1.015  1.633   -2.078  1.00 21.27 ?  176 ASN   A OD1 1 
ATOM   1300 N ND2 . ASN   A 1 176 ? -0.605  3.831   -2.154  1.00 20.79 ?  176 ASN   A ND2 1 
ATOM   1301 N N   . ALA   A 1 177 ? 0.331   2.029   2.704   1.00 14.06 ?  177 ALA   A N   1 
ATOM   1302 C CA  . ALA   A 1 177 ? 0.583   1.778   4.116   1.00 14.09 ?  177 ALA   A CA  1 
ATOM   1303 C C   . ALA   A 1 177 ? 0.587   3.083   4.896   1.00 14.76 ?  177 ALA   A C   1 
ATOM   1304 O O   . ALA   A 1 177 ? 0.967   4.134   4.402   1.00 14.70 ?  177 ALA   A O   1 
ATOM   1305 C CB  . ALA   A 1 177 ? 1.878   1.021   4.324   1.00 14.62 ?  177 ALA   A CB  1 
ATOM   1306 N N   . THR   A 1 178 ? 0.208   2.966   6.176   1.00 14.53 ?  178 THR   A N   1 
ATOM   1307 C CA  . THR   A 1 178 ? 0.472   3.981   7.178   1.00 15.09 ?  178 THR   A CA  1 
ATOM   1308 C C   . THR   A 1 178 ? 1.024   3.262   8.407   1.00 15.02 ?  178 THR   A C   1 
ATOM   1309 O O   . THR   A 1 178 ? 0.843   2.065   8.557   1.00 14.13 ?  178 THR   A O   1 
ATOM   1310 C CB  . THR   A 1 178 ? -0.787  4.780   7.520   1.00 15.55 ?  178 THR   A CB  1 
ATOM   1311 O OG1 . THR   A 1 178 ? -1.633  3.886   8.235   1.00 17.09 ?  178 THR   A OG1 1 
ATOM   1312 C CG2 . THR   A 1 178 ? -1.571  5.185   6.291   1.00 16.34 ?  178 THR   A CG2 1 
ATOM   1313 N N   . PRO   A 1 179 ? 1.672   3.964   9.346   1.00 17.52 ?  179 PRO   A N   1 
ATOM   1314 C CA  . PRO   A 1 179 ? 2.082   3.318   10.592  1.00 17.88 ?  179 PRO   A CA  1 
ATOM   1315 C C   . PRO   A 1 179 ? 0.928   2.654   11.348  1.00 17.44 ?  179 PRO   A C   1 
ATOM   1316 O O   . PRO   A 1 179 ? 1.072   1.567   11.889  1.00 16.75 ?  179 PRO   A O   1 
ATOM   1317 C CB  . PRO   A 1 179 ? 2.719   4.482   11.340  1.00 18.51 ?  179 PRO   A CB  1 
ATOM   1318 C CG  . PRO   A 1 179 ? 3.232   5.382   10.233  1.00 18.26 ?  179 PRO   A CG  1 
ATOM   1319 C CD  . PRO   A 1 179 ? 2.095   5.375   9.245   1.00 19.67 ?  179 PRO   A CD  1 
ATOM   1320 N N   . GLU   A 1 180 ? -0.236  3.302   11.317  1.00 17.02 ?  180 GLU   A N   1 
ATOM   1321 C CA  . GLU   A 1 180 ? -1.444  2.818   11.954  1.00 17.79 ?  180 GLU   A CA  1 
ATOM   1322 C C   . GLU   A 1 180 ? -1.913  1.521   11.314  1.00 16.25 ?  180 GLU   A C   1 
ATOM   1323 O O   . GLU   A 1 180 ? -2.140  0.535   11.992  1.00 15.43 ?  180 GLU   A O   1 
ATOM   1324 C CB  . GLU   A 1 180 ? -2.423  3.997   11.939  1.00 22.12 ?  180 GLU   A CB  1 
ATOM   1325 C CG  . GLU   A 1 180 ? -3.784  3.668   12.518  1.00 30.33 ?  180 GLU   A CG  1 
ATOM   1326 C CD  . GLU   A 1 180 ? -4.782  4.814   12.616  1.00 39.40 ?  180 GLU   A CD  1 
ATOM   1327 O OE1 . GLU   A 1 180 ? -4.617  5.891   11.993  1.00 47.53 ?  180 GLU   A OE1 1 
ATOM   1328 O OE2 . GLU   A 1 180 ? -5.770  4.583   13.341  1.00 42.24 ?  180 GLU   A OE2 1 
ATOM   1329 N N   . SER   A 1 181 ? -2.001  1.464   9.966   1.00 15.14 ?  181 SER   A N   1 
ATOM   1330 C CA  . SER   A 1 181 ? -2.472  0.216   9.374   1.00 16.14 ?  181 SER   A CA  1 
ATOM   1331 C C   . SER   A 1 181 ? -1.467  -0.903  9.581   1.00 14.80 ?  181 SER   A C   1 
ATOM   1332 O O   . SER   A 1 181 ? -1.840  -2.061  9.725   1.00 15.09 ?  181 SER   A O   1 
ATOM   1333 C CB  . SER   A 1 181 ? -2.906  0.383   7.899   1.00 17.06 ?  181 SER   A CB  1 
ATOM   1334 O OG  . SER   A 1 181 ? -1.826  0.811   7.099   1.00 18.47 ?  181 SER   A OG  1 
ATOM   1335 N N   . ALA   A 1 182 ? -0.177  -0.567  9.549   1.00 15.13 ?  182 ALA   A N   1 
ATOM   1336 C CA  . ALA   A 1 182 ? 0.874   -1.539  9.824   1.00 15.62 ?  182 ALA   A CA  1 
ATOM   1337 C C   . ALA   A 1 182 ? 0.734   -2.093  11.238  1.00 14.86 ?  182 ALA   A C   1 
ATOM   1338 O O   . ALA   A 1 182 ? 0.737   -3.301  11.451  1.00 14.40 ?  182 ALA   A O   1 
ATOM   1339 C CB  . ALA   A 1 182 ? 2.220   -0.883  9.641   1.00 16.33 ?  182 ALA   A CB  1 
ATOM   1340 N N   . ARG   A 1 183 ? 0.526   -1.202  12.208  1.00 15.60 ?  183 ARG   A N   1 
ATOM   1341 C CA  . ARG   A 1 183 ? 0.320   -1.620  13.601  1.00 17.17 ?  183 ARG   A CA  1 
ATOM   1342 C C   . ARG   A 1 183 ? -0.868  -2.582  13.727  1.00 15.28 ?  183 ARG   A C   1 
ATOM   1343 O O   . ARG   A 1 183 ? -0.782  -3.645  14.352  1.00 15.85 ?  183 ARG   A O   1 
ATOM   1344 C CB  . ARG   A 1 183 ? 0.129   -0.391  14.506  1.00 18.44 ?  183 ARG   A CB  1 
ATOM   1345 C CG  . ARG   A 1 183 ? -0.047  -0.766  15.969  1.00 22.41 ?  183 ARG   A CG  1 
ATOM   1346 C CD  . ARG   A 1 183 ? -0.490  0.423   16.822  1.00 25.06 ?  183 ARG   A CD  1 
ATOM   1347 N NE  . ARG   A 1 183 ? -1.654  1.135   16.300  1.00 26.85 ?  183 ARG   A NE  1 
ATOM   1348 C CZ  . ARG   A 1 183 ? -2.929  0.786   16.487  1.00 31.33 ?  183 ARG   A CZ  1 
ATOM   1349 N NH1 . ARG   A 1 183 ? -3.239  -0.332  17.110  1.00 32.55 ?  183 ARG   A NH1 1 
ATOM   1350 N NH2 . ARG   A 1 183 ? -3.895  1.570   16.057  1.00 35.27 ?  183 ARG   A NH2 1 
ATOM   1351 N N   . ILE   A 1 184 ? -1.985  -2.200  13.100  1.00 15.19 ?  184 ILE   A N   1 
ATOM   1352 C CA  . ILE   A 1 184 ? -3.220  -2.960  13.223  1.00 14.01 ?  184 ILE   A CA  1 
ATOM   1353 C C   . ILE   A 1 184 ? -2.964  -4.353  12.693  1.00 13.98 ?  184 ILE   A C   1 
ATOM   1354 O O   . ILE   A 1 184 ? -3.373  -5.330  13.289  1.00 14.67 ?  184 ILE   A O   1 
ATOM   1355 C CB  . ILE   A 1 184 ? -4.396  -2.254  12.532  1.00 14.99 ?  184 ILE   A CB  1 
ATOM   1356 C CG1 . ILE   A 1 184 ? -4.813  -0.953  13.254  1.00 15.87 ?  184 ILE   A CG1 1 
ATOM   1357 C CG2 . ILE   A 1 184 ? -5.586  -3.182  12.340  1.00 14.50 ?  184 ILE   A CG2 1 
ATOM   1358 C CD1 . ILE   A 1 184 ? -5.608  -0.018  12.349  1.00 15.87 ?  184 ILE   A CD1 1 
ATOM   1359 N N   . MET   A 1 185 ? -2.337  -4.456  11.511  1.00 13.07 ?  185 MET   A N   1 
ATOM   1360 C CA  . MET   A 1 185 ? -2.098  -5.747  10.908  1.00 13.50 ?  185 MET   A CA  1 
ATOM   1361 C C   . MET   A 1 185 ? -1.159  -6.615  11.729  1.00 13.07 ?  185 MET   A C   1 
ATOM   1362 O O   . MET   A 1 185 ? -1.385  -7.819  11.900  1.00 14.28 ?  185 MET   A O   1 
ATOM   1363 C CB  . MET   A 1 185 ? -1.523  -5.545  9.500   1.00 13.32 ?  185 MET   A CB  1 
ATOM   1364 C CG  . MET   A 1 185 ? -2.567  -5.093  8.527   1.00 13.70 ?  185 MET   A CG  1 
ATOM   1365 S SD  . MET   A 1 185 ? -2.061  -4.773  6.823   1.00 14.34 ?  185 MET   A SD  1 
ATOM   1366 C CE  . MET   A 1 185 ? -1.931  -6.509  6.415   1.00 15.09 ?  185 MET   A CE  1 
ATOM   1367 N N   . MET   A 1 186 ? -0.091  -6.025  12.259  1.00 13.88 ?  186 MET   A N   1 
ATOM   1368 C CA  . MET   A 1 186 ? 0.826   -6.806  13.078  1.00 14.46 ?  186 MET   A CA  1 
ATOM   1369 C C   . MET   A 1 186 ? 0.171   -7.199  14.416  1.00 14.00 ?  186 MET   A C   1 
ATOM   1370 O O   . MET   A 1 186 ? 0.407   -8.303  14.923  1.00 13.75 ?  186 MET   A O   1 
ATOM   1371 C CB  . MET   A 1 186 ? 2.136   -6.044  13.275  1.00 15.23 ?  186 MET   A CB  1 
ATOM   1372 C CG  . MET   A 1 186 ? 3.015   -6.045  12.050  1.00 16.44 ?  186 MET   A CG  1 
ATOM   1373 S SD  . MET   A 1 186 ? 4.638   -5.323  12.363  1.00 17.94 ?  186 MET   A SD  1 
ATOM   1374 C CE  . MET   A 1 186 ? 4.340   -3.603  11.963  1.00 18.75 ?  186 MET   A CE  1 
ATOM   1375 N N   . GLU   A 1 187 ? -0.673  -6.333  14.963  1.00 14.85 ?  187 GLU   A N   1 
ATOM   1376 C CA  . GLU   A 1 187 ? -1.510  -6.733  16.109  1.00 16.67 ?  187 GLU   A CA  1 
ATOM   1377 C C   . GLU   A 1 187 ? -2.375  -7.960  15.809  1.00 17.22 ?  187 GLU   A C   1 
ATOM   1378 O O   . GLU   A 1 187 ? -2.561  -8.826  16.658  1.00 16.81 ?  187 GLU   A O   1 
ATOM   1379 C CB  . GLU   A 1 187 ? -2.391  -5.618  16.663  1.00 19.01 ?  187 GLU   A CB  1 
ATOM   1380 C CG  . GLU   A 1 187 ? -1.606  -4.541  17.409  1.00 21.97 ?  187 GLU   A CG  1 
ATOM   1381 C CD  . GLU   A 1 187 ? -2.475  -3.353  17.775  1.00 23.43 ?  187 GLU   A CD  1 
ATOM   1382 O OE1 . GLU   A 1 187 ? -3.625  -3.394  17.388  1.00 26.28 ?  187 GLU   A OE1 1 
ATOM   1383 O OE2 . GLU   A 1 187 ? -1.990  -2.371  18.352  1.00 25.19 ?  187 GLU   A OE2 1 
ATOM   1384 N N   . VAL   A 1 188 ? -2.906  -8.086  14.592  1.00 14.73 ?  188 VAL   A N   1 
ATOM   1385 C CA  . VAL   A 1 188 ? -3.663  -9.277  14.291  1.00 14.46 ?  188 VAL   A CA  1 
ATOM   1386 C C   . VAL   A 1 188 ? -2.776  -10.516 14.329  1.00 13.95 ?  188 VAL   A C   1 
ATOM   1387 O O   . VAL   A 1 188 ? -3.191  -11.575 14.804  1.00 14.15 ?  188 VAL   A O   1 
ATOM   1388 C CB  . VAL   A 1 188 ? -4.409  -9.182  12.944  1.00 14.57 ?  188 VAL   A CB  1 
ATOM   1389 C CG1 . VAL   A 1 188 ? -5.150  -10.471 12.615  1.00 14.55 ?  188 VAL   A CG1 1 
ATOM   1390 C CG2 . VAL   A 1 188 ? -5.354  -8.001  12.932  1.00 14.62 ?  188 VAL   A CG2 1 
ATOM   1391 N N   . ILE   A 1 189 ? -1.589  -10.422 13.720  1.00 13.99 ?  189 ILE   A N   1 
ATOM   1392 C CA  . ILE   A 1 189 ? -0.684  -11.556 13.744  1.00 14.29 ?  189 ILE   A CA  1 
ATOM   1393 C C   . ILE   A 1 189 ? -0.493  -11.991 15.221  1.00 13.76 ?  189 ILE   A C   1 
ATOM   1394 O O   . ILE   A 1 189 ? -0.541  -13.195 15.549  1.00 13.94 ?  189 ILE   A O   1 
ATOM   1395 C CB  . ILE   A 1 189 ? 0.617   -11.144 13.030  1.00 14.62 ?  189 ILE   A CB  1 
ATOM   1396 C CG1 . ILE   A 1 189 ? 0.400   -10.968 11.543  1.00 14.39 ?  189 ILE   A CG1 1 
ATOM   1397 C CG2 . ILE   A 1 189 ? 1.743   -12.125 13.352  1.00 15.32 ?  189 ILE   A CG2 1 
ATOM   1398 C CD1 . ILE   A 1 189 ? 1.580   -10.415 10.819  1.00 14.96 ?  189 ILE   A CD1 1 
ATOM   1399 N N   . ARG   A 1 190 ? -0.193  -11.014 16.073  1.00 14.39 ?  190 ARG   A N   1 
ATOM   1400 C CA  . ARG   A 1 190 ? 0.107   -11.287 17.474  1.00 16.29 ?  190 ARG   A CA  1 
ATOM   1401 C C   . ARG   A 1 190 ? -1.103  -11.899 18.189  1.00 15.55 ?  190 ARG   A C   1 
ATOM   1402 O O   . ARG   A 1 190 ? -0.970  -12.912 18.881  1.00 17.36 ?  190 ARG   A O   1 
ATOM   1403 C CB  . ARG   A 1 190 ? 0.459   -9.983  18.174  1.00 19.22 ?  190 ARG   A CB  1 
ATOM   1404 C CG  . ARG   A 1 190 ? 1.077   -10.263 19.537  1.00 23.70 ?  190 ARG   A CG  1 
ATOM   1405 C CD  . ARG   A 1 190 ? 0.700   -9.276  20.596  1.00 26.61 ?  190 ARG   A CD  1 
ATOM   1406 N NE  . ARG   A 1 190 ? -0.580  -8.604  20.443  1.00 28.44 ?  190 ARG   A NE  1 
ATOM   1407 C CZ  . ARG   A 1 190 ? -0.745  -7.347  20.760  1.00 30.81 ?  190 ARG   A CZ  1 
ATOM   1408 N NH1 . ARG   A 1 190 ? 0.222   -6.735  21.426  1.00 33.52 ?  190 ARG   A NH1 1 
ATOM   1409 N NH2 . ARG   A 1 190 ? -1.859  -6.712  20.441  1.00 30.47 ?  190 ARG   A NH2 1 
ATOM   1410 N N   . ASP   A 1 191 ? -2.268  -11.263 18.006  1.00 14.76 ?  191 ASP   A N   1 
ATOM   1411 C CA  . ASP   A 1 191 ? -3.515  -11.664 18.650  1.00 14.89 ?  191 ASP   A CA  1 
ATOM   1412 C C   . ASP   A 1 191 ? -3.930  -13.051 18.192  1.00 15.00 ?  191 ASP   A C   1 
ATOM   1413 O O   . ASP   A 1 191 ? -4.582  -13.781 18.918  1.00 15.32 ?  191 ASP   A O   1 
ATOM   1414 C CB  . ASP   A 1 191 ? -4.644  -10.679 18.412  1.00 15.43 ?  191 ASP   A CB  1 
ATOM   1415 C CG  . ASP   A 1 191 ? -4.483  -9.306  19.062  1.00 17.51 ?  191 ASP   A CG  1 
ATOM   1416 O OD1 . ASP   A 1 191 ? -3.606  -9.150  19.954  1.00 20.08 ?  191 ASP   A OD1 1 
ATOM   1417 O OD2 . ASP   A 1 191 ? -5.200  -8.406  18.647  1.00 19.69 ?  191 ASP   A OD2 1 
ATOM   1418 N N   . MET   A 1 192 ? -3.609  -13.398 16.924  1.00 14.68 ?  192 MET   A N   1 
ATOM   1419 C CA  . MET   A 1 192 ? -3.943  -14.717 16.433  1.00 14.91 ?  192 MET   A CA  1 
ATOM   1420 C C   . MET   A 1 192 ? -2.933  -15.750 16.909  1.00 14.77 ?  192 MET   A C   1 
ATOM   1421 O O   . MET   A 1 192 ? -3.179  -16.954 16.862  1.00 14.44 ?  192 MET   A O   1 
ATOM   1422 C CB  . MET   A 1 192 ? -4.111  -14.676 14.921  1.00 16.48 ?  192 MET   A CB  1 
ATOM   1423 C CG  . MET   A 1 192 ? -5.366  -13.918 14.550  1.00 17.94 ?  192 MET   A CG  1 
ATOM   1424 S SD  . MET   A 1 192 ? -5.635  -14.043 12.765  1.00 20.72 ?  192 MET   A SD  1 
ATOM   1425 C CE  . MET   A 1 192 ? -6.264  -15.734 12.700  1.00 19.70 ?  192 MET   A CE  1 
ATOM   1426 N N   . GLY   A 1 193 ? -1.777  -15.266 17.363  1.00 15.07 ?  193 GLY   A N   1 
ATOM   1427 C CA  . GLY   A 1 193 ? -0.739  -16.159 17.818  1.00 16.23 ?  193 GLY   A CA  1 
ATOM   1428 C C   . GLY   A 1 193 ? 0.078   -16.779 16.689  1.00 16.16 ?  193 GLY   A C   1 
ATOM   1429 O O   . GLY   A 1 193 ? 0.664   -17.841 16.901  1.00 16.09 ?  193 GLY   A O   1 
ATOM   1430 N N   . VAL   A 1 194 ? 0.112   -16.131 15.503  1.00 15.62 ?  194 VAL   A N   1 
ATOM   1431 C CA  . VAL   A 1 194 ? 0.725   -16.757 14.325  1.00 15.93 ?  194 VAL   A CA  1 
ATOM   1432 C C   . VAL   A 1 194 ? 2.040   -16.106 13.896  1.00 16.58 ?  194 VAL   A C   1 
ATOM   1433 O O   . VAL   A 1 194 ? 2.466   -16.245 12.742  1.00 16.08 ?  194 VAL   A O   1 
ATOM   1434 C CB  . VAL   A 1 194 ? -0.274  -16.811 13.154  1.00 15.58 ?  194 VAL   A CB  1 
ATOM   1435 C CG1 . VAL   A 1 194 ? -1.449  -17.687 13.548  1.00 16.71 ?  194 VAL   A CG1 1 
ATOM   1436 C CG2 . VAL   A 1 194 ? -0.735  -15.426 12.736  1.00 15.25 ?  194 VAL   A CG2 1 
ATOM   1437 N N   . GLU   A 1 195 ? 2.721   -15.424 14.812  1.00 18.20 ?  195 GLU   A N   1 
ATOM   1438 C CA  . GLU   A 1 195 ? 3.916   -14.669 14.449  1.00 18.75 ?  195 GLU   A CA  1 
ATOM   1439 C C   . GLU   A 1 195 ? 5.028   -15.586 13.929  1.00 18.76 ?  195 GLU   A C   1 
ATOM   1440 O O   . GLU   A 1 195 ? 5.881   -15.135 13.184  1.00 18.50 ?  195 GLU   A O   1 
ATOM   1441 C CB  . GLU   A 1 195 ? 4.414   -13.797 15.604  1.00 19.74 ?  195 GLU   A CB  1 
ATOM   1442 C CG  . GLU   A 1 195 ? 4.858   -14.597 16.822  1.00 20.21 ?  195 GLU   A CG  1 
ATOM   1443 C CD  . GLU   A 1 195 ? 3.760   -14.940 17.813  1.00 23.52 ?  195 GLU   A CD  1 
ATOM   1444 O OE1 . GLU   A 1 195 ? 2.575   -14.676 17.555  1.00 19.53 ?  195 GLU   A OE1 1 
ATOM   1445 O OE2 . GLU   A 1 195 ? 4.152   -15.427 18.904  1.00 26.61 ?  195 GLU   A OE2 1 
ATOM   1446 N N   . LYS   A 1 196 ? 5.025   -16.875 14.256  1.00 18.83 ?  196 LYS   A N   1 
ATOM   1447 C CA  . LYS   A 1 196 ? 6.044   -17.783 13.755  1.00 20.68 ?  196 LYS   A CA  1 
ATOM   1448 C C   . LYS   A 1 196 ? 5.843   -18.033 12.260  1.00 19.21 ?  196 LYS   A C   1 
ATOM   1449 O O   . LYS   A 1 196 ? 6.828   -18.131 11.537  1.00 20.77 ?  196 LYS   A O   1 
ATOM   1450 C CB  . LYS   A 1 196 ? 5.982   -19.144 14.454  1.00 24.26 ?  196 LYS   A CB  1 
ATOM   1451 C CG  . LYS   A 1 196 ? 6.895   -20.220 13.891  1.00 30.50 ?  196 LYS   A CG  1 
ATOM   1452 C CD  . LYS   A 1 196 ? 6.569   -21.622 14.408  1.00 36.07 ?  196 LYS   A CD  1 
ATOM   1453 C CE  . LYS   A 1 196 ? 7.491   -22.667 13.888  1.00 44.33 ?  196 LYS   A CE  1 
ATOM   1454 N NZ  . LYS   A 1 196 ? 7.624   -23.733 14.894  1.00 51.95 ?  196 LYS   A NZ  1 
ATOM   1455 N N   . SER   A 1 197 ? 4.584   -18.115 11.816  1.00 16.36 ?  197 SER   A N   1 
ATOM   1456 C CA  . SER   A 1 197 ? 4.256   -18.543 10.454  1.00 17.26 ?  197 SER   A CA  1 
ATOM   1457 C C   . SER   A 1 197 ? 3.841   -17.407 9.533   1.00 16.14 ?  197 SER   A C   1 
ATOM   1458 O O   . SER   A 1 197 ? 3.724   -17.635 8.325   1.00 17.15 ?  197 SER   A O   1 
ATOM   1459 C CB  . SER   A 1 197 ? 3.216   -19.609 10.414  1.00 16.59 ?  197 SER   A CB  1 
ATOM   1460 O OG  . SER   A 1 197 ? 2.056   -19.180 11.105  1.00 20.10 ?  197 SER   A OG  1 
ATOM   1461 N N   . VAL   A 1 198 ? 3.583   -16.206 10.039  1.00 15.20 ?  198 VAL   A N   1 
ATOM   1462 C CA  . VAL   A 1 198 ? 2.963   -15.198 9.196   1.00 14.95 ?  198 VAL   A CA  1 
ATOM   1463 C C   . VAL   A 1 198 ? 3.806   -13.938 9.287   1.00 14.94 ?  198 VAL   A C   1 
ATOM   1464 O O   . VAL   A 1 198 ? 4.064   -13.435 10.374  1.00 15.02 ?  198 VAL   A O   1 
ATOM   1465 C CB  . VAL   A 1 198 ? 1.497   -14.878 9.555   1.00 15.39 ?  198 VAL   A CB  1 
ATOM   1466 C CG1 . VAL   A 1 198 ? 0.917   -13.757 8.706   1.00 15.66 ?  198 VAL   A CG1 1 
ATOM   1467 C CG2 . VAL   A 1 198 ? 0.606   -16.112 9.421   1.00 15.54 ?  198 VAL   A CG2 1 
ATOM   1468 N N   . GLY   A 1 199 ? 4.285   -13.467 8.134   1.00 13.42 ?  199 GLY   A N   1 
ATOM   1469 C CA  . GLY   A 1 199 ? 5.022   -12.219 8.060   1.00 12.86 ?  199 GLY   A CA  1 
ATOM   1470 C C   . GLY   A 1 199 ? 4.126   -11.039 7.713   1.00 13.01 ?  199 GLY   A C   1 
ATOM   1471 O O   . GLY   A 1 199 ? 2.951   -11.194 7.339   1.00 13.72 ?  199 GLY   A O   1 
ATOM   1472 N N   . PHE   A 1 200 ? 4.734   -9.853  7.723   1.00 12.78 ?  200 PHE   A N   1 
ATOM   1473 C CA  . PHE   A 1 200 ? 4.061   -8.600  7.433   1.00 12.69 ?  200 PHE   A CA  1 
ATOM   1474 C C   . PHE   A 1 200 ? 4.845   -7.864  6.349   1.00 13.88 ?  200 PHE   A C   1 
ATOM   1475 O O   . PHE   A 1 200 ? 6.075   -7.785  6.451   1.00 12.99 ?  200 PHE   A O   1 
ATOM   1476 C CB  . PHE   A 1 200 ? 3.991   -7.742  8.682   1.00 13.92 ?  200 PHE   A CB  1 
ATOM   1477 C CG  . PHE   A 1 200 ? 3.458   -6.353  8.408   1.00 13.79 ?  200 PHE   A CG  1 
ATOM   1478 C CD1 . PHE   A 1 200 ? 2.136   -6.163  7.980   1.00 15.02 ?  200 PHE   A CD1 1 
ATOM   1479 C CD2 . PHE   A 1 200 ? 4.297   -5.251  8.464   1.00 14.86 ?  200 PHE   A CD2 1 
ATOM   1480 C CE1 . PHE   A 1 200 ? 1.672   -4.884  7.691   1.00 15.12 ?  200 PHE   A CE1 1 
ATOM   1481 C CE2 . PHE   A 1 200 ? 3.844   -3.979  8.137   1.00 15.57 ?  200 PHE   A CE2 1 
ATOM   1482 C CZ  . PHE   A 1 200 ? 2.524   -3.792  7.730   1.00 15.29 ?  200 PHE   A CZ  1 
ATOM   1483 N N   . LYS   A 1 201 ? 4.147   -7.301  5.352   1.00 13.29 ?  201 LYS   A N   1 
ATOM   1484 C CA  A LYS   A 1 201 ? 4.817   -6.479  4.357   0.60 13.30 ?  201 LYS   A CA  1 
ATOM   1485 C CA  B LYS   A 1 201 ? 4.813   -6.481  4.354   0.40 13.39 ?  201 LYS   A CA  1 
ATOM   1486 C C   . LYS   A 1 201 ? 4.146   -5.112  4.229   1.00 13.72 ?  201 LYS   A C   1 
ATOM   1487 O O   . LYS   A 1 201 ? 2.929   -5.001  3.993   1.00 13.40 ?  201 LYS   A O   1 
ATOM   1488 C CB  A LYS   A 1 201 ? 4.899   -7.192  2.999   0.60 13.74 ?  201 LYS   A CB  1 
ATOM   1489 C CB  B LYS   A 1 201 ? 4.871   -7.164  2.981   0.40 13.68 ?  201 LYS   A CB  1 
ATOM   1490 C CG  A LYS   A 1 201 ? 5.400   -6.348  1.855   0.60 13.63 ?  201 LYS   A CG  1 
ATOM   1491 C CG  B LYS   A 1 201 ? 5.400   -6.283  1.875   0.40 13.63 ?  201 LYS   A CG  1 
ATOM   1492 C CD  A LYS   A 1 201 ? 5.640   -7.228  0.636   0.60 14.43 ?  201 LYS   A CD  1 
ATOM   1493 C CD  B LYS   A 1 201 ? 5.765   -7.103  0.649   0.40 14.21 ?  201 LYS   A CD  1 
ATOM   1494 C CE  A LYS   A 1 201 ? 5.939   -6.414  -0.590  0.60 14.69 ?  201 LYS   A CE  1 
ATOM   1495 C CE  B LYS   A 1 201 ? 6.527   -6.303  -0.357  0.40 14.30 ?  201 LYS   A CE  1 
ATOM   1496 N NZ  A LYS   A 1 201 ? 6.058   -7.214  -1.813  0.60 14.96 ?  201 LYS   A NZ  1 
ATOM   1497 N NZ  B LYS   A 1 201 ? 5.697   -5.332  -1.077  0.40 14.54 ?  201 LYS   A NZ  1 
ATOM   1498 N N   . VAL   A 1 202 ? 4.983   -4.086  4.291   1.00 13.57 ?  202 VAL   A N   1 
ATOM   1499 C CA  . VAL   A 1 202 ? 4.623   -2.697  4.070   1.00 15.67 ?  202 VAL   A CA  1 
ATOM   1500 C C   . VAL   A 1 202 ? 4.806   -2.378  2.586   1.00 15.59 ?  202 VAL   A C   1 
ATOM   1501 O O   . VAL   A 1 202 ? 5.921   -2.444  2.099   1.00 16.34 ?  202 VAL   A O   1 
ATOM   1502 C CB  . VAL   A 1 202 ? 5.521   -1.728  4.865   1.00 19.11 ?  202 VAL   A CB  1 
ATOM   1503 C CG1 . VAL   A 1 202 ? 5.112   -0.274  4.670   1.00 20.09 ?  202 VAL   A CG1 1 
ATOM   1504 C CG2 . VAL   A 1 202 ? 5.567   -2.046  6.348   1.00 22.87 ?  202 VAL   A CG2 1 
ATOM   1505 N N   . THR   A 1 203 ? 3.756   -1.918  1.905   1.00 16.08 ?  203 THR   A N   1 
ATOM   1506 C CA  . THR   A 1 203 ? 3.898   -1.371  0.545   1.00 16.91 ?  203 THR   A CA  1 
ATOM   1507 C C   . THR   A 1 203 ? 3.366   0.051   0.515   1.00 17.35 ?  203 THR   A C   1 
ATOM   1508 O O   . THR   A 1 203 ? 2.244   0.333   0.963   1.00 14.85 ?  203 THR   A O   1 
ATOM   1509 C CB  . THR   A 1 203 ? 3.126   -2.230  -0.436  1.00 17.88 ?  203 THR   A CB  1 
ATOM   1510 O OG1 . THR   A 1 203 ? 3.798   -3.479  -0.420  1.00 22.90 ?  203 THR   A OG1 1 
ATOM   1511 C CG2 . THR   A 1 203 ? 3.106   -1.620  -1.824  1.00 17.37 ?  203 THR   A CG2 1 
ATOM   1512 N N   . GLY   A 1 204 ? 4.223   0.938   0.040   1.00 16.56 ?  204 GLY   A N   1 
ATOM   1513 C CA  . GLY   A 1 204 ? 3.967   2.362   0.034   1.00 18.12 ?  204 GLY   A CA  1 
ATOM   1514 C C   . GLY   A 1 204 ? 4.051   2.928   1.446   1.00 20.11 ?  204 GLY   A C   1 
ATOM   1515 O O   . GLY   A 1 204 ? 4.362   2.213   2.396   1.00 18.41 ?  204 GLY   A O   1 
ATOM   1516 N N   . GLY   A 1 205 ? 3.800   4.241   1.553   1.00 22.18 ?  205 GLY   A N   1 
ATOM   1517 C CA  . GLY   A 1 205 ? 3.931   4.972   2.792   1.00 22.86 ?  205 GLY   A CA  1 
ATOM   1518 C C   . GLY   A 1 205 ? 5.306   4.889   3.444   1.00 24.58 ?  205 GLY   A C   1 
ATOM   1519 O O   . GLY   A 1 205 ? 5.425   5.160   4.625   1.00 26.44 ?  205 GLY   A O   1 
ATOM   1520 N N   . VAL   A 1 206 ? 6.367   4.540   2.725   1.00 23.63 ?  206 VAL   A N   1 
ATOM   1521 C CA  . VAL   A 1 206 ? 7.651   4.360   3.383   1.00 23.30 ?  206 VAL   A CA  1 
ATOM   1522 C C   . VAL   A 1 206 ? 8.719   4.889   2.425   1.00 24.98 ?  206 VAL   A C   1 
ATOM   1523 O O   . VAL   A 1 206 ? 9.463   4.133   1.849   1.00 23.74 ?  206 VAL   A O   1 
ATOM   1524 C CB  . VAL   A 1 206 ? 7.888   2.905   3.846   1.00 23.60 ?  206 VAL   A CB  1 
ATOM   1525 C CG1 . VAL   A 1 206 ? 7.765   1.899   2.700   1.00 26.72 ?  206 VAL   A CG1 1 
ATOM   1526 C CG2 . VAL   A 1 206 ? 9.221   2.738   4.573   1.00 23.75 ?  206 VAL   A CG2 1 
ATOM   1527 N N   . SER   A 1 207 ? 8.795   6.217   2.334   1.00 25.88 ?  207 SER   A N   1 
ATOM   1528 C CA  . SER   A 1 207 ? 9.608   6.949   1.388   1.00 29.16 ?  207 SER   A CA  1 
ATOM   1529 C C   . SER   A 1 207 ? 11.045  7.098   1.852   1.00 29.24 ?  207 SER   A C   1 
ATOM   1530 O O   . SER   A 1 207 ? 11.934  7.235   1.017   1.00 29.60 ?  207 SER   A O   1 
ATOM   1531 C CB  . SER   A 1 207 ? 9.003   8.296   1.137   1.00 30.48 ?  207 SER   A CB  1 
ATOM   1532 O OG  . SER   A 1 207 ? 7.965   8.084   0.203   1.00 35.15 ?  207 SER   A OG  1 
ATOM   1533 N N   . THR   A 1 208 ? 11.268  7.111   3.159   1.00 24.65 ?  208 THR   A N   1 
ATOM   1534 C CA  . THR   A 1 208 ? 12.575  7.467   3.671   1.00 23.99 ?  208 THR   A CA  1 
ATOM   1535 C C   . THR   A 1 208 ? 13.094  6.422   4.638   1.00 23.81 ?  208 THR   A C   1 
ATOM   1536 O O   . THR   A 1 208 ? 12.339  5.618   5.184   1.00 23.21 ?  208 THR   A O   1 
ATOM   1537 C CB  . THR   A 1 208 ? 12.567  8.838   4.353   1.00 24.46 ?  208 THR   A CB  1 
ATOM   1538 O OG1 . THR   A 1 208 ? 11.845  8.714   5.582   1.00 22.51 ?  208 THR   A OG1 1 
ATOM   1539 C CG2 . THR   A 1 208 ? 11.939  9.909   3.482   1.00 25.34 ?  208 THR   A CG2 1 
ATOM   1540 N N   . ALA   A 1 209 ? 14.416  6.483   4.838   1.00 22.51 ?  209 ALA   A N   1 
ATOM   1541 C CA  . ALA   A 1 209 ? 15.114  5.747   5.875   1.00 24.94 ?  209 ALA   A CA  1 
ATOM   1542 C C   . ALA   A 1 209 ? 14.436  5.914   7.233   1.00 24.84 ?  209 ALA   A C   1 
ATOM   1543 O O   . ALA   A 1 209 ? 14.347  4.977   8.006   1.00 22.24 ?  209 ALA   A O   1 
ATOM   1544 C CB  . ALA   A 1 209 ? 16.538  6.228   5.953   1.00 26.20 ?  209 ALA   A CB  1 
ATOM   1545 N N   . GLU   A 1 210 ? 14.047  7.147   7.553   1.00 24.34 ?  210 GLU   A N   1 
ATOM   1546 C CA  . GLU   A 1 210 ? 13.453  7.433   8.847   1.00 23.11 ?  210 GLU   A CA  1 
ATOM   1547 C C   . GLU   A 1 210 ? 12.088  6.721   8.968   1.00 22.93 ?  210 GLU   A C   1 
ATOM   1548 O O   . GLU   A 1 210 ? 11.736  6.153   10.004  1.00 20.99 ?  210 GLU   A O   1 
ATOM   1549 C CB  . GLU   A 1 210 ? 13.329  8.945   9.006   1.00 25.92 ?  210 GLU   A CB  1 
ATOM   1550 C CG  . GLU   A 1 210 ? 14.670  9.652   9.158   1.00 27.86 ?  210 GLU   A CG  1 
ATOM   1551 C CD  . GLU   A 1 210 ? 15.399  10.033  7.876   1.00 31.17 ?  210 GLU   A CD  1 
ATOM   1552 O OE1 . GLU   A 1 210 ? 15.045  9.666   6.735   1.00 27.09 ?  210 GLU   A OE1 1 
ATOM   1553 O OE2 . GLU   A 1 210 ? 16.386  10.775  8.072   1.00 36.34 ?  210 GLU   A OE2 1 
ATOM   1554 N N   . ASP   A 1 211 ? 11.330  6.723   7.877   1.00 19.82 ?  211 ASP   A N   1 
ATOM   1555 C CA  . ASP   A 1 211 ? 10.079  6.008   7.830   1.00 19.34 ?  211 ASP   A CA  1 
ATOM   1556 C C   . ASP   A 1 211 ? 10.283  4.525   8.071   1.00 19.08 ?  211 ASP   A C   1 
ATOM   1557 O O   . ASP   A 1 211 ? 9.564   3.908   8.847   1.00 17.91 ?  211 ASP   A O   1 
ATOM   1558 C CB  . ASP   A 1 211 ? 9.361   6.174   6.503   1.00 19.58 ?  211 ASP   A CB  1 
ATOM   1559 C CG  . ASP   A 1 211 ? 8.919   7.583   6.164   1.00 22.46 ?  211 ASP   A CG  1 
ATOM   1560 O OD1 . ASP   A 1 211 ? 8.564   8.321   7.104   1.00 24.80 ?  211 ASP   A OD1 1 
ATOM   1561 O OD2 . ASP   A 1 211 ? 8.876   7.896   4.965   1.00 24.19 ?  211 ASP   A OD2 1 
ATOM   1562 N N   . ALA   A 1 212 ? 11.263  3.944   7.395   1.00 16.92 ?  212 ALA   A N   1 
ATOM   1563 C CA  . ALA   A 1 212 ? 11.522  2.522   7.536   1.00 18.13 ?  212 ALA   A CA  1 
ATOM   1564 C C   . ALA   A 1 212 ? 11.857  2.152   8.980   1.00 18.51 ?  212 ALA   A C   1 
ATOM   1565 O O   . ALA   A 1 212 ? 11.406  1.120   9.488   1.00 18.41 ?  212 ALA   A O   1 
ATOM   1566 C CB  . ALA   A 1 212 ? 12.591  2.074   6.564   1.00 17.46 ?  212 ALA   A CB  1 
ATOM   1567 N N   . GLN   A 1 213 ? 12.619  3.009   9.631   1.00 19.69 ?  213 GLN   A N   1 
ATOM   1568 C CA  . GLN   A 1 213 ? 12.999  2.751   11.012  1.00 19.20 ?  213 GLN   A CA  1 
ATOM   1569 C C   . GLN   A 1 213 ? 11.758  2.654   11.901  1.00 18.66 ?  213 GLN   A C   1 
ATOM   1570 O O   . GLN   A 1 213 ? 11.703  1.818   12.801  1.00 20.07 ?  213 GLN   A O   1 
ATOM   1571 C CB  . GLN   A 1 213 ? 13.881  3.912   11.438  1.00 22.74 ?  213 GLN   A CB  1 
ATOM   1572 C CG  . GLN   A 1 213 ? 14.438  3.758   12.843  1.00 25.34 ?  213 GLN   A CG  1 
ATOM   1573 C CD  . GLN   A 1 213 ? 15.347  4.911   13.185  1.00 30.29 ?  213 GLN   A CD  1 
ATOM   1574 O OE1 . GLN   A 1 213 ? 14.949  6.077   13.109  1.00 34.87 ?  213 GLN   A OE1 1 
ATOM   1575 N NE2 . GLN   A 1 213 ? 16.573  4.594   13.558  1.00 32.72 ?  213 GLN   A NE2 1 
ATOM   1576 N N   . LYS   A 1 214 ? 10.775  3.518   11.656  1.00 20.07 ?  214 LYS   A N   1 
ATOM   1577 C CA  . LYS   A 1 214 ? 9.551   3.552   12.470  1.00 22.14 ?  214 LYS   A CA  1 
ATOM   1578 C C   . LYS   A 1 214 ? 8.730   2.278   12.298  1.00 19.45 ?  214 LYS   A C   1 
ATOM   1579 O O   . LYS   A 1 214 ? 8.238   1.659   13.248  1.00 18.32 ?  214 LYS   A O   1 
ATOM   1580 C CB  . LYS   A 1 214 ? 8.753   4.795   12.095  1.00 24.08 ?  214 LYS   A CB  1 
ATOM   1581 C CG  . LYS   A 1 214 ? 7.526   4.963   12.980  1.00 30.78 ?  214 LYS   A CG  1 
ATOM   1582 C CD  . LYS   A 1 214 ? 6.442   5.757   12.276  1.00 35.47 ?  214 LYS   A CD  1 
ATOM   1583 C CE  . LYS   A 1 214 ? 6.999   7.057   11.848  1.00 38.54 ?  214 LYS   A CE  1 
ATOM   1584 N NZ  . LYS   A 1 214 ? 6.005   7.809   11.102  1.00 44.70 ?  214 LYS   A NZ  1 
ATOM   1585 N N   . TYR   A 1 215 ? 8.581   1.855   11.036  1.00 18.06 ?  215 TYR   A N   1 
ATOM   1586 C CA  . TYR   A 1 215 ? 7.879   0.636   10.731  1.00 16.95 ?  215 TYR   A CA  1 
ATOM   1587 C C   . TYR   A 1 215 ? 8.537   -0.560  11.383  1.00 15.68 ?  215 TYR   A C   1 
ATOM   1588 O O   . TYR   A 1 215 ? 7.845   -1.411  11.888  1.00 16.43 ?  215 TYR   A O   1 
ATOM   1589 C CB  . TYR   A 1 215 ? 7.784   0.431   9.210   1.00 16.87 ?  215 TYR   A CB  1 
ATOM   1590 C CG  . TYR   A 1 215 ? 6.696   1.277   8.570   1.00 19.11 ?  215 TYR   A CG  1 
ATOM   1591 C CD1 . TYR   A 1 215 ? 5.371   0.865   8.576   1.00 18.83 ?  215 TYR   A CD1 1 
ATOM   1592 C CD2 . TYR   A 1 215 ? 6.988   2.479   7.939   1.00 21.28 ?  215 TYR   A CD2 1 
ATOM   1593 C CE1 . TYR   A 1 215 ? 4.385   1.631   7.990   1.00 18.05 ?  215 TYR   A CE1 1 
ATOM   1594 C CE2 . TYR   A 1 215 ? 6.016   3.211   7.272   1.00 21.68 ?  215 TYR   A CE2 1 
ATOM   1595 C CZ  . TYR   A 1 215 ? 4.700   2.805   7.331   1.00 22.18 ?  215 TYR   A CZ  1 
ATOM   1596 O OH  . TYR   A 1 215 ? 3.708   3.546   6.716   1.00 19.71 ?  215 TYR   A OH  1 
ATOM   1597 N N   . LEU   A 1 216 ? 9.863   -0.653  11.345  1.00 15.74 ?  216 LEU   A N   1 
ATOM   1598 C CA  . LEU   A 1 216 ? 10.527  -1.761  11.996  1.00 16.31 ?  216 LEU   A CA  1 
ATOM   1599 C C   . LEU   A 1 216 ? 10.352  -1.668  13.509  1.00 16.46 ?  216 LEU   A C   1 
ATOM   1600 O O   . LEU   A 1 216 ? 10.334  -2.693  14.160  1.00 17.21 ?  216 LEU   A O   1 
ATOM   1601 C CB  . LEU   A 1 216 ? 12.003  -1.782  11.662  1.00 17.69 ?  216 LEU   A CB  1 
ATOM   1602 C CG  . LEU   A 1 216 ? 12.281  -2.316  10.264  1.00 17.98 ?  216 LEU   A CG  1 
ATOM   1603 C CD1 . LEU   A 1 216 ? 13.663  -1.898  9.799   1.00 21.19 ?  216 LEU   A CD1 1 
ATOM   1604 C CD2 . LEU   A 1 216 ? 12.082  -3.827  10.309  1.00 17.88 ?  216 LEU   A CD2 1 
ATOM   1605 N N   . ALA   A 1 217 ? 10.339  -0.452  14.054  1.00 15.86 ?  217 ALA   A N   1 
ATOM   1606 C CA  . ALA   A 1 217 ? 10.204  -0.286  15.494  1.00 17.86 ?  217 ALA   A CA  1 
ATOM   1607 C C   . ALA   A 1 217 ? 8.877   -0.881  15.966  1.00 19.65 ?  217 ALA   A C   1 
ATOM   1608 O O   . ALA   A 1 217 ? 8.796   -1.474  17.035  1.00 19.99 ?  217 ALA   A O   1 
ATOM   1609 C CB  . ALA   A 1 217 ? 10.308  1.183   15.861  1.00 17.63 ?  217 ALA   A CB  1 
ATOM   1610 N N   . ILE   A 1 218 ? 7.812   -0.731  15.173  1.00 18.46 ?  218 ILE   A N   1 
ATOM   1611 C CA  . ILE   A 1 218 ? 6.539   -1.319  15.565  1.00 19.64 ?  218 ILE   A CA  1 
ATOM   1612 C C   . ILE   A 1 218 ? 6.714   -2.830  15.746  1.00 18.14 ?  218 ILE   A C   1 
ATOM   1613 O O   . ILE   A 1 218 ? 6.209   -3.434  16.691  1.00 18.79 ?  218 ILE   A O   1 
ATOM   1614 C CB  . ILE   A 1 218 ? 5.444   -0.945  14.535  1.00 18.51 ?  218 ILE   A CB  1 
ATOM   1615 C CG1 . ILE   A 1 218 ? 5.213   0.548   14.498  1.00 18.53 ?  218 ILE   A CG1 1 
ATOM   1616 C CG2 . ILE   A 1 218 ? 4.162   -1.701  14.855  1.00 20.67 ?  218 ILE   A CG2 1 
ATOM   1617 C CD1 . ILE   A 1 218 ? 4.491   1.089   13.285  1.00 20.10 ?  218 ILE   A CD1 1 
ATOM   1618 N N   . ALA   A 1 219 ? 7.376   -3.482  14.785  1.00 17.39 ?  219 ALA   A N   1 
ATOM   1619 C CA  . ALA   A 1 219 ? 7.555   -4.926  14.818  1.00 17.47 ?  219 ALA   A CA  1 
ATOM   1620 C C   . ALA   A 1 219 ? 8.409   -5.326  16.029  1.00 18.13 ?  219 ALA   A C   1 
ATOM   1621 O O   . ALA   A 1 219 ? 8.125   -6.324  16.697  1.00 18.33 ?  219 ALA   A O   1 
ATOM   1622 C CB  . ALA   A 1 219 ? 8.204   -5.372  13.509  1.00 19.15 ?  219 ALA   A CB  1 
ATOM   1623 N N   . ASP   A 1 220 ? 9.497   -4.572  16.240  1.00 17.73 ?  220 ASP   A N   1 
ATOM   1624 C CA  . ASP   A 1 220 ? 10.388  -4.798  17.359  1.00 19.55 ?  220 ASP   A CA  1 
ATOM   1625 C C   . ASP   A 1 220 ? 9.613   -4.791  18.680  1.00 20.96 ?  220 ASP   A C   1 
ATOM   1626 O O   . ASP   A 1 220 ? 9.879   -5.646  19.544  1.00 19.28 ?  220 ASP   A O   1 
ATOM   1627 C CB  . ASP   A 1 220 ? 11.565  -3.828  17.321  1.00 19.79 ?  220 ASP   A CB  1 
ATOM   1628 C CG  . ASP   A 1 220 ? 12.532  -4.039  16.165  1.00 20.39 ?  220 ASP   A CG  1 
ATOM   1629 O OD1 . ASP   A 1 220 ? 12.399  -5.041  15.414  1.00 18.65 ?  220 ASP   A OD1 1 
ATOM   1630 O OD2 . ASP   A 1 220 ? 13.406  -3.162  15.993  1.00 23.24 ?  220 ASP   A OD2 1 
ATOM   1631 N N   . GLU   A 1 221 ? 8.740   -3.791  18.836  1.00 21.71 ?  221 GLU   A N   1 
ATOM   1632 C CA  . GLU   A 1 221 ? 7.989   -3.593  20.074  1.00 22.79 ?  221 GLU   A CA  1 
ATOM   1633 C C   . GLU   A 1 221 ? 6.957   -4.714  20.259  1.00 23.26 ?  221 GLU   A C   1 
ATOM   1634 O O   . GLU   A 1 221 ? 6.747   -5.207  21.365  1.00 23.42 ?  221 GLU   A O   1 
ATOM   1635 C CB  . GLU   A 1 221 ? 7.353   -2.207  20.020  1.00 26.06 ?  221 GLU   A CB  1 
ATOM   1636 C CG  . GLU   A 1 221 ? 8.394   -1.103  20.180  1.00 34.86 ?  221 GLU   A CG  1 
ATOM   1637 C CD  . GLU   A 1 221 ? 8.043   0.325   19.758  1.00 44.78 ?  221 GLU   A CD  1 
ATOM   1638 O OE1 . GLU   A 1 221 ? 6.873   0.620   19.423  1.00 47.76 ?  221 GLU   A OE1 1 
ATOM   1639 O OE2 . GLU   A 1 221 ? 8.978   1.166   19.767  1.00 48.72 ?  221 GLU   A OE2 1 
ATOM   1640 N N   . LEU   A 1 222 ? 6.321   -5.163  19.178  1.00 19.09 ?  222 LEU   A N   1 
ATOM   1641 C CA  . LEU   A 1 222 ? 5.314   -6.194  19.285  1.00 19.27 ?  222 LEU   A CA  1 
ATOM   1642 C C   . LEU   A 1 222 ? 5.953   -7.561  19.444  1.00 18.47 ?  222 LEU   A C   1 
ATOM   1643 O O   . LEU   A 1 222 ? 5.373   -8.374  20.146  1.00 21.81 ?  222 LEU   A O   1 
ATOM   1644 C CB  . LEU   A 1 222 ? 4.457   -6.130  18.025  1.00 18.61 ?  222 LEU   A CB  1 
ATOM   1645 C CG  . LEU   A 1 222 ? 3.336   -5.103  18.027  1.00 19.46 ?  222 LEU   A CG  1 
ATOM   1646 C CD1 . LEU   A 1 222 ? 2.724   -5.104  16.632  1.00 19.72 ?  222 LEU   A CD1 1 
ATOM   1647 C CD2 . LEU   A 1 222 ? 2.272   -5.430  19.070  1.00 21.35 ?  222 LEU   A CD2 1 
ATOM   1648 N N   . PHE   A 1 223 ? 7.070   -7.876  18.751  1.00 17.17 ?  223 PHE   A N   1 
ATOM   1649 C CA  . PHE   A 1 223 ? 7.498   -9.268  18.654  1.00 18.42 ?  223 PHE   A CA  1 
ATOM   1650 C C   . PHE   A 1 223 ? 8.920   -9.482  19.186  1.00 20.50 ?  223 PHE   A C   1 
ATOM   1651 O O   . PHE   A 1 223 ? 9.399   -10.609 19.169  1.00 21.77 ?  223 PHE   A O   1 
ATOM   1652 C CB  . PHE   A 1 223 ? 7.457   -9.813  17.224  1.00 19.91 ?  223 PHE   A CB  1 
ATOM   1653 C CG  . PHE   A 1 223 ? 6.067   -9.747  16.621  1.00 19.65 ?  223 PHE   A CG  1 
ATOM   1654 C CD1 . PHE   A 1 223 ? 5.041   -10.510 17.167  1.00 21.54 ?  223 PHE   A CD1 1 
ATOM   1655 C CD2 . PHE   A 1 223 ? 5.769   -8.900  15.563  1.00 19.41 ?  223 PHE   A CD2 1 
ATOM   1656 C CE1 . PHE   A 1 223 ? 3.752   -10.452 16.653  1.00 21.54 ?  223 PHE   A CE1 1 
ATOM   1657 C CE2 . PHE   A 1 223 ? 4.467   -8.806  15.085  1.00 21.22 ?  223 PHE   A CE2 1 
ATOM   1658 C CZ  . PHE   A 1 223 ? 3.464   -9.582  15.649  1.00 19.88 ?  223 PHE   A CZ  1 
ATOM   1659 N N   . GLY   A 1 224 ? 9.622   -8.414  19.560  1.00 20.69 ?  224 GLY   A N   1 
ATOM   1660 C CA  . GLY   A 1 224 ? 11.045  -8.472  19.847  1.00 21.87 ?  224 GLY   A CA  1 
ATOM   1661 C C   . GLY   A 1 224 ? 11.855  -8.205  18.578  1.00 23.37 ?  224 GLY   A C   1 
ATOM   1662 O O   . GLY   A 1 224 ? 11.370  -8.414  17.468  1.00 21.24 ?  224 GLY   A O   1 
ATOM   1663 N N   . ALA   A 1 225 ? 13.122  -7.825  18.767  1.00 25.68 ?  225 ALA   A N   1 
ATOM   1664 C CA  . ALA   A 1 225 ? 13.972  -7.273  17.722  1.00 25.14 ?  225 ALA   A CA  1 
ATOM   1665 C C   . ALA   A 1 225 ? 14.479  -8.343  16.753  1.00 24.57 ?  225 ALA   A C   1 
ATOM   1666 O O   . ALA   A 1 225 ? 14.906  -8.009  15.662  1.00 24.03 ?  225 ALA   A O   1 
ATOM   1667 C CB  . ALA   A 1 225 ? 15.128  -6.503  18.375  1.00 25.47 ?  225 ALA   A CB  1 
ATOM   1668 N N   . ASP   A 1 226 ? 14.324  -9.628  17.081  1.00 22.72 ?  226 ASP   A N   1 
ATOM   1669 C CA  . ASP   A 1 226 ? 14.805  -10.701 16.219  1.00 25.94 ?  226 ASP   A CA  1 
ATOM   1670 C C   . ASP   A 1 226 ? 13.702  -11.157 15.263  1.00 23.62 ?  226 ASP   A C   1 
ATOM   1671 O O   . ASP   A 1 226 ? 13.963  -11.909 14.335  1.00 23.13 ?  226 ASP   A O   1 
ATOM   1672 C CB  . ASP   A 1 226 ? 15.282  -11.895 17.031  1.00 28.76 ?  226 ASP   A CB  1 
ATOM   1673 C CG  . ASP   A 1 226 ? 16.476  -11.574 17.921  1.00 37.45 ?  226 ASP   A CG  1 
ATOM   1674 O OD1 . ASP   A 1 226 ? 17.381  -10.872 17.436  1.00 40.52 ?  226 ASP   A OD1 1 
ATOM   1675 O OD2 . ASP   A 1 226 ? 16.492  -12.001 19.098  1.00 48.71 ?  226 ASP   A OD2 1 
ATOM   1676 N N   . TRP   A 1 227 ? 12.470  -10.688 15.467  1.00 21.06 ?  227 TRP   A N   1 
ATOM   1677 C CA  . TRP   A 1 227 ? 11.377  -11.248 14.705  1.00 19.91 ?  227 TRP   A CA  1 
ATOM   1678 C C   . TRP   A 1 227 ? 11.452  -10.920 13.205  1.00 18.57 ?  227 TRP   A C   1 
ATOM   1679 O O   . TRP   A 1 227 ? 11.228  -11.796 12.388  1.00 16.15 ?  227 TRP   A O   1 
ATOM   1680 C CB  . TRP   A 1 227 ? 10.043  -10.792 15.285  1.00 18.77 ?  227 TRP   A CB  1 
ATOM   1681 C CG  . TRP   A 1 227 ? 8.879   -11.388 14.546  1.00 18.22 ?  227 TRP   A CG  1 
ATOM   1682 C CD1 . TRP   A 1 227 ? 8.420   -12.676 14.593  1.00 16.77 ?  227 TRP   A CD1 1 
ATOM   1683 C CD2 . TRP   A 1 227 ? 8.037   -10.701 13.594  1.00 18.34 ?  227 TRP   A CD2 1 
ATOM   1684 N NE1 . TRP   A 1 227 ? 7.345   -12.842 13.763  1.00 17.39 ?  227 TRP   A NE1 1 
ATOM   1685 C CE2 . TRP   A 1 227 ? 7.091   -11.649 13.134  1.00 17.17 ?  227 TRP   A CE2 1 
ATOM   1686 C CE3 . TRP   A 1 227 ? 7.994   -9.394  13.083  1.00 18.08 ?  227 TRP   A CE3 1 
ATOM   1687 C CZ2 . TRP   A 1 227 ? 6.106   -11.306 12.221  1.00 16.38 ?  227 TRP   A CZ2 1 
ATOM   1688 C CZ3 . TRP   A 1 227 ? 7.036   -9.071  12.165  1.00 17.64 ?  227 TRP   A CZ3 1 
ATOM   1689 C CH2 . TRP   A 1 227 ? 6.098   -10.018 11.750  1.00 17.13 ?  227 TRP   A CH2 1 
ATOM   1690 N N   . ALA   A 1 228 ? 11.740  -9.671  12.870  1.00 18.15 ?  228 ALA   A N   1 
ATOM   1691 C CA  . ALA   A 1 228 ? 11.622  -9.147  11.517  1.00 18.50 ?  228 ALA   A CA  1 
ATOM   1692 C C   . ALA   A 1 228 ? 12.798  -9.535  10.613  1.00 17.62 ?  228 ALA   A C   1 
ATOM   1693 O O   . ALA   A 1 228 ? 13.521  -8.653  10.155  1.00 17.34 ?  228 ALA   A O   1 
ATOM   1694 C CB  . ALA   A 1 228 ? 11.524  -7.640  11.612  1.00 19.75 ?  228 ALA   A CB  1 
ATOM   1695 N N   . ASP   A 1 229 ? 12.917  -10.831 10.308  1.00 16.95 ?  229 ASP   A N   1 
ATOM   1696 C CA  . ASP   A 1 229 ? 13.848  -11.325 9.324   1.00 17.17 ?  229 ASP   A CA  1 
ATOM   1697 C C   . ASP   A 1 229 ? 13.076  -11.378 7.999   1.00 15.43 ?  229 ASP   A C   1 
ATOM   1698 O O   . ASP   A 1 229 ? 11.908  -10.979 7.919   1.00 15.65 ?  229 ASP   A O   1 
ATOM   1699 C CB  . ASP   A 1 229 ? 14.400  -12.671 9.761   1.00 18.98 ?  229 ASP   A CB  1 
ATOM   1700 C CG  . ASP   A 1 229 ? 13.395  -13.817 9.893   1.00 20.35 ?  229 ASP   A CG  1 
ATOM   1701 O OD1 . ASP   A 1 229 ? 12.203  -13.645 9.496   1.00 19.47 ?  229 ASP   A OD1 1 
ATOM   1702 O OD2 . ASP   A 1 229 ? 13.769  -14.886 10.450  1.00 22.47 ?  229 ASP   A OD2 1 
ATOM   1703 N N   . ALA   A 1 230 ? 13.712  -11.879 6.967   1.00 14.94 ?  230 ALA   A N   1 
ATOM   1704 C CA  . ALA   A 1 230 ? 13.112  -11.771 5.647   1.00 15.76 ?  230 ALA   A CA  1 
ATOM   1705 C C   . ALA   A 1 230 ? 11.933  -12.735 5.534   1.00 15.93 ?  230 ALA   A C   1 
ATOM   1706 O O   . ALA   A 1 230 ? 11.157  -12.569 4.614   1.00 14.72 ?  230 ALA   A O   1 
ATOM   1707 C CB  . ALA   A 1 230 ? 14.128  -12.023 4.577   1.00 16.37 ?  230 ALA   A CB  1 
ATOM   1708 N N   . ARG   A 1 231 ? 11.820  -13.767 6.378   1.00 15.17 ?  231 ARG   A N   1 
ATOM   1709 C CA  . ARG   A 1 231 ? 10.622  -14.585 6.353   1.00 16.11 ?  231 ARG   A CA  1 
ATOM   1710 C C   . ARG   A 1 231 ? 9.439   -13.875 7.029   1.00 16.46 ?  231 ARG   A C   1 
ATOM   1711 O O   . ARG   A 1 231 ? 8.304   -14.303 6.790   1.00 17.86 ?  231 ARG   A O   1 
ATOM   1712 C CB  . ARG   A 1 231 ? 10.901  -15.965 6.961   1.00 16.31 ?  231 ARG   A CB  1 
ATOM   1713 C CG  . ARG   A 1 231 ? 9.690   -16.884 7.120   1.00 16.11 ?  231 ARG   A CG  1 
ATOM   1714 C CD  . ARG   A 1 231 ? 9.052   -17.259 5.787   1.00 16.06 ?  231 ARG   A CD  1 
ATOM   1715 N NE  . ARG   A 1 231 ? 7.867   -18.075 5.922   1.00 16.40 ?  231 ARG   A NE  1 
ATOM   1716 C CZ  . ARG   A 1 231 ? 6.646   -17.640 6.248   1.00 14.88 ?  231 ARG   A CZ  1 
ATOM   1717 N NH1 . ARG   A 1 231 ? 6.411   -16.360 6.423   1.00 14.40 ?  231 ARG   A NH1 1 
ATOM   1718 N NH2 . ARG   A 1 231 ? 5.659   -18.510 6.377   1.00 15.74 ?  231 ARG   A NH2 1 
ATOM   1719 N N   . HIS   A 1 232 ? 9.656   -12.780 7.801   1.00 14.14 ?  232 HIS   A N   1 
ATOM   1720 C CA  . HIS   A 1 232 ? 8.571   -12.173 8.565   1.00 14.62 ?  232 HIS   A CA  1 
ATOM   1721 C C   . HIS   A 1 232 ? 8.310   -10.702 8.245   1.00 13.56 ?  232 HIS   A C   1 
ATOM   1722 O O   . HIS   A 1 232 ? 7.325   -10.133 8.734   1.00 13.10 ?  232 HIS   A O   1 
ATOM   1723 C CB  . HIS   A 1 232 ? 8.817   -12.378 10.072  1.00 14.68 ?  232 HIS   A CB  1 
ATOM   1724 C CG  . HIS   A 1 232 ? 8.776   -13.821 10.390  1.00 15.79 ?  232 HIS   A CG  1 
ATOM   1725 N ND1 . HIS   A 1 232 ? 9.895   -14.627 10.317  1.00 15.66 ?  232 HIS   A ND1 1 
ATOM   1726 C CD2 . HIS   A 1 232 ? 7.768   -14.614 10.746  1.00 14.88 ?  232 HIS   A CD2 1 
ATOM   1727 C CE1 . HIS   A 1 232 ? 9.554   -15.885 10.612  1.00 16.40 ?  232 HIS   A CE1 1 
ATOM   1728 N NE2 . HIS   A 1 232 ? 8.259   -15.901 10.882  1.00 16.24 ?  232 HIS   A NE2 1 
ATOM   1729 N N   . TYR   A 1 233 ? 9.186   -10.052 7.471   1.00 12.43 ?  233 TYR   A N   1 
ATOM   1730 C CA  . TYR   A 1 233 ? 9.043   -8.629  7.249   1.00 12.25 ?  233 TYR   A CA  1 
ATOM   1731 C C   . TYR   A 1 233 ? 9.609   -8.271  5.873   1.00 12.90 ?  233 TYR   A C   1 
ATOM   1732 O O   . TYR   A 1 233 ? 10.710  -8.698  5.534   1.00 12.82 ?  233 TYR   A O   1 
ATOM   1733 C CB  . TYR   A 1 233 ? 9.720   -7.851  8.377   1.00 13.51 ?  233 TYR   A CB  1 
ATOM   1734 C CG  . TYR   A 1 233 ? 9.120   -6.480  8.585   1.00 14.37 ?  233 TYR   A CG  1 
ATOM   1735 C CD1 . TYR   A 1 233 ? 9.313   -5.455  7.677   1.00 15.96 ?  233 TYR   A CD1 1 
ATOM   1736 C CD2 . TYR   A 1 233 ? 8.303   -6.232  9.680   1.00 16.03 ?  233 TYR   A CD2 1 
ATOM   1737 C CE1 . TYR   A 1 233 ? 8.777   -4.189  7.902   1.00 17.38 ?  233 TYR   A CE1 1 
ATOM   1738 C CE2 . TYR   A 1 233 ? 7.729   -4.988  9.888   1.00 16.08 ?  233 TYR   A CE2 1 
ATOM   1739 C CZ  . TYR   A 1 233 ? 7.982   -3.954  9.011   1.00 17.81 ?  233 TYR   A CZ  1 
ATOM   1740 O OH  . TYR   A 1 233 ? 7.368   -2.742  9.241   1.00 18.34 ?  233 TYR   A OH  1 
ATOM   1741 N N   . ARG   A 1 234 ? 8.845   -7.471  5.118   1.00 11.03 ?  234 ARG   A N   1 
ATOM   1742 C CA  . ARG   A 1 234 ? 9.307   -6.905  3.883   1.00 11.60 ?  234 ARG   A CA  1 
ATOM   1743 C C   . ARG   A 1 234 ? 8.828   -5.475  3.691   1.00 12.72 ?  234 ARG   A C   1 
ATOM   1744 O O   . ARG   A 1 234 ? 7.801   -5.054  4.247   1.00 12.69 ?  234 ARG   A O   1 
ATOM   1745 C CB  . ARG   A 1 234 ? 8.846   -7.725  2.673   1.00 11.36 ?  234 ARG   A CB  1 
ATOM   1746 C CG  . ARG   A 1 234 ? 9.295   -9.167  2.641   1.00 11.42 ?  234 ARG   A CG  1 
ATOM   1747 C CD  . ARG   A 1 234 ? 10.765  -9.384  2.354   1.00 11.06 ?  234 ARG   A CD  1 
ATOM   1748 N NE  . ARG   A 1 234 ? 11.001  -10.825 2.370   1.00 11.39 ?  234 ARG   A NE  1 
ATOM   1749 C CZ  . ARG   A 1 234 ? 10.537  -11.710 1.483   1.00 12.32 ?  234 ARG   A CZ  1 
ATOM   1750 N NH1 . ARG   A 1 234 ? 10.109  -11.315 0.296   1.00 13.54 ?  234 ARG   A NH1 1 
ATOM   1751 N NH2 . ARG   A 1 234 ? 10.537  -13.003 1.768   1.00 12.98 ?  234 ARG   A NH2 1 
ATOM   1752 N N   . PHE   A 1 235 ? 9.579   -4.744  2.845   1.00 12.96 ?  235 PHE   A N   1 
ATOM   1753 C CA  . PHE   A 1 235 ? 9.254   -3.384  2.441   1.00 13.02 ?  235 PHE   A CA  1 
ATOM   1754 C C   . PHE   A 1 235 ? 9.270   -3.257  0.926   1.00 14.54 ?  235 PHE   A C   1 
ATOM   1755 O O   . PHE   A 1 235 ? 10.111  -3.842  0.294   1.00 13.18 ?  235 PHE   A O   1 
ATOM   1756 C CB  . PHE   A 1 235 ? 10.315  -2.357  2.840   1.00 14.27 ?  235 PHE   A CB  1 
ATOM   1757 C CG  . PHE   A 1 235 ? 10.406  -2.014  4.318   1.00 15.93 ?  235 PHE   A CG  1 
ATOM   1758 C CD1 . PHE   A 1 235 ? 9.583   -1.023  4.836   1.00 16.98 ?  235 PHE   A CD1 1 
ATOM   1759 C CD2 . PHE   A 1 235 ? 11.319  -2.650  5.140   1.00 16.47 ?  235 PHE   A CD2 1 
ATOM   1760 C CE1 . PHE   A 1 235 ? 9.648   -0.713  6.180   1.00 18.76 ?  235 PHE   A CE1 1 
ATOM   1761 C CE2 . PHE   A 1 235 ? 11.395  -2.294  6.462   1.00 18.16 ?  235 PHE   A CE2 1 
ATOM   1762 C CZ  . PHE   A 1 235 ? 10.595  -1.300  6.960   1.00 18.07 ?  235 PHE   A CZ  1 
ATOM   1763 N N   . SER   A 1 236 ? 8.321   -2.476  0.387   1.00 16.09 ?  236 SER   A N   1 
ATOM   1764 C CA  A SER   A 1 236 ? 8.361   -2.011  -0.995  0.25 15.69 ?  236 SER   A CA  1 
ATOM   1765 C CA  B SER   A 1 236 ? 8.424   -1.984  -0.978  0.25 16.00 ?  236 SER   A CA  1 
ATOM   1766 C CA  C SER   A 1 236 ? 8.400   -1.994  -0.975  0.50 16.16 ?  236 SER   A CA  1 
ATOM   1767 C C   . SER   A 1 236 ? 7.847   -0.575  -1.045  1.00 16.60 ?  236 SER   A C   1 
ATOM   1768 O O   . SER   A 1 236 ? 6.762   -0.308  -0.537  1.00 16.33 ?  236 SER   A O   1 
ATOM   1769 C CB  A SER   A 1 236 ? 7.531   -2.886  -1.927  0.25 15.78 ?  236 SER   A CB  1 
ATOM   1770 C CB  B SER   A 1 236 ? 7.748   -2.898  -1.973  0.25 16.50 ?  236 SER   A CB  1 
ATOM   1771 C CB  C SER   A 1 236 ? 7.655   -2.915  -1.876  0.50 17.76 ?  236 SER   A CB  1 
ATOM   1772 O OG  A SER   A 1 236 ? 7.930   -4.250  -1.914  0.25 14.70 ?  236 SER   A OG  1 
ATOM   1773 O OG  B SER   A 1 236 ? 6.339   -2.721  -1.953  0.25 16.15 ?  236 SER   A OG  1 
ATOM   1774 O OG  C SER   A 1 236 ? 7.572   -2.323  -3.152  0.50 18.01 ?  236 SER   A OG  1 
ATOM   1775 N N   . ALA   A 1 237 ? 8.595   0.327   -1.683  1.00 18.21 ?  237 ALA   A N   1 
ATOM   1776 C CA  . ALA   A 1 237 ? 8.126   1.671   -1.926  1.00 20.90 ?  237 ALA   A CA  1 
ATOM   1777 C C   . ALA   A 1 237 ? 9.081   2.378   -2.884  1.00 22.88 ?  237 ALA   A C   1 
ATOM   1778 O O   . ALA   A 1 237 ? 10.307  2.281   -2.760  1.00 20.99 ?  237 ALA   A O   1 
ATOM   1779 C CB  . ALA   A 1 237 ? 7.987   2.416   -0.631  1.00 23.07 ?  237 ALA   A CB  1 
ATOM   1780 N N   . SER   A 1 238 ? 8.493   3.132   -3.795  1.00 24.30 ?  238 SER   A N   1 
ATOM   1781 C CA  A SER   A 1 238 ? 9.268   3.927   -4.727  0.50 24.23 ?  238 SER   A CA  1 
ATOM   1782 C CA  B SER   A 1 238 ? 9.253   3.945   -4.726  0.50 24.95 ?  238 SER   A CA  1 
ATOM   1783 C C   . SER   A 1 238 ? 10.147  4.894   -3.947  1.00 22.89 ?  238 SER   A C   1 
ATOM   1784 O O   . SER   A 1 238 ? 9.687   5.550   -3.024  1.00 24.24 ?  238 SER   A O   1 
ATOM   1785 C CB  A SER   A 1 238 ? 8.364   4.666   -5.672  0.50 25.83 ?  238 SER   A CB  1 
ATOM   1786 C CB  B SER   A 1 238 ? 8.343   4.708   -5.663  0.50 27.47 ?  238 SER   A CB  1 
ATOM   1787 O OG  A SER   A 1 238 ? 7.560   5.554   -4.918  0.50 26.25 ?  238 SER   A OG  1 
ATOM   1788 O OG  B SER   A 1 238 ? 7.794   3.832   -6.632  0.50 30.09 ?  238 SER   A OG  1 
ATOM   1789 N N   . GLY   A 1 239 ? 11.431  4.948   -4.311  1.00 22.73 ?  239 GLY   A N   1 
ATOM   1790 C CA  . GLY   A 1 239 ? 12.313  5.932   -3.720  1.00 20.74 ?  239 GLY   A CA  1 
ATOM   1791 C C   . GLY   A 1 239 ? 12.982  5.427   -2.443  1.00 21.11 ?  239 GLY   A C   1 
ATOM   1792 O O   . GLY   A 1 239 ? 13.976  6.002   -2.008  1.00 19.68 ?  239 GLY   A O   1 
ATOM   1793 N N   . LEU   A 1 240 ? 12.457  4.347   -1.846  1.00 18.26 ?  240 LEU   A N   1 
ATOM   1794 C CA  . LEU   A 1 240 ? 12.968  3.942   -0.552  1.00 17.57 ?  240 LEU   A CA  1 
ATOM   1795 C C   . LEU   A 1 240 ? 14.406  3.449   -0.672  1.00 18.31 ?  240 LEU   A C   1 
ATOM   1796 O O   . LEU   A 1 240 ? 15.238  3.762   0.163   1.00 18.24 ?  240 LEU   A O   1 
ATOM   1797 C CB  . LEU   A 1 240 ? 12.061  2.881   0.071   1.00 17.73 ?  240 LEU   A CB  1 
ATOM   1798 C CG  . LEU   A 1 240 ? 12.583  2.267   1.377   1.00 17.79 ?  240 LEU   A CG  1 
ATOM   1799 C CD1 . LEU   A 1 240 ? 12.781  3.389   2.385   1.00 18.59 ?  240 LEU   A CD1 1 
ATOM   1800 C CD2 . LEU   A 1 240 ? 11.683  1.177   1.979   1.00 18.71 ?  240 LEU   A CD2 1 
ATOM   1801 N N   . LEU   A 1 241 ? 14.728  2.687   -1.721  1.00 17.96 ?  241 LEU   A N   1 
ATOM   1802 C CA  . LEU   A 1 241 ? 16.071  2.115   -1.805  1.00 18.28 ?  241 LEU   A CA  1 
ATOM   1803 C C   . LEU   A 1 241 ? 17.122  3.235   -1.831  1.00 18.76 ?  241 LEU   A C   1 
ATOM   1804 O O   . LEU   A 1 241 ? 18.134  3.184   -1.124  1.00 18.32 ?  241 LEU   A O   1 
ATOM   1805 C CB  . LEU   A 1 241 ? 16.227  1.158   -2.981  1.00 18.37 ?  241 LEU   A CB  1 
ATOM   1806 C CG  . LEU   A 1 241 ? 17.638  0.567   -3.166  1.00 18.25 ?  241 LEU   A CG  1 
ATOM   1807 C CD1 . LEU   A 1 241 ? 18.083  -0.198  -1.981  1.00 19.35 ?  241 LEU   A CD1 1 
ATOM   1808 C CD2 . LEU   A 1 241 ? 17.733  -0.310  -4.377  1.00 19.32 ?  241 LEU   A CD2 1 
ATOM   1809 N N   . ALA   A 1 242 ? 16.874  4.232   -2.674  1.00 20.44 ?  242 ALA   A N   1 
ATOM   1810 C CA  . ALA   A 1 242 ? 17.732  5.407   -2.797  1.00 22.96 ?  242 ALA   A CA  1 
ATOM   1811 C C   . ALA   A 1 242 ? 17.900  6.093   -1.442  1.00 23.15 ?  242 ALA   A C   1 
ATOM   1812 O O   . ALA   A 1 242 ? 19.010  6.478   -1.081  1.00 23.01 ?  242 ALA   A O   1 
ATOM   1813 C CB  . ALA   A 1 242 ? 17.206  6.334   -3.872  1.00 21.75 ?  242 ALA   A CB  1 
ATOM   1814 N N   . SER   A 1 243 ? 16.834  6.153   -0.632  1.00 21.67 ?  243 SER   A N   1 
ATOM   1815 C CA  . SER   A 1 243 ? 16.894  6.831   0.654   1.00 20.22 ?  243 SER   A CA  1 
ATOM   1816 C C   . SER   A 1 243 ? 17.751  6.022   1.622   1.00 19.26 ?  243 SER   A C   1 
ATOM   1817 O O   . SER   A 1 243 ? 18.541  6.585   2.375   1.00 20.68 ?  243 SER   A O   1 
ATOM   1818 C CB  . SER   A 1 243 ? 15.508  7.082   1.216   1.00 19.78 ?  243 SER   A CB  1 
ATOM   1819 O OG  . SER   A 1 243 ? 15.532  7.767   2.473   1.00 20.41 ?  243 SER   A OG  1 
ATOM   1820 N N   . LEU   A 1 244 ? 17.565  4.692   1.618   1.00 18.61 ?  244 LEU   A N   1 
ATOM   1821 C CA  . LEU   A 1 244 ? 18.356  3.792   2.450   1.00 17.78 ?  244 LEU   A CA  1 
ATOM   1822 C C   . LEU   A 1 244 ? 19.840  3.907   2.116   1.00 19.50 ?  244 LEU   A C   1 
ATOM   1823 O O   . LEU   A 1 244 ? 20.681  4.022   2.996   1.00 21.30 ?  244 LEU   A O   1 
ATOM   1824 C CB  . LEU   A 1 244 ? 17.814  2.373   2.264   1.00 16.66 ?  244 LEU   A CB  1 
ATOM   1825 C CG  . LEU   A 1 244 ? 16.398  2.134   2.822   1.00 17.05 ?  244 LEU   A CG  1 
ATOM   1826 C CD1 . LEU   A 1 244 ? 15.975  0.696   2.629   1.00 16.62 ?  244 LEU   A CD1 1 
ATOM   1827 C CD2 . LEU   A 1 244 ? 16.289  2.508   4.305   1.00 17.73 ?  244 LEU   A CD2 1 
ATOM   1828 N N   . LEU   A 1 245 ? 20.159  3.904   0.828   1.00 19.81 ?  245 LEU   A N   1 
ATOM   1829 C CA  . LEU   A 1 245 ? 21.547  3.945   0.399   1.00 21.31 ?  245 LEU   A CA  1 
ATOM   1830 C C   . LEU   A 1 245 ? 22.204  5.254   0.801   1.00 21.51 ?  245 LEU   A C   1 
ATOM   1831 O O   . LEU   A 1 245 ? 23.341  5.256   1.270   1.00 22.46 ?  245 LEU   A O   1 
ATOM   1832 C CB  . LEU   A 1 245 ? 21.626  3.715   -1.104  1.00 20.55 ?  245 LEU   A CB  1 
ATOM   1833 C CG  . LEU   A 1 245 ? 21.431  2.253   -1.505  1.00 20.45 ?  245 LEU   A CG  1 
ATOM   1834 C CD1 . LEU   A 1 245 ? 21.367  2.189   -2.976  1.00 20.24 ?  245 LEU   A CD1 1 
ATOM   1835 C CD2 . LEU   A 1 245 ? 22.507  1.349   -0.930  1.00 20.71 ?  245 LEU   A CD2 1 
ATOM   1836 N N   . LYS   A 1 246 ? 21.446  6.333   0.662   1.00 25.10 ?  246 LYS   A N   1 
ATOM   1837 C CA  . LYS   A 1 246 ? 21.897  7.650   1.063   1.00 27.96 ?  246 LYS   A CA  1 
ATOM   1838 C C   . LYS   A 1 246 ? 22.205  7.673   2.553   1.00 27.39 ?  246 LYS   A C   1 
ATOM   1839 O O   . LYS   A 1 246 ? 23.218  8.231   2.934   1.00 27.63 ?  246 LYS   A O   1 
ATOM   1840 C CB  . LYS   A 1 246 ? 20.864  8.689   0.638   1.00 32.40 ?  246 LYS   A CB  1 
ATOM   1841 C CG  . LYS   A 1 246 ? 21.332  10.065  1.025   1.00 37.30 ?  246 LYS   A CG  1 
ATOM   1842 C CD  . LYS   A 1 246 ? 20.468  11.208  0.515   1.00 40.98 ?  246 LYS   A CD  1 
ATOM   1843 C CE  . LYS   A 1 246 ? 20.913  12.454  1.257   1.00 45.72 ?  246 LYS   A CE  1 
ATOM   1844 N NZ  . LYS   A 1 246 ? 19.866  13.473  1.255   1.00 48.15 ?  246 LYS   A NZ  1 
ATOM   1845 N N   . ALA   A 1 247 ? 21.335  7.085   3.394   1.00 25.54 ?  247 ALA   A N   1 
ATOM   1846 C CA  . ALA   A 1 247 ? 21.588  7.025   4.826   1.00 26.23 ?  247 ALA   A CA  1 
ATOM   1847 C C   . ALA   A 1 247 ? 22.892  6.278   5.093   1.00 28.05 ?  247 ALA   A C   1 
ATOM   1848 O O   . ALA   A 1 247 ? 23.587  6.581   6.056   1.00 27.67 ?  247 ALA   A O   1 
ATOM   1849 C CB  . ALA   A 1 247 ? 20.403  6.400   5.558   1.00 25.49 ?  247 ALA   A CB  1 
ATOM   1850 N N   . LEU   A 1 248 ? 23.226  5.314   4.226   1.00 28.51 ?  248 LEU   A N   1 
ATOM   1851 C CA  . LEU   A 1 248 ? 24.372  4.444   4.437   1.00 28.43 ?  248 LEU   A CA  1 
ATOM   1852 C C   . LEU   A 1 248 ? 25.604  5.022   3.741   1.00 29.93 ?  248 LEU   A C   1 
ATOM   1853 O O   . LEU   A 1 248 ? 26.658  4.422   3.774   1.00 30.62 ?  248 LEU   A O   1 
ATOM   1854 C CB  . LEU   A 1 248 ? 24.063  3.026   3.973   1.00 27.39 ?  248 LEU   A CB  1 
ATOM   1855 C CG  . LEU   A 1 248 ? 23.027  2.285   4.829   1.00 26.92 ?  248 LEU   A CG  1 
ATOM   1856 C CD1 . LEU   A 1 248 ? 22.451  1.071   4.129   1.00 26.07 ?  248 LEU   A CD1 1 
ATOM   1857 C CD2 . LEU   A 1 248 ? 23.649  1.839   6.166   1.00 26.39 ?  248 LEU   A CD2 1 
ATOM   1858 N N   . GLY   A 1 249 ? 25.459  6.172   3.087   1.00 34.54 ?  249 GLY   A N   1 
ATOM   1859 C CA  . GLY   A 1 249 ? 26.605  6.900   2.569   1.00 35.21 ?  249 GLY   A CA  1 
ATOM   1860 C C   . GLY   A 1 249 ? 26.835  6.692   1.080   1.00 36.81 ?  249 GLY   A C   1 
ATOM   1861 O O   . GLY   A 1 249 ? 27.849  7.151   0.576   1.00 38.70 ?  249 GLY   A O   1 
ATOM   1862 N N   . HIS   A 1 250 ? 25.924  5.994   0.389   1.00 35.86 ?  250 HIS   A N   1 
ATOM   1863 C CA  . HIS   A 1 250 ? 26.058  5.720   -1.033  1.00 35.89 ?  250 HIS   A CA  1 
ATOM   1864 C C   . HIS   A 1 250 ? 25.236  6.731   -1.839  1.00 38.49 ?  250 HIS   A C   1 
ATOM   1865 O O   . HIS   A 1 250 ? 24.052  6.439   -2.037  1.00 42.83 ?  250 HIS   A O   1 
ATOM   1866 C CB  . HIS   A 1 250 ? 25.720  4.254   -1.313  1.00 34.22 ?  250 HIS   A CB  1 
ATOM   1867 C CG  . HIS   A 1 250 ? 26.832  3.376   -0.836  1.00 36.60 ?  250 HIS   A CG  1 
ATOM   1868 N ND1 . HIS   A 1 250 ? 26.903  2.852   0.438   1.00 39.81 ?  250 HIS   A ND1 1 
ATOM   1869 C CD2 . HIS   A 1 250 ? 27.975  3.021   -1.440  1.00 37.18 ?  250 HIS   A CD2 1 
ATOM   1870 C CE1 . HIS   A 1 250 ? 28.019  2.155   0.574   1.00 37.60 ?  250 HIS   A CE1 1 
ATOM   1871 N NE2 . HIS   A 1 250 ? 28.687  2.257   -0.549  1.00 37.71 ?  250 HIS   A NE2 1 
ATOM   1872 N N   . ASP   B 1 3   ? -17.360 -22.386 -54.907 1.00 48.77 ?  3   ASP   B N   1 
ATOM   1873 C CA  . ASP   B 1 3   ? -17.822 -21.046 -54.457 1.00 49.28 ?  3   ASP   B CA  1 
ATOM   1874 C C   . ASP   B 1 3   ? -16.781 -20.420 -53.527 1.00 44.65 ?  3   ASP   B C   1 
ATOM   1875 O O   . ASP   B 1 3   ? -16.116 -21.104 -52.739 1.00 38.90 ?  3   ASP   B O   1 
ATOM   1876 C CB  . ASP   B 1 3   ? -19.185 -21.102 -53.772 1.00 53.11 ?  3   ASP   B CB  1 
ATOM   1877 C CG  . ASP   B 1 3   ? -20.069 -19.900 -54.093 1.00 58.92 ?  3   ASP   B CG  1 
ATOM   1878 O OD1 . ASP   B 1 3   ? -19.760 -18.780 -53.607 1.00 48.97 ?  3   ASP   B OD1 1 
ATOM   1879 O OD2 . ASP   B 1 3   ? -21.011 -20.072 -54.909 1.00 58.88 ?  3   ASP   B OD2 1 
ATOM   1880 N N   . LEU   B 1 4   ? -16.689 -19.088 -53.618 1.00 41.46 ?  4   LEU   B N   1 
ATOM   1881 C CA  . LEU   B 1 4   ? -15.926 -18.296 -52.675 1.00 38.87 ?  4   LEU   B CA  1 
ATOM   1882 C C   . LEU   B 1 4   ? -16.653 -18.287 -51.339 1.00 36.20 ?  4   LEU   B C   1 
ATOM   1883 O O   . LEU   B 1 4   ? -16.016 -18.133 -50.305 1.00 30.65 ?  4   LEU   B O   1 
ATOM   1884 C CB  . LEU   B 1 4   ? -15.770 -16.886 -53.232 1.00 40.81 ?  4   LEU   B CB  1 
ATOM   1885 C CG  . LEU   B 1 4   ? -14.834 -15.960 -52.454 1.00 41.62 ?  4   LEU   B CG  1 
ATOM   1886 C CD1 . LEU   B 1 4   ? -13.414 -16.474 -52.488 1.00 43.56 ?  4   LEU   B CD1 1 
ATOM   1887 C CD2 . LEU   B 1 4   ? -14.889 -14.530 -52.988 1.00 42.46 ?  4   LEU   B CD2 1 
ATOM   1888 N N   . LYS   B 1 5   ? -17.986 -18.429 -51.373 1.00 36.17 ?  5   LYS   B N   1 
ATOM   1889 C CA  . LYS   B 1 5   ? -18.785 -18.495 -50.156 1.00 36.71 ?  5   LYS   B CA  1 
ATOM   1890 C C   . LYS   B 1 5   ? -18.452 -19.766 -49.378 1.00 35.55 ?  5   LYS   B C   1 
ATOM   1891 O O   . LYS   B 1 5   ? -18.171 -19.699 -48.180 1.00 33.18 ?  5   LYS   B O   1 
ATOM   1892 C CB  . LYS   B 1 5   ? -20.297 -18.460 -50.422 1.00 39.32 ?  5   LYS   B CB  1 
ATOM   1893 C CG  . LYS   B 1 5   ? -20.818 -17.088 -50.850 1.00 44.57 ?  5   LYS   B CG  1 
ATOM   1894 C CD  . LYS   B 1 5   ? -22.143 -16.696 -50.204 1.00 51.98 ?  5   LYS   B CD  1 
ATOM   1895 C CE  . LYS   B 1 5   ? -22.593 -15.284 -50.473 1.00 54.57 ?  5   LYS   B CE  1 
ATOM   1896 N NZ  . LYS   B 1 5   ? -23.623 -15.231 -51.515 1.00 58.12 ?  5   LYS   B NZ  1 
ATOM   1897 N N   . ALA   B 1 6   ? -18.513 -20.919 -50.058 1.00 31.58 ?  6   ALA   B N   1 
ATOM   1898 C CA  . ALA   B 1 6   ? -18.161 -22.190 -49.445 1.00 31.60 ?  6   ALA   B CA  1 
ATOM   1899 C C   . ALA   B 1 6   ? -16.766 -22.114 -48.825 1.00 29.55 ?  6   ALA   B C   1 
ATOM   1900 O O   . ALA   B 1 6   ? -16.558 -22.500 -47.662 1.00 29.06 ?  6   ALA   B O   1 
ATOM   1901 C CB  . ALA   B 1 6   ? -18.246 -23.298 -50.456 1.00 31.87 ?  6   ALA   B CB  1 
ATOM   1902 N N   . SER   B 1 7   ? -15.817 -21.602 -49.610 1.00 27.80 ?  7   SER   B N   1 
ATOM   1903 C CA  . SER   B 1 7   ? -14.438 -21.485 -49.175 1.00 26.52 ?  7   SER   B CA  1 
ATOM   1904 C C   . SER   B 1 7   ? -14.310 -20.597 -47.935 1.00 27.13 ?  7   SER   B C   1 
ATOM   1905 O O   . SER   B 1 7   ? -13.550 -20.904 -46.992 1.00 26.31 ?  7   SER   B O   1 
ATOM   1906 C CB  . SER   B 1 7   ? -13.616 -20.945 -50.334 1.00 27.72 ?  7   SER   B CB  1 
ATOM   1907 O OG  . SER   B 1 7   ? -12.258 -21.139 -50.032 1.00 35.76 ?  7   SER   B OG  1 
ATOM   1908 N N   . SER   B 1 8   ? -14.999 -19.452 -47.979 1.00 23.35 ?  8   SER   B N   1 
ATOM   1909 C CA  . SER   B 1 8   ? -14.943 -18.460 -46.922 1.00 23.68 ?  8   SER   B CA  1 
ATOM   1910 C C   . SER   B 1 8   ? -15.498 -19.012 -45.608 1.00 24.20 ?  8   SER   B C   1 
ATOM   1911 O O   . SER   B 1 8   ? -14.923 -18.774 -44.536 1.00 22.22 ?  8   SER   B O   1 
ATOM   1912 C CB  . SER   B 1 8   ? -15.697 -17.227 -47.328 1.00 24.44 ?  8   SER   B CB  1 
ATOM   1913 O OG  . SER   B 1 8   ? -15.068 -16.589 -48.438 1.00 26.06 ?  8   SER   B OG  1 
ATOM   1914 N N   . LEU   B 1 9   ? -16.649 -19.692 -45.696 1.00 23.12 ?  9   LEU   B N   1 
ATOM   1915 C CA  . LEU   B 1 9   ? -17.237 -20.333 -44.525 1.00 23.40 ?  9   LEU   B CA  1 
ATOM   1916 C C   . LEU   B 1 9   ? -16.273 -21.346 -43.917 1.00 21.25 ?  9   LEU   B C   1 
ATOM   1917 O O   . LEU   B 1 9   ? -16.074 -21.387 -42.704 1.00 19.32 ?  9   LEU   B O   1 
ATOM   1918 C CB  . LEU   B 1 9   ? -18.542 -21.034 -44.883 1.00 24.65 ?  9   LEU   B CB  1 
ATOM   1919 C CG  . LEU   B 1 9   ? -19.338 -21.562 -43.692 1.00 27.50 ?  9   LEU   B CG  1 
ATOM   1920 C CD1 . LEU   B 1 9   ? -19.663 -20.413 -42.772 1.00 27.36 ?  9   LEU   B CD1 1 
ATOM   1921 C CD2 . LEU   B 1 9   ? -20.609 -22.248 -44.177 1.00 30.09 ?  9   LEU   B CD2 1 
ATOM   1922 N N   . ARG   B 1 10  ? -15.640 -22.143 -44.767 1.00 20.96 ?  10  ARG   B N   1 
ATOM   1923 C CA  . ARG   B 1 10  ? -14.679 -23.125 -44.318 1.00 21.73 ?  10  ARG   B CA  1 
ATOM   1924 C C   . ARG   B 1 10  ? -13.513 -22.421 -43.607 1.00 20.58 ?  10  ARG   B C   1 
ATOM   1925 O O   . ARG   B 1 10  ? -13.081 -22.836 -42.522 1.00 20.35 ?  10  ARG   B O   1 
ATOM   1926 C CB  . ARG   B 1 10  ? -14.224 -23.946 -45.531 1.00 24.83 ?  10  ARG   B CB  1 
ATOM   1927 C CG  . ARG   B 1 10  ? -13.315 -25.106 -45.154 1.00 26.81 ?  10  ARG   B CG  1 
ATOM   1928 C CD  . ARG   B 1 10  ? -12.775 -25.877 -46.361 1.00 32.22 ?  10  ARG   B CD  1 
ATOM   1929 N NE  . ARG   B 1 10  ? -12.257 -27.130 -45.812 1.00 36.56 ?  10  ARG   B NE  1 
ATOM   1930 C CZ  . ARG   B 1 10  ? -11.503 -28.005 -46.468 1.00 36.11 ?  10  ARG   B CZ  1 
ATOM   1931 N NH1 . ARG   B 1 10  ? -10.946 -27.661 -47.610 1.00 29.45 ?  10  ARG   B NH1 1 
ATOM   1932 N NH2 . ARG   B 1 10  ? -11.303 -29.222 -45.958 1.00 37.96 ?  10  ARG   B NH2 1 
ATOM   1933 N N   . ALA   B 1 11  ? -12.954 -21.388 -44.249 1.00 19.05 ?  11  ALA   B N   1 
ATOM   1934 C CA  . ALA   B 1 11  ? -11.818 -20.693 -43.677 1.00 19.63 ?  11  ALA   B CA  1 
ATOM   1935 C C   . ALA   B 1 11  ? -12.167 -20.029 -42.345 1.00 17.45 ?  11  ALA   B C   1 
ATOM   1936 O O   . ALA   B 1 11  ? -11.339 -20.007 -41.454 1.00 16.15 ?  11  ALA   B O   1 
ATOM   1937 C CB  . ALA   B 1 11  ? -11.324 -19.668 -44.660 1.00 20.94 ?  11  ALA   B CB  1 
ATOM   1938 N N   . LEU   B 1 12  ? -13.340 -19.411 -42.231 1.00 17.59 ?  12  LEU   B N   1 
ATOM   1939 C CA  . LEU   B 1 12  ? -13.739 -18.774 -40.970 1.00 16.93 ?  12  LEU   B CA  1 
ATOM   1940 C C   . LEU   B 1 12  ? -13.674 -19.760 -39.813 1.00 17.37 ?  12  LEU   B C   1 
ATOM   1941 O O   . LEU   B 1 12  ? -13.139 -19.421 -38.753 1.00 16.90 ?  12  LEU   B O   1 
ATOM   1942 C CB  . LEU   B 1 12  ? -15.131 -18.189 -41.167 1.00 18.57 ?  12  LEU   B CB  1 
ATOM   1943 C CG  . LEU   B 1 12  ? -15.765 -17.446 -39.977 1.00 19.72 ?  12  LEU   B CG  1 
ATOM   1944 C CD1 . LEU   B 1 12  ? -16.712 -16.450 -40.561 1.00 20.10 ?  12  LEU   B CD1 1 
ATOM   1945 C CD2 . LEU   B 1 12  ? -16.476 -18.342 -38.959 1.00 19.30 ?  12  LEU   B CD2 1 
ATOM   1946 N N   . LYS   B 1 13  ? -14.143 -20.991 -40.056 1.00 17.90 ?  13  LYS   B N   1 
ATOM   1947 C CA  . LYS   B 1 13  ? -14.200 -22.034 -39.044 1.00 18.57 ?  13  LYS   B CA  1 
ATOM   1948 C C   . LYS   B 1 13  ? -12.828 -22.596 -38.716 1.00 17.51 ?  13  LYS   B C   1 
ATOM   1949 O O   . LYS   B 1 13  ? -12.701 -23.381 -37.773 1.00 18.14 ?  13  LYS   B O   1 
ATOM   1950 C CB  . LYS   B 1 13  ? -15.147 -23.169 -39.458 1.00 19.65 ?  13  LYS   B CB  1 
ATOM   1951 C CG  . LYS   B 1 13  ? -16.591 -22.696 -39.440 1.00 24.24 ?  13  LYS   B CG  1 
ATOM   1952 C CD  . LYS   B 1 13  ? -17.618 -23.715 -39.918 1.00 26.77 ?  13  LYS   B CD  1 
ATOM   1953 C CE  . LYS   B 1 13  ? -18.898 -23.009 -40.138 1.00 30.91 ?  13  LYS   B CE  1 
ATOM   1954 N NZ  . LYS   B 1 13  ? -20.005 -23.944 -40.318 1.00 36.01 ?  13  LYS   B NZ  1 
ATOM   1955 N N   . LEU   B 1 14  ? -11.808 -22.204 -39.506 1.00 16.15 ?  14  LEU   B N   1 
ATOM   1956 C CA  . LEU   B 1 14  ? -10.434 -22.611 -39.244 1.00 16.31 ?  14  LEU   B CA  1 
ATOM   1957 C C   . LEU   B 1 14  ? -9.611  -21.456 -38.654 1.00 16.16 ?  14  LEU   B C   1 
ATOM   1958 O O   . LEU   B 1 14  ? -8.385  -21.569 -38.563 1.00 14.84 ?  14  LEU   B O   1 
ATOM   1959 C CB  . LEU   B 1 14  ? -9.828  -23.121 -40.554 1.00 16.34 ?  14  LEU   B CB  1 
ATOM   1960 C CG  . LEU   B 1 14  ? -10.519 -24.348 -41.174 1.00 17.57 ?  14  LEU   B CG  1 
ATOM   1961 C CD1 . LEU   B 1 14  ? -10.019 -24.580 -42.573 1.00 17.56 ?  14  LEU   B CD1 1 
ATOM   1962 C CD2 . LEU   B 1 14  ? -10.344 -25.576 -40.315 1.00 18.22 ?  14  LEU   B CD2 1 
ATOM   1963 N N   . MET   B 1 15  ? -10.234 -20.314 -38.307 1.00 15.33 ?  15  MET   B N   1 
ATOM   1964 C CA  . MET   B 1 15  ? -9.441  -19.168 -37.897 1.00 15.41 ?  15  MET   B CA  1 
ATOM   1965 C C   . MET   B 1 15  ? -9.031  -19.288 -36.424 1.00 14.95 ?  15  MET   B C   1 
ATOM   1966 O O   . MET   B 1 15  ? -9.798  -19.748 -35.573 1.00 15.30 ?  15  MET   B O   1 
ATOM   1967 C CB  . MET   B 1 15  ? -10.143 -17.818 -38.047 1.00 16.73 ?  15  MET   B CB  1 
ATOM   1968 C CG  . MET   B 1 15  ? -10.279 -17.358 -39.479 1.00 20.86 ?  15  MET   B CG  1 
ATOM   1969 S SD  . MET   B 1 15  ? -10.690 -15.609 -39.636 1.00 24.61 ?  15  MET   B SD  1 
ATOM   1970 C CE  . MET   B 1 15  ? -9.286  -14.733 -38.925 1.00 30.24 ?  15  MET   B CE  1 
ATOM   1971 N N   . ASP   B 1 16  ? -7.781  -18.880 -36.160 1.00 14.76 ?  16  ASP   B N   1 
ATOM   1972 C CA  . ASP   B 1 16  ? -7.366  -18.548 -34.809 1.00 14.27 ?  16  ASP   B CA  1 
ATOM   1973 C C   . ASP   B 1 16  ? -7.431  -17.036 -34.690 1.00 15.61 ?  16  ASP   B C   1 
ATOM   1974 O O   . ASP   B 1 16  ? -6.556  -16.337 -35.174 1.00 16.50 ?  16  ASP   B O   1 
ATOM   1975 C CB  . ASP   B 1 16  ? -5.949  -18.952 -34.515 1.00 14.12 ?  16  ASP   B CB  1 
ATOM   1976 C CG  . ASP   B 1 16  ? -5.682  -20.428 -34.301 1.00 14.67 ?  16  ASP   B CG  1 
ATOM   1977 O OD1 . ASP   B 1 16  ? -6.574  -21.268 -34.493 1.00 15.43 ?  16  ASP   B OD1 1 
ATOM   1978 O OD2 . ASP   B 1 16  ? -4.551  -20.727 -33.884 1.00 18.61 ?  16  ASP   B OD2 1 
ATOM   1979 N N   . LEU   B 1 17  ? -8.541  -16.521 -34.160 1.00 16.70 ?  17  LEU   B N   1 
ATOM   1980 C CA  . LEU   B 1 17  ? -8.791  -15.092 -34.244 1.00 17.78 ?  17  LEU   B CA  1 
ATOM   1981 C C   . LEU   B 1 17  ? -7.966  -14.366 -33.181 1.00 20.87 ?  17  LEU   B C   1 
ATOM   1982 O O   . LEU   B 1 17  ? -8.038  -14.698 -32.007 1.00 19.75 ?  17  LEU   B O   1 
ATOM   1983 C CB  . LEU   B 1 17  ? -10.278 -14.814 -34.079 1.00 17.34 ?  17  LEU   B CB  1 
ATOM   1984 C CG  . LEU   B 1 17  ? -10.717 -13.375 -34.362 1.00 18.42 ?  17  LEU   B CG  1 
ATOM   1985 C CD1 . LEU   B 1 17  ? -10.556 -13.071 -35.860 1.00 19.53 ?  17  LEU   B CD1 1 
ATOM   1986 C CD2 . LEU   B 1 17  ? -12.152 -13.194 -33.860 1.00 19.29 ?  17  LEU   B CD2 1 
ATOM   1987 N N   . SER   B 1 18  ? -7.256  -13.312 -33.562 1.00 23.75 ?  18  SER   B N   1 
ATOM   1988 C CA  . SER   B 1 18  ? -6.474  -12.546 -32.592 1.00 27.41 ?  18  SER   B CA  1 
ATOM   1989 C C   . SER   B 1 18  ? -6.790  -11.071 -32.794 1.00 32.11 ?  18  SER   B C   1 
ATOM   1990 O O   . SER   B 1 18  ? -7.298  -10.703 -33.847 1.00 36.62 ?  18  SER   B O   1 
ATOM   1991 C CB  . SER   B 1 18  ? -5.041  -12.797 -32.760 1.00 29.07 ?  18  SER   B CB  1 
ATOM   1992 O OG  . SER   B 1 18  ? -4.786  -12.610 -34.139 1.00 35.93 ?  18  SER   B OG  1 
ATOM   1993 N N   . THR   B 1 19  ? -6.588  -10.256 -31.757 1.00 41.41 ?  19  THR   B N   1 
ATOM   1994 C CA  . THR   B 1 19  ? -7.022  -8.867  -31.808 1.00 46.20 ?  19  THR   B CA  1 
ATOM   1995 C C   . THR   B 1 19  ? -6.402  -8.184  -33.004 1.00 47.74 ?  19  THR   B C   1 
ATOM   1996 O O   . THR   B 1 19  ? -5.156  -8.254  -33.082 1.00 53.89 ?  19  THR   B O   1 
ATOM   1997 C CB  . THR   B 1 19  ? -6.646  -8.145  -30.520 1.00 50.92 ?  19  THR   B CB  1 
ATOM   1998 O OG1 . THR   B 1 19  ? -7.078  -6.828  -30.845 1.00 54.98 ?  19  THR   B OG1 1 
ATOM   1999 C CG2 . THR   B 1 19  ? -5.159  -8.188  -30.210 1.00 51.11 ?  19  THR   B CG2 1 
ATOM   2000 N N   . THR   B 1 25  ? -5.883  -4.827  -23.330 1.00 35.35 ?  25  THR   B N   1 
ATOM   2001 C CA  . THR   B 1 25  ? -6.920  -4.639  -22.281 1.00 31.79 ?  25  THR   B CA  1 
ATOM   2002 C C   . THR   B 1 25  ? -7.917  -5.804  -22.284 1.00 31.21 ?  25  THR   B C   1 
ATOM   2003 O O   . THR   B 1 25  ? -8.214  -6.427  -23.313 1.00 27.65 ?  25  THR   B O   1 
ATOM   2004 C CB  . THR   B 1 25  ? -7.653  -3.313  -22.450 1.00 34.02 ?  25  THR   B CB  1 
ATOM   2005 O OG1 . THR   B 1 25  ? -8.357  -3.492  -23.678 1.00 34.66 ?  25  THR   B OG1 1 
ATOM   2006 C CG2 . THR   B 1 25  ? -6.728  -2.106  -22.461 1.00 35.67 ?  25  THR   B CG2 1 
ATOM   2007 N N   . ASP   B 1 26  ? -8.507  -6.025  -21.104 1.00 30.63 ?  26  ASP   B N   1 
ATOM   2008 C CA  . ASP   B 1 26  ? -9.547  -7.024  -20.925 1.00 29.59 ?  26  ASP   B CA  1 
ATOM   2009 C C   . ASP   B 1 26  ? -10.725 -6.730  -21.849 1.00 29.30 ?  26  ASP   B C   1 
ATOM   2010 O O   . ASP   B 1 26  ? -11.324 -7.648  -22.405 1.00 27.14 ?  26  ASP   B O   1 
ATOM   2011 C CB  . ASP   B 1 26  ? -9.939  -7.098  -19.461 1.00 30.85 ?  26  ASP   B CB  1 
ATOM   2012 C CG  . ASP   B 1 26  ? -8.938  -7.785  -18.536 1.00 33.52 ?  26  ASP   B CG  1 
ATOM   2013 O OD1 . ASP   B 1 26  ? -7.902  -8.265  -19.020 1.00 31.43 ?  26  ASP   B OD1 1 
ATOM   2014 O OD2 . ASP   B 1 26  ? -9.216  -7.839  -17.330 1.00 38.42 ?  26  ASP   B OD2 1 
ATOM   2015 N N   . GLU   B 1 27  ? -11.025 -5.449  -22.061 1.00 29.81 ?  27  GLU   B N   1 
ATOM   2016 C CA  . GLU   B 1 27  ? -12.168 -5.080  -22.887 1.00 31.68 ?  27  GLU   B CA  1 
ATOM   2017 C C   . GLU   B 1 27  ? -11.932 -5.582  -24.310 1.00 30.21 ?  27  GLU   B C   1 
ATOM   2018 O O   . GLU   B 1 27  ? -12.841 -6.058  -24.995 1.00 26.46 ?  27  GLU   B O   1 
ATOM   2019 C CB  . GLU   B 1 27  ? -12.365 -3.565  -22.911 1.00 37.85 ?  27  GLU   B CB  1 
ATOM   2020 C CG  . GLU   B 1 27  ? -12.733 -2.950  -21.563 1.00 45.45 ?  27  GLU   B CG  1 
ATOM   2021 C CD  . GLU   B 1 27  ? -12.700 -1.417  -21.577 1.00 58.88 ?  27  GLU   B CD  1 
ATOM   2022 O OE1 . GLU   B 1 27  ? -11.632 -0.823  -21.906 1.00 59.36 ?  27  GLU   B OE1 1 
ATOM   2023 O OE2 . GLU   B 1 27  ? -13.751 -0.803  -21.256 1.00 59.14 ?  27  GLU   B OE2 1 
ATOM   2024 N N   . LYS   B 1 28  ? -10.696 -5.436  -24.768 1.00 27.85 ?  28  LYS   B N   1 
ATOM   2025 C CA  . LYS   B 1 28  ? -10.358 -5.857  -26.114 1.00 29.34 ?  28  LYS   B CA  1 
ATOM   2026 C C   . LYS   B 1 28  ? -10.448 -7.374  -26.231 1.00 26.75 ?  28  LYS   B C   1 
ATOM   2027 O O   . LYS   B 1 28  ? -10.797 -7.871  -27.298 1.00 24.67 ?  28  LYS   B O   1 
ATOM   2028 C CB  . LYS   B 1 28  ? -8.943  -5.427  -26.493 1.00 31.33 ?  28  LYS   B CB  1 
ATOM   2029 C CG  . LYS   B 1 28  ? -8.787  -3.933  -26.654 1.00 38.36 ?  28  LYS   B CG  1 
ATOM   2030 C CD  . LYS   B 1 28  ? -9.356  -3.472  -27.983 1.00 44.50 ?  28  LYS   B CD  1 
ATOM   2031 C CE  . LYS   B 1 28  ? -9.355  -1.984  -28.111 1.00 52.15 ?  28  LYS   B CE  1 
ATOM   2032 N NZ  . LYS   B 1 28  ? -10.088 -1.657  -29.336 1.00 54.51 ?  28  LYS   B NZ  1 
ATOM   2033 N N   . VAL   B 1 29  ? -10.037 -8.089  -25.164 1.00 23.96 ?  29  VAL   B N   1 
ATOM   2034 C CA  . VAL   B 1 29  ? -10.077 -9.536  -25.170 1.00 22.27 ?  29  VAL   B CA  1 
ATOM   2035 C C   . VAL   B 1 29  ? -11.537 -9.995  -25.225 1.00 22.58 ?  29  VAL   B C   1 
ATOM   2036 O O   . VAL   B 1 29  ? -11.875 -10.960 -25.928 1.00 20.73 ?  29  VAL   B O   1 
ATOM   2037 C CB  . VAL   B 1 29  ? -9.311  -10.121 -23.962 1.00 22.78 ?  29  VAL   B CB  1 
ATOM   2038 C CG1 . VAL   B 1 29  ? -9.517  -11.627 -23.805 1.00 20.87 ?  29  VAL   B CG1 1 
ATOM   2039 C CG2 . VAL   B 1 29  ? -7.821  -9.824  -24.087 1.00 23.77 ?  29  VAL   B CG2 1 
ATOM   2040 N N   . ILE   B 1 30  ? -12.378 -9.335  -24.426 1.00 22.96 ?  30  ILE   B N   1 
ATOM   2041 C CA  . ILE   B 1 30  ? -13.789 -9.688  -24.332 1.00 21.58 ?  30  ILE   B CA  1 
ATOM   2042 C C   . ILE   B 1 30  ? -14.412 -9.480  -25.702 1.00 20.48 ?  30  ILE   B C   1 
ATOM   2043 O O   . ILE   B 1 30  ? -15.111 -10.361 -26.168 1.00 20.90 ?  30  ILE   B O   1 
ATOM   2044 C CB  . ILE   B 1 30  ? -14.494 -8.878  -23.226 1.00 23.29 ?  30  ILE   B CB  1 
ATOM   2045 C CG1 . ILE   B 1 30  ? -14.051 -9.332  -21.838 1.00 23.89 ?  30  ILE   B CG1 1 
ATOM   2046 C CG2 . ILE   B 1 30  ? -16.016 -8.906  -23.380 1.00 23.25 ?  30  ILE   B CG2 1 
ATOM   2047 C CD1 . ILE   B 1 30  ? -14.430 -8.361  -20.730 1.00 26.95 ?  30  ILE   B CD1 1 
ATOM   2048 N N   . ALA   B 1 31  ? -14.126 -8.337  -26.327 1.00 22.51 ?  31  ALA   B N   1 
ATOM   2049 C CA  . ALA   B 1 31  ? -14.626 -8.053  -27.670 1.00 23.56 ?  31  ALA   B CA  1 
ATOM   2050 C C   . ALA   B 1 31  ? -14.152 -9.105  -28.666 1.00 24.95 ?  31  ALA   B C   1 
ATOM   2051 O O   . ALA   B 1 31  ? -14.919 -9.551  -29.507 1.00 24.37 ?  31  ALA   B O   1 
ATOM   2052 C CB  . ALA   B 1 31  ? -14.210 -6.681  -28.134 1.00 23.72 ?  31  ALA   B CB  1 
ATOM   2053 N N   . LEU   B 1 32  ? -12.891 -9.515  -28.565 1.00 22.45 ?  32  LEU   B N   1 
ATOM   2054 C CA  . LEU   B 1 32  ? -12.359 -10.543 -29.444 1.00 20.78 ?  32  LEU   B CA  1 
ATOM   2055 C C   . LEU   B 1 32  ? -13.225 -11.776 -29.310 1.00 18.90 ?  32  LEU   B C   1 
ATOM   2056 O O   . LEU   B 1 32  ? -13.575 -12.422 -30.311 1.00 19.64 ?  32  LEU   B O   1 
ATOM   2057 C CB  . LEU   B 1 32  ? -10.908 -10.860 -29.071 1.00 20.63 ?  32  LEU   B CB  1 
ATOM   2058 C CG  . LEU   B 1 32  ? -10.203 -11.914 -29.927 1.00 21.86 ?  32  LEU   B CG  1 
ATOM   2059 C CD1 . LEU   B 1 32  ? -10.117 -11.523 -31.388 1.00 21.99 ?  32  LEU   B CD1 1 
ATOM   2060 C CD2 . LEU   B 1 32  ? -8.802  -12.140 -29.427 1.00 23.40 ?  32  LEU   B CD2 1 
ATOM   2061 N N   . CYS   B 1 33  ? -13.518 -12.134 -28.050 1.00 17.83 ?  33  CYS   B N   1 
ATOM   2062 C CA  . CYS   B 1 33  ? -14.291 -13.338 -27.804 1.00 18.40 ?  33  CYS   B CA  1 
ATOM   2063 C C   . CYS   B 1 33  ? -15.656 -13.239 -28.484 1.00 18.64 ?  33  CYS   B C   1 
ATOM   2064 O O   . CYS   B 1 33  ? -16.139 -14.202 -29.102 1.00 18.84 ?  33  CYS   B O   1 
ATOM   2065 C CB  . CYS   B 1 33  ? -14.427 -13.561 -26.304 1.00 19.37 ?  33  CYS   B CB  1 
ATOM   2066 S SG  . CYS   B 1 33  ? -12.873 -14.122 -25.571 1.00 21.27 ?  33  CYS   B SG  1 
ATOM   2067 N N   . HIS   B 1 34  ? -16.271 -12.061 -28.352 1.00 19.86 ?  34  HIS   B N   1 
ATOM   2068 C CA  . HIS   B 1 34  ? -17.570 -11.808 -28.964 1.00 21.80 ?  34  HIS   B CA  1 
ATOM   2069 C C   . HIS   B 1 34  ? -17.487 -11.932 -30.476 1.00 21.76 ?  34  HIS   B C   1 
ATOM   2070 O O   . HIS   B 1 34  ? -18.388 -12.499 -31.122 1.00 21.36 ?  34  HIS   B O   1 
ATOM   2071 C CB  . HIS   B 1 34  ? -18.110 -10.441 -28.540 1.00 23.72 ?  34  HIS   B CB  1 
ATOM   2072 C CG  . HIS   B 1 34  ? -18.394 -10.370 -27.086 1.00 23.13 ?  34  HIS   B CG  1 
ATOM   2073 N ND1 . HIS   B 1 34  ? -18.569 -9.166  -26.452 1.00 25.11 ?  34  HIS   B ND1 1 
ATOM   2074 C CD2 . HIS   B 1 34  ? -18.593 -11.310 -26.177 1.00 22.96 ?  34  HIS   B CD2 1 
ATOM   2075 C CE1 . HIS   B 1 34  ? -18.815 -9.382  -25.179 1.00 23.21 ?  34  HIS   B CE1 1 
ATOM   2076 N NE2 . HIS   B 1 34  ? -18.854 -10.680 -24.985 1.00 23.84 ?  34  HIS   B NE2 1 
ATOM   2077 N N   . GLN   B 1 35  ? -16.419 -11.372 -31.040 1.00 22.02 ?  35  GLN   B N   1 
ATOM   2078 C CA  . GLN   B 1 35  ? -16.257 -11.385 -32.481 1.00 24.16 ?  35  GLN   B CA  1 
ATOM   2079 C C   . GLN   B 1 35  ? -16.039 -12.798 -33.019 1.00 22.40 ?  35  GLN   B C   1 
ATOM   2080 O O   . GLN   B 1 35  ? -16.363 -13.041 -34.172 1.00 23.12 ?  35  GLN   B O   1 
ATOM   2081 C CB  . GLN   B 1 35  ? -15.063 -10.555 -32.915 1.00 27.79 ?  35  GLN   B CB  1 
ATOM   2082 C CG  . GLN   B 1 35  ? -15.191 -9.070  -32.607 1.00 33.31 ?  35  GLN   B CG  1 
ATOM   2083 C CD  . GLN   B 1 35  ? -13.850 -8.370  -32.578 1.00 40.32 ?  35  GLN   B CD  1 
