data_9J11
# 
_entry.id   9J11 
# 
_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   9J11         pdb_00009j11 10.2210/pdb9j11/pdb 
WWPDB D_1300050124 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-16 
_pdbx_audit_revision_history.part_number         ? 
# 
_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_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9J11 
_pdbx_database_status.recvd_initial_deposition_date   2024-08-03 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBC 
_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           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              zhengshuping_ibp@163.com 
_pdbx_contact_author.name_first         shuping 
_pdbx_contact_author.name_last          zheng 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-4695-2758 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Zheng, S.P.' 1 ? 
'Shi, X.R.'   2 ? 
# 
_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                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Acta Crystallogr D Struct Biol' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2059-7983 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            81 
_citation.language                  ? 
_citation.page_first                181 
_citation.page_last                 195 
_citation.title                     'Structural basis for the fast maturation of pcStar, a photoconvertible fluorescent protein.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1107/S2059798325002141 
_citation.pdbx_database_id_PubMed   40094266 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zheng, S.' 1  0000-0002-4695-2758 
primary 'Shi, X.'   2  0000-0001-8137-2305 
primary 'Lin, J.'   3  ?                   
primary 'Yang, Y.'  4  ?                   
primary 'Xin, Y.'   5  ?                   
primary 'Bai, X.'   6  ?                   
primary 'Zhu, H.'   7  ?                   
primary 'Chen, H.'  8  ?                   
primary 'Wu, J.'    9  ?                   
primary 'Zheng, X.' 10 ?                   
primary 'Lin, L.'   11 ?                   
primary 'Huang, Z.' 12 ?                   
primary 'Yang, S.'  13 ?                   
primary 'Hu, F.'    14 ?                   
primary 'Liu, W.'   15 0000-0003-0436-1797 
# 
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 'Green to red photoconvertible GFP-like protein EosFP' 28542.238 2   ? 
N11K,E70K,H74N,I102N,H121Y,V123T,T158E,Y189A ? 
;Fusion protein: MGSSHHHHHHSQDPLEVLFQGPEFMSAIKPDMKIKLRMEGNVNGHHFVIDGDGTGKPFEGKQSMDLEVKEGGPLPFAFDILTTAFHYGNRVFAKYPDNIQDYFKQSFPKGYSWERSLTFEDGGICNARNDITMEGDTFYNKVRFYGTNFPANGPVMQKKTLKWEPSTEKMYVRDGVLTGDIEMALLLEGNAHYRCDFRTTYKAKEKGVKLPGAHFVDHCIEILSHDKDYNKVKLYEHAVAHSGLPDNARR
;
2 non-polymer syn 2,3-DIHYDROXY-1,4-DITHIOBUTANE                         154.251   1   ? ? ? ? 
3 water       nat water                                                  18.015    431 ? ? ? ? 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   yes 
_entity_poly.pdbx_seq_one_letter_code       
;MGSSHHHHHHSQDPLEVLFQGPEFMSAIKPDMKIKLRMEGNVNGHHFVIDGDGTGKPFEGKQSMDLEVKEGGPLPFAFDI
LTTAF(5SQ)NRVFAKYPDNIQDYFKQSFPKGYSWERSLTFEDGGICNARNDITMEGDTFYNKVRFYGTNFPANGPVMQK
KTLKWEPSTEKMYVRDGVLTGDIEMALLLEGNAHYRCDFRTTYKAKEKGVKLPGAHFVDHCIEILSHDKDYNKVKLYEHA
VAHSGLPDNARR
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MGSSHHHHHHSQDPLEVLFQGPEFMSAIKPDMKIKLRMEGNVNGHHFVIDGDGTGKPFEGKQSMDLEVKEGGPLPFAFDI
LTTAFHYGNRVFAKYPDNIQDYFKQSFPKGYSWERSLTFEDGGICNARNDITMEGDTFYNKVRFYGTNFPANGPVMQKKT
LKWEPSTEKMYVRDGVLTGDIEMALLLEGNAHYRCDFRTTYKAKEKGVKLPGAHFVDHCIEILSHDKDYNKVKLYEHAVA
HSGLPDNARR
;
_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 2,3-DIHYDROXY-1,4-DITHIOBUTANE DTT 
3 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   GLY n 
1 3   SER n 
1 4   SER n 
1 5   HIS n 
1 6   HIS n 
1 7   HIS n 
1 8   HIS n 
1 9   HIS n 
1 10  HIS n 
1 11  SER n 
1 12  GLN n 
1 13  ASP n 
1 14  PRO n 
1 15  LEU n 
1 16  GLU n 
1 17  VAL n 
1 18  LEU n 
1 19  PHE n 
1 20  GLN n 
1 21  GLY n 
1 22  PRO n 
1 23  GLU n 
1 24  PHE n 
1 25  MET n 
1 26  SER n 
1 27  ALA n 
1 28  ILE n 
1 29  LYS n 
1 30  PRO n 
1 31  ASP n 
1 32  MET n 
1 33  LYS n 
1 34  ILE n 
1 35  LYS n 
1 36  LEU n 
1 37  ARG n 
1 38  MET n 
1 39  GLU n 
1 40  GLY n 
1 41  ASN n 
1 42  VAL n 
1 43  ASN n 
1 44  GLY n 
1 45  HIS n 
1 46  HIS n 
1 47  PHE n 
1 48  VAL n 
1 49  ILE n 
1 50  ASP n 
1 51  GLY n 
1 52  ASP n 
1 53  GLY n 
1 54  THR n 
1 55  GLY n 
1 56  LYS n 
1 57  PRO n 
1 58  PHE n 
1 59  GLU n 
1 60  GLY n 
1 61  LYS n 
1 62  GLN n 
1 63  SER n 
1 64  MET n 
1 65  ASP n 
1 66  LEU n 
1 67  GLU n 
1 68  VAL n 
1 69  LYS n 
1 70  GLU n 
1 71  GLY n 
1 72  GLY n 
1 73  PRO n 
1 74  LEU n 
1 75  PRO n 
1 76  PHE n 
1 77  ALA n 
1 78  PHE n 
1 79  ASP n 
1 80  ILE n 
1 81  LEU n 
1 82  THR n 
1 83  THR n 
1 84  ALA n 
1 85  PHE n 
1 86  5SQ n 
1 87  ASN n 
1 88  ARG n 
1 89  VAL n 
1 90  PHE n 
1 91  ALA n 
1 92  LYS n 
1 93  TYR n 
1 94  PRO n 
1 95  ASP n 
1 96  ASN n 
1 97  ILE n 
1 98  GLN n 
1 99  ASP n 
1 100 TYR n 
1 101 PHE n 
1 102 LYS n 
1 103 GLN n 
1 104 SER n 
1 105 PHE n 
1 106 PRO n 
1 107 LYS n 
1 108 GLY n 
1 109 TYR n 
1 110 SER n 
1 111 TRP n 
1 112 GLU n 
1 113 ARG n 
1 114 SER n 
1 115 LEU n 
1 116 THR n 
1 117 PHE n 
1 118 GLU n 
1 119 ASP n 
1 120 GLY n 
1 121 GLY n 
1 122 ILE n 
1 123 CYS n 
1 124 ASN n 
1 125 ALA n 
1 126 ARG n 
1 127 ASN n 
1 128 ASP n 
1 129 ILE n 
1 130 THR n 
1 131 MET n 
1 132 GLU n 
1 133 GLY n 
1 134 ASP n 
1 135 THR n 
1 136 PHE n 
1 137 TYR n 
1 138 ASN n 
1 139 LYS n 
1 140 VAL n 
1 141 ARG n 
1 142 PHE n 
1 143 TYR n 
1 144 GLY n 
1 145 THR n 
1 146 ASN n 
1 147 PHE n 
1 148 PRO n 
1 149 ALA n 
1 150 ASN n 
1 151 GLY n 
1 152 PRO n 
1 153 VAL n 
1 154 MET n 
1 155 GLN n 
1 156 LYS n 
1 157 LYS n 
1 158 THR n 
1 159 LEU n 
1 160 LYS n 
1 161 TRP n 
1 162 GLU n 
1 163 PRO n 
1 164 SER n 
1 165 THR n 
1 166 GLU n 
1 167 LYS n 
1 168 MET n 
1 169 TYR n 
1 170 VAL n 
1 171 ARG n 
1 172 ASP n 
1 173 GLY n 
1 174 VAL n 
1 175 LEU n 
1 176 THR n 
1 177 GLY n 
1 178 ASP n 
1 179 ILE n 
1 180 GLU n 
1 181 MET n 
1 182 ALA n 
1 183 LEU n 
1 184 LEU n 
1 185 LEU n 
1 186 GLU n 
1 187 GLY n 
1 188 ASN n 
1 189 ALA n 
1 190 HIS n 
1 191 TYR n 
1 192 ARG n 
1 193 CYS n 
1 194 ASP n 
1 195 PHE n 
1 196 ARG n 
1 197 THR n 
1 198 THR n 
1 199 TYR n 
1 200 LYS n 
1 201 ALA n 
1 202 LYS n 
1 203 GLU n 
1 204 LYS n 
1 205 GLY n 
1 206 VAL n 
1 207 LYS n 
1 208 LEU n 
1 209 PRO n 
1 210 GLY n 
1 211 ALA n 
1 212 HIS n 
1 213 PHE n 
1 214 VAL n 
1 215 ASP n 
1 216 HIS n 
1 217 CYS n 
1 218 ILE n 
1 219 GLU n 
1 220 ILE n 
1 221 LEU n 
1 222 SER n 
1 223 HIS n 
1 224 ASP n 
1 225 LYS n 
1 226 ASP n 
1 227 TYR n 
1 228 ASN n 
1 229 LYS n 
1 230 VAL n 
1 231 LYS n 
1 232 LEU n 
1 233 TYR n 
1 234 GLU n 
1 235 HIS n 
1 236 ALA n 
1 237 VAL n 
1 238 ALA n 
1 239 HIS n 
1 240 SER n 
1 241 GLY n 
1 242 LEU n 
1 243 PRO n 
1 244 ASP n 
1 245 ASN n 
1 246 ALA n 
1 247 ARG n 
1 248 ARG 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                   248 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_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      'Lobophyllia hemprichii' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     46758 
_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 
5SQ 'L-peptide linking' n 
'2-[2-[(1S)-1-azanyl-2-(1H-imidazol-4-yl)ethyl]-4-[(4-hydroxyphenyl)methylidene]-5-oxidanylidene-imidazol-1-yl]ethanoic acid' 
'GREEN CHROMOPHORE (HIS-TYR-GLY)' 'C17 H17 N5 O4'  355.348 
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 
DTT non-polymer         . 2,3-DIHYDROXY-1,4-DITHIOBUTANE 1,4-DITHIOTHREITOL                'C4 H10 O2 S2'   154.251 
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  
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   -23 ?   ?   ?   A . n 
A 1 2   GLY 2   -22 ?   ?   ?   A . n 
A 1 3   SER 3   -21 ?   ?   ?   A . n 
A 1 4   SER 4   -20 ?   ?   ?   A . n 
A 1 5   HIS 5   -19 ?   ?   ?   A . n 
A 1 6   HIS 6   -18 ?   ?   ?   A . n 
A 1 7   HIS 7   -17 ?   ?   ?   A . n 
A 1 8   HIS 8   -16 ?   ?   ?   A . n 
A 1 9   HIS 9   -15 ?   ?   ?   A . n 
A 1 10  HIS 10  -14 ?   ?   ?   A . n 
A 1 11  SER 11  -13 ?   ?   ?   A . n 
A 1 12  GLN 12  -12 ?   ?   ?   A . n 
A 1 13  ASP 13  -11 ?   ?   ?   A . n 
A 1 14  PRO 14  -10 ?   ?   ?   A . n 
A 1 15  LEU 15  -9  ?   ?   ?   A . n 
A 1 16  GLU 16  -8  ?   ?   ?   A . n 
A 1 17  VAL 17  -7  ?   ?   ?   A . n 
A 1 18  LEU 18  -6  ?   ?   ?   A . n 
A 1 19  PHE 19  -5  ?   ?   ?   A . n 
A 1 20  GLN 20  -4  ?   ?   ?   A . n 
A 1 21  GLY 21  -3  ?   ?   ?   A . n 
A 1 22  PRO 22  -2  ?   ?   ?   A . n 
A 1 23  GLU 23  -1  ?   ?   ?   A . n 
A 1 24  PHE 24  0   ?   ?   ?   A . n 
A 1 25  MET 25  1   ?   ?   ?   A . n 
A 1 26  SER 26  2   2   SER SER A . n 
A 1 27  ALA 27  3   3   ALA ALA A . n 
A 1 28  ILE 28  4   4   ILE ILE A . n 
A 1 29  LYS 29  5   5   LYS LYS A . n 
A 1 30  PRO 30  6   6   PRO PRO A . n 
A 1 31  ASP 31  7   7   ASP ASP A . n 
A 1 32  MET 32  8   8   MET MET A . n 
A 1 33  LYS 33  9   9   LYS LYS A . n 
A 1 34  ILE 34  10  10  ILE ILE A . n 
A 1 35  LYS 35  11  11  LYS LYS A . n 
A 1 36  LEU 36  12  12  LEU LEU A . n 
A 1 37  ARG 37  13  13  ARG ARG A . n 
A 1 38  MET 38  14  14  MET MET A . n 
A 1 39  GLU 39  15  15  GLU GLU A . n 
A 1 40  GLY 40  16  16  GLY GLY A . n 
A 1 41  ASN 41  17  17  ASN ASN A . n 
A 1 42  VAL 42  18  18  VAL VAL A . n 
A 1 43  ASN 43  19  19  ASN ASN A . n 
A 1 44  GLY 44  20  20  GLY GLY A . n 
A 1 45  HIS 45  21  21  HIS HIS A . n 
A 1 46  HIS 46  22  22  HIS HIS A . n 
A 1 47  PHE 47  23  23  PHE PHE A . n 
A 1 48  VAL 48  24  24  VAL VAL A . n 
A 1 49  ILE 49  25  25  ILE ILE A . n 
A 1 50  ASP 50  26  26  ASP ASP A . n 
A 1 51  GLY 51  27  27  GLY GLY A . n 
A 1 52  ASP 52  28  28  ASP ASP A . n 
A 1 53  GLY 53  29  29  GLY GLY A . n 
A 1 54  THR 54  30  30  THR THR A . n 
A 1 55  GLY 55  31  31  GLY GLY A . n 
A 1 56  LYS 56  32  32  LYS LYS A . n 
A 1 57  PRO 57  33  33  PRO PRO A . n 
A 1 58  PHE 58  34  34  PHE PHE A . n 
A 1 59  GLU 59  35  35  GLU GLU A . n 
A 1 60  GLY 60  36  36  GLY GLY A . n 
A 1 61  LYS 61  37  37  LYS LYS A . n 
A 1 62  GLN 62  38  38  GLN GLN A . n 
A 1 63  SER 63  39  39  SER SER A . n 
A 1 64  MET 64  40  40  MET MET A . n 
A 1 65  ASP 65  41  41  ASP ASP A . n 
A 1 66  LEU 66  42  42  LEU LEU A . n 
A 1 67  GLU 67  43  43  GLU GLU A . n 
A 1 68  VAL 68  44  44  VAL VAL A . n 
A 1 69  LYS 69  45  45  LYS LYS A . n 
A 1 70  GLU 70  46  46  GLU GLU A . n 
A 1 71  GLY 71  47  47  GLY GLY A . n 
A 1 72  GLY 72  48  48  GLY GLY A . n 
A 1 73  PRO 73  49  49  PRO PRO A . n 
A 1 74  LEU 74  50  50  LEU LEU A . n 
A 1 75  PRO 75  51  51  PRO PRO A . n 
A 1 76  PHE 76  52  52  PHE PHE A . n 
A 1 77  ALA 77  53  53  ALA ALA A . n 
A 1 78  PHE 78  54  54  PHE PHE A . n 
A 1 79  ASP 79  55  55  ASP ASP A . n 
A 1 80  ILE 80  56  56  ILE ILE A . n 
A 1 81  LEU 81  57  57  LEU LEU A . n 
A 1 82  THR 82  58  58  THR THR A . n 
A 1 83  THR 83  59  59  THR THR A . n 
A 1 84  ALA 84  60  60  ALA ALA A . n 
A 1 85  PHE 85  61  61  PHE PHE A . n 
A 1 86  5SQ 86  64  64  5SQ 5SQ A . n 
A 1 87  ASN 87  65  65  ASN ASN A . n 
A 1 88  ARG 88  66  66  ARG ARG A . n 
A 1 89  VAL 89  67  67  VAL VAL A . n 
A 1 90  PHE 90  68  68  PHE PHE A . n 
A 1 91  ALA 91  69  69  ALA ALA A . n 
A 1 92  LYS 92  70  70  LYS LYS A . n 
A 1 93  TYR 93  71  71  TYR TYR A . n 
A 1 94  PRO 94  72  72  PRO PRO A . n 
A 1 95  ASP 95  73  73  ASP ASP A . n 
A 1 96  ASN 96  74  74  ASN ASN A . n 
A 1 97  ILE 97  75  75  ILE ILE A . n 
A 1 98  GLN 98  76  76  GLN GLN A . n 
A 1 99  ASP 99  77  77  ASP ASP A . n 
A 1 100 TYR 100 78  78  TYR TYR A . n 
A 1 101 PHE 101 79  79  PHE PHE A . n 
A 1 102 LYS 102 80  80  LYS LYS A . n 
A 1 103 GLN 103 81  81  GLN GLN A . n 
A 1 104 SER 104 82  82  SER SER A . n 
A 1 105 PHE 105 83  83  PHE PHE A . n 
A 1 106 PRO 106 84  84  PRO PRO A . n 
A 1 107 LYS 107 85  85  LYS LYS A . n 
A 1 108 GLY 108 86  86  GLY GLY A . n 
A 1 109 TYR 109 87  87  TYR TYR A . n 
A 1 110 SER 110 88  88  SER SER A . n 
A 1 111 TRP 111 89  89  TRP TRP A . n 
A 1 112 GLU 112 90  90  GLU GLU A . n 
A 1 113 ARG 113 91  91  ARG ARG A . n 
A 1 114 SER 114 92  92  SER SER A . n 
A 1 115 LEU 115 93  93  LEU LEU A . n 
A 1 116 THR 116 94  94  THR THR A . n 
A 1 117 PHE 117 95  95  PHE PHE A . n 
A 1 118 GLU 118 96  96  GLU GLU A . n 
A 1 119 ASP 119 97  97  ASP ASP A . n 
A 1 120 GLY 120 98  98  GLY GLY A . n 
A 1 121 GLY 121 99  99  GLY GLY A . n 
A 1 122 ILE 122 100 100 ILE ILE A . n 
A 1 123 CYS 123 101 101 CYS CYS A . n 
A 1 124 ASN 124 102 102 ASN ASN A . n 
A 1 125 ALA 125 103 103 ALA ALA A . n 
A 1 126 ARG 126 104 104 ARG ARG A . n 
A 1 127 ASN 127 105 105 ASN ASN A . n 
A 1 128 ASP 128 106 106 ASP ASP A . n 
A 1 129 ILE 129 107 107 ILE ILE A . n 
A 1 130 THR 130 108 108 THR THR A . n 
A 1 131 MET 131 109 109 MET MET A . n 
A 1 132 GLU 132 110 110 GLU GLU A . n 
A 1 133 GLY 133 111 111 GLY GLY A . n 
A 1 134 ASP 134 112 112 ASP ASP A . n 
A 1 135 THR 135 113 113 THR THR A . n 
A 1 136 PHE 136 114 114 PHE PHE A . n 
A 1 137 TYR 137 115 115 TYR TYR A . n 
A 1 138 ASN 138 116 116 ASN ASN A . n 
A 1 139 LYS 139 117 117 LYS LYS A . n 
A 1 140 VAL 140 118 118 VAL VAL A . n 
A 1 141 ARG 141 119 119 ARG ARG A . n 
A 1 142 PHE 142 120 120 PHE PHE A . n 
A 1 143 TYR 143 121 121 TYR TYR A . n 
A 1 144 GLY 144 122 122 GLY GLY A . n 
A 1 145 THR 145 123 123 THR THR A . n 
A 1 146 ASN 146 124 124 ASN ASN A . n 
A 1 147 PHE 147 125 125 PHE PHE A . n 
A 1 148 PRO 148 126 126 PRO PRO A . n 
A 1 149 ALA 149 127 127 ALA ALA A . n 
A 1 150 ASN 150 128 128 ASN ASN A . n 
A 1 151 GLY 151 129 129 GLY GLY A . n 
A 1 152 PRO 152 130 130 PRO PRO A . n 
A 1 153 VAL 153 131 131 VAL VAL A . n 
A 1 154 MET 154 132 132 MET MET A . n 
A 1 155 GLN 155 133 133 GLN GLN A . n 
A 1 156 LYS 156 134 134 LYS LYS A . n 
A 1 157 LYS 157 135 135 LYS LYS A . n 
A 1 158 THR 158 136 136 THR THR A . n 
A 1 159 LEU 159 137 137 LEU LEU A . n 
A 1 160 LYS 160 138 138 LYS LYS A . n 
A 1 161 TRP 161 139 139 TRP TRP A . n 
A 1 162 GLU 162 140 140 GLU GLU A . n 
A 1 163 PRO 163 141 141 PRO PRO A . n 
A 1 164 SER 164 142 142 SER SER A . n 
A 1 165 THR 165 143 143 THR THR A . n 
A 1 166 GLU 166 144 144 GLU GLU A . n 
A 1 167 LYS 167 145 145 LYS LYS A . n 
A 1 168 MET 168 146 146 MET MET A . n 
A 1 169 TYR 169 147 147 TYR TYR A . n 
A 1 170 VAL 170 148 148 VAL VAL A . n 
A 1 171 ARG 171 149 149 ARG ARG A . n 
A 1 172 ASP 172 150 150 ASP ASP A . n 
A 1 173 GLY 173 151 151 GLY GLY A . n 
A 1 174 VAL 174 152 152 VAL VAL A . n 
A 1 175 LEU 175 153 153 LEU LEU A . n 
A 1 176 THR 176 154 154 THR THR A . n 
A 1 177 GLY 177 155 155 GLY GLY A . n 
A 1 178 ASP 178 156 156 ASP ASP A . n 
A 1 179 ILE 179 157 157 ILE ILE A . n 
A 1 180 GLU 180 158 158 GLU GLU A . n 
A 1 181 MET 181 159 159 MET MET A . n 
A 1 182 ALA 182 160 160 ALA ALA A . n 
A 1 183 LEU 183 161 161 LEU LEU A . n 
A 1 184 LEU 184 162 162 LEU LEU A . n 
A 1 185 LEU 185 163 163 LEU LEU A . n 
A 1 186 GLU 186 164 164 GLU GLU A . n 
A 1 187 GLY 187 165 165 GLY GLY A . n 
A 1 188 ASN 188 166 166 ASN ASN A . n 
A 1 189 ALA 189 167 167 ALA ALA A . n 
A 1 190 HIS 190 168 168 HIS HIS A . n 
A 1 191 TYR 191 169 169 TYR TYR A . n 
A 1 192 ARG 192 170 170 ARG ARG A . n 
A 1 193 CYS 193 171 171 CYS CYS A . n 
A 1 194 ASP 194 172 172 ASP ASP A . n 
A 1 195 PHE 195 173 173 PHE PHE A . n 
A 1 196 ARG 196 174 174 ARG ARG A . n 
A 1 197 THR 197 175 175 THR THR A . n 
A 1 198 THR 198 176 176 THR THR A . n 
A 1 199 TYR 199 177 177 TYR TYR A . n 
A 1 200 LYS 200 178 178 LYS LYS A . n 
A 1 201 ALA 201 179 179 ALA ALA A . n 
A 1 202 LYS 202 180 180 LYS LYS A . n 
A 1 203 GLU 203 181 181 GLU GLU A . n 
A 1 204 LYS 204 182 182 LYS LYS A . n 
A 1 205 GLY 205 183 183 GLY GLY A . n 
A 1 206 VAL 206 184 184 VAL VAL A . n 
A 1 207 LYS 207 185 185 LYS LYS A . n 
A 1 208 LEU 208 186 186 LEU LEU A . n 
A 1 209 PRO 209 187 187 PRO PRO A . n 
A 1 210 GLY 210 188 188 GLY GLY A . n 
A 1 211 ALA 211 189 189 ALA ALA A . n 
A 1 212 HIS 212 190 190 HIS HIS A . n 
A 1 213 PHE 213 191 191 PHE PHE A . n 
A 1 214 VAL 214 192 192 VAL VAL A . n 
A 1 215 ASP 215 193 193 ASP ASP A . n 
A 1 216 HIS 216 194 194 HIS HIS A . n 
A 1 217 CYS 217 195 195 CYS CYS A . n 
A 1 218 ILE 218 196 196 ILE ILE A . n 
A 1 219 GLU 219 197 197 GLU GLU A . n 
A 1 220 ILE 220 198 198 ILE ILE A . n 
A 1 221 LEU 221 199 199 LEU LEU A . n 
A 1 222 SER 222 200 200 SER SER A . n 
A 1 223 HIS 223 201 201 HIS HIS A . n 
A 1 224 ASP 224 202 202 ASP ASP A . n 
A 1 225 LYS 225 203 203 LYS LYS A . n 
A 1 226 ASP 226 204 204 ASP ASP A . n 
A 1 227 TYR 227 205 205 TYR TYR A . n 
A 1 228 ASN 228 206 206 ASN ASN A . n 
A 1 229 LYS 229 207 207 LYS LYS A . n 
A 1 230 VAL 230 208 208 VAL VAL A . n 
A 1 231 LYS 231 209 209 LYS LYS A . n 
A 1 232 LEU 232 210 210 LEU LEU A . n 
A 1 233 TYR 233 211 211 TYR TYR A . n 
A 1 234 GLU 234 212 212 GLU GLU A . n 
A 1 235 HIS 235 213 213 HIS HIS A . n 
A 1 236 ALA 236 214 214 ALA ALA A . n 
A 1 237 VAL 237 215 215 VAL VAL A . n 
A 1 238 ALA 238 216 216 ALA ALA A . n 
A 1 239 HIS 239 217 217 HIS HIS A . n 
A 1 240 SER 240 218 218 SER SER A . n 
A 1 241 GLY 241 219 219 GLY GLY A . n 
A 1 242 LEU 242 220 ?   ?   ?   A . n 
A 1 243 PRO 243 221 ?   ?   ?   A . n 
A 1 244 ASP 244 222 ?   ?   ?   A . n 
A 1 245 ASN 245 223 ?   ?   ?   A . n 
A 1 246 ALA 246 224 ?   ?   ?   A . n 
A 1 247 ARG 247 225 ?   ?   ?   A . n 
A 1 248 ARG 248 226 ?   ?   ?   A . n 
B 1 1   MET 1   -23 ?   ?   ?   B . n 
B 1 2   GLY 2   -22 ?   ?   ?   B . n 
B 1 3   SER 3   -21 ?   ?   ?   B . n 
B 1 4   SER 4   -20 ?   ?   ?   B . n 
B 1 5   HIS 5   -19 ?   ?   ?   B . n 
B 1 6   HIS 6   -18 ?   ?   ?   B . n 
B 1 7   HIS 7   -17 ?   ?   ?   B . n 
B 1 8   HIS 8   -16 ?   ?   ?   B . n 
B 1 9   HIS 9   -15 ?   ?   ?   B . n 
B 1 10  HIS 10  -14 ?   ?   ?   B . n 
B 1 11  SER 11  -13 ?   ?   ?   B . n 
B 1 12  GLN 12  -12 ?   ?   ?   B . n 
B 1 13  ASP 13  -11 ?   ?   ?   B . n 
B 1 14  PRO 14  -10 ?   ?   ?   B . n 
B 1 15  LEU 15  -9  ?   ?   ?   B . n 
B 1 16  GLU 16  -8  ?   ?   ?   B . n 
B 1 17  VAL 17  -7  ?   ?   ?   B . n 
B 1 18  LEU 18  -6  ?   ?   ?   B . n 
B 1 19  PHE 19  -5  ?   ?   ?   B . n 
B 1 20  GLN 20  -4  ?   ?   ?   B . n 
B 1 21  GLY 21  -3  ?   ?   ?   B . n 
B 1 22  PRO 22  -2  ?   ?   ?   B . n 
B 1 23  GLU 23  -1  ?   ?   ?   B . n 
B 1 24  PHE 24  0   ?   ?   ?   B . n 
B 1 25  MET 25  1   ?   ?   ?   B . n 
B 1 26  SER 26  2   2   SER SER B . n 
B 1 27  ALA 27  3   3   ALA ALA B . n 
B 1 28  ILE 28  4   4   ILE ILE B . n 
B 1 29  LYS 29  5   5   LYS LYS B . n 
B 1 30  PRO 30  6   6   PRO PRO B . n 
B 1 31  ASP 31  7   7   ASP ASP B . n 
B 1 32  MET 32  8   8   MET MET B . n 
B 1 33  LYS 33  9   9   LYS LYS B . n 
B 1 34  ILE 34  10  10  ILE ILE B . n 
B 1 35  LYS 35  11  11  LYS LYS B . n 
B 1 36  LEU 36  12  12  LEU LEU B . n 
B 1 37  ARG 37  13  13  ARG ARG B . n 
B 1 38  MET 38  14  14  MET MET B . n 
B 1 39  GLU 39  15  15  GLU GLU B . n 
B 1 40  GLY 40  16  16  GLY GLY B . n 
B 1 41  ASN 41  17  17  ASN ASN B . n 
B 1 42  VAL 42  18  18  VAL VAL B . n 
B 1 43  ASN 43  19  19  ASN ASN B . n 
B 1 44  GLY 44  20  20  GLY GLY B . n 
B 1 45  HIS 45  21  21  HIS HIS B . n 
B 1 46  HIS 46  22  22  HIS HIS B . n 
B 1 47  PHE 47  23  23  PHE PHE B . n 
B 1 48  VAL 48  24  24  VAL VAL B . n 
B 1 49  ILE 49  25  25  ILE ILE B . n 
B 1 50  ASP 50  26  26  ASP ASP B . n 
B 1 51  GLY 51  27  27  GLY GLY B . n 
B 1 52  ASP 52  28  28  ASP ASP B . n 
B 1 53  GLY 53  29  29  GLY GLY B . n 
B 1 54  THR 54  30  30  THR THR B . n 
B 1 55  GLY 55  31  31  GLY GLY B . n 
B 1 56  LYS 56  32  32  LYS LYS B . n 
B 1 57  PRO 57  33  33  PRO PRO B . n 
B 1 58  PHE 58  34  34  PHE PHE B . n 
B 1 59  GLU 59  35  35  GLU GLU B . n 
B 1 60  GLY 60  36  36  GLY GLY B . n 
B 1 61  LYS 61  37  37  LYS LYS B . n 
B 1 62  GLN 62  38  38  GLN GLN B . n 
B 1 63  SER 63  39  39  SER SER B . n 
B 1 64  MET 64  40  40  MET MET B . n 
B 1 65  ASP 65  41  41  ASP ASP B . n 
B 1 66  LEU 66  42  42  LEU LEU B . n 
B 1 67  GLU 67  43  43  GLU GLU B . n 
B 1 68  VAL 68  44  44  VAL VAL B . n 
B 1 69  LYS 69  45  45  LYS LYS B . n 
B 1 70  GLU 70  46  46  GLU GLU B . n 
B 1 71  GLY 71  47  47  GLY GLY B . n 
B 1 72  GLY 72  48  48  GLY GLY B . n 
B 1 73  PRO 73  49  49  PRO PRO B . n 
B 1 74  LEU 74  50  50  LEU LEU B . n 
B 1 75  PRO 75  51  51  PRO PRO B . n 
B 1 76  PHE 76  52  52  PHE PHE B . n 
B 1 77  ALA 77  53  53  ALA ALA B . n 
B 1 78  PHE 78  54  54  PHE PHE B . n 
B 1 79  ASP 79  55  55  ASP ASP B . n 
B 1 80  ILE 80  56  56  ILE ILE B . n 
B 1 81  LEU 81  57  57  LEU LEU B . n 
B 1 82  THR 82  58  58  THR THR B . n 
B 1 83  THR 83  59  59  THR THR B . n 
B 1 84  ALA 84  60  60  ALA ALA B . n 
B 1 85  PHE 85  61  61  PHE PHE B . n 
B 1 86  5SQ 86  64  64  5SQ 5SQ B . n 
B 1 87  ASN 87  65  65  ASN ASN B . n 
B 1 88  ARG 88  66  66  ARG ARG B . n 
B 1 89  VAL 89  67  67  VAL VAL B . n 
B 1 90  PHE 90  68  68  PHE PHE B . n 
B 1 91  ALA 91  69  69  ALA ALA B . n 
B 1 92  LYS 92  70  70  LYS LYS B . n 
B 1 93  TYR 93  71  71  TYR TYR B . n 
B 1 94  PRO 94  72  72  PRO PRO B . n 
B 1 95  ASP 95  73  73  ASP ASP B . n 
B 1 96  ASN 96  74  74  ASN ASN B . n 
B 1 97  ILE 97  75  75  ILE ILE B . n 
B 1 98  GLN 98  76  76  GLN GLN B . n 
B 1 99  ASP 99  77  77  ASP ASP B . n 
B 1 100 TYR 100 78  78  TYR TYR B . n 
B 1 101 PHE 101 79  79  PHE PHE B . n 
B 1 102 LYS 102 80  80  LYS LYS B . n 
B 1 103 GLN 103 81  81  GLN GLN B . n 
B 1 104 SER 104 82  82  SER SER B . n 
B 1 105 PHE 105 83  83  PHE PHE B . n 
B 1 106 PRO 106 84  84  PRO PRO B . n 
B 1 107 LYS 107 85  85  LYS LYS B . n 
B 1 108 GLY 108 86  86  GLY GLY B . n 
B 1 109 TYR 109 87  87  TYR TYR B . n 
B 1 110 SER 110 88  88  SER SER B . n 
B 1 111 TRP 111 89  89  TRP TRP B . n 
B 1 112 GLU 112 90  90  GLU GLU B . n 
B 1 113 ARG 113 91  91  ARG ARG B . n 
B 1 114 SER 114 92  92  SER SER B . n 
B 1 115 LEU 115 93  93  LEU LEU B . n 
B 1 116 THR 116 94  94  THR THR B . n 
B 1 117 PHE 117 95  95  PHE PHE B . n 
B 1 118 GLU 118 96  96  GLU GLU B . n 
B 1 119 ASP 119 97  97  ASP ASP B . n 
B 1 120 GLY 120 98  98  GLY GLY B . n 
B 1 121 GLY 121 99  99  GLY GLY B . n 
B 1 122 ILE 122 100 100 ILE ILE B . n 
B 1 123 CYS 123 101 101 CYS CYS B . n 
B 1 124 ASN 124 102 102 ASN ASN B . n 
B 1 125 ALA 125 103 103 ALA ALA B . n 
B 1 126 ARG 126 104 104 ARG ARG B . n 
B 1 127 ASN 127 105 105 ASN ASN B . n 
B 1 128 ASP 128 106 106 ASP ASP B . n 
B 1 129 ILE 129 107 107 ILE ILE B . n 
B 1 130 THR 130 108 108 THR THR B . n 
B 1 131 MET 131 109 109 MET MET B . n 
B 1 132 GLU 132 110 110 GLU GLU B . n 
B 1 133 GLY 133 111 111 GLY GLY B . n 
B 1 134 ASP 134 112 112 ASP ASP B . n 
B 1 135 THR 135 113 113 THR THR B . n 
B 1 136 PHE 136 114 114 PHE PHE B . n 
B 1 137 TYR 137 115 115 TYR TYR B . n 
B 1 138 ASN 138 116 116 ASN ASN B . n 
B 1 139 LYS 139 117 117 LYS LYS B . n 
B 1 140 VAL 140 118 118 VAL VAL B . n 
B 1 141 ARG 141 119 119 ARG ARG B . n 
B 1 142 PHE 142 120 120 PHE PHE B . n 
B 1 143 TYR 143 121 121 TYR TYR B . n 
B 1 144 GLY 144 122 122 GLY GLY B . n 
B 1 145 THR 145 123 123 THR THR B . n 
B 1 146 ASN 146 124 124 ASN ASN B . n 
B 1 147 PHE 147 125 125 PHE PHE B . n 
B 1 148 PRO 148 126 126 PRO PRO B . n 
B 1 149 ALA 149 127 127 ALA ALA B . n 
B 1 150 ASN 150 128 128 ASN ASN B . n 
B 1 151 GLY 151 129 129 GLY GLY B . n 
B 1 152 PRO 152 130 130 PRO PRO B . n 
B 1 153 VAL 153 131 131 VAL VAL B . n 
B 1 154 MET 154 132 132 MET MET B . n 
B 1 155 GLN 155 133 133 GLN GLN B . n 
B 1 156 LYS 156 134 134 LYS LYS B . n 
B 1 157 LYS 157 135 135 LYS LYS B . n 
B 1 158 THR 158 136 136 THR THR B . n 
B 1 159 LEU 159 137 137 LEU LEU B . n 
B 1 160 LYS 160 138 138 LYS LYS B . n 
B 1 161 TRP 161 139 139 TRP TRP B . n 
B 1 162 GLU 162 140 140 GLU GLU B . n 
B 1 163 PRO 163 141 141 PRO PRO B . n 
B 1 164 SER 164 142 142 SER SER B . n 
B 1 165 THR 165 143 143 THR THR B . n 
B 1 166 GLU 166 144 144 GLU GLU B . n 
B 1 167 LYS 167 145 145 LYS LYS B . n 
B 1 168 MET 168 146 146 MET MET B . n 
B 1 169 TYR 169 147 147 TYR TYR B . n 
B 1 170 VAL 170 148 148 VAL VAL B . n 
B 1 171 ARG 171 149 149 ARG ARG B . n 
B 1 172 ASP 172 150 150 ASP ASP B . n 
B 1 173 GLY 173 151 151 GLY GLY B . n 
B 1 174 VAL 174 152 152 VAL VAL B . n 
B 1 175 LEU 175 153 153 LEU LEU B . n 
B 1 176 THR 176 154 154 THR THR B . n 
B 1 177 GLY 177 155 155 GLY GLY B . n 
B 1 178 ASP 178 156 156 ASP ASP B . n 
B 1 179 ILE 179 157 157 ILE ILE B . n 
B 1 180 GLU 180 158 158 GLU GLU B . n 
B 1 181 MET 181 159 159 MET MET B . n 
B 1 182 ALA 182 160 160 ALA ALA B . n 
B 1 183 LEU 183 161 161 LEU LEU B . n 
B 1 184 LEU 184 162 162 LEU LEU B . n 
B 1 185 LEU 185 163 163 LEU LEU B . n 
B 1 186 GLU 186 164 164 GLU GLU B . n 
B 1 187 GLY 187 165 165 GLY GLY B . n 
B 1 188 ASN 188 166 166 ASN ASN B . n 
B 1 189 ALA 189 167 167 ALA ALA B . n 
B 1 190 HIS 190 168 168 HIS HIS B . n 
B 1 191 TYR 191 169 169 TYR TYR B . n 
B 1 192 ARG 192 170 170 ARG ARG B . n 
B 1 193 CYS 193 171 171 CYS CYS B . n 
B 1 194 ASP 194 172 172 ASP ASP B . n 
B 1 195 PHE 195 173 173 PHE PHE B . n 
B 1 196 ARG 196 174 174 ARG ARG B . n 
B 1 197 THR 197 175 175 THR THR B . n 
B 1 198 THR 198 176 176 THR THR B . n 
B 1 199 TYR 199 177 177 TYR TYR B . n 
B 1 200 LYS 200 178 178 LYS LYS B . n 
B 1 201 ALA 201 179 179 ALA ALA B . n 
B 1 202 LYS 202 180 180 LYS LYS B . n 
B 1 203 GLU 203 181 181 GLU GLU B . n 
B 1 204 LYS 204 182 182 LYS LYS B . n 
B 1 205 GLY 205 183 183 GLY GLY B . n 
B 1 206 VAL 206 184 184 VAL VAL B . n 
B 1 207 LYS 207 185 185 LYS LYS B . n 
B 1 208 LEU 208 186 186 LEU LEU B . n 
B 1 209 PRO 209 187 187 PRO PRO B . n 
B 1 210 GLY 210 188 188 GLY GLY B . n 
B 1 211 ALA 211 189 189 ALA ALA B . n 
B 1 212 HIS 212 190 190 HIS HIS B . n 
B 1 213 PHE 213 191 191 PHE PHE B . n 
B 1 214 VAL 214 192 192 VAL VAL B . n 
B 1 215 ASP 215 193 193 ASP ASP B . n 
B 1 216 HIS 216 194 194 HIS HIS B . n 
B 1 217 CYS 217 195 195 CYS CYS B . n 
B 1 218 ILE 218 196 196 ILE ILE B . n 
B 1 219 GLU 219 197 197 GLU GLU B . n 
B 1 220 ILE 220 198 198 ILE ILE B . n 
B 1 221 LEU 221 199 199 LEU LEU B . n 
B 1 222 SER 222 200 200 SER SER B . n 
B 1 223 HIS 223 201 201 HIS HIS B . n 
B 1 224 ASP 224 202 202 ASP ASP B . n 
B 1 225 LYS 225 203 203 LYS LYS B . n 
B 1 226 ASP 226 204 204 ASP ASP B . n 
B 1 227 TYR 227 205 205 TYR TYR B . n 
B 1 228 ASN 228 206 206 ASN ASN B . n 
B 1 229 LYS 229 207 207 LYS LYS B . n 
B 1 230 VAL 230 208 208 VAL VAL B . n 
B 1 231 LYS 231 209 209 LYS LYS B . n 
B 1 232 LEU 232 210 210 LEU LEU B . n 
B 1 233 TYR 233 211 211 TYR TYR B . n 
B 1 234 GLU 234 212 212 GLU GLU B . n 
B 1 235 HIS 235 213 213 HIS HIS B . n 
B 1 236 ALA 236 214 214 ALA ALA B . n 
B 1 237 VAL 237 215 215 VAL VAL B . n 
B 1 238 ALA 238 216 216 ALA ALA B . n 
B 1 239 HIS 239 217 217 HIS HIS B . n 
B 1 240 SER 240 218 218 SER SER B . n 
B 1 241 GLY 241 219 219 GLY GLY B . n 
B 1 242 LEU 242 220 ?   ?   ?   B . n 
B 1 243 PRO 243 221 ?   ?   ?   B . n 
B 1 244 ASP 244 222 ?   ?   ?   B . n 
B 1 245 ASN 245 223 ?   ?   ?   B . n 
B 1 246 ALA 246 224 ?   ?   ?   B . n 
B 1 247 ARG 247 225 ?   ?   ?   B . n 
B 1 248 ARG 248 226 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        5SQ 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   5SQ 
_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 DTT 1   301 301 DTT DTT B . 