ATOM   2084 O OE1 . GLN   B 1 35  ? -12.784 -8.983  -32.716 1.00 47.03 ?  35  GLN   B OE1 1 
ATOM   2085 N NE2 . GLN   B 1 35  ? -13.887 -7.063  -32.385 1.00 49.82 ?  35  GLN   B NE2 1 
ATOM   2086 N N   . ALA   B 1 36  ? -15.457 -13.708 -32.222 1.00 20.14 ?  36  ALA   B N   1 
ATOM   2087 C CA  . ALA   B 1 36  ? -15.257 -15.098 -32.631 1.00 18.26 ?  36  ALA   B CA  1 
ATOM   2088 C C   . ALA   B 1 36  ? -16.553 -15.875 -32.846 1.00 18.10 ?  36  ALA   B C   1 
ATOM   2089 O O   . ALA   B 1 36  ? -16.525 -16.904 -33.511 1.00 17.08 ?  36  ALA   B O   1 
ATOM   2090 C CB  . ALA   B 1 36  ? -14.388 -15.846 -31.627 1.00 17.10 ?  36  ALA   B CB  1 
ATOM   2091 N N   . LYS   B 1 37  ? -17.649 -15.439 -32.195 1.00 19.77 ?  37  LYS   B N   1 
ATOM   2092 C CA  . LYS   B 1 37  ? -18.954 -16.051 -32.367 1.00 20.44 ?  37  LYS   B CA  1 
ATOM   2093 C C   . LYS   B 1 37  ? -19.718 -15.272 -33.431 1.00 21.53 ?  37  LYS   B C   1 
ATOM   2094 O O   . LYS   B 1 37  ? -20.364 -14.265 -33.146 1.00 21.18 ?  37  LYS   B O   1 
ATOM   2095 C CB  . LYS   B 1 37  ? -19.643 -15.996 -31.010 1.00 21.27 ?  37  LYS   B CB  1 
ATOM   2096 C CG  . LYS   B 1 37  ? -21.082 -16.483 -30.983 1.00 21.33 ?  37  LYS   B CG  1 
ATOM   2097 C CD  . LYS   B 1 37  ? -21.724 -16.292 -29.607 1.00 22.85 ?  37  LYS   B CD  1 
ATOM   2098 C CE  . LYS   B 1 37  ? -23.024 -17.012 -29.560 1.00 24.51 ?  37  LYS   B CE  1 
ATOM   2099 N NZ  . LYS   B 1 37  ? -23.776 -16.761 -28.320 1.00 26.19 ?  37  LYS   B NZ  1 
ATOM   2100 N N   . THR   B 1 38  ? -19.516 -15.677 -34.669 1.00 19.52 ?  38  THR   B N   1 
ATOM   2101 C CA  . THR   B 1 38  ? -19.970 -14.878 -35.792 1.00 20.67 ?  38  THR   B CA  1 
ATOM   2102 C C   . THR   B 1 38  ? -21.368 -15.338 -36.166 1.00 19.62 ?  38  THR   B C   1 
ATOM   2103 O O   . THR   B 1 38  ? -21.758 -16.473 -35.857 1.00 19.45 ?  38  THR   B O   1 
ATOM   2104 C CB  . THR   B 1 38  ? -19.021 -14.991 -36.993 1.00 20.13 ?  38  THR   B CB  1 
ATOM   2105 O OG1 . THR   B 1 38  ? -19.429 -16.056 -37.870 1.00 19.15 ?  38  THR   B OG1 1 
ATOM   2106 C CG2 . THR   B 1 38  ? -17.549 -15.084 -36.594 1.00 20.17 ?  38  THR   B CG2 1 
ATOM   2107 N N   . PRO   B 1 39  ? -22.096 -14.541 -36.971 1.00 22.55 ?  39  PRO   B N   1 
ATOM   2108 C CA  . PRO   B 1 39  ? -23.414 -14.967 -37.459 1.00 21.31 ?  39  PRO   B CA  1 
ATOM   2109 C C   . PRO   B 1 39  ? -23.423 -16.256 -38.273 1.00 20.64 ?  39  PRO   B C   1 
ATOM   2110 O O   . PRO   B 1 39  ? -24.506 -16.823 -38.480 1.00 19.99 ?  39  PRO   B O   1 
ATOM   2111 C CB  . PRO   B 1 39  ? -23.871 -13.777 -38.301 1.00 22.98 ?  39  PRO   B CB  1 
ATOM   2112 C CG  . PRO   B 1 39  ? -23.094 -12.605 -37.803 1.00 24.23 ?  39  PRO   B CG  1 
ATOM   2113 C CD  . PRO   B 1 39  ? -21.749 -13.175 -37.396 1.00 23.92 ?  39  PRO   B CD  1 
ATOM   2114 N N   . VAL   B 1 40  ? -22.275 -16.644 -38.885 1.00 20.11 ?  40  VAL   B N   1 
ATOM   2115 C CA  . VAL   B 1 40  ? -22.242 -17.868 -39.679 1.00 19.79 ?  40  VAL   B CA  1 
ATOM   2116 C C   . VAL   B 1 40  ? -21.535 -19.031 -38.993 1.00 19.82 ?  40  VAL   B C   1 
ATOM   2117 O O   . VAL   B 1 40  ? -21.301 -20.062 -39.627 1.00 19.28 ?  40  VAL   B O   1 
ATOM   2118 C CB  . VAL   B 1 40  ? -21.614 -17.618 -41.068 1.00 21.30 ?  40  VAL   B CB  1 
ATOM   2119 C CG1 . VAL   B 1 40  ? -22.399 -16.540 -41.794 1.00 22.09 ?  40  VAL   B CG1 1 
ATOM   2120 C CG2 . VAL   B 1 40  ? -20.137 -17.270 -40.978 1.00 22.26 ?  40  VAL   B CG2 1 
ATOM   2121 N N   . GLY   B 1 41  ? -21.094 -18.839 -37.742 1.00 19.41 ?  41  GLY   B N   1 
ATOM   2122 C CA  . GLY   B 1 41  ? -20.408 -19.879 -37.009 1.00 18.84 ?  41  GLY   B CA  1 
ATOM   2123 C C   . GLY   B 1 41  ? -19.216 -19.329 -36.213 1.00 17.80 ?  41  GLY   B C   1 
ATOM   2124 O O   . GLY   B 1 41  ? -18.935 -18.139 -36.213 1.00 17.53 ?  41  GLY   B O   1 
ATOM   2125 N N   . ASN   B 1 42  ? -18.601 -20.233 -35.464 1.00 18.20 ?  42  ASN   B N   1 
ATOM   2126 C CA  . ASN   B 1 42  ? -17.519 -19.901 -34.556 1.00 18.02 ?  42  ASN   B CA  1 
ATOM   2127 C C   . ASN   B 1 42  ? -16.196 -20.110 -35.275 1.00 18.06 ?  42  ASN   B C   1 
ATOM   2128 O O   . ASN   B 1 42  ? -16.045 -21.051 -36.044 1.00 16.72 ?  42  ASN   B O   1 
ATOM   2129 C CB  . ASN   B 1 42  ? -17.559 -20.743 -33.301 1.00 18.71 ?  42  ASN   B CB  1 
ATOM   2130 C CG  . ASN   B 1 42  ? -18.796 -20.514 -32.462 1.00 19.49 ?  42  ASN   B CG  1 
ATOM   2131 O OD1 . ASN   B 1 42  ? -19.424 -19.457 -32.547 1.00 18.18 ?  42  ASN   B OD1 1 
ATOM   2132 N ND2 . ASN   B 1 42  ? -19.101 -21.474 -31.600 1.00 22.71 ?  42  ASN   B ND2 1 
ATOM   2133 N N   . THR   B 1 43  ? -15.229 -19.244 -34.982 1.00 18.36 ?  43  THR   B N   1 
ATOM   2134 C CA  . THR   B 1 43  ? -13.852 -19.544 -35.384 1.00 16.87 ?  43  THR   B CA  1 
ATOM   2135 C C   . THR   B 1 43  ? -13.386 -20.796 -34.643 1.00 16.53 ?  43  THR   B C   1 
ATOM   2136 O O   . THR   B 1 43  ? -14.014 -21.196 -33.667 1.00 17.08 ?  43  THR   B O   1 
ATOM   2137 C CB  . THR   B 1 43  ? -12.951 -18.342 -35.126 1.00 15.82 ?  43  THR   B CB  1 
ATOM   2138 O OG1 . THR   B 1 43  ? -12.903 -17.919 -33.764 1.00 14.75 ?  43  THR   B OG1 1 
ATOM   2139 C CG2 . THR   B 1 43  ? -13.381 -17.143 -35.931 1.00 16.13 ?  43  THR   B CG2 1 
ATOM   2140 N N   . ALA   B 1 44  ? -12.247 -21.382 -35.045 1.00 15.65 ?  44  ALA   B N   1 
ATOM   2141 C CA  . ALA   B 1 44  ? -11.698 -22.538 -34.367 1.00 14.54 ?  44  ALA   B CA  1 
ATOM   2142 C C   . ALA   B 1 44  ? -11.233 -22.138 -32.959 1.00 15.12 ?  44  ALA   B C   1 
ATOM   2143 O O   . ALA   B 1 44  ? -11.337 -22.901 -31.981 1.00 15.93 ?  44  ALA   B O   1 
ATOM   2144 C CB  . ALA   B 1 44  ? -10.543 -23.058 -35.171 1.00 14.75 ?  44  ALA   B CB  1 
ATOM   2145 N N   . ALA   B 1 45  ? -10.645 -20.939 -32.898 1.00 14.57 ?  45  ALA   B N   1 
ATOM   2146 C CA  . ALA   B 1 45  ? -9.928  -20.497 -31.716 1.00 14.55 ?  45  ALA   B CA  1 
ATOM   2147 C C   . ALA   B 1 45  ? -9.933  -18.989 -31.650 1.00 14.08 ?  45  ALA   B C   1 
ATOM   2148 O O   . ALA   B 1 45  ? -10.204 -18.303 -32.649 1.00 14.09 ?  45  ALA   B O   1 
ATOM   2149 C CB  . ALA   B 1 45  ? -8.504  -21.029 -31.747 1.00 13.78 ?  45  ALA   B CB  1 
ATOM   2150 N N   . ILE   B 1 46  ? -9.582  -18.504 -30.455 1.00 14.01 ?  46  ILE   B N   1 
ATOM   2151 C CA  . ILE   B 1 46  ? -9.061  -17.165 -30.299 1.00 14.98 ?  46  ILE   B CA  1 
ATOM   2152 C C   . ILE   B 1 46  ? -7.600  -17.317 -29.875 1.00 15.01 ?  46  ILE   B C   1 
ATOM   2153 O O   . ILE   B 1 46  ? -7.253  -18.371 -29.337 1.00 15.76 ?  46  ILE   B O   1 
ATOM   2154 C CB  . ILE   B 1 46  ? -9.893  -16.336 -29.306 1.00 17.13 ?  46  ILE   B CB  1 
ATOM   2155 C CG1 . ILE   B 1 46  ? -10.039 -17.079 -27.999 1.00 19.12 ?  46  ILE   B CG1 1 
ATOM   2156 C CG2 . ILE   B 1 46  ? -11.272 -15.972 -29.883 1.00 18.00 ?  46  ILE   B CG2 1 
ATOM   2157 C CD1 . ILE   B 1 46  ? -10.104 -16.151 -26.821 1.00 24.14 ?  46  ILE   B CD1 1 
ATOM   2158 N N   . SER   B 1 47  ? -6.817  -16.263 -30.131 1.00 14.55 ?  47  SER   B N   1 
ATOM   2159 C CA  A SER   B 1 47  ? -5.389  -16.244 -29.836 0.50 14.41 ?  47  SER   B CA  1 
ATOM   2160 C CA  B SER   B 1 47  ? -5.388  -16.209 -29.871 0.50 14.85 ?  47  SER   B CA  1 
ATOM   2161 C C   . SER   B 1 47  ? -5.078  -14.962 -29.066 1.00 14.43 ?  47  SER   B C   1 
ATOM   2162 O O   . SER   B 1 47  ? -5.296  -13.862 -29.534 1.00 14.95 ?  47  SER   B O   1 
ATOM   2163 C CB  A SER   B 1 47  ? -4.524  -16.412 -31.095 0.50 14.22 ?  47  SER   B CB  1 
ATOM   2164 C CB  B SER   B 1 47  ? -4.607  -16.206 -31.148 0.50 15.25 ?  47  SER   B CB  1 
ATOM   2165 O OG  A SER   B 1 47  ? -3.160  -16.709 -30.798 0.50 14.14 ?  47  SER   B OG  1 
ATOM   2166 O OG  B SER   B 1 47  ? -4.475  -17.537 -31.593 0.50 15.97 ?  47  SER   B OG  1 
ATOM   2167 N N   . VAL   B 1 48  ? -4.579  -15.135 -27.830 1.00 14.80 ?  48  VAL   B N   1 
ATOM   2168 C CA  . VAL   B 1 48  ? -4.345  -14.024 -26.929 1.00 14.69 ?  48  VAL   B CA  1 
ATOM   2169 C C   . VAL   B 1 48  ? -3.010  -14.314 -26.248 1.00 14.96 ?  48  VAL   B C   1 
ATOM   2170 O O   . VAL   B 1 48  ? -2.553  -15.480 -26.254 1.00 15.37 ?  48  VAL   B O   1 
ATOM   2171 C CB  . VAL   B 1 48  ? -5.486  -13.864 -25.896 1.00 15.00 ?  48  VAL   B CB  1 
ATOM   2172 C CG1 . VAL   B 1 48  ? -6.836  -13.546 -26.553 1.00 15.24 ?  48  VAL   B CG1 1 
ATOM   2173 C CG2 . VAL   B 1 48  ? -5.621  -15.102 -25.031 1.00 15.46 ?  48  VAL   B CG2 1 
ATOM   2174 N N   . TYR   B 1 49  ? -2.418  -13.253 -25.683 1.00 14.65 ?  49  TYR   B N   1 
ATOM   2175 C CA  . TYR   B 1 49  ? -1.300  -13.409 -24.765 1.00 16.83 ?  49  TYR   B CA  1 
ATOM   2176 C C   . TYR   B 1 49  ? -1.684  -14.238 -23.530 1.00 15.02 ?  49  TYR   B C   1 
ATOM   2177 O O   . TYR   B 1 49  ? -2.833  -14.260 -23.121 1.00 15.28 ?  49  TYR   B O   1 
ATOM   2178 C CB  . TYR   B 1 49  ? -0.763  -12.043 -24.315 1.00 19.26 ?  49  TYR   B CB  1 
ATOM   2179 C CG  . TYR   B 1 49  ? -0.047  -11.345 -25.452 1.00 24.56 ?  49  TYR   B CG  1 
ATOM   2180 C CD1 . TYR   B 1 49  ? 0.775   -12.055 -26.302 1.00 26.63 ?  49  TYR   B CD1 1 
ATOM   2181 C CD2 . TYR   B 1 49  ? -0.235  -9.992  -25.698 1.00 32.13 ?  49  TYR   B CD2 1 
ATOM   2182 C CE1 . TYR   B 1 49  ? 1.435   -11.436 -27.353 1.00 28.62 ?  49  TYR   B CE1 1 
ATOM   2183 C CE2 . TYR   B 1 49  ? 0.395   -9.367  -26.759 1.00 35.55 ?  49  TYR   B CE2 1 
ATOM   2184 C CZ  . TYR   B 1 49  ? 1.237   -10.094 -27.583 1.00 34.77 ?  49  TYR   B CZ  1 
ATOM   2185 O OH  . TYR   B 1 49  ? 1.896   -9.507  -28.617 1.00 41.53 ?  49  TYR   B OH  1 
ATOM   2186 N N   . PRO   B 1 50  ? -0.720  -14.957 -22.914 1.00 14.03 ?  50  PRO   B N   1 
ATOM   2187 C CA  . PRO   B 1 50  ? -1.029  -15.895 -21.833 1.00 14.48 ?  50  PRO   B CA  1 
ATOM   2188 C C   . PRO   B 1 50  ? -1.854  -15.279 -20.707 1.00 14.55 ?  50  PRO   B C   1 
ATOM   2189 O O   . PRO   B 1 50  ? -2.821  -15.879 -20.249 1.00 14.31 ?  50  PRO   B O   1 
ATOM   2190 C CB  . PRO   B 1 50  ? 0.402   -16.280 -21.384 1.00 14.24 ?  50  PRO   B CB  1 
ATOM   2191 C CG  . PRO   B 1 50  ? 1.143   -16.325 -22.710 1.00 14.50 ?  50  PRO   B CG  1 
ATOM   2192 C CD  . PRO   B 1 50  ? 0.694   -15.009 -23.324 1.00 13.94 ?  50  PRO   B CD  1 
ATOM   2193 N N   . ARG   B 1 51  ? -1.510  -14.044 -20.347 1.00 14.47 ?  51  ARG   B N   1 
ATOM   2194 C CA  . ARG   B 1 51  ? -2.143  -13.379 -19.219 1.00 16.97 ?  51  ARG   B CA  1 
ATOM   2195 C C   . ARG   B 1 51  ? -3.634  -13.148 -19.465 1.00 16.01 ?  51  ARG   B C   1 
ATOM   2196 O O   . ARG   B 1 51  ? -4.406  -13.016 -18.501 1.00 15.69 ?  51  ARG   B O   1 
ATOM   2197 C CB  . ARG   B 1 51  ? -1.419  -12.075 -18.869 1.00 21.08 ?  51  ARG   B CB  1 
ATOM   2198 C CG  . ARG   B 1 51  ? -1.572  -10.947 -19.878 1.00 25.86 ?  51  ARG   B CG  1 
ATOM   2199 C CD  . ARG   B 1 51  ? -0.825  -9.718  -19.380 1.00 29.63 ?  51  ARG   B CD  1 
ATOM   2200 N NE  . ARG   B 1 51  ? -0.658  -8.762  -20.465 1.00 35.70 ?  51  ARG   B NE  1 
ATOM   2201 C CZ  . ARG   B 1 51  ? 0.273   -8.828  -21.428 1.00 42.40 ?  51  ARG   B CZ  1 
ATOM   2202 N NH1 . ARG   B 1 51  ? 1.205   -9.775  -21.428 1.00 41.72 ?  51  ARG   B NH1 1 
ATOM   2203 N NH2 . ARG   B 1 51  ? 0.271   -7.928  -22.391 1.00 48.55 ?  51  ARG   B NH2 1 
ATOM   2204 N N   . SER   B 1 52  ? -4.065  -13.172 -20.728 1.00 15.25 ?  52  SER   B N   1 
ATOM   2205 C CA  . SER   B 1 52  ? -5.461  -12.931 -21.069 1.00 15.34 ?  52  SER   B CA  1 
ATOM   2206 C C   . SER   B 1 52  ? -6.307  -14.203 -21.117 1.00 13.93 ?  52  SER   B C   1 
ATOM   2207 O O   . SER   B 1 52  ? -7.505  -14.131 -21.365 1.00 15.58 ?  52  SER   B O   1 
ATOM   2208 C CB  . SER   B 1 52  ? -5.509  -12.243 -22.434 1.00 17.10 ?  52  SER   B CB  1 
ATOM   2209 O OG  . SER   B 1 52  ? -4.873  -10.982 -22.383 1.00 17.89 ?  52  SER   B OG  1 
ATOM   2210 N N   . ILE   B 1 53  ? -5.713  -15.366 -20.914 1.00 13.16 ?  53  ILE   B N   1 
ATOM   2211 C CA  . ILE   B 1 53  ? -6.434  -16.605 -21.055 1.00 13.64 ?  53  ILE   B CA  1 
ATOM   2212 C C   . ILE   B 1 53  ? -7.590  -16.693 -20.064 1.00 15.00 ?  53  ILE   B C   1 
ATOM   2213 O O   . ILE   B 1 53  ? -8.691  -17.071 -20.444 1.00 15.02 ?  53  ILE   B O   1 
ATOM   2214 C CB  . ILE   B 1 53  ? -5.463  -17.789 -20.984 1.00 14.10 ?  53  ILE   B CB  1 
ATOM   2215 C CG1 . ILE   B 1 53  ? -4.469  -17.784 -22.183 1.00 15.29 ?  53  ILE   B CG1 1 
ATOM   2216 C CG2 . ILE   B 1 53  ? -6.221  -19.107 -20.906 1.00 14.77 ?  53  ILE   B CG2 1 
ATOM   2217 C CD1 . ILE   B 1 53  ? -3.357  -18.795 -22.044 1.00 14.98 ?  53  ILE   B CD1 1 
ATOM   2218 N N   . PRO   B 1 54  ? -7.408  -16.399 -18.760 1.00 15.95 ?  54  PRO   B N   1 
ATOM   2219 C CA  . PRO   B 1 54  ? -8.533  -16.599 -17.839 1.00 16.10 ?  54  PRO   B CA  1 
ATOM   2220 C C   . PRO   B 1 54  ? -9.760  -15.775 -18.205 1.00 16.59 ?  54  PRO   B C   1 
ATOM   2221 O O   . PRO   B 1 54  ? -10.865 -16.303 -18.215 1.00 17.32 ?  54  PRO   B O   1 
ATOM   2222 C CB  . PRO   B 1 54  ? -7.928  -16.207 -16.488 1.00 16.18 ?  54  PRO   B CB  1 
ATOM   2223 C CG  . PRO   B 1 54  ? -6.460  -16.545 -16.686 1.00 16.11 ?  54  PRO   B CG  1 
ATOM   2224 C CD  . PRO   B 1 54  ? -6.149  -16.039 -18.080 1.00 15.55 ?  54  PRO   B CD  1 
ATOM   2225 N N   . ILE   B 1 55  ? -9.580  -14.492 -18.504 1.00 16.66 ?  55  ILE   B N   1 
ATOM   2226 C CA  . ILE   B 1 55  ? -10.736 -13.681 -18.843 1.00 18.20 ?  55  ILE   B CA  1 
ATOM   2227 C C   . ILE   B 1 55  ? -11.342 -14.124 -20.188 1.00 18.42 ?  55  ILE   B C   1 
ATOM   2228 O O   . ILE   B 1 55  ? -12.567 -14.076 -20.380 1.00 17.95 ?  55  ILE   B O   1 
ATOM   2229 C CB  . ILE   B 1 55  ? -10.418 -12.177 -18.801 1.00 20.38 ?  55  ILE   B CB  1 
ATOM   2230 C CG1 . ILE   B 1 55  ? -11.733 -11.332 -18.776 1.00 24.02 ?  55  ILE   B CG1 1 
ATOM   2231 C CG2 . ILE   B 1 55  ? -9.550  -11.751 -19.958 1.00 19.82 ?  55  ILE   B CG2 1 
ATOM   2232 C CD1 . ILE   B 1 55  ? -12.746 -11.776 -17.735 1.00 27.11 ?  55  ILE   B CD1 1 
ATOM   2233 N N   . ALA   B 1 56  ? -10.523 -14.620 -21.117 1.00 16.44 ?  56  ALA   B N   1 
ATOM   2234 C CA  . ALA   B 1 56  ? -11.059 -15.146 -22.365 1.00 17.75 ?  56  ALA   B CA  1 
ATOM   2235 C C   . ALA   B 1 56  ? -11.927 -16.366 -22.084 1.00 16.68 ?  56  ALA   B C   1 
ATOM   2236 O O   . ALA   B 1 56  ? -13.029 -16.472 -22.622 1.00 16.93 ?  56  ALA   B O   1 
ATOM   2237 C CB  . ALA   B 1 56  ? -9.949  -15.505 -23.286 1.00 17.40 ?  56  ALA   B CB  1 
ATOM   2238 N N   . ARG   B 1 57  ? -11.447 -17.254 -21.191 1.00 18.00 ?  57  ARG   B N   1 
ATOM   2239 C CA  . ARG   B 1 57  ? -12.154 -18.497 -20.931 1.00 17.85 ?  57  ARG   B CA  1 
ATOM   2240 C C   . ARG   B 1 57  ? -13.500 -18.157 -20.302 1.00 17.40 ?  57  ARG   B C   1 
ATOM   2241 O O   . ARG   B 1 57  ? -14.523 -18.725 -20.687 1.00 17.49 ?  57  ARG   B O   1 
ATOM   2242 C CB  . ARG   B 1 57  ? -11.373 -19.443 -20.018 1.00 19.48 ?  57  ARG   B CB  1 
ATOM   2243 C CG  . ARG   B 1 57  ? -12.081 -20.757 -19.713 1.00 20.83 ?  57  ARG   B CG  1 
ATOM   2244 C CD  . ARG   B 1 57  ? -12.046 -21.744 -20.846 1.00 23.51 ?  57  ARG   B CD  1 
ATOM   2245 N NE  . ARG   B 1 57  ? -10.668 -22.232 -21.026 1.00 23.84 ?  57  ARG   B NE  1 
ATOM   2246 C CZ  . ARG   B 1 57  ? -10.229 -22.936 -22.074 1.00 24.48 ?  57  ARG   B CZ  1 
ATOM   2247 N NH1 . ARG   B 1 57  ? -11.017 -23.159 -23.127 1.00 25.92 ?  57  ARG   B NH1 1 
ATOM   2248 N NH2 . ARG   B 1 57  ? -8.996  -23.407 -22.068 1.00 21.32 ?  57  ARG   B NH2 1 
ATOM   2249 N N   . LYS   B 1 58  ? -13.482 -17.228 -19.345 1.00 18.01 ?  58  LYS   B N   1 
ATOM   2250 C CA  . LYS   B 1 58  ? -14.730 -16.781 -18.725 1.00 19.49 ?  58  LYS   B CA  1 
ATOM   2251 C C   . LYS   B 1 58  ? -15.705 -16.242 -19.774 1.00 19.32 ?  58  LYS   B C   1 
ATOM   2252 O O   . LYS   B 1 58  ? -16.905 -16.554 -19.721 1.00 18.27 ?  58  LYS   B O   1 
ATOM   2253 C CB  . LYS   B 1 58  ? -14.455 -15.694 -17.702 1.00 19.43 ?  58  LYS   B CB  1 
ATOM   2254 C CG  . LYS   B 1 58  ? -15.621 -15.329 -16.825 1.00 21.82 ?  58  LYS   B CG  1 
ATOM   2255 C CD  . LYS   B 1 58  ? -15.249 -14.224 -15.850 1.00 22.21 ?  58  LYS   B CD  1 
ATOM   2256 C CE  . LYS   B 1 58  ? -16.384 -14.068 -14.880 1.00 25.59 ?  58  LYS   B CE  1 
ATOM   2257 N NZ  . LYS   B 1 58  ? -15.903 -13.284 -13.743 1.00 26.01 ?  58  LYS   B NZ  1 
ATOM   2258 N N   . THR   B 1 59  ? -15.209 -15.427 -20.721 1.00 17.64 ?  59  THR   B N   1 
ATOM   2259 C CA  . THR   B 1 59  ? -16.082 -14.790 -21.689 1.00 18.80 ?  59  THR   B CA  1 
ATOM   2260 C C   . THR   B 1 59  ? -16.646 -15.838 -22.641 1.00 21.42 ?  59  THR   B C   1 
ATOM   2261 O O   . THR   B 1 59  ? -17.842 -15.806 -22.941 1.00 20.93 ?  59  THR   B O   1 
ATOM   2262 C CB  . THR   B 1 59  ? -15.338 -13.693 -22.438 1.00 19.70 ?  59  THR   B CB  1 
ATOM   2263 O OG1 . THR   B 1 59  ? -14.750 -12.867 -21.441 1.00 19.98 ?  59  THR   B OG1 1 
ATOM   2264 C CG2 . THR   B 1 59  ? -16.257 -12.847 -23.306 1.00 19.49 ?  59  THR   B CG2 1 
ATOM   2265 N N   . LEU   B 1 60  ? -15.801 -16.773 -23.123 1.00 19.46 ?  60  LEU   B N   1 
ATOM   2266 C CA  . LEU   B 1 60  ? -16.280 -17.810 -24.030 1.00 19.49 ?  60  LEU   B CA  1 
ATOM   2267 C C   . LEU   B 1 60  ? -17.375 -18.642 -23.363 1.00 19.64 ?  60  LEU   B C   1 
ATOM   2268 O O   . LEU   B 1 60  ? -18.340 -18.989 -24.040 1.00 21.40 ?  60  LEU   B O   1 
ATOM   2269 C CB  . LEU   B 1 60  ? -15.109 -18.662 -24.539 1.00 17.70 ?  60  LEU   B CB  1 
ATOM   2270 C CG  . LEU   B 1 60  ? -14.065 -17.909 -25.384 1.00 18.66 ?  60  LEU   B CG  1 
ATOM   2271 C CD1 . LEU   B 1 60  ? -12.858 -18.834 -25.653 1.00 17.43 ?  60  LEU   B CD1 1 
ATOM   2272 C CD2 . LEU   B 1 60  ? -14.659 -17.357 -26.680 1.00 19.24 ?  60  LEU   B CD2 1 
ATOM   2273 N N   . LYS   B 1 61  ? -17.216 -18.986 -22.071 1.00 20.09 ?  61  LYS   B N   1 
ATOM   2274 C CA  . LYS   B 1 61  ? -18.183 -19.815 -21.365 1.00 21.93 ?  61  LYS   B CA  1 
ATOM   2275 C C   . LYS   B 1 61  ? -19.488 -19.049 -21.205 1.00 23.32 ?  61  LYS   B C   1 
ATOM   2276 O O   . LYS   B 1 61  ? -20.564 -19.577 -21.514 1.00 22.26 ?  61  LYS   B O   1 
ATOM   2277 C CB  . LYS   B 1 61  ? -17.698 -20.252 -19.972 1.00 23.47 ?  61  LYS   B CB  1 
ATOM   2278 C CG  . LYS   B 1 61  ? -16.664 -21.359 -20.026 1.00 26.58 ?  61  LYS   B CG  1 
ATOM   2279 C CD  . LYS   B 1 61  ? -16.181 -21.740 -18.631 1.00 33.45 ?  61  LYS   B CD  1 
ATOM   2280 C CE  . LYS   B 1 61  ? -15.116 -22.777 -18.648 1.00 37.76 ?  61  LYS   B CE  1 
ATOM   2281 N NZ  . LYS   B 1 61  ? -14.220 -22.564 -17.499 1.00 40.81 ?  61  LYS   B NZ  1 
ATOM   2282 N N   . GLU   B 1 62  ? -19.356 -17.755 -20.894 1.00 21.87 ?  62  GLU   B N   1 
ATOM   2283 C CA  . GLU   B 1 62  ? -20.507 -16.915 -20.627 1.00 24.31 ?  62  GLU   B CA  1 
ATOM   2284 C C   . GLU   B 1 62  ? -21.358 -16.762 -21.879 1.00 22.86 ?  62  GLU   B C   1 
ATOM   2285 O O   . GLU   B 1 62  ? -22.571 -16.745 -21.772 1.00 24.55 ?  62  GLU   B O   1 
ATOM   2286 C CB  . GLU   B 1 62  ? -20.145 -15.532 -20.074 1.00 25.24 ?  62  GLU   B CB  1 
ATOM   2287 C CG  . GLU   B 1 62  ? -19.827 -15.640 -18.591 1.00 32.18 ?  62  GLU   B CG  1 
ATOM   2288 C CD  . GLU   B 1 62  ? -19.657 -14.375 -17.763 1.00 37.27 ?  62  GLU   B CD  1 
ATOM   2289 O OE1 . GLU   B 1 62  ? -19.686 -13.249 -18.278 1.00 40.07 ?  62  GLU   B OE1 1 
ATOM   2290 O OE2 . GLU   B 1 62  ? -19.511 -14.577 -16.537 1.00 44.02 ?  62  GLU   B OE2 1 
ATOM   2291 N N   . GLN   B 1 63  ? -20.742 -16.630 -23.056 1.00 22.17 ?  63  GLN   B N   1 
ATOM   2292 C CA  . GLN   B 1 63  ? -21.515 -16.436 -24.268 1.00 21.42 ?  63  GLN   B CA  1 
ATOM   2293 C C   . GLN   B 1 63  ? -21.947 -17.743 -24.917 1.00 21.99 ?  63  GLN   B C   1 
ATOM   2294 O O   . GLN   B 1 63  ? -22.493 -17.710 -26.013 1.00 24.71 ?  63  GLN   B O   1 
ATOM   2295 C CB  . GLN   B 1 63  ? -20.706 -15.657 -25.292 1.00 21.63 ?  63  GLN   B CB  1 
ATOM   2296 C CG  . GLN   B 1 63  ? -19.566 -16.438 -25.939 1.00 20.47 ?  63  GLN   B CG  1 
ATOM   2297 C CD  . GLN   B 1 63  ? -18.763 -15.524 -26.825 1.00 21.84 ?  63  GLN   B CD  1 
ATOM   2298 O OE1 . GLN   B 1 63  ? -18.903 -14.297 -26.792 1.00 24.58 ?  63  GLN   B OE1 1 
ATOM   2299 N NE2 . GLN   B 1 63  ? -17.912 -16.123 -27.642 1.00 20.47 ?  63  GLN   B NE2 1 
ATOM   2300 N N   . GLY   B 1 64  ? -21.675 -18.882 -24.286 1.00 21.63 ?  64  GLY   B N   1 
ATOM   2301 C CA  . GLY   B 1 64  ? -22.151 -20.154 -24.783 1.00 22.89 ?  64  GLY   B CA  1 
ATOM   2302 C C   . GLY   B 1 64  ? -21.309 -20.708 -25.926 1.00 24.19 ?  64  GLY   B C   1 
ATOM   2303 O O   . GLY   B 1 64  ? -21.808 -21.503 -26.699 1.00 27.77 ?  64  GLY   B O   1 
ATOM   2304 N N   . THR   B 1 65  ? -20.014 -20.375 -25.985 1.00 22.56 ?  65  THR   B N   1 
ATOM   2305 C CA  . THR   B 1 65  ? -19.173 -21.003 -26.991 1.00 21.66 ?  65  THR   B CA  1 
ATOM   2306 C C   . THR   B 1 65  ? -17.955 -21.630 -26.327 1.00 22.66 ?  65  THR   B C   1 
ATOM   2307 O O   . THR   B 1 65  ? -16.832 -21.257 -26.662 1.00 19.65 ?  65  THR   B O   1 
ATOM   2308 C CB  . THR   B 1 65  ? -18.755 -19.972 -28.037 1.00 22.50 ?  65  THR   B CB  1 
ATOM   2309 O OG1 . THR   B 1 65  ? -17.914 -19.014 -27.374 1.00 20.52 ?  65  THR   B OG1 1 
ATOM   2310 C CG2 . THR   B 1 65  ? -19.970 -19.357 -28.725 1.00 21.83 ?  65  THR   B CG2 1 
ATOM   2311 N N   . PRO   B 1 66  ? -18.137 -22.586 -25.392 1.00 23.88 ?  66  PRO   B N   1 
ATOM   2312 C CA  . PRO   B 1 66  ? -17.017 -23.162 -24.643 1.00 24.81 ?  66  PRO   B CA  1 
ATOM   2313 C C   . PRO   B 1 66  ? -16.072 -23.995 -25.500 1.00 25.82 ?  66  PRO   B C   1 
ATOM   2314 O O   . PRO   B 1 66  ? -14.980 -24.307 -25.049 1.00 27.28 ?  66  PRO   B O   1 
ATOM   2315 C CB  . PRO   B 1 66  ? -17.729 -24.019 -23.568 1.00 25.39 ?  66  PRO   B CB  1 
ATOM   2316 C CG  . PRO   B 1 66  ? -18.994 -24.423 -24.267 1.00 25.33 ?  66  PRO   B CG  1 
ATOM   2317 C CD  . PRO   B 1 66  ? -19.431 -23.170 -24.992 1.00 25.58 ?  66  PRO   B CD  1 
ATOM   2318 N N   . GLU   B 1 67  ? -16.508 -24.349 -26.719 1.00 24.02 ?  67  GLU   B N   1 
ATOM   2319 C CA  . GLU   B 1 67  ? -15.711 -25.157 -27.630 1.00 25.25 ?  67  GLU   B CA  1 
ATOM   2320 C C   . GLU   B 1 67  ? -14.798 -24.307 -28.505 1.00 22.04 ?  67  GLU   B C   1 
ATOM   2321 O O   . GLU   B 1 67  ? -14.012 -24.878 -29.252 1.00 23.43 ?  67  GLU   B O   1 
ATOM   2322 C CB  . GLU   B 1 67  ? -16.577 -26.093 -28.480 1.00 30.97 ?  67  GLU   B CB  1 
ATOM   2323 C CG  . GLU   B 1 67  ? -17.177 -27.219 -27.637 1.00 38.79 ?  67  GLU   B CG  1 
ATOM   2324 C CD  . GLU   B 1 67  ? -17.736 -28.400 -28.413 1.00 48.26 ?  67  GLU   B CD  1 
ATOM   2325 O OE1 . GLU   B 1 67  ? -18.081 -28.231 -29.606 1.00 54.93 ?  67  GLU   B OE1 1 
ATOM   2326 O OE2 . GLU   B 1 67  ? -17.773 -29.512 -27.830 1.00 55.62 ?  67  GLU   B OE2 1 
ATOM   2327 N N   . ILE   B 1 68  ? -14.873 -22.970 -28.436 1.00 18.47 ?  68  ILE   B N   1 
ATOM   2328 C CA  . ILE   B 1 68  ? -13.870 -22.169 -29.118 1.00 16.86 ?  68  ILE   B CA  1 
ATOM   2329 C C   . ILE   B 1 68  ? -12.557 -22.354 -28.352 1.00 15.65 ?  68  ILE   B C   1 
ATOM   2330 O O   . ILE   B 1 68  ? -12.559 -22.172 -27.159 1.00 15.90 ?  68  ILE   B O   1 
ATOM   2331 C CB  . ILE   B 1 68  ? -14.286 -20.697 -29.228 1.00 15.87 ?  68  ILE   B CB  1 
ATOM   2332 C CG1 . ILE   B 1 68  ? -15.541 -20.552 -30.123 1.00 16.95 ?  68  ILE   B CG1 1 
ATOM   2333 C CG2 . ILE   B 1 68  ? -13.121 -19.884 -29.779 1.00 15.99 ?  68  ILE   B CG2 1 
ATOM   2334 C CD1 . ILE   B 1 68  ? -15.983 -19.101 -30.346 1.00 17.19 ?  68  ILE   B CD1 1 
ATOM   2335 N N   . ARG   B 1 69  ? -11.487 -22.788 -29.029 1.00 15.05 ?  69  ARG   B N   1 
ATOM   2336 C CA  . ARG   B 1 69  ? -10.228 -23.108 -28.352 1.00 16.31 ?  69  ARG   B CA  1 
ATOM   2337 C C   . ARG   B 1 69  ? -9.516  -21.818 -27.986 1.00 16.01 ?  69  ARG   B C   1 
ATOM   2338 O O   . ARG   B 1 69  ? -9.744  -20.781 -28.615 1.00 15.48 ?  69  ARG   B O   1 
ATOM   2339 C CB  . ARG   B 1 69  ? -9.323  -23.999 -29.191 1.00 19.85 ?  69  ARG   B CB  1 
ATOM   2340 C CG  . ARG   B 1 69  ? -9.928  -25.319 -29.641 1.00 24.82 ?  69  ARG   B CG  1 
ATOM   2341 C CD  . ARG   B 1 69  ? -9.405  -25.589 -31.057 1.00 30.59 ?  69  ARG   B CD  1 
ATOM   2342 N NE  . ARG   B 1 69  ? -9.950  -26.760 -31.752 1.00 37.67 ?  69  ARG   B NE  1 
ATOM   2343 C CZ  . ARG   B 1 69  ? -11.117 -26.794 -32.394 1.00 38.74 ?  69  ARG   B CZ  1 
ATOM   2344 N NH1 . ARG   B 1 69  ? -11.789 -25.677 -32.619 1.00 37.83 ?  69  ARG   B NH1 1 
ATOM   2345 N NH2 . ARG   B 1 69  ? -11.607 -27.951 -32.805 1.00 38.75 ?  69  ARG   B NH2 1 
ATOM   2346 N N   . ILE   B 1 70  ? -8.685  -21.869 -26.925 1.00 13.53 ?  70  ILE   B N   1 
ATOM   2347 C CA  . ILE   B 1 70  ? -7.856  -20.726 -26.591 1.00 14.26 ?  70  ILE   B CA  1 
ATOM   2348 C C   . ILE   B 1 70  ? -6.403  -21.079 -26.918 1.00 13.97 ?  70  ILE   B C   1 
ATOM   2349 O O   . ILE   B 1 70  ? -5.798  -21.921 -26.268 1.00 14.57 ?  70  ILE   B O   1 
ATOM   2350 C CB  . ILE   B 1 70  ? -8.031  -20.292 -25.123 1.00 15.25 ?  70  ILE   B CB  1 
ATOM   2351 C CG1 . ILE   B 1 70  ? -9.488  -19.932 -24.816 1.00 15.51 ?  70  ILE   B CG1 1 
ATOM   2352 C CG2 . ILE   B 1 70  ? -7.088  -19.145 -24.829 1.00 15.48 ?  70  ILE   B CG2 1 
ATOM   2353 C CD1 . ILE   B 1 70  ? -9.775  -19.619 -23.344 1.00 15.85 ?  70  ILE   B CD1 1 
ATOM   2354 N N   . ALA   B 1 71  ? -5.855  -20.408 -27.930 1.00 13.06 ?  71  ALA   B N   1 
ATOM   2355 C CA  . ALA   B 1 71  ? -4.439  -20.529 -28.234 1.00 13.08 ?  71  ALA   B CA  1 
ATOM   2356 C C   . ALA   B 1 71  ? -3.689  -19.330 -27.686 1.00 13.30 ?  71  ALA   B C   1 
ATOM   2357 O O   . ALA   B 1 71  ? -4.244  -18.216 -27.575 1.00 13.03 ?  71  ALA   B O   1 
ATOM   2358 C CB  . ALA   B 1 71  ? -4.211  -20.642 -29.714 1.00 13.74 ?  71  ALA   B CB  1 
ATOM   2359 N N   . THR   B 1 72  ? -2.379  -19.531 -27.433 1.00 12.18 ?  72  THR   B N   1 
ATOM   2360 C CA  . THR   B 1 72  ? -1.549  -18.424 -26.990 1.00 11.98 ?  72  THR   B CA  1 
ATOM   2361 C C   . THR   B 1 72  ? -0.192  -18.554 -27.656 1.00 12.88 ?  72  THR   B C   1 
ATOM   2362 O O   . THR   B 1 72  ? -0.057  -19.407 -28.509 1.00 14.05 ?  72  THR   B O   1 
ATOM   2363 C CB  . THR   B 1 72  ? -1.485  -18.401 -25.445 1.00 11.95 ?  72  THR   B CB  1 
ATOM   2364 O OG1 . THR   B 1 72  ? -0.896  -17.149 -25.062 1.00 11.40 ?  72  THR   B OG1 1 
ATOM   2365 C CG2 . THR   B 1 72  ? -0.793  -19.628 -24.889 1.00 12.10 ?  72  THR   B CG2 1 
ATOM   2366 N N   . VAL   B 1 73  ? 0.765   -17.705 -27.277 1.00 13.29 ?  73  VAL   B N   1 
ATOM   2367 C CA  . VAL   B 1 73  ? 2.085   -17.692 -27.880 1.00 13.05 ?  73  VAL   B CA  1 
ATOM   2368 C C   . VAL   B 1 73  ? 3.121   -17.665 -26.767 1.00 12.55 ?  73  VAL   B C   1 
ATOM   2369 O O   . VAL   B 1 73  ? 2.903   -16.995 -25.738 1.00 12.51 ?  73  VAL   B O   1 
ATOM   2370 C CB  . VAL   B 1 73  ? 2.275   -16.474 -28.774 1.00 14.94 ?  73  VAL   B CB  1 
ATOM   2371 C CG1 . VAL   B 1 73  ? 1.516   -16.689 -30.092 1.00 15.51 ?  73  VAL   B CG1 1 
ATOM   2372 C CG2 . VAL   B 1 73  ? 1.960   -15.154 -28.078 1.00 15.85 ?  73  VAL   B CG2 1 
ATOM   2373 N N   . THR   B 1 74  ? 4.219   -18.394 -27.035 1.00 11.36 ?  74  THR   B N   1 
ATOM   2374 C CA  . THR   B 1 74  ? 5.390   -18.390 -26.168 1.00 11.19 ?  74  THR   B CA  1 
ATOM   2375 C C   . THR   B 1 74  ? 6.671   -18.275 -27.001 1.00 11.84 ?  74  THR   B C   1 
ATOM   2376 O O   . THR   B 1 74  ? 6.674   -18.491 -28.201 1.00 12.21 ?  74  THR   B O   1 
ATOM   2377 C CB  . THR   B 1 74  ? 5.427   -19.609 -25.265 1.00 11.58 ?  74  THR   B CB  1 
ATOM   2378 O OG1 . THR   B 1 74  ? 5.551   -20.783 -26.036 1.00 11.70 ?  74  THR   B OG1 1 
ATOM   2379 C CG2 . THR   B 1 74  ? 4.191   -19.712 -24.392 1.00 11.98 ?  74  THR   B CG2 1 
ATOM   2380 N N   . ASN   B 1 75  ? 7.772   -17.926 -26.310 1.00 13.16 ?  75  ASN   B N   1 
ATOM   2381 C CA  . ASN   B 1 75  ? 9.057   -17.676 -26.941 1.00 13.39 ?  75  ASN   B CA  1 
ATOM   2382 C C   . ASN   B 1 75  ? 8.858   -16.627 -28.017 1.00 13.94 ?  75  ASN   B C   1 
ATOM   2383 O O   . ASN   B 1 75  ? 9.543   -16.654 -29.048 1.00 13.69 ?  75  ASN   B O   1 
ATOM   2384 C CB  . ASN   B 1 75  ? 9.709   -18.968 -27.415 1.00 13.22 ?  75  ASN   B CB  1 
ATOM   2385 C CG  . ASN   B 1 75  ? 11.215  -18.825 -27.533 1.00 14.41 ?  75  ASN   B CG  1 
ATOM   2386 O OD1 . ASN   B 1 75  ? 11.809  -18.210 -26.631 1.00 14.13 ?  75  ASN   B OD1 1 
ATOM   2387 N ND2 . ASN   B 1 75  ? 11.841  -19.415 -28.560 1.00 13.69 ?  75  ASN   B ND2 1 
ATOM   2388 N N   . PHE   B 1 76  ? 7.933   -15.684 -27.770 1.00 15.28 ?  76  PHE   B N   1 
ATOM   2389 C CA  . PHE   B 1 76  ? 7.340   -14.898 -28.833 1.00 16.02 ?  76  PHE   B CA  1 
ATOM   2390 C C   . PHE   B 1 76  ? 7.585   -13.396 -28.665 1.00 17.59 ?  76  PHE   B C   1 
ATOM   2391 O O   . PHE   B 1 76  ? 7.516   -12.911 -27.546 1.00 16.91 ?  76  PHE   B O   1 
ATOM   2392 C CB  . PHE   B 1 76  ? 5.832   -15.167 -28.760 1.00 15.57 ?  76  PHE   B CB  1 
ATOM   2393 C CG  . PHE   B 1 76  ? 5.015   -14.463 -29.833 1.00 14.68 ?  76  PHE   B CG  1 
ATOM   2394 C CD1 . PHE   B 1 76  ? 4.585   -13.148 -29.660 1.00 15.10 ?  76  PHE   B CD1 1 
ATOM   2395 C CD2 . PHE   B 1 76  ? 4.681   -15.138 -31.003 1.00 14.77 ?  76  PHE   B CD2 1 
ATOM   2396 C CE1 . PHE   B 1 76  ? 3.851   -12.530 -30.664 1.00 16.13 ?  76  PHE   B CE1 1 
ATOM   2397 C CE2 . PHE   B 1 76  ? 3.928   -14.522 -32.001 1.00 15.31 ?  76  PHE   B CE2 1 
ATOM   2398 C CZ  . PHE   B 1 76  ? 3.519   -13.224 -31.816 1.00 16.68 ?  76  PHE   B CZ  1 
ATOM   2399 N N   . PRO   B 1 77  ? 7.787   -12.592 -29.754 1.00 17.39 ?  77  PRO   B N   1 
ATOM   2400 C CA  . PRO   B 1 77  ? 7.922   -13.114 -31.121 1.00 17.10 ?  77  PRO   B CA  1 
ATOM   2401 C C   . PRO   B 1 77  ? 9.336   -13.486 -31.536 1.00 16.66 ?  77  PRO   B C   1 
ATOM   2402 O O   . PRO   B 1 77  ? 9.564   -13.933 -32.667 1.00 16.78 ?  77  PRO   B O   1 
ATOM   2403 C CB  . PRO   B 1 77  ? 7.413   -11.903 -31.919 1.00 19.03 ?  77  PRO   B CB  1 
ATOM   2404 C CG  . PRO   B 1 77  ? 7.992   -10.718 -31.195 1.00 18.62 ?  77  PRO   B CG  1 
ATOM   2405 C CD  . PRO   B 1 77  ? 7.756   -11.115 -29.738 1.00 17.73 ?  77  PRO   B CD  1 
ATOM   2406 N N   . HIS   B 1 78  ? 10.285  -13.374 -30.594 1.00 15.97 ?  78  HIS   B N   1 
ATOM   2407 C CA  . HIS   B 1 78  ? 11.710  -13.376 -30.891 1.00 15.91 ?  78  HIS   B CA  1 
ATOM   2408 C C   . HIS   B 1 78  ? 12.265  -14.718 -31.330 1.00 14.38 ?  78  HIS   B C   1 
ATOM   2409 O O   . HIS   B 1 78  ? 13.218  -14.738 -32.104 1.00 14.38 ?  78  HIS   B O   1 
ATOM   2410 C CB  . HIS   B 1 78  ? 12.510  -12.937 -29.676 1.00 16.79 ?  78  HIS   B CB  1 
ATOM   2411 C CG  . HIS   B 1 78  ? 12.010  -13.556 -28.435 1.00 16.90 ?  78  HIS   B CG  1 
ATOM   2412 N ND1 . HIS   B 1 78  ? 12.300  -14.856 -28.092 1.00 16.94 ?  78  HIS   B ND1 1 
ATOM   2413 C CD2 . HIS   B 1 78  ? 11.274  -13.022 -27.414 1.00 18.18 ?  78  HIS   B CD2 1 
ATOM   2414 C CE1 . HIS   B 1 78  ? 11.767  -15.098 -26.886 1.00 17.90 ?  78  HIS   B CE1 1 
ATOM   2415 N NE2 . HIS   B 1 78  ? 11.151  -13.997 -26.473 1.00 17.98 ?  78  HIS   B NE2 1 
ATOM   2416 N N   . GLY   B 1 79  ? 11.711  -15.832 -30.888 1.00 14.79 ?  79  GLY   B N   1 
ATOM   2417 C CA  . GLY   B 1 79  ? 12.298  -17.142 -31.178 1.00 14.81 ?  79  GLY   B CA  1 
ATOM   2418 C C   . GLY   B 1 79  ? 13.735  -17.291 -30.664 1.00 15.72 ?  79  GLY   B C   1 
ATOM   2419 O O   . GLY   B 1 79  ? 14.642  -17.873 -31.317 1.00 15.91 ?  79  GLY   B O   1 
ATOM   2420 N N   . ASN   B 1 80  ? 13.957  -16.752 -29.479 1.00 15.36 ?  80  ASN   B N   1 
ATOM   2421 C CA  . ASN   B 1 80  ? 15.270  -16.896 -28.871 1.00 16.04 ?  80  ASN   B CA  1 
ATOM   2422 C C   . ASN   B 1 80  ? 15.574  -18.373 -28.639 1.00 16.10 ?  80  ASN   B C   1 
ATOM   2423 O O   . ASN   B 1 80  ? 14.683  -19.205 -28.653 1.00 16.48 ?  80  ASN   B O   1 
ATOM   2424 C CB  . ASN   B 1 80  ? 15.346  -16.149 -27.534 1.00 17.30 ?  80  ASN   B CB  1 
ATOM   2425 C CG  . ASN   B 1 80  ? 15.417  -14.660 -27.712 1.00 18.72 ?  80  ASN   B CG  1 
ATOM   2426 O OD1 . ASN   B 1 80  ? 15.663  -14.149 -28.816 1.00 19.83 ?  80  ASN   B OD1 1 
ATOM   2427 N ND2 . ASN   B 1 80  ? 15.161  -13.944 -26.623 1.00 20.18 ?  80  ASN   B ND2 1 
ATOM   2428 N N   . ASP   B 1 81  ? 16.828  -18.706 -28.296 1.00 15.61 ?  81  ASP   B N   1 
ATOM   2429 C CA  . ASP   B 1 81  ? 17.243  -20.091 -28.162 1.00 16.15 ?  81  ASP   B CA  1 
ATOM   2430 C C   . ASP   B 1 81  ? 17.548  -20.470 -26.709 1.00 16.50 ?  81  ASP   B C   1 
ATOM   2431 O O   . ASP   B 1 81  ? 18.259  -21.459 -26.465 1.00 17.42 ?  81  ASP   B O   1 
ATOM   2432 C CB  . ASP   B 1 81  ? 18.478  -20.370 -29.010 1.00 19.00 ?  81  ASP   B CB  1 
ATOM   2433 C CG  . ASP   B 1 81  ? 19.691  -19.522 -28.661 1.00 20.75 ?  81  ASP   B CG  1 
ATOM   2434 O OD1 . ASP   B 1 81  ? 19.652  -18.743 -27.708 1.00 22.65 ?  81  ASP   B OD1 1 
ATOM   2435 O OD2 . ASP   B 1 81  ? 20.695  -19.638 -29.348 1.00 24.80 ?  81  ASP   B OD2 1 
ATOM   2436 N N   . ASP   B 1 82  ? 16.904  -19.779 -25.768 1.00 16.22 ?  82  ASP   B N   1 
ATOM   2437 C CA  . ASP   B 1 82  ? 16.952  -20.174 -24.373 1.00 16.79 ?  82  ASP   B CA  1 
ATOM   2438 C C   . ASP   B 1 82  ? 15.790  -21.122 -24.072 1.00 15.67 ?  82  ASP   B C   1 
ATOM   2439 O O   . ASP   B 1 82  ? 14.649  -20.693 -23.977 1.00 15.76 ?  82  ASP   B O   1 
ATOM   2440 C CB  . ASP   B 1 82  ? 16.996  -18.951 -23.491 1.00 17.46 ?  82  ASP   B CB  1 
ATOM   2441 C CG  . ASP   B 1 82  ? 17.171  -19.294 -22.020 1.00 18.88 ?  82  ASP   B CG  1 
ATOM   2442 O OD1 . ASP   B 1 82  ? 16.572  -20.334 -21.589 1.00 19.07 ?  82  ASP   B OD1 1 
ATOM   2443 O OD2 . ASP   B 1 82  ? 17.815  -18.488 -21.326 1.00 20.68 ?  82  ASP   B OD2 1 
ATOM   2444 N N   . ILE   B 1 83  ? 16.103  -22.413 -23.940 1.00 15.56 ?  83  ILE   B N   1 
ATOM   2445 C CA  . ILE   B 1 83  ? 15.101  -23.455 -23.790 1.00 15.72 ?  83  ILE   B CA  1 
ATOM   2446 C C   . ILE   B 1 83  ? 14.388  -23.294 -22.456 1.00 16.55 ?  83  ILE   B C   1 
ATOM   2447 O O   . ILE   B 1 83  ? 13.189  -23.543 -22.366 1.00 17.52 ?  83  ILE   B O   1 
ATOM   2448 C CB  . ILE   B 1 83  ? 15.681  -24.873 -23.902 1.00 16.85 ?  83  ILE   B CB  1 
ATOM   2449 C CG1 . ILE   B 1 83  ? 16.217  -25.201 -25.285 1.00 19.85 ?  83  ILE   B CG1 1 
ATOM   2450 C CG2 . ILE   B 1 83  ? 14.636  -25.898 -23.493 1.00 17.91 ?  83  ILE   B CG2 1 
ATOM   2451 C CD1 . ILE   B 1 83  ? 17.157  -26.412 -25.282 1.00 20.61 ?  83  ILE   B CD1 1 
ATOM   2452 N N   . GLU   B 1 84  ? 15.151  -22.943 -21.410 1.00 17.51 ?  84  GLU   B N   1 
ATOM   2453 C CA  . GLU   B 1 84  ? 14.536  -22.845 -20.104 1.00 19.09 ?  84  GLU   B CA  1 
ATOM   2454 C C   . GLU   B 1 84  ? 13.482  -21.742 -20.112 1.00 17.31 ?  84  GLU   B C   1 
ATOM   2455 O O   . GLU   B 1 84  ? 12.447  -21.921 -19.460 1.00 18.15 ?  84  GLU   B O   1 
ATOM   2456 C CB  . GLU   B 1 84  ? 15.590  -22.670 -19.002 1.00 21.50 ?  84  GLU   B CB  1 
ATOM   2457 C CG  . GLU   B 1 84  ? 16.367  -23.961 -18.781 1.00 27.60 ?  84  GLU   B CG  1 
ATOM   2458 C CD  . GLU   B 1 84  ? 15.488  -25.173 -18.473 1.00 39.00 ?  84  GLU   B CD  1 
ATOM   2459 O OE1 . GLU   B 1 84  ? 14.543  -25.052 -17.652 1.00 41.05 ?  84  GLU   B OE1 1 
ATOM   2460 O OE2 . GLU   B 1 84  ? 15.729  -26.262 -19.057 1.00 51.65 ?  84  GLU   B OE2 1 
ATOM   2461 N N   . ILE   B 1 85  ? 13.773  -20.597 -20.732 1.00 16.34 ?  85  ILE   B N   1 
ATOM   2462 C CA  . ILE   B 1 85  ? 12.785  -19.535 -20.834 1.00 16.55 ?  85  ILE   B CA  1 
ATOM   2463 C C   . ILE   B 1 85  ? 11.555  -19.975 -21.619 1.00 15.52 ?  85  ILE   B C   1 
ATOM   2464 O O   . ILE   B 1 85  ? 10.423  -19.723 -21.188 1.00 15.31 ?  85  ILE   B O   1 
ATOM   2465 C CB  . ILE   B 1 85  ? 13.384  -18.240 -21.372 1.00 16.95 ?  85  ILE   B CB  1 
ATOM   2466 C CG1 . ILE   B 1 85  ? 14.388  -17.669 -20.358 1.00 18.71 ?  85  ILE   B CG1 1 
ATOM   2467 C CG2 . ILE   B 1 85  ? 12.293  -17.240 -21.765 1.00 18.37 ?  85  ILE   B CG2 1 
ATOM   2468 C CD1 . ILE   B 1 85  ? 14.943  -16.304 -20.731 1.00 20.35 ?  85  ILE   B CD1 1 
ATOM   2469 N N   . ALA   B 1 86  ? 11.770  -20.573 -22.800 1.00 15.05 ?  86  ALA   B N   1 
ATOM   2470 C CA  . ALA   B 1 86  ? 10.662  -20.972 -23.634 1.00 14.90 ?  86  ALA   B CA  1 
ATOM   2471 C C   . ALA   B 1 86  ? 9.784   -21.971 -22.898 1.00 15.65 ?  86  ALA   B C   1 
ATOM   2472 O O   . ALA   B 1 86  ? 8.551   -21.876 -22.943 1.00 14.09 ?  86  ALA   B O   1 
ATOM   2473 C CB  . ALA   B 1 86  ? 11.160  -21.549 -24.941 1.00 14.55 ?  86  ALA   B CB  1 
ATOM   2474 N N   . LEU   B 1 87  ? 10.419  -22.921 -22.211 1.00 18.06 ?  87  LEU   B N   1 
ATOM   2475 C CA  . LEU   B 1 87  ? 9.702   -23.913 -21.429 1.00 17.68 ?  87  LEU   B CA  1 
ATOM   2476 C C   . LEU   B 1 87  ? 8.883   -23.267 -20.297 1.00 15.68 ?  87  LEU   B C   1 
ATOM   2477 O O   . LEU   B 1 87  ? 7.743   -23.659 -20.059 1.00 14.95 ?  87  LEU   B O   1 
ATOM   2478 C CB  . LEU   B 1 87  ? 10.731  -24.903 -20.864 1.00 18.69 ?  87  LEU   B CB  1 
ATOM   2479 C CG  . LEU   B 1 87  ? 10.150  -26.070 -20.053 1.00 19.03 ?  87  LEU   B CG  1 
ATOM   2480 C CD1 . LEU   B 1 87  ? 9.022   -26.814 -20.765 1.00 18.37 ?  87  LEU   B CD1 1 
ATOM   2481 C CD2 . LEU   B 1 87  ? 11.241  -27.035 -19.627 1.00 19.89 ?  87  LEU   B CD2 1 
ATOM   2482 N N   . ALA   B 1 88  ? 9.506   -22.351 -19.526 1.00 15.50 ?  88  ALA   B N   1 
ATOM   2483 C CA  . ALA   B 1 88  ? 8.846   -21.672 -18.424 1.00 16.46 ?  88  ALA   B CA  1 
ATOM   2484 C C   . ALA   B 1 88  ? 7.582   -20.981 -18.922 1.00 14.94 ?  88  ALA   B C   1 
ATOM   2485 O O   . ALA   B 1 88  ? 6.531   -21.072 -18.306 1.00 14.40 ?  88  ALA   B O   1 
ATOM   2486 C CB  . ALA   B 1 88  ? 9.784   -20.671 -17.754 1.00 16.09 ?  88  ALA   B CB  1 
ATOM   2487 N N   . GLU   B 1 89  ? 7.699   -20.274 -20.043 1.00 14.03 ?  89  GLU   B N   1 
ATOM   2488 C CA  . GLU   B 1 89  ? 6.580   -19.541 -20.621 1.00 14.90 ?  89  GLU   B CA  1 
ATOM   2489 C C   . GLU   B 1 89  ? 5.496   -20.523 -21.052 1.00 15.41 ?  89  GLU   B C   1 
ATOM   2490 O O   . GLU   B 1 89  ? 4.305   -20.259 -20.836 1.00 14.91 ?  89  GLU   B O   1 
ATOM   2491 C CB  . GLU   B 1 89  ? 7.052   -18.730 -21.831 1.00 15.26 ?  89  GLU   B CB  1 
ATOM   2492 C CG  . GLU   B 1 89  ? 7.959   -17.561 -21.486 1.00 17.01 ?  89  GLU   B CG  1 
ATOM   2493 C CD  . GLU   B 1 89  ? 8.356   -16.617 -22.599 1.00 16.45 ?  89  GLU   B CD  1 
ATOM   2494 O OE1 . GLU   B 1 89  ? 8.083   -16.962 -23.774 1.00 18.27 ?  89  GLU   B OE1 1 
ATOM   2495 O OE2 . GLU   B 1 89  ? 8.854   -15.518 -22.298 1.00 15.97 ?  89  GLU   B OE2 1 
ATOM   2496 N N   . THR   B 1 90  ? 5.917   -21.652 -21.644 1.00 14.64 ?  90  THR   B N   1 
ATOM   2497 C CA  . THR   B 1 90  ? 4.994   -22.686 -22.132 1.00 14.66 ?  90  THR   B CA  1 
ATOM   2498 C C   . THR   B 1 90  ? 4.259   -23.272 -20.924 1.00 13.07 ?  90  THR   B C   1 
ATOM   2499 O O   . THR   B 1 90  ? 3.049   -23.472 -20.932 1.00 13.95 ?  90  THR   B O   1 
ATOM   2500 C CB  . THR   B 1 90  ? 5.723   -23.762 -22.953 1.00 14.92 ?  90  THR   B CB  1 
ATOM   2501 O OG1 . THR   B 1 90  ? 6.286   -23.139 -24.107 1.00 15.12 ?  90  THR   B OG1 1 
ATOM   2502 C CG2 . THR   B 1 90  ? 4.820   -24.909 -23.392 1.00 15.21 ?  90  THR   B CG2 1 
ATOM   2503 N N   . ARG   B 1 91  ? 4.977   -23.611 -19.861 1.00 13.40 ?  91  ARG   B N   1 
ATOM   2504 C CA  . ARG   B 1 91  ? 4.318   -24.121 -18.656 1.00 14.35 ?  91  ARG   B CA  1 
ATOM   2505 C C   . ARG   B 1 91  ? 3.374   -23.089 -18.067 1.00 14.04 ?  91  ARG   B C   1 
ATOM   2506 O O   . ARG   B 1 91  ? 2.307   -23.424 -17.592 1.00 13.66 ?  91  ARG   B O   1 
ATOM   2507 C CB  . ARG   B 1 91  ? 5.344   -24.518 -17.587 1.00 15.16 ?  91  ARG   B CB  1 
ATOM   2508 C CG  . ARG   B 1 91  ? 6.168   -25.725 -17.985 1.00 16.41 ?  91  ARG   B CG  1 
ATOM   2509 C CD  . ARG   B 1 91  ? 7.244   -25.986 -16.953 1.00 19.57 ?  91  ARG   B CD  1 
ATOM   2510 N NE  . ARG   B 1 91  ? 7.870   -27.263 -17.201 1.00 22.75 ?  91  ARG   B NE  1 
ATOM   2511 C CZ  . ARG   B 1 91  ? 9.090   -27.583 -16.777 1.00 31.35 ?  91  ARG   B CZ  1 
ATOM   2512 N NH1 . ARG   B 1 91  ? 9.880   -26.655 -16.259 1.00 33.97 ?  91  ARG   B NH1 1 
ATOM   2513 N NH2 . ARG   B 1 91  ? 9.525   -28.823 -16.894 1.00 35.72 ?  91  ARG   B NH2 1 
ATOM   2514 N N   . ALA   B 1 92  ? 3.742   -21.819 -18.075 1.00 14.55 ?  92  ALA   B N   1 
ATOM   2515 C CA  . ALA   B 1 92  ? 2.803   -20.811 -17.598 1.00 14.41 ?  92  ALA   B CA  1 
ATOM   2516 C C   . ALA   B 1 92  ? 1.559   -20.725 -18.478 1.00 13.61 ?  92  ALA   B C   1 
ATOM   2517 O O   . ALA   B 1 92  ? 0.446   -20.612 -17.957 1.00 13.61 ?  92  ALA   B O   1 
ATOM   2518 C CB  . ALA   B 1 92  ? 3.463   -19.445 -17.512 1.00 15.81 ?  92  ALA   B CB  1 
ATOM   2519 N N   . ALA   B 1 93  ? 1.736   -20.723 -19.813 1.00 13.40 ?  93  ALA   B N   1 
ATOM   2520 C CA  . ALA   B 1 93  ? 0.594   -20.759 -20.727 1.00 12.98 ?  93  ALA   B CA  1 
ATOM   2521 C C   . ALA   B 1 93  ? -0.361  -21.891 -20.357 1.00 13.51 ?  93  ALA   B C   1 
ATOM   2522 O O   . ALA   B 1 93  ? -1.588  -21.729 -20.314 1.00 14.79 ?  93  ALA   B O   1 
ATOM   2523 C CB  . ALA   B 1 93  ? 1.102   -20.929 -22.156 1.00 13.17 ?  93  ALA   B CB  1 
ATOM   2524 N N   . ILE   B 1 94  ? 0.193   -23.082 -20.150 1.00 13.12 ?  94  ILE   B N   1 
ATOM   2525 C CA  . ILE   B 1 94  ? -0.593  -24.253 -19.788 1.00 13.94 ?  94  ILE   B CA  1 
ATOM   2526 C C   . ILE   B 1 94  ? -1.337  -23.986 -18.481 1.00 15.59 ?  94  ILE   B C   1 
ATOM   2527 O O   . ILE   B 1 94  ? -2.529  -24.232 -18.372 1.00 16.14 ?  94  ILE   B O   1 
ATOM   2528 C CB  . ILE   B 1 94  ? 0.294   -25.494 -19.678 1.00 14.29 ?  94  ILE   B CB  1 
ATOM   2529 C CG1 . ILE   B 1 94  ? 0.864   -25.915 -21.040 1.00 14.07 ?  94  ILE   B CG1 1 
ATOM   2530 C CG2 . ILE   B 1 94  ? -0.461  -26.656 -19.023 1.00 16.03 ?  94  ILE   B CG2 1 
ATOM   2531 C CD1 . ILE   B 1 94  ? 2.056   -26.841 -20.963 1.00 14.86 ?  94  ILE   B CD1 1 
ATOM   2532 N N   . ALA   B 1 95  ? -0.624  -23.421 -17.498 1.00 14.63 ?  95  ALA   B N   1 
ATOM   2533 C CA  . ALA   B 1 95  ? -1.202  -23.208 -16.199 1.00 15.23 ?  95  ALA   B CA  1 
ATOM   2534 C C   . ALA   B 1 95  ? -2.285  -22.142 -16.221 1.00 14.87 ?  95  ALA   B C   1 
ATOM   2535 O O   . ALA   B 1 95  ? -3.230  -22.179 -15.440 1.00 15.04 ?  95  ALA   B O   1 
ATOM   2536 C CB  . ALA   B 1 95  ? -0.100  -22.842 -15.228 1.00 14.92 ?  95  ALA   B CB  1 
ATOM   2537 N N   . TYR   B 1 96  ? -2.146  -21.146 -17.082 1.00 15.38 ?  96  TYR   B N   1 
ATOM   2538 C CA  . TYR   B 1 96  ? -3.215  -20.175 -17.298 1.00 15.10 ?  96  TYR   B CA  1 
ATOM   2539 C C   . TYR   B 1 96  ? -4.515  -20.790 -17.838 1.00 16.62 ?  96  TYR   B C   1 
ATOM   2540 O O   . TYR   B 1 96  ? -5.575  -20.258 -17.526 1.00 17.30 ?  96  TYR   B O   1 
ATOM   2541 C CB  . TYR   B 1 96  ? -2.844  -19.036 -18.236 1.00 14.45 ?  96  TYR   B CB  1 
ATOM   2542 C CG  . TYR   B 1 96  ? -2.021  -17.894 -17.687 1.00 14.62 ?  96  TYR   B CG  1 
ATOM   2543 C CD1 . TYR   B 1 96  ? -2.514  -17.034 -16.696 1.00 13.60 ?  96  TYR   B CD1 1 
ATOM   2544 C CD2 . TYR   B 1 96  ? -0.747  -17.610 -18.186 1.00 13.70 ?  96  TYR   B CD2 1 
ATOM   2545 C CE1 . TYR   B 1 96  ? -1.833  -15.900 -16.310 1.00 14.02 ?  96  TYR   B CE1 1 
ATOM   2546 C CE2 . TYR   B 1 96  ? -0.045  -16.486 -17.783 1.00 14.14 ?  96  TYR   B CE2 1 
ATOM   2547 C CZ  . TYR   B 1 96  ? -0.557  -15.663 -16.789 1.00 14.54 ?  96  TYR   B CZ  1 
ATOM   2548 O OH  . TYR   B 1 96  ? 0.102   -14.541 -16.368 1.00 15.87 ?  96  TYR   B OH  1 
ATOM   2549 N N   . GLY   B 1 97  ? -4.430  -21.920 -18.559 1.00 15.92 ?  97  GLY   B N   1 
ATOM   2550 C CA  . GLY   B 1 97  ? -5.574  -22.644 -19.103 1.00 15.33 ?  97  GLY   B CA  1 
ATOM   2551 C C   . GLY   B 1 97  ? -5.573  -22.741 -20.629 1.00 15.00 ?  97  GLY   B C   1 
ATOM   2552 O O   . GLY   B 1 97  ? -6.598  -23.044 -21.201 1.00 15.13 ?  97  GLY   B O   1 
ATOM   2553 N N   . ALA   B 1 98  ? -4.431  -22.503 -21.273 1.00 14.74 ?  98  ALA   B N   1 
ATOM   2554 C CA  . ALA   B 1 98  ? -4.433  -22.587 -22.729 1.00 13.57 ?  98  ALA   B CA  1 
ATOM   2555 C C   . ALA   B 1 98  ? -4.924  -23.962 -23.190 1.00 12.49 ?  98  ALA   B C   1 
ATOM   2556 O O   . ALA   B 1 98  ? -4.562  -24.979 -22.619 1.00 13.55 ?  98  ALA   B O   1 
ATOM   2557 C CB  . ALA   B 1 98  ? -3.007  -22.338 -23.272 1.00 13.73 ?  98  ALA   B CB  1 
ATOM   2558 N N   . ASP   B 1 99  ? -5.549  -24.015 -24.361 1.00 12.94 ?  99  ASP   B N   1 
ATOM   2559 C CA  . ASP   B 1 99  ? -5.807  -25.251 -25.080 1.00 13.44 ?  99  ASP   B CA  1 
ATOM   2560 C C   . ASP   B 1 99  ? -4.686  -25.566 -26.082 1.00 12.42 ?  99  ASP   B C   1 
ATOM   2561 O O   . ASP   B 1 99  ? -4.458  -26.730 -26.396 1.00 12.22 ?  99  ASP   B O   1 
ATOM   2562 C CB  . ASP   B 1 99  ? -7.115  -25.160 -25.861 1.00 14.84 ?  99  ASP   B CB  1 
ATOM   2563 C CG  . ASP   B 1 99  ? -8.332  -24.985 -24.964 1.00 14.44 ?  99  ASP   B CG  1 
ATOM   2564 O OD1 . ASP   B 1 99  ? -8.398  -25.744 -23.988 1.00 17.08 ?  99  ASP   B OD1 1 
ATOM   2565 O OD2 . ASP   B 1 99  ? -9.111  -24.031 -25.171 1.00 15.65 ?  99  ASP   B OD2 1 
ATOM   2566 N N   . GLU   B 1 100 ? -4.043  -24.515 -26.579 1.00 12.08 ?  100 GLU   B N   1 
ATOM   2567 C CA  . GLU   B 1 100 ? -2.947  -24.640 -27.540 1.00 12.42 ?  100 GLU   B CA  1 
ATOM   2568 C C   . GLU   B 1 100 ? -1.906  -23.574 -27.269 1.00 12.45 ?  100 GLU   B C   1 
ATOM   2569 O O   . GLU   B 1 100 ? -2.260  -22.452 -26.929 1.00 12.74 ?  100 GLU   B O   1 
ATOM   2570 C CB  . GLU   B 1 100 ? -3.503  -24.420 -28.956 1.00 13.00 ?  100 GLU   B CB  1 
ATOM   2571 C CG  . GLU   B 1 100 ? -4.739  -25.254 -29.229 1.00 13.98 ?  100 GLU   B CG  1 
ATOM   2572 C CD  . GLU   B 1 100 ? -5.231  -25.143 -30.664 1.00 15.23 ?  100 GLU   B CD  1 
ATOM   2573 O OE1 . GLU   B 1 100 ? -4.908  -24.161 -31.334 1.00 16.08 ?  100 GLU   B OE1 1 
ATOM   2574 O OE2 . GLU   B 1 100 ? -6.058  -25.993 -31.006 1.00 16.84 ?  100 GLU   B OE2 1 
ATOM   2575 N N   . VAL   B 1 101 ? -0.618  -23.914 -27.503 1.00 12.94 ?  101 VAL   B N   1 
ATOM   2576 C CA  . VAL   B 1 101 ? 0.492   -22.995 -27.396 1.00 13.13 ?  101 VAL   B CA  1 
ATOM   2577 C C   . VAL   B 1 101 ? 1.215   -22.975 -28.735 1.00 13.05 ?  101 VAL   B C   1 
ATOM   2578 O O   . VAL   B 1 101 ? 1.475   -24.045 -29.272 1.00 13.65 ?  101 VAL   B O   1 
ATOM   2579 C CB  . VAL   B 1 101 ? 1.436   -23.450 -26.275 1.00 14.36 ?  101 VAL   B CB  1 
ATOM   2580 C CG1 . VAL   B 1 101 ? 2.758   -22.678 -26.250 1.00 14.60 ?  101 VAL   B CG1 1 
ATOM   2581 C CG2 . VAL   B 1 101 ? 0.727   -23.412 -24.930 1.00 14.98 ?  101 VAL   B CG2 1 
ATOM   2582 N N   . ASP   B 1 102 ? 1.407   -21.770 -29.241 1.00 12.48 ?  102 ASP   B N   1 
ATOM   2583 C CA  . ASP   B 1 102 ? 2.145   -21.558 -30.471 1.00 13.42 ?  102 ASP   B CA  1 
ATOM   2584 C C   . ASP   B 1 102 ? 3.503   -21.014 -30.028 1.00 13.62 ?  102 ASP   B C   1 
ATOM   2585 O O   . ASP   B 1 102 ? 3.628   -19.842 -29.642 1.00 13.11 ?  102 ASP   B O   1 
ATOM   2586 C CB  . ASP   B 1 102 ? 1.398   -20.593 -31.365 1.00 13.60 ?  102 ASP   B CB  1 
ATOM   2587 C CG  . ASP   B 1 102 ? 0.004   -20.972 -31.855 1.00 15.29 ?  102 ASP   B CG  1 
ATOM   2588 O OD1 . ASP   B 1 102 ? -0.568  -21.972 -31.384 1.00 14.10 ?  102 ASP   B OD1 1 
ATOM   2589 O OD2 . ASP   B 1 102 ? -0.488  -20.197 -32.721 1.00 17.28 ?  102 ASP   B OD2 1 
ATOM   2590 N N   . VAL   B 1 103 ? 4.519   -21.862 -30.050 1.00 13.52 ?  103 VAL   B N   1 
ATOM   2591 C CA  . VAL   B 1 103 ? 5.852   -21.436 -29.640 1.00 13.73 ?  103 VAL   B CA  1 
ATOM   2592 C C   . VAL   B 1 103 ? 6.665   -21.053 -30.870 1.00 14.02 ?  103 VAL   B C   1 
ATOM   2593 O O   . VAL   B 1 103 ? 6.517   -21.646 -31.945 1.00 13.24 ?  103 VAL   B O   1 
ATOM   2594 C CB  . VAL   B 1 103 ? 6.523   -22.573 -28.858 1.00 13.64 ?  103 VAL   B CB  1 
ATOM   2595 C CG1 . VAL   B 1 103 ? 6.790   -23.811 -29.718 1.00 13.94 ?  103 VAL   B CG1 1 
ATOM   2596 C CG2 . VAL   B 1 103 ? 7.798   -22.110 -28.188 1.00 13.96 ?  103 VAL   B CG2 1 
ATOM   2597 N N   . VAL   B 1 104 ? 7.571   -20.086 -30.682 1.00 13.28 ?  104 VAL   B N   1 
ATOM   2598 C CA  . VAL   B 1 104 ? 8.441   -19.663 -31.771 1.00 12.43 ?  104 VAL   B CA  1 
ATOM   2599 C C   . VAL   B 1 104 ? 9.700   -20.540 -31.753 1.00 13.42 ?  104 VAL   B C   1 
ATOM   2600 O O   . VAL   B 1 104 ? 10.444  -20.640 -30.753 1.00 13.07 ?  104 VAL   B O   1 
ATOM   2601 C CB  . VAL   B 1 104 ? 8.793   -18.173 -31.781 1.00 12.37 ?  104 VAL   B CB  1 
ATOM   2602 C CG1 . VAL   B 1 104 ? 9.580   -17.813 -33.051 1.00 12.16 ?  104 VAL   B CG1 1 
ATOM   2603 C CG2 . VAL   B 1 104 ? 7.562   -17.302 -31.723 1.00 12.97 ?  104 VAL   B CG2 1 
ATOM   2604 N N   . PHE   B 1 105 ? 9.942   -21.195 -32.895 1.00 13.55 ?  105 PHE   B N   1 
ATOM   2605 C CA  . PHE   B 1 105 ? 11.138  -21.995 -33.113 1.00 14.09 ?  105 PHE   B CA  1 
ATOM   2606 C C   . PHE   B 1 105 ? 12.345  -21.074 -33.103 1.00 13.85 ?  105 PHE   B C   1 
ATOM   2607 O O   . PHE   B 1 105 ? 12.227  -19.906 -33.527 1.00 13.70 ?  105 PHE   B O   1 
ATOM   2608 C CB  . PHE   B 1 105 ? 11.019  -22.617 -34.507 1.00 13.93 ?  105 PHE   B CB  1 
ATOM   2609 C CG  . PHE   B 1 105 ? 12.142  -23.564 -34.857 1.00 14.70 ?  105 PHE   B CG  1 
ATOM   2610 C CD1 . PHE   B 1 105 ? 13.264  -23.095 -35.547 1.00 15.31 ?  105 PHE   B CD1 1 
ATOM   2611 C CD2 . PHE   B 1 105 ? 12.008  -24.929 -34.654 1.00 15.49 ?  105 PHE   B CD2 1 
ATOM   2612 C CE1 . PHE   B 1 105 ? 14.270  -23.972 -35.930 1.00 15.57 ?  105 PHE   B CE1 1 
ATOM   2613 C CE2 . PHE   B 1 105 ? 13.035  -25.796 -35.023 1.00 15.84 ?  105 PHE   B CE2 1 
ATOM   2614 C CZ  . PHE   B 1 105 ? 14.152  -25.325 -35.655 1.00 15.43 ?  105 PHE   B CZ  1 
ATOM   2615 N N   . PRO   B 1 106 ? 13.510  -21.551 -32.590 1.00 14.34 ?  106 PRO   B N   1 
ATOM   2616 C CA  . PRO   B 1 106 ? 14.741  -20.757 -32.580 1.00 14.75 ?  106 PRO   B CA  1 
ATOM   2617 C C   . PRO   B 1 106 ? 15.351  -20.695 -33.977 1.00 15.45 ?  106 PRO   B C   1 
ATOM   2618 O O   . PRO   B 1 106 ? 16.354  -21.352 -34.270 1.00 15.85 ?  106 PRO   B O   1 
ATOM   2619 C CB  . PRO   B 1 106 ? 15.645  -21.470 -31.546 1.00 14.66 ?  106 PRO   B CB  1 
ATOM   2620 C CG  . PRO   B 1 106 ? 15.242  -22.917 -31.664 1.00 14.46 ?  106 PRO   B CG  1 
ATOM   2621 C CD  . PRO   B 1 106 ? 13.714  -22.890 -31.997 1.00 14.03 ?  106 PRO   B CD  1 
ATOM   2622 N N   . TYR   B 1 107 ? 14.724  -19.890 -34.828 1.00 15.21 ?  107 TYR   B N   1 
ATOM   2623 C CA  . TYR   B 1 107 ? 15.089  -19.901 -36.249 1.00 15.40 ?  107 TYR   B CA  1 
ATOM   2624 C C   . TYR   B 1 107 ? 16.448  -19.247 -36.514 1.00 16.55 ?  107 TYR   B C   1 
ATOM   2625 O O   . TYR   B 1 107 ? 17.173  -19.671 -37.413 1.00 18.08 ?  107 TYR   B O   1 
ATOM   2626 C CB  . TYR   B 1 107 ? 13.952  -19.247 -37.036 1.00 14.57 ?  107 TYR   B CB  1 
ATOM   2627 C CG  . TYR   B 1 107 ? 13.658  -17.799 -36.718 1.00 13.96 ?  107 TYR   B CG  1 
ATOM   2628 C CD1 . TYR   B 1 107 ? 14.406  -16.775 -37.263 1.00 15.33 ?  107 TYR   B CD1 1 
ATOM   2629 C CD2 . TYR   B 1 107 ? 12.623  -17.458 -35.892 1.00 12.89 ?  107 TYR   B CD2 1 
ATOM   2630 C CE1 . TYR   B 1 107 ? 14.093  -15.450 -37.060 1.00 15.29 ?  107 TYR   B CE1 1 
ATOM   2631 C CE2 . TYR   B 1 107 ? 12.323  -16.128 -35.642 1.00 13.83 ?  107 TYR   B CE2 1 
ATOM   2632 C CZ  . TYR   B 1 107 ? 13.060  -15.119 -36.223 1.00 14.79 ?  107 TYR   B CZ  1 
ATOM   2633 O OH  . TYR   B 1 107 ? 12.774  -13.811 -36.002 1.00 15.55 ?  107 TYR   B OH  1 
ATOM   2634 N N   . ARG   B 1 108 ? 16.817  -18.222 -35.737 1.00 16.46 ?  108 ARG   B N   1 
ATOM   2635 C CA  . ARG   B 1 108 ? 18.144  -17.643 -35.864 1.00 16.77 ?  108 ARG   B CA  1 
ATOM   2636 C C   . ARG   B 1 108 ? 19.214  -18.655 -35.489 1.00 17.87 ?  108 ARG   B C   1 
ATOM   2637 O O   . ARG   B 1 108 ? 20.300  -18.630 -36.082 1.00 18.56 ?  108 ARG   B O   1 
ATOM   2638 C CB  . ARG   B 1 108 ? 18.302  -16.382 -35.019 1.00 16.93 ?  108 ARG   B CB  1 
ATOM   2639 C CG  . ARG   B 1 108 ? 17.588  -15.196 -35.648 1.00 18.53 ?  108 ARG   B CG  1 
ATOM   2640 C CD  . ARG   B 1 108 ? 17.814  -13.891 -34.913 1.00 22.05 ?  108 ARG   B CD  1 
ATOM   2641 N NE  . ARG   B 1 108 ? 17.522  -13.963 -33.487 1.00 26.56 ?  108 ARG   B NE  1 
ATOM   2642 C CZ  . ARG   B 1 108 ? 16.314  -13.921 -32.963 1.00 26.43 ?  108 ARG   B CZ  1 
ATOM   2643 N NH1 . ARG   B 1 108 ? 15.296  -13.492 -33.707 1.00 28.49 ?  108 ARG   B NH1 1 
ATOM   2644 N NH2 . ARG   B 1 108 ? 16.124  -14.295 -31.700 1.00 22.98 ?  108 ARG   B NH2 1 
ATOM   2645 N N   . ALA   B 1 109 ? 18.955  -19.515 -34.487 1.00 17.44 ?  109 ALA   B N   1 
ATOM   2646 C CA  . ALA   B 1 109 ? 19.919  -20.545 -34.118 1.00 18.20 ?  109 ALA   B CA  1 
ATOM   2647 C C   . ALA   B 1 109 ? 20.102  -21.517 -35.269 1.00 18.80 ?  109 ALA   B C   1 
ATOM   2648 O O   . ALA   B 1 109 ? 21.202  -21.957 -35.564 1.00 17.45 ?  109 ALA   B O   1 
ATOM   2649 C CB  . ALA   B 1 109 ? 19.460  -21.275 -32.895 1.00 18.82 ?  109 ALA   B CB  1 
ATOM   2650 N N   . LEU   B 1 110 ? 18.998  -21.839 -35.954 1.00 17.49 ?  110 LEU   B N   1 
ATOM   2651 C CA  . LEU   B 1 110 ? 19.094  -22.754 -37.084 1.00 17.98 ?  110 LEU   B CA  1 
ATOM   2652 C C   . LEU   B 1 110 ? 19.891  -22.114 -38.223 1.00 16.89 ?  110 LEU   B C   1 
ATOM   2653 O O   . LEU   B 1 110 ? 20.697  -22.776 -38.899 1.00 17.43 ?  110 LEU   B O   1 
ATOM   2654 C CB  . LEU   B 1 110 ? 17.698  -23.135 -37.544 1.00 17.22 ?  110 LEU   B CB  1 
ATOM   2655 C CG  . LEU   B 1 110 ? 17.682  -23.973 -38.832 1.00 17.69 ?  110 LEU   B CG  1 
ATOM   2656 C CD1 . LEU   B 1 110 ? 18.274  -25.351 -38.589 1.00 18.81 ?  110 LEU   B CD1 1 
ATOM   2657 C CD2 . LEU   B 1 110 ? 16.261  -24.067 -39.375 1.00 17.87 ?  110 LEU   B CD2 1 
ATOM   2658 N N   . MET   B 1 111 ? 19.696  -20.813 -38.420 1.00 16.22 ?  111 MET   B N   1 
ATOM   2659 C CA  . MET   B 1 111 ? 20.382  -20.136 -39.505 1.00 17.44 ?  111 MET   B CA  1 
ATOM   2660 C C   . MET   B 1 111 ? 21.873  -20.051 -39.196 1.00 18.26 ?  111 MET   B C   1 
ATOM   2661 O O   . MET   B 1 111 ? 22.689  -19.870 -40.094 1.00 18.70 ?  111 MET   B O   1 
ATOM   2662 C CB  . MET   B 1 111 ? 19.786  -18.751 -39.739 1.00 19.72 ?  111 MET   B CB  1 
ATOM   2663 C CG  . MET   B 1 111 ? 18.369  -18.811 -40.292 1.00 22.82 ?  111 MET   B CG  1 
ATOM   2664 S SD  . MET   B 1 111 ? 17.469  -17.238 -40.288 1.00 28.22 ?  111 MET   B SD  1 
ATOM   2665 C CE  . MET   B 1 111 ? 18.216  -16.639 -41.801 1.00 30.24 ?  111 MET   B CE  1 
ATOM   2666 N N   . ALA   B 1 112 ? 22.215  -20.159 -37.921 1.00 18.58 ?  112 ALA   B N   1 
ATOM   2667 C CA  . ALA   B 1 112 ? 23.594  -20.205 -37.489 1.00 19.54 ?  112 ALA   B CA  1 
ATOM   2668 C C   . ALA   B 1 112 ? 24.100  -21.641 -37.374 1.00 20.15 ?  112 ALA   B C   1 
ATOM   2669 O O   . ALA   B 1 112 ? 25.147  -21.856 -36.771 1.00 19.47 ?  112 ALA   B O   1 
ATOM   2670 C CB  . ALA   B 1 112 ? 23.681  -19.489 -36.169 1.00 21.90 ?  112 ALA   B CB  1 
ATOM   2671 N N   . GLY   B 1 113 ? 23.363  -22.627 -37.882 1.00 18.96 ?  113 GLY   B N   1 
ATOM   2672 C CA  . GLY   B 1 113 ? 23.853  -23.995 -38.019 1.00 20.32 ?  113 GLY   B CA  1 
ATOM   2673 C C   . GLY   B 1 113 ? 23.505  -24.907 -36.851 1.00 21.82 ?  113 GLY   B C   1 
ATOM   2674 O O   . GLY   B 1 113 ? 24.049  -25.998 -36.723 1.00 24.54 ?  113 GLY   B O   1 
ATOM   2675 N N   . ASN   B 1 114 ? 22.705  -24.422 -35.901 1.00 20.81 ?  114 ASN   B N   1 
ATOM   2676 C CA  . ASN   B 1 114 ? 22.395  -25.167 -34.702 1.00 20.23 ?  114 ASN   B CA  1 
ATOM   2677 C C   . ASN   B 1 114 ? 20.998  -25.746 -34.869 1.00 21.53 ?  114 ASN   B C   1 
ATOM   2678 O O   . ASN   B 1 114 ? 20.009  -25.070 -34.636 1.00 23.30 ?  114 ASN   B O   1 
ATOM   2679 C CB  . ASN   B 1 114 ? 22.513  -24.304 -33.451 1.00 21.76 ?  114 ASN   B CB  1 
ATOM   2680 C CG  . ASN   B 1 114 ? 22.331  -25.122 -32.196 1.00 22.38 ?  114 ASN   B CG  1 
ATOM   2681 O OD1 . ASN   B 1 114 ? 21.848  -26.260 -32.233 1.00 23.68 ?  114 ASN   B OD1 1 
ATOM   2682 N ND2 . ASN   B 1 114 ? 22.752  -24.577 -31.072 1.00 23.99 ?  114 ASN   B ND2 1 
ATOM   2683 N N   . GLU   B 1 115 ? 20.947  -26.994 -35.296 1.00 20.51 ?  115 GLU   B N   1 
ATOM   2684 C CA  . GLU   B 1 115 ? 19.713  -27.726 -35.456 1.00 20.65 ?  115 GLU   B CA  1 
ATOM   2685 C C   . GLU   B 1 115 ? 19.249  -28.261 -34.115 1.00 20.37 ?  115 GLU   B C   1 
ATOM   2686 O O   . GLU   B 1 115 ? 18.042  -28.370 -33.888 1.00 19.49 ?  115 GLU   B O   1 
ATOM   2687 C CB  . GLU   B 1 115 ? 19.940  -28.894 -36.402 1.00 22.08 ?  115 GLU   B CB  1 
ATOM   2688 C CG  . GLU   B 1 115 ? 20.153  -28.413 -37.836 1.00 22.89 ?  115 GLU   B CG  1 
ATOM   2689 C CD  . GLU   B 1 115 ? 20.320  -29.532 -38.837 1.00 26.37 ?  115 GLU   B CD  1 
ATOM   2690 O OE1 . GLU   B 1 115 ? 20.122  -30.697 -38.465 1.00 29.09 ?  115 GLU   B OE1 1 
ATOM   2691 O OE2 . GLU   B 1 115 ? 20.617  -29.230 -40.005 1.00 29.81 ?  115 GLU   B OE2 1 
ATOM   2692 N N   . GLN   B 1 116 ? 20.214  -28.609 -33.252 1.00 20.03 ?  116 GLN   B N   1 
ATOM   2693 C CA  . GLN   B 1 116 ? 19.922  -29.359 -32.044 1.00 20.88 ?  116 GLN   B CA  1 
ATOM   2694 C C   . GLN   B 1 116 ? 19.055  -28.527 -31.101 1.00 20.01 ?  116 GLN   B C   1 
ATOM   2695 O O   . GLN   B 1 116 ? 18.141  -29.068 -30.503 1.00 21.01 ?  116 GLN   B O   1 
ATOM   2696 C CB  . GLN   B 1 116 ? 21.194  -29.833 -31.337 1.00 22.83 ?  116 GLN   B CB  1 
ATOM   2697 C CG  . GLN   B 1 116 ? 20.924  -30.855 -30.246 1.00 24.22 ?  116 GLN   B CG  1 
ATOM   2698 C CD  . GLN   B 1 116 ? 20.299  -32.123 -30.781 1.00 29.93 ?  116 GLN   B CD  1 
ATOM   2699 O OE1 . GLN   B 1 116 ? 20.765  -32.715 -31.760 1.00 34.93 ?  116 GLN   B OE1 1 
ATOM   2700 N NE2 . GLN   B 1 116 ? 19.253  -32.596 -30.133 1.00 31.62 ?  116 GLN   B NE2 1 
ATOM   2701 N N   . VAL   B 1 117 ? 19.344  -27.228 -30.965 1.00 19.23 ?  117 VAL   B N   1 
ATOM   2702 C CA  . VAL   B 1 117 ? 18.643  -26.440 -29.977 1.00 20.38 ?  117 VAL   B CA  1 
ATOM   2703 C C   . VAL   B 1 117 ? 17.167  -26.342 -30.378 1.00 18.39 ?  117 VAL   B C   1 
ATOM   2704 O O   . VAL   B 1 117 ? 16.281  -26.383 -29.520 1.00 17.44 ?  117 VAL   B O   1 
ATOM   2705 C CB  . VAL   B 1 117 ? 19.265  -25.054 -29.720 1.00 20.53 ?  117 VAL   B CB  1 
ATOM   2706 C CG1 . VAL   B 1 117 ? 19.169  -24.131 -30.940 1.00 20.50 ?  117 VAL   B CG1 1 
ATOM   2707 C CG2 . VAL   B 1 117 ? 18.598  -24.403 -28.517 1.00 21.45 ?  117 VAL   B CG2 1 
ATOM   2708 N N   . GLY   B 1 118 ? 16.901  -26.210 -31.684 1.00 17.99 ?  118 GLY   B N   1 
ATOM   2709 C CA  . GLY   B 1 118 ? 15.520  -26.184 -32.140 1.00 16.49 ?  118 GLY   B CA  1 
ATOM   2710 C C   . GLY   B 1 118 ? 14.759  -27.460 -31.788 1.00 15.59 ?  118 GLY   B C   1 
ATOM   2711 O O   . GLY   B 1 118 ? 13.586  -27.449 -31.347 1.00 16.81 ?  118 GLY   B O   1 
ATOM   2712 N N   . PHE   B 1 119 ? 15.423  -28.589 -32.005 1.00 15.52 ?  119 PHE   B N   1 
ATOM   2713 C CA  . PHE   B 1 119 ? 14.846  -29.871 -31.650 1.00 15.80 ?  119 PHE   B CA  1 
ATOM   2714 C C   . PHE   B 1 119 ? 14.563  -29.914 -30.154 1.00 16.43 ?  119 PHE   B C   1 
ATOM   2715 O O   . PHE   B 1 119 ? 13.454  -30.283 -29.741 1.00 15.23 ?  119 PHE   B O   1 
ATOM   2716 C CB  . PHE   B 1 119 ? 15.780  -31.023 -32.004 1.00 17.02 ?  119 PHE   B CB  1 
ATOM   2717 C CG  . PHE   B 1 119 ? 15.199  -32.386 -31.669 1.00 20.22 ?  119 PHE   B CG  1 
ATOM   2718 C CD1 . PHE   B 1 119 ? 14.408  -33.077 -32.563 1.00 21.14 ?  119 PHE   B CD1 1 
ATOM   2719 C CD2 . PHE   B 1 119 ? 15.444  -32.979 -30.429 1.00 21.72 ?  119 PHE   B CD2 1 
ATOM   2720 C CE1 . PHE   B 1 119 ? 13.890  -34.326 -32.225 1.00 22.62 ?  119 PHE   B CE1 1 
ATOM   2721 C CE2 . PHE   B 1 119 ? 14.926  -34.220 -30.115 1.00 23.09 ?  119 PHE   B CE2 1 
ATOM   2722 C CZ  . PHE   B 1 119 ? 14.139  -34.890 -31.022 1.00 23.76 ?  119 PHE   B CZ  1 
ATOM   2723 N N   . ASP   B 1 120 ? 15.571  -29.544 -29.350 1.00 16.64 ?  120 ASP   B N   1 
ATOM   2724 C CA  . ASP   B 1 120 ? 15.415  -29.678 -27.923 1.00 18.06 ?  120 ASP   B CA  1 
ATOM   2725 C C   . ASP   B 1 120 ? 14.357  -28.709 -27.399 1.00 16.48 ?  120 ASP   B C   1 
ATOM   2726 O O   . ASP   B 1 120 ? 13.623  -29.053 -26.458 1.00 16.61 ?  120 ASP   B O   1 
ATOM   2727 C CB  . ASP   B 1 120 ? 16.744  -29.472 -27.202 1.00 19.61 ?  120 ASP   B CB  1 
ATOM   2728 C CG  . ASP   B 1 120 ? 17.787  -30.539 -27.473 1.00 21.24 ?  120 ASP   B CG  1 
ATOM   2729 O OD1 . ASP   B 1 120 ? 17.413  -31.625 -27.906 1.00 23.51 ?  120 ASP   B OD1 1 
ATOM   2730 O OD2 . ASP   B 1 120 ? 18.965  -30.240 -27.261 1.00 24.06 ?  120 ASP   B OD2 1 
ATOM   2731 N N   . LEU   B 1 121 ? 14.299  -27.488 -27.944 1.00 15.40 ?  121 LEU   B N   1 
ATOM   2732 C CA  . LEU   B 1 121 ? 13.337  -26.493 -27.487 1.00 16.44 ?  121 LEU   B CA  1 
ATOM   2733 C C   . LEU   B 1 121 ? 11.915  -26.988 -27.781 1.00 16.02 ?  121 LEU   B C   1 
ATOM   2734 O O   . LEU   B 1 121 ? 11.023  -26.944 -26.908 1.00 16.28 ?  121 LEU   B O   1 
ATOM   2735 C CB  . LEU   B 1 121 ? 13.662  -25.138 -28.100 1.00 16.48 ?  121 LEU   B CB  1 
ATOM   2736 C CG  . LEU   B 1 121 ? 12.883  -23.946 -27.538 1.00 18.28 ?  121 LEU   B CG  1 
ATOM   2737 C CD1 . LEU   B 1 121 ? 13.713  -22.698 -27.669 1.00 18.51 ?  121 LEU   B CD1 1 
ATOM   2738 C CD2 . LEU   B 1 121 ? 11.501  -23.690 -28.166 1.00 19.33 ?  121 LEU   B CD2 1 
ATOM   2739 N N   . VAL   B 1 122 ? 11.706  -27.458 -29.022 1.00 14.46 ?  122 VAL   B N   1 
ATOM   2740 C CA  . VAL   B 1 122 ? 10.388  -27.915 -29.437 1.00 14.82 ?  122 VAL   B CA  1 
ATOM   2741 C C   . VAL   B 1 122 ? 9.996   -29.124 -28.589 1.00 16.79 ?  122 VAL   B C   1 
ATOM   2742 O O   . VAL   B 1 122 ? 8.889   -29.202 -28.075 1.00 16.71 ?  122 VAL   B O   1 
ATOM   2743 C CB  . VAL   B 1 122 ? 10.255  -28.207 -30.934 1.00 15.23 ?  122 VAL   B CB  1 
ATOM   2744 C CG1 . VAL   B 1 122 ? 8.915   -28.895 -31.230 1.00 15.21 ?  122 VAL   B CG1 1 
ATOM   2745 C CG2 . VAL   B 1 122 ? 10.367  -26.895 -31.694 1.00 15.16 ?  122 VAL   B CG2 1 
ATOM   2746 N N   . LYS   B 1 123 ? 10.940  -30.033 -28.376 1.00 17.65 ?  123 LYS   B N   1 
ATOM   2747 C CA  . LYS   B 1 123 ? 10.628  -31.249 -27.653 1.00 18.20 ?  123 LYS   B CA  1 
ATOM   2748 C C   . LYS   B 1 123 ? 10.248  -30.943 -26.202 1.00 16.75 ?  123 LYS   B C   1 
ATOM   2749 O O   . LYS   B 1 123 ? 9.327   -31.555 -25.639 1.00 17.32 ?  123 LYS   B O   1 
ATOM   2750 C CB  . LYS   B 1 123 ? 11.829  -32.188 -27.731 1.00 21.51 ?  123 LYS   B CB  1 
ATOM   2751 C CG  . LYS   B 1 123 ? 11.642  -33.429 -26.878 1.00 26.44 ?  123 LYS   B CG  1 
ATOM   2752 C CD  . LYS   B 1 123 ? 12.735  -34.460 -27.086 1.00 31.95 ?  123 LYS   B CD  1 
ATOM   2753 C CE  . LYS   B 1 123 ? 12.463  -35.792 -26.423 1.00 37.56 ?  123 LYS   B CE  1 
ATOM   2754 N NZ  . LYS   B 1 123 ? 11.134  -36.321 -26.784 1.00 43.85 ?  123 LYS   B NZ  1 
ATOM   2755 N N   . ALA   B 1 124 ? 11.013  -30.054 -25.553 1.00 16.62 ?  124 ALA   B N   1 
ATOM   2756 C CA  . ALA   B 1 124 ? 10.747  -29.731 -24.154 1.00 17.37 ?  124 ALA   B CA  1 
ATOM   2757 C C   . ALA   B 1 124 ? 9.336   -29.130 -24.044 1.00 17.56 ?  124 ALA   B C   1 
ATOM   2758 O O   . ALA   B 1 124 ? 8.569   -29.447 -23.123 1.00 17.58 ?  124 ALA   B O   1 
ATOM   2759 C CB  . ALA   B 1 124 ? 11.790  -28.759 -23.632 1.00 18.60 ?  124 ALA   B CB  1 
ATOM   2760 N N   . CYS   B 1 125 ? 9.006   -28.214 -24.979 1.00 17.32 ?  125 CYS   B N   1 
ATOM   2761 C CA  . CYS   B 1 125 ? 7.701   -27.591 -24.960 1.00 15.76 ?  125 CYS   B CA  1 
ATOM   2762 C C   . CYS   B 1 125 ? 6.610   -28.616 -25.236 1.00 17.04 ?  125 CYS   B C   1 
ATOM   2763 O O   . CYS   B 1 125 ? 5.535   -28.526 -24.630 1.00 15.46 ?  125 CYS   B O   1 
ATOM   2764 C CB  . CYS   B 1 125 ? 7.628   -26.402 -25.900 1.00 15.73 ?  125 CYS   B CB  1 
ATOM   2765 S SG  . CYS   B 1 125 ? 8.694   -25.042 -25.384 1.00 16.69 ?  125 CYS   B SG  1 
ATOM   2766 N N   . LYS   B 1 126 ? 6.837   -29.509 -26.216 1.00 16.50 ?  126 LYS   B N   1 
ATOM   2767 C CA  . LYS   B 1 126 ? 5.876   -30.548 -26.547 1.00 17.07 ?  126 LYS   B CA  1 
ATOM   2768 C C   . LYS   B 1 126 ? 5.593   -31.443 -25.331 1.00 18.67 ?  126 LYS   B C   1 
ATOM   2769 O O   . LYS   B 1 126 ? 4.450   -31.775 -25.031 1.00 18.73 ?  126 LYS   B O   1 
ATOM   2770 C CB  . LYS   B 1 126 ? 6.375   -31.436 -27.685 1.00 18.46 ?  126 LYS   B CB  1 
ATOM   2771 C CG  . LYS   B 1 126 ? 5.454   -32.579 -28.009 1.00 19.46 ?  126 LYS   B CG  1 
ATOM   2772 C CD  . LYS   B 1 126 ? 4.002   -32.181 -28.280 1.00 21.80 ?  126 LYS   B CD  1 
ATOM   2773 C CE  . LYS   B 1 126 ? 3.136   -33.415 -28.452 1.00 23.34 ?  126 LYS   B CE  1 
ATOM   2774 N NZ  . LYS   B 1 126 ? 3.423   -34.053 -29.728 1.00 25.64 ?  126 LYS   B NZ  1 
ATOM   2775 N N   . GLU   B 1 127 ? 6.647   -31.833 -24.618 1.00 20.02 ?  127 GLU   B N   1 
ATOM   2776 C CA  . GLU   B 1 127 ? 6.508   -32.700 -23.459 1.00 21.56 ?  127 GLU   B CA  1 
ATOM   2777 C C   . GLU   B 1 127 ? 5.550   -32.077 -22.454 1.00 20.05 ?  127 GLU   B C   1 
ATOM   2778 O O   . GLU   B 1 127 ? 4.660   -32.777 -21.946 1.00 20.11 ?  127 GLU   B O   1 
ATOM   2779 C CB  . GLU   B 1 127 ? 7.880   -33.010 -22.854 1.00 25.51 ?  127 GLU   B CB  1 
ATOM   2780 C CG  . GLU   B 1 127 ? 8.615   -34.085 -23.641 1.00 30.00 ?  127 GLU   B CG  1 
ATOM   2781 C CD  . GLU   B 1 127 ? 10.033  -34.385 -23.205 1.00 35.80 ?  127 GLU   B CD  1 
ATOM   2782 O OE1 . GLU   B 1 127 ? 10.604  -33.697 -22.322 1.00 37.19 ?  127 GLU   B OE1 1 
ATOM   2783 O OE2 . GLU   B 1 127 ? 10.556  -35.333 -23.830 1.00 39.44 ?  127 GLU   B OE2 1 
ATOM   2784 N N   . ALA   B 1 128 ? 5.724   -30.775 -22.178 1.00 18.55 ?  128 ALA   B N   1 
ATOM   2785 C CA  . ALA   B 1 128 ? 4.880   -30.088 -21.214 1.00 16.70 ?  128 ALA   B CA  1 
ATOM   2786 C C   . ALA   B 1 128 ? 3.444   -30.061 -21.700 1.00 15.93 ?  128 ALA   B C   1 
ATOM   2787 O O   . ALA   B 1 128 ? 2.498   -30.308 -20.951 1.00 17.73 ?  128 ALA   B O   1 
ATOM   2788 C CB  . ALA   B 1 128 ? 5.404   -28.664 -20.968 1.00 15.95 ?  128 ALA   B CB  1 
ATOM   2789 N N   . CYS   B 1 129 ? 3.275   -29.693 -22.968 1.00 14.92 ?  129 CYS   B N   1 
ATOM   2790 C CA  . CYS   B 1 129 ? 1.958   -29.592 -23.576 1.00 15.04 ?  129 CYS   B CA  1 
ATOM   2791 C C   . CYS   B 1 129 ? 1.209   -30.931 -23.508 1.00 15.40 ?  129 CYS   B C   1 
ATOM   2792 O O   . CYS   B 1 129 ? 0.022   -31.017 -23.094 1.00 15.66 ?  129 CYS   B O   1 
ATOM   2793 C CB  . CYS   B 1 129 ? 2.136   -29.028 -24.993 1.00 14.54 ?  129 CYS   B CB  1 
ATOM   2794 S SG  . CYS   B 1 129 ? 2.415   -27.237 -24.999 1.00 15.87 ?  129 CYS   B SG  1 
ATOM   2795 N N   . ALA   B 1 130 ? 1.869   -31.986 -23.975 1.00 16.44 ?  130 ALA   B N   1 
ATOM   2796 C CA  . ALA   B 1 130 ? 1.251   -33.292 -24.110 1.00 18.53 ?  130 ALA   B CA  1 
ATOM   2797 C C   . ALA   B 1 130 ? 0.782   -33.804 -22.760 1.00 19.11 ?  130 ALA   B C   1 
ATOM   2798 O O   . ALA   B 1 130 ? -0.288  -34.398 -22.660 1.00 18.80 ?  130 ALA   B O   1 
ATOM   2799 C CB  . ALA   B 1 130 ? 2.199   -34.290 -24.712 1.00 20.01 ?  130 ALA   B CB  1 
ATOM   2800 N N   . ALA   B 1 131 ? 1.587   -33.523 -21.730 1.00 17.93 ?  131 ALA   B N   1 
ATOM   2801 C CA  . ALA   B 1 131 ? 1.225   -33.843 -20.364 1.00 19.77 ?  131 ALA   B CA  1 
ATOM   2802 C C   . ALA   B 1 131 ? -0.100  -33.196 -19.950 1.00 19.32 ?  131 ALA   B C   1 
ATOM   2803 O O   . ALA   B 1 131 ? -0.779  -33.747 -19.110 1.00 20.94 ?  131 ALA   B O   1 
ATOM   2804 C CB  . ALA   B 1 131 ? 2.319   -33.369 -19.461 1.00 19.26 ?  131 ALA   B CB  1 
ATOM   2805 N N   . ALA   B 1 132 ? -0.435  -32.008 -20.467 1.00 18.78 ?  132 ALA   B N   1 
ATOM   2806 C CA  . ALA   B 1 132 ? -1.644  -31.305 -20.107 1.00 19.57 ?  132 ALA   B CA  1 
ATOM   2807 C C   . ALA   B 1 132 ? -2.718  -31.395 -21.205 1.00 19.68 ?  132 ALA   B C   1 
ATOM   2808 O O   . ALA   B 1 132 ? -3.723  -30.683 -21.157 1.00 19.15 ?  132 ALA   B O   1 
ATOM   2809 C CB  . ALA   B 1 132 ? -1.247  -29.866 -19.813 1.00 20.68 ?  132 ALA   B CB  1 
ATOM   2810 N N   . ASN   B 1 133 ? -2.534  -32.266 -22.199 1.00 20.85 ?  133 ASN   B N   1 
ATOM   2811 C CA  . ASN   B 1 133 ? -3.432  -32.381 -23.346 1.00 22.63 ?  133 ASN   B CA  1 
ATOM   2812 C C   . ASN   B 1 133 ? -3.611  -31.043 -24.054 1.00 19.48 ?  133 ASN   B C   1 
ATOM   2813 O O   . ASN   B 1 133 ? -4.707  -30.712 -24.524 1.00 19.32 ?  133 ASN   B O   1 
ATOM   2814 C CB  . ASN   B 1 133 ? -4.804  -32.956 -22.973 1.00 28.15 ?  133 ASN   B CB  1 
ATOM   2815 C CG  . ASN   B 1 133 ? -4.705  -34.403 -22.558 1.00 34.90 ?  133 ASN   B CG  1 
ATOM   2816 O OD1 . ASN   B 1 133 ? -5.094  -34.766 -21.439 1.00 46.46 ?  133 ASN   B OD1 1 
ATOM   2817 N ND2 . ASN   B 1 133 ? -4.141  -35.233 -23.420 1.00 37.54 ?  133 ASN   B ND2 1 
ATOM   2818 N N   . VAL   B 1 134 ? -2.494  -30.349 -24.240 1.00 17.29 ?  134 VAL   B N   1 
ATOM   2819 C CA  . VAL   B 1 134 ? -2.447  -29.065 -24.921 1.00 15.61 ?  134 VAL   B CA  1 
ATOM   2820 C C   . VAL   B 1 134 ? -1.717  -29.276 -26.243 1.00 15.24 ?  134 VAL   B C   1 
ATOM   2821 O O   . VAL   B 1 134 ? -0.706  -29.965 -26.279 1.00 14.70 ?  134 VAL   B O   1 
ATOM   2822 C CB  . VAL   B 1 134 ? -1.757  -28.045 -24.002 1.00 15.40 ?  134 VAL   B CB  1 
ATOM   2823 C CG1 . VAL   B 1 134 ? -1.349  -26.743 -24.682 1.00 15.42 ?  134 VAL   B CG1 1 
ATOM   2824 C CG2 . VAL   B 1 134 ? -2.675  -27.691 -22.843 1.00 17.63 ?  134 VAL   B CG2 1 
ATOM   2825 N N   . LEU   B 1 135 ? -2.263  -28.695 -27.324 1.00 14.94 ?  135 LEU   B N   1 
ATOM   2826 C CA  . LEU   B 1 135 ? -1.630  -28.806 -28.610 1.00 15.64 ?  135 LEU   B CA  1 
ATOM   2827 C C   . LEU   B 1 135 ? -0.504  -27.769 -28.698 1.00 14.76 ?  135 LEU   B C   1 
ATOM   2828 O O   . LEU   B 1 135 ? -0.642  -26.617 -28.262 1.00 15.40 ?  135 LEU   B O   1 
ATOM   2829 C CB  . LEU   B 1 135 ? -2.626  -28.631 -29.758 1.00 18.88 ?  135 LEU   B CB  1 
ATOM   2830 C CG  . LEU   B 1 135 ? -3.605  -29.785 -30.021 1.00 23.83 ?  135 LEU   B CG  1 
ATOM   2831 C CD1 . LEU   B 1 135 ? -4.217  -29.553 -31.412 1.00 25.18 ?  135 LEU   B CD1 1 
ATOM   2832 C CD2 . LEU   B 1 135 ? -3.054  -31.213 -29.979 1.00 25.77 ?  135 LEU   B CD2 1 
ATOM   2833 N N   . LEU   B 1 136 ? 0.573   -28.193 -29.355 1.00 13.49 ?  136 LEU   B N   1 
ATOM   2834 C CA  . LEU   B 1 136 ? 1.715   -27.339 -29.633 1.00 13.04 ?  136 LEU   B CA  1 
ATOM   2835 C C   . LEU   B 1 136 ? 1.867   -27.065 -31.127 1.00 13.04 ?  136 LEU   B C   1 
ATOM   2836 O O   . LEU   B 1 136 ? 2.046   -27.993 -31.919 1.00 15.26 ?  136 LEU   B O   1 
ATOM   2837 C CB  . LEU   B 1 136 ? 3.022   -27.996 -29.172 1.00 14.12 ?  136 LEU   B CB  1 
ATOM   2838 C CG  . LEU   B 1 136 ? 4.271   -27.098 -29.272 1.00 15.11 ?  136 LEU   B CG  1 
ATOM   2839 C CD1 . LEU   B 1 136 ? 4.275   -25.974 -28.259 1.00 14.21 ?  136 LEU   B CD1 1 
ATOM   2840 C CD2 . LEU   B 1 136 ? 5.530   -27.919 -29.172 1.00 15.92 ?  136 LEU   B CD2 1 
ATOM   2841 N N   . LYS   B 1 137 ? 1.819   -25.774 -31.445 1.00 12.57 ?  137 LYS   B N   1 
ATOM   2842 C CA  . LYS   B 1 137 ? 2.091   -25.294 -32.793 1.00 13.00 ?  137 LYS   B CA  1 
ATOM   2843 C C   . LYS   B 1 137 ? 3.480   -24.671 -32.727 1.00 13.73 ?  137 LYS   B C   1 
ATOM   2844 O O   . LYS   B 1 137 ? 3.838   -24.017 -31.750 1.00 13.12 ?  137 LYS   B O   1 
ATOM   2845 C CB  . LYS   B 1 137 ? 1.102   -24.222 -33.267 1.00 13.02 ?  137 LYS   B CB  1 
ATOM   2846 C CG  . LYS   B 1 137 ? -0.367  -24.550 -33.048 1.00 12.77 ?  137 LYS   B CG  1 
ATOM   2847 C CD  . LYS   B 1 137 ? -1.324  -23.810 -33.976 1.00 13.46 ?  137 LYS   B CD  1 
ATOM   2848 C CE  . LYS   B 1 137 ? -2.791  -23.717 -33.617 1.00 14.05 ?  137 LYS   B CE  1 
ATOM   2849 N NZ  . LYS   B 1 137 ? -3.061  -22.847 -32.448 1.00 14.78 ?  137 LYS   B NZ  1 
ATOM   2850 N N   . VAL   B 1 138 ? 4.260   -24.846 -33.780 1.00 12.77 ?  138 VAL   B N   1 
ATOM   2851 C CA  . VAL   B 1 138 ? 5.598   -24.277 -33.843 1.00 12.59 ?  138 VAL   B CA  1 
ATOM   2852 C C   . VAL   B 1 138 ? 5.691   -23.324 -35.012 1.00 12.75 ?  138 VAL   B C   1 
ATOM   2853 O O   . VAL   B 1 138 ? 5.534   -23.715 -36.175 1.00 13.51 ?  138 VAL   B O   1 
ATOM   2854 C CB  . VAL   B 1 138 ? 6.647   -25.394 -33.955 1.00 13.82 ?  138 VAL   B CB  1 
ATOM   2855 C CG1 . VAL   B 1 138 ? 8.072   -24.815 -34.090 1.00 14.21 ?  138 VAL   B CG1 1 
ATOM   2856 C CG2 . VAL   B 1 138 ? 6.559   -26.372 -32.771 1.00 14.47 ?  138 VAL   B CG2 1 
ATOM   2857 N N   . ILE   B 1 139 ? 5.988   -22.081 -34.668 1.00 13.78 ?  139 ILE   B N   1 
ATOM   2858 C CA  . ILE   B 1 139 ? 6.190   -21.003 -35.618 1.00 14.12 ?  139 ILE   B CA  1 
ATOM   2859 C C   . ILE   B 1 139 ? 7.642   -21.067 -36.050 1.00 14.58 ?  139 ILE   B C   1 
ATOM   2860 O O   . ILE   B 1 139 ? 8.547   -20.850 -35.214 1.00 14.09 ?  139 ILE   B O   1 
ATOM   2861 C CB  . ILE   B 1 139 ? 5.897   -19.632 -34.977 1.00 13.97 ?  139 ILE   B CB  1 
ATOM   2862 C CG1 . ILE   B 1 139 ? 4.499   -19.579 -34.387 1.00 14.71 ?  139 ILE   B CG1 1 
ATOM   2863 C CG2 . ILE   B 1 139 ? 6.167   -18.501 -35.954 1.00 14.22 ?  139 ILE   B CG2 1 
ATOM   2864 C CD1 . ILE   B 1 139 ? 4.321   -18.495 -33.351 1.00 14.46 ?  139 ILE   B CD1 1 
ATOM   2865 N N   . ILE   B 1 140 ? 7.851   -21.250 -37.365 1.00 13.36 ?  140 ILE   B N   1 
ATOM   2866 C CA  . ILE   B 1 140 ? 9.201   -21.310 -37.887 1.00 13.32 ?  140 ILE   B CA  1 
ATOM   2867 C C   . ILE   B 1 140 ? 9.703   -19.982 -38.463 1.00 14.00 ?  140 ILE   B C   1 