D 3 HOH 1   301 318 HOH HOH A . 
D 3 HOH 2   302 132 HOH HOH A . 
D 3 HOH 3   303 314 HOH HOH A . 
D 3 HOH 4   304 411 HOH HOH A . 
D 3 HOH 5   305 5   HOH HOH A . 
D 3 HOH 6   306 207 HOH HOH A . 
D 3 HOH 7   307 4   HOH HOH A . 
D 3 HOH 8   308 122 HOH HOH A . 
D 3 HOH 9   309 185 HOH HOH A . 
D 3 HOH 10  310 204 HOH HOH A . 
D 3 HOH 11  311 422 HOH HOH A . 
D 3 HOH 12  312 305 HOH HOH A . 
D 3 HOH 13  313 362 HOH HOH A . 
D 3 HOH 14  314 290 HOH HOH A . 
D 3 HOH 15  315 316 HOH HOH A . 
D 3 HOH 16  316 117 HOH HOH A . 
D 3 HOH 17  317 253 HOH HOH A . 
D 3 HOH 18  318 63  HOH HOH A . 
D 3 HOH 19  319 66  HOH HOH A . 
D 3 HOH 20  320 283 HOH HOH A . 
D 3 HOH 21  321 14  HOH HOH A . 
D 3 HOH 22  322 81  HOH HOH A . 
D 3 HOH 23  323 212 HOH HOH A . 
D 3 HOH 24  324 23  HOH HOH A . 
D 3 HOH 25  325 134 HOH HOH A . 
D 3 HOH 26  326 163 HOH HOH A . 
D 3 HOH 27  327 109 HOH HOH A . 
D 3 HOH 28  328 125 HOH HOH A . 
D 3 HOH 29  329 28  HOH HOH A . 
D 3 HOH 30  330 42  HOH HOH A . 
D 3 HOH 31  331 36  HOH HOH A . 
D 3 HOH 32  332 323 HOH HOH A . 
D 3 HOH 33  333 111 HOH HOH A . 
D 3 HOH 34  334 414 HOH HOH A . 
D 3 HOH 35  335 413 HOH HOH A . 
D 3 HOH 36  336 57  HOH HOH A . 
D 3 HOH 37  337 306 HOH HOH A . 
D 3 HOH 38  338 9   HOH HOH A . 
D 3 HOH 39  339 56  HOH HOH A . 
D 3 HOH 40  340 231 HOH HOH A . 
D 3 HOH 41  341 79  HOH HOH A . 
D 3 HOH 42  342 101 HOH HOH A . 
D 3 HOH 43  343 11  HOH HOH A . 
D 3 HOH 44  344 131 HOH HOH A . 
D 3 HOH 45  345 191 HOH HOH A . 
D 3 HOH 46  346 218 HOH HOH A . 
D 3 HOH 47  347 60  HOH HOH A . 
D 3 HOH 48  348 22  HOH HOH A . 
D 3 HOH 49  349 29  HOH HOH A . 
D 3 HOH 50  350 390 HOH HOH A . 
D 3 HOH 51  351 47  HOH HOH A . 
D 3 HOH 52  352 338 HOH HOH A . 
D 3 HOH 53  353 189 HOH HOH A . 
D 3 HOH 54  354 104 HOH HOH A . 
D 3 HOH 55  355 100 HOH HOH A . 
D 3 HOH 56  356 202 HOH HOH A . 
D 3 HOH 57  357 181 HOH HOH A . 
D 3 HOH 58  358 91  HOH HOH A . 
D 3 HOH 59  359 236 HOH HOH A . 
D 3 HOH 60  360 347 HOH HOH A . 
D 3 HOH 61  361 27  HOH HOH A . 
D 3 HOH 62  362 46  HOH HOH A . 
D 3 HOH 63  363 282 HOH HOH A . 
D 3 HOH 64  364 8   HOH HOH A . 
D 3 HOH 65  365 150 HOH HOH A . 
D 3 HOH 66  366 18  HOH HOH A . 
D 3 HOH 67  367 144 HOH HOH A . 
D 3 HOH 68  368 2   HOH HOH A . 
D 3 HOH 69  369 135 HOH HOH A . 
D 3 HOH 70  370 26  HOH HOH A . 
D 3 HOH 71  371 77  HOH HOH A . 
D 3 HOH 72  372 256 HOH HOH A . 
D 3 HOH 73  373 216 HOH HOH A . 
D 3 HOH 74  374 195 HOH HOH A . 
D 3 HOH 75  375 106 HOH HOH A . 
D 3 HOH 76  376 33  HOH HOH A . 
D 3 HOH 77  377 35  HOH HOH A . 
D 3 HOH 78  378 7   HOH HOH A . 
D 3 HOH 79  379 382 HOH HOH A . 
D 3 HOH 80  380 365 HOH HOH A . 
D 3 HOH 81  381 261 HOH HOH A . 
D 3 HOH 82  382 85  HOH HOH A . 
D 3 HOH 83  383 374 HOH HOH A . 
D 3 HOH 84  384 246 HOH HOH A . 
D 3 HOH 85  385 208 HOH HOH A . 
D 3 HOH 86  386 59  HOH HOH A . 
D 3 HOH 87  387 307 HOH HOH A . 
D 3 HOH 88  388 348 HOH HOH A . 
D 3 HOH 89  389 431 HOH HOH A . 
D 3 HOH 90  390 93  HOH HOH A . 
D 3 HOH 91  391 78  HOH HOH A . 
D 3 HOH 92  392 238 HOH HOH A . 
D 3 HOH 93  393 242 HOH HOH A . 
D 3 HOH 94  394 67  HOH HOH A . 
D 3 HOH 95  395 127 HOH HOH A . 
D 3 HOH 96  396 397 HOH HOH A . 
D 3 HOH 97  397 82  HOH HOH A . 
D 3 HOH 98  398 151 HOH HOH A . 
D 3 HOH 99  399 169 HOH HOH A . 
D 3 HOH 100 400 369 HOH HOH A . 
D 3 HOH 101 401 39  HOH HOH A . 
D 3 HOH 102 402 19  HOH HOH A . 
D 3 HOH 103 403 159 HOH HOH A . 
D 3 HOH 104 404 373 HOH HOH A . 
D 3 HOH 105 405 32  HOH HOH A . 
D 3 HOH 106 406 248 HOH HOH A . 
D 3 HOH 107 407 73  HOH HOH A . 
D 3 HOH 108 408 214 HOH HOH A . 
D 3 HOH 109 409 1   HOH HOH A . 
D 3 HOH 110 410 429 HOH HOH A . 
D 3 HOH 111 411 234 HOH HOH A . 
D 3 HOH 112 412 58  HOH HOH A . 
D 3 HOH 113 413 71  HOH HOH A . 
D 3 HOH 114 414 34  HOH HOH A . 
D 3 HOH 115 415 427 HOH HOH A . 
D 3 HOH 116 416 43  HOH HOH A . 
D 3 HOH 117 417 388 HOH HOH A . 
D 3 HOH 118 418 355 HOH HOH A . 
D 3 HOH 119 419 408 HOH HOH A . 
D 3 HOH 120 420 297 HOH HOH A . 
D 3 HOH 121 421 107 HOH HOH A . 
D 3 HOH 122 422 298 HOH HOH A . 
D 3 HOH 123 423 13  HOH HOH A . 
D 3 HOH 124 424 260 HOH HOH A . 
D 3 HOH 125 425 400 HOH HOH A . 
D 3 HOH 126 426 137 HOH HOH A . 
D 3 HOH 127 427 356 HOH HOH A . 
D 3 HOH 128 428 251 HOH HOH A . 
D 3 HOH 129 429 178 HOH HOH A . 
D 3 HOH 130 430 105 HOH HOH A . 
D 3 HOH 131 431 406 HOH HOH A . 
D 3 HOH 132 432 176 HOH HOH A . 
D 3 HOH 133 433 25  HOH HOH A . 
D 3 HOH 134 434 54  HOH HOH A . 
D 3 HOH 135 435 372 HOH HOH A . 
D 3 HOH 136 436 319 HOH HOH A . 
D 3 HOH 137 437 209 HOH HOH A . 
D 3 HOH 138 438 287 HOH HOH A . 
D 3 HOH 139 439 367 HOH HOH A . 
D 3 HOH 140 440 364 HOH HOH A . 
D 3 HOH 141 441 310 HOH HOH A . 
D 3 HOH 142 442 228 HOH HOH A . 
D 3 HOH 143 443 349 HOH HOH A . 
D 3 HOH 144 444 392 HOH HOH A . 
D 3 HOH 145 445 387 HOH HOH A . 
D 3 HOH 146 446 267 HOH HOH A . 
D 3 HOH 147 447 410 HOH HOH A . 
D 3 HOH 148 448 420 HOH HOH A . 
D 3 HOH 149 449 340 HOH HOH A . 
D 3 HOH 150 450 221 HOH HOH A . 
D 3 HOH 151 451 389 HOH HOH A . 
D 3 HOH 152 452 220 HOH HOH A . 
D 3 HOH 153 453 393 HOH HOH A . 
D 3 HOH 154 454 154 HOH HOH A . 
D 3 HOH 155 455 331 HOH HOH A . 
D 3 HOH 156 456 263 HOH HOH A . 
D 3 HOH 157 457 311 HOH HOH A . 
D 3 HOH 158 458 325 HOH HOH A . 
D 3 HOH 159 459 173 HOH HOH A . 
D 3 HOH 160 460 293 HOH HOH A . 
D 3 HOH 161 461 300 HOH HOH A . 
D 3 HOH 162 462 423 HOH HOH A . 
D 3 HOH 163 463 312 HOH HOH A . 
D 3 HOH 164 464 103 HOH HOH A . 
D 3 HOH 165 465 240 HOH HOH A . 
D 3 HOH 166 466 405 HOH HOH A . 
D 3 HOH 167 467 391 HOH HOH A . 
D 3 HOH 168 468 258 HOH HOH A . 
D 3 HOH 169 469 271 HOH HOH A . 
D 3 HOH 170 470 326 HOH HOH A . 
D 3 HOH 171 471 359 HOH HOH A . 
D 3 HOH 172 472 320 HOH HOH A . 
D 3 HOH 173 473 417 HOH HOH A . 
D 3 HOH 174 474 250 HOH HOH A . 
D 3 HOH 175 475 203 HOH HOH A . 
D 3 HOH 176 476 308 HOH HOH A . 
D 3 HOH 177 477 289 HOH HOH A . 
D 3 HOH 178 478 339 HOH HOH A . 
D 3 HOH 179 479 140 HOH HOH A . 
D 3 HOH 180 480 303 HOH HOH A . 
D 3 HOH 181 481 164 HOH HOH A . 
D 3 HOH 182 482 313 HOH HOH A . 
D 3 HOH 183 483 363 HOH HOH A . 
D 3 HOH 184 484 375 HOH HOH A . 
D 3 HOH 185 485 295 HOH HOH A . 
D 3 HOH 186 486 334 HOH HOH A . 
D 3 HOH 187 487 249 HOH HOH A . 
D 3 HOH 188 488 87  HOH HOH A . 
D 3 HOH 189 489 394 HOH HOH A . 
D 3 HOH 190 490 412 HOH HOH A . 
D 3 HOH 191 491 343 HOH HOH A . 
D 3 HOH 192 492 399 HOH HOH A . 
D 3 HOH 193 493 344 HOH HOH A . 
D 3 HOH 194 494 224 HOH HOH A . 
D 3 HOH 195 495 336 HOH HOH A . 
D 3 HOH 196 496 285 HOH HOH A . 
D 3 HOH 197 497 276 HOH HOH A . 
D 3 HOH 198 498 190 HOH HOH A . 
D 3 HOH 199 499 286 HOH HOH A . 
D 3 HOH 200 500 278 HOH HOH A . 
D 3 HOH 201 501 227 HOH HOH A . 
D 3 HOH 202 502 376 HOH HOH A . 
D 3 HOH 203 503 317 HOH HOH A . 
D 3 HOH 204 504 156 HOH HOH A . 
D 3 HOH 205 505 193 HOH HOH A . 
D 3 HOH 206 506 327 HOH HOH A . 
D 3 HOH 207 507 419 HOH HOH A . 
D 3 HOH 208 508 328 HOH HOH A . 
D 3 HOH 209 509 229 HOH HOH A . 
D 3 HOH 210 510 335 HOH HOH A . 
D 3 HOH 211 511 197 HOH HOH A . 
D 3 HOH 212 512 426 HOH HOH A . 
D 3 HOH 213 513 418 HOH HOH A . 
D 3 HOH 214 514 179 HOH HOH A . 
D 3 HOH 215 515 383 HOH HOH A . 
D 3 HOH 216 516 421 HOH HOH A . 
D 3 HOH 217 517 153 HOH HOH A . 
D 3 HOH 218 518 280 HOH HOH A . 
D 3 HOH 219 519 333 HOH HOH A . 
D 3 HOH 220 520 299 HOH HOH A . 
D 3 HOH 221 521 395 HOH HOH A . 
D 3 HOH 222 522 377 HOH HOH A . 
D 3 HOH 223 523 381 HOH HOH A . 
E 3 HOH 1   401 269 HOH HOH B . 
E 3 HOH 2   402 198 HOH HOH B . 
E 3 HOH 3   403 386 HOH HOH B . 
E 3 HOH 4   404 120 HOH HOH B . 
E 3 HOH 5   405 329 HOH HOH B . 
E 3 HOH 6   406 162 HOH HOH B . 
E 3 HOH 7   407 3   HOH HOH B . 
E 3 HOH 8   408 16  HOH HOH B . 
E 3 HOH 9   409 252 HOH HOH B . 
E 3 HOH 10  410 155 HOH HOH B . 
E 3 HOH 11  411 199 HOH HOH B . 
E 3 HOH 12  412 130 HOH HOH B . 
E 3 HOH 13  413 217 HOH HOH B . 
E 3 HOH 14  414 30  HOH HOH B . 
E 3 HOH 15  415 92  HOH HOH B . 
E 3 HOH 16  416 113 HOH HOH B . 
E 3 HOH 17  417 232 HOH HOH B . 
E 3 HOH 18  418 302 HOH HOH B . 
E 3 HOH 19  419 84  HOH HOH B . 
E 3 HOH 20  420 121 HOH HOH B . 
E 3 HOH 21  421 53  HOH HOH B . 
E 3 HOH 22  422 291 HOH HOH B . 
E 3 HOH 23  423 275 HOH HOH B . 
E 3 HOH 24  424 114 HOH HOH B . 
E 3 HOH 25  425 168 HOH HOH B . 
E 3 HOH 26  426 38  HOH HOH B . 
E 3 HOH 27  427 170 HOH HOH B . 
E 3 HOH 28  428 239 HOH HOH B . 
E 3 HOH 29  429 309 HOH HOH B . 
E 3 HOH 30  430 184 HOH HOH B . 
E 3 HOH 31  431 44  HOH HOH B . 
E 3 HOH 32  432 215 HOH HOH B . 
E 3 HOH 33  433 88  HOH HOH B . 
E 3 HOH 34  434 83  HOH HOH B . 
E 3 HOH 35  435 254 HOH HOH B . 
E 3 HOH 36  436 64  HOH HOH B . 
E 3 HOH 37  437 200 HOH HOH B . 
E 3 HOH 38  438 268 HOH HOH B . 
E 3 HOH 39  439 330 HOH HOH B . 
E 3 HOH 40  440 171 HOH HOH B . 
E 3 HOH 41  441 270 HOH HOH B . 
E 3 HOH 42  442 49  HOH HOH B . 
E 3 HOH 43  443 226 HOH HOH B . 
E 3 HOH 44  444 149 HOH HOH B . 
E 3 HOH 45  445 31  HOH HOH B . 
E 3 HOH 46  446 124 HOH HOH B . 
E 3 HOH 47  447 10  HOH HOH B . 
E 3 HOH 48  448 167 HOH HOH B . 
E 3 HOH 49  449 158 HOH HOH B . 
E 3 HOH 50  450 17  HOH HOH B . 
E 3 HOH 51  451 118 HOH HOH B . 
E 3 HOH 52  452 211 HOH HOH B . 
E 3 HOH 53  453 116 HOH HOH B . 
E 3 HOH 54  454 141 HOH HOH B . 
E 3 HOH 55  455 129 HOH HOH B . 
E 3 HOH 56  456 21  HOH HOH B . 
E 3 HOH 57  457 61  HOH HOH B . 
E 3 HOH 58  458 24  HOH HOH B . 
E 3 HOH 59  459 201 HOH HOH B . 
E 3 HOH 60  460 123 HOH HOH B . 
E 3 HOH 61  461 48  HOH HOH B . 
E 3 HOH 62  462 379 HOH HOH B . 
E 3 HOH 63  463 273 HOH HOH B . 
E 3 HOH 64  464 86  HOH HOH B . 
E 3 HOH 65  465 45  HOH HOH B . 
E 3 HOH 66  466 20  HOH HOH B . 
E 3 HOH 67  467 97  HOH HOH B . 
E 3 HOH 68  468 75  HOH HOH B . 
E 3 HOH 69  469 62  HOH HOH B . 
E 3 HOH 70  470 172 HOH HOH B . 
E 3 HOH 71  471 230 HOH HOH B . 
E 3 HOH 72  472 161 HOH HOH B . 
E 3 HOH 73  473 257 HOH HOH B . 
E 3 HOH 74  474 281 HOH HOH B . 
E 3 HOH 75  475 279 HOH HOH B . 
E 3 HOH 76  476 143 HOH HOH B . 
E 3 HOH 77  477 12  HOH HOH B . 
E 3 HOH 78  478 102 HOH HOH B . 
E 3 HOH 79  479 112 HOH HOH B . 
E 3 HOH 80  480 139 HOH HOH B . 
E 3 HOH 81  481 41  HOH HOH B . 
E 3 HOH 82  482 68  HOH HOH B . 
E 3 HOH 83  483 288 HOH HOH B . 
E 3 HOH 84  484 192 HOH HOH B . 
E 3 HOH 85  485 15  HOH HOH B . 
E 3 HOH 86  486 206 HOH HOH B . 
E 3 HOH 87  487 262 HOH HOH B . 
E 3 HOH 88  488 378 HOH HOH B . 
E 3 HOH 89  489 51  HOH HOH B . 
E 3 HOH 90  490 244 HOH HOH B . 
E 3 HOH 91  491 223 HOH HOH B . 
E 3 HOH 92  492 115 HOH HOH B . 
E 3 HOH 93  493 401 HOH HOH B . 
E 3 HOH 94  494 196 HOH HOH B . 
E 3 HOH 95  495 187 HOH HOH B . 
E 3 HOH 96  496 292 HOH HOH B . 
E 3 HOH 97  497 284 HOH HOH B . 
E 3 HOH 98  498 95  HOH HOH B . 
E 3 HOH 99  499 265 HOH HOH B . 
E 3 HOH 100 500 69  HOH HOH B . 
E 3 HOH 101 501 213 HOH HOH B . 
E 3 HOH 102 502 52  HOH HOH B . 
E 3 HOH 103 503 138 HOH HOH B . 
E 3 HOH 104 504 166 HOH HOH B . 
E 3 HOH 105 505 175 HOH HOH B . 
E 3 HOH 106 506 40  HOH HOH B . 
E 3 HOH 107 507 354 HOH HOH B . 
E 3 HOH 108 508 108 HOH HOH B . 
E 3 HOH 109 509 65  HOH HOH B . 
E 3 HOH 110 510 165 HOH HOH B . 
E 3 HOH 111 511 94  HOH HOH B . 
E 3 HOH 112 512 152 HOH HOH B . 
E 3 HOH 113 513 371 HOH HOH B . 
E 3 HOH 114 514 37  HOH HOH B . 
E 3 HOH 115 515 99  HOH HOH B . 
E 3 HOH 116 516 415 HOH HOH B . 
E 3 HOH 117 517 89  HOH HOH B . 
E 3 HOH 118 518 6   HOH HOH B . 
E 3 HOH 119 519 370 HOH HOH B . 
E 3 HOH 120 520 247 HOH HOH B . 
E 3 HOH 121 521 80  HOH HOH B . 
E 3 HOH 122 522 277 HOH HOH B . 
E 3 HOH 123 523 430 HOH HOH B . 
E 3 HOH 124 524 119 HOH HOH B . 
E 3 HOH 125 525 110 HOH HOH B . 
E 3 HOH 126 526 133 HOH HOH B . 
E 3 HOH 127 527 274 HOH HOH B . 
E 3 HOH 128 528 96  HOH HOH B . 
E 3 HOH 129 529 259 HOH HOH B . 
E 3 HOH 130 530 183 HOH HOH B . 
E 3 HOH 131 531 425 HOH HOH B . 
E 3 HOH 132 532 55  HOH HOH B . 
E 3 HOH 133 533 361 HOH HOH B . 
E 3 HOH 134 534 126 HOH HOH B . 
E 3 HOH 135 535 90  HOH HOH B . 
E 3 HOH 136 536 186 HOH HOH B . 
E 3 HOH 137 537 409 HOH HOH B . 
E 3 HOH 138 538 70  HOH HOH B . 
E 3 HOH 139 539 241 HOH HOH B . 
E 3 HOH 140 540 72  HOH HOH B . 
E 3 HOH 141 541 301 HOH HOH B . 
E 3 HOH 142 542 148 HOH HOH B . 
E 3 HOH 143 543 407 HOH HOH B . 
E 3 HOH 144 544 136 HOH HOH B . 
E 3 HOH 145 545 210 HOH HOH B . 
E 3 HOH 146 546 322 HOH HOH B . 
E 3 HOH 147 547 352 HOH HOH B . 
E 3 HOH 148 548 225 HOH HOH B . 
E 3 HOH 149 549 147 HOH HOH B . 
E 3 HOH 150 550 98  HOH HOH B . 
E 3 HOH 151 551 235 HOH HOH B . 
E 3 HOH 152 552 205 HOH HOH B . 
E 3 HOH 153 553 324 HOH HOH B . 
E 3 HOH 154 554 157 HOH HOH B . 
E 3 HOH 155 555 360 HOH HOH B . 
E 3 HOH 156 556 296 HOH HOH B . 
E 3 HOH 157 557 174 HOH HOH B . 
E 3 HOH 158 558 146 HOH HOH B . 
E 3 HOH 159 559 357 HOH HOH B . 
E 3 HOH 160 560 428 HOH HOH B . 
E 3 HOH 161 561 188 HOH HOH B . 
E 3 HOH 162 562 294 HOH HOH B . 
E 3 HOH 163 563 76  HOH HOH B . 
E 3 HOH 164 564 341 HOH HOH B . 
E 3 HOH 165 565 353 HOH HOH B . 
E 3 HOH 166 566 342 HOH HOH B . 
E 3 HOH 167 567 266 HOH HOH B . 
E 3 HOH 168 568 255 HOH HOH B . 
E 3 HOH 169 569 219 HOH HOH B . 
E 3 HOH 170 570 345 HOH HOH B . 
E 3 HOH 171 571 396 HOH HOH B . 
E 3 HOH 172 572 424 HOH HOH B . 
E 3 HOH 173 573 380 HOH HOH B . 
E 3 HOH 174 574 177 HOH HOH B . 
E 3 HOH 175 575 403 HOH HOH B . 
E 3 HOH 176 576 304 HOH HOH B . 
E 3 HOH 177 577 180 HOH HOH B . 
E 3 HOH 178 578 351 HOH HOH B . 
E 3 HOH 179 579 160 HOH HOH B . 
E 3 HOH 180 580 243 HOH HOH B . 
E 3 HOH 181 581 222 HOH HOH B . 
E 3 HOH 182 582 321 HOH HOH B . 
E 3 HOH 183 583 74  HOH HOH B . 
E 3 HOH 184 584 50  HOH HOH B . 
E 3 HOH 185 585 384 HOH HOH B . 
E 3 HOH 186 586 402 HOH HOH B . 
E 3 HOH 187 587 145 HOH HOH B . 
E 3 HOH 188 588 237 HOH HOH B . 
E 3 HOH 189 589 233 HOH HOH B . 
E 3 HOH 190 590 346 HOH HOH B . 
E 3 HOH 191 591 128 HOH HOH B . 
E 3 HOH 192 592 337 HOH HOH B . 
E 3 HOH 193 593 368 HOH HOH B . 
E 3 HOH 194 594 194 HOH HOH B . 
E 3 HOH 195 595 416 HOH HOH B . 
E 3 HOH 196 596 366 HOH HOH B . 
E 3 HOH 197 597 358 HOH HOH B . 
E 3 HOH 198 598 398 HOH HOH B . 
E 3 HOH 199 599 272 HOH HOH B . 
E 3 HOH 200 600 264 HOH HOH B . 
E 3 HOH 201 601 404 HOH HOH B . 
E 3 HOH 202 602 182 HOH HOH B . 
E 3 HOH 203 603 350 HOH HOH B . 
E 3 HOH 204 604 245 HOH HOH B . 
E 3 HOH 205 605 315 HOH HOH B . 
E 3 HOH 206 606 332 HOH HOH B . 
E 3 HOH 207 607 142 HOH HOH B . 
E 3 HOH 208 608 385 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       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? autoPROC ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   101.93 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9J11 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.357 
_cell.length_a_esd                 ? 
_cell.length_b                     82.392 
_cell.length_b_esd                 ? 
_cell.length_c                     61.775 
_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                         9J11 
_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                   9J11 
_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             2.24 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          45.09 
_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, SITTING DROP' 
_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    '0.2 M Ammonium acetate, 0.1 M Sodium acetate trihydrate, pH 6.0,  30% (w/v) PEG 4000' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-10-04 
_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   0.97853 
_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                        'SSRF BEAMLINE BL18U1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97853 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL18U1 
_diffrn_source.pdbx_synchrotron_site       SSRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9J11 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.85 
_reflns.d_resolution_low                               48.73 
_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                                     43073 
_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                           100 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.8 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          12.8 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_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                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_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                                    1.85 
_reflns_shell.d_res_low                                     1.95 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             6286 
_reflns_shell.percent_possible_obs                          ? 
_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                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.842 
_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                                  ? 
_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]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_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                                 9J11 
_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                            1.85 
_refine.ls_d_res_low                             28.64 
_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                     41044 
_refine.ls_number_reflns_R_free                  1903 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.33 
_refine.ls_percent_reflns_R_free                 4.64 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1548 
_refine.ls_R_factor_R_free                       0.1840 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1533 
_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                    'FLAT BULK SOLVENT MODEL' 
_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                          0.03 
_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               NONE 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      5OOZ 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_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                 17.84 
_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                             ? 
_refine.overall_SU_ML                            0.14 
_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                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.85 
_refine_hist.d_res_low                        28.64 
_refine_hist.number_atoms_solvent             431 
_refine_hist.number_atoms_total               3931 
_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        3500 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         0 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008 ? 3611 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.462 ? 4867 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 9.436 ? 483  ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.064 ? 493  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.009 ? 631  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_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 
_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 
_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 
'X-RAY DIFFRACTION' 1.85 1.90  . . 125 2522 86.00  . . . . 0.1976 . . . . . . . . . . . 0.2502 
'X-RAY DIFFRACTION' 1.90 1.95  . . 123 2622 89.00  . . . . 0.1895 . . . . . . . . . . . 0.2044 
'X-RAY DIFFRACTION' 1.95 2.00  . . 122 2640 91.00  . . . . 0.1695 . . . . . . . . . . . 0.2131 
'X-RAY DIFFRACTION' 2.00 2.07  . . 134 2723 93.00  . . . . 0.1636 . . . . . . . . . . . 0.1910 
'X-RAY DIFFRACTION' 2.07 2.14  . . 133 2746 94.00  . . . . 0.1610 . . . . . . . . . . . 0.2026 
'X-RAY DIFFRACTION' 2.14 2.23  . . 135 2782 95.00  . . . . 0.1510 . . . . . . . . . . . 0.1998 
'X-RAY DIFFRACTION' 2.23 2.33  . . 136 2801 96.00  . . . . 0.1596 . . . . . . . . . . . 0.1988 
'X-RAY DIFFRACTION' 2.33 2.45  . . 141 2813 97.00  . . . . 0.1623 . . . . . . . . . . . 0.2113 
'X-RAY DIFFRACTION' 2.45 2.61  . . 140 2869 98.00  . . . . 0.1567 . . . . . . . . . . . 0.1830 
'X-RAY DIFFRACTION' 2.61 2.81  . . 141 2877 98.00  . . . . 0.1481 . . . . . . . . . . . 0.1605 
'X-RAY DIFFRACTION' 2.81 3.09  . . 142 2904 99.00  . . . . 0.1476 . . . . . . . . . . . 0.1939 
'X-RAY DIFFRACTION' 3.09 3.54  . . 142 2913 99.00  . . . . 0.1395 . . . . . . . . . . . 0.1923 
'X-RAY DIFFRACTION' 3.54 4.45  . . 143 2942 100.00 . . . . 0.1341 . . . . . . . . . . . 0.1453 
'X-RAY DIFFRACTION' 4.45 28.64 . . 146 2987 100.00 . . . . 0.1635 . . . . . . . . . . . 0.1810 
# 
_struct.entry_id                     9J11 
_struct.title                        'Structure of mEos3.2 in the green fluorescent state' 
_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        9J11 
_struct_keywords.text            'Green-to-red photoconvertible fluorescent protein, FLUORESCENT PROTEIN' 
_struct_keywords.pdbx_keywords   'FLUORESCENT PROTEIN' 
# 
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 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    Q5S6Z9_LOBHE 
_struct_ref.pdbx_db_accession          Q5S6Z9 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MSAIKPDMKINLRMEGNVNGHHFVIDGDGTGKPFEGKQSMDLEVKEGGPLPFAFDILTTAFHYGNRVFAEYPDHIQDYFK
QSFPKGYSWERSLTFEDGGICIARNDITMEGDTFYNKVRFHGVNFPANGPVMQKKTLKWEPSTEKMYVRDGVLTGDITMA
LLLEGNAHYRCDFRTTYKAKEKGVKLPGYHFVDHCIEILSHDKDYNKVKLYEHAVAHSGLPDNARR
;
_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 9J11 A 25 ? 248 ? Q5S6Z9 1 ? 226 ? 1 226 
2 1 9J11 B 25 ? 248 ? Q5S6Z9 1 ? 226 ? 1 226 
# 
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 9J11 MET A 1   ? UNP Q5S6Z9 ?   ?   'initiating methionine' -23 1  
1 9J11 GLY A 2   ? UNP Q5S6Z9 ?   ?   'expression tag'        -22 2  
1 9J11 SER A 3   ? UNP Q5S6Z9 ?   ?   'expression tag'        -21 3  
1 9J11 SER A 4   ? UNP Q5S6Z9 ?   ?   'expression tag'        -20 4  
1 9J11 HIS A 5   ? UNP Q5S6Z9 ?   ?   'expression tag'        -19 5  
1 9J11 HIS A 6   ? UNP Q5S6Z9 ?   ?   'expression tag'        -18 6  
1 9J11 HIS A 7   ? UNP Q5S6Z9 ?   ?   'expression tag'        -17 7  
1 9J11 HIS A 8   ? UNP Q5S6Z9 ?   ?   'expression tag'        -16 8  
1 9J11 HIS A 9   ? UNP Q5S6Z9 ?   ?   'expression tag'        -15 9  
1 9J11 HIS A 10  ? UNP Q5S6Z9 ?   ?   'expression tag'        -14 10 
1 9J11 SER A 11  ? UNP Q5S6Z9 ?   ?   'expression tag'        -13 11 
1 9J11 GLN A 12  ? UNP Q5S6Z9 ?   ?   'expression tag'        -12 12 
1 9J11 ASP A 13  ? UNP Q5S6Z9 ?   ?   'expression tag'        -11 13 
1 9J11 PRO A 14  ? UNP Q5S6Z9 ?   ?   'expression tag'        -10 14 
1 9J11 LEU A 15  ? UNP Q5S6Z9 ?   ?   'expression tag'        -9  15 
1 9J11 GLU A 16  ? UNP Q5S6Z9 ?   ?   'expression tag'        -8  16 
1 9J11 VAL A 17  ? UNP Q5S6Z9 ?   ?   'expression tag'        -7  17 
1 9J11 LEU A 18  ? UNP Q5S6Z9 ?   ?   'expression tag'        -6  18 
1 9J11 PHE A 19  ? UNP Q5S6Z9 ?   ?   'expression tag'        -5  19 
1 9J11 GLN A 20  ? UNP Q5S6Z9 ?   ?   'expression tag'        -4  20 
1 9J11 GLY A 21  ? UNP Q5S6Z9 ?   ?   'expression tag'        -3  21 
1 9J11 PRO A 22  ? UNP Q5S6Z9 ?   ?   'expression tag'        -2  22 
1 9J11 GLU A 23  ? UNP Q5S6Z9 ?   ?   'expression tag'        -1  23 
1 9J11 PHE A 24  ? UNP Q5S6Z9 ?   ?   'expression tag'        0   24 
1 9J11 LYS A 35  ? UNP Q5S6Z9 ASN 11  'engineered mutation'   11  25 
1 9J11 5SQ A 86  ? UNP Q5S6Z9 HIS 62  chromophore             64  26 
1 9J11 5SQ A 86  ? UNP Q5S6Z9 TYR 63  chromophore             64  27 
1 9J11 5SQ A 86  ? UNP Q5S6Z9 GLY 64  chromophore             64  28 
1 9J11 LYS A 92  ? UNP Q5S6Z9 GLU 70  'engineered mutation'   70  29 
1 9J11 ASN A 96  ? UNP Q5S6Z9 HIS 74  'engineered mutation'   74  30 
1 9J11 ASN A 124 ? UNP Q5S6Z9 ILE 102 'engineered mutation'   102 31 
1 9J11 TYR A 143 ? UNP Q5S6Z9 HIS 121 'engineered mutation'   121 32 
1 9J11 THR A 145 ? UNP Q5S6Z9 VAL 123 'engineered mutation'   123 33 
1 9J11 GLU A 180 ? UNP Q5S6Z9 THR 158 'engineered mutation'   158 34 
1 9J11 ALA A 211 ? UNP Q5S6Z9 TYR 189 'engineered mutation'   189 35 
2 9J11 MET B 1   ? UNP Q5S6Z9 ?   ?   'initiating methionine' -23 36 
2 9J11 GLY B 2   ? UNP Q5S6Z9 ?   ?   'expression tag'        -22 37 
2 9J11 SER B 3   ? UNP Q5S6Z9 ?   ?   'expression tag'        -21 38 
2 9J11 SER B 4   ? UNP Q5S6Z9 ?   ?   'expression tag'        -20 39 
2 9J11 HIS B 5   ? UNP Q5S6Z9 ?   ?   'expression tag'        -19 40 
2 9J11 HIS B 6   ? UNP Q5S6Z9 ?   ?   'expression tag'        -18 41 
2 9J11 HIS B 7   ? UNP Q5S6Z9 ?   ?   'expression tag'        -17 42 
2 9J11 HIS B 8   ? UNP Q5S6Z9 ?   ?   'expression tag'        -16 43 
2 9J11 HIS B 9   ? UNP Q5S6Z9 ?   ?   'expression tag'        -15 44 
2 9J11 HIS B 10  ? UNP Q5S6Z9 ?   ?   'expression tag'        -14 45 
2 9J11 SER B 11  ? UNP Q5S6Z9 ?   ?   'expression tag'        -13 46 
2 9J11 GLN B 12  ? UNP Q5S6Z9 ?   ?   'expression tag'        -12 47 
2 9J11 ASP B 13  ? UNP Q5S6Z9 ?   ?   'expression tag'        -11 48 
2 9J11 PRO B 14  ? UNP Q5S6Z9 ?   ?   'expression tag'        -10 49 
2 9J11 LEU B 15  ? UNP Q5S6Z9 ?   ?   'expression tag'        -9  50 
2 9J11 GLU B 16  ? UNP Q5S6Z9 ?   ?   'expression tag'        -8  51 
2 9J11 VAL B 17  ? UNP Q5S6Z9 ?   ?   'expression tag'        -7  52 
2 9J11 LEU B 18  ? UNP Q5S6Z9 ?   ?   'expression tag'        -6  53 
2 9J11 PHE B 19  ? UNP Q5S6Z9 ?   ?   'expression tag'        -5  54 
2 9J11 GLN B 20  ? UNP Q5S6Z9 ?   ?   'expression tag'        -4  55 
2 9J11 GLY B 21  ? UNP Q5S6Z9 ?   ?   'expression tag'        -3  56 
2 9J11 PRO B 22  ? UNP Q5S6Z9 ?   ?   'expression tag'        -2  57 
2 9J11 GLU B 23  ? UNP Q5S6Z9 ?   ?   'expression tag'        -1  58 
2 9J11 PHE B 24  ? UNP Q5S6Z9 ?   ?   'expression tag'        0   59 
2 9J11 LYS B 35  ? UNP Q5S6Z9 ASN 11  'engineered mutation'   11  60 
2 9J11 5SQ B 86  ? UNP Q5S6Z9 HIS 62  chromophore             64  61 
2 9J11 5SQ B 86  ? UNP Q5S6Z9 TYR 63  chromophore             64  62 
2 9J11 5SQ B 86  ? UNP Q5S6Z9 GLY 64  chromophore             64  63 
2 9J11 LYS B 92  ? UNP Q5S6Z9 GLU 70  'engineered mutation'   70  64 
2 9J11 ASN B 96  ? UNP Q5S6Z9 HIS 74  'engineered mutation'   74  65 
2 9J11 ASN B 124 ? UNP Q5S6Z9 ILE 102 'engineered mutation'   102 66 
2 9J11 TYR B 143 ? UNP Q5S6Z9 HIS 121 'engineered mutation'   121 67 
2 9J11 THR B 145 ? UNP Q5S6Z9 VAL 123 'engineered mutation'   123 68 
2 9J11 GLU B 180 ? UNP Q5S6Z9 THR 158 'engineered mutation'   158 69 
2 9J11 ALA B 211 ? UNP Q5S6Z9 TYR 189 'engineered mutation'   189 70 
# 
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,D   
2 1 B,C,E 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_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 PRO A 57  ? GLU A 59  ? PRO A 33 GLU A 35 5 ? 3 
HELX_P HELX_P2 AA2 ALA A 77  ? PHE A 85  ? ALA A 53 PHE A 61 5 ? 9 
HELX_P HELX_P3 AA3 PHE A 101 ? PHE A 105 ? PHE A 79 PHE A 83 5 ? 5 
HELX_P HELX_P4 AA4 ALA B 77  ? PHE B 85  ? ALA B 53 PHE B 61 5 ? 9 
HELX_P HELX_P5 AA5 PHE B 101 ? PHE B 105 ? PHE B 79 PHE B 83 5 ? 5 
# 
_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 both ? A PHE 85  C  ? ? ? 1_555 A 5SQ 86 N1 ? ? A PHE 61  A 5SQ 64  1_555 ? ? ? ? ? ? ? 1.335 ? ? 
covale2 covale both ? A 5SQ 86  C3 ? ? ? 1_555 A ASN 87 N  ? ? A 5SQ 64  A ASN 65  1_555 ? ? ? ? ? ? ? 1.324 ? ? 
covale3 covale none ? A CYS 217 SG ? ? ? 1_555 C DTT .  S1 ? ? A CYS 195 B DTT 301 1_555 ? ? ? ? ? ? ? 2.013 ? ? 
covale4 covale both ? B PHE 85  C  ? ? ? 1_555 B 5SQ 86 N1 ? ? B PHE 61  B 5SQ 64  1_555 ? ? ? ? ? ? ? 1.340 ? ? 
covale5 covale both ? B 5SQ 86  C3 ? ? ? 1_555 B ASN 87 N  ? ? B 5SQ 64  B ASN 65  1_555 ? ? ? ? ? ? ? 1.328 ? ? 
covale6 covale none ? B CYS 217 SG ? ? ? 1_555 C DTT .  S4 ? ? B CYS 195 B DTT 301 1_555 ? ? ? ? ? ? ? 2.007 ? ? 