ATOM   2868 O O   . ILE   B 1 140 ? 10.905  -19.854 -38.670 1.00 14.65 ?  140 ILE   B O   1 
ATOM   2869 C CB  . ILE   B 1 140 ? 9.394   -22.474 -38.862 1.00 14.12 ?  140 ILE   B CB  1 
ATOM   2870 C CG1 . ILE   B 1 140 ? 8.580   -22.310 -40.128 1.00 14.92 ?  140 ILE   B CG1 1 
ATOM   2871 C CG2 . ILE   B 1 140 ? 9.159   -23.855 -38.223 1.00 14.63 ?  140 ILE   B CG2 1 
ATOM   2872 C CD1 . ILE   B 1 140 ? 9.108   -23.149 -41.263 1.00 16.04 ?  140 ILE   B CD1 1 
ATOM   2873 N N   . GLU   B 1 141 ? 8.832   -19.006 -38.702 1.00 15.14 ?  141 GLU   B N   1 
ATOM   2874 C CA  . GLU   B 1 141 ? 9.197   -17.686 -39.215 1.00 14.54 ?  141 GLU   B CA  1 
ATOM   2875 C C   . GLU   B 1 141 ? 9.778   -17.761 -40.638 1.00 15.73 ?  141 GLU   B C   1 
ATOM   2876 O O   . GLU   B 1 141 ? 10.928  -17.378 -40.914 1.00 14.67 ?  141 GLU   B O   1 
ATOM   2877 C CB  . GLU   B 1 141 ? 10.087  -16.892 -38.266 1.00 14.02 ?  141 GLU   B CB  1 
ATOM   2878 C CG  . GLU   B 1 141 ? 9.934   -15.393 -38.456 1.00 14.87 ?  141 GLU   B CG  1 
ATOM   2879 C CD  . GLU   B 1 141 ? 8.597   -14.859 -37.961 1.00 16.75 ?  141 GLU   B CD  1 
ATOM   2880 O OE1 . GLU   B 1 141 ? 8.626   -14.173 -36.904 1.00 16.05 ?  141 GLU   B OE1 1 
ATOM   2881 O OE2 . GLU   B 1 141 ? 7.541   -15.098 -38.588 1.00 15.81 ?  141 GLU   B OE2 1 
ATOM   2882 N N   . THR   B 1 142 ? 8.927   -18.218 -41.571 1.00 14.41 ?  142 THR   B N   1 
ATOM   2883 C CA  . THR   B 1 142 ? 9.380   -18.472 -42.949 1.00 14.94 ?  142 THR   B CA  1 
ATOM   2884 C C   . THR   B 1 142 ? 9.937   -17.189 -43.590 1.00 15.76 ?  142 THR   B C   1 
ATOM   2885 O O   . THR   B 1 142 ? 10.815  -17.224 -44.466 1.00 16.45 ?  142 THR   B O   1 
ATOM   2886 C CB  . THR   B 1 142 ? 8.241   -19.044 -43.788 1.00 14.66 ?  142 THR   B CB  1 
ATOM   2887 O OG1 . THR   B 1 142 ? 7.129   -18.181 -43.667 1.00 16.32 ?  142 THR   B OG1 1 
ATOM   2888 C CG2 . THR   B 1 142 ? 7.816   -20.428 -43.353 1.00 14.48 ?  142 THR   B CG2 1 
ATOM   2889 N N   . GLY   B 1 143 ? 9.407   -16.059 -43.165 1.00 15.73 ?  143 GLY   B N   1 
ATOM   2890 C CA  . GLY   B 1 143 ? 9.778   -14.747 -43.654 1.00 17.37 ?  143 GLY   B CA  1 
ATOM   2891 C C   . GLY   B 1 143 ? 11.181  -14.337 -43.246 1.00 19.14 ?  143 GLY   B C   1 
ATOM   2892 O O   . GLY   B 1 143 ? 11.788  -13.514 -43.928 1.00 23.40 ?  143 GLY   B O   1 
ATOM   2893 N N   . GLU   B 1 144 ? 11.730  -14.965 -42.200 1.00 17.97 ?  144 GLU   B N   1 
ATOM   2894 C CA  . GLU   B 1 144 ? 13.110  -14.687 -41.829 1.00 18.88 ?  144 GLU   B CA  1 
ATOM   2895 C C   . GLU   B 1 144 ? 14.033  -15.776 -42.374 1.00 17.74 ?  144 GLU   B C   1 
ATOM   2896 O O   . GLU   B 1 144 ? 15.168  -15.493 -42.686 1.00 19.80 ?  144 GLU   B O   1 
ATOM   2897 C CB  . GLU   B 1 144 ? 13.221  -14.540 -40.304 1.00 20.20 ?  144 GLU   B CB  1 
ATOM   2898 C CG  . GLU   B 1 144 ? 12.538  -13.298 -39.743 1.00 20.75 ?  144 GLU   B CG  1 
ATOM   2899 C CD  . GLU   B 1 144 ? 13.106  -11.996 -40.256 1.00 24.84 ?  144 GLU   B CD  1 
ATOM   2900 O OE1 . GLU   B 1 144 ? 14.348  -11.925 -40.349 1.00 25.03 ?  144 GLU   B OE1 1 
ATOM   2901 O OE2 . GLU   B 1 144 ? 12.328  -11.102 -40.638 1.00 27.26 ?  144 GLU   B OE2 1 
ATOM   2902 N N   . LEU   B 1 145 ? 13.584  -17.025 -42.436 1.00 16.64 ?  145 LEU   B N   1 
ATOM   2903 C CA  . LEU   B 1 145 ? 14.364  -18.125 -42.935 1.00 17.57 ?  145 LEU   B CA  1 
ATOM   2904 C C   . LEU   B 1 145 ? 14.612  -17.895 -44.431 1.00 19.55 ?  145 LEU   B C   1 
ATOM   2905 O O   . LEU   B 1 145 ? 15.722  -18.131 -44.894 1.00 21.60 ?  145 LEU   B O   1 
ATOM   2906 C CB  . LEU   B 1 145 ? 13.653  -19.457 -42.712 1.00 16.91 ?  145 LEU   B CB  1 
ATOM   2907 C CG  . LEU   B 1 145 ? 13.491  -19.895 -41.258 1.00 17.30 ?  145 LEU   B CG  1 
ATOM   2908 C CD1 . LEU   B 1 145 ? 12.631  -21.107 -41.142 1.00 18.70 ?  145 LEU   B CD1 1 
ATOM   2909 C CD2 . LEU   B 1 145 ? 14.875  -20.185 -40.686 1.00 18.07 ?  145 LEU   B CD2 1 
ATOM   2910 N N   . LYS   B 1 146 ? 13.554  -17.463 -45.134 1.00 19.37 ?  146 LYS   B N   1 
ATOM   2911 C CA  . LYS   B 1 146 ? 13.552  -17.120 -46.559 1.00 25.96 ?  146 LYS   B CA  1 
ATOM   2912 C C   . LYS   B 1 146 ? 13.761  -18.353 -47.446 1.00 26.10 ?  146 LYS   B C   1 
ATOM   2913 O O   . LYS   B 1 146 ? 12.943  -18.696 -48.291 1.00 36.50 ?  146 LYS   B O   1 
ATOM   2914 C CB  . LYS   B 1 146 ? 14.615  -16.106 -46.986 1.00 31.59 ?  146 LYS   B CB  1 
ATOM   2915 C CG  . LYS   B 1 146 ? 14.758  -14.835 -46.173 1.00 38.34 ?  146 LYS   B CG  1 
ATOM   2916 C CD  . LYS   B 1 146 ? 13.564  -13.916 -46.320 1.00 43.76 ?  146 LYS   B CD  1 
ATOM   2917 C CE  . LYS   B 1 146 ? 13.928  -12.466 -46.174 1.00 48.01 ?  146 LYS   B CE  1 
ATOM   2918 N NZ  . LYS   B 1 146 ? 12.681  -11.685 -46.226 1.00 50.68 ?  146 LYS   B NZ  1 
ATOM   2919 N N   . ASP   B 1 147 ? 14.852  -19.032 -47.216 1.00 25.52 ?  147 ASP   B N   1 
ATOM   2920 C CA  . ASP   B 1 147 ? 15.338  -20.103 -48.038 1.00 24.87 ?  147 ASP   B CA  1 
ATOM   2921 C C   . ASP   B 1 147 ? 14.479  -21.362 -47.925 1.00 22.37 ?  147 ASP   B C   1 
ATOM   2922 O O   . ASP   B 1 147 ? 14.200  -21.852 -46.820 1.00 19.91 ?  147 ASP   B O   1 
ATOM   2923 C CB  . ASP   B 1 147 ? 16.735  -20.405 -47.544 1.00 26.53 ?  147 ASP   B CB  1 
ATOM   2924 C CG  . ASP   B 1 147 ? 17.307  -21.618 -48.213 1.00 30.97 ?  147 ASP   B CG  1 
ATOM   2925 O OD1 . ASP   B 1 147 ? 17.477  -21.522 -49.431 1.00 34.80 ?  147 ASP   B OD1 1 
ATOM   2926 O OD2 . ASP   B 1 147 ? 17.405  -22.662 -47.544 1.00 33.92 ?  147 ASP   B OD2 1 
ATOM   2927 N N   . GLU   B 1 148 ? 14.183  -21.967 -49.081 1.00 20.30 ?  148 GLU   B N   1 
ATOM   2928 C CA  . GLU   B 1 148 ? 13.432  -23.212 -49.146 1.00 19.77 ?  148 GLU   B CA  1 
ATOM   2929 C C   . GLU   B 1 148 ? 14.069  -24.306 -48.281 1.00 20.17 ?  148 GLU   B C   1 
ATOM   2930 O O   . GLU   B 1 148 ? 13.380  -24.995 -47.514 1.00 20.44 ?  148 GLU   B O   1 
ATOM   2931 C CB  . GLU   B 1 148 ? 13.182  -23.610 -50.600 1.00 21.56 ?  148 GLU   B CB  1 
ATOM   2932 C CG  . GLU   B 1 148 ? 12.551  -24.992 -50.697 1.00 22.78 ?  148 GLU   B CG  1 
ATOM   2933 C CD  . GLU   B 1 148 ? 12.104  -25.517 -52.056 1.00 28.58 ?  148 GLU   B CD  1 
ATOM   2934 O OE1 . GLU   B 1 148 ? 12.251  -24.807 -53.050 1.00 30.34 ?  148 GLU   B OE1 1 
ATOM   2935 O OE2 . GLU   B 1 148 ? 11.591  -26.671 -52.081 1.00 32.23 ?  148 GLU   B OE2 1 
ATOM   2936 N N   . ALA   B 1 149 ? 15.390  -24.454 -48.338 1.00 19.37 ?  149 ALA   B N   1 
ATOM   2937 C CA  . ALA   B 1 149 ? 16.032  -25.528 -47.608 1.00 20.10 ?  149 ALA   B CA  1 
ATOM   2938 C C   . ALA   B 1 149 ? 15.843  -25.350 -46.103 1.00 18.52 ?  149 ALA   B C   1 
ATOM   2939 O O   . ALA   B 1 149 ? 15.647  -26.331 -45.390 1.00 17.66 ?  149 ALA   B O   1 
ATOM   2940 C CB  . ALA   B 1 149 ? 17.500  -25.646 -47.976 1.00 20.66 ?  149 ALA   B CB  1 
ATOM   2941 N N   . LEU   B 1 150 ? 16.000  -24.102 -45.641 1.00 19.20 ?  150 LEU   B N   1 
ATOM   2942 C CA  . LEU   B 1 150 ? 15.876  -23.793 -44.228 1.00 19.04 ?  150 LEU   B CA  1 
ATOM   2943 C C   . LEU   B 1 150 ? 14.420  -23.975 -43.803 1.00 17.97 ?  150 LEU   B C   1 
ATOM   2944 O O   . LEU   B 1 150 ? 14.171  -24.428 -42.705 1.00 16.23 ?  150 LEU   B O   1 
ATOM   2945 C CB  . LEU   B 1 150 ? 16.355  -22.362 -43.995 1.00 19.04 ?  150 LEU   B CB  1 
ATOM   2946 C CG  . LEU   B 1 150 ? 17.876  -22.181 -43.912 1.00 21.96 ?  150 LEU   B CG  1 
ATOM   2947 C CD1 . LEU   B 1 150 ? 18.182  -20.704 -43.854 1.00 23.53 ?  150 LEU   B CD1 1 
ATOM   2948 C CD2 . LEU   B 1 150 ? 18.391  -22.821 -42.653 1.00 24.14 ?  150 LEU   B CD2 1 
ATOM   2949 N N   . ILE   B 1 151 ? 13.461  -23.597 -44.652 1.00 16.84 ?  151 ILE   B N   1 
ATOM   2950 C CA  . ILE   B 1 151 ? 12.056  -23.744 -44.274 1.00 16.17 ?  151 ILE   B CA  1 
ATOM   2951 C C   . ILE   B 1 151 ? 11.758  -25.229 -44.097 1.00 15.39 ?  151 ILE   B C   1 
ATOM   2952 O O   . ILE   B 1 151 ? 11.069  -25.620 -43.165 1.00 15.70 ?  151 ILE   B O   1 
ATOM   2953 C CB  . ILE   B 1 151 ? 11.141  -23.067 -45.302 1.00 15.93 ?  151 ILE   B CB  1 
ATOM   2954 C CG1 . ILE   B 1 151 ? 11.282  -21.546 -45.206 1.00 15.23 ?  151 ILE   B CG1 1 
ATOM   2955 C CG2 . ILE   B 1 151 ? 9.698   -23.553 -45.146 1.00 16.72 ?  151 ILE   B CG2 1 
ATOM   2956 C CD1 . ILE   B 1 151 ? 10.692  -20.778 -46.371 1.00 15.66 ?  151 ILE   B CD1 1 
ATOM   2957 N N   . ARG   B 1 152 ? 12.242  -26.058 -45.040 1.00 15.25 ?  152 ARG   B N   1 
ATOM   2958 C CA  . ARG   B 1 152 ? 12.053  -27.486 -44.909 1.00 16.75 ?  152 ARG   B CA  1 
ATOM   2959 C C   . ARG   B 1 152 ? 12.709  -27.975 -43.625 1.00 17.23 ?  152 ARG   B C   1 
ATOM   2960 O O   . ARG   B 1 152 ? 12.131  -28.803 -42.924 1.00 17.45 ?  152 ARG   B O   1 
ATOM   2961 C CB  . ARG   B 1 152 ? 12.603  -28.270 -46.104 1.00 18.22 ?  152 ARG   B CB  1 
ATOM   2962 C CG  . ARG   B 1 152 ? 11.801  -28.059 -47.374 1.00 21.08 ?  152 ARG   B CG  1 
ATOM   2963 C CD  . ARG   B 1 152 ? 12.233  -28.966 -48.504 1.00 23.24 ?  152 ARG   B CD  1 
ATOM   2964 N NE  . ARG   B 1 152 ? 11.589  -28.516 -49.745 1.00 27.67 ?  152 ARG   B NE  1 
ATOM   2965 C CZ  . ARG   B 1 152 ? 10.336  -28.796 -50.127 1.00 31.01 ?  152 ARG   B CZ  1 
ATOM   2966 N NH1 . ARG   B 1 152 ? 9.573   -29.610 -49.405 1.00 31.42 ?  152 ARG   B NH1 1 
ATOM   2967 N NH2 . ARG   B 1 152 ? 9.859   -28.260 -51.244 1.00 29.80 ?  152 ARG   B NH2 1 
ATOM   2968 N N   . LYS   B 1 153 ? 13.933  -27.504 -43.370 1.00 17.64 ?  153 LYS   B N   1 
ATOM   2969 C CA  . LYS   B 1 153 ? 14.726  -28.019 -42.270 1.00 19.13 ?  153 LYS   B CA  1 
ATOM   2970 C C   . LYS   B 1 153 ? 14.013  -27.715 -40.959 1.00 17.09 ?  153 LYS   B C   1 
ATOM   2971 O O   . LYS   B 1 153 ? 13.863  -28.607 -40.124 1.00 17.01 ?  153 LYS   B O   1 
ATOM   2972 C CB  . LYS   B 1 153 ? 16.155  -27.459 -42.207 1.00 20.86 ?  153 LYS   B CB  1 
ATOM   2973 C CG  . LYS   B 1 153 ? 17.036  -28.084 -41.108 1.00 23.12 ?  153 LYS   B CG  1 
ATOM   2974 C CD  . LYS   B 1 153 ? 17.083  -29.614 -41.107 1.00 25.18 ?  153 LYS   B CD  1 
ATOM   2975 C CE  . LYS   B 1 153 ? 17.725  -30.158 -42.345 1.00 29.52 ?  153 LYS   B CE  1 
ATOM   2976 N NZ  . LYS   B 1 153 ? 17.842  -31.629 -42.326 1.00 31.76 ?  153 LYS   B NZ  1 
ATOM   2977 N N   . ALA   B 1 154 ? 13.553  -26.462 -40.814 1.00 16.51 ?  154 ALA   B N   1 
ATOM   2978 C CA  . ALA   B 1 154 ? 12.870  -26.054 -39.593 1.00 14.79 ?  154 ALA   B CA  1 
ATOM   2979 C C   . ALA   B 1 154 ? 11.611  -26.903 -39.392 1.00 15.02 ?  154 ALA   B C   1 
ATOM   2980 O O   . ALA   B 1 154 ? 11.247  -27.262 -38.269 1.00 14.19 ?  154 ALA   B O   1 
ATOM   2981 C CB  . ALA   B 1 154 ? 12.541  -24.584 -39.642 1.00 14.09 ?  154 ALA   B CB  1 
ATOM   2982 N N   . SER   B 1 155 ? 10.872  -27.112 -40.485 1.00 14.75 ?  155 SER   B N   1 
ATOM   2983 C CA  . SER   B 1 155 ? 9.654   -27.899 -40.447 1.00 14.95 ?  155 SER   B CA  1 
ATOM   2984 C C   . SER   B 1 155 ? 9.930   -29.346 -40.052 1.00 14.58 ?  155 SER   B C   1 
ATOM   2985 O O   . SER   B 1 155 ? 9.260   -29.896 -39.192 1.00 15.26 ?  155 SER   B O   1 
ATOM   2986 C CB  . SER   B 1 155 ? 8.926   -27.863 -41.767 1.00 15.35 ?  155 SER   B CB  1 
ATOM   2987 O OG  . SER   B 1 155 ? 8.656   -26.545 -42.195 1.00 14.87 ?  155 SER   B OG  1 
ATOM   2988 N N   . GLU   B 1 156 ? 10.970  -29.942 -40.618 1.00 14.77 ?  156 GLU   B N   1 
ATOM   2989 C CA  . GLU   B 1 156 ? 11.316  -31.317 -40.305 1.00 16.81 ?  156 GLU   B CA  1 
ATOM   2990 C C   . GLU   B 1 156 ? 11.706  -31.465 -38.829 1.00 16.22 ?  156 GLU   B C   1 
ATOM   2991 O O   . GLU   B 1 156 ? 11.320  -32.441 -38.187 1.00 16.93 ?  156 GLU   B O   1 
ATOM   2992 C CB  . GLU   B 1 156 ? 12.515  -31.650 -41.191 1.00 20.22 ?  156 GLU   B CB  1 
ATOM   2993 C CG  . GLU   B 1 156 ? 13.213  -32.963 -40.866 1.00 23.79 ?  156 GLU   B CG  1 
ATOM   2994 C CD  . GLU   B 1 156 ? 14.649  -32.968 -41.377 1.00 30.46 ?  156 GLU   B CD  1 
ATOM   2995 O OE1 . GLU   B 1 156 ? 14.895  -32.409 -42.470 1.00 29.86 ?  156 GLU   B OE1 1 
ATOM   2996 O OE2 . GLU   B 1 156 ? 15.526  -33.460 -40.639 1.00 40.93 ?  156 GLU   B OE2 1 
ATOM   2997 N N   . ILE   B 1 157 ? 12.554  -30.554 -38.343 1.00 15.82 ?  157 ILE   B N   1 
ATOM   2998 C CA  . ILE   B 1 157 ? 13.057  -30.627 -36.974 1.00 16.12 ?  157 ILE   B CA  1 
ATOM   2999 C C   . ILE   B 1 157 ? 11.858  -30.523 -36.025 1.00 17.38 ?  157 ILE   B C   1 
ATOM   3000 O O   . ILE   B 1 157 ? 11.735  -31.301 -35.080 1.00 17.13 ?  157 ILE   B O   1 
ATOM   3001 C CB  . ILE   B 1 157 ? 14.091  -29.516 -36.716 1.00 17.01 ?  157 ILE   B CB  1 
ATOM   3002 C CG1 . ILE   B 1 157 ? 15.400  -29.768 -37.507 1.00 16.63 ?  157 ILE   B CG1 1 
ATOM   3003 C CG2 . ILE   B 1 157 ? 14.376  -29.366 -35.217 1.00 16.98 ?  157 ILE   B CG2 1 
ATOM   3004 C CD1 . ILE   B 1 157 ? 16.347  -28.584 -37.495 1.00 15.96 ?  157 ILE   B CD1 1 
ATOM   3005 N N   . SER   B 1 158 ? 11.023  -29.498 -36.258 1.00 17.41 ?  158 SER   B N   1 
ATOM   3006 C CA  . SER   B 1 158 ? 9.808   -29.304 -35.482 1.00 16.21 ?  158 SER   B CA  1 
ATOM   3007 C C   . SER   B 1 158 ? 8.987   -30.578 -35.438 1.00 16.93 ?  158 SER   B C   1 
ATOM   3008 O O   . SER   B 1 158 ? 8.546   -30.973 -34.381 1.00 17.41 ?  158 SER   B O   1 
ATOM   3009 C CB  . SER   B 1 158 ? 9.023   -28.158 -36.006 1.00 16.41 ?  158 SER   B CB  1 
ATOM   3010 O OG  . SER   B 1 158 ? 9.806   -26.974 -35.894 1.00 15.83 ?  158 SER   B OG  1 
ATOM   3011 N N   . ILE   B 1 159 ? 8.670   -31.151 -36.596 1.00 16.09 ?  159 ILE   B N   1 
ATOM   3012 C CA  . ILE   B 1 159 ? 7.876   -32.363 -36.630 1.00 16.57 ?  159 ILE   B CA  1 
ATOM   3013 C C   . ILE   B 1 159 ? 8.527   -33.512 -35.842 1.00 17.85 ?  159 ILE   B C   1 
ATOM   3014 O O   . ILE   B 1 159 ? 7.868   -34.178 -35.023 1.00 17.76 ?  159 ILE   B O   1 
ATOM   3015 C CB  . ILE   B 1 159 ? 7.598   -32.743 -38.086 1.00 16.19 ?  159 ILE   B CB  1 
ATOM   3016 C CG1 . ILE   B 1 159 ? 6.600   -31.802 -38.685 1.00 16.35 ?  159 ILE   B CG1 1 
ATOM   3017 C CG2 . ILE   B 1 159 ? 7.153   -34.211 -38.193 1.00 16.20 ?  159 ILE   B CG2 1 
ATOM   3018 C CD1 . ILE   B 1 159 ? 6.537   -31.895 -40.207 1.00 17.29 ?  159 ILE   B CD1 1 
ATOM   3019 N N   . LYS   B 1 160 ? 9.815   -33.753 -36.085 1.00 17.59 ?  160 LYS   B N   1 
ATOM   3020 C CA  . LYS   B 1 160 ? 10.529  -34.814 -35.387 1.00 19.03 ?  160 LYS   B CA  1 
ATOM   3021 C C   . LYS   B 1 160 ? 10.485  -34.607 -33.872 1.00 18.78 ?  160 LYS   B C   1 
ATOM   3022 O O   . LYS   B 1 160 ? 10.414  -35.576 -33.131 1.00 19.45 ?  160 LYS   B O   1 
ATOM   3023 C CB  . LYS   B 1 160 ? 11.988  -34.908 -35.812 1.00 20.64 ?  160 LYS   B CB  1 
ATOM   3024 C CG  . LYS   B 1 160 ? 12.137  -35.378 -37.232 1.00 23.35 ?  160 LYS   B CG  1 
ATOM   3025 C CD  . LYS   B 1 160 ? 13.598  -35.524 -37.630 1.00 27.39 ?  160 LYS   B CD  1 
ATOM   3026 C CE  . LYS   B 1 160 ? 13.735  -36.383 -38.861 1.00 31.93 ?  160 LYS   B CE  1 
ATOM   3027 N NZ  . LYS   B 1 160 ? 14.988  -36.116 -39.586 1.00 35.28 ?  160 LYS   B NZ  1 
ATOM   3028 N N   . ALA   B 1 161 ? 10.513  -33.342 -33.432 1.00 18.36 ?  161 ALA   B N   1 
ATOM   3029 C CA  . ALA   B 1 161 ? 10.467  -33.045 -32.002 1.00 19.17 ?  161 ALA   B CA  1 
ATOM   3030 C C   . ALA   B 1 161 ? 9.051   -33.126 -31.414 1.00 21.00 ?  161 ALA   B C   1 
ATOM   3031 O O   . ALA   B 1 161 ? 8.913   -32.978 -30.185 1.00 19.48 ?  161 ALA   B O   1 
ATOM   3032 C CB  . ALA   B 1 161 ? 11.116  -31.695 -31.751 1.00 18.91 ?  161 ALA   B CB  1 
ATOM   3033 N N   . GLY   B 1 162 ? 8.012   -33.300 -32.250 1.00 18.43 ?  162 GLY   B N   1 
ATOM   3034 C CA  . GLY   B 1 162 ? 6.650   -33.606 -31.807 1.00 19.57 ?  162 GLY   B CA  1 
ATOM   3035 C C   . GLY   B 1 162 ? 5.673   -32.437 -31.986 1.00 17.54 ?  162 GLY   B C   1 
ATOM   3036 O O   . GLY   B 1 162 ? 4.610   -32.397 -31.388 1.00 18.48 ?  162 GLY   B O   1 
ATOM   3037 N N   . ALA   B 1 163 ? 6.004   -31.468 -32.821 1.00 16.40 ?  163 ALA   B N   1 
ATOM   3038 C CA  . ALA   B 1 163 ? 5.049   -30.429 -33.202 1.00 16.57 ?  163 ALA   B CA  1 
ATOM   3039 C C   . ALA   B 1 163 ? 3.707   -31.038 -33.622 1.00 15.91 ?  163 ALA   B C   1 
ATOM   3040 O O   . ALA   B 1 163 ? 3.660   -31.969 -34.420 1.00 17.84 ?  163 ALA   B O   1 
ATOM   3041 C CB  . ALA   B 1 163 ? 5.659   -29.573 -34.288 1.00 16.89 ?  163 ALA   B CB  1 
ATOM   3042 N N   . ASP   B 1 164 ? 2.603   -30.498 -33.104 1.00 15.33 ?  164 ASP   B N   1 
ATOM   3043 C CA  . ASP   B 1 164 ? 1.258   -30.891 -33.508 1.00 16.15 ?  164 ASP   B CA  1 
ATOM   3044 C C   . ASP   B 1 164 ? 0.817   -30.098 -34.737 1.00 14.96 ?  164 ASP   B C   1 
ATOM   3045 O O   . ASP   B 1 164 ? -0.104  -30.508 -35.436 1.00 17.29 ?  164 ASP   B O   1 
ATOM   3046 C CB  . ASP   B 1 164 ? 0.267   -30.746 -32.369 1.00 15.43 ?  164 ASP   B CB  1 
ATOM   3047 C CG  . ASP   B 1 164 ? 0.663   -31.553 -31.136 1.00 16.72 ?  164 ASP   B CG  1 
ATOM   3048 O OD1 . ASP   B 1 164 ? 0.904   -32.772 -31.311 1.00 17.01 ?  164 ASP   B OD1 1 
ATOM   3049 O OD2 . ASP   B 1 164 ? 0.723   -30.995 -29.995 1.00 16.46 ?  164 ASP   B OD2 1 
ATOM   3050 N N   . PHE   B 1 165 ? 1.375   -28.897 -34.886 1.00 15.10 ?  165 PHE   B N   1 
ATOM   3051 C CA  . PHE   B 1 165 ? 1.211   -28.038 -36.048 1.00 15.02 ?  165 PHE   B CA  1 
ATOM   3052 C C   . PHE   B 1 165 ? 2.533   -27.361 -36.363 1.00 14.38 ?  165 PHE   B C   1 
ATOM   3053 O O   . PHE   B 1 165 ? 3.310   -27.064 -35.428 1.00 13.14 ?  165 PHE   B O   1 
ATOM   3054 C CB  . PHE   B 1 165 ? 0.293   -26.860 -35.716 1.00 16.48 ?  165 PHE   B CB  1 
ATOM   3055 C CG  . PHE   B 1 165 ? -1.195  -27.047 -35.982 1.00 18.45 ?  165 PHE   B CG  1 
ATOM   3056 C CD1 . PHE   B 1 165 ? -2.000  -27.713 -35.065 1.00 21.32 ?  165 PHE   B CD1 1 
ATOM   3057 C CD2 . PHE   B 1 165 ? -1.774  -26.546 -37.134 1.00 19.73 ?  165 PHE   B CD2 1 
ATOM   3058 C CE1 . PHE   B 1 165 ? -3.364  -27.887 -35.322 1.00 21.33 ?  165 PHE   B CE1 1 
ATOM   3059 C CE2 . PHE   B 1 165 ? -3.131  -26.709 -37.370 1.00 19.84 ?  165 PHE   B CE2 1 
ATOM   3060 C CZ  . PHE   B 1 165 ? -3.916  -27.387 -36.458 1.00 20.29 ?  165 PHE   B CZ  1 
ATOM   3061 N N   . ILE   B 1 166 ? 2.748   -27.098 -37.650 1.00 14.14 ?  166 ILE   B N   1 
ATOM   3062 C CA  . ILE   B 1 166 ? 3.753   -26.132 -38.038 1.00 14.10 ?  166 ILE   B CA  1 
ATOM   3063 C C   . ILE   B 1 166 ? 3.066   -24.913 -38.647 1.00 14.68 ?  166 ILE   B C   1 
ATOM   3064 O O   . ILE   B 1 166 ? 2.105   -25.019 -39.411 1.00 14.92 ?  166 ILE   B O   1 
ATOM   3065 C CB  . ILE   B 1 166 ? 4.851   -26.752 -38.920 1.00 14.59 ?  166 ILE   B CB  1 
ATOM   3066 C CG1 . ILE   B 1 166 ? 4.288   -27.383 -40.192 1.00 15.81 ?  166 ILE   B CG1 1 
ATOM   3067 C CG2 . ILE   B 1 166 ? 5.724   -27.697 -38.090 1.00 16.59 ?  166 ILE   B CG2 1 
ATOM   3068 C CD1 . ILE   B 1 166 ? 5.389   -27.854 -41.134 1.00 16.46 ?  166 ILE   B CD1 1 
ATOM   3069 N N   . LYS   B 1 167 ? 3.601   -23.753 -38.284 1.00 14.45 ?  167 LYS   B N   1 
ATOM   3070 C CA  . LYS   B 1 167 ? 2.995   -22.467 -38.546 1.00 15.41 ?  167 LYS   B CA  1 
ATOM   3071 C C   . LYS   B 1 167 ? 4.003   -21.542 -39.233 1.00 15.06 ?  167 LYS   B C   1 
ATOM   3072 O O   . LYS   B 1 167 ? 5.168   -21.498 -38.847 1.00 14.68 ?  167 LYS   B O   1 
ATOM   3073 C CB  . LYS   B 1 167 ? 2.552   -21.997 -37.139 1.00 15.91 ?  167 LYS   B CB  1 
ATOM   3074 C CG  . LYS   B 1 167 ? 2.088   -20.573 -37.120 1.00 17.07 ?  167 LYS   B CG  1 
ATOM   3075 C CD  . LYS   B 1 167 ? 1.444   -20.298 -35.758 1.00 16.55 ?  167 LYS   B CD  1 
ATOM   3076 C CE  . LYS   B 1 167 ? 1.179   -18.872 -35.740 1.00 18.03 ?  167 LYS   B CE  1 
ATOM   3077 N NZ  . LYS   B 1 167 ? 0.504   -18.394 -34.541 1.00 21.53 ?  167 LYS   B NZ  1 
ATOM   3078 N N   . THR   B 1 168 ? 3.547   -20.712 -40.186 1.00 14.72 ?  168 THR   B N   1 
ATOM   3079 C CA  . THR   B 1 168 ? 4.484   -19.962 -41.015 1.00 15.01 ?  168 THR   B CA  1 
ATOM   3080 C C   . THR   B 1 168 ? 5.228   -18.916 -40.190 1.00 15.74 ?  168 THR   B C   1 
ATOM   3081 O O   . THR   B 1 168 ? 6.431   -18.785 -40.340 1.00 13.83 ?  168 THR   B O   1 
ATOM   3082 C CB  . THR   B 1 168 ? 3.789   -19.342 -42.233 1.00 16.17 ?  168 THR   B CB  1 
ATOM   3083 O OG1 . THR   B 1 168 ? 2.827   -18.356 -41.808 1.00 15.69 ?  168 THR   B OG1 1 
ATOM   3084 C CG2 . THR   B 1 168 ? 3.171   -20.441 -43.085 1.00 16.38 ?  168 THR   B CG2 1 
ATOM   3085 N N   . SER   B 1 169 ? 4.515   -18.165 -39.347 1.00 13.39 ?  169 SER   B N   1 
ATOM   3086 C CA  . SER   B 1 169 ? 4.901   -16.799 -39.039 1.00 14.22 ?  169 SER   B CA  1 
ATOM   3087 C C   . SER   B 1 169 ? 4.381   -16.328 -37.686 1.00 14.31 ?  169 SER   B C   1 
ATOM   3088 O O   . SER   B 1 169 ? 3.363   -16.809 -37.234 1.00 14.67 ?  169 SER   B O   1 
ATOM   3089 C CB  . SER   B 1 169 ? 4.457   -15.814 -40.079 1.00 15.55 ?  169 SER   B CB  1 
ATOM   3090 O OG  . SER   B 1 169 ? 4.875   -16.211 -41.376 1.00 14.45 ?  169 SER   B OG  1 
ATOM   3091 N N   . THR   B 1 170 ? 5.064   -15.321 -37.107 1.00 15.95 ?  170 THR   B N   1 
ATOM   3092 C CA  . THR   B 1 170 ? 4.570   -14.649 -35.897 1.00 16.10 ?  170 THR   B CA  1 
ATOM   3093 C C   . THR   B 1 170 ? 3.600   -13.530 -36.235 1.00 16.92 ?  170 THR   B C   1 
ATOM   3094 O O   . THR   B 1 170 ? 2.815   -13.113 -35.377 1.00 16.86 ?  170 THR   B O   1 
ATOM   3095 C CB  . THR   B 1 170 ? 5.720   -14.015 -35.121 1.00 16.28 ?  170 THR   B CB  1 
ATOM   3096 O OG1 . THR   B 1 170 ? 6.318   -13.063 -36.024 1.00 15.70 ?  170 THR   B OG1 1 
ATOM   3097 C CG2 . THR   B 1 170 ? 6.679   -15.065 -34.609 1.00 16.03 ?  170 THR   B CG2 1 
ATOM   3098 N N   . GLY   B 1 171 ? 3.663   -13.019 -37.474 1.00 16.45 ?  171 GLY   B N   1 
ATOM   3099 C CA  . GLY   B 1 171 ? 2.888   -11.846 -37.843 1.00 17.93 ?  171 GLY   B CA  1 
ATOM   3100 C C   . GLY   B 1 171 ? 3.573   -10.562 -37.403 1.00 19.23 ?  171 GLY   B C   1 
ATOM   3101 O O   . GLY   B 1 171 ? 3.011   -9.479  -37.569 1.00 23.12 ?  171 GLY   B O   1 
ATOM   3102 N N   . ARG   B 1 172 ? 4.792   -10.677 -36.863 1.00 20.54 ?  172 ARG   B N   1 
ATOM   3103 C CA  . ARG   B 1 172 ? 5.461   -9.519  -36.274 1.00 23.12 ?  172 ARG   B CA  1 
ATOM   3104 C C   . ARG   B 1 172 ? 6.719   -9.126  -37.041 1.00 21.91 ?  172 ARG   B C   1 
ATOM   3105 O O   . ARG   B 1 172 ? 7.439   -8.274  -36.550 1.00 24.41 ?  172 ARG   B O   1 
ATOM   3106 C CB  . ARG   B 1 172 ? 5.852   -9.757  -34.809 1.00 22.99 ?  172 ARG   B CB  1 
ATOM   3107 C CG  . ARG   B 1 172 ? 4.669   -9.920  -33.880 1.00 26.20 ?  172 ARG   B CG  1 
ATOM   3108 C CD  . ARG   B 1 172 ? 3.668   -8.793  -33.977 1.00 31.74 ?  172 ARG   B CD  1 
ATOM   3109 N NE  . ARG   B 1 172 ? 2.590   -9.019  -33.026 1.00 38.47 ?  172 ARG   B NE  1 
ATOM   3110 C CZ  . ARG   B 1 172 ? 2.710   -8.915  -31.700 1.00 46.07 ?  172 ARG   B CZ  1 
ATOM   3111 N NH1 . ARG   B 1 172 ? 3.825   -8.447  -31.159 1.00 46.94 ?  172 ARG   B NH1 1 
ATOM   3112 N NH2 . ARG   B 1 172 ? 1.699   -9.265  -30.918 1.00 51.67 ?  172 ARG   B NH2 1 
ATOM   3113 N N   . VAL   B 1 173 ? 6.993   -9.767  -38.182 1.00 20.48 ?  173 VAL   B N   1 
ATOM   3114 C CA  . VAL   B 1 173 ? 8.142   -9.426  -39.007 1.00 20.91 ?  173 VAL   B CA  1 
ATOM   3115 C C   . VAL   B 1 173 ? 7.614   -8.915  -40.347 1.00 22.05 ?  173 VAL   B C   1 
ATOM   3116 O O   . VAL   B 1 173 ? 6.438   -9.035  -40.612 1.00 22.71 ?  173 VAL   B O   1 
ATOM   3117 C CB  . VAL   B 1 173 ? 9.094   -10.622 -39.188 1.00 20.51 ?  173 VAL   B CB  1 
ATOM   3118 C CG1 . VAL   B 1 173 ? 9.745   -11.026 -37.861 1.00 21.76 ?  173 VAL   B CG1 1 
ATOM   3119 C CG2 . VAL   B 1 173 ? 8.389   -11.819 -39.802 1.00 20.16 ?  173 VAL   B CG2 1 
ATOM   3120 N N   . ALA   B 1 174 ? 8.502   -8.434  -41.221 1.00 22.81 ?  174 ALA   B N   1 
ATOM   3121 C CA  . ALA   B 1 174 ? 8.123   -7.797  -42.475 1.00 24.17 ?  174 ALA   B CA  1 
ATOM   3122 C C   . ALA   B 1 174 ? 7.368   -8.759  -43.386 1.00 22.96 ?  174 ALA   B C   1 
ATOM   3123 O O   . ALA   B 1 174 ? 6.430   -8.352  -44.067 1.00 23.33 ?  174 ALA   B O   1 
ATOM   3124 C CB  . ALA   B 1 174 ? 9.373   -7.289  -43.182 1.00 25.25 ?  174 ALA   B CB  1 
ATOM   3125 N N   . VAL   B 1 175 ? 7.807   -10.025 -43.432 1.00 21.14 ?  175 VAL   B N   1 
ATOM   3126 C CA  . VAL   B 1 175 ? 7.241   -10.962 -44.378 1.00 19.61 ?  175 VAL   B CA  1 
ATOM   3127 C C   . VAL   B 1 175 ? 6.701   -12.148 -43.601 1.00 18.56 ?  175 VAL   B C   1 
ATOM   3128 O O   . VAL   B 1 175 ? 7.465   -12.764 -42.865 1.00 16.81 ?  175 VAL   B O   1 
ATOM   3129 C CB  . VAL   B 1 175 ? 8.242   -11.404 -45.451 1.00 20.53 ?  175 VAL   B CB  1 
ATOM   3130 C CG1 . VAL   B 1 175 ? 7.593   -12.364 -46.448 1.00 20.34 ?  175 VAL   B CG1 1 
ATOM   3131 C CG2 . VAL   B 1 175 ? 8.795   -10.192 -46.195 1.00 22.13 ?  175 VAL   B CG2 1 
ATOM   3132 N N   . ASN   B 1 176 ? 5.395   -12.422 -43.778 1.00 17.62 ?  176 ASN   B N   1 
ATOM   3133 C CA  . ASN   B 1 176 ? 4.719   -13.513 -43.091 1.00 17.36 ?  176 ASN   B CA  1 
ATOM   3134 C C   . ASN   B 1 176 ? 4.489   -14.589 -44.146 1.00 16.60 ?  176 ASN   B C   1 
ATOM   3135 O O   . ASN   B 1 176 ? 5.383   -14.864 -44.930 1.00 16.28 ?  176 ASN   B O   1 
ATOM   3136 C CB  . ASN   B 1 176 ? 3.556   -12.946 -42.279 1.00 18.36 ?  176 ASN   B CB  1 
ATOM   3137 C CG  . ASN   B 1 176 ? 4.078   -11.931 -41.282 1.00 20.97 ?  176 ASN   B CG  1 
ATOM   3138 O OD1 . ASN   B 1 176 ? 3.986   -10.702 -41.468 1.00 25.70 ?  176 ASN   B OD1 1 
ATOM   3139 N ND2 . ASN   B 1 176 ? 4.738   -12.427 -40.272 1.00 17.82 ?  176 ASN   B ND2 1 
ATOM   3140 N N   . ALA   B 1 177 ? 3.310   -15.185 -44.197 1.00 16.08 ?  177 ALA   B N   1 
ATOM   3141 C CA  . ALA   B 1 177 ? 3.091   -16.333 -45.056 1.00 15.74 ?  177 ALA   B CA  1 
ATOM   3142 C C   . ALA   B 1 177 ? 3.136   -15.873 -46.510 1.00 14.61 ?  177 ALA   B C   1 
ATOM   3143 O O   . ALA   B 1 177 ? 2.812   -14.728 -46.789 1.00 15.59 ?  177 ALA   B O   1 
ATOM   3144 C CB  . ALA   B 1 177 ? 1.760   -16.968 -44.803 1.00 15.34 ?  177 ALA   B CB  1 
ATOM   3145 N N   . THR   B 1 178 ? 3.599   -16.770 -47.357 1.00 14.76 ?  178 THR   B N   1 
ATOM   3146 C CA  . THR   B 1 178 ? 3.351   -16.690 -48.799 1.00 14.84 ?  178 THR   B CA  1 
ATOM   3147 C C   . THR   B 1 178 ? 2.789   -18.024 -49.234 1.00 14.55 ?  178 THR   B C   1 
ATOM   3148 O O   . THR   B 1 178 ? 3.009   -19.030 -48.602 1.00 15.17 ?  178 THR   B O   1 
ATOM   3149 C CB  . THR   B 1 178 ? 4.634   -16.363 -49.577 1.00 14.85 ?  178 THR   B CB  1 
ATOM   3150 O OG1 . THR   B 1 178 ? 5.486   -17.500 -49.507 1.00 16.29 ?  178 THR   B OG1 1 
ATOM   3151 C CG2 . THR   B 1 178 ? 5.356   -15.159 -49.001 1.00 15.34 ?  178 THR   B CG2 1 
ATOM   3152 N N   . PRO   B 1 179 ? 2.166   -18.109 -50.443 1.00 15.57 ?  179 PRO   B N   1 
ATOM   3153 C CA  . PRO   B 1 179 ? 1.716   -19.408 -50.927 1.00 15.75 ?  179 PRO   B CA  1 
ATOM   3154 C C   . PRO   B 1 179 ? 2.820   -20.436 -51.089 1.00 15.70 ?  179 PRO   B C   1 
ATOM   3155 O O   . PRO   B 1 179 ? 2.634   -21.632 -50.868 1.00 16.75 ?  179 PRO   B O   1 
ATOM   3156 C CB  . PRO   B 1 179 ? 1.058   -19.078 -52.276 1.00 16.51 ?  179 PRO   B CB  1 
ATOM   3157 C CG  . PRO   B 1 179 ? 0.742   -17.598 -52.164 1.00 17.95 ?  179 PRO   B CG  1 
ATOM   3158 C CD  . PRO   B 1 179 ? 1.716   -16.948 -51.215 1.00 16.32 ?  179 PRO   B CD  1 
ATOM   3159 N N   . GLU   B 1 180 ? 3.985   -19.965 -51.520 1.00 16.39 ?  180 GLU   B N   1 
ATOM   3160 C CA  . GLU   B 1 180 ? 5.114   -20.848 -51.683 1.00 17.14 ?  180 GLU   B CA  1 
ATOM   3161 C C   . GLU   B 1 180 ? 5.613   -21.375 -50.334 1.00 16.04 ?  180 GLU   B C   1 
ATOM   3162 O O   . GLU   B 1 180 ? 5.886   -22.558 -50.236 1.00 15.01 ?  180 GLU   B O   1 
ATOM   3163 C CB  . GLU   B 1 180 ? 6.214   -20.074 -52.404 1.00 18.86 ?  180 GLU   B CB  1 
ATOM   3164 C CG  . GLU   B 1 180 ? 7.409   -20.946 -52.694 1.00 23.37 ?  180 GLU   B CG  1 
ATOM   3165 C CD  . GLU   B 1 180 ? 7.140   -21.908 -53.837 1.00 28.48 ?  180 GLU   B CD  1 
ATOM   3166 O OE1 . GLU   B 1 180 ? 8.174   -22.600 -54.055 1.00 33.56 ?  180 GLU   B OE1 1 
ATOM   3167 O OE2 . GLU   B 1 180 ? 6.014   -21.966 -54.448 1.00 29.02 ?  180 GLU   B OE2 1 
ATOM   3168 N N   . SER   B 1 181 ? 5.741   -20.531 -49.315 1.00 15.43 ?  181 SER   B N   1 
ATOM   3169 C CA  . SER   B 1 181 ? 6.176   -21.076 -48.029 1.00 16.07 ?  181 SER   B CA  1 
ATOM   3170 C C   . SER   B 1 181 ? 5.126   -22.024 -47.418 1.00 15.84 ?  181 SER   B C   1 
ATOM   3171 O O   . SER   B 1 181 ? 5.470   -23.066 -46.858 1.00 15.64 ?  181 SER   B O   1 
ATOM   3172 C CB  . SER   B 1 181 ? 6.632   -19.999 -47.106 1.00 17.61 ?  181 SER   B CB  1 
ATOM   3173 O OG  . SER   B 1 181 ? 5.559   -19.139 -46.822 1.00 20.75 ?  181 SER   B OG  1 
ATOM   3174 N N   . ALA   B 1 182 ? 3.831   -21.765 -47.658 1.00 15.09 ?  182 ALA   B N   1 
ATOM   3175 C CA  . ALA   B 1 182 ? 2.767   -22.699 -47.290 1.00 16.25 ?  182 ALA   B CA  1 
ATOM   3176 C C   . ALA   B 1 182 ? 2.899   -24.049 -47.998 1.00 17.00 ?  182 ALA   B C   1 
ATOM   3177 O O   . ALA   B 1 182 ? 2.811   -25.097 -47.374 1.00 16.29 ?  182 ALA   B O   1 
ATOM   3178 C CB  . ALA   B 1 182 ? 1.414   -22.032 -47.582 1.00 16.66 ?  182 ALA   B CB  1 
ATOM   3179 N N   . ARG   B 1 183 ? 3.165   -24.019 -49.315 1.00 17.23 ?  183 ARG   B N   1 
ATOM   3180 C CA  . ARG   B 1 183 ? 3.313   -25.240 -50.081 1.00 19.33 ?  183 ARG   B CA  1 
ATOM   3181 C C   . ARG   B 1 183 ? 4.501   -26.048 -49.587 1.00 16.38 ?  183 ARG   B C   1 
ATOM   3182 O O   . ARG   B 1 183 ? 4.414   -27.271 -49.438 1.00 15.57 ?  183 ARG   B O   1 
ATOM   3183 C CB  . ARG   B 1 183 ? 3.500   -24.946 -51.579 1.00 22.25 ?  183 ARG   B CB  1 
ATOM   3184 C CG  . ARG   B 1 183 ? 3.762   -26.191 -52.409 1.00 25.17 ?  183 ARG   B CG  1 
ATOM   3185 C CD  . ARG   B 1 183 ? 4.091   -25.841 -53.857 1.00 29.60 ?  183 ARG   B CD  1 
ATOM   3186 N NE  . ARG   B 1 183 ? 5.337   -25.066 -53.959 1.00 36.61 ?  183 ARG   B NE  1 
ATOM   3187 C CZ  . ARG   B 1 183 ? 6.577   -25.571 -53.932 1.00 38.79 ?  183 ARG   B CZ  1 
ATOM   3188 N NH1 . ARG   B 1 183 ? 6.781   -26.874 -53.877 1.00 40.45 ?  183 ARG   B NH1 1 
ATOM   3189 N NH2 . ARG   B 1 183 ? 7.618   -24.762 -53.980 1.00 42.15 ?  183 ARG   B NH2 1 
ATOM   3190 N N   . ILE   B 1 184 ? 5.620   -25.370 -49.344 1.00 16.39 ?  184 ILE   B N   1 
ATOM   3191 C CA  . ILE   B 1 184 ? 6.826   -26.047 -48.888 1.00 16.21 ?  184 ILE   B CA  1 
ATOM   3192 C C   . ILE   B 1 184 ? 6.542   -26.756 -47.570 1.00 15.99 ?  184 ILE   B C   1 
ATOM   3193 O O   . ILE   B 1 184 ? 6.856   -27.938 -47.422 1.00 15.53 ?  184 ILE   B O   1 
ATOM   3194 C CB  . ILE   B 1 184 ? 7.999   -25.066 -48.781 1.00 16.77 ?  184 ILE   B CB  1 
ATOM   3195 C CG1 . ILE   B 1 184 ? 8.400   -24.513 -50.133 1.00 17.38 ?  184 ILE   B CG1 1 
ATOM   3196 C CG2 . ILE   B 1 184 ? 9.174   -25.716 -48.041 1.00 15.88 ?  184 ILE   B CG2 1 
ATOM   3197 C CD1 . ILE   B 1 184 ? 9.235   -23.253 -50.064 1.00 17.72 ?  184 ILE   B CD1 1 
ATOM   3198 N N   . MET   B 1 185 ? 5.881   -26.049 -46.635 1.00 15.27 ?  185 MET   B N   1 
ATOM   3199 C CA  . MET   B 1 185 ? 5.638   -26.622 -45.316 1.00 15.04 ?  185 MET   B CA  1 
ATOM   3200 C C   . MET   B 1 185 ? 4.673   -27.795 -45.418 1.00 14.72 ?  185 MET   B C   1 
ATOM   3201 O O   . MET   B 1 185 ? 4.897   -28.817 -44.793 1.00 13.94 ?  185 MET   B O   1 
ATOM   3202 C CB  . MET   B 1 185 ? 5.155   -25.542 -44.351 1.00 14.71 ?  185 MET   B CB  1 
ATOM   3203 C CG  . MET   B 1 185 ? 6.191   -24.490 -44.098 1.00 15.38 ?  185 MET   B CG  1 
ATOM   3204 S SD  . MET   B 1 185 ? 5.698   -23.212 -42.926 1.00 15.60 ?  185 MET   B SD  1 
ATOM   3205 C CE  . MET   B 1 185 ? 5.433   -24.083 -41.370 1.00 15.59 ?  185 MET   B CE  1 
ATOM   3206 N N   . MET   B 1 186 ? 3.625   -27.681 -46.250 1.00 16.26 ?  186 MET   B N   1 
ATOM   3207 C CA  . MET   B 1 186 ? 2.702   -28.796 -46.366 1.00 16.45 ?  186 MET   B CA  1 
ATOM   3208 C C   . MET   B 1 186 ? 3.352   -29.968 -47.082 1.00 17.08 ?  186 MET   B C   1 
ATOM   3209 O O   . MET   B 1 186 ? 3.046   -31.136 -46.801 1.00 17.66 ?  186 MET   B O   1 
ATOM   3210 C CB  . MET   B 1 186 ? 1.396   -28.344 -46.994 1.00 17.30 ?  186 MET   B CB  1 
ATOM   3211 C CG  . MET   B 1 186 ? 0.540   -27.559 -46.011 1.00 18.97 ?  186 MET   B CG  1 
ATOM   3212 S SD  . MET   B 1 186 ? -1.083  -27.150 -46.691 1.00 19.89 ?  186 MET   B SD  1 
ATOM   3213 C CE  . MET   B 1 186 ? -0.822  -25.486 -47.311 1.00 19.87 ?  186 MET   B CE  1 
ATOM   3214 N N   . GLU   B 1 187 ? 4.290   -29.673 -47.977 1.00 18.40 ?  187 GLU   B N   1 
ATOM   3215 C CA  . GLU   B 1 187 ? 5.019   -30.735 -48.650 1.00 21.00 ?  187 GLU   B CA  1 
ATOM   3216 C C   . GLU   B 1 187 ? 5.854   -31.512 -47.644 1.00 19.08 ?  187 GLU   B C   1 
ATOM   3217 O O   . GLU   B 1 187 ? 5.967   -32.727 -47.730 1.00 19.06 ?  187 GLU   B O   1 
ATOM   3218 C CB  . GLU   B 1 187 ? 5.927   -30.221 -49.767 1.00 19.72 ?  187 GLU   B CB  1 
ATOM   3219 C CG  . GLU   B 1 187 ? 5.154   -29.833 -51.010 1.00 23.05 ?  187 GLU   B CG  1 
ATOM   3220 C CD  . GLU   B 1 187 ? 6.047   -29.293 -52.103 1.00 26.13 ?  187 GLU   B CD  1 
ATOM   3221 O OE1 . GLU   B 1 187 ? 7.283   -29.252 -51.948 1.00 29.12 ?  187 GLU   B OE1 1 
ATOM   3222 O OE2 . GLU   B 1 187 ? 5.473   -28.989 -53.159 1.00 26.76 ?  187 GLU   B OE2 1 
ATOM   3223 N N   . VAL   B 1 188 ? 6.442   -30.818 -46.670 1.00 17.94 ?  188 VAL   B N   1 
ATOM   3224 C CA  . VAL   B 1 188 ? 7.174   -31.538 -45.643 1.00 19.07 ?  188 VAL   B CA  1 
ATOM   3225 C C   . VAL   B 1 188 ? 6.266   -32.470 -44.847 1.00 18.78 ?  188 VAL   B C   1 
ATOM   3226 O O   . VAL   B 1 188 ? 6.624   -33.617 -44.600 1.00 18.53 ?  188 VAL   B O   1 
ATOM   3227 C CB  . VAL   B 1 188 ? 7.921   -30.573 -44.706 1.00 19.25 ?  188 VAL   B CB  1 
ATOM   3228 C CG1 . VAL   B 1 188 ? 8.556   -31.327 -43.554 1.00 18.40 ?  188 VAL   B CG1 1 
ATOM   3229 C CG2 . VAL   B 1 188 ? 8.943   -29.735 -45.454 1.00 19.54 ?  188 VAL   B CG2 1 
ATOM   3230 N N   . ILE   B 1 189 ? 5.077   -32.006 -44.471 1.00 19.18 ?  189 ILE   B N   1 
ATOM   3231 C CA  . ILE   B 1 189 ? 4.097   -32.845 -43.777 1.00 19.66 ?  189 ILE   B CA  1 
ATOM   3232 C C   . ILE   B 1 189 ? 3.795   -34.105 -44.589 1.00 19.62 ?  189 ILE   B C   1 
ATOM   3233 O O   . ILE   B 1 189 ? 3.834   -35.225 -44.077 1.00 18.16 ?  189 ILE   B O   1 
ATOM   3234 C CB  . ILE   B 1 189 ? 2.813   -32.047 -43.472 1.00 18.96 ?  189 ILE   B CB  1 
ATOM   3235 C CG1 . ILE   B 1 189 ? 3.082   -30.964 -42.444 1.00 19.32 ?  189 ILE   B CG1 1 
ATOM   3236 C CG2 . ILE   B 1 189 ? 1.663   -32.947 -43.019 1.00 21.28 ?  189 ILE   B CG2 1 
ATOM   3237 C CD1 . ILE   B 1 189 ? 1.936   -30.012 -42.201 1.00 18.40 ?  189 ILE   B CD1 1 
ATOM   3238 N N   . ARG   B 1 190 ? 3.544   -33.923 -45.885 1.00 20.93 ?  190 ARG   B N   1 
ATOM   3239 C CA  . ARG   B 1 190 ? 3.233   -35.050 -46.736 1.00 22.77 ?  190 ARG   B CA  1 
ATOM   3240 C C   . ARG   B 1 190 ? 4.435   -35.980 -46.861 1.00 23.32 ?  190 ARG   B C   1 
ATOM   3241 O O   . ARG   B 1 190 ? 4.306   -37.194 -46.706 1.00 23.89 ?  190 ARG   B O   1 
ATOM   3242 C CB  . ARG   B 1 190 ? 2.846   -34.561 -48.132 1.00 23.53 ?  190 ARG   B CB  1 
ATOM   3243 C CG  . ARG   B 1 190 ? 2.389   -35.677 -49.068 1.00 25.01 ?  190 ARG   B CG  1 
ATOM   3244 C CD  . ARG   B 1 190 ? 2.409   -35.173 -50.499 1.00 27.83 ?  190 ARG   B CD  1 
ATOM   3245 N NE  . ARG   B 1 190 ? 3.769   -34.736 -50.854 1.00 32.64 ?  190 ARG   B NE  1 
ATOM   3246 C CZ  . ARG   B 1 190 ? 4.083   -34.057 -51.949 1.00 32.94 ?  190 ARG   B CZ  1 
ATOM   3247 N NH1 . ARG   B 1 190 ? 3.157   -33.798 -52.845 1.00 33.52 ?  190 ARG   B NH1 1 
ATOM   3248 N NH2 . ARG   B 1 190 ? 5.324   -33.641 -52.147 1.00 32.32 ?  190 ARG   B NH2 1 
ATOM   3249 N N   . ASP   B 1 191 ? 5.591   -35.407 -47.213 1.00 23.56 ?  191 ASP   B N   1 
ATOM   3250 C CA  . ASP   B 1 191 ? 6.774   -36.195 -47.486 1.00 24.83 ?  191 ASP   B CA  1 
ATOM   3251 C C   . ASP   B 1 191 ? 7.170   -37.004 -46.256 1.00 26.14 ?  191 ASP   B C   1 
ATOM   3252 O O   . ASP   B 1 191 ? 7.677   -38.118 -46.401 1.00 23.09 ?  191 ASP   B O   1 
ATOM   3253 C CB  . ASP   B 1 191 ? 7.939   -35.322 -47.901 1.00 26.09 ?  191 ASP   B CB  1 
ATOM   3254 C CG  . ASP   B 1 191 ? 7.814   -34.705 -49.281 1.00 27.72 ?  191 ASP   B CG  1 
ATOM   3255 O OD1 . ASP   B 1 191 ? 6.910   -35.128 -50.014 1.00 30.09 ?  191 ASP   B OD1 1 
ATOM   3256 O OD2 . ASP   B 1 191 ? 8.566   -33.752 -49.544 1.00 29.46 ?  191 ASP   B OD2 1 
ATOM   3257 N N   . MET   B 1 192 ? 6.946   -36.449 -45.051 1.00 22.86 ?  192 MET   B N   1 
ATOM   3258 C CA  . MET   B 1 192 ? 7.308   -37.158 -43.848 1.00 22.92 ?  192 MET   B CA  1 
ATOM   3259 C C   . MET   B 1 192 ? 6.245   -38.171 -43.426 1.00 23.44 ?  192 MET   B C   1 
ATOM   3260 O O   . MET   B 1 192 ? 6.451   -38.893 -42.463 1.00 24.01 ?  192 MET   B O   1 
ATOM   3261 C CB  . MET   B 1 192 ? 7.586   -36.151 -42.732 1.00 22.68 ?  192 MET   B CB  1 
ATOM   3262 C CG  . MET   B 1 192 ? 8.812   -35.314 -42.984 1.00 22.05 ?  192 MET   B CG  1 
ATOM   3263 S SD  . MET   B 1 192 ? 9.244   -34.299 -41.556 1.00 22.15 ?  192 MET   B SD  1 
ATOM   3264 C CE  . MET   B 1 192 ? 9.881   -35.481 -40.366 1.00 25.82 ?  192 MET   B CE  1 
ATOM   3265 N N   . GLY   B 1 193 ? 5.104   -38.189 -44.125 1.00 23.05 ?  193 GLY   B N   1 
ATOM   3266 C CA  . GLY   B 1 193 ? 4.024   -39.105 -43.858 1.00 23.65 ?  193 GLY   B CA  1 
ATOM   3267 C C   . GLY   B 1 193 ? 3.298   -38.779 -42.555 1.00 23.65 ?  193 GLY   B C   1 
ATOM   3268 O O   . GLY   B 1 193 ? 2.762   -39.707 -41.951 1.00 23.24 ?  193 GLY   B O   1 
ATOM   3269 N N   . VAL   B 1 194 ? 3.292   -37.496 -42.122 1.00 20.34 ?  194 VAL   B N   1 
ATOM   3270 C CA  . VAL   B 1 194 ? 2.752   -37.161 -40.801 1.00 19.80 ?  194 VAL   B CA  1 
ATOM   3271 C C   . VAL   B 1 194 ? 1.442   -36.387 -40.929 1.00 20.32 ?  194 VAL   B C   1 
ATOM   3272 O O   . VAL   B 1 194 ? 1.044   -35.707 -39.990 1.00 21.13 ?  194 VAL   B O   1 
ATOM   3273 C CB  . VAL   B 1 194 ? 3.761   -36.429 -39.902 1.00 19.63 ?  194 VAL   B CB  1 
ATOM   3274 C CG1 . VAL   B 1 194 ? 4.992   -37.292 -39.643 1.00 20.64 ?  194 VAL   B CG1 1 
ATOM   3275 C CG2 . VAL   B 1 194 ? 4.179   -35.083 -40.474 1.00 20.07 ?  194 VAL   B CG2 1 
ATOM   3276 N N   . GLU   B 1 195 ? 0.750   -36.482 -42.080 1.00 19.41 ?  195 GLU   B N   1 
ATOM   3277 C CA  . GLU   B 1 195 ? -0.445  -35.691 -42.310 1.00 20.78 ?  195 GLU   B CA  1 
ATOM   3278 C C   . GLU   B 1 195 ? -1.562  -36.004 -41.310 1.00 21.70 ?  195 GLU   B C   1 
ATOM   3279 O O   . GLU   B 1 195 ? -2.398  -35.144 -41.049 1.00 22.24 ?  195 GLU   B O   1 
ATOM   3280 C CB  . GLU   B 1 195 ? -0.939  -35.790 -43.758 1.00 22.19 ?  195 GLU   B CB  1 
ATOM   3281 C CG  . GLU   B 1 195 ? -1.611  -37.117 -44.093 1.00 24.72 ?  195 GLU   B CG  1 
ATOM   3282 C CD  . GLU   B 1 195 ? -0.682  -38.291 -44.273 1.00 29.04 ?  195 GLU   B CD  1 
ATOM   3283 O OE1 . GLU   B 1 195 ? 0.568   -38.106 -44.305 1.00 31.08 ?  195 GLU   B OE1 1 
ATOM   3284 O OE2 . GLU   B 1 195 ? -1.245  -39.396 -44.441 1.00 34.54 ?  195 GLU   B OE2 1 
ATOM   3285 N N   . LYS   B 1 196 ? -1.552  -37.179 -40.685 1.00 23.14 ?  196 LYS   B N   1 
ATOM   3286 C CA  . LYS   B 1 196 ? -2.566  -37.483 -39.689 1.00 25.06 ?  196 LYS   B CA  1 
ATOM   3287 C C   . LYS   B 1 196 ? -2.328  -36.707 -38.404 1.00 24.02 ?  196 LYS   B C   1 
ATOM   3288 O O   . LYS   B 1 196 ? -3.297  -36.229 -37.840 1.00 23.15 ?  196 LYS   B O   1 
ATOM   3289 C CB  . LYS   B 1 196 ? -2.745  -38.983 -39.444 1.00 28.87 ?  196 LYS   B CB  1 
ATOM   3290 C CG  . LYS   B 1 196 ? -3.587  -39.537 -40.557 1.00 35.27 ?  196 LYS   B CG  1 
ATOM   3291 C CD  . LYS   B 1 196 ? -3.920  -41.009 -40.416 1.00 45.54 ?  196 LYS   B CD  1 
ATOM   3292 C CE  . LYS   B 1 196 ? -4.751  -41.432 -41.583 1.00 48.72 ?  196 LYS   B CE  1 
ATOM   3293 N NZ  . LYS   B 1 196 ? -4.722  -42.893 -41.646 1.00 54.15 ?  196 LYS   B NZ  1 
ATOM   3294 N N   . SER   B 1 197 ? -1.071  -36.520 -37.998 1.00 22.30 ?  197 SER   B N   1 
ATOM   3295 C CA  . SER   B 1 197 ? -0.754  -36.012 -36.670 1.00 21.58 ?  197 SER   B CA  1 
ATOM   3296 C C   . SER   B 1 197 ? -0.282  -34.552 -36.678 1.00 19.98 ?  197 SER   B C   1 
ATOM   3297 O O   . SER   B 1 197 ? -0.117  -33.954 -35.619 1.00 19.39 ?  197 SER   B O   1 
ATOM   3298 C CB  . SER   B 1 197 ? 0.251   -36.912 -36.003 1.00 22.45 ?  197 SER   B CB  1 
ATOM   3299 O OG  . SER   B 1 197 ? 1.421   -37.056 -36.809 1.00 23.83 ?  197 SER   B OG  1 
ATOM   3300 N N   . VAL   B 1 198 ? 0.002   -33.963 -37.852 1.00 19.03 ?  198 VAL   B N   1 
ATOM   3301 C CA  . VAL   B 1 198 ? 0.548   -32.620 -37.877 1.00 17.41 ?  198 VAL   B CA  1 
ATOM   3302 C C   . VAL   B 1 198 ? -0.278  -31.725 -38.785 1.00 16.86 ?  198 VAL   B C   1 
ATOM   3303 O O   . VAL   B 1 198 ? -0.460  -32.055 -39.958 1.00 16.69 ?  198 VAL   B O   1 
ATOM   3304 C CB  . VAL   B 1 198 ? 2.010   -32.647 -38.364 1.00 16.27 ?  198 VAL   B CB  1 
ATOM   3305 C CG1 . VAL   B 1 198 ? 2.607   -31.252 -38.443 1.00 15.09 ?  198 VAL   B CG1 1 
ATOM   3306 C CG2 . VAL   B 1 198 ? 2.867   -33.583 -37.513 1.00 17.03 ?  198 VAL   B CG2 1 
ATOM   3307 N N   . GLY   B 1 199 ? -0.682  -30.572 -38.256 1.00 16.09 ?  199 GLY   B N   1 
ATOM   3308 C CA  . GLY   B 1 199 ? -1.417  -29.569 -39.008 1.00 16.21 ?  199 GLY   B CA  1 
ATOM   3309 C C   . GLY   B 1 199 ? -0.518  -28.448 -39.539 1.00 16.22 ?  199 GLY   B C   1 
ATOM   3310 O O   . GLY   B 1 199 ? 0.654   -28.349 -39.162 1.00 13.82 ?  199 GLY   B O   1 
ATOM   3311 N N   . PHE   B 1 200 ? -1.126  -27.561 -40.326 1.00 13.65 ?  200 PHE   B N   1 
ATOM   3312 C CA  . PHE   B 1 200 ? -0.463  -26.398 -40.849 1.00 13.70 ?  200 PHE   B CA  1 
ATOM   3313 C C   . PHE   B 1 200 ? -1.252  -25.152 -40.528 1.00 14.05 ?  200 PHE   B C   1 
ATOM   3314 O O   . PHE   B 1 200 ? -2.493  -25.146 -40.668 1.00 14.80 ?  200 PHE   B O   1 
ATOM   3315 C CB  . PHE   B 1 200 ? -0.376  -26.619 -42.357 1.00 14.40 ?  200 PHE   B CB  1 
ATOM   3316 C CG  . PHE   B 1 200 ? 0.087   -25.370 -43.081 1.00 15.66 ?  200 PHE   B CG  1 
ATOM   3317 C CD1 . PHE   B 1 200 ? 1.410   -24.949 -42.963 1.00 16.55 ?  200 PHE   B CD1 1 
ATOM   3318 C CD2 . PHE   B 1 200 ? -0.799  -24.560 -43.767 1.00 17.15 ?  200 PHE   B CD2 1 
ATOM   3319 C CE1 . PHE   B 1 200 ? 1.837   -23.786 -43.546 1.00 17.37 ?  200 PHE   B CE1 1 
ATOM   3320 C CE2 . PHE   B 1 200 ? -0.350  -23.391 -44.358 1.00 18.44 ?  200 PHE   B CE2 1 
ATOM   3321 C CZ  . PHE   B 1 200 ? 0.974   -23.008 -44.246 1.00 18.59 ?  200 PHE   B CZ  1 
ATOM   3322 N N   . LYS   B 1 201 ? -0.545  -24.082 -40.167 1.00 13.52 ?  201 LYS   B N   1 
ATOM   3323 C CA  A LYS   B 1 201 ? -1.214  -22.834 -39.891 0.50 13.96 ?  201 LYS   B CA  1 
ATOM   3324 C CA  B LYS   B 1 201 ? -1.210  -22.833 -39.882 0.50 13.46 ?  201 LYS   B CA  1 
ATOM   3325 C C   . LYS   B 1 201 ? -0.528  -21.715 -40.650 1.00 13.84 ?  201 LYS   B C   1 
ATOM   3326 O O   . LYS   B 1 201 ? 0.681   -21.575 -40.571 1.00 13.52 ?  201 LYS   B O   1 
ATOM   3327 C CB  A LYS   B 1 201 ? -1.261  -22.495 -38.397 0.50 13.72 ?  201 LYS   B CB  1 
ATOM   3328 C CB  B LYS   B 1 201 ? -1.249  -22.562 -38.372 0.50 12.56 ?  201 LYS   B CB  1 
ATOM   3329 C CG  A LYS   B 1 201 ? -1.799  -21.100 -38.148 0.50 14.32 ?  201 LYS   B CG  1 
ATOM   3330 C CG  B LYS   B 1 201 ? -1.868  -21.225 -37.994 0.50 12.44 ?  201 LYS   B CG  1 
ATOM   3331 C CD  A LYS   B 1 201 ? -2.089  -20.786 -36.697 0.50 14.65 ?  201 LYS   B CD  1 
ATOM   3332 C CD  B LYS   B 1 201 ? -2.089  -21.035 -36.503 0.50 12.12 ?  201 LYS   B CD  1 
ATOM   3333 C CE  A LYS   B 1 201 ? -2.862  -19.504 -36.570 0.50 16.28 ?  201 LYS   B CE  1 
ATOM   3334 C CE  B LYS   B 1 201 ? -2.311  -19.582 -36.159 0.50 12.36 ?  201 LYS   B CE  1 
ATOM   3335 N NZ  A LYS   B 1 201 ? -2.159  -18.243 -36.317 0.50 16.44 ?  201 LYS   B NZ  1 
ATOM   3336 N NZ  B LYS   B 1 201 ? -2.432  -19.291 -34.721 0.50 12.35 ?  201 LYS   B NZ  1 
ATOM   3337 N N   . VAL   B 1 202 ? -1.340  -20.965 -41.415 1.00 14.72 ?  202 VAL   B N   1 
ATOM   3338 C CA  . VAL   B 1 202 ? -0.879  -19.784 -42.130 1.00 16.43 ?  202 VAL   B CA  1 
ATOM   3339 C C   . VAL   B 1 202 ? -1.165  -18.550 -41.278 1.00 17.61 ?  202 VAL   B C   1 
ATOM   3340 O O   . VAL   B 1 202 ? -2.289  -18.347 -40.821 1.00 17.81 ?  202 VAL   B O   1 
ATOM   3341 C CB  . VAL   B 1 202 ? -1.531  -19.662 -43.534 1.00 19.61 ?  202 VAL   B CB  1 
ATOM   3342 C CG1 . VAL   B 1 202 ? -2.973  -20.044 -43.522 1.00 23.66 ?  202 VAL   B CG1 1 
ATOM   3343 C CG2 . VAL   B 1 202 ? -1.400  -18.266 -44.131 1.00 20.36 ?  202 VAL   B CG2 1 
ATOM   3344 N N   . THR   B 1 203 ? -0.126  -17.750 -41.032 1.00 16.15 ?  203 THR   B N   1 
ATOM   3345 C CA  . THR   B 1 203 ? -0.229  -16.485 -40.353 1.00 16.05 ?  203 THR   B CA  1 
ATOM   3346 C C   . THR   B 1 203 ? 0.251   -15.386 -41.287 1.00 17.48 ?  203 THR   B C   1 
ATOM   3347 O O   . THR   B 1 203 ? 1.367   -15.444 -41.784 1.00 16.95 ?  203 THR   B O   1 
ATOM   3348 C CB  . THR   B 1 203 ? 0.592   -16.523 -39.062 1.00 17.85 ?  203 THR   B CB  1 
ATOM   3349 O OG1 . THR   B 1 203 ? -0.053  -17.462 -38.212 1.00 19.11 ?  203 THR   B OG1 1 
ATOM   3350 C CG2 . THR   B 1 203 ? 0.636   -15.183 -38.343 1.00 17.31 ?  203 THR   B CG2 1 
ATOM   3351 N N   . GLY   B 1 204 ? -0.584  -14.384 -41.496 1.00 18.52 ?  204 GLY   B N   1 
ATOM   3352 C CA  . GLY   B 1 204 ? -0.273  -13.265 -42.365 1.00 21.21 ?  204 GLY   B CA  1 
ATOM   3353 C C   . GLY   B 1 204 ? -0.451  -13.681 -43.826 1.00 25.13 ?  204 GLY   B C   1 
ATOM   3354 O O   . GLY   B 1 204 ? -0.697  -14.854 -44.116 1.00 22.22 ?  204 GLY   B O   1 
ATOM   3355 N N   . GLY   B 1 205 ? -0.373  -12.678 -44.709 1.00 31.87 ?  205 GLY   B N   1 
ATOM   3356 C CA  . GLY   B 1 205 ? -0.474  -12.833 -46.152 1.00 34.04 ?  205 GLY   B CA  1 
ATOM   3357 C C   . GLY   B 1 205 ? -1.822  -13.394 -46.619 1.00 37.24 ?  205 GLY   B C   1 
ATOM   3358 O O   . GLY   B 1 205 ? -1.932  -13.847 -47.760 1.00 43.35 ?  205 GLY   B O   1 
ATOM   3359 N N   . VAL   B 1 206 ? -2.855  -13.362 -45.761 1.00 36.39 ?  206 VAL   B N   1 
ATOM   3360 C CA  . VAL   B 1 206 ? -4.182  -13.780 -46.168 1.00 38.27 ?  206 VAL   B CA  1 
ATOM   3361 C C   . VAL   B 1 206 ? -5.157  -12.656 -45.814 1.00 40.99 ?  206 VAL   B C   1 
ATOM   3362 O O   . VAL   B 1 206 ? -5.859  -12.701 -44.801 1.00 41.04 ?  206 VAL   B O   1 
ATOM   3363 C CB  . VAL   B 1 206 ? -4.611  -15.118 -45.544 1.00 39.02 ?  206 VAL   B CB  1 
ATOM   3364 C CG1 . VAL   B 1 206 ? -5.855  -15.681 -46.225 1.00 39.41 ?  206 VAL   B CG1 1 
ATOM   3365 C CG2 . VAL   B 1 206 ? -3.482  -16.130 -45.563 1.00 42.66 ?  206 VAL   B CG2 1 
ATOM   3366 N N   . SER   B 1 207 ? -5.191  -11.641 -46.673 1.00 37.35 ?  207 SER   B N   1 
ATOM   3367 C CA  . SER   B 1 207 ? -5.974  -10.445 -46.406 1.00 42.50 ?  207 SER   B CA  1 
ATOM   3368 C C   . SER   B 1 207 ? -7.442  -10.655 -46.783 1.00 38.51 ?  207 SER   B C   1 
ATOM   3369 O O   . SER   B 1 207 ? -8.312  -10.053 -46.166 1.00 40.95 ?  207 SER   B O   1 
ATOM   3370 C CB  . SER   B 1 207 ? -5.405  -9.273  -47.140 1.00 43.07 ?  207 SER   B CB  1 
ATOM   3371 O OG  . SER   B 1 207 ? -4.019  -9.478  -47.347 1.00 50.52 ?  207 SER   B OG  1 
ATOM   3372 N N   . THR   B 1 208 ? -7.700  -11.502 -47.796 1.00 34.68 ?  208 THR   B N   1 
ATOM   3373 C CA  . THR   B 1 208 ? -8.992  -11.566 -48.456 1.00 32.64 ?  208 THR   B CA  1 
ATOM   3374 C C   . THR   B 1 208 ? -9.510  -12.997 -48.464 1.00 31.00 ?  208 THR   B C   1 
ATOM   3375 O O   . THR   B 1 208 ? -8.753  -13.950 -48.374 1.00 29.54 ?  208 THR   B O   1 
ATOM   3376 C CB  . THR   B 1 208 ? -8.872  -11.043 -49.892 1.00 33.87 ?  208 THR   B CB  1 
ATOM   3377 O OG1 . THR   B 1 208 ? -8.149  -11.986 -50.690 1.00 33.86 ?  208 THR   B OG1 1 
ATOM   3378 C CG2 . THR   B 1 208 ? -8.224  -9.673  -49.950 1.00 34.28 ?  208 THR   B CG2 1 
ATOM   3379 N N   . ALA   B 1 209 ? -10.824 -13.131 -48.626 1.00 30.36 ?  209 ALA   B N   1 
ATOM   3380 C CA  . ALA   B 1 209 ? -11.442 -14.412 -48.910 1.00 30.01 ?  209 ALA   B CA  1 
ATOM   3381 C C   . ALA   B 1 209 ? -10.765 -15.141 -50.080 1.00 30.40 ?  209 ALA   B C   1 
ATOM   3382 O O   . ALA   B 1 209 ? -10.606 -16.354 -50.019 1.00 28.37 ?  209 ALA   B O   1 
ATOM   3383 C CB  . ALA   B 1 209 ? -12.916 -14.204 -49.198 1.00 30.75 ?  209 ALA   B CB  1 
ATOM   3384 N N   . GLU   B 1 210 ? -10.457 -14.436 -51.185 1.00 31.97 ?  210 GLU   B N   1 
ATOM   3385 C CA  . GLU   B 1 210 ? -9.784  -15.058 -52.323 1.00 29.42 ?  210 GLU   B CA  1 
ATOM   3386 C C   . GLU   B 1 210 ? -8.434  -15.668 -51.915 1.00 25.79 ?  210 GLU   B C   1 
ATOM   3387 O O   . GLU   B 1 210 ? -8.107  -16.800 -52.266 1.00 27.76 ?  210 GLU   B O   1 
ATOM   3388 C CB  . GLU   B 1 210 ? -9.615  -14.051 -53.463 1.00 31.92 ?  210 GLU   B CB  1 
ATOM   3389 C CG  . GLU   B 1 210 ? -10.955 -13.605 -54.060 1.00 33.95 ?  210 GLU   B CG  1 
ATOM   3390 C CD  . GLU   B 1 210 ? -11.694 -12.494 -53.320 1.00 37.70 ?  210 GLU   B CD  1 
ATOM   3391 O OE1 . GLU   B 1 210 ? -11.283 -11.993 -52.234 1.00 36.52 ?  210 GLU   B OE1 1 
ATOM   3392 O OE2 . GLU   B 1 210 ? -12.759 -12.141 -53.856 1.00 42.50 ?  210 GLU   B OE2 1 
ATOM   3393 N N   . ASP   B 1 211 ? -7.626  -14.898 -51.205 1.00 25.45 ?  211 ASP   B N   1 
ATOM   3394 C CA  . ASP   B 1 211 ? -6.414  -15.428 -50.598 1.00 27.14 ?  211 ASP   B CA  1 
ATOM   3395 C C   . ASP   B 1 211 ? -6.696  -16.725 -49.837 1.00 24.06 ?  211 ASP   B C   1 
ATOM   3396 O O   . ASP   B 1 211 ? -6.014  -17.744 -50.013 1.00 20.58 ?  211 ASP   B O   1 
ATOM   3397 C CB  . ASP   B 1 211 ? -5.771  -14.404 -49.678 1.00 27.58 ?  211 ASP   B CB  1 
ATOM   3398 C CG  . ASP   B 1 211 ? -5.274  -13.139 -50.370 1.00 29.38 ?  211 ASP   B CG  1 
ATOM   3399 O OD1 . ASP   B 1 211 ? -4.846  -13.256 -51.538 1.00 29.35 ?  211 ASP   B OD1 1 
ATOM   3400 O OD2 . ASP   B 1 211 ? -5.304  -12.057 -49.730 1.00 31.08 ?  211 ASP   B OD2 1 
ATOM   3401 N N   . ALA   B 1 212 ? -7.727  -16.716 -48.988 1.00 22.76 ?  212 ALA   B N   1 
ATOM   3402 C CA  . ALA   B 1 212 ? -7.895  -17.884 -48.148 1.00 21.49 ?  212 ALA   B CA  1 
ATOM   3403 C C   . ALA   B 1 212 ? -8.202  -19.095 -49.008 1.00 21.00 ?  212 ALA   B C   1 
ATOM   3404 O O   . ALA   B 1 212 ? -7.788  -20.217 -48.714 1.00 20.25 ?  212 ALA   B O   1 
ATOM   3405 C CB  . ALA   B 1 212 ? -8.989  -17.649 -47.132 1.00 22.62 ?  212 ALA   B CB  1 
ATOM   3406 N N   . GLN   B 1 213 ? -9.022  -18.876 -50.038 1.00 23.12 ?  213 GLN   B N   1 
ATOM   3407 C CA  . GLN   B 1 213 ? -9.397  -19.955 -50.923 1.00 24.71 ?  213 GLN   B CA  1 
ATOM   3408 C C   . GLN   B 1 213 ? -8.157  -20.585 -51.561 1.00 22.08 ?  213 GLN   B C   1 
ATOM   3409 O O   . GLN   B 1 213 ? -8.070  -21.803 -51.713 1.00 21.79 ?  213 GLN   B O   1 
ATOM   3410 C CB  . GLN   B 1 213 ? -10.348 -19.387 -51.977 1.00 25.71 ?  213 GLN   B CB  1 
ATOM   3411 C CG  . GLN   B 1 213 ? -10.826 -20.434 -52.962 1.00 29.80 ?  213 GLN   B CG  1 
ATOM   3412 C CD  . GLN   B 1 213 ? -11.755 -19.819 -53.988 1.00 31.68 ?  213 GLN   B CD  1 
ATOM   3413 O OE1 . GLN   B 1 213 ? -11.433 -18.812 -54.625 1.00 36.69 ?  213 GLN   B OE1 1 
ATOM   3414 N NE2 . GLN   B 1 213 ? -12.960 -20.338 -54.055 1.00 31.70 ?  213 GLN   B NE2 1 
ATOM   3415 N N   . LYS   B 1 214 ? -7.194  -19.740 -51.908 1.00 26.13 ?  214 LYS   B N   1 
ATOM   3416 C CA  . LYS   B 1 214 ? -5.976  -20.182 -52.580 1.00 26.15 ?  214 LYS   B CA  1 
ATOM   3417 C C   . LYS   B 1 214 ? -5.144  -21.020 -51.612 1.00 24.77 ?  214 LYS   B C   1 
ATOM   3418 O O   . LYS   B 1 214 ? -4.671  -22.091 -51.977 1.00 25.12 ?  214 LYS   B O   1 
ATOM   3419 C CB  . LYS   B 1 214 ? -5.245  -18.942 -53.101 1.00 30.45 ?  214 LYS   B CB  1 
ATOM   3420 C CG  . LYS   B 1 214 ? -3.961  -19.257 -53.821 1.00 37.72 ?  214 LYS   B CG  1 
ATOM   3421 C CD  . LYS   B 1 214 ? -3.326  -18.064 -54.523 1.00 43.86 ?  214 LYS   B CD  1 
ATOM   3422 C CE  . LYS   B 1 214 ? -2.622  -17.052 -53.646 1.00 43.58 ?  214 LYS   B CE  1 
ATOM   3423 N NZ  . LYS   B 1 214 ? -1.737  -16.212 -54.478 1.00 45.99 ?  214 LYS   B NZ  1 
ATOM   3424 N N   . TYR   B 1 215 ? -5.013  -20.560 -50.348 1.00 22.20 ?  215 TYR   B N   1 
ATOM   3425 C CA  . TYR   B 1 215 ? -4.255  -21.329 -49.367 1.00 19.23 ?  215 TYR   B CA  1 
ATOM   3426 C C   . TYR   B 1 215 ? -4.934  -22.664 -49.097 1.00 18.38 ?  215 TYR   B C   1 
ATOM   3427 O O   . TYR   B 1 215 ? -4.258  -23.663 -48.908 1.00 19.57 ?  215 TYR   B O   1 
ATOM   3428 C CB  . TYR   B 1 215 ? -4.028  -20.565 -48.072 1.00 19.12 ?  215 TYR   B CB  1 
ATOM   3429 C CG  . TYR   B 1 215 ? -2.925  -19.529 -48.124 1.00 19.84 ?  215 TYR   B CG  1 
ATOM   3430 C CD1 . TYR   B 1 215 ? -1.608  -19.875 -47.872 1.00 19.74 ?  215 TYR   B CD1 1 
ATOM   3431 C CD2 . TYR   B 1 215 ? -3.189  -18.208 -48.448 1.00 23.47 ?  215 TYR   B CD2 1 
ATOM   3432 C CE1 . TYR   B 1 215 ? -0.596  -18.928 -47.894 1.00 19.18 ?  215 TYR   B CE1 1 
ATOM   3433 C CE2 . TYR   B 1 215 ? -2.174  -17.261 -48.522 1.00 24.58 ?  215 TYR   B CE2 1 
ATOM   3434 C CZ  . TYR   B 1 215 ? -0.874  -17.617 -48.215 1.00 20.29 ?  215 TYR   B CZ  1 
ATOM   3435 O OH  . TYR   B 1 215 ? 0.125   -16.683 -48.286 1.00 20.58 ?  215 TYR   B OH  1 
ATOM   3436 N N   . LEU   B 1 216 ? -6.271  -22.685 -48.985 1.00 18.08 ?  216 LEU   B N   1 
ATOM   3437 C CA  . LEU   B 1 216 ? -6.971  -23.949 -48.760 1.00 18.91 ?  216 LEU   B CA  1 
ATOM   3438 C C   . LEU   B 1 216 ? -6.811  -24.929 -49.917 1.00 20.87 ?  216 LEU   B C   1 
ATOM   3439 O O   . LEU   B 1 216 ? -6.733  -26.140 -49.700 1.00 21.66 ?  216 LEU   B O   1 
ATOM   3440 C CB  . LEU   B 1 216 ? -8.451  -23.732 -48.472 1.00 20.50 ?  216 LEU   B CB  1 
ATOM   3441 C CG  . LEU   B 1 216 ? -8.734  -23.412 -47.008 1.00 22.40 ?  216 LEU   B CG  1 
ATOM   3442 C CD1 . LEU   B 1 216 ? -10.139 -22.936 -46.825 1.00 24.34 ?  216 LEU   B CD1 1 
ATOM   3443 C CD2 . LEU   B 1 216 ? -8.450  -24.618 -46.110 1.00 22.59 ?  216 LEU   B CD2 1 
ATOM   3444 N N   . ALA   B 1 217 ? -6.792  -24.384 -51.142 1.00 22.87 ?  217 ALA   B N   1 
ATOM   3445 C CA  . ALA   B 1 217 ? -6.630  -25.167 -52.359 1.00 23.47 ?  217 ALA   B CA  1 
ATOM   3446 C C   . ALA   B 1 217 ? -5.298  -25.905 -52.355 1.00 22.27 ?  217 ALA   B C   1 
ATOM   3447 O O   . ALA   B 1 217 ? -5.237  -27.047 -52.792 1.00 23.67 ?  217 ALA   B O   1 
ATOM   3448 C CB  . ALA   B 1 217 ? -6.774  -24.288 -53.567 1.00 23.42 ?  217 ALA   B CB  1 
ATOM   3449 N N   . ILE   B 1 218 ? -4.263  -25.313 -51.745 1.00 21.63 ?  218 ILE   B N   1 
ATOM   3450 C CA  . ILE   B 1 218 ? -2.976  -25.990 -51.648 1.00 21.41 ?  218 ILE   B CA  1 
ATOM   3451 C C   . ILE   B 1 218 ? -3.142  -27.272 -50.839 1.00 21.38 ?  218 ILE   B C   1 
ATOM   3452 O O   . ILE   B 1 218 ? -2.632  -28.332 -51.202 1.00 21.63 ?  218 ILE   B O   1 
ATOM   3453 C CB  . ILE   B 1 218 ? -1.869  -25.070 -51.092 1.00 21.49 ?  218 ILE   B CB  1 
ATOM   3454 C CG1 . ILE   B 1 218 ? -1.622  -23.857 -51.967 1.00 21.63 ?  218 ILE   B CG1 1 
ATOM   3455 C CG2 . ILE   B 1 218 ? -0.589  -25.894 -50.883 1.00 21.15 ?  218 ILE   B CG2 1 
ATOM   3456 C CD1 . ILE   B 1 218 ? -0.903  -22.710 -51.277 1.00 21.41 ?  218 ILE   B CD1 1 
ATOM   3457 N N   . ALA   B 1 219 ? -3.847  -27.173 -49.710 1.00 20.89 ?  219 ALA   B N   1 
ATOM   3458 C CA  . ALA   B 1 219 ? -4.029  -28.325 -48.848 1.00 19.79 ?  219 ALA   B CA  1 
ATOM   3459 C C   . ALA   B 1 219 ? -4.849  -29.390 -49.559 1.00 20.00 ?  219 ALA   B C   1 
ATOM   3460 O O   . ALA   B 1 219 ? -4.485  -30.553 -49.534 1.00 19.90 ?  219 ALA   B O   1 
ATOM   3461 C CB  . ALA   B 1 219 ? -4.688  -27.875 -47.542 1.00 20.71 ?  219 ALA   B CB  1 
ATOM   3462 N N   . ASP   B 1 220 ? -5.951  -28.963 -50.185 1.00 22.33 ?  220 ASP   B N   1 
ATOM   3463 C CA  . ASP   B 1 220 ? -6.856  -29.835 -50.927 1.00 23.52 ?  220 ASP   B CA  1 
ATOM   3464 C C   . ASP   B 1 220 ? -6.090  -30.575 -52.014 1.00 22.89 ?  220 ASP   B C   1 
ATOM   3465 O O   . ASP   B 1 220 ? -6.187  -31.786 -52.123 1.00 22.95 ?  220 ASP   B O   1 
ATOM   3466 C CB  . ASP   B 1 220 ? -8.030  -29.039 -51.472 1.00 24.42 ?  220 ASP   B CB  1 
ATOM   3467 C CG  . ASP   B 1 220 ? -9.009  -28.488 -50.443 1.00 25.02 ?  220 ASP   B CG  1 
ATOM   3468 O OD1 . ASP   B 1 220 ? -8.878  -28.807 -49.238 1.00 26.61 ?  220 ASP   B OD1 1 
ATOM   3469 O OD2 . ASP   B 1 220 ? -9.911  -27.741 -50.847 1.00 27.02 ?  220 ASP   B OD2 1 
ATOM   3470 N N   . GLU   B 1 221 ? -5.217  -29.863 -52.701 1.00 22.94 ?  221 GLU   B N   1 
ATOM   3471 C CA  . GLU   B 1 221 ? -4.405  -30.462 -53.740 1.00 26.92 ?  221 GLU   B CA  1 
ATOM   3472 C C   . GLU   B 1 221 ? -3.478  -31.532 -53.170 1.00 25.50 ?  221 GLU   B C   1 
ATOM   3473 O O   . GLU   B 1 221 ? -3.379  -32.609 -53.730 1.00 25.80 ?  221 GLU   B O   1 
ATOM   3474 C CB  . GLU   B 1 221 ? -3.688  -29.317 -54.442 1.00 31.61 ?  221 GLU   B CB  1 
ATOM   3475 C CG  . GLU   B 1 221 ? -2.842  -29.776 -55.621 1.00 39.96 ?  221 GLU   B CG  1 
ATOM   3476 C CD  . GLU   B 1 221 ? -2.006  -28.682 -56.274 1.00 49.40 ?  221 GLU   B CD  1 
ATOM   3477 O OE1 . GLU   B 1 221 ? -1.875  -27.557 -55.724 1.00 48.11 ?  221 GLU   B OE1 1 
ATOM   3478 O OE2 . GLU   B 1 221 ? -1.493  -28.982 -57.375 1.00 59.35 ?  221 GLU   B OE2 1 
ATOM   3479 N N   . LEU   B 1 222 ? -2.797  -31.238 -52.046 1.00 22.92 ?  222 LEU   B N   1 
ATOM   3480 C CA  . LEU   B 1 222 ? -1.753  -32.093 -51.536 1.00 21.13 ?  222 LEU   B CA  1 
ATOM   3481 C C   . LEU   B 1 222 ? -2.339  -33.334 -50.887 1.00 21.38 ?  222 LEU   B C   1 
ATOM   3482 O O   . LEU   B 1 222 ? -1.742  -34.397 -50.963 1.00 21.93 ?  222 LEU   B O   1 
ATOM   3483 C CB  . LEU   B 1 222 ? -0.874  -31.330 -50.550 1.00 22.31 ?  222 LEU   B CB  1 
ATOM   3484 C CG  . LEU   B 1 222 ? 0.287   -30.520 -51.134 1.00 25.18 ?  222 LEU   B CG  1 
ATOM   3485 C CD1 . LEU   B 1 222 ? 1.028   -29.773 -50.030 1.00 24.10 ?  222 LEU   B CD1 1 
ATOM   3486 C CD2 . LEU   B 1 222 ? 1.268   -31.404 -51.917 1.00 24.63 ?  222 LEU   B CD2 1 
ATOM   3487 N N   . PHE   B 1 223 ? -3.405  -33.152 -50.104 1.00 22.03 ?  223 PHE   B N   1 
ATOM   3488 C CA  . PHE   B 1 223 ? -3.863  -34.156 -49.169 1.00 21.69 ?  223 PHE   B CA  1 
ATOM   3489 C C   . PHE   B 1 223 ? -5.268  -34.658 -49.495 1.00 22.45 ?  223 PHE   B C   1 
ATOM   3490 O O   . PHE   B 1 223 ? -5.629  -35.701 -48.990 1.00 26.81 ?  223 PHE   B O   1 
ATOM   3491 C CB  . PHE   B 1 223 ? -3.920  -33.606 -47.745 1.00 19.95 ?  223 PHE   B CB  1 
ATOM   3492 C CG  . PHE   B 1 223 ? -2.573  -33.160 -47.242 1.00 19.27 ?  223 PHE   B CG  1 
ATOM   3493 C CD1 . PHE   B 1 223 ? -1.569  -34.104 -47.043 1.00 20.07 ?  223 PHE   B CD1 1 
ATOM   3494 C CD2 . PHE   B 1 223 ? -2.301  -31.818 -47.033 1.00 19.24 ?  223 PHE   B CD2 1 
ATOM   3495 C CE1 . PHE   B 1 223 ? -0.326  -33.708 -46.581 1.00 20.13 ?  223 PHE   B CE1 1 
ATOM   3496 C CE2 . PHE   B 1 223 ? -1.041  -31.436 -46.605 1.00 18.27 ?  223 PHE   B CE2 1 
ATOM   3497 C CZ  . PHE   B 1 223 ? -0.084  -32.385 -46.351 1.00 19.16 ?  223 PHE   B CZ  1 
ATOM   3498 N N   . GLY   B 1 224 ? -6.014  -33.986 -50.380 1.00 23.64 ?  224 GLY   B N   1 
ATOM   3499 C CA  . GLY   B 1 224 ? -7.429  -34.247 -50.543 1.00 24.02 ?  224 GLY   B CA  1 
ATOM   3500 C C   . GLY   B 1 224 ? -8.251  -33.267 -49.712 1.00 26.07 ?  224 GLY   B C   1 
ATOM   3501 O O   . GLY   B 1 224 ? -7.792  -32.780 -48.676 1.00 24.87 ?  224 GLY   B O   1 
ATOM   3502 N N   . ALA   B 1 225 ? -9.483  -33.016 -50.146 1.00 25.61 ?  225 ALA   B N   1 
ATOM   3503 C CA  . ALA   B 1 225 ? -10.214 -31.845 -49.693 1.00 26.80 ?  225 ALA   B CA  1 
ATOM   3504 C C   . ALA   B 1 225 ? -10.806 -32.036 -48.302 1.00 24.92 ?  225 ALA   B C   1 
ATOM   3505 O O   . ALA   B 1 225 ? -11.359 -31.084 -47.783 1.00 25.47 ?  225 ALA   B O   1 
ATOM   3506 C CB  . ALA   B 1 225 ? -11.299 -31.498 -50.685 1.00 29.50 ?  225 ALA   B CB  1 
ATOM   3507 N N   . ASP   B 1 226 ? -10.739 -33.236 -47.716 1.00 24.50 ?  226 ASP   B N   1 
ATOM   3508 C CA  . ASP   B 1 226 ? -11.256 -33.439 -46.363 1.00 27.14 ?  226 ASP   B CA  1 
ATOM   3509 C C   . ASP   B 1 226 ? -10.162 -33.255 -45.319 1.00 24.36 ?  226 ASP   B C   1 
ATOM   3510 O O   . ASP   B 1 226 ? -10.437 -33.310 -44.127 1.00 25.20 ?  226 ASP   B O   1 
ATOM   3511 C CB  . ASP   B 1 226 ? -11.817 -34.841 -46.131 1.00 29.87 ?  226 ASP   B CB  1 
ATOM   3512 C CG  . ASP   B 1 226 ? -13.068 -35.162 -46.924 1.00 35.88 ?  226 ASP   B CG  1 
ATOM   3513 O OD1 . ASP   B 1 226 ? -13.862 -34.226 -47.168 1.00 40.32 ?  226 ASP   B OD1 1 
ATOM   3514 O OD2 . ASP   B 1 226 ? -13.254 -36.344 -47.245 1.00 41.40 ?  226 ASP   B OD2 1 
ATOM   3515 N N   . TRP   B 1 227 ? -8.904  -33.158 -45.741 1.00 21.79 ?  227 TRP   B N   1 
ATOM   3516 C CA  . TRP   B 1 227 ? -7.823  -33.136 -44.774 1.00 21.55 ?  227 TRP   B CA  1 
ATOM   3517 C C   . TRP   B 1 227 ? -7.877  -31.922 -43.844 1.00 19.63 ?  227 TRP   B C   1 
ATOM   3518 O O   . TRP   B 1 227 ? -7.622  -32.072 -42.643 1.00 20.42 ?  227 TRP   B O   1 
ATOM   3519 C CB  . TRP   B 1 227 ? -6.485  -33.164 -45.506 1.00 21.18 ?  227 TRP   B CB  1 
ATOM   3520 C CG  . TRP   B 1 227 ? -5.331  -33.146 -44.559 1.00 20.11 ?  227 TRP   B CG  1 
ATOM   3521 C CD1 . TRP   B 1 227 ? -4.835  -34.196 -43.854 1.00 21.43 ?  227 TRP   B CD1 1 
ATOM   3522 C CD2 . TRP   B 1 227 ? -4.504  -32.014 -44.254 1.00 18.57 ?  227 TRP   B CD2 1 
ATOM   3523 N NE1 . TRP   B 1 227 ? -3.777  -33.780 -43.086 1.00 20.87 ?  227 TRP   B NE1 1 
ATOM   3524 C CE2 . TRP   B 1 227 ? -3.547  -32.454 -43.313 1.00 18.44 ?  227 TRP   B CE2 1 
ATOM   3525 C CE3 . TRP   B 1 227 ? -4.492  -30.679 -44.639 1.00 18.16 ?  227 TRP   B CE3 1 
ATOM   3526 C CZ2 . TRP   B 1 227 ? -2.557  -31.608 -42.809 1.00 17.80 ?  227 TRP   B CZ2 1 
ATOM   3527 C CZ3 . TRP   B 1 227 ? -3.507  -29.850 -44.144 1.00 19.72 ?  227 TRP   B CZ3 1 
ATOM   3528 C CH2 . TRP   B 1 227 ? -2.540  -30.307 -43.250 1.00 18.16 ?  227 TRP   B CH2 1 
ATOM   3529 N N   . ALA   B 1 228 ? -8.191  -30.748 -44.405 1.00 18.56 ?  228 ALA   B N   1 
ATOM   3530 C CA  . ALA   B 1 228 ? -8.083  -29.481 -43.678 1.00 18.79 ?  228 ALA   B CA  1 
ATOM   3531 C C   . ALA   B 1 228 ? -9.262  -29.196 -42.745 1.00 18.72 ?  228 ALA   B C   1 
ATOM   3532 O O   . ALA   B 1 228 ? -9.991  -28.246 -42.918 1.00 21.13 ?  228 ALA   B O   1 
ATOM   3533 C CB  . ALA   B 1 228 ? -7.899  -28.341 -44.643 1.00 18.51 ?  228 ALA   B CB  1 
ATOM   3534 N N   . ASP   B 1 229 ? -9.354  -29.959 -41.672 1.00 19.67 ?  229 ASP   B N   1 
ATOM   3535 C CA  . ASP   B 1 229 ? -10.280 -29.688 -40.583 1.00 19.84 ?  229 ASP   B CA  1 
ATOM   3536 C C   . ASP   B 1 229 ? -9.532  -28.883 -39.517 1.00 17.98 ?  229 ASP   B C   1 
ATOM   3537 O O   . ASP   B 1 229 ? -8.360  -28.553 -39.685 1.00 17.92 ?  229 ASP   B O   1 
ATOM   3538 C CB  . ASP   B 1 229 ? -10.847 -30.992 -40.078 1.00 21.00 ?  229 ASP   B CB  1 
ATOM   3539 C CG  . ASP   B 1 229 ? -9.820  -31.944 -39.481 1.00 23.80 ?  229 ASP   B CG  1 
ATOM   3540 O OD1 . ASP   B 1 229 ? -8.718  -31.488 -39.183 1.00 20.91 ?  229 ASP   B OD1 1 
ATOM   3541 O OD2 . ASP   B 1 229 ? -10.158 -33.116 -39.228 1.00 28.53 ?  229 ASP   B OD2 1 
ATOM   3542 N N   . ALA   B 1 230 ? -10.216 -28.557 -38.419 1.00 17.67 ?  230 ALA   B N   1 
ATOM   3543 C CA  . ALA   B 1 230 ? -9.640  -27.648 -37.441 1.00 18.69 ?  230 ALA   B CA  1 
ATOM   3544 C C   . ALA   B 1 230 ? -8.403  -28.277 -36.782 1.00 17.26 ?  230 ALA   B C   1 
ATOM   3545 O O   . ALA   B 1 230 ? -7.593  -27.553 -36.229 1.00 17.61 ?  230 ALA   B O   1 
ATOM   3546 C CB  . ALA   B 1 230 ? -10.680 -27.211 -36.417 1.00 20.52 ?  230 ALA   B CB  1 
ATOM   3547 N N   . ARG   B 1 231 ? -8.239  -29.607 -36.820 1.00 17.02 ?  231 ARG   B N   1 
ATOM   3548 C CA  . ARG   B 1 231 ? -7.071  -30.243 -36.219 1.00 17.58 ?  231 ARG   B CA  1 
ATOM   3549 C C   . ARG   B 1 231 ? -5.858  -30.122 -37.134 1.00 18.60 ?  231 ARG   B C   1 
ATOM   3550 O O   . ARG   B 1 231 ? -4.733  -30.345 -36.684 1.00 17.58 ?  231 ARG   B O   1 
ATOM   3551 C CB  . ARG   B 1 231 ? -7.402  -31.700 -35.903 1.00 18.08 ?  231 ARG   B CB  1 
ATOM   3552 C CG  . ARG   B 1 231 ? -6.273  -32.518 -35.290 1.00 18.62 ?  231 ARG   B CG  1 
ATOM   3553 C CD  . ARG   B 1 231 ? -5.463  -31.922 -34.159 1.00 18.61 ?  231 ARG   B CD  1 
ATOM   3554 N NE  . ARG   B 1 231 ? -4.325  -32.737 -33.743 1.00 19.20 ?  231 ARG   B NE  1 
ATOM   3555 C CZ  . ARG   B 1 231 ? -3.068  -32.594 -34.200 1.00 19.27 ?  231 ARG   B CZ  1 
ATOM   3556 N NH1 . ARG   B 1 231 ? -2.795  -31.667 -35.093 1.00 19.66 ?  231 ARG   B NH1 1 
ATOM   3557 N NH2 . ARG   B 1 231 ? -2.093  -33.393 -33.780 1.00 19.03 ?  231 ARG   B NH2 1 
ATOM   3558 N N   . HIS   B 1 232 ? -6.101  -29.785 -38.421 1.00 16.90 ?  232 HIS   B N   1 
ATOM   3559 C CA  . HIS   B 1 232 ? -5.041  -29.825 -39.415 1.00 17.20 ?  232 HIS   B CA  1 
ATOM   3560 C C   . HIS   B 1 232 ? -4.777  -28.516 -40.140 1.00 16.32 ?  232 HIS   B C   1 
ATOM   3561 O O   . HIS   B 1 232 ? -3.792  -28.418 -40.888 1.00 15.54 ?  232 HIS   B O   1 
ATOM   3562 C CB  . HIS   B 1 232 ? -5.352  -30.936 -40.411 1.00 17.64 ?  232 HIS   B CB  1 
ATOM   3563 C CG  . HIS   B 1 232 ? -5.330  -32.274 -39.754 1.00 18.60 ?  232 HIS   B CG  1 
ATOM   3564 N ND1 . HIS   B 1 232 ? -6.445  -32.832 -39.164 1.00 19.23 ?  232 HIS   B ND1 1 
ATOM   3565 C CD2 . HIS   B 1 232 ? -4.355  -33.153 -39.599 1.00 18.37 ?  232 HIS   B CD2 1 
ATOM   3566 C CE1 . HIS   B 1 232 ? -6.116  -34.031 -38.699 1.00 18.92 ?  232 HIS   B CE1 1 
ATOM   3567 N NE2 . HIS   B 1 232 ? -4.841  -34.218 -38.885 1.00 18.26 ?  232 HIS   B NE2 1 
ATOM   3568 N N   . TYR   B 1 233 ? -5.642  -27.525 -40.001 1.00 14.76 ?  233 TYR   B N   1 
ATOM   3569 C CA  . TYR   B 1 233 ? -5.460  -26.295 -40.731 1.00 15.08 ?  233 TYR   B CA  1 
ATOM   3570 C C   . TYR   B 1 233 ? -6.020  -25.132 -39.921 1.00 14.50 ?  233 TYR   B C   1 
ATOM   3571 O O   . TYR   B 1 233 ? -7.135  -25.228 -39.380 1.00 17.23 ?  233 TYR   B O   1 
ATOM   3572 C CB  . TYR   B 1 233 ? -6.183  -26.359 -42.075 1.00 14.67 ?  233 TYR   B CB  1 
ATOM   3573 C CG  . TYR   B 1 233 ? -5.585  -25.469 -43.150 1.00 14.33 ?  233 TYR   B CG  1 
ATOM   3574 C CD1 . TYR   B 1 233 ? -5.786  -24.100 -43.146 1.00 15.71 ?  233 TYR   B CD1 1 
ATOM   3575 C CD2 . TYR   B 1 233 ? -4.766  -25.987 -44.145 1.00 16.51 ?  233 TYR   B CD2 1 
ATOM   3576 C CE1 . TYR   B 1 233 ? -5.149  -23.259 -44.057 1.00 17.36 ?  233 TYR   B CE1 1 
ATOM   3577 C CE2 . TYR   B 1 233 ? -4.180  -25.174 -45.107 1.00 16.59 ?  233 TYR   B CE2 1 
ATOM   3578 C CZ  . TYR   B 1 233 ? -4.394  -23.804 -45.077 1.00 17.78 ?  233 TYR   B CZ  1 
ATOM   3579 O OH  . TYR   B 1 233 ? -3.802  -23.006 -46.035 1.00 20.39 ?  233 TYR   B OH  1 
ATOM   3580 N N   . ARG   B 1 234 ? -5.283  -24.024 -39.922 1.00 13.51 ?  234 ARG   B N   1 
ATOM   3581 C CA  . ARG   B 1 234 ? -5.723  -22.793 -39.296 1.00 13.74 ?  234 ARG   B CA  1 
ATOM   3582 C C   . ARG   B 1 234 ? -5.211  -21.585 -40.066 1.00 14.03 ?  234 ARG   B C   1 
ATOM   3583 O O   . ARG   B 1 234 ? -4.212  -21.632 -40.785 1.00 14.12 ?  234 ARG   B O   1 
ATOM   3584 C CB  . ARG   B 1 234 ? -5.212  -22.700 -37.845 1.00 13.28 ?  234 ARG   B CB  1 
ATOM   3585 C CG  . ARG   B 1 234 ? -5.650  -23.813 -36.927 1.00 13.83 ?  234 ARG   B CG  1 
ATOM   3586 C CD  . ARG   B 1 234 ? -7.075  -23.694 -36.471 1.00 14.05 ?  234 ARG   B CD  1 
ATOM   3587 N NE  . ARG   B 1 234 ? -7.360  -24.832 -35.637 1.00 14.60 ?  234 ARG   B NE  1 
ATOM   3588 C CZ  . ARG   B 1 234 ? -6.964  -24.926 -34.361 1.00 14.89 ?  234 ARG   B CZ  1 
ATOM   3589 N NH1 . ARG   B 1 234 ? -6.537  -23.855 -33.708 1.00 14.50 ?  234 ARG   B NH1 1 
ATOM   3590 N NH2 . ARG   B 1 234 ? -6.984  -26.091 -33.770 1.00 15.74 ?  234 ARG   B NH2 1 
ATOM   3591 N N   . PHE   B 1 235 ? -5.914  -20.476 -39.877 1.00 14.03 ?  235 PHE   B N   1 
ATOM   3592 C CA  . PHE   B 1 235 ? -5.563  -19.193 -40.426 1.00 15.12 ?  235 PHE   B CA  1 
ATOM   3593 C C   . PHE   B 1 235 ? -5.570  -18.122 -39.354 1.00 16.87 ?  235 PHE   B C   1 
ATOM   3594 O O   . PHE   B 1 235 ? -6.431  -18.115 -38.472 1.00 17.00 ?  235 PHE   B O   1 
ATOM   3595 C CB  . PHE   B 1 235 ? -6.636  -18.636 -41.362 1.00 16.87 ?  235 PHE   B CB  1 
ATOM   3596 C CG  . PHE   B 1 235 ? -6.781  -19.316 -42.709 1.00 17.24 ?  235 PHE   B CG  1 
ATOM   3597 C CD1 . PHE   B 1 235 ? -6.008  -18.895 -43.786 1.00 18.05 ?  235 PHE   B CD1 1 
ATOM   3598 C CD2 . PHE   B 1 235 ? -7.690  -20.330 -42.911 1.00 17.84 ?  235 PHE   B CD2 1 
ATOM   3599 C CE1 . PHE   B 1 235 ? -6.157  -19.486 -45.042 1.00 19.08 ?  235 PHE   B CE1 1 
ATOM   3600 C CE2 . PHE   B 1 235 ? -7.818  -20.916 -44.167 1.00 18.87 ?  235 PHE   B CE2 1 
ATOM   3601 C CZ  . PHE   B 1 235 ? -7.054  -20.505 -45.216 1.00 17.74 ?  235 PHE   B CZ  1 
ATOM   3602 N N   A SER   B 1 236 ? -4.633  -17.186 -39.473 0.33 16.98 ?  236 SER   B N   1 
ATOM   3603 N N   B SER   B 1 236 ? -4.646  -17.168 -39.472 0.33 17.02 ?  236 SER   B N   1 
ATOM   3604 N N   C SER   B 1 236 ? -4.593  -17.220 -39.433 0.33 17.42 ?  236 SER   B N   1 
ATOM   3605 C CA  A SER   B 1 236 ? -4.724  -15.939 -38.739 0.33 17.94 ?  236 SER   B CA  1 
ATOM   3606 C CA  B SER   B 1 236 ? -4.736  -15.931 -38.715 0.33 17.98 ?  236 SER   B CA  1 
ATOM   3607 C CA  C SER   B 1 236 ? -4.634  -15.955 -38.719 0.33 18.82 ?  236 SER   B CA  1 
ATOM   3608 C C   A SER   B 1 236 ? -4.136  -14.817 -39.577 0.33 19.24 ?  236 SER   B C   1 
ATOM   3609 C C   B SER   B 1 236 ? -4.121  -14.798 -39.522 0.33 19.24 ?  236 SER   B C   1 
ATOM   3610 C C   C SER   B 1 236 ? -4.183  -14.865 -39.684 0.33 19.82 ?  236 SER   B C   1 
ATOM   3611 O O   A SER   B 1 236 ? -3.014  -14.913 -40.043 0.33 18.50 ?  236 SER   B O   1 
ATOM   3612 O O   B SER   B 1 236 ? -2.969  -14.870 -39.920 0.33 18.31 ?  236 SER   B O   1 
ATOM   3613 O O   C SER   B 1 236 ? -3.218  -15.060 -40.401 0.33 19.52 ?  236 SER   B O   1 
ATOM   3614 C CB  A SER   B 1 236 ? -4.026  -16.025 -37.426 0.33 17.84 ?  236 SER   B CB  1 
ATOM   3615 C CB  B SER   B 1 236 ? -4.072  -16.048 -37.376 0.33 17.93 ?  236 SER   B CB  1 
ATOM   3616 C CB  C SER   B 1 236 ? -3.761  -15.988 -37.483 0.33 19.25 ?  236 SER   B CB  1 
ATOM   3617 O OG  A SER   B 1 236 ? -4.173  -14.799 -36.728 0.33 17.02 ?  236 SER   B OG  1 
ATOM   3618 O OG  B SER   B 1 236 ? -2.671  -16.241 -37.512 0.33 16.89 ?  236 SER   B OG  1 
ATOM   3619 O OG  C SER   B 1 236 ? -4.203  -16.955 -36.534 0.33 19.32 ?  236 SER   B OG  1 
ATOM   3620 N N   . ALA   B 1 237 ? -4.901  -13.741 -39.729 1.00 21.41 ?  237 ALA   B N   1 
ATOM   3621 C CA  . ALA   B 1 237 ? -4.424  -12.570 -40.421 1.00 23.55 ?  237 ALA   B CA  1 
ATOM   3622 C C   . ALA   B 1 237 ? -5.317  -11.385 -40.071 1.00 27.93 ?  237 ALA   B C   1 
ATOM   3623 O O   . ALA   B 1 237 ? -6.529  -11.521 -39.907 1.00 27.08 ?  237 ALA   B O   1 
ATOM   3624 C CB  . ALA   B 1 237 ? -4.370  -12.838 -41.904 1.00 23.70 ?  237 ALA   B CB  1 
ATOM   3625 N N   . SER   B 1 238 ? -4.676  -10.227 -39.950 1.00 30.63 ?  238 SER   B N   1 
ATOM   3626 C CA  . SER   B 1 238 ? -5.360  -8.950  -39.841 1.00 36.69 ?  238 SER   B CA  1 
ATOM   3627 C C   . SER   B 1 238 ? -6.308  -8.737  -41.030 1.00 34.51 ?  238 SER   B C   1 
ATOM   3628 O O   . SER   B 1 238 ? -5.950  -8.929  -42.193 1.00 32.09 ?  238 SER   B O   1 
ATOM   3629 C CB  . SER   B 1 238 ? -4.349  -7.834  -39.705 1.00 39.01 ?  238 SER   B CB  1 
ATOM   3630 O OG  . SER   B 1 238 ? -4.837  -6.658  -40.324 1.00 46.95 ?  238 SER   B OG  1 
ATOM   3631 N N   . GLY   B 1 239 ? -7.577  -8.456  -40.712 1.00 34.26 ?  239 GLY   B N   1 
ATOM   3632 C CA  . GLY   B 1 239 ? -8.563  -8.102  -41.721 1.00 34.12 ?  239 GLY   B CA  1 
ATOM   3633 C C   . GLY   B 1 239 ? -9.243  -9.313  -42.356 1.00 33.01 ?  239 GLY   B C   1 
ATOM   3634 O O   . GLY   B 1 239 ? -10.164 -9.149  -43.135 1.00 31.04 ?  239 GLY   B O   1 
ATOM   3635 N N   . LEU   B 1 240 ? -8.796  -10.539 -42.064 1.00 28.09 ?  240 LEU   B N   1 
ATOM   3636 C CA  . LEU   B 1 240 ? -9.336  -11.674 -42.799 1.00 24.07 ?  240 LEU   B CA  1 
ATOM   3637 C C   . LEU   B 1 240 ? -10.795 -11.918 -42.392 1.00 23.61 ?  240 LEU   B C   1 
ATOM   3638 O O   . LEU   B 1 240 ? -11.607 -12.252 -43.224 1.00 22.75 ?  240 LEU   B O   1 
ATOM   3639 C CB  . LEU   B 1 240 ? -8.501  -12.933 -42.561 1.00 22.97 ?  240 LEU   B CB  1 
ATOM   3640 C CG  . LEU   B 1 240 ? -8.997  -14.183 -43.295 1.00 22.24 ?  240 LEU   B CG  1 
ATOM   3641 C CD1 . LEU   B 1 240 ? -9.061  -13.907 -44.754 1.00 23.78 ?  240 LEU   B CD1 1 
ATOM   3642 C CD2 . LEU   B 1 240 ? -8.160  -15.412 -43.065 1.00 23.16 ?  240 LEU   B CD2 1 
ATOM   3643 N N   . LEU   B 1 241 ? -11.111 -11.842 -41.100 1.00 23.75 ?  241 LEU   B N   1 
ATOM   3644 C CA  . LEU   B 1 241 ? -12.440 -12.228 -40.649 1.00 23.73 ?  241 LEU   B CA  1 
ATOM   3645 C C   . LEU   B 1 241 ? -13.467 -11.320 -41.328 1.00 24.67 ?  241 LEU   B C   1 
ATOM   3646 O O   . LEU   B 1 241 ? -14.482 -11.796 -41.816 1.00 24.14 ?  241 LEU   B O   1 
ATOM   3647 C CB  . LEU   B 1 241 ? -12.562 -12.135 -39.134 1.00 21.92 ?  241 LEU   B CB  1 
ATOM   3648 C CG  . LEU   B 1 241 ? -13.959 -12.427 -38.575 1.00 22.74 ?  241 LEU   B CG  1 
ATOM   3649 C CD1 . LEU   B 1 241 ? -14.437 -13.814 -39.043 1.00 22.52 ?  241 LEU   B CD1 1 
ATOM   3650 C CD2 . LEU   B 1 241 ? -14.033 -12.281 -37.055 1.00 22.88 ?  241 LEU   B CD2 1 
ATOM   3651 N N   . ALA   B 1 242 ? -13.186 -10.016 -41.321 1.00 24.62 ?  242 ALA   B N   1 
ATOM   3652 C CA  . ALA   B 1 242 ? -14.048 -9.059  -41.990 1.00 26.65 ?  242 ALA   B CA  1 
ATOM   3653 C C   . ALA   B 1 242 ? -14.200 -9.378  -43.480 1.00 28.90 ?  242 ALA   B C   1 
ATOM   3654 O O   . ALA   B 1 242 ? -15.309 -9.411  -44.004 1.00 31.96 ?  242 ALA   B O   1 
ATOM   3655 C CB  . ALA   B 1 242 ? -13.530 -7.650  -41.744 1.00 27.44 ?  242 ALA   B CB  1 
ATOM   3656 N N   . SER   B 1 243 ? -13.101 -9.682  -44.171 1.00 27.32 ?  243 SER   B N   1 
ATOM   3657 C CA  . SER   B 1 243 ? -13.168 -10.021 -45.581 1.00 26.88 ?  243 SER   B CA  1 
ATOM   3658 C C   . SER   B 1 243 ? -13.973 -11.312 -45.765 1.00 27.41 ?  243 SER   B C   1 
ATOM   3659 O O   . SER   B 1 243 ? -14.750 -11.445 -46.712 1.00 27.89 ?  243 SER   B O   1 
ATOM   3660 C CB  . SER   B 1 243 ? -11.780 -10.098 -46.180 1.00 27.97 ?  243 SER   B CB  1 
ATOM   3661 O OG  . SER   B 1 243 ? -11.860 -10.523 -47.539 1.00 31.90 ?  243 SER   B OG  1 
ATOM   3662 N N   . LEU   B 1 244 ? -13.844 -12.270 -44.839 1.00 24.68 ?  244 LEU   B N   1 
ATOM   3663 C CA  . LEU   B 1 244 ? -14.626 -13.493 -44.978 1.00 25.72 ?  244 LEU   B CA  1 
ATOM   3664 C C   . LEU   B 1 244 ? -16.110 -13.213 -44.758 1.00 24.95 ?  244 LEU   B C   1 
ATOM   3665 O O   . LEU   B 1 244 ? -16.944 -13.775 -45.454 1.00 23.91 ?  244 LEU   B O   1 
ATOM   3666 C CB  . LEU   B 1 244 ? -14.158 -14.594 -44.031 1.00 24.40 ?  244 LEU   B CB  1 
ATOM   3667 C CG  . LEU   B 1 244 ? -12.722 -15.085 -44.264 1.00 24.12 ?  244 LEU   B CG  1 
ATOM   3668 C CD1 . LEU   B 1 244 ? -12.303 -15.925 -43.097 1.00 22.65 ?  244 LEU   B CD1 1 
ATOM   3669 C CD2 . LEU   B 1 244 ? -12.601 -15.908 -45.545 1.00 24.61 ?  244 LEU   B CD2 1 
ATOM   3670 N N   . LEU   B 1 245 ? -16.438 -12.394 -43.758 1.00 25.41 ?  245 LEU   B N   1 
ATOM   3671 C CA  . LEU   B 1 245 ? -17.841 -12.159 -43.467 1.00 26.61 ?  245 LEU   B CA  1 
ATOM   3672 C C   . LEU   B 1 245 ? -18.482 -11.399 -44.622 1.00 28.49 ?  245 LEU   B C   1 
ATOM   3673 O O   . LEU   B 1 245 ? -19.650 -11.602 -44.930 1.00 29.01 ?  245 LEU   B O   1 
ATOM   3674 C CB  . LEU   B 1 245 ? -18.030 -11.442 -42.140 1.00 26.09 ?  245 LEU   B CB  1 
ATOM   3675 C CG  . LEU   B 1 245 ? -17.847 -12.335 -40.911 1.00 26.26 ?  245 LEU   B CG  1 
ATOM   3676 C CD1 . LEU   B 1 245 ? -17.676 -11.464 -39.691 1.00 26.27 ?  245 LEU   B CD1 1 
ATOM   3677 C CD2 . LEU   B 1 245 ? -18.987 -13.337 -40.725 1.00 24.83 ?  245 LEU   B CD2 1 
ATOM   3678 N N   . LYS   B 1 246 ? -17.711 -10.514 -45.249 1.00 32.08 ?  246 LYS   B N   1 
ATOM   3679 C CA  . LYS   B 1 246 ? -18.256 -9.701  -46.321 1.00 33.51 ?  246 LYS   B CA  1 
ATOM   3680 C C   . LYS   B 1 246 ? -18.622 -10.634 -47.464 1.00 33.15 ?  246 LYS   B C   1 
ATOM   3681 O O   . LYS   B 1 246 ? -19.728 -10.583 -47.983 1.00 33.77 ?  246 LYS   B O   1 
ATOM   3682 C CB  . LYS   B 1 246 ? -17.199 -8.651  -46.660 1.00 39.01 ?  246 LYS   B CB  1 
ATOM   3683 C CG  . LYS   B 1 246 ? -17.533 -7.739  -47.831 1.00 45.82 ?  246 LYS   B CG  1 
ATOM   3684 C CD  . LYS   B 1 246 ? -16.489 -6.644  -48.025 1.00 50.47 ?  246 LYS   B CD  1 
ATOM   3685 C CE  . LYS   B 1 246 ? -16.967 -5.514  -48.896 1.00 58.63 ?  246 LYS   B CE  1 
ATOM   3686 N NZ  . LYS   B 1 246 ? -17.169 -5.918  -50.291 1.00 60.16 ?  246 LYS   B NZ  1 
ATOM   3687 N N   . ALA   B 1 247 ? -17.694 -11.527 -47.822 1.00 29.83 ?  247 ALA   B N   1 
ATOM   3688 C CA  . ALA   B 1 247 ? -17.971 -12.516 -48.836 1.00 30.08 ?  247 ALA   B CA  1 
ATOM   3689 C C   . ALA   B 1 247 ? -19.234 -13.304 -48.515 1.00 33.03 ?  247 ALA   B C   1 
ATOM   3690 O O   . ALA   B 1 247 ? -19.864 -13.809 -49.438 1.00 32.29 ?  247 ALA   B O   1 
ATOM   3691 C CB  . ALA   B 1 247 ? -16.790 -13.420 -49.052 1.00 29.19 ?  247 ALA   B CB  1 
ATOM   3692 N N   . LEU   B 1 248 ? -19.587 -13.432 -47.224 1.00 32.32 ?  248 LEU   B N   1 
ATOM   3693 C CA  . LEU   B 1 248 ? -20.698 -14.275 -46.819 1.00 32.44 ?  248 LEU   B CA  1 
ATOM   3694 C C   . LEU   B 1 248 ? -21.966 -13.430 -46.648 1.00 34.24 ?  248 LEU   B C   1 
ATOM   3695 O O   . LEU   B 1 248 ? -22.994 -13.960 -46.265 1.00 34.67 ?  248 LEU   B O   1 
ATOM   3696 C CB  . LEU   B 1 248 ? -20.339 -15.062 -45.554 1.00 29.25 ?  248 LEU   B CB  1 
ATOM   3697 C CG  . LEU   B 1 248 ? -19.305 -16.173 -45.778 1.00 29.36 ?  248 LEU   B CG  1 
ATOM   3698 C CD1 . LEU   B 1 248 ? -18.629 -16.728 -44.528 1.00 28.40 ?  248 LEU   B CD1 1 
ATOM   3699 C CD2 . LEU   B 1 248 ? -19.928 -17.321 -46.538 1.00 29.66 ?  248 LEU   B CD2 1 
ATOM   3700 N N   . GLY   B 1 249 ? -21.870 -12.118 -46.879 1.00 35.26 ?  249 GLY   B N   1 
ATOM   3701 C CA  . GLY   B 1 249 ? -23.028 -11.244 -46.812 1.00 37.47 ?  249 GLY   B CA  1 
ATOM   3702 C C   . GLY   B 1 249 ? -23.147 -10.510 -45.477 1.00 41.18 ?  249 GLY   B C   1 
ATOM   3703 O O   . GLY   B 1 249 ? -24.149 -9.844  -45.257 1.00 41.55 ?  249 GLY   B O   1 
ATOM   3704 N N   . HIS   B 1 250 ? -22.136 -10.579 -44.601 1.00 37.67 ?  250 HIS   B N   1 
ATOM   3705 C CA  . HIS   B 1 250 ? -22.189 -9.803  -43.370 1.00 40.86 ?  250 HIS   B CA  1 
ATOM   3706 C C   . HIS   B 1 250 ? -21.353 -8.526  -43.500 1.00 43.59 ?  250 HIS   B C   1 
ATOM   3707 O O   . HIS   B 1 250 ? -20.253 -8.562  -42.932 1.00 56.15 ?  250 HIS   B O   1 
ATOM   3708 C CB  . HIS   B 1 250 ? -21.909 -10.703 -42.163 1.00 37.69 ?  250 HIS   B CB  1 
ATOM   3709 C CG  . HIS   B 1 250 ? -23.057 -11.640 -42.003 1.00 38.31 ?  250 HIS   B CG  1 
ATOM   3710 N ND1 . HIS   B 1 250 ? -23.151 -12.821 -42.712 1.00 38.52 ?  250 HIS   B ND1 1 
ATOM   3711 C CD2 . HIS   B 1 250 ? -24.195 -11.538 -41.301 1.00 38.21 ?  250 HIS   B CD2 1 
ATOM   3712 C CE1 . HIS   B 1 250 ? -24.288 -13.427 -42.397 1.00 35.83 ?  250 HIS   B CE1 1 
ATOM   3713 N NE2 . HIS   B 1 250 ? -24.942 -12.657 -41.571 1.00 34.65 ?  250 HIS   B NE2 1 
HETATM 3714 C C1  . A1IB9 C 2 .   ? 2.914   -5.469  -3.661  0.50 21.29 ?  301 A1IB9 A C1  1 
HETATM 3715 C C2  . A1IB9 C 2 .   ? 3.456   -5.562  -4.971  0.50 20.85 ?  301 A1IB9 A C2  1 
HETATM 3716 C C3  . A1IB9 C 2 .   ? 3.231   -4.628  -5.829  0.50 22.74 ?  301 A1IB9 A C3  1 
HETATM 3717 C C4  . A1IB9 C 2 .   ? 3.826   -4.573  -7.160  0.50 24.85 ?  301 A1IB9 A C4  1 
HETATM 3718 C C5  . A1IB9 C 2 .   ? 3.593   -3.549  -8.081  0.50 27.20 ?  301 A1IB9 A C5  1 
HETATM 3719 C C6  . A1IB9 C 2 .   ? 4.200   -3.554  -9.321  0.50 28.09 ?  301 A1IB9 A C6  1 
HETATM 3720 C C7  . A1IB9 C 2 .   ? 5.023   -4.636  -9.639  0.50 29.15 ?  301 A1IB9 A C7  1 
HETATM 3721 C C8  . A1IB9 C 2 .   ? 5.284   -5.669  -8.748  0.50 26.59 ?  301 A1IB9 A C8  1 
HETATM 3722 C C9  . A1IB9 C 2 .   ? 4.674   -5.621  -7.518  0.50 24.39 ?  301 A1IB9 A C9  1 
HETATM 3723 N N1  . A1IB9 C 2 .   ? 5.673   -4.689  -10.910 0.50 29.64 1  301 A1IB9 A N1  1 
HETATM 3724 O O2  . A1IB9 C 2 .   ? 6.005   -5.776  -11.311 0.50 28.76 ?  301 A1IB9 A O2  1 
HETATM 3725 O O3  . A1IB9 C 2 .   ? 5.952   -3.643  -11.476 0.50 34.40 -1 301 A1IB9 A O3  1 
HETATM 3726 C C1  . GOL   D 3 .   ? -7.184  3.209   10.236  1.00 43.90 ?  302 GOL   A C1  1 
HETATM 3727 O O1  . GOL   D 3 .   ? -7.965  2.022   10.303  1.00 43.29 ?  302 GOL   A O1  1 
HETATM 3728 C C2  . GOL   D 3 .   ? -6.117  3.135   9.161   1.00 42.57 ?  302 GOL   A C2  1 
HETATM 3729 O O2  . GOL   D 3 .   ? -6.730  3.267   7.877   1.00 44.62 ?  302 GOL   A O2  1 
HETATM 3730 C C3  . GOL   D 3 .   ? -5.067  4.208   9.367   1.00 43.46 ?  302 GOL   A C3  1 
HETATM 3731 O O3  . GOL   D 3 .   ? -4.271  4.444   8.215   1.00 36.36 ?  302 GOL   A O3  1 
HETATM 3732 C C1  . A1IB9 E 2 .   ? 0.620   -17.145 -34.450 0.70 22.17 ?  301 A1IB9 B C1  1 
HETATM 3733 C C2  . A1IB9 E 2 .   ? 0.100   -16.386 -33.379 0.70 21.74 ?  301 A1IB9 B C2  1 
HETATM 3734 C C3  . A1IB9 E 2 .   ? 0.200   -15.104 -33.430 0.70 23.02 ?  301 A1IB9 B C3  1 
HETATM 3735 C C4  . A1IB9 E 2 .   ? -0.336  -14.177 -32.442 0.70 25.30 ?  301 A1IB9 B C4  1 
HETATM 3736 C C5  . A1IB9 E 2 .   ? -0.047  -12.813 -32.507 0.70 28.12 ?  301 A1IB9 B C5  1 
HETATM 3737 C C6  . A1IB9 E 2 .   ? -0.506  -11.948 -31.541 0.70 30.44 ?  301 A1IB9 B C6  1 
HETATM 3738 C C7  . A1IB9 E 2 .   ? -1.314  -12.459 -30.530 0.70 29.83 ?  301 A1IB9 B C7  1 
HETATM 3739 C C8  . A1IB9 E 2 .   ? -1.611  -13.812 -30.418 0.70 27.17 ?  301 A1IB9 B C8  1 
HETATM 3740 C C9  . A1IB9 E 2 .   ? -1.150  -14.645 -31.410 0.70 22.70 ?  301 A1IB9 B C9  1 
HETATM 3741 N N1  . A1IB9 E 2 .   ? -1.758  -11.565 -29.539 0.70 33.61 1  301 A1IB9 B N1  1 
HETATM 3742 O O2  . A1IB9 E 2 .   ? -2.567  -11.932 -28.722 0.70 36.86 ?  301 A1IB9 B O2  1 
HETATM 3743 O O3  . A1IB9 E 2 .   ? -1.229  -10.487 -29.513 0.70 43.07 -1 301 A1IB9 B O3  1 
HETATM 3744 O O   . HOH   F 4 .   ? -8.748  -21.676 -12.183 1.00 30.25 ?  401 HOH   A O   1 
HETATM 3745 O O   . HOH   F 4 .   ? -5.838  3.159   5.619   1.00 25.41 ?  402 HOH   A O   1 
HETATM 3746 O O   . HOH   F 4 .   ? -5.997  -9.895  -13.639 1.00 28.45 ?  403 HOH   A O   1 
HETATM 3747 O O   . HOH   F 4 .   ? 12.556  -11.594 -23.836 1.00 37.03 ?  404 HOH   A O   1 
HETATM 3748 O O   . HOH   F 4 .   ? -17.100 -21.810 0.282   1.00 38.13 ?  405 HOH   A O   1 
HETATM 3749 O O   . HOH   F 4 .   ? 24.426  -17.222 -9.876  1.00 30.22 ?  406 HOH   A O   1 
HETATM 3750 O O   . HOH   F 4 .   ? 15.984  10.018  4.447   1.00 39.13 ?  407 HOH   A O   1 
HETATM 3751 O O   . HOH   F 4 .   ? 25.186  -6.807  -3.071  1.00 15.51 ?  408 HOH   A O   1 
HETATM 3752 O O   . HOH   F 4 .   ? -6.707  -2.263  -5.567  1.00 16.12 ?  409 HOH   A O   1 
HETATM 3753 O O   . HOH   F 4 .   ? -3.643  -12.290 -15.987 1.00 18.83 ?  410 HOH   A O   1 
HETATM 3754 O O   . HOH   F 4 .   ? 4.896   -15.416 -21.170 1.00 18.22 ?  411 HOH   A O   1 
HETATM 3755 O O   . HOH   F 4 .   ? 1.348   -25.836 -7.395  1.00 23.60 ?  412 HOH   A O   1 
HETATM 3756 O O   . HOH   F 4 .   ? 14.465  8.548   -2.273  1.00 30.36 ?  413 HOH   A O   1 
HETATM 3757 O O   . HOH   F 4 .   ? 0.198   -1.837  19.671  1.00 43.30 ?  414 HOH   A O   1 
HETATM 3758 O O   . HOH   F 4 .   ? -17.755 -3.295  -1.984  1.00 18.23 ?  415 HOH   A O   1 
HETATM 3759 O O   . HOH   F 4 .   ? 13.766  0.771   14.045  1.00 34.04 ?  416 HOH   A O   1 
HETATM 3760 O O   . HOH   F 4 .   ? 8.098   10.371  4.542   1.00 32.92 ?  417 HOH   A O   1 
HETATM 3761 O O   . HOH   F 4 .   ? -14.606 0.875   4.246   1.00 44.89 ?  418 HOH   A O   1 
HETATM 3762 O O   . HOH   F 4 .   ? -3.024  -10.195 -12.034 1.00 16.85 ?  419 HOH   A O   1 
HETATM 3763 O O   . HOH   F 4 .   ? -7.611  6.461   13.041  1.00 46.85 ?  420 HOH   A O   1 
HETATM 3764 O O   . HOH   F 4 .   ? -10.487 -12.428 -9.777  1.00 14.41 ?  421 HOH   A O   1 
HETATM 3765 O O   . HOH   F 4 .   ? 24.090  8.950   -2.920  1.00 43.36 ?  422 HOH   A O   1 
HETATM 3766 O O   . HOH   F 4 .   ? 1.469   -24.006 -11.747 1.00 19.78 ?  423 HOH   A O   1 
HETATM 3767 O O   . HOH   F 4 .   ? -10.857 -22.436 -2.115  1.00 22.51 ?  424 HOH   A O   1 
HETATM 3768 O O   . HOH   F 4 .   ? -7.071  4.484   -1.446  1.00 22.42 ?  425 HOH   A O   1 
HETATM 3769 O O   . HOH   F 4 .   ? -16.654 -18.463 -2.136  1.00 33.25 ?  426 HOH   A O   1 
HETATM 3770 O O   . HOH   F 4 .   ? 11.945  -19.051 -14.454 1.00 23.93 ?  427 HOH   A O   1 
HETATM 3771 O O   . HOH   F 4 .   ? 8.689   -4.163  -10.802 1.00 30.59 ?  428 HOH   A O   1 
HETATM 3772 O O   . HOH   F 4 .   ? 10.805  -17.177 -0.456  1.00 29.11 ?  429 HOH   A O   1 
HETATM 3773 O O   . HOH   F 4 .   ? -11.065 2.583   11.931  1.00 34.45 ?  430 HOH   A O   1 
HETATM 3774 O O   . HOH   F 4 .   ? 1.224   -14.014 19.990  1.00 20.60 ?  431 HOH   A O   1 
HETATM 3775 O O   . HOH   F 4 .   ? 21.731  -0.591  -6.052  1.00 40.17 ?  432 HOH   A O   1 
HETATM 3776 O O   . HOH   F 4 .   ? -5.799  -24.737 -5.141  1.00 28.52 ?  433 HOH   A O   1 
HETATM 3777 O O   . HOH   F 4 .   ? -12.837 2.781   0.232   1.00 36.89 ?  434 HOH   A O   1 
HETATM 3778 O O   . HOH   F 4 .   ? -3.416  2.137   5.011   1.00 15.60 ?  435 HOH   A O   1 
HETATM 3779 O O   . HOH   F 4 .   ? 9.846   -8.559  -19.320 1.00 44.24 ?  436 HOH   A O   1 
HETATM 3780 O O   . HOH   F 4 .   ? -0.307  6.612   -0.469  1.00 32.38 ?  437 HOH   A O   1 
HETATM 3781 O O   . HOH   F 4 .   ? 18.652  -11.644 -0.806  1.00 19.24 ?  438 HOH   A O   1 
HETATM 3782 O O   . HOH   F 4 .   ? 2.515   -11.120 -16.757 1.00 18.28 ?  439 HOH   A O   1 
HETATM 3783 O O   A HOH   F 4 .   ? 5.453   -8.877  -5.491  0.50 10.80 ?  440 HOH   A O   1 
HETATM 3784 O O   B HOH   F 4 .   ? 6.319   -8.370  -3.841  0.50 18.83 ?  440 HOH   A O   1 
HETATM 3785 O O   . HOH   F 4 .   ? 12.493  7.079   12.455  1.00 30.67 ?  441 HOH   A O   1 
HETATM 3786 O O   . HOH   F 4 .   ? 7.747   -21.581 -8.839  1.00 14.85 ?  442 HOH   A O   1 
HETATM 3787 O O   . HOH   F 4 .   ? -3.781  0.265   0.471   1.00 11.11 ?  443 HOH   A O   1 
HETATM 3788 O O   . HOH   F 4 .   ? 16.162  2.977   8.470   1.00 21.66 ?  444 HOH   A O   1 
HETATM 3789 O O   . HOH   F 4 .   ? 14.790  -19.726 -5.545  1.00 37.52 ?  445 HOH   A O   1 
HETATM 3790 O O   . HOH   F 4 .   ? -16.565 -12.759 -9.805  1.00 46.04 ?  446 HOH   A O   1 
HETATM 3791 O O   . HOH   F 4 .   ? -12.651 0.157   -3.275  1.00 29.35 ?  447 HOH   A O   1 
HETATM 3792 O O   . HOH   F 4 .   ? -1.628  9.214   -3.115  1.00 38.37 ?  448 HOH   A O   1 
HETATM 3793 O O   . HOH   F 4 .   ? -11.533 -5.684  -4.236  1.00 15.06 ?  449 HOH   A O   1 
HETATM 3794 O O   . HOH   F 4 .   ? -13.814 -17.371 -14.359 1.00 26.92 ?  450 HOH   A O   1 
HETATM 3795 O O   . HOH   F 4 .   ? -0.627  -11.252 -12.617 1.00 25.98 ?  451 HOH   A O   1 
HETATM 3796 O O   . HOH   F 4 .   ? 15.247  -18.315 -16.668 1.00 25.80 ?  452 HOH   A O   1 
HETATM 3797 O O   . HOH   F 4 .   ? 2.071   -20.118 13.724  1.00 24.46 ?  453 HOH   A O   1 
HETATM 3798 O O   . HOH   F 4 .   ? 12.885  -19.926 -11.964 1.00 25.05 ?  454 HOH   A O   1 
HETATM 3799 O O   . HOH   F 4 .   ? 3.143   -18.520 15.834  1.00 21.04 ?  455 HOH   A O   1 
HETATM 3800 O O   . HOH   F 4 .   ? 17.170  -15.859 -7.923  1.00 24.31 ?  456 HOH   A O   1 
HETATM 3801 O O   . HOH   F 4 .   ? 16.796  -16.626 -0.507  1.00 45.59 ?  457 HOH   A O   1 
HETATM 3802 O O   . HOH   F 4 .   ? 9.774   -19.533 -1.769  1.00 32.52 ?  458 HOH   A O   1 
HETATM 3803 O O   . HOH   F 4 .   ? 6.563   -5.382  -4.090  1.00 23.60 ?  459 HOH   A O   1 
HETATM 3804 O O   . HOH   F 4 .   ? 15.624  10.401  1.502   1.00 38.73 ?  460 HOH   A O   1 
HETATM 3805 O O   . HOH   F 4 .   ? 12.855  1.641   -3.766  1.00 21.37 ?  461 HOH   A O   1 
HETATM 3806 O O   . HOH   F 4 .   ? 14.132  -0.826  -13.524 1.00 40.03 ?  462 HOH   A O   1 
HETATM 3807 O O   . HOH   F 4 .   ? 24.687  -4.440  -9.536  1.00 34.87 ?  463 HOH   A O   1 
HETATM 3808 O O   . HOH   F 4 .   ? -11.143 -6.064  -13.528 1.00 33.84 ?  464 HOH   A O   1 
HETATM 3809 O O   . HOH   F 4 .   ? -8.390  2.058   17.833  1.00 44.61 ?  465 HOH   A O   1 
HETATM 3810 O O   . HOH   F 4 .   ? 8.651   -29.252 0.985   1.00 35.86 ?  466 HOH   A O   1 
HETATM 3811 O O   . HOH   F 4 .   ? 23.266  6.028   12.638  1.00 37.06 ?  467 HOH   A O   1 
HETATM 3812 O O   . HOH   F 4 .   ? -4.814  -18.489 15.108  1.00 25.82 ?  468 HOH   A O   1 
HETATM 3813 O O   . HOH   F 4 .   ? -14.181 2.697   8.267   1.00 38.51 ?  469 HOH   A O   1 
HETATM 3814 O O   . HOH   F 4 .   ? 12.190  3.390   -6.574  1.00 35.75 ?  470 HOH   A O   1 
HETATM 3815 O O   . HOH   F 4 .   ? 10.854  -13.162 -18.823 1.00 19.01 ?  471 HOH   A O   1 
HETATM 3816 O O   . HOH   F 4 .   ? 21.105  -12.616 -19.836 1.00 46.71 ?  472 HOH   A O   1 
HETATM 3817 O O   . HOH   F 4 .   ? 23.251  -1.811  -7.875  1.00 41.94 ?  473 HOH   A O   1 
HETATM 3818 O O   . HOH   F 4 .   ? 15.798  -21.720 -11.252 1.00 47.17 ?  474 HOH   A O   1 
HETATM 3819 O O   . HOH   F 4 .   ? 0.027   5.752   2.207   1.00 32.51 ?  475 HOH   A O   1 
HETATM 3820 O O   . HOH   F 4 .   ? 28.213  -13.944 -5.795  1.00 44.96 ?  476 HOH   A O   1 
HETATM 3821 O O   . HOH   F 4 .   ? -14.896 -7.154  -7.438  1.00 34.98 ?  477 HOH   A O   1 
HETATM 3822 O O   . HOH   F 4 .   ? 21.525  -17.265 -15.986 1.00 35.35 ?  478 HOH   A O   1 
HETATM 3823 O O   . HOH   F 4 .   ? 27.294  -7.406  -10.887 1.00 39.62 ?  479 HOH   A O   1 
HETATM 3824 O O   . HOH   F 4 .   ? 6.397   5.723   -0.462  1.00 47.43 ?  480 HOH   A O   1 
HETATM 3825 O O   . HOH   F 4 .   ? 18.476  9.173   3.725   1.00 35.94 ?  481 HOH   A O   1 
HETATM 3826 O O   . HOH   F 4 .   ? -15.283 -17.029 -7.725  1.00 30.81 ?  482 HOH   A O   1 
HETATM 3827 O O   . HOH   F 4 .   ? 1.791   6.841   5.233   1.00 29.80 ?  483 HOH   A O   1 
HETATM 3828 O O   . HOH   F 4 .   ? 14.243  -3.945  -23.420 1.00 33.60 ?  484 HOH   A O   1 
HETATM 3829 O O   . HOH   F 4 .   ? -13.747 -8.227  -4.381  1.00 16.25 ?  485 HOH   A O   1 
HETATM 3830 O O   . HOH   F 4 .   ? 10.497  11.073  6.775   1.00 41.39 ?  486 HOH   A O   1 
HETATM 3831 O O   . HOH   F 4 .   ? -2.423  -26.262 -9.039  1.00 35.89 ?  487 HOH   A O   1 
HETATM 3832 O O   . HOH   F 4 .   ? 24.966  -12.738 -3.881  1.00 31.03 ?  488 HOH   A O   1 
HETATM 3833 O O   . HOH   F 4 .   ? -1.469  -3.981  -13.704 1.00 39.58 ?  489 HOH   A O   1 
HETATM 3834 O O   . HOH   F 4 .   ? -18.974 -16.468 -1.944  1.00 32.50 ?  490 HOH   A O   1 
HETATM 3835 O O   . HOH   F 4 .   ? -0.551  6.255   10.822  1.00 25.87 ?  491 HOH   A O   1 
HETATM 3836 O O   . HOH   F 4 .   ? -11.067 -11.119 -12.182 1.00 19.21 ?  492 HOH   A O   1 
HETATM 3837 O O   . HOH   F 4 .   ? -16.110 -7.889  -5.449  1.00 30.92 ?  493 HOH   A O   1 
HETATM 3838 O O   . HOH   F 4 .   ? 8.150   -23.998 -7.715  1.00 28.29 ?  494 HOH   A O   1 
HETATM 3839 O O   . HOH   F 4 .   ? -7.637  5.331   -4.899  1.00 35.13 ?  495 HOH   A O   1 
HETATM 3840 O O   . HOH   F 4 .   ? 0.286   -5.763  -17.456 1.00 39.31 ?  496 HOH   A O   1 
HETATM 3841 O O   . HOH   F 4 .   ? 25.046  -6.377  -11.393 1.00 28.93 ?  497 HOH   A O   1 
HETATM 3842 O O   . HOH   F 4 .   ? -14.522 -18.586 -9.763  1.00 38.25 ?  498 HOH   A O   1 
HETATM 3843 O O   . HOH   F 4 .   ? 17.297  -15.077 -23.597 1.00 31.52 ?  499 HOH   A O   1 
HETATM 3844 O O   . HOH   F 4 .   ? 21.766  -1.390  -14.763 1.00 34.79 ?  500 HOH   A O   1 
HETATM 3845 O O   . HOH   F 4 .   ? 14.772  3.919   -4.944  1.00 24.81 ?  501 HOH   A O   1 
HETATM 3846 O O   . HOH   F 4 .   ? -11.619 -0.501  -5.545  1.00 34.40 ?  502 HOH   A O   1 
HETATM 3847 O O   . HOH   F 4 .   ? 10.449  -1.201  -3.775  1.00 27.23 ?  503 HOH   A O   1 
HETATM 3848 O O   . HOH   F 4 .   ? 12.009  -20.413 -2.966  1.00 35.94 ?  504 HOH   A O   1 
HETATM 3849 O O   . HOH   F 4 .   ? -8.895  -24.613 -2.230  1.00 28.24 ?  505 HOH   A O   1 
HETATM 3850 O O   . HOH   F 4 .   ? -9.546  -19.292 -15.314 1.00 27.58 ?  506 HOH   A O   1 
HETATM 3851 O O   . HOH   F 4 .   ? 10.443  -21.957 -6.587  1.00 37.45 ?  507 HOH   A O   1 
HETATM 3852 O O   . HOH   F 4 .   ? -3.916  -25.796 -6.661  1.00 41.46 ?  508 HOH   A O   1 
HETATM 3853 O O   . HOH   F 4 .   ? -8.121  -2.024  -10.129 1.00 33.02 ?  509 HOH   A O   1 
HETATM 3854 O O   . HOH   F 4 .   ? -18.437 -6.508  -4.569  1.00 34.54 ?  510 HOH   A O   1 
HETATM 3855 O O   . HOH   F 4 .   ? 0.126   -10.151 -15.343 1.00 34.11 ?  511 HOH   A O   1 
HETATM 3856 O O   . HOH   F 4 .   ? -7.525  -0.877  -7.888  1.00 37.91 ?  512 HOH   A O   1 
HETATM 3857 O O   . HOH   F 4 .   ? 3.480   -27.624 -8.217  1.00 37.86 ?  513 HOH   A O   1 
HETATM 3858 O O   . HOH   F 4 .   ? 12.135  -22.108 -10.200 1.00 38.30 ?  514 HOH   A O   1 
HETATM 3859 O O   . HOH   F 4 .   ? -2.529  -9.568  -16.289 1.00 41.17 ?  515 HOH   A O   1 
HETATM 3860 O O   . HOH   F 4 .   ? -12.927 -22.398 -4.333  1.00 35.79 ?  516 HOH   A O   1 
HETATM 3861 O O   . HOH   G 4 .   ? -5.077  -6.856  -22.983 1.00 39.63 ?  401 HOH   B O   1 
HETATM 3862 O O   . HOH   G 4 .   ? -10.116 -29.629 -33.366 1.00 50.35 ?  402 HOH   B O   1 
HETATM 3863 O O   . HOH   G 4 .   ? -6.313  -8.719  -20.728 1.00 42.36 ?  403 HOH   B O   1 
HETATM 3864 O O   . HOH   G 4 .   ? -0.466  -14.731 -49.591 1.00 38.13 ?  404 HOH   B O   1 
HETATM 3865 O O   . HOH   G 4 .   ? 4.008   -20.591 -55.172 1.00 40.74 ?  405 HOH   B O   1 
HETATM 3866 O O   . HOH   G 4 .   ? -5.177  -11.327 -29.682 1.00 33.25 ?  406 HOH   B O   1 
HETATM 3867 O O   . HOH   G 4 .   ? -8.999  -34.764 -37.672 1.00 29.46 ?  407 HOH   B O   1 
HETATM 3868 O O   . HOH   G 4 .   ? 9.974   -31.824 -48.210 1.00 34.97 ?  408 HOH   B O   1 
HETATM 3869 O O   . HOH   G 4 .   ? 8.100   -30.093 -18.584 1.00 51.03 ?  409 HOH   B O   1 
HETATM 3870 O O   . HOH   G 4 .   ? -1.278  -12.993 -14.841 1.00 20.38 ?  410 HOH   B O   1 
HETATM 3871 O O   . HOH   G 4 .   ? 4.665   -35.358 -21.974 1.00 30.95 ?  411 HOH   B O   1 
HETATM 3872 O O   . HOH   G 4 .   ? -20.838 -22.116 -21.927 1.00 33.84 ?  412 HOH   B O   1 
HETATM 3873 O O   . HOH   G 4 .   ? -14.970 -23.329 -32.555 1.00 21.72 ?  413 HOH   B O   1 
HETATM 3874 O O   . HOH   G 4 .   ? -17.918 -24.428 -46.579 1.00 29.21 ?  414 HOH   B O   1 
HETATM 3875 O O   . HOH   G 4 .   ? 12.442  -23.539 -17.404 1.00 25.54 ?  415 HOH   B O   1 
HETATM 3876 O O   . HOH   G 4 .   ? -26.785 -16.522 -37.253 1.00 19.81 ?  416 HOH   B O   1 
HETATM 3877 O O   . HOH   G 4 .   ? -12.314 -18.062 -49.030 1.00 26.08 ?  417 HOH   B O   1 
HETATM 3878 O O   . HOH   G 4 .   ? -0.204  -18.069 -55.493 1.00 28.14 ?  418 HOH   B O   1 
HETATM 3879 O O   . HOH   G 4 .   ? -3.015  -16.659 -34.210 1.00 18.49 ?  419 HOH   B O   1 
HETATM 3880 O O   . HOH   G 4 .   ? 9.700   -13.882 -24.178 1.00 26.70 ?  420 HOH   B O   1 
HETATM 3881 O O   . HOH   G 4 .   ? 10.359  -13.275 -35.091 1.00 14.05 ?  421 HOH   B O   1 
HETATM 3882 O O   . HOH   G 4 .   ? 8.245   -32.364 -51.768 1.00 39.98 ?  422 HOH   B O   1 
HETATM 3883 O O   A HOH   G 4 .   ? -2.750  -18.839 -32.573 0.50 21.89 ?  423 HOH   B O   1 
HETATM 3884 O O   . HOH   G 4 .   ? -8.834  -17.408 -54.742 1.00 39.67 ?  424 HOH   B O   1 
HETATM 3885 O O   . HOH   G 4 .   ? 21.359  -24.468 -40.833 1.00 33.44 ?  425 HOH   B O   1 
HETATM 3886 O O   . HOH   G 4 .   ? -6.159  -28.578 -27.263 1.00 28.69 ?  426 HOH   B O   1 
HETATM 3887 O O   . HOH   G 4 .   ? 14.137  -18.355 -25.351 1.00 15.61 ?  427 HOH   B O   1 
HETATM 3888 O O   . HOH   G 4 .   ? 10.734  -10.706 -42.734 1.00 24.78 ?  428 HOH   B O   1 
HETATM 3889 O O   . HOH   G 4 .   ? -8.241  -20.218 -17.497 1.00 22.89 ?  429 HOH   B O   1 
HETATM 3890 O O   . HOH   G 4 .   ? 17.310  -18.808 -18.727 1.00 29.40 ?  430 HOH   B O   1 
HETATM 3891 O O   . HOH   G 4 .   ? -4.041  -25.773 -20.119 1.00 17.40 ?  431 HOH   B O   1 
HETATM 3892 O O   . HOH   G 4 .   ? 5.113   -34.182 -34.817 1.00 20.68 ?  432 HOH   B O   1 
HETATM 3893 O O   . HOH   G 4 .   ? -7.804  -34.506 -41.537 1.00 28.70 ?  433 HOH   B O   1 
HETATM 3894 O O   . HOH   G 4 .   ? 16.255  -28.914 -45.789 1.00 33.17 ?  434 HOH   B O   1 
HETATM 3895 O O   . HOH   G 4 .   ? 20.449  -22.875 -25.832 1.00 47.03 ?  435 HOH   B O   1 
HETATM 3896 O O   . HOH   G 4 .   ? 4.249   -15.573 -23.901 1.00 23.29 ?  436 HOH   B O   1 
HETATM 3897 O O   . HOH   G 4 .   ? -12.627 -27.539 -43.182 1.00 34.89 ?  437 HOH   B O   1 
HETATM 3898 O O   . HOH   G 4 .   ? 6.011   -29.205 -17.276 1.00 36.61 ?  438 HOH   B O   1 
HETATM 3899 O O   . HOH   G 4 .   ? 2.001   -13.283 -48.908 1.00 18.37 ?  439 HOH   B O   1 
HETATM 3900 O O   . HOH   G 4 .   ? 7.228   -14.056 -20.723 1.00 17.80 ?  440 HOH   B O   1 
HETATM 3901 O O   . HOH   G 4 .   ? 0.531   -32.023 -27.505 1.00 28.14 ?  441 HOH   B O   1 
HETATM 3902 O O   . HOH   G 4 .   ? 16.487  -13.181 -42.245 1.00 41.67 ?  442 HOH   B O   1 
HETATM 3903 O O   . HOH   G 4 .   ? 2.520   -30.042 -18.264 1.00 29.28 ?  443 HOH   B O   1 
HETATM 3904 O O   . HOH   G 4 .   ? -13.449 -22.164 -24.418 1.00 24.23 ?  444 HOH   B O   1 
HETATM 3905 O O   . HOH   G 4 .   ? 7.116   -16.675 -45.957 1.00 16.99 ?  445 HOH   B O   1 
HETATM 3906 O O   . HOH   G 4 .   ? -17.476 -7.960  -43.264 1.00 36.20 ?  446 HOH   B O   1 
HETATM 3907 O O   . HOH   G 4 .   ? -7.198  -27.919 -29.475 1.00 31.32 ?  447 HOH   B O   1 
HETATM 3908 O O   . HOH   G 4 .   ? -7.700  -30.438 -47.309 1.00 20.30 ?  448 HOH   B O   1 
HETATM 3909 O O   . HOH   G 4 .   ? -0.915  -34.401 -30.116 1.00 41.54 ?  449 HOH   B O   1 
HETATM 3910 O O   . HOH   G 4 .   ? 9.514   -30.495 -20.795 1.00 27.16 ?  450 HOH   B O   1 
HETATM 3911 O O   . HOH   G 4 .   ? 8.202   -34.995 -28.500 1.00 36.35 ?  451 HOH   B O   1 
HETATM 3912 O O   . HOH   G 4 .   ? 1.730   -13.481 -18.276 1.00 15.82 ?  452 HOH   B O   1 
HETATM 3913 O O   . HOH   G 4 .   ? -18.057 -11.703 -35.832 1.00 33.45 ?  453 HOH   B O   1 
HETATM 3914 O O   . HOH   G 4 .   ? -12.106 -30.791 -43.878 1.00 47.68 ?  454 HOH   B O   1 
HETATM 3915 O O   . HOH   G 4 .   ? 1.314   -39.469 -38.089 1.00 26.63 ?  455 HOH   B O   1 
HETATM 3916 O O   . HOH   G 4 .   ? -21.625 -18.520 -34.046 1.00 19.99 ?  456 HOH   B O   1 
HETATM 3917 O O   . HOH   G 4 .   ? 7.448   -15.220 -41.327 1.00 16.18 ?  457 HOH   B O   1 
HETATM 3918 O O   . HOH   G 4 .   ? 17.350  -24.505 -34.251 1.00 17.97 ?  458 HOH   B O   1 
HETATM 3919 O O   . HOH   G 4 .   ? 3.898   -36.418 -35.803 1.00 27.63 ?  459 HOH   B O   1 
HETATM 3920 O O   . HOH   G 4 .   ? -21.075 -12.393 -30.549 1.00 31.30 ?  460 HOH   B O   1 
HETATM 3921 O O   . HOH   G 4 .   ? 19.005  -32.720 -40.078 1.00 37.58 ?  461 HOH   B O   1 
HETATM 3922 O O   . HOH   G 4 .   ? 1.293   -34.700 -33.245 1.00 23.68 ?  462 HOH   B O   1 
HETATM 3923 O O   . HOH   G 4 .   ? -22.383 -22.595 -40.691 1.00 32.14 ?  463 HOH   B O   1 
HETATM 3924 O O   . HOH   G 4 .   ? 6.611   -15.086 -25.172 1.00 16.53 ?  464 HOH   B O   1 
HETATM 3925 O O   . HOH   G 4 .   ? -6.569  -13.425 -36.884 1.00 26.85 ?  465 HOH   B O   1 
HETATM 3926 O O   . HOH   G 4 .   ? 11.133  -19.934 -49.987 1.00 35.13 ?  466 HOH   B O   1 
HETATM 3927 O O   . HOH   G 4 .   ? 16.127  -12.908 -38.456 1.00 34.20 ?  467 HOH   B O   1 
HETATM 3928 O O   . HOH   G 4 .   ? -12.985 -28.716 -38.611 1.00 27.66 ?  468 HOH   B O   1 
HETATM 3929 O O   . HOH   G 4 .   ? 0.239   -39.424 -40.813 1.00 24.49 ?  469 HOH   B O   1 
HETATM 3930 O O   . HOH   G 4 .   ? -9.153  -11.270 -38.990 1.00 25.56 ?  470 HOH   B O   1 
HETATM 3931 O O   . HOH   G 4 .   ? -14.741 -24.279 -36.077 1.00 31.75 ?  471 HOH   B O   1 
HETATM 3932 O O   . HOH   G 4 .   ? -10.307 -23.491 -51.847 1.00 35.18 ?  472 HOH   B O   1 
HETATM 3933 O O   B HOH   G 4 .   ? -1.887  -18.155 -30.692 0.50 12.60 ?  473 HOH   B O   1 
HETATM 3934 O O   . HOH   G 4 .   ? 8.285   -17.261 -49.409 1.00 25.51 ?  474 HOH   B O   1 
HETATM 3935 O O   . HOH   G 4 .   ? -9.125  -22.501 -18.687 1.00 23.79 ?  475 HOH   B O   1 
HETATM 3936 O O   . HOH   G 4 .   ? -10.988 -9.148  -39.789 1.00 32.52 ?  476 HOH   B O   1 
HETATM 3937 O O   . HOH   G 4 .   ? 15.139  -16.712 -33.852 1.00 15.28 ?  477 HOH   B O   1 
HETATM 3938 O O   . HOH   G 4 .   ? -4.987  -34.806 -31.925 1.00 45.70 ?  478 HOH   B O   1 
HETATM 3939 O O   . HOH   G 4 .   ? 9.544   -16.434 -46.882 1.00 36.04 ?  479 HOH   B O   1 
HETATM 3940 O O   . HOH   G 4 .   ? -2.729  -34.804 -31.385 1.00 37.76 ?  480 HOH   B O   1 
HETATM 3941 O O   . HOH   G 4 .   ? -7.194  -12.880 -17.912 1.00 18.28 ?  481 HOH   B O   1 
HETATM 3942 O O   . HOH   G 4 .   ? -18.630 -23.741 -28.527 1.00 31.53 ?  482 HOH   B O   1 
HETATM 3943 O O   . HOH   G 4 .   ? -13.950 -26.104 -34.442 1.00 37.81 ?  483 HOH   B O   1 
HETATM 3944 O O   . HOH   G 4 .   ? 18.383  -17.092 -45.100 1.00 33.85 ?  484 HOH   B O   1 
HETATM 3945 O O   . HOH   G 4 .   ? 2.122   -25.946 -16.228 1.00 28.52 ?  485 HOH   B O   1 
HETATM 3946 O O   . HOH   G 4 .   ? 1.116   -12.605 -20.924 1.00 18.25 ?  486 HOH   B O   1 
HETATM 3947 O O   . HOH   G 4 .   ? -11.747 -18.123 -16.169 1.00 24.89 ?  487 HOH   B O   1 
HETATM 3948 O O   . HOH   G 4 .   ? -10.631 -6.876  -29.995 1.00 42.10 ?  488 HOH   B O   1 
HETATM 3949 O O   . HOH   G 4 .   ? 17.286  -18.607 -32.204 1.00 14.97 ?  489 HOH   B O   1 
HETATM 3950 O O   . HOH   G 4 .   ? -13.862 -25.532 -41.858 1.00 25.31 ?  490 HOH   B O   1 
HETATM 3951 O O   . HOH   G 4 .   ? 3.357   -11.982 -46.023 1.00 28.66 ?  491 HOH   B O   1 
HETATM 3952 O O   . HOH   G 4 .   ? -3.922  -10.789 -25.299 1.00 28.26 ?  492 HOH   B O   1 
HETATM 3953 O O   . HOH   G 4 .   ? 14.547  -20.777 -51.722 1.00 28.13 ?  493 HOH   B O   1 
HETATM 3954 O O   . HOH   G 4 .   ? -17.304 -23.758 -31.291 1.00 33.02 ?  494 HOH   B O   1 
HETATM 3955 O O   . HOH   G 4 .   ? 20.476  -27.717 -27.345 1.00 32.67 ?  495 HOH   B O   1 
HETATM 3956 O O   . HOH   G 4 .   ? -5.783  -22.998 -14.204 1.00 38.51 ?  496 HOH   B O   1 
HETATM 3957 O O   . HOH   G 4 .   ? -19.438 -23.070 -35.458 1.00 36.00 ?  497 HOH   B O   1 
HETATM 3958 O O   . HOH   G 4 .   ? 18.289  -22.731 -21.267 1.00 37.61 ?  498 HOH   B O   1 
HETATM 3959 O O   . HOH   G 4 .   ? 19.005  -23.052 -23.704 1.00 36.26 ?  499 HOH   B O   1 
HETATM 3960 O O   . HOH   G 4 .   ? 11.077  -22.047 -53.564 1.00 45.81 ?  500 HOH   B O   1 
HETATM 3961 O O   . HOH   G 4 .   ? 9.300   -36.046 -30.382 1.00 45.07 ?  501 HOH   B O   1 
HETATM 3962 O O   . HOH   G 4 .   ? 3.694   -35.243 -32.474 1.00 32.81 ?  502 HOH   B O   1 
HETATM 3963 O O   . HOH   G 4 .   ? -16.603 -11.510 -19.478 1.00 41.42 ?  503 HOH   B O   1 
HETATM 3964 O O   . HOH   G 4 .   ? -21.238 -12.769 -27.979 1.00 44.41 ?  504 HOH   B O   1 
HETATM 3965 O O   . HOH   G 4 .   ? -1.266  -14.251 -52.117 1.00 37.90 ?  505 HOH   B O   1 
HETATM 3966 O O   . HOH   G 4 .   ? -1.974  -36.434 -20.119 1.00 49.34 ?  506 HOH   B O   1 
HETATM 3967 O O   . HOH   G 4 .   ? 14.722  -15.864 -24.209 1.00 20.39 ?  507 HOH   B O   1 
HETATM 3968 O O   . HOH   G 4 .   ? 15.234  -11.710 -36.298 1.00 34.59 ?  508 HOH   B O   1 
HETATM 3969 O O   . HOH   G 4 .   ? 12.483  -9.313  -44.140 1.00 37.24 ?  509 HOH   B O   1 
HETATM 3970 O O   . HOH   G 4 .   ? -15.907 -5.280  -24.732 1.00 41.82 ?  510 HOH   B O   1 
HETATM 3971 O O   . HOH   G 4 .   ? -7.569  -10.422 -16.482 1.00 39.66 ?  511 HOH   B O   1 
HETATM 3972 O O   . HOH   G 4 .   ? -12.147 -25.459 -25.929 1.00 43.67 ?  512 HOH   B O   1 
HETATM 3973 O O   . HOH   G 4 .   ? -13.883 -10.989 -12.844 1.00 34.59 ?  513 HOH   B O   1 
HETATM 3974 O O   . HOH   G 4 .   ? -6.963  -27.381 -21.647 1.00 38.49 ?  514 HOH   B O   1 
HETATM 3975 O O   . HOH   G 4 .   ? 18.551  -15.870 -30.336 1.00 41.79 ?  515 HOH   B O   1 
HETATM 3976 O O   . HOH   G 4 .   ? -7.099  -4.431  -18.711 1.00 42.13 ?  516 HOH   B O   1 
HETATM 3977 O O   . HOH   G 4 .   ? -21.423 -22.819 -29.605 1.00 32.29 ?  517 HOH   B O   1 
HETATM 3978 O O   . HOH   G 4 .   ? 18.471  -16.357 -25.769 1.00 38.40 ?  518 HOH   B O   1 
HETATM 3979 O O   . HOH   G 4 .   ? -1.271  -10.539 -40.131 1.00 37.50 ?  519 HOH   B O   1 
HETATM 3980 O O   . HOH   G 4 .   ? 22.524  -26.787 -28.459 1.00 39.19 ?  520 HOH   B O   1 
HETATM 3981 O O   . HOH   G 4 .   ? -11.218 -31.386 -36.241 1.00 33.68 ?  521 HOH   B O   1 
HETATM 3982 O O   . HOH   G 4 .   ? 13.321  -19.654 -16.821 1.00 28.31 ?  522 HOH   B O   1 
HETATM 3983 O O   . HOH   G 4 .   ? -17.825 -24.913 -43.833 1.00 37.02 ?  523 HOH   B O   1 
HETATM 3984 O O   . HOH   G 4 .   ? -14.358 -10.216 -15.046 1.00 48.44 ?  524 HOH   B O   1 
HETATM 3985 O O   . HOH   G 4 .   ? -0.263  -26.500 -15.413 1.00 35.84 ?  525 HOH   B O   1 
HETATM 3986 O O   . HOH   G 4 .   ? 3.388   -12.572 -22.687 1.00 31.48 ?  526 HOH   B O   1 
HETATM 3987 O O   . HOH   G 4 .   ? -23.591 -18.912 -32.576 1.00 31.46 ?  527 HOH   B O   1 
HETATM 3988 O O   . HOH   G 4 .   ? -0.754  -34.533 -27.420 1.00 38.34 ?  528 HOH   B O   1 
HETATM 3989 O O   . HOH   G 4 .   ? 6.249   -11.701 -22.610 1.00 38.99 ?  529 HOH   B O   1 
HETATM 3990 O O   A HOH   G 4 .   ? -16.260 -26.394 -42.918 1.00 43.20 ?  530 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   . ASP   A 3   ? 0.5284 0.6633 0.5460 -0.0116 0.0131  -0.0465 3   ASP   A N   
2    C CA  . ASP   A 3   ? 0.4801 0.6152 0.4989 -0.0113 0.0132  -0.0470 3   ASP   A CA  
3    C C   . ASP   A 3   ? 0.3885 0.5150 0.4063 -0.0108 0.0138  -0.0428 3   ASP   A C   
4    O O   . ASP   A 3   ? 0.3209 0.4442 0.3347 -0.0085 0.0117  -0.0389 3   ASP   A O   
5    C CB  . ASP   A 3   ? 0.5166 0.6581 0.5330 -0.0090 0.0104  -0.0473 3   ASP   A CB  
6    C CG  . ASP   A 3   ? 0.5652 0.7074 0.5826 -0.0084 0.0101  -0.0477 3   ASP   A CG  
7    O OD1 . ASP   A 3   ? 0.5498 0.6869 0.5691 -0.0097 0.0122  -0.0471 3   ASP   A OD1 
8    O OD2 . ASP   A 3   ? 0.6273 0.7756 0.6437 -0.0065 0.0079  -0.0487 3   ASP   A OD2 
9    N N   . LEU   A 4   ? 0.3499 0.4724 0.3712 -0.0130 0.0168  -0.0438 4   LEU   A N   
10   C CA  . LEU   A 4   ? 0.3629 0.4775 0.3834 -0.0127 0.0175  -0.0400 4   LEU   A CA  
11   C C   . LEU   A 4   ? 0.3348 0.4488 0.3533 -0.0114 0.0163  -0.0382 4   LEU   A C   
12   O O   . LEU   A 4   ? 0.3191 0.4280 0.3351 -0.0100 0.0155  -0.0343 4   LEU   A O   
13   C CB  . LEU   A 4   ? 0.3893 0.5001 0.4140 -0.0154 0.0211  -0.0416 4   LEU   A CB  
14   C CG  . LEU   A 4   ? 0.3863 0.4886 0.4102 -0.0151 0.0220  -0.0376 4   LEU   A CG  
15   C CD1 . LEU   A 4   ? 0.3630 0.4621 0.3838 -0.0133 0.0202  -0.0341 4   LEU   A CD1 
16   C CD2 . LEU   A 4   ? 0.4150 0.5138 0.4434 -0.0176 0.0256  -0.0393 4   LEU   A CD2 
17   N N   . LYS   A 5   ? 0.3230 0.4429 0.3432 -0.0117 0.0163  -0.0414 5   LYS   A N   
18   C CA  . LYS   A 5   ? 0.2977 0.4175 0.3165 -0.0105 0.0152  -0.0401 5   LYS   A CA  
19   C C   . LYS   A 5   ? 0.2903 0.4102 0.3048 -0.0073 0.0118  -0.0369 5   LYS   A C   
20   O O   . LYS   A 5   ? 0.2660 0.3820 0.2784 -0.0060 0.0110  -0.0338 5   LYS   A O   
21   C CB  . LYS   A 5   ? 0.3648 0.4916 0.3866 -0.0114 0.0158  -0.0446 5   LYS   A CB  
22   C CG  . LYS   A 5   ? 0.4268 0.5519 0.4525 -0.0147 0.0195  -0.0470 5   LYS   A CG  
23   C CD  . LYS   A 5   ? 0.4918 0.6243 0.5207 -0.0159 0.0202  -0.0521 5   LYS   A CD  
24   C CE  . LYS   A 5   ? 0.5618 0.6936 0.5952 -0.0196 0.0243  -0.0554 5   LYS   A CE  
25   N NZ  . LYS   A 5   ? 0.6130 0.7393 0.6463 -0.0208 0.0262  -0.0534 5   LYS   A NZ  
26   N N   . ALA   A 6   ? 0.2799 0.4043 0.2931 -0.0061 0.0100  -0.0378 6   ALA   A N   
27   C CA  . ALA   A 6   ? 0.2685 0.3930 0.2776 -0.0032 0.0069  -0.0348 6   ALA   A CA  
28   C C   . ALA   A 6   ? 0.2608 0.3780 0.2670 -0.0025 0.0067  -0.0304 6   ALA   A C   
29   O O   . ALA   A 6   ? 0.2562 0.3708 0.2596 -0.0005 0.0049  -0.0274 6   ALA   A O   
30   C CB  . ALA   A 6   ? 0.3095 0.4404 0.3177 -0.0025 0.0054  -0.0367 6   ALA   A CB  
31   N N   . SER   A 7   ? 0.2461 0.3602 0.2533 -0.0042 0.0084  -0.0304 7   SER   A N   
32   C CA  . SER   A 7   ? 0.2699 0.3776 0.2747 -0.0037 0.0082  -0.0266 7   SER   A CA  
33   C C   . SER   A 7   ? 0.2339 0.3364 0.2389 -0.0037 0.0091  -0.0244 7   SER   A C   
34   O O   . SER   A 7   ? 0.2206 0.3193 0.2230 -0.0024 0.0080  -0.0212 7   SER   A O   
35   C CB  . SER   A 7   ? 0.2725 0.3786 0.2785 -0.0051 0.0096  -0.0271 7   SER   A CB  
36   O OG  . SER   A 7   ? 0.3381 0.4447 0.3483 -0.0074 0.0122  -0.0300 7   SER   A OG  
37   N N   . SER   A 8   ? 0.2282 0.3310 0.2363 -0.0054 0.0111  -0.0264 8   SER   A N   
38   C CA  . SER   A 8   ? 0.2072 0.3054 0.2153 -0.0057 0.0121  -0.0243 8   SER   A CA  
39   C C   . SER   A 8   ? 0.2043 0.3032 0.2103 -0.0039 0.0103  -0.0229 8   SER   A C   
40   O O   . SER   A 8   ? 0.1959 0.2906 0.2001 -0.0032 0.0100  -0.0200 8   SER   A O   
41   C CB  . SER   A 8   ? 0.2274 0.3259 0.2391 -0.0081 0.0149  -0.0268 8   SER   A CB  
42   O OG  . SER   A 8   ? 0.2681 0.3648 0.2819 -0.0097 0.0167  -0.0278 8   SER   A OG  
43   N N   . LEU   A 9   ? 0.2036 0.3079 0.2100 -0.0031 0.0091  -0.0252 9   LEU   A N   
44   C CA  . LEU   A 9   ? 0.2165 0.3219 0.2212 -0.0011 0.0072  -0.0242 9   LEU   A CA  
45   C C   . LEU   A 9   ? 0.1999 0.3023 0.2011 0.0011  0.0051  -0.0208 9   LEU   A C   
46   O O   . LEU   A 9   ? 0.1967 0.2963 0.1963 0.0022  0.0044  -0.0186 9   LEU   A O   
47   C CB  . LEU   A 9   ? 0.2471 0.3594 0.2531 -0.0003 0.0060  -0.0274 9   LEU   A CB  
48   C CG  . LEU   A 9   ? 0.2725 0.3864 0.2777 0.0019  0.0042  -0.0269 9   LEU   A CG  
49   C CD1 . LEU   A 9   ? 0.2775 0.3890 0.2836 0.0009  0.0056  -0.0266 9   LEU   A CD1 
50   C CD2 . LEU   A 9   ? 0.3267 0.4482 0.3337 0.0027  0.0030  -0.0305 9   LEU   A CD2 
51   N N   A ARG   A 10  ? 0.1968 0.2999 0.1966 0.0016  0.0043  -0.0205 10  ARG   A N   
52   N N   B ARG   A 10  ? 0.2000 0.3032 0.1999 0.0015  0.0044  -0.0206 10  ARG   A N   
53   C CA  A ARG   A 10  ? 0.1830 0.2831 0.1794 0.0033  0.0026  -0.0173 10  ARG   A CA  
54   C CA  B ARG   A 10  ? 0.1880 0.2883 0.1845 0.0032  0.0027  -0.0176 10  ARG   A CA  
55   C C   A ARG   A 10  ? 0.1722 0.2663 0.1679 0.0027  0.0036  -0.0148 10  ARG   A C   
56   C C   B ARG   A 10  ? 0.1746 0.2688 0.1702 0.0027  0.0036  -0.0149 10  ARG   A C   
57   O O   A ARG   A 10  ? 0.1685 0.2597 0.1620 0.0040  0.0026  -0.0124 10  ARG   A O   
58   O O   B ARG   A 10  ? 0.1695 0.2611 0.1630 0.0040  0.0026  -0.0125 10  ARG   A O   
59   C CB  A ARG   A 10  ? 0.1858 0.2875 0.1805 0.0035  0.0018  -0.0173 10  ARG   A CB  
60   C CB  B ARG   A 10  ? 0.1945 0.2973 0.1901 0.0030  0.0022  -0.0183 10  ARG   A CB  
61   C CG  A ARG   A 10  ? 0.1860 0.2834 0.1773 0.0046  0.0008  -0.0140 10  ARG   A CG  
62   C CG  B ARG   A 10  ? 0.1955 0.2975 0.1873 0.0051  0.0001  -0.0158 10  ARG   A CG  
63   C CD  A ARG   A 10  ? 0.1928 0.2920 0.1813 0.0055  -0.0005 -0.0134 10  ARG   A CD  
64   C CD  B ARG   A 10  ? 0.1978 0.3012 0.1881 0.0045  0.0000  -0.0160 10  ARG   A CD  
65   N NE  A ARG   A 10  ? 0.1755 0.2779 0.1653 0.0038  0.0004  -0.0157 10  ARG   A NE  
66   N NE  B ARG   A 10  ? 0.2013 0.3021 0.1876 0.0062  -0.0016 -0.0129 10  ARG   A NE  
67   C CZ  A ARG   A 10  ? 0.1680 0.2706 0.1559 0.0033  0.0004  -0.0152 10  ARG   A CZ  
68   C CZ  B ARG   A 10  ? 0.2148 0.3159 0.1986 0.0061  -0.0020 -0.0120 10  ARG   A CZ  
69   N NH1 A ARG   A 10  ? 0.1638 0.2639 0.1479 0.0046  -0.0009 -0.0124 10  ARG   A NH1 
70   N NH1 B ARG   A 10  ? 0.2208 0.3240 0.2059 0.0042  -0.0008 -0.0140 10  ARG   A NH1 
71   N NH2 A ARG   A 10  ? 0.1537 0.2588 0.1436 0.0015  0.0017  -0.0177 10  ARG   A NH2 
72   N NH2 B ARG   A 10  ? 0.2070 0.3062 0.1871 0.0078  -0.0035 -0.0093 10  ARG   A NH2 
73   N N   . ALA   A 11  ? 0.1633 0.2556 0.1608 0.0007  0.0056  -0.0153 11  ALA   A N   
74   C CA  . ALA   A 11  ? 0.1535 0.2406 0.1504 0.0004  0.0064  -0.0129 11  ALA   A CA  
75   C C   . ALA   A 11  ? 0.1472 0.2324 0.1438 0.0007  0.0066  -0.0116 11  ALA   A C   
76   O O   . ALA   A 11  ? 0.1446 0.2267 0.1394 0.0014  0.0061  -0.0093 11  ALA   A O   
77   C CB  . ALA   A 11  ? 0.1535 0.2391 0.1527 -0.0014 0.0085  -0.0137 11  ALA   A CB  
78   N N   . LEU   A 12  ? 0.1553 0.2429 0.1537 -0.0001 0.0074  -0.0135 12  LEU   A N   
79   C CA  . LEU   A 12  ? 0.1622 0.2488 0.1605 -0.0001 0.0078  -0.0128 12  LEU   A CA  
80   C C   . LEU   A 12  ? 0.1641 0.2504 0.1602 0.0019  0.0058  -0.0113 12  LEU   A C   
81   O O   . LEU   A 12  ? 0.1512 0.2348 0.1462 0.0022  0.0059  -0.0094 12  LEU   A O   
82   C CB  . LEU   A 12  ? 0.1776 0.2676 0.1784 -0.0014 0.0090  -0.0155 12  LEU   A CB  
83   C CG  . LEU   A 12  ? 0.1758 0.2652 0.1766 -0.0018 0.0097  -0.0151 12  LEU   A CG  
84   C CD1 . LEU   A 12  ? 0.1892 0.2803 0.1926 -0.0041 0.0120  -0.0175 12  LEU   A CD1 
85   C CD2 . LEU   A 12  ? 0.1841 0.2763 0.1842 0.0000  0.0078  -0.0157 12  LEU   A CD2 
86   N N   . LYS   A 13  ? 0.1626 0.2518 0.1582 0.0035  0.0041  -0.0121 13  LYS   A N   
87   C CA  . LYS   A 13  ? 0.1673 0.2561 0.1611 0.0055  0.0023  -0.0109 13  LYS   A CA  
88   C C   . LYS   A 13  ? 0.1564 0.2413 0.1477 0.0062  0.0016  -0.0082 13  LYS   A C   
89   O O   . LYS   A 13  ? 0.1620 0.2458 0.1519 0.0078  0.0004  -0.0071 13  LYS   A O   
90   C CB  . LYS   A 13  ? 0.1773 0.2703 0.1712 0.0071  0.0006  -0.0125 13  LYS   A CB  
91   C CG  . LYS   A 13  ? 0.2016 0.2990 0.1981 0.0068  0.0010  -0.0154 13  LYS   A CG  
92   C CD  . LYS   A 13  ? 0.2432 0.3458 0.2404 0.0084  -0.0007 -0.0173 13  LYS   A CD  
93   C CE  . LYS   A 13  ? 0.2614 0.3684 0.2616 0.0075  0.0001  -0.0205 13  LYS   A CE  
94   N NZ  . LYS   A 13  ? 0.3032 0.4160 0.3043 0.0092  -0.0016 -0.0227 13  LYS   A NZ  
95   N N   . LEU   A 14  ? 0.1495 0.2324 0.1406 0.0051  0.0026  -0.0076 14  LEU   A N   
96   C CA  . LEU   A 14  ? 0.1606 0.2400 0.1497 0.0053  0.0023  -0.0054 14  LEU   A CA  
97   C C   . LEU   A 14  ? 0.1617 0.2381 0.1511 0.0044  0.0035  -0.0042 14  LEU   A C   
98   O O   . LEU   A 14  ? 0.1479 0.2219 0.1362 0.0045  0.0035  -0.0027 14  LEU   A O   
99   C CB  . LEU   A 14  ? 0.1597 0.2395 0.1483 0.0049  0.0023  -0.0057 14  LEU   A CB  
100  C CG  . LEU   A 14  ? 0.1714 0.2545 0.1591 0.0059  0.0010  -0.0066 14  LEU   A CG  
101  C CD1 . LEU   A 14  ? 0.1645 0.2487 0.1520 0.0050  0.0013  -0.0073 14  LEU   A CD1 
102  C CD2 . LEU   A 14  ? 0.1721 0.2537 0.1572 0.0078  -0.0006 -0.0048 14  LEU   A CD2 
103  N N   . MET   A 15  ? 0.1687 0.2456 0.1595 0.0036  0.0045  -0.0047 15  MET   A N   
104  C CA  . MET   A 15  ? 0.1701 0.2444 0.1609 0.0029  0.0055  -0.0032 15  MET   A CA  
105  C C   . MET   A 15  ? 0.1646 0.2378 0.1539 0.0038  0.0048  -0.0018 15  MET   A C   
106  O O   . MET   A 15  ? 0.1713 0.2458 0.1604 0.0044  0.0042  -0.0024 15  MET   A O   
107  C CB  . MET   A 15  ? 0.1854 0.2600 0.1779 0.0015  0.0072  -0.0039 15  MET   A CB  
108  C CG  . MET   A 15  ? 0.2126 0.2871 0.2069 0.0003  0.0084  -0.0049 15  MET   A CG  
109  S SD  . MET   A 15  ? 0.2360 0.3094 0.2321 -0.0015 0.0108  -0.0050 15  MET   A SD  
110  C CE  . MET   A 15  ? 0.2452 0.3145 0.2398 -0.0011 0.0110  -0.0017 15  MET   A CE  
111  N N   . ASP   A 16  ? 0.1584 0.2292 0.1469 0.0037  0.0050  -0.0002 16  ASP   A N   
112  C CA  . ASP   A 16  ? 0.1771 0.2473 0.1646 0.0040  0.0049  0.0009  16  ASP   A CA  
113  C C   . ASP   A 16  ? 0.1824 0.2520 0.1704 0.0030  0.0062  0.0017  16  ASP   A C   
114  O O   . ASP   A 16  ? 0.1702 0.2381 0.1583 0.0028  0.0067  0.0028  16  ASP   A O   
115  C CB  . ASP   A 16  ? 0.1872 0.2556 0.1735 0.0045  0.0044  0.0021  16  ASP   A CB  
116  C CG  . ASP   A 16  ? 0.1860 0.2542 0.1713 0.0054  0.0033  0.0018  16  ASP   A CG  
117  O OD1 . ASP   A 16  ? 0.1833 0.2525 0.1687 0.0058  0.0028  0.0009  16  ASP   A OD1 
118  O OD2 . ASP   A 16  ? 0.1962 0.2630 0.1806 0.0056  0.0031  0.0026  16  ASP   A OD2 
119  N N   . LEU   A 17  ? 0.1579 0.2292 0.1463 0.0024  0.0068  0.0010  17  LEU   A N   
120  C CA  . LEU   A 17  ? 0.1787 0.2493 0.1674 0.0012  0.0083  0.0017  17  LEU   A CA  
121  C C   . LEU   A 17  ? 0.1833 0.2531 0.1704 0.0014  0.0083  0.0037  17  LEU   A C   
122  O O   . LEU   A 17  ? 0.1867 0.2579 0.1728 0.0019  0.0075  0.0035  17  LEU   A O   
123  C CB  . LEU   A 17  ? 0.1788 0.2517 0.1685 0.0003  0.0091  0.0000  17  LEU   A CB  
124  C CG  . LEU   A 17  ? 0.1997 0.2717 0.1898 -0.0014 0.0110  0.0005  17  LEU   A CG  
125  C CD1 . LEU   A 17  ? 0.1945 0.2650 0.1864 -0.0020 0.0120  0.0001  17  LEU   A CD1 
126  C CD2 . LEU   A 17  ? 0.2049 0.2798 0.1957 -0.0025 0.0119  -0.0013 17  LEU   A CD2 
127  N N   . SER   A 18  ? 0.2254 0.2931 0.2123 0.0012  0.0090  0.0055  18  SER   A N   
128  C CA  . SER   A 18  ? 0.3350 0.4024 0.3202 0.0016  0.0088  0.0075  18  SER   A CA  
129  C C   . SER   A 18  ? 0.4103 0.4761 0.3952 0.0007  0.0103  0.0092  18  SER   A C   
130  O O   . SER   A 18  ? 0.4163 0.4805 0.4028 -0.0001 0.0115  0.0089  18  SER   A O   
131  C CB  . SER   A 18  ? 0.3995 0.4659 0.3845 0.0028  0.0078  0.0085  18  SER   A CB  
132  O OG  . SER   A 18  ? 0.4778 0.5418 0.4641 0.0028  0.0084  0.0090  18  SER   A OG  
133  N N   . THR   A 19  ? 0.4683 0.5348 0.4512 0.0007  0.0104  0.0110  19  THR   A N   
134  C CA  . THR   A 19  ? 0.5357 0.6005 0.5177 -0.0001 0.0119  0.0131  19  THR   A CA  
135  C C   . THR   A 19  ? 0.5927 0.6538 0.5757 0.0005  0.0124  0.0148  19  THR   A C   
136  O O   . THR   A 19  ? 0.6026 0.6634 0.5859 0.0019  0.0111  0.0152  19  THR   A O   
137  C CB  . THR   A 19  ? 0.5892 0.6558 0.5684 0.0001  0.0116  0.0149  19  THR   A CB  
138  O OG1 . THR   A 19  ? 0.6135 0.6811 0.5922 0.0017  0.0099  0.0153  19  THR   A OG1 
139  C CG2 . THR   A 19  ? 0.5432 0.6132 0.5217 -0.0011 0.0119  0.0132  19  THR   A CG2 
140  N N   . THR   A 25  ? 0.3865 0.4742 0.3508 -0.0015 0.0104  0.0186  25  THR   A N   
141  C CA  . THR   A 25  ? 0.3757 0.4673 0.3385 -0.0035 0.0115  0.0174  25  THR   A CA  
142  C C   . THR   A 25  ? 0.3639 0.4562 0.3299 -0.0044 0.0120  0.0134  25  THR   A C   
143  O O   . THR   A 25  ? 0.3004 0.3893 0.2689 -0.0039 0.0119  0.0126  25  THR   A O   
144  C CB  . THR   A 25  ? 0.3800 0.4701 0.3401 -0.0049 0.0134  0.0203  25  THR   A CB  
145  O OG1 . THR   A 25  ? 0.3606 0.4462 0.3228 -0.0057 0.0147  0.0200  25  THR   A OG1 
146  C CG2 . THR   A 25  ? 0.3764 0.4652 0.3332 -0.0036 0.0129  0.0248  25  THR   A CG2 
147  N N   . ASP   A 26  ? 0.3828 0.4796 0.3485 -0.0058 0.0125  0.0111  26  ASP   A N   
148  C CA  . ASP   A 26  ? 0.3598 0.4578 0.3286 -0.0065 0.0129  0.0073  26  ASP   A CA  
149  C C   . ASP   A 26  ? 0.3600 0.4550 0.3298 -0.0077 0.0144  0.0073  26  ASP   A C   
150  O O   . ASP   A 26  ? 0.2729 0.3666 0.2457 -0.0073 0.0141  0.0052  26  ASP   A O   
151  C CB  . ASP   A 26  ? 0.3704 0.4742 0.3389 -0.0076 0.0132  0.0047  26  ASP   A CB  
152  C CG  . ASP   A 26  ? 0.3625 0.4690 0.3316 -0.0064 0.0117  0.0033  26  ASP   A CG  
153  O OD1 . ASP   A 26  ? 0.3603 0.4641 0.3303 -0.0047 0.0104  0.0040  26  ASP   A OD1 
154  O OD2 . ASP   A 26  ? 0.4505 0.5621 0.4191 -0.0073 0.0119  0.0014  26  ASP   A OD2 
155  N N   . GLU   A 27  ? 0.3192 0.4132 0.2864 -0.0091 0.0160  0.0099  27  GLU   A N   
156  C CA  . GLU   A 27  ? 0.3167 0.4079 0.2848 -0.0106 0.0178  0.0098  27  GLU   A CA  
157  C C   . GLU   A 27  ? 0.2970 0.3835 0.2675 -0.0092 0.0172  0.0102  27  GLU   A C   
158  O O   . GLU   A 27  ? 0.3104 0.3961 0.2835 -0.0099 0.0178  0.0081  27  GLU   A O   
159  C CB  . GLU   A 27  ? 0.3766 0.4664 0.3411 -0.0122 0.0197  0.0132  27  GLU   A CB  
160  C CG  . GLU   A 27  ? 0.4344 0.5205 0.4001 -0.0139 0.0218  0.0133  27  GLU   A CG  
161  C CD  . GLU   A 27  ? 0.4653 0.5504 0.4278 -0.0162 0.0244  0.0159  27  GLU   A CD  
162  O OE1 . GLU   A 27  ? 0.4858 0.5716 0.4443 -0.0164 0.0245  0.0190  27  GLU   A OE1 
163  O OE2 . GLU   A 27  ? 0.4600 0.5436 0.4243 -0.0181 0.0263  0.0144  27  GLU   A OE2 
164  N N   . LYS   A 28  ? 0.2748 0.3588 0.2445 -0.0074 0.0159  0.0127  28  LYS   A N   
165  C CA  . LYS   A 28  ? 0.2869 0.3668 0.2589 -0.0062 0.0154  0.0129  28  LYS   A CA  
166  C C   . LYS   A 28  ? 0.2709 0.3521 0.2458 -0.0052 0.0140  0.0097  28  LYS   A C   
167  O O   . LYS   A 28  ? 0.2458 0.3248 0.2230 -0.0050 0.0141  0.0086  28  LYS   A O   
168  C CB  . LYS   A 28  ? 0.2902 0.3674 0.2610 -0.0044 0.0143  0.0161  28  LYS   A CB  
169  C CG  . LYS   A 28  ? 0.3312 0.4060 0.2993 -0.0049 0.0156  0.0199  28  LYS   A CG  
170  C CD  . LYS   A 28  ? 0.3633 0.4330 0.3328 -0.0055 0.0172  0.0210  28  LYS   A CD  
171  C CE  . LYS   A 28  ? 0.4110 0.4778 0.3825 -0.0035 0.0159  0.0214  28  LYS   A CE  
172  N NZ  . LYS   A 28  ? 0.4186 0.4817 0.3928 -0.0043 0.0173  0.0206  28  LYS   A NZ  
173  N N   . VAL   A 29  ? 0.2373 0.3217 0.2121 -0.0044 0.0127  0.0083  29  VAL   A N   
174  C CA  . VAL   A 29  ? 0.2196 0.3047 0.1970 -0.0034 0.0114  0.0055  29  VAL   A CA  
175  C C   . VAL   A 29  ? 0.2117 0.2983 0.1912 -0.0044 0.0122  0.0027  29  VAL   A C   
176  O O   . VAL   A 29  ? 0.1801 0.2657 0.1618 -0.0038 0.0118  0.0011  29  VAL   A O   
177  C CB  . VAL   A 29  ? 0.2307 0.3188 0.2078 -0.0026 0.0103  0.0043  29  VAL   A CB  
178  C CG1 . VAL   A 29  ? 0.2215 0.3101 0.2012 -0.0017 0.0093  0.0014  29  VAL   A CG1 
179  C CG2 . VAL   A 29  ? 0.2411 0.3284 0.2166 -0.0014 0.0093  0.0066  29  VAL   A CG2 
180  N N   . ILE   A 30  ? 0.1916 0.2812 0.1703 -0.0060 0.0134  0.0018  30  ILE   A N   
181  C CA  . ILE   A 30  ? 0.2038 0.2957 0.1846 -0.0070 0.0142  -0.0013 30  ILE   A CA  
182  C C   . ILE   A 30  ? 0.2047 0.2941 0.1867 -0.0078 0.0153  -0.0012 30  ILE   A C   
183  O O   . ILE   A 30  ? 0.2129 0.3030 0.1976 -0.0074 0.0149  -0.0037 30  ILE   A O   
184  C CB  . ILE   A 30  ? 0.2251 0.3210 0.2046 -0.0089 0.0156  -0.0022 30  ILE   A CB  
185  C CG1 . ILE   A 30  ? 0.2328 0.3323 0.2124 -0.0083 0.0145  -0.0038 30  ILE   A CG1 
186  C CG2 . ILE   A 30  ? 0.2343 0.3324 0.2160 -0.0105 0.0169  -0.0052 30  ILE   A CG2 
187  C CD1 . ILE   A 30  ? 0.2452 0.3487 0.2227 -0.0102 0.0158  -0.0040 30  ILE   A CD1 
188  N N   . ALA   A 31  ? 0.2087 0.2949 0.1889 -0.0086 0.0165  0.0017  31  ALA   A N   
189  C CA  . ALA   A 31  ? 0.2180 0.3017 0.1996 -0.0095 0.0178  0.0016  31  ALA   A CA  
190  C C   . ALA   A 31  ? 0.2095 0.2912 0.1932 -0.0077 0.0163  0.0011  31  ALA   A C   
191  O O   . ALA   A 31  ? 0.1997 0.2817 0.1858 -0.0080 0.0166  -0.0010 31  ALA   A O   
192  C CB  . ALA   A 31  ? 0.2316 0.3118 0.2109 -0.0106 0.0194  0.0052  31  ALA   A CB  
193  N N   . LEU   A 32  ? 0.2057 0.2859 0.1885 -0.0059 0.0147  0.0028  32  LEU   A N   
194  C CA  . LEU   A 32  ? 0.1872 0.2657 0.1716 -0.0043 0.0133  0.0022  32  LEU   A CA  
195  C C   . LEU   A 32  ? 0.1936 0.2749 0.1802 -0.0037 0.0124  -0.0010 32  LEU   A C   
196  O O   . LEU   A 32  ? 0.1994 0.2804 0.1878 -0.0034 0.0121  -0.0024 32  LEU   A O   
197  C CB  . LEU   A 32  ? 0.1798 0.2571 0.1629 -0.0027 0.0118  0.0041  32  LEU   A CB  
198  C CG  . LEU   A 32  ? 0.1880 0.2636 0.1722 -0.0012 0.0104  0.0037  32  LEU   A CG  
199  C CD1 . LEU   A 32  ? 0.1948 0.2675 0.1799 -0.0016 0.0113  0.0046  32  LEU   A CD1 
200  C CD2 . LEU   A 32  ? 0.1824 0.2577 0.1654 0.0002  0.0090  0.0050  32  LEU   A CD2 
201  N N   . CYS   A 33  ? 0.1940 0.2781 0.1804 -0.0034 0.0117  -0.0022 33  CYS   A N   
202  C CA  . CYS   A 33  ? 0.2114 0.2979 0.1999 -0.0025 0.0107  -0.0051 33  CYS   A CA  
203  C C   . CYS   A 33  ? 0.2064 0.2949 0.1970 -0.0036 0.0118  -0.0074 33  CYS   A C   
204  O O   . CYS   A 33  ? 0.1753 0.2646 0.1677 -0.0026 0.0109  -0.0092 33  CYS   A O   
205  C CB  . CYS   A 33  ? 0.1901 0.2796 0.1786 -0.0023 0.0103  -0.0065 33  CYS   A CB  
206  S SG  . CYS   A 33  ? 0.2202 0.3086 0.2071 -0.0010 0.0091  -0.0049 33  CYS   A SG  
207  N N   . HIS   A 34  ? 0.2150 0.3045 0.2051 -0.0057 0.0137  -0.0076 34  HIS   A N   
208  C CA  . HIS   A 34  ? 0.2101 0.3016 0.2022 -0.0072 0.0151  -0.0100 34  HIS   A CA  
209  C C   . HIS   A 34  ? 0.2108 0.3001 0.2041 -0.0071 0.0153  -0.0098 34  HIS   A C   
210  O O   . HIS   A 34  ? 0.1957 0.2874 0.1914 -0.0072 0.0152  -0.0125 34  HIS   A O   
211  C CB  . HIS   A 34  ? 0.2323 0.3244 0.2232 -0.0099 0.0175  -0.0095 34  HIS   A CB  
212  C CG  . HIS   A 34  ? 0.2269 0.3224 0.2172 -0.0103 0.0176  -0.0106 34  HIS   A CG  
213  N ND1 . HIS   A 34  ? 0.2538 0.3501 0.2421 -0.0126 0.0196  -0.0098 34  HIS   A ND1 
214  C CD2 . HIS   A 34  ? 0.2297 0.3281 0.2210 -0.0089 0.0160  -0.0125 34  HIS   A CD2 
215  C CE1 . HIS   A 34  ? 0.2490 0.3490 0.2372 -0.0126 0.0192  -0.0114 34  HIS   A CE1 
216  N NE2 . HIS   A 34  ? 0.2387 0.3400 0.2291 -0.0104 0.0171  -0.0132 34  HIS   A NE2 
217  N N   . GLN   A 35  ? 0.2007 0.2859 0.1925 -0.0072 0.0156  -0.0069 35  GLN   A N   
218  C CA  . GLN   A 35  ? 0.2115 0.2945 0.2045 -0.0073 0.0161  -0.0068 35  GLN   A CA  
219  C C   . GLN   A 35  ? 0.1974 0.2813 0.1916 -0.0053 0.0140  -0.0080 35  GLN   A C   
220  O O   . GLN   A 35  ? 0.1895 0.2738 0.1856 -0.0056 0.0143  -0.0095 35  GLN   A O   
221  C CB  . GLN   A 35  ? 0.2593 0.3377 0.2505 -0.0074 0.0167  -0.0033 35  GLN   A CB  
222  C CG  . GLN   A 35  ? 0.3512 0.4281 0.3413 -0.0096 0.0191  -0.0018 35  GLN   A CG  
223  C CD  . GLN   A 35  ? 0.4594 0.5323 0.4471 -0.0091 0.0193  0.0021  35  GLN   A CD  
224  O OE1 . GLN   A 35  ? 0.5731 0.6450 0.5588 -0.0103 0.0207  0.0041  35  GLN   A OE1 
225  N NE2 . GLN   A 35  ? 0.5109 0.5817 0.4988 -0.0074 0.0178  0.0032  35  GLN   A NE2 
226  N N   . ALA   A 36  ? 0.1785 0.2626 0.1717 -0.0034 0.0120  -0.0074 36  ALA   A N   
227  C CA  . ALA   A 36  ? 0.1737 0.2582 0.1674 -0.0015 0.0101  -0.0081 36  ALA   A CA  
228  C C   . ALA   A 36  ? 0.1813 0.2698 0.1772 -0.0010 0.0095  -0.0113 36  ALA   A C   
229  O O   . ALA   A 36  ? 0.1776 0.2669 0.1743 0.0003  0.0083  -0.0120 36  ALA   A O   
230  C CB  . ALA   A 36  ? 0.1723 0.2559 0.1645 0.0002  0.0085  -0.0068 36  ALA   A CB  
231  N N   . LYS   A 37  ? 0.1824 0.2739 0.1794 -0.0021 0.0104  -0.0132 37  LYS   A N   
232  C CA  . LYS   A 37  ? 0.1964 0.2924 0.1960 -0.0017 0.0100  -0.0165 37  LYS   A CA  
233  C C   . LYS   A 37  ? 0.1912 0.2885 0.1924 -0.0037 0.0118  -0.0183 37  LYS   A C   
234  O O   . LYS   A 37  ? 0.2082 0.3066 0.2100 -0.0060 0.0139  -0.0193 37  LYS   A O   
235  C CB  . LYS   A 37  ? 0.1997 0.2986 0.1999 -0.0019 0.0102  -0.0182 37  LYS   A CB  
236  C CG  . LYS   A 37  ? 0.1999 0.3038 0.2030 -0.0011 0.0095  -0.0218 37  LYS   A CG  
237  C CD  . LYS   A 37  ? 0.2174 0.3241 0.2214 -0.0016 0.0100  -0.0235 37  LYS   A CD  
238  C CE  . LYS   A 37  ? 0.2367 0.3484 0.2438 -0.0001 0.0088  -0.0272 37  LYS   A CE  
239  N NZ  . LYS   A 37  ? 0.2592 0.3742 0.2676 -0.0010 0.0096  -0.0294 37  LYS   A NZ  
240  N N   . THR   A 38  ? 0.1878 0.2852 0.1899 -0.0033 0.0113  -0.0188 38  THR   A N   
241  C CA  . THR   A 38  ? 0.1746 0.2724 0.1783 -0.0055 0.0134  -0.0202 38  THR   A CA  
242  C C   . THR   A 38  ? 0.1709 0.2746 0.1775 -0.0055 0.0132  -0.0244 38  THR   A C   
243  O O   . THR   A 38  ? 0.1583 0.2650 0.1654 -0.0033 0.0110  -0.0256 38  THR   A O   
244  C CB  . THR   A 38  ? 0.1780 0.2728 0.1813 -0.0055 0.0135  -0.0188 38  THR   A CB  
245  O OG1 . THR   A 38  ? 0.1636 0.2616 0.1683 -0.0044 0.0122  -0.0209 38  THR   A OG1 
246  C CG2 . THR   A 38  ? 0.1907 0.2810 0.1913 -0.0041 0.0124  -0.0152 38  THR   A CG2 
247  N N   . PRO   A 39  ? 0.1886 0.2937 0.1973 -0.0080 0.0155  -0.0266 39  PRO   A N   
248  C CA  . PRO   A 39  ? 0.1999 0.3112 0.2117 -0.0082 0.0155  -0.0310 39  PRO   A CA  
249  C C   . PRO   A 39  ? 0.1984 0.3128 0.2110 -0.0060 0.0132  -0.0323 39  PRO   A C   
250  O O   . PRO   A 39  ? 0.2230 0.3433 0.2380 -0.0054 0.0123  -0.0358 39  PRO   A O   
251  C CB  . PRO   A 39  ? 0.2164 0.3275 0.2301 -0.0118 0.0189  -0.0327 39  PRO   A CB  
252  C CG  . PRO   A 39  ? 0.2248 0.3296 0.2359 -0.0132 0.0207  -0.0289 39  PRO   A CG  
253  C CD  . PRO   A 39  ? 0.2027 0.3038 0.2111 -0.0106 0.0183  -0.0252 39  PRO   A CD  
254  N N   . VAL   A 40  ? 0.1887 0.2995 0.1994 -0.0049 0.0122  -0.0296 40  VAL   A N   
255  C CA  . VAL   A 40  ? 0.1767 0.2903 0.1876 -0.0029 0.0100  -0.0305 40  VAL   A CA  
256  C C   . VAL   A 40  ? 0.1741 0.2857 0.1823 0.0002  0.0072  -0.0276 40  VAL   A C   
257  O O   . VAL   A 40  ? 0.1744 0.2873 0.1819 0.0019  0.0054  -0.0274 40  VAL   A O   
258  C CB  . VAL   A 40  ? 0.2024 0.3145 0.2138 -0.0045 0.0113  -0.0306 40  VAL   A CB  
259  C CG1 . VAL   A 40  ? 0.2284 0.3424 0.2429 -0.0076 0.0143  -0.0337 40  VAL   A CG1 
260  C CG2 . VAL   A 40  ? 0.2133 0.3187 0.2222 -0.0046 0.0117  -0.0265 40  VAL   A CG2 
261  N N   . GLY   A 41  ? 0.1651 0.2734 0.1717 0.0007  0.0070  -0.0253 41  GLY   A N   
262  C CA  . GLY   A 41  ? 0.1575 0.2634 0.1617 0.0033  0.0048  -0.0228 41  GLY   A CA  
263  C C   . GLY   A 41  ? 0.1581 0.2585 0.1602 0.0027  0.0056  -0.0195 41  GLY   A C   
264  O O   . GLY   A 41  ? 0.1749 0.2731 0.1769 0.0005  0.0076  -0.0189 41  GLY   A O   
265  N N   . ASN   A 42  ? 0.1528 0.2513 0.1532 0.0048  0.0038  -0.0176 42  ASN   A N   
266  C CA  . ASN   A 42  ? 0.1549 0.2490 0.1532 0.0046  0.0041  -0.0149 42  ASN   A CA  
267  C C   . ASN   A 42  ? 0.1514 0.2418 0.1477 0.0047  0.0039  -0.0125 42  ASN   A C   
268  O O   . ASN   A 42  ? 0.1516 0.2426 0.1476 0.0059  0.0027  -0.0125 42  ASN   A O   
269  C CB  . ASN   A 42  ? 0.1619 0.2560 0.1598 0.0066  0.0026  -0.0145 42  ASN   A CB  
270  C CG  . ASN   A 42  ? 0.1914 0.2891 0.1913 0.0065  0.0029  -0.0171 42  ASN   A CG  
271  O OD1 . ASN   A 42  ? 0.1988 0.2984 0.2000 0.0044  0.0046  -0.0186 42  ASN   A OD1 
272  N ND2 . ASN   A 42  ? 0.2065 0.3052 0.2071 0.0086  0.0013  -0.0177 42  ASN   A ND2 
273  N N   . THR   A 43  ? 0.1497 0.2367 0.1449 0.0036  0.0050  -0.0104 43  THR   A N   
274  C CA  . THR   A 43  ? 0.1477 0.2313 0.1412 0.0040  0.0046  -0.0082 43  THR   A CA  
275  C C   . THR   A 43  ? 0.1571 0.2396 0.1491 0.0059  0.0029  -0.0072 43  THR   A C   
276  O O   . THR   A 43  ? 0.1633 0.2471 0.1557 0.0069  0.0022  -0.0080 43  THR   A O   
277  C CB  . THR   A 43  ? 0.1557 0.2363 0.1484 0.0026  0.0060  -0.0064 43  THR   A CB  
278  O OG1 . THR   A 43  ? 0.1534 0.2336 0.1453 0.0028  0.0060  -0.0056 43  THR   A OG1 
279  C CG2 . THR   A 43  ? 0.1548 0.2356 0.1489 0.0007  0.0079  -0.0072 43  THR   A CG2 
280  N N   . ALA   A 44  ? 0.1439 0.2239 0.1343 0.0064  0.0023  -0.0056 44  ALA   A N   
281  C CA  . ALA   A 44  ? 0.1371 0.2155 0.1260 0.0080  0.0010  -0.0045 44  ALA   A CA  
282  C C   . ALA   A 44  ? 0.1340 0.2108 0.1225 0.0079  0.0013  -0.0037 44  ALA   A C   
283  O O   . ALA   A 44  ? 0.1477 0.2240 0.1359 0.0091  0.0005  -0.0036 44  ALA   A O   
284  C CB  . ALA   A 44  ? 0.1413 0.2175 0.1287 0.0081  0.0008  -0.0031 44  ALA   A CB  
285  N N   . ALA   A 45  ? 0.1348 0.2107 0.1232 0.0066  0.0025  -0.0029 45  ALA   A N   
286  C CA  . ALA   A 45  ? 0.1341 0.2089 0.1218 0.0064  0.0028  -0.0020 45  ALA   A CA  
287  C C   . ALA   A 45  ? 0.1432 0.2183 0.1310 0.0049  0.0041  -0.0016 45  ALA   A C   
288  O O   . ALA   A 45  ? 0.1425 0.2177 0.1310 0.0040  0.0049  -0.0016 45  ALA   A O   
289  C CB  . ALA   A 45  ? 0.1348 0.2069 0.1210 0.0067  0.0024  -0.0005 45  ALA   A CB  
290  N N   . ILE   A 46  ? 0.1529 0.2281 0.1400 0.0047  0.0044  -0.0011 46  ILE   A N   
291  C CA  . ILE   A 46  ? 0.1754 0.2501 0.1618 0.0036  0.0054  0.0003  46  ILE   A CA  
292  C C   . ILE   A 46  ? 0.1657 0.2390 0.1509 0.0041  0.0049  0.0017  46  ILE   A C   
293  O O   . ILE   A 46  ? 0.1636 0.2367 0.1486 0.0049  0.0041  0.0012  46  ILE   A O   
294  C CB  . ILE   A 46  ? 0.2022 0.2792 0.1886 0.0028  0.0061  -0.0003 46  ILE   A CB  
295  C CG1 . ILE   A 46  ? 0.2168 0.2953 0.2033 0.0034  0.0054  -0.0014 46  ILE   A CG1 
296  C CG2 . ILE   A 46  ? 0.2026 0.2813 0.1905 0.0019  0.0069  -0.0019 46  ILE   A CG2 
297  C CD1 . ILE   A 46  ? 0.2477 0.3288 0.2339 0.0025  0.0062  -0.0020 46  ILE   A CD1 
298  N N   A SER   A 47  ? 0.1767 0.2489 0.1612 0.0037  0.0054  0.0033  47  SER   A N   
299  N N   B SER   A 47  ? 0.1644 0.2367 0.1490 0.0037  0.0054  0.0033  47  SER   A N   
300  C CA  A SER   A 47  ? 0.1875 0.2591 0.1711 0.0041  0.0050  0.0045  47  SER   A CA  
301  C CA  B SER   A 47  ? 0.1663 0.2379 0.1499 0.0042  0.0050  0.0044  47  SER   A CA  
302  C C   A SER   A 47  ? 0.1737 0.2467 0.1562 0.0037  0.0054  0.0056  47  SER   A C   
303  C C   B SER   A 47  ? 0.1629 0.2358 0.1455 0.0038  0.0054  0.0056  47  SER   A C   
304  O O   A SER   A 47  ? 0.1655 0.2381 0.1478 0.0031  0.0063  0.0067  47  SER   A O   
305  O O   B SER   A 47  ? 0.1543 0.2266 0.1366 0.0032  0.0063  0.0067  47  SER   A O   
306  C CB  A SER   A 47  ? 0.2174 0.2869 0.2013 0.0044  0.0050  0.0054  47  SER   A CB  
307  C CB  B SER   A 47  ? 0.1759 0.2454 0.1599 0.0044  0.0049  0.0052  47  SER   A CB  
308  O OG  A SER   A 47  ? 0.2438 0.3124 0.2281 0.0048  0.0044  0.0045  47  SER   A OG  
309  O OG  B SER   A 47  ? 0.1753 0.2444 0.1586 0.0049  0.0045  0.0061  47  SER   A OG  
310  N N   . VAL   A 48  ? 0.1529 0.2275 0.1347 0.0040  0.0049  0.0053  48  VAL   A N   
311  C CA  . VAL   A 48  ? 0.1680 0.2448 0.1485 0.0037  0.0052  0.0062  48  VAL   A CA  
312  C C   . VAL   A 48  ? 0.1648 0.2427 0.1448 0.0043  0.0045  0.0063  48  VAL   A C   
313  O O   . VAL   A 48  ? 0.1745 0.2516 0.1552 0.0047  0.0040  0.0051  48  VAL   A O   
314  C CB  . VAL   A 48  ? 0.1563 0.2358 0.1367 0.0029  0.0057  0.0047  48  VAL   A CB  
315  C CG1 . VAL   A 48  ? 0.1714 0.2505 0.1524 0.0021  0.0066  0.0045  48  VAL   A CG1 
316  C CG2 . VAL   A 48  ? 0.1544 0.2349 0.1359 0.0033  0.0051  0.0024  48  VAL   A CG2 
317  N N   . TYR   A 49  ? 0.1703 0.2503 0.1488 0.0043  0.0044  0.0074  49  TYR   A N   
318  C CA  . TYR   A 49  ? 0.1644 0.2467 0.1426 0.0048  0.0038  0.0069  49  TYR   A CA  
319  C C   . TYR   A 49  ? 0.1503 0.2349 0.1291 0.0043  0.0038  0.0044  49  TYR   A C   
320  O O   . TYR   A 49  ? 0.1527 0.2382 0.1319 0.0036  0.0043  0.0034  49  TYR   A O   
321  C CB  . TYR   A 49  ? 0.1829 0.2677 0.1594 0.0051  0.0036  0.0088  49  TYR   A CB  
322  C CG  . TYR   A 49  ? 0.2288 0.3112 0.2050 0.0060  0.0033  0.0113  49  TYR   A CG  
323  C CD1 . TYR   A 49  ? 0.2620 0.3429 0.2394 0.0068  0.0027  0.0110  49  TYR   A CD1 
324  C CD2 . TYR   A 49  ? 0.2733 0.3544 0.2483 0.0059  0.0039  0.0138  49  TYR   A CD2 
325  C CE1 . TYR   A 49  ? 0.3065 0.3853 0.2841 0.0078  0.0025  0.0130  49  TYR   A CE1 
326  C CE2 . TYR   A 49  ? 0.3412 0.4197 0.3163 0.0069  0.0038  0.0160  49  TYR   A CE2 
327  C CZ  . TYR   A 49  ? 0.3568 0.4343 0.3334 0.0080  0.0030  0.0155  49  TYR   A CZ  
328  O OH  . TYR   A 49  ? 0.4308 0.5059 0.4082 0.0091  0.0029  0.0173  49  TYR   A OH  
329  N N   . PRO   A 50  ? 0.1573 0.2431 0.1367 0.0045  0.0034  0.0030  50  PRO   A N   
330  C CA  . PRO   A 50  ? 0.1557 0.2430 0.1364 0.0040  0.0037  0.0003  50  PRO   A CA  
331  C C   . PRO   A 50  ? 0.1561 0.2471 0.1364 0.0032  0.0041  -0.0007 50  PRO   A C   
332  O O   . PRO   A 50  ? 0.1695 0.2605 0.1510 0.0029  0.0045  -0.0025 50  PRO   A O   
333  C CB  . PRO   A 50  ? 0.1585 0.2470 0.1396 0.0041  0.0034  -0.0007 50  PRO   A CB  
334  C CG  . PRO   A 50  ? 0.1525 0.2383 0.1334 0.0048  0.0029  0.0011  50  PRO   A CG  
335  C CD  . PRO   A 50  ? 0.1509 0.2362 0.1305 0.0052  0.0028  0.0036  50  PRO   A CD  
336  N N   . ARG   A 51  ? 0.1585 0.2526 0.1369 0.0031  0.0040  0.0006  51  ARG   A N   
337  C CA  . ARG   A 51  ? 0.1706 0.2690 0.1483 0.0021  0.0045  -0.0004 51  ARG   A CA  
338  C C   . ARG   A 51  ? 0.1684 0.2660 0.1462 0.0014  0.0052  -0.0004 51  ARG   A C   
339  O O   . ARG   A 51  ? 0.1591 0.2599 0.1371 0.0005  0.0058  -0.0022 51  ARG   A O   
340  C CB  . ARG   A 51  ? 0.1901 0.2921 0.1653 0.0022  0.0042  0.0015  51  ARG   A CB  
341  C CG  . ARG   A 51  ? 0.2203 0.3196 0.1936 0.0027  0.0041  0.0052  51  ARG   A CG  
342  C CD  . ARG   A 51  ? 0.2896 0.3926 0.2603 0.0031  0.0036  0.0072  51  ARG   A CD  
343  N NE  . ARG   A 51  ? 0.4051 0.5046 0.3745 0.0041  0.0034  0.0108  51  ARG   A NE  
344  C CZ  . ARG   A 51  ? 0.4959 0.5931 0.4661 0.0055  0.0026  0.0119  51  ARG   A CZ  
345  N NH1 . ARG   A 51  ? 0.4717 0.5698 0.4437 0.0060  0.0019  0.0098  51  ARG   A NH1 
346  N NH2 . ARG   A 51  ? 0.5880 0.6818 0.5573 0.0063  0.0026  0.0150  51  ARG   A NH2 
347  N N   . SER   A 52  ? 0.1750 0.2685 0.1529 0.0018  0.0053  0.0012  52  SER   A N   
348  C CA  . SER   A 52  ? 0.1696 0.2624 0.1478 0.0011  0.0061  0.0011  52  SER   A CA  
349  C C   . SER   A 52  ? 0.1701 0.2615 0.1508 0.0013  0.0060  -0.0013 52  SER   A C   
350  O O   . SER   A 52  ? 0.1612 0.2526 0.1425 0.0008  0.0066  -0.0020 52  SER   A O   
351  C CB  . SER   A 52  ? 0.1856 0.2749 0.1629 0.0012  0.0063  0.0038  52  SER   A CB  
352  O OG  . SER   A 52  ? 0.2015 0.2916 0.1765 0.0013  0.0063  0.0064  52  SER   A OG  
353  N N   . ILE   A 53  ? 0.1694 0.2595 0.1515 0.0021  0.0054  -0.0025 53  ILE   A N   
354  C CA  . ILE   A 53  ? 0.1627 0.2509 0.1468 0.0027  0.0052  -0.0043 53  ILE   A CA  
355  C C   . ILE   A 53  ? 0.1694 0.2604 0.1550 0.0023  0.0057  -0.0068 53  ILE   A C   
356  O O   . ILE   A 53  ? 0.1553 0.2458 0.1422 0.0025  0.0057  -0.0076 53  ILE   A O   
357  C CB  . ILE   A 53  ? 0.1834 0.2693 0.1684 0.0036  0.0047  -0.0047 53  ILE   A CB  
358  C CG1 . ILE   A 53  ? 0.1771 0.2600 0.1609 0.0040  0.0043  -0.0025 53  ILE   A CG1 
359  C CG2 . ILE   A 53  ? 0.1822 0.2662 0.1692 0.0043  0.0045  -0.0064 53  ILE   A CG2 
360  C CD1 . ILE   A 53  ? 0.1757 0.2569 0.1598 0.0044  0.0040  -0.0029 53  ILE   A CD1 
361  N N   . PRO   A 54  ? 0.1664 0.2612 0.1523 0.0015  0.0061  -0.0085 54  PRO   A N   
362  C CA  . PRO   A 54  ? 0.1681 0.2659 0.1559 0.0010  0.0067  -0.0113 54  PRO   A CA  
363  C C   . PRO   A 54  ? 0.1817 0.2810 0.1692 0.0002  0.0073  -0.0112 54  PRO   A C   
364  O O   . PRO   A 54  ? 0.1903 0.2899 0.1800 0.0005  0.0073  -0.0131 54  PRO   A O   
365  C CB  . PRO   A 54  ? 0.1706 0.2726 0.1580 0.0001  0.0071  -0.0127 54  PRO   A CB  
366  C CG  . PRO   A 54  ? 0.1707 0.2708 0.1574 0.0007  0.0065  -0.0115 54  PRO   A CG  
367  C CD  . PRO   A 54  ? 0.1661 0.2628 0.1508 0.0012  0.0060  -0.0082 54  PRO   A CD  
368  N N   . ILE   A 55  ? 0.1638 0.2640 0.1485 -0.0008 0.0078  -0.0090 55  ILE   A N   
369  C CA  . ILE   A 55  ? 0.1904 0.2919 0.1746 -0.0020 0.0087  -0.0088 55  ILE   A CA  
370  C C   . ILE   A 55  ? 0.1748 0.2728 0.1600 -0.0013 0.0085  -0.0082 55  ILE   A C   
371  O O   . ILE   A 55  ? 0.1757 0.2748 0.1623 -0.0018 0.0090  -0.0097 55  ILE   A O   
372  C CB  . ILE   A 55  ? 0.2303 0.3332 0.2112 -0.0033 0.0095  -0.0063 55  ILE   A CB  
373  C CG1 . ILE   A 55  ? 0.2522 0.3576 0.2328 -0.0051 0.0109  -0.0072 55  ILE   A CG1 
374  C CG2 . ILE   A 55  ? 0.2548 0.3536 0.2340 -0.0027 0.0092  -0.0028 55  ILE   A CG2 
375  C CD1 . ILE   A 55  ? 0.2859 0.3963 0.2681 -0.0060 0.0114  -0.0107 55  ILE   A CD1 
376  N N   . ALA   A 56  ? 0.1670 0.2612 0.1519 -0.0002 0.0077  -0.0063 56  ALA   A N   
377  C CA  . ALA   A 56  ? 0.1670 0.2584 0.1530 0.0005  0.0074  -0.0061 56  ALA   A CA  
378  C C   . ALA   A 56  ? 0.1681 0.2599 0.1568 0.0016  0.0067  -0.0087 56  ALA   A C   
379  O O   . ALA   A 56  ? 0.1685 0.2607 0.1586 0.0017  0.0068  -0.0097 56  ALA   A O   
380  C CB  . ALA   A 56  ? 0.1705 0.2581 0.1555 0.0014  0.0067  -0.0038 56  ALA   A CB  
381  N N   . ARG   A 57  ? 0.1655 0.2572 0.1552 0.0025  0.0061  -0.0099 57  ARG   A N   
382  C CA  . ARG   A 57  ? 0.1665 0.2581 0.1588 0.0039  0.0054  -0.0121 57  ARG   A CA  
383  C C   . ARG   A 57  ? 0.1775 0.2730 0.1717 0.0033  0.0060  -0.0147 57  ARG   A C   
384  O O   . ARG   A 57  ? 0.1821 0.2779 0.1783 0.0042  0.0056  -0.0161 57  ARG   A O   
385  C CB  . ARG   A 57  ? 0.1764 0.2670 0.1696 0.0047  0.0050  -0.0130 57  ARG   A CB  
386  C CG  . ARG   A 57  ? 0.1972 0.2866 0.1931 0.0065  0.0043  -0.0147 57  ARG   A CG  
387  C CD  . ARG   A 57  ? 0.2080 0.2936 0.2034 0.0080  0.0033  -0.0131 57  ARG   A CD  
388  N NE  . ARG   A 57  ? 0.2237 0.3057 0.2177 0.0083  0.0031  -0.0114 57  ARG   A NE  
389  C CZ  . ARG   A 57  ? 0.2249 0.3036 0.2176 0.0090  0.0025  -0.0094 57  ARG   A CZ  
390  N NH1 . ARG   A 57  ? 0.2279 0.3064 0.2205 0.0097  0.0019  -0.0088 57  ARG   A NH1 
391  N NH2 . ARG   A 57  ? 0.2051 0.2810 0.1966 0.0089  0.0025  -0.0082 57  ARG   A NH2 
392  N N   A LYS   A 58  ? 0.1758 0.2747 0.1694 0.0017  0.0070  -0.0155 58  LYS   A N   
393  N N   B LYS   A 58  ? 0.1688 0.2677 0.1624 0.0017  0.0070  -0.0156 58  LYS   A N   
394  C CA  A LYS   A 58  ? 0.1805 0.2837 0.1758 0.0007  0.0079  -0.0183 58  LYS   A CA  
395  C CA  B LYS   A 58  ? 0.1685 0.2716 0.1637 0.0006  0.0079  -0.0182 58  LYS   A CA  
396  C C   A LYS   A 58  ? 0.1746 0.2781 0.1698 0.0000  0.0084  -0.0180 58  LYS   A C   
397  C C   B LYS   A 58  ? 0.1679 0.2714 0.1631 0.0000  0.0084  -0.0179 58  LYS   A C   
398  O O   A LYS   A 58  ? 0.1913 0.2969 0.1890 0.0002  0.0084  -0.0205 58  LYS   A O   
399  O O   B LYS   A 58  ? 0.1845 0.2900 0.1822 0.0003  0.0084  -0.0205 58  LYS   A O   
400  C CB  A LYS   A 58  ? 0.1853 0.2922 0.1793 -0.0011 0.0089  -0.0189 58  LYS   A CB  
401  C CB  B LYS   A 58  ? 0.1641 0.2709 0.1577 -0.0013 0.0090  -0.0185 58  LYS   A CB  
402  C CG  A LYS   A 58  ? 0.1974 0.3092 0.1937 -0.0021 0.0098  -0.0225 58  LYS   A CG  
403  C CG  B LYS   A 58  ? 0.1651 0.2767 0.1595 -0.0030 0.0103  -0.0209 58  LYS   A CG  
404  C CD  A LYS   A 58  ? 0.1989 0.3150 0.1938 -0.0040 0.0109  -0.0234 58  LYS   A CD  
405  C CD  B LYS   A 58  ? 0.1606 0.2761 0.1532 -0.0048 0.0112  -0.0213 58  LYS   A CD  
406  C CE  A LYS   A 58  ? 0.2181 0.3394 0.2153 -0.0052 0.0119  -0.0272 58  LYS   A CE  
407  C CE  B LYS   A 58  ? 0.1665 0.2873 0.1609 -0.0062 0.0124  -0.0249 58  LYS   A CE  
408  N NZ  A LYS   A 58  ? 0.2240 0.3461 0.2208 -0.0064 0.0127  -0.0270 58  LYS   A NZ  
409  N NZ  B LYS   A 58  ? 0.1630 0.2879 0.1571 -0.0073 0.0129  -0.0265 58  LYS   A NZ  
410  N N   . THR   A 59  ? 0.1638 0.2654 0.1563 -0.0010 0.0089  -0.0151 59  THR   A N   
411  C CA  . THR   A 59  ? 0.1639 0.2656 0.1563 -0.0020 0.0098  -0.0148 59  THR   A CA  
412  C C   . THR   A 59  ? 0.1668 0.2671 0.1614 -0.0004 0.0087  -0.0157 59  THR   A C   
413  O O   . THR   A 59  ? 0.1631 0.2656 0.1595 -0.0008 0.0091  -0.0178 59  THR   A O   
414  C CB  . THR   A 59  ? 0.1696 0.2687 0.1589 -0.0031 0.0105  -0.0114 59  THR   A CB  
415  O OG1 . THR   A 59  ? 0.1769 0.2774 0.1638 -0.0043 0.0112  -0.0102 59  THR   A OG1 
416  C CG2 . THR   A 59  ? 0.1721 0.2713 0.1613 -0.0047 0.0119  -0.0113 59  THR   A CG2 
417  N N   . LEU   A 60  ? 0.1517 0.2484 0.1459 0.0014  0.0074  -0.0142 60  LEU   A N   
418  C CA  . LEU   A 60  ? 0.1674 0.2631 0.1632 0.0030  0.0062  -0.0147 60  LEU   A CA  
419  C C   . LEU   A 60  ? 0.1923 0.2908 0.1912 0.0043  0.0055  -0.0179 60  LEU   A C   
420  O O   . LEU   A 60  ? 0.1868 0.2868 0.1875 0.0051  0.0050  -0.0194 60  LEU   A O   
421  C CB  . LEU   A 60  ? 0.1814 0.2730 0.1760 0.0046  0.0050  -0.0126 60  LEU   A CB  
422  C CG  . LEU   A 60  ? 0.1936 0.2823 0.1857 0.0037  0.0054  -0.0097 60  LEU   A CG  
423  C CD1 . LEU   A 60  ? 0.1891 0.2744 0.1804 0.0052  0.0043  -0.0082 60  LEU   A CD1 
424  C CD2 . LEU   A 60  ? 0.1999 0.2886 0.1922 0.0029  0.0061  -0.0095 60  LEU   A CD2 
425  N N   . LYS   A 61  ? 0.2001 0.2993 0.1998 0.0049  0.0053  -0.0191 61  LYS   A N   
426  C CA  . LYS   A 61  ? 0.2239 0.3258 0.2270 0.0062  0.0047  -0.0222 61  LYS   A CA  
427  C C   . LYS   A 61  ? 0.2251 0.3319 0.2299 0.0048  0.0057  -0.0250 61  LYS   A C   
428  O O   . LYS   A 61  ? 0.2087 0.3175 0.2161 0.0060  0.0050  -0.0272 61  LYS   A O   
429  C CB  . LYS   A 61  ? 0.2765 0.3783 0.2804 0.0066  0.0047  -0.0232 61  LYS   A CB  
430  C CG  . LYS   A 61  ? 0.3380 0.4351 0.3413 0.0085  0.0035  -0.0214 61  LYS   A CG  
431  C CD  . LYS   A 61  ? 0.4092 0.5062 0.4131 0.0083  0.0039  -0.0223 61  LYS   A CD  
432  C CE  . LYS   A 61  ? 0.4596 0.5520 0.4633 0.0100  0.0031  -0.0209 61  LYS   A CE  
433  N NZ  . LYS   A 61  ? 0.4750 0.5676 0.4789 0.0091  0.0039  -0.0218 61  LYS   A NZ  
434  N N   . GLU   A 62  ? 0.2298 0.3384 0.2330 0.0021  0.0074  -0.0248 62  GLU   A N   
435  C CA  . GLU   A 62  ? 0.2509 0.3641 0.2554 0.0002  0.0089  -0.0274 62  GLU   A CA  
436  C C   . GLU   A 62  ? 0.2449 0.3586 0.2500 -0.0002 0.0091  -0.0277 62  GLU   A C   
437  O O   . GLU   A 62  ? 0.2345 0.3523 0.2421 -0.0008 0.0097  -0.0308 62  GLU   A O   
438  C CB  . GLU   A 62  ? 0.2755 0.3902 0.2774 -0.0026 0.0107  -0.0266 62  GLU   A CB  
439  C CG  . GLU   A 62  ? 0.3425 0.4592 0.3449 -0.0026 0.0107  -0.0279 62  GLU   A CG  
440  C CD  . GLU   A 62  ? 0.3867 0.5061 0.3866 -0.0054 0.0125  -0.0275 62  GLU   A CD  
441  O OE1 . GLU   A 62  ? 0.5110 0.6305 0.5086 -0.0074 0.0139  -0.0261 62  GLU   A OE1 
442  O OE2 . GLU   A 62  ? 0.4213 0.5426 0.4213 -0.0055 0.0125  -0.0286 62  GLU   A OE2 
443  N N   . GLN   A 63  ? 0.2003 0.3102 0.2034 0.0002  0.0087  -0.0249 63  GLN   A N   
444  C CA  . GLN   A 63  ? 0.2097 0.3204 0.2137 -0.0004 0.0092  -0.0255 63  GLN   A CA  
445  C C   . GLN   A 63  ? 0.2133 0.3243 0.2195 0.0023  0.0072  -0.0266 63  GLN   A C   
446  O O   . GLN   A 63  ? 0.1911 0.3029 0.1980 0.0022  0.0072  -0.0272 63  GLN   A O   
447  C CB  . GLN   A 63  ? 0.2260 0.3331 0.2270 -0.0019 0.0102  -0.0223 63  GLN   A CB  
448  C CG  . GLN   A 63  ? 0.2154 0.3179 0.2147 -0.0002 0.0088  -0.0193 63  GLN   A CG  
449  C CD  . GLN   A 63  ? 0.2180 0.3174 0.2152 -0.0017 0.0099  -0.0166 63  GLN   A CD  
450  O OE1 . GLN   A 63  ? 0.2450 0.3448 0.2413 -0.0040 0.0118  -0.0162 63  GLN   A OE1 
451  N NE2 . GLN   A 63  ? 0.1776 0.2737 0.1739 -0.0003 0.0088  -0.0147 63  GLN   A NE2 
452  N N   . GLY   A 64  ? 0.2192 0.3299 0.2267 0.0048  0.0055  -0.0272 64  GLY   A N   
453  C CA  . GLY   A 64  ? 0.2252 0.3359 0.2344 0.0078  0.0034  -0.0279 64  GLY   A CA  
454  C C   . GLY   A 64  ? 0.2268 0.3334 0.2336 0.0087  0.0025  -0.0247 64  GLY   A C   
455  O O   . GLY   A 64  ? 0.2297 0.3373 0.2376 0.0104  0.0012  -0.0253 64  GLY   A O   
456  N N   . THR   A 65  ? 0.2028 0.3052 0.2066 0.0077  0.0031  -0.0217 65  THR   A N   
457  C CA  . THR   A 65  ? 0.1853 0.2840 0.1872 0.0088  0.0021  -0.0190 65  THR   A CA  
458  C C   . THR   A 65  ? 0.2269 0.3215 0.2271 0.0098  0.0014  -0.0169 65  THR   A C   
459  O O   . THR   A 65  ? 0.2063 0.2979 0.2042 0.0090  0.0019  -0.0144 65  THR   A O   
460  C CB  . THR   A 65  ? 0.1920 0.2896 0.1923 0.0067  0.0034  -0.0176 65  THR   A CB  
461  O OG1 . THR   A 65  ? 0.2018 0.2977 0.2003 0.0048  0.0048  -0.0160 65  THR   A OG1 
462  C CG2 . THR   A 65  ? 0.2034 0.3047 0.2055 0.0054  0.0044  -0.0199 65  THR   A CG2 
463  N N   . PRO   A 66  ? 0.2528 0.3473 0.2545 0.0119  0.0003  -0.0178 66  PRO   A N   
464  C CA  . PRO   A 66  ? 0.2537 0.3446 0.2544 0.0126  0.0000  -0.0162 66  PRO   A CA  
465  C C   . PRO   A 66  ? 0.2824 0.3691 0.2808 0.0137  -0.0009 -0.0135 66  PRO   A C   