# 
_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 5SQ A 86 ? .   . .   . 5SQ A 64  ? 1_555 .   . .   . .     .  .  'HIS, TYR, GLY' 1 5SQ None Chromophore/chromophore-like 
2 5SQ B 86 ? .   . .   . 5SQ B 64  ? 1_555 .   . .   . .     .  .  'HIS, TYR, GLY' 1 5SQ None Chromophore/chromophore-like 
3 DTT C .  ? CYS A 217 ? DTT B 301 ? 1_555 CYS A 195 ? 1_555 S1 SG CYS             1 DTT None Crosslinker                  
4 DTT C .  ? CYS B 217 ? DTT B 301 ? 1_555 CYS B 195 ? 1_555 S4 SG CYS             2 DTT None Crosslinker                  
# 
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 GLY 72  A . ? GLY 48 A PRO 73  A ? PRO 49 A 1 -2.07 
2 PHE 105 A . ? PHE 83 A PRO 106 A ? PRO 84 A 1 11.14 
3 GLY 72  B . ? GLY 48 B PRO 73  B ? PRO 49 B 1 -4.09 
4 PHE 105 B . ? PHE 83 B PRO 106 B ? PRO 84 B 1 11.30 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 13 ? 
AA2 ? 13 ? 
# 
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  ? anti-parallel 
AA1 2  3  ? anti-parallel 
AA1 3  4  ? anti-parallel 
AA1 4  5  ? anti-parallel 
AA1 5  6  ? anti-parallel 
AA1 6  7  ? parallel      
AA1 7  8  ? anti-parallel 
AA1 8  9  ? anti-parallel 
AA1 9  10 ? anti-parallel 
AA1 10 11 ? anti-parallel 
AA1 11 12 ? anti-parallel 
AA1 12 13 ? anti-parallel 
AA2 1  2  ? anti-parallel 
AA2 2  3  ? anti-parallel 
AA2 3  4  ? anti-parallel 
AA2 4  5  ? anti-parallel 
AA2 5  6  ? anti-parallel 
AA2 6  7  ? parallel      
AA2 7  8  ? anti-parallel 
AA2 8  9  ? anti-parallel 
AA2 9  10 ? anti-parallel 
AA2 10 11 ? anti-parallel 
AA2 11 12 ? anti-parallel 
AA2 12 13 ? 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  THR A 158 ? TRP A 161 ? THR A 136 TRP A 139 
AA1 2  VAL A 174 ? LEU A 185 ? VAL A 152 LEU A 163 
AA1 3  HIS A 190 ? ALA A 201 ? HIS A 168 ALA A 179 
AA1 4  TYR A 109 ? PHE A 117 ? TYR A 87  PHE A 95  
AA1 5  ILE A 122 ? GLU A 132 ? ILE A 100 GLU A 110 
AA1 6  THR A 135 ? THR A 145 ? THR A 113 THR A 123 
AA1 7  MET A 32  ? VAL A 42  ? MET A 8   VAL A 18  
AA1 8  HIS A 45  ? LYS A 56  ? HIS A 21  LYS A 32  
AA1 9  LYS A 61  ? GLU A 70  ? LYS A 37  GLU A 46  
AA1 10 LYS A 229 ? HIS A 239 ? LYS A 207 HIS A 217 
AA1 11 HIS A 212 ? HIS A 223 ? HIS A 190 HIS A 201 
AA1 12 SER A 164 ? ARG A 171 ? SER A 142 ARG A 149 
AA1 13 VAL A 174 ? LEU A 185 ? VAL A 152 LEU A 163 
AA2 1  THR B 158 ? TRP B 161 ? THR B 136 TRP B 139 
AA2 2  VAL B 174 ? LEU B 185 ? VAL B 152 LEU B 163 
AA2 3  HIS B 190 ? ALA B 201 ? HIS B 168 ALA B 179 
AA2 4  TYR B 109 ? PHE B 117 ? TYR B 87  PHE B 95  
AA2 5  ILE B 122 ? GLU B 132 ? ILE B 100 GLU B 110 
AA2 6  THR B 135 ? THR B 145 ? THR B 113 THR B 123 
AA2 7  MET B 32  ? VAL B 42  ? MET B 8   VAL B 18  
AA2 8  HIS B 45  ? LYS B 56  ? HIS B 21  LYS B 32  
AA2 9  LYS B 61  ? GLU B 70  ? LYS B 37  GLU B 46  
AA2 10 LYS B 229 ? HIS B 239 ? LYS B 207 HIS B 217 
AA2 11 HIS B 212 ? HIS B 223 ? HIS B 190 HIS B 201 
AA2 12 SER B 164 ? ARG B 171 ? SER B 142 ARG B 149 
AA2 13 VAL B 174 ? LEU B 185 ? VAL B 152 LEU B 163 
# 
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 159 ? N LEU A 137 O LEU A 184 ? O LEU A 162 
AA1 2  3  N ILE A 179 ? N ILE A 157 O PHE A 195 ? O PHE A 173 
AA1 3  4  O ASP A 194 ? O ASP A 172 N THR A 116 ? N THR A 94  
AA1 4  5  N ARG A 113 ? N ARG A 91  O ALA A 125 ? O ALA A 103 
AA1 5  6  N ASN A 124 ? N ASN A 102 O TYR A 143 ? O TYR A 121 
AA1 6  7  O VAL A 140 ? O VAL A 118 N ARG A 37  ? N ARG A 13  
AA1 7  8  N LEU A 36  ? N LEU A 12  O GLY A 51  ? O GLY A 27  
AA1 8  9  N ASP A 52  ? N ASP A 28  O ASP A 65  ? O ASP A 41  
AA1 9  10 N LEU A 66  ? N LEU A 42  O VAL A 230 ? O VAL A 208 
AA1 10 11 O VAL A 237 ? O VAL A 215 N ASP A 215 ? N ASP A 193 
AA1 11 12 O VAL A 214 ? O VAL A 192 N GLU A 166 ? N GLU A 144 
AA1 12 13 N TYR A 169 ? N TYR A 147 O THR A 176 ? O THR A 154 
AA2 1  2  N LEU B 159 ? N LEU B 137 O LEU B 184 ? O LEU B 162 
AA2 2  3  N MET B 181 ? N MET B 159 O CYS B 193 ? O CYS B 171 
AA2 3  4  O ASP B 194 ? O ASP B 172 N THR B 116 ? N THR B 94  
AA2 4  5  N ARG B 113 ? N ARG B 91  O ALA B 125 ? O ALA B 103 
AA2 5  6  N ASN B 124 ? N ASN B 102 O TYR B 143 ? O TYR B 121 
AA2 6  7  O PHE B 136 ? O PHE B 114 N LYS B 35  ? N LYS B 11  
AA2 7  8  N MET B 38  ? N MET B 14  O ILE B 49  ? O ILE B 25  
AA2 8  9  N LYS B 56  ? N LYS B 32  O LYS B 61  ? O LYS B 37  
AA2 9  10 N LEU B 66  ? N LEU B 42  O VAL B 230 ? O VAL B 208 
AA2 10 11 O VAL B 237 ? O VAL B 215 N ASP B 215 ? N ASP B 193 
AA2 11 12 O VAL B 214 ? O VAL B 192 N GLU B 166 ? N GLU B 144 
AA2 12 13 N LYS B 167 ? N LYS B 145 O ASP B 178 ? O ASP B 156 
# 
_pdbx_entry_details.entry_id                   9J11 
_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_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1  1 O   A HOH 445 ? ? O   A HOH 453 ? ? 1.83 
2  1 O   A HOH 335 ? ? O   A HOH 467 ? ? 1.85 
3  1 O   A HOH 457 ? ? O   B HOH 595 ? ? 1.87 
4  1 O   A HOH 335 ? ? O   A HOH 447 ? ? 1.88 
5  1 O   A HOH 516 ? ? O   A HOH 521 ? ? 1.91 
6  1 O   B HOH 566 ? ? O   B HOH 603 ? ? 1.92 
7  1 O   A HOH 447 ? ? O   A HOH 467 ? ? 1.94 
8  1 O   B HOH 575 ? ? O   B HOH 601 ? ? 1.99 
9  1 O   A HOH 511 ? ? O   A HOH 517 ? ? 2.01 
10 1 O   A HOH 471 ? ? O   A HOH 502 ? ? 2.03 
11 1 O   A HOH 352 ? ? O   A HOH 471 ? ? 2.03 
12 1 O   B HOH 536 ? ? O   B HOH 588 ? ? 2.03 
13 1 O   A HOH 444 ? ? O   A HOH 448 ? ? 2.03 
14 1 O   B HOH 552 ? ? O   B HOH 580 ? ? 2.06 
15 1 O   B HOH 546 ? ? O   B HOH 582 ? ? 2.09 
16 1 ND2 B ASN 124 ? ? O   B HOH 401 ? ? 2.12 
17 1 O   A HOH 443 ? ? O   A HOH 484 ? ? 2.12 
18 1 O   A HOH 449 ? ? O   A HOH 491 ? ? 2.12 
19 1 O   B HOH 558 ? ? O   B HOH 579 ? ? 2.13 
20 1 O   A HOH 471 ? ? O   A HOH 493 ? ? 2.14 
21 1 O   B HOH 503 ? ? O   B HOH 534 ? ? 2.14 
22 1 O   B HOH 555 ? ? O   B HOH 578 ? ? 2.14 
23 1 O   A HOH 304 ? ? O   A HOH 431 ? ? 2.16 
24 1 OE1 B GLU 158 ? ? O   B HOH 402 ? ? 2.16 
25 1 O   A HOH 522 ? ? O   A HOH 523 ? ? 2.17 
26 1 NZ  A LYS 145 ? ? O   A HOH 301 ? ? 2.18 
27 1 O   A HOH 495 ? ? O   B HOH 592 ? ? 2.18 
28 1 NH2 A ARG 104 ? ? OD2 A ASP 106 ? ? 2.19 
# 
loop_
_pdbx_validate_symm_contact.id 
_pdbx_validate_symm_contact.PDB_model_num 
_pdbx_validate_symm_contact.auth_atom_id_1 
_pdbx_validate_symm_contact.auth_asym_id_1 
_pdbx_validate_symm_contact.auth_comp_id_1 
_pdbx_validate_symm_contact.auth_seq_id_1 
_pdbx_validate_symm_contact.PDB_ins_code_1 
_pdbx_validate_symm_contact.label_alt_id_1 
_pdbx_validate_symm_contact.site_symmetry_1 
_pdbx_validate_symm_contact.auth_atom_id_2 
_pdbx_validate_symm_contact.auth_asym_id_2 
_pdbx_validate_symm_contact.auth_comp_id_2 
_pdbx_validate_symm_contact.auth_seq_id_2 
_pdbx_validate_symm_contact.PDB_ins_code_2 
_pdbx_validate_symm_contact.label_alt_id_2 
_pdbx_validate_symm_contact.site_symmetry_2 
_pdbx_validate_symm_contact.dist 
1 1 O A HOH 465 ? ? 1_555 O B HOH 597 ? ? 2_545 1.98 
2 1 O A HOH 460 ? ? 1_555 O B HOH 556 ? ? 2_545 2.03 
# 
_pdbx_validate_torsion.id              1 
_pdbx_validate_torsion.PDB_model_num   1 
_pdbx_validate_torsion.auth_comp_id    ASN 
_pdbx_validate_torsion.auth_asym_id    B 
_pdbx_validate_torsion.auth_seq_id     166 
_pdbx_validate_torsion.PDB_ins_code    ? 
_pdbx_validate_torsion.label_alt_id    ? 
_pdbx_validate_torsion.phi             83.19 
_pdbx_validate_torsion.psi             1.30 
# 
loop_
_pdbx_struct_mod_residue.id 
_pdbx_struct_mod_residue.label_asym_id 
_pdbx_struct_mod_residue.label_comp_id 
_pdbx_struct_mod_residue.label_seq_id 
_pdbx_struct_mod_residue.auth_asym_id 
_pdbx_struct_mod_residue.auth_comp_id 
_pdbx_struct_mod_residue.auth_seq_id 
_pdbx_struct_mod_residue.PDB_ins_code 
_pdbx_struct_mod_residue.parent_comp_id 
_pdbx_struct_mod_residue.details 
1 A 5SQ 86 A 5SQ 64 ? HIS chromophore 
2 A 5SQ 86 A 5SQ 64 ? TYR chromophore 
3 A 5SQ 86 A 5SQ 64 ? GLY chromophore 
4 B 5SQ 86 B 5SQ 64 ? HIS chromophore 
5 B 5SQ 86 B 5SQ 64 ? TYR chromophore 
6 B 5SQ 86 B 5SQ 64 ? GLY chromophore 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 0.2381   22.3059 -9.1096  0.1598 ? -0.0100 ? -0.0101 ? 0.1443 ? 0.0028  ? 0.1207 ? 4.7984 ? 
-0.4566 ? 0.2404  ? 2.0392 ? 0.1747  ? 1.9479 ? 0.0088  ? -0.5202 ? -0.1780 ? 0.2235  ? 0.0272  ? -0.0290 ? 0.0189  ? 0.0291  ? 
-0.0367 ? 
2  'X-RAY DIFFRACTION' ? refined -13.9532 16.8056 -17.3215 0.1083 ? -0.0065 ? 0.0172  ? 0.1509 ? -0.0126 ? 0.1582 ? 4.1839 ? 
0.5686  ? 0.3986  ? 3.1946 ? 0.4800  ? 2.8775 ? -0.0376 ? 0.0035  ? -0.1971 ? 0.0612  ? -0.0329 ? 0.3168  ? 0.0805  ? -0.3323 ? 
0.0732  ? 
3  'X-RAY DIFFRACTION' ? refined 1.2057   14.3736 -18.1693 0.1640 ? 0.0078  ? -0.0232 ? 0.1651 ? -0.0032 ? 0.1945 ? 6.9457 ? 
3.3135  ? -7.4518 ? 2.1445 ? -3.1831 ? 8.2338 ? -0.1330 ? -0.1445 ? -0.5455 ? -0.1262 ? -0.0625 ? -0.2436 ? 0.2782  ? 0.0954  ? 
0.3317  ? 
4  'X-RAY DIFFRACTION' ? refined -0.4793  14.9455 -9.6558  0.1618 ? -0.0034 ? -0.0436 ? 0.2129 ? -0.0031 ? 0.1635 ? 5.2464 ? 
1.4646  ? -5.9665 ? 1.6835 ? -1.3124 ? 6.8477 ? -0.2278 ? -0.3816 ? -0.5857 ? 0.0770  ? 0.0073  ? -0.0646 ? 0.3562  ? 0.1657  ? 
0.2066  ? 
5  'X-RAY DIFFRACTION' ? refined 3.3726   22.4117 -25.6953 0.1272 ? 0.0177  ? 0.0183  ? 0.1339 ? -0.0148 ? 0.1115 ? 3.2579 ? 
0.2304  ? -0.3178 ? 2.0385 ? -0.0148 ? 1.3608 ? -0.0272 ? 0.1585  ? -0.0080 ? -0.2715 ? 0.0852  ? -0.2189 ? -0.0313 ? 0.1375  ? 
-0.0706 ? 
6  'X-RAY DIFFRACTION' ? refined -3.6636  16.3094 -24.2501 0.1204 ? 0.0361  ? -0.0064 ? 0.1140 ? -0.0336 ? 0.1194 ? 5.4197 ? 
2.1605  ? -0.4933 ? 3.6970 ? -0.3397 ? 3.3597 ? -0.0362 ? -0.0032 ? -0.2144 ? -0.1160 ? 0.0045  ? -0.0161 ? 0.1199  ? -0.0599 ? 
0.0277  ? 
7  'X-RAY DIFFRACTION' ? refined -3.0876  28.8126 -16.7771 0.1100 ? 0.0249  ? 0.0274  ? 0.0978 ? -0.0033 ? 0.1072 ? 5.4741 ? 
2.2503  ? 2.0129  ? 4.1655 ? 1.5911  ? 3.3385 ? -0.1561 ? -0.1250 ? 0.4109  ? -0.0447 ? 0.0099  ? 0.1196  ? -0.2302 ? 0.0042  ? 
0.1783  ? 
8  'X-RAY DIFFRACTION' ? refined -11.3707 46.7563 -6.9948  0.2144 ? 0.0076  ? 0.0169  ? 0.1436 ? 0.0070  ? 0.1355 ? 5.5116 ? 
-0.1424 ? -0.4315 ? 0.9846 ? -0.0908 ? 1.3166 ? -0.0408 ? -0.3441 ? -0.0004 ? 0.1932  ? 0.0528  ? 0.0296  ? 0.0024  ? -0.0661 ? 
-0.0137 ? 
9  'X-RAY DIFFRACTION' ? refined 4.3614   52.6260 -18.3186 0.1754 ? -0.0062 ? -0.0311 ? 0.1658 ? 0.0055  ? 0.1663 ? 6.4918 ? 
-1.6797 ? -3.4838 ? 3.6814 ? 0.5127  ? 6.8823 ? -0.1799 ? 0.0960  ? -0.0676 ? -0.0897 ? -0.0240 ? -0.2860 ? 0.1226  ? 0.2527  ? 
0.1801  ? 
10 'X-RAY DIFFRACTION' ? refined -13.7112 53.6013 -12.1875 0.1536 ? 0.0182  ? 0.0231  ? 0.1177 ? 0.0028  ? 0.1158 ? 4.3243 ? 
0.2371  ? 1.5183  ? 1.0568 ? 0.0281  ? 2.6723 ? -0.0783 ? -0.2164 ? 0.1362  ? 0.0867  ? 0.0974  ? 0.1013  ? -0.1492 ? -0.2567 ? 
0.0113  ? 
11 'X-RAY DIFFRACTION' ? refined -10.5842 51.1459 -24.1892 0.1752 ? 0.0131  ? -0.0182 ? 0.1512 ? 0.0192  ? 0.1068 ? 5.5051 ? 
4.8185  ? -0.8856 ? 6.5734 ? 0.0892  ? 1.8478 ? -0.0642 ? 0.1456  ? 0.0682  ? -0.3113 ? 0.0992  ? 0.0708  ? -0.0076 ? -0.0447 ? 
-0.0482 ? 
12 'X-RAY DIFFRACTION' ? refined -8.9849  55.2474 -20.5304 0.1673 ? 0.0382  ? 0.0042  ? 0.0844 ? 0.0181  ? 0.1092 ? 4.9729 ? 
1.0495  ? -0.1649 ? 1.5897 ? -0.4725 ? 3.2402 ? 0.0720  ? -0.0506 ? 0.1313  ? 0.0174  ? -0.0408 ? 0.0448  ? -0.0831 ? -0.0766 ? 
-0.0034 ? 
13 'X-RAY DIFFRACTION' ? refined -9.0223  41.4475 -15.2804 0.1492 ? 0.0102  ? -0.0011 ? 0.1050 ? -0.0166 ? 0.1194 ? 5.5835 ? 
2.1068  ? -2.3633 ? 3.7969 ? -1.3553 ? 2.9206 ? -0.2477 ? -0.1386 ? -0.4463 ? -0.0906 ? -0.0318 ? -0.0871 ? 0.2887  ? 0.0357  ? 
0.2942  ? 
# 
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  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 2 through 60 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 61 through 86 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 87 through 110 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 111 through 123 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 124 through 163 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 164 through 189 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resid 190 through 219 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 2 through 65 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 66 through 79 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 80 through 135 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 136 through 163 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 164 through 189 )
;
13 'X-RAY DIFFRACTION' 13 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resid 190 through 219 )
;
# 
loop_
_pdbx_distant_solvent_atoms.id 
_pdbx_distant_solvent_atoms.PDB_model_num 
_pdbx_distant_solvent_atoms.auth_atom_id 
_pdbx_distant_solvent_atoms.label_alt_id 
_pdbx_distant_solvent_atoms.auth_asym_id 
_pdbx_distant_solvent_atoms.auth_comp_id 
_pdbx_distant_solvent_atoms.auth_seq_id 
_pdbx_distant_solvent_atoms.PDB_ins_code 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance 
1 1 O ? A HOH 519 ? 5.90 . 
2 1 O ? A HOH 520 ? 6.12 . 
3 1 O ? A HOH 521 ? 6.78 . 
4 1 O ? A HOH 522 ? 6.79 . 
5 1 O ? A HOH 523 ? 6.88 . 
6 1 O ? B HOH 608 ? 6.52 . 
# 
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 -23 ? A MET 1   
2  1 Y 1 A GLY -22 ? A GLY 2   
3  1 Y 1 A SER -21 ? A SER 3   
4  1 Y 1 A SER -20 ? A SER 4   
5  1 Y 1 A HIS -19 ? A HIS 5   
6  1 Y 1 A HIS -18 ? A HIS 6   
7  1 Y 1 A HIS -17 ? A HIS 7   
8  1 Y 1 A HIS -16 ? A HIS 8   
9  1 Y 1 A HIS -15 ? A HIS 9   
10 1 Y 1 A HIS -14 ? A HIS 10  
11 1 Y 1 A SER -13 ? A SER 11  
12 1 Y 1 A GLN -12 ? A GLN 12  
13 1 Y 1 A ASP -11 ? A ASP 13  
14 1 Y 1 A PRO -10 ? A PRO 14  
15 1 Y 1 A LEU -9  ? A LEU 15  
16 1 Y 1 A GLU -8  ? A GLU 16  
17 1 Y 1 A VAL -7  ? A VAL 17  
18 1 Y 1 A LEU -6  ? A LEU 18  
19 1 Y 1 A PHE -5  ? A PHE 19  
20 1 Y 1 A GLN -4  ? A GLN 20  
21 1 Y 1 A GLY -3  ? A GLY 21  
22 1 Y 1 A PRO -2  ? A PRO 22  
23 1 Y 1 A GLU -1  ? A GLU 23  
24 1 Y 1 A PHE 0   ? A PHE 24  
25 1 Y 1 A MET 1   ? A MET 25  
26 1 Y 1 A LEU 220 ? A LEU 242 
27 1 Y 1 A PRO 221 ? A PRO 243 
28 1 Y 1 A ASP 222 ? A ASP 244 
29 1 Y 1 A ASN 223 ? A ASN 245 
30 1 Y 1 A ALA 224 ? A ALA 246 
31 1 Y 1 A ARG 225 ? A ARG 247 
32 1 Y 1 A ARG 226 ? A ARG 248 
33 1 Y 1 B MET -23 ? B MET 1   
34 1 Y 1 B GLY -22 ? B GLY 2   
35 1 Y 1 B SER -21 ? B SER 3   
36 1 Y 1 B SER -20 ? B SER 4   
37 1 Y 1 B HIS -19 ? B HIS 5   
38 1 Y 1 B HIS -18 ? B HIS 6   
39 1 Y 1 B HIS -17 ? B HIS 7   
40 1 Y 1 B HIS -16 ? B HIS 8   
41 1 Y 1 B HIS -15 ? B HIS 9   
42 1 Y 1 B HIS -14 ? B HIS 10  
43 1 Y 1 B SER -13 ? B SER 11  
44 1 Y 1 B GLN -12 ? B GLN 12  
45 1 Y 1 B ASP -11 ? B ASP 13  
46 1 Y 1 B PRO -10 ? B PRO 14  
47 1 Y 1 B LEU -9  ? B LEU 15  
48 1 Y 1 B GLU -8  ? B GLU 16  
49 1 Y 1 B VAL -7  ? B VAL 17  
50 1 Y 1 B LEU -6  ? B LEU 18  
51 1 Y 1 B PHE -5  ? B PHE 19  
52 1 Y 1 B GLN -4  ? B GLN 20  
53 1 Y 1 B GLY -3  ? B GLY 21  
54 1 Y 1 B PRO -2  ? B PRO 22  
55 1 Y 1 B GLU -1  ? B GLU 23  
56 1 Y 1 B PHE 0   ? B PHE 24  
57 1 Y 1 B MET 1   ? B MET 25  
58 1 Y 1 B LEU 220 ? B LEU 242 
59 1 Y 1 B PRO 221 ? B PRO 243 
60 1 Y 1 B ASP 222 ? B ASP 244 
61 1 Y 1 B ASN 223 ? B ASN 245 
62 1 Y 1 B ALA 224 ? B ALA 246 
63 1 Y 1 B ARG 225 ? B ARG 247 
64 1 Y 1 B ARG 226 ? B ARG 248 
# 
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 
5SQ C1   C N N 1   
5SQ C2   C N N 2   
5SQ O3   O N N 3   
5SQ C3   C N N 4   
5SQ CA3  C N N 5   
5SQ N3   N N N 6   
5SQ O2   O N N 7   
5SQ CA1  C N S 8   
5SQ N1   N N N 9   
5SQ CB1  C N N 10  
5SQ CG1  C Y N 11  
5SQ C2H  C Y N 12  
5SQ N2H  N Y N 13  
5SQ N1H  N Y N 14  
5SQ C1H  C Y N 15  
5SQ N2   N N N 16  
5SQ CA2  C N N 17  
5SQ CB2  C N N 18  
5SQ CG2  C Y N 19  
5SQ CD2  C Y N 20  
5SQ CE2  C Y N 21  
5SQ CD1  C Y N 22  
5SQ CE1  C Y N 23  
5SQ CZ1  C Y N 24  
5SQ OH   O N N 25  
5SQ OXT  O N N 26  
5SQ HA31 H N N 27  
5SQ HA32 H N N 28  
5SQ HA1  H N N 29  
5SQ H    H N N 30  
5SQ H2   H N N 31  
5SQ H7   H N N 32  
5SQ H8   H N N 33  
5SQ H9   H N N 34  
5SQ H10  H N N 35  
5SQ H12  H N N 36  
5SQ H14  H N N 37  
5SQ H16  H N N 38  
5SQ H17  H N N 39  
5SQ H18  H N N 40  
5SQ H19  H N N 41  
5SQ H20  H N N 42  
5SQ HXT  H N N 43  
ALA N    N N N 44  
ALA CA   C N S 45  
ALA C    C N N 46  
ALA O    O N N 47  
ALA CB   C N N 48  
ALA OXT  O N N 49  
ALA H    H N N 50  
ALA H2   H N N 51  
ALA HA   H N N 52  
ALA HB1  H N N 53  
ALA HB2  H N N 54  
ALA HB3  H N N 55  
ALA HXT  H N N 56  
ARG N    N N N 57  
ARG CA   C N S 58  
ARG C    C N N 59  
ARG O    O N N 60  
ARG CB   C N N 61  
ARG CG   C N N 62  
ARG CD   C N N 63  
ARG NE   N N N 64  
ARG CZ   C N N 65  
ARG NH1  N N N 66  
ARG NH2  N N N 67  
ARG OXT  O N N 68  
ARG H    H N N 69  
ARG H2   H N N 70  
ARG HA   H N N 71  
ARG HB2  H N N 72  
ARG HB3  H N N 73  
ARG HG2  H N N 74  
ARG HG3  H N N 75  
ARG HD2  H N N 76  
ARG HD3  H N N 77  
ARG HE   H N N 78  
ARG HH11 H N N 79  
ARG HH12 H N N 80  
ARG HH21 H N N 81  
ARG HH22 H N N 82  
ARG HXT  H N N 83  
ASN N    N N N 84  
ASN CA   C N S 85  
ASN C    C N N 86  
ASN O    O N N 87  
ASN CB   C N N 88  
ASN CG   C N N 89  
ASN OD1  O N N 90  
ASN ND2  N N N 91  
ASN OXT  O N N 92  
ASN H    H N N 93  
ASN H2   H N N 94  
ASN HA   H N N 95  
ASN HB2  H N N 96  
ASN HB3  H N N 97  
ASN HD21 H N N 98  
ASN HD22 H N N 99  
ASN HXT  H N N 100 
ASP N    N N N 101 
ASP CA   C N S 102 
ASP C    C N N 103 
ASP O    O N N 104 
ASP CB   C N N 105 
ASP CG   C N N 106 
ASP OD1  O N N 107 
ASP OD2  O N N 108 
ASP OXT  O N N 109 
ASP H    H N N 110 
ASP H2   H N N 111 
ASP HA   H N N 112 
ASP HB2  H N N 113 
ASP HB3  H N N 114 
ASP HD2  H N N 115 
ASP HXT  H N N 116 
CYS N    N N N 117 
CYS CA   C N R 118 
CYS C    C N N 119 
CYS O    O N N 120 
CYS CB   C N N 121 
CYS SG   S N N 122 
CYS OXT  O N N 123 
CYS H    H N N 124 
CYS H2   H N N 125 
CYS HA   H N N 126 
CYS HB2  H N N 127 
CYS HB3  H N N 128 
CYS HG   H N N 129 
CYS HXT  H N N 130 
DTT S1   S N N 131 
DTT C1   C N N 132 
DTT C2   C N R 133 
DTT O2   O N N 134 
DTT C3   C N R 135 
DTT O3   O N N 136 
DTT C4   C N N 137 
DTT S4   S N N 138 
DTT HS1  H N N 139 
DTT H11  H N N 140 
DTT H12  H N N 141 
DTT H2   H N N 142 
DTT HO2  H N N 143 
DTT H3   H N N 144 
DTT HO3  H N N 145 
DTT H41  H N N 146 
DTT H42  H N N 147 
DTT HS2  H N N 148 
GLN N    N N N 149 
GLN CA   C N S 150 
GLN C    C N N 151 
GLN O    O N N 152 
GLN CB   C N N 153 
GLN CG   C N N 154 
GLN CD   C N N 155 
GLN OE1  O N N 156 
GLN NE2  N N N 157 
GLN OXT  O N N 158 
GLN H    H N N 159 
GLN H2   H N N 160 
GLN HA   H N N 161 
GLN HB2  H N N 162 
GLN HB3  H N N 163 
GLN HG2  H N N 164 
GLN HG3  H N N 165 
GLN HE21 H N N 166 
GLN HE22 H N N 167 
GLN HXT  H N N 168 
GLU N    N N N 169 
GLU CA   C N S 170 
GLU C    C N N 171 
GLU O    O N N 172 
GLU CB   C N N 173 
GLU CG   C N N 174 
GLU CD   C N N 175 
GLU OE1  O N N 176 
GLU OE2  O N N 177 
GLU OXT  O N N 178 
GLU H    H N N 179 
GLU H2   H N N 180 
GLU HA   H N N 181 
GLU HB2  H N N 182 
GLU HB3  H N N 183 
GLU HG2  H N N 184 
GLU HG3  H N N 185 
GLU HE2  H N N 186 
GLU HXT  H N N 187 
GLY N    N N N 188 
GLY CA   C N N 189 
GLY C    C N N 190 
GLY O    O N N 191 
GLY OXT  O N N 192 
GLY H    H N N 193 
GLY H2   H N N 194 
GLY HA2  H N N 195 
GLY HA3  H N N 196 
GLY HXT  H N N 197 
HIS N    N N N 198 
HIS CA   C N S 199 
HIS C    C N N 200 
HIS O    O N N 201 
HIS CB   C N N 202 
HIS CG   C Y N 203 
HIS ND1  N Y N 204 
HIS CD2  C Y N 205 
HIS CE1  C Y N 206 
HIS NE2  N Y N 207 
HIS OXT  O N N 208 
HIS H    H N N 209 
HIS H2   H N N 210 
HIS HA   H N N 211 
HIS HB2  H N N 212 
HIS HB3  H N N 213 
HIS HD1  H N N 214 
HIS HD2  H N N 215 
HIS HE1  H N N 216 
HIS HE2  H N N 217 
HIS HXT  H N N 218 
HOH O    O N N 219 
HOH H1   H N N 220 
HOH H2   H N N 221 
ILE N    N N N 222 
ILE CA   C N S 223 
ILE C    C N N 224 
ILE O    O N N 225 
ILE CB   C N S 226 
ILE CG1  C N N 227 
ILE CG2  C N N 228 
ILE CD1  C N N 229 
ILE OXT  O N N 230 
ILE H    H N N 231 
ILE H2   H N N 232 
ILE HA   H N N 233 
ILE HB   H N N 234 
ILE HG12 H N N 235 
ILE HG13 H N N 236 
ILE HG21 H N N 237 
ILE HG22 H N N 238 
ILE HG23 H N N 239 
ILE HD11 H N N 240 
ILE HD12 H N N 241 
ILE HD13 H N N 242 
ILE HXT  H N N 243 
LEU N    N N N 244 
LEU CA   C N S 245 
LEU C    C N N 246 
LEU O    O N N 247 
LEU CB   C N N 248 
LEU CG   C N N 249 
LEU CD1  C N N 250 
LEU CD2  C N N 251 
LEU OXT  O N N 252 
LEU H    H N N 253 
LEU H2   H N N 254 
LEU HA   H N N 255 
LEU HB2  H N N 256 
LEU HB3  H N N 257 
LEU HG   H N N 258 
LEU HD11 H N N 259 
LEU HD12 H N N 260 
LEU HD13 H N N 261 
LEU HD21 H N N 262 
LEU HD22 H N N 263 
LEU HD23 H N N 264 
LEU HXT  H N N 265 
LYS N    N N N 266 
LYS CA   C N S 267 
LYS C    C N N 268 
LYS O    O N N 269 
LYS CB   C N N 270 
LYS CG   C N N 271 
LYS CD   C N N 272 
LYS CE   C N N 273 
LYS NZ   N N N 274 
LYS OXT  O N N 275 
LYS H    H N N 276 
LYS H2   H N N 277 
LYS HA   H N N 278 
LYS HB2  H N N 279 
LYS HB3  H N N 280 
LYS HG2  H N N 281 
LYS HG3  H N N 282 
LYS HD2  H N N 283 
LYS HD3  H N N 284 
LYS HE2  H N N 285 
LYS HE3  H N N 286 
LYS HZ1  H N N 287 
LYS HZ2  H N N 288 
LYS HZ3  H N N 289 
LYS HXT  H N N 290 
MET N    N N N 291 
MET CA   C N S 292 
MET C    C N N 293 
MET O    O N N 294 
MET CB   C N N 295 
MET CG   C N N 296 
MET SD   S N N 297 
MET CE   C N N 298 
MET OXT  O N N 299 
MET H    H N N 300 
MET H2   H N N 301 
MET HA   H N N 302 
MET HB2  H N N 303 
MET HB3  H N N 304 
MET HG2  H N N 305 
MET HG3  H N N 306 
MET HE1  H N N 307 
MET HE2  H N N 308 
MET HE3  H N N 309 
MET HXT  H N N 310 
PHE N    N N N 311 
PHE CA   C N S 312 
PHE C    C N N 313 
PHE O    O N N 314 
PHE CB   C N N 315 
PHE CG   C Y N 316 
PHE CD1  C Y N 317 
PHE CD2  C Y N 318 
PHE CE1  C Y N 319 
PHE CE2  C Y N 320 
PHE CZ   C Y N 321 
PHE OXT  O N N 322 
PHE H    H N N 323 
PHE H2   H N N 324 
PHE HA   H N N 325 
PHE HB2  H N N 326 
PHE HB3  H N N 327 
PHE HD1  H N N 328 
PHE HD2  H N N 329 
PHE HE1  H N N 330 
PHE HE2  H N N 331 
PHE HZ   H N N 332 
PHE HXT  H N N 333 
PRO N    N N N 334 
PRO CA   C N S 335 
PRO C    C N N 336 
PRO O    O N N 337 
PRO CB   C N N 338 
PRO CG   C N N 339 
PRO CD   C N N 340 
PRO OXT  O N N 341 
PRO H    H N N 342 
PRO HA   H N N 343 
PRO HB2  H N N 344 
PRO HB3  H N N 345 
PRO HG2  H N N 346 
PRO HG3  H N N 347 
PRO HD2  H N N 348 
PRO HD3  H N N 349 
PRO HXT  H N N 350 
SER N    N N N 351 
SER CA   C N S 352 
SER C    C N N 353 
SER O    O N N 354 
SER CB   C N N 355 
SER OG   O N N 356 
SER OXT  O N N 357 
SER H    H N N 358 
SER H2   H N N 359 
SER HA   H N N 360 
SER HB2  H N N 361 
SER HB3  H N N 362 
SER HG   H N N 363 
SER HXT  H N N 364 
THR N    N N N 365 
THR CA   C N S 366 
THR C    C N N 367 
THR O    O N N 368 
THR CB   C N R 369 
THR OG1  O N N 370 
THR CG2  C N N 371 
THR OXT  O N N 372 
THR H    H N N 373 
THR H2   H N N 374 
THR HA   H N N 375 
THR HB   H N N 376 
THR HG1  H N N 377 
THR HG21 H N N 378 
THR HG22 H N N 379 
THR HG23 H N N 380 
THR HXT  H N N 381 
TRP N    N N N 382 
TRP CA   C N S 383 
TRP C    C N N 384 
TRP O    O N N 385 
TRP CB   C N N 386 
TRP CG   C Y N 387 
TRP CD1  C Y N 388 
TRP CD2  C Y N 389 
TRP NE1  N Y N 390 
TRP CE2  C Y N 391 
TRP CE3  C Y N 392 
TRP CZ2  C Y N 393 
TRP CZ3  C Y N 394 
TRP CH2  C Y N 395 
TRP OXT  O N N 396 
TRP H    H N N 397 
TRP H2   H N N 398 
TRP HA   H N N 399 
TRP HB2  H N N 400 
TRP HB3  H N N 401 
TRP HD1  H N N 402 
TRP HE1  H N N 403 
TRP HE3  H N N 404 
TRP HZ2  H N N 405 
TRP HZ3  H N N 406 
TRP HH2  H N N 407 
TRP HXT  H N N 408 
TYR N    N N N 409 
TYR CA   C N S 410 
TYR C    C N N 411 
TYR O    O N N 412 
TYR CB   C N N 413 
TYR CG   C Y N 414 
TYR CD1  C Y N 415 
TYR CD2  C Y N 416 
TYR CE1  C Y N 417 
TYR CE2  C Y N 418 
TYR CZ   C Y N 419 
TYR OH   O N N 420 
TYR OXT  O N N 421 
TYR H    H N N 422 
TYR H2   H N N 423 
TYR HA   H N N 424 
TYR HB2  H N N 425 
TYR HB3  H N N 426 
TYR HD1  H N N 427 
TYR HD2  H N N 428 
TYR HE1  H N N 429 
TYR HE2  H N N 430 
TYR HH   H N N 431 
TYR HXT  H N N 432 
VAL N    N N N 433 
VAL CA   C N S 434 
VAL C    C N N 435 
VAL O    O N N 436 
VAL CB   C N N 437 
VAL CG1  C N N 438 
VAL CG2  C N N 439 
VAL OXT  O N N 440 
VAL H    H N N 441 
VAL H2   H N N 442 
VAL HA   H N N 443 
VAL HB   H N N 444 
VAL HG11 H N N 445 
VAL HG12 H N N 446 
VAL HG13 H N N 447 
VAL HG21 H N N 448 
VAL HG22 H N N 449 
VAL HG23 H N N 450 
VAL HXT  H N N 451 
# 
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 
5SQ OH  CZ1  sing N N 1   
5SQ N1  CA1  sing N N 2   
5SQ CZ1 CE1  doub Y N 3   
5SQ CZ1 CE2  sing Y N 4   
5SQ CE1 CD1  sing Y N 5   
5SQ CE2 CD2  doub Y N 6   
5SQ CD1 CG2  doub Y N 7   
5SQ CD2 CG2  sing Y N 8   
5SQ CG2 CB2  sing N N 9   
5SQ CA3 N3   sing N N 10  
5SQ CA3 C3   sing N N 11  
5SQ CB1 CA1  sing N N 12  
5SQ CB1 CG1  sing N N 13  
5SQ CA1 C1   sing N N 14  
5SQ N3  C1   sing N N 15  
5SQ N3  C2   sing N N 16  
5SQ C1  N2   doub N N 17  
5SQ C2  O2   doub N N 18  
5SQ C2  CA2  sing N N 19  
5SQ N2  CA2  sing N N 20  
5SQ CA2 CB2  doub N Z 21  
5SQ CG1 N1H  sing Y N 22  
5SQ CG1 C2H  doub Y N 23  
5SQ N1H C1H  doub Y N 24  
5SQ C2H N2H  sing Y N 25  
5SQ C1H N2H  sing Y N 26  
5SQ O3  C3   doub N N 27  
5SQ C3  OXT  sing N N 28  
5SQ CA3 HA31 sing N N 29  
5SQ CA3 HA32 sing N N 30  
5SQ CA1 HA1  sing N N 31  
5SQ N1  H    sing N N 32  
5SQ N1  H2   sing N N 33  
5SQ CB1 H7   sing N N 34  
5SQ CB1 H8   sing N N 35  
5SQ C2H H9   sing N N 36  
5SQ N2H H10  sing N N 37  
5SQ C1H H12  sing N N 38  
5SQ CB2 H14  sing N N 39  
5SQ CD2 H16  sing N N 40  
5SQ CE2 H17  sing N N 41  
5SQ CD1 H18  sing N N 42  
5SQ CE1 H19  sing N N 43  
5SQ OH  H20  sing N N 44  
5SQ OXT HXT  sing N N 45  
ALA N   CA   sing N N 46  
ALA N   H    sing N N 47  
ALA N   H2   sing N N 48  
ALA CA  C    sing N N 49  
ALA CA  CB   sing N N 50  
ALA CA  HA   sing N N 51  
ALA C   O    doub N N 52  
ALA C   OXT  sing N N 53  
ALA CB  HB1  sing N N 54  
ALA CB  HB2  sing N N 55  
ALA CB  HB3  sing N N 56  
ALA OXT HXT  sing N N 57  
ARG N   CA   sing N N 58  
ARG N   H    sing N N 59  
ARG N   H2   sing N N 60  
ARG CA  C    sing N N 61  
ARG CA  CB   sing N N 62  
ARG CA  HA   sing N N 63  
ARG C   O    doub N N 64  
ARG C   OXT  sing N N 65  
ARG CB  CG   sing N N 66  
ARG CB  HB2  sing N N 67  
ARG CB  HB3  sing N N 68  
ARG CG  CD   sing N N 69  
ARG CG  HG2  sing N N 70  
ARG CG  HG3  sing N N 71  
ARG CD  NE   sing N N 72  
ARG CD  HD2  sing N N 73  
ARG CD  HD3  sing N N 74  
ARG NE  CZ   sing N N 75  
ARG NE  HE   sing N N 76  
ARG CZ  NH1  sing N N 77  
ARG CZ  NH2  doub N N 78  
ARG NH1 HH11 sing N N 79  
ARG NH1 HH12 sing N N 80  
ARG NH2 HH21 sing N N 81  
ARG NH2 HH22 sing N N 82  
ARG OXT HXT  sing N N 83  
ASN N   CA   sing N N 84  
ASN N   H    sing N N 85  
ASN N   H2   sing N N 86  
ASN CA  C    sing N N 87  
ASN CA  CB   sing N N 88  
ASN CA  HA   sing N N 89  
ASN C   O    doub N N 90  
ASN C   OXT  sing N N 91  
ASN CB  CG   sing N N 92  
ASN CB  HB2  sing N N 93  
ASN CB  HB3  sing N N 94  
ASN CG  OD1  doub N N 95  
ASN CG  ND2  sing N N 96  
ASN ND2 HD21 sing N N 97  
ASN ND2 HD22 sing N N 98  
ASN OXT HXT  sing N N 99  
ASP N   CA   sing N N 100 
ASP N   H    sing N N 101 
ASP N   H2   sing N N 102 
ASP CA  C    sing N N 103 
ASP CA  CB   sing N N 104 
ASP CA  HA   sing N N 105 
ASP C   O    doub N N 106 
ASP C   OXT  sing N N 107 
ASP CB  CG   sing N N 108 
ASP CB  HB2  sing N N 109 
ASP CB  HB3  sing N N 110 
ASP CG  OD1  doub N N 111 
ASP CG  OD2  sing N N 112 
ASP OD2 HD2  sing N N 113 
ASP OXT HXT  sing N N 114 
CYS N   CA   sing N N 115 
CYS N   H    sing N N 116 
CYS N   H2   sing N N 117 
CYS CA  C    sing N N 118 
CYS CA  CB   sing N N 119 
CYS CA  HA   sing N N 120 
CYS C   O    doub N N 121 
CYS C   OXT  sing N N 122 
CYS CB  SG   sing N N 123 
CYS CB  HB2  sing N N 124 
CYS CB  HB3  sing N N 125 
CYS SG  HG   sing N N 126 
CYS OXT HXT  sing N N 127 
DTT S1  C1   sing N N 128 
DTT S1  HS1  sing N N 129 
DTT C1  C2   sing N N 130 
DTT C1  H11  sing N N 131 
DTT C1  H12  sing N N 132 
DTT C2  O2   sing N N 133 
DTT C2  C3   sing N N 134 
DTT C2  H2   sing N N 135 
DTT O2  HO2  sing N N 136 
DTT C3  O3   sing N N 137 
DTT C3  C4   sing N N 138 
DTT C3  H3   sing N N 139 
DTT O3  HO3  sing N N 140 
DTT C4  S4   sing N N 141 
DTT C4  H41  sing N N 142 
DTT C4  H42  sing N N 143 
DTT S4  HS2  sing N N 144 
GLN N   CA   sing N N 145 
GLN N   H    sing N N 146 
GLN N   H2   sing N N 147 
GLN CA  C    sing N N 148 
GLN CA  CB   sing N N 149 
GLN CA  HA   sing N N 150 
GLN C   O    doub N N 151 
GLN C   OXT  sing N N 152 
GLN CB  CG   sing N N 153 
GLN CB  HB2  sing N N 154 
GLN CB  HB3  sing N N 155 
GLN CG  CD   sing N N 156 
GLN CG  HG2  sing N N 157 
GLN CG  HG3  sing N N 158 
GLN CD  OE1  doub N N 159 
GLN CD  NE2  sing N N 160 
GLN NE2 HE21 sing N N 161 
GLN NE2 HE22 sing N N 162 
GLN OXT HXT  sing N N 163 
GLU N   CA   sing N N 164 
GLU N   H    sing N N 165 
GLU N   H2   sing N N 166 
GLU CA  C    sing N N 167 
GLU CA  CB   sing N N 168 
GLU CA  HA   sing N N 169 
GLU C   O    doub N N 170 
GLU C   OXT  sing N N 171 
GLU CB  CG   sing N N 172 
GLU CB  HB2  sing N N 173 
GLU CB  HB3  sing N N 174 
GLU CG  CD   sing N N 175 
GLU CG  HG2  sing N N 176 
GLU CG  HG3  sing N N 177 
GLU CD  OE1  doub N N 178 
GLU CD  OE2  sing N N 179 
GLU OE2 HE2  sing N N 180 
GLU OXT HXT  sing N N 181 
GLY N   CA   sing N N 182 
GLY N   H    sing N N 183 
GLY N   H2   sing N N 184 
GLY CA  C    sing N N 185 
GLY CA  HA2  sing N N 186 
GLY CA  HA3  sing N N 187 
GLY C   O    doub N N 188 
GLY C   OXT  sing N N 189 
GLY OXT HXT  sing N N 190 
HIS N   CA   sing N N 191 
HIS N   H    sing N N 192 
HIS N   H2   sing N N 193 
HIS CA  C    sing N N 194 
HIS CA  CB   sing N N 195 
HIS CA  HA   sing N N 196 
HIS C   O    doub N N 197 
HIS C   OXT  sing N N 198 
HIS CB  CG   sing N N 199 
HIS CB  HB2  sing N N 200 
HIS CB  HB3  sing N N 201 
HIS CG  ND1  sing Y N 202 
HIS CG  CD2  doub Y N 203 
HIS ND1 CE1  doub Y N 204 
HIS ND1 HD1  sing N N 205 
HIS CD2 NE2  sing Y N 206 
HIS CD2 HD2  sing N N 207 
HIS CE1 NE2  sing Y N 208 
HIS CE1 HE1  sing N N 209 
HIS NE2 HE2  sing N N 210 
HIS OXT HXT  sing N N 211 
HOH O   H1   sing N N 212 
HOH O   H2   sing N N 213 
ILE N   CA   sing N N 214 
ILE N   H    sing N N 215 
ILE N   H2   sing N N 216 
ILE CA  C    sing N N 217 
ILE CA  CB   sing N N 218 
ILE CA  HA   sing N N 219 
ILE C   O    doub N N 220 
ILE C   OXT  sing N N 221 
ILE CB  CG1  sing N N 222 
ILE CB  CG2  sing N N 223 
ILE CB  HB   sing N N 224 
ILE CG1 CD1  sing N N 225 
ILE CG1 HG12 sing N N 226 
ILE CG1 HG13 sing N N 227 
ILE CG2 HG21 sing N N 228 
ILE CG2 HG22 sing N N 229 
ILE CG2 HG23 sing N N 230 
ILE CD1 HD11 sing N N 231 
ILE CD1 HD12 sing N N 232 
ILE CD1 HD13 sing N N 233 
ILE OXT HXT  sing N N 234 
LEU N   CA   sing N N 235 
LEU N   H    sing N N 236 
LEU N   H2   sing N N 237 
LEU CA  C    sing N N 238 
LEU CA  CB   sing N N 239 
LEU CA  HA   sing N N 240 
LEU C   O    doub N N 241 
LEU C   OXT  sing N N 242 
LEU CB  CG   sing N N 243 
LEU CB  HB2  sing N N 244 
LEU CB  HB3  sing N N 245 
LEU CG  CD1  sing N N 246 
LEU CG  CD2  sing N N 247 
LEU CG  HG   sing N N 248 
LEU CD1 HD11 sing N N 249 
LEU CD1 HD12 sing N N 250 
LEU CD1 HD13 sing N N 251 
LEU CD2 HD21 sing N N 252 
LEU CD2 HD22 sing N N 253 
LEU CD2 HD23 sing N N 254 
LEU OXT HXT  sing N N 255 
LYS N   CA   sing N N 256 
LYS N   H    sing N N 257 
LYS N   H2   sing N N 258 
LYS CA  C    sing N N 259 
LYS CA  CB   sing N N 260 
LYS CA  HA   sing N N 261 
LYS C   O    doub N N 262 
LYS C   OXT  sing N N 263 
LYS CB  CG   sing N N 264 
LYS CB  HB2  sing N N 265 
LYS CB  HB3  sing N N 266 
LYS CG  CD   sing N N 267 
LYS CG  HG2  sing N N 268 
LYS CG  HG3  sing N N 269 
LYS CD  CE   sing N N 270 
LYS CD  HD2  sing N N 271 
LYS CD  HD3  sing N N 272 
LYS CE  NZ   sing N N 273 
LYS CE  HE2  sing N N 274 
LYS CE  HE3  sing N N 275 
LYS NZ  HZ1  sing N N 276 
LYS NZ  HZ2  sing N N 277 
LYS NZ  HZ3  sing N N 278 
LYS OXT HXT  sing N N 279 
MET N   CA   sing N N 280 
MET N   H    sing N N 281 
MET N   H2   sing N N 282 
MET CA  C    sing N N 283 
MET CA  CB   sing N N 284 
MET CA  HA   sing N N 285 
MET C   O    doub N N 286 
MET C   OXT  sing N N 287 
MET CB  CG   sing N N 288 
MET CB  HB2  sing N N 289 
MET CB  HB3  sing N N 290 
MET CG  SD   sing N N 291 
MET CG  HG2  sing N N 292 
MET CG  HG3  sing N N 293 
MET SD  CE   sing N N 294 
MET CE  HE1  sing N N 295 
MET CE  HE2  sing N N 296 
MET CE  HE3  sing N N 297 
MET OXT HXT  sing N N 298 
PHE N   CA   sing N N 299 
PHE N   H    sing N N 300 
PHE N   H2   sing N N 301 
PHE CA  C    sing N N 302 
PHE CA  CB   sing N N 303 
PHE CA  HA   sing N N 304 
PHE C   O    doub N N 305 
PHE C   OXT  sing N N 306 
PHE CB  CG   sing N N 307 
PHE CB  HB2  sing N N 308 
PHE CB  HB3  sing N N 309 
PHE CG  CD1  doub Y N 310 
PHE CG  CD2  sing Y N 311 
PHE CD1 CE1  sing Y N 312 
PHE CD1 HD1  sing N N 313 
PHE CD2 CE2  doub Y N 314 
PHE CD2 HD2  sing N N 315 
PHE CE1 CZ   doub Y N 316 
PHE CE1 HE1  sing N N 317 
PHE CE2 CZ   sing Y N 318 
PHE CE2 HE2  sing N N 319 
PHE CZ  HZ   sing N N 320 
PHE OXT HXT  sing N N 321 
PRO N   CA   sing N N 322 
PRO N   CD   sing N N 323 
PRO N   H    sing N N 324 
PRO CA  C    sing N N 325 
PRO CA  CB   sing N N 326 
PRO CA  HA   sing N N 327 
PRO C   O    doub N N 328 
PRO C   OXT  sing N N 329 
PRO CB  CG   sing N N 330 
PRO CB  HB2  sing N N 331 
PRO CB  HB3  sing N N 332 
PRO CG  CD   sing N N 333 
PRO CG  HG2  sing N N 334 
PRO CG  HG3  sing N N 335 
PRO CD  HD2  sing N N 336 
PRO CD  HD3  sing N N 337 
PRO OXT HXT  sing N N 338 
SER N   CA   sing N N 339 
SER N   H    sing N N 340 
SER N   H2   sing N N 341 
SER CA  C    sing N N 342 
SER CA  CB   sing N N 343 
SER CA  HA   sing N N 344 
SER C   O    doub N N 345 
SER C   OXT  sing N N 346 
SER CB  OG   sing N N 347 
SER CB  HB2  sing N N 348 
SER CB  HB3  sing N N 349 
SER OG  HG   sing N N 350 
SER OXT HXT  sing N N 351 
THR N   CA   sing N N 352 
THR N   H    sing N N 353 
THR N   H2   sing N N 354 
THR CA  C    sing N N 355 
THR CA  CB   sing N N 356 
THR CA  HA   sing N N 357 
THR C   O    doub N N 358 
THR C   OXT  sing N N 359 
THR CB  OG1  sing N N 360 
THR CB  CG2  sing N N 361 
THR CB  HB   sing N N 362 
THR OG1 HG1  sing N N 363 
THR CG2 HG21 sing N N 364 
THR CG2 HG22 sing N N 365 
THR CG2 HG23 sing N N 366 
THR OXT HXT  sing N N 367 
TRP N   CA   sing N N 368 
TRP N   H    sing N N 369 
TRP N   H2   sing N N 370 
TRP CA  C    sing N N 371 
TRP CA  CB   sing N N 372 
TRP CA  HA   sing N N 373 
TRP C   O    doub N N 374 
TRP C   OXT  sing N N 375 
TRP CB  CG   sing N N 376 
TRP CB  HB2  sing N N 377 
TRP CB  HB3  sing N N 378 
TRP CG  CD1  doub Y N 379 
TRP CG  CD2  sing Y N 380 
TRP CD1 NE1  sing Y N 381 
TRP CD1 HD1  sing N N 382 
TRP CD2 CE2  doub Y N 383 
TRP CD2 CE3  sing Y N 384 
TRP NE1 CE2  sing Y N 385 
TRP NE1 HE1  sing N N 386 
TRP CE2 CZ2  sing Y N 387 
TRP CE3 CZ3  doub Y N 388 
TRP CE3 HE3  sing N N 389 
TRP CZ2 CH2  doub Y N 390 
TRP CZ2 HZ2  sing N N 391 
TRP CZ3 CH2  sing Y N 392 
TRP CZ3 HZ3  sing N N 393 
TRP CH2 HH2  sing N N 394 
TRP OXT HXT  sing N N 395 
TYR N   CA   sing N N 396 
TYR N   H    sing N N 397 
TYR N   H2   sing N N 398 
TYR CA  C    sing N N 399 
TYR CA  CB   sing N N 400 
TYR CA  HA   sing N N 401 
TYR C   O    doub N N 402 
TYR C   OXT  sing N N 403 
TYR CB  CG   sing N N 404 
TYR CB  HB2  sing N N 405 
TYR CB  HB3  sing N N 406 
TYR CG  CD1  doub Y N 407 
TYR CG  CD2  sing Y N 408 
TYR CD1 CE1  sing Y N 409 
TYR CD1 HD1  sing N N 410 
TYR CD2 CE2  doub Y N 411 
TYR CD2 HD2  sing N N 412 
TYR CE1 CZ   doub Y N 413 
TYR CE1 HE1  sing N N 414 
TYR CE2 CZ   sing Y N 415 
TYR CE2 HE2  sing N N 416 
TYR CZ  OH   sing N N 417 
TYR OH  HH   sing N N 418 
TYR OXT HXT  sing N N 419 
VAL N   CA   sing N N 420 
VAL N   H    sing N N 421 
VAL N   H2   sing N N 422 
VAL CA  C    sing N N 423 
VAL CA  CB   sing N N 424 
VAL CA  HA   sing N N 425 
VAL C   O    doub N N 426 
VAL C   OXT  sing N N 427 
VAL CB  CG1  sing N N 428 
VAL CB  CG2  sing N N 429 
VAL CB  HB   sing N N 430 
VAL CG1 HG11 sing N N 431 
VAL CG1 HG12 sing N N 432 
VAL CG1 HG13 sing N N 433 
VAL CG2 HG21 sing N N 434 
VAL CG2 HG22 sing N N 435 
VAL CG2 HG23 sing N N 436 
VAL OXT HXT  sing N N 437 
# 
_pdbx_audit_support.funding_organization   'Other government' 
_pdbx_audit_support.country                ? 
_pdbx_audit_support.grant_number           ? 
_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      PDB 
_pdbx_initial_refinement_model.accession_code   5OOZ 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9J11 
_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]   0.019472 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.004114 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012137 
_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]   0.016545 
_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   . SER A 1 26  ? -23.530 15.081 -10.041 1.00 64.50 ? 2   SER A N   1 
ATOM   2    C CA  . SER A 1 26  ? -23.805 14.929 -8.615  1.00 56.50 ? 2   SER A CA  1 
ATOM   3    C C   . SER A 1 26  ? -22.513 14.791 -7.818  1.00 48.35 ? 2   SER A C   1 
ATOM   4    O O   . SER A 1 26  ? -22.392 15.342 -6.724  1.00 57.68 ? 2   SER A O   1 
ATOM   5    C CB  . SER A 1 26  ? -24.712 13.720 -8.364  1.00 54.61 ? 2   SER A CB  1 
ATOM   6    O OG  . SER A 1 26  ? -24.888 13.498 -6.974  1.00 59.23 ? 2   SER A OG  1 
ATOM   7    N N   . ALA A 1 27  ? -21.539 14.069 -8.381  1.00 50.54 ? 3   ALA A N   1 
ATOM   8    C CA  . ALA A 1 27  ? -20.282 13.857 -7.671  1.00 36.11 ? 3   ALA A CA  1 
ATOM   9    C C   . ALA A 1 27  ? -19.454 15.136 -7.619  1.00 38.09 ? 3   ALA A C   1 
ATOM   10   O O   . ALA A 1 27  ? -18.796 15.412 -6.610  1.00 51.46 ? 3   ALA A O   1 
ATOM   11   C CB  . ALA A 1 27  ? -19.492 12.725 -8.327  1.00 38.03 ? 3   ALA A CB  1 
ATOM   12   N N   . ILE A 1 28  ? -19.468 15.919 -8.695  1.00 33.72 ? 4   ILE A N   1 
ATOM   13   C CA  . ILE A 1 28  ? -18.730 17.177 -8.782  1.00 33.72 ? 4   ILE A CA  1 
ATOM   14   C C   . ILE A 1 28  ? -19.581 18.307 -8.225  1.00 27.23 ? 4   ILE A C   1 
ATOM   15   O O   . ILE A 1 28  ? -20.679 18.562 -8.729  1.00 31.84 ? 4   ILE A O   1 
ATOM   16   C CB  . ILE A 1 28  ? -18.330 17.482 -10.234 1.00 37.98 ? 4   ILE A CB  1 
ATOM   17   C CG1 . ILE A 1 28  ? -17.943 16.203 -10.983 1.00 44.19 ? 4   ILE A CG1 1 
ATOM   18   C CG2 . ILE A 1 28  ? -17.262 18.529 -10.269 1.00 35.13 ? 4   ILE A CG2 1 
ATOM   19   C CD1 . ILE A 1 28  ? -16.538 15.764 -10.691 1.00 28.77 ? 4   ILE A CD1 1 
ATOM   20   N N   . LYS A 1 29  ? -19.061 19.014 -7.196  1.00 34.31 ? 5   LYS A N   1 
ATOM   21   C CA  . LYS A 1 29  ? -19.758 20.196 -6.694  1.00 35.60 ? 5   LYS A CA  1 
ATOM   22   C C   . LYS A 1 29  ? -19.356 21.422 -7.504  1.00 31.48 ? 5   LYS A C   1 
ATOM   23   O O   . LYS A 1 29  ? -18.288 21.446 -8.117  1.00 26.66 ? 5   LYS A O   1 
ATOM   24   C CB  . LYS A 1 29  ? -19.442 20.453 -5.213  1.00 32.73 ? 5   LYS A CB  1 
ATOM   25   C CG  . LYS A 1 29  ? -19.252 19.269 -4.242  1.00 44.12 ? 5   LYS A CG  1 
ATOM   26   C CD  . LYS A 1 29  ? -19.970 17.978 -4.595  1.00 55.00 ? 5   LYS A CD  1 
ATOM   27   C CE  . LYS A 1 29  ? -19.358 16.832 -3.800  1.00 62.74 ? 5   LYS A CE  1 
ATOM   28   N NZ  . LYS A 1 29  ? -18.042 16.437 -4.419  1.00 40.38 ? 5   LYS A NZ  1 
ATOM   29   N N   . PRO A 1 30  ? -20.195 22.463 -7.526  1.00 29.82 ? 6   PRO A N   1 
ATOM   30   C CA  . PRO A 1 30  ? -19.829 23.692 -8.259  1.00 28.31 ? 6   PRO A CA  1 
ATOM   31   C C   . PRO A 1 30  ? -18.570 24.360 -7.738  1.00 22.23 ? 6   PRO A C   1 
ATOM   32   O O   . PRO A 1 30  ? -17.963 25.159 -8.465  1.00 24.07 ? 6   PRO A O   1 
ATOM   33   C CB  . PRO A 1 30  ? -21.052 24.607 -8.073  1.00 26.93 ? 6   PRO A CB  1 
ATOM   34   C CG  . PRO A 1 30  ? -22.017 23.871 -7.238  1.00 40.50 ? 6   PRO A CG  1 
ATOM   35   C CD  . PRO A 1 30  ? -21.610 22.442 -7.126  1.00 27.78 ? 6   PRO A CD  1 
ATOM   36   N N   . ASP A 1 31  ? -18.161 24.074 -6.505  1.00 22.95 ? 7   ASP A N   1 
ATOM   37   C CA  . ASP A 1 31  ? -16.934 24.624 -5.932  1.00 24.15 ? 7   ASP A CA  1 
ATOM   38   C C   . ASP A 1 31  ? -16.146 23.464 -5.350  1.00 24.65 ? 7   ASP A C   1 
ATOM   39   O O   . ASP A 1 31  ? -16.636 22.772 -4.450  1.00 26.49 ? 7   ASP A O   1 
ATOM   40   C CB  . ASP A 1 31  ? -17.238 25.663 -4.840  1.00 24.86 ? 7   ASP A CB  1 
ATOM   41   C CG  . ASP A 1 31  ? -17.858 26.935 -5.397  1.00 29.73 ? 7   ASP A CG  1 
ATOM   42   O OD1 . ASP A 1 31  ? -17.150 27.712 -6.071  1.00 30.55 ? 7   ASP A OD1 1 
ATOM   43   O OD2 . ASP A 1 31  ? -19.059 27.147 -5.180  1.00 32.89 ? 7   ASP A OD2 1 
ATOM   44   N N   . MET A 1 32  ? -14.943 23.244 -5.867  1.00 26.90 ? 8   MET A N   1 
ATOM   45   C CA  . MET A 1 32  ? -14.115 22.131 -5.443  1.00 24.39 ? 8   MET A CA  1 
ATOM   46   C C   . MET A 1 32  ? -12.759 22.647 -4.997  1.00 25.12 ? 8   MET A C   1 
ATOM   47   O O   . MET A 1 32  ? -12.245 23.635 -5.533  1.00 22.49 ? 8   MET A O   1 
ATOM   48   C CB  . MET A 1 32  ? -13.916 21.094 -6.571  1.00 19.49 ? 8   MET A CB  1 
ATOM   49   C CG  . MET A 1 32  ? -15.207 20.460 -7.051  1.00 25.35 ? 8   MET A CG  1 
ATOM   50   S SD  . MET A 1 32  ? -15.782 19.248 -5.849  1.00 33.14 ? 8   MET A SD  1 
ATOM   51   C CE  . MET A 1 32  ? -14.582 17.941 -6.085  1.00 27.62 ? 8   MET A CE  1 
ATOM   52   N N   . LYS A 1 33  ? -12.189 21.969 -4.008  1.00 22.36 ? 9   LYS A N   1 
ATOM   53   C CA  . LYS A 1 33  ? -10.805 22.191 -3.636  1.00 20.99 ? 9   LYS A CA  1 
ATOM   54   C C   . LYS A 1 33  ? -9.896  21.258 -4.422  1.00 24.50 ? 9   LYS A C   1 
ATOM   55   O O   . LYS A 1 33  ? -10.320 20.224 -4.950  1.00 22.27 ? 9   LYS A O   1 
ATOM   56   C CB  . LYS A 1 33  ? -10.604 21.975 -2.139  1.00 22.62 ? 9   LYS A CB  1 
ATOM   57   C CG  . LYS A 1 33  ? -11.502 22.845 -1.299  1.00 30.94 ? 9   LYS A CG  1 
ATOM   58   C CD  . LYS A 1 33  ? -11.619 22.274 0.106   1.00 37.43 ? 9   LYS A CD  1 
ATOM   59   C CE  . LYS A 1 33  ? -12.350 23.218 1.037   1.00 41.48 ? 9   LYS A CE  1 
ATOM   60   N NZ  . LYS A 1 33  ? -12.082 22.868 2.462   1.00 41.15 ? 9   LYS A NZ  1 
ATOM   61   N N   . ILE A 1 34  ? -8.625  21.638 -4.491  1.00 20.18 ? 10  ILE A N   1 
ATOM   62   C CA  . ILE A 1 34  ? -7.656  20.949 -5.329  1.00 21.08 ? 10  ILE A CA  1 
ATOM   63   C C   . ILE A 1 34  ? -6.366  20.832 -4.531  1.00 23.39 ? 10  ILE A C   1 
ATOM   64   O O   . ILE A 1 34  ? -5.831  21.842 -4.062  1.00 23.96 ? 10  ILE A O   1 
ATOM   65   C CB  . ILE A 1 34  ? -7.413  21.687 -6.659  1.00 23.06 ? 10  ILE A CB  1 
ATOM   66   C CG1 . ILE A 1 34  ? -8.748  22.078 -7.313  1.00 23.17 ? 10  ILE A CG1 1 
ATOM   67   C CG2 . ILE A 1 34  ? -6.581  20.831 -7.603  1.00 23.35 ? 10  ILE A CG2 1 
ATOM   68   C CD1 . ILE A 1 34  ? -8.637  23.167 -8.325  1.00 20.12 ? 10  ILE A CD1 1 
ATOM   69   N N   . LYS A 1 35  ? -5.892  19.607 -4.337  1.00 19.23 ? 11  LYS A N   1 
ATOM   70   C CA  . LYS A 1 35  ? -4.612  19.362 -3.691  1.00 23.23 ? 11  LYS A CA  1 
ATOM   71   C C   . LYS A 1 35  ? -3.715  18.613 -4.661  1.00 21.41 ? 11  LYS A C   1 
ATOM   72   O O   . LYS A 1 35  ? -4.168  17.688 -5.343  1.00 22.07 ? 11  LYS A O   1 
ATOM   73   C CB  . LYS A 1 35  ? -4.769  18.548 -2.424  1.00 20.51 ? 11  LYS A CB  1 
ATOM   74   C CG  . LYS A 1 35  ? -5.737  19.098 -1.394  1.00 35.11 ? 11  LYS A CG  1 
ATOM   75   C CD  . LYS A 1 35  ? -5.209  20.331 -0.690  1.00 34.15 ? 11  LYS A CD  1 
ATOM   76   C CE  . LYS A 1 35  ? -6.288  20.868 0.266   1.00 35.11 ? 11  LYS A CE  1 
ATOM   77   N NZ  . LYS A 1 35  ? -5.855  22.057 1.030   1.00 49.14 ? 11  LYS A NZ  1 
ATOM   78   N N   . LEU A 1 36  ? -2.439  18.985 -4.705  1.00 20.54 ? 12  LEU A N   1 
ATOM   79   C CA  . LEU A 1 36  ? -1.564  18.446 -5.737  1.00 18.56 ? 12  LEU A CA  1 
ATOM   80   C C   . LEU A 1 36  ? -0.147  18.280 -5.209  1.00 21.33 ? 12  LEU A C   1 
ATOM   81   O O   . LEU A 1 36  ? 0.357   19.134 -4.472  1.00 19.13 ? 12  LEU A O   1 
ATOM   82   C CB  . LEU A 1 36  ? -1.568  19.368 -6.964  1.00 19.19 ? 12  LEU A CB  1 
ATOM   83   C CG  . LEU A 1 36  ? -0.717  18.900 -8.148  1.00 23.63 ? 12  LEU A CG  1 
ATOM   84   C CD1 . LEU A 1 36  ? -1.391  19.295 -9.489  1.00 23.08 ? 12  LEU A CD1 1 
ATOM   85   C CD2 . LEU A 1 36  ? 0.705   19.460 -8.068  1.00 19.94 ? 12  LEU A CD2 1 
ATOM   86   N N   . ARG A 1 37  ? 0.500   17.187 -5.607  1.00 17.67 ? 13  ARG A N   1 
ATOM   87   C CA  . ARG A 1 37  ? 1.935   17.034 -5.393  1.00 18.09 ? 13  ARG A CA  1 
ATOM   88   C C   . ARG A 1 37  ? 2.578   16.632 -6.712  1.00 22.15 ? 13  ARG A C   1 
ATOM   89   O O   . ARG A 1 37  ? 2.104   15.703 -7.377  1.00 22.70 ? 13  ARG A O   1 
ATOM   90   C CB  . ARG A 1 37  ? 2.245   15.989 -4.312  1.00 21.51 ? 13  ARG A CB  1 
ATOM   91   C CG  . ARG A 1 37  ? 3.755   15.787 -4.015  1.00 26.41 ? 13  ARG A CG  1 
ATOM   92   C CD  . ARG A 1 37  ? 3.945   15.024 -2.690  1.00 26.08 ? 13  ARG A CD  1 
ATOM   93   N NE  . ARG A 1 37  ? 5.338   14.792 -2.309  1.00 30.79 ? 13  ARG A NE  1 
ATOM   94   C CZ  . ARG A 1 37  ? 6.143   13.942 -2.931  1.00 28.46 ? 13  ARG A CZ  1 
ATOM   95   N NH1 . ARG A 1 37  ? 5.741   13.269 -4.000  1.00 26.01 ? 13  ARG A NH1 1 
ATOM   96   N NH2 . ARG A 1 37  ? 7.370   13.744 -2.457  1.00 30.53 ? 13  ARG A NH2 1 
ATOM   97   N N   . MET A 1 38  ? 3.663   17.310 -7.075  1.00 15.74 ? 14  MET A N   1 
ATOM   98   C CA  . MET A 1 38  ? 4.434   16.959 -8.255  1.00 25.56 ? 14  MET A CA  1 
ATOM   99   C C   . MET A 1 38  ? 5.841   16.572 -7.837  1.00 21.89 ? 14  MET A C   1 
ATOM   100  O O   . MET A 1 38  ? 6.513   17.319 -7.118  1.00 22.46 ? 14  MET A O   1 
ATOM   101  C CB  . MET A 1 38  ? 4.471   18.113 -9.262  1.00 19.23 ? 14  MET A CB  1 
ATOM   102  C CG  . MET A 1 38  ? 5.228   17.781 -10.562 1.00 18.21 ? 14  MET A CG  1 
ATOM   103  S SD  . MET A 1 38  ? 5.784   19.250 -11.468 1.00 19.37 ? 14  MET A SD  1 
ATOM   104  C CE  . MET A 1 38  ? 4.491   19.201 -12.687 1.00 17.26 ? 14  MET A CE  1 
ATOM   105  N N   . GLU A 1 39  ? 6.275   15.402 -8.269  1.00 19.63 ? 15  GLU A N   1 
ATOM   106  C CA  . GLU A 1 39  ? 7.657   14.985 -8.120  1.00 22.95 ? 15  GLU A CA  1 
ATOM   107  C C   . GLU A 1 39  ? 8.259   14.922 -9.512  1.00 25.69 ? 15  GLU A C   1 
ATOM   108  O O   . GLU A 1 39  ? 7.688   14.298 -10.411 1.00 19.06 ? 15  GLU A O   1 
ATOM   109  C CB  . GLU A 1 39  ? 7.745   13.639 -7.411  1.00 22.07 ? 15  GLU A CB  1 
ATOM   110  C CG  . GLU A 1 39  ? 9.159   13.189 -7.193  1.00 31.20 ? 15  GLU A CG  1 
ATOM   111  C CD  . GLU A 1 39  ? 9.287   12.279 -6.008  1.00 43.67 ? 15  GLU A CD  1 
ATOM   112  O OE1 . GLU A 1 39  ? 8.290   11.593 -5.682  1.00 38.51 ? 15  GLU A OE1 1 
ATOM   113  O OE2 . GLU A 1 39  ? 10.400  12.212 -5.444  1.00 33.75 ? 15  GLU A OE2 1 
ATOM   114  N N   . GLY A 1 40  ? 9.384   15.600 -9.702  1.00 20.92 ? 16  GLY A N   1 
ATOM   115  C CA  . GLY A 1 40  ? 9.890   15.820 -11.035 1.00 23.89 ? 16  GLY A CA  1 