466  O O   . PRO   A 66  ? 0.2680 0.3515 0.2652 0.0137  -0.0008 -0.0121 66  PRO   A O   
467  C CB  . PRO   A 66  ? 0.2743 0.3662 0.2777 0.0146  -0.0008 -0.0184 66  PRO   A CB  
468  C CG  . PRO   A 66  ? 0.2639 0.3591 0.2694 0.0160  -0.0019 -0.0201 66  PRO   A CG  
469  C CD  . PRO   A 66  ? 0.2541 0.3522 0.2590 0.0135  -0.0006 -0.0207 66  PRO   A CD  
470  N N   . GLU   A 67  ? 0.2572 0.3444 0.2553 0.0144  -0.0017 -0.0132 67  GLU   A N   
471  C CA  . GLU   A 67  ? 0.2553 0.3392 0.2512 0.0153  -0.0025 -0.0108 67  GLU   A CA  
472  C C   . GLU   A 67  ? 0.2240 0.3066 0.2178 0.0132  -0.0014 -0.0092 67  GLU   A C   
473  O O   . GLU   A 67  ? 0.2090 0.2891 0.2010 0.0135  -0.0019 -0.0074 67  GLU   A O   
474  C CB  . GLU   A 67  ? 0.3161 0.4018 0.3126 0.0172  -0.0040 -0.0113 67  GLU   A CB  
475  C CG  . GLU   A 67  ? 0.4008 0.4867 0.3990 0.0199  -0.0054 -0.0121 67  GLU   A CG  
476  C CD  . GLU   A 67  ? 0.5010 0.5872 0.4988 0.0226  -0.0073 -0.0115 67  GLU   A CD  
477  O OE1 . GLU   A 67  ? 0.6146 0.6991 0.6099 0.0227  -0.0077 -0.0095 67  GLU   A OE1 
478  O OE2 . GLU   A 67  ? 0.6139 0.7025 0.6141 0.0248  -0.0084 -0.0132 67  GLU   A OE2 
479  N N   . ILE   A 68  ? 0.1916 0.2759 0.1858 0.0112  -0.0001 -0.0098 68  ILE   A N   
480  C CA  . ILE   A 68  ? 0.1752 0.2576 0.1675 0.0095  0.0009  -0.0080 68  ILE   A CA  
481  C C   . ILE   A 68  ? 0.1759 0.2553 0.1668 0.0095  0.0010  -0.0064 68  ILE   A C   
482  O O   . ILE   A 68  ? 0.1622 0.2422 0.1537 0.0094  0.0013  -0.0071 68  ILE   A O   
483  C CB  . ILE   A 68  ? 0.1773 0.2616 0.1701 0.0074  0.0024  -0.0086 68  ILE   A CB  
484  C CG1 . ILE   A 68  ? 0.1713 0.2588 0.1659 0.0071  0.0026  -0.0105 68  ILE   A CG1 
485  C CG2 . ILE   A 68  ? 0.1781 0.2600 0.1692 0.0061  0.0033  -0.0065 68  ILE   A CG2 
486  C CD1 . ILE   A 68  ? 0.1674 0.2563 0.1624 0.0048  0.0044  -0.0112 68  ILE   A CD1 
487  N N   . ARG   A 69  ? 0.1613 0.2379 0.1506 0.0095  0.0008  -0.0046 69  ARG   A N   
488  C CA  . ARG   A 69  ? 0.1699 0.2440 0.1580 0.0095  0.0009  -0.0035 69  ARG   A CA  
489  C C   . ARG   A 69  ? 0.1508 0.2253 0.1383 0.0080  0.0019  -0.0029 69  ARG   A C   
490  O O   . ARG   A 69  ? 0.1413 0.2167 0.1287 0.0069  0.0026  -0.0025 69  ARG   A O   
491  C CB  . ARG   A 69  ? 0.1847 0.2559 0.1712 0.0100  0.0004  -0.0020 69  ARG   A CB  
492  C CG  . ARG   A 69  ? 0.2214 0.2923 0.2079 0.0116  -0.0008 -0.0020 69  ARG   A CG  
493  C CD  . ARG   A 69  ? 0.2871 0.3566 0.2719 0.0114  -0.0009 -0.0008 69  ARG   A CD  
494  N NE  . ARG   A 69  ? 0.3713 0.4408 0.3554 0.0128  -0.0020 -0.0005 69  ARG   A NE  
495  C CZ  . ARG   A 69  ? 0.3642 0.4367 0.3491 0.0135  -0.0027 -0.0016 69  ARG   A CZ  
496  N NH1 . ARG   A 69  ? 0.3473 0.4227 0.3340 0.0125  -0.0021 -0.0031 69  ARG   A NH1 
497  N NH2 . ARG   A 69  ? 0.4234 0.4960 0.4074 0.0151  -0.0040 -0.0011 69  ARG   A NH2 
498  N N   . ILE   A 70  ? 0.1468 0.2206 0.1339 0.0079  0.0021  -0.0028 70  ILE   A N   
499  C CA  . ILE   A 70  ? 0.1436 0.2180 0.1298 0.0067  0.0028  -0.0020 70  ILE   A CA  
500  C C   . ILE   A 70  ? 0.1398 0.2120 0.1250 0.0067  0.0027  -0.0007 70  ILE   A C   
501  O O   . ILE   A 70  ? 0.1341 0.2050 0.1192 0.0071  0.0025  -0.0011 70  ILE   A O   
502  C CB  . ILE   A 70  ? 0.1506 0.2274 0.1375 0.0063  0.0032  -0.0033 70  ILE   A CB  
503  C CG1 . ILE   A 70  ? 0.1467 0.2262 0.1349 0.0062  0.0034  -0.0049 70  ILE   A CG1 
504  C CG2 . ILE   A 70  ? 0.1534 0.2312 0.1389 0.0053  0.0038  -0.0022 70  ILE   A CG2 
505  C CD1 . ILE   A 70  ? 0.1504 0.2327 0.1393 0.0056  0.0039  -0.0065 70  ILE   A CD1 
506  N N   . ALA   A 71  ? 0.1332 0.2048 0.1177 0.0062  0.0029  0.0005  71  ALA   A N   
507  C CA  . ALA   A 71  ? 0.1402 0.2103 0.1239 0.0061  0.0029  0.0015  71  ALA   A CA  
508  C C   . ALA   A 71  ? 0.1524 0.2239 0.1356 0.0056  0.0033  0.0022  71  ALA   A C   
509  O O   . ALA   A 71  ? 0.1497 0.2227 0.1328 0.0052  0.0037  0.0026  71  ALA   A O   
510  C CB  . ALA   A 71  ? 0.1525 0.2210 0.1360 0.0061  0.0028  0.0023  71  ALA   A CB  
511  N N   . THR   A 72  ? 0.1386 0.2098 0.1214 0.0056  0.0032  0.0024  72  THR   A N   
512  C CA  . THR   A 72  ? 0.1536 0.2265 0.1359 0.0054  0.0032  0.0031  72  THR   A CA  
513  C C   . THR   A 72  ? 0.1591 0.2309 0.1414 0.0056  0.0031  0.0036  72  THR   A C   
514  O O   . THR   A 72  ? 0.1753 0.2450 0.1578 0.0056  0.0030  0.0035  72  THR   A O   
515  C CB  . THR   A 72  ? 0.1655 0.2409 0.1478 0.0052  0.0033  0.0019  72  THR   A CB  
516  O OG1 . THR   A 72  ? 0.1660 0.2439 0.1475 0.0051  0.0033  0.0028  72  THR   A OG1 
517  C CG2 . THR   A 72  ? 0.1626 0.2373 0.1454 0.0052  0.0033  0.0004  72  THR   A CG2 
518  N N   . VAL   A 73  ? 0.1431 0.2168 0.1251 0.0057  0.0029  0.0041  73  VAL   A N   
519  C CA  . VAL   A 73  ? 0.1499 0.2232 0.1322 0.0060  0.0027  0.0045  73  VAL   A CA  
520  C C   . VAL   A 73  ? 0.1543 0.2304 0.1366 0.0060  0.0025  0.0034  73  VAL   A C   
521  O O   . VAL   A 73  ? 0.1443 0.2231 0.1261 0.0060  0.0024  0.0033  73  VAL   A O   
522  C CB  . VAL   A 73  ? 0.1527 0.2256 0.1351 0.0066  0.0026  0.0063  73  VAL   A CB  
523  C CG1 . VAL   A 73  ? 0.1721 0.2423 0.1550 0.0063  0.0030  0.0067  73  VAL   A CG1 
524  C CG2 . VAL   A 73  ? 0.1753 0.2502 0.1567 0.0068  0.0026  0.0075  73  VAL   A CG2 
525  N N   . THR   A 74  ? 0.1556 0.2313 0.1385 0.0059  0.0025  0.0025  74  THR   A N   
526  C CA  . THR   A 74  ? 0.1413 0.2201 0.1246 0.0058  0.0024  0.0012  74  THR   A CA  
527  C C   . THR   A 74  ? 0.1501 0.2290 0.1343 0.0061  0.0021  0.0012  74  THR   A C   
528  O O   . THR   A 74  ? 0.1431 0.2194 0.1275 0.0063  0.0022  0.0020  74  THR   A O   
529  C CB  . THR   A 74  ? 0.1326 0.2111 0.1162 0.0048  0.0030  -0.0010 74  THR   A CB  
530  O OG1 . THR   A 74  ? 0.1435 0.2186 0.1273 0.0043  0.0035  -0.0012 74  THR   A OG1 
531  C CG2 . THR   A 74  ? 0.1429 0.2216 0.1263 0.0046  0.0032  -0.0013 74  THR   A CG2 
532  N N   . ASN   A 75  ? 0.1417 0.2243 0.1264 0.0064  0.0018  0.0001  75  ASN   A N   
533  C CA  . ASN   A 75  ? 0.1379 0.2219 0.1236 0.0070  0.0014  -0.0001 75  ASN   A CA  
534  C C   . ASN   A 75  ? 0.1409 0.2235 0.1267 0.0083  0.0008  0.0023  75  ASN   A C   
535  O O   . ASN   A 75  ? 0.1354 0.2170 0.1225 0.0086  0.0007  0.0022  75  ASN   A O   
536  C CB  . ASN   A 75  ? 0.1342 0.2164 0.1208 0.0059  0.0021  -0.0018 75  ASN   A CB  
537  C CG  . ASN   A 75  ? 0.1345 0.2199 0.1227 0.0062  0.0019  -0.0033 75  ASN   A CG  
538  O OD1 . ASN   A 75  ? 0.1416 0.2313 0.1301 0.0068  0.0013  -0.0041 75  ASN   A OD1 
539  N ND2 . ASN   A 75  ? 0.1312 0.2149 0.1203 0.0056  0.0023  -0.0041 75  ASN   A ND2 
540  N N   . PHE   A 76  ? 0.1496 0.2322 0.1343 0.0089  0.0005  0.0042  76  PHE   A N   
541  C CA  . PHE   A 76  ? 0.1550 0.2348 0.1396 0.0096  0.0005  0.0064  76  PHE   A CA  
542  C C   . PHE   A 76  ? 0.1783 0.2599 0.1624 0.0110  -0.0003 0.0086  76  PHE   A C   
543  O O   . PHE   A 76  ? 0.1713 0.2560 0.1540 0.0112  -0.0006 0.0088  76  PHE   A O   
544  C CB  . PHE   A 76  ? 0.1608 0.2384 0.1444 0.0087  0.0011  0.0068  76  PHE   A CB  
545  C CG  . PHE   A 76  ? 0.1776 0.2524 0.1612 0.0089  0.0015  0.0088  76  PHE   A CG  
546  C CD1 . PHE   A 76  ? 0.1792 0.2544 0.1618 0.0095  0.0014  0.0108  76  PHE   A CD1 
547  C CD2 . PHE   A 76  ? 0.1786 0.2504 0.1632 0.0084  0.0020  0.0083  76  PHE   A CD2 
548  C CE1 . PHE   A 76  ? 0.1899 0.2622 0.1727 0.0095  0.0020  0.0124  76  PHE   A CE1 
549  C CE2 . PHE   A 76  ? 0.1987 0.2682 0.1838 0.0085  0.0025  0.0097  76  PHE   A CE2 
550  C CZ  . PHE   A 76  ? 0.1832 0.2527 0.1675 0.0090  0.0026  0.0116  76  PHE   A CZ  
551  N N   . PRO   A 77  A 0.1766 0.2561 0.1615 0.0121  -0.0004 0.0103  77  PRO   A N   
552  C CA  . PRO   A 77  A 0.1741 0.2505 0.1609 0.0119  0.0001  0.0097  77  PRO   A CA  
553  C C   . PRO   A 77  A 0.1684 0.2462 0.1572 0.0125  -0.0003 0.0082  77  PRO   A C   
554  O O   . PRO   A 77  A 0.1832 0.2588 0.1737 0.0123  0.0001  0.0075  77  PRO   A O   
555  C CB  . PRO   A 77  A 0.1956 0.2694 0.1826 0.0129  0.0003  0.0123  77  PRO   A CB  
556  C CG  . PRO   A 77  A 0.1900 0.2665 0.1759 0.0145  -0.0007 0.0141  77  PRO   A CG  
557  C CD  . PRO   A 77  A 0.1882 0.2684 0.1722 0.0137  -0.0010 0.0130  77  PRO   A CD  
558  N N   . HIS   A 78  ? 0.1596 0.2415 0.1484 0.0132  -0.0012 0.0073  78  HIS   A N   
559  C CA  . HIS   A 78  ? 0.1723 0.2566 0.1632 0.0141  -0.0018 0.0060  78  HIS   A CA  
560  C C   . HIS   A 78  ? 0.1626 0.2465 0.1549 0.0126  -0.0010 0.0031  78  HIS   A C   
561  O O   . HIS   A 78  ? 0.1673 0.2517 0.1618 0.0132  -0.0012 0.0021  78  HIS   A O   
562  C CB  . HIS   A 78  ? 0.1680 0.2576 0.1584 0.0151  -0.0029 0.0055  78  HIS   A CB  
563  C CG  . HIS   A 78  ? 0.1747 0.2661 0.1633 0.0135  -0.0025 0.0042  78  HIS   A CG  
564  N ND1 . HIS   A 78  ? 0.1662 0.2583 0.1554 0.0118  -0.0017 0.0013  78  HIS   A ND1 
565  C CD2 . HIS   A 78  ? 0.1695 0.2622 0.1560 0.0135  -0.0026 0.0054  78  HIS   A CD2 
566  C CE1 . HIS   A 78  ? 0.1783 0.2720 0.1661 0.0108  -0.0014 0.0006  78  HIS   A CE1 
567  N NE2 . HIS   A 78  ? 0.1676 0.2619 0.1536 0.0118  -0.0020 0.0030  78  HIS   A NE2 
568  N N   . GLY   A 79  ? 0.1537 0.2367 0.1447 0.0107  -0.0002 0.0019  79  GLY   A N   
569  C CA  . GLY   A 79  ? 0.1498 0.2325 0.1416 0.0092  0.0007  -0.0006 79  GLY   A CA  
570  C C   . GLY   A 79  ? 0.1636 0.2506 0.1569 0.0093  0.0004  -0.0029 79  GLY   A C   
571  O O   . GLY   A 79  ? 0.1495 0.2369 0.1444 0.0088  0.0008  -0.0047 79  GLY   A O   
572  N N   . ASN   A 80  ? 0.1604 0.2512 0.1531 0.0099  -0.0003 -0.0032 80  ASN   A N   
573  C CA  . ASN   A 80  ? 0.1658 0.2614 0.1600 0.0099  -0.0006 -0.0057 80  ASN   A CA  
574  C C   . ASN   A 80  ? 0.1720 0.2669 0.1663 0.0074  0.0010  -0.0085 80  ASN   A C   
575  O O   . ASN   A 80  ? 0.1649 0.2557 0.1577 0.0060  0.0020  -0.0080 80  ASN   A O   
576  C CB  . ASN   A 80  ? 0.1723 0.2724 0.1656 0.0109  -0.0016 -0.0054 80  ASN   A CB  
577  C CG  . ASN   A 80  ? 0.1936 0.2950 0.1867 0.0135  -0.0031 -0.0027 80  ASN   A CG  
578  O OD1 . ASN   A 80  ? 0.1825 0.2822 0.1769 0.0148  -0.0036 -0.0015 80  ASN   A OD1 
579  N ND2 . ASN   A 80  ? 0.2157 0.3200 0.2070 0.0142  -0.0039 -0.0015 80  ASN   A ND2 
580  N N   . ASP   A 81  ? 0.1836 0.2824 0.1797 0.0068  0.0012  -0.0115 81  ASP   A N   
581  C CA  . ASP   A 81  ? 0.1854 0.2833 0.1817 0.0043  0.0029  -0.0142 81  ASP   A CA  
582  C C   . ASP   A 81  ? 0.1710 0.2720 0.1672 0.0031  0.0035  -0.0164 81  ASP   A C   
583  O O   . ASP   A 81  ? 0.1773 0.2789 0.1745 0.0011  0.0050  -0.0193 81  ASP   A O   
584  C CB  . ASP   A 81  ? 0.2008 0.3005 0.1994 0.0038  0.0033  -0.0165 81  ASP   A CB  
585  C CG  . ASP   A 81  ? 0.2528 0.3590 0.2539 0.0055  0.0020  -0.0181 81  ASP   A CG  
586  O OD1 . ASP   A 81  ? 0.2335 0.3429 0.2342 0.0069  0.0008  -0.0175 81  ASP   A OD1 
587  O OD2 . ASP   A 81  ? 0.2973 0.4052 0.3007 0.0055  0.0021  -0.0200 81  ASP   A OD2 
588  N N   . ASP   A 82  ? 0.1643 0.2669 0.1595 0.0041  0.0027  -0.0153 82  ASP   A N   
589  C CA  . ASP   A 82  ? 0.1800 0.2855 0.1753 0.0028  0.0034  -0.0176 82  ASP   A CA  
590  C C   . ASP   A 82  ? 0.1733 0.2734 0.1670 0.0013  0.0048  -0.0168 82  ASP   A C   
591  O O   . ASP   A 82  ? 0.1553 0.2536 0.1474 0.0022  0.0041  -0.0145 82  ASP   A O   
592  C CB  . ASP   A 82  ? 0.1696 0.2805 0.1646 0.0044  0.0019  -0.0172 82  ASP   A CB  
593  C CG  . ASP   A 82  ? 0.1934 0.3084 0.1891 0.0029  0.0028  -0.0203 82  ASP   A CG  
594  O OD1 . ASP   A 82  ? 0.1947 0.3062 0.1900 0.0011  0.0044  -0.0212 82  ASP   A OD1 
595  O OD2 . ASP   A 82  ? 0.2346 0.3564 0.2313 0.0038  0.0018  -0.0220 82  ASP   A OD2 
596  N N   . ILE   A 83  ? 0.1721 0.2697 0.1662 -0.0009 0.0066  -0.0189 83  ILE   A N   
597  C CA  . ILE   A 83  ? 0.1758 0.2680 0.1685 -0.0023 0.0079  -0.0182 83  ILE   A CA  
598  C C   . ILE   A 83  ? 0.1819 0.2755 0.1745 -0.0022 0.0079  -0.0187 83  ILE   A C   
599  O O   . ILE   A 83  ? 0.1799 0.2698 0.1711 -0.0019 0.0079  -0.0168 83  ILE   A O   
600  C CB  . ILE   A 83  ? 0.1905 0.2798 0.1835 -0.0047 0.0101  -0.0203 83  ILE   A CB  
601  C CG1 . ILE   A 83  ? 0.2106 0.2982 0.2035 -0.0049 0.0102  -0.0197 83  ILE   A CG1 
602  C CG2 . ILE   A 83  ? 0.1959 0.2796 0.1876 -0.0057 0.0113  -0.0194 83  ILE   A CG2 
603  C CD1 . ILE   A 83  ? 0.2173 0.3033 0.2106 -0.0075 0.0124  -0.0221 83  ILE   A CD1 
604  N N   . GLU   A 84  ? 0.1779 0.2771 0.1720 -0.0027 0.0081  -0.0215 84  GLU   A N   
605  C CA  . GLU   A 84  ? 0.2052 0.3064 0.1994 -0.0030 0.0083  -0.0226 84  GLU   A CA  
606  C C   . GLU   A 84  ? 0.1664 0.2682 0.1590 -0.0010 0.0066  -0.0196 84  GLU   A C   
607  O O   . GLU   A 84  ? 0.1732 0.2733 0.1652 -0.0012 0.0069  -0.0192 84  GLU   A O   
608  C CB  . GLU   A 84  ? 0.2491 0.3574 0.2454 -0.0038 0.0086  -0.0264 84  GLU   A CB  
609  C CG  . GLU   A 84  ? 0.3206 0.4280 0.3188 -0.0063 0.0109  -0.0299 84  GLU   A CG  
610  C CD  . GLU   A 84  ? 0.4961 0.5991 0.4946 -0.0081 0.0129  -0.0311 84  GLU   A CD  
611  O OE1 . GLU   A 84  ? 0.5765 0.6772 0.5739 -0.0073 0.0125  -0.0293 84  GLU   A OE1 
612  O OE2 . GLU   A 84  ? 0.6476 0.7493 0.6476 -0.0104 0.0151  -0.0340 84  GLU   A OE2 
613  N N   . ILE   A 85  ? 0.1518 0.2563 0.1439 0.0008  0.0049  -0.0177 85  ILE   A N   
614  C CA  . ILE   A 85  ? 0.1390 0.2435 0.1293 0.0025  0.0035  -0.0147 85  ILE   A CA  
615  C C   . ILE   A 85  ? 0.1362 0.2339 0.1252 0.0025  0.0039  -0.0121 85  ILE   A C   
616  O O   . ILE   A 85  ? 0.1361 0.2326 0.1241 0.0026  0.0038  -0.0110 85  ILE   A O   
617  C CB  . ILE   A 85  ? 0.1510 0.2589 0.1409 0.0045  0.0018  -0.0129 85  ILE   A CB  
618  C CG1 . ILE   A 85  ? 0.1588 0.2747 0.1498 0.0048  0.0011  -0.0154 85  ILE   A CG1 
619  C CG2 . ILE   A 85  ? 0.1515 0.2579 0.1395 0.0060  0.0007  -0.0092 85  ILE   A CG2 
620  C CD1 . ILE   A 85  ? 0.1639 0.2838 0.1547 0.0071  -0.0008 -0.0137 85  ILE   A CD1 
621  N N   . ALA   A 86  ? 0.1426 0.2363 0.1316 0.0024  0.0041  -0.0113 86  ALA   A N   
622  C CA  . ALA   A 86  ? 0.1388 0.2268 0.1266 0.0025  0.0043  -0.0091 86  ALA   A CA  
623  C C   . ALA   A 86  ? 0.1481 0.2333 0.1356 0.0014  0.0054  -0.0099 86  ALA   A C   
624  O O   . ALA   A 86  ? 0.1486 0.2315 0.1352 0.0018  0.0052  -0.0083 86  ALA   A O   
625  C CB  . ALA   A 86  ? 0.1501 0.2353 0.1381 0.0022  0.0046  -0.0087 86  ALA   A CB  
626  N N   . LEU   A 87  ? 0.1424 0.2280 0.1311 -0.0001 0.0067  -0.0125 87  LEU   A N   
627  C CA  . LEU   A 87  ? 0.1450 0.2274 0.1338 -0.0011 0.0079  -0.0135 87  LEU   A CA  
628  C C   . LEU   A 87  ? 0.1433 0.2286 0.1325 -0.0007 0.0076  -0.0140 87  LEU   A C   
629  O O   . LEU   A 87  ? 0.1477 0.2301 0.1365 -0.0005 0.0078  -0.0133 87  LEU   A O   
630  C CB  . LEU   A 87  ? 0.1550 0.2371 0.1451 -0.0029 0.0096  -0.0163 87  LEU   A CB  
631  C CG  . LEU   A 87  ? 0.1686 0.2472 0.1594 -0.0040 0.0112  -0.0175 87  LEU   A CG  
632  C CD1 . LEU   A 87  ? 0.1774 0.2497 0.1666 -0.0033 0.0111  -0.0149 87  LEU   A CD1 
633  C CD2 . LEU   A 87  ? 0.1809 0.2590 0.1730 -0.0061 0.0132  -0.0204 87  LEU   A CD2 
634  N N   . ALA   A 88  ? 0.1440 0.2353 0.1338 -0.0006 0.0071  -0.0154 88  ALA   A N   
635  C CA  . ALA   A 88  ? 0.1488 0.2436 0.1388 -0.0005 0.0069  -0.0162 88  ALA   A CA  
636  C C   . ALA   A 88  ? 0.1542 0.2474 0.1425 0.0008  0.0058  -0.0132 88  ALA   A C   
637  O O   . ALA   A 88  ? 0.1597 0.2524 0.1481 0.0007  0.0061  -0.0135 88  ALA   A O   
638  C CB  . ALA   A 88  ? 0.1429 0.2448 0.1334 -0.0004 0.0063  -0.0179 88  ALA   A CB  
639  N N   . GLU   A 89  ? 0.1454 0.2381 0.1324 0.0020  0.0047  -0.0106 89  GLU   A N   
640  C CA  . GLU   A 89  ? 0.1451 0.2361 0.1307 0.0030  0.0040  -0.0079 89  GLU   A CA  
641  C C   . GLU   A 89  ? 0.1448 0.2305 0.1304 0.0028  0.0045  -0.0073 89  GLU   A C   
642  O O   . GLU   A 89  ? 0.1444 0.2297 0.1297 0.0030  0.0045  -0.0068 89  GLU   A O   
643  C CB  . GLU   A 89  ? 0.1603 0.2511 0.1450 0.0041  0.0030  -0.0055 89  GLU   A CB  
644  C CG  . GLU   A 89  ? 0.1781 0.2744 0.1627 0.0048  0.0021  -0.0055 89  GLU   A CG  
645  C CD  . GLU   A 89  ? 0.1961 0.2918 0.1799 0.0063  0.0011  -0.0027 89  GLU   A CD  
646  O OE1 . GLU   A 89  ? 0.2206 0.3118 0.2046 0.0064  0.0013  -0.0015 89  GLU   A OE1 
647  O OE2 . GLU   A 89  ? 0.1988 0.2982 0.1821 0.0074  0.0001  -0.0017 89  GLU   A OE2 
648  N N   . THR   A 90  ? 0.1399 0.2219 0.1259 0.0023  0.0051  -0.0076 90  THR   A N   
649  C CA  . THR   A 90  ? 0.1397 0.2167 0.1254 0.0023  0.0055  -0.0069 90  THR   A CA  
650  C C   . THR   A 90  ? 0.1447 0.2212 0.1314 0.0019  0.0063  -0.0087 90  THR   A C   
651  O O   . THR   A 90  ? 0.1310 0.2060 0.1177 0.0025  0.0061  -0.0080 90  THR   A O   
652  C CB  . THR   A 90  ? 0.1442 0.2178 0.1296 0.0019  0.0060  -0.0067 90  THR   A CB  
653  O OG1 . THR   A 90  ? 0.1539 0.2280 0.1387 0.0024  0.0053  -0.0051 90  THR   A OG1 
654  C CG2 . THR   A 90  ? 0.1487 0.2174 0.1335 0.0020  0.0064  -0.0058 90  THR   A CG2 
655  N N   . ARG   A 91  ? 0.1611 0.2396 0.1491 0.0009  0.0072  -0.0112 91  ARG   A N   
656  C CA  . ARG   A 91  ? 0.1673 0.2458 0.1569 0.0005  0.0080  -0.0132 91  ARG   A CA  
657  C C   . ARG   A 91  ? 0.1507 0.2329 0.1403 0.0010  0.0073  -0.0132 91  ARG   A C   
658  O O   . ARG   A 91  ? 0.1461 0.2270 0.1365 0.0013  0.0075  -0.0137 91  ARG   A O   
659  C CB  . ARG   A 91  ? 0.1834 0.2642 0.1748 -0.0009 0.0092  -0.0164 91  ARG   A CB  
660  C CG  . ARG   A 91  ? 0.2111 0.2877 0.2026 -0.0018 0.0104  -0.0168 91  ARG   A CG  
661  C CD  . ARG   A 91  ? 0.2603 0.3404 0.2539 -0.0034 0.0117  -0.0203 91  ARG   A CD  
662  N NE  . ARG   A 91  ? 0.2863 0.3623 0.2801 -0.0046 0.0132  -0.0210 91  ARG   A NE  
663  C CZ  . ARG   A 91  ? 0.3074 0.3858 0.3027 -0.0063 0.0145  -0.0239 91  ARG   A CZ  
664  N NH1 . ARG   A 91  ? 0.3037 0.3891 0.3002 -0.0066 0.0142  -0.0261 91  ARG   A NH1 
665  N NH2 . ARG   A 91  ? 0.3019 0.3758 0.2976 -0.0077 0.0163  -0.0246 91  ARG   A NH2 
666  N N   . ALA   A 92  ? 0.1528 0.2395 0.1414 0.0012  0.0065  -0.0126 92  ALA   A N   
667  C CA  . ALA   A 92  ? 0.1541 0.2443 0.1422 0.0015  0.0060  -0.0124 92  ALA   A CA  
668  C C   . ALA   A 92  ? 0.1461 0.2331 0.1333 0.0023  0.0055  -0.0101 92  ALA   A C   
669  O O   . ALA   A 92  ? 0.1333 0.2209 0.1211 0.0023  0.0057  -0.0108 92  ALA   A O   
670  C CB  . ALA   A 92  ? 0.1684 0.2636 0.1551 0.0016  0.0053  -0.0116 92  ALA   A CB  
671  N N   . ALA   A 93  ? 0.1454 0.2293 0.1314 0.0030  0.0050  -0.0078 93  ALA   A N   
672  C CA  . ALA   A 93  ? 0.1482 0.2292 0.1336 0.0037  0.0046  -0.0060 93  ALA   A CA  
673  C C   . ALA   A 93  ? 0.1528 0.2311 0.1395 0.0039  0.0050  -0.0071 93  ALA   A C   
674  O O   . ALA   A 93  ? 0.1421 0.2206 0.1290 0.0043  0.0048  -0.0070 93  ALA   A O   
675  C CB  . ALA   A 93  ? 0.1417 0.2197 0.1262 0.0041  0.0042  -0.0040 93  ALA   A CB  
676  N N   . ILE   A 94  ? 0.1564 0.2320 0.1438 0.0037  0.0055  -0.0081 94  ILE   A N   
677  C CA  . ILE   A 94  ? 0.1605 0.2330 0.1492 0.0041  0.0059  -0.0090 94  ILE   A CA  
678  C C   . ILE   A 94  ? 0.1487 0.2243 0.1392 0.0039  0.0063  -0.0113 94  ILE   A C   
679  O O   . ILE   A 94  ? 0.1561 0.2307 0.1475 0.0047  0.0061  -0.0116 94  ILE   A O   
680  C CB  . ILE   A 94  ? 0.1700 0.2390 0.1590 0.0037  0.0067  -0.0096 94  ILE   A CB  
681  C CG1 . ILE   A 94  ? 0.1669 0.2329 0.1541 0.0038  0.0064  -0.0074 94  ILE   A CG1 
682  C CG2 . ILE   A 94  ? 0.1899 0.2556 0.1805 0.0042  0.0073  -0.0105 94  ILE   A CG2 
683  C CD1 . ILE   A 94  ? 0.1548 0.2181 0.1419 0.0029  0.0075  -0.0079 94  ILE   A CD1 
684  N N   . ALA   A 95  ? 0.1455 0.2250 0.1367 0.0029  0.0068  -0.0132 95  ALA   A N   
685  C CA  . ALA   A 95  ? 0.1512 0.2341 0.1444 0.0024  0.0074  -0.0159 95  ALA   A CA  
686  C C   . ALA   A 95  ? 0.1474 0.2335 0.1399 0.0026  0.0068  -0.0153 95  ALA   A C   
687  O O   . ALA   A 95  ? 0.1470 0.2344 0.1412 0.0027  0.0071  -0.0171 95  ALA   A O   
688  C CB  . ALA   A 95  ? 0.1513 0.2383 0.1450 0.0011  0.0081  -0.0180 95  ALA   A CB  
689  N N   . TYR   A 96  ? 0.1389 0.2258 0.1291 0.0028  0.0061  -0.0128 96  TYR   A N   
690  C CA  . TYR   A 96  ? 0.1427 0.2319 0.1321 0.0028  0.0058  -0.0120 96  TYR   A CA  
691  C C   . TYR   A 96  ? 0.1558 0.2421 0.1461 0.0037  0.0055  -0.0118 96  TYR   A C   
692  O O   . TYR   A 96  ? 0.1581 0.2466 0.1485 0.0036  0.0056  -0.0121 96  TYR   A O   
693  C CB  . TYR   A 96  ? 0.1371 0.2269 0.1239 0.0028  0.0052  -0.0092 96  TYR   A CB  
694  C CG  . TYR   A 96  ? 0.1407 0.2351 0.1262 0.0022  0.0052  -0.0090 96  TYR   A CG  
695  C CD1 . TYR   A 96  ? 0.1473 0.2463 0.1323 0.0014  0.0055  -0.0099 96  TYR   A CD1 
696  C CD2 . TYR   A 96  ? 0.1512 0.2455 0.1355 0.0024  0.0047  -0.0076 96  TYR   A CD2 
697  C CE1 . TYR   A 96  ? 0.1440 0.2475 0.1273 0.0009  0.0054  -0.0095 96  TYR   A CE1 
698  C CE2 . TYR   A 96  ? 0.1500 0.2486 0.1328 0.0022  0.0045  -0.0071 96  TYR   A CE2 
699  C CZ  . TYR   A 96  ? 0.1503 0.2536 0.1325 0.0015  0.0047  -0.0078 96  TYR   A CZ  
700  O OH  . TYR   A 96  ? 0.1602 0.2681 0.1406 0.0014  0.0043  -0.0071 96  TYR   A OH  
701  N N   . GLY   A 97  ? 0.1519 0.2335 0.1424 0.0046  0.0052  -0.0109 97  GLY   A N   
702  C CA  . GLY   A 97  ? 0.1499 0.2288 0.1411 0.0058  0.0047  -0.0106 97  GLY   A CA  
703  C C   . GLY   A 97  ? 0.1533 0.2295 0.1429 0.0064  0.0041  -0.0080 97  GLY   A C   
704  O O   . GLY   A 97  ? 0.1559 0.2311 0.1459 0.0073  0.0035  -0.0077 97  GLY   A O   
705  N N   . ALA   A 98  ? 0.1448 0.2199 0.1328 0.0060  0.0040  -0.0065 98  ALA   A N   
706  C CA  . ALA   A 98  ? 0.1495 0.2223 0.1362 0.0064  0.0035  -0.0044 98  ALA   A CA  
707  C C   . ALA   A 98  ? 0.1469 0.2161 0.1338 0.0076  0.0031  -0.0042 98  ALA   A C   
708  O O   . ALA   A 98  ? 0.1574 0.2246 0.1450 0.0078  0.0034  -0.0049 98  ALA   A O   
709  C CB  . ALA   A 98  ? 0.1452 0.2172 0.1306 0.0059  0.0036  -0.0032 98  ALA   A CB  
710  N N   . ASP   A 99  ? 0.1472 0.2158 0.1337 0.0082  0.0025  -0.0031 99  ASP   A N   
711  C CA  . ASP   A 99  ? 0.1402 0.2058 0.1261 0.0092  0.0019  -0.0023 99  ASP   A CA  
712  C C   . ASP   A 99  ? 0.1403 0.2038 0.1245 0.0087  0.0020  -0.0008 99  ASP   A C   
713  O O   . ASP   A 99  ? 0.1629 0.2235 0.1463 0.0092  0.0019  -0.0001 99  ASP   A O   
714  C CB  . ASP   A 99  ? 0.1502 0.2171 0.1366 0.0100  0.0012  -0.0023 99  ASP   A CB  
715  C CG  . ASP   A 99  ? 0.1565 0.2257 0.1448 0.0106  0.0011  -0.0041 99  ASP   A CG  
716  O OD1 . ASP   A 99  ? 0.1719 0.2401 0.1614 0.0114  0.0011  -0.0051 99  ASP   A OD1 
717  O OD2 . ASP   A 99  ? 0.1747 0.2467 0.1636 0.0101  0.0012  -0.0046 99  ASP   A OD2 
718  N N   . GLU   A 100 ? 0.1380 0.2030 0.1218 0.0078  0.0023  -0.0003 100 GLU   A N   
719  C CA  . GLU   A 100 ? 0.1467 0.2101 0.1293 0.0073  0.0024  0.0008  100 GLU   A CA  
720  C C   . GLU   A 100 ? 0.1513 0.2163 0.1338 0.0064  0.0028  0.0008  100 GLU   A C   
721  O O   . GLU   A 100 ? 0.1602 0.2277 0.1433 0.0062  0.0029  0.0006  100 GLU   A O   
722  C CB  . GLU   A 100 ? 0.1510 0.2146 0.1332 0.0075  0.0020  0.0016  100 GLU   A CB  
723  C CG  . GLU   A 100 ? 0.1591 0.2219 0.1411 0.0086  0.0013  0.0016  100 GLU   A CG  
724  C CD  . GLU   A 100 ? 0.1764 0.2401 0.1582 0.0087  0.0010  0.0019  100 GLU   A CD  
725  O OE1 . GLU   A 100 ? 0.1663 0.2310 0.1484 0.0079  0.0014  0.0021  100 GLU   A OE1 
726  O OE2 . GLU   A 100 ? 0.1892 0.2527 0.1708 0.0097  0.0002  0.0019  100 GLU   A OE2 
727  N N   . VAL   A 101 ? 0.1373 0.2013 0.1194 0.0059  0.0031  0.0010  101 VAL   A N   
728  C CA  . VAL   A 101 ? 0.1493 0.2150 0.1315 0.0054  0.0034  0.0010  101 VAL   A CA  
729  C C   . VAL   A 101 ? 0.1505 0.2153 0.1323 0.0052  0.0033  0.0018  101 VAL   A C   
730  O O   . VAL   A 101 ? 0.1519 0.2147 0.1331 0.0049  0.0035  0.0018  101 VAL   A O   
731  C CB  . VAL   A 101 ? 0.1591 0.2254 0.1417 0.0048  0.0039  -0.0003 101 VAL   A CB  
732  C CG1 . VAL   A 101 ? 0.1671 0.2357 0.1499 0.0044  0.0039  -0.0005 101 VAL   A CG1 
733  C CG2 . VAL   A 101 ? 0.1679 0.2356 0.1513 0.0049  0.0040  -0.0015 101 VAL   A CG2 
734  N N   . ASP   A 102 ? 0.1595 0.2258 0.1417 0.0053  0.0032  0.0025  102 ASP   A N   
735  C CA  . ASP   A 102 ? 0.1540 0.2197 0.1364 0.0052  0.0032  0.0030  102 ASP   A CA  
736  C C   . ASP   A 102 ? 0.1491 0.2166 0.1320 0.0051  0.0032  0.0026  102 ASP   A C   
737  O O   . ASP   A 102 ? 0.1551 0.2245 0.1383 0.0055  0.0030  0.0032  102 ASP   A O   
738  C CB  . ASP   A 102 ? 0.1542 0.2201 0.1371 0.0054  0.0031  0.0039  102 ASP   A CB  
739  C CG  . ASP   A 102 ? 0.1677 0.2327 0.1504 0.0055  0.0031  0.0039  102 ASP   A CG  
740  O OD1 . ASP   A 102 ? 0.1671 0.2315 0.1492 0.0056  0.0029  0.0034  102 ASP   A OD1 
741  O OD2 . ASP   A 102 ? 0.1937 0.2588 0.1772 0.0054  0.0033  0.0043  102 ASP   A OD2 
742  N N   . VAL   A 103 ? 0.1419 0.2089 0.1248 0.0045  0.0036  0.0017  103 VAL   A N   
743  C CA  . VAL   A 103 ? 0.1398 0.2089 0.1234 0.0044  0.0036  0.0008  103 VAL   A CA  
744  C C   . VAL   A 103 ? 0.1425 0.2118 0.1270 0.0046  0.0035  0.0011  103 VAL   A C   
745  O O   . VAL   A 103 ? 0.1464 0.2138 0.1308 0.0042  0.0038  0.0011  103 VAL   A O   
746  C CB  . VAL   A 103 ? 0.1405 0.2094 0.1241 0.0034  0.0043  -0.0008 103 VAL   A CB  
747  C CG1 . VAL   A 103 ? 0.1530 0.2192 0.1359 0.0026  0.0049  -0.0010 103 VAL   A CG1 
748  C CG2 . VAL   A 103 ? 0.1401 0.2122 0.1247 0.0033  0.0043  -0.0021 103 VAL   A CG2 
749  N N   . VAL   A 104 ? 0.1456 0.2174 0.1312 0.0053  0.0030  0.0010  104 VAL   A N   
750  C CA  . VAL   A 104 ? 0.1478 0.2200 0.1349 0.0057  0.0029  0.0010  104 VAL   A CA  
751  C C   . VAL   A 104 ? 0.1461 0.2193 0.1338 0.0048  0.0034  -0.0010 104 VAL   A C   
752  O O   . VAL   A 104 ? 0.1404 0.2160 0.1283 0.0046  0.0034  -0.0023 104 VAL   A O   
753  C CB  . VAL   A 104 ? 0.1518 0.2258 0.1398 0.0072  0.0021  0.0021  104 VAL   A CB  
754  C CG1 . VAL   A 104 ? 0.1624 0.2360 0.1523 0.0077  0.0021  0.0020  104 VAL   A CG1 
755  C CG2 . VAL   A 104 ? 0.1683 0.2415 0.1554 0.0078  0.0019  0.0041  104 VAL   A CG2 
756  N N   . PHE   A 105 ? 0.1300 0.2016 0.1180 0.0040  0.0039  -0.0016 105 PHE   A N   
757  C CA  . PHE   A 105 ? 0.1375 0.2101 0.1262 0.0029  0.0046  -0.0035 105 PHE   A CA  
758  C C   . PHE   A 105 ? 0.1316 0.2076 0.1225 0.0039  0.0040  -0.0045 105 PHE   A C   
759  O O   . PHE   A 105 ? 0.1264 0.2030 0.1185 0.0055  0.0032  -0.0033 105 PHE   A O   
760  C CB  . PHE   A 105 ? 0.1342 0.2047 0.1226 0.0021  0.0052  -0.0037 105 PHE   A CB  
761  C CG  . PHE   A 105 ? 0.1363 0.2076 0.1251 0.0006  0.0062  -0.0057 105 PHE   A CG  
762  C CD1 . PHE   A 105 ? 0.1454 0.2191 0.1367 0.0008  0.0062  -0.0072 105 PHE   A CD1 
763  C CD2 . PHE   A 105 ? 0.1467 0.2161 0.1335 -0.0011 0.0072  -0.0061 105 PHE   A CD2 
764  C CE1 . PHE   A 105 ? 0.1639 0.2384 0.1555 -0.0009 0.0072  -0.0093 105 PHE   A CE1 
765  C CE2 . PHE   A 105 ? 0.1585 0.2282 0.1452 -0.0028 0.0084  -0.0078 105 PHE   A CE2 
766  C CZ  . PHE   A 105 ? 0.1601 0.2326 0.1493 -0.0028 0.0084  -0.0096 105 PHE   A CZ  
767  N N   . PRO   A 106 ? 0.1371 0.2154 0.1288 0.0030  0.0045  -0.0067 106 PRO   A N   
768  C CA  . PRO   A 106 ? 0.1515 0.2338 0.1456 0.0041  0.0039  -0.0080 106 PRO   A CA  
769  C C   . PRO   A 106 ? 0.1493 0.2314 0.1453 0.0041  0.0041  -0.0088 106 PRO   A C   
770  O O   . PRO   A 106 ? 0.1408 0.2244 0.1378 0.0028  0.0049  -0.0112 106 PRO   A O   
771  C CB  . PRO   A 106 ? 0.1478 0.2328 0.1420 0.0028  0.0045  -0.0105 106 PRO   A CB  
772  C CG  . PRO   A 106 ? 0.1471 0.2286 0.1395 0.0006  0.0060  -0.0108 106 PRO   A CG  
773  C CD  . PRO   A 106 ? 0.1401 0.2177 0.1306 0.0012  0.0057  -0.0081 106 PRO   A CD  
774  N N   . TYR   A 107 ? 0.1459 0.2265 0.1425 0.0055  0.0034  -0.0070 107 TYR   A N   
775  C CA  . TYR   A 107 ? 0.1606 0.2407 0.1592 0.0054  0.0038  -0.0078 107 TYR   A CA  
776  C C   . TYR   A 107 ? 0.1574 0.2411 0.1593 0.0067  0.0032  -0.0094 107 TYR   A C   
777  O O   . TYR   A 107 ? 0.1637 0.2483 0.1675 0.0059  0.0038  -0.0116 107 TYR   A O   
778  C CB  . TYR   A 107 ? 0.1567 0.2338 0.1553 0.0063  0.0036  -0.0056 107 TYR   A CB  
779  C CG  . TYR   A 107 ? 0.1466 0.2237 0.1458 0.0085  0.0025  -0.0034 107 TYR   A CG  
780  C CD1 . TYR   A 107 ? 0.1628 0.2410 0.1648 0.0103  0.0018  -0.0033 107 TYR   A CD1 
781  C CD2 . TYR   A 107 ? 0.1391 0.2150 0.1359 0.0088  0.0021  -0.0013 107 TYR   A CD2 
782  C CE1 . TYR   A 107 ? 0.1614 0.2391 0.1636 0.0124  0.0009  -0.0009 107 TYR   A CE1 
783  C CE2 . TYR   A 107 ? 0.1419 0.2178 0.1389 0.0106  0.0013  0.0009  107 TYR   A CE2 
784  C CZ  . TYR   A 107 ? 0.1621 0.2386 0.1615 0.0124  0.0007  0.0013  107 TYR   A CZ  
785  O OH  . TYR   A 107 ? 0.1678 0.2440 0.1671 0.0143  -0.0001 0.0038  107 TYR   A OH  
786  N N   . ARG   A 108 ? 0.1488 0.2351 0.1515 0.0087  0.0019  -0.0087 108 ARG   A N   
787  C CA  . ARG   A 108 ? 0.1409 0.2311 0.1467 0.0102  0.0011  -0.0104 108 ARG   A CA  
788  C C   . ARG   A 108 ? 0.1404 0.2338 0.1469 0.0083  0.0019  -0.0139 108 ARG   A C   
789  O O   . ARG   A 108 ? 0.1589 0.2549 0.1685 0.0085  0.0020  -0.0163 108 ARG   A O   
790  C CB  . ARG   A 108 ? 0.1471 0.2397 0.1531 0.0128  -0.0006 -0.0087 108 ARG   A CB  
791  C CG  . ARG   A 108 ? 0.1798 0.2693 0.1860 0.0148  -0.0012 -0.0054 108 ARG   A CG  
792  C CD  . ARG   A 108 ? 0.2249 0.3165 0.2311 0.0176  -0.0029 -0.0033 108 ARG   A CD  
793  N NE  . ARG   A 108 ? 0.2809 0.3748 0.2843 0.0169  -0.0032 -0.0032 108 ARG   A NE  
794  C CZ  . ARG   A 108 ? 0.3187 0.4105 0.3192 0.0163  -0.0029 -0.0011 108 ARG   A CZ  
795  N NH1 . ARG   A 108 ? 0.3780 0.4653 0.3776 0.0165  -0.0026 0.0014  108 ARG   A NH1 
796  N NH2 . ARG   A 108 ? 0.2924 0.3867 0.2910 0.0153  -0.0029 -0.0019 108 ARG   A NH2 
797  N N   . ALA   A 109 ? 0.1281 0.2213 0.1321 0.0065  0.0027  -0.0143 109 ALA   A N   
798  C CA  . ALA   A 109 ? 0.1372 0.2328 0.1416 0.0043  0.0039  -0.0176 109 ALA   A CA  
799  C C   . ALA   A 109 ? 0.1424 0.2359 0.1470 0.0022  0.0055  -0.0190 109 ALA   A C   
800  O O   . ALA   A 109 ? 0.1463 0.2427 0.1529 0.0011  0.0062  -0.0220 109 ALA   A O   
801  C CB  . ALA   A 109 ? 0.1437 0.2386 0.1456 0.0027  0.0047  -0.0177 109 ALA   A CB  
802  N N   . LEU   A 110 ? 0.1442 0.2332 0.1467 0.0016  0.0059  -0.0169 110 LEU   A N   
803  C CA  . LEU   A 110 ? 0.1347 0.2222 0.1371 -0.0004 0.0073  -0.0181 110 LEU   A CA  
804  C C   . LEU   A 110 ? 0.1470 0.2368 0.1531 0.0006  0.0070  -0.0197 110 LEU   A C   
805  O O   . LEU   A 110 ? 0.1610 0.2523 0.1682 -0.0011 0.0082  -0.0223 110 LEU   A O   
806  C CB  . LEU   A 110 ? 0.1399 0.2228 0.1392 -0.0010 0.0077  -0.0156 110 LEU   A CB  
807  C CG  . LEU   A 110 ? 0.1489 0.2307 0.1480 -0.0028 0.0089  -0.0166 110 LEU   A CG  
808  C CD1 . LEU   A 110 ? 0.1546 0.2367 0.1522 -0.0055 0.0105  -0.0185 110 LEU   A CD1 
809  C CD2 . LEU   A 110 ? 0.1589 0.2370 0.1556 -0.0027 0.0088  -0.0141 110 LEU   A CD2 
810  N N   . MET   A 111 ? 0.1486 0.2386 0.1567 0.0034  0.0055  -0.0182 111 MET   A N   
811  C CA  . MET   A 111 ? 0.1640 0.2560 0.1762 0.0047  0.0051  -0.0197 111 MET   A CA  
812  C C   . MET   A 111 ? 0.1650 0.2622 0.1801 0.0052  0.0048  -0.0228 111 MET   A C   
813  O O   . MET   A 111 ? 0.1604 0.2598 0.1789 0.0053  0.0050  -0.0253 111 MET   A O   
814  C CB  . MET   A 111 ? 0.1881 0.2782 0.2015 0.0076  0.0037  -0.0169 111 MET   A CB  
815  C CG  . MET   A 111 ? 0.2107 0.2961 0.2217 0.0070  0.0042  -0.0144 111 MET   A CG  
816  S SD  . MET   A 111 ? 0.2789 0.3619 0.2903 0.0100  0.0029  -0.0107 111 MET   A SD  
817  C CE  . MET   A 111 ? 0.2898 0.3730 0.3062 0.0111  0.0031  -0.0124 111 MET   A CE  
818  N N   . ALA   A 112 ? 0.1761 0.2755 0.1899 0.0050  0.0045  -0.0231 112 ALA   A N   
819  C CA  . ALA   A 112 ? 0.1841 0.2890 0.2007 0.0050  0.0044  -0.0265 112 ALA   A CA  
820  C C   . ALA   A 112 ? 0.1999 0.3054 0.2154 0.0013  0.0066  -0.0295 112 ALA   A C   
821  O O   . ALA   A 112 ? 0.2028 0.3127 0.2198 0.0005  0.0070  -0.0326 112 ALA   A O   
822  C CB  . ALA   A 112 ? 0.1778 0.2856 0.1940 0.0068  0.0029  -0.0257 112 ALA   A CB  
823  N N   . GLY   A 113 ? 0.1828 0.2839 0.1954 -0.0011 0.0081  -0.0286 113 GLY   A N   
824  C CA  . GLY   A 113 ? 0.1783 0.2793 0.1894 -0.0047 0.0103  -0.0309 113 GLY   A CA  
825  C C   . GLY   A 113 ? 0.2007 0.3000 0.2085 -0.0065 0.0114  -0.0304 113 GLY   A C   
826  O O   . GLY   A 113 ? 0.2258 0.3244 0.2322 -0.0096 0.0134  -0.0321 113 GLY   A O   
827  N N   . ASN   A 114 ? 0.1847 0.2827 0.1910 -0.0049 0.0102  -0.0279 114 ASN   A N   
828  C CA  . ASN   A 114 ? 0.1839 0.2800 0.1874 -0.0066 0.0112  -0.0276 114 ASN   A CA  
829  C C   . ASN   A 114 ? 0.1977 0.2879 0.1975 -0.0072 0.0116  -0.0242 114 ASN   A C   
830  O O   . ASN   A 114 ? 0.1946 0.2831 0.1934 -0.0052 0.0102  -0.0215 114 ASN   A O   
831  C CB  . ASN   A 114 ? 0.1892 0.2886 0.1938 -0.0049 0.0099  -0.0277 114 ASN   A CB  
832  C CG  . ASN   A 114 ? 0.1876 0.2858 0.1902 -0.0068 0.0113  -0.0283 114 ASN   A CG  
833  O OD1 . ASN   A 114 ? 0.2076 0.3013 0.2075 -0.0090 0.0129  -0.0275 114 ASN   A OD1 
834  N ND2 . ASN   A 114 ? 0.2258 0.3283 0.2298 -0.0060 0.0105  -0.0297 114 ASN   A ND2 
835  N N   . GLU   A 115 ? 0.2038 0.2910 0.2013 -0.0098 0.0134  -0.0244 115 GLU   A N   
836  C CA  . GLU   A 115 ? 0.2082 0.2900 0.2018 -0.0104 0.0138  -0.0215 115 GLU   A CA  
837  C C   . GLU   A 115 ? 0.2083 0.2878 0.1999 -0.0111 0.0145  -0.0207 115 GLU   A C   
838  O O   . GLU   A 115 ? 0.1855 0.2613 0.1747 -0.0103 0.0140  -0.0180 115 GLU   A O   
839  C CB  . GLU   A 115 ? 0.2268 0.3067 0.2185 -0.0130 0.0156  -0.0220 115 GLU   A CB  
840  C CG  . GLU   A 115 ? 0.2428 0.3250 0.2366 -0.0126 0.0153  -0.0232 115 GLU   A CG  
841  C CD  . GLU   A 115 ? 0.2602 0.3410 0.2518 -0.0152 0.0170  -0.0236 115 GLU   A CD  
842  O OE1 . GLU   A 115 ? 0.3032 0.3807 0.2913 -0.0172 0.0184  -0.0226 115 GLU   A OE1 
843  O OE2 . GLU   A 115 ? 0.2651 0.3479 0.2585 -0.0152 0.0169  -0.0248 115 GLU   A OE2 
844  N N   . GLN   A 116 ? 0.1970 0.2789 0.1899 -0.0124 0.0155  -0.0234 116 GLN   A N   
845  C CA  . GLN   A 116 ? 0.2079 0.2872 0.1991 -0.0138 0.0168  -0.0233 116 GLN   A CA  
846  C C   . GLN   A 116 ? 0.1924 0.2717 0.1837 -0.0116 0.0152  -0.0217 116 GLN   A C   
847  O O   . GLN   A 116 ? 0.1999 0.2755 0.1892 -0.0118 0.0157  -0.0201 116 GLN   A O   
848  C CB  . GLN   A 116 ? 0.2379 0.3200 0.2307 -0.0161 0.0187  -0.0271 116 GLN   A CB  
849  C CG  . GLN   A 116 ? 0.2675 0.3461 0.2587 -0.0179 0.0205  -0.0272 116 GLN   A CG  
850  C CD  . GLN   A 116 ? 0.3376 0.4096 0.3250 -0.0197 0.0221  -0.0249 116 GLN   A CD  
851  O OE1 . GLN   A 116 ? 0.3391 0.4104 0.3254 -0.0214 0.0233  -0.0253 116 GLN   A OE1 
852  N NE2 . GLN   A 116 ? 0.3334 0.4007 0.3186 -0.0193 0.0222  -0.0225 116 GLN   A NE2 
853  N N   . VAL   A 117 ? 0.1884 0.2721 0.1820 -0.0093 0.0133  -0.0220 117 VAL   A N   
854  C CA  . VAL   A 117 ? 0.1686 0.2531 0.1623 -0.0075 0.0120  -0.0207 117 VAL   A CA  
855  C C   . VAL   A 117 ? 0.1899 0.2700 0.1812 -0.0061 0.0110  -0.0171 117 VAL   A C   
856  O O   . VAL   A 117 ? 0.1682 0.2468 0.1585 -0.0056 0.0108  -0.0159 117 VAL   A O   
857  C CB  . VAL   A 117 ? 0.1736 0.2640 0.1700 -0.0053 0.0102  -0.0217 117 VAL   A CB  
858  C CG1 . VAL   A 117 ? 0.1737 0.2645 0.1710 -0.0032 0.0086  -0.0200 117 VAL   A CG1 
859  C CG2 . VAL   A 117 ? 0.1763 0.2681 0.1724 -0.0040 0.0092  -0.0209 117 VAL   A CG2 
860  N N   . GLY   A 118 ? 0.1757 0.2544 0.1667 -0.0056 0.0105  -0.0157 118 GLY   A N   
861  C CA  . GLY   A 118 ? 0.1656 0.2405 0.1545 -0.0047 0.0099  -0.0127 118 GLY   A CA  
862  C C   . GLY   A 118 ? 0.1865 0.2570 0.1726 -0.0061 0.0111  -0.0117 118 GLY   A C   
863  O O   . GLY   A 118 ? 0.1612 0.2294 0.1460 -0.0052 0.0105  -0.0099 118 GLY   A O   
864  N N   . PHE   A 119 ? 0.1677 0.2369 0.1530 -0.0083 0.0128  -0.0131 119 PHE   A N   
865  C CA  . PHE   A 119 ? 0.1789 0.2434 0.1614 -0.0097 0.0141  -0.0120 119 PHE   A CA  
866  C C   . PHE   A 119 ? 0.1774 0.2414 0.1603 -0.0095 0.0143  -0.0123 119 PHE   A C   
867  O O   . PHE   A 119 ? 0.1707 0.2314 0.1521 -0.0088 0.0141  -0.0105 119 PHE   A O   
868  C CB  . PHE   A 119 ? 0.1797 0.2431 0.1612 -0.0123 0.0162  -0.0134 119 PHE   A CB  
869  C CG  . PHE   A 119 ? 0.1942 0.2521 0.1726 -0.0136 0.0177  -0.0118 119 PHE   A CG  
870  C CD1 . PHE   A 119 ? 0.1959 0.2502 0.1712 -0.0133 0.0174  -0.0091 119 PHE   A CD1 
871  C CD2 . PHE   A 119 ? 0.1973 0.2537 0.1760 -0.0148 0.0191  -0.0130 119 PHE   A CD2 
872  C CE1 . PHE   A 119 ? 0.2153 0.2644 0.1877 -0.0141 0.0186  -0.0074 119 PHE   A CE1 
873  C CE2 . PHE   A 119 ? 0.2270 0.2778 0.2030 -0.0157 0.0205  -0.0114 119 PHE   A CE2 
874  C CZ  . PHE   A 119 ? 0.2161 0.2632 0.1889 -0.0152 0.0201  -0.0084 119 PHE   A CZ  
875  N N   . ASP   A 120 ? 0.1720 0.2398 0.1573 -0.0100 0.0147  -0.0150 120 ASP   A N   
876  C CA  . ASP   A 120 ? 0.1785 0.2462 0.1644 -0.0103 0.0153  -0.0160 120 ASP   A CA  
877  C C   . ASP   A 120 ? 0.1674 0.2361 0.1536 -0.0080 0.0135  -0.0145 120 ASP   A C   
878  O O   . ASP   A 120 ? 0.1668 0.2335 0.1526 -0.0080 0.0139  -0.0142 120 ASP   A O   
879  C CB  . ASP   A 120 ? 0.1962 0.2686 0.1847 -0.0115 0.0162  -0.0197 120 ASP   A CB  
880  C CG  . ASP   A 120 ? 0.2300 0.3014 0.2184 -0.0144 0.0186  -0.0218 120 ASP   A CG  
881  O OD1 . ASP   A 120 ? 0.2649 0.3310 0.2508 -0.0157 0.0199  -0.0202 120 ASP   A OD1 
882  O OD2 . ASP   A 120 ? 0.2423 0.3184 0.2331 -0.0153 0.0191  -0.0250 120 ASP   A OD2 
883  N N   . LEU   A 121 ? 0.1593 0.2311 0.1463 -0.0062 0.0117  -0.0136 121 LEU   A N   
884  C CA  . LEU   A 121 ? 0.1542 0.2272 0.1413 -0.0042 0.0101  -0.0122 121 LEU   A CA  
885  C C   . LEU   A 121 ? 0.1459 0.2142 0.1309 -0.0037 0.0099  -0.0096 121 LEU   A C   
886  O O   . LEU   A 121 ? 0.1530 0.2207 0.1378 -0.0031 0.0097  -0.0092 121 LEU   A O   
887  C CB  . LEU   A 121 ? 0.1484 0.2251 0.1368 -0.0025 0.0085  -0.0116 121 LEU   A CB  
888  C CG  . LEU   A 121 ? 0.1482 0.2268 0.1366 -0.0006 0.0070  -0.0102 121 LEU   A CG  
889  C CD1 . LEU   A 121 ? 0.1614 0.2447 0.1514 0.0007  0.0058  -0.0106 121 LEU   A CD1 
890  C CD2 . LEU   A 121 ? 0.1495 0.2248 0.1364 0.0004  0.0063  -0.0074 121 LEU   A CD2 
891  N N   . VAL   A 122 ? 0.1336 0.1994 0.1173 -0.0038 0.0099  -0.0082 122 VAL   A N   
892  C CA  . VAL   A 122 ? 0.1430 0.2050 0.1247 -0.0031 0.0095  -0.0059 122 VAL   A CA  
893  C C   . VAL   A 122 ? 0.1631 0.2215 0.1437 -0.0039 0.0107  -0.0059 122 VAL   A C   
894  O O   . VAL   A 122 ? 0.1652 0.2218 0.1452 -0.0030 0.0102  -0.0048 122 VAL   A O   
895  C CB  . VAL   A 122 ? 0.1405 0.2010 0.1209 -0.0033 0.0094  -0.0048 122 VAL   A CB  
896  C CG1 . VAL   A 122 ? 0.1427 0.1997 0.1210 -0.0027 0.0092  -0.0027 122 VAL   A CG1 
897  C CG2 . VAL   A 122 ? 0.1405 0.2040 0.1225 -0.0021 0.0083  -0.0046 122 VAL   A CG2 
898  N N   . LYS   A 123 ? 0.1829 0.2400 0.1632 -0.0058 0.0124  -0.0073 123 LYS   A N   
899  C CA  . LYS   A 123 ? 0.2045 0.2573 0.1837 -0.0067 0.0137  -0.0071 123 LYS   A CA  
900  C C   . LYS   A 123 ? 0.2044 0.2582 0.1854 -0.0062 0.0137  -0.0082 123 LYS   A C   
901  O O   . LYS   A 123 ? 0.2074 0.2578 0.1876 -0.0055 0.0138  -0.0071 123 LYS   A O   
902  C CB  . LYS   A 123 ? 0.2402 0.2919 0.2190 -0.0091 0.0158  -0.0087 123 LYS   A CB  
903  C CG  . LYS   A 123 ? 0.2935 0.3402 0.2713 -0.0102 0.0176  -0.0084 123 LYS   A CG  
904  C CD  . LYS   A 123 ? 0.3524 0.3967 0.3291 -0.0128 0.0199  -0.0093 123 LYS   A CD  
905  C CE  . LYS   A 123 ? 0.4605 0.5000 0.4370 -0.0138 0.0218  -0.0095 123 LYS   A CE  
906  N NZ  . LYS   A 123 ? 0.5516 0.5873 0.5264 -0.0165 0.0243  -0.0098 123 LYS   A NZ  
907  N N   . ALA   A 124 ? 0.1890 0.2474 0.1721 -0.0065 0.0137  -0.0106 124 ALA   A N   
908  C CA  . ALA   A 124 ? 0.1754 0.2357 0.1603 -0.0062 0.0137  -0.0120 124 ALA   A CA  
909  C C   . ALA   A 124 ? 0.1687 0.2289 0.1532 -0.0042 0.0121  -0.0102 124 ALA   A C   
910  O O   . ALA   A 124 ? 0.1685 0.2270 0.1535 -0.0039 0.0124  -0.0104 124 ALA   A O   
911  C CB  . ALA   A 124 ? 0.1671 0.2333 0.1541 -0.0066 0.0136  -0.0146 124 ALA   A CB  
912  N N   . CYS   A 125 ? 0.1496 0.2114 0.1335 -0.0029 0.0105  -0.0085 125 CYS   A N   
913  C CA  . CYS   A 125 ? 0.1446 0.2066 0.1282 -0.0012 0.0092  -0.0069 125 CYS   A CA  
914  C C   . CYS   A 125 ? 0.1576 0.2149 0.1397 -0.0006 0.0092  -0.0051 125 CYS   A C   
915  O O   . CYS   A 125 ? 0.1640 0.2208 0.1464 0.0003  0.0087  -0.0048 125 CYS   A O   
916  C CB  . CYS   A 125 ? 0.1462 0.2109 0.1297 -0.0002 0.0078  -0.0057 125 CYS   A CB  
917  S SG  . CYS   A 125 ? 0.1734 0.2441 0.1585 0.0000  0.0073  -0.0072 125 CYS   A SG  
918  N N   A LYS   A 126 ? 0.1644 0.2186 0.1448 -0.0011 0.0096  -0.0040 126 LYS   A N   
919  N N   B LYS   A 126 ? 0.1575 0.2116 0.1379 -0.0012 0.0096  -0.0040 126 LYS   A N   
920  C CA  A LYS   A 126 ? 0.1859 0.2358 0.1646 -0.0005 0.0096  -0.0022 126 LYS   A CA  
921  C CA  B LYS   A 126 ? 0.1718 0.2216 0.1504 -0.0005 0.0095  -0.0022 126 LYS   A CA  
922  C C   A LYS   A 126 ? 0.1898 0.2366 0.1690 -0.0007 0.0106  -0.0029 126 LYS   A C   
923  C C   B LYS   A 126 ? 0.1814 0.2281 0.1605 -0.0007 0.0106  -0.0028 126 LYS   A C   
924  O O   A LYS   A 126 ? 0.1981 0.2430 0.1772 0.0006  0.0100  -0.0019 126 LYS   A O   
925  O O   B LYS   A 126 ? 0.1885 0.2331 0.1675 0.0006  0.0101  -0.0018 126 LYS   A O   
926  C CB  A LYS   A 126 ? 0.1921 0.2392 0.1686 -0.0014 0.0102  -0.0011 126 LYS   A CB  
927  C CB  B LYS   A 126 ? 0.1670 0.2146 0.1435 -0.0011 0.0099  -0.0009 126 LYS   A CB  
928  C CG  A LYS   A 126 ? 0.2103 0.2524 0.1848 -0.0010 0.0106  0.0007  126 LYS   A CG  
929  C CG  B LYS   A 126 ? 0.1749 0.2180 0.1491 -0.0005 0.0099  0.0012  126 LYS   A CG  
930  C CD  A LYS   A 126 ? 0.2118 0.2539 0.1854 0.0010  0.0089  0.0025  126 LYS   A CD  
931  C CD  B LYS   A 126 ? 0.1703 0.2139 0.1444 0.0016  0.0082  0.0026  126 LYS   A CD  
932  C CE  A LYS   A 126 ? 0.2175 0.2554 0.1892 0.0020  0.0088  0.0044  126 LYS   A CE  
933  C CE  B LYS   A 126 ? 0.1685 0.2081 0.1403 0.0026  0.0080  0.0046  126 LYS   A CE  
934  N NZ  A LYS   A 126 ? 0.2171 0.2559 0.1871 0.0031  0.0074  0.0060  126 LYS   A NZ  
935  N NZ  B LYS   A 126 ? 0.1667 0.2046 0.1358 0.0016  0.0085  0.0058  126 LYS   A NZ  
936  N N   . GLU   A 127 ? 0.1898 0.2364 0.1700 -0.0024 0.0122  -0.0048 127 GLU   A N   
937  C CA  . GLU   A 127 ? 0.2229 0.2661 0.2039 -0.0028 0.0136  -0.0057 127 GLU   A CA  
938  C C   . GLU   A 127 ? 0.2030 0.2484 0.1861 -0.0016 0.0128  -0.0067 127 GLU   A C   
939  O O   . GLU   A 127 ? 0.2097 0.2520 0.1932 -0.0006 0.0130  -0.0063 127 GLU   A O   
940  C CB  . GLU   A 127 ? 0.2580 0.3013 0.2401 -0.0051 0.0157  -0.0081 127 GLU   A CB  
941  C CG  . GLU   A 127 ? 0.3331 0.3725 0.3128 -0.0065 0.0169  -0.0069 127 GLU   A CG  
942  C CD  . GLU   A 127 ? 0.4391 0.4774 0.4197 -0.0091 0.0194  -0.0093 127 GLU   A CD  
943  O OE1 . GLU   A 127 ? 0.6109 0.6481 0.5936 -0.0097 0.0208  -0.0112 127 GLU   A OE1 
944  O OE2 . GLU   A 127 ? 0.5471 0.5855 0.5264 -0.0105 0.0202  -0.0093 127 GLU   A OE2 
945  N N   . ALA   A 128 ? 0.2039 0.2549 0.1884 -0.0015 0.0120  -0.0081 128 ALA   A N   
946  C CA  . ALA   A 128 ? 0.1842 0.2380 0.1704 -0.0006 0.0114  -0.0091 128 ALA   A CA  
947  C C   . ALA   A 128 ? 0.1798 0.2320 0.1652 0.0013  0.0100  -0.0070 128 ALA   A C   
948  O O   . ALA   A 128 ? 0.1913 0.2423 0.1779 0.0022  0.0100  -0.0075 128 ALA   A O   
949  C CB  . ALA   A 128 ? 0.1794 0.2393 0.1665 -0.0008 0.0106  -0.0102 128 ALA   A CB  
950  N N   . CYS   A 129 ? 0.1667 0.2193 0.1503 0.0020  0.0088  -0.0050 129 CYS   A N   
951  C CA  . CYS   A 129 ? 0.1665 0.2183 0.1493 0.0036  0.0075  -0.0032 129 CYS   A CA  
952  C C   . CYS   A 129 ? 0.1777 0.2248 0.1600 0.0045  0.0077  -0.0022 129 CYS   A C   
953  O O   . CYS   A 129 ? 0.1906 0.2375 0.1737 0.0059  0.0070  -0.0021 129 CYS   A O   
954  C CB  . CYS   A 129 ? 0.1802 0.2333 0.1615 0.0038  0.0066  -0.0017 129 CYS   A CB  
955  S SG  . CYS   A 129 ? 0.1816 0.2401 0.1639 0.0036  0.0060  -0.0023 129 CYS   A SG  
956  N N   . ALA   A 130 ? 0.1892 0.2324 0.1699 0.0037  0.0087  -0.0013 130 ALA   A N   
957  C CA  . ALA   A 130 ? 0.1970 0.2353 0.1764 0.0048  0.0087  0.0004  130 ALA   A CA  
958  C C   . ALA   A 130 ? 0.2236 0.2595 0.2051 0.0054  0.0094  -0.0008 130 ALA   A C   
959  O O   . ALA   A 130 ? 0.2293 0.2630 0.2109 0.0073  0.0087  0.0002  130 ALA   A O   
960  C CB  . ALA   A 130 ? 0.2111 0.2458 0.1880 0.0035  0.0098  0.0016  130 ALA   A CB  
961  N N   . ALA   A 131 ? 0.2147 0.2520 0.1983 0.0039  0.0108  -0.0033 131 ALA   A N   
962  C CA  . ALA   A 131 ? 0.2391 0.2749 0.2254 0.0042  0.0117  -0.0051 131 ALA   A CA  
963  C C   . ALA   A 131 ? 0.2373 0.2762 0.2255 0.0058  0.0103  -0.0060 131 ALA   A C   
964  O O   . ALA   A 131 ? 0.2493 0.2864 0.2397 0.0067  0.0108  -0.0070 131 ALA   A O   
965  C CB  . ALA   A 131 ? 0.2647 0.3024 0.2529 0.0020  0.0135  -0.0081 131 ALA   A CB  
966  N N   . ALA   A 132 ? 0.2110 0.2545 0.1987 0.0062  0.0089  -0.0056 132 ALA   A N   
967  C CA  . ALA   A 132 ? 0.2163 0.2630 0.2055 0.0075  0.0077  -0.0063 132 ALA   A CA  
968  C C   . ALA   A 132 ? 0.2007 0.2471 0.1884 0.0093  0.0061  -0.0041 132 ALA   A C   
969  O O   . ALA   A 132 ? 0.2154 0.2651 0.2041 0.0101  0.0051  -0.0047 132 ALA   A O   
970  C CB  . ALA   A 132 ? 0.2259 0.2785 0.2157 0.0064  0.0076  -0.0078 132 ALA   A CB  
971  N N   . ASN   A 133 ? 0.1984 0.2412 0.1836 0.0098  0.0058  -0.0017 133 ASN   A N   
972  C CA  . ASN   A 133 ? 0.2163 0.2593 0.2000 0.0114  0.0042  0.0002  133 ASN   A CA  
973  C C   . ASN   A 133 ? 0.2078 0.2556 0.1912 0.0109  0.0034  0.0000  133 ASN   A C   
974  O O   . ASN   A 133 ? 0.1918 0.2419 0.1756 0.0120  0.0023  0.0001  133 ASN   A O   
975  C CB  . ASN   A 133 ? 0.2653 0.3073 0.2504 0.0137  0.0033  0.0001  133 ASN   A CB  
976  C CG  . ASN   A 133 ? 0.3383 0.3747 0.3236 0.0145  0.0041  0.0008  133 ASN   A CG  
977  O OD1 . ASN   A 133 ? 0.4611 0.4967 0.4492 0.0150  0.0047  -0.0010 133 ASN   A OD1 
978  N ND2 . ASN   A 133 ? 0.3754 0.4077 0.3577 0.0146  0.0042  0.0032  133 ASN   A ND2 
979  N N   . VAL   A 134 ? 0.1675 0.2170 0.1505 0.0092  0.0041  -0.0004 134 VAL   A N   
980  C CA  . VAL   A 134 ? 0.1716 0.2249 0.1543 0.0086  0.0036  -0.0003 134 VAL   A CA  
981  C C   . VAL   A 134 ? 0.1902 0.2422 0.1708 0.0080  0.0036  0.0012  134 VAL   A C   
982  O O   . VAL   A 134 ? 0.1806 0.2301 0.1602 0.0071  0.0045  0.0015  134 VAL   A O   
983  C CB  . VAL   A 134 ? 0.1674 0.2237 0.1514 0.0073  0.0043  -0.0020 134 VAL   A CB  
984  C CG1 . VAL   A 134 ? 0.1603 0.2195 0.1437 0.0066  0.0040  -0.0015 134 VAL   A CG1 
985  C CG2 . VAL   A 134 ? 0.1768 0.2351 0.1628 0.0077  0.0043  -0.0037 134 VAL   A CG2 
986  N N   . LEU   A 135 ? 0.1921 0.2459 0.1721 0.0083  0.0028  0.0020  135 LEU   A N   
987  C CA  . LEU   A 135 ? 0.2008 0.2540 0.1790 0.0077  0.0028  0.0031  135 LEU   A CA  
988  C C   . LEU   A 135 ? 0.1819 0.2371 0.1607 0.0064  0.0034  0.0024  135 LEU   A C   
989  O O   . LEU   A 135 ? 0.1913 0.2491 0.1714 0.0063  0.0032  0.0017  135 LEU   A O   
990  C CB  . LEU   A 135 ? 0.2514 0.3059 0.2292 0.0084  0.0018  0.0037  135 LEU   A CB  
991  C CG  . LEU   A 135 ? 0.2976 0.3508 0.2746 0.0100  0.0010  0.0045  135 LEU   A CG  
992  C CD1 . LEU   A 135 ? 0.3085 0.3640 0.2850 0.0101  0.0003  0.0048  135 LEU   A CD1 
993  C CD2 . LEU   A 135 ? 0.3150 0.3642 0.2901 0.0102  0.0013  0.0058  135 LEU   A CD2 
994  N N   . LEU   A 136 ? 0.1694 0.2235 0.1472 0.0054  0.0039  0.0028  136 LEU   A N   
995  C CA  . LEU   A 136 ? 0.1568 0.2128 0.1352 0.0045  0.0043  0.0022  136 LEU   A CA  
996  C C   . LEU   A 136 ? 0.1472 0.2039 0.1251 0.0043  0.0040  0.0028  136 LEU   A C   
997  O O   . LEU   A 136 ? 0.1674 0.2226 0.1439 0.0039  0.0042  0.0033  136 LEU   A O   
998  C CB  . LEU   A 136 ? 0.1522 0.2073 0.1305 0.0033  0.0053  0.0013  136 LEU   A CB  
999  C CG  . LEU   A 136 ? 0.1590 0.2168 0.1383 0.0026  0.0055  0.0005  136 LEU   A CG  
1000 C CD1 . LEU   A 136 ? 0.1567 0.2176 0.1376 0.0029  0.0053  -0.0004 136 LEU   A CD1 
1001 C CD2 . LEU   A 136 ? 0.1799 0.2365 0.1589 0.0012  0.0067  -0.0004 136 LEU   A CD2 
1002 N N   . LYS   A 137 ? 0.1443 0.2034 0.1235 0.0045  0.0037  0.0027  137 LYS   A N   
1003 C CA  . LYS   A 137 ? 0.1417 0.2016 0.1212 0.0042  0.0037  0.0029  137 LYS   A CA  
1004 C C   . LYS   A 137 ? 0.1422 0.2032 0.1227 0.0036  0.0041  0.0023  137 LYS   A C   
1005 O O   . LYS   A 137 ? 0.1369 0.1992 0.1181 0.0037  0.0041  0.0019  137 LYS   A O   
1006 C CB  . LYS   A 137 ? 0.1412 0.2025 0.1217 0.0047  0.0033  0.0032  137 LYS   A CB  
1007 C CG  . LYS   A 137 ? 0.1465 0.2078 0.1267 0.0054  0.0028  0.0034  137 LYS   A CG  
1008 C CD  . LYS   A 137 ? 0.1587 0.2213 0.1399 0.0055  0.0027  0.0033  137 LYS   A CD  
1009 C CE  . LYS   A 137 ? 0.1538 0.2173 0.1352 0.0062  0.0022  0.0031  137 LYS   A CE  
1010 N NZ  . LYS   A 137 ? 0.1488 0.2132 0.1310 0.0062  0.0024  0.0030  137 LYS   A NZ  
1011 N N   . VAL   A 138 ? 0.1329 0.1940 0.1135 0.0030  0.0044  0.0020  138 VAL   A N   
1012 C CA  . VAL   A 138 ? 0.1281 0.1905 0.1099 0.0026  0.0047  0.0011  138 VAL   A CA  
1013 C C   . VAL   A 138 ? 0.1328 0.1962 0.1162 0.0029  0.0045  0.0012  138 VAL   A C   
1014 O O   . VAL   A 138 ? 0.1317 0.1947 0.1150 0.0025  0.0048  0.0010  138 VAL   A O   
1015 C CB  . VAL   A 138 ? 0.1221 0.1838 0.1031 0.0013  0.0055  0.0002  138 VAL   A CB  
1016 C CG1 . VAL   A 138 ? 0.1234 0.1873 0.1063 0.0011  0.0057  -0.0010 138 VAL   A CG1 
1017 C CG2 . VAL   A 138 ? 0.1290 0.1890 0.1087 0.0009  0.0060  0.0001  138 VAL   A CG2 
1018 N N   . ILE   A 139 ? 0.1341 0.1990 0.1189 0.0037  0.0042  0.0015  139 ILE   A N   
1019 C CA  . ILE   A 139 ? 0.1407 0.2061 0.1273 0.0042  0.0041  0.0017  139 ILE   A CA  
1020 C C   . ILE   A 139 ? 0.1534 0.2200 0.1415 0.0040  0.0043  0.0006  139 ILE   A C   
1021 O O   . ILE   A 139 ? 0.1471 0.2153 0.1357 0.0044  0.0040  0.0002  139 ILE   A O   
1022 C CB  . ILE   A 139 ? 0.1470 0.2131 0.1342 0.0053  0.0036  0.0030  139 ILE   A CB  
1023 C CG1 . ILE   A 139 ? 0.1611 0.2266 0.1470 0.0054  0.0035  0.0038  139 ILE   A CG1 
1024 C CG2 . ILE   A 139 ? 0.1520 0.2180 0.1412 0.0060  0.0037  0.0035  139 ILE   A CG2 
1025 C CD1 . ILE   A 139 ? 0.1584 0.2252 0.1442 0.0061  0.0032  0.0048  139 ILE   A CD1 
1026 N N   . ILE   A 140 ? 0.1446 0.2110 0.1336 0.0035  0.0048  -0.0003 140 ILE   A N   
1027 C CA  . ILE   A 140 ? 0.1406 0.2083 0.1312 0.0031  0.0050  -0.0018 140 ILE   A CA  
1028 C C   . ILE   A 140 ? 0.1336 0.2021 0.1271 0.0044  0.0047  -0.0017 140 ILE   A C   
1029 O O   . ILE   A 140 ? 0.1395 0.2097 0.1349 0.0046  0.0047  -0.0030 140 ILE   A O   
1030 C CB  . ILE   A 140 ? 0.1388 0.2062 0.1289 0.0016  0.0058  -0.0030 140 ILE   A CB  
1031 C CG1 . ILE   A 140 ? 0.1390 0.2059 0.1299 0.0015  0.0061  -0.0031 140 ILE   A CG1 
1032 C CG2 . ILE   A 140 ? 0.1413 0.2075 0.1283 0.0006  0.0062  -0.0028 140 ILE   A CG2 
1033 C CD1 . ILE   A 140 ? 0.1591 0.2266 0.1496 -0.0001 0.0069  -0.0047 140 ILE   A CD1 
1034 N N   . GLU   A 141 ? 0.1313 0.1987 0.1255 0.0053  0.0046  -0.0003 141 GLU   A N   
1035 C CA  . GLU   A 141 ? 0.1374 0.2046 0.1342 0.0066  0.0044  0.0002  141 GLU   A CA  
1036 C C   . GLU   A 141 ? 0.1410 0.2086 0.1405 0.0062  0.0050  -0.0016 141 GLU   A C   
1037 O O   . GLU   A 141 ? 0.1488 0.2176 0.1507 0.0071  0.0048  -0.0024 141 GLU   A O   
1038 C CB  . GLU   A 141 ? 0.1370 0.2058 0.1342 0.0082  0.0035  0.0010  141 GLU   A CB  
1039 C CG  . GLU   A 141 ? 0.1414 0.2091 0.1401 0.0099  0.0032  0.0029  141 GLU   A CG  
1040 C CD  . GLU   A 141 ? 0.1484 0.2146 0.1451 0.0098  0.0033  0.0050  141 GLU   A CD  
1041 O OE1 . GLU   A 141 ? 0.1600 0.2271 0.1555 0.0109  0.0025  0.0065  141 GLU   A OE1 
1042 O OE2 . GLU   A 141 ? 0.1345 0.1988 0.1310 0.0088  0.0040  0.0049  141 GLU   A OE2 
1043 N N   . THR   A 142 ? 0.1537 0.2202 0.1531 0.0050  0.0058  -0.0022 142 THR   A N   
1044 C CA  . THR   A 142 ? 0.1617 0.2287 0.1635 0.0043  0.0066  -0.0043 142 THR   A CA  
1045 C C   . THR   A 142 ? 0.1614 0.2279 0.1670 0.0057  0.0066  -0.0043 142 THR   A C   
1046 O O   . THR   A 142 ? 0.1565 0.2243 0.1649 0.0057  0.0070  -0.0062 142 THR   A O   
1047 C CB  . THR   A 142 ? 0.1552 0.2216 0.1563 0.0030  0.0073  -0.0048 142 THR   A CB  
1048 O OG1 . THR   A 142 ? 0.1623 0.2270 0.1637 0.0037  0.0073  -0.0032 142 THR   A OG1 
1049 C CG2 . THR   A 142 ? 0.1661 0.2331 0.1636 0.0018  0.0072  -0.0048 142 THR   A CG2 
1050 N N   . GLY   A 143 ? 0.1767 0.2414 0.1825 0.0071  0.0063  -0.0021 143 GLY   A N   
1051 C CA  . GLY   A 143 ? 0.1926 0.2561 0.2019 0.0086  0.0065  -0.0016 143 GLY   A CA  
1052 C C   . GLY   A 143 ? 0.1842 0.2493 0.1950 0.0104  0.0055  -0.0016 143 GLY   A C   
1053 O O   . GLY   A 143 ? 0.2077 0.2721 0.2219 0.0118  0.0055  -0.0018 143 GLY   A O   
1054 N N   . GLU   A 144 ? 0.1687 0.2360 0.1772 0.0104  0.0046  -0.0016 144 GLU   A N   
1055 C CA  . GLU   A 144 ? 0.1709 0.2408 0.1809 0.0118  0.0037  -0.0023 144 GLU   A CA  
1056 C C   . GLU   A 144 ? 0.1809 0.2534 0.1922 0.0103  0.0042  -0.0056 144 GLU   A C   
1057 O O   . GLU   A 144 ? 0.1899 0.2643 0.2043 0.0113  0.0039  -0.0073 144 GLU   A O   
1058 C CB  . GLU   A 144 ? 0.1782 0.2497 0.1855 0.0126  0.0026  -0.0007 144 GLU   A CB  
1059 C CG  . GLU   A 144 ? 0.1887 0.2583 0.1950 0.0143  0.0020  0.0025  144 GLU   A CG  
1060 C CD  . GLU   A 144 ? 0.2142 0.2832 0.2237 0.0167  0.0015  0.0035  144 GLU   A CD  
1061 O OE1 . GLU   A 144 ? 0.2402 0.3120 0.2519 0.0180  0.0007  0.0022  144 GLU   A OE1 
1062 O OE2 . GLU   A 144 ? 0.2413 0.3070 0.2513 0.0174  0.0019  0.0055  144 GLU   A OE2 
1063 N N   . LEU   A 145 ? 0.1687 0.2412 0.1775 0.0080  0.0050  -0.0066 145 LEU   A N   
1064 C CA  . LEU   A 145 ? 0.1714 0.2460 0.1808 0.0063  0.0057  -0.0096 145 LEU   A CA  
1065 C C   . LEU   A 145 ? 0.1733 0.2480 0.1864 0.0061  0.0065  -0.0115 145 LEU   A C   
1066 O O   . LEU   A 145 ? 0.1765 0.2537 0.1920 0.0058  0.0068  -0.0141 145 LEU   A O   
1067 C CB  . LEU   A 145 ? 0.1655 0.2394 0.1711 0.0040  0.0064  -0.0096 145 LEU   A CB  
1068 C CG  . LEU   A 145 ? 0.1649 0.2388 0.1671 0.0038  0.0059  -0.0084 145 LEU   A CG  
1069 C CD1 . LEU   A 145 ? 0.1726 0.2451 0.1713 0.0021  0.0065  -0.0080 145 LEU   A CD1 
1070 C CD2 . LEU   A 145 ? 0.1747 0.2515 0.1777 0.0037  0.0058  -0.0101 145 LEU   A CD2 
1071 N N   . LYS   A 146 ? 0.1999 0.2723 0.2132 0.0059  0.0071  -0.0108 146 LYS   A N   
1072 C CA  . LYS   A 146 ? 0.2357 0.3078 0.2529 0.0057  0.0080  -0.0126 146 LYS   A CA  
1073 C C   . LYS   A 146 ? 0.2277 0.3021 0.2453 0.0033  0.0091  -0.0157 146 LYS   A C   
1074 O O   . LYS   A 146 ? 0.2379 0.3118 0.2558 0.0021  0.0101  -0.0166 146 LYS   A O   
1075 C CB  . LYS   A 146 ? 0.2912 0.3633 0.3129 0.0081  0.0075  -0.0128 146 LYS   A CB  
1076 C CG  . LYS   A 146 ? 0.3233 0.3926 0.3448 0.0104  0.0067  -0.0094 146 LYS   A CG  
1077 C CD  . LYS   A 146 ? 0.4071 0.4766 0.4326 0.0131  0.0059  -0.0091 146 LYS   A CD  
1078 C CE  . LYS   A 146 ? 0.4462 0.5135 0.4705 0.0155  0.0049  -0.0054 146 LYS   A CE  
1079 N NZ  . LYS   A 146 ? 0.4954 0.5584 0.5202 0.0156  0.0058  -0.0035 146 LYS   A NZ  
1080 N N   . ASP   A 147 ? 0.2182 0.2952 0.2356 0.0027  0.0091  -0.0174 147 ASP   A N   
1081 C CA  . ASP   A 147 ? 0.2514 0.3309 0.2690 0.0003  0.0102  -0.0205 147 ASP   A CA  
1082 C C   . ASP   A 147 ? 0.1973 0.2764 0.2100 -0.0019 0.0107  -0.0198 147 ASP   A C   
1083 O O   . ASP   A 147 ? 0.1793 0.2574 0.1884 -0.0019 0.0102  -0.0178 147 ASP   A O   
1084 C CB  . ASP   A 147 ? 0.3106 0.3929 0.3289 0.0001  0.0101  -0.0223 147 ASP   A CB  
1085 C CG  . ASP   A 147 ? 0.4120 0.4972 0.4305 -0.0025 0.0115  -0.0256 147 ASP   A CG  
1086 O OD1 . ASP   A 147 ? 0.5020 0.5890 0.5248 -0.0026 0.0121  -0.0283 147 ASP   A OD1 
1087 O OD2 . ASP   A 147 ? 0.5253 0.6106 0.5395 -0.0045 0.0120  -0.0252 147 ASP   A OD2 
1088 N N   . GLU   A 148 ? 0.2044 0.2847 0.2172 -0.0037 0.0118  -0.0217 148 GLU   A N   
1089 C CA  . GLU   A 148 ? 0.2061 0.2863 0.2143 -0.0056 0.0122  -0.0209 148 GLU   A CA  
1090 C C   . GLU   A 148 ? 0.1889 0.2695 0.1933 -0.0068 0.0122  -0.0204 148 GLU   A C   
1091 O O   . GLU   A 148 ? 0.1816 0.2605 0.1818 -0.0070 0.0119  -0.0182 148 GLU   A O   
1092 C CB  . GLU   A 148 ? 0.2441 0.3266 0.2532 -0.0074 0.0133  -0.0234 148 GLU   A CB  
1093 C CG  . GLU   A 148 ? 0.2778 0.3605 0.2816 -0.0091 0.0135  -0.0223 148 GLU   A CG  
1094 C CD  . GLU   A 148 ? 0.3365 0.4220 0.3404 -0.0109 0.0144  -0.0245 148 GLU   A CD  
1095 O OE1 . GLU   A 148 ? 0.3011 0.3880 0.3096 -0.0108 0.0151  -0.0269 148 GLU   A OE1 
1096 O OE2 . GLU   A 148 ? 0.3371 0.4234 0.3364 -0.0123 0.0145  -0.0237 148 GLU   A OE2 
1097 N N   . ALA   A 149 ? 0.1877 0.2707 0.1936 -0.0077 0.0129  -0.0228 149 ALA   A N   
1098 C CA  . ALA   A 149 ? 0.2027 0.2858 0.2052 -0.0092 0.0133  -0.0227 149 ALA   A CA  
1099 C C   . ALA   A 149 ? 0.1882 0.2692 0.1892 -0.0077 0.0123  -0.0202 149 ALA   A C   
1100 O O   . ALA   A 149 ? 0.1876 0.2672 0.1845 -0.0087 0.0125  -0.0189 149 ALA   A O   
1101 C CB  . ALA   A 149 ? 0.2071 0.2936 0.2123 -0.0103 0.0143  -0.0260 149 ALA   A CB  
1102 N N   . LEU   A 150 ? 0.1902 0.2710 0.1942 -0.0052 0.0112  -0.0196 150 LEU   A N   
1103 C CA  . LEU   A 150 ? 0.1944 0.2738 0.1971 -0.0038 0.0102  -0.0175 150 LEU   A CA  
1104 C C   . LEU   A 150 ? 0.1692 0.2456 0.1685 -0.0035 0.0097  -0.0145 150 LEU   A C   
1105 O O   . LEU   A 150 ? 0.1650 0.2401 0.1614 -0.0036 0.0095  -0.0131 150 LEU   A O   
1106 C CB  . LEU   A 150 ? 0.1886 0.2689 0.1950 -0.0013 0.0091  -0.0174 150 LEU   A CB  
1107 C CG  . LEU   A 150 ? 0.2241 0.3078 0.2338 -0.0011 0.0092  -0.0202 150 LEU   A CG  
1108 C CD1 . LEU   A 150 ? 0.2322 0.3169 0.2461 0.0018  0.0080  -0.0200 150 LEU   A CD1 
1109 C CD2 . LEU   A 150 ? 0.2473 0.3321 0.2548 -0.0020 0.0093  -0.0204 150 LEU   A CD2 
1110 N N   . ILE   A 151 ? 0.1747 0.2501 0.1745 -0.0031 0.0096  -0.0139 151 ILE   A N   
1111 C CA  . ILE   A 151 ? 0.1610 0.2341 0.1578 -0.0029 0.0092  -0.0116 151 ILE   A CA  
1112 C C   . ILE   A 151 ? 0.1571 0.2297 0.1498 -0.0046 0.0097  -0.0112 151 ILE   A C   
1113 O O   . ILE   A 151 ? 0.1668 0.2375 0.1566 -0.0043 0.0092  -0.0092 151 ILE   A O   
1114 C CB  . ILE   A 151 ? 0.1665 0.2393 0.1652 -0.0024 0.0092  -0.0117 151 ILE   A CB  
1115 C CG1 . ILE   A 151 ? 0.1779 0.2502 0.1803 -0.0005 0.0087  -0.0112 151 ILE   A CG1 
1116 C CG2 . ILE   A 151 ? 0.1654 0.2368 0.1612 -0.0025 0.0089  -0.0098 151 ILE   A CG2 
1117 C CD1 . ILE   A 151 ? 0.1930 0.2649 0.1982 -0.0003 0.0092  -0.0119 151 ILE   A CD1 
1118 N N   . ARG   A 152 ? 0.1606 0.2348 0.1528 -0.0065 0.0107  -0.0130 152 ARG   A N   
1119 C CA  . ARG   A 152 ? 0.1738 0.2471 0.1616 -0.0082 0.0113  -0.0123 152 ARG   A CA  
1120 C C   . ARG   A 152 ? 0.1778 0.2499 0.1637 -0.0086 0.0116  -0.0117 152 ARG   A C   
1121 O O   . ARG   A 152 ? 0.1730 0.2427 0.1553 -0.0089 0.0116  -0.0098 152 ARG   A O   
1122 C CB  . ARG   A 152 ? 0.1878 0.2634 0.1750 -0.0103 0.0125  -0.0143 152 ARG   A CB  
1123 C CG  . ARG   A 152 ? 0.2037 0.2810 0.1922 -0.0103 0.0125  -0.0152 152 ARG   A CG  
1124 C CD  . ARG   A 152 ? 0.2350 0.3147 0.2217 -0.0128 0.0137  -0.0169 152 ARG   A CD  
1125 N NE  . ARG   A 152 ? 0.2641 0.3461 0.2530 -0.0128 0.0137  -0.0184 152 ARG   A NE  
1126 C CZ  . ARG   A 152 ? 0.3109 0.3931 0.2979 -0.0125 0.0132  -0.0173 152 ARG   A CZ  
1127 N NH1 . ARG   A 152 ? 0.3151 0.3953 0.2974 -0.0122 0.0125  -0.0145 152 ARG   A NH1 
1128 N NH2 . ARG   A 152 ? 0.3032 0.3875 0.2931 -0.0125 0.0134  -0.0191 152 ARG   A NH2 
1129 N N   . LYS   A 153 ? 0.1782 0.2518 0.1668 -0.0086 0.0119  -0.0135 153 LYS   A N   
1130 C CA  . LYS   A 153 ? 0.1813 0.2544 0.1686 -0.0094 0.0124  -0.0136 153 LYS   A CA  
1131 C C   . LYS   A 153 ? 0.1767 0.2476 0.1631 -0.0078 0.0114  -0.0114 153 LYS   A C   
1132 O O   . LYS   A 153 ? 0.1790 0.2479 0.1627 -0.0085 0.0118  -0.0105 153 LYS   A O   
1133 C CB  . LYS   A 153 ? 0.2042 0.2804 0.1951 -0.0097 0.0128  -0.0164 153 LYS   A CB  
1134 C CG  . LYS   A 153 ? 0.2421 0.3184 0.2321 -0.0108 0.0136  -0.0172 153 LYS   A CG  
1135 C CD  . LYS   A 153 ? 0.3004 0.3747 0.2864 -0.0134 0.0153  -0.0170 153 LYS   A CD  
1136 C CE  . LYS   A 153 ? 0.3276 0.4039 0.3136 -0.0156 0.0166  -0.0191 153 LYS   A CE  
1137 N NZ  . LYS   A 153 ? 0.3557 0.4295 0.3372 -0.0181 0.0182  -0.0183 153 LYS   A NZ  
1138 N N   . ALA   A 154 ? 0.1649 0.2363 0.1536 -0.0057 0.0101  -0.0107 154 ALA   A N   
1139 C CA  . ALA   A 154 ? 0.1669 0.2368 0.1549 -0.0042 0.0092  -0.0088 154 ALA   A CA  
1140 C C   . ALA   A 154 ? 0.1480 0.2151 0.1325 -0.0044 0.0091  -0.0068 154 ALA   A C   
1141 O O   . ALA   A 154 ? 0.1442 0.2097 0.1271 -0.0042 0.0090  -0.0057 154 ALA   A O   
1142 C CB  . ALA   A 154 ? 0.1570 0.2278 0.1477 -0.0021 0.0081  -0.0083 154 ALA   A CB  
1143 N N   . SER   A 155 ? 0.1468 0.2137 0.1306 -0.0046 0.0091  -0.0064 155 SER   A N   
1144 C CA  . SER   A 155 ? 0.1431 0.2080 0.1239 -0.0046 0.0088  -0.0046 155 SER   A CA  
1145 C C   . SER   A 155 ? 0.1549 0.2179 0.1324 -0.0060 0.0097  -0.0042 155 SER   A C   
1146 O O   . SER   A 155 ? 0.1628 0.2234 0.1382 -0.0055 0.0095  -0.0026 155 SER   A O   
1147 C CB  . SER   A 155 ? 0.1394 0.2053 0.1203 -0.0047 0.0087  -0.0048 155 SER   A CB  
1148 O OG  . SER   A 155 ? 0.1374 0.2045 0.1215 -0.0036 0.0082  -0.0053 155 SER   A OG  
1149 N N   . GLU   A 156 ? 0.1483 0.2123 0.1256 -0.0078 0.0109  -0.0057 156 GLU   A N   
1150 C CA  . GLU   A 156 ? 0.1825 0.2446 0.1565 -0.0095 0.0121  -0.0053 156 GLU   A CA  
1151 C C   . GLU   A 156 ? 0.1687 0.2288 0.1425 -0.0096 0.0125  -0.0051 156 GLU   A C   
1152 O O   . GLU   A 156 ? 0.1778 0.2347 0.1488 -0.0099 0.0130  -0.0036 156 GLU   A O   
1153 C CB  . GLU   A 156 ? 0.2191 0.2832 0.1933 -0.0117 0.0135  -0.0075 156 GLU   A CB  
1154 C CG  . GLU   A 156 ? 0.2906 0.3525 0.2613 -0.0139 0.0151  -0.0071 156 GLU   A CG  
1155 C CD  . GLU   A 156 ? 0.3994 0.4638 0.3706 -0.0163 0.0167  -0.0096 156 GLU   A CD  
1156 O OE1 . GLU   A 156 ? 0.4077 0.4752 0.3829 -0.0161 0.0166  -0.0121 156 GLU   A OE1 
1157 O OE2 . GLU   A 156 ? 0.4235 0.4868 0.3911 -0.0182 0.0179  -0.0090 156 GLU   A OE2 
1158 N N   . ILE   A 157 ? 0.1675 0.2298 0.1446 -0.0092 0.0124  -0.0069 157 ILE   A N   
1159 C CA  . ILE   A 157 ? 0.1671 0.2286 0.1445 -0.0093 0.0128  -0.0073 157 ILE   A CA  
1160 C C   . ILE   A 157 ? 0.1547 0.2140 0.1313 -0.0076 0.0118  -0.0052 157 ILE   A C   
1161 O O   . ILE   A 157 ? 0.1639 0.2206 0.1389 -0.0082 0.0125  -0.0046 157 ILE   A O   
1162 C CB  . ILE   A 157 ? 0.1647 0.2300 0.1459 -0.0089 0.0126  -0.0095 157 ILE   A CB  
1163 C CG1 . ILE   A 157 ? 0.1814 0.2491 0.1638 -0.0107 0.0137  -0.0120 157 ILE   A CG1 
1164 C CG2 . ILE   A 157 ? 0.1592 0.2245 0.1411 -0.0088 0.0128  -0.0101 157 ILE   A CG2 
1165 C CD1 . ILE   A 157 ? 0.1852 0.2571 0.1717 -0.0096 0.0130  -0.0141 157 ILE   A CD1 
1166 N N   . SER   A 158 ? 0.1484 0.2086 0.1260 -0.0058 0.0103  -0.0042 158 SER   A N   
1167 C CA  . SER   A 158 ? 0.1597 0.2183 0.1367 -0.0043 0.0094  -0.0026 158 SER   A CA  
1168 C C   . SER   A 158 ? 0.1680 0.2232 0.1417 -0.0045 0.0097  -0.0008 158 SER   A C   
1169 O O   . SER   A 158 ? 0.1652 0.2182 0.1382 -0.0042 0.0098  -0.0002 158 SER   A O   
1170 C CB  . SER   A 158 ? 0.1577 0.2180 0.1363 -0.0027 0.0081  -0.0020 158 SER   A CB  
1171 O OG  . SER   A 158 ? 0.1610 0.2240 0.1424 -0.0022 0.0078  -0.0032 158 SER   A OG  
1172 N N   . ILE   A 159 ? 0.1727 0.2275 0.1446 -0.0051 0.0099  -0.0002 159 ILE   A N   
1173 C CA  . ILE   A 159 ? 0.1733 0.2251 0.1418 -0.0051 0.0099  0.0017  159 ILE   A CA  
1174 C C   . ILE   A 159 ? 0.1866 0.2352 0.1532 -0.0065 0.0114  0.0019  159 ILE   A C   
1175 O O   . ILE   A 159 ? 0.1827 0.2280 0.1477 -0.0059 0.0114  0.0034  159 ILE   A O   
1176 C CB  . ILE   A 159 ? 0.2004 0.2535 0.1673 -0.0056 0.0098  0.0020  159 ILE   A CB  
1177 C CG1 . ILE   A 159 ? 0.2161 0.2717 0.1848 -0.0041 0.0084  0.0019  159 ILE   A CG1 
1178 C CG2 . ILE   A 159 ? 0.2145 0.2645 0.1771 -0.0060 0.0102  0.0040  159 ILE   A CG2 
1179 C CD1 . ILE   A 159 ? 0.2183 0.2763 0.1866 -0.0048 0.0084  0.0013  159 ILE   A CD1 
1180 N N   . LYS   A 160 ? 0.1904 0.2399 0.1574 -0.0085 0.0128  0.0002  160 LYS   A N   
1181 C CA  . LYS   A 160 ? 0.2143 0.2608 0.1797 -0.0102 0.0146  0.0001  160 LYS   A CA  
1182 C C   . LYS   A 160 ? 0.2111 0.2562 0.1782 -0.0096 0.0148  -0.0003 160 LYS   A C   
1183 O O   . LYS   A 160 ? 0.2004 0.2415 0.1659 -0.0103 0.0159  0.0005  160 LYS   A O   
1184 C CB  . LYS   A 160 ? 0.2371 0.2857 0.2034 -0.0126 0.0162  -0.0023 160 LYS   A CB  
1185 C CG  . LYS   A 160 ? 0.3009 0.3500 0.2648 -0.0140 0.0168  -0.0020 160 LYS   A CG  
1186 C CD  . LYS   A 160 ? 0.3584 0.4101 0.3239 -0.0164 0.0184  -0.0049 160 LYS   A CD  
1187 C CE  . LYS   A 160 ? 0.4321 0.4848 0.3953 -0.0181 0.0193  -0.0050 160 LYS   A CE  
1188 N NZ  . LYS   A 160 ? 0.4696 0.5253 0.4347 -0.0203 0.0208  -0.0082 160 LYS   A NZ  
1189 N N   . ALA   A 161 ? 0.1951 0.2433 0.1653 -0.0085 0.0137  -0.0016 161 ALA   A N   
1190 C CA  . ALA   A 161 ? 0.2038 0.2518 0.1758 -0.0080 0.0138  -0.0024 161 ALA   A CA  
1191 C C   . ALA   A 161 ? 0.1985 0.2441 0.1698 -0.0061 0.0128  -0.0005 161 ALA   A C   
1192 O O   . ALA   A 161 ? 0.1849 0.2302 0.1576 -0.0057 0.0129  -0.0012 161 ALA   A O   
1193 C CB  . ALA   A 161 ? 0.2021 0.2548 0.1774 -0.0075 0.0131  -0.0044 161 ALA   A CB  
1194 N N   . GLY   A 162 ? 0.1865 0.2313 0.1561 -0.0049 0.0116  0.0015  162 GLY   A N   
1195 C CA  . GLY   A 162 ? 0.1873 0.2300 0.1561 -0.0030 0.0106  0.0032  162 GLY   A CA  
1196 C C   . GLY   A 162 ? 0.1725 0.2183 0.1429 -0.0012 0.0088  0.0034  162 GLY   A C   
1197 O O   . GLY   A 162 ? 0.1842 0.2291 0.1548 0.0003  0.0080  0.0041  162 GLY   A O   
1198 N N   . ALA   A 163 ? 0.1633 0.2124 0.1349 -0.0013 0.0083  0.0027  163 ALA   A N   
1199 C CA  . ALA   A 163 ? 0.1505 0.2018 0.1233 0.0002  0.0069  0.0030  163 ALA   A CA  
1200 C C   . ALA   A 163 ? 0.1553 0.2053 0.1264 0.0014  0.0060  0.0046  163 ALA   A C   
1201 O O   . ALA   A 163 ? 0.1509 0.1996 0.1198 0.0010  0.0062  0.0055  163 ALA   A O   
1202 C CB  . ALA   A 163 ? 0.1436 0.1978 0.1177 -0.0001 0.0067  0.0022  163 ALA   A CB  
1203 N N   . ASP   A 164 ? 0.1568 0.2075 0.1291 0.0028  0.0050  0.0048  164 ASP   A N   
1204 C CA  . ASP   A 164 ? 0.1626 0.2131 0.1338 0.0042  0.0040  0.0059  164 ASP   A CA  
1205 C C   . ASP   A 164 ? 0.1571 0.2107 0.1291 0.0043  0.0034  0.0055  164 ASP   A C   
1206 O O   . ASP   A 164 ? 0.1578 0.2121 0.1289 0.0051  0.0026  0.0060  164 ASP   A O   
1207 C CB  . ASP   A 164 ? 0.1643 0.2144 0.1366 0.0056  0.0034  0.0059  164 ASP   A CB  
1208 C CG  . ASP   A 164 ? 0.1680 0.2149 0.1400 0.0055  0.0041  0.0060  164 ASP   A CG  
1209 O OD1 . ASP   A 164 ? 0.1789 0.2228 0.1487 0.0053  0.0046  0.0071  164 ASP   A OD1 
1210 O OD2 . ASP   A 164 ? 0.1903 0.2378 0.1642 0.0056  0.0044  0.0049  164 ASP   A OD2 
1211 N N   . PHE   A 165 ? 0.1481 0.2037 0.1222 0.0037  0.0036  0.0045  165 PHE   A N   
1212 C CA  . PHE   A 165 ? 0.1399 0.1978 0.1152 0.0036  0.0035  0.0039  165 PHE   A CA  
1213 C C   . PHE   A 165 ? 0.1500 0.2087 0.1266 0.0025  0.0042  0.0030  165 PHE   A C   
1214 O O   . PHE   A 165 ? 0.1426 0.2010 0.1199 0.0023  0.0045  0.0027  165 PHE   A O   
1215 C CB  . PHE   A 165 ? 0.1457 0.2052 0.1229 0.0044  0.0030  0.0037  165 PHE   A CB  
1216 C CG  . PHE   A 165 ? 0.1613 0.2216 0.1383 0.0054  0.0022  0.0038  165 PHE   A CG  
1217 C CD1 . PHE   A 165 ? 0.1849 0.2441 0.1610 0.0064  0.0016  0.0044  165 PHE   A CD1 
1218 C CD2 . PHE   A 165 ? 0.1598 0.2221 0.1377 0.0053  0.0021  0.0032  165 PHE   A CD2 
1219 C CE1 . PHE   A 165 ? 0.1892 0.2497 0.1654 0.0075  0.0008  0.0043  165 PHE   A CE1 
1220 C CE2 . PHE   A 165 ? 0.1682 0.2320 0.1462 0.0061  0.0014  0.0030  165 PHE   A CE2 
1221 C CZ  . PHE   A 165 ? 0.1817 0.2447 0.1589 0.0073  0.0006  0.0035  165 PHE   A CZ  
1222 N N   . ILE   A 166 ? 0.1414 0.2016 0.1187 0.0020  0.0044  0.0024  166 ILE   A N   
1223 C CA  . ILE   A 166 ? 0.1432 0.2045 0.1226 0.0015  0.0049  0.0015  166 ILE   A CA  
1224 C C   . ILE   A 166 ? 0.1553 0.2179 0.1369 0.0020  0.0046  0.0012  166 ILE   A C   
1225 O O   . ILE   A 166 ? 0.1453 0.2086 0.1267 0.0021  0.0044  0.0011  166 ILE   A O   
1226 C CB  . ILE   A 166 ? 0.1495 0.2112 0.1285 0.0002  0.0056  0.0005  166 ILE   A CB  
1227 C CG1 . ILE   A 166 ? 0.1369 0.1994 0.1148 -0.0003 0.0056  0.0003  166 ILE   A CG1 
1228 C CG2 . ILE   A 166 ? 0.1647 0.2248 0.1419 -0.0006 0.0062  0.0007  166 ILE   A CG2 
1229 C CD1 . ILE   A 166 ? 0.1467 0.2102 0.1243 -0.0019 0.0065  -0.0009 166 ILE   A CD1 
1230 N N   . LYS   A 167 ? 0.1464 0.2094 0.1299 0.0024  0.0047  0.0012  167 LYS   A N   
1231 C CA  . LYS   A 167 ? 0.1571 0.2206 0.1424 0.0030  0.0046  0.0015  167 LYS   A CA  
1232 C C   . LYS   A 167 ? 0.1462 0.2102 0.1339 0.0029  0.0050  0.0009  167 LYS   A C   
1233 O O   . LYS   A 167 ? 0.1398 0.2040 0.1278 0.0030  0.0050  0.0007  167 LYS   A O   
1234 C CB  . LYS   A 167 ? 0.1661 0.2294 0.1509 0.0037  0.0042  0.0025  167 LYS   A CB  
1235 C CG  . LYS   A 167 ? 0.2025 0.2660 0.1887 0.0043  0.0043  0.0031  167 LYS   A CG  
1236 C CD  . LYS   A 167 ? 0.1926 0.2563 0.1779 0.0048  0.0039  0.0039  167 LYS   A CD  
1237 C CE  . LYS   A 167 ? 0.2130 0.2769 0.1995 0.0051  0.0042  0.0047  167 LYS   A CE  
1238 N NZ  . LYS   A 167 ? 0.2343 0.2988 0.2199 0.0054  0.0040  0.0055  167 LYS   A NZ  
1239 N N   . THR   A 168 ? 0.1336 0.1976 0.1231 0.0029  0.0055  0.0005  168 THR   A N   
1240 C CA  . THR   A 168 ? 0.1435 0.2077 0.1357 0.0030  0.0059  -0.0001 168 THR   A CA  
1241 C C   . THR   A 168 ? 0.1430 0.2069 0.1361 0.0042  0.0055  0.0010  168 THR   A C   
1242 O O   . THR   A 168 ? 0.1452 0.2097 0.1396 0.0045  0.0055  0.0004  168 THR   A O   
1243 C CB  . THR   A 168 ? 0.1510 0.2150 0.1454 0.0027  0.0067  -0.0008 168 THR   A CB  
1244 O OG1 . THR   A 168 ? 0.1394 0.2024 0.1340 0.0032  0.0067  0.0004  168 THR   A OG1 
1245 C CG2 . THR   A 168 ? 0.1622 0.2274 0.1560 0.0016  0.0070  -0.0023 168 THR   A CG2 
1246 N N   . SER   A 169 ? 0.1442 0.2074 0.1366 0.0049  0.0053  0.0025  169 SER   A N   
1247 C CA  . SER   A 169 ? 0.1428 0.2057 0.1365 0.0060  0.0051  0.0038  169 SER   A CA  
1248 C C   . SER   A 169 ? 0.1475 0.2105 0.1392 0.0065  0.0047  0.0055  169 SER   A C   
1249 O O   . SER   A 169 ? 0.1590 0.2220 0.1491 0.0060  0.0047  0.0055  169 SER   A O   
1250 C CB  . SER   A 169 ? 0.1417 0.2030 0.1377 0.0061  0.0060  0.0040  169 SER   A CB  
1251 O OG  . SER   A 169 ? 0.1583 0.2198 0.1562 0.0054  0.0066  0.0021  169 SER   A OG  
1252 N N   . THR   A 170 ? 0.1476 0.2111 0.1396 0.0077  0.0042  0.0067  170 THR   A N   
1253 C CA  . THR   A 170 ? 0.1486 0.2127 0.1389 0.0082  0.0038  0.0083  170 THR   A CA  
1254 C C   . THR   A 170 ? 0.1805 0.2428 0.1711 0.0081  0.0046  0.0097  170 THR   A C   
1255 O O   . THR   A 170 ? 0.1929 0.2556 0.1819 0.0080  0.0046  0.0108  170 THR   A O   
1256 C CB  . THR   A 170 ? 0.1435 0.2094 0.1339 0.0095  0.0030  0.0091  170 THR   A CB  
1257 O OG1 . THR   A 170 ? 0.1557 0.2204 0.1481 0.0106  0.0030  0.0100  170 THR   A OG1 
1258 C CG2 . THR   A 170 ? 0.1362 0.2043 0.1262 0.0093  0.0024  0.0074  170 THR   A CG2 
1259 N N   . GLY   A 171 ? 0.1653 0.2256 0.1581 0.0083  0.0053  0.0098  171 GLY   A N   
1260 C CA  . GLY   A 171 ? 0.1982 0.2563 0.1914 0.0082  0.0062  0.0114  171 GLY   A CA  
1261 C C   . GLY   A 171 ? 0.2248 0.2823 0.2178 0.0098  0.0058  0.0139  171 GLY   A C   
1262 O O   . GLY   A 171 ? 0.2799 0.3352 0.2730 0.0099  0.0067  0.0157  171 GLY   A O   
1263 N N   . ARG   A 172 ? 0.2105 0.2700 0.2035 0.0111  0.0046  0.0140  172 ARG   A N   
1264 C CA  . ARG   A 172 ? 0.2480 0.3078 0.2404 0.0130  0.0039  0.0164  172 ARG   A CA  
1265 C C   . ARG   A 172 ? 0.2521 0.3115 0.2472 0.0146  0.0034  0.0164  172 ARG   A C   
1266 O O   . ARG   A 172 ? 0.2806 0.3410 0.2754 0.0165  0.0024  0.0181  172 ARG   A O   
1267 C CB  . ARG   A 172 ? 0.2758 0.3394 0.2658 0.0134  0.0026  0.0164  172 ARG   A CB  
1268 C CG  . ARG   A 172 ? 0.3073 0.3718 0.2948 0.0120  0.0030  0.0165  172 ARG   A CG  
1269 C CD  . ARG   A 172 ? 0.3489 0.4116 0.3349 0.0119  0.0037  0.0190  172 ARG   A CD  
1270 N NE  . ARG   A 172 ? 0.4614 0.5268 0.4447 0.0112  0.0035  0.0192  172 ARG   A NE  
1271 C CZ  . ARG   A 172 ? 0.4749 0.5436 0.4565 0.0122  0.0024  0.0199  172 ARG   A CZ  
1272 N NH1 . ARG   A 172 ? 0.5030 0.5728 0.4852 0.0140  0.0014  0.0209  172 ARG   A NH1 
1273 N NH2 . ARG   A 172 ? 0.5362 0.6076 0.5158 0.0113  0.0024  0.0195  172 ARG   A NH2 
1274 N N   . VAL   A 173 ? 0.2192 0.2776 0.2171 0.0140  0.0040  0.0142  173 VAL   A N   
1275 C CA  . VAL   A 173 ? 0.2165 0.2745 0.2176 0.0154  0.0037  0.0136  173 VAL   A CA  
1276 C C   . VAL   A 173 ? 0.2153 0.2696 0.2191 0.0148  0.0053  0.0133  173 VAL   A C   
1277 O O   . VAL   A 173 ? 0.2193 0.2719 0.2223 0.0132  0.0065  0.0132  173 VAL   A O   
1278 C CB  . VAL   A 173 ? 0.2327 0.2937 0.2348 0.0150  0.0031  0.0106  173 VAL   A CB  
1279 C CG1 . VAL   A 173 ? 0.2584 0.3231 0.2581 0.0154  0.0018  0.0107  173 VAL   A CG1 
1280 C CG2 . VAL   A 173 ? 0.2324 0.2933 0.2345 0.0127  0.0041  0.0082  173 VAL   A CG2 
1281 N N   . ALA   A 174 ? 0.2209 0.2738 0.2281 0.0162  0.0054  0.0130  174 ALA   A N   
1282 C CA  . ALA   A 174 ? 0.2381 0.2872 0.2483 0.0159  0.0070  0.0130  174 ALA   A CA  
1283 C C   . ALA   A 174 ? 0.2046 0.2541 0.2160 0.0134  0.0083  0.0097  174 ALA   A C   
1284 O O   . ALA   A 174 ? 0.2314 0.2784 0.2438 0.0121  0.0098  0.0095  174 ALA   A O   
1285 C CB  . ALA   A 174 ? 0.2478 0.2958 0.2617 0.0182  0.0066  0.0133  174 ALA   A CB  