ATOM   116  C C   . GLY A 1 40  ? 11.390  15.635 -11.118 1.00 19.80 ? 16  GLY A C   1 
ATOM   117  O O   . GLY A 1 40  ? 12.109  15.669 -10.120 1.00 21.84 ? 16  GLY A O   1 
ATOM   118  N N   . ASN A 1 41  ? 11.848  15.462 -12.351 1.00 20.80 ? 17  ASN A N   1 
ATOM   119  C CA  . ASN A 1 41  ? 13.273  15.493 -12.643 1.00 19.53 ? 17  ASN A CA  1 
ATOM   120  C C   . ASN A 1 41  ? 13.455  16.026 -14.052 1.00 20.97 ? 17  ASN A C   1 
ATOM   121  O O   . ASN A 1 41  ? 12.997  15.395 -15.011 1.00 24.23 ? 17  ASN A O   1 
ATOM   122  C CB  . ASN A 1 41  ? 13.891  14.112 -12.529 1.00 22.92 ? 17  ASN A CB  1 
ATOM   123  C CG  . ASN A 1 41  ? 15.383  14.188 -12.425 1.00 34.91 ? 17  ASN A CG  1 
ATOM   124  O OD1 . ASN A 1 41  ? 16.065  14.259 -13.444 1.00 33.00 ? 17  ASN A OD1 1 
ATOM   125  N ND2 . ASN A 1 41  ? 15.911  14.135 -11.199 1.00 46.58 ? 17  ASN A ND2 1 
ATOM   126  N N   . VAL A 1 42  ? 14.143  17.159 -14.184 1.00 20.42 ? 18  VAL A N   1 
ATOM   127  C CA  . VAL A 1 42  ? 14.315  17.827 -15.468 1.00 19.38 ? 18  VAL A CA  1 
ATOM   128  C C   . VAL A 1 42  ? 15.804  18.067 -15.692 1.00 20.73 ? 18  VAL A C   1 
ATOM   129  O O   . VAL A 1 42  ? 16.463  18.725 -14.877 1.00 21.88 ? 18  VAL A O   1 
ATOM   130  C CB  . VAL A 1 42  ? 13.525  19.143 -15.530 1.00 19.06 ? 18  VAL A CB  1 
ATOM   131  C CG1 . VAL A 1 42  ? 13.874  19.896 -16.797 1.00 18.09 ? 18  VAL A CG1 1 
ATOM   132  C CG2 . VAL A 1 42  ? 12.022  18.848 -15.452 1.00 16.48 ? 18  VAL A CG2 1 
ATOM   133  N N   . ASN A 1 43  ? 16.333  17.525 -16.788 1.00 23.26 ? 19  ASN A N   1 
ATOM   134  C CA  . ASN A 1 43  ? 17.770  17.559 -17.075 1.00 21.97 ? 19  ASN A CA  1 
ATOM   135  C C   . ASN A 1 43  ? 18.585  17.113 -15.861 1.00 28.95 ? 19  ASN A C   1 
ATOM   136  O O   . ASN A 1 43  ? 19.630  17.682 -15.554 1.00 28.88 ? 19  ASN A O   1 
ATOM   137  C CB  . ASN A 1 43  ? 18.228  18.948 -17.530 1.00 25.92 ? 19  ASN A CB  1 
ATOM   138  C CG  . ASN A 1 43  ? 18.131  19.138 -19.030 1.00 28.94 ? 19  ASN A CG  1 
ATOM   139  O OD1 . ASN A 1 43  ? 17.273  18.549 -19.688 1.00 23.32 ? 19  ASN A OD1 1 
ATOM   140  N ND2 . ASN A 1 43  ? 19.030  19.951 -19.584 1.00 26.00 ? 19  ASN A ND2 1 
ATOM   141  N N   . GLY A 1 44  ? 18.083  16.109 -15.138 1.00 23.00 ? 20  GLY A N   1 
ATOM   142  C CA  . GLY A 1 44  ? 18.804  15.579 -13.998 1.00 30.57 ? 20  GLY A CA  1 
ATOM   143  C C   . GLY A 1 44  ? 18.558  16.293 -12.685 1.00 27.02 ? 20  GLY A C   1 
ATOM   144  O O   . GLY A 1 44  ? 19.076  15.851 -11.657 1.00 32.61 ? 20  GLY A O   1 
ATOM   145  N N   . HIS A 1 45  ? 17.756  17.355 -12.669 1.00 28.45 ? 21  HIS A N   1 
ATOM   146  C CA  . HIS A 1 45  ? 17.525  18.113 -11.447 1.00 28.34 ? 21  HIS A CA  1 
ATOM   147  C C   . HIS A 1 45  ? 16.204  17.667 -10.821 1.00 28.74 ? 21  HIS A C   1 
ATOM   148  O O   . HIS A 1 45  ? 15.139  17.856 -11.420 1.00 25.88 ? 21  HIS A O   1 
ATOM   149  C CB  . HIS A 1 45  ? 17.523  19.618 -11.725 1.00 26.54 ? 21  HIS A CB  1 
ATOM   150  C CG  . HIS A 1 45  ? 17.276  20.443 -10.502 1.00 37.98 ? 21  HIS A CG  1 
ATOM   151  N ND1 . HIS A 1 45  ? 18.299  21.055 -9.809  1.00 36.34 ? 21  HIS A ND1 1 
ATOM   152  C CD2 . HIS A 1 45  ? 16.133  20.757 -9.844  1.00 35.83 ? 21  HIS A CD2 1 
ATOM   153  C CE1 . HIS A 1 45  ? 17.798  21.701 -8.770  1.00 38.93 ? 21  HIS A CE1 1 
ATOM   154  N NE2 . HIS A 1 45  ? 16.486  21.539 -8.770  1.00 33.77 ? 21  HIS A NE2 1 
ATOM   155  N N   . HIS A 1 46  ? 16.278  17.088 -9.616  1.00 23.90 ? 22  HIS A N   1 
ATOM   156  C CA  . HIS A 1 46  ? 15.094  16.595 -8.920  1.00 26.32 ? 22  HIS A CA  1 
ATOM   157  C C   . HIS A 1 46  ? 14.395  17.719 -8.162  1.00 28.55 ? 22  HIS A C   1 
ATOM   158  O O   . HIS A 1 46  ? 15.040  18.613 -7.603  1.00 28.73 ? 22  HIS A O   1 
ATOM   159  C CB  . HIS A 1 46  ? 15.470  15.475 -7.941  1.00 29.56 ? 22  HIS A CB  1 
ATOM   160  C CG  . HIS A 1 46  ? 14.335  15.036 -7.062  1.00 43.45 ? 22  HIS A CG  1 
ATOM   161  N ND1 . HIS A 1 46  ? 14.102  15.575 -5.813  1.00 40.04 ? 22  HIS A ND1 1 
ATOM   162  C CD2 . HIS A 1 46  ? 13.356  14.119 -7.263  1.00 47.59 ? 22  HIS A CD2 1 
ATOM   163  C CE1 . HIS A 1 46  ? 13.034  15.005 -5.282  1.00 43.86 ? 22  HIS A CE1 1 
ATOM   164  N NE2 . HIS A 1 46  ? 12.561  14.118 -6.141  1.00 40.91 ? 22  HIS A NE2 1 
ATOM   165  N N   . PHE A 1 47  ? 13.063  17.653 -8.118  1.00 22.32 ? 23  PHE A N   1 
ATOM   166  C CA  . PHE A 1 47  ? 12.288  18.663 -7.405  1.00 23.05 ? 23  PHE A CA  1 
ATOM   167  C C   . PHE A 1 47  ? 10.951  18.082 -6.968  1.00 22.34 ? 23  PHE A C   1 
ATOM   168  O O   . PHE A 1 47  ? 10.491  17.056 -7.482  1.00 20.05 ? 23  PHE A O   1 
ATOM   169  C CB  . PHE A 1 47  ? 12.081  19.927 -8.256  1.00 20.58 ? 23  PHE A CB  1 
ATOM   170  C CG  . PHE A 1 47  ? 11.423  19.667 -9.598  1.00 18.44 ? 23  PHE A CG  1 
ATOM   171  C CD1 . PHE A 1 47  ? 12.191  19.295 -10.689 1.00 24.02 ? 23  PHE A CD1 1 
ATOM   172  C CD2 . PHE A 1 47  ? 10.053  19.812 -9.763  1.00 23.99 ? 23  PHE A CD2 1 
ATOM   173  C CE1 . PHE A 1 47  ? 11.605  19.040 -11.925 1.00 19.05 ? 23  PHE A CE1 1 
ATOM   174  C CE2 . PHE A 1 47  ? 9.454   19.567 -10.990 1.00 26.00 ? 23  PHE A CE2 1 
ATOM   175  C CZ  . PHE A 1 47  ? 10.236  19.194 -12.082 1.00 19.43 ? 23  PHE A CZ  1 
ATOM   176  N N   . VAL A 1 48  ? 10.346  18.751 -5.982  1.00 21.72 ? 24  VAL A N   1 
ATOM   177  C CA  . VAL A 1 48  ? 9.000   18.446 -5.500  1.00 24.04 ? 24  VAL A CA  1 
ATOM   178  C C   . VAL A 1 48  ? 8.253   19.761 -5.335  1.00 20.77 ? 24  VAL A C   1 
ATOM   179  O O   . VAL A 1 48  ? 8.783   20.710 -4.749  1.00 22.25 ? 24  VAL A O   1 
ATOM   180  C CB  . VAL A 1 48  ? 9.009   17.684 -4.157  1.00 22.89 ? 24  VAL A CB  1 
ATOM   181  C CG1 . VAL A 1 48  ? 7.567   17.454 -3.667  1.00 27.65 ? 24  VAL A CG1 1 
ATOM   182  C CG2 . VAL A 1 48  ? 9.757   16.363 -4.274  1.00 22.38 ? 24  VAL A CG2 1 
ATOM   183  N N   . ILE A 1 49  ? 7.016   19.814 -5.821  1.00 18.38 ? 25  ILE A N   1 
ATOM   184  C CA  . ILE A 1 49  ? 6.178   21.007 -5.758  1.00 17.07 ? 25  ILE A CA  1 
ATOM   185  C C   . ILE A 1 49  ? 4.816   20.593 -5.214  1.00 23.25 ? 25  ILE A C   1 
ATOM   186  O O   . ILE A 1 49  ? 4.225   19.629 -5.708  1.00 21.53 ? 25  ILE A O   1 
ATOM   187  C CB  . ILE A 1 49  ? 6.042   21.651 -7.154  1.00 18.88 ? 25  ILE A CB  1 
ATOM   188  C CG1 . ILE A 1 49  ? 7.418   22.099 -7.664  1.00 17.53 ? 25  ILE A CG1 1 
ATOM   189  C CG2 . ILE A 1 49  ? 5.028   22.810 -7.155  1.00 19.57 ? 25  ILE A CG2 1 
ATOM   190  C CD1 . ILE A 1 49  ? 7.384   22.566 -9.124  1.00 16.10 ? 25  ILE A CD1 1 
ATOM   191  N N   . ASP A 1 50  ? 4.331   21.302 -4.191  1.00 18.33 ? 26  ASP A N   1 
ATOM   192  C CA  . ASP A 1 50  ? 2.997   21.074 -3.633  1.00 17.20 ? 26  ASP A CA  1 
ATOM   193  C C   . ASP A 1 50  ? 2.050   22.148 -4.146  1.00 21.06 ? 26  ASP A C   1 
ATOM   194  O O   . ASP A 1 50  ? 2.454   23.303 -4.328  1.00 20.02 ? 26  ASP A O   1 
ATOM   195  C CB  . ASP A 1 50  ? 3.011   21.100 -2.098  1.00 19.28 ? 26  ASP A CB  1 
ATOM   196  C CG  . ASP A 1 50  ? 3.650   19.850 -1.491  1.00 25.73 ? 26  ASP A CG  1 
ATOM   197  O OD1 . ASP A 1 50  ? 3.886   18.873 -2.230  1.00 30.16 ? 26  ASP A OD1 1 
ATOM   198  O OD2 . ASP A 1 50  ? 3.920   19.853 -0.275  1.00 29.36 ? 26  ASP A OD2 1 
ATOM   199  N N   . GLY A 1 51  ? 0.793   21.775 -4.362  1.00 20.49 ? 27  GLY A N   1 
ATOM   200  C CA  . GLY A 1 51  ? -0.209  22.720 -4.831  1.00 20.15 ? 27  GLY A CA  1 
ATOM   201  C C   . GLY A 1 51  ? -1.465  22.683 -3.990  1.00 23.15 ? 27  GLY A C   1 
ATOM   202  O O   . GLY A 1 51  ? -1.882  21.622 -3.520  1.00 18.03 ? 27  GLY A O   1 
ATOM   203  N N   . ASP A 1 52  ? -2.060  23.860 -3.789  1.00 21.39 ? 28  ASP A N   1 
ATOM   204  C CA  . ASP A 1 52  ? -3.308  23.969 -3.042  1.00 22.52 ? 28  ASP A CA  1 
ATOM   205  C C   . ASP A 1 52  ? -4.147  24.990 -3.802  1.00 25.58 ? 28  ASP A C   1 
ATOM   206  O O   . ASP A 1 52  ? -3.705  26.125 -4.010  1.00 21.69 ? 28  ASP A O   1 
ATOM   207  C CB  . ASP A 1 52  ? -3.024  24.395 -1.585  1.00 23.90 ? 28  ASP A CB  1 
ATOM   208  C CG  . ASP A 1 52  ? -4.279  24.660 -0.762  1.00 39.65 ? 28  ASP A CG  1 
ATOM   209  O OD1 . ASP A 1 52  ? -5.320  25.109 -1.271  1.00 38.15 ? 28  ASP A OD1 1 
ATOM   210  O OD2 . ASP A 1 52  ? -4.207  24.405 0.452   1.00 56.79 ? 28  ASP A OD2 1 
ATOM   211  N N   . GLY A 1 53  ? -5.341  24.592 -4.248  1.00 23.54 ? 29  GLY A N   1 
ATOM   212  C CA  . GLY A 1 53  ? -6.123  25.475 -5.087  1.00 23.44 ? 29  GLY A CA  1 
ATOM   213  C C   . GLY A 1 53  ? -7.613  25.243 -4.957  1.00 18.30 ? 29  GLY A C   1 
ATOM   214  O O   . GLY A 1 53  ? -8.069  24.430 -4.155  1.00 17.67 ? 29  GLY A O   1 
ATOM   215  N N   . THR A 1 54  ? -8.377  25.988 -5.758  1.00 18.13 ? 30  THR A N   1 
ATOM   216  C CA  . THR A 1 54  ? -9.827  25.868 -5.796  1.00 20.67 ? 30  THR A CA  1 
ATOM   217  C C   . THR A 1 54  ? -10.278 26.089 -7.231  1.00 21.63 ? 30  THR A C   1 
ATOM   218  O O   . THR A 1 54  ? -9.580  26.719 -8.032  1.00 20.32 ? 30  THR A O   1 
ATOM   219  C CB  . THR A 1 54  ? -10.529 26.900 -4.901  1.00 22.19 ? 30  THR A CB  1 
ATOM   220  O OG1 . THR A 1 54  ? -10.103 28.204 -5.303  1.00 26.08 ? 30  THR A OG1 1 
ATOM   221  C CG2 . THR A 1 54  ? -10.210 26.687 -3.405  1.00 23.03 ? 30  THR A CG2 1 
ATOM   222  N N   . GLY A 1 55  ? -11.481 25.615 -7.542  1.00 18.71 ? 31  GLY A N   1 
ATOM   223  C CA  . GLY A 1 55  ? -11.980 25.910 -8.874  1.00 19.71 ? 31  GLY A CA  1 
ATOM   224  C C   . GLY A 1 55  ? -13.463 25.655 -8.998  1.00 17.26 ? 31  GLY A C   1 
ATOM   225  O O   . GLY A 1 55  ? -14.110 25.107 -8.104  1.00 20.02 ? 31  GLY A O   1 
ATOM   226  N N   . LYS A 1 56  ? -13.992 26.058 -10.148 1.00 17.32 ? 32  LYS A N   1 
ATOM   227  C CA  . LYS A 1 56  ? -15.403 25.873 -10.490 1.00 18.78 ? 32  LYS A CA  1 
ATOM   228  C C   . LYS A 1 56  ? -15.484 24.952 -11.693 1.00 20.76 ? 32  LYS A C   1 
ATOM   229  O O   . LYS A 1 56  ? -15.290 25.403 -12.838 1.00 19.12 ? 32  LYS A O   1 
ATOM   230  C CB  . LYS A 1 56  ? -16.062 27.211 -10.796 1.00 22.46 ? 32  LYS A CB  1 
ATOM   231  C CG  . LYS A 1 56  ? -16.230 28.066 -9.579  1.00 29.85 ? 32  LYS A CG  1 
ATOM   232  C CD  . LYS A 1 56  ? -17.249 29.134 -9.862  1.00 35.40 ? 32  LYS A CD  1 
ATOM   233  C CE  . LYS A 1 56  ? -17.388 30.021 -8.690  1.00 35.98 ? 32  LYS A CE  1 
ATOM   234  N NZ  . LYS A 1 56  ? -18.298 29.438 -7.656  1.00 29.24 ? 32  LYS A NZ  1 
ATOM   235  N N   . PRO A 1 57  ? -15.721 23.656 -11.489 1.00 19.07 ? 33  PRO A N   1 
ATOM   236  C CA  . PRO A 1 57  ? -15.661 22.716 -12.626 1.00 17.85 ? 33  PRO A CA  1 
ATOM   237  C C   . PRO A 1 57  ? -16.605 23.064 -13.769 1.00 19.99 ? 33  PRO A C   1 
ATOM   238  O O   . PRO A 1 57  ? -16.245 22.875 -14.941 1.00 19.65 ? 33  PRO A O   1 
ATOM   239  C CB  . PRO A 1 57  ? -16.017 21.373 -11.970 1.00 17.39 ? 33  PRO A CB  1 
ATOM   240  C CG  . PRO A 1 57  ? -15.585 21.545 -10.555 1.00 18.37 ? 33  PRO A CG  1 
ATOM   241  C CD  . PRO A 1 57  ? -15.909 22.957 -10.208 1.00 18.84 ? 33  PRO A CD  1 
ATOM   242  N N   . PHE A 1 58  ? -17.791 23.604 -13.474 1.00 20.55 ? 34  PHE A N   1 
ATOM   243  C CA  . PHE A 1 58  ? -18.766 23.824 -14.535 1.00 18.88 ? 34  PHE A CA  1 
ATOM   244  C C   . PHE A 1 58  ? -18.558 25.144 -15.263 1.00 23.10 ? 34  PHE A C   1 
ATOM   245  O O   . PHE A 1 58  ? -19.181 25.358 -16.314 1.00 22.41 ? 34  PHE A O   1 
ATOM   246  C CB  . PHE A 1 58  ? -20.186 23.729 -13.964 1.00 22.67 ? 34  PHE A CB  1 
ATOM   247  C CG  . PHE A 1 58  ? -20.463 22.408 -13.318 1.00 24.87 ? 34  PHE A CG  1 
ATOM   248  C CD1 . PHE A 1 58  ? -20.811 21.315 -14.085 1.00 22.14 ? 34  PHE A CD1 1 
ATOM   249  C CD2 . PHE A 1 58  ? -20.323 22.251 -11.945 1.00 32.42 ? 34  PHE A CD2 1 
ATOM   250  C CE1 . PHE A 1 58  ? -21.033 20.085 -13.498 1.00 34.91 ? 34  PHE A CE1 1 
ATOM   251  C CE2 . PHE A 1 58  ? -20.541 21.030 -11.347 1.00 30.03 ? 34  PHE A CE2 1 
ATOM   252  C CZ  . PHE A 1 58  ? -20.898 19.939 -12.127 1.00 30.41 ? 34  PHE A CZ  1 
ATOM   253  N N   . GLU A 1 59  ? -17.697 26.021 -14.741 1.00 19.35 ? 35  GLU A N   1 
ATOM   254  C CA  . GLU A 1 59  ? -17.251 27.205 -15.460 1.00 17.79 ? 35  GLU A CA  1 
ATOM   255  C C   . GLU A 1 59  ? -15.920 26.980 -16.158 1.00 18.71 ? 35  GLU A C   1 
ATOM   256  O O   . GLU A 1 59  ? -15.474 27.858 -16.903 1.00 22.05 ? 35  GLU A O   1 
ATOM   257  C CB  . GLU A 1 59  ? -17.109 28.410 -14.512 1.00 20.30 ? 35  GLU A CB  1 
ATOM   258  C CG  . GLU A 1 59  ? -18.434 28.897 -13.918 1.00 23.64 ? 35  GLU A CG  1 
ATOM   259  C CD  . GLU A 1 59  ? -18.341 30.274 -13.251 1.00 29.79 ? 35  GLU A CD  1 
ATOM   260  O OE1 . GLU A 1 59  ? -17.243 30.861 -13.194 1.00 32.15 ? 35  GLU A OE1 1 
ATOM   261  O OE2 . GLU A 1 59  ? -19.380 30.767 -12.755 1.00 29.75 ? 35  GLU A OE2 1 
ATOM   262  N N   . GLY A 1 60  ? -15.289 25.830 -15.947 1.00 17.46 ? 36  GLY A N   1 
ATOM   263  C CA  . GLY A 1 60  ? -13.966 25.592 -16.514 1.00 18.58 ? 36  GLY A CA  1 
ATOM   264  C C   . GLY A 1 60  ? -12.878 26.520 -16.013 1.00 20.66 ? 36  GLY A C   1 
ATOM   265  O O   . GLY A 1 60  ? -11.964 26.869 -16.777 1.00 17.16 ? 36  GLY A O   1 
ATOM   266  N N   . LYS A 1 61  ? -12.921 26.895 -14.730 1.00 16.91 ? 37  LYS A N   1 
ATOM   267  C CA  . LYS A 1 61  ? -11.937 27.808 -14.158 1.00 16.87 ? 37  LYS A CA  1 
ATOM   268  C C   . LYS A 1 61  ? -11.295 27.209 -12.912 1.00 18.75 ? 37  LYS A C   1 
ATOM   269  O O   . LYS A 1 61  ? -11.984 26.609 -12.088 1.00 17.77 ? 37  LYS A O   1 
ATOM   270  C CB  . LYS A 1 61  ? -12.585 29.150 -13.773 1.00 15.47 ? 37  LYS A CB  1 
ATOM   271  C CG  . LYS A 1 61  ? -13.128 29.908 -14.985 1.00 19.56 ? 37  LYS A CG  1 
ATOM   272  C CD  . LYS A 1 61  ? -13.737 31.265 -14.627 1.00 19.78 ? 37  LYS A CD  1 
ATOM   273  C CE  . LYS A 1 61  ? -13.943 32.084 -15.891 1.00 20.60 ? 37  LYS A CE  1 
ATOM   274  N NZ  . LYS A 1 61  ? -14.288 33.498 -15.627 1.00 21.09 ? 37  LYS A NZ  1 
ATOM   275  N N   . GLN A 1 62  ? -9.989  27.418 -12.742 1.00 13.15 ? 38  GLN A N   1 
ATOM   276  C CA  . GLN A 1 62  ? -9.337  26.946 -11.523 1.00 16.44 ? 38  GLN A CA  1 
ATOM   277  C C   . GLN A 1 62  ? -8.091  27.771 -11.264 1.00 19.64 ? 38  GLN A C   1 
ATOM   278  O O   . GLN A 1 62  ? -7.461  28.279 -12.195 1.00 15.50 ? 38  GLN A O   1 
ATOM   279  C CB  . GLN A 1 62  ? -8.971  25.452 -11.606 1.00 17.08 ? 38  GLN A CB  1 
ATOM   280  C CG  . GLN A 1 62  ? -7.927  25.142 -12.681 1.00 16.45 ? 38  GLN A CG  1 
ATOM   281  C CD  . GLN A 1 62  ? -7.480  23.698 -12.673 1.00 19.25 ? 38  GLN A CD  1 
ATOM   282  O OE1 . GLN A 1 62  ? -7.151  23.137 -11.622 1.00 15.46 ? 38  GLN A OE1 1 
ATOM   283  N NE2 . GLN A 1 62  ? -7.449  23.089 -13.849 1.00 16.85 ? 38  GLN A NE2 1 
ATOM   284  N N   . SER A 1 63  ? -7.751  27.901 -9.978  1.00 19.65 ? 39  SER A N   1 
ATOM   285  C CA  A SER A 1 63  ? -6.538  28.580 -9.556  0.27 19.88 ? 39  SER A CA  1 
ATOM   286  C CA  B SER A 1 63  ? -6.564  28.609 -9.508  0.73 19.83 ? 39  SER A CA  1 
ATOM   287  C C   . SER A 1 63  ? -5.808  27.732 -8.520  1.00 23.71 ? 39  SER A C   1 
ATOM   288  O O   . SER A 1 63  ? -6.413  26.960 -7.773  1.00 22.67 ? 39  SER A O   1 
ATOM   289  C CB  A SER A 1 63  ? -6.857  29.988 -9.010  0.27 24.65 ? 39  SER A CB  1 
ATOM   290  C CB  B SER A 1 63  ? -6.916  29.936 -8.799  0.73 24.96 ? 39  SER A CB  1 
ATOM   291  O OG  A SER A 1 63  ? -7.337  29.943 -7.679  0.27 24.83 ? 39  SER A OG  1 
ATOM   292  O OG  B SER A 1 63  ? -7.377  30.918 -9.695  0.73 22.35 ? 39  SER A OG  1 
ATOM   293  N N   . MET A 1 64  ? -4.484  27.869 -8.495  1.00 19.38 ? 40  MET A N   1 
ATOM   294  C CA  . MET A 1 64  ? -3.655  27.058 -7.608  1.00 18.74 ? 40  MET A CA  1 
ATOM   295  C C   . MET A 1 64  ? -2.496  27.879 -7.074  1.00 23.29 ? 40  MET A C   1 
ATOM   296  O O   . MET A 1 64  ? -1.845  28.594 -7.843  1.00 21.76 ? 40  MET A O   1 
ATOM   297  C CB  . MET A 1 64  ? -3.060  25.857 -8.342  1.00 20.41 ? 40  MET A CB  1 
ATOM   298  C CG  . MET A 1 64  ? -2.277  24.929 -7.449  1.00 21.72 ? 40  MET A CG  1 
ATOM   299  S SD  . MET A 1 64  ? -2.088  23.294 -8.152  1.00 21.58 ? 40  MET A SD  1 
ATOM   300  C CE  . MET A 1 64  ? -3.770  22.705 -8.118  1.00 28.07 ? 40  MET A CE  1 
ATOM   301  N N   . ASP A 1 65  ? -2.215  27.737 -5.774  1.00 19.61 ? 41  ASP A N   1 
ATOM   302  C CA  . ASP A 1 65  ? -0.968  28.215 -5.179  1.00 22.58 ? 41  ASP A CA  1 
ATOM   303  C C   . ASP A 1 65  ? 0.046   27.079 -5.143  1.00 22.91 ? 41  ASP A C   1 
ATOM   304  O O   . ASP A 1 65  ? -0.237  26.000 -4.609  1.00 21.76 ? 41  ASP A O   1 
ATOM   305  C CB  . ASP A 1 65  ? -1.192  28.746 -3.764  1.00 24.25 ? 41  ASP A CB  1 
ATOM   306  C CG  . ASP A 1 65  ? -2.137  29.927 -3.728  1.00 37.86 ? 41  ASP A CG  1 
ATOM   307  O OD1 . ASP A 1 65  ? -1.865  30.923 -4.436  1.00 37.95 ? 41  ASP A OD1 1 
ATOM   308  O OD2 . ASP A 1 65  ? -3.140  29.869 -2.991  1.00 36.27 ? 41  ASP A OD2 1 
ATOM   309  N N   . LEU A 1 66  ? 1.235   27.336 -5.675  1.00 21.17 ? 42  LEU A N   1 
ATOM   310  C CA  . LEU A 1 66  ? 2.257   26.317 -5.842  1.00 19.68 ? 42  LEU A CA  1 
ATOM   311  C C   . LEU A 1 66  ? 3.495   26.721 -5.064  1.00 18.76 ? 42  LEU A C   1 
ATOM   312  O O   . LEU A 1 66  ? 3.823   27.909 -4.978  1.00 20.23 ? 42  LEU A O   1 
ATOM   313  C CB  . LEU A 1 66  ? 2.613   26.136 -7.323  1.00 20.01 ? 42  LEU A CB  1 
ATOM   314  C CG  . LEU A 1 66  ? 1.474   25.626 -8.205  1.00 15.04 ? 42  LEU A CG  1 
ATOM   315  C CD1 . LEU A 1 66  ? 1.702   26.036 -9.646  1.00 19.56 ? 42  LEU A CD1 1 
ATOM   316  C CD2 . LEU A 1 66  ? 1.310   24.099 -8.084  1.00 18.01 ? 42  LEU A CD2 1 
ATOM   317  N N   . GLU A 1 67  ? 4.177   25.737 -4.484  1.00 20.03 ? 43  GLU A N   1 
ATOM   318  C CA  . GLU A 1 67  ? 5.359   26.013 -3.680  1.00 24.11 ? 43  GLU A CA  1 
ATOM   319  C C   . GLU A 1 67  ? 6.367   24.906 -3.920  1.00 28.44 ? 43  GLU A C   1 
ATOM   320  O O   . GLU A 1 67  ? 6.049   23.729 -3.730  1.00 21.57 ? 43  GLU A O   1 
ATOM   321  C CB  . GLU A 1 67  ? 5.014   26.121 -2.191  1.00 23.02 ? 43  GLU A CB  1 
ATOM   322  C CG  . GLU A 1 67  ? 6.249   26.341 -1.314  1.00 36.84 ? 43  GLU A CG  1 
ATOM   323  C CD  . GLU A 1 67  ? 5.900   26.753 0.103   1.00 38.94 ? 43  GLU A CD  1 
ATOM   324  O OE1 . GLU A 1 67  ? 4.715   27.050 0.375   1.00 49.08 ? 43  GLU A OE1 1 
ATOM   325  O OE2 . GLU A 1 67  ? 6.821   26.784 0.943   1.00 42.69 ? 43  GLU A OE2 1 
ATOM   326  N N   . VAL A 1 68  ? 7.572   25.285 -4.341  1.00 23.40 ? 44  VAL A N   1 
ATOM   327  C CA  . VAL A 1 68  ? 8.667   24.334 -4.498  1.00 27.74 ? 44  VAL A CA  1 
ATOM   328  C C   . VAL A 1 68  ? 9.144   23.916 -3.111  1.00 26.65 ? 44  VAL A C   1 
ATOM   329  O O   . VAL A 1 68  ? 9.620   24.747 -2.330  1.00 26.15 ? 44  VAL A O   1 
ATOM   330  C CB  . VAL A 1 68  ? 9.807   24.950 -5.321  1.00 25.44 ? 44  VAL A CB  1 
ATOM   331  C CG1 . VAL A 1 68  ? 10.946  23.957 -5.492  1.00 27.99 ? 44  VAL A CG1 1 
ATOM   332  C CG2 . VAL A 1 68  ? 9.288   25.441 -6.679  1.00 21.35 ? 44  VAL A CG2 1 
ATOM   333  N N   . LYS A 1 69  ? 9.001   22.628 -2.793  1.00 21.25 ? 45  LYS A N   1 
ATOM   334  C CA  . LYS A 1 69  ? 9.346   22.082 -1.479  1.00 23.81 ? 45  LYS A CA  1 
ATOM   335  C C   . LYS A 1 69  ? 10.732  21.466 -1.440  1.00 24.39 ? 45  LYS A C   1 
ATOM   336  O O   . LYS A 1 69  ? 11.354  21.402 -0.372  1.00 30.35 ? 45  LYS A O   1 
ATOM   337  C CB  . LYS A 1 69  ? 8.331   21.009 -1.065  1.00 28.60 ? 45  LYS A CB  1 
ATOM   338  C CG  . LYS A 1 69  ? 6.886   21.470 -0.981  1.00 26.14 ? 45  LYS A CG  1 
ATOM   339  C CD  . LYS A 1 69  ? 6.753   22.824 -0.284  1.00 33.03 ? 45  LYS A CD  1 
ATOM   340  C CE  . LYS A 1 69  ? 7.006   22.703 1.189   1.00 40.58 ? 45  LYS A CE  1 
ATOM   341  N NZ  . LYS A 1 69  ? 6.584   23.927 1.943   1.00 60.92 ? 45  LYS A NZ  1 
ATOM   342  N N   . GLU A 1 70  ? 11.211  21.001 -2.583  1.00 23.91 ? 46  GLU A N   1 
ATOM   343  C CA  . GLU A 1 70  ? 12.505  20.361 -2.720  1.00 28.52 ? 46  GLU A CA  1 
ATOM   344  C C   . GLU A 1 70  ? 13.093  20.761 -4.060  1.00 24.71 ? 46  GLU A C   1 
ATOM   345  O O   . GLU A 1 70  ? 12.378  20.804 -5.066  1.00 22.30 ? 46  GLU A O   1 
ATOM   346  C CB  . GLU A 1 70  ? 12.381  18.839 -2.651  1.00 28.97 ? 46  GLU A CB  1 
ATOM   347  C CG  . GLU A 1 70  ? 11.792  18.338 -1.365  1.00 36.82 ? 46  GLU A CG  1 
ATOM   348  C CD  . GLU A 1 70  ? 11.743  16.837 -1.313  1.00 38.44 ? 46  GLU A CD  1 
ATOM   349  O OE1 . GLU A 1 70  ? 12.685  16.200 -1.834  1.00 46.88 ? 46  GLU A OE1 1 
ATOM   350  O OE2 . GLU A 1 70  ? 10.759  16.307 -0.755  1.00 39.50 ? 46  GLU A OE2 1 
ATOM   351  N N   . GLY A 1 71  ? 14.397  21.046 -4.071  1.00 29.30 ? 47  GLY A N   1 
ATOM   352  C CA  . GLY A 1 71  ? 15.075  21.336 -5.320  1.00 32.73 ? 47  GLY A CA  1 
ATOM   353  C C   . GLY A 1 71  ? 14.965  22.759 -5.817  1.00 33.62 ? 47  GLY A C   1 
ATOM   354  O O   . GLY A 1 71  ? 15.284  23.023 -6.983  1.00 31.73 ? 47  GLY A O   1 
ATOM   355  N N   . GLY A 1 72  ? 14.519  23.686 -4.974  1.00 29.33 ? 48  GLY A N   1 
ATOM   356  C CA  . GLY A 1 72  ? 14.540  25.088 -5.310  1.00 29.24 ? 48  GLY A CA  1 
ATOM   357  C C   . GLY A 1 72  ? 15.909  25.687 -5.060  1.00 34.56 ? 48  GLY A C   1 
ATOM   358  O O   . GLY A 1 72  ? 16.665  25.225 -4.200  1.00 31.00 ? 48  GLY A O   1 
ATOM   359  N N   . PRO A 1 73  ? 16.266  26.731 -5.821  1.00 27.80 ? 49  PRO A N   1 
ATOM   360  C CA  . PRO A 1 73  ? 15.505  27.351 -6.909  1.00 26.16 ? 49  PRO A CA  1 
ATOM   361  C C   . PRO A 1 73  ? 15.614  26.534 -8.193  1.00 29.62 ? 49  PRO A C   1 
ATOM   362  O O   . PRO A 1 73  ? 16.684  26.031 -8.517  1.00 22.35 ? 49  PRO A O   1 
ATOM   363  C CB  . PRO A 1 73  ? 16.155  28.739 -7.026  1.00 26.05 ? 49  PRO A CB  1 
ATOM   364  C CG  . PRO A 1 73  ? 17.580  28.493 -6.648  1.00 30.82 ? 49  PRO A CG  1 
ATOM   365  C CD  . PRO A 1 73  ? 17.519  27.460 -5.546  1.00 34.29 ? 49  PRO A CD  1 
ATOM   366  N N   . LEU A 1 74  ? 14.521  26.377 -8.935  1.00 24.94 ? 50  LEU A N   1 
ATOM   367  C CA  . LEU A 1 74  ? 14.567  25.559 -10.140 1.00 23.28 ? 50  LEU A CA  1 
ATOM   368  C C   . LEU A 1 74  ? 15.450  26.228 -11.190 1.00 24.66 ? 50  LEU A C   1 
ATOM   369  O O   . LEU A 1 74  ? 15.358  27.441 -11.397 1.00 23.65 ? 50  LEU A O   1 
ATOM   370  C CB  . LEU A 1 74  ? 13.161  25.354 -10.710 1.00 20.64 ? 50  LEU A CB  1 
ATOM   371  C CG  . LEU A 1 74  ? 12.129  24.675 -9.795  1.00 22.95 ? 50  LEU A CG  1 
ATOM   372  C CD1 . LEU A 1 74  ? 10.781  24.666 -10.482 1.00 21.83 ? 50  LEU A CD1 1 
ATOM   373  C CD2 . LEU A 1 74  ? 12.542  23.253 -9.418  1.00 22.86 ? 50  LEU A CD2 1 
ATOM   374  N N   . PRO A 1 75  ? 16.316  25.464 -11.868 1.00 23.26 ? 51  PRO A N   1 
ATOM   375  C CA  . PRO A 1 75  ? 17.203  26.073 -12.866 1.00 25.20 ? 51  PRO A CA  1 
ATOM   376  C C   . PRO A 1 75  ? 16.606  26.059 -14.273 1.00 24.57 ? 51  PRO A C   1 
ATOM   377  O O   . PRO A 1 75  ? 17.334  26.233 -15.257 1.00 28.05 ? 51  PRO A O   1 
ATOM   378  C CB  . PRO A 1 75  ? 18.453  25.194 -12.772 1.00 26.70 ? 51  PRO A CB  1 
ATOM   379  C CG  . PRO A 1 75  ? 17.852  23.823 -12.550 1.00 24.67 ? 51  PRO A CG  1 
ATOM   380  C CD  . PRO A 1 75  ? 16.693  24.064 -11.590 1.00 25.71 ? 51  PRO A CD  1 
ATOM   381  N N   . PHE A 1 76  ? 15.289  25.869 -14.386 1.00 23.43 ? 52  PHE A N   1 
ATOM   382  C CA  . PHE A 1 76  ? 14.626  25.831 -15.684 1.00 21.28 ? 52  PHE A CA  1 
ATOM   383  C C   . PHE A 1 76  ? 13.317  26.615 -15.621 1.00 28.54 ? 52  PHE A C   1 