1286 N N   . VAL   A 175 ? 0.2097 0.2626 0.2210 0.0127  0.0076  0.0072  175 VAL   A N   
1287 C CA  . VAL   A 175 ? 0.1960 0.2498 0.2084 0.0105  0.0086  0.0041  175 VAL   A CA  
1288 C C   . VAL   A 175 ? 0.1904 0.2463 0.1989 0.0091  0.0081  0.0038  175 VAL   A C   
1289 O O   . VAL   A 175 ? 0.1907 0.2490 0.1974 0.0094  0.0069  0.0036  175 VAL   A O   
1290 C CB  . VAL   A 175 ? 0.1750 0.2306 0.1905 0.0106  0.0086  0.0013  175 VAL   A CB  
1291 C CG1 . VAL   A 175 ? 0.1815 0.2386 0.1974 0.0083  0.0095  -0.0018 175 VAL   A CG1 
1292 C CG2 . VAL   A 175 ? 0.1805 0.2336 0.2004 0.0122  0.0091  0.0014  175 VAL   A CG2 
1293 N N   . ASN   A 176 ? 0.1928 0.2481 0.2005 0.0076  0.0090  0.0034  176 ASN   A N   
1294 C CA  . ASN   A 176 ? 0.1858 0.2430 0.1902 0.0064  0.0085  0.0030  176 ASN   A CA  
1295 C C   . ASN   A 176 ? 0.1594 0.2181 0.1645 0.0048  0.0091  0.0003  176 ASN   A C   
1296 O O   . ASN   A 176 ? 0.1602 0.2195 0.1675 0.0047  0.0094  -0.0014 176 ASN   A O   
1297 C CB  . ASN   A 176 ? 0.2046 0.2606 0.2068 0.0064  0.0086  0.0050  176 ASN   A CB  
1298 C CG  . ASN   A 176 ? 0.2322 0.2877 0.2333 0.0080  0.0078  0.0076  176 ASN   A CG  
1299 O OD1 . ASN   A 176 ? 0.2506 0.3080 0.2495 0.0085  0.0066  0.0080  176 ASN   A OD1 
1300 N ND2 . ASN   A 176 ? 0.2448 0.2977 0.2475 0.0089  0.0085  0.0092  176 ASN   A ND2 
1301 N N   . ALA   A 177 ? 0.1571 0.2166 0.1604 0.0037  0.0093  -0.0002 177 ALA   A N   
1302 C CA  . ALA   A 177 ? 0.1569 0.2184 0.1603 0.0023  0.0096  -0.0027 177 ALA   A CA  
1303 C C   . ALA   A 177 ? 0.1641 0.2254 0.1714 0.0016  0.0110  -0.0047 177 ALA   A C   
1304 O O   . ALA   A 177 ? 0.1633 0.2224 0.1728 0.0018  0.0120  -0.0042 177 ALA   A O   
1305 C CB  . ALA   A 177 ? 0.1639 0.2266 0.1649 0.0016  0.0094  -0.0027 177 ALA   A CB  
1306 N N   . THR   A 178 ? 0.1602 0.2237 0.1682 0.0006  0.0112  -0.0071 178 THR   A N   
1307 C CA  . THR   A 178 ? 0.1659 0.2304 0.1771 -0.0006 0.0126  -0.0098 178 THR   A CA  
1308 C C   . THR   A 178 ? 0.1645 0.2324 0.1737 -0.0020 0.0124  -0.0116 178 THR   A C   
1309 O O   . THR   A 178 ? 0.1540 0.2230 0.1597 -0.0019 0.0113  -0.0107 178 THR   A O   
1310 C CB  . THR   A 178 ? 0.1705 0.2347 0.1854 -0.0003 0.0132  -0.0112 178 THR   A CB  
1311 O OG1 . THR   A 178 ? 0.1899 0.2565 0.2030 -0.0007 0.0125  -0.0122 178 THR   A OG1 
1312 C CG2 . THR   A 178 ? 0.1812 0.2425 0.1972 0.0016  0.0128  -0.0089 178 THR   A CG2 
1313 N N   . PRO   A 179 ? 0.1948 0.2647 0.2061 -0.0034 0.0135  -0.0142 179 PRO   A N   
1314 C CA  . PRO   A 179 ? 0.1988 0.2725 0.2080 -0.0046 0.0132  -0.0159 179 PRO   A CA  
1315 C C   . PRO   A 179 ? 0.1932 0.2686 0.2009 -0.0049 0.0127  -0.0164 179 PRO   A C   
1316 O O   . PRO   A 179 ? 0.1852 0.2623 0.1890 -0.0052 0.0118  -0.0159 179 PRO   A O   
1317 C CB  . PRO   A 179 ? 0.2049 0.2806 0.2179 -0.0060 0.0148  -0.0190 179 PRO   A CB  
1318 C CG  . PRO   A 179 ? 0.2020 0.2741 0.2175 -0.0055 0.0157  -0.0180 179 PRO   A CG  
1319 C CD  . PRO   A 179 ? 0.2210 0.2895 0.2366 -0.0039 0.0152  -0.0156 179 PRO   A CD  
1320 N N   . GLU   A 180 ? 0.1872 0.2617 0.1979 -0.0048 0.0133  -0.0174 180 GLU   A N   
1321 C CA  . GLU   A 180 ? 0.1966 0.2727 0.2066 -0.0053 0.0132  -0.0183 180 GLU   A CA  
1322 C C   . GLU   A 180 ? 0.1789 0.2537 0.1849 -0.0044 0.0119  -0.0156 180 GLU   A C   
1323 O O   . GLU   A 180 ? 0.1691 0.2454 0.1718 -0.0052 0.0115  -0.0156 180 GLU   A O   
1324 C CB  . GLU   A 180 ? 0.2500 0.3255 0.2651 -0.0051 0.0142  -0.0202 180 GLU   A CB  
1325 C CG  . GLU   A 180 ? 0.3533 0.4306 0.3686 -0.0056 0.0142  -0.0217 180 GLU   A CG  
1326 C CD  . GLU   A 180 ? 0.4663 0.5437 0.4871 -0.0053 0.0152  -0.0241 180 GLU   A CD  
1327 O OE1 . GLU   A 180 ? 0.5688 0.6436 0.5934 -0.0042 0.0157  -0.0239 180 GLU   A OE1 
1328 O OE2 . GLU   A 180 ? 0.5012 0.5811 0.5224 -0.0062 0.0155  -0.0261 180 GLU   A OE2 
1329 N N   . SER   A 181 ? 0.1658 0.2376 0.1718 -0.0028 0.0112  -0.0133 181 SER   A N   
1330 C CA  . SER   A 181 ? 0.1799 0.2509 0.1824 -0.0021 0.0101  -0.0112 181 SER   A CA  
1331 C C   . SER   A 181 ? 0.1642 0.2355 0.1625 -0.0024 0.0094  -0.0099 181 SER   A C   
1332 O O   . SER   A 181 ? 0.1689 0.2403 0.1642 -0.0026 0.0089  -0.0091 181 SER   A O   
1333 C CB  . SER   A 181 ? 0.1920 0.2606 0.1956 -0.0004 0.0096  -0.0092 181 SER   A CB  
1334 O OG  . SER   A 181 ? 0.2104 0.2772 0.2141 0.0003  0.0096  -0.0077 181 SER   A OG  
1335 N N   . ALA   A 182 ? 0.1684 0.2398 0.1668 -0.0024 0.0095  -0.0098 182 ALA   A N   
1336 C CA  . ALA   A 182 ? 0.1754 0.2476 0.1704 -0.0024 0.0087  -0.0088 182 ALA   A CA  
1337 C C   . ALA   A 182 ? 0.1657 0.2404 0.1584 -0.0036 0.0087  -0.0100 182 ALA   A C   
1338 O O   . ALA   A 182 ? 0.1612 0.2357 0.1503 -0.0035 0.0080  -0.0086 182 ALA   A O   
1339 C CB  . ALA   A 182 ? 0.1838 0.2565 0.1801 -0.0023 0.0090  -0.0092 182 ALA   A CB  
1340 N N   . ARG   A 183 ? 0.1735 0.2507 0.1686 -0.0048 0.0097  -0.0125 183 ARG   A N   
1341 C CA  . ARG   A 183 ? 0.1931 0.2733 0.1860 -0.0061 0.0098  -0.0138 183 ARG   A CA  
1342 C C   . ARG   A 183 ? 0.1704 0.2495 0.1607 -0.0065 0.0097  -0.0129 183 ARG   A C   
1343 O O   . ARG   A 183 ? 0.1788 0.2584 0.1650 -0.0069 0.0093  -0.0118 183 ARG   A O   
1344 C CB  . ARG   A 183 ? 0.2070 0.2901 0.2035 -0.0075 0.0111  -0.0172 183 ARG   A CB  
1345 C CG  . ARG   A 183 ? 0.2568 0.3437 0.2509 -0.0091 0.0113  -0.0187 183 ARG   A CG  
1346 C CD  . ARG   A 183 ? 0.2880 0.3781 0.2862 -0.0107 0.0128  -0.0225 183 ARG   A CD  
1347 N NE  . ARG   A 183 ? 0.3099 0.3981 0.3120 -0.0105 0.0136  -0.0235 183 ARG   A NE  
1348 C CZ  . ARG   A 183 ? 0.3668 0.4551 0.3686 -0.0111 0.0139  -0.0239 183 ARG   A CZ  
1349 N NH1 . ARG   A 183 ? 0.3834 0.4727 0.3806 -0.0119 0.0135  -0.0230 183 ARG   A NH1 
1350 N NH2 . ARG   A 183 ? 0.4155 0.5028 0.4217 -0.0107 0.0146  -0.0253 183 ARG   A NH2 
1351 N N   . ILE   A 184 ? 0.1688 0.2465 0.1617 -0.0063 0.0102  -0.0133 184 ILE   A N   
1352 C CA  . ILE   A 184 ? 0.1546 0.2319 0.1459 -0.0069 0.0104  -0.0132 184 ILE   A CA  
1353 C C   . ILE   A 184 ? 0.1562 0.2313 0.1435 -0.0062 0.0095  -0.0104 184 ILE   A C   
1354 O O   . ILE   A 184 ? 0.1661 0.2411 0.1502 -0.0072 0.0097  -0.0099 184 ILE   A O   
1355 C CB  . ILE   A 184 ? 0.1658 0.2426 0.1611 -0.0064 0.0108  -0.0143 184 ILE   A CB  
1356 C CG1 . ILE   A 184 ? 0.1747 0.2539 0.1743 -0.0073 0.0119  -0.0174 184 ILE   A CG1 
1357 C CG2 . ILE   A 184 ? 0.1603 0.2366 0.1540 -0.0068 0.0109  -0.0139 184 ILE   A CG2 
1358 C CD1 . ILE   A 184 ? 0.1736 0.2516 0.1779 -0.0060 0.0120  -0.0180 184 ILE   A CD1 
1359 N N   . MET   A 185 ? 0.1454 0.2183 0.1330 -0.0047 0.0087  -0.0087 185 MET   A N   
1360 C CA  . MET   A 185 ? 0.1526 0.2233 0.1370 -0.0040 0.0080  -0.0064 185 MET   A CA  
1361 C C   . MET   A 185 ? 0.1483 0.2192 0.1289 -0.0041 0.0075  -0.0053 185 MET   A C   
1362 O O   . MET   A 185 ? 0.1653 0.2346 0.1426 -0.0043 0.0074  -0.0040 185 MET   A O   
1363 C CB  . MET   A 185 ? 0.1505 0.2194 0.1362 -0.0024 0.0073  -0.0051 185 MET   A CB  
1364 C CG  . MET   A 185 ? 0.1546 0.2230 0.1429 -0.0018 0.0075  -0.0054 185 MET   A CG  
1365 S SD  . MET   A 185 ? 0.1628 0.2296 0.1525 -0.0001 0.0068  -0.0037 185 MET   A SD  
1366 C CE  . MET   A 185 ? 0.1740 0.2394 0.1600 0.0000  0.0062  -0.0022 185 MET   A CE  
1367 N N   . MET   A 186 ? 0.1579 0.2307 0.1389 -0.0040 0.0072  -0.0059 186 MET   A N   
1368 C CA  . MET   A 186 ? 0.1662 0.2398 0.1436 -0.0038 0.0065  -0.0049 186 MET   A CA  
1369 C C   . MET   A 186 ? 0.1607 0.2359 0.1355 -0.0054 0.0071  -0.0054 186 MET   A C   
1370 O O   . MET   A 186 ? 0.1592 0.2334 0.1299 -0.0052 0.0067  -0.0036 186 MET   A O   
1371 C CB  . MET   A 186 ? 0.1746 0.2507 0.1535 -0.0033 0.0061  -0.0058 186 MET   A CB  
1372 C CG  . MET   A 186 ? 0.1900 0.2646 0.1702 -0.0018 0.0054  -0.0048 186 MET   A CG  
1373 S SD  . MET   A 186 ? 0.2074 0.2852 0.1890 -0.0015 0.0050  -0.0061 186 MET   A SD  
1374 C CE  . MET   A 186 ? 0.2157 0.2940 0.2025 -0.0024 0.0065  -0.0084 186 MET   A CE  
1375 N N   . GLU   A 187 ? 0.1700 0.2473 0.1470 -0.0068 0.0082  -0.0077 187 GLU   A N   
1376 C CA  . GLU   A 187 ? 0.1935 0.2721 0.1679 -0.0086 0.0090  -0.0083 187 GLU   A CA  
1377 C C   . GLU   A 187 ? 0.2024 0.2778 0.1740 -0.0089 0.0093  -0.0066 187 GLU   A C   
1378 O O   . GLU   A 187 ? 0.1987 0.2738 0.1663 -0.0099 0.0096  -0.0055 187 GLU   A O   
1379 C CB  . GLU   A 187 ? 0.2209 0.3025 0.1988 -0.0102 0.0102  -0.0115 187 GLU   A CB  
1380 C CG  . GLU   A 187 ? 0.2565 0.3420 0.2364 -0.0106 0.0103  -0.0138 187 GLU   A CG  
1381 C CD  . GLU   A 187 ? 0.2727 0.3607 0.2570 -0.0120 0.0117  -0.0172 187 GLU   A CD  
1382 O OE1 . GLU   A 187 ? 0.3088 0.3953 0.2944 -0.0123 0.0123  -0.0176 187 GLU   A OE1 
1383 O OE2 . GLU   A 187 ? 0.2930 0.3842 0.2798 -0.0125 0.0121  -0.0196 187 GLU   A OE2 
1384 N N   . VAL   A 188 ? 0.1711 0.2439 0.1447 -0.0082 0.0093  -0.0062 188 VAL   A N   
1385 C CA  . VAL   A 188 ? 0.1694 0.2393 0.1406 -0.0086 0.0098  -0.0049 188 VAL   A CA  
1386 C C   . VAL   A 188 ? 0.1652 0.2325 0.1323 -0.0077 0.0090  -0.0020 188 VAL   A C   
1387 O O   . VAL   A 188 ? 0.1695 0.2349 0.1331 -0.0086 0.0096  -0.0008 188 VAL   A O   
1388 C CB  . VAL   A 188 ? 0.1702 0.2388 0.1445 -0.0080 0.0098  -0.0053 188 VAL   A CB  
1389 C CG1 . VAL   A 188 ? 0.1716 0.2375 0.1437 -0.0086 0.0104  -0.0043 188 VAL   A CG1 
1390 C CG2 . VAL   A 188 ? 0.1687 0.2397 0.1471 -0.0086 0.0105  -0.0079 188 VAL   A CG2 
1391 N N   . ILE   A 189 ? 0.1656 0.2325 0.1334 -0.0058 0.0077  -0.0010 189 ILE   A N   
1392 C CA  . ILE   A 189 ? 0.1713 0.2359 0.1357 -0.0046 0.0069  0.0015  189 ILE   A CA  
1393 C C   . ILE   A 189 ? 0.1656 0.2312 0.1259 -0.0054 0.0069  0.0024  189 ILE   A C   
1394 O O   . ILE   A 189 ? 0.1701 0.2328 0.1266 -0.0054 0.0071  0.0046  189 ILE   A O   
1395 C CB  . ILE   A 189 ? 0.1746 0.2398 0.1409 -0.0027 0.0056  0.0018  189 ILE   A CB  
1396 C CG1 . ILE   A 189 ? 0.1712 0.2350 0.1406 -0.0020 0.0056  0.0015  189 ILE   A CG1 
1397 C CG2 . ILE   A 189 ? 0.1849 0.2491 0.1481 -0.0012 0.0044  0.0039  189 ILE   A CG2 
1398 C CD1 . ILE   A 189 ? 0.1774 0.2421 0.1489 -0.0005 0.0046  0.0014  189 ILE   A CD1 
1399 N N   . ARG   A 190 ? 0.1720 0.2417 0.1331 -0.0060 0.0069  0.0008  190 ARG   A N   
1400 C CA  . ARG   A 190 ? 0.1967 0.2685 0.1538 -0.0067 0.0067  0.0014  190 ARG   A CA  
1401 C C   . ARG   A 190 ? 0.1887 0.2594 0.1429 -0.0088 0.0082  0.0017  190 ARG   A C   
1402 O O   . ARG   A 190 ? 0.2138 0.2827 0.1631 -0.0089 0.0082  0.0042  190 ARG   A O   
1403 C CB  . ARG   A 190 ? 0.2313 0.3084 0.1907 -0.0073 0.0067  -0.0013 190 ARG   A CB  
1404 C CG  . ARG   A 190 ? 0.2884 0.3686 0.2437 -0.0075 0.0061  -0.0005 190 ARG   A CG  
1405 C CD  . ARG   A 190 ? 0.3232 0.4086 0.2794 -0.0095 0.0070  -0.0035 190 ARG   A CD  
1406 N NE  . ARG   A 190 ? 0.3452 0.4308 0.3046 -0.0115 0.0087  -0.0059 190 ARG   A NE  
1407 C CZ  . ARG   A 190 ? 0.3726 0.4622 0.3359 -0.0126 0.0094  -0.0094 190 ARG   A CZ  
1408 N NH1 . ARG   A 190 ? 0.4053 0.4993 0.3690 -0.0124 0.0088  -0.0107 190 ARG   A NH1 
1409 N NH2 . ARG   A 190 ? 0.3672 0.4566 0.3341 -0.0138 0.0107  -0.0116 190 ARG   A NH2 
1410 N N   . ASP   A 191 ? 0.1774 0.2489 0.1344 -0.0105 0.0096  -0.0007 191 ASP   A N   
1411 C CA  . ASP   A 191 ? 0.1798 0.2510 0.1349 -0.0129 0.0112  -0.0012 191 ASP   A CA  
1412 C C   . ASP   A 191 ? 0.1839 0.2499 0.1362 -0.0130 0.0118  0.0012  191 ASP   A C   
1413 O O   . ASP   A 191 ? 0.1896 0.2543 0.1382 -0.0148 0.0131  0.0020  191 ASP   A O   
1414 C CB  . ASP   A 191 ? 0.1844 0.2578 0.1439 -0.0144 0.0124  -0.0046 191 ASP   A CB  
1415 C CG  . ASP   A 191 ? 0.2080 0.2866 0.1706 -0.0149 0.0124  -0.0075 191 ASP   A CG  
1416 O OD1 . ASP   A 191 ? 0.2404 0.3216 0.2008 -0.0148 0.0118  -0.0072 191 ASP   A OD1 
1417 O OD2 . ASP   A 191 ? 0.2337 0.3136 0.2008 -0.0153 0.0130  -0.0101 191 ASP   A OD2 
1418 N N   . MET   A 192 ? 0.1802 0.2432 0.1344 -0.0112 0.0110  0.0021  192 MET   A N   
1419 C CA  . MET   A 192 ? 0.1854 0.2436 0.1375 -0.0112 0.0117  0.0041  192 MET   A CA  
1420 C C   . MET   A 192 ? 0.1860 0.2414 0.1336 -0.0099 0.0108  0.0075  192 MET   A C   
1421 O O   . MET   A 192 ? 0.1843 0.2352 0.1291 -0.0102 0.0116  0.0095  192 MET   A O   
1422 C CB  . MET   A 192 ? 0.2044 0.2612 0.1605 -0.0101 0.0114  0.0033  192 MET   A CB  
1423 C CG  . MET   A 192 ? 0.2209 0.2800 0.1806 -0.0116 0.0124  0.0003  192 MET   A CG  
1424 S SD  . MET   A 192 ? 0.2554 0.3131 0.2189 -0.0102 0.0121  -0.0002 192 MET   A SD  
1425 C CE  . MET   A 192 ? 0.2450 0.2980 0.2053 -0.0116 0.0136  0.0010  192 MET   A CE  
1426 N N   . GLY   A 193 ? 0.1892 0.2472 0.1363 -0.0083 0.0092  0.0080  193 GLY   A N   
1427 C CA  . GLY   A 193 ? 0.2058 0.2618 0.1490 -0.0066 0.0081  0.0111  193 GLY   A CA  
1428 C C   . GLY   A 193 ? 0.2055 0.2583 0.1501 -0.0041 0.0069  0.0125  193 GLY   A C   
1429 O O   . GLY   A 193 ? 0.2067 0.2562 0.1482 -0.0027 0.0064  0.0153  193 GLY   A O   
1430 N N   . VAL   A 194 ? 0.1968 0.2506 0.1462 -0.0035 0.0066  0.0105  194 VAL   A N   
1431 C CA  . VAL   A 194 ? 0.2011 0.2520 0.1521 -0.0015 0.0059  0.0114  194 VAL   A CA  
1432 C C   . VAL   A 194 ? 0.2077 0.2614 0.1610 0.0006  0.0041  0.0109  194 VAL   A C   
1433 O O   . VAL   A 194 ? 0.2009 0.2535 0.1567 0.0018  0.0036  0.0107  194 VAL   A O   
1434 C CB  . VAL   A 194 ? 0.1963 0.2456 0.1502 -0.0025 0.0071  0.0099  194 VAL   A CB  
1435 C CG1 . VAL   A 194 ? 0.2124 0.2585 0.1639 -0.0046 0.0089  0.0104  194 VAL   A CG1 
1436 C CG2 . VAL   A 194 ? 0.1894 0.2426 0.1473 -0.0033 0.0072  0.0072  194 VAL   A CG2 
1437 N N   . GLU   A 195 ? 0.2271 0.2847 0.1796 0.0009  0.0032  0.0105  195 GLU   A N   
1438 C CA  . GLU   A 195 ? 0.2322 0.2930 0.1873 0.0025  0.0018  0.0095  195 GLU   A CA  
1439 C C   . GLU   A 195 ? 0.2331 0.2920 0.1878 0.0050  0.0005  0.0112  195 GLU   A C   
1440 O O   . GLU   A 195 ? 0.2283 0.2888 0.1858 0.0062  -0.0004 0.0101  195 GLU   A O   
1441 C CB  . GLU   A 195 ? 0.2432 0.3090 0.1976 0.0022  0.0013  0.0084  195 GLU   A CB  
1442 C CG  . GLU   A 195 ? 0.2507 0.3168 0.2004 0.0029  0.0005  0.0106  195 GLU   A CG  
1443 C CD  . GLU   A 195 ? 0.2942 0.3593 0.2402 0.0009  0.0018  0.0115  195 GLU   A CD  
1444 O OE1 . GLU   A 195 ? 0.2436 0.3076 0.1909 -0.0012 0.0034  0.0102  195 GLU   A OE1 
1445 O OE2 . GLU   A 195 ? 0.3344 0.4004 0.2761 0.0014  0.0011  0.0133  195 GLU   A OE2 
1446 N N   . LYS   A 196 ? 0.2364 0.2914 0.1877 0.0058  0.0004  0.0138  196 LYS   A N   
1447 C CA  . LYS   A 196 ? 0.2605 0.3134 0.2118 0.0084  -0.0009 0.0152  196 LYS   A CA  
1448 C C   . LYS   A 196 ? 0.2416 0.2920 0.1962 0.0085  -0.0003 0.0143  196 LYS   A C   
1449 O O   . LYS   A 196 ? 0.2605 0.3116 0.2173 0.0103  -0.0014 0.0139  196 LYS   A O   
1450 C CB  . LYS   A 196 ? 0.3088 0.3572 0.2558 0.0093  -0.0009 0.0184  196 LYS   A CB  
1451 C CG  . LYS   A 196 ? 0.3887 0.4341 0.3360 0.0120  -0.0020 0.0200  196 LYS   A CG  
1452 C CD  . LYS   A 196 ? 0.4626 0.5020 0.4060 0.0125  -0.0015 0.0232  196 LYS   A CD  
1453 C CE  . LYS   A 196 ? 0.5680 0.6042 0.5122 0.0154  -0.0026 0.0247  196 LYS   A CE  
1454 N NZ  . LYS   A 196 ? 0.6674 0.6996 0.6069 0.0168  -0.0029 0.0284  196 LYS   A NZ  
1455 N N   . SER   A 197 ? 0.2061 0.2542 0.1612 0.0065  0.0013  0.0137  197 SER   A N   
1456 C CA  . SER   A 197 ? 0.2174 0.2633 0.1752 0.0065  0.0020  0.0130  197 SER   A CA  
1457 C C   . SER   A 197 ? 0.2010 0.2498 0.1624 0.0054  0.0024  0.0106  197 SER   A C   
1458 O O   . SER   A 197 ? 0.2134 0.2613 0.1770 0.0056  0.0027  0.0099  197 SER   A O   
1459 C CB  . SER   A 197 ? 0.2109 0.2522 0.1671 0.0053  0.0036  0.0139  197 SER   A CB  
1460 O OG  . SER   A 197 ? 0.2557 0.2976 0.2105 0.0029  0.0048  0.0134  197 SER   A OG  
1461 N N   . VAL   A 198 ? 0.1878 0.2400 0.1498 0.0044  0.0025  0.0094  198 VAL   A N   
1462 C CA  . VAL   A 198 ? 0.1830 0.2369 0.1481 0.0034  0.0031  0.0075  198 VAL   A CA  
1463 C C   . VAL   A 198 ? 0.1810 0.2387 0.1481 0.0039  0.0023  0.0064  198 VAL   A C   
1464 O O   . VAL   A 198 ? 0.1816 0.2415 0.1477 0.0036  0.0021  0.0061  198 VAL   A O   
1465 C CB  . VAL   A 198 ? 0.1886 0.2426 0.1536 0.0013  0.0044  0.0066  198 VAL   A CB  
1466 C CG1 . VAL   A 198 ? 0.1902 0.2462 0.1587 0.0008  0.0048  0.0048  198 VAL   A CG1 
1467 C CG2 . VAL   A 198 ? 0.1923 0.2426 0.1557 0.0005  0.0055  0.0074  198 VAL   A CG2 
1468 N N   . GLY   A 199 ? 0.1605 0.2192 0.1304 0.0045  0.0020  0.0056  199 GLY   A N   
1469 C CA  . GLY   A 199 ? 0.1515 0.2133 0.1236 0.0047  0.0017  0.0044  199 GLY   A CA  
1470 C C   . GLY   A 199 ? 0.1524 0.2152 0.1268 0.0034  0.0026  0.0031  199 GLY   A C   
1471 O O   . GLY   A 199 ? 0.1617 0.2231 0.1363 0.0027  0.0033  0.0031  199 GLY   A O   
1472 N N   . PHE   A 200 ? 0.1480 0.2131 0.1245 0.0034  0.0026  0.0020  200 PHE   A N   
1473 C CA  . PHE   A 200 ? 0.1457 0.2116 0.1248 0.0025  0.0034  0.0008  200 PHE   A CA  
1474 C C   . PHE   A 200 ? 0.1599 0.2263 0.1412 0.0030  0.0034  0.0006  200 PHE   A C   
1475 O O   . PHE   A 200 ? 0.1481 0.2159 0.1296 0.0035  0.0030  0.0002  200 PHE   A O   
1476 C CB  . PHE   A 200 ? 0.1604 0.2285 0.1399 0.0015  0.0039  -0.0006 200 PHE   A CB  
1477 C CG  . PHE   A 200 ? 0.1574 0.2262 0.1402 0.0008  0.0048  -0.0019 200 PHE   A CG  
1478 C CD1 . PHE   A 200 ? 0.1731 0.2407 0.1570 0.0004  0.0053  -0.0019 200 PHE   A CD1 
1479 C CD2 . PHE   A 200 ? 0.1697 0.2402 0.1548 0.0006  0.0051  -0.0031 200 PHE   A CD2 
1480 C CE1 . PHE   A 200 ? 0.1731 0.2410 0.1602 0.0001  0.0061  -0.0030 200 PHE   A CE1 
1481 C CE2 . PHE   A 200 ? 0.1777 0.2480 0.1660 0.0001  0.0061  -0.0041 200 PHE   A CE2 
1482 C CZ  . PHE   A 200 ? 0.1743 0.2432 0.1636 0.0000  0.0065  -0.0039 200 PHE   A CZ  
1483 N N   . LYS   A 201 ? 0.1521 0.2176 0.1351 0.0029  0.0040  0.0007  201 LYS   A N   
1484 C CA  A LYS   A 201 ? 0.1516 0.2173 0.1365 0.0031  0.0042  0.0007  201 LYS   A CA  
1485 C CA  B LYS   A 201 ? 0.1526 0.2184 0.1376 0.0031  0.0042  0.0007  201 LYS   A CA  
1486 C C   . LYS   A 201 ? 0.1561 0.2217 0.1435 0.0026  0.0051  0.0002  201 LYS   A C   
1487 O O   . LYS   A 201 ? 0.1521 0.2169 0.1400 0.0026  0.0052  0.0004  201 LYS   A O   
1488 C CB  A LYS   A 201 ? 0.1577 0.2225 0.1421 0.0039  0.0038  0.0018  201 LYS   A CB  
1489 C CB  B LYS   A 201 ? 0.1569 0.2216 0.1413 0.0039  0.0038  0.0018  201 LYS   A CB  
1490 C CG  A LYS   A 201 ? 0.1557 0.2206 0.1416 0.0040  0.0042  0.0021  201 LYS   A CG  
1491 C CG  B LYS   A 201 ? 0.1556 0.2205 0.1416 0.0039  0.0043  0.0020  201 LYS   A CG  
1492 C CD  A LYS   A 201 ? 0.1662 0.2309 0.1512 0.0046  0.0038  0.0028  201 LYS   A CD  
1493 C CD  B LYS   A 201 ? 0.1634 0.2281 0.1485 0.0045  0.0038  0.0028  201 LYS   A CD  
1494 C CE  A LYS   A 201 ? 0.1692 0.2340 0.1551 0.0045  0.0043  0.0034  201 LYS   A CE  
1495 C CE  B LYS   A 201 ? 0.1640 0.2293 0.1502 0.0044  0.0043  0.0030  201 LYS   A CE  
1496 N NZ  A LYS   A 201 ? 0.1727 0.2379 0.1577 0.0049  0.0040  0.0040  201 LYS   A NZ  
1497 N NZ  B LYS   A 201 ? 0.1670 0.2314 0.1540 0.0043  0.0049  0.0039  201 LYS   A NZ  
1498 N N   . VAL   A 202 ? 0.1534 0.2198 0.1426 0.0023  0.0057  -0.0006 202 VAL   A N   
1499 C CA  . VAL   A 202 ? 0.1792 0.2449 0.1711 0.0019  0.0067  -0.0010 202 VAL   A CA  
1500 C C   . VAL   A 202 ? 0.1786 0.2429 0.1709 0.0024  0.0068  0.0005  202 VAL   A C   
1501 O O   . VAL   A 202 ? 0.1881 0.2528 0.1801 0.0024  0.0069  0.0006  202 VAL   A O   
1502 C CB  . VAL   A 202 ? 0.2217 0.2889 0.2156 0.0010  0.0075  -0.0028 202 VAL   A CB  
1503 C CG1 . VAL   A 202 ? 0.2334 0.2993 0.2306 0.0005  0.0088  -0.0033 202 VAL   A CG1 
1504 C CG2 . VAL   A 202 ? 0.2688 0.3382 0.2620 0.0004  0.0073  -0.0044 202 VAL   A CG2 
1505 N N   . THR   A 203 ? 0.1850 0.2479 0.1781 0.0029  0.0070  0.0014  203 THR   A N   
1506 C CA  . THR   A 203 ? 0.1958 0.2574 0.1893 0.0034  0.0073  0.0031  203 THR   A CA  
1507 C C   . THR   A 203 ? 0.2010 0.2610 0.1971 0.0035  0.0082  0.0032  203 THR   A C   
1508 O O   . THR   A 203 ? 0.1691 0.2289 0.1664 0.0038  0.0082  0.0028  203 THR   A O   
1509 C CB  . THR   A 203 ? 0.2086 0.2703 0.2003 0.0043  0.0063  0.0044  203 THR   A CB  
1510 O OG1 . THR   A 203 ? 0.2726 0.3353 0.2623 0.0042  0.0057  0.0041  203 THR   A OG1 
1511 C CG2 . THR   A 203 ? 0.2025 0.2633 0.1943 0.0049  0.0065  0.0063  203 THR   A CG2 
1512 N N   . GLY   A 204 ? 0.1911 0.2499 0.1882 0.0031  0.0093  0.0037  204 GLY   A N   
1513 C CA  . GLY   A 204 ? 0.2106 0.2672 0.2105 0.0030  0.0105  0.0038  204 GLY   A CA  
1514 C C   . GLY   A 204 ? 0.2347 0.2921 0.2372 0.0020  0.0114  0.0012  204 GLY   A C   
1515 O O   . GLY   A 204 ? 0.2127 0.2724 0.2143 0.0013  0.0109  -0.0005 204 GLY   A O   
1516 N N   . GLY   A 205 ? 0.2607 0.3159 0.2663 0.0018  0.0127  0.0009  205 GLY   A N   
1517 C CA  . GLY   A 205 ? 0.2680 0.3240 0.2767 0.0007  0.0139  -0.0019 205 GLY   A CA  
1518 C C   . GLY   A 205 ? 0.2890 0.3471 0.2977 -0.0009 0.0146  -0.0040 205 GLY   A C   
1519 O O   . GLY   A 205 ? 0.3113 0.3715 0.3217 -0.0020 0.0151  -0.0067 205 GLY   A O   
1520 N N   . VAL   A 206 ? 0.2775 0.3358 0.2844 -0.0012 0.0146  -0.0031 206 VAL   A N   
1521 C CA  . VAL   A 206 ? 0.2724 0.3336 0.2794 -0.0025 0.0150  -0.0054 206 VAL   A CA  
1522 C C   . VAL   A 206 ? 0.2940 0.3537 0.3013 -0.0033 0.0163  -0.0047 206 VAL   A C   
1523 O O   . VAL   A 206 ? 0.2786 0.3396 0.2837 -0.0032 0.0156  -0.0040 206 VAL   A O   
1524 C CB  . VAL   A 206 ? 0.2761 0.3405 0.2800 -0.0020 0.0131  -0.0056 206 VAL   A CB  
1525 C CG1 . VAL   A 206 ? 0.3170 0.3805 0.3178 -0.0008 0.0118  -0.0030 206 VAL   A CG1 
1526 C CG2 . VAL   A 206 ? 0.2767 0.3447 0.2809 -0.0030 0.0133  -0.0080 206 VAL   A CG2 
1527 N N   . SER   A 207 ? 0.3053 0.3624 0.3156 -0.0042 0.0184  -0.0051 207 SER   A N   
1528 C CA  . SER   A 207 ? 0.3474 0.4022 0.3583 -0.0051 0.0201  -0.0042 207 SER   A CA  
1529 C C   . SER   A 207 ? 0.3470 0.4047 0.3593 -0.0070 0.0213  -0.0072 207 SER   A C   
1530 O O   . SER   A 207 ? 0.3521 0.4091 0.3636 -0.0078 0.0223  -0.0066 207 SER   A O   
1531 C CB  . SER   A 207 ? 0.3647 0.4149 0.3785 -0.0052 0.0219  -0.0033 207 SER   A CB  
1532 O OG  . SER   A 207 ? 0.4254 0.4730 0.4371 -0.0032 0.0207  0.0002  207 SER   A OG  
1533 N N   . THR   A 208 ? 0.2872 0.3483 0.3012 -0.0077 0.0213  -0.0105 208 THR   A N   
1534 C CA  . THR   A 208 ? 0.2771 0.3414 0.2931 -0.0096 0.0227  -0.0138 208 THR   A CA  
1535 C C   . THR   A 208 ? 0.2733 0.3433 0.2879 -0.0093 0.0209  -0.0160 208 THR   A C   
1536 O O   . THR   A 208 ? 0.2659 0.3371 0.2787 -0.0080 0.0189  -0.0153 208 THR   A O   
1537 C CB  . THR   A 208 ? 0.2818 0.3451 0.3024 -0.0113 0.0252  -0.0165 208 THR   A CB  
1538 O OG1 . THR   A 208 ? 0.2559 0.3216 0.2775 -0.0109 0.0243  -0.0184 208 THR   A OG1 
1539 C CG2 . THR   A 208 ? 0.2947 0.3515 0.3168 -0.0113 0.0270  -0.0140 208 THR   A CG2 
1540 N N   . ALA   A 209 ? 0.2554 0.3289 0.2711 -0.0106 0.0216  -0.0186 209 ALA   A N   
1541 C CA  . ALA   A 209 ? 0.2842 0.3638 0.2994 -0.0105 0.0202  -0.0212 209 ALA   A CA  
1542 C C   . ALA   A 209 ? 0.2818 0.3637 0.2982 -0.0105 0.0198  -0.0231 209 ALA   A C   
1543 O O   . ALA   A 209 ? 0.2486 0.3338 0.2627 -0.0095 0.0178  -0.0234 209 ALA   A O   
1544 C CB  . ALA   A 209 ? 0.2982 0.3813 0.3159 -0.0123 0.0218  -0.0245 209 ALA   A CB  
1545 N N   . GLU   A 210 ? 0.2749 0.3550 0.2948 -0.0119 0.0220  -0.0247 210 GLU   A N   
1546 C CA  . GLU   A 210 ? 0.2579 0.3405 0.2795 -0.0124 0.0220  -0.0271 210 GLU   A CA  
1547 C C   . GLU   A 210 ? 0.2572 0.3379 0.2760 -0.0106 0.0201  -0.0244 210 GLU   A C   
1548 O O   . GLU   A 210 ? 0.2319 0.3161 0.2494 -0.0103 0.0188  -0.0254 210 GLU   A O   
1549 C CB  . GLU   A 210 ? 0.2926 0.3731 0.3191 -0.0143 0.0250  -0.0295 210 GLU   A CB  
1550 C CG  . GLU   A 210 ? 0.3151 0.3985 0.3448 -0.0165 0.0271  -0.0331 210 GLU   A CG  
1551 C CD  . GLU   A 210 ? 0.3582 0.4379 0.3882 -0.0172 0.0287  -0.0317 210 GLU   A CD  
1552 O OE1 . GLU   A 210 ? 0.3090 0.3842 0.3362 -0.0159 0.0280  -0.0276 210 GLU   A OE1 
1553 O OE2 . GLU   A 210 ? 0.4218 0.5037 0.4551 -0.0194 0.0309  -0.0352 210 GLU   A OE2 
1554 N N   . ASP   A 211 ? 0.2200 0.2953 0.2377 -0.0095 0.0200  -0.0209 211 ASP   A N   
1555 C CA  . ASP   A 211 ? 0.2153 0.2890 0.2306 -0.0079 0.0183  -0.0185 211 ASP   A CA  
1556 C C   . ASP   A 211 ? 0.2125 0.2890 0.2235 -0.0067 0.0159  -0.0174 211 ASP   A C   
1557 O O   . ASP   A 211 ? 0.1976 0.2757 0.2071 -0.0062 0.0147  -0.0174 211 ASP   A O   
1558 C CB  . ASP   A 211 ? 0.2203 0.2886 0.2350 -0.0068 0.0184  -0.0149 211 ASP   A CB  
1559 C CG  . ASP   A 211 ? 0.2568 0.3211 0.2753 -0.0074 0.0206  -0.0150 211 ASP   A CG  
1560 O OD1 . ASP   A 211 ? 0.2851 0.3503 0.3068 -0.0083 0.0217  -0.0177 211 ASP   A OD1 
1561 O OD2 . ASP   A 211 ? 0.2803 0.3406 0.2983 -0.0069 0.0211  -0.0123 211 ASP   A OD2 
1562 N N   . ALA   A 212 ? 0.1853 0.2626 0.1947 -0.0064 0.0153  -0.0166 212 ALA   A N   
1563 C CA  . ALA   A 212 ? 0.2012 0.2806 0.2069 -0.0050 0.0131  -0.0154 212 ALA   A CA  
1564 C C   . ALA   A 212 ? 0.2045 0.2890 0.2097 -0.0052 0.0122  -0.0178 212 ALA   A C   
1565 O O   . ALA   A 212 ? 0.2041 0.2894 0.2062 -0.0042 0.0105  -0.0166 212 ALA   A O   
1566 C CB  . ALA   A 212 ? 0.1930 0.2726 0.1978 -0.0047 0.0128  -0.0147 212 ALA   A CB  
1567 N N   . GLN   A 213 ? 0.2174 0.3052 0.2255 -0.0067 0.0135  -0.0211 213 GLN   A N   
1568 C CA  . GLN   A 213 ? 0.2095 0.3028 0.2171 -0.0070 0.0127  -0.0236 213 GLN   A CA  
1569 C C   . GLN   A 213 ? 0.2030 0.2963 0.2097 -0.0070 0.0124  -0.0234 213 GLN   A C   
1570 O O   . GLN   A 213 ? 0.2208 0.3172 0.2247 -0.0064 0.0108  -0.0233 213 GLN   A O   
1571 C CB  . GLN   A 213 ? 0.2518 0.3485 0.2636 -0.0089 0.0146  -0.0276 213 GLN   A CB  
1572 C CG  . GLN   A 213 ? 0.2825 0.3861 0.2942 -0.0093 0.0139  -0.0307 213 GLN   A CG  
1573 C CD  . GLN   A 213 ? 0.3425 0.4498 0.3586 -0.0114 0.0160  -0.0351 213 GLN   A CD  
1574 O OE1 . GLN   A 213 ? 0.4000 0.5050 0.4199 -0.0131 0.0184  -0.0366 213 GLN   A OE1 
1575 N NE2 . GLN   A 213 ? 0.3713 0.4843 0.3874 -0.0113 0.0152  -0.0372 213 GLN   A NE2 
1576 N N   . LYS   A 214 ? 0.2212 0.3109 0.2302 -0.0077 0.0138  -0.0233 214 LYS   A N   
1577 C CA  . LYS   A 214 ? 0.2474 0.3373 0.2563 -0.0080 0.0138  -0.0237 214 LYS   A CA  
1578 C C   . LYS   A 214 ? 0.2155 0.3035 0.2200 -0.0065 0.0119  -0.0204 214 LYS   A C   
1579 O O   . LYS   A 214 ? 0.2012 0.2914 0.2034 -0.0065 0.0111  -0.0205 214 LYS   A O   
1580 C CB  . LYS   A 214 ? 0.2718 0.3582 0.2848 -0.0088 0.0158  -0.0243 214 LYS   A CB  
1581 C CG  . LYS   A 214 ? 0.3563 0.4434 0.3699 -0.0093 0.0159  -0.0254 214 LYS   A CG  
1582 C CD  . LYS   A 214 ? 0.4163 0.4986 0.4328 -0.0090 0.0170  -0.0245 214 LYS   A CD  
1583 C CE  . LYS   A 214 ? 0.4544 0.5348 0.4753 -0.0099 0.0192  -0.0261 214 LYS   A CE  
1584 N NZ  . LYS   A 214 ? 0.5332 0.6085 0.5567 -0.0092 0.0201  -0.0247 214 LYS   A NZ  
1585 N N   . TYR   A 215 ? 0.1997 0.2836 0.2031 -0.0053 0.0114  -0.0175 215 TYR   A N   
1586 C CA  . TYR   A 215 ? 0.1876 0.2695 0.1872 -0.0040 0.0099  -0.0146 215 TYR   A CA  
1587 C C   . TYR   A 215 ? 0.1717 0.2564 0.1677 -0.0032 0.0083  -0.0142 215 TYR   A C   
1588 O O   . TYR   A 215 ? 0.1822 0.2668 0.1754 -0.0029 0.0074  -0.0130 215 TYR   A O   
1589 C CB  . TYR   A 215 ? 0.1880 0.2657 0.1872 -0.0029 0.0097  -0.0120 215 TYR   A CB  
1590 C CG  . TYR   A 215 ? 0.2167 0.2911 0.2183 -0.0030 0.0108  -0.0114 215 TYR   A CG  
1591 C CD1 . TYR   A 215 ? 0.2140 0.2869 0.2145 -0.0025 0.0103  -0.0103 215 TYR   A CD1 
1592 C CD2 . TYR   A 215 ? 0.2438 0.3163 0.2486 -0.0035 0.0123  -0.0119 215 TYR   A CD2 
1593 C CE1 . TYR   A 215 ? 0.2043 0.2745 0.2071 -0.0023 0.0110  -0.0098 215 TYR   A CE1 
1594 C CE2 . TYR   A 215 ? 0.2493 0.3185 0.2561 -0.0032 0.0131  -0.0108 215 TYR   A CE2 
1595 C CZ  . TYR   A 215 ? 0.2562 0.3244 0.2620 -0.0024 0.0123  -0.0099 215 TYR   A CZ  
1596 O OH  . TYR   A 215 ? 0.2252 0.2906 0.2332 -0.0018 0.0128  -0.0090 215 TYR   A OH  
1597 N N   . LEU   A 216 ? 0.1716 0.2589 0.1677 -0.0030 0.0079  -0.0150 216 LEU   A N   
1598 C CA  . LEU   A 216 ? 0.1789 0.2690 0.1718 -0.0019 0.0061  -0.0145 216 LEU   A CA  
1599 C C   . LEU   A 216 ? 0.1796 0.2739 0.1717 -0.0027 0.0060  -0.0163 216 LEU   A C   
1600 O O   . LEU   A 216 ? 0.1900 0.2855 0.1785 -0.0018 0.0046  -0.0150 216 LEU   A O   
1601 C CB  . LEU   A 216 ? 0.1953 0.2879 0.1891 -0.0014 0.0058  -0.0156 216 LEU   A CB  
1602 C CG  . LEU   A 216 ? 0.2002 0.2895 0.1936 -0.0003 0.0054  -0.0134 216 LEU   A CG  
1603 C CD1 . LEU   A 216 ? 0.2393 0.3310 0.2348 -0.0006 0.0058  -0.0152 216 LEU   A CD1 
1604 C CD2 . LEU   A 216 ? 0.2005 0.2886 0.1900 0.0014  0.0035  -0.0109 216 LEU   A CD2 
1605 N N   . ALA   A 217 ? 0.1702 0.2669 0.1656 -0.0044 0.0075  -0.0194 217 ALA   A N   
1606 C CA  . ALA   A 217 ? 0.1941 0.2956 0.1890 -0.0054 0.0075  -0.0215 217 ALA   A CA  
1607 C C   . ALA   A 217 ? 0.2183 0.3180 0.2104 -0.0055 0.0072  -0.0199 217 ALA   A C   
1608 O O   . ALA   A 217 ? 0.2226 0.3253 0.2116 -0.0055 0.0064  -0.0198 217 ALA   A O   
1609 C CB  . ALA   A 217 ? 0.1887 0.2926 0.1884 -0.0074 0.0096  -0.0254 217 ALA   A CB  
1610 N N   . ILE   A 218 ? 0.2045 0.2993 0.1975 -0.0055 0.0079  -0.0185 218 ILE   A N   
1611 C CA  . ILE   A 218 ? 0.2208 0.3141 0.2115 -0.0057 0.0078  -0.0172 218 ILE   A CA  
1612 C C   . ILE   A 218 ? 0.2037 0.2964 0.1892 -0.0044 0.0060  -0.0143 218 ILE   A C   
1613 O O   . ILE   A 218 ? 0.2125 0.3065 0.1948 -0.0048 0.0057  -0.0138 218 ILE   A O   
1614 C CB  . ILE   A 218 ? 0.2074 0.2959 0.2001 -0.0056 0.0086  -0.0162 218 ILE   A CB  
1615 C CG1 . ILE   A 218 ? 0.2058 0.2946 0.2036 -0.0068 0.0104  -0.0189 218 ILE   A CG1 
1616 C CG2 . ILE   A 218 ? 0.2361 0.3232 0.2262 -0.0058 0.0084  -0.0149 218 ILE   A CG2 
1617 C CD1 . ILE   A 218 ? 0.2264 0.3106 0.2268 -0.0062 0.0110  -0.0178 218 ILE   A CD1 
1618 N N   . ALA   A 219 ? 0.1953 0.2856 0.1798 -0.0028 0.0051  -0.0122 219 ALA   A N   
1619 C CA  . ALA   A 219 ? 0.1983 0.2871 0.1784 -0.0013 0.0036  -0.0095 219 ALA   A CA  
1620 C C   . ALA   A 219 ? 0.2059 0.2994 0.1835 -0.0009 0.0024  -0.0099 219 ALA   A C   
1621 O O   . ALA   A 219 ? 0.2099 0.3030 0.1834 -0.0005 0.0016  -0.0080 219 ALA   A O   
1622 C CB  . ALA   A 219 ? 0.2203 0.3064 0.2010 0.0002  0.0029  -0.0079 219 ALA   A CB  
1623 N N   . ASP   A 220 ? 0.1986 0.2963 0.1786 -0.0010 0.0024  -0.0123 220 ASP   A N   
1624 C CA  . ASP   A 220 ? 0.2205 0.3237 0.1986 -0.0006 0.0013  -0.0133 220 ASP   A CA  
1625 C C   . ASP   A 220 ? 0.2383 0.3441 0.2140 -0.0019 0.0016  -0.0138 220 ASP   A C   
1626 O O   . ASP   A 220 ? 0.2178 0.3257 0.1893 -0.0010 0.0002  -0.0123 220 ASP   A O   
1627 C CB  . ASP   A 220 ? 0.2208 0.3285 0.2027 -0.0009 0.0016  -0.0165 220 ASP   A CB  
1628 C CG  . ASP   A 220 ? 0.2284 0.3346 0.2119 0.0005  0.0011  -0.0159 220 ASP   A CG  
1629 O OD1 . ASP   A 220 ? 0.2085 0.3104 0.1898 0.0020  0.0002  -0.0129 220 ASP   A OD1 
1630 O OD2 . ASP   A 220 ? 0.2623 0.3716 0.2493 -0.0002 0.0018  -0.0188 220 ASP   A OD2 
1631 N N   . GLU   A 221 ? 0.2467 0.3527 0.2253 -0.0040 0.0034  -0.0160 221 GLU   A N   
1632 C CA  . GLU   A 221 ? 0.2599 0.3690 0.2370 -0.0056 0.0040  -0.0173 221 GLU   A CA  
1633 C C   . GLU   A 221 ? 0.2686 0.3739 0.2411 -0.0055 0.0037  -0.0141 221 GLU   A C   
1634 O O   . GLU   A 221 ? 0.2711 0.3791 0.2398 -0.0060 0.0033  -0.0136 221 GLU   A O   
1635 C CB  . GLU   A 221 ? 0.2995 0.4091 0.2817 -0.0077 0.0061  -0.0207 221 GLU   A CB  
1636 C CG  . GLU   A 221 ? 0.4079 0.5222 0.3944 -0.0083 0.0067  -0.0244 221 GLU   A CG  
1637 C CD  . GLU   A 221 ? 0.5319 0.6453 0.5244 -0.0099 0.0089  -0.0275 221 GLU   A CD  
1638 O OE1 . GLU   A 221 ? 0.5703 0.6801 0.5643 -0.0105 0.0099  -0.0272 221 GLU   A OE1 
1639 O OE2 . GLU   A 221 ? 0.5795 0.6960 0.5755 -0.0105 0.0096  -0.0303 221 GLU   A OE2 
1640 N N   . LEU   A 222 ? 0.2177 0.3171 0.1904 -0.0049 0.0039  -0.0119 222 LEU   A N   
1641 C CA  . LEU   A 222 ? 0.2225 0.3182 0.1914 -0.0050 0.0039  -0.0093 222 LEU   A CA  
1642 C C   . LEU   A 222 ? 0.2145 0.3088 0.1785 -0.0031 0.0022  -0.0060 222 LEU   A C   
1643 O O   . LEU   A 222 ? 0.2585 0.3520 0.2183 -0.0035 0.0022  -0.0041 222 LEU   A O   
1644 C CB  . LEU   A 222 ? 0.2151 0.3056 0.1864 -0.0050 0.0047  -0.0086 222 LEU   A CB  
1645 C CG  . LEU   A 222 ? 0.2245 0.3154 0.1994 -0.0068 0.0064  -0.0111 222 LEU   A CG  
1646 C CD1 . LEU   A 222 ? 0.2286 0.3147 0.2058 -0.0061 0.0067  -0.0100 222 LEU   A CD1 
1647 C CD2 . LEU   A 222 ? 0.2490 0.3410 0.2212 -0.0085 0.0071  -0.0114 222 LEU   A CD2 
1648 N N   . PHE   A 223 ? 0.1980 0.2918 0.1627 -0.0010 0.0009  -0.0050 223 PHE   A N   
1649 C CA  . PHE   A 223 ? 0.2161 0.3070 0.1767 0.0010  -0.0005 -0.0016 223 PHE   A CA  
1650 C C   . PHE   A 223 ? 0.2414 0.3366 0.2009 0.0029  -0.0023 -0.0016 223 PHE   A C   
1651 O O   . PHE   A 223 ? 0.2592 0.3524 0.2156 0.0049  -0.0037 0.0012  223 PHE   A O   
1652 C CB  . PHE   A 223 ? 0.2363 0.3219 0.1984 0.0022  -0.0006 0.0000  223 PHE   A CB  
1653 C CG  . PHE   A 223 ? 0.2340 0.3156 0.1970 0.0007  0.0009  0.0001  223 PHE   A CG  
1654 C CD1 . PHE   A 223 ? 0.2599 0.3391 0.2195 -0.0002 0.0015  0.0017  223 PHE   A CD1 
1655 C CD2 . PHE   A 223 ? 0.2299 0.3104 0.1972 0.0002  0.0018  -0.0014 223 PHE   A CD2 
1656 C CE1 . PHE   A 223 ? 0.2604 0.3367 0.2212 -0.0016 0.0029  0.0014  223 PHE   A CE1 
1657 C CE2 . PHE   A 223 ? 0.2534 0.3311 0.2217 -0.0010 0.0030  -0.0015 223 PHE   A CE2 
1658 C CZ  . PHE   A 223 ? 0.2381 0.3140 0.2033 -0.0019 0.0036  -0.0003 223 PHE   A CZ  
1659 N N   . GLY   A 224 ? 0.2409 0.3418 0.2032 0.0023  -0.0023 -0.0048 224 GLY   A N   
1660 C CA  . GLY   A 224 ? 0.2544 0.3600 0.2167 0.0041  -0.0040 -0.0055 224 GLY   A CA  
1661 C C   . GLY   A 224 ? 0.2724 0.3768 0.2388 0.0051  -0.0041 -0.0064 224 GLY   A C   
1662 O O   . GLY   A 224 ? 0.2468 0.3458 0.2144 0.0052  -0.0034 -0.0052 224 GLY   A O   
1663 N N   . ALA   A 225 ? 0.2993 0.4090 0.2675 0.0060  -0.0050 -0.0085 225 ALA   A N   
1664 C CA  . ALA   A 225 ? 0.2909 0.4010 0.2634 0.0063  -0.0047 -0.0104 225 ALA   A CA  
1665 C C   . ALA   A 225 ? 0.2851 0.3914 0.2569 0.0087  -0.0060 -0.0079 225 ALA   A C   
1666 O O   . ALA   A 225 ? 0.2777 0.3827 0.2527 0.0086  -0.0054 -0.0089 225 ALA   A O   
1667 C CB  . ALA   A 225 ? 0.2918 0.4096 0.2665 0.0061  -0.0051 -0.0140 225 ALA   A CB  
1668 N N   . ASP   A 226 ? 0.2640 0.3678 0.2315 0.0105  -0.0074 -0.0046 226 ASP   A N   
1669 C CA  . ASP   A 226 ? 0.3060 0.4062 0.2732 0.0129  -0.0085 -0.0024 226 ASP   A CA  
1670 C C   . ASP   A 226 ? 0.2793 0.3723 0.2461 0.0122  -0.0073 -0.0003 226 ASP   A C   
1671 O O   . ASP   A 226 ? 0.2739 0.3636 0.2412 0.0136  -0.0078 0.0009  226 ASP   A O   
1672 C CB  . ASP   A 226 ? 0.3430 0.4438 0.3060 0.0156  -0.0107 0.0002  226 ASP   A CB  
1673 C CG  . ASP   A 226 ? 0.4504 0.5590 0.4136 0.0168  -0.0123 -0.0018 226 ASP   A CG  
1674 O OD1 . ASP   A 226 ? 0.4867 0.5991 0.4539 0.0167  -0.0122 -0.0049 226 ASP   A OD1 
1675 O OD2 . ASP   A 226 ? 0.5935 0.7045 0.5528 0.0177  -0.0135 -0.0004 226 ASP   A OD2 
1676 N N   . TRP   A 227 ? 0.2476 0.3387 0.2139 0.0100  -0.0058 -0.0004 227 TRP   A N   
1677 C CA  . TRP   A 227 ? 0.2353 0.3203 0.2010 0.0095  -0.0048 0.0016  227 TRP   A CA  
1678 C C   . TRP   A 227 ? 0.2178 0.3006 0.1871 0.0093  -0.0041 0.0008  227 TRP   A C   
1679 O O   . TRP   A 227 ? 0.1888 0.2674 0.1576 0.0101  -0.0042 0.0025  227 TRP   A O   
1680 C CB  . TRP   A 227 ? 0.2214 0.3055 0.1861 0.0072  -0.0034 0.0014  227 TRP   A CB  
1681 C CG  . TRP   A 227 ? 0.2166 0.2951 0.1806 0.0066  -0.0024 0.0031  227 TRP   A CG  
1682 C CD1 . TRP   A 227 ? 0.2007 0.2749 0.1614 0.0073  -0.0027 0.0058  227 TRP   A CD1 
1683 C CD2 . TRP   A 227 ? 0.2178 0.2943 0.1848 0.0051  -0.0010 0.0020  227 TRP   A CD2 
1684 N NE1 . TRP   A 227 ? 0.2096 0.2799 0.1712 0.0062  -0.0014 0.0062  227 TRP   A NE1 
1685 C CE2 . TRP   A 227 ? 0.2051 0.2769 0.1705 0.0050  -0.0005 0.0040  227 TRP   A CE2 
1686 C CE3 . TRP   A 227 ? 0.2127 0.2908 0.1836 0.0040  0.0000  -0.0003 227 TRP   A CE3 
1687 C CZ2 . TRP   A 227 ? 0.1951 0.2646 0.1625 0.0039  0.0007  0.0034  227 TRP   A CZ2 
1688 C CZ3 . TRP   A 227 ? 0.2073 0.2826 0.1801 0.0031  0.0011  -0.0004 227 TRP   A CZ3 
1689 C CH2 . TRP   A 227 ? 0.2028 0.2742 0.1737 0.0031  0.0013  0.0014  227 TRP   A CH2 
1690 N N   . ALA   A 228 ? 0.2104 0.2958 0.1832 0.0080  -0.0032 -0.0018 228 ALA   A N   
1691 C CA  . ALA   A 228 ? 0.2146 0.2979 0.1905 0.0074  -0.0021 -0.0024 228 ALA   A CA  
1692 C C   . ALA   A 228 ? 0.2028 0.2865 0.1801 0.0089  -0.0029 -0.0026 228 ALA   A C   
1693 O O   . ALA   A 228 ? 0.1974 0.2836 0.1777 0.0083  -0.0024 -0.0047 228 ALA   A O   
1694 C CB  . ALA   A 228 ? 0.2286 0.3142 0.2075 0.0055  -0.0008 -0.0050 228 ALA   A CB  
1695 N N   . ASP   A 229 ? 0.1958 0.2770 0.1712 0.0107  -0.0040 -0.0007 229 ASP   A N   
1696 C CA  . ASP   A 229 ? 0.1980 0.2791 0.1750 0.0120  -0.0046 -0.0009 229 ASP   A CA  
1697 C C   . ASP   A 229 ? 0.1770 0.2542 0.1549 0.0112  -0.0035 -0.0002 229 ASP   A C   
1698 O O   . ASP   A 229 ? 0.1806 0.2557 0.1583 0.0097  -0.0024 0.0003  229 ASP   A O   
1699 C CB  . ASP   A 229 ? 0.2219 0.3025 0.1967 0.0145  -0.0063 0.0007  229 ASP   A CB  
1700 C CG  . ASP   A 229 ? 0.2420 0.3175 0.2138 0.0150  -0.0063 0.0035  229 ASP   A CG  
1701 O OD1 . ASP   A 229 ? 0.2320 0.3044 0.2035 0.0133  -0.0050 0.0040  229 ASP   A OD1 
1702 O OD2 . ASP   A 229 ? 0.2699 0.3444 0.2394 0.0170  -0.0077 0.0052  229 ASP   A OD2 
1703 N N   . ALA   A 230 ? 0.1705 0.2472 0.1498 0.0121  -0.0037 -0.0004 230 ALA   A N   
1704 C CA  . ALA   A 230 ? 0.1814 0.2556 0.1618 0.0112  -0.0026 -0.0002 230 ALA   A CA  
1705 C C   . ALA   A 230 ? 0.1857 0.2557 0.1641 0.0113  -0.0025 0.0018  230 ALA   A C   
1706 O O   . ALA   A 230 ? 0.1707 0.2389 0.1497 0.0103  -0.0016 0.0019  230 ALA   A O   
1707 C CB  . ALA   A 230 ? 0.1881 0.2635 0.1705 0.0119  -0.0028 -0.0012 230 ALA   A CB  
1708 N N   . ARG   A 231 ? 0.1773 0.2457 0.1533 0.0124  -0.0033 0.0032  231 ARG   A N   
1709 C CA  . ARG   A 231 ? 0.1912 0.2556 0.1653 0.0120  -0.0028 0.0048  231 ARG   A CA  
1710 C C   . ARG   A 231 ? 0.1961 0.2602 0.1692 0.0103  -0.0019 0.0049  231 ARG   A C   
1711 O O   . ARG   A 231 ? 0.2151 0.2763 0.1873 0.0094  -0.0010 0.0057  231 ARG   A O   
1712 C CB  . ARG   A 231 ? 0.1953 0.2573 0.1672 0.0138  -0.0038 0.0064  231 ARG   A CB  
1713 C CG  . ARG   A 231 ? 0.1950 0.2525 0.1647 0.0132  -0.0029 0.0081  231 ARG   A CG  
1714 C CD  . ARG   A 231 ? 0.1944 0.2498 0.1658 0.0125  -0.0019 0.0076  231 ARG   A CD  
1715 N NE  . ARG   A 231 ? 0.2007 0.2522 0.1704 0.0116  -0.0009 0.0087  231 ARG   A NE  
1716 C CZ  . ARG   A 231 ? 0.1819 0.2329 0.1506 0.0097  0.0001  0.0087  231 ARG   A CZ  
1717 N NH1 . ARG   A 231 ? 0.1746 0.2285 0.1442 0.0087  0.0003  0.0077  231 ARG   A NH1 
1718 N NH2 . ARG   A 231 ? 0.1944 0.2419 0.1617 0.0089  0.0012  0.0094  231 ARG   A NH2 
1719 N N   . HIS   A 232 ? 0.1656 0.2327 0.1391 0.0095  -0.0018 0.0039  232 HIS   A N   
1720 C CA  . HIS   A 232 ? 0.1719 0.2390 0.1445 0.0079  -0.0010 0.0038  232 HIS   A CA  
1721 C C   . HIS   A 232 ? 0.1570 0.2260 0.1323 0.0065  0.0000  0.0021  232 HIS   A C   
1722 O O   . HIS   A 232 ? 0.1512 0.2201 0.1265 0.0052  0.0008  0.0017  232 HIS   A O   
1723 C CB  . HIS   A 232 ? 0.1730 0.2417 0.1430 0.0082  -0.0017 0.0042  232 HIS   A CB  
1724 C CG  . HIS   A 232 ? 0.1891 0.2548 0.1561 0.0095  -0.0023 0.0064  232 HIS   A CG  
1725 N ND1 . HIS   A 232 ? 0.1875 0.2533 0.1541 0.0117  -0.0037 0.0072  232 HIS   A ND1 
1726 C CD2 . HIS   A 232 ? 0.1794 0.2418 0.1439 0.0089  -0.0017 0.0080  232 HIS   A CD2 
1727 C CE1 . HIS   A 232 ? 0.1990 0.2611 0.1629 0.0125  -0.0039 0.0094  232 HIS   A CE1 
1728 N NE2 . HIS   A 232 ? 0.1983 0.2581 0.1607 0.0107  -0.0026 0.0099  232 HIS   A NE2 
1729 N N   . TYR   A 233 ? 0.1413 0.2119 0.1191 0.0067  0.0000  0.0010  233 TYR   A N   
1730 C CA  . TYR   A 233 ? 0.1377 0.2097 0.1181 0.0054  0.0011  -0.0004 233 TYR   A CA  
1731 C C   . TYR   A 233 ? 0.1453 0.2170 0.1277 0.0056  0.0014  -0.0007 233 TYR   A C   
1732 O O   . TYR   A 233 ? 0.1438 0.2167 0.1264 0.0065  0.0008  -0.0010 233 TYR   A O   
1733 C CB  . TYR   A 233 ? 0.1522 0.2278 0.1332 0.0050  0.0011  -0.0021 233 TYR   A CB  
1734 C CG  . TYR   A 233 ? 0.1621 0.2383 0.1454 0.0034  0.0024  -0.0035 233 TYR   A CG  
1735 C CD1 . TYR   A 233 ? 0.1814 0.2573 0.1675 0.0028  0.0034  -0.0043 233 TYR   A CD1 
1736 C CD2 . TYR   A 233 ? 0.1831 0.2601 0.1657 0.0025  0.0027  -0.0040 233 TYR   A CD2 
1737 C CE1 . TYR   A 233 ? 0.1986 0.2746 0.1870 0.0015  0.0047  -0.0056 233 TYR   A CE1 
1738 C CE2 . TYR   A 233 ? 0.1827 0.2603 0.1678 0.0011  0.0040  -0.0056 233 TYR   A CE2 
1739 C CZ  . TYR   A 233 ? 0.2038 0.2808 0.1920 0.0007  0.0050  -0.0063 233 TYR   A CZ  
1740 O OH  . TYR   A 233 ? 0.2097 0.2867 0.2006 -0.0005 0.0063  -0.0078 233 TYR   A OH  
1741 N N   . ARG   A 234 ? 0.1216 0.1920 0.1054 0.0047  0.0025  -0.0006 234 ARG   A N   
1742 C CA  . ARG   A 234 ? 0.1283 0.1986 0.1139 0.0045  0.0030  -0.0007 234 ARG   A CA  
1743 C C   . ARG   A 234 ? 0.1419 0.2118 0.1295 0.0034  0.0043  -0.0012 234 ARG   A C   
1744 O O   . ARG   A 234 ? 0.1417 0.2109 0.1295 0.0029  0.0047  -0.0012 234 ARG   A O   
1745 C CB  . ARG   A 234 ? 0.1262 0.1946 0.1109 0.0051  0.0028  0.0006  234 ARG   A CB  
1746 C CG  . ARG   A 234 ? 0.1275 0.1956 0.1106 0.0062  0.0018  0.0010  234 ARG   A CG  
1747 C CD  . ARG   A 234 ? 0.1220 0.1922 0.1060 0.0069  0.0013  0.0001  234 ARG   A CD  
1748 N NE  . ARG   A 234 ? 0.1269 0.1962 0.1095 0.0082  0.0003  0.0006  234 ARG   A NE  
1749 C CZ  . ARG   A 234 ? 0.1394 0.2070 0.1217 0.0085  0.0003  0.0013  234 ARG   A CZ  
1750 N NH1 . ARG   A 234 ? 0.1547 0.2221 0.1377 0.0078  0.0011  0.0013  234 ARG   A NH1 
1751 N NH2 . ARG   A 234 ? 0.1486 0.2147 0.1297 0.0096  -0.0003 0.0018  234 ARG   A NH2 
1752 N N   . PHE   A 235 ? 0.1443 0.2146 0.1335 0.0030  0.0050  -0.0015 235 PHE   A N   
1753 C CA  . PHE   A 235 ? 0.1448 0.2139 0.1359 0.0021  0.0064  -0.0016 235 PHE   A CA  
1754 C C   . PHE   A 235 ? 0.1645 0.2322 0.1555 0.0022  0.0068  -0.0001 235 PHE   A C   
1755 O O   . PHE   A 235 ? 0.1473 0.2160 0.1377 0.0025  0.0065  -0.0002 235 PHE   A O   
1756 C CB  . PHE   A 235 ? 0.1593 0.2301 0.1526 0.0011  0.0075  -0.0034 235 PHE   A CB  
1757 C CG  . PHE   A 235 ? 0.1794 0.2523 0.1736 0.0005  0.0075  -0.0053 235 PHE   A CG  
1758 C CD1 . PHE   A 235 ? 0.1924 0.2644 0.1884 -0.0003 0.0085  -0.0059 235 PHE   A CD1 
1759 C CD2 . PHE   A 235 ? 0.1853 0.2614 0.1788 0.0009  0.0066  -0.0066 235 PHE   A CD2 
1760 C CE1 . PHE   A 235 ? 0.2138 0.2883 0.2107 -0.0009 0.0087  -0.0080 235 PHE   A CE1 
1761 C CE2 . PHE   A 235 ? 0.2058 0.2844 0.1999 0.0003  0.0067  -0.0085 235 PHE   A CE2 
1762 C CZ  . PHE   A 235 ? 0.2042 0.2821 0.2001 -0.0007 0.0078  -0.0093 235 PHE   A CZ  
1763 N N   . SER   A 236 ? 0.1846 0.2503 0.1763 0.0021  0.0074  0.0010  236 SER   A N   
1764 C CA  A SER   A 236 ? 0.1800 0.2444 0.1716 0.0021  0.0080  0.0025  236 SER   A CA  
1765 C CA  B SER   A 236 ? 0.1839 0.2484 0.1756 0.0020  0.0081  0.0024  236 SER   A CA  
1766 C CA  C SER   A 236 ? 0.1859 0.2503 0.1776 0.0021  0.0081  0.0025  236 SER   A CA  
1767 C C   . SER   A 236 ? 0.1917 0.2540 0.1852 0.0017  0.0093  0.0030  236 SER   A C   
1768 O O   . SER   A 236 ? 0.1883 0.2497 0.1825 0.0021  0.0091  0.0031  236 SER   A O   
1769 C CB  A SER   A 236 ? 0.1819 0.2459 0.1716 0.0030  0.0071  0.0041  236 SER   A CB  
1770 C CB  B SER   A 236 ? 0.1909 0.2552 0.1807 0.0029  0.0072  0.0040  236 SER   A CB  
1771 C CB  C SER   A 236 ? 0.2069 0.2711 0.1967 0.0030  0.0071  0.0039  236 SER   A CB  
1772 O OG  A SER   A 236 ? 0.1683 0.2338 0.1566 0.0035  0.0061  0.0036  236 SER   A OG  
1773 O OG  B SER   A 236 ? 0.1869 0.2499 0.1767 0.0035  0.0069  0.0049  236 SER   A OG  
1774 O OG  C SER   A 236 ? 0.2105 0.2737 0.2000 0.0030  0.0077  0.0055  236 SER   A OG  
1775 N N   . ALA   A 237 ? 0.2120 0.2734 0.2064 0.0009  0.0106  0.0034  237 ALA   A N   
1776 C CA  . ALA   A 237 ? 0.2464 0.3050 0.2425 0.0006  0.0119  0.0043  237 ALA   A CA  
1777 C C   . ALA   A 237 ? 0.2718 0.3293 0.2680 -0.0004 0.0135  0.0052  237 ALA   A C   
1778 O O   . ALA   A 237 ? 0.2473 0.3064 0.2438 -0.0015 0.0141  0.0035  237 ALA   A O   
1779 C CB  . ALA   A 237 ? 0.2731 0.3316 0.2720 0.0000  0.0127  0.0023  237 ALA   A CB  
1780 N N   . SER   A 238 ? 0.2908 0.3455 0.2868 0.0001  0.0141  0.0076  238 SER   A N   
1781 C CA  A SER   A 238 ? 0.2906 0.3435 0.2863 -0.0010 0.0158  0.0089  238 SER   A CA  
1782 C CA  B SER   A 238 ? 0.2998 0.3526 0.2955 -0.0010 0.0158  0.0089  238 SER   A CA  
1783 C C   . SER   A 238 ? 0.2730 0.3251 0.2717 -0.0027 0.0178  0.0067  238 SER   A C   
1784 O O   . SER   A 238 ? 0.2897 0.3406 0.2908 -0.0027 0.0183  0.0055  238 SER   A O   
1785 C CB  A SER   A 238 ? 0.3123 0.3619 0.3072 0.0001  0.0160  0.0121  238 SER   A CB  
1786 C CB  B SER   A 238 ? 0.3331 0.3826 0.3281 0.0001  0.0161  0.0122  238 SER   A CB  
1787 O OG  A SER   A 238 ? 0.3175 0.3646 0.3151 0.0006  0.0165  0.0119  238 SER   A OG  
1788 O OG  B SER   A 238 ? 0.3667 0.4177 0.3588 0.0013  0.0144  0.0140  238 SER   A OG  
1789 N N   . GLY   A 239 ? 0.2707 0.3239 0.2691 -0.0043 0.0190  0.0057  239 GLY   A N   
1790 C CA  . GLY   A 239 ? 0.2447 0.2973 0.2460 -0.0062 0.0213  0.0034  239 GLY   A CA  
1791 C C   . GLY   A 239 ? 0.2474 0.3042 0.2504 -0.0068 0.0207  -0.0004 239 GLY   A C   
1792 O O   . GLY   A 239 ? 0.2281 0.2860 0.2334 -0.0086 0.0224  -0.0029 239 GLY   A O   
1793 N N   . LEU   A 240 ? 0.2109 0.2701 0.2127 -0.0053 0.0184  -0.0008 240 LEU   A N   
1794 C CA  . LEU   A 240 ? 0.2004 0.2634 0.2036 -0.0056 0.0178  -0.0040 240 LEU   A CA  
1795 C C   . LEU   A 240 ? 0.2087 0.2752 0.2117 -0.0065 0.0179  -0.0059 240 LEU   A C   
1796 O O   . LEU   A 240 ? 0.2062 0.2754 0.2113 -0.0076 0.0187  -0.0090 240 LEU   A O   
1797 C CB  . LEU   A 240 ? 0.2026 0.2669 0.2042 -0.0039 0.0155  -0.0036 240 LEU   A CB  
1798 C CG  . LEU   A 240 ? 0.2018 0.2701 0.2038 -0.0039 0.0145  -0.0063 240 LEU   A CG  
1799 C CD1 . LEU   A 240 ? 0.2108 0.2797 0.2159 -0.0053 0.0160  -0.0089 240 LEU   A CD1 
1800 C CD2 . LEU   A 240 ? 0.2139 0.2830 0.2138 -0.0024 0.0124  -0.0056 240 LEU   A CD2 
1801 N N   . LEU   A 241 ? 0.2049 0.2720 0.2056 -0.0060 0.0172  -0.0045 241 LEU   A N   
1802 C CA  . LEU   A 241 ? 0.2076 0.2785 0.2084 -0.0066 0.0172  -0.0067 241 LEU   A CA  
1803 C C   . LEU   A 241 ? 0.2127 0.2840 0.2161 -0.0090 0.0198  -0.0088 241 LEU   A C   
1804 O O   . LEU   A 241 ? 0.2052 0.2805 0.2105 -0.0097 0.0200  -0.0121 241 LEU   A O   
1805 C CB  . LEU   A 241 ? 0.2094 0.2809 0.2078 -0.0059 0.0162  -0.0052 241 LEU   A CB  
1806 C CG  . LEU   A 241 ? 0.2062 0.2819 0.2051 -0.0065 0.0162  -0.0076 241 LEU   A CG  
1807 C CD1 . LEU   A 241 ? 0.2187 0.2980 0.2184 -0.0054 0.0145  -0.0100 241 LEU   A CD1 
1808 C CD2 . LEU   A 241 ? 0.2204 0.2965 0.2171 -0.0059 0.0155  -0.0063 241 LEU   A CD2 
1809 N N   . ALA   A 242 ? 0.2353 0.3026 0.2388 -0.0101 0.0218  -0.0069 242 ALA   A N   
1810 C CA  . ALA   A 242 ? 0.2667 0.3332 0.2725 -0.0126 0.0247  -0.0085 242 ALA   A CA  
1811 C C   . ALA   A 242 ? 0.2675 0.3353 0.2768 -0.0135 0.0256  -0.0117 242 ALA   A C   
1812 O O   . ALA   A 242 ? 0.2640 0.3347 0.2757 -0.0153 0.0271  -0.0151 242 ALA   A O   
1813 C CB  . ALA   A 242 ? 0.2535 0.3145 0.2584 -0.0132 0.0266  -0.0052 242 ALA   A CB  
1814 N N   . SER   A 243 ? 0.2490 0.3156 0.2587 -0.0122 0.0245  -0.0112 243 SER   A N   
1815 C CA  . SER   A 243 ? 0.2290 0.2971 0.2421 -0.0131 0.0254  -0.0143 243 SER   A CA  
1816 C C   . SER   A 243 ? 0.2145 0.2891 0.2280 -0.0129 0.0239  -0.0177 243 SER   A C   
1817 O O   . SER   A 243 ? 0.2305 0.3082 0.2469 -0.0145 0.0252  -0.0214 243 SER   A O   
1818 C CB  . SER   A 243 ? 0.2242 0.2896 0.2376 -0.0118 0.0246  -0.0130 243 SER   A CB  
1819 O OG  . SER   A 243 ? 0.2306 0.2977 0.2473 -0.0129 0.0256  -0.0163 243 SER   A OG  
1820 N N   . LEU   A 244 ? 0.2066 0.2832 0.2172 -0.0108 0.0211  -0.0165 244 LEU   A N   
1821 C CA  . LEU   A 244 ? 0.1942 0.2767 0.2047 -0.0101 0.0194  -0.0191 244 LEU   A CA  
1822 C C   . LEU   A 244 ? 0.2142 0.3003 0.2263 -0.0115 0.0205  -0.0218 244 LEU   A C   
1823 O O   . LEU   A 244 ? 0.2347 0.3257 0.2488 -0.0122 0.0206  -0.0254 244 LEU   A O   
1824 C CB  . LEU   A 244 ? 0.1812 0.2637 0.1882 -0.0076 0.0165  -0.0166 244 LEU   A CB  
1825 C CG  . LEU   A 244 ? 0.1874 0.2675 0.1930 -0.0063 0.0153  -0.0147 244 LEU   A CG  
1826 C CD1 . LEU   A 244 ? 0.1829 0.2631 0.1853 -0.0042 0.0128  -0.0126 244 LEU   A CD1 
1827 C CD2 . LEU   A 244 ? 0.1945 0.2773 0.2018 -0.0067 0.0152  -0.0172 244 LEU   A CD2 
1828 N N   . LEU   A 245 ? 0.2192 0.3032 0.2302 -0.0121 0.0214  -0.0203 245 LEU   A N   
1829 C CA  . LEU   A 245 ? 0.2366 0.3242 0.2490 -0.0136 0.0226  -0.0229 245 LEU   A CA  
1830 C C   . LEU   A 245 ? 0.2377 0.3260 0.2538 -0.0164 0.0256  -0.0261 245 LEU   A C   
1831 O O   . LEU   A 245 ? 0.2470 0.3408 0.2654 -0.0173 0.0260  -0.0300 245 LEU   A O   
1832 C CB  . LEU   A 245 ? 0.2285 0.3135 0.2388 -0.0139 0.0232  -0.0204 245 LEU   A CB  
1833 C CG  . LEU   A 245 ? 0.2278 0.3140 0.2353 -0.0114 0.0204  -0.0187 245 LEU   A CG  
1834 C CD1 . LEU   A 245 ? 0.2266 0.3102 0.2321 -0.0120 0.0212  -0.0163 245 LEU   A CD1 
1835 C CD2 . LEU   A 245 ? 0.2287 0.3211 0.2372 -0.0105 0.0187  -0.0219 245 LEU   A CD2 
1836 N N   . LYS   A 246 ? 0.2845 0.3676 0.3014 -0.0175 0.0276  -0.0246 246 LYS   A N   
1837 C CA  . LYS   A 246 ? 0.3197 0.4024 0.3404 -0.0202 0.0308  -0.0274 246 LYS   A CA  
1838 C C   . LYS   A 246 ? 0.3097 0.3979 0.3330 -0.0202 0.0301  -0.0316 246 LYS   A C   
1839 O O   . LYS   A 246 ? 0.3104 0.4025 0.3369 -0.0223 0.0319  -0.0357 246 LYS   A O   
1840 C CB  . LYS   A 246 ? 0.3783 0.4536 0.3992 -0.0208 0.0327  -0.0244 246 LYS   A CB  
1841 C CG  . LYS   A 246 ? 0.4393 0.5135 0.4644 -0.0237 0.0362  -0.0275 246 LYS   A CG  
1842 C CD  . LYS   A 246 ? 0.4883 0.5547 0.5142 -0.0243 0.0386  -0.0245 246 LYS   A CD  
1843 C CE  . LYS   A 246 ? 0.5466 0.6130 0.5775 -0.0271 0.0418  -0.0286 246 LYS   A CE  
1844 N NZ  . LYS   A 246 ? 0.5791 0.6387 0.6115 -0.0270 0.0434  -0.0264 246 LYS   A NZ  
1845 N N   . ALA   A 247 ? 0.2864 0.3754 0.3084 -0.0180 0.0275  -0.0306 247 ALA   A N   
1846 C CA  . ALA   A 247 ? 0.2927 0.3874 0.3165 -0.0179 0.0266  -0.0343 247 ALA   A CA  
1847 C C   . ALA   A 247 ? 0.3133 0.4152 0.3373 -0.0176 0.0253  -0.0374 247 ALA   A C   
1848 O O   . ALA   A 247 ? 0.3056 0.4134 0.3324 -0.0186 0.0257  -0.0416 247 ALA   A O   
1849 C CB  . ALA   A 247 ? 0.2843 0.3783 0.3059 -0.0157 0.0241  -0.0322 247 ALA   A CB  
1850 N N   . LEU   A 248 ? 0.3199 0.4220 0.3415 -0.0162 0.0238  -0.0354 248 LEU   A N   
1851 C CA  . LEU   A 248 ? 0.3166 0.4253 0.3382 -0.0153 0.0221  -0.0379 248 LEU   A CA  
1852 C C   . LEU   A 248 ? 0.3340 0.4448 0.3583 -0.0178 0.0247  -0.0409 248 LEU   A C   
1853 O O   . LEU   A 248 ? 0.3406 0.4572 0.3656 -0.0172 0.0237  -0.0434 248 LEU   A O   
1854 C CB  . LEU   A 248 ? 0.3049 0.4128 0.3228 -0.0123 0.0191  -0.0346 248 LEU   A CB  
1855 C CG  . LEU   A 248 ? 0.3001 0.4072 0.3155 -0.0099 0.0165  -0.0324 248 LEU   A CG  
1856 C CD1 . LEU   A 248 ? 0.2915 0.3956 0.3033 -0.0075 0.0143  -0.0285 248 LEU   A CD1 
1857 C CD2 . LEU   A 248 ? 0.2908 0.4049 0.3068 -0.0087 0.0146  -0.0354 248 LEU   A CD2 
1858 N N   . GLY   A 249 ? 0.3935 0.4995 0.4192 -0.0204 0.0280  -0.0405 249 GLY   A N   
1859 C CA  . GLY   A 249 ? 0.4005 0.5083 0.4290 -0.0234 0.0311  -0.0437 249 GLY   A CA  
1860 C C   . GLY   A 249 ? 0.4225 0.5270 0.4490 -0.0240 0.0320  -0.0411 249 GLY   A C   
1861 O O   . GLY   A 249 ? 0.4452 0.5516 0.4736 -0.0265 0.0344  -0.0438 249 GLY   A O   
1862 N N   . HIS   A 250 ? 0.4133 0.5134 0.4360 -0.0219 0.0302  -0.0364 250 HIS   A N   
1863 C CA  . HIS   A 250 ? 0.4153 0.5127 0.4357 -0.0223 0.0308  -0.0339 250 HIS   A CA  
1864 C C   . HIS   A 250 ? 0.4512 0.5407 0.4704 -0.0238 0.0334  -0.0302 250 HIS   A C   
1865 O O   . HIS   A 250 ? 0.5086 0.5938 0.5251 -0.0218 0.0318  -0.0262 250 HIS   A O   
1866 C CB  . HIS   A 250 ? 0.3949 0.4934 0.4121 -0.0191 0.0273  -0.0316 250 HIS   A CB  
1867 C CG  . HIS   A 250 ? 0.4219 0.5279 0.4406 -0.0181 0.0255  -0.0353 250 HIS   A CG  
1868 N ND1 . HIS   A 250 ? 0.4609 0.5713 0.4804 -0.0161 0.0231  -0.0372 250 HIS   A ND1 
1869 C CD2 . HIS   A 250 ? 0.4276 0.5378 0.4473 -0.0188 0.0260  -0.0378 250 HIS   A CD2 
1870 C CE1 . HIS   A 250 ? 0.4303 0.5471 0.4512 -0.0153 0.0219  -0.0403 250 HIS   A CE1 
1871 N NE2 . HIS   A 250 ? 0.4315 0.5484 0.4528 -0.0170 0.0236  -0.0409 250 HIS   A NE2 
1872 N N   . ASP   B 3   ? 0.5286 0.8057 0.5186 0.0062  0.0045  -0.0085 3   ASP   B N   
1873 C CA  . ASP   B 3   ? 0.5346 0.8118 0.5261 0.0114  0.0047  -0.0026 3   ASP   B CA  
1874 C C   . ASP   B 3   ? 0.4819 0.7405 0.4741 0.0125  0.0049  0.0016  3   ASP   B C   
1875 O O   . ASP   B 3   ? 0.4137 0.6592 0.4052 0.0081  0.0048  -0.0011 3   ASP   B O   
1876 C CB  . ASP   B 3   ? 0.5810 0.8644 0.5725 0.0098  0.0046  -0.0056 3   ASP   B CB  
1877 C CG  . ASP   B 3   ? 0.6502 0.9455 0.6429 0.0165  0.0048  -0.0010 3   ASP   B CG  
1878 O OD1 . ASP   B 3   ? 0.5267 0.8134 0.5206 0.0211  0.0051  0.0048  3   ASP   B OD1 
1879 O OD2 . ASP   B 3   ? 0.6438 0.9572 0.6363 0.0174  0.0047  -0.0031 3   ASP   B OD2 
1880 N N   . LEU   B 4   ? 0.4411 0.6993 0.4348 0.0185  0.0054  0.0083  4   LEU   B N   
1881 C CA  . LEU   B 4   ? 0.4133 0.6555 0.4082 0.0198  0.0057  0.0122  4   LEU   B CA  
1882 C C   . LEU   B 4   ? 0.3812 0.6179 0.3764 0.0178  0.0055  0.0098  4   LEU   B C   
1883 O O   . LEU   B 4   ? 0.3155 0.5381 0.3112 0.0164  0.0056  0.0102  4   LEU   B O   
1884 C CB  . LEU   B 4   ? 0.4366 0.6808 0.4330 0.0267  0.0065  0.0197  4   LEU   B CB  
1885 C CG  . LEU   B 4   ? 0.4517 0.6797 0.4498 0.0282  0.0071  0.0241  4   LEU   B CG  
1886 C CD1 . LEU   B 4   ? 0.4797 0.6980 0.4774 0.0250  0.0071  0.0236  4   LEU   B CD1 
1887 C CD2 . LEU   B 4   ? 0.4613 0.6913 0.4608 0.0350  0.0081  0.0315  4   LEU   B CD2 
1888 N N   . LYS   B 5   ? 0.3768 0.6258 0.3717 0.0178  0.0053  0.0072  5   LYS   B N   
1889 C CA  . LYS   B 5   ? 0.3846 0.6307 0.3796 0.0156  0.0052  0.0045  5   LYS   B CA  
1890 C C   . LYS   B 5   ? 0.3733 0.6105 0.3668 0.0082  0.0049  -0.0009 5   LYS   B C   
1891 O O   . LYS   B 5   ? 0.3472 0.5725 0.3409 0.0065  0.0050  -0.0011 5   LYS   B O   
1892 C CB  . LYS   B 5   ? 0.4120 0.6751 0.4069 0.0168  0.0050  0.0025  5   LYS   B CB  
1893 C CG  . LYS   B 5   ? 0.4755 0.7460 0.4717 0.0248  0.0053  0.0081  5   LYS   B CG  
1894 C CD  . LYS   B 5   ? 0.5666 0.8451 0.5633 0.0265  0.0052  0.0068  5   LYS   B CD  
1895 C CE  . LYS   B 5   ? 0.5974 0.8806 0.5953 0.0352  0.0055  0.0126  5   LYS   B CE  
1896 N NZ  . LYS   B 5   ? 0.6358 0.9394 0.6331 0.0387  0.0054  0.0126  5   LYS   B NZ  
1897 N N   . ALA   B 6   ? 0.3216 0.5649 0.3136 0.0041  0.0048  -0.0053 6   ALA   B N   
1898 C CA  . ALA   B 6   ? 0.3254 0.5596 0.3157 -0.0027 0.0048  -0.0103 6   ALA   B CA  
1899 C C   . ALA   B 6   ? 0.3052 0.5223 0.2954 -0.0027 0.0048  -0.0080 6   ALA   B C   
1900 O O   . ALA   B 6   ? 0.3028 0.5089 0.2923 -0.0060 0.0048  -0.0094 6   ALA   B O   
1901 C CB  . ALA   B 6   ? 0.3266 0.5690 0.3155 -0.0062 0.0047  -0.0149 6   ALA   B CB  
1902 N N   . SER   B 7   ? 0.2832 0.4990 0.2741 0.0009  0.0048  -0.0042 7   SER   B N   
1903 C CA  . SER   B 7   ? 0.2717 0.4732 0.2627 0.0011  0.0048  -0.0021 7   SER   B CA  
1904 C C   . SER   B 7   ? 0.2822 0.4739 0.2747 0.0027  0.0049  0.0007  7   SER   B C   
1905 O O   . SER   B 7   ? 0.2761 0.4555 0.2681 0.0004  0.0049  0.0000  7   SER   B O   
1906 C CB  . SER   B 7   ? 0.2855 0.4904 0.2774 0.0051  0.0049  0.0018  7   SER   B CB  
1907 O OG  . SER   B 7   ? 0.3914 0.5842 0.3830 0.0042  0.0049  0.0025  7   SER   B OG  
1908 N N   . SER   B 8   ? 0.2319 0.4292 0.2262 0.0070  0.0052  0.0041  8   SER   B N   
1909 C CA  . SER   B 8   ? 0.2381 0.4273 0.2342 0.0092  0.0054  0.0067  8   SER   B CA  
1910 C C   . SER   B 8   ? 0.2464 0.4314 0.2416 0.0053  0.0051  0.0028  8   SER   B C   
1911 O O   . SER   B 8   ? 0.2249 0.3989 0.2207 0.0046  0.0052  0.0032  8   SER   B O   
1912 C CB  . SER   B 8   ? 0.2446 0.4415 0.2424 0.0150  0.0058  0.0106  8   SER   B CB  
1913 O OG  . SER   B 8   ? 0.2643 0.4632 0.2628 0.0189  0.0062  0.0152  8   SER   B OG  
1914 N N   . LEU   B 9   ? 0.2299 0.4247 0.2239 0.0027  0.0050  -0.0008 9   LEU   B N   
1915 C CA  . LEU   B 9   ? 0.2347 0.4268 0.2277 -0.0017 0.0049  -0.0045 9   LEU   B CA  
1916 C C   . LEU   B 9   ? 0.2121 0.3920 0.2032 -0.0063 0.0049  -0.0065 9   LEU   B C   
1917 O O   . LEU   B 9   ? 0.1906 0.3620 0.1816 -0.0079 0.0049  -0.0069 9   LEU   B O   
1918 C CB  . LEU   B 9   ? 0.2465 0.4518 0.2383 -0.0046 0.0049  -0.0083 9   LEU   B CB  
1919 C CG  . LEU   B 9   ? 0.2832 0.4878 0.2741 -0.0090 0.0051  -0.0116 9   LEU   B CG  
1920 C CD1 . LEU   B 9   ? 0.2812 0.4843 0.2740 -0.0051 0.0050  -0.0092 9   LEU   B CD1 
1921 C CD2 . LEU   B 9   ? 0.3114 0.5303 0.3015 -0.0122 0.0052  -0.0156 9   LEU   B CD2 
1922 N N   . ARG   B 10  ? 0.2092 0.3884 0.1989 -0.0080 0.0049  -0.0077 10  ARG   B N   
1923 C CA  . ARG   B 10  ? 0.2233 0.3912 0.2110 -0.0116 0.0049  -0.0095 10  ARG   B CA  
1924 C C   . ARG   B 10  ? 0.2122 0.3687 0.2011 -0.0091 0.0048  -0.0063 10  ARG   B C   
1925 O O   . ARG   B 10  ? 0.2128 0.3598 0.2006 -0.0114 0.0048  -0.0072 10  ARG   B O   
1926 C CB  . ARG   B 10  ? 0.2620 0.4329 0.2484 -0.0128 0.0048  -0.0114 10  ARG   B CB  
1927 C CG  . ARG   B 10  ? 0.2917 0.4514 0.2757 -0.0164 0.0049  -0.0138 10  ARG   B CG  
1928 C CD  . ARG   B 10  ? 0.3597 0.5219 0.3425 -0.0169 0.0048  -0.0158 10  ARG   B CD  
1929 N NE  . ARG   B 10  ? 0.4191 0.5706 0.3992 -0.0209 0.0050  -0.0190 10  ARG   B NE  
1930 C CZ  . ARG   B 10  ? 0.4151 0.5634 0.3935 -0.0218 0.0049  -0.0212 10  ARG   B CZ  
1931 N NH1 . ARG   B 10  ? 0.3284 0.4826 0.3078 -0.0186 0.0046  -0.0201 10  ARG   B NH1 
1932 N NH2 . ARG   B 10  ? 0.4425 0.5816 0.4182 -0.0256 0.0053  -0.0244 10  ARG   B NH2 
1933 N N   . ALA   B 11  ? 0.1917 0.3493 0.1827 -0.0046 0.0048  -0.0025 11  ALA   B N   
1934 C CA  . ALA   B 11  ? 0.2019 0.3496 0.1944 -0.0026 0.0048  0.0003  11  ALA   B CA  
1935 C C   . ALA   B 11  ? 0.1754 0.3186 0.1691 -0.0022 0.0049  0.0007  11  ALA   B C   
1936 O O   . ALA   B 11  ? 0.1618 0.2959 0.1557 -0.0029 0.0048  0.0007  11  ALA   B O   
1937 C CB  . ALA   B 11  ? 0.2168 0.3674 0.2113 0.0017  0.0051  0.0045  11  ALA   B CB  
1938 N N   . LEU   B 12  ? 0.1744 0.3248 0.1693 -0.0005 0.0050  0.0010  12  LEU   B N   
1939 C CA  . LEU   B 12  ? 0.1665 0.3137 0.1628 0.0001  0.0050  0.0008  12  LEU   B CA  
1940 C C   . LEU   B 12  ? 0.1748 0.3163 0.1689 -0.0044 0.0048  -0.0023 12  LEU   B C   
1941 O O   . LEU   B 12  ? 0.1710 0.3052 0.1659 -0.0043 0.0048  -0.0021 12  LEU   B O   
1942 C CB  . LEU   B 12  ? 0.1835 0.3413 0.1808 0.0025  0.0051  0.0010  12  LEU   B CB  
1943 C CG  . LEU   B 12  ? 0.1978 0.3548 0.1966 0.0039  0.0050  0.0005  12  LEU   B CG  
1944 C CD1 . LEU   B 12  ? 0.1990 0.3652 0.1995 0.0087  0.0052  0.0025  12  LEU   B CD1 
1945 C CD2 . LEU   B 12  ? 0.1927 0.3512 0.1896 -0.0007 0.0049  -0.0032 12  LEU   B CD2 
1946 N N   . LYS   B 13  ? 0.1813 0.3261 0.1727 -0.0085 0.0048  -0.0051 13  LYS   B N   
1947 C CA  . LYS   B 13  ? 0.1923 0.3320 0.1813 -0.0131 0.0049  -0.0078 13  LYS   B CA  
1948 C C   . LYS   B 13  ? 0.1830 0.3116 0.1706 -0.0141 0.0048  -0.0075 13  LYS   B C   
1949 O O   . LYS   B 13  ? 0.1937 0.3166 0.1791 -0.0172 0.0050  -0.0089 13  LYS   B O   
1950 C CB  . LYS   B 13  ? 0.2046 0.3507 0.1912 -0.0175 0.0052  -0.0109 13  LYS   B CB  
1951 C CG  . LYS   B 13  ? 0.2585 0.4162 0.2463 -0.0170 0.0053  -0.0118 13  LYS   B CG  
1952 C CD  . LYS   B 13  ? 0.2884 0.4545 0.2743 -0.0216 0.0057  -0.0152 13  LYS   B CD  
1953 C CE  . LYS   B 13  ? 0.3358 0.5152 0.3235 -0.0196 0.0056  -0.0155 13  LYS   B CE  
1954 N NZ  . LYS   B 13  ? 0.3979 0.5863 0.3841 -0.0247 0.0061  -0.0193 13  LYS   B NZ  
1955 N N   . LEU   B 14  ? 0.1662 0.2924 0.1548 -0.0114 0.0047  -0.0055 14  LEU   B N   
1956 C CA  . LEU   B 14  ? 0.1717 0.2886 0.1592 -0.0116 0.0046  -0.0051 14  LEU   B CA  
1957 C C   . LEU   B 14  ? 0.1704 0.2827 0.1607 -0.0086 0.0045  -0.0028 14  LEU   B C   
1958 O O   . LEU   B 14  ? 0.1558 0.2620 0.1459 -0.0081 0.0044  -0.0022 14  LEU   B O   
1959 C CB  . LEU   B 14  ? 0.1720 0.2902 0.1586 -0.0113 0.0045  -0.0052 14  LEU   B CB  
1960 C CG  . LEU   B 14  ? 0.1871 0.3092 0.1711 -0.0147 0.0046  -0.0083 14  LEU   B CG  
1961 C CD1 . LEU   B 14  ? 0.1859 0.3117 0.1697 -0.0136 0.0045  -0.0083 14  LEU   B CD1 
1962 C CD2 . LEU   B 14  ? 0.1991 0.3132 0.1798 -0.0185 0.0048  -0.0106 14  LEU   B CD2 
1963 N N   . MET   B 15  ? 0.1580 0.2734 0.1511 -0.0063 0.0046  -0.0016 15  MET   B N   
1964 C CA  . MET   B 15  ? 0.1595 0.2704 0.1556 -0.0036 0.0047  0.0003  15  MET   B CA  
1965 C C   . MET   B 15  ? 0.1558 0.2607 0.1516 -0.0049 0.0046  -0.0012 15  MET   B C   
1966 O O   . MET   B 15  ? 0.1603 0.2664 0.1546 -0.0068 0.0045  -0.0030 15  MET   B O   
1967 C CB  . MET   B 15  ? 0.1739 0.2888 0.1731 -0.0002 0.0050  0.0021  15  MET   B CB  
1968 C CG  . MET   B 15  ? 0.2240 0.3443 0.2242 0.0024  0.0054  0.0048  15  MET   B CG  
1969 S SD  . MET   B 15  ? 0.2697 0.3913 0.2739 0.0073  0.0060  0.0080  15  MET   B SD  
1970 C CE  . MET   B 15  ? 0.3437 0.4547 0.3507 0.0079  0.0065  0.0091  15  MET   B CE  
1971 N N   . ASP   B 16  ? 0.1549 0.2541 0.1520 -0.0039 0.0046  -0.0004 16  ASP   B N   
1972 C CA  . ASP   B 16  ? 0.1497 0.2448 0.1477 -0.0041 0.0045  -0.0015 16  ASP   B CA  
1973 C C   . ASP   B 16  ? 0.1652 0.2604 0.1675 -0.0014 0.0049  -0.0004 16  ASP   B C   
1974 O O   . ASP   B 16  ? 0.1766 0.2691 0.1811 0.0000  0.0053  0.0012  16  ASP   B O   
1975 C CB  . ASP   B 16  ? 0.1499 0.2395 0.1471 -0.0047 0.0043  -0.0017 16  ASP   B CB  
1976 C CG  . ASP   B 16  ? 0.1591 0.2464 0.1520 -0.0069 0.0040  -0.0028 16  ASP   B CG  
1977 O OD1 . ASP   B 16  ? 0.1689 0.2581 0.1592 -0.0087 0.0040  -0.0036 16  ASP   B OD1 
1978 O OD2 . ASP   B 16  ? 0.2105 0.2937 0.2026 -0.0068 0.0038  -0.0031 16  ASP   B OD2 
1979 N N   . LEU   B 17  ? 0.1774 0.2760 0.1809 -0.0005 0.0049  -0.0013 17  LEU   B N   
1980 C CA  . LEU   B 17  ? 0.1899 0.2886 0.1972 0.0026  0.0054  -0.0002 17  LEU   B CA  
1981 C C   . LEU   B 17  ? 0.2298 0.3233 0.2398 0.0028  0.0056  -0.0015 17  LEU   B C   
1982 O O   . LEU   B 17  ? 0.2160 0.3094 0.2252 0.0015  0.0052  -0.0041 17  LEU   B O   
1983 C CB  . LEU   B 17  ? 0.1821 0.2871 0.1897 0.0039  0.0054  -0.0008 17  LEU   B CB  
1984 C CG  . LEU   B 17  ? 0.1943 0.2999 0.2055 0.0080  0.0060  0.0007  17  LEU   B CG  
1985 C CD1 . LEU   B 17  ? 0.2079 0.3146 0.2194 0.0100  0.0065  0.0044  17  LEU   B CD1 
1986 C CD2 . LEU   B 17  ? 0.2032 0.3154 0.2144 0.0093  0.0057  -0.0009 17  LEU   B CD2 
1987 N N   . SER   B 18  ? 0.2666 0.3562 0.2798 0.0045  0.0063  0.0000  18  SER   B N   
1988 C CA  . SER   B 18  ? 0.3134 0.3984 0.3296 0.0044  0.0067  -0.0018 18  SER   B CA  
1989 C C   . SER   B 18  ? 0.3724 0.4551 0.3926 0.0074  0.0076  -0.0008 18  SER   B C   
1990 O O   . SER   B 18  ? 0.4289 0.5131 0.4494 0.0095  0.0081  0.0023  18  SER   B O   
1991 C CB  . SER   B 18  ? 0.3357 0.4170 0.3519 0.0028  0.0068  -0.0015 18  SER   B CB  
1992 O OG  . SER   B 18  ? 0.4226 0.5037 0.4390 0.0037  0.0074  0.0020  18  SER   B OG  
1993 N N   . THR   B 19  ? 0.4901 0.5699 0.5134 0.0077  0.0079  -0.0034 19  THR   B N   
1994 C CA  . THR   B 19  ? 0.5505 0.6274 0.5775 0.0106  0.0089  -0.0030 19  THR   B CA  
1995 C C   . THR   B 19  ? 0.5709 0.6433 0.5996 0.0116  0.0102  0.0011  19  THR   B C   
1996 O O   . THR   B 19  ? 0.6497 0.7188 0.6792 0.0093  0.0105  0.0012  19  THR   B O   
1997 C CB  . THR   B 19  ? 0.6103 0.6840 0.6405 0.0102  0.0091  -0.0071 19  THR   B CB  
1998 O OG1 . THR   B 19  ? 0.6619 0.7316 0.6955 0.0134  0.0103  -0.0059 19  THR   B OG1 
1999 C CG2 . THR   B 19  ? 0.6136 0.6835 0.6450 0.0072  0.0094  -0.0084 19  THR   B CG2 
2000 N N   . THR   B 25  ? 0.4075 0.4815 0.4540 0.0090  0.0092  -0.0361 25  THR   B N   
2001 C CA  . THR   B 25  ? 0.3604 0.4402 0.4074 0.0110  0.0085  -0.0401 25  THR   B CA  
2002 C C   . THR   B 25  ? 0.3521 0.4396 0.3940 0.0115  0.0072  -0.0378 25  THR   B C   
2003 O O   . THR   B 25  ? 0.3082 0.3954 0.3471 0.0115  0.0071  -0.0330 25  THR   B O   
2004 C CB  . THR   B 25  ? 0.3891 0.4639 0.4397 0.0147  0.0095  -0.0412 25  THR   B CB  
2005 O OG1 . THR   B 25  ? 0.3983 0.4718 0.4467 0.0169  0.0096  -0.0355 25  THR   B OG1 
2006 C CG2 . THR   B 25  ? 0.4111 0.4770 0.4670 0.0140  0.0111  -0.0436 25  THR   B CG2 
2007 N N   . ASP   B 26  ? 0.3425 0.4376 0.3838 0.0118  0.0063  -0.0416 26  ASP   B N   
2008 C CA  . ASP   B 26  ? 0.3280 0.4310 0.3651 0.0119  0.0053  -0.0401 26  ASP   B CA  
2009 C C   . ASP   B 26  ? 0.3245 0.4275 0.3612 0.0149  0.0055  -0.0372 26  ASP   B C   
2010 O O   . ASP   B 26  ? 0.2973 0.4040 0.3301 0.0142  0.0051  -0.0339 26  ASP   B O   
2011 C CB  . ASP   B 26  ? 0.3411 0.4524 0.3784 0.0119  0.0046  -0.0449 26  ASP   B CB  
2012 C CG  . ASP   B 26  ? 0.3743 0.4888 0.4103 0.0089  0.0041  -0.0468 26  ASP   B CG  
2013 O OD1 . ASP   B 26  ? 0.3497 0.4599 0.3845 0.0068  0.0043  -0.0444 26  ASP   B OD1 
2014 O OD2 . ASP   B 26  ? 0.4340 0.5559 0.4700 0.0090  0.0035  -0.0506 26  ASP   B OD2 
2015 N N   . GLU   B 27  ? 0.3311 0.4296 0.3717 0.0183  0.0063  -0.0384 27  GLU   B N   
2016 C CA  . GLU   B 27  ? 0.3548 0.4540 0.3950 0.0221  0.0065  -0.0358 27  GLU   B CA  
2017 C C   . GLU   B 27  ? 0.3381 0.4338 0.3759 0.0213  0.0069  -0.0299 27  GLU   B C   
2018 O O   . GLU   B 27  ? 0.2899 0.3904 0.3251 0.0224  0.0065  -0.0269 27  GLU   B O   
2019 C CB  . GLU   B 27  ? 0.4334 0.5265 0.4783 0.0262  0.0076  -0.0377 27  GLU   B CB  
2020 C CG  . GLU   B 27  ? 0.5274 0.6243 0.5750 0.0278  0.0072  -0.0441 27  GLU   B CG  
2021 C CD  . GLU   B 27  ? 0.6987 0.7871 0.7513 0.0315  0.0085  -0.0465 27  GLU   B CD  
2022 O OE1 . GLU   B 27  ? 0.7072 0.7857 0.7626 0.0301  0.0098  -0.0462 27  GLU   B OE1 
2023 O OE2 . GLU   B 27  ? 0.7006 0.7921 0.7543 0.0360  0.0084  -0.0488 27  GLU   B OE2 
2024 N N   . LYS   B 28  ? 0.3103 0.3985 0.3494 0.0193  0.0076  -0.0284 28  LYS   B N   
2025 C CA  . LYS   B 28  ? 0.3309 0.4159 0.3679 0.0186  0.0080  -0.0230 28  LYS   B CA  
2026 C C   . LYS   B 28  ? 0.2976 0.3888 0.3298 0.0155  0.0069  -0.0215 28  LYS   B C   
2027 O O   . LYS   B 28  ? 0.2716 0.3641 0.3014 0.0157  0.0069  -0.0176 28  LYS   B O   
2028 C CB  . LYS   B 28  ? 0.3582 0.4348 0.3975 0.0166  0.0090  -0.0221 28  LYS   B CB  
2029 C CG  . LYS   B 28  ? 0.4483 0.5168 0.4923 0.0192  0.0105  -0.0226 28  LYS   B CG  
2030 C CD  . LYS   B 28  ? 0.5270 0.5927 0.5708 0.0226  0.0114  -0.0173 28  LYS   B CD  
2031 C CE  . LYS   B 28  ? 0.6254 0.6825 0.6735 0.0257  0.0130  -0.0174 28  LYS   B CE  
2032 N NZ  . LYS   B 28  ? 0.6559 0.7122 0.7030 0.0298  0.0137  -0.0119 28  LYS   B NZ  
2033 N N   . VAL   B 29  ? 0.2617 0.3560 0.2926 0.0126  0.0062  -0.0244 29  VAL   B N   
2034 C CA  . VAL   B 29  ? 0.2404 0.3392 0.2666 0.0097  0.0054  -0.0229 29  VAL   B CA  
2035 C C   . VAL   B 29  ? 0.2426 0.3489 0.2663 0.0106  0.0049  -0.0224 29  VAL   B C   
2036 O O   . VAL   B 29  ? 0.2195 0.3282 0.2397 0.0090  0.0046  -0.0198 29  VAL   B O   
2037 C CB  . VAL   B 29  ? 0.2467 0.3471 0.2719 0.0070  0.0048  -0.0258 29  VAL   B CB  
2038 C CG1 . VAL   B 29  ? 0.2228 0.3274 0.2428 0.0043  0.0041  -0.0243 29  VAL   B CG1 
2039 C CG2 . VAL   B 29  ? 0.2606 0.3548 0.2878 0.0058  0.0053  -0.0260 29  VAL   B CG2 
2040 N N   . ILE   B 30  ? 0.2454 0.3561 0.2710 0.0128  0.0047  -0.0255 30  ILE   B N   
2041 C CA  . ILE   B 30  ? 0.2256 0.3450 0.2493 0.0137  0.0042  -0.0257 30  ILE   B CA  
2042 C C   . ILE   B 30  ? 0.2118 0.3312 0.2352 0.0160  0.0046  -0.0222 30  ILE   B C   
2043 O O   . ILE   B 30  ? 0.2162 0.3413 0.2364 0.0145  0.0043  -0.0206 30  ILE   B O   
2044 C CB  . ILE   B 30  ? 0.2449 0.3690 0.2712 0.0163  0.0040  -0.0300 30  ILE   B CB  
2045 C CG1 . ILE   B 30  ? 0.2516 0.3787 0.2772 0.0136  0.0036  -0.0333 30  ILE   B CG1 
2046 C CG2 . ILE   B 30  ? 0.2417 0.3748 0.2668 0.0184  0.0037  -0.0299 30  ILE   B CG2 
2047 C CD1 . ILE   B 30  ? 0.2881 0.4187 0.3171 0.0163  0.0034  -0.0382 30  ILE   B CD1 
2048 N N   . ALA   B 31  ? 0.2384 0.3516 0.2651 0.0194  0.0054  -0.0210 31  ALA   B N   
2049 C CA  . ALA   B 31  ? 0.2519 0.3651 0.2783 0.0222  0.0058  -0.0171 31  ALA   B CA  
2050 C C   . ALA   B 31  ? 0.2707 0.3834 0.2939 0.0190  0.0057  -0.0137 31  ALA   B C   
2051 O O   . ALA   B 31  ? 0.2622 0.3805 0.2832 0.0195  0.0056  -0.0116 31  ALA   B O   
2052 C CB  . ALA   B 31  ? 0.2553 0.3603 0.2855 0.0260  0.0069  -0.0159 31  ALA   B CB  
2053 N N   . LEU   B 32  ? 0.2411 0.3478 0.2640 0.0159  0.0058  -0.0135 32  LEU   B N   
2054 C CA  . LEU   B 32  ? 0.2213 0.3273 0.2411 0.0130  0.0057  -0.0107 32  LEU   B CA  
2055 C C   . LEU   B 32  ? 0.1961 0.3098 0.2121 0.0105  0.0050  -0.0113 32  LEU   B C   
2056 O O   . LEU   B 32  ? 0.2053 0.3220 0.2189 0.0097  0.0050  -0.0091 32  LEU   B O   
2057 C CB  . LEU   B 32  ? 0.2214 0.3211 0.2413 0.0102  0.0057  -0.0113 32  LEU   B CB  
2058 C CG  . LEU   B 32  ? 0.2385 0.3367 0.2554 0.0075  0.0056  -0.0088 32  LEU   B CG  
2059 C CD1 . LEU   B 32  ? 0.2405 0.3372 0.2580 0.0094  0.0062  -0.0051 32  LEU   B CD1 
2060 C CD2 . LEU   B 32  ? 0.2597 0.3527 0.2769 0.0054  0.0056  -0.0098 32  LEU   B CD2 
2061 N N   . CYS   B 33  ? 0.1818 0.2987 0.1970 0.0088  0.0045  -0.0144 33  CYS   B N   
2062 C CA  . CYS   B 33  ? 0.1881 0.3116 0.1995 0.0057  0.0041  -0.0149 33  CYS   B CA  
2063 C C   . CYS   B 33  ? 0.1885 0.3201 0.1995 0.0074  0.0041  -0.0143 33  CYS   B C   
2064 O O   . CYS   B 33  ? 0.1907 0.3265 0.1987 0.0049  0.0040  -0.0133 33  CYS   B O   
2065 C CB  . CYS   B 33  ? 0.1995 0.3258 0.2105 0.0042  0.0038  -0.0180 33  CYS   B CB  
2066 S SG  . CYS   B 33  ? 0.2263 0.3455 0.2363 0.0014  0.0037  -0.0184 33  CYS   B SG  
2067 N N   . HIS   B 34  ? 0.2022 0.3362 0.2163 0.0118  0.0042  -0.0151 34  HIS   B N   
2068 C CA  . HIS   B 34  ? 0.2239 0.3664 0.2378 0.0145  0.0042  -0.0146 34  HIS   B CA  
2069 C C   . HIS   B 34  ? 0.2238 0.3660 0.2370 0.0153  0.0045  -0.0110 34  HIS   B C   
2070 O O   . HIS   B 34  ? 0.2166 0.3672 0.2278 0.0147  0.0043  -0.0105 34  HIS   B O   
2071 C CB  . HIS   B 34  ? 0.2467 0.3904 0.2642 0.0199  0.0043  -0.0160 34  HIS   B CB  
2072 C CG  . HIS   B 34  ? 0.2379 0.3847 0.2560 0.0192  0.0039  -0.0199 34  HIS   B CG  
2073 N ND1 . HIS   B 34  ? 0.2622 0.4079 0.2837 0.0235  0.0040  -0.0222 34  HIS   B ND1 
2074 C CD2 . HIS   B 34  ? 0.2351 0.3866 0.2509 0.0150  0.0035  -0.0219 34  HIS   B CD2 
2075 C CE1 . HIS   B 34  ? 0.2368 0.3870 0.2581 0.0219  0.0035  -0.0257 34  HIS   B CE1 
2076 N NE2 . HIS   B 34  ? 0.2446 0.3986 0.2624 0.0168  0.0032  -0.0254 34  HIS   B NE2 
2077 N N   . GLN   B 35  ? 0.2295 0.3627 0.2443 0.0168  0.0050  -0.0088 35  GLN   B N   
2078 C CA  . GLN   B 35  ? 0.2568 0.3899 0.2711 0.0180  0.0053  -0.0052 35  GLN   B CA  
2079 C C   . GLN   B 35  ? 0.2351 0.3702 0.2458 0.0133  0.0050  -0.0048 35  GLN   B C   
2080 O O   . GLN   B 35  ? 0.2430 0.3826 0.2527 0.0139  0.0051  -0.0028 35  GLN   B O   
2081 C CB  . GLN   B 35  ? 0.3054 0.4284 0.3221 0.0198  0.0060  -0.0027 35  GLN   B CB  
2082 C CG  . GLN   B 35  ? 0.3753 0.4944 0.3958 0.0246  0.0067  -0.0026 35  GLN   B CG  
2083 C CD  . GLN   B 35  ? 0.4670 0.5750 0.4901 0.0245  0.0075  -0.0016 35  GLN   B CD  
2084 O OE1 . GLN   B 35  ? 0.5536 0.6574 0.5758 0.0210  0.0075  -0.0012 35  GLN   B OE1 
2085 N NE2 . GLN   B 35  ? 0.5879 0.6909 0.6144 0.0285  0.0083  -0.0015 35  GLN   B NE2 
2086 N N   . ALA   B 36  ? 0.2082 0.3399 0.2171 0.0088  0.0047  -0.0067 36  ALA   B N   
2087 C CA  . ALA   B 36  ? 0.1853 0.3177 0.1907 0.0044  0.0046  -0.0066 36  ALA   B CA  
2088 C C   . ALA   B 36  ? 0.1807 0.3231 0.1838 0.0023  0.0044  -0.0079 36  ALA   B C   
2089 O O   . ALA   B 36  ? 0.1682 0.3119 0.1687 -0.0009 0.0045  -0.0077 36  ALA   B O   
2090 C CB  . ALA   B 36  ? 0.1732 0.2995 0.1770 0.0008  0.0044  -0.0081 36  ALA   B CB  
2091 N N   . LYS   B 37  ? 0.1993 0.3488 0.2032 0.0037  0.0043  -0.0096 37  LYS   B N   
2092 C CA  . LYS   B 37  ? 0.2046 0.3652 0.2068 0.0018  0.0042  -0.0110 37  LYS   B CA  
2093 C C   . LYS   B 37  ? 0.2154 0.3835 0.2191 0.0065  0.0043  -0.0095 37  LYS   B C   
2094 O O   . LYS   B 37  ? 0.2089 0.3812 0.2148 0.0109  0.0042  -0.0097 37  LYS   B O   
2095 C CB  . LYS   B 37  ? 0.2137 0.3785 0.2160 0.0009  0.0041  -0.0136 37  LYS   B CB  
2096 C CG  . LYS   B 37  ? 0.2106 0.3881 0.2115 -0.0010 0.0041  -0.0155 37  LYS   B CG  
2097 C CD  . LYS   B 37  ? 0.2282 0.4104 0.2295 -0.0013 0.0040  -0.0179 37  LYS   B CD  
2098 C CE  . LYS   B 37  ? 0.2458 0.4403 0.2452 -0.0047 0.0041  -0.0198 37  LYS   B CE  
2099 N NZ  . LYS   B 37  ? 0.2646 0.4660 0.2645 -0.0047 0.0040  -0.0221 37  LYS   B NZ  
2100 N N   . THR   B 38  ? 0.1900 0.3592 0.1926 0.0060  0.0044  -0.0078 38  THR   B N   
2101 C CA  . THR   B 38  ? 0.2021 0.3773 0.2061 0.0110  0.0045  -0.0055 38  THR   B CA  
2102 C C   . THR   B 38  ? 0.1844 0.3740 0.1871 0.0102  0.0044  -0.0073 38  THR   B C   
2103 O O   . THR   B 38  ? 0.1818 0.3752 0.1822 0.0045  0.0044  -0.0100 38  THR   B O   
2104 C CB  . THR   B 38  ? 0.1968 0.3673 0.2005 0.0115  0.0048  -0.0027 38  THR   B CB  
2105 O OG1 . THR   B 38  ? 0.1827 0.3607 0.1840 0.0081  0.0047  -0.0036 38  THR   B OG1 
2106 C CG2 . THR   B 38  ? 0.2017 0.3588 0.2056 0.0097  0.0049  -0.0019 38  THR   B CG2 
2107 N N   . PRO   B 39  ? 0.2182 0.4164 0.2221 0.0156  0.0044  -0.0056 39  PRO   B N   
2108 C CA  . PRO   B 39  ? 0.1978 0.4115 0.2005 0.0150  0.0043  -0.0074 39  PRO   B CA  
2109 C C   . PRO   B 39  ? 0.1886 0.4068 0.1888 0.0094  0.0044  -0.0088 39  PRO   B C   
2110 O O   . PRO   B 39  ? 0.1765 0.4076 0.1756 0.0070  0.0044  -0.0114 39  PRO   B O   
2111 C CB  . PRO   B 39  ? 0.2163 0.4362 0.2208 0.0228  0.0044  -0.0043 39  PRO   B CB  
2112 C CG  . PRO   B 39  ? 0.2354 0.4429 0.2423 0.0274  0.0046  -0.0019 39  PRO   B CG  
2113 C CD  . PRO   B 39  ? 0.2363 0.4301 0.2426 0.0225  0.0047  -0.0020 39  PRO   B CD  
2114 N N   . VAL   B 40  ? 0.1851 0.3943 0.1846 0.0078  0.0045  -0.0072 40  VAL   B N   
2115 C CA  . VAL   B 40  ? 0.1806 0.3934 0.1779 0.0027  0.0047  -0.0090 40  VAL   B CA  
2116 C C   . VAL   B 40  ? 0.1849 0.3877 0.1802 -0.0039 0.0048  -0.0111 40  VAL   B C   
2117 O O   . VAL   B 40  ? 0.1788 0.3817 0.1722 -0.0081 0.0050  -0.0126 40  VAL   B O   
2118 C CB  . VAL   B 40  ? 0.1996 0.4126 0.1972 0.0059  0.0047  -0.0060 40  VAL   B CB  
2119 C CG1 . VAL   B 40  ? 0.2054 0.4293 0.2046 0.0127  0.0047  -0.0035 40  VAL   B CG1 
2120 C CG2 . VAL   B 40  ? 0.2164 0.4145 0.2147 0.0070  0.0048  -0.0031 40  VAL   B CG2 
2121 N N   . GLY   B 41  ? 0.1827 0.3763 0.1784 -0.0045 0.0048  -0.0111 41  GLY   B N   
2122 C CA  . GLY   B 41  ? 0.1794 0.3634 0.1729 -0.0101 0.0050  -0.0126 41  GLY   B CA  
2123 C C   . GLY   B 41  ? 0.1701 0.3413 0.1648 -0.0081 0.0048  -0.0107 41  GLY   B C   
2124 O O   . GLY   B 41  ? 0.1665 0.3357 0.1637 -0.0030 0.0047  -0.0085 41  GLY   B O   
2125 N N   . ASN   B 42  ? 0.1787 0.3417 0.1713 -0.0125 0.0050  -0.0117 42  ASN   B N   
2126 C CA  . ASN   B 42  ? 0.1797 0.3320 0.1729 -0.0115 0.0049  -0.0107 42  ASN   B CA  
2127 C C   . ASN   B 42  ? 0.1831 0.3270 0.1760 -0.0110 0.0048  -0.0090 42  ASN   B C   
2128 O O   . ASN   B 42  ? 0.1670 0.3107 0.1577 -0.0137 0.0050  -0.0095 42  ASN   B O   
2129 C CB  . ASN   B 42  ? 0.1903 0.3392 0.1813 -0.0158 0.0051  -0.0123 42  ASN   B CB  
2130 C CG  . ASN   B 42  ? 0.1972 0.3547 0.1886 -0.0164 0.0051  -0.0140 42  ASN   B CG  
2131 O OD1 . ASN   B 42  ? 0.1776 0.3417 0.1716 -0.0123 0.0049  -0.0139 42  ASN   B OD1 
2132 N ND2 . ASN   B 42  ? 0.2389 0.3961 0.2277 -0.0213 0.0056  -0.0154 42  ASN   B ND2 
2133 N N   . THR   B 43  ? 0.1886 0.3255 0.1835 -0.0078 0.0047  -0.0072 43  THR   B N   
2134 C CA  . THR   B 43  ? 0.1727 0.3012 0.1670 -0.0080 0.0046  -0.0060 43  THR   B CA  
2135 C C   . THR   B 43  ? 0.1715 0.2941 0.1626 -0.0122 0.0047  -0.0075 43  THR   B C   
2136 O O   . THR   B 43  ? 0.1784 0.3024 0.1682 -0.0146 0.0048  -0.0090 43  THR   B O   
2137 C CB  . THR   B 43  ? 0.1602 0.2831 0.1577 -0.0042 0.0046  -0.0041 43  THR   B CB  
2138 O OG1 . THR   B 43  ? 0.1473 0.2674 0.1459 -0.0041 0.0045  -0.0053 43  THR   B OG1 
2139 C CG2 . THR   B 43  ? 0.1617 0.2890 0.1621 0.0001  0.0048  -0.0021 43  THR   B CG2 
2140 N N   . ALA   B 44  ? 0.1630 0.2789 0.1527 -0.0129 0.0047  -0.0069 44  ALA   B N   
2141 C CA  . ALA   B 44  ? 0.1522 0.2616 0.1387 -0.0161 0.0048  -0.0078 44  ALA   B CA  
2142 C C   . ALA   B 44  ? 0.1607 0.2659 0.1479 -0.0154 0.0046  -0.0077 44  ALA   B C   
2143 O O   . ALA   B 44  ? 0.1726 0.2753 0.1572 -0.0179 0.0048  -0.0085 44  ALA   B O   
2144 C CB  . ALA   B 44  ? 0.1570 0.2610 0.1423 -0.0157 0.0047  -0.0072 44  ALA   B CB  
2145 N N   . ALA   B 45  ? 0.1529 0.2571 0.1434 -0.0119 0.0044  -0.0067 45  ALA   B N   
2146 C CA  . ALA   B 45  ? 0.1537 0.2538 0.1453 -0.0109 0.0042  -0.0069 45  ALA   B CA  
2147 C C   . ALA   B 45  ? 0.1458 0.2475 0.1418 -0.0075 0.0042  -0.0066 45  ALA   B C   
2148 O O   . ALA   B 45  ? 0.1443 0.2485 0.1424 -0.0055 0.0043  -0.0053 45  ALA   B O   
2149 C CB  . ALA   B 45  ? 0.1468 0.2401 0.1369 -0.0110 0.0041  -0.0063 45  ALA   B CB  
2150 N N   . ILE   B 46  ? 0.1449 0.2449 0.1424 -0.0069 0.0041  -0.0077 46  ILE   B N   
2151 C CA  . ILE   B 46  ? 0.1565 0.2547 0.1581 -0.0041 0.0042  -0.0077 46  ILE   B CA  
2152 C C   . ILE   B 46  ? 0.1587 0.2515 0.1603 -0.0045 0.0041  -0.0079 46  ILE   B C   
2153 O O   . ILE   B 46  ? 0.1697 0.2610 0.1680 -0.0064 0.0038  -0.0083 46  ILE   B O   
2154 C CB  . ILE   B 46  ? 0.1816 0.2835 0.1855 -0.0028 0.0042  -0.0096 46  ILE   B CB  
2155 C CG1 . ILE   B 46  ? 0.2072 0.3105 0.2088 -0.0050 0.0039  -0.0114 46  ILE   B CG1 
2156 C CG2 . ILE   B 46  ? 0.1904 0.2985 0.1949 -0.0015 0.0043  -0.0092 46  ILE   B CG2 
2157 C CD1 . ILE   B 46  ? 0.2693 0.3742 0.2737 -0.0035 0.0038  -0.0137 46  ILE   B CD1 
2158 N N   . SER   B 47  ? 0.1525 0.2425 0.1577 -0.0026 0.0044  -0.0074 47  SER   B N   
2159 C CA  A SER   B 47  ? 0.1519 0.2379 0.1577 -0.0029 0.0044  -0.0078 47  SER   B CA  
2160 C CA  B SER   B 47  ? 0.1575 0.2435 0.1633 -0.0029 0.0044  -0.0078 47  SER   B CA  
2161 C C   . SER   B 47  ? 0.1510 0.2362 0.1612 -0.0017 0.0047  -0.0096 47  SER   B C   
2162 O O   . SER   B 47  ? 0.1566 0.2409 0.1702 -0.0001 0.0053  -0.0090 47  SER   B O   
2163 C CB  A SER   B 47  ? 0.1503 0.2340 0.1558 -0.0027 0.0046  -0.0056 47  SER   B CB  
2164 C CB  B SER   B 47  ? 0.1632 0.2469 0.1693 -0.0025 0.0047  -0.0055 47  SER   B CB  
2165 O OG  A SER   B 47  ? 0.1504 0.2314 0.1555 -0.0033 0.0044  -0.0061 47  SER   B OG  
2166 O OG  B SER   B 47  ? 0.1738 0.2574 0.1757 -0.0038 0.0043  -0.0048 47  SER   B OG  
2167 N N   . VAL   B 48  ? 0.1556 0.2412 0.1656 -0.0024 0.0044  -0.0121 48  VAL   B N   
2168 C CA  . VAL   B 48  ? 0.1528 0.2385 0.1668 -0.0017 0.0046  -0.0148 48  VAL   B CA  
2169 C C   . VAL   B 48  ? 0.1564 0.2416 0.1702 -0.0026 0.0044  -0.0163 48  VAL   B C   
2170 O O   . VAL   B 48  ? 0.1629 0.2481 0.1728 -0.0035 0.0039  -0.0153 48  VAL   B O   
2171 C CB  . VAL   B 48  ? 0.1553 0.2453 0.1694 -0.0012 0.0043  -0.0171 48  VAL   B CB  
2172 C CG1 . VAL   B 48  ? 0.1575 0.2495 0.1720 0.0001  0.0045  -0.0158 48  VAL   B CG1 
2173 C CG2 . VAL   B 48  ? 0.1615 0.2546 0.1713 -0.0028 0.0037  -0.0175 48  VAL   B CG2 
2174 N N   . TYR   B 49  ? 0.1513 0.2360 0.1694 -0.0024 0.0048  -0.0189 49  TYR   B N   
2175 C CA  . TYR   B 49  ? 0.1782 0.2646 0.1965 -0.0032 0.0045  -0.0214 49  TYR   B CA  
2176 C C   . TYR   B 49  ? 0.1549 0.2459 0.1699 -0.0033 0.0038  -0.0229 49  TYR   B C   
2177 O O   . TYR   B 49  ? 0.1576 0.2510 0.1720 -0.0029 0.0036  -0.0233 49  TYR   B O   
2178 C CB  . TYR   B 49  ? 0.2074 0.2931 0.2313 -0.0033 0.0052  -0.0248 49  TYR   B CB  
2179 C CG  . TYR   B 49  ? 0.2752 0.3560 0.3019 -0.0037 0.0062  -0.0230 49  TYR   B CG  
2180 C CD1 . TYR   B 49  ? 0.3025 0.3824 0.3269 -0.0043 0.0061  -0.0203 49  TYR   B CD1 
2181 C CD2 . TYR   B 49  ? 0.3707 0.4479 0.4023 -0.0034 0.0073  -0.0238 49  TYR   B CD2 
2182 C CE1 . TYR   B 49  ? 0.3281 0.4046 0.3549 -0.0049 0.0071  -0.0184 49  TYR   B CE1 
2183 C CE2 . TYR   B 49  ? 0.4147 0.4873 0.4486 -0.0039 0.0084  -0.0215 49  TYR   B CE2 
2184 C CZ  . TYR   B 49  ? 0.4055 0.4783 0.4371 -0.0048 0.0083  -0.0188 49  TYR   B CZ  
2185 O OH  . TYR   B 49  ? 0.4917 0.5610 0.5254 -0.0056 0.0094  -0.0164 49  TYR   B OH  
2186 N N   . PRO   B 50  ? 0.1424 0.2355 0.1553 -0.0036 0.0033  -0.0235 50  PRO   B N   
2187 C CA  . PRO   B 50  ? 0.1480 0.2453 0.1570 -0.0036 0.0027  -0.0238 50  PRO   B CA  
2188 C C   . PRO   B 50  ? 0.1465 0.2486 0.1575 -0.0033 0.0026  -0.0269 50  PRO   B C   
2189 O O   . PRO   B 50  ? 0.1437 0.2484 0.1518 -0.0035 0.0024  -0.0261 50  PRO   B O   
2190 C CB  . PRO   B 50  ? 0.1446 0.2436 0.1526 -0.0033 0.0025  -0.0246 50  PRO   B CB  
2191 C CG  . PRO   B 50  ? 0.1495 0.2437 0.1578 -0.0035 0.0027  -0.0225 50  PRO   B CG  
2192 C CD  . PRO   B 50  ? 0.1415 0.2333 0.1549 -0.0039 0.0034  -0.0233 50  PRO   B CD  
2193 N N   . ARG   B 51  ? 0.1434 0.2466 0.1596 -0.0030 0.0030  -0.0306 51  ARG   B N   
2194 C CA  . ARG   B 51  ? 0.1726 0.2810 0.1912 -0.0025 0.0028  -0.0344 51  ARG   B CA  
2195 C C   . ARG   B 51  ? 0.1605 0.2687 0.1791 -0.0019 0.0029  -0.0336 51  ARG   B C   
2196 O O   . ARG   B 51  ? 0.1545 0.2684 0.1733 -0.0014 0.0027  -0.0359 51  ARG   B O   
2197 C CB  . ARG   B 51  ? 0.2226 0.3312 0.2470 -0.0025 0.0033  -0.0389 51  ARG   B CB  
2198 C CG  . ARG   B 51  ? 0.2839 0.3859 0.3127 -0.0024 0.0042  -0.0387 51  ARG   B CG  
2199 C CD  . ARG   B 51  ? 0.3298 0.4318 0.3643 -0.0030 0.0049  -0.0437 51  ARG   B CD  
2200 N NE  . ARG   B 51  ? 0.4080 0.5022 0.4461 -0.0033 0.0060  -0.0425 51  ARG   B NE  
2201 C CZ  . ARG   B 51  ? 0.4942 0.5842 0.5324 -0.0045 0.0066  -0.0399 51  ARG   B CZ  
2202 N NH1 . ARG   B 51  ? 0.4857 0.5785 0.5209 -0.0054 0.0060  -0.0387 51  ARG   B NH1 
2203 N NH2 . ARG   B 51  ? 0.5734 0.6565 0.6148 -0.0046 0.0078  -0.0383 51  ARG   B NH2 
2204 N N   . SER   B 52  ? 0.1527 0.2558 0.1708 -0.0018 0.0033  -0.0304 52  SER   B N   
2205 C CA  . SER   B 52  ? 0.1535 0.2574 0.1717 -0.0009 0.0034  -0.0296 52  SER   B CA  
2206 C C   . SER   B 52  ? 0.1365 0.2431 0.1495 -0.0020 0.0030  -0.0268 52  SER   B C   
2207 O O   . SER   B 52  ? 0.1569 0.2656 0.1696 -0.0016 0.0030  -0.0262 52  SER   B O   
2208 C CB  . SER   B 52  ? 0.1771 0.2751 0.1976 -0.0001 0.0040  -0.0274 52  SER   B CB  
2209 O OG  . SER   B 52  ? 0.1864 0.2813 0.2120 0.0006  0.0046  -0.0299 52  SER   B OG  
2210 N N   . ILE   B 53  ? 0.1284 0.2346 0.1372 -0.0034 0.0027  -0.0251 53  ILE   B N   
2211 C CA  . ILE   B 53  ? 0.1358 0.2429 0.1397 -0.0048 0.0027  -0.0223 53  ILE   B CA  
2212 C C   . ILE   B 53  ? 0.1510 0.2648 0.1540 -0.0052 0.0026  -0.0237 53  ILE   B C   
2213 O O   . ILE   B 53  ? 0.1513 0.2667 0.1525 -0.0062 0.0027  -0.0223 53  ILE   B O   
2214 C CB  . ILE   B 53  ? 0.1440 0.2483 0.1436 -0.0058 0.0026  -0.0203 53  ILE   B CB  
2215 C CG1 . ILE   B 53  ? 0.1609 0.2591 0.1610 -0.0054 0.0027  -0.0187 53  ILE   B CG1 
2216 C CG2 . ILE   B 53  ? 0.1542 0.2587 0.1485 -0.0076 0.0027  -0.0177 53  ILE   B CG2 
2217 C CD1 . ILE   B 53  ? 0.1588 0.2548 0.1554 -0.0055 0.0025  -0.0172 53  ILE   B CD1 
2218 N N   . PRO   B 54  ? 0.1610 0.2800 0.1650 -0.0046 0.0023  -0.0265 54  PRO   B N   
2219 C CA  . PRO   B 54  ? 0.1609 0.2873 0.1636 -0.0051 0.0023  -0.0274 54  PRO   B CA  
2220 C C   . PRO   B 54  ? 0.1652 0.2944 0.1707 -0.0041 0.0023  -0.0288 54  PRO   B C   
2221 O O   . PRO   B 54  ? 0.1739 0.3070 0.1771 -0.0054 0.0025  -0.0276 54  PRO   B O   
2222 C CB  . PRO   B 54  ? 0.1596 0.2914 0.1638 -0.0041 0.0019  -0.0307 54  PRO   B CB  
2223 C CG  . PRO   B 54  ? 0.1606 0.2876 0.1640 -0.0041 0.0019  -0.0297 54  PRO   B CG  
2224 C CD  . PRO   B 54  ? 0.1552 0.2747 0.1610 -0.0038 0.0021  -0.0287 54  PRO   B CD  
2225 N N   . ILE   B 55  ? 0.1651 0.2924 0.1756 -0.0019 0.0023  -0.0312 55  ILE   B N   
2226 C CA  . ILE   B 55  ? 0.1829 0.3126 0.1959 -0.0001 0.0024  -0.0324 55  ILE   B CA  
2227 C C   . ILE   B 55  ? 0.1872 0.3141 0.1983 -0.0008 0.0027  -0.0287 55  ILE   B C   
2228 O O   . ILE   B 55  ? 0.1798 0.3116 0.1905 -0.0003 0.0027  -0.0287 55  ILE   B O   
2229 C CB  . ILE   B 55  ? 0.2093 0.3368 0.2280 0.0027  0.0026  -0.0358 55  ILE   B CB  
2230 C CG1 . ILE   B 55  ? 0.2533 0.3851 0.2743 0.0053  0.0026  -0.0377 55  ILE   B CG1 
2231 C CG2 . ILE   B 55  ? 0.2047 0.3232 0.2252 0.0031  0.0030  -0.0339 55  ILE   B CG2 
2232 C CD1 . ILE   B 55  ? 0.2897 0.4317 0.3088 0.0048  0.0021  -0.0394 55  ILE   B CD1 
2233 N N   . ALA   B 56  ? 0.1649 0.2851 0.1745 -0.0018 0.0029  -0.0259 56  ALA   B N   
2234 C CA  . ALA   B 56  ? 0.1828 0.3013 0.1904 -0.0026 0.0031  -0.0228 56  ALA   B CA  
2235 C C   . ALA   B 56  ? 0.1691 0.2923 0.1722 -0.0055 0.0031  -0.0216 56  ALA   B C   
2236 O O   . ALA   B 56  ? 0.1712 0.2983 0.1737 -0.0058 0.0032  -0.0210 56  ALA   B O   
2237 C CB  . ALA   B 56  ? 0.1810 0.2923 0.1877 -0.0032 0.0032  -0.0204 56  ALA   B CB  
2238 N N   . ARG   B 57  ? 0.1869 0.3102 0.1869 -0.0075 0.0031  -0.0214 57  ARG   B N   
2239 C CA  . ARG   B 57  ? 0.1856 0.3117 0.1809 -0.0107 0.0034  -0.0198 57  ARG   B CA  
2240 C C   . ARG   B 57  ? 0.1766 0.3119 0.1728 -0.0108 0.0034  -0.0216 57  ARG   B C   
2241 O O   . ARG   B 57  ? 0.1771 0.3161 0.1713 -0.0129 0.0037  -0.0207 57  ARG   B O   
2242 C CB  . ARG   B 57  ? 0.2080 0.3323 0.1998 -0.0123 0.0035  -0.0187 57  ARG   B CB  
2243 C CG  . ARG   B 57  ? 0.2262 0.3521 0.2130 -0.0159 0.0041  -0.0166 57  ARG   B CG  
2244 C CD  . ARG   B 57  ? 0.2632 0.3828 0.2470 -0.0182 0.0046  -0.0141 57  ARG   B CD  
2245 N NE  . ARG   B 57  ? 0.2707 0.3824 0.2528 -0.0175 0.0045  -0.0126 57  ARG   B NE  
2246 C CZ  . ARG   B 57  ? 0.2817 0.3866 0.2618 -0.0184 0.0048  -0.0108 57  ARG   B CZ  
2247 N NH1 . ARG   B 57  ? 0.3000 0.4050 0.2798 -0.0201 0.0051  -0.0106 57  ARG   B NH1 
2248 N NH2 . ARG   B 57  ? 0.2443 0.3431 0.2225 -0.0173 0.0047  -0.0096 57  ARG   B NH2 
2249 N N   . LYS   B 58  ? 0.1818 0.3214 0.1810 -0.0084 0.0030  -0.0246 58  LYS   B N   
2250 C CA  . LYS   B 58  ? 0.1969 0.3461 0.1974 -0.0078 0.0029  -0.0268 58  LYS   B CA  
2251 C C   . LYS   B 58  ? 0.1935 0.3447 0.1957 -0.0063 0.0029  -0.0268 58  LYS   B C   
2252 O O   . LYS   B 58  ? 0.1781 0.3370 0.1791 -0.0076 0.0031  -0.0270 58  LYS   B O   
2253 C CB  . LYS   B 58  ? 0.1938 0.3464 0.1981 -0.0048 0.0025  -0.0307 58  LYS   B CB  
2254 C CG  . LYS   B 58  ? 0.2201 0.3835 0.2253 -0.0040 0.0023  -0.0334 58  LYS   B CG  
2255 C CD  . LYS   B 58  ? 0.2228 0.3890 0.2321 -0.0009 0.0018  -0.0378 58  LYS   B CD  
2256 C CE  . LYS   B 58  ? 0.2617 0.4397 0.2711 -0.0004 0.0017  -0.0404 58  LYS   B CE  
2257 N NZ  . LYS   B 58  ? 0.2647 0.4463 0.2772 0.0018  0.0013  -0.0448 58  LYS   B NZ  
2258 N N   . THR   B 59  ? 0.1732 0.3184 0.1785 -0.0036 0.0029  -0.0265 59  THR   B N   
2259 C CA  . THR   B 59  ? 0.1867 0.3341 0.1937 -0.0013 0.0029  -0.0263 59  THR   B CA  
2260 C C   . THR   B 59  ? 0.2205 0.3691 0.2241 -0.0043 0.0032  -0.0236 59  THR   B C   
2261 O O   . THR   B 59  ? 0.2119 0.3680 0.2153 -0.0041 0.0033  -0.0240 59  THR   B O   
2262 C CB  . THR   B 59  ? 0.1992 0.3392 0.2100 0.0023  0.0030  -0.0261 59  THR   B CB  
2263 O OG1 . THR   B 59  ? 0.2021 0.3409 0.2160 0.0041  0.0028  -0.0291 59  THR   B OG1 
2264 C CG2 . THR   B 59  ? 0.1950 0.3377 0.2079 0.0058  0.0030  -0.0258 59  THR   B CG2 
2265 N N   . LEU   B 60  ? 0.1990 0.3407 0.1998 -0.0070 0.0034  -0.0213 60  LEU   B N   
2266 C CA  . LEU   B 60  ? 0.2002 0.3426 0.1978 -0.0102 0.0038  -0.0193 60  LEU   B CA  
2267 C C   . LEU   B 60  ? 0.2004 0.3507 0.1952 -0.0138 0.0042  -0.0200 60  LEU   B C   
2268 O O   . LEU   B 60  ? 0.2212 0.3768 0.2150 -0.0154 0.0045  -0.0198 60  LEU   B O   
2269 C CB  . LEU   B 60  ? 0.1814 0.3146 0.1766 -0.0122 0.0040  -0.0172 60  LEU   B CB  
2270 C CG  . LEU   B 60  ? 0.1950 0.3213 0.1928 -0.0091 0.0038  -0.0162 60  LEU   B CG  
2271 C CD1 . LEU   B 60  ? 0.1829 0.3012 0.1780 -0.0111 0.0039  -0.0145 60  LEU   B CD1 
2272 C CD2 . LEU   B 60  ? 0.2010 0.3295 0.2005 -0.0071 0.0039  -0.0153 60  LEU   B CD2 
2273 N N   . LYS   B 61  ? 0.2061 0.3576 0.1995 -0.0153 0.0043  -0.0206 61  LYS   B N   
2274 C CA  . LYS   B 61  ? 0.2280 0.3868 0.2185 -0.0192 0.0048  -0.0208 61  LYS   B CA  
2275 C C   . LYS   B 61  ? 0.2409 0.4112 0.2338 -0.0175 0.0046  -0.0231 61  LYS   B C   
2276 O O   . LYS   B 61  ? 0.2258 0.4029 0.2171 -0.0203 0.0050  -0.0232 61  LYS   B O   
2277 C CB  . LYS   B 61  ? 0.2482 0.4067 0.2368 -0.0206 0.0050  -0.0207 61  LYS   B CB  
2278 C CG  . LYS   B 61  ? 0.2921 0.4410 0.2769 -0.0231 0.0055  -0.0179 61  LYS   B CG  
2279 C CD  . LYS   B 61  ? 0.3795 0.5290 0.3623 -0.0237 0.0057  -0.0174 61  LYS   B CD  
2280 C CE  . LYS   B 61  ? 0.4386 0.5786 0.4176 -0.0252 0.0061  -0.0146 61  LYS   B CE  
2281 N NZ  . LYS   B 61  ? 0.4772 0.6173 0.4563 -0.0231 0.0057  -0.0148 61  LYS   B NZ  
2282 N N   . GLU   B 62  ? 0.2208 0.3924 0.2177 -0.0125 0.0039  -0.0252 62  GLU   B N   
2283 C CA  . GLU   B 62  ? 0.2474 0.4295 0.2467 -0.0098 0.0036  -0.0278 62  GLU   B CA  
2284 C C   . GLU   B 62  ? 0.2276 0.4136 0.2274 -0.0088 0.0036  -0.0272 62  GLU   B C   
2285 O O   . GLU   B 62  ? 0.2453 0.4422 0.2451 -0.0091 0.0037  -0.0285 62  GLU   B O   
2286 C CB  . GLU   B 62  ? 0.2580 0.4395 0.2617 -0.0044 0.0029  -0.0304 62  GLU   B CB  
2287 C CG  . GLU   B 62  ? 0.3451 0.5293 0.3484 -0.0053 0.0028  -0.0322 62  GLU   B CG  
2288 C CD  . GLU   B 62  ? 0.4075 0.5938 0.4149 -0.0007 0.0022  -0.0360 62  GLU   B CD  
2289 O OE1 . GLU   B 62  ? 0.4425 0.6264 0.4537 0.0037  0.0020  -0.0374 62  GLU   B OE1 
2290 O OE2 . GLU   B 62  ? 0.4917 0.6823 0.4984 -0.0018 0.0021  -0.0376 62  GLU   B OE2 
2291 N N   . GLN   B 63  ? 0.2212 0.3995 0.2216 -0.0075 0.0036  -0.0253 63  GLN   B N   
2292 C CA  . GLN   B 63  ? 0.2100 0.3928 0.2109 -0.0061 0.0036  -0.0247 63  GLN   B CA  
2293 C C   . GLN   B 63  ? 0.2176 0.4029 0.2150 -0.0116 0.0042  -0.0234 63  GLN   B C   
2294 O O   . GLN   B 63  ? 0.2507 0.4400 0.2482 -0.0109 0.0043  -0.0229 63  GLN   B O   
2295 C CB  . GLN   B 63  ? 0.2146 0.3892 0.2179 -0.0021 0.0035  -0.0230 63  GLN   B CB  
2296 C CG  . GLN   B 63  ? 0.2040 0.3683 0.2053 -0.0049 0.0037  -0.0206 63  GLN   B CG  
2297 C CD  . GLN   B 63  ? 0.2229 0.3801 0.2269 -0.0007 0.0036  -0.0190 63  GLN   B CD  
2298 O OE1 . GLN   B 63  ? 0.2564 0.4139 0.2637 0.0041  0.0035  -0.0196 63  GLN   B OE1 
2299 N NE2 . GLN   B 63  ? 0.2084 0.3586 0.2109 -0.0025 0.0038  -0.0169 63  GLN   B NE2 
2300 N N   . GLY   B 64  ? 0.2150 0.3975 0.2091 -0.0169 0.0048  -0.0229 64  GLY   B N   
2301 C CA  . GLY   B 64  ? 0.2316 0.4159 0.2222 -0.0227 0.0056  -0.0222 64  GLY   B CA  
2302 C C   . GLY   B 64  ? 0.2515 0.4265 0.2409 -0.0237 0.0058  -0.0204 64  GLY   B C   
2303 O O   . GLY   B 64  ? 0.2966 0.4742 0.2842 -0.0273 0.0063  -0.0204 64  GLY   B O   
2304 N N   . THR   B 65  ? 0.2341 0.3986 0.2244 -0.0212 0.0054  -0.0190 65  THR   B N   
2305 C CA  . THR   B 65  ? 0.2260 0.3820 0.2147 -0.0224 0.0055  -0.0174 65  THR   B CA  
2306 C C   . THR   B 65  ? 0.2428 0.3885 0.2295 -0.0239 0.0057  -0.0161 65  THR   B C   
2307 O O   . THR   B 65  ? 0.2069 0.3450 0.1947 -0.0212 0.0053  -0.0151 65  THR   B O   
2308 C CB  . THR   B 65  ? 0.2362 0.3905 0.2281 -0.0174 0.0050  -0.0166 65  THR   B CB  
2309 O OG1 . THR   B 65  ? 0.2121 0.3612 0.2065 -0.0136 0.0045  -0.0164 65  THR   B OG1 
2310 C CG2 . THR   B 65  ? 0.2236 0.3886 0.2173 -0.0152 0.0048  -0.0174 65  THR   B CG2 
2311 N N   . PRO   B 66  ? 0.2595 0.4049 0.2430 -0.0281 0.0064  -0.0160 66  PRO   B N   
2312 C CA  . PRO   B 66  ? 0.2750 0.4115 0.2562 -0.0288 0.0065  -0.0146 66  PRO   B CA  
2313 C C   . PRO   B 66  ? 0.2918 0.4185 0.2707 -0.0300 0.0068  -0.0131 66  PRO   B C   
2314 O O   . PRO   B 66  ? 0.3133 0.4323 0.2907 -0.0293 0.0067  -0.0118 66  PRO   B O   
2315 C CB  . PRO   B 66  ? 0.2821 0.4224 0.2602 -0.0332 0.0074  -0.0145 66  PRO   B CB  
2316 C CG  . PRO   B 66  ? 0.2792 0.4266 0.2567 -0.0367 0.0080  -0.0155 66  PRO   B CG  
2317 C CD  . PRO   B 66  ? 0.2787 0.4328 0.2604 -0.0323 0.0071  -0.0170 66  PRO   B CD  
2318 N N   . GLU   B 67  ? 0.2688 0.3965 0.2474 -0.0315 0.0070  -0.0134 67  GLU   B N   
2319 C CA  . GLU   B 67  ? 0.2878 0.4072 0.2643 -0.0326 0.0072  -0.0125 67  GLU   B CA  
2320 C C   . GLU   B 67  ? 0.2472 0.3636 0.2265 -0.0281 0.0064  -0.0119 67  GLU   B C   
2321 O O   . GLU   B 67  ? 0.2675 0.3774 0.2454 -0.0283 0.0064  -0.0113 67  GLU   B O   
2322 C CB  . GLU   B 67  ? 0.3601 0.4821 0.3346 -0.0371 0.0081  -0.0135 67  GLU   B CB  
2323 C CG  . GLU   B 67  ? 0.4606 0.5819 0.4313 -0.0427 0.0093  -0.0135 67  GLU   B CG  
2324 C CD  . GLU   B 67  ? 0.5818 0.7021 0.5499 -0.0481 0.0105  -0.0146 67  GLU   B CD  
2325 O OE1 . GLU   B 67  ? 0.6642 0.7891 0.6339 -0.0478 0.0102  -0.0162 67  GLU   B OE1 
2326 O OE2 . GLU   B 67  ? 0.6780 0.7927 0.6424 -0.0525 0.0117  -0.0139 67  GLU   B OE2 
2327 N N   . ILE   B 68  ? 0.1993 0.3199 0.1825 -0.0240 0.0057  -0.0122 68  ILE   B N   
2328 C CA  . ILE   B 68  ? 0.1794 0.2959 0.1653 -0.0200 0.0051  -0.0113 68  ILE   B CA  
2329 C C   . ILE   B 68  ? 0.1670 0.2756 0.1519 -0.0193 0.0050  -0.0106 68  ILE   B C   
2330 O O   . ILE   B 68  ? 0.1699 0.2794 0.1549 -0.0192 0.0049  -0.0111 68  ILE   B O   
2331 C CB  . ILE   B 68  ? 0.1637 0.2856 0.1538 -0.0159 0.0047  -0.0117 68  ILE   B CB  
2332 C CG1 . ILE   B 68  ? 0.1742 0.3048 0.1650 -0.0159 0.0048  -0.0121 68  ILE   B CG1 
2333 C CG2 . ILE   B 68  ? 0.1661 0.2824 0.1589 -0.0124 0.0044  -0.0104 68  ILE   B CG2 
2334 C CD1 . ILE   B 68  ? 0.1743 0.3097 0.1691 -0.0111 0.0045  -0.0120 68  ILE   B CD1 
2335 N N   . ARG   B 69  ? 0.1620 0.2640 0.1458 -0.0190 0.0049  -0.0095 69  ARG   B N   
2336 C CA  . ARG   B 69  ? 0.1806 0.2759 0.1631 -0.0183 0.0047  -0.0089 69  ARG   B CA  
2337 C C   . ARG   B 69  ? 0.1754 0.2709 0.1619 -0.0148 0.0042  -0.0091 69  ARG   B C   
2338 O O   . ARG   B 69  ? 0.1667 0.2648 0.1567 -0.0126 0.0041  -0.0092 69  ARG   B O   
2339 C CB  . ARG   B 69  ? 0.2284 0.3173 0.2084 -0.0187 0.0048  -0.0079 69  ARG   B CB  
2340 C CG  . ARG   B 69  ? 0.2933 0.3805 0.2693 -0.0224 0.0055  -0.0081 69  ARG   B CG  
2341 C CD  . ARG   B 69  ? 0.3672 0.4521 0.3431 -0.0218 0.0053  -0.0080 69  ARG   B CD  
2342 N NE  . ARG   B 69  ? 0.4582 0.5420 0.4311 -0.0252 0.0060  -0.0089 69  ARG   B NE  
2343 C CZ  . ARG   B 69  ? 0.4695 0.5596 0.4429 -0.0273 0.0063  -0.0101 69  ARG   B CZ  
2344 N NH1 . ARG   B 69  ? 0.4541 0.5522 0.4310 -0.0256 0.0059  -0.0102 69  ARG   B NH1 
2345 N NH2 . ARG   B 69  ? 0.4710 0.5597 0.4415 -0.0312 0.0070  -0.0114 69  ARG   B NH2 
2346 N N   . ILE   B 70  ? 0.1451 0.2380 0.1311 -0.0141 0.0041  -0.0093 70  ILE   B N   
2347 C CA  . ILE   B 70  ? 0.1530 0.2457 0.1428 -0.0113 0.0037  -0.0101 70  ILE   B CA  
2348 C C   . ILE   B 70  ? 0.1516 0.2387 0.1404 -0.0105 0.0035  -0.0092 70  ILE   B C   
2349 O O   . ILE   B 70  ? 0.1611 0.2458 0.1469 -0.0110 0.0035  -0.0089 70  ILE   B O   
2350 C CB  . ILE   B 70  ? 0.1640 0.2603 0.1549 -0.0109 0.0036  -0.0118 70  ILE   B CB  
2351 C CG1 . ILE   B 70  ? 0.1650 0.2677 0.1568 -0.0115 0.0037  -0.0129 70  ILE   B CG1 
2352 C CG2 . ILE   B 70  ? 0.1658 0.2614 0.1608 -0.0085 0.0033  -0.0132 70  ILE   B CG2 
2353 C CD1 . ILE   B 70  ? 0.1675 0.2749 0.1599 -0.0113 0.0035  -0.0147 70  ILE   B CD1 
2354 N N   . ALA   B 71  ? 0.1397 0.2255 0.1312 -0.0090 0.0035  -0.0087 71  ALA   B N   
2355 C CA  . ALA   B 71  ? 0.1412 0.2232 0.1327 -0.0079 0.0033  -0.0082 71  ALA   B CA  
2356 C C   . ALA   B 71  ? 0.1422 0.2250 0.1379 -0.0064 0.0033  -0.0095 71  ALA   B C   
2357 O O   . ALA   B 71  ? 0.1369 0.2219 0.1363 -0.0056 0.0035  -0.0104 71  ALA   B O   
2358 C CB  . ALA   B 71  ? 0.1500 0.2305 0.1415 -0.0077 0.0034  -0.0068 71  ALA   B CB  
2359 N N   . THR   B 72  ? 0.1288 0.2098 0.1241 -0.0057 0.0031  -0.0098 72  THR   B N   
2360 C CA  . THR   B 72  ? 0.1245 0.2066 0.1240 -0.0048 0.0031  -0.0114 72  THR   B CA  
2361 C C   . THR   B 72  ? 0.1366 0.2167 0.1362 -0.0042 0.0031  -0.0107 72  THR   B C   
2362 O O   . THR   B 72  ? 0.1530 0.2311 0.1497 -0.0043 0.0030  -0.0089 72  THR   B O   
2363 C CB  . THR   B 72  ? 0.1231 0.2082 0.1225 -0.0047 0.0029  -0.0136 72  THR   B CB  
2364 O OG1 . THR   B 72  ? 0.1141 0.2006 0.1184 -0.0041 0.0031  -0.0160 72  THR   B OG1 
2365 C CG2 . THR   B 72  ? 0.1268 0.2114 0.1216 -0.0045 0.0025  -0.0130 72  THR   B CG2 
2366 N N   . VAL   B 73  ? 0.1402 0.2215 0.1433 -0.0038 0.0033  -0.0123 73  VAL   B N   
2367 C CA  . VAL   B 73  ? 0.1371 0.2178 0.1408 -0.0035 0.0034  -0.0119 73  VAL   B CA  
2368 C C   . VAL   B 73  ? 0.1296 0.2133 0.1338 -0.0032 0.0031  -0.0143 73  VAL   B C   
2369 O O   . VAL   B 73  ? 0.1276 0.2137 0.1342 -0.0035 0.0031  -0.0168 73  VAL   B O   
2370 C CB  . VAL   B 73  ? 0.1598 0.2395 0.1682 -0.0039 0.0042  -0.0113 73  VAL   B CB  
2371 C CG1 . VAL   B 73  ? 0.1680 0.2460 0.1753 -0.0037 0.0044  -0.0084 73  VAL   B CG1 
2372 C CG2 . VAL   B 73  ? 0.1696 0.2498 0.1829 -0.0043 0.0047  -0.0136 73  VAL   B CG2 
2373 N N   . THR   B 74  ? 0.1152 0.1993 0.1171 -0.0024 0.0028  -0.0137 74  THR   B N   
2374 C CA  . THR   B 74  ? 0.1115 0.1997 0.1138 -0.0017 0.0025  -0.0159 74  THR   B CA  
2375 C C   . THR   B 74  ? 0.1191 0.2084 0.1225 -0.0015 0.0026  -0.0156 74  THR   B C   
2376 O O   . THR   B 74  ? 0.1248 0.2115 0.1275 -0.0015 0.0028  -0.0134 74  THR   B O   
2377 C CB  . THR   B 74  ? 0.1180 0.2071 0.1150 -0.0001 0.0018  -0.0155 74  THR   B CB  
2378 O OG1 . THR   B 74  ? 0.1222 0.2078 0.1146 0.0010  0.0015  -0.0130 74  THR   B OG1 
2379 C CG2 . THR   B 74  ? 0.1233 0.2124 0.1192 -0.0006 0.0018  -0.0157 74  THR   B CG2 
2380 N N   . ASN   B 75  ? 0.1335 0.2278 0.1388 -0.0014 0.0026  -0.0181 75  ASN   B N   
2381 C CA  . ASN   B 75  ? 0.1349 0.2319 0.1420 -0.0016 0.0028  -0.0185 75  ASN   B CA  
2382 C C   . ASN   B 75  ? 0.1413 0.2355 0.1528 -0.0037 0.0039  -0.0175 75  ASN   B C   
2383 O O   . ASN   B 75  ? 0.1379 0.2325 0.1496 -0.0039 0.0042  -0.0160 75  ASN   B O   
2384 C CB  . ASN   B 75  ? 0.1343 0.2316 0.1364 0.0008  0.0021  -0.0167 75  ASN   B CB  
2385 C CG  . ASN   B 75  ? 0.1469 0.2501 0.1503 0.0012  0.0021  -0.0182 75  ASN   B CG  
2386 O OD1 . ASN   B 75  ? 0.1406 0.2494 0.1469 0.0005  0.0022  -0.0212 75  ASN   B OD1 
2387 N ND2 . ASN   B 75  ? 0.1385 0.2418 0.1400 0.0025  0.0019  -0.0165 75  ASN   B ND2 
2388 N N   . PHE   B 76  ? 0.1581 0.2498 0.1729 -0.0051 0.0045  -0.0181 76  PHE   B N   
2389 C CA  . PHE   B 76  ? 0.1680 0.2554 0.1854 -0.0062 0.0054  -0.0159 76  PHE   B CA  
2390 C C   . PHE   B 76  ? 0.1860 0.2729 0.2096 -0.0084 0.0067  -0.0179 76  PHE   B C   
2391 O O   . PHE   B 76  ? 0.1761 0.2645 0.2017 -0.0090 0.0067  -0.0213 76  PHE   B O   
2392 C CB  . PHE   B 76  ? 0.1640 0.2481 0.1794 -0.0054 0.0051  -0.0146 76  PHE   B CB  
2393 C CG  . PHE   B 76  ? 0.1534 0.2337 0.1708 -0.0057 0.0059  -0.0120 76  PHE   B CG  
2394 C CD1 . PHE   B 76  ? 0.1577 0.2360 0.1798 -0.0065 0.0069  -0.0129 76  PHE   B CD1 
2395 C CD2 . PHE   B 76  ? 0.1559 0.2351 0.1704 -0.0049 0.0058  -0.0088 76  PHE   B CD2 
2396 C CE1 . PHE   B 76  ? 0.1714 0.2464 0.1950 -0.0061 0.0077  -0.0100 76  PHE   B CE1 
2397 C CE2 . PHE   B 76  ? 0.1629 0.2399 0.1790 -0.0048 0.0065  -0.0062 76  PHE   B CE2 
2398 C CZ  . PHE   B 76  ? 0.1794 0.2544 0.1999 -0.0052 0.0075  -0.0066 76  PHE   B CZ  
2399 N N   . PRO   B 77  ? 0.1833 0.2675 0.2099 -0.0097 0.0079  -0.0157 77  PRO   B N   
2400 C CA  . PRO   B 77  ? 0.1807 0.2642 0.2050 -0.0090 0.0080  -0.0118 77  PRO   B CA  
2401 C C   . PRO   B 77  ? 0.1738 0.2618 0.1976 -0.0095 0.0079  -0.0119 77  PRO   B C   
2402 O O   . PRO   B 77  ? 0.1757 0.2641 0.1977 -0.0088 0.0079  -0.0090 77  PRO   B O   
2403 C CB  . PRO   B 77  ? 0.2052 0.2843 0.2334 -0.0100 0.0095  -0.0095 77  PRO   B CB  
2404 C CG  . PRO   B 77  ? 0.1985 0.2771 0.2319 -0.0124 0.0106  -0.0126 77  PRO   B CG  
2405 C CD  . PRO   B 77  ? 0.1868 0.2679 0.2190 -0.0117 0.0095  -0.0168 77  PRO   B CD  
2406 N N   . HIS   B 78  ? 0.1631 0.2555 0.1884 -0.0104 0.0078  -0.0155 78  HIS   B N   
2407 C CA  . HIS   B 78  ? 0.1602 0.2579 0.1865 -0.0114 0.0081  -0.0163 78  HIS   B CA  
2408 C C   . HIS   B 78  ? 0.1413 0.2425 0.1625 -0.0088 0.0069  -0.0151 78  HIS   B C   
2409 O O   . HIS   B 78  ? 0.1399 0.2448 0.1616 -0.0093 0.0072  -0.0142 78  HIS   B O   
2410 C CB  . HIS   B 78  ? 0.1687 0.2714 0.1977 -0.0129 0.0082  -0.0210 78  HIS   B CB  
2411 C CG  . HIS   B 78  ? 0.1706 0.2746 0.1970 -0.0109 0.0069  -0.0232 78  HIS   B CG  
2412 N ND1 . HIS   B 78  ? 0.1717 0.2792 0.1929 -0.0079 0.0055  -0.0230 78  HIS   B ND1 
2413 C CD2 . HIS   B 78  ? 0.1866 0.2892 0.2148 -0.0114 0.0070  -0.0258 78  HIS   B CD2 
2414 C CE1 . HIS   B 78  ? 0.1840 0.2923 0.2038 -0.0069 0.0048  -0.0250 78  HIS   B CE1 
2415 N NE2 . HIS   B 78  ? 0.1843 0.2902 0.2085 -0.0090 0.0057  -0.0269 78  HIS   B NE2 
2416 N N   . GLY   B 79  ? 0.1485 0.2486 0.1649 -0.0061 0.0055  -0.0149 79  GLY   B N   
2417 C CA  . GLY   B 79  ? 0.1496 0.2522 0.1610 -0.0033 0.0044  -0.0141 79  GLY   B CA  
2418 C C   . GLY   B 79  ? 0.1584 0.2687 0.1701 -0.0028 0.0041  -0.0167 79  GLY   B C   
2419 O O   . GLY   B 79  ? 0.1601 0.2743 0.1699 -0.0013 0.0038  -0.0161 79  GLY   B O   
2420 N N   . ASN   B 80  ? 0.1521 0.2655 0.1662 -0.0038 0.0042  -0.0199 80  ASN   B N   
2421 C CA  . ASN   B 80  ? 0.1576 0.2797 0.1720 -0.0032 0.0039  -0.0228 80  ASN   B CA  
2422 C C   . ASN   B 80  ? 0.1599 0.2838 0.1680 0.0014  0.0025  -0.0220 80  ASN   B C   
2423 O O   . ASN   B 80  ? 0.1681 0.2860 0.1720 0.0034  0.0019  -0.0198 80  ASN   B O   
2424 C CB  . ASN   B 80  ? 0.1712 0.2971 0.1889 -0.0049 0.0042  -0.0268 80  ASN   B CB  
2425 C CG  . ASN   B 80  ? 0.1873 0.3124 0.2117 -0.0095 0.0058  -0.0285 80  ASN   B CG  
2426 O OD1 . ASN   B 80  ? 0.2011 0.3244 0.2278 -0.0115 0.0068  -0.0265 80  ASN   B OD1 
2427 N ND2 . ASN   B 80  ? 0.2043 0.3306 0.2318 -0.0111 0.0061  -0.0320 80  ASN   B ND2 
2428 N N   . ASP   B 81  ? 0.1512 0.2835 0.1585 0.0031  0.0020  -0.0239 81  ASP   B N   
2429 C CA  . ASP   B 81  ? 0.1595 0.2934 0.1607 0.0081  0.0008  -0.0229 81  ASP   B CA  
2430 C C   . ASP   B 81  ? 0.1629 0.3021 0.1621 0.0106  0.0000  -0.0251 81  ASP   B C   
2431 O O   . ASP   B 81  ? 0.1746 0.3177 0.1694 0.0149  -0.0008 -0.0248 81  ASP   B O   
2432 C CB  . ASP   B 81  ? 0.1936 0.3338 0.1944 0.0094  0.0006  -0.0230 81  ASP   B CB  
2433 C CG  . ASP   B 81  ? 0.2107 0.3618 0.2160 0.0073  0.0011  -0.0265 81  ASP   B CG  
2434 O OD1 . ASP   B 81  ? 0.2325 0.3867 0.2413 0.0049  0.0016  -0.0293 81  ASP   B OD1 
2435 O OD2 . ASP   B 81  ? 0.2598 0.4172 0.2653 0.0079  0.0011  -0.0267 81  ASP   B OD2 
2436 N N   . ASP   B 82  ? 0.1586 0.2974 0.1604 0.0083  0.0004  -0.0268 82  ASP   B N   
2437 C CA  . ASP   B 82  ? 0.1650 0.3084 0.1646 0.0108  -0.0003 -0.0283 82  ASP   B CA  
2438 C C   . ASP   B 82  ? 0.1553 0.2903 0.1496 0.0131  -0.0008 -0.0251 82  ASP   B C   
2439 O O   . ASP   B 82  ? 0.1580 0.2871 0.1538 0.0106  -0.0003 -0.0246 82  ASP   B O   
2440 C CB  . ASP   B 82  ? 0.1696 0.3188 0.1750 0.0073  0.0003  -0.0325 82  ASP   B CB  
2441 C CG  . ASP   B 82  ? 0.1858 0.3423 0.1892 0.0098  -0.0004 -0.0345 82  ASP   B CG  
2442 O OD1 . ASP   B 82  ? 0.1915 0.3440 0.1892 0.0134  -0.0011 -0.0316 82  ASP   B OD1 
2443 O OD2 . ASP   B 82  ? 0.2041 0.3699 0.2118 0.0080  -0.0001 -0.0389 82  ASP   B OD2 
2444 N N   . ILE   B 83  ? 0.1561 0.2906 0.1443 0.0178  -0.0015 -0.0230 83  ILE   B N   
2445 C CA  . ILE   B 83  ? 0.1629 0.2885 0.1457 0.0198  -0.0018 -0.0197 83  ILE   B CA  
2446 C C   . ILE   B 83  ? 0.1731 0.3000 0.1556 0.0194  -0.0017 -0.0203 83  ILE   B C   
2447 O O   . ILE   B 83  ? 0.1884 0.3080 0.1693 0.0183  -0.0015 -0.0183 83  ILE   B O   
2448 C CB  . ILE   B 83  ? 0.1801 0.3041 0.1562 0.0251  -0.0024 -0.0173 83  ILE   B CB  
2449 C CG1 . ILE   B 83  ? 0.2190 0.3407 0.1945 0.0259  -0.0025 -0.0166 83  ILE   B CG1 
2450 C CG2 . ILE   B 83  ? 0.1983 0.3133 0.1689 0.0267  -0.0023 -0.0141 83  ILE   B CG2 
2451 C CD1 . ILE   B 83  ? 0.2299 0.3532 0.1999 0.0319  -0.0032 -0.0155 83  ILE   B CD1 
2452 N N   . GLU   B 84  ? 0.1813 0.3186 0.1652 0.0205  -0.0020 -0.0231 84  GLU   B N   
2453 C CA  . GLU   B 84  ? 0.2006 0.3407 0.1842 0.0205  -0.0020 -0.0238 84  GLU   B CA  
2454 C C   . GLU   B 84  ? 0.1774 0.3143 0.1660 0.0157  -0.0014 -0.0255 84  GLU   B C   
2455 O O   . GLU   B 84  ? 0.1895 0.3235 0.1766 0.0154  -0.0013 -0.0244 84  GLU   B O   
2456 C CB  . GLU   B 84  ? 0.2265 0.3798 0.2107 0.0228  -0.0025 -0.0268 84  GLU   B CB  
2457 C CG  . GLU   B 84  ? 0.3051 0.4607 0.2828 0.0288  -0.0031 -0.0242 84  GLU   B CG  
2458 C CD  . GLU   B 84  ? 0.4548 0.6012 0.4256 0.0316  -0.0031 -0.0193 84  GLU   B CD  
2459 O OE1 . GLU   B 84  ? 0.4812 0.6267 0.4519 0.0302  -0.0029 -0.0189 84  GLU   B OE1 
2460 O OE2 . GLU   B 84  ? 0.6189 0.7590 0.5846 0.0351  -0.0033 -0.0160 84  GLU   B OE2 
2461 N N   . ILE   B 85  ? 0.1627 0.3009 0.1574 0.0121  -0.0009 -0.0282 85  ILE   B N   
2462 C CA  . ILE   B 85  ? 0.1651 0.2993 0.1645 0.0081  -0.0002 -0.0295 85  ILE   B CA  
2463 C C   . ILE   B 85  ? 0.1565 0.2798 0.1534 0.0075  0.0000  -0.0257 85  ILE   B C   
2464 O O   . ILE   B 85  ? 0.1545 0.2750 0.1520 0.0062  0.0002  -0.0256 85  ILE   B O   
2465 C CB  . ILE   B 85  ? 0.1671 0.3038 0.1732 0.0045  0.0006  -0.0327 85  ILE   B CB  
2466 C CG1 . ILE   B 85  ? 0.1844 0.3328 0.1937 0.0041  0.0005  -0.0376 85  ILE   B CG1 
2467 C CG2 . ILE   B 85  ? 0.1860 0.3158 0.1963 0.0010  0.0014  -0.0330 85  ILE   B CG2 
2468 C CD1 . ILE   B 85  ? 0.2020 0.3528 0.2184 -0.0002 0.0016  -0.0414 85  ILE   B CD1 
2469 N N   . ALA   B 86  ? 0.1529 0.2712 0.1476 0.0083  0.0000  -0.0229 86  ALA   B N   
2470 C CA  . ALA   B 86  ? 0.1548 0.2639 0.1475 0.0075  0.0002  -0.0198 86  ALA   B CA  
2471 C C   . ALA   B 86  ? 0.1671 0.2728 0.1546 0.0091  -0.0001 -0.0177 86  ALA   B C   
2472 O O   . ALA   B 86  ? 0.1489 0.2500 0.1365 0.0074  0.0002  -0.0167 86  ALA   B O   
2473 C CB  . ALA   B 86  ? 0.1521 0.2578 0.1429 0.0085  0.0001  -0.0177 86  ALA   B CB  
2474 N N   . LEU   B 87  ? 0.1983 0.3068 0.1813 0.0125  -0.0006 -0.0169 87  LEU   B N   
2475 C CA  . LEU   B 87  ? 0.1962 0.3016 0.1738 0.0141  -0.0007 -0.0145 87  LEU   B CA  
2476 C C   . LEU   B 87  ? 0.1689 0.2781 0.1488 0.0124  -0.0005 -0.0161 87  LEU   B C   
2477 O O   . LEU   B 87  ? 0.1619 0.2667 0.1395 0.0114  -0.0002 -0.0142 87  LEU   B O   
2478 C CB  . LEU   B 87  ? 0.2095 0.3182 0.1823 0.0187  -0.0011 -0.0133 87  LEU   B CB  
2479 C CG  . LEU   B 87  ? 0.2172 0.3221 0.1837 0.0209  -0.0010 -0.0100 87  LEU   B CG  
2480 C CD1 . LEU   B 87  ? 0.2136 0.3072 0.1770 0.0192  -0.0004 -0.0070 87  LEU   B CD1 
2481 C CD2 . LEU   B 87  ? 0.2289 0.3363 0.1904 0.0261  -0.0014 -0.0085 87  LEU   B CD2 
2482 N N   . ALA   B 88  ? 0.1622 0.2805 0.1462 0.0122  -0.0007 -0.0198 88  ALA   B N   
2483 C CA  . ALA   B 88  ? 0.1719 0.2951 0.1583 0.0108  -0.0006 -0.0221 88  ALA   B CA  
2484 C C   . ALA   B 88  ? 0.1535 0.2711 0.1431 0.0075  -0.0001 -0.0223 88  ALA   B C   
2485 O O   . ALA   B 88  ? 0.1472 0.2644 0.1357 0.0068  0.0000  -0.0218 88  ALA   B O   
2486 C CB  . ALA   B 88  ? 0.1622 0.2956 0.1535 0.0105  -0.0007 -0.0270 88  ALA   B CB  
2487 N N   . GLU   B 89  ? 0.1419 0.2559 0.1353 0.0055  0.0002  -0.0230 89  GLU   B N   
2488 C CA  . GLU   B 89  ? 0.1535 0.2626 0.1500 0.0029  0.0007  -0.0230 89  GLU   B CA  
2489 C C   . GLU   B 89  ? 0.1638 0.2662 0.1556 0.0030  0.0008  -0.0192 89  GLU   B C   
2490 O O   . GLU   B 89  ? 0.1576 0.2589 0.1501 0.0016  0.0010  -0.0192 89  GLU   B O   
2491 C CB  . GLU   B 89  ? 0.1576 0.2641 0.1583 0.0014  0.0012  -0.0235 89  GLU   B CB  
2492 C CG  . GLU   B 89  ? 0.1759 0.2881 0.1822 0.0001  0.0015  -0.0276 89  GLU   B CG  
2493 C CD  . GLU   B 89  ? 0.1683 0.2776 0.1792 -0.0019 0.0023  -0.0280 89  GLU   B CD  
2494 O OE1 . GLU   B 89  ? 0.1937 0.2974 0.2030 -0.0019 0.0024  -0.0247 89  GLU   B OE1 
2495 O OE2 . GLU   B 89  ? 0.1593 0.2720 0.1754 -0.0038 0.0029  -0.0315 89  GLU   B OE2 
2496 N N   . THR   B 90  ? 0.1569 0.2554 0.1441 0.0045  0.0006  -0.0163 90  THR   B N   
2497 C CA  . THR   B 90  ? 0.1609 0.2525 0.1435 0.0042  0.0008  -0.0131 90  THR   B CA  
2498 C C   . THR   B 90  ? 0.1415 0.2344 0.1207 0.0044  0.0009  -0.0121 90  THR   B C   
2499 O O   . THR   B 90  ? 0.1539 0.2441 0.1320 0.0026  0.0012  -0.0110 90  THR   B O   
2500 C CB  . THR   B 90  ? 0.1671 0.2542 0.1455 0.0061  0.0007  -0.0108 90  THR   B CB  
2501 O OG1 . THR   B 90  ? 0.1686 0.2554 0.1505 0.0055  0.0007  -0.0116 90  THR   B OG1 
2502 C CG2 . THR   B 90  ? 0.1749 0.2546 0.1485 0.0055  0.0010  -0.0079 90  THR   B CG2 
2503 N N   . ARG   B 91  ? 0.1448 0.2426 0.1219 0.0067  0.0006  -0.0124 91  ARG   B N   
2504 C CA  . ARG   B 91  ? 0.1570 0.2571 0.1309 0.0071  0.0008  -0.0112 91  ARG   B CA  
2505 C C   . ARG   B 91  ? 0.1502 0.2550 0.1284 0.0048  0.0009  -0.0138 91  ARG   B C   
2506 O O   . ARG   B 91  ? 0.1462 0.2506 0.1224 0.0036  0.0012  -0.0125 91  ARG   B O   
2507 C CB  . ARG   B 91  ? 0.1659 0.2724 0.1375 0.0104  0.0004  -0.0112 91  ARG   B CB  
2508 C CG  . ARG   B 91  ? 0.1852 0.2869 0.1513 0.0135  0.0004  -0.0081 91  ARG   B CG  
2509 C CD  . ARG   B 91  ? 0.2233 0.3327 0.1875 0.0173  0.0000  -0.0083 91  ARG   B CD  
2510 N NE  . ARG   B 91  ? 0.2674 0.3715 0.2255 0.0209  0.0000  -0.0048 91  ARG   B NE  
2511 C CZ  . ARG   B 91  ? 0.3751 0.4847 0.3313 0.0251  -0.0004 -0.0047 91  ARG   B CZ  
2512 N NH1 . ARG   B 91  ? 0.4032 0.5240 0.3636 0.0257  -0.0010 -0.0086 91  ARG   B NH1 
2513 N NH2 . ARG   B 91  ? 0.4343 0.5384 0.3843 0.0289  -0.0002 -0.0011 91  ARG   B NH2 
2514 N N   . ALA   B 92  ? 0.1531 0.2625 0.1372 0.0042  0.0006  -0.0177 92  ALA   B N   
2515 C CA  . ALA   B 92  ? 0.1487 0.2616 0.1370 0.0024  0.0008  -0.0204 92  ALA   B CA  
2516 C C   . ALA   B 92  ? 0.1405 0.2474 0.1292 0.0003  0.0012  -0.0190 92  ALA   B C   
2517 O O   . ALA   B 92  ? 0.1399 0.2487 0.1285 -0.0008 0.0013  -0.0192 92  ALA   B O   
2518 C CB  . ALA   B 92  ? 0.1628 0.2803 0.1575 0.0020  0.0007  -0.0250 92  ALA   B CB  
2519 N N   . ALA   B 93  ? 0.1397 0.2405 0.1290 -0.0003 0.0013  -0.0177 93  ALA   B N   
2520 C CA  . ALA   B 93  ? 0.1360 0.2320 0.1252 -0.0020 0.0017  -0.0161 93  ALA   B CA  
2521 C C   . ALA   B 93  ? 0.1449 0.2394 0.1290 -0.0028 0.0019  -0.0135 93  ALA   B C   
2522 O O   . ALA   B 93  ? 0.1607 0.2559 0.1452 -0.0044 0.0022  -0.0135 93  ALA   B O   
2523 C CB  . ALA   B 93  ? 0.1403 0.2308 0.1295 -0.0020 0.0017  -0.0145 93  ALA   B CB  
2524 N N   . ILE   B 94  ? 0.1426 0.2345 0.1215 -0.0017 0.0019  -0.0111 94  ILE   B N   
2525 C CA  . ILE   B 94  ? 0.1556 0.2448 0.1293 -0.0028 0.0025  -0.0083 94  ILE   B CA  
2526 C C   . ILE   B 94  ? 0.1742 0.2700 0.1481 -0.0033 0.0026  -0.0092 94  ILE   B C   
2527 O O   . ILE   B 94  ? 0.1815 0.2773 0.1542 -0.0056 0.0031  -0.0083 94  ILE   B O   
2528 C CB  . ILE   B 94  ? 0.1633 0.2482 0.1315 -0.0008 0.0026  -0.0056 94  ILE   B CB  
2529 C CG1 . ILE   B 94  ? 0.1630 0.2412 0.1304 -0.0003 0.0025  -0.0047 94  ILE   B CG1 
2530 C CG2 . ILE   B 94  ? 0.1881 0.2703 0.1507 -0.0018 0.0034  -0.0025 94  ILE   B CG2 
2531 C CD1 . ILE   B 94  ? 0.1753 0.2506 0.1386 0.0028  0.0024  -0.0031 94  ILE   B CD1 
2532 N N   . ALA   B 95  ? 0.1592 0.2617 0.1350 -0.0015 0.0021  -0.0113 95  ALA   B N   
2533 C CA  . ALA   B 95  ? 0.1643 0.2742 0.1401 -0.0016 0.0022  -0.0123 95  ALA   B CA  
2534 C C   . ALA   B 95  ? 0.1569 0.2705 0.1374 -0.0033 0.0021  -0.0152 95  ALA   B C   
2535 O O   . ALA   B 95  ? 0.1577 0.2760 0.1375 -0.0043 0.0024  -0.0153 95  ALA   B O   
2536 C CB  . ALA   B 95  ? 0.1576 0.2747 0.1346 0.0010  0.0016  -0.0145 95  ALA   B CB  
2537 N N   . TYR   B 96  ? 0.1625 0.2742 0.1478 -0.0034 0.0019  -0.0175 96  TYR   B N   
2538 C CA  . TYR   B 96  ? 0.1569 0.2705 0.1463 -0.0045 0.0020  -0.0196 96  TYR   B CA  
2539 C C   . TYR   B 96  ? 0.1779 0.2888 0.1646 -0.0066 0.0024  -0.0172 96  TYR   B C   
2540 O O   . TYR   B 96  ? 0.1844 0.2998 0.1731 -0.0073 0.0025  -0.0187 96  TYR   B O   
2541 C CB  . TYR   B 96  ? 0.1479 0.2587 0.1425 -0.0042 0.0019  -0.0217 96  TYR   B CB  
2542 C CG  . TYR   B 96  ? 0.1471 0.2619 0.1467 -0.0030 0.0016  -0.0258 96  TYR   B CG  
2543 C CD1 . TYR   B 96  ? 0.1309 0.2522 0.1338 -0.0027 0.0015  -0.0296 96  TYR   B CD1 
2544 C CD2 . TYR   B 96  ? 0.1355 0.2480 0.1370 -0.0025 0.0016  -0.0264 96  TYR   B CD2 
2545 C CE1 . TYR   B 96  ? 0.1336 0.2577 0.1416 -0.0021 0.0015  -0.0340 96  TYR   B CE1 
2546 C CE2 . TYR   B 96  ? 0.1383 0.2541 0.1449 -0.0021 0.0016  -0.0306 96  TYR   B CE2 
2547 C CZ  . TYR   B 96  ? 0.1404 0.2619 0.1501 -0.0020 0.0015  -0.0345 96  TYR   B CZ  
2548 O OH  . TYR   B 96  ? 0.1545 0.2791 0.1695 -0.0020 0.0017  -0.0392 96  TYR   B OH  
2549 N N   . GLY   B 97  ? 0.1726 0.2772 0.1551 -0.0076 0.0028  -0.0138 97  GLY   B N   
2550 C CA  . GLY   B 97  ? 0.1669 0.2689 0.1465 -0.0101 0.0034  -0.0117 97  GLY   B CA  
2551 C C   . GLY   B 97  ? 0.1646 0.2605 0.1447 -0.0108 0.0034  -0.0107 97  GLY   B C   
2552 O O   . GLY   B 97  ? 0.1668 0.2621 0.1460 -0.0128 0.0038  -0.0100 97  GLY   B O   
2553 N N   . ALA   B 98  ? 0.1620 0.2543 0.1435 -0.0091 0.0031  -0.0109 98  ALA   B N   
2554 C CA  . ALA   B 98  ? 0.1487 0.2363 0.1305 -0.0095 0.0032  -0.0099 98  ALA   B CA  
2555 C C   . ALA   B 98  ? 0.1382 0.2212 0.1150 -0.0116 0.0037  -0.0076 98  ALA   B C   
2556 O O   . ALA   B 98  ? 0.1541 0.2343 0.1266 -0.0118 0.0040  -0.0060 98  ALA   B O   
2557 C CB  . ALA   B 98  ? 0.1512 0.2359 0.1344 -0.0075 0.0028  -0.0101 98  ALA   B CB  
2558 N N   . ASP   B 99  ? 0.1443 0.2258 0.1215 -0.0130 0.0039  -0.0073 99  ASP   B N   
2559 C CA  . ASP   B 99  ? 0.1537 0.2301 0.1268 -0.0150 0.0045  -0.0058 99  ASP   B CA  
2560 C C   . ASP   B 99  ? 0.1427 0.2139 0.1152 -0.0134 0.0042  -0.0053 99  ASP   B C   
2561 O O   . ASP   B 99  ? 0.1434 0.2091 0.1118 -0.0141 0.0046  -0.0042 99  ASP   B O   
2562 C CB  . ASP   B 99  ? 0.1702 0.2494 0.1443 -0.0174 0.0048  -0.0064 99  ASP   B CB  
2563 C CG  . ASP   B 99  ? 0.1632 0.2481 0.1374 -0.0193 0.0051  -0.0070 99  ASP   B CG  
2564 O OD1 . ASP   B 99  ? 0.1981 0.2820 0.1690 -0.0206 0.0056  -0.0060 99  ASP   B OD1 
2565 O OD2 . ASP   B 99  ? 0.1753 0.2660 0.1531 -0.0189 0.0049  -0.0083 99  ASP   B OD2 
2566 N N   . GLU   B 100 ? 0.1364 0.2096 0.1131 -0.0113 0.0036  -0.0061 100 GLU   B N   
2567 C CA  . GLU   B 100 ? 0.1417 0.2116 0.1184 -0.0097 0.0034  -0.0057 100 GLU   B CA  
2568 C C   . GLU   B 100 ? 0.1400 0.2123 0.1206 -0.0074 0.0029  -0.0066 100 GLU   B C   
2569 O O   . GLU   B 100 ? 0.1411 0.2172 0.1256 -0.0073 0.0029  -0.0077 100 GLU   B O   
2570 C CB  . GLU   B 100 ? 0.1484 0.2189 0.1266 -0.0105 0.0035  -0.0057 100 GLU   B CB  
2571 C CG  . GLU   B 100 ? 0.1618 0.2320 0.1373 -0.0134 0.0040  -0.0056 100 GLU   B CG  
2572 C CD  . GLU   B 100 ? 0.1766 0.2486 0.1534 -0.0140 0.0041  -0.0058 100 GLU   B CD  
2573 O OE1 . GLU   B 100 ? 0.1854 0.2599 0.1657 -0.0122 0.0038  -0.0056 100 GLU   B OE1 
2574 O OE2 . GLU   B 100 ? 0.1981 0.2695 0.1723 -0.0165 0.0045  -0.0062 100 GLU   B OE2 
2575 N N   . VAL   B 101 ? 0.1474 0.2174 0.1268 -0.0056 0.0026  -0.0063 101 VAL   B N   
2576 C CA  . VAL   B 101 ? 0.1478 0.2203 0.1308 -0.0039 0.0023  -0.0073 101 VAL   B CA  
2577 C C   . VAL   B 101 ? 0.1470 0.2182 0.1307 -0.0032 0.0023  -0.0066 101 VAL   B C   
2578 O O   . VAL   B 101 ? 0.1569 0.2248 0.1369 -0.0028 0.0022  -0.0058 101 VAL   B O   
2579 C CB  . VAL   B 101 ? 0.1639 0.2372 0.1447 -0.0023 0.0020  -0.0076 101 VAL   B CB  
2580 C CG1 . VAL   B 101 ? 0.1647 0.2412 0.1488 -0.0007 0.0018  -0.0090 101 VAL   B CG1 
2581 C CG2 . VAL   B 101 ? 0.1710 0.2469 0.1512 -0.0029 0.0021  -0.0082 101 VAL   B CG2 
2582 N N   . ASP   B 102 ? 0.1373 0.2109 0.1258 -0.0031 0.0024  -0.0071 102 ASP   B N   
2583 C CA  . ASP   B 102 ? 0.1489 0.2224 0.1387 -0.0025 0.0025  -0.0063 102 ASP   B CA  
2584 C C   . ASP   B 102 ? 0.1499 0.2257 0.1420 -0.0015 0.0024  -0.0074 102 ASP   B C   
2585 O O   . ASP   B 102 ? 0.1413 0.2192 0.1377 -0.0020 0.0027  -0.0085 102 ASP   B O   
2586 C CB  . ASP   B 102 ? 0.1496 0.2243 0.1429 -0.0033 0.0030  -0.0055 102 ASP   B CB  
2587 C CG  . ASP   B 102 ? 0.1716 0.2461 0.1634 -0.0043 0.0031  -0.0047 102 ASP   B CG  
2588 O OD1 . ASP   B 102 ? 0.1583 0.2312 0.1463 -0.0051 0.0029  -0.0050 102 ASP   B OD1 
2589 O OD2 . ASP   B 102 ? 0.1953 0.2714 0.1898 -0.0042 0.0034  -0.0037 102 ASP   B OD2 
2590 N N   . VAL   B 103 ? 0.1497 0.2252 0.1389 0.0000  0.0020  -0.0074 103 VAL   B N   
2591 C CA  . VAL   B 103 ? 0.1506 0.2295 0.1416 0.0010  0.0019  -0.0086 103 VAL   B CA  
2592 C C   . VAL   B 103 ? 0.1531 0.2335 0.1462 0.0011  0.0021  -0.0080 103 VAL   B C   
2593 O O   . VAL   B 103 ? 0.1444 0.2231 0.1355 0.0015  0.0020  -0.0066 103 VAL   B O   
2594 C CB  . VAL   B 103 ? 0.1509 0.2298 0.1374 0.0031  0.0013  -0.0089 103 VAL   B CB  
2595 C CG1 . VAL   B 103 ? 0.1575 0.2328 0.1394 0.0047  0.0010  -0.0075 103 VAL   B CG1 
2596 C CG2 . VAL   B 103 ? 0.1526 0.2369 0.1410 0.0042  0.0011  -0.0107 103 VAL   B CG2 
2597 N N   . VAL   B 104 ? 0.1410 0.2252 0.1382 0.0006  0.0024  -0.0092 104 VAL   B N   
2598 C CA  . VAL   B 104 ? 0.1289 0.2153 0.1282 0.0003  0.0028  -0.0085 104 VAL   B CA  
2599 C C   . VAL   B 104 ? 0.1413 0.2307 0.1377 0.0025  0.0022  -0.0092 104 VAL   B C   
2600 O O   . VAL   B 104 ? 0.1359 0.2286 0.1320 0.0034  0.0018  -0.0111 104 VAL   B O   
2601 C CB  . VAL   B 104 ? 0.1253 0.2139 0.1307 -0.0018 0.0038  -0.0092 104 VAL   B CB  
2602 C CG1 . VAL   B 104 ? 0.1213 0.2120 0.1285 -0.0023 0.0044  -0.0077 104 VAL   B CG1 
2603 C CG2 . VAL   B 104 ? 0.1332 0.2185 0.1412 -0.0032 0.0044  -0.0087 104 VAL   B CG2 
2604 N N   . PHE   B 105 ? 0.1438 0.2328 0.1381 0.0036  0.0020  -0.0078 105 PHE   B N   
2605 C CA  . PHE   B 105 ? 0.1506 0.2426 0.1422 0.0061  0.0014  -0.0084 105 PHE   B CA  
2606 C C   . PHE   B 105 ? 0.1439 0.2426 0.1396 0.0052  0.0018  -0.0096 105 PHE   B C   
2607 O O   . PHE   B 105 ? 0.1401 0.2397 0.1405 0.0024  0.0028  -0.0090 105 PHE   B O   
2608 C CB  . PHE   B 105 ? 0.1496 0.2404 0.1392 0.0069  0.0013  -0.0069 105 PHE   B CB  
2609 C CG  . PHE   B 105 ? 0.1596 0.2530 0.1459 0.0100  0.0006  -0.0076 105 PHE   B CG  
2610 C CD1 . PHE   B 105 ? 0.1643 0.2643 0.1530 0.0101  0.0008  -0.0079 105 PHE   B CD1 
2611 C CD2 . PHE   B 105 ? 0.1729 0.2620 0.1537 0.0127  -0.0001 -0.0079 105 PHE   B CD2 
2612 C CE1 . PHE   B 105 ? 0.1675 0.2708 0.1533 0.0133  0.0001  -0.0087 105 PHE   B CE1 
2613 C CE2 . PHE   B 105 ? 0.1776 0.2688 0.1554 0.0162  -0.0007 -0.0086 105 PHE   B CE2 
2614 C CZ  . PHE   B 105 ? 0.1691 0.2677 0.1493 0.0166  -0.0007 -0.0091 105 PHE   B CZ  
2615 N N   . PRO   B 106 ? 0.1490 0.2525 0.1431 0.0074  0.0012  -0.0112 106 PRO   B N   
2616 C CA  . PRO   B 106 ? 0.1504 0.2615 0.1483 0.0063  0.0017  -0.0127 106 PRO   B CA  
2617 C C   . PRO   B 106 ? 0.1580 0.2723 0.1568 0.0061  0.0020  -0.0115 106 PRO   B C   
2618 O O   . PRO   B 106 ? 0.1622 0.2813 0.1588 0.0086  0.0014  -0.0121 106 PRO   B O   
2619 C CB  . PRO   B 106 ? 0.1486 0.2645 0.1438 0.0094  0.0008  -0.0148 106 PRO   B CB  
2620 C CG  . PRO   B 106 ? 0.1500 0.2605 0.1388 0.0131  -0.0001 -0.0134 106 PRO   B CG  
2621 C CD  . PRO   B 106 ? 0.1475 0.2496 0.1360 0.0111  0.0002  -0.0115 106 PRO   B CD  
2622 N N   . TYR   B 107 ? 0.1547 0.2666 0.1566 0.0034  0.0029  -0.0096 107 TYR   B N   
2623 C CA  . TYR   B 107 ? 0.1561 0.2706 0.1583 0.0033  0.0033  -0.0077 107 TYR   B CA  
2624 C C   . TYR   B 107 ? 0.1668 0.2896 0.1724 0.0019  0.0039  -0.0086 107 TYR   B C   
2625 O O   . TYR   B 107 ? 0.1850 0.3127 0.1893 0.0033  0.0037  -0.0081 107 TYR   B O   
2626 C CB  . TYR   B 107 ? 0.1464 0.2564 0.1506 0.0013  0.0041  -0.0050 107 TYR   B CB  
2627 C CG  . TYR   B 107 ? 0.1375 0.2460 0.1470 -0.0022 0.0055  -0.0046 107 TYR   B CG  
2628 C CD1 . TYR   B 107 ? 0.1522 0.2645 0.1660 -0.0048 0.0068  -0.0037 107 TYR   B CD1 
2629 C CD2 . TYR   B 107 ? 0.1255 0.2286 0.1357 -0.0030 0.0056  -0.0050 107 TYR   B CD2 
2630 C CE1 . TYR   B 107 ? 0.1510 0.2605 0.1695 -0.0080 0.0083  -0.0031 107 TYR   B CE1 
2631 C CE2 . TYR   B 107 ? 0.1365 0.2376 0.1516 -0.0058 0.0069  -0.0048 107 TYR   B CE2 
2632 C CZ  . TYR   B 107 ? 0.1463 0.2500 0.1656 -0.0083 0.0083  -0.0038 107 TYR   B CZ  
2633 O OH  . TYR   B 107 ? 0.1554 0.2559 0.1794 -0.0110 0.0098  -0.0036 107 TYR   B OH  
2634 N N   . ARG   B 108 ? 0.1636 0.2885 0.1734 -0.0010 0.0048  -0.0102 108 ARG   B N   
2635 C CA  . ARG   B 108 ? 0.1636 0.2970 0.1766 -0.0028 0.0055  -0.0115 108 ARG   B CA  
2636 C C   . ARG   B 108 ? 0.1763 0.3169 0.1859 0.0008  0.0042  -0.0138 108 ARG   B C   
2637 O O   . ARG   B 108 ? 0.1820 0.3306 0.1925 0.0008  0.0044  -0.0143 108 ARG   B O   
2638 C CB  . ARG   B 108 ? 0.1636 0.2976 0.1820 -0.0069 0.0068  -0.0135 108 ARG   B CB  
2639 C CG  . ARG   B 108 ? 0.1844 0.3127 0.2070 -0.0106 0.0085  -0.0109 108 ARG   B CG  
2640 C CD  . ARG   B 108 ? 0.2271 0.3553 0.2553 -0.0149 0.0100  -0.0131 108 ARG   B CD  
2641 N NE  . ARG   B 108 ? 0.2847 0.4118 0.3127 -0.0143 0.0092  -0.0166 108 ARG   B NE  
2642 C CZ  . ARG   B 108 ? 0.2857 0.4057 0.3130 -0.0135 0.0089  -0.0163 108 ARG   B CZ  
2643 N NH1 . ARG   B 108 ? 0.3138 0.4266 0.3418 -0.0141 0.0096  -0.0129 108 ARG   B NH1 
2644 N NH2 . ARG   B 108 ? 0.2422 0.3630 0.2681 -0.0121 0.0079  -0.0193 108 ARG   B NH2 
2645 N N   . ALA   B 109 ? 0.1729 0.3111 0.1787 0.0041  0.0030  -0.0153 109 ALA   B N   
2646 C CA  . ALA   B 109 ? 0.1818 0.3260 0.1836 0.0084  0.0017  -0.0170 109 ALA   B CA  
2647 C C   . ALA   B 109 ? 0.1907 0.3349 0.1887 0.0117  0.0011  -0.0155 109 ALA   B C   
2648 O O   . ALA   B 109 ? 0.1713 0.3234 0.1681 0.0142  0.0006  -0.0166 109 ALA   B O   
2649 C CB  . ALA   B 109 ? 0.1922 0.3326 0.1903 0.0113  0.0008  -0.0179 109 ALA   B CB  
2650 N N   . LEU   B 110 ? 0.1774 0.3134 0.1737 0.0118  0.0011  -0.0132 110 LEU   B N   
2651 C CA  . LEU   B 110 ? 0.1847 0.3207 0.1775 0.0147  0.0005  -0.0122 110 LEU   B CA  
2652 C C   . LEU   B 110 ? 0.1672 0.3113 0.1633 0.0128  0.0012  -0.0115 110 LEU   B C   
2653 O O   . LEU   B 110 ? 0.1729 0.3227 0.1668 0.0157  0.0006  -0.0122 110 LEU   B O   
2654 C CB  . LEU   B 110 ? 0.1790 0.3055 0.1698 0.0144  0.0004  -0.0103 110 LEU   B CB  
2655 C CG  . LEU   B 110 ? 0.1859 0.3125 0.1737 0.0167  0.0000  -0.0096 110 LEU   B CG  
2656 C CD1 . LEU   B 110 ? 0.2019 0.3283 0.1844 0.0219  -0.0012 -0.0114 110 LEU   B CD1 
2657 C CD2 . LEU   B 110 ? 0.1909 0.3100 0.1781 0.0153  0.0002  -0.0079 110 LEU   B CD2 
2658 N N   . MET   B 111 ? 0.1568 0.3014 0.1581 0.0080  0.0027  -0.0102 111 MET   B N   
2659 C CA  . MET   B 111 ? 0.1688 0.3206 0.1733 0.0057  0.0037  -0.0089 111 MET   B CA  
2660 C C   . MET   B 111 ? 0.1751 0.3378 0.1808 0.0059  0.0037  -0.0114 111 MET   B C   
2661 O O   . MET   B 111 ? 0.1775 0.3483 0.1845 0.0052  0.0042  -0.0109 111 MET   B O   
2662 C CB  . MET   B 111 ? 0.1971 0.3456 0.2067 0.0006  0.0055  -0.0066 111 MET   B CB  
2663 C CG  . MET   B 111 ? 0.2396 0.3796 0.2480 0.0007  0.0056  -0.0038 111 MET   B CG  
2664 S SD  . MET   B 111 ? 0.3081 0.4421 0.3218 -0.0041 0.0075  -0.0011 111 MET   B SD  
2665 C CE  . MET   B 111 ? 0.3304 0.4719 0.3466 -0.0060 0.0089  0.0021  111 MET   B CE  
2666 N N   . ALA   B 112 ? 0.1789 0.3428 0.1843 0.0068  0.0031  -0.0142 112 ALA   B N   
2667 C CA  . ALA   B 112 ? 0.1871 0.3621 0.1931 0.0077  0.0029  -0.0170 112 ALA   B CA  
2668 C C   . ALA   B 112 ? 0.1959 0.3738 0.1961 0.0143  0.0011  -0.0184 112 ALA   B C   
2669 O O   . ALA   B 112 ? 0.1844 0.3712 0.1841 0.0164  0.0006  -0.0210 112 ALA   B O   
2670 C CB  . ALA   B 112 ? 0.2157 0.3915 0.2247 0.0050  0.0033  -0.0194 112 ALA   B CB  
2671 N N   . GLY   B 113 ? 0.1849 0.3551 0.1805 0.0179  0.0002  -0.0169 113 GLY   B N   
2672 C CA  . GLY   B 113 ? 0.2034 0.3752 0.1934 0.0243  -0.0013 -0.0180 113 GLY   B CA  
2673 C C   . GLY   B 113 ? 0.2261 0.3913 0.2115 0.0284  -0.0023 -0.0188 113 GLY   B C   
2674 O O   . GLY   B 113 ? 0.2617 0.4283 0.2425 0.0341  -0.0034 -0.0199 113 GLY   B O   
2675 N N   . ASN   B 114 ? 0.2149 0.3739 0.2017 0.0257  -0.0019 -0.0184 114 ASN   B N   
2676 C CA  . ASN   B 114 ? 0.2105 0.3645 0.1934 0.0291  -0.0027 -0.0189 114 ASN   B CA  
2677 C C   . ASN   B 114 ? 0.2324 0.3732 0.2123 0.0292  -0.0027 -0.0168 114 ASN   B C   
2678 O O   . ASN   B 114 ? 0.2558 0.3911 0.2382 0.0251  -0.0020 -0.0157 114 ASN   B O   
2679 C CB  . ASN   B 114 ? 0.2275 0.3853 0.2138 0.0264  -0.0023 -0.0203 114 ASN   B CB  
2680 C CG  . ASN   B 114 ? 0.2379 0.3925 0.2197 0.0305  -0.0031 -0.0206 114 ASN   B CG  
2681 O OD1 . ASN   B 114 ? 0.2589 0.4055 0.2353 0.0345  -0.0037 -0.0191 114 ASN   B OD1 
2682 N ND2 . ASN   B 114 ? 0.2554 0.4166 0.2393 0.0297  -0.0030 -0.0225 114 ASN   B ND2 
2683 N N   . GLU   B 115 ? 0.2228 0.3590 0.1974 0.0337  -0.0035 -0.0164 115 GLU   B N   
2684 C CA  . GLU   B 115 ? 0.2297 0.3538 0.2010 0.0340  -0.0035 -0.0149 115 GLU   B CA  
2685 C C   . GLU   B 115 ? 0.2294 0.3473 0.1974 0.0357  -0.0038 -0.0145 115 GLU   B C   
2686 O O   . GLU   B 115 ? 0.2215 0.3304 0.1886 0.0336  -0.0034 -0.0132 115 GLU   B O   
2687 C CB  . GLU   B 115 ? 0.2501 0.3718 0.2170 0.0382  -0.0041 -0.0153 115 GLU   B CB  
2688 C CG  . GLU   B 115 ? 0.2575 0.3848 0.2275 0.0361  -0.0038 -0.0154 115 GLU   B CG  
2689 C CD  . GLU   B 115 ? 0.3034 0.4289 0.2695 0.0401  -0.0044 -0.0163 115 GLU   B CD  
2690 O OE1 . GLU   B 115 ? 0.3423 0.4599 0.3031 0.0440  -0.0049 -0.0168 115 GLU   B OE1 
2691 O OE2 . GLU   B 115 ? 0.3443 0.4760 0.3124 0.0391  -0.0043 -0.0166 115 GLU   B OE2 
2692 N N   . GLN   B 116 ? 0.2239 0.3472 0.1898 0.0398  -0.0043 -0.0155 116 GLN   B N   
2693 C CA  . GLN   B 116 ? 0.2380 0.3559 0.1996 0.0429  -0.0046 -0.0146 116 GLN   B CA  
2694 C C   . GLN   B 116 ? 0.2265 0.3426 0.1911 0.0385  -0.0040 -0.0141 116 GLN   B C   
2695 O O   . GLN   B 116 ? 0.2431 0.3506 0.2046 0.0387  -0.0039 -0.0125 116 GLN   B O   
2696 C CB  . GLN   B 116 ? 0.2608 0.3868 0.2197 0.0486  -0.0053 -0.0156 116 GLN   B CB  
2697 C CG  . GLN   B 116 ? 0.2826 0.4019 0.2357 0.0531  -0.0055 -0.0140 116 GLN   B CG  
2698 C CD  . GLN   B 116 ? 0.3611 0.4674 0.3087 0.0557  -0.0055 -0.0123 116 GLN   B CD  
2699 O OE1 . GLN   B 116 ? 0.4252 0.5309 0.3710 0.0586  -0.0058 -0.0131 116 GLN   B OE1 
2700 N NE2 . GLN   B 116 ? 0.3869 0.4828 0.3316 0.0549  -0.0050 -0.0102 116 GLN   B NE2 
2701 N N   . VAL   B 117 ? 0.2121 0.3361 0.1825 0.0344  -0.0036 -0.0155 117 VAL   B N   
2702 C CA  . VAL   B 117 ? 0.2259 0.3491 0.1992 0.0309  -0.0031 -0.0157 117 VAL   B CA  
2703 C C   . VAL   B 117 ? 0.2041 0.3170 0.1777 0.0274  -0.0026 -0.0139 117 VAL   B C   
2704 O O   . VAL   B 117 ? 0.1938 0.3020 0.1666 0.0264  -0.0024 -0.0131 117 VAL   B O   
2705 C CB  . VAL   B 117 ? 0.2223 0.3556 0.2020 0.0271  -0.0027 -0.0180 117 VAL   B CB  
2706 C CG1 . VAL   B 117 ? 0.2202 0.3540 0.2048 0.0227  -0.0019 -0.0179 117 VAL   B CG1 
2707 C CG2 . VAL   B 117 ? 0.2334 0.3661 0.2153 0.0245  -0.0023 -0.0188 117 VAL   B CG2 
2708 N N   . GLY   B 118 ? 0.1993 0.3099 0.1743 0.0256  -0.0023 -0.0132 118 GLY   B N   
2709 C CA  . GLY   B 118 ? 0.1832 0.2852 0.1582 0.0227  -0.0018 -0.0117 118 GLY   B CA  
2710 C C   . GLY   B 118 ? 0.1768 0.2697 0.1460 0.0250  -0.0021 -0.0104 118 GLY   B C   
2711 O O   . GLY   B 118 ? 0.1943 0.2811 0.1631 0.0228  -0.0017 -0.0094 118 GLY   B O   
2712 N N   . PHE   B 119 ? 0.1779 0.2694 0.1424 0.0296  -0.0026 -0.0104 119 PHE   B N   
2713 C CA  . PHE   B 119 ? 0.1865 0.2685 0.1451 0.0320  -0.0026 -0.0091 119 PHE   B CA  
2714 C C   . PHE   B 119 ? 0.1953 0.2763 0.1525 0.0324  -0.0025 -0.0082 119 PHE   B C   
2715 O O   . PHE   B 119 ? 0.1834 0.2568 0.1386 0.0308  -0.0020 -0.0069 119 PHE   B O   
2716 C CB  . PHE   B 119 ? 0.2039 0.2851 0.1578 0.0376  -0.0032 -0.0095 119 PHE   B CB  
2717 C CG  . PHE   B 119 ? 0.2503 0.3200 0.1980 0.0401  -0.0029 -0.0080 119 PHE   B CG  
2718 C CD1 . PHE   B 119 ? 0.2654 0.3265 0.2111 0.0388  -0.0026 -0.0080 119 PHE   B CD1 
2719 C CD2 . PHE   B 119 ? 0.2713 0.3391 0.2150 0.0436  -0.0030 -0.0066 119 PHE   B CD2 
2720 C CE1 . PHE   B 119 ? 0.2898 0.3397 0.2298 0.0406  -0.0021 -0.0068 119 PHE   B CE1 
2721 C CE2 . PHE   B 119 ? 0.2943 0.3508 0.2321 0.0457  -0.0025 -0.0049 119 PHE   B CE2 
2722 C CZ  . PHE   B 119 ? 0.3066 0.3536 0.2426 0.0439  -0.0020 -0.0051 119 PHE   B CZ  
2723 N N   . ASP   B 120 ? 0.1948 0.2844 0.1530 0.0347  -0.0029 -0.0092 120 ASP   B N   
2724 C CA  . ASP   B 120 ? 0.2132 0.3033 0.1695 0.0359  -0.0029 -0.0084 120 ASP   B CA  
2725 C C   . ASP   B 120 ? 0.1921 0.2819 0.1523 0.0307  -0.0024 -0.0085 120 ASP   B C   
2726 O O   . ASP   B 120 ? 0.1958 0.2817 0.1537 0.0306  -0.0021 -0.0071 120 ASP   B O   
2727 C CB  . ASP   B 120 ? 0.2291 0.3300 0.1858 0.0394  -0.0035 -0.0098 120 ASP   B CB  
2728 C CG  . ASP   B 120 ? 0.2512 0.3528 0.2030 0.0457  -0.0041 -0.0094 120 ASP   B CG  
2729 O OD1 . ASP   B 120 ? 0.2848 0.3765 0.2319 0.0479  -0.0039 -0.0078 120 ASP   B OD1 
2730 O OD2 . ASP   B 120 ? 0.2829 0.3953 0.2361 0.0482  -0.0046 -0.0112 120 ASP   B OD2 
2731 N N   . LEU   B 121 ? 0.1749 0.2691 0.1412 0.0267  -0.0022 -0.0101 121 LEU   B N   
2732 C CA  . LEU   B 121 ? 0.1867 0.2809 0.1570 0.0223  -0.0017 -0.0106 121 LEU   B CA  
2733 C C   . LEU   B 121 ? 0.1853 0.2699 0.1535 0.0204  -0.0012 -0.0086 121 LEU   B C   
2734 O O   . LEU   B 121 ? 0.1895 0.2719 0.1571 0.0190  -0.0009 -0.0081 121 LEU   B O   
2735 C CB  . LEU   B 121 ? 0.1831 0.2830 0.1600 0.0189  -0.0013 -0.0124 121 LEU   B CB  
2736 C CG  . LEU   B 121 ? 0.2040 0.3048 0.1857 0.0149  -0.0008 -0.0134 121 LEU   B CG  
2737 C CD1 . LEU   B 121 ? 0.2024 0.3108 0.1900 0.0128  -0.0004 -0.0158 121 LEU   B CD1 
2738 C CD2 . LEU   B 121 ? 0.2192 0.3131 0.2020 0.0119  -0.0003 -0.0120 121 LEU   B CD2 
2739 N N   . VAL   B 122 ? 0.1675 0.2473 0.1345 0.0202  -0.0011 -0.0079 122 VAL   B N   
2740 C CA  . VAL   B 122 ? 0.1753 0.2471 0.1406 0.0179  -0.0007 -0.0066 122 VAL   B CA  
2741 C C   . VAL   B 122 ? 0.2045 0.2698 0.1638 0.0198  -0.0005 -0.0051 122 VAL   B C   
2742 O O   . VAL   B 122 ? 0.2049 0.2665 0.1636 0.0175  -0.0001 -0.0042 122 VAL   B O   
2743 C CB  . VAL   B 122 ? 0.1815 0.2505 0.1466 0.0174  -0.0006 -0.0066 122 VAL   B CB  
2744 C CG1 . VAL   B 122 ? 0.1848 0.2459 0.1473 0.0153  -0.0002 -0.0057 122 VAL   B CG1 
2745 C CG2 . VAL   B 122 ? 0.1766 0.2515 0.1477 0.0148  -0.0005 -0.0073 122 VAL   B CG2 
2746 N N   . LYS   B 123 ? 0.2170 0.2815 0.1722 0.0243  -0.0009 -0.0046 123 LYS   B N   
2747 C CA  . LYS   B 123 ? 0.2283 0.2855 0.1775 0.0265  -0.0005 -0.0026 123 LYS   B CA  
2748 C C   . LYS   B 123 ? 0.2091 0.2690 0.1582 0.0259  -0.0003 -0.0016 123 LYS   B C   
2749 O O   . LYS   B 123 ? 0.2195 0.2732 0.1654 0.0247  0.0004  0.0003  123 LYS   B O   
2750 C CB  . LYS   B 123 ? 0.2720 0.3285 0.2169 0.0322  -0.0009 -0.0022 123 LYS   B CB  
2751 C CG  . LYS   B 123 ? 0.3392 0.3878 0.2775 0.0352  -0.0004 0.0004  123 LYS   B CG  
2752 C CD  . LYS   B 123 ? 0.4114 0.4576 0.3450 0.0413  -0.0007 0.0009  123 LYS   B CD  
2753 C CE  . LYS   B 123 ? 0.4883 0.5240 0.4149 0.0443  0.0001  0.0039  123 LYS   B CE  
2754 N NZ  . LYS   B 123 ? 0.5721 0.5967 0.4972 0.0398  0.0012  0.0048  123 LYS   B NZ  
2755 N N   . ALA   B 124 ? 0.2032 0.2728 0.1556 0.0268  -0.0008 -0.0031 124 ALA   B N   
2756 C CA  . ALA   B 124 ? 0.2112 0.2851 0.1638 0.0266  -0.0007 -0.0028 124 ALA   B CA  
2757 C C   . ALA   B 124 ? 0.2134 0.2851 0.1688 0.0215  -0.0002 -0.0028 124 ALA   B C   
2758 O O   . ALA   B 124 ? 0.2150 0.2849 0.1682 0.0208  0.0003  -0.0013 124 ALA   B O   
2759 C CB  . ALA   B 124 ? 0.2215 0.3071 0.1782 0.0277  -0.0013 -0.0053 124 ALA   B CB  
2760 N N   . CYS   B 125 ? 0.2083 0.2811 0.1687 0.0182  -0.0002 -0.0045 125 CYS   B N   
2761 C CA  . CYS   B 125 ? 0.1880 0.2595 0.1511 0.0140  0.0003  -0.0048 125 CYS   B CA  
2762 C C   . CYS   B 125 ? 0.2087 0.2713 0.1675 0.0126  0.0009  -0.0026 125 CYS   B C   
2763 O O   . CYS   B 125 ? 0.1889 0.2508 0.1477 0.0102  0.0014  -0.0021 125 CYS   B O   
2764 C CB  . CYS   B 125 ? 0.1848 0.2591 0.1538 0.0114  0.0002  -0.0066 125 CYS   B CB  
2765 S SG  . CYS   B 125 ? 0.1916 0.2759 0.1664 0.0116  -0.0001 -0.0094 125 CYS   B SG  
2766 N N   . LYS   B 126 ? 0.2048 0.2614 0.1607 0.0137  0.0010  -0.0019 126 LYS   B N   
2767 C CA  . LYS   B 126 ? 0.2162 0.2641 0.1681 0.0121  0.0017  -0.0004 126 LYS   B CA  
2768 C C   . LYS   B 126 ? 0.2396 0.2835 0.1864 0.0131  0.0023  0.0019  126 LYS   B C   
2769 O O   . LYS   B 126 ? 0.2420 0.2821 0.1874 0.0100  0.0031  0.0030  126 LYS   B O   
2770 C CB  . LYS   B 126 ? 0.2367 0.2789 0.1858 0.0139  0.0017  -0.0005 126 LYS   B CB  
2771 C CG  . LYS   B 126 ? 0.2540 0.2867 0.1988 0.0120  0.0026  0.0005  126 LYS   B CG  
2772 C CD  . LYS   B 126 ? 0.2828 0.3154 0.2300 0.0068  0.0031  0.0000  126 LYS   B CD  
2773 C CE  . LYS   B 126 ? 0.3070 0.3303 0.2497 0.0046  0.0042  0.0008  126 LYS   B CE  
2774 N NZ  . LYS   B 126 ? 0.3378 0.3569 0.2793 0.0052  0.0042  -0.0006 126 LYS   B NZ  
2775 N N   . GLU   B 127 ? 0.2570 0.3025 0.2011 0.0175  0.0020  0.0029  127 GLU   B N   
2776 C CA  . GLU   B 127 ? 0.2794 0.3215 0.2183 0.0192  0.0027  0.0057  127 GLU   B CA  
2777 C C   . GLU   B 127 ? 0.2580 0.3047 0.1989 0.0161  0.0030  0.0060  127 GLU   B C   
2778 O O   . GLU   B 127 ? 0.2617 0.3031 0.1991 0.0143  0.0040  0.0083  127 GLU   B O   
2779 C CB  . GLU   B 127 ? 0.3290 0.3747 0.2654 0.0250  0.0021  0.0065  127 GLU   B CB  
2780 C CG  . GLU   B 127 ? 0.3898 0.4282 0.3220 0.0288  0.0021  0.0073  127 GLU   B CG  
2781 C CD  . GLU   B 127 ? 0.4625 0.5053 0.3924 0.0351  0.0015  0.0078  127 GLU   B CD  
2782 O OE1 . GLU   B 127 ? 0.4760 0.5290 0.4078 0.0368  0.0009  0.0071  127 GLU   B OE1 
2783 O OE2 . GLU   B 127 ? 0.5122 0.5481 0.4382 0.0385  0.0016  0.0084  127 GLU   B OE2 
2784 N N   . ALA   B 128 ? 0.2340 0.2903 0.1804 0.0153  0.0023  0.0035  128 ALA   B N   
2785 C CA  . ALA   B 128 ? 0.2080 0.2697 0.1567 0.0128  0.0025  0.0031  128 ALA   B CA  
2786 C C   . ALA   B 128 ? 0.1994 0.2569 0.1489 0.0081  0.0031  0.0032  128 ALA   B C   
2787 O O   . ALA   B 128 ? 0.2229 0.2801 0.1708 0.0060  0.0038  0.0045  128 ALA   B O   
2788 C CB  . ALA   B 128 ? 0.1930 0.2650 0.1479 0.0128  0.0016  -0.0003 128 ALA   B CB  
2789 N N   . CYS   B 129 ? 0.1862 0.2419 0.1387 0.0063  0.0029  0.0016  129 CYS   B N   
2790 C CA  . CYS   B 129 ? 0.1881 0.2413 0.1419 0.0021  0.0035  0.0013  129 CYS   B CA  
2791 C C   . CYS   B 129 ? 0.1974 0.2423 0.1455 0.0004  0.0046  0.0037  129 CYS   B C   
2792 O O   . CYS   B 129 ? 0.2007 0.2457 0.1484 -0.0030 0.0053  0.0043  129 CYS   B O   
2793 C CB  . CYS   B 129 ? 0.1807 0.2339 0.1380 0.0015  0.0030  -0.0005 129 CYS   B CB  
2794 S SG  . CYS   B 129 ? 0.1919 0.2542 0.1567 0.0014  0.0023  -0.0032 129 CYS   B SG  
2795 N N   . ALA   B 130 ? 0.2143 0.2519 0.1583 0.0026  0.0048  0.0049  130 ALA   B N   
2796 C CA  . ALA   B 130 ? 0.2458 0.2737 0.1846 0.0008  0.0061  0.0068  130 ALA   B CA  
2797 C C   . ALA   B 130 ? 0.2547 0.2816 0.1899 0.0002  0.0070  0.0097  130 ALA   B C   
2798 O O   . ALA   B 130 ? 0.2530 0.2754 0.1859 -0.0036 0.0082  0.0108  130 ALA   B O   
2799 C CB  . ALA   B 130 ? 0.2684 0.2887 0.2034 0.0041  0.0061  0.0074  130 ALA   B CB  
2800 N N   . ALA   B 131 ? 0.2380 0.2702 0.1728 0.0040  0.0065  0.0107  131 ALA   B N   
2801 C CA  . ALA   B 131 ? 0.2619 0.2957 0.1937 0.0040  0.0073  0.0134  131 ALA   B CA  
2802 C C   . ALA   B 131 ? 0.2533 0.2926 0.1880 -0.0008 0.0076  0.0126  131 ALA   B C   
2803 O O   . ALA   B 131 ? 0.2753 0.3134 0.2068 -0.0025 0.0087  0.0152  131 ALA   B O   
2804 C CB  . ALA   B 131 ? 0.2526 0.2942 0.1850 0.0087  0.0063  0.0135  131 ALA   B CB  
2805 N N   . ALA   B 132 ? 0.2423 0.2882 0.1830 -0.0025 0.0067  0.0092  132 ALA   B N   
2806 C CA  . ALA   B 132 ? 0.2493 0.3013 0.1930 -0.0062 0.0069  0.0080  132 ALA   B CA  
2807 C C   . ALA   B 132 ? 0.2513 0.3000 0.1962 -0.0105 0.0074  0.0068  132 ALA   B C   
2808 O O   . ALA   B 132 ? 0.2417 0.2960 0.1898 -0.0133 0.0073  0.0053  132 ALA   B O   
2809 C CB  . ALA   B 132 ? 0.2581 0.3201 0.2076 -0.0045 0.0056  0.0050  132 ALA   B CB  
2810 N N   . ASN   B 133 ? 0.2700 0.3099 0.2123 -0.0110 0.0078  0.0073  133 ASN   B N   
2811 C CA  . ASN   B 133 ? 0.2929 0.3305 0.2364 -0.0148 0.0082  0.0057  133 ASN   B CA  
2812 C C   . ASN   B 133 ? 0.2484 0.2936 0.1981 -0.0148 0.0071  0.0028  133 ASN   B C   
2813 O O   . ASN   B 133 ? 0.2446 0.2929 0.1964 -0.0181 0.0073  0.0015  133 ASN   B O   
2814 C CB  . ASN   B 133 ? 0.3638 0.4004 0.3052 -0.0198 0.0096  0.0067  133 ASN   B CB  
2815 C CG  . ASN   B 133 ? 0.4548 0.4814 0.3898 -0.0205 0.0111  0.0098  133 ASN   B CG  
2816 O OD1 . ASN   B 133 ? 0.6020 0.6290 0.5343 -0.0216 0.0121  0.0123  133 ASN   B OD1 
2817 N ND2 . ASN   B 133 ? 0.4921 0.5096 0.4246 -0.0195 0.0114  0.0097  133 ASN   B ND2 
2818 N N   . VAL   B 134 ? 0.2189 0.2666 0.1712 -0.0111 0.0060  0.0018  134 VAL   B N   
2819 C CA  . VAL   B 134 ? 0.1939 0.2475 0.1519 -0.0106 0.0051  -0.0004 134 VAL   B CA  
2820 C C   . VAL   B 134 ? 0.1903 0.2402 0.1485 -0.0093 0.0047  -0.0010 134 VAL   B C   
2821 O O   . VAL   B 134 ? 0.1859 0.2314 0.1412 -0.0068 0.0046  -0.0002 134 VAL   B O   
2822 C CB  . VAL   B 134 ? 0.1879 0.2480 0.1490 -0.0080 0.0043  -0.0012 134 VAL   B CB  
2823 C CG1 . VAL   B 134 ? 0.1849 0.2493 0.1517 -0.0069 0.0035  -0.0033 134 VAL   B CG1 
2824 C CG2 . VAL   B 134 ? 0.2143 0.2796 0.1760 -0.0096 0.0046  -0.0013 134 VAL   B CG2 
2825 N N   . LEU   B 135 ? 0.1846 0.2369 0.1460 -0.0108 0.0046  -0.0024 135 LEU   B N   
2826 C CA  . LEU   B 135 ? 0.1940 0.2443 0.1559 -0.0096 0.0042  -0.0030 135 LEU   B CA  
2827 C C   . LEU   B 135 ? 0.1802 0.2346 0.1459 -0.0066 0.0034  -0.0035 135 LEU   B C   
2828 O O   . LEU   B 135 ? 0.1852 0.2450 0.1550 -0.0065 0.0031  -0.0041 135 LEU   B O   
2829 C CB  . LEU   B 135 ? 0.2337 0.2860 0.1975 -0.0122 0.0044  -0.0040 135 LEU   B CB  
2830 C CG  . LEU   B 135 ? 0.2991 0.3472 0.2592 -0.0156 0.0053  -0.0042 135 LEU   B CG  
2831 C CD1 . LEU   B 135 ? 0.3143 0.3658 0.2765 -0.0171 0.0053  -0.0057 135 LEU   B CD1 
2832 C CD2 . LEU   B 135 ? 0.3283 0.3676 0.2831 -0.0153 0.0059  -0.0036 135 LEU   B CD2 
2833 N N   . LEU   B 136 ? 0.1653 0.2173 0.1298 -0.0043 0.0031  -0.0035 136 LEU   B N   
2834 C CA  . LEU   B 136 ? 0.1572 0.2130 0.1250 -0.0019 0.0024  -0.0040 136 LEU   B CA  
2835 C C   . LEU   B 136 ? 0.1563 0.2132 0.1261 -0.0019 0.0023  -0.0045 136 LEU   B C   
2836 O O   . LEU   B 136 ? 0.1865 0.2399 0.1535 -0.0016 0.0023  -0.0046 136 LEU   B O   
2837 C CB  . LEU   B 136 ? 0.1726 0.2265 0.1374 0.0013  0.0021  -0.0036 136 LEU   B CB  
2838 C CG  . LEU   B 136 ? 0.1822 0.2415 0.1506 0.0035  0.0015  -0.0045 136 LEU   B CG  
2839 C CD1 . LEU   B 136 ? 0.1677 0.2324 0.1399 0.0031  0.0014  -0.0053 136 LEU   B CD1 
2840 C CD2 . LEU   B 136 ? 0.1940 0.2519 0.1591 0.0070  0.0011  -0.0043 136 LEU   B CD2 
2841 N N   . LYS   B 137 ? 0.1469 0.2089 0.1217 -0.0023 0.0022  -0.0047 137 LYS   B N   
2842 C CA  . LYS   B 137 ? 0.1508 0.2152 0.1281 -0.0020 0.0021  -0.0046 137 LYS   B CA  
2843 C C   . LYS   B 137 ? 0.1583 0.2253 0.1379 0.0000  0.0018  -0.0048 137 LYS   B C   
2844 O O   . LYS   B 137 ? 0.1493 0.2182 0.1308 0.0003  0.0018  -0.0052 137 LYS   B O   
2845 C CB  . LYS   B 137 ? 0.1486 0.2164 0.1297 -0.0035 0.0025  -0.0042 137 LYS   B CB  
2846 C CG  . LYS   B 137 ? 0.1460 0.2134 0.1258 -0.0057 0.0028  -0.0044 137 LYS   B CG  
2847 C CD  . LYS   B 137 ? 0.1524 0.2238 0.1351 -0.0065 0.0030  -0.0040 137 LYS   B CD  
2848 C CE  . LYS   B 137 ? 0.1592 0.2326 0.1420 -0.0084 0.0033  -0.0043 137 LYS   B CE  
2849 N NZ  . LYS   B 137 ? 0.1672 0.2419 0.1523 -0.0082 0.0033  -0.0046 137 LYS   B NZ  
2850 N N   . VAL   B 138 ? 0.1459 0.2140 0.1254 0.0012  0.0017  -0.0046 138 VAL   B N   
2851 C CA  . VAL   B 138 ? 0.1416 0.2132 0.1234 0.0027  0.0015  -0.0048 138 VAL   B CA  
2852 C C   . VAL   B 138 ? 0.1411 0.2164 0.1268 0.0021  0.0019  -0.0039 138 VAL   B C   
2853 O O   . VAL   B 138 ? 0.1509 0.2267 0.1356 0.0022  0.0019  -0.0034 138 VAL   B O   
2854 C CB  . VAL   B 138 ? 0.1590 0.2293 0.1368 0.0053  0.0010  -0.0053 138 VAL   B CB  
2855 C CG1 . VAL   B 138 ? 0.1614 0.2369 0.1417 0.0068  0.0008  -0.0058 138 VAL   B CG1 
2856 C CG2 . VAL   B 138 ? 0.1701 0.2361 0.1436 0.0064  0.0008  -0.0056 138 VAL   B CG2 
2857 N N   . ILE   B 139 ? 0.1518 0.2298 0.1419 0.0013  0.0023  -0.0038 139 ILE   B N   
2858 C CA  . ILE   B 139 ? 0.1537 0.2348 0.1480 0.0006  0.0029  -0.0025 139 ILE   B CA  
2859 C C   . ILE   B 139 ? 0.1583 0.2428 0.1529 0.0017  0.0028  -0.0027 139 ILE   B C   
2860 O O   . ILE   B 139 ? 0.1512 0.2374 0.1468 0.0019  0.0027  -0.0041 139 ILE   B O   
2861 C CB  . ILE   B 139 ? 0.1502 0.2315 0.1491 -0.0008 0.0036  -0.0025 139 ILE   B CB  
2862 C CG1 . ILE   B 139 ? 0.1606 0.2394 0.1590 -0.0015 0.0036  -0.0027 139 ILE   B CG1 
2863 C CG2 . ILE   B 139 ? 0.1513 0.2347 0.1543 -0.0015 0.0046  -0.0006 139 ILE   B CG2 
2864 C CD1 . ILE   B 139 ? 0.1562 0.2349 0.1583 -0.0023 0.0041  -0.0038 139 ILE   B CD1 
2865 N N   . ILE   B 140 ? 0.1422 0.2290 0.1364 0.0022  0.0029  -0.0015 140 ILE   B N   
2866 C CA  . ILE   B 140 ? 0.1401 0.2312 0.1346 0.0032  0.0029  -0.0016 140 ILE   B CA  
2867 C C   . ILE   B 140 ? 0.1458 0.2408 0.1453 0.0016  0.0040  0.0000  140 ILE   B C   
2868 O O   . ILE   B 140 ? 0.1523 0.2517 0.1528 0.0018  0.0041  -0.0004 140 ILE   B O   
2869 C CB  . ILE   B 140 ? 0.1513 0.2433 0.1420 0.0051  0.0023  -0.0019 140 ILE   B CB  
2870 C CG1 . ILE   B 140 ? 0.1607 0.2541 0.1520 0.0044  0.0026  -0.0002 140 ILE   B CG1 
2871 C CG2 . ILE   B 140 ? 0.1611 0.2483 0.1467 0.0067  0.0014  -0.0036 140 ILE   B CG2 
2872 C CD1 . ILE   B 140 ? 0.1745 0.2714 0.1634 0.0062  0.0022  -0.0006 140 ILE   B CD1 
2873 N N   . GLU   B 141 ? 0.1597 0.2533 0.1622 0.0000  0.0048  0.0019  141 GLU   B N   
2874 C CA  . GLU   B 141 ? 0.1499 0.2456 0.1571 -0.0016 0.0062  0.0039  141 GLU   B CA  
2875 C C   . GLU   B 141 ? 0.1633 0.2640 0.1704 -0.0011 0.0065  0.0061  141 GLU   B C   
2876 O O   . GLU   B 141 ? 0.1479 0.2528 0.1568 -0.0019 0.0071  0.0064  141 GLU   B O   
2877 C CB  . GLU   B 141 ? 0.1420 0.2381 0.1525 -0.0032 0.0067  0.0023  141 GLU   B CB  
2878 C CG  . GLU   B 141 ? 0.1516 0.2462 0.1671 -0.0055 0.0084  0.0042  141 GLU   B CG  
2879 C CD  . GLU   B 141 ? 0.1768 0.2661 0.1933 -0.0055 0.0087  0.0046  141 GLU   B CD  
2880 O OE1 . GLU   B 141 ? 0.1678 0.2549 0.1871 -0.0068 0.0091  0.0025  141 GLU   B OE1 
2881 O OE2 . GLU   B 141 ? 0.1658 0.2541 0.1807 -0.0043 0.0085  0.0066  141 GLU   B OE2 
2882 N N   . THR   B 142 ? 0.1471 0.2484 0.1521 0.0000  0.0063  0.0076  142 THR   B N   
2883 C CA  . THR   B 142 ? 0.1521 0.2592 0.1563 0.0009  0.0064  0.0093  142 THR   B CA  
2884 C C   . THR   B 142 ? 0.1600 0.2703 0.1685 -0.0006 0.0080  0.0126  142 THR   B C   
2885 O O   . THR   B 142 ? 0.1667 0.2830 0.1755 -0.0005 0.0083  0.0137  142 THR   B O   
2886 C CB  . THR   B 142 ? 0.1492 0.2569 0.1510 0.0020  0.0060  0.0100  142 THR   B CB  
2887 O OG1 . THR   B 142 ? 0.1703 0.2754 0.1743 0.0013  0.0067  0.0121  142 THR   B OG1 
2888 C CG2 . THR   B 142 ? 0.1493 0.2542 0.1468 0.0031  0.0046  0.0068  142 THR   B CG2 
2889 N N   . GLY   B 143 ? 0.1599 0.2661 0.1717 -0.0021 0.0091  0.0142  143 GLY   B N   
2890 C CA  . GLY   B 143 ? 0.1790 0.2859 0.1950 -0.0038 0.0109  0.0176  143 GLY   B CA  
2891 C C   . GLY   B 143 ? 0.1999 0.3089 0.2183 -0.0060 0.0116  0.0164  143 GLY   B C   
2892 O O   . GLY   B 143 ? 0.2521 0.3636 0.2733 -0.0076 0.0132  0.0192  143 GLY   B O   
2893 N N   . GLU   B 144 ? 0.1857 0.2943 0.2028 -0.0059 0.0105  0.0122  144 GLU   B N   
2894 C CA  . GLU   B 144 ? 0.1952 0.3077 0.2144 -0.0078 0.0109  0.0105  144 GLU   B CA  
2895 C C   . GLU   B 144 ? 0.1794 0.2991 0.1955 -0.0059 0.0098  0.0092  144 GLU   B C   
2896 O O   . GLU   B 144 ? 0.2030 0.3285 0.2208 -0.0072 0.0105  0.0093  144 GLU   B O   
2897 C CB  . GLU   B 144 ? 0.2127 0.3217 0.2330 -0.0088 0.0106  0.0067  144 GLU   B CB  
2898 C CG  . GLU   B 144 ? 0.2204 0.3232 0.2447 -0.0109 0.0119  0.0073  144 GLU   B CG  
2899 C CD  . GLU   B 144 ? 0.2706 0.3736 0.2996 -0.0141 0.0142  0.0097  144 GLU   B CD  
2900 O OE1 . GLU   B 144 ? 0.2707 0.3793 0.3010 -0.0159 0.0146  0.0087  144 GLU   B OE1 
2901 O OE2 . GLU   B 144 ? 0.3022 0.4002 0.3334 -0.0146 0.0155  0.0129  144 GLU   B OE2 
2902 N N   . LEU   B 145 ? 0.1671 0.2863 0.1787 -0.0029 0.0082  0.0078  145 LEU   B N   
2903 C CA  . LEU   B 145 ? 0.1782 0.3031 0.1864 -0.0005 0.0070  0.0063  145 LEU   B CA  
2904 C C   . LEU   B 145 ? 0.2009 0.3320 0.2098 -0.0005 0.0078  0.0093  145 LEU   B C   
2905 O O   . LEU   B 145 ? 0.2246 0.3629 0.2333 -0.0001 0.0077  0.0088  145 LEU   B O   
2906 C CB  . LEU   B 145 ? 0.1727 0.2938 0.1760 0.0025  0.0054  0.0043  145 LEU   B CB  
2907 C CG  . LEU   B 145 ? 0.1799 0.2957 0.1816 0.0030  0.0046  0.0014  145 LEU   B CG  
2908 C CD1 . LEU   B 145 ? 0.2008 0.3118 0.1979 0.0052  0.0034  0.0003  145 LEU   B CD1 
2909 C CD2 . LEU   B 145 ? 0.1883 0.3088 0.1896 0.0040  0.0041  -0.0010 145 LEU   B CD2 
2910 N N   . LYS   B 146 ? 0.1992 0.3282 0.2087 -0.0008 0.0085  0.0125  146 LYS   B N   
2911 C CA  . LYS   B 146 ? 0.2804 0.4153 0.2907 -0.0008 0.0094  0.0162  146 LYS   B CA  
2912 C C   . LYS   B 146 ? 0.2814 0.4223 0.2878 0.0021  0.0081  0.0146  146 LYS   B C   
2913 O O   . LYS   B 146 ? 0.4133 0.5556 0.4180 0.0035  0.0078  0.0158  146 LYS   B O   
2914 C CB  . LYS   B 146 ? 0.3487 0.4887 0.3627 -0.0033 0.0111  0.0187  146 LYS   B CB  
2915 C CG  . LYS   B 146 ? 0.4344 0.5694 0.4528 -0.0068 0.0127  0.0197  146 LYS   B CG  
2916 C CD  . LYS   B 146 ? 0.5046 0.6331 0.5249 -0.0074 0.0139  0.0233  146 LYS   B CD  
2917 C CE  . LYS   B 146 ? 0.5578 0.6834 0.5829 -0.0110 0.0163  0.0260  146 LYS   B CE  
2918 N NZ  . LYS   B 146 ? 0.5935 0.7121 0.6199 -0.0106 0.0172  0.0291  146 LYS   B NZ  
2919 N N   . ASP   B 147 ? 0.2732 0.4180 0.2782 0.0032  0.0072  0.0117  147 ASP   B N   
2920 C CA  . ASP   B 147 ? 0.2639 0.4152 0.2657 0.0060  0.0061  0.0099  147 ASP   B CA  
2921 C C   . ASP   B 147 ? 0.2354 0.3817 0.2328 0.0087  0.0046  0.0070  147 ASP   B C   
2922 O O   . ASP   B 147 ? 0.2072 0.3463 0.2029 0.0091  0.0038  0.0046  147 ASP   B O   
2923 C CB  . ASP   B 147 ? 0.2836 0.4392 0.2852 0.0067  0.0056  0.0072  147 ASP   B CB  
2924 C CG  . ASP   B 147 ? 0.3391 0.5006 0.3370 0.0103  0.0043  0.0045  147 ASP   B CG  