ATOM   384  O O   . PHE A 1 76  ? 12.775  26.879 -14.541 1.00 19.24 ? 52  PHE A O   1 
ATOM   385  C CB  . PHE A 1 76  ? 14.358  24.383 -16.128 1.00 19.40 ? 52  PHE A CB  1 
ATOM   386  C CG  . PHE A 1 76  ? 13.488  23.610 -15.173 1.00 19.44 ? 52  PHE A CG  1 
ATOM   387  C CD1 . PHE A 1 76  ? 12.100  23.746 -15.195 1.00 20.96 ? 52  PHE A CD1 1 
ATOM   388  C CD2 . PHE A 1 76  ? 14.063  22.770 -14.230 1.00 20.96 ? 52  PHE A CD2 1 
ATOM   389  C CE1 . PHE A 1 76  ? 11.306  23.049 -14.311 1.00 18.94 ? 52  PHE A CE1 1 
ATOM   390  C CE2 . PHE A 1 76  ? 13.273  22.068 -13.338 1.00 19.69 ? 52  PHE A CE2 1 
ATOM   391  C CZ  . PHE A 1 76  ? 11.889  22.211 -13.379 1.00 23.05 ? 52  PHE A CZ  1 
ATOM   392  N N   . ALA A 1 77  ? 12.811  26.976 -16.805 1.00 22.24 ? 53  ALA A N   1 
ATOM   393  C CA  . ALA A 1 77  ? 11.568  27.742 -16.919 1.00 18.11 ? 53  ALA A CA  1 
ATOM   394  C C   . ALA A 1 77  ? 10.410  27.035 -16.233 1.00 18.83 ? 53  ALA A C   1 
ATOM   395  O O   . ALA A 1 77  ? 10.048  25.915 -16.605 1.00 17.71 ? 53  ALA A O   1 
ATOM   396  C CB  . ALA A 1 77  ? 11.225  27.965 -18.397 1.00 23.01 ? 53  ALA A CB  1 
ATOM   397  N N   . PHE A 1 78  ? 9.779   27.725 -15.276 1.00 17.47 ? 54  PHE A N   1 
ATOM   398  C CA  . PHE A 1 78  ? 8.622   27.160 -14.588 1.00 18.56 ? 54  PHE A CA  1 
ATOM   399  C C   . PHE A 1 78  ? 7.477   26.842 -15.555 1.00 18.11 ? 54  PHE A C   1 
ATOM   400  O O   . PHE A 1 78  ? 6.707   25.908 -15.306 1.00 14.08 ? 54  PHE A O   1 
ATOM   401  C CB  . PHE A 1 78  ? 8.156   28.129 -13.486 1.00 19.73 ? 54  PHE A CB  1 
ATOM   402  C CG  . PHE A 1 78  ? 7.289   27.487 -12.415 1.00 17.04 ? 54  PHE A CG  1 
ATOM   403  C CD1 . PHE A 1 78  ? 5.912   27.398 -12.575 1.00 17.76 ? 54  PHE A CD1 1 
ATOM   404  C CD2 . PHE A 1 78  ? 7.850   27.011 -11.237 1.00 20.74 ? 54  PHE A CD2 1 
ATOM   405  C CE1 . PHE A 1 78  ? 5.112   26.811 -11.579 1.00 17.19 ? 54  PHE A CE1 1 
ATOM   406  C CE2 . PHE A 1 78  ? 7.058   26.440 -10.230 1.00 16.89 ? 54  PHE A CE2 1 
ATOM   407  C CZ  . PHE A 1 78  ? 5.695   26.342 -10.401 1.00 18.00 ? 54  PHE A CZ  1 
ATOM   408  N N   . ASP A 1 79  ? 7.372   27.579 -16.673 1.00 13.46 ? 55  ASP A N   1 
ATOM   409  C CA  . ASP A 1 79  ? 6.288   27.373 -17.639 1.00 15.08 ? 55  ASP A CA  1 
ATOM   410  C C   . ASP A 1 79  ? 6.220   25.951 -18.194 1.00 19.79 ? 55  ASP A C   1 
ATOM   411  O O   . ASP A 1 79  ? 5.147   25.521 -18.638 1.00 16.16 ? 55  ASP A O   1 
ATOM   412  C CB  . ASP A 1 79  ? 6.418   28.333 -18.823 1.00 16.25 ? 55  ASP A CB  1 
ATOM   413  C CG  . ASP A 1 79  ? 6.053   29.750 -18.466 1.00 21.95 ? 55  ASP A CG  1 
ATOM   414  O OD1 . ASP A 1 79  ? 5.115   29.933 -17.669 1.00 17.65 ? 55  ASP A OD1 1 
ATOM   415  O OD2 . ASP A 1 79  ? 6.682   30.670 -19.017 1.00 19.96 ? 55  ASP A OD2 1 
ATOM   416  N N   . ILE A 1 80  ? 7.339   25.220 -18.255 1.00 16.02 ? 56  ILE A N   1 
ATOM   417  C CA  . ILE A 1 80  ? 7.222   23.873 -18.828 1.00 14.49 ? 56  ILE A CA  1 
ATOM   418  C C   . ILE A 1 80  ? 6.355   22.970 -17.951 1.00 13.97 ? 56  ILE A C   1 
ATOM   419  O O   . ILE A 1 80  ? 5.808   21.979 -18.443 1.00 15.49 ? 56  ILE A O   1 
ATOM   420  C CB  . ILE A 1 80  ? 8.592   23.210 -19.095 1.00 18.95 ? 56  ILE A CB  1 
ATOM   421  C CG1 . ILE A 1 80  ? 9.298   22.798 -17.791 1.00 16.76 ? 56  ILE A CG1 1 
ATOM   422  C CG2 . ILE A 1 80  ? 9.476   24.076 -19.998 1.00 18.63 ? 56  ILE A CG2 1 
ATOM   423  C CD1 . ILE A 1 80  ? 10.577  21.941 -18.053 1.00 18.04 ? 56  ILE A CD1 1 
ATOM   424  N N   . LEU A 1 81  ? 6.209   23.302 -16.669 1.00 15.58 ? 57  LEU A N   1 
ATOM   425  C CA  . LEU A 1 81  ? 5.477   22.497 -15.705 1.00 17.04 ? 57  LEU A CA  1 
ATOM   426  C C   . LEU A 1 81  ? 3.997   22.827 -15.631 1.00 15.54 ? 57  LEU A C   1 
ATOM   427  O O   . LEU A 1 81  ? 3.233   22.028 -15.092 1.00 16.28 ? 57  LEU A O   1 
ATOM   428  C CB  . LEU A 1 81  ? 6.045   22.723 -14.301 1.00 12.25 ? 57  LEU A CB  1 
ATOM   429  C CG  . LEU A 1 81  ? 7.542   22.531 -14.079 1.00 17.29 ? 57  LEU A CG  1 
ATOM   430  C CD1 . LEU A 1 81  ? 7.883   22.961 -12.655 1.00 18.27 ? 57  LEU A CD1 1 
ATOM   431  C CD2 . LEU A 1 81  ? 7.921   21.056 -14.359 1.00 15.16 ? 57  LEU A CD2 1 
ATOM   432  N N   . THR A 1 82  ? 3.572   23.999 -16.104 1.00 15.38 ? 58  THR A N   1 
ATOM   433  C CA  . THR A 1 82  ? 2.295   24.523 -15.615 1.00 15.85 ? 58  THR A CA  1 
ATOM   434  C C   . THR A 1 82  ? 1.087   23.750 -16.144 1.00 15.51 ? 58  THR A C   1 
ATOM   435  O O   . THR A 1 82  ? 0.096   23.623 -15.421 1.00 13.22 ? 58  THR A O   1 
ATOM   436  C CB  . THR A 1 82  ? 2.159   26.000 -15.929 1.00 13.17 ? 58  THR A CB  1 
ATOM   437  O OG1 . THR A 1 82  ? 2.386   26.222 -17.323 1.00 12.77 ? 58  THR A OG1 1 
ATOM   438  C CG2 . THR A 1 82  ? 3.148   26.817 -15.079 1.00 10.96 ? 58  THR A CG2 1 
ATOM   439  N N   . THR A 1 83  ? 1.135   23.199 -17.364 1.00 12.75 ? 59  THR A N   1 
ATOM   440  C CA  . THR A 1 83  ? -0.027  22.399 -17.764 1.00 12.72 ? 59  THR A CA  1 
ATOM   441  C C   . THR A 1 83  ? -0.101  21.049 -17.052 1.00 17.96 ? 59  THR A C   1 
ATOM   442  O O   . THR A 1 83  ? -1.129  20.363 -17.159 1.00 16.15 ? 59  THR A O   1 
ATOM   443  C CB  . THR A 1 83  ? -0.072  22.173 -19.279 1.00 15.18 ? 59  THR A CB  1 
ATOM   444  O OG1 . THR A 1 83  ? 0.971   21.275 -19.669 1.00 16.33 ? 59  THR A OG1 1 
ATOM   445  C CG2 . THR A 1 83  ? 0.071   23.523 -20.031 1.00 15.44 ? 59  THR A CG2 1 
ATOM   446  N N   . ALA A 1 84  ? 0.937   20.641 -16.324 1.00 16.34 ? 60  ALA A N   1 
ATOM   447  C CA  . ALA A 1 84  ? 0.782   19.438 -15.527 1.00 17.04 ? 60  ALA A CA  1 
ATOM   448  C C   . ALA A 1 84  ? 0.103   19.736 -14.191 1.00 18.14 ? 60  ALA A C   1 
ATOM   449  O O   . ALA A 1 84  ? -0.431  18.813 -13.576 1.00 18.88 ? 60  ALA A O   1 
ATOM   450  C CB  . ALA A 1 84  ? 2.134   18.740 -15.303 1.00 14.81 ? 60  ALA A CB  1 
ATOM   451  N N   . PHE A 1 85  ? 0.100   20.998 -13.749 1.00 14.96 ? 61  PHE A N   1 
ATOM   452  C CA  . PHE A 1 85  ? -0.658  21.445 -12.582 1.00 17.66 ? 61  PHE A CA  1 
ATOM   453  C C   . PHE A 1 85  ? -2.118  21.689 -12.983 1.00 16.83 ? 61  PHE A C   1 
ATOM   454  O O   . PHE A 1 85  ? -3.038  21.334 -12.241 1.00 16.21 ? 61  PHE A O   1 
ATOM   455  C CB  . PHE A 1 85  ? -0.075  22.743 -11.989 1.00 15.30 ? 61  PHE A CB  1 
ATOM   456  C CG  . PHE A 1 85  ? 1.349   22.628 -11.561 1.00 16.88 ? 61  PHE A CG  1 
ATOM   457  C CD1 . PHE A 1 85  ? 1.751   21.621 -10.698 1.00 21.35 ? 61  PHE A CD1 1 
ATOM   458  C CD2 . PHE A 1 85  ? 2.294   23.537 -12.015 1.00 15.12 ? 61  PHE A CD2 1 
ATOM   459  C CE1 . PHE A 1 85  ? 3.072   21.524 -10.301 1.00 21.63 ? 61  PHE A CE1 1 
ATOM   460  C CE2 . PHE A 1 85  ? 3.613   23.449 -11.626 1.00 16.56 ? 61  PHE A CE2 1 
ATOM   461  C CZ  . PHE A 1 85  ? 4.011   22.447 -10.763 1.00 20.65 ? 61  PHE A CZ  1 
HETATM 462  C C1  . 5SQ A 1 86  ? -3.738  21.766 -16.139 1.00 16.31 ? 64  5SQ A C1  1 
HETATM 463  C C2  . 5SQ A 1 86  ? -3.985  19.818 -17.402 1.00 15.79 ? 64  5SQ A C2  1 
HETATM 464  O O3  . 5SQ A 1 86  ? -4.719  17.338 -14.341 1.00 15.85 ? 64  5SQ A O3  1 
HETATM 465  C C3  . 5SQ A 1 86  ? -4.925  18.448 -14.903 1.00 13.71 ? 64  5SQ A C3  1 
HETATM 466  C CA3 . 5SQ A 1 86  ? -3.886  19.550 -14.816 1.00 18.56 ? 64  5SQ A CA3 1 
HETATM 467  N N3  . 5SQ A 1 86  ? -3.881  20.367 -16.034 1.00 16.87 ? 64  5SQ A N3  1 
HETATM 468  O O2  . 5SQ A 1 86  ? -4.103  18.710 -17.824 1.00 15.80 ? 64  5SQ A O2  1 
HETATM 469  C CA1 . 5SQ A 1 86  ? -3.616  22.552 -14.795 1.00 17.31 ? 64  5SQ A CA1 1 
HETATM 470  N N1  . 5SQ A 1 86  ? -2.317  22.293 -14.157 1.00 16.23 ? 64  5SQ A N1  1 
HETATM 471  C CB1 . 5SQ A 1 86  ? -3.859  24.053 -15.021 1.00 14.54 ? 64  5SQ A CB1 1 
HETATM 472  C CG1 . 5SQ A 1 86  ? -4.021  24.830 -13.687 1.00 15.66 ? 64  5SQ A CG1 1 
HETATM 473  C C2H . 5SQ A 1 86  ? -4.078  26.201 -13.583 1.00 12.62 ? 64  5SQ A C2H 1 
HETATM 474  N N2H . 5SQ A 1 86  ? -4.212  26.488 -12.294 1.00 20.64 ? 64  5SQ A N2H 1 
HETATM 475  N N1H . 5SQ A 1 86  ? -4.143  24.318 -12.473 1.00 20.39 ? 64  5SQ A N1H 1 
HETATM 476  C C1H . 5SQ A 1 86  ? -4.271  25.343 -11.595 1.00 14.43 ? 64  5SQ A C1H 1 
HETATM 477  N N2  . 5SQ A 1 86  ? -3.745  22.248 -17.480 1.00 16.87 ? 64  5SQ A N2  1 
HETATM 478  C CA2 . 5SQ A 1 86  ? -3.878  21.041 -18.341 1.00 17.16 ? 64  5SQ A CA2 1 
HETATM 479  C CB2 . 5SQ A 1 86  ? -3.926  21.456 -19.616 1.00 14.25 ? 64  5SQ A CB2 1 
HETATM 480  C CG2 . 5SQ A 1 86  ? -3.732  22.721 -20.415 1.00 17.06 ? 64  5SQ A CG2 1 
HETATM 481  C CD2 . 5SQ A 1 86  ? -3.679  24.028 -19.965 1.00 15.47 ? 64  5SQ A CD2 1 
HETATM 482  C CE2 . 5SQ A 1 86  ? -3.417  25.008 -20.928 1.00 16.69 ? 64  5SQ A CE2 1 
HETATM 483  C CD1 . 5SQ A 1 86  ? -3.484  22.358 -21.736 1.00 14.77 ? 64  5SQ A CD1 1 
HETATM 484  C CE1 . 5SQ A 1 86  ? -3.236  23.319 -22.684 1.00 16.82 ? 64  5SQ A CE1 1 
HETATM 485  C CZ1 . 5SQ A 1 86  ? -3.206  24.650 -22.261 1.00 16.53 ? 64  5SQ A CZ1 1 
HETATM 486  O OH  . 5SQ A 1 86  ? -2.953  25.640 -23.231 1.00 18.83 ? 64  5SQ A OH  1 
ATOM   487  N N   . ASN A 1 87  ? -6.129  18.959 -15.110 1.00 15.51 ? 65  ASN A N   1 
ATOM   488  C CA  . ASN A 1 87  ? -7.324  18.178 -14.810 1.00 15.84 ? 65  ASN A CA  1 
ATOM   489  C C   . ASN A 1 87  ? -8.495  18.692 -15.664 1.00 17.09 ? 65  ASN A C   1 
ATOM   490  O O   . ASN A 1 87  ? -9.059  19.758 -15.406 1.00 14.55 ? 65  ASN A O   1 
ATOM   491  C CB  . ASN A 1 87  ? -7.632  18.247 -13.302 1.00 16.65 ? 65  ASN A CB  1 
ATOM   492  C CG  . ASN A 1 87  ? -8.872  17.459 -12.915 1.00 17.33 ? 65  ASN A CG  1 
ATOM   493  O OD1 . ASN A 1 87  ? -9.477  16.782 -13.752 1.00 17.91 ? 65  ASN A OD1 1 
ATOM   494  N ND2 . ASN A 1 87  ? -9.231  17.504 -11.623 1.00 15.74 ? 65  ASN A ND2 1 
ATOM   495  N N   . ARG A 1 88  ? -8.844  17.937 -16.707 1.00 17.49 ? 66  ARG A N   1 
ATOM   496  C CA  . ARG A 1 88  ? -9.875  18.382 -17.647 1.00 17.99 ? 66  ARG A CA  1 
ATOM   497  C C   . ARG A 1 88  ? -11.294 18.336 -17.061 1.00 20.46 ? 66  ARG A C   1 
ATOM   498  O O   . ARG A 1 88  ? -12.259 18.684 -17.765 1.00 18.65 ? 66  ARG A O   1 
ATOM   499  C CB  . ARG A 1 88  ? -9.764  17.566 -18.948 1.00 15.04 ? 66  ARG A CB  1 
ATOM   500  C CG  . ARG A 1 88  ? -10.229 18.312 -20.238 1.00 17.66 ? 66  ARG A CG  1 
ATOM   501  C CD  . ARG A 1 88  ? -9.344  19.520 -20.617 1.00 14.32 ? 66  ARG A CD  1 
ATOM   502  N NE  . ARG A 1 88  ? -7.974  19.072 -20.837 1.00 13.67 ? 66  ARG A NE  1 
ATOM   503  C CZ  . ARG A 1 88  ? -7.017  19.133 -19.920 1.00 17.38 ? 66  ARG A CZ  1 
ATOM   504  N NH1 . ARG A 1 88  ? -7.187  19.803 -18.786 1.00 15.07 ? 66  ARG A NH1 1 
ATOM   505  N NH2 . ARG A 1 88  ? -5.860  18.518 -20.150 1.00 16.19 ? 66  ARG A NH2 1 
ATOM   506  N N   . VAL A 1 89  ? -11.462 17.946 -15.790 1.00 14.04 ? 67  VAL A N   1 
ATOM   507  C CA  . VAL A 1 89  ? -12.699 18.284 -15.088 1.00 13.71 ? 67  VAL A CA  1 
ATOM   508  C C   . VAL A 1 89  ? -12.936 19.784 -15.135 1.00 20.23 ? 67  VAL A C   1 
ATOM   509  O O   . VAL A 1 89  ? -14.075 20.244 -15.218 1.00 19.64 ? 67  VAL A O   1 
ATOM   510  C CB  . VAL A 1 89  ? -12.652 17.779 -13.634 1.00 18.50 ? 67  VAL A CB  1 
ATOM   511  C CG1 . VAL A 1 89  ? -13.686 18.516 -12.765 1.00 27.02 ? 67  VAL A CG1 1 
ATOM   512  C CG2 . VAL A 1 89  ? -12.959 16.309 -13.614 1.00 24.21 ? 67  VAL A CG2 1 
ATOM   513  N N   . PHE A 1 90  ? -11.865 20.575 -15.063 1.00 16.53 ? 68  PHE A N   1 
ATOM   514  C CA  . PHE A 1 90  ? -12.013 22.030 -15.037 1.00 18.00 ? 68  PHE A CA  1 
ATOM   515  C C   . PHE A 1 90  ? -12.038 22.540 -16.479 1.00 21.96 ? 68  PHE A C   1 
ATOM   516  O O   . PHE A 1 90  ? -11.092 23.140 -17.005 1.00 18.87 ? 68  PHE A O   1 
ATOM   517  C CB  . PHE A 1 90  ? -10.917 22.655 -14.174 1.00 16.03 ? 68  PHE A CB  1 
ATOM   518  C CG  . PHE A 1 90  ? -11.068 22.322 -12.705 1.00 19.50 ? 68  PHE A CG  1 
ATOM   519  C CD1 . PHE A 1 90  ? -11.995 22.997 -11.918 1.00 12.63 ? 68  PHE A CD1 1 
ATOM   520  C CD2 . PHE A 1 90  ? -10.328 21.291 -12.128 1.00 18.97 ? 68  PHE A CD2 1 
ATOM   521  C CE1 . PHE A 1 90  ? -12.164 22.685 -10.574 1.00 17.07 ? 68  PHE A CE1 1 
ATOM   522  C CE2 . PHE A 1 90  ? -10.487 20.974 -10.788 1.00 16.84 ? 68  PHE A CE2 1 
ATOM   523  C CZ  . PHE A 1 90  ? -11.407 21.661 -10.011 1.00 21.43 ? 68  PHE A CZ  1 
ATOM   524  N N   . ALA A 1 91  ? -13.153 22.213 -17.138 1.00 15.69 ? 69  ALA A N   1 
ATOM   525  C CA  . ALA A 1 91  ? -13.457 22.644 -18.499 1.00 16.17 ? 69  ALA A CA  1 
ATOM   526  C C   . ALA A 1 91  ? -14.967 22.747 -18.589 1.00 18.43 ? 69  ALA A C   1 
ATOM   527  O O   . ALA A 1 91  ? -15.669 21.836 -18.143 1.00 19.84 ? 69  ALA A O   1 
ATOM   528  C CB  . ALA A 1 91  ? -12.933 21.654 -19.550 1.00 16.18 ? 69  ALA A CB  1 
ATOM   529  N N   . LYS A 1 92  ? -15.467 23.831 -19.168 1.00 16.05 ? 70  LYS A N   1 
ATOM   530  C CA  . LYS A 1 92  ? -16.906 24.001 -19.311 1.00 16.54 ? 70  LYS A CA  1 
ATOM   531  C C   . LYS A 1 92  ? -17.375 23.191 -20.516 1.00 20.17 ? 70  LYS A C   1 
ATOM   532  O O   . LYS A 1 92  ? -17.029 23.507 -21.663 1.00 20.83 ? 70  LYS A O   1 
ATOM   533  C CB  . LYS A 1 92  ? -17.249 25.474 -19.457 1.00 18.27 ? 70  LYS A CB  1 
ATOM   534  C CG  . LYS A 1 92  ? -18.737 25.728 -19.665 1.00 24.07 ? 70  LYS A CG  1 
ATOM   535  C CD  . LYS A 1 92  ? -18.989 27.171 -20.023 1.00 25.50 ? 70  LYS A CD  1 
ATOM   536  C CE  . LYS A 1 92  ? -20.482 27.423 -20.205 1.00 44.33 ? 70  LYS A CE  1 
ATOM   537  N NZ  . LYS A 1 92  ? -21.160 27.654 -18.899 1.00 53.01 ? 70  LYS A NZ  1 
ATOM   538  N N   . TYR A 1 93  ? -18.168 22.136 -20.258 1.00 21.15 ? 71  TYR A N   1 
ATOM   539  C CA  . TYR A 1 93  ? -18.692 21.290 -21.330 1.00 17.55 ? 71  TYR A CA  1 
ATOM   540  C C   . TYR A 1 93  ? -20.136 21.647 -21.614 1.00 26.43 ? 71  TYR A C   1 
ATOM   541  O O   . TYR A 1 93  ? -20.948 21.696 -20.683 1.00 21.88 ? 71  TYR A O   1 
ATOM   542  C CB  . TYR A 1 93  ? -18.605 19.810 -20.952 1.00 17.42 ? 71  TYR A CB  1 
ATOM   543  C CG  . TYR A 1 93  ? -17.349 19.133 -21.446 1.00 19.79 ? 71  TYR A CG  1 
ATOM   544  C CD1 . TYR A 1 93  ? -16.136 19.289 -20.773 1.00 18.94 ? 71  TYR A CD1 1 
ATOM   545  C CD2 . TYR A 1 93  ? -17.370 18.357 -22.601 1.00 20.91 ? 71  TYR A CD2 1 
ATOM   546  C CE1 . TYR A 1 93  ? -14.968 18.672 -21.250 1.00 18.69 ? 71  TYR A CE1 1 
ATOM   547  C CE2 . TYR A 1 93  ? -16.219 17.733 -23.080 1.00 17.37 ? 71  TYR A CE2 1 
ATOM   548  C CZ  . TYR A 1 93  ? -15.029 17.898 -22.406 1.00 15.64 ? 71  TYR A CZ  1 
ATOM   549  O OH  . TYR A 1 93  ? -13.887 17.290 -22.881 1.00 18.53 ? 71  TYR A OH  1 
ATOM   550  N N   . PRO A 1 94  ? -20.505 21.870 -22.868 1.00 26.81 ? 72  PRO A N   1 
ATOM   551  C CA  . PRO A 1 94  ? -21.920 22.058 -23.193 1.00 27.35 ? 72  PRO A CA  1 
ATOM   552  C C   . PRO A 1 94  ? -22.684 20.742 -23.088 1.00 26.51 ? 72  PRO A C   1 
ATOM   553  O O   . PRO A 1 94  ? -22.107 19.654 -23.136 1.00 27.99 ? 72  PRO A O   1 
ATOM   554  C CB  . PRO A 1 94  ? -21.874 22.581 -24.632 1.00 29.41 ? 72  PRO A CB  1 
ATOM   555  C CG  . PRO A 1 94  ? -20.679 21.931 -25.197 1.00 27.81 ? 72  PRO A CG  1 
ATOM   556  C CD  . PRO A 1 94  ? -19.654 21.884 -24.073 1.00 18.75 ? 72  PRO A CD  1 
ATOM   557  N N   . ASP A 1 95  ? -24.011 20.858 -22.949 1.00 29.99 ? 73  ASP A N   1 
ATOM   558  C CA  . ASP A 1 95  ? -24.847 19.695 -22.660 1.00 32.30 ? 73  ASP A CA  1 
ATOM   559  C C   . ASP A 1 95  ? -24.865 18.671 -23.794 1.00 35.73 ? 73  ASP A C   1 
ATOM   560  O O   . ASP A 1 95  ? -25.289 17.531 -23.573 1.00 39.93 ? 73  ASP A O   1 
ATOM   561  C CB  . ASP A 1 95  ? -26.284 20.140 -22.338 1.00 27.81 ? 73  ASP A CB  1 
ATOM   562  C CG  . ASP A 1 95  ? -26.924 20.950 -23.468 1.00 39.81 ? 73  ASP A CG  1 
ATOM   563  O OD1 . ASP A 1 95  ? -26.320 21.059 -24.559 1.00 48.60 ? 73  ASP A OD1 1 
ATOM   564  O OD2 . ASP A 1 95  ? -28.052 21.460 -23.278 1.00 45.92 ? 73  ASP A OD2 1 
ATOM   565  N N   . ASN A 1 96  ? -24.430 19.044 -24.997 1.00 34.32 ? 74  ASN A N   1 
ATOM   566  C CA  . ASN A 1 96  ? -24.481 18.151 -26.151 1.00 32.74 ? 74  ASN A CA  1 
ATOM   567  C C   . ASN A 1 96  ? -23.112 17.567 -26.506 1.00 32.89 ? 74  ASN A C   1 
ATOM   568  O O   . ASN A 1 96  ? -22.925 17.070 -27.620 1.00 32.19 ? 74  ASN A O   1 
ATOM   569  C CB  . ASN A 1 96  ? -25.082 18.888 -27.346 1.00 35.28 ? 74  ASN A CB  1 
ATOM   570  C CG  . ASN A 1 96  ? -24.147 19.924 -27.926 1.00 42.92 ? 74  ASN A CG  1 
ATOM   571  O OD1 . ASN A 1 96  ? -23.405 20.588 -27.202 1.00 39.50 ? 74  ASN A OD1 1 
ATOM   572  N ND2 . ASN A 1 96  ? -24.233 20.123 -29.238 1.00 59.49 ? 74  ASN A ND2 1 
ATOM   573  N N   . ILE A 1 97  ? -22.154 17.627 -25.588 1.00 28.17 ? 75  ILE A N   1 
ATOM   574  C CA  . ILE A 1 97  ? -20.901 16.890 -25.716 1.00 27.38 ? 75  ILE A CA  1 
ATOM   575  C C   . ILE A 1 97  ? -20.716 16.064 -24.452 1.00 25.73 ? 75  ILE A C   1 
ATOM   576  O O   . ILE A 1 97  ? -20.844 16.586 -23.342 1.00 25.67 ? 75  ILE A O   1 
ATOM   577  C CB  . ILE A 1 97  ? -19.689 17.813 -25.966 1.00 27.03 ? 75  ILE A CB  1 
ATOM   578  C CG1 . ILE A 1 97  ? -19.910 18.685 -27.209 1.00 28.14 ? 75  ILE A CG1 1 
ATOM   579  C CG2 . ILE A 1 97  ? -18.387 16.998 -26.110 1.00 25.74 ? 75  ILE A CG2 1 
ATOM   580  C CD1 . ILE A 1 97  ? -18.931 19.846 -27.314 1.00 28.41 ? 75  ILE A CD1 1 
ATOM   581  N N   . GLN A 1 98  ? -20.447 14.774 -24.626 1.00 22.98 ? 76  GLN A N   1 
ATOM   582  C CA  . GLN A 1 98  ? -20.207 13.884 -23.494 1.00 22.77 ? 76  GLN A CA  1 
ATOM   583  C C   . GLN A 1 98  ? -19.010 14.388 -22.684 1.00 22.59 ? 76  GLN A C   1 
ATOM   584  O O   . GLN A 1 98  ? -17.921 14.583 -23.230 1.00 23.93 ? 76  GLN A O   1 
ATOM   585  C CB  . GLN A 1 98  ? -19.936 12.469 -24.012 1.00 21.04 ? 76  GLN A CB  1 
ATOM   586  C CG  . GLN A 1 98  ? -19.329 11.509 -22.990 1.00 30.27 ? 76  GLN A CG  1 
ATOM   587  C CD  . GLN A 1 98  ? -20.253 11.150 -21.826 1.00 44.73 ? 76  GLN A CD  1 
ATOM   588  O OE1 . GLN A 1 98  ? -21.241 11.824 -21.550 1.00 48.00 ? 76  GLN A OE1 1 
ATOM   589  N NE2 . GLN A 1 98  ? -19.877 10.102 -21.091 1.00 52.08 ? 76  GLN A NE2 1 
ATOM   590  N N   . ASP A 1 99  ? -19.205 14.603 -21.383 1.00 22.31 ? 77  ASP A N   1 
ATOM   591  C CA  . ASP A 1 99  ? -18.148 15.079 -20.486 1.00 21.09 ? 77  ASP A CA  1 
ATOM   592  C C   . ASP A 1 99  ? -17.531 13.864 -19.783 1.00 22.39 ? 77  ASP A C   1 
ATOM   593  O O   . ASP A 1 99  ? -17.935 13.474 -18.683 1.00 22.08 ? 77  ASP A O   1 
ATOM   594  C CB  . ASP A 1 99  ? -18.720 16.103 -19.513 1.00 21.08 ? 77  ASP A CB  1 
ATOM   595  C CG  . ASP A 1 99  ? -17.662 16.752 -18.633 1.00 20.34 ? 77  ASP A CG  1 
ATOM   596  O OD1 . ASP A 1 99  ? -16.512 16.265 -18.571 1.00 19.24 ? 77  ASP A OD1 1 
ATOM   597  O OD2 . ASP A 1 99  ? -17.998 17.792 -18.014 1.00 19.57 ? 77  ASP A OD2 1 
ATOM   598  N N   . TYR A 1 100 ? -16.537 13.267 -20.443 1.00 20.37 ? 78  TYR A N   1 
ATOM   599  C CA  . TYR A 1 100 ? -15.883 12.061 -19.938 1.00 25.11 ? 78  TYR A CA  1 
ATOM   600  C C   . TYR A 1 100 ? -15.273 12.297 -18.567 1.00 20.53 ? 78  TYR A C   1 
ATOM   601  O O   . TYR A 1 100 ? -15.265 11.400 -17.719 1.00 21.75 ? 78  TYR A O   1 
ATOM   602  C CB  . TYR A 1 100 ? -14.799 11.632 -20.926 1.00 19.10 ? 78  TYR A CB  1 
ATOM   603  C CG  . TYR A 1 100 ? -14.055 10.330 -20.649 1.00 25.19 ? 78  TYR A CG  1 
ATOM   604  C CD1 . TYR A 1 100 ? -14.586 9.105  -21.039 1.00 20.60 ? 78  TYR A CD1 1 
ATOM   605  C CD2 . TYR A 1 100 ? -12.789 10.337 -20.075 1.00 21.43 ? 78  TYR A CD2 1 
ATOM   606  C CE1 . TYR A 1 100 ? -13.893 7.920  -20.827 1.00 21.00 ? 78  TYR A CE1 1 
ATOM   607  C CE2 . TYR A 1 100 ? -12.086 9.148  -19.855 1.00 19.15 ? 78  TYR A CE2 1 
ATOM   608  C CZ  . TYR A 1 100 ? -12.636 7.951  -20.237 1.00 23.51 ? 78  TYR A CZ  1 
ATOM   609  O OH  . TYR A 1 100 ? -11.929 6.771  -20.034 1.00 22.19 ? 78  TYR A OH  1 
ATOM   610  N N   . PHE A 1 101 ? -14.751 13.499 -18.338 1.00 20.34 ? 79  PHE A N   1 
ATOM   611  C CA  . PHE A 1 101 ? -13.985 13.788 -17.134 1.00 17.82 ? 79  PHE A CA  1 
ATOM   612  C C   . PHE A 1 101 ? -14.875 13.927 -15.912 1.00 20.48 ? 79  PHE A C   1 
ATOM   613  O O   . PHE A 1 101 ? -14.594 13.338 -14.860 1.00 22.96 ? 79  PHE A O   1 
ATOM   614  C CB  . PHE A 1 101 ? -13.142 15.038 -17.386 1.00 16.02 ? 79  PHE A CB  1 
ATOM   615  C CG  . PHE A 1 101 ? -12.304 14.900 -18.612 1.00 15.50 ? 79  PHE A CG  1 
ATOM   616  C CD1 . PHE A 1 101 ? -11.205 14.056 -18.606 1.00 16.16 ? 79  PHE A CD1 1 
ATOM   617  C CD2 . PHE A 1 101 ? -12.661 15.540 -19.799 1.00 18.27 ? 79  PHE A CD2 1 
ATOM   618  C CE1 . PHE A 1 101 ? -10.443 13.867 -19.751 1.00 16.50 ? 79  PHE A CE1 1 
ATOM   619  C CE2 . PHE A 1 101 ? -11.897 15.363 -20.952 1.00 19.63 ? 79  PHE A CE2 1 
ATOM   620  C CZ  . PHE A 1 101 ? -10.790 14.523 -20.932 1.00 19.67 ? 79  PHE A CZ  1 
ATOM   621  N N   . LYS A 1 102 ? -15.973 14.674 -16.033 1.00 21.24 ? 80  LYS A N   1 
ATOM   622  C CA  . LYS A 1 102 ? -16.887 14.742 -14.904 1.00 19.77 ? 80  LYS A CA  1 
ATOM   623  C C   . LYS A 1 102 ? -17.574 13.397 -14.671 1.00 21.93 ? 80  LYS A C   1 
ATOM   624  O O   . LYS A 1 102 ? -17.880 13.052 -13.526 1.00 23.38 ? 80  LYS A O   1 
ATOM   625  C CB  . LYS A 1 102 ? -17.883 15.885 -15.112 1.00 24.75 ? 80  LYS A CB  1 
ATOM   626  C CG  . LYS A 1 102 ? -17.202 17.253 -14.918 1.00 22.67 ? 80  LYS A CG  1 
ATOM   627  C CD  . LYS A 1 102 ? -18.200 18.404 -14.981 1.00 20.88 ? 80  LYS A CD  1 
ATOM   628  C CE  . LYS A 1 102 ? -17.506 19.767 -14.979 1.00 17.42 ? 80  LYS A CE  1 
ATOM   629  N NZ  . LYS A 1 102 ? -16.902 20.109 -16.305 1.00 18.35 ? 80  LYS A NZ  1 
ATOM   630  N N   . GLN A 1 103 ? -17.762 12.595 -15.721 1.00 21.31 ? 81  GLN A N   1 
ATOM   631  C CA  . GLN A 1 103 ? -18.382 11.280 -15.557 1.00 24.01 ? 81  GLN A CA  1 
ATOM   632  C C   . GLN A 1 103 ? -17.423 10.247 -14.980 1.00 19.75 ? 81  GLN A C   1 
ATOM   633  O O   . GLN A 1 103 ? -17.854 9.131  -14.681 1.00 24.74 ? 81  GLN A O   1 
ATOM   634  C CB  . GLN A 1 103 ? -18.916 10.769 -16.897 1.00 27.78 ? 81  GLN A CB  1 
ATOM   635  C CG  . GLN A 1 103 ? -20.117 11.544 -17.425 1.00 31.57 ? 81  GLN A CG  1 
ATOM   636  C CD  . GLN A 1 103 ? -21.327 11.367 -16.555 1.00 37.83 ? 81  GLN A CD  1 
ATOM   637  O OE1 . GLN A 1 103 ? -21.862 12.329 -16.008 1.00 51.12 ? 81  GLN A OE1 1 
ATOM   638  N NE2 . GLN A 1 103 ? -21.779 10.127 -16.426 1.00 41.81 ? 81  GLN A NE2 1 
ATOM   639  N N   . SER A 1 104 ? -16.141 10.588 -14.849 1.00 20.09 ? 82  SER A N   1 
ATOM   640  C CA  A SER A 1 104 ? -15.112 9.705  -14.314 0.61 24.98 ? 82  SER A CA  1 
ATOM   641  C CA  B SER A 1 104 ? -15.165 9.646  -14.312 0.39 24.93 ? 82  SER A CA  1 
ATOM   642  C C   . SER A 1 104 ? -15.134 9.637  -12.792 1.00 26.20 ? 82  SER A C   1 
ATOM   643  O O   . SER A 1 104 ? -14.421 8.809  -12.201 1.00 25.69 ? 82  SER A O   1 
ATOM   644  C CB  A SER A 1 104 ? -13.741 10.202 -14.781 0.61 22.40 ? 82  SER A CB  1 
ATOM   645  C CB  B SER A 1 104 ? -13.767 9.961  -14.852 0.39 22.50 ? 82  SER A CB  1 
ATOM   646  O OG  A SER A 1 104 ? -13.425 9.686  -16.061 0.61 20.30 ? 82  SER A OG  1 
ATOM   647  O OG  B SER A 1 104 ? -13.327 11.233 -14.418 0.39 23.42 ? 82  SER A OG  1 
ATOM   648  N N   . PHE A 1 105 ? -15.899 10.496 -12.150 1.00 23.09 ? 83  PHE A N   1 
ATOM   649  C CA  . PHE A 1 105 ? -15.915 10.596 -10.711 1.00 22.76 ? 83  PHE A CA  1 
ATOM   650  C C   . PHE A 1 105 ? -17.219 10.062 -10.150 1.00 28.96 ? 83  PHE A C   1 