2925 O OD1 . ASP   B 147 ? 0.3849 0.5541 0.3832 0.0106  0.0047  0.0062  147 ASP   B OD1 
2926 O OD2 . ASP   B 147 ? 0.3789 0.5365 0.3734 0.0130  0.0030  0.0010  147 ASP   B OD2 
2927 N N   . GLU   B 148 ? 0.2082 0.3594 0.2037 0.0104  0.0042  0.0068  148 GLU   B N   
2928 C CA  . GLU   B 148 ? 0.2042 0.3515 0.1956 0.0125  0.0029  0.0037  148 GLU   B CA  
2929 C C   . GLU   B 148 ? 0.2117 0.3547 0.1998 0.0148  0.0017  -0.0004 148 GLU   B C   
2930 O O   . GLU   B 148 ? 0.2188 0.3534 0.2044 0.0152  0.0011  -0.0024 148 GLU   B O   
2931 C CB  . GLU   B 148 ? 0.2246 0.3796 0.2150 0.0138  0.0028  0.0038  148 GLU   B CB  
2932 C CG  . GLU   B 148 ? 0.2427 0.3939 0.2289 0.0158  0.0015  -0.0004 148 GLU   B CG  
2933 C CD  . GLU   B 148 ? 0.3142 0.4726 0.2992 0.0169  0.0013  -0.0015 148 GLU   B CD  
2934 O OE1 . GLU   B 148 ? 0.3327 0.5003 0.3198 0.0166  0.0020  0.0015  148 GLU   B OE1 
2935 O OE2 . GLU   B 148 ? 0.3629 0.5173 0.3445 0.0181  0.0004  -0.0055 148 GLU   B OE2 
2936 N N   . ALA   B 149 ? 0.1997 0.3486 0.1878 0.0163  0.0014  -0.0015 149 ALA   B N   
2937 C CA  . ALA   B 149 ? 0.2112 0.3569 0.1958 0.0193  0.0002  -0.0052 149 ALA   B CA  
2938 C C   . ALA   B 149 ? 0.1939 0.3314 0.1785 0.0184  0.0002  -0.0054 149 ALA   B C   
2939 O O   . ALA   B 149 ? 0.1865 0.3171 0.1675 0.0204  -0.0006 -0.0077 149 ALA   B O   
2940 C CB  . ALA   B 149 ? 0.2150 0.3702 0.1997 0.0215  0.0000  -0.0063 149 ALA   B CB  
2941 N N   . LEU   B 150 ? 0.2006 0.3394 0.1894 0.0153  0.0013  -0.0030 150 LEU   B N   
2942 C CA  . LEU   B 150 ? 0.2004 0.3331 0.1899 0.0142  0.0013  -0.0034 150 LEU   B CA  
2943 C C   . LEU   B 150 ? 0.1904 0.3139 0.1786 0.0131  0.0013  -0.0030 150 LEU   B C   
2944 O O   . LEU   B 150 ? 0.1710 0.2883 0.1573 0.0138  0.0008  -0.0044 150 LEU   B O   
2945 C CB  . LEU   B 150 ? 0.1974 0.3339 0.1920 0.0108  0.0026  -0.0013 150 LEU   B CB  
2946 C CG  . LEU   B 150 ? 0.2312 0.3762 0.2271 0.0112  0.0027  -0.0025 150 LEU   B CG  
2947 C CD1 . LEU   B 150 ? 0.2483 0.3963 0.2496 0.0069  0.0043  -0.0003 150 LEU   B CD1 
2948 C CD2 . LEU   B 150 ? 0.2603 0.4032 0.2538 0.0134  0.0017  -0.0054 150 LEU   B CD2 
2949 N N   . ILE   B 151 ? 0.1755 0.2992 0.1650 0.0116  0.0018  -0.0010 151 ILE   B N   
2950 C CA  . ILE   B 151 ? 0.1698 0.2861 0.1583 0.0105  0.0018  -0.0008 151 ILE   B CA  
2951 C C   . ILE   B 151 ? 0.1634 0.2747 0.1468 0.0128  0.0008  -0.0038 151 ILE   B C   
2952 O O   . ILE   B 151 ? 0.1702 0.2743 0.1520 0.0124  0.0006  -0.0046 151 ILE   B O   
2953 C CB  . ILE   B 151 ? 0.1653 0.2843 0.1558 0.0090  0.0026  0.0019  151 ILE   B CB  
2954 C CG1 . ILE   B 151 ? 0.1541 0.2749 0.1496 0.0066  0.0039  0.0051  151 ILE   B CG1 
2955 C CG2 . ILE   B 151 ? 0.1777 0.2911 0.1664 0.0085  0.0023  0.0012  151 ILE   B CG2 
2956 C CD1 . ILE   B 151 ? 0.1574 0.2825 0.1550 0.0058  0.0049  0.0086  151 ILE   B CD1 
2957 N N   . ARG   B 152 ? 0.1611 0.2762 0.1422 0.0151  0.0002  -0.0054 152 ARG   B N   
2958 C CA  . ARG   B 152 ? 0.1835 0.2931 0.1600 0.0173  -0.0006 -0.0084 152 ARG   B CA  
2959 C C   . ARG   B 152 ? 0.1920 0.2965 0.1662 0.0192  -0.0011 -0.0096 152 ARG   B C   
2960 O O   . ARG   B 152 ? 0.1986 0.2948 0.1695 0.0196  -0.0013 -0.0107 152 ARG   B O   
2961 C CB  . ARG   B 152 ? 0.2010 0.3158 0.1755 0.0199  -0.0011 -0.0105 152 ARG   B CB  
2962 C CG  . ARG   B 152 ? 0.2352 0.3550 0.2109 0.0184  -0.0008 -0.0099 152 ARG   B CG  
2963 C CD  . ARG   B 152 ? 0.2616 0.3864 0.2351 0.0210  -0.0014 -0.0127 152 ARG   B CD  
2964 N NE  . ARG   B 152 ? 0.3145 0.4468 0.2899 0.0196  -0.0009 -0.0116 152 ARG   B NE  
2965 C CZ  . ARG   B 152 ? 0.3576 0.4882 0.3324 0.0180  -0.0008 -0.0124 152 ARG   B CZ  
2966 N NH1 . ARG   B 152 ? 0.3669 0.4878 0.3391 0.0172  -0.0010 -0.0147 152 ARG   B NH1 
2967 N NH2 . ARG   B 152 ? 0.3387 0.4780 0.3155 0.0171  -0.0004 -0.0109 152 ARG   B NH2 
2968 N N   . LYS   B 153 ? 0.1948 0.3049 0.1705 0.0204  -0.0011 -0.0093 153 LYS   B N   
2969 C CA  . LYS   B 153 ? 0.2152 0.3229 0.1887 0.0230  -0.0017 -0.0106 153 LYS   B CA  
2970 C C   . LYS   B 153 ? 0.1916 0.2925 0.1653 0.0211  -0.0014 -0.0097 153 LYS   B C   
2971 O O   . LYS   B 153 ? 0.1940 0.2883 0.1640 0.0229  -0.0018 -0.0106 153 LYS   B O   
2972 C CB  . LYS   B 153 ? 0.2334 0.3501 0.2090 0.0241  -0.0018 -0.0107 153 LYS   B CB  
2973 C CG  . LYS   B 153 ? 0.2633 0.3791 0.2362 0.0276  -0.0024 -0.0122 153 LYS   B CG  
2974 C CD  . LYS   B 153 ? 0.2933 0.4031 0.2603 0.0322  -0.0033 -0.0142 153 LYS   B CD  
2975 C CE  . LYS   B 153 ? 0.3468 0.4621 0.3126 0.0350  -0.0037 -0.0158 153 LYS   B CE  
2976 N NZ  . LYS   B 153 ? 0.3793 0.4880 0.3395 0.0397  -0.0044 -0.0180 153 LYS   B NZ  
2977 N N   . ALA   B 154 ? 0.1821 0.2849 0.1603 0.0175  -0.0006 -0.0078 154 ALA   B N   
2978 C CA  . ALA   B 154 ? 0.1617 0.2593 0.1407 0.0156  -0.0004 -0.0072 154 ALA   B CA  
2979 C C   . ALA   B 154 ? 0.1686 0.2579 0.1442 0.0152  -0.0005 -0.0075 154 ALA   B C   
2980 O O   . ALA   B 154 ? 0.1606 0.2444 0.1342 0.0153  -0.0006 -0.0077 154 ALA   B O   
2981 C CB  . ALA   B 154 ? 0.1502 0.2507 0.1346 0.0121  0.0006  -0.0054 154 ALA   B CB  
2982 N N   . SER   B 155 ? 0.1652 0.2544 0.1406 0.0143  -0.0003 -0.0073 155 SER   B N   
2983 C CA  . SER   B 155 ? 0.1710 0.2534 0.1435 0.0133  -0.0003 -0.0079 155 SER   B CA  
2984 C C   . SER   B 155 ? 0.1702 0.2462 0.1374 0.0160  -0.0007 -0.0098 155 SER   B C   
2985 O O   . SER   B 155 ? 0.1820 0.2510 0.1467 0.0153  -0.0006 -0.0099 155 SER   B O   
2986 C CB  . SER   B 155 ? 0.1748 0.2601 0.1482 0.0120  0.0000  -0.0079 155 SER   B CB  
2987 O OG  . SER   B 155 ? 0.1654 0.2563 0.1434 0.0100  0.0005  -0.0056 155 SER   B OG  
2988 N N   . GLU   B 156 ? 0.1723 0.2509 0.1378 0.0192  -0.0013 -0.0112 156 GLU   B N   
2989 C CA  . GLU   B 156 ? 0.2021 0.2741 0.1624 0.0225  -0.0016 -0.0129 156 GLU   B CA  
2990 C C   . GLU   B 156 ? 0.1966 0.2647 0.1551 0.0241  -0.0017 -0.0120 156 GLU   B C   
2991 O O   . GLU   B 156 ? 0.2098 0.2693 0.1641 0.0250  -0.0015 -0.0122 156 GLU   B O   
2992 C CB  . GLU   B 156 ? 0.2436 0.3213 0.2032 0.0261  -0.0022 -0.0144 156 GLU   B CB  
2993 C CG  . GLU   B 156 ? 0.2924 0.3646 0.2469 0.0308  -0.0027 -0.0162 156 GLU   B CG  
2994 C CD  . GLU   B 156 ? 0.3740 0.4545 0.3286 0.0348  -0.0034 -0.0173 156 GLU   B CD  
2995 O OE1 . GLU   B 156 ? 0.3626 0.4517 0.3203 0.0339  -0.0034 -0.0176 156 GLU   B OE1 
2996 O OE2 . GLU   B 156 ? 0.5079 0.5874 0.4599 0.0389  -0.0038 -0.0175 156 GLU   B OE2 
2997 N N   . ILE   B 157 ? 0.1883 0.2631 0.1497 0.0246  -0.0019 -0.0112 157 ILE   B N   
2998 C CA  . ILE   B 157 ? 0.1929 0.2665 0.1529 0.0265  -0.0021 -0.0106 157 ILE   B CA  
2999 C C   . ILE   B 157 ? 0.2110 0.2784 0.1708 0.0235  -0.0015 -0.0094 157 ILE   B C   
3000 O O   . ILE   B 157 ? 0.2112 0.2725 0.1670 0.0252  -0.0015 -0.0089 157 ILE   B O   
3001 C CB  . ILE   B 157 ? 0.1995 0.2830 0.1636 0.0265  -0.0022 -0.0106 157 ILE   B CB  
3002 C CG1 . ILE   B 157 ? 0.1925 0.2830 0.1563 0.0299  -0.0028 -0.0119 157 ILE   B CG1 
3003 C CG2 . ILE   B 157 ? 0.1993 0.2828 0.1629 0.0274  -0.0023 -0.0102 157 ILE   B CG2 
3004 C CD1 . ILE   B 157 ? 0.1789 0.2800 0.1474 0.0288  -0.0027 -0.0119 157 ILE   B CD1 
3005 N N   . SER   B 158 ? 0.2094 0.2790 0.1733 0.0194  -0.0011 -0.0087 158 SER   B N   
3006 C CA  . SER   B 158 ? 0.1955 0.2606 0.1597 0.0164  -0.0006 -0.0078 158 SER   B CA  
3007 C C   . SER   B 158 ? 0.2092 0.2654 0.1685 0.0164  -0.0003 -0.0079 158 SER   B C   
3008 O O   . SER   B 158 ? 0.2178 0.2690 0.1747 0.0161  0.0000  -0.0071 158 SER   B O   
3009 C CB  . SER   B 158 ? 0.1954 0.2640 0.1642 0.0128  -0.0002 -0.0071 158 SER   B CB  
3010 O OG  . SER   B 158 ? 0.1842 0.2597 0.1575 0.0126  -0.0002 -0.0069 158 SER   B OG  
3011 N N   . ILE   B 159 ? 0.1996 0.2540 0.1577 0.0160  -0.0003 -0.0090 159 ILE   B N   
3012 C CA  . ILE   B 159 ? 0.2100 0.2557 0.1639 0.0153  0.0002  -0.0097 159 ILE   B CA  
3013 C C   . ILE   B 159 ? 0.2304 0.2690 0.1790 0.0190  0.0002  -0.0095 159 ILE   B C   
3014 O O   . ILE   B 159 ? 0.2328 0.2638 0.1782 0.0181  0.0008  -0.0086 159 ILE   B O   
3015 C CB  . ILE   B 159 ? 0.2049 0.2514 0.1588 0.0146  0.0002  -0.0116 159 ILE   B CB  
3016 C CG1 . ILE   B 159 ? 0.2038 0.2555 0.1618 0.0107  0.0005  -0.0113 159 ILE   B CG1 
3017 C CG2 . ILE   B 159 ? 0.2100 0.2467 0.1588 0.0147  0.0007  -0.0132 159 ILE   B CG2 
3018 C CD1 . ILE   B 159 ? 0.2139 0.2701 0.1728 0.0105  0.0003  -0.0129 159 ILE   B CD1 
3019 N N   . LYS   B 160 ? 0.2264 0.2677 0.1740 0.0234  -0.0005 -0.0102 160 LYS   B N   
3020 C CA  . LYS   B 160 ? 0.2484 0.2837 0.1909 0.0279  -0.0005 -0.0098 160 LYS   B CA  
3021 C C   . LYS   B 160 ? 0.2459 0.2802 0.1875 0.0282  -0.0003 -0.0076 160 LYS   B C   
3022 O O   . LYS   B 160 ? 0.2587 0.2850 0.1955 0.0302  0.0002  -0.0064 160 LYS   B O   
3023 C CB  . LYS   B 160 ? 0.2671 0.3081 0.2092 0.0330  -0.0014 -0.0110 160 LYS   B CB  
3024 C CG  . LYS   B 160 ? 0.3013 0.3427 0.2431 0.0337  -0.0016 -0.0134 160 LYS   B CG  
3025 C CD  . LYS   B 160 ? 0.3507 0.3983 0.2919 0.0390  -0.0025 -0.0146 160 LYS   B CD  
3026 C CE  . LYS   B 160 ? 0.4094 0.4549 0.3487 0.0409  -0.0026 -0.0174 160 LYS   B CE  
3027 N NZ  . LYS   B 160 ? 0.4480 0.5037 0.3887 0.0444  -0.0035 -0.0188 160 LYS   B NZ  
3028 N N   . ALA   B 161 ? 0.2364 0.2788 0.1826 0.0263  -0.0006 -0.0070 161 ALA   B N   
3029 C CA  . ALA   B 161 ? 0.2464 0.2896 0.1924 0.0264  -0.0004 -0.0054 161 ALA   B CA  
3030 C C   . ALA   B 161 ? 0.2717 0.3092 0.2170 0.0223  0.0004  -0.0041 161 ALA   B C   
3031 O O   . ALA   B 161 ? 0.2525 0.2905 0.1971 0.0224  0.0006  -0.0027 161 ALA   B O   
3032 C CB  . ALA   B 161 ? 0.2378 0.2918 0.1890 0.0260  -0.0010 -0.0059 161 ALA   B CB  
3033 N N   . GLY   B 162 ? 0.2403 0.2740 0.1860 0.0187  0.0009  -0.0048 162 GLY   B N   
3034 C CA  . GLY   B 162 ? 0.2571 0.2851 0.2015 0.0148  0.0018  -0.0039 162 GLY   B CA  
3035 C C   . GLY   B 162 ? 0.2277 0.2615 0.1773 0.0104  0.0019  -0.0043 162 GLY   B C   
3036 O O   . GLY   B 162 ? 0.2402 0.2722 0.1896 0.0073  0.0025  -0.0035 162 GLY   B O   
3037 N N   . ALA   B 163 ? 0.2094 0.2502 0.1634 0.0102  0.0013  -0.0053 163 ALA   B N   
3038 C CA  . ALA   B 163 ? 0.2085 0.2539 0.1671 0.0065  0.0015  -0.0055 163 ALA   B CA  
3039 C C   . ALA   B 163 ? 0.2021 0.2431 0.1591 0.0031  0.0022  -0.0059 163 ALA   B C   
3040 O O   . ALA   B 163 ? 0.2289 0.2657 0.1832 0.0032  0.0024  -0.0070 163 ALA   B O   
3041 C CB  . ALA   B 163 ? 0.2090 0.2610 0.1716 0.0071  0.0010  -0.0061 163 ALA   B CB  
3042 N N   . ASP   B 164 ? 0.1938 0.2362 0.1524 0.0001  0.0026  -0.0054 164 ASP   B N   
3043 C CA  . ASP   B 164 ? 0.2051 0.2457 0.1630 -0.0036 0.0032  -0.0060 164 ASP   B CA  
3044 C C   . ASP   B 164 ? 0.1865 0.2335 0.1484 -0.0048 0.0030  -0.0069 164 ASP   B C   
3045 O O   . ASP   B 164 ? 0.2163 0.2631 0.1775 -0.0073 0.0034  -0.0080 164 ASP   B O   
3046 C CB  . ASP   B 164 ? 0.1961 0.2364 0.1538 -0.0061 0.0038  -0.0051 164 ASP   B CB  
3047 C CG  . ASP   B 164 ? 0.2157 0.2502 0.1692 -0.0048 0.0041  -0.0037 164 ASP   B CG  
3048 O OD1 . ASP   B 164 ? 0.2234 0.2505 0.1725 -0.0042 0.0046  -0.0037 164 ASP   B OD1 
3049 O OD2 . ASP   B 164 ? 0.2113 0.2486 0.1657 -0.0043 0.0040  -0.0026 164 ASP   B OD2 
3050 N N   . PHE   B 165 ? 0.1850 0.2379 0.1510 -0.0033 0.0025  -0.0062 165 PHE   B N   
3051 C CA  . PHE   B 165 ? 0.1807 0.2397 0.1504 -0.0035 0.0024  -0.0062 165 PHE   B CA  
3052 C C   . PHE   B 165 ? 0.1707 0.2331 0.1428 -0.0009 0.0019  -0.0057 165 PHE   B C   
3053 O O   . PHE   B 165 ? 0.1549 0.2169 0.1274 0.0005  0.0017  -0.0053 165 PHE   B O   
3054 C CB  . PHE   B 165 ? 0.1964 0.2597 0.1699 -0.0051 0.0026  -0.0054 165 PHE   B CB  
3055 C CG  . PHE   B 165 ? 0.2211 0.2857 0.1943 -0.0079 0.0031  -0.0059 165 PHE   B CG  
3056 C CD1 . PHE   B 165 ? 0.2595 0.3207 0.2300 -0.0101 0.0035  -0.0064 165 PHE   B CD1 
3057 C CD2 . PHE   B 165 ? 0.2346 0.3048 0.2101 -0.0083 0.0031  -0.0059 165 PHE   B CD2 
3058 C CE1 . PHE   B 165 ? 0.2589 0.3224 0.2293 -0.0130 0.0039  -0.0072 165 PHE   B CE1 
3059 C CE2 . PHE   B 165 ? 0.2353 0.3080 0.2105 -0.0108 0.0035  -0.0067 165 PHE   B CE2 
3060 C CZ  . PHE   B 165 ? 0.2428 0.3124 0.2156 -0.0133 0.0039  -0.0075 165 PHE   B CZ  
3061 N N   . ILE   B 166 ? 0.1657 0.2322 0.1394 -0.0004 0.0019  -0.0057 166 ILE   B N   
3062 C CA  . ILE   B 166 ? 0.1624 0.2337 0.1395 0.0012  0.0017  -0.0047 166 ILE   B CA  
3063 C C   . ILE   B 166 ? 0.1668 0.2430 0.1481 0.0000  0.0021  -0.0031 166 ILE   B C   
3064 O O   . ILE   B 166 ? 0.1692 0.2474 0.1504 -0.0010 0.0023  -0.0031 166 ILE   B O   
3065 C CB  . ILE   B 166 ? 0.1688 0.2414 0.1443 0.0034  0.0013  -0.0054 166 ILE   B CB  
3066 C CG1 . ILE   B 166 ? 0.1842 0.2582 0.1583 0.0029  0.0014  -0.0064 166 ILE   B CG1 
3067 C CG2 . ILE   B 166 ? 0.1968 0.2647 0.1687 0.0055  0.0009  -0.0064 166 ILE   B CG2 
3068 C CD1 . ILE   B 166 ? 0.1919 0.2686 0.1650 0.0053  0.0010  -0.0074 166 ILE   B CD1 
3069 N N   . LYS   B 167 ? 0.1620 0.2403 0.1469 0.0004  0.0024  -0.0019 167 LYS   B N   
3070 C CA  . LYS   B 167 ? 0.1717 0.2531 0.1608 -0.0004 0.0030  -0.0002 167 LYS   B CA  
3071 C C   . LYS   B 167 ? 0.1650 0.2500 0.1574 0.0004  0.0034  0.0014  167 LYS   B C   
3072 O O   . LYS   B 167 ? 0.1599 0.2450 0.1527 0.0010  0.0033  0.0008  167 LYS   B O   
3073 C CB  . LYS   B 167 ? 0.1786 0.2573 0.1688 -0.0012 0.0031  -0.0008 167 LYS   B CB  
3074 C CG  . LYS   B 167 ? 0.1911 0.2716 0.1858 -0.0016 0.0037  0.0006  167 LYS   B CG  
3075 C CD  . LYS   B 167 ? 0.1852 0.2635 0.1803 -0.0024 0.0037  -0.0006 167 LYS   B CD  
3076 C CE  . LYS   B 167 ? 0.2019 0.2813 0.2016 -0.0023 0.0044  0.0005  167 LYS   B CE  
3077 N NZ  . LYS   B 167 ? 0.2463 0.3246 0.2473 -0.0028 0.0044  -0.0009 167 LYS   B NZ  
3078 N N   . THR   B 168 ? 0.1585 0.2470 0.1535 0.0003  0.0040  0.0036  168 THR   B N   
3079 C CA  . THR   B 168 ? 0.1602 0.2524 0.1578 0.0008  0.0046  0.0056  168 THR   B CA  
3080 C C   . THR   B 168 ? 0.1687 0.2594 0.1699 0.0001  0.0052  0.0059  168 THR   B C   
3081 O O   . THR   B 168 ? 0.1435 0.2362 0.1456 0.0001  0.0054  0.0059  168 THR   B O   
3082 C CB  . THR   B 168 ? 0.1730 0.2693 0.1722 0.0012  0.0053  0.0085  168 THR   B CB  
3083 O OG1 . THR   B 168 ? 0.1666 0.2613 0.1684 0.0009  0.0059  0.0098  168 THR   B OG1 
3084 C CG2 . THR   B 168 ? 0.1758 0.2751 0.1716 0.0017  0.0046  0.0074  168 THR   B CG2 
3085 N N   . SER   B 169 ? 0.1392 0.2269 0.1425 -0.0007 0.0056  0.0059  169 SER   B N   
3086 C CA  . SER   B 169 ? 0.1486 0.2354 0.1564 -0.0015 0.0067  0.0069  169 SER   B CA  
3087 C C   . SER   B 169 ? 0.1505 0.2336 0.1597 -0.0022 0.0067  0.0050  169 SER   B C   
3088 O O   . SER   B 169 ? 0.1561 0.2380 0.1633 -0.0019 0.0061  0.0041  169 SER   B O   
3089 C CB  . SER   B 169 ? 0.1641 0.2522 0.1744 -0.0012 0.0078  0.0105  169 SER   B CB  
3090 O OG  . SER   B 169 ? 0.1490 0.2417 0.1582 -0.0005 0.0078  0.0124  169 SER   B OG  
3091 N N   . THR   B 170 ? 0.1703 0.2522 0.1833 -0.0033 0.0075  0.0044  170 THR   B N   
3092 C CA  . THR   B 170 ? 0.1725 0.2515 0.1876 -0.0038 0.0077  0.0025  170 THR   B CA  
3093 C C   . THR   B 170 ? 0.1826 0.2594 0.2007 -0.0034 0.0087  0.0045  170 THR   B C   
3094 O O   . THR   B 170 ? 0.1822 0.2570 0.2014 -0.0032 0.0087  0.0030  170 THR   B O   
3095 C CB  . THR   B 170 ? 0.1737 0.2528 0.1920 -0.0054 0.0082  0.0003  170 THR   B CB  
3096 O OG1 . THR   B 170 ? 0.1652 0.2443 0.1869 -0.0064 0.0096  0.0027  170 THR   B OG1 
3097 C CG2 . THR   B 170 ? 0.1705 0.2524 0.1859 -0.0052 0.0071  -0.0020 170 THR   B CG2 
3098 N N   . GLY   B 171 ? 0.1761 0.2536 0.1954 -0.0030 0.0097  0.0081  171 GLY   B N   
3099 C CA  . GLY   B 171 ? 0.1946 0.2696 0.2169 -0.0021 0.0109  0.0107  171 GLY   B CA  
3100 C C   . GLY   B 171 ? 0.2108 0.2819 0.2379 -0.0037 0.0124  0.0103  171 GLY   B C   
3101 O O   . GLY   B 171 ? 0.2604 0.3279 0.2902 -0.0029 0.0136  0.0123  171 GLY   B O   
3102 N N   . ARG   B 172 ? 0.2269 0.2987 0.2549 -0.0058 0.0124  0.0078  172 ARG   B N   
3103 C CA  . ARG   B 172 ? 0.2591 0.3275 0.2918 -0.0079 0.0138  0.0063  172 ARG   B CA  
3104 C C   . ARG   B 172 ? 0.2427 0.3124 0.2773 -0.0100 0.0150  0.0082  172 ARG   B C   
3105 O O   . ARG   B 172 ? 0.2738 0.3414 0.3123 -0.0126 0.0163  0.0065  172 ARG   B O   
3106 C CB  . ARG   B 172 ? 0.2572 0.3263 0.2903 -0.0092 0.0129  0.0010  172 ARG   B CB  
3107 C CG  . ARG   B 172 ? 0.2986 0.3664 0.3306 -0.0076 0.0120  -0.0012 172 ARG   B CG  
3108 C CD  . ARG   B 172 ? 0.3694 0.4324 0.4042 -0.0065 0.0131  0.0002  172 ARG   B CD  
3109 N NE  . ARG   B 172 ? 0.4549 0.5181 0.4886 -0.0050 0.0121  -0.0024 172 ARG   B NE  
3110 C CZ  . ARG   B 172 ? 0.5506 0.6143 0.5855 -0.0059 0.0116  -0.0069 172 ARG   B CZ  
3111 N NH1 . ARG   B 172 ? 0.5607 0.6243 0.5986 -0.0082 0.0123  -0.0097 172 ARG   B NH1 
3112 N NH2 . ARG   B 172 ? 0.6216 0.6867 0.6548 -0.0045 0.0106  -0.0088 172 ARG   B NH2 
3113 N N   . VAL   B 173 ? 0.2240 0.2978 0.2561 -0.0092 0.0148  0.0113  173 VAL   B N   
3114 C CA  . VAL   B 173 ? 0.2281 0.3044 0.2618 -0.0111 0.0160  0.0135  173 VAL   B CA  
3115 C C   . VAL   B 173 ? 0.2427 0.3183 0.2766 -0.0098 0.0172  0.0193  173 VAL   B C   
3116 O O   . VAL   B 173 ? 0.2520 0.3266 0.2843 -0.0072 0.0168  0.0209  173 VAL   B O   
3117 C CB  . VAL   B 173 ? 0.2218 0.3049 0.2524 -0.0112 0.0146  0.0119  173 VAL   B CB  
3118 C CG1 . VAL   B 173 ? 0.2373 0.3216 0.2679 -0.0122 0.0136  0.0067  173 VAL   B CG1 
3119 C CG2 . VAL   B 173 ? 0.2180 0.3040 0.2438 -0.0082 0.0130  0.0130  173 VAL   B CG2 
3120 N N   . ALA   B 174 ? 0.2512 0.3288 0.2868 -0.0115 0.0188  0.0224  174 ALA   B N   
3121 C CA  . ALA   B 174 ? 0.2683 0.3455 0.3045 -0.0104 0.0203  0.0284  174 ALA   B CA  
3122 C C   . ALA   B 174 ? 0.2526 0.3353 0.2845 -0.0070 0.0189  0.0305  174 ALA   B C   
3123 O O   . ALA   B 174 ? 0.2577 0.3395 0.2893 -0.0046 0.0195  0.0344  174 ALA   B O   
3124 C CB  . ALA   B 174 ? 0.2804 0.3601 0.3188 -0.0133 0.0221  0.0310  174 ALA   B CB  
3125 N N   . VAL   B 175 ? 0.2287 0.3173 0.2573 -0.0067 0.0171  0.0278  175 VAL   B N   
3126 C CA  . VAL   B 175 ? 0.2087 0.3031 0.2335 -0.0040 0.0159  0.0292  175 VAL   B CA  
3127 C C   . VAL   B 175 ? 0.1965 0.2909 0.2179 -0.0030 0.0137  0.0247  175 VAL   B C   
3128 O O   . VAL   B 175 ? 0.1745 0.2692 0.1951 -0.0041 0.0128  0.0209  175 VAL   B O   
3129 C CB  . VAL   B 175 ? 0.2181 0.3200 0.2419 -0.0044 0.0160  0.0309  175 VAL   B CB  
3130 C CG1 . VAL   B 175 ? 0.2150 0.3231 0.2349 -0.0016 0.0148  0.0318  175 VAL   B CG1 
3131 C CG2 . VAL   B 175 ? 0.2373 0.3392 0.2645 -0.0059 0.0184  0.0358  175 VAL   B CG2 
3132 N N   . ASN   B 176 ? 0.1852 0.2795 0.2048 -0.0008 0.0130  0.0252  176 ASN   B N   
3133 C CA  . ASN   B 176 ? 0.1831 0.2770 0.1994 -0.0001 0.0113  0.0214  176 ASN   B CA  
3134 C C   . ASN   B 176 ? 0.1726 0.2727 0.1853 0.0013  0.0103  0.0217  176 ASN   B C   
3135 O O   . ASN   B 176 ? 0.1673 0.2718 0.1795 0.0012  0.0104  0.0226  176 ASN   B O   
3136 C CB  . ASN   B 176 ? 0.1969 0.2862 0.2144 0.0004  0.0114  0.0209  176 ASN   B CB  
3137 C CG  . ASN   B 176 ? 0.2306 0.3143 0.2519 -0.0012 0.0124  0.0198  176 ASN   B CG  
3138 O OD1 . ASN   B 176 ? 0.2905 0.3710 0.3151 -0.0012 0.0140  0.0225  176 ASN   B OD1 
3139 N ND2 . ASN   B 176 ? 0.1913 0.2739 0.2120 -0.0027 0.0116  0.0158  176 ASN   B ND2 
3140 N N   . ALA   B 177 ? 0.1665 0.2677 0.1769 0.0024  0.0095  0.0208  177 ALA   B N   
3141 C CA  . ALA   B 177 ? 0.1615 0.2681 0.1683 0.0033  0.0085  0.0199  177 ALA   B CA  
3142 C C   . ALA   B 177 ? 0.1447 0.2579 0.1524 0.0046  0.0093  0.0240  177 ALA   B C   
3143 O O   . ALA   B 177 ? 0.1564 0.2692 0.1667 0.0054  0.0106  0.0278  177 ALA   B O   
3144 C CB  . ALA   B 177 ? 0.1572 0.2639 0.1618 0.0037  0.0076  0.0179  177 ALA   B CB  
3145 N N   . THR   B 178 ? 0.1455 0.2644 0.1508 0.0051  0.0087  0.0230  178 THR   B N   
3146 C CA  . THR   B 178 ? 0.1439 0.2712 0.1489 0.0067  0.0091  0.0260  178 THR   B CA  
3147 C C   . THR   B 178 ? 0.1399 0.2716 0.1413 0.0071  0.0077  0.0224  178 THR   B C   
3148 O O   . THR   B 178 ? 0.1496 0.2778 0.1488 0.0062  0.0067  0.0182  178 THR   B O   
3149 C CB  . THR   B 178 ? 0.1422 0.2738 0.1484 0.0065  0.0099  0.0285  178 THR   B CB  
3150 O OG1 . THR   B 178 ? 0.1607 0.2936 0.1646 0.0061  0.0087  0.0245  178 THR   B OG1 
3151 C CG2 . THR   B 178 ? 0.1489 0.2751 0.1587 0.0051  0.0113  0.0310  178 THR   B CG2 
3152 N N   . PRO   B 179 ? 0.1502 0.2905 0.1508 0.0087  0.0078  0.0240  179 PRO   B N   
3153 C CA  . PRO   B 179 ? 0.1520 0.2969 0.1494 0.0087  0.0067  0.0199  179 PRO   B CA  
3154 C C   . PRO   B 179 ? 0.1518 0.2972 0.1473 0.0083  0.0059  0.0165  179 PRO   B C   
3155 O O   . PRO   B 179 ? 0.1668 0.3103 0.1595 0.0077  0.0048  0.0119  179 PRO   B O   
3156 C CB  . PRO   B 179 ? 0.1580 0.3137 0.1557 0.0106  0.0071  0.0228  179 PRO   B CB  
3157 C CG  . PRO   B 179 ? 0.1758 0.3297 0.1764 0.0118  0.0085  0.0284  179 PRO   B CG  
3158 C CD  . PRO   B 179 ? 0.1575 0.3023 0.1603 0.0104  0.0091  0.0295  179 PRO   B CD  
3159 N N   . GLU   B 180 ? 0.1593 0.3072 0.1561 0.0088  0.0064  0.0189  180 GLU   B N   
3160 C CA  . GLU   B 180 ? 0.1689 0.3181 0.1641 0.0090  0.0057  0.0159  180 GLU   B CA  
3161 C C   . GLU   B 180 ? 0.1586 0.2982 0.1527 0.0079  0.0050  0.0126  180 GLU   B C   
3162 O O   . GLU   B 180 ? 0.1470 0.2852 0.1382 0.0083  0.0040  0.0085  180 GLU   B O   
3163 C CB  . GLU   B 180 ? 0.1881 0.3430 0.1854 0.0095  0.0066  0.0197  180 GLU   B CB  
3164 C CG  . GLU   B 180 ? 0.2447 0.4029 0.2403 0.0102  0.0058  0.0167  180 GLU   B CG  
3165 C CD  . GLU   B 180 ? 0.3074 0.4741 0.3006 0.0117  0.0051  0.0141  180 GLU   B CD  
3166 O OE1 . GLU   B 180 ? 0.3714 0.5406 0.3632 0.0126  0.0044  0.0114  180 GLU   B OE1 
3167 O OE2 . GLU   B 180 ? 0.3130 0.4840 0.3057 0.0121  0.0051  0.0143  180 GLU   B OE2 
3168 N N   . SER   B 181 ? 0.1522 0.2854 0.1486 0.0068  0.0056  0.0143  181 SER   B N   
3169 C CA  . SER   B 181 ? 0.1634 0.2888 0.1585 0.0061  0.0049  0.0111  181 SER   B CA  
3170 C C   . SER   B 181 ? 0.1631 0.2835 0.1553 0.0056  0.0041  0.0078  181 SER   B C   
3171 O O   . SER   B 181 ? 0.1629 0.2791 0.1523 0.0057  0.0033  0.0044  181 SER   B O   
3172 C CB  . SER   B 181 ? 0.1833 0.3042 0.1815 0.0049  0.0057  0.0130  181 SER   B CB  
3173 O OG  . SER   B 181 ? 0.2233 0.3417 0.2235 0.0043  0.0064  0.0152  181 SER   B OG  
3174 N N   . ALA   B 182 ? 0.1530 0.2747 0.1456 0.0052  0.0043  0.0087  182 ALA   B N   
3175 C CA  . ALA   B 182 ? 0.1696 0.2884 0.1595 0.0042  0.0037  0.0055  182 ALA   B CA  
3176 C C   . ALA   B 182 ? 0.1794 0.3006 0.1660 0.0046  0.0030  0.0019  182 ALA   B C   
3177 O O   . ALA   B 182 ? 0.1733 0.2886 0.1570 0.0038  0.0024  -0.0015 182 ALA   B O   
3178 C CB  . ALA   B 182 ? 0.1731 0.2954 0.1645 0.0040  0.0042  0.0075  182 ALA   B CB  
3179 N N   . ARG   B 183 ? 0.1793 0.3091 0.1662 0.0059  0.0031  0.0026  183 ARG   B N   
3180 C CA  . ARG   B 183 ? 0.2058 0.3386 0.1899 0.0064  0.0024  -0.0012 183 ARG   B CA  
3181 C C   . ARG   B 183 ? 0.1710 0.2984 0.1530 0.0073  0.0018  -0.0037 183 ARG   B C   
3182 O O   . ARG   B 183 ? 0.1633 0.2864 0.1421 0.0071  0.0012  -0.0078 183 ARG   B O   
3183 C CB  . ARG   B 183 ? 0.2386 0.3830 0.2237 0.0079  0.0026  0.0002  183 ARG   B CB  
3184 C CG  . ARG   B 183 ? 0.2752 0.4236 0.2576 0.0087  0.0019  -0.0043 183 ARG   B CG  
3185 C CD  . ARG   B 183 ? 0.3267 0.4878 0.3103 0.0104  0.0021  -0.0027 183 ARG   B CD  
3186 N NE  . ARG   B 183 ? 0.4141 0.5774 0.3996 0.0117  0.0025  0.0009  183 ARG   B NE  
3187 C CZ  . ARG   B 183 ? 0.4422 0.6049 0.4266 0.0129  0.0020  -0.0009 183 ARG   B CZ  
3188 N NH1 . ARG   B 183 ? 0.4654 0.6249 0.4467 0.0136  0.0011  -0.0062 183 ARG   B NH1 
3189 N NH2 . ARG   B 183 ? 0.4832 0.6486 0.4696 0.0135  0.0025  0.0025  183 ARG   B NH2 
3190 N N   . ILE   B 184 ? 0.1705 0.2981 0.1542 0.0083  0.0020  -0.0014 184 ILE   B N   
3191 C CA  . ILE   B 184 ? 0.1699 0.2940 0.1518 0.0096  0.0014  -0.0035 184 ILE   B CA  
3192 C C   . ILE   B 184 ? 0.1715 0.2851 0.1509 0.0089  0.0011  -0.0057 184 ILE   B C   
3193 O O   . ILE   B 184 ? 0.1681 0.2775 0.1442 0.0100  0.0005  -0.0091 184 ILE   B O   
3194 C CB  . ILE   B 184 ? 0.1750 0.3023 0.1597 0.0102  0.0018  -0.0005 184 ILE   B CB  
3195 C CG1 . ILE   B 184 ? 0.1786 0.3165 0.1652 0.0110  0.0023  0.0017  184 ILE   B CG1 
3196 C CG2 . ILE   B 184 ? 0.1657 0.2891 0.1485 0.0118  0.0012  -0.0028 184 ILE   B CG2 
3197 C CD1 . ILE   B 184 ? 0.1808 0.3216 0.1710 0.0104  0.0033  0.0057  184 ILE   B CD1 
3198 N N   . MET   B 185 ? 0.1633 0.2726 0.1444 0.0072  0.0015  -0.0038 185 MET   B N   
3199 C CA  . MET   B 185 ? 0.1641 0.2643 0.1430 0.0065  0.0013  -0.0054 185 MET   B CA  
3200 C C   . MET   B 185 ? 0.1625 0.2588 0.1380 0.0054  0.0011  -0.0084 185 MET   B C   
3201 O O   . MET   B 185 ? 0.1560 0.2454 0.1283 0.0058  0.0008  -0.0106 185 MET   B O   
3202 C CB  . MET   B 185 ? 0.1598 0.2576 0.1414 0.0049  0.0018  -0.0029 185 MET   B CB  
3203 C CG  . MET   B 185 ? 0.1664 0.2665 0.1513 0.0055  0.0021  -0.0007 185 MET   B CG  
3204 S SD  . MET   B 185 ? 0.1692 0.2660 0.1575 0.0038  0.0027  0.0014  185 MET   B SD  
3205 C CE  . MET   B 185 ? 0.1727 0.2615 0.1579 0.0034  0.0022  -0.0011 185 MET   B CE  
3206 N N   . MET   B 186 ? 0.1801 0.2813 0.1564 0.0040  0.0013  -0.0086 186 MET   B N   
3207 C CA  . MET   B 186 ? 0.1844 0.2826 0.1579 0.0023  0.0013  -0.0119 186 MET   B CA  
3208 C C   . MET   B 186 ? 0.1936 0.2914 0.1641 0.0038  0.0009  -0.0154 186 MET   B C   
3209 O O   . MET   B 186 ? 0.2043 0.2952 0.1715 0.0029  0.0009  -0.0186 186 MET   B O   
3210 C CB  . MET   B 186 ? 0.1925 0.2971 0.1676 0.0005  0.0017  -0.0115 186 MET   B CB  
3211 C CG  . MET   B 186 ? 0.2140 0.3161 0.1908 -0.0012 0.0021  -0.0092 186 MET   B CG  
3212 S SD  . MET   B 186 ? 0.2224 0.3326 0.2007 -0.0029 0.0025  -0.0091 186 MET   B SD  
3213 C CE  . MET   B 186 ? 0.2181 0.3362 0.2007 -0.0005 0.0028  -0.0040 186 MET   B CE  
3214 N N   . GLU   B 187 ? 0.2075 0.3123 0.1792 0.0062  0.0006  -0.0149 187 GLU   B N   
3215 C CA  . GLU   B 187 ? 0.2412 0.3463 0.2103 0.0082  0.0001  -0.0184 187 GLU   B CA  
3216 C C   . GLU   B 187 ? 0.2211 0.3164 0.1873 0.0099  -0.0002 -0.0196 187 GLU   B C   
3217 O O   . GLU   B 187 ? 0.2238 0.3137 0.1865 0.0107  -0.0004 -0.0232 187 GLU   B O   
3218 C CB  . GLU   B 187 ? 0.2209 0.3365 0.1919 0.0106  -0.0002 -0.0173 187 GLU   B CB  
3219 C CG  . GLU   B 187 ? 0.2590 0.3851 0.2319 0.0097  0.0001  -0.0171 187 GLU   B CG  
3220 C CD  . GLU   B 187 ? 0.2936 0.4307 0.2683 0.0119  0.0000  -0.0155 187 GLU   B CD  
3221 O OE1 . GLU   B 187 ? 0.3315 0.4686 0.3061 0.0140  -0.0003 -0.0149 187 GLU   B OE1 
3222 O OE2 . GLU   B 187 ? 0.2980 0.4446 0.2740 0.0117  0.0002  -0.0150 187 GLU   B OE2 
3223 N N   . VAL   B 188 ? 0.2071 0.3000 0.1744 0.0106  -0.0002 -0.0167 188 VAL   B N   
3224 C CA  . VAL   B 188 ? 0.2253 0.3098 0.1896 0.0125  -0.0005 -0.0175 188 VAL   B CA  
3225 C C   . VAL   B 188 ? 0.2261 0.3002 0.1872 0.0106  -0.0001 -0.0191 188 VAL   B C   
3226 O O   . VAL   B 188 ? 0.2267 0.2935 0.1839 0.0123  -0.0002 -0.0213 188 VAL   B O   
3227 C CB  . VAL   B 188 ? 0.2265 0.3118 0.1930 0.0133  -0.0005 -0.0144 188 VAL   B CB  
3228 C CG1 . VAL   B 188 ? 0.2196 0.2968 0.1828 0.0154  -0.0008 -0.0151 188 VAL   B CG1 
3229 C CG2 . VAL   B 188 ? 0.2259 0.3209 0.1954 0.0148  -0.0007 -0.0130 188 VAL   B CG2 
3230 N N   . ILE   B 189 ? 0.2310 0.3043 0.1935 0.0072  0.0004  -0.0178 189 ILE   B N   
3231 C CA  . ILE   B 189 ? 0.2409 0.3055 0.2006 0.0046  0.0010  -0.0192 189 ILE   B CA  
3232 C C   . ILE   B 189 ? 0.2424 0.3040 0.1991 0.0041  0.0012  -0.0233 189 ILE   B C   
3233 O O   . ILE   B 189 ? 0.2285 0.2803 0.1813 0.0042  0.0015  -0.0250 189 ILE   B O   
3234 C CB  . ILE   B 189 ? 0.2304 0.2976 0.1925 0.0010  0.0015  -0.0175 189 ILE   B CB  
3235 C CG1 . ILE   B 189 ? 0.2339 0.3015 0.1985 0.0015  0.0014  -0.0141 189 ILE   B CG1 
3236 C CG2 . ILE   B 189 ? 0.2629 0.3233 0.2224 -0.0024 0.0022  -0.0194 189 ILE   B CG2 
3237 C CD1 . ILE   B 189 ? 0.2201 0.2913 0.1876 -0.0012 0.0018  -0.0124 189 ILE   B CD1 
3238 N N   . ARG   B 190 ? 0.2555 0.3258 0.2140 0.0036  0.0010  -0.0249 190 ARG   B N   
3239 C CA  . ARG   B 190 ? 0.2800 0.3490 0.2362 0.0029  0.0012  -0.0295 190 ARG   B CA  
3240 C C   . ARG   B 190 ? 0.2897 0.3536 0.2428 0.0068  0.0008  -0.0317 190 ARG   B C   
3241 O O   . ARG   B 190 ? 0.3012 0.3556 0.2507 0.0065  0.0012  -0.0349 190 ARG   B O   
3242 C CB  . ARG   B 190 ? 0.2845 0.3662 0.2435 0.0023  0.0010  -0.0306 190 ARG   B CB  
3243 C CG  . ARG   B 190 ? 0.3038 0.3857 0.2609 0.0010  0.0012  -0.0361 190 ARG   B CG  
3244 C CD  . ARG   B 190 ? 0.3338 0.4300 0.2935 0.0019  0.0008  -0.0370 190 ARG   B CD  
3245 N NE  . ARG   B 190 ? 0.3928 0.4938 0.3534 0.0063  0.0000  -0.0352 190 ARG   B NE  
3246 C CZ  . ARG   B 190 ? 0.3915 0.5053 0.3546 0.0078  -0.0003 -0.0342 190 ARG   B CZ  
3247 N NH1 . ARG   B 190 ? 0.3952 0.5185 0.3600 0.0060  -0.0001 -0.0351 190 ARG   B NH1 
3248 N NH2 . ARG   B 190 ? 0.3821 0.4999 0.3460 0.0113  -0.0009 -0.0322 190 ARG   B NH2 
3249 N N   . ASP   B 191 ? 0.2900 0.3606 0.2447 0.0106  0.0000  -0.0302 191 ASP   B N   
3250 C CA  . ASP   B 191 ? 0.3077 0.3760 0.2598 0.0149  -0.0005 -0.0325 191 ASP   B CA  
3251 C C   . ASP   B 191 ? 0.3299 0.3852 0.2780 0.0166  -0.0003 -0.0322 191 ASP   B C   
3252 O O   . ASP   B 191 ? 0.2946 0.3434 0.2392 0.0193  -0.0003 -0.0352 191 ASP   B O   
3253 C CB  . ASP   B 191 ? 0.3194 0.3978 0.2740 0.0181  -0.0013 -0.0304 191 ASP   B CB  
3254 C CG  . ASP   B 191 ? 0.3346 0.4262 0.2923 0.0176  -0.0015 -0.0308 191 ASP   B CG  
3255 O OD1 . ASP   B 191 ? 0.3641 0.4574 0.3216 0.0154  -0.0012 -0.0336 191 ASP   B OD1 
3256 O OD2 . ASP   B 191 ? 0.3528 0.4531 0.3133 0.0190  -0.0018 -0.0280 191 ASP   B OD2 
3257 N N   . MET   B 192 ? 0.2894 0.3410 0.2380 0.0153  0.0000  -0.0285 192 MET   B N   
3258 C CA  . MET   B 192 ? 0.2952 0.3356 0.2401 0.0172  0.0003  -0.0276 192 MET   B CA  
3259 C C   . MET   B 192 ? 0.3066 0.3356 0.2483 0.0139  0.0014  -0.0292 192 MET   B C   
3260 O O   . MET   B 192 ? 0.3185 0.3370 0.2565 0.0153  0.0018  -0.0283 192 MET   B O   
3261 C CB  . MET   B 192 ? 0.2908 0.3332 0.2376 0.0173  0.0001  -0.0234 192 MET   B CB  
3262 C CG  . MET   B 192 ? 0.2788 0.3307 0.2282 0.0206  -0.0008 -0.0221 192 MET   B CG  
3263 S SD  . MET   B 192 ? 0.2791 0.3322 0.2303 0.0209  -0.0009 -0.0182 192 MET   B SD  
3264 C CE  . MET   B 192 ? 0.3311 0.3734 0.2767 0.0249  -0.0008 -0.0181 192 MET   B CE  
3265 N N   . GLY   B 193 ? 0.3003 0.3319 0.2434 0.0095  0.0019  -0.0313 193 GLY   B N   
3266 C CA  . GLY   B 193 ? 0.3120 0.3341 0.2525 0.0054  0.0031  -0.0332 193 GLY   B CA  
3267 C C   . GLY   B 193 ? 0.3135 0.3310 0.2539 0.0025  0.0038  -0.0297 193 GLY   B C   
3268 O O   . GLY   B 193 ? 0.3131 0.3198 0.2501 0.0003  0.0049  -0.0302 193 GLY   B O   
3269 N N   . VAL   B 194 ? 0.2679 0.2932 0.2117 0.0024  0.0032  -0.0262 194 VAL   B N   
3270 C CA  . VAL   B 194 ? 0.2623 0.2838 0.2060 0.0004  0.0037  -0.0230 194 VAL   B CA  
3271 C C   . VAL   B 194 ? 0.2656 0.2938 0.2126 -0.0044 0.0041  -0.0226 194 VAL   B C   
3272 O O   . VAL   B 194 ? 0.2751 0.3042 0.2234 -0.0056 0.0042  -0.0198 194 VAL   B O   
3273 C CB  . VAL   B 194 ? 0.2594 0.2827 0.2038 0.0041  0.0030  -0.0195 194 VAL   B CB  
3274 C CG1 . VAL   B 194 ? 0.2756 0.2923 0.2162 0.0090  0.0028  -0.0198 194 VAL   B CG1 
3275 C CG2 . VAL   B 194 ? 0.2593 0.2947 0.2087 0.0051  0.0021  -0.0184 194 VAL   B CG2 
3276 N N   . GLU   B 195 ? 0.2519 0.2854 0.2003 -0.0068 0.0042  -0.0255 195 GLU   B N   
3277 C CA  . GLU   B 195 ? 0.2654 0.3071 0.2171 -0.0105 0.0044  -0.0252 195 GLU   B CA  
3278 C C   . GLU   B 195 ? 0.2793 0.3155 0.2295 -0.0148 0.0054  -0.0246 195 GLU   B C   
3279 O O   . GLU   B 195 ? 0.2832 0.3256 0.2362 -0.0169 0.0055  -0.0231 195 GLU   B O   
3280 C CB  . GLU   B 195 ? 0.2801 0.3298 0.2332 -0.0119 0.0043  -0.0286 195 GLU   B CB  
3281 C CG  . GLU   B 195 ? 0.3152 0.3587 0.2654 -0.0154 0.0053  -0.0331 195 GLU   B CG  
3282 C CD  . GLU   B 195 ? 0.3742 0.4084 0.3208 -0.0129 0.0054  -0.0356 195 GLU   B CD  
3283 O OE1 . GLU   B 195 ? 0.4002 0.4342 0.3465 -0.0080 0.0045  -0.0342 195 GLU   B OE1 
3284 O OE2 . GLU   B 195 ? 0.4470 0.4744 0.3911 -0.0161 0.0065  -0.0393 195 GLU   B OE2 
3285 N N   . LYS   B 196 ? 0.3029 0.3274 0.2489 -0.0159 0.0064  -0.0254 196 LYS   B N   
3286 C CA  . LYS   B 196 ? 0.3294 0.3489 0.2739 -0.0201 0.0075  -0.0245 196 LYS   B CA  
3287 C C   . LYS   B 196 ? 0.3160 0.3356 0.2612 -0.0185 0.0072  -0.0202 196 LYS   B C   
3288 O O   . LYS   B 196 ? 0.3033 0.3263 0.2499 -0.0216 0.0076  -0.0191 196 LYS   B O   
3289 C CB  . LYS   B 196 ? 0.3835 0.3902 0.3232 -0.0224 0.0089  -0.0264 196 LYS   B CB  
3290 C CG  . LYS   B 196 ? 0.4635 0.4729 0.4038 -0.0266 0.0096  -0.0312 196 LYS   B CG  
3291 C CD  . LYS   B 196 ? 0.5993 0.5958 0.5353 -0.0300 0.0113  -0.0338 196 LYS   B CD  
3292 C CE  . LYS   B 196 ? 0.6376 0.6388 0.5747 -0.0344 0.0119  -0.0392 196 LYS   B CE  
3293 N NZ  . LYS   B 196 ? 0.7122 0.6999 0.6453 -0.0365 0.0134  -0.0424 196 LYS   B NZ  
3294 N N   . SER   B 197 ? 0.2951 0.3125 0.2396 -0.0136 0.0064  -0.0182 197 SER   B N   
3295 C CA  . SER   B 197 ? 0.2864 0.3026 0.2308 -0.0121 0.0063  -0.0147 197 SER   B CA  
3296 C C   . SER   B 197 ? 0.2613 0.2874 0.2104 -0.0096 0.0051  -0.0130 197 SER   B C   
3297 O O   . SER   B 197 ? 0.2533 0.2803 0.2031 -0.0087 0.0049  -0.0107 197 SER   B O   
3298 C CB  . SER   B 197 ? 0.3021 0.3086 0.2421 -0.0086 0.0065  -0.0135 197 SER   B CB  
3299 O OG  . SER   B 197 ? 0.3195 0.3268 0.2594 -0.0042 0.0056  -0.0148 197 SER   B OG  
3300 N N   . VAL   B 198 ? 0.2459 0.2793 0.1979 -0.0085 0.0044  -0.0142 198 VAL   B N   
3301 C CA  . VAL   B 198 ? 0.2212 0.2626 0.1775 -0.0062 0.0035  -0.0124 198 VAL   B CA  
3302 C C   . VAL   B 198 ? 0.2101 0.2603 0.1703 -0.0081 0.0034  -0.0128 198 VAL   B C   
3303 O O   . VAL   B 198 ? 0.2069 0.2601 0.1671 -0.0086 0.0034  -0.0148 198 VAL   B O   
3304 C CB  . VAL   B 198 ? 0.2067 0.2489 0.1628 -0.0019 0.0028  -0.0126 198 VAL   B CB  
3305 C CG1 . VAL   B 198 ? 0.1875 0.2377 0.1481 -0.0003 0.0021  -0.0108 198 VAL   B CG1 
3306 C CG2 . VAL   B 198 ? 0.2205 0.2544 0.1723 0.0007  0.0028  -0.0122 198 VAL   B CG2 
3307 N N   . GLY   B 199 ? 0.1976 0.2525 0.1611 -0.0086 0.0033  -0.0109 199 GLY   B N   
3308 C CA  . GLY   B 199 ? 0.1951 0.2585 0.1624 -0.0095 0.0033  -0.0105 199 GLY   B CA  
3309 C C   . GLY   B 199 ? 0.1921 0.2610 0.1630 -0.0066 0.0028  -0.0088 199 GLY   B C   
3310 O O   . GLY   B 199 ? 0.1625 0.2293 0.1332 -0.0043 0.0024  -0.0081 199 GLY   B O   
3311 N N   . PHE   B 200 ? 0.1561 0.2323 0.1302 -0.0069 0.0028  -0.0080 200 PHE   B N   
3312 C CA  . PHE   B 200 ? 0.1538 0.2351 0.1315 -0.0047 0.0027  -0.0058 200 PHE   B CA  
3313 C C   . PHE   B 200 ? 0.1560 0.2408 0.1371 -0.0051 0.0030  -0.0039 200 PHE   B C   
3314 O O   . PHE   B 200 ? 0.1644 0.2521 0.1456 -0.0067 0.0032  -0.0043 200 PHE   B O   
3315 C CB  . PHE   B 200 ? 0.1608 0.2478 0.1385 -0.0041 0.0026  -0.0064 200 PHE   B CB  
3316 C CG  . PHE   B 200 ? 0.1734 0.2667 0.1549 -0.0022 0.0027  -0.0036 200 PHE   B CG  
3317 C CD1 . PHE   B 200 ? 0.1845 0.2771 0.1672 -0.0004 0.0026  -0.0024 200 PHE   B CD1 
3318 C CD2 . PHE   B 200 ? 0.1893 0.2892 0.1732 -0.0023 0.0031  -0.0020 200 PHE   B CD2 
3319 C CE1 . PHE   B 200 ? 0.1921 0.2897 0.1783 0.0007  0.0030  0.0004  200 PHE   B CE1 
3320 C CE2 . PHE   B 200 ? 0.2029 0.3074 0.1901 -0.0005 0.0034  0.0012  200 PHE   B CE2 
3321 C CZ  . PHE   B 200 ? 0.2050 0.3079 0.1933 0.0007  0.0034  0.0024  200 PHE   B CZ  
3322 N N   . LYS   B 201 ? 0.1482 0.2332 0.1323 -0.0037 0.0031  -0.0019 201 LYS   B N   
3323 C CA  A LYS   B 201 ? 0.1518 0.2393 0.1394 -0.0036 0.0034  -0.0002 201 LYS   B CA  
3324 C CA  B LYS   B 201 ? 0.1455 0.2329 0.1331 -0.0036 0.0034  -0.0002 201 LYS   B CA  
3325 C C   . LYS   B 201 ? 0.1480 0.2389 0.1391 -0.0018 0.0038  0.0023  201 LYS   B C   
3326 O O   . LYS   B 201 ? 0.1442 0.2337 0.1358 -0.0011 0.0038  0.0027  201 LYS   B O   
3327 C CB  A LYS   B 201 ? 0.1499 0.2333 0.1381 -0.0041 0.0034  -0.0006 201 LYS   B CB  
3328 C CB  B LYS   B 201 ? 0.1354 0.2186 0.1234 -0.0042 0.0034  -0.0007 201 LYS   B CB  
3329 C CG  A LYS   B 201 ? 0.1554 0.2410 0.1476 -0.0035 0.0039  0.0009  201 LYS   B CG  
3330 C CG  B LYS   B 201 ? 0.1319 0.2170 0.1237 -0.0038 0.0038  0.0006  201 LYS   B CG  
3331 C CD  A LYS   B 201 ? 0.1603 0.2432 0.1532 -0.0041 0.0039  -0.0001 201 LYS   B CD  
3332 C CD  B LYS   B 201 ? 0.1287 0.2109 0.1208 -0.0044 0.0038  -0.0005 201 LYS   B CD  
3333 C CE  A LYS   B 201 ? 0.1790 0.2641 0.1755 -0.0034 0.0043  0.0010  201 LYS   B CE  
3334 C CE  B LYS   B 201 ? 0.1300 0.2132 0.1264 -0.0035 0.0042  0.0005  201 LYS   B CE  
3335 N NZ  A LYS   B 201 ? 0.1801 0.2639 0.1806 -0.0022 0.0048  0.0020  201 LYS   B NZ  
3336 N NZ  B LYS   B 201 ? 0.1303 0.2116 0.1275 -0.0039 0.0041  -0.0010 201 LYS   B NZ  
3337 N N   . VAL   B 202 ? 0.1568 0.2526 0.1499 -0.0012 0.0043  0.0042  202 VAL   B N   
3338 C CA  . VAL   B 202 ? 0.1764 0.2751 0.1728 0.0004  0.0049  0.0074  202 VAL   B CA  
3339 C C   . VAL   B 202 ? 0.1911 0.2871 0.1909 0.0007  0.0055  0.0087  202 VAL   B C   
3340 O O   . VAL   B 202 ? 0.1935 0.2899 0.1934 0.0006  0.0055  0.0082  202 VAL   B O   
3341 C CB  . VAL   B 202 ? 0.2142 0.3202 0.2108 0.0015  0.0052  0.0092  202 VAL   B CB  
3342 C CG1 . VAL   B 202 ? 0.2648 0.3739 0.2601 0.0008  0.0050  0.0078  202 VAL   B CG1 
3343 C CG2 . VAL   B 202 ? 0.2217 0.3301 0.2218 0.0033  0.0062  0.0133  202 VAL   B CG2 
3344 N N   . THR   B 203 ? 0.1726 0.2661 0.1749 0.0010  0.0060  0.0099  203 THR   B N   
3345 C CA  . THR   B 203 ? 0.1711 0.2617 0.1771 0.0012  0.0068  0.0109  203 THR   B CA  
3346 C C   . THR   B 203 ? 0.1878 0.2797 0.1968 0.0023  0.0080  0.0146  203 THR   B C   
3347 O O   . THR   B 203 ? 0.1807 0.2734 0.1900 0.0019  0.0082  0.0155  203 THR   B O   
3348 C CB  . THR   B 203 ? 0.1953 0.2813 0.2017 0.0000  0.0065  0.0084  203 THR   B CB  
3349 O OG1 . THR   B 203 ? 0.2125 0.2975 0.2160 -0.0007 0.0057  0.0058  203 THR   B OG1 
3350 C CG2 . THR   B 203 ? 0.1880 0.2709 0.1986 0.0000  0.0074  0.0088  203 THR   B CG2 
3351 N N   . GLY   B 204 ? 0.2001 0.2921 0.2113 0.0037  0.0088  0.0170  204 GLY   B N   
3352 C CA  . GLY   B 204 ? 0.2331 0.3255 0.2471 0.0050  0.0102  0.0213  204 GLY   B CA  
3353 C C   . GLY   B 204 ? 0.2811 0.3805 0.2933 0.0063  0.0102  0.0239  204 GLY   B C   
3354 O O   . GLY   B 204 ? 0.2439 0.3473 0.2529 0.0059  0.0091  0.0217  204 GLY   B O   
3355 N N   . GLY   B 205 ? 0.3653 0.4660 0.3796 0.0079  0.0116  0.0285  205 GLY   B N   
3356 C CA  . GLY   B 205 ? 0.3907 0.4989 0.4038 0.0095  0.0118  0.0318  205 GLY   B CA  
3357 C C   . GLY   B 205 ? 0.4298 0.5446 0.4405 0.0113  0.0110  0.0313  205 GLY   B C   
3358 O O   . GLY   B 205 ? 0.5051 0.6278 0.5142 0.0124  0.0108  0.0325  205 GLY   B O   
3359 N N   . VAL   B 206 ? 0.4198 0.5325 0.4304 0.0116  0.0105  0.0291  206 VAL   B N   
3360 C CA  . VAL   B 206 ? 0.4418 0.5616 0.4506 0.0131  0.0099  0.0285  206 VAL   B CA  
3361 C C   . VAL   B 206 ? 0.4761 0.5944 0.4869 0.0158  0.0106  0.0307  206 VAL   B C   
3362 O O   . VAL   B 206 ? 0.4776 0.5934 0.4885 0.0154  0.0101  0.0279  206 VAL   B O   
3363 C CB  . VAL   B 206 ? 0.4520 0.5726 0.4579 0.0107  0.0085  0.0232  206 VAL   B CB  
3364 C CG1 . VAL   B 206 ? 0.4546 0.5843 0.4585 0.0115  0.0079  0.0223  206 VAL   B CG1 
3365 C CG2 . VAL   B 206 ? 0.4993 0.6181 0.5035 0.0082  0.0078  0.0208  206 VAL   B CG2 
3366 N N   . SER   B 207 ? 0.4289 0.5489 0.4413 0.0189  0.0119  0.0359  207 SER   B N   
3367 C CA  . SER   B 207 ? 0.4944 0.6117 0.5089 0.0221  0.0129  0.0386  207 SER   B CA  
3368 C C   . SER   B 207 ? 0.4413 0.5676 0.4541 0.0249  0.0123  0.0385  207 SER   B C   
3369 O O   . SER   B 207 ? 0.4724 0.5971 0.4863 0.0271  0.0124  0.0382  207 SER   B O   
3370 C CB  . SER   B 207 ? 0.5017 0.6162 0.5184 0.0243  0.0148  0.0446  207 SER   B CB  
3371 O OG  . SER   B 207 ? 0.5969 0.7085 0.6141 0.0213  0.0151  0.0449  207 SER   B OG  
3372 N N   . THR   B 208 ? 0.3902 0.5267 0.4007 0.0250  0.0116  0.0383  208 THR   B N   
3373 C CA  . THR   B 208 ? 0.3612 0.5086 0.3703 0.0281  0.0113  0.0391  208 THR   B CA  
3374 C C   . THR   B 208 ? 0.3390 0.4937 0.3454 0.0250  0.0098  0.0337  208 THR   B C   
3375 O O   . THR   B 208 ? 0.3215 0.4741 0.3266 0.0213  0.0092  0.0306  208 THR   B O   
3376 C CB  . THR   B 208 ? 0.3745 0.5290 0.3836 0.0316  0.0124  0.0449  208 THR   B CB  
3377 O OG1 . THR   B 208 ? 0.3731 0.5329 0.3805 0.0292  0.0118  0.0437  208 THR   B OG1 
3378 C CG2 . THR   B 208 ? 0.3815 0.5276 0.3932 0.0340  0.0142  0.0507  208 THR   B CG2 
3379 N N   . ALA   B 209 ? 0.3281 0.4918 0.3335 0.0267  0.0094  0.0326  209 ALA   B N   
3380 C CA  . ALA   B 209 ? 0.3215 0.4942 0.3244 0.0240  0.0083  0.0279  209 ALA   B CA  
3381 C C   . ALA   B 209 ? 0.3250 0.5036 0.3265 0.0229  0.0081  0.0279  209 ALA   B C   
3382 O O   . ALA   B 209 ? 0.2996 0.4790 0.2992 0.0190  0.0073  0.0232  209 ALA   B O   
3383 C CB  . ALA   B 209 ? 0.3272 0.5114 0.3298 0.0269  0.0081  0.0279  209 ALA   B CB  
3384 N N   . GLU   B 210 ? 0.3430 0.5266 0.3452 0.0266  0.0090  0.0332  210 GLU   B N   
3385 C CA  . GLU   B 210 ? 0.3089 0.4991 0.3099 0.0259  0.0088  0.0333  210 GLU   B CA  
3386 C C   . GLU   B 210 ? 0.2663 0.4468 0.2670 0.0220  0.0086  0.0311  210 GLU   B C   
3387 O O   . GLU   B 210 ? 0.2907 0.4744 0.2896 0.0193  0.0078  0.0271  210 GLU   B O   
3388 C CB  . GLU   B 210 ? 0.3382 0.5344 0.3401 0.0306  0.0100  0.0402  210 GLU   B CB  
3389 C CG  . GLU   B 210 ? 0.3599 0.5684 0.3615 0.0350  0.0102  0.0423  210 GLU   B CG  
3390 C CD  . GLU   B 210 ? 0.4087 0.6120 0.4118 0.0384  0.0108  0.0451  210 GLU   B CD  
3391 O OE1 . GLU   B 210 ? 0.3977 0.5875 0.4024 0.0373  0.0112  0.0452  210 GLU   B OE1 
3392 O OE2 . GLU   B 210 ? 0.4660 0.6802 0.4686 0.0426  0.0109  0.0470  210 GLU   B OE2 
3393 N N   . ASP   B 211 ? 0.2651 0.4343 0.2677 0.0220  0.0093  0.0335  211 ASP   B N   
3394 C CA  . ASP   B 211 ? 0.2896 0.4497 0.2920 0.0186  0.0089  0.0311  211 ASP   B CA  
3395 C C   . ASP   B 211 ? 0.2519 0.4099 0.2522 0.0148  0.0077  0.0246  211 ASP   B C   
3396 O O   . ASP   B 211 ? 0.2086 0.3662 0.2072 0.0124  0.0070  0.0215  211 ASP   B O   
3397 C CB  . ASP   B 211 ? 0.2981 0.4467 0.3031 0.0187  0.0098  0.0335  211 ASP   B CB  
3398 C CG  . ASP   B 211 ? 0.3203 0.4684 0.3275 0.0216  0.0114  0.0400  211 ASP   B CG  
3399 O OD1 . ASP   B 211 ? 0.3177 0.4731 0.3243 0.0225  0.0117  0.0425  211 ASP   B OD1 
3400 O OD2 . ASP   B 211 ? 0.3435 0.4841 0.3532 0.0227  0.0124  0.0425  211 ASP   B OD2 
3401 N N   . ALA   B 212 ? 0.2359 0.3927 0.2362 0.0143  0.0074  0.0225  212 ALA   B N   
3402 C CA  . ALA   B 212 ? 0.2217 0.3748 0.2199 0.0104  0.0065  0.0170  212 ALA   B CA  
3403 C C   . ALA   B 212 ? 0.2135 0.3749 0.2093 0.0087  0.0058  0.0135  212 ALA   B C   
3404 O O   . ALA   B 212 ? 0.2061 0.3635 0.1998 0.0055  0.0053  0.0095  212 ALA   B O   
3405 C CB  . ALA   B 212 ? 0.2364 0.3882 0.2350 0.0101  0.0063  0.0156  212 ALA   B CB  
3406 N N   . GLN   B 213 ? 0.2365 0.4096 0.2322 0.0109  0.0060  0.0148  213 GLN   B N   
3407 C CA  . GLN   B 213 ? 0.2542 0.4367 0.2480 0.0093  0.0055  0.0111  213 GLN   B CA  
3408 C C   . GLN   B 213 ? 0.2217 0.4027 0.2145 0.0085  0.0053  0.0103  213 GLN   B C   
3409 O O   . GLN   B 213 ? 0.2186 0.4000 0.2093 0.0056  0.0047  0.0054  213 GLN   B O   
3410 C CB  . GLN   B 213 ? 0.2620 0.4585 0.2563 0.0127  0.0058  0.0135  213 GLN   B CB  
3411 C CG  . GLN   B 213 ? 0.3105 0.5188 0.3030 0.0111  0.0053  0.0092  213 GLN   B CG  
3412 C CD  . GLN   B 213 ? 0.3290 0.5526 0.3221 0.0149  0.0056  0.0118  213 GLN   B CD  
3413 O OE1 . GLN   B 213 ? 0.3910 0.6177 0.3854 0.0193  0.0062  0.0177  213 GLN   B OE1 
3414 N NE2 . GLN   B 213 ? 0.3264 0.5593 0.3188 0.0134  0.0052  0.0079  213 GLN   B NE2 
3415 N N   . LYS   B 214 ? 0.2732 0.4521 0.2675 0.0110  0.0058  0.0150  214 LYS   B N   
3416 C CA  . LYS   B 214 ? 0.2736 0.4526 0.2673 0.0108  0.0057  0.0148  214 LYS   B CA  
3417 C C   . LYS   B 214 ? 0.2603 0.4279 0.2528 0.0078  0.0052  0.0111  214 LYS   B C   
3418 O O   . LYS   B 214 ? 0.2653 0.4335 0.2557 0.0063  0.0046  0.0073  214 LYS   B O   
3419 C CB  . LYS   B 214 ? 0.3270 0.5068 0.3229 0.0140  0.0067  0.0212  214 LYS   B CB  
3420 C CG  . LYS   B 214 ? 0.4188 0.6000 0.4143 0.0141  0.0067  0.0216  214 LYS   B CG  
3421 C CD  . LYS   B 214 ? 0.4950 0.6790 0.4925 0.0169  0.0079  0.0283  214 LYS   B CD  
3422 C CE  . LYS   B 214 ? 0.4943 0.6672 0.4942 0.0167  0.0088  0.0319  214 LYS   B CE  
3423 N NZ  . LYS   B 214 ? 0.5234 0.6993 0.5248 0.0184  0.0100  0.0375  214 LYS   B NZ  
3424 N N   . TYR   B 215 ? 0.2309 0.3882 0.2243 0.0070  0.0053  0.0119  215 TYR   B N   
3425 C CA  . TYR   B 215 ? 0.1972 0.3443 0.1892 0.0046  0.0049  0.0087  215 TYR   B CA  
3426 C C   . TYR   B 215 ? 0.1875 0.3340 0.1767 0.0016  0.0042  0.0033  215 TYR   B C   
3427 O O   . TYR   B 215 ? 0.2049 0.3465 0.1920 0.0001  0.0038  0.0002  215 TYR   B O   
3428 C CB  . TYR   B 215 ? 0.1983 0.3361 0.1920 0.0044  0.0052  0.0104  215 TYR   B CB  
3429 C CG  . TYR   B 215 ? 0.2076 0.3425 0.2038 0.0061  0.0058  0.0144  215 TYR   B CG  
3430 C CD1 . TYR   B 215 ? 0.2081 0.3380 0.2038 0.0053  0.0056  0.0136  215 TYR   B CD1 
3431 C CD2 . TYR   B 215 ? 0.2519 0.3891 0.2508 0.0084  0.0068  0.0191  215 TYR   B CD2 
3432 C CE1 . TYR   B 215 ? 0.2009 0.3287 0.1991 0.0062  0.0064  0.0169  215 TYR   B CE1 
3433 C CE2 . TYR   B 215 ? 0.2662 0.4002 0.2675 0.0093  0.0077  0.0228  215 TYR   B CE2 
3434 C CZ  . TYR   B 215 ? 0.2134 0.3429 0.2145 0.0079  0.0075  0.0215  215 TYR   B CZ  
3435 O OH  . TYR   B 215 ? 0.2170 0.3441 0.2206 0.0083  0.0085  0.0249  215 TYR   B OH  
3436 N N   . LEU   B 216 ? 0.1822 0.3333 0.1713 0.0007  0.0043  0.0021  216 LEU   B N   
3437 C CA  . LEU   B 216 ? 0.1938 0.3445 0.1802 -0.0027 0.0040  -0.0030 216 LEU   B CA  
3438 C C   . LEU   B 216 ? 0.2170 0.3740 0.2018 -0.0035 0.0037  -0.0064 216 LEU   B C   
3439 O O   . LEU   B 216 ? 0.2295 0.3818 0.2118 -0.0063 0.0035  -0.0108 216 LEU   B O   
3440 C CB  . LEU   B 216 ? 0.2119 0.3680 0.1988 -0.0037 0.0041  -0.0037 216 LEU   B CB  
3441 C CG  . LEU   B 216 ? 0.2387 0.3864 0.2260 -0.0048 0.0042  -0.0032 216 LEU   B CG  
3442 C CD1 . LEU   B 216 ? 0.2606 0.4154 0.2489 -0.0047 0.0044  -0.0031 216 LEU   B CD1 
3443 C CD2 . LEU   B 216 ? 0.2452 0.3835 0.2298 -0.0085 0.0041  -0.0069 216 LEU   B CD2 
3444 N N   . ALA   B 217 ? 0.2384 0.4060 0.2244 -0.0007 0.0038  -0.0042 217 ALA   B N   
3445 C CA  . ALA   B 217 ? 0.2437 0.4195 0.2285 -0.0009 0.0035  -0.0072 217 ALA   B CA  
3446 C C   . ALA   B 217 ? 0.2313 0.3999 0.2147 -0.0011 0.0032  -0.0090 217 ALA   B C   
3447 O O   . ALA   B 217 ? 0.2495 0.4190 0.2309 -0.0029 0.0029  -0.0139 217 ALA   B O   
3448 C CB  . ALA   B 217 ? 0.2382 0.4269 0.2248 0.0026  0.0038  -0.0034 217 ALA   B CB  
3449 N N   . ILE   B 218 ? 0.2256 0.3863 0.2099 0.0003  0.0033  -0.0056 218 ILE   B N   
3450 C CA  . ILE   B 218 ? 0.2256 0.3797 0.2084 0.0005  0.0029  -0.0073 218 ILE   B CA  
3451 C C   . ILE   B 218 ? 0.2292 0.3741 0.2092 -0.0025 0.0026  -0.0122 218 ILE   B C   
3452 O O   . ILE   B 218 ? 0.2336 0.3767 0.2114 -0.0030 0.0023  -0.0161 218 ILE   B O   
3453 C CB  . ILE   B 218 ? 0.2278 0.3763 0.2124 0.0023  0.0031  -0.0029 218 ILE   B CB  
3454 C CG1 . ILE   B 218 ? 0.2259 0.3827 0.2131 0.0050  0.0036  0.0022  218 ILE   B CG1 
3455 C CG2 . ILE   B 218 ? 0.2263 0.3684 0.2090 0.0025  0.0026  -0.0052 218 ILE   B CG2 
3456 C CD1 . ILE   B 218 ? 0.2242 0.3752 0.2139 0.0060  0.0042  0.0068  218 ILE   B CD1 
3457 N N   . ALA   B 219 ? 0.2252 0.3637 0.2050 -0.0045 0.0029  -0.0120 219 ALA   B N   
3458 C CA  . ALA   B 219 ? 0.2153 0.3442 0.1922 -0.0075 0.0029  -0.0159 219 ALA   B CA  
3459 C C   . ALA   B 219 ? 0.2170 0.3505 0.1923 -0.0102 0.0030  -0.0209 219 ALA   B C   
3460 O O   . ALA   B 219 ? 0.2188 0.3460 0.1914 -0.0116 0.0030  -0.0247 219 ALA   B O   
3461 C CB  . ALA   B 219 ? 0.2287 0.3521 0.2062 -0.0090 0.0032  -0.0142 219 ALA   B CB  
3462 N N   . ASP   B 220 ? 0.2424 0.3867 0.2192 -0.0108 0.0032  -0.0209 220 ASP   B N   
3463 C CA  . ASP   B 220 ? 0.2556 0.4069 0.2313 -0.0136 0.0034  -0.0259 220 ASP   B CA  
3464 C C   . ASP   B 220 ? 0.2469 0.4012 0.2215 -0.0126 0.0030  -0.0292 220 ASP   B C   
3465 O O   . ASP   B 220 ? 0.2498 0.4002 0.2221 -0.0153 0.0032  -0.0345 220 ASP   B O   
3466 C CB  . ASP   B 220 ? 0.2619 0.4264 0.2397 -0.0132 0.0035  -0.0246 220 ASP   B CB  
3467 C CG  . ASP   B 220 ? 0.2697 0.4325 0.2483 -0.0146 0.0038  -0.0227 220 ASP   B CG  
3468 O OD1 . ASP   B 220 ? 0.2941 0.4453 0.2715 -0.0166 0.0040  -0.0229 220 ASP   B OD1 
3469 O OD2 . ASP   B 220 ? 0.2908 0.4644 0.2712 -0.0135 0.0039  -0.0212 220 ASP   B OD2 
3470 N N   . GLU   B 221 ? 0.2454 0.4050 0.2214 -0.0086 0.0026  -0.0259 221 GLU   B N   
3471 C CA  . GLU   B 221 ? 0.2947 0.4584 0.2698 -0.0071 0.0023  -0.0286 221 GLU   B CA  
3472 C C   . GLU   B 221 ? 0.2819 0.4326 0.2544 -0.0077 0.0021  -0.0317 221 GLU   B C   
3473 O O   . GLU   B 221 ? 0.2864 0.4369 0.2570 -0.0087 0.0020  -0.0370 221 GLU   B O   
3474 C CB  . GLU   B 221 ? 0.3505 0.5225 0.3280 -0.0029 0.0021  -0.0234 221 GLU   B CB  
3475 C CG  . GLU   B 221 ? 0.4541 0.6332 0.4311 -0.0009 0.0016  -0.0256 221 GLU   B CG  
3476 C CD  . GLU   B 221 ? 0.5704 0.7570 0.5494 0.0030  0.0016  -0.0200 221 GLU   B CD  
3477 O OE1 . GLU   B 221 ? 0.5544 0.7383 0.5353 0.0041  0.0020  -0.0142 221 GLU   B OE1 
3478 O OE2 . GLU   B 221 ? 0.6935 0.8891 0.6723 0.0046  0.0013  -0.0217 221 GLU   B OE2 
3479 N N   . LEU   B 222 ? 0.2530 0.3926 0.2251 -0.0068 0.0021  -0.0285 222 LEU   B N   
3480 C CA  . LEU   B 222 ? 0.2350 0.3634 0.2046 -0.0061 0.0019  -0.0303 222 LEU   B CA  
3481 C C   . LEU   B 222 ? 0.2425 0.3608 0.2091 -0.0097 0.0024  -0.0348 222 LEU   B C   
3482 O O   . LEU   B 222 ? 0.2526 0.3640 0.2166 -0.0094 0.0023  -0.0384 222 LEU   B O   
3483 C CB  . LEU   B 222 ? 0.2518 0.3735 0.2221 -0.0039 0.0017  -0.0255 222 LEU   B CB  
3484 C CG  . LEU   B 222 ? 0.2856 0.4133 0.2578 -0.0002 0.0013  -0.0222 222 LEU   B CG  
3485 C CD1 . LEU   B 222 ? 0.2739 0.3948 0.2471 0.0010  0.0013  -0.0181 222 LEU   B CD1 
3486 C CD2 . LEU   B 222 ? 0.2789 0.4078 0.2493 0.0019  0.0008  -0.0257 222 LEU   B CD2 
3487 N N   . PHE   B 223 ? 0.2514 0.3673 0.2183 -0.0128 0.0029  -0.0339 223 PHE   B N   
3488 C CA  . PHE   B 223 ? 0.2519 0.3562 0.2160 -0.0164 0.0036  -0.0365 223 PHE   B CA  
3489 C C   . PHE   B 223 ? 0.2601 0.3690 0.2240 -0.0212 0.0043  -0.0404 223 PHE   B C   
3490 O O   . PHE   B 223 ? 0.3192 0.4190 0.2806 -0.0247 0.0051  -0.0436 223 PHE   B O   
3491 C CB  . PHE   B 223 ? 0.2324 0.3291 0.1965 -0.0167 0.0038  -0.0323 223 PHE   B CB  
3492 C CG  . PHE   B 223 ? 0.2255 0.3171 0.1896 -0.0126 0.0032  -0.0288 223 PHE   B CG  
3493 C CD1 . PHE   B 223 ? 0.2396 0.3221 0.2008 -0.0110 0.0031  -0.0306 223 PHE   B CD1 
3494 C CD2 . PHE   B 223 ? 0.2225 0.3190 0.1897 -0.0103 0.0028  -0.0242 223 PHE   B CD2 
3495 C CE1 . PHE   B 223 ? 0.2415 0.3208 0.2027 -0.0072 0.0025  -0.0277 223 PHE   B CE1 
3496 C CE2 . PHE   B 223 ? 0.2114 0.3041 0.1788 -0.0071 0.0024  -0.0216 223 PHE   B CE2 
3497 C CZ  . PHE   B 223 ? 0.2263 0.3109 0.1908 -0.0056 0.0022  -0.0234 223 PHE   B CZ  
3498 N N   . GLY   B 224 ? 0.2695 0.3927 0.2361 -0.0212 0.0042  -0.0404 224 GLY   B N   
3499 C CA  . GLY   B 224 ? 0.2720 0.4016 0.2390 -0.0257 0.0048  -0.0435 224 GLY   B CA  
3500 C C   . GLY   B 224 ? 0.2966 0.4285 0.2653 -0.0263 0.0050  -0.0394 224 GLY   B C   
3501 O O   . GLY   B 224 ? 0.2842 0.4080 0.2528 -0.0248 0.0048  -0.0353 224 GLY   B O   
3502 N N   . ALA   B 225 ? 0.2865 0.4300 0.2566 -0.0285 0.0052  -0.0408 225 ALA   B N   
3503 C CA  . ALA   B 225 ? 0.2987 0.4484 0.2711 -0.0274 0.0051  -0.0366 225 ALA   B CA  
3504 C C   . ALA   B 225 ? 0.2782 0.4191 0.2495 -0.0308 0.0058  -0.0361 225 ALA   B C   
3505 O O   . ALA   B 225 ? 0.2833 0.4281 0.2564 -0.0297 0.0057  -0.0328 225 ALA   B O   
3506 C CB  . ALA   B 225 ? 0.3267 0.4932 0.3009 -0.0278 0.0051  -0.0382 225 ALA   B CB  
3507 N N   . ASP   B 226 ? 0.2776 0.4073 0.2460 -0.0347 0.0065  -0.0393 226 ASP   B N   
3508 C CA  . ASP   B 226 ? 0.3142 0.4356 0.2814 -0.0380 0.0072  -0.0384 226 ASP   B CA  
3509 C C   . ASP   B 226 ? 0.2836 0.3923 0.2496 -0.0352 0.0069  -0.0344 226 ASP   B C   
3510 O O   . ASP   B 226 ? 0.2968 0.3988 0.2618 -0.0370 0.0074  -0.0329 226 ASP   B O   
3511 C CB  . ASP   B 226 ? 0.3519 0.4668 0.3163 -0.0441 0.0085  -0.0433 226 ASP   B CB  
3512 C CG  . ASP   B 226 ? 0.4235 0.5506 0.3889 -0.0485 0.0091  -0.0480 226 ASP   B CG  
3513 O OD1 . ASP   B 226 ? 0.4745 0.6148 0.4425 -0.0474 0.0086  -0.0466 226 ASP   B OD1 
3514 O OD2 . ASP   B 226 ? 0.4954 0.6186 0.4589 -0.0529 0.0100  -0.0531 226 ASP   B OD2 
3515 N N   . TRP   B 227 ? 0.2521 0.3576 0.2181 -0.0311 0.0062  -0.0332 227 TRP   B N   
3516 C CA  . TRP   B 227 ? 0.2534 0.3473 0.2180 -0.0287 0.0060  -0.0302 227 TRP   B CA  
3517 C C   . TRP   B 227 ? 0.2281 0.3230 0.1949 -0.0266 0.0057  -0.0256 227 TRP   B C   
3518 O O   . TRP   B 227 ? 0.2416 0.3276 0.2069 -0.0270 0.0059  -0.0240 227 TRP   B O   
3519 C CB  . TRP   B 227 ? 0.2491 0.3419 0.2136 -0.0245 0.0053  -0.0300 227 TRP   B CB  
3520 C CG  . TRP   B 227 ? 0.2395 0.3219 0.2027 -0.0218 0.0050  -0.0272 227 TRP   B CG  
3521 C CD1 . TRP   B 227 ? 0.2615 0.3317 0.2212 -0.0225 0.0054  -0.0283 227 TRP   B CD1 
3522 C CD2 . TRP   B 227 ? 0.2188 0.3027 0.1842 -0.0178 0.0043  -0.0230 227 TRP   B CD2 
3523 N NE1 . TRP   B 227 ? 0.2562 0.3212 0.2156 -0.0190 0.0049  -0.0250 227 TRP   B NE1 
3524 C CE2 . TRP   B 227 ? 0.2214 0.2947 0.1846 -0.0164 0.0042  -0.0220 227 TRP   B CE2 
3525 C CE3 . TRP   B 227 ? 0.2094 0.3022 0.1785 -0.0154 0.0038  -0.0200 227 TRP   B CE3 
3526 C CZ2 . TRP   B 227 ? 0.2131 0.2856 0.1777 -0.0129 0.0036  -0.0187 227 TRP   B CZ2 
3527 C CZ3 . TRP   B 227 ? 0.2294 0.3200 0.2000 -0.0123 0.0034  -0.0166 227 TRP   B CZ3 
3528 C CH2 . TRP   B 227 ? 0.2134 0.2946 0.1819 -0.0112 0.0033  -0.0162 227 TRP   B CH2 
3529 N N   . ALA   B 228 ? 0.2098 0.3154 0.1799 -0.0243 0.0052  -0.0235 228 ALA   B N   
3530 C CA  . ALA   B 228 ? 0.2117 0.3181 0.1843 -0.0217 0.0048  -0.0193 228 ALA   B CA  
3531 C C   . ALA   B 228 ? 0.2101 0.3180 0.1832 -0.0241 0.0053  -0.0189 228 ALA   B C   
3532 O O   . ALA   B 228 ? 0.2370 0.3534 0.2126 -0.0230 0.0051  -0.0175 228 ALA   B O   
3533 C CB  . ALA   B 228 ? 0.2039 0.3197 0.1797 -0.0179 0.0043  -0.0168 228 ALA   B CB  
3534 N N   . ASP   B 229 ? 0.2258 0.3251 0.1963 -0.0270 0.0058  -0.0198 229 ASP   B N   
3535 C CA  . ASP   B 229 ? 0.2277 0.3276 0.1985 -0.0291 0.0062  -0.0191 229 ASP   B CA  
3536 C C   . ASP   B 229 ? 0.2055 0.3002 0.1773 -0.0260 0.0058  -0.0157 229 ASP   B C   
3537 O O   . ASP   B 229 ? 0.2057 0.2970 0.1781 -0.0227 0.0052  -0.0142 229 ASP   B O   
3538 C CB  . ASP   B 229 ? 0.2455 0.3397 0.2129 -0.0343 0.0072  -0.0218 229 ASP   B CB  
3539 C CG  . ASP   B 229 ? 0.2864 0.3674 0.2504 -0.0344 0.0075  -0.0216 229 ASP   B CG  
3540 O OD1 . ASP   B 229 ? 0.2510 0.3280 0.2155 -0.0304 0.0068  -0.0192 229 ASP   B OD1 
3541 O OD2 . ASP   B 229 ? 0.3495 0.4244 0.3104 -0.0384 0.0085  -0.0237 229 ASP   B OD2 
3542 N N   . ALA   B 230 ? 0.2014 0.2964 0.1736 -0.0273 0.0060  -0.0150 230 ALA   B N   
3543 C CA  . ALA   B 230 ? 0.2147 0.3069 0.1885 -0.0244 0.0056  -0.0123 230 ALA   B CA  
3544 C C   . ALA   B 230 ? 0.2008 0.2827 0.1721 -0.0237 0.0055  -0.0117 230 ALA   B C   
3545 O O   . ALA   B 230 ? 0.2055 0.2853 0.1783 -0.0208 0.0051  -0.0098 230 ALA   B O   
3546 C CB  . ALA   B 230 ? 0.2364 0.3321 0.2110 -0.0258 0.0059  -0.0121 230 ALA   B CB  
3547 N N   . ARG   B 231 ? 0.2012 0.2766 0.1688 -0.0261 0.0061  -0.0132 231 ARG   B N   
3548 C CA  . ARG   B 231 ? 0.2125 0.2783 0.1773 -0.0247 0.0061  -0.0124 231 ARG   B CA  
3549 C C   . ARG   B 231 ? 0.2253 0.2904 0.1909 -0.0212 0.0054  -0.0123 231 ARG   B C   
3550 O O   . ARG   B 231 ? 0.2148 0.2740 0.1790 -0.0188 0.0051  -0.0113 231 ARG   B O   
3551 C CB  . ARG   B 231 ? 0.2228 0.2811 0.1832 -0.0284 0.0071  -0.0138 231 ARG   B CB  
3552 C CG  . ARG   B 231 ? 0.2343 0.2821 0.1912 -0.0266 0.0072  -0.0128 231 ARG   B CG  
3553 C CD  . ARG   B 231 ? 0.2345 0.2806 0.1918 -0.0234 0.0067  -0.0102 231 ARG   B CD  
3554 N NE  . ARG   B 231 ? 0.2462 0.2834 0.1999 -0.0211 0.0068  -0.0093 231 ARG   B NE  
3555 C CZ  . ARG   B 231 ? 0.2472 0.2835 0.2013 -0.0171 0.0059  -0.0091 231 ARG   B CZ  
3556 N NH1 . ARG   B 231 ? 0.2485 0.2918 0.2065 -0.0154 0.0051  -0.0096 231 ARG   B NH1 
3557 N NH2 . ARG   B 231 ? 0.2479 0.2767 0.1985 -0.0146 0.0060  -0.0084 231 ARG   B NH2 
3558 N N   . HIS   B 232 ? 0.2009 0.2728 0.1684 -0.0208 0.0051  -0.0132 232 HIS   B N   
3559 C CA  . HIS   B 232 ? 0.2045 0.2767 0.1723 -0.0180 0.0046  -0.0134 232 HIS   B CA  
3560 C C   . HIS   B 232 ? 0.1894 0.2695 0.1613 -0.0151 0.0040  -0.0115 232 HIS   B C   
3561 O O   . HIS   B 232 ? 0.1791 0.2600 0.1515 -0.0126 0.0036  -0.0112 232 HIS   B O   
3562 C CB  . HIS   B 232 ? 0.2109 0.2829 0.1765 -0.0201 0.0049  -0.0166 232 HIS   B CB  
3563 C CG  . HIS   B 232 ? 0.2278 0.2897 0.1891 -0.0225 0.0057  -0.0182 232 HIS   B CG  
3564 N ND1 . HIS   B 232 ? 0.2369 0.2970 0.1967 -0.0268 0.0066  -0.0192 232 HIS   B ND1 
3565 C CD2 . HIS   B 232 ? 0.2289 0.2821 0.1871 -0.0210 0.0057  -0.0186 232 HIS   B CD2 
3566 C CE1 . HIS   B 232 ? 0.2379 0.2874 0.1936 -0.0281 0.0073  -0.0201 232 HIS   B CE1 
3567 N NE2 . HIS   B 232 ? 0.2314 0.2764 0.1861 -0.0242 0.0067  -0.0196 232 HIS   B NE2 
3568 N N   . TYR   B 233 ? 0.1667 0.2528 0.1414 -0.0153 0.0041  -0.0103 233 TYR   B N   
3569 C CA  . TYR   B 233 ? 0.1674 0.2600 0.1457 -0.0125 0.0038  -0.0081 233 TYR   B CA  
3570 C C   . TYR   B 233 ? 0.1584 0.2530 0.1395 -0.0118 0.0039  -0.0062 233 TYR   B C   
3571 O O   . TYR   B 233 ? 0.1925 0.2889 0.1732 -0.0138 0.0042  -0.0072 233 TYR   B O   
3572 C CB  . TYR   B 233 ? 0.1591 0.2603 0.1380 -0.0129 0.0039  -0.0091 233 TYR   B CB  
3573 C CG  . TYR   B 233 ? 0.1520 0.2590 0.1335 -0.0096 0.0037  -0.0068 233 TYR   B CG  
3574 C CD1 . TYR   B 233 ? 0.1671 0.2779 0.1519 -0.0074 0.0039  -0.0036 233 TYR   B CD1 
3575 C CD2 . TYR   B 233 ? 0.1796 0.2877 0.1601 -0.0087 0.0035  -0.0076 233 TYR   B CD2 
3576 C CE1 . TYR   B 233 ? 0.1858 0.3008 0.1729 -0.0046 0.0039  -0.0009 233 TYR   B CE1 
3577 C CE2 . TYR   B 233 ? 0.1779 0.2916 0.1606 -0.0059 0.0034  -0.0051 233 TYR   B CE2 
3578 C CZ  . TYR   B 233 ? 0.1908 0.3079 0.1768 -0.0040 0.0037  -0.0015 233 TYR   B CZ  
3579 O OH  . TYR   B 233 ? 0.2215 0.3436 0.2096 -0.0014 0.0039  0.0015  233 TYR   B OH  
3580 N N   . ARG   B 234 ? 0.1448 0.2397 0.1289 -0.0090 0.0038  -0.0038 234 ARG   B N   
3581 C CA  . ARG   B 234 ? 0.1461 0.2426 0.1333 -0.0079 0.0040  -0.0022 234 ARG   B CA  
3582 C C   . ARG   B 234 ? 0.1476 0.2471 0.1382 -0.0050 0.0042  0.0006  234 ARG   B C   
3583 O O   . ARG   B 234 ? 0.1488 0.2480 0.1395 -0.0039 0.0041  0.0015  234 ARG   B O   
3584 C CB  . ARG   B 234 ? 0.1423 0.2327 0.1295 -0.0081 0.0039  -0.0025 234 ARG   B CB  
3585 C CG  . ARG   B 234 ? 0.1517 0.2385 0.1354 -0.0108 0.0039  -0.0044 234 ARG   B CG  
3586 C CD  . ARG   B 234 ? 0.1531 0.2437 0.1369 -0.0125 0.0041  -0.0052 234 ARG   B CD  
3587 N NE  . ARG   B 234 ? 0.1626 0.2493 0.1429 -0.0154 0.0043  -0.0067 234 ARG   B NE  
3588 C CZ  . ARG   B 234 ? 0.1680 0.2502 0.1474 -0.0155 0.0043  -0.0065 234 ARG   B CZ  
3589 N NH1 . ARG   B 234 ? 0.1620 0.2445 0.1443 -0.0133 0.0041  -0.0057 234 ARG   B NH1 
3590 N NH2 . ARG   B 234 ? 0.1817 0.2591 0.1573 -0.0178 0.0046  -0.0072 234 ARG   B NH2 
3591 N N   . PHE   B 235 ? 0.1459 0.2481 0.1392 -0.0036 0.0045  0.0021  235 PHE   B N   
3592 C CA  . PHE   B 235 ? 0.1579 0.2616 0.1547 -0.0009 0.0050  0.0051  235 PHE   B CA  
3593 C C   . PHE   B 235 ? 0.1805 0.2805 0.1801 0.0000  0.0053  0.0057  235 PHE   B C   
3594 O O   . PHE   B 235 ? 0.1820 0.2823 0.1815 -0.0007 0.0051  0.0041  235 PHE   B O   
3595 C CB  . PHE   B 235 ? 0.1773 0.2886 0.1752 0.0008  0.0053  0.0069  235 PHE   B CB  
3596 C CG  . PHE   B 235 ? 0.1804 0.2981 0.1765 0.0008  0.0052  0.0069  235 PHE   B CG  
3597 C CD1 . PHE   B 235 ? 0.1896 0.3095 0.1868 0.0027  0.0055  0.0096  235 PHE   B CD1 
3598 C CD2 . PHE   B 235 ? 0.1873 0.3095 0.1809 -0.0013 0.0048  0.0041  235 PHE   B CD2 
3599 C CE1 . PHE   B 235 ? 0.2007 0.3278 0.1964 0.0029  0.0054  0.0094  235 PHE   B CE1 
3600 C CE2 . PHE   B 235 ? 0.1985 0.3274 0.1909 -0.0014 0.0047  0.0035  235 PHE   B CE2 
3601 C CZ  . PHE   B 235 ? 0.1830 0.3146 0.1764 0.0009  0.0049  0.0061  235 PHE   B CZ  
3602 N N   A SER   B 236 ? 0.1818 0.2790 0.1842 0.0014  0.0058  0.0077  236 SER   B N   
3603 N N   B SER   B 236 ? 0.1823 0.2796 0.1847 0.0014  0.0058  0.0077  236 SER   B N   
3604 N N   C SER   B 236 ? 0.1875 0.2845 0.1898 0.0013  0.0058  0.0076  236 SER   B N   
3605 C CA  A SER   B 236 ? 0.1938 0.2882 0.1996 0.0026  0.0064  0.0084  236 SER   B CA  
3606 C CA  B SER   B 236 ? 0.1943 0.2886 0.2001 0.0026  0.0064  0.0084  236 SER   B CA  
3607 C CA  C SER   B 236 ? 0.2051 0.2992 0.2109 0.0025  0.0063  0.0084  236 SER   B CA  
3608 C C   A SER   B 236 ? 0.2095 0.3033 0.2183 0.0045  0.0074  0.0119  236 SER   B C   
3609 C C   B SER   B 236 ? 0.2095 0.3031 0.2185 0.0045  0.0074  0.0118  236 SER   B C   
3610 C C   C SER   B 236 ? 0.2167 0.3110 0.2254 0.0046  0.0073  0.0120  236 SER   B C   
3611 O O   A SER   B 236 ? 0.2005 0.2931 0.2095 0.0040  0.0076  0.0129  236 SER   B O   
3612 O O   B SER   B 236 ? 0.1981 0.2902 0.2073 0.0039  0.0076  0.0127  236 SER   B O   
3613 O O   C SER   B 236 ? 0.2130 0.3074 0.2214 0.0043  0.0075  0.0133  236 SER   B O   
3614 C CB  A SER   B 236 ? 0.1942 0.2834 0.2003 0.0012  0.0061  0.0060  236 SER   B CB  
3615 C CB  B SER   B 236 ? 0.1954 0.2846 0.2014 0.0011  0.0061  0.0059  236 SER   B CB  
3616 C CB  C SER   B 236 ? 0.2122 0.3008 0.2185 0.0011  0.0062  0.0062  236 SER   B CB  
3617 O OG  A SER   B 236 ? 0.1834 0.2702 0.1930 0.0023  0.0067  0.0060  236 SER   B OG  
3618 O OG  B SER   B 236 ? 0.1831 0.2696 0.1891 0.0004  0.0061  0.0060  236 SER   B OG  
3619 O OG  C SER   B 236 ? 0.2141 0.3025 0.2176 -0.0006 0.0054  0.0034  236 SER   B OG  
3620 N N   . ALA   B 237 ? 0.2359 0.3305 0.2471 0.0069  0.0081  0.0139  237 ALA   B N   
3621 C CA  . ALA   B 237 ? 0.2627 0.3554 0.2768 0.0088  0.0093  0.0177  237 ALA   B CA  
3622 C C   . ALA   B 237 ? 0.3178 0.4090 0.3345 0.0114  0.0101  0.0188  237 ALA   B C   
3623 O O   . ALA   B 237 ? 0.3059 0.4012 0.3216 0.0127  0.0096  0.0179  237 ALA   B O   
3624 C CB  . ALA   B 237 ? 0.2630 0.3615 0.2759 0.0098  0.0095  0.0208  237 ALA   B CB  
3625 N N   . SER   B 238 ? 0.3527 0.4380 0.3729 0.0121  0.0113  0.0206  238 SER   B N   
3626 C CA  . SER   B 238 ? 0.4296 0.5120 0.4526 0.0152  0.0124  0.0224  238 SER   B CA  
3627 C C   . SER   B 238 ? 0.4003 0.4887 0.4221 0.0188  0.0128  0.0265  238 SER   B C   
3628 O O   . SER   B 238 ? 0.3688 0.4608 0.3896 0.0192  0.0131  0.0299  238 SER   B O   
3629 C CB  . SER   B 238 ? 0.4604 0.5348 0.4871 0.0146  0.0140  0.0239  238 SER   B CB  
3630 O OG  . SER   B 238 ? 0.5610 0.6331 0.5896 0.0182  0.0155  0.0282  238 SER   B OG  
3631 N N   . GLY   B 239 ? 0.3962 0.4874 0.4180 0.0216  0.0125  0.0259  239 GLY   B N   
3632 C CA  . GLY   B 239 ? 0.3926 0.4902 0.4136 0.0258  0.0128  0.0296  239 GLY   B CA  
3633 C C   . GLY   B 239 ? 0.3761 0.4844 0.3936 0.0252  0.0116  0.0286  239 GLY   B C   
3634 O O   . GLY   B 239 ? 0.3489 0.4647 0.3656 0.0285  0.0117  0.0310  239 GLY   B O   
3635 N N   . LEU   B 240 ? 0.3142 0.4237 0.3296 0.0210  0.0105  0.0251  240 LEU   B N   
3636 C CA  . LEU   B 240 ? 0.2612 0.3800 0.2734 0.0200  0.0095  0.0241  240 LEU   B CA  
3637 C C   . LEU   B 240 ? 0.2534 0.3790 0.2645 0.0209  0.0088  0.0217  240 LEU   B C   
3638 O O   . LEU   B 240 ? 0.2400 0.3750 0.2495 0.0223  0.0086  0.0223  240 LEU   B O   
3639 C CB  . LEU   B 240 ? 0.2485 0.3657 0.2585 0.0155  0.0087  0.0209  240 LEU   B CB  
3640 C CG  . LEU   B 240 ? 0.2375 0.3632 0.2443 0.0140  0.0078  0.0191  240 LEU   B CG  
3641 C CD1 . LEU   B 240 ? 0.2548 0.3874 0.2615 0.0166  0.0083  0.0229  240 LEU   B CD1 
3642 C CD2 . LEU   B 240 ? 0.2509 0.3736 0.2555 0.0100  0.0071  0.0161  240 LEU   B CD2 
3643 N N   . LEU   B 241 ? 0.2563 0.3781 0.2680 0.0199  0.0085  0.0185  241 LEU   B N   
3644 C CA  . LEU   B 241 ? 0.2541 0.3831 0.2646 0.0200  0.0077  0.0158  241 LEU   B CA  
3645 C C   . LEU   B 241 ? 0.2634 0.3991 0.2749 0.0253  0.0082  0.0187  241 LEU   B C   
3646 O O   . LEU   B 241 ? 0.2538 0.3999 0.2636 0.0258  0.0078  0.0180  241 LEU   B O   
3647 C CB  . LEU   B 241 ? 0.2324 0.3566 0.2437 0.0185  0.0074  0.0123  241 LEU   B CB  
3648 C CG  . LEU   B 241 ? 0.2405 0.3726 0.2508 0.0186  0.0068  0.0095  241 LEU   B CG  
3649 C CD1 . LEU   B 241 ? 0.2363 0.3761 0.2432 0.0150  0.0061  0.0076  241 LEU   B CD1 
3650 C CD2 . LEU   B 241 ? 0.2434 0.3712 0.2546 0.0173  0.0065  0.0062  241 LEU   B CD2 
3651 N N   . ALA   B 242 ? 0.2638 0.3934 0.2781 0.0291  0.0093  0.0219  242 ALA   B N   
3652 C CA  . ALA   B 242 ? 0.2877 0.4221 0.3028 0.0349  0.0100  0.0255  242 ALA   B CA  
3653 C C   . ALA   B 242 ? 0.3138 0.4572 0.3271 0.0364  0.0101  0.0289  242 ALA   B C   
3654 O O   . ALA   B 242 ? 0.3492 0.5035 0.3614 0.0394  0.0098  0.0294  242 ALA   B O   
3655 C CB  . ALA   B 242 ? 0.3001 0.4240 0.3184 0.0382  0.0113  0.0285  242 ALA   B CB  
3656 N N   . SER   B 243 ? 0.2949 0.4354 0.3078 0.0343  0.0104  0.0308  243 SER   B N   
3657 C CA  . SER   B 243 ? 0.2868 0.4365 0.2981 0.0356  0.0105  0.0337  243 SER   B CA  
3658 C C   . SER   B 243 ? 0.2906 0.4516 0.2992 0.0329  0.0092  0.0295  243 SER   B C   
3659 O O   . SER   B 243 ? 0.2932 0.4660 0.3006 0.0353  0.0091  0.0306  243 SER   B O   
3660 C CB  . SER   B 243 ? 0.3023 0.4466 0.3139 0.0337  0.0111  0.0362  243 SER   B CB  
3661 O OG  . SER   B 243 ? 0.3492 0.5038 0.3591 0.0347  0.0111  0.0384  243 SER   B OG  
3662 N N   . LEU   B 244 ? 0.2574 0.4153 0.2650 0.0278  0.0083  0.0244  244 LEU   B N   
3663 C CA  . LEU   B 244 ? 0.2682 0.4357 0.2733 0.0246  0.0074  0.0202  244 LEU   B CA  
3664 C C   . LEU   B 244 ? 0.2553 0.4322 0.2604 0.0272  0.0071  0.0191  244 LEU   B C   
3665 O O   . LEU   B 244 ? 0.2386 0.4277 0.2421 0.0270  0.0068  0.0178  244 LEU   B O   
3666 C CB  . LEU   B 244 ? 0.2540 0.4152 0.2577 0.0187  0.0067  0.0155  244 LEU   B CB  
3667 C CG  . LEU   B 244 ? 0.2532 0.4067 0.2563 0.0161  0.0068  0.0159  244 LEU   B CG  
3668 C CD1 . LEU   B 244 ? 0.2375 0.3836 0.2395 0.0115  0.0062  0.0119  244 LEU   B CD1 
3669 C CD2 . LEU   B 244 ? 0.2574 0.4187 0.2587 0.0151  0.0066  0.0157  244 LEU   B CD2 
3670 N N   . LEU   B 245 ? 0.2622 0.4341 0.2690 0.0293  0.0073  0.0191  245 LEU   B N   
3671 C CA  . LEU   B 245 ? 0.2743 0.4556 0.2810 0.0317  0.0070  0.0176  245 LEU   B CA  
3672 C C   . LEU   B 245 ? 0.2949 0.4858 0.3019 0.0380  0.0075  0.0218  245 LEU   B C   
3673 O O   . LEU   B 245 ? 0.2974 0.5014 0.3034 0.0394  0.0071  0.0205  245 LEU   B O   
3674 C CB  . LEU   B 245 ? 0.2695 0.4438 0.2781 0.0329  0.0071  0.0163  245 LEU   B CB  
3675 C CG  . LEU   B 245 ? 0.2734 0.4431 0.2811 0.0270  0.0064  0.0115  245 LEU   B CG  
3676 C CD1 . LEU   B 245 ? 0.2756 0.4367 0.2857 0.0286  0.0066  0.0108  245 LEU   B CD1 
3677 C CD2 . LEU   B 245 ? 0.2522 0.4333 0.2578 0.0238  0.0057  0.0075  245 LEU   B CD2 
3678 N N   . LYS   B 246 ? 0.3419 0.5267 0.3502 0.0416  0.0085  0.0271  246 LYS   B N   
3679 C CA  . LYS   B 246 ? 0.3573 0.5501 0.3657 0.0482  0.0091  0.0320  246 LYS   B CA  
3680 C C   . LYS   B 246 ? 0.3488 0.5559 0.3549 0.0469  0.0086  0.0312  246 LYS   B C   
3681 O O   . LYS   B 246 ? 0.3523 0.5731 0.3576 0.0502  0.0084  0.0313  246 LYS   B O   
3682 C CB  . LYS   B 246 ? 0.4303 0.6115 0.4405 0.0512  0.0105  0.0377  246 LYS   B CB  
3683 C CG  . LYS   B 246 ? 0.5145 0.7017 0.5247 0.0582  0.0116  0.0442  246 LYS   B CG  
3684 C CD  . LYS   B 246 ? 0.5771 0.7511 0.5893 0.0605  0.0132  0.0500  246 LYS   B CD  
3685 C CE  . LYS   B 246 ? 0.6794 0.8567 0.6917 0.0685  0.0146  0.0569  246 LYS   B CE  
3686 N NZ  . LYS   B 246 ? 0.6948 0.8861 0.7050 0.0703  0.0145  0.0599  246 LYS   B NZ  
3687 N N   . ALA   B 247 ? 0.3080 0.5123 0.3132 0.0419  0.0084  0.0299  247 ALA   B N   
3688 C CA  . ALA   B 247 ? 0.3075 0.5247 0.3107 0.0399  0.0078  0.0280  247 ALA   B CA  
3689 C C   . ALA   B 247 ? 0.3414 0.5702 0.3433 0.0374  0.0070  0.0226  247 ALA   B C   
3690 O O   . ALA   B 247 ? 0.3277 0.5708 0.3283 0.0376  0.0067  0.0215  247 ALA   B O   
3691 C CB  . ALA   B 247 ? 0.2986 0.5096 0.3009 0.0346  0.0076  0.0264  247 ALA   B CB  
3692 N N   . LEU   B 248 ? 0.3341 0.5574 0.3364 0.0349  0.0066  0.0191  248 LEU   B N   
3693 C CA  . LEU   B 248 ? 0.3327 0.5660 0.3337 0.0313  0.0059  0.0137  248 LEU   B CA  
3694 C C   . LEU   B 248 ? 0.3520 0.5952 0.3539 0.0368  0.0059  0.0146  248 LEU   B C   
3695 O O   . LEU   B 248 ? 0.3544 0.6072 0.3556 0.0345  0.0054  0.0104  248 LEU   B O   
3696 C CB  . LEU   B 248 ? 0.2959 0.5190 0.2965 0.0249  0.0056  0.0094  248 LEU   B CB  
3697 C CG  . LEU   B 248 ? 0.3000 0.5164 0.2991 0.0191  0.0054  0.0074  248 LEU   B CG  
3698 C CD1 . LEU   B 248 ? 0.2924 0.4955 0.2912 0.0142  0.0053  0.0048  248 LEU   B CD1 
3699 C CD2 . LEU   B 248 ? 0.3004 0.5290 0.2976 0.0153  0.0051  0.0035  248 LEU   B CD2 
3700 N N   . GLY   B 249 ? 0.3655 0.6055 0.3688 0.0440  0.0065  0.0201  249 GLY   B N   
3701 C CA  . GLY   B 249 ? 0.3902 0.6393 0.3942 0.0504  0.0066  0.0214  249 GLY   B CA  
3702 C C   . GLY   B 249 ? 0.4400 0.6791 0.4457 0.0520  0.0067  0.0207  249 GLY   B C   
3703 O O   . GLY   B 249 ? 0.4420 0.6883 0.4482 0.0571  0.0066  0.0210  249 GLY   B O   
3704 N N   . HIS   B 250 ? 0.4004 0.6237 0.4070 0.0481  0.0068  0.0198  250 HIS   B N   
3705 C CA  . HIS   B 250 ? 0.4433 0.6574 0.4517 0.0499  0.0069  0.0191  250 HIS   B CA  
3706 C C   . HIS   B 250 ? 0.4816 0.6827 0.4921 0.0549  0.0080  0.0243  250 HIS   B C   
3707 O O   . HIS   B 250 ? 0.6448 0.8324 0.6563 0.0513  0.0083  0.0239  250 HIS   B O   
3708 C CB  . HIS   B 250 ? 0.4052 0.6135 0.4133 0.0426  0.0063  0.0138  250 HIS   B CB  
3709 C CG  . HIS   B 250 ? 0.4089 0.6313 0.4153 0.0393  0.0056  0.0093  250 HIS   B CG  
3710 N ND1 . HIS   B 250 ? 0.4098 0.6400 0.4140 0.0344  0.0053  0.0073  250 HIS   B ND1 
3711 C CD2 . HIS   B 250 ? 0.4048 0.6357 0.4113 0.0403  0.0052  0.0064  250 HIS   B CD2 
3712 C CE1 . HIS   B 250 ? 0.3719 0.6143 0.3752 0.0319  0.0048  0.0032  250 HIS   B CE1 
3713 N NE2 . HIS   B 250 ? 0.3561 0.5997 0.3606 0.0355  0.0047  0.0028  250 HIS   B NE2 
3714 C C1  . A1IB9 C .   ? 0.2528 0.3174 0.2389 0.0057  0.0042  0.0066  301 A1IB9 A C1  
3715 C C2  . A1IB9 C .   ? 0.2472 0.3127 0.2324 0.0058  0.0042  0.0074  301 A1IB9 A C2  
3716 C C3  . A1IB9 C .   ? 0.2710 0.3365 0.2564 0.0062  0.0045  0.0089  301 A1IB9 A C3  
3717 C C4  . A1IB9 C .   ? 0.2978 0.3643 0.2820 0.0061  0.0046  0.0100  301 A1IB9 A C4  
3718 C C5  . A1IB9 C .   ? 0.3278 0.3939 0.3116 0.0066  0.0049  0.0120  301 A1IB9 A C5  
3719 C C6  . A1IB9 C .   ? 0.3393 0.4067 0.3215 0.0063  0.0052  0.0130  301 A1IB9 A C6  
3720 C C7  . A1IB9 C .   ? 0.3523 0.4216 0.3337 0.0056  0.0051  0.0116  301 A1IB9 A C7  
3721 C C8  . A1IB9 C .   ? 0.3195 0.3891 0.3017 0.0054  0.0048  0.0096  301 A1IB9 A C8  
3722 C C9  . A1IB9 C .   ? 0.2918 0.3598 0.2751 0.0056  0.0045  0.0090  301 A1IB9 A C9  
3723 N N1  . A1IB9 C .   ? 0.3583 0.4295 0.3382 0.0051  0.0055  0.0123  301 A1IB9 A N1  
3724 O O2  . A1IB9 C .   ? 0.3466 0.4201 0.3260 0.0047  0.0052  0.0109  301 A1IB9 A O2  
3725 O O3  . A1IB9 C .   ? 0.4192 0.4894 0.3984 0.0048  0.0063  0.0142  301 A1IB9 A O3  
3726 C C1  . GOL   D .   ? 0.5254 0.5996 0.5432 -0.0016 0.0124  -0.0192 302 GOL   A C1  
3727 O O1  . GOL   D .   ? 0.5181 0.5939 0.5330 -0.0021 0.0118  -0.0190 302 GOL   A O1  
3728 C C2  . GOL   D .   ? 0.5101 0.5814 0.5260 -0.0003 0.0117  -0.0159 302 GOL   A C2  
3729 O O2  . GOL   D .   ? 0.5364 0.6059 0.5532 0.0018  0.0108  -0.0140 302 GOL   A O2  
3730 C C3  . GOL   D .   ? 0.5209 0.5910 0.5392 -0.0006 0.0127  -0.0165 302 GOL   A C3  
3731 O O3  . GOL   D .   ? 0.4323 0.4993 0.4499 0.0006  0.0123  -0.0137 302 GOL   A O3  
3732 C C1  . A1IB9 E .   ? 0.2530 0.3312 0.2581 -0.0025 0.0051  -0.0004 301 A1IB9 B C1  
3733 C C2  . A1IB9 E .   ? 0.2470 0.3245 0.2544 -0.0026 0.0053  -0.0019 301 A1IB9 B C2  
3734 C C3  . A1IB9 E .   ? 0.2621 0.3387 0.2738 -0.0023 0.0061  -0.0015 301 A1IB9 B C3  
3735 C C4  . A1IB9 E .   ? 0.2904 0.3661 0.3050 -0.0021 0.0064  -0.0033 301 A1IB9 B C4  
3736 C C5  . A1IB9 E .   ? 0.3252 0.3986 0.3445 -0.0019 0.0075  -0.0031 301 A1IB9 B C5  
3737 C C6  . A1IB9 E .   ? 0.3541 0.4263 0.3763 -0.0016 0.0078  -0.0054 301 A1IB9 B C6  
3738 C C7  . A1IB9 E .   ? 0.3462 0.4208 0.3665 -0.0014 0.0069  -0.0077 301 A1IB9 B C7  
3739 C C8  . A1IB9 E .   ? 0.3133 0.3903 0.3289 -0.0019 0.0059  -0.0076 301 A1IB9 B C8  
3740 C C9  . A1IB9 E .   ? 0.2575 0.3346 0.2704 -0.0023 0.0057  -0.0054 301 A1IB9 B C9  
3741 N N1  . A1IB9 E .   ? 0.3932 0.4673 0.4165 -0.0009 0.0072  -0.0105 301 A1IB9 B N1  
3742 O O2  . A1IB9 E .   ? 0.4339 0.5108 0.4557 -0.0007 0.0065  -0.0123 301 A1IB9 B O2  
3743 O O3  . A1IB9 E .   ? 0.5126 0.5838 0.5400 -0.0011 0.0082  -0.0112 301 A1IB9 B O3  
# 