ATOM   651  O O   . PHE A 1 105 ? -18.238 10.017 -10.848 1.00 27.13 ? 83  PHE A O   1 
ATOM   652  C CB  . PHE A 1 105 ? -15.683 12.058 -10.314 1.00 25.65 ? 83  PHE A CB  1 
ATOM   653  C CG  . PHE A 1 105 ? -14.271 12.485 -10.554 1.00 22.77 ? 83  PHE A CG  1 
ATOM   654  C CD1 . PHE A 1 105 ? -13.289 12.243 -9.605  1.00 21.67 ? 83  PHE A CD1 1 
ATOM   655  C CD2 . PHE A 1 105 ? -13.904 13.032 -11.778 1.00 23.03 ? 83  PHE A CD2 1 
ATOM   656  C CE1 . PHE A 1 105 ? -11.966 12.599 -9.852  1.00 17.75 ? 83  PHE A CE1 1 
ATOM   657  C CE2 . PHE A 1 105 ? -12.583 13.385 -12.031 1.00 23.29 ? 83  PHE A CE2 1 
ATOM   658  C CZ  . PHE A 1 105 ? -11.612 13.171 -11.059 1.00 22.20 ? 83  PHE A CZ  1 
ATOM   659  N N   . PRO A 1 106 ? -17.223 9.630  -8.878  1.00 28.08 ? 84  PRO A N   1 
ATOM   660  C CA  . PRO A 1 106 ? -16.170 9.807  -7.857  1.00 28.91 ? 84  PRO A CA  1 
ATOM   661  C C   . PRO A 1 106 ? -14.880 8.979  -7.973  1.00 32.86 ? 84  PRO A C   1 
ATOM   662  O O   . PRO A 1 106 ? -13.921 9.361  -7.311  1.00 28.49 ? 84  PRO A O   1 
ATOM   663  C CB  . PRO A 1 106 ? -16.922 9.449  -6.561  1.00 29.51 ? 84  PRO A CB  1 
ATOM   664  C CG  . PRO A 1 106 ? -17.867 8.391  -7.001  1.00 30.24 ? 84  PRO A CG  1 
ATOM   665  C CD  . PRO A 1 106 ? -18.387 8.923  -8.320  1.00 29.70 ? 84  PRO A CD  1 
ATOM   666  N N   . LYS A 1 107 ? -14.770 7.901  -8.763  1.00 27.51 ? 85  LYS A N   1 
ATOM   667  C CA  . LYS A 1 107 ? -13.566 7.068  -8.688  1.00 26.86 ? 85  LYS A CA  1 
ATOM   668  C C   . LYS A 1 107 ? -12.342 7.788  -9.243  1.00 27.32 ? 85  LYS A C   1 
ATOM   669  O O   . LYS A 1 107 ? -11.237 7.638  -8.709  1.00 31.48 ? 85  LYS A O   1 
ATOM   670  C CB  . LYS A 1 107 ? -13.765 5.747  -9.423  1.00 25.41 ? 85  LYS A CB  1 
ATOM   671  C CG  . LYS A 1 107 ? -14.409 4.654  -8.583  1.00 34.11 ? 85  LYS A CG  1 
ATOM   672  C CD  . LYS A 1 107 ? -15.356 3.819  -9.421  1.00 49.62 ? 85  LYS A CD  1 
ATOM   673  C CE  . LYS A 1 107 ? -15.511 2.411  -8.849  1.00 54.24 ? 85  LYS A CE  1 
ATOM   674  N NZ  . LYS A 1 107 ? -16.710 1.715  -9.397  1.00 53.77 ? 85  LYS A NZ  1 
ATOM   675  N N   . GLY A 1 108 ? -12.507 8.554  -10.311 1.00 23.37 ? 86  GLY A N   1 
ATOM   676  C CA  . GLY A 1 108 ? -11.421 9.348  -10.860 1.00 21.75 ? 86  GLY A CA  1 
ATOM   677  C C   . GLY A 1 108 ? -10.878 8.786  -12.164 1.00 20.57 ? 86  GLY A C   1 
ATOM   678  O O   . GLY A 1 108 ? -11.434 7.862  -12.767 1.00 24.10 ? 86  GLY A O   1 
ATOM   679  N N   . TYR A 1 109 ? -9.767  9.381  -12.602 1.00 18.58 ? 87  TYR A N   1 
ATOM   680  C CA  . TYR A 1 109 ? -9.135  9.021  -13.867 1.00 19.74 ? 87  TYR A CA  1 
ATOM   681  C C   . TYR A 1 109 ? -7.670  9.422  -13.812 1.00 19.55 ? 87  TYR A C   1 
ATOM   682  O O   . TYR A 1 109 ? -7.220  10.085 -12.874 1.00 19.37 ? 87  TYR A O   1 
ATOM   683  C CB  . TYR A 1 109 ? -9.833  9.682  -15.061 1.00 21.41 ? 87  TYR A CB  1 
ATOM   684  C CG  . TYR A 1 109 ? -9.529  11.157 -15.224 1.00 18.59 ? 87  TYR A CG  1 
ATOM   685  C CD1 . TYR A 1 109 ? -10.103 12.114 -14.373 1.00 18.90 ? 87  TYR A CD1 1 
ATOM   686  C CD2 . TYR A 1 109 ? -8.665  11.598 -16.213 1.00 18.39 ? 87  TYR A CD2 1 
ATOM   687  C CE1 . TYR A 1 109 ? -9.813  13.487 -14.531 1.00 19.55 ? 87  TYR A CE1 1 
ATOM   688  C CE2 . TYR A 1 109 ? -8.378  12.963 -16.381 1.00 18.80 ? 87  TYR A CE2 1 
ATOM   689  C CZ  . TYR A 1 109 ? -8.947  13.894 -15.534 1.00 19.67 ? 87  TYR A CZ  1 
ATOM   690  O OH  . TYR A 1 109 ? -8.648  15.233 -15.696 1.00 18.71 ? 87  TYR A OH  1 
ATOM   691  N N   . SER A 1 110 ? -6.923  9.011  -14.835 1.00 18.75 ? 88  SER A N   1 
ATOM   692  C CA  A SER A 1 110 ? -5.519  9.377  -14.931 0.61 18.19 ? 88  SER A CA  1 
ATOM   693  C CA  B SER A 1 110 ? -5.507  9.343  -14.938 0.39 18.24 ? 88  SER A CA  1 
ATOM   694  C C   . SER A 1 110 ? -5.196  9.808  -16.354 1.00 18.09 ? 88  SER A C   1 
ATOM   695  O O   . SER A 1 110 ? -5.893  9.457  -17.310 1.00 19.98 ? 88  SER A O   1 
ATOM   696  C CB  A SER A 1 110 ? -4.613  8.217  -14.486 0.61 21.79 ? 88  SER A CB  1 
ATOM   697  C CB  B SER A 1 110 ? -4.615  8.143  -14.584 0.39 21.82 ? 88  SER A CB  1 
ATOM   698  O OG  A SER A 1 110 ? -4.616  7.181  -15.448 0.61 21.99 ? 88  SER A OG  1 
ATOM   699  O OG  B SER A 1 110 ? -4.802  7.751  -13.239 0.39 22.17 ? 88  SER A OG  1 
ATOM   700  N N   . TRP A 1 111 ? -4.124  10.587 -16.489 1.00 16.88 ? 89  TRP A N   1 
ATOM   701  C CA  . TRP A 1 111 ? -3.677  10.945 -17.824 1.00 19.33 ? 89  TRP A CA  1 
ATOM   702  C C   . TRP A 1 111 ? -2.163  10.860 -17.898 1.00 17.06 ? 89  TRP A C   1 
ATOM   703  O O   . TRP A 1 111 ? -1.460  10.972 -16.883 1.00 17.98 ? 89  TRP A O   1 
ATOM   704  C CB  . TRP A 1 111 ? -4.206  12.337 -18.254 1.00 16.05 ? 89  TRP A CB  1 
ATOM   705  C CG  . TRP A 1 111 ? -3.806  13.517 -17.404 1.00 14.38 ? 89  TRP A CG  1 
ATOM   706  C CD1 . TRP A 1 111 ? -4.620  14.221 -16.570 1.00 16.18 ? 89  TRP A CD1 1 
ATOM   707  C CD2 . TRP A 1 111 ? -2.529  14.185 -17.382 1.00 15.51 ? 89  TRP A CD2 1 
ATOM   708  N NE1 . TRP A 1 111 ? -3.920  15.256 -15.990 1.00 17.36 ? 89  TRP A NE1 1 
ATOM   709  C CE2 . TRP A 1 111 ? -2.636  15.257 -16.475 1.00 16.36 ? 89  TRP A CE2 1 
ATOM   710  C CE3 . TRP A 1 111 ? -1.295  13.955 -18.013 1.00 16.52 ? 89  TRP A CE3 1 
ATOM   711  C CZ2 . TRP A 1 111 ? -1.546  16.102 -16.164 1.00 15.69 ? 89  TRP A CZ2 1 
ATOM   712  C CZ3 . TRP A 1 111 ? -0.213  14.800 -17.714 1.00 15.14 ? 89  TRP A CZ3 1 
ATOM   713  C CH2 . TRP A 1 111 ? -0.352  15.863 -16.801 1.00 15.96 ? 89  TRP A CH2 1 
ATOM   714  N N   . GLU A 1 112 ? -1.677  10.639 -19.113 1.00 18.08 ? 90  GLU A N   1 
ATOM   715  C CA  . GLU A 1 112 ? -0.255  10.641 -19.429 1.00 18.29 ? 90  GLU A CA  1 
ATOM   716  C C   . GLU A 1 112 ? -0.019  11.541 -20.635 1.00 17.58 ? 90  GLU A C   1 
ATOM   717  O O   . GLU A 1 112 ? -0.814  11.539 -21.573 1.00 18.41 ? 90  GLU A O   1 
ATOM   718  C CB  . GLU A 1 112 ? 0.245   9.206  -19.690 1.00 22.83 ? 90  GLU A CB  1 
ATOM   719  C CG  . GLU A 1 112 ? 1.744   9.125  -19.709 1.00 37.72 ? 90  GLU A CG  1 
ATOM   720  C CD  . GLU A 1 112 ? 2.265   7.713  -19.709 1.00 48.07 ? 90  GLU A CD  1 
ATOM   721  O OE1 . GLU A 1 112 ? 3.503   7.567  -19.696 1.00 53.72 ? 90  GLU A OE1 1 
ATOM   722  O OE2 . GLU A 1 112 ? 1.450   6.763  -19.674 1.00 48.65 ? 90  GLU A OE2 1 
ATOM   723  N N   . ARG A 1 113 ? 1.061   12.321 -20.607 1.00 18.37 ? 91  ARG A N   1 
ATOM   724  C CA  . ARG A 1 113 ? 1.284   13.360 -21.610 1.00 15.65 ? 91  ARG A CA  1 
ATOM   725  C C   . ARG A 1 113 ? 2.736   13.356 -22.068 1.00 17.58 ? 91  ARG A C   1 
ATOM   726  O O   . ARG A 1 113 ? 3.644   13.221 -21.248 1.00 17.38 ? 91  ARG A O   1 
ATOM   727  C CB  . ARG A 1 113 ? 0.938   14.746 -21.040 1.00 14.03 ? 91  ARG A CB  1 
ATOM   728  C CG  . ARG A 1 113 ? 1.169   15.917 -22.033 1.00 14.78 ? 91  ARG A CG  1 
ATOM   729  C CD  . ARG A 1 113 ? 0.657   17.244 -21.440 1.00 15.84 ? 91  ARG A CD  1 
ATOM   730  N NE  . ARG A 1 113 ? -0.728  17.086 -21.006 1.00 15.56 ? 91  ARG A NE  1 
ATOM   731  C CZ  . ARG A 1 113 ? -1.305  17.772 -20.028 1.00 18.63 ? 91  ARG A CZ  1 
ATOM   732  N NH1 . ARG A 1 113 ? -0.666  18.749 -19.397 1.00 16.60 ? 91  ARG A NH1 1 
ATOM   733  N NH2 . ARG A 1 113 ? -2.549  17.456 -19.664 1.00 16.35 ? 91  ARG A NH2 1 
ATOM   734  N N   . SER A 1 114 ? 2.953   13.502 -23.375 1.00 17.07 ? 92  SER A N   1 
ATOM   735  C CA  . SER A 1 114 ? 4.272   13.821 -23.901 1.00 18.75 ? 92  SER A CA  1 
ATOM   736  C C   . SER A 1 114 ? 4.281   15.283 -24.315 1.00 18.77 ? 92  SER A C   1 
ATOM   737  O O   . SER A 1 114 ? 3.313   15.773 -24.902 1.00 17.39 ? 92  SER A O   1 
ATOM   738  C CB  . SER A 1 114 ? 4.633   12.928 -25.092 1.00 21.36 ? 92  SER A CB  1 
ATOM   739  O OG  . SER A 1 114 ? 3.679   13.064 -26.137 1.00 23.31 ? 92  SER A OG  1 
ATOM   740  N N   . LEU A 1 115 ? 5.363   15.981 -23.971 1.00 18.30 ? 93  LEU A N   1 
ATOM   741  C CA  . LEU A 1 115 ? 5.589   17.375 -24.347 1.00 13.37 ? 93  LEU A CA  1 
ATOM   742  C C   . LEU A 1 115 ? 6.886   17.394 -25.149 1.00 17.83 ? 93  LEU A C   1 
ATOM   743  O O   . LEU A 1 115 ? 7.962   17.203 -24.584 1.00 20.33 ? 93  LEU A O   1 
ATOM   744  C CB  . LEU A 1 115 ? 5.701   18.279 -23.120 1.00 15.26 ? 93  LEU A CB  1 
ATOM   745  C CG  . LEU A 1 115 ? 4.536   18.394 -22.129 1.00 15.81 ? 93  LEU A CG  1 
ATOM   746  C CD1 . LEU A 1 115 ? 4.497   17.209 -21.150 1.00 16.46 ? 93  LEU A CD1 1 
ATOM   747  C CD2 . LEU A 1 115 ? 4.636   19.730 -21.366 1.00 17.69 ? 93  LEU A CD2 1 
ATOM   748  N N   . THR A 1 116 ? 6.789   17.587 -26.463 1.00 18.30 ? 94  THR A N   1 
ATOM   749  C CA  . THR A 1 116 ? 7.940   17.473 -27.353 1.00 19.89 ? 94  THR A CA  1 
ATOM   750  C C   . THR A 1 116 ? 8.280   18.870 -27.865 1.00 19.56 ? 94  THR A C   1 
ATOM   751  O O   . THR A 1 116 ? 7.560   19.416 -28.711 1.00 18.12 ? 94  THR A O   1 
ATOM   752  C CB  . THR A 1 116 ? 7.626   16.504 -28.493 1.00 21.73 ? 94  THR A CB  1 
ATOM   753  O OG1 . THR A 1 116 ? 7.175   15.259 -27.939 1.00 23.00 ? 94  THR A OG1 1 
ATOM   754  C CG2 . THR A 1 116 ? 8.851   16.251 -29.379 1.00 25.42 ? 94  THR A CG2 1 
ATOM   755  N N   . PHE A 1 117 ? 9.370   19.444 -27.356 1.00 17.86 ? 95  PHE A N   1 
ATOM   756  C CA  . PHE A 1 117 ? 9.756   20.803 -27.710 1.00 18.05 ? 95  PHE A CA  1 
ATOM   757  C C   . PHE A 1 117 ? 10.641  20.806 -28.951 1.00 19.37 ? 95  PHE A C   1 
ATOM   758  O O   . PHE A 1 117 ? 11.408  19.869 -29.203 1.00 17.48 ? 95  PHE A O   1 
ATOM   759  C CB  . PHE A 1 117 ? 10.477  21.510 -26.553 1.00 17.31 ? 95  PHE A CB  1 
ATOM   760  C CG  . PHE A 1 117 ? 9.635   21.693 -25.327 1.00 17.05 ? 95  PHE A CG  1 
ATOM   761  C CD1 . PHE A 1 117 ? 9.494   20.669 -24.399 1.00 19.67 ? 95  PHE A CD1 1 
ATOM   762  C CD2 . PHE A 1 117 ? 8.997   22.902 -25.085 1.00 21.61 ? 95  PHE A CD2 1 
ATOM   763  C CE1 . PHE A 1 117 ? 8.713   20.837 -23.266 1.00 13.98 ? 95  PHE A CE1 1 
ATOM   764  C CE2 . PHE A 1 117 ? 8.225   23.094 -23.929 1.00 14.52 ? 95  PHE A CE2 1 
ATOM   765  C CZ  . PHE A 1 117 ? 8.076   22.063 -23.022 1.00 17.46 ? 95  PHE A CZ  1 
ATOM   766  N N   . GLU A 1 118 ? 10.525  21.886 -29.735 1.00 17.36 ? 96  GLU A N   1 
ATOM   767  C CA  . GLU A 1 118 ? 11.109  21.891 -31.074 1.00 18.68 ? 96  GLU A CA  1 
ATOM   768  C C   . GLU A 1 118 ? 12.630  21.798 -31.074 1.00 20.35 ? 96  GLU A C   1 
ATOM   769  O O   . GLU A 1 118 ? 13.202  21.390 -32.089 1.00 21.73 ? 96  GLU A O   1 
ATOM   770  C CB  . GLU A 1 118 ? 10.689  23.149 -31.832 1.00 19.78 ? 96  GLU A CB  1 
ATOM   771  C CG  . GLU A 1 118 ? 11.004  24.435 -31.096 1.00 19.80 ? 96  GLU A CG  1 
ATOM   772  C CD  . GLU A 1 118 ? 10.938  25.631 -32.015 1.00 32.18 ? 96  GLU A CD  1 
ATOM   773  O OE1 . GLU A 1 118 ? 11.769  25.733 -32.946 1.00 31.67 ? 96  GLU A OE1 1 
ATOM   774  O OE2 . GLU A 1 118 ? 9.983   26.416 -31.863 1.00 24.03 ? 96  GLU A OE2 1 
ATOM   775  N N   . ASP A 1 119 ? 13.295  22.182 -29.988 1.00 20.71 ? 97  ASP A N   1 
ATOM   776  C CA  . ASP A 1 119 ? 14.747  22.094 -29.917 1.00 23.13 ? 97  ASP A CA  1 
ATOM   777  C C   . ASP A 1 119 ? 15.224  20.769 -29.336 1.00 22.10 ? 97  ASP A C   1 
ATOM   778  O O   . ASP A 1 119 ? 16.415  20.624 -29.040 1.00 21.08 ? 97  ASP A O   1 
ATOM   779  C CB  . ASP A 1 119 ? 15.322  23.295 -29.138 1.00 20.18 ? 97  ASP A CB  1 
ATOM   780  C CG  . ASP A 1 119 ? 14.933  23.320 -27.663 1.00 23.33 ? 97  ASP A CG  1 
ATOM   781  O OD1 . ASP A 1 119 ? 14.042  22.571 -27.222 1.00 21.47 ? 97  ASP A OD1 1 
ATOM   782  O OD2 . ASP A 1 119 ? 15.524  24.131 -26.931 1.00 21.96 ? 97  ASP A OD2 1 
ATOM   783  N N   . GLY A 1 120 ? 14.333  19.783 -29.210 1.00 18.91 ? 98  GLY A N   1 
ATOM   784  C CA  . GLY A 1 120 ? 14.702  18.458 -28.768 1.00 19.56 ? 98  GLY A CA  1 
ATOM   785  C C   . GLY A 1 120 ? 14.469  18.185 -27.298 1.00 18.46 ? 98  GLY A C   1 
ATOM   786  O O   . GLY A 1 120 ? 14.648  17.042 -26.866 1.00 20.16 ? 98  GLY A O   1 
ATOM   787  N N   . GLY A 1 121 ? 14.074  19.187 -26.516 1.00 21.49 ? 99  GLY A N   1 
ATOM   788  C CA  . GLY A 1 121 ? 13.709  18.920 -25.133 1.00 24.99 ? 99  GLY A CA  1 
ATOM   789  C C   . GLY A 1 121 ? 12.448  18.082 -25.109 1.00 18.94 ? 99  GLY A C   1 
ATOM   790  O O   . GLY A 1 121 ? 11.500  18.360 -25.851 1.00 20.41 ? 99  GLY A O   1 
ATOM   791  N N   . ILE A 1 122 ? 12.443  17.025 -24.290 1.00 18.95 ? 100 ILE A N   1 
ATOM   792  C CA  . ILE A 1 122 ? 11.331  16.075 -24.233 1.00 20.61 ? 100 ILE A CA  1 
ATOM   793  C C   . ILE A 1 122 ? 10.886  15.932 -22.784 1.00 20.51 ? 100 ILE A C   1 
ATOM   794  O O   . ILE A 1 122 ? 11.708  15.657 -21.905 1.00 20.76 ? 100 ILE A O   1 
ATOM   795  C CB  . ILE A 1 122 ? 11.710  14.679 -24.766 1.00 30.57 ? 100 ILE A CB  1 
ATOM   796  C CG1 . ILE A 1 122 ? 12.150  14.702 -26.228 1.00 30.73 ? 100 ILE A CG1 1 
ATOM   797  C CG2 . ILE A 1 122 ? 10.515  13.738 -24.606 1.00 31.14 ? 100 ILE A CG2 1 
ATOM   798  C CD1 . ILE A 1 122 ? 11.321  15.570 -27.090 1.00 39.93 ? 100 ILE A CD1 1 
ATOM   799  N N   . CYS A 1 123 ? 9.590   16.059 -22.540 1.00 18.42 ? 101 CYS A N   1 
ATOM   800  C CA  . CYS A 1 123 ? 9.057   15.813 -21.213 1.00 17.68 ? 101 CYS A CA  1 
ATOM   801  C C   . CYS A 1 123 ? 7.964   14.764 -21.288 1.00 20.18 ? 101 CYS A C   1 
ATOM   802  O O   . CYS A 1 123 ? 7.280   14.632 -22.309 1.00 20.59 ? 101 CYS A O   1 
ATOM   803  C CB  . CYS A 1 123 ? 8.484   17.080 -20.577 1.00 18.96 ? 101 CYS A CB  1 
ATOM   804  S SG  . CYS A 1 123 ? 9.721   18.361 -20.325 1.00 20.12 ? 101 CYS A SG  1 
ATOM   805  N N   . ASN A 1 124 ? 7.798   14.040 -20.184 1.00 18.54 ? 102 ASN A N   1 
ATOM   806  C CA  . ASN A 1 124 ? 6.695   13.111 -20.021 1.00 21.12 ? 102 ASN A CA  1 
ATOM   807  C C   . ASN A 1 124 ? 6.049   13.427 -18.678 1.00 18.05 ? 102 ASN A C   1 
ATOM   808  O O   . ASN A 1 124 ? 6.754   13.650 -17.689 1.00 20.76 ? 102 ASN A O   1 
ATOM   809  C CB  . ASN A 1 124 ? 7.203   11.659 -20.056 1.00 27.97 ? 102 ASN A CB  1 
ATOM   810  C CG  . ASN A 1 124 ? 7.637   11.234 -21.456 1.00 37.62 ? 102 ASN A CG  1 
ATOM   811  O OD1 . ASN A 1 124 ? 6.934   11.456 -22.439 1.00 41.44 ? 102 ASN A OD1 1 
ATOM   812  N ND2 . ASN A 1 124 ? 8.821   10.632 -21.546 1.00 54.07 ? 102 ASN A ND2 1 
ATOM   813  N N   . ALA A 1 125 ? 4.720   13.438 -18.621 1.00 16.73 ? 103 ALA A N   1 
ATOM   814  C CA  . ALA A 1 125 ? 4.059   13.765 -17.364 1.00 16.91 ? 103 ALA A CA  1 
ATOM   815  C C   . ALA A 1 125 ? 2.864   12.849 -17.167 1.00 18.90 ? 103 ALA A C   1 
ATOM   816  O O   . ALA A 1 125 ? 2.294   12.320 -18.125 1.00 18.65 ? 103 ALA A O   1 
ATOM   817  C CB  . ALA A 1 125 ? 3.607   15.241 -17.304 1.00 14.69 ? 103 ALA A CB  1 
ATOM   818  N N   . ARG A 1 126 ? 2.478   12.667 -15.908 1.00 19.59 ? 104 ARG A N   1 
ATOM   819  C CA  . ARG A 1 126 ? 1.341   11.812 -15.620 1.00 16.80 ? 104 ARG A CA  1 
ATOM   820  C C   . ARG A 1 126 ? 0.651   12.359 -14.379 1.00 19.09 ? 104 ARG A C   1 
ATOM   821  O O   . ARG A 1 126 ? 1.296   12.953 -13.511 1.00 18.85 ? 104 ARG A O   1 
ATOM   822  C CB  . ARG A 1 126 ? 1.828   10.365 -15.456 1.00 26.50 ? 104 ARG A CB  1 
ATOM   823  C CG  . ARG A 1 126 ? 0.790   9.252  -15.289 1.00 43.57 ? 104 ARG A CG  1 
ATOM   824  C CD  . ARG A 1 126 ? 1.285   8.172  -14.306 1.00 39.74 ? 104 ARG A CD  1 
ATOM   825  N NE  . ARG A 1 126 ? 0.223   7.568  -13.507 1.00 51.65 ? 104 ARG A NE  1 
ATOM   826  C CZ  . ARG A 1 126 ? -0.573  6.604  -13.959 1.00 60.87 ? 104 ARG A CZ  1 
ATOM   827  N NH1 . ARG A 1 126 ? -0.505  6.183  -15.213 1.00 55.80 ? 104 ARG A NH1 1 
ATOM   828  N NH2 . ARG A 1 126 ? -1.447  6.034  -13.131 1.00 55.35 ? 104 ARG A NH2 1 
ATOM   829  N N   . ASN A 1 127 ? -0.669  12.182 -14.310 1.00 15.73 ? 105 ASN A N   1 
ATOM   830  C CA  . ASN A 1 127 ? -1.445  12.621 -13.155 1.00 18.10 ? 105 ASN A CA  1 
ATOM   831  C C   . ASN A 1 127 ? -2.476  11.555 -12.846 1.00 18.23 ? 105 ASN A C   1 
ATOM   832  O O   . ASN A 1 127 ? -3.187  11.103 -13.743 1.00 18.91 ? 105 ASN A O   1 
ATOM   833  C CB  . ASN A 1 127 ? -2.133  13.969 -13.407 1.00 18.13 ? 105 ASN A CB  1 
ATOM   834  C CG  . ASN A 1 127 ? -2.743  14.561 -12.152 1.00 15.43 ? 105 ASN A CG  1 
ATOM   835  O OD1 . ASN A 1 127 ? -2.642  13.985 -11.062 1.00 21.38 ? 105 ASN A OD1 1 
ATOM   836  N ND2 . ASN A 1 127 ? -3.371  15.724 -12.292 1.00 16.61 ? 105 ASN A ND2 1 
ATOM   837  N N   . ASP A 1 128 ? -2.504  11.116 -11.592 1.00 16.36 ? 106 ASP A N   1 
ATOM   838  C CA  . ASP A 1 128 ? -3.506  10.194 -11.074 1.00 17.61 ? 106 ASP A CA  1 
ATOM   839  C C   . ASP A 1 128 ? -4.426  11.021 -10.200 1.00 18.82 ? 106 ASP A C   1 
ATOM   840  O O   . ASP A 1 128 ? -3.992  11.541 -9.163  1.00 18.05 ? 106 ASP A O   1 
ATOM   841  C CB  . ASP A 1 128 ? -2.856  9.066  -10.281 1.00 21.44 ? 106 ASP A CB  1 
ATOM   842  C CG  . ASP A 1 128 ? -2.056  8.144  -11.157 1.00 46.64 ? 106 ASP A CG  1 
ATOM   843  O OD1 . ASP A 1 128 ? -0.810  8.224  -11.150 1.00 56.48 ? 106 ASP A OD1 1 
ATOM   844  O OD2 . ASP A 1 128 ? -2.686  7.353  -11.898 1.00 53.04 ? 106 ASP A OD2 1 
ATOM   845  N N   . ILE A 1 129 ? -5.679  11.164 -10.620 1.00 17.64 ? 107 ILE A N   1 
ATOM   846  C CA  . ILE A 1 129 ? -6.606  12.087 -9.983  1.00 19.85 ? 107 ILE A CA  1 
ATOM   847  C C   . ILE A 1 129 ? -7.681  11.287 -9.264  1.00 18.98 ? 107 ILE A C   1 
ATOM   848  O O   . ILE A 1 129 ? -8.332  10.423 -9.863  1.00 19.39 ? 107 ILE A O   1 
ATOM   849  C CB  . ILE A 1 129 ? -7.238  13.057 -10.995 1.00 16.63 ? 107 ILE A CB  1 
ATOM   850  C CG1 . ILE A 1 129 ? -6.152  13.782 -11.794 1.00 17.91 ? 107 ILE A CG1 1 
ATOM   851  C CG2 . ILE A 1 129 ? -8.158  14.052 -10.268 1.00 17.67 ? 107 ILE A CG2 1 
ATOM   852  C CD1 . ILE A 1 129 ? -6.705  14.608 -12.980 1.00 16.94 ? 107 ILE A CD1 1 
ATOM   853  N N   . THR A 1 130 ? -7.874  11.589 -7.980  1.00 20.63 ? 108 THR A N   1 
ATOM   854  C CA  . THR A 1 130 ? -8.962  11.012 -7.200  1.00 25.93 ? 108 THR A CA  1 
ATOM   855  C C   . THR A 1 130 ? -9.780  12.137 -6.579  1.00 23.59 ? 108 THR A C   1 
ATOM   856  O O   . THR A 1 130 ? -9.404  13.314 -6.615  1.00 21.00 ? 108 THR A O   1 
ATOM   857  C CB  . THR A 1 130 ? -8.442  10.083 -6.091  1.00 25.16 ? 108 THR A CB  1 
ATOM   858  O OG1 . THR A 1 130 ? -7.487  10.781 -5.290  1.00 21.51 ? 108 THR A OG1 1 
ATOM   859  C CG2 . THR A 1 130 ? -7.821  8.804  -6.674  1.00 22.56 ? 108 THR A CG2 1 
ATOM   860  N N   . MET A 1 131 ? -10.904 11.746 -5.994  1.00 21.31 ? 109 MET A N   1 
ATOM   861  C CA  . MET A 1 131 ? -11.809 12.635 -5.277  1.00 26.40 ? 109 MET A CA  1 
ATOM   862  C C   . MET A 1 131 ? -12.133 12.093 -3.902  1.00 22.87 ? 109 MET A C   1 
ATOM   863  O O   . MET A 1 131 ? -12.467 10.918 -3.760  1.00 23.71 ? 109 MET A O   1 
ATOM   864  C CB  . MET A 1 131 ? -13.170 12.807 -5.922  1.00 26.10 ? 109 MET A CB  1 
ATOM   865  C CG  . MET A 1 131 ? -13.765 14.186 -5.758  1.00 23.50 ? 109 MET A CG  1 
ATOM   866  S SD  . MET A 1 131 ? -15.342 14.223 -6.617  1.00 32.05 ? 109 MET A SD  1 
ATOM   867  C CE  . MET A 1 131 ? -16.292 13.131 -5.585  1.00 32.38 ? 109 MET A CE  1 
ATOM   868  N N   . GLU A 1 132 ? -12.127 12.987 -2.918  1.00 25.42 ? 110 GLU A N   1 
ATOM   869  C CA  . GLU A 1 132 ? -12.633 12.710 -1.577  1.00 28.79 ? 110 GLU A CA  1 
ATOM   870  C C   . GLU A 1 132 ? -13.462 13.918 -1.162  1.00 26.34 ? 110 GLU A C   1 
ATOM   871  O O   . GLU A 1 132 ? -12.920 15.020 -1.030  1.00 23.61 ? 110 GLU A O   1 
ATOM   872  C CB  . GLU A 1 132 ? -11.482 12.452 -0.601  1.00 28.42 ? 110 GLU A CB  1 
ATOM   873  C CG  . GLU A 1 132 ? -10.675 11.189 -0.910  1.00 26.61 ? 110 GLU A CG  1 
ATOM   874  C CD  . GLU A 1 132 ? -9.473  11.037 0.005   1.00 33.19 ? 110 GLU A CD  1 
ATOM   875  O OE1 . GLU A 1 132 ? -9.520  11.596 1.121   1.00 31.23 ? 110 GLU A OE1 1 
ATOM   876  O OE2 . GLU A 1 132 ? -8.512  10.313 -0.360  1.00 28.51 ? 110 GLU A OE2 1 
ATOM   877  N N   . GLY A 1 133 ? -14.768 13.719 -0.980  1.00 30.98 ? 111 GLY A N   1 
ATOM   878  C CA  . GLY A 1 133 ? -15.636 14.846 -0.670  1.00 26.43 ? 111 GLY A CA  1 
ATOM   879  C C   . GLY A 1 133 ? -15.535 15.943 -1.714  1.00 26.66 ? 111 GLY A C   1 
ATOM   880  O O   . GLY A 1 133 ? -15.657 15.708 -2.921  1.00 32.12 ? 111 GLY A O   1 
ATOM   881  N N   . ASP A 1 134 ? -15.275 17.166 -1.253  1.00 25.40 ? 112 ASP A N   1 
ATOM   882  C CA  . ASP A 1 134 ? -15.161 18.312 -2.144  1.00 25.02 ? 112 ASP A CA  1 
ATOM   883  C C   . ASP A 1 134 ? -13.727 18.567 -2.632  1.00 24.17 ? 112 ASP A C   1 
ATOM   884  O O   . ASP A 1 134 ? -13.451 19.655 -3.153  1.00 25.64 ? 112 ASP A O   1 
ATOM   885  C CB  . ASP A 1 134 ? -15.719 19.558 -1.450  1.00 27.83 ? 112 ASP A CB  1 
ATOM   886  C CG  . ASP A 1 134 ? -14.859 20.022 -0.290  1.00 33.09 ? 112 ASP A CG  1 
ATOM   887  O OD1 . ASP A 1 134 ? -13.960 19.270 0.138   1.00 36.76 ? 112 ASP A OD1 1 
ATOM   888  O OD2 . ASP A 1 134 ? -15.107 21.135 0.221   1.00 42.06 ? 112 ASP A OD2 1 
ATOM   889  N N   . THR A 1 135 ? -12.821 17.593 -2.507  1.00 22.68 ? 113 THR A N   1 
ATOM   890  C CA  . THR A 1 135 ? -11.411 17.802 -2.834  1.00 23.71 ? 113 THR A CA  1 
ATOM   891  C C   . THR A 1 135 ? -10.937 16.846 -3.926  1.00 26.44 ? 113 THR A C   1 
ATOM   892  O O   . THR A 1 135 ? -11.182 15.638 -3.847  1.00 21.16 ? 113 THR A O   1 
ATOM   893  C CB  . THR A 1 135 ? -10.542 17.638 -1.580  1.00 22.56 ? 113 THR A CB  1 
ATOM   894  O OG1 . THR A 1 135 ? -10.988 18.553 -0.565  1.00 21.57 ? 113 THR A OG1 1 
ATOM   895  C CG2 . THR A 1 135 ? -9.086  17.940 -1.900  1.00 20.31 ? 113 THR A CG2 1 
ATOM   896  N N   . PHE A 1 136 ? -10.266 17.394 -4.947  1.00 23.04 ? 114 PHE A N   1 
ATOM   897  C CA  . PHE A 1 136 ? -9.507  16.595 -5.909  1.00 18.72 ? 114 PHE A CA  1 
ATOM   898  C C   . PHE A 1 136 ? -8.084  16.437 -5.387  1.00 17.33 ? 114 PHE A C   1 
ATOM   899  O O   . PHE A 1 136 ? -7.474  17.411 -4.935  1.00 22.89 ? 114 PHE A O   1 
ATOM   900  C CB  . PHE A 1 136 ? -9.461  17.264 -7.287  1.00 20.59 ? 114 PHE A CB  1 
ATOM   901  C CG  . PHE A 1 136 ? -10.763 17.213 -8.054  1.00 22.18 ? 114 PHE A CG  1 
ATOM   902  C CD1 . PHE A 1 136 ? -11.318 16.000 -8.462  1.00 21.88 ? 114 PHE A CD1 1 
ATOM   903  C CD2 . PHE A 1 136 ? -11.431 18.383 -8.369  1.00 18.62 ? 114 PHE A CD2 1 
ATOM   904  C CE1 . PHE A 1 136 ? -12.517 15.966 -9.178  1.00 26.26 ? 114 PHE A CE1 1 
ATOM   905  C CE2 . PHE A 1 136 ? -12.629 18.356 -9.078  1.00 21.80 ? 114 PHE A CE2 1 
ATOM   906  C CZ  . PHE A 1 136 ? -13.175 17.137 -9.479  1.00 28.94 ? 114 PHE A CZ  1 
ATOM   907  N N   . TYR A 1 137 ? -7.562  15.212 -5.426  1.00 19.23 ? 115 TYR A N   1 
ATOM   908  C CA  . TYR A 1 137 ? -6.167  14.946 -5.111  1.00 21.82 ? 115 TYR A CA  1 
ATOM   909  C C   . TYR A 1 137 ? -5.439  14.554 -6.389  1.00 19.63 ? 115 TYR A C   1 
ATOM   910  O O   . TYR A 1 137 ? -5.979  13.813 -7.216  1.00 19.93 ? 115 TYR A O   1 
ATOM   911  C CB  . TYR A 1 137 ? -6.032  13.834 -4.062  1.00 20.43 ? 115 TYR A CB  1 
ATOM   912  C CG  . TYR A 1 137 ? -6.472  14.294 -2.691  1.00 18.84 ? 115 TYR A CG  1 
ATOM   913  C CD1 . TYR A 1 137 ? -5.680  15.160 -1.939  1.00 20.17 ? 115 TYR A CD1 1 
ATOM   914  C CD2 . TYR A 1 137 ? -7.703  13.897 -2.163  1.00 22.40 ? 115 TYR A CD2 1 
ATOM   915  C CE1 . TYR A 1 137 ? -6.088  15.590 -0.671  1.00 23.10 ? 115 TYR A CE1 1 
ATOM   916  C CE2 . TYR A 1 137 ? -8.123  14.333 -0.906  1.00 23.30 ? 115 TYR A CE2 1 
ATOM   917  C CZ  . TYR A 1 137 ? -7.308  15.190 -0.174  1.00 24.63 ? 115 TYR A CZ  1 
ATOM   918  O OH  . TYR A 1 137 ? -7.707  15.621 1.073   1.00 24.15 ? 115 TYR A OH  1 
ATOM   919  N N   . ASN A 1 138 ? -4.218  15.061 -6.555  1.00 18.30 ? 116 ASN A N   1 
ATOM   920  C CA  . ASN A 1 138 ? -3.470  14.918 -7.802  1.00 19.80 ? 116 ASN A CA  1 
ATOM   921  C C   . ASN A 1 138 ? -2.072  14.437 -7.469  1.00 17.09 ? 116 ASN A C   1 
ATOM   922  O O   . ASN A 1 138 ? -1.317  15.154 -6.801  1.00 20.26 ? 116 ASN A O   1 
ATOM   923  C CB  . ASN A 1 138 ? -3.372  16.250 -8.575  1.00 16.16 ? 116 ASN A CB  1 
ATOM   924  C CG  . ASN A 1 138 ? -4.715  16.816 -8.956  1.00 18.79 ? 116 ASN A CG  1 
ATOM   925  O OD1 . ASN A 1 138 ? -5.155  16.702 -10.112 1.00 19.25 ? 116 ASN A OD1 1 
ATOM   926  N ND2 . ASN A 1 138 ? -5.382  17.449 -7.990  1.00 17.85 ? 116 ASN A ND2 1 
ATOM   927  N N   . LYS A 1 139 ? -1.723  13.235 -7.934  1.00 17.16 ? 117 LYS A N   1 
ATOM   928  C CA  . LYS A 1 139 ? -0.374  12.702 -7.801  1.00 18.31 ? 117 LYS A CA  1 
ATOM   929  C C   . LYS A 1 139 ? 0.293   12.851 -9.161  1.00 17.95 ? 117 LYS A C   1 
ATOM   930  O O   . LYS A 1 139 ? -0.012  12.095 -10.088 1.00 18.13 ? 117 LYS A O   1 
ATOM   931  C CB  . LYS A 1 139 ? -0.392  11.236 -7.370  1.00 20.66 ? 117 LYS A CB  1 
ATOM   932  C CG  . LYS A 1 139 ? -1.049  10.982 -6.041  1.00 20.72 ? 117 LYS A CG  1 
ATOM   933  C CD  . LYS A 1 139 ? -1.172  9.475  -5.797  1.00 24.90 ? 117 LYS A CD  1 
ATOM   934  C CE  . LYS A 1 139 ? -1.871  9.206  -4.483  1.00 24.33 ? 117 LYS A CE  1 
ATOM   935  N NZ  . LYS A 1 139 ? -2.219  7.767  -4.326  1.00 28.86 ? 117 LYS A NZ  1 
ATOM   936  N N   . VAL A 1 140 ? 1.195   13.820 -9.284  1.00 17.40 ? 118 VAL A N   1 
ATOM   937  C CA  . VAL A 1 140 ? 1.769   14.192 -10.570 1.00 16.24 ? 118 VAL A CA  1 
ATOM   938  C C   . VAL A 1 140 ? 3.237   13.780 -10.614 1.00 18.64 ? 118 VAL A C   1 
ATOM   939  O O   . VAL A 1 140 ? 3.986   13.992 -9.654  1.00 19.04 ? 118 VAL A O   1 
ATOM   940  C CB  . VAL A 1 140 ? 1.602   15.704 -10.826 1.00 19.78 ? 118 VAL A CB  1 
ATOM   941  C CG1 . VAL A 1 140 ? 2.265   16.102 -12.135 1.00 16.97 ? 118 VAL A CG1 1 
ATOM   942  C CG2 . VAL A 1 140 ? 0.114   16.067 -10.828 1.00 17.98 ? 118 VAL A CG2 1 
ATOM   943  N N   . ARG A 1 141 ? 3.643   13.196 -11.735 1.00 17.81 ? 119 ARG A N   1 
ATOM   944  C CA  . ARG A 1 141 ? 5.035   12.898 -12.020 1.00 18.03 ? 119 ARG A CA  1 
ATOM   945  C C   . ARG A 1 141 ? 5.455   13.651 -13.274 1.00 21.73 ? 119 ARG A C   1 
ATOM   946  O O   . ARG A 1 141 ? 4.704   13.708 -14.251 1.00 19.83 ? 119 ARG A O   1 
ATOM   947  C CB  . ARG A 1 141 ? 5.233   11.397 -12.205 1.00 24.37 ? 119 ARG A CB  1 
ATOM   948  C CG  . ARG A 1 141 ? 4.896   10.582 -10.966 1.00 29.74 ? 119 ARG A CG  1 
ATOM   949  C CD  . ARG A 1 141 ? 4.103   9.332  -11.324 1.00 50.82 ? 119 ARG A CD  1 
ATOM   950  N NE  . ARG A 1 141 ? 3.385   8.785  -10.175 1.00 63.37 ? 119 ARG A NE  1 
ATOM   951  C CZ  . ARG A 1 141 ? 2.090   8.962  -9.930  1.00 63.03 ? 119 ARG A CZ  1 
ATOM   952  N NH1 . ARG A 1 141 ? 1.328   9.726  -10.712 1.00 31.77 ? 119 ARG A NH1 1 
ATOM   953  N NH2 . ARG A 1 141 ? 1.544   8.360  -8.873  1.00 54.91 ? 119 ARG A NH2 1 
ATOM   954  N N   . PHE A 1 142 ? 6.653   14.241 -13.250 1.00 19.49 ? 120 PHE A N   1 
ATOM   955  C CA  . PHE A 1 142 ? 7.130   15.038 -14.377 1.00 17.81 ? 120 PHE A CA  1 
ATOM   956  C C   . PHE A 1 142 ? 8.578   14.671 -14.655 1.00 18.66 ? 120 PHE A C   1 
ATOM   957  O O   . PHE A 1 142 ? 9.392   14.662 -13.731 1.00 22.04 ? 120 PHE A O   1 
ATOM   958  C CB  . PHE A 1 142 ? 7.029   16.548 -14.080 1.00 17.41 ? 120 PHE A CB  1 
ATOM   959  C CG  . PHE A 1 142 ? 7.150   17.421 -15.310 1.00 16.00 ? 120 PHE A CG  1 
ATOM   960  C CD1 . PHE A 1 142 ? 8.401   17.720 -15.848 1.00 17.44 ? 120 PHE A CD1 1 
ATOM   961  C CD2 . PHE A 1 142 ? 6.021   17.948 -15.912 1.00 17.47 ? 120 PHE A CD2 1 
ATOM   962  C CE1 . PHE A 1 142 ? 8.515   18.517 -16.978 1.00 17.48 ? 120 PHE A CE1 1 
ATOM   963  C CE2 . PHE A 1 142 ? 6.119   18.757 -17.033 1.00 17.64 ? 120 PHE A CE2 1 
ATOM   964  C CZ  . PHE A 1 142 ? 7.372   19.036 -17.584 1.00 19.31 ? 120 PHE A CZ  1 
ATOM   965  N N   . TYR A 1 143 ? 8.900   14.361 -15.910 1.00 18.06 ? 121 TYR A N   1 
ATOM   966  C CA  . TYR A 1 143 ? 10.266  14.015 -16.289 1.00 18.42 ? 121 TYR A CA  1 
ATOM   967  C C   . TYR A 1 143 ? 10.644  14.799 -17.531 1.00 22.66 ? 121 TYR A C   1 
ATOM   968  O O   . TYR A 1 143 ? 9.873   14.834 -18.487 1.00 21.35 ? 121 TYR A O   1 
ATOM   969  C CB  . TYR A 1 143 ? 10.410  12.514 -16.568 1.00 20.78 ? 121 TYR A CB  1 
ATOM   970  C CG  . TYR A 1 143 ? 11.772  12.133 -17.112 1.00 31.77 ? 121 TYR A CG  1 
ATOM   971  C CD1 . TYR A 1 143 ? 12.843  11.895 -16.254 1.00 26.83 ? 121 TYR A CD1 1 
ATOM   972  C CD2 . TYR A 1 143 ? 11.997  12.034 -18.489 1.00 25.96 ? 121 TYR A CD2 1 
ATOM   973  C CE1 . TYR A 1 143 ? 14.096  11.542 -16.746 1.00 27.44 ? 121 TYR A CE1 1 
ATOM   974  C CE2 . TYR A 1 143 ? 13.256  11.676 -18.993 1.00 28.23 ? 121 TYR A CE2 1 
ATOM   975  C CZ  . TYR A 1 143 ? 14.294  11.445 -18.116 1.00 34.53 ? 121 TYR A CZ  1 
ATOM   976  O OH  . TYR A 1 143 ? 15.535  11.099 -18.615 1.00 38.60 ? 121 TYR A OH  1 
ATOM   977  N N   . GLY A 1 144 ? 11.835  15.382 -17.541 1.00 17.43 ? 122 GLY A N   1 
ATOM   978  C CA  . GLY A 1 144 ? 12.288  16.139 -18.691 1.00 20.03 ? 122 GLY A CA  1 
ATOM   979  C C   . GLY A 1 144 ? 13.753  15.868 -18.955 1.00 19.63 ? 122 GLY A C   1 
ATOM   980  O O   . GLY A 1 144 ? 14.545  15.667 -18.031 1.00 22.23 ? 122 GLY A O   1 
ATOM   981  N N   . THR A 1 145 ? 14.115  15.879 -20.234 1.00 22.40 ? 123 THR A N   1 
ATOM   982  C CA  . THR A 1 145 ? 15.497  15.603 -20.605 1.00 20.50 ? 123 THR A CA  1 
ATOM   983  C C   . THR A 1 145 ? 15.808  16.261 -21.943 1.00 20.74 ? 123 THR A C   1 
ATOM   984  O O   . THR A 1 145 ? 14.912  16.735 -22.645 1.00 24.84 ? 123 THR A O   1 
ATOM   985  C CB  . THR A 1 145 ? 15.765  14.094 -20.641 1.00 26.75 ? 123 THR A CB  1 
ATOM   986  O OG1 . THR A 1 145 ? 17.181  13.867 -20.656 1.00 30.96 ? 123 THR A OG1 1 
ATOM   987  C CG2 . THR A 1 145 ? 15.107  13.444 -21.862 1.00 28.96 ? 123 THR A CG2 1 
ATOM   988  N N   . ASN A 1 146 ? 17.110  16.315 -22.270 1.00 25.14 ? 124 ASN A N   1 
ATOM   989  C CA  . ASN A 1 146 ? 17.589  16.815 -23.559 1.00 23.38 ? 124 ASN A CA  1 
ATOM   990  C C   . ASN A 1 146 ? 17.313  18.306 -23.775 1.00 26.32 ? 124 ASN A C   1 
ATOM   991  O O   . ASN A 1 146 ? 17.321  18.774 -24.921 1.00 24.40 ? 124 ASN A O   1 
ATOM   992  C CB  . ASN A 1 146 ? 16.990  16.022 -24.733 1.00 28.44 ? 124 ASN A CB  1 
ATOM   993  C CG  . ASN A 1 146 ? 17.565  14.637 -24.869 1.00 37.95 ? 124 ASN A CG  1 
ATOM   994  O OD1 . ASN A 1 146 ? 18.412  14.214 -24.080 1.00 39.34 ? 124 ASN A OD1 1 
ATOM   995  N ND2 . ASN A 1 146 ? 17.106  13.915 -25.889 1.00 41.31 ? 124 ASN A ND2 1 
ATOM   996  N N   . PHE A 1 147 ? 17.067  19.088 -22.721 1.00 24.65 ? 125 PHE A N   1 
ATOM   997  C CA  . PHE A 1 147 ? 16.992  20.533 -22.937 1.00 19.48 ? 125 PHE A CA  1 
ATOM   998  C C   . PHE A 1 147 ? 18.397  21.100 -23.129 1.00 25.21 ? 125 PHE A C   1 
ATOM   999  O O   . PHE A 1 147 ? 19.294  20.815 -22.321 1.00 26.48 ? 125 PHE A O   1 
ATOM   1000 C CB  . PHE A 1 147 ? 16.306  21.236 -21.770 1.00 18.49 ? 125 PHE A CB  1 
ATOM   1001 C CG  . PHE A 1 147 ? 14.821  21.048 -21.742 1.00 17.20 ? 125 PHE A CG  1 
ATOM   1002 C CD1 . PHE A 1 147 ? 14.003  21.697 -22.666 1.00 17.70 ? 125 PHE A CD1 1 
ATOM   1003 C CD2 . PHE A 1 147 ? 14.236  20.213 -20.798 1.00 21.67 ? 125 PHE A CD2 1 
ATOM   1004 C CE1 . PHE A 1 147 ? 12.622  21.546 -22.636 1.00 18.80 ? 125 PHE A CE1 1 
ATOM   1005 C CE2 . PHE A 1 147 ? 12.854  20.038 -20.768 1.00 22.61 ? 125 PHE A CE2 1 
ATOM   1006 C CZ  . PHE A 1 147 ? 12.039  20.713 -21.689 1.00 19.60 ? 125 PHE A CZ  1 
ATOM   1007 N N   . PRO A 1 148 ? 18.633  21.882 -24.184 1.00 27.84 ? 126 PRO A N   1 
ATOM   1008 C CA  . PRO A 1 148 ? 19.959  22.496 -24.367 1.00 26.79 ? 126 PRO A CA  1 
ATOM   1009 C C   . PRO A 1 148 ? 20.264  23.497 -23.258 1.00 24.67 ? 126 PRO A C   1 
ATOM   1010 O O   . PRO A 1 148 ? 19.381  24.225 -22.798 1.00 22.39 ? 126 PRO A O   1 
ATOM   1011 C CB  . PRO A 1 148 ? 19.854  23.197 -25.726 1.00 26.66 ? 126 PRO A CB  1 
ATOM   1012 C CG  . PRO A 1 148 ? 18.519  22.825 -26.305 1.00 28.42 ? 126 PRO A CG  1 
ATOM   1013 C CD  . PRO A 1 148 ? 17.664  22.257 -25.231 1.00 21.86 ? 126 PRO A CD  1 
ATOM   1014 N N   . ALA A 1 149 ? 21.534  23.527 -22.834 1.00 24.22 ? 127 ALA A N   1 
ATOM   1015 C CA  . ALA A 1 149 ? 21.945  24.445 -21.774 1.00 27.85 ? 127 ALA A CA  1 
ATOM   1016 C C   . ALA A 1 149 ? 21.641  25.892 -22.140 1.00 31.99 ? 127 ALA A C   1 
ATOM   1017 O O   . ALA A 1 149 ? 21.249  26.691 -21.275 1.00 32.09 ? 127 ALA A O   1 
ATOM   1018 C CB  . ALA A 1 149 ? 23.441  24.277 -21.477 1.00 33.13 ? 127 ALA A CB  1 
ATOM   1019 N N   . ASN A 1 150 ? 21.815  26.253 -23.413 1.00 25.02 ? 128 ASN A N   1 
ATOM   1020 C CA  . ASN A 1 150 ? 21.602  27.620 -23.876 1.00 31.82 ? 128 ASN A CA  1 
ATOM   1021 C C   . ASN A 1 150 ? 20.208  27.865 -24.455 1.00 35.05 ? 128 ASN A C   1 
ATOM   1022 O O   . ASN A 1 150 ? 19.972  28.930 -25.033 1.00 30.68 ? 128 ASN A O   1 
ATOM   1023 C CB  . ASN A 1 150 ? 22.669  27.991 -24.912 1.00 34.97 ? 128 ASN A CB  1 
ATOM   1024 C CG  . ASN A 1 150 ? 22.679  27.056 -26.108 1.00 41.73 ? 128 ASN A CG  1 
ATOM   1025 O OD1 . ASN A 1 150 ? 21.815  26.191 -26.246 1.00 35.37 ? 128 ASN A OD1 1 
ATOM   1026 N ND2 . ASN A 1 150 ? 23.662  27.230 -26.984 1.00 44.12 ? 128 ASN A ND2 1 
ATOM   1027 N N   . GLY A 1 151 ? 19.285  26.919 -24.315 1.00 27.09 ? 129 GLY A N   1 
ATOM   1028 C CA  . GLY A 1 151 ? 17.939  27.095 -24.823 1.00 28.53 ? 129 GLY A CA  1 
ATOM   1029 C C   . GLY A 1 151 ? 17.092  27.957 -23.907 1.00 25.59 ? 129 GLY A C   1 
ATOM   1030 O O   . GLY A 1 151 ? 17.499  28.355 -22.808 1.00 27.40 ? 129 GLY A O   1 
ATOM   1031 N N   . PRO A 1 152 ? 15.875  28.274 -24.360 1.00 21.92 ? 130 PRO A N   1 
ATOM   1032 C CA  . PRO A 1 152 ? 15.015  29.164 -23.561 1.00 23.58 ? 130 PRO A CA  1 
ATOM   1033 C C   . PRO A 1 152 ? 14.521  28.545 -22.267 1.00 23.37 ? 130 PRO A C   1 
ATOM   1034 O O   . PRO A 1 152 ? 14.129  29.289 -21.358 1.00 22.48 ? 130 PRO A O   1 
ATOM   1035 C CB  . PRO A 1 152 ? 13.840  29.475 -24.502 1.00 23.05 ? 130 PRO A CB  1 
ATOM   1036 C CG  . PRO A 1 152 ? 13.877  28.397 -25.558 1.00 26.03 ? 130 PRO A CG  1 
ATOM   1037 C CD  . PRO A 1 152 ? 15.305  27.963 -25.682 1.00 20.39 ? 130 PRO A CD  1 
ATOM   1038 N N   . VAL A 1 153 ? 14.504  27.215 -22.153 1.00 22.44 ? 131 VAL A N   1 
ATOM   1039 C CA  . VAL A 1 153 ? 14.017  26.590 -20.925 1.00 22.16 ? 131 VAL A CA  1 
ATOM   1040 C C   . VAL A 1 153 ? 15.079  26.657 -19.827 1.00 20.67 ? 131 VAL A C   1 
ATOM   1041 O O   . VAL A 1 153 ? 14.823  27.157 -18.724 1.00 20.13 ? 131 VAL A O   1 
ATOM   1042 C CB  . VAL A 1 153 ? 13.560  25.141 -21.203 1.00 22.89 ? 131 VAL A CB  1 
ATOM   1043 C CG1 . VAL A 1 153 ? 13.284  24.391 -19.882 1.00 18.45 ? 131 VAL A CG1 1 
ATOM   1044 C CG2 . VAL A 1 153 ? 12.309  25.135 -22.093 1.00 17.52 ? 131 VAL A CG2 1 
ATOM   1045 N N   . MET A 1 154 ? 16.283  26.151 -20.099 1.00 19.70 ? 132 MET A N   1 
ATOM   1046 C CA  . MET A 1 154 ? 17.361  26.289 -19.123 1.00 19.87 ? 132 MET A CA  1 
ATOM   1047 C C   . MET A 1 154 ? 17.759  27.742 -18.874 1.00 24.74 ? 132 MET A C   1 
ATOM   1048 O O   . MET A 1 154 ? 18.279  28.058 -17.795 1.00 27.36 ? 132 MET A O   1 
ATOM   1049 C CB  . MET A 1 154 ? 18.581  25.452 -19.550 1.00 24.11 ? 132 MET A CB  1 
ATOM   1050 C CG  . MET A 1 154 ? 18.355  23.943 -19.654 1.00 23.27 ? 132 MET A CG  1 
ATOM   1051 S SD  . MET A 1 154 ? 17.213  23.266 -18.415 1.00 29.65 ? 132 MET A SD  1 
ATOM   1052 C CE  . MET A 1 154 ? 18.274  23.395 -16.975 1.00 28.41 ? 132 MET A CE  1 
ATOM   1053 N N   . GLN A 1 155 ? 17.572  28.635 -19.847 1.00 21.78 ? 133 GLN A N   1 
ATOM   1054 C CA  . GLN A 1 155 ? 17.937  30.035 -19.633 1.00 26.01 ? 133 GLN A CA  1 
ATOM   1055 C C   . GLN A 1 155 ? 16.797  30.865 -19.064 1.00 27.62 ? 133 GLN A C   1 
ATOM   1056 O O   . GLN A 1 155 ? 16.991  32.059 -18.797 1.00 27.87 ? 133 GLN A O   1 
ATOM   1057 C CB  . GLN A 1 155 ? 18.425  30.680 -20.935 1.00 26.02 ? 133 GLN A CB  1 
ATOM   1058 C CG  . GLN A 1 155 ? 19.765  30.155 -21.436 1.00 31.45 ? 133 GLN A CG  1 
ATOM   1059 C CD  . GLN A 1 155 ? 20.895  30.355 -20.440 1.00 40.31 ? 133 GLN A CD  1 
ATOM   1060 O OE1 . GLN A 1 155 ? 21.507  29.395 -19.962 1.00 44.07 ? 133 GLN A OE1 1 
ATOM   1061 N NE2 . GLN A 1 155 ? 21.169  31.608 -20.114 1.00 30.48 ? 133 GLN A NE2 1 
ATOM   1062 N N   . LYS A 1 156 ? 15.622  30.268 -18.873 1.00 24.94 ? 134 LYS A N   1 
ATOM   1063 C CA  . LYS A 1 156 ? 14.482  30.938 -18.242 1.00 25.71 ? 134 LYS A CA  1 
ATOM   1064 C C   . LYS A 1 156 ? 14.073  32.190 -19.021 1.00 24.47 ? 134 LYS A C   1 
ATOM   1065 O O   . LYS A 1 156 ? 13.950  33.289 -18.473 1.00 25.11 ? 134 LYS A O   1 
ATOM   1066 C CB  . LYS A 1 156 ? 14.782  31.257 -16.769 1.00 23.62 ? 134 LYS A CB  1 
ATOM   1067 C CG  . LYS A 1 156 ? 14.885  29.986 -15.904 1.00 29.15 ? 134 LYS A CG  1 
ATOM   1068 C CD  . LYS A 1 156 ? 15.437  30.240 -14.501 1.00 33.99 ? 134 LYS A CD  1 
ATOM   1069 C CE  . LYS A 1 156 ? 14.514  31.156 -13.704 1.00 42.99 ? 134 LYS A CE  1 
ATOM   1070 N NZ  . LYS A 1 156 ? 15.108  31.654 -12.417 1.00 44.06 ? 134 LYS A NZ  1 
ATOM   1071 N N   . LYS A 1 157 ? 13.852  32.009 -20.322 1.00 25.38 ? 135 LYS A N   1 
ATOM   1072 C CA  . LYS A 1 157 ? 13.504  33.102 -21.218 1.00 25.19 ? 135 LYS A CA  1 
ATOM   1073 C C   . LYS A 1 157 ? 12.062  33.011 -21.706 1.00 24.33 ? 135 LYS A C   1 
ATOM   1074 O O   . LYS A 1 157 ? 11.706  33.664 -22.692 1.00 25.05 ? 135 LYS A O   1 
ATOM   1075 C CB  . LYS A 1 157 ? 14.474  33.124 -22.401 1.00 26.15 ? 135 LYS A CB  1 
ATOM   1076 C CG  . LYS A 1 157 ? 15.906  33.406 -21.990 1.00 32.62 ? 135 LYS A CG  1 
ATOM   1077 C CD  . LYS A 1 157 ? 16.815  33.423 -23.202 1.00 49.62 ? 135 LYS A CD  1 
ATOM   1078 C CE  . LYS A 1 157 ? 18.223  33.866 -22.845 1.00 51.22 ? 135 LYS A CE  1 
ATOM   1079 N NZ  . LYS A 1 157 ? 19.180  33.395 -23.886 1.00 50.77 ? 135 LYS A NZ  1 
ATOM   1080 N N   . THR A 1 158 ? 11.225  32.222 -21.041 1.00 20.80 ? 136 THR A N   1 
ATOM   1081 C CA  . THR A 1 158 ? 9.838   32.058 -21.468 1.00 16.92 ? 136 THR A CA  1 
ATOM   1082 C C   . THR A 1 158 ? 8.941   33.065 -20.757 1.00 19.93 ? 136 THR A C   1 
ATOM   1083 O O   . THR A 1 158 ? 9.200   33.471 -19.620 1.00 24.12 ? 136 THR A O   1 
ATOM   1084 C CB  . THR A 1 158 ? 9.330   30.632 -21.211 1.00 19.67 ? 136 THR A CB  1 
ATOM   1085 O OG1 . THR A 1 158 ? 9.157   30.419 -19.805 1.00 20.98 ? 136 THR A OG1 1 
ATOM   1086 C CG2 . THR A 1 158 ? 10.314  29.588 -21.755 1.00 18.47 ? 136 THR A CG2 1 
ATOM   1087 N N   . LEU A 1 159 ? 7.885   33.485 -21.453 1.00 21.19 ? 137 LEU A N   1 
ATOM   1088 C CA  . LEU A 1 159 ? 6.942   34.462 -20.930 1.00 21.55 ? 137 LEU A CA  1 
ATOM   1089 C C   . LEU A 1 159 ? 5.598   33.839 -20.586 1.00 19.57 ? 137 LEU A C   1 
ATOM   1090 O O   . LEU A 1 159 ? 5.086   34.061 -19.487 1.00 18.71 ? 137 LEU A O   1 
ATOM   1091 C CB  . LEU A 1 159 ? 6.736   35.601 -21.937 1.00 22.62 ? 137 LEU A CB  1 
ATOM   1092 C CG  . LEU A 1 159 ? 7.904   36.567 -22.118 1.00 26.27 ? 137 LEU A CG  1 
ATOM   1093 C CD1 . LEU A 1 159 ? 7.502   37.720 -23.032 1.00 29.41 ? 137 LEU A CD1 1 
ATOM   1094 C CD2 . LEU A 1 159 ? 8.333   37.095 -20.746 1.00 26.87 ? 137 LEU A CD2 1 
ATOM   1095 N N   . LYS A 1 160 ? 5.032   33.035 -21.484 1.00 16.47 ? 138 LYS A N   1 
ATOM   1096 C CA  . LYS A 1 160 ? 3.719   32.427 -21.256 1.00 12.94 ? 138 LYS A CA  1 
ATOM   1097 C C   . LYS A 1 160 ? 3.446   31.415 -22.358 1.00 19.02 ? 138 LYS A C   1 
ATOM   1098 O O   . LYS A 1 160 ? 4.085   31.438 -23.413 1.00 17.86 ? 138 LYS A O   1 
ATOM   1099 C CB  . LYS A 1 160 ? 2.595   33.484 -21.236 1.00 17.22 ? 138 LYS A CB  1 
ATOM   1100 C CG  . LYS A 1 160 ? 2.348   34.116 -22.595 1.00 19.33 ? 138 LYS A CG  1 
ATOM   1101 C CD  . LYS A 1 160 ? 1.045   34.881 -22.624 1.00 26.45 ? 138 LYS A CD  1 
ATOM   1102 C CE  . LYS A 1 160 ? 0.729   35.342 -24.017 1.00 25.90 ? 138 LYS A CE  1 
ATOM   1103 N NZ  . LYS A 1 160 ? -0.570  36.075 -24.069 1.00 43.28 ? 138 LYS A NZ  1 
ATOM   1104 N N   . TRP A 1 161 ? 2.468   30.539 -22.105 1.00 16.32 ? 139 TRP A N   1 
ATOM   1105 C CA  . TRP A 1 161 ? 1.881   29.723 -23.159 1.00 16.92 ? 139 TRP A CA  1 
ATOM   1106 C C   . TRP A 1 161 ? 0.835   30.542 -23.901 1.00 18.46 ? 139 TRP A C   1 
ATOM   1107 O O   . TRP A 1 161 ? 0.007   31.211 -23.272 1.00 18.60 ? 139 TRP A O   1 
ATOM   1108 C CB  . TRP A 1 161 ? 1.208   28.463 -22.586 1.00 13.31 ? 139 TRP A CB  1 
ATOM   1109 C CG  . TRP A 1 161 ? 2.122   27.457 -21.971 1.00 13.59 ? 139 TRP A CG  1 
ATOM   1110 C CD1 . TRP A 1 161 ? 2.316   27.229 -20.641 1.00 16.62 ? 139 TRP A CD1 1 
ATOM   1111 C CD2 . TRP A 1 161 ? 2.926   26.488 -22.670 1.00 16.89 ? 139 TRP A CD2 1 
ATOM   1112 N NE1 . TRP A 1 161 ? 3.218   26.194 -20.462 1.00 17.28 ? 139 TRP A NE1 1 
ATOM   1113 C CE2 . TRP A 1 161 ? 3.604   25.724 -21.695 1.00 12.58 ? 139 TRP A CE2 1 
ATOM   1114 C CE3 . TRP A 1 161 ? 3.145   26.209 -24.023 1.00 15.05 ? 139 TRP A CE3 1 
ATOM   1115 C CZ2 . TRP A 1 161 ? 4.503   24.701 -22.031 1.00 16.04 ? 139 TRP A CZ2 1 
ATOM   1116 C CZ3 . TRP A 1 161 ? 4.037   25.190 -24.360 1.00 17.42 ? 139 TRP A CZ3 1 
ATOM   1117 C CH2 . TRP A 1 161 ? 4.688   24.437 -23.368 1.00 13.34 ? 139 TRP A CH2 1 
ATOM   1118 N N   . GLU A 1 162 ? 0.845   30.467 -25.232 1.00 16.94 ? 140 GLU A N   1 
ATOM   1119 C CA  . GLU A 1 162 ? -0.244  31.056 -25.991 1.00 14.91 ? 140 GLU A CA  1 
ATOM   1120 C C   . GLU A 1 162 ? -1.535  30.269 -25.757 1.00 15.11 ? 140 GLU A C   1 
ATOM   1121 O O   . GLU A 1 162 ? -1.497  29.061 -25.488 1.00 19.12 ? 140 GLU A O   1 
ATOM   1122 C CB  . GLU A 1 162 ? 0.084   31.083 -27.482 1.00 14.29 ? 140 GLU A CB  1 
ATOM   1123 C CG  . GLU A 1 162 ? 1.299   31.966 -27.853 1.00 18.87 ? 140 GLU A CG  1 
ATOM   1124 C CD  . GLU A 1 162 ? 1.020   33.461 -27.741 1.00 25.55 ? 140 GLU A CD  1 
ATOM   1125 O OE1 . GLU A 1 162 ? -0.121  33.850 -27.396 1.00 23.71 ? 140 GLU A OE1 1 
ATOM   1126 O OE2 . GLU A 1 162 ? 1.960   34.255 -28.001 1.00 23.88 ? 140 GLU A OE2 1 
ATOM   1127 N N   . PRO A 1 163 ? -2.691  30.929 -25.842 1.00 18.57 ? 141 PRO A N   1 
ATOM   1128 C CA  . PRO A 1 163 ? -3.958  30.198 -25.804 1.00 17.62 ? 141 PRO A CA  1 
ATOM   1129 C C   . PRO A 1 163 ? -3.953  29.125 -26.888 1.00 18.14 ? 141 PRO A C   1 
ATOM   1130 O O   . PRO A 1 163 ? -3.373  29.308 -27.960 1.00 18.18 ? 141 PRO A O   1 
ATOM   1131 C CB  . PRO A 1 163 ? -5.000  31.289 -26.086 1.00 18.52 ? 141 PRO A CB  1 
ATOM   1132 C CG  . PRO A 1 163 ? -4.357  32.532 -25.551 1.00 29.28 ? 141 PRO A CG  1 
ATOM   1133 C CD  . PRO A 1 163 ? -2.910  32.382 -25.988 1.00 21.61 ? 141 PRO A CD  1 
ATOM   1134 N N   . SER A 1 164 ? -4.602  27.998 -26.598 1.00 16.29 ? 142 SER A N   1 
ATOM   1135 C CA  . SER A 1 164 ? -4.503  26.813 -27.439 1.00 17.08 ? 142 SER A CA  1 
ATOM   1136 C C   . SER A 1 164 ? -5.872  26.184 -27.641 1.00 20.28 ? 142 SER A C   1 
ATOM   1137 O O   . SER A 1 164 ? -6.839  26.511 -26.955 1.00 17.50 ? 142 SER A O   1 
ATOM   1138 C CB  . SER A 1 164 ? -3.575  25.792 -26.812 1.00 18.75 ? 142 SER A CB  1 
ATOM   1139 O OG  . SER A 1 164 ? -4.206  25.265 -25.656 1.00 17.54 ? 142 SER A OG  1 
ATOM   1140 N N   . THR A 1 165 ? -5.942  25.264 -28.597 1.00 17.71 ? 143 THR A N   1 
ATOM   1141 C CA  . THR A 1 165 ? -7.122  24.440 -28.804 1.00 17.73 ? 143 THR A CA  1 
ATOM   1142 C C   . THR A 1 165 ? -6.690  22.988 -28.825 1.00 20.96 ? 143 THR A C   1 
ATOM   1143 O O   . THR A 1 165 ? -5.913  22.582 -29.697 1.00 19.75 ? 143 THR A O   1 
ATOM   1144 C CB  . THR A 1 165 ? -7.851  24.797 -30.095 1.00 24.47 ? 143 THR A CB  1 
ATOM   1145 O OG1 . THR A 1 165 ? -8.365  26.128 -29.994 1.00 24.18 ? 143 THR A OG1 1 
ATOM   1146 C CG2 . THR A 1 165 ? -9.013  23.810 -30.348 1.00 26.52 ? 143 THR A CG2 1 
ATOM   1147 N N   . GLU A 1 166 ? -7.179  22.221 -27.858 1.00 17.39 ? 144 GLU A N   1 
ATOM   1148 C CA  . GLU A 1 166 ? -6.862  20.803 -27.746 1.00 14.84 ? 144 GLU A CA  1 
ATOM   1149 C C   . GLU A 1 166 ? -7.860  20.004 -28.583 1.00 18.30 ? 144 GLU A C   1 
ATOM   1150 O O   . GLU A 1 166 ? -9.077  20.164 -28.430 1.00 16.89 ? 144 GLU A O   1 
ATOM   1151 C CB  . GLU A 1 166 ? -6.913  20.378 -26.270 1.00 14.92 ? 144 GLU A CB  1 
ATOM   1152 C CG  . GLU A 1 166 ? -6.811  18.871 -26.029 1.00 17.09 ? 144 GLU A CG  1 
ATOM   1153 C CD  . GLU A 1 166 ? -6.588  18.523 -24.565 1.00 19.58 ? 144 GLU A CD  1 
ATOM   1154 O OE1 . GLU A 1 166 ? -7.145  19.208 -23.677 1.00 14.08 ? 144 GLU A OE1 1 
ATOM   1155 O OE2 . GLU A 1 166 ? -5.922  17.514 -24.286 1.00 17.19 ? 144 GLU A OE2 1 
ATOM   1156 N N   . LYS A 1 167 ? -7.352  19.176 -29.498 1.00 16.21 ? 145 LYS A N   1 
ATOM   1157 C CA  . LYS A 1 167 ? -8.204  18.324 -30.325 1.00 19.69 ? 145 LYS A CA  1 
ATOM   1158 C C   . LYS A 1 167 ? -8.429  17.008 -29.601 1.00 21.26 ? 145 LYS A C   1 
ATOM   1159 O O   . LYS A 1 167 ? -7.488  16.248 -29.374 1.00 15.68 ? 145 LYS A O   1 
ATOM   1160 C CB  . LYS A 1 167 ? -7.586  18.112 -31.705 1.00 22.67 ? 145 LYS A CB  1 
ATOM   1161 C CG  . LYS A 1 167 ? -7.363  19.434 -32.434 1.00 37.66 ? 145 LYS A CG  1 
ATOM   1162 C CD  . LYS A 1 167 ? -6.620  19.276 -33.764 1.00 48.55 ? 145 LYS A CD  1 
ATOM   1163 C CE  . LYS A 1 167 ? -5.666  20.449 -34.004 1.00 43.70 ? 145 LYS A CE  1 
ATOM   1164 N NZ  . LYS A 1 167 ? -4.238  20.105 -33.732 1.00 62.18 ? 145 LYS A NZ  1 
ATOM   1165 N N   . MET A 1 168 ? -9.676  16.742 -29.232 1.00 15.45 ? 146 MET A N   1 
ATOM   1166 C CA  . MET A 1 168 ? -10.024 15.546 -28.484 1.00 17.20 ? 146 MET A CA  1 
ATOM   1167 C C   . MET A 1 168 ? -10.659 14.524 -29.407 1.00 16.14 ? 146 MET A C   1 
ATOM   1168 O O   . MET A 1 168 ? -11.633 14.832 -30.092 1.00 20.13 ? 146 MET A O   1 
ATOM   1169 C CB  . MET A 1 168 ? -10.972 15.836 -27.328 1.00 18.95 ? 146 MET A CB  1 
ATOM   1170 C CG  . MET A 1 168 ? -10.436 16.835 -26.354 1.00 20.06 ? 146 MET A CG  1 
ATOM   1171 S SD  . MET A 1 168 ? -9.427  15.875 -25.196 1.00 21.29 ? 146 MET A SD  1 
ATOM   1172 C CE  . MET A 1 168 ? -9.363  16.940 -23.780 1.00 22.83 ? 146 MET A CE  1 
ATOM   1173 N N   . TYR A 1 169 ? -10.131 13.307 -29.394 1.00 17.12 ? 147 TYR A N   1 
ATOM   1174 C CA  . TYR A 1 169 ? -10.628 12.272 -30.284 1.00 21.98 ? 147 TYR A CA  1 
ATOM   1175 C C   . TYR A 1 169 ? -10.335 10.921 -29.649 1.00 20.43 ? 147 TYR A C   1 
ATOM   1176 O O   . TYR A 1 169 ? -9.625  10.827 -28.648 1.00 20.69 ? 147 TYR A O   1 
ATOM   1177 C CB  . TYR A 1 169 ? -10.003 12.434 -31.672 1.00 25.42 ? 147 TYR A CB  1 
ATOM   1178 C CG  . TYR A 1 169 ? -8.501  12.263 -31.689 1.00 22.40 ? 147 TYR A CG  1 
ATOM   1179 C CD1 . TYR A 1 169 ? -7.654  13.299 -31.278 1.00 21.32 ? 147 TYR A CD1 1 
ATOM   1180 C CD2 . TYR A 1 169 ? -7.920  11.089 -32.154 1.00 27.93 ? 147 TYR A CD2 1 
ATOM   1181 C CE1 . TYR A 1 169 ? -6.283  13.156 -31.302 1.00 19.65 ? 147 TYR A CE1 1 
ATOM   1182 C CE2 . TYR A 1 169 ? -6.532  10.934 -32.178 1.00 28.98 ? 147 TYR A CE2 1 
ATOM   1183 C CZ  . TYR A 1 169 ? -5.724  11.965 -31.763 1.00 22.38 ? 147 TYR A CZ  1 
ATOM   1184 O OH  . TYR A 1 169 ? -4.352  11.816 -31.800 1.00 23.18 ? 147 TYR A OH  1 
ATOM   1185 N N   . VAL A 1 170 ? -10.930 9.878  -30.218 1.00 23.82 ? 148 VAL A N   1 
ATOM   1186 C CA  . VAL A 1 170 ? -10.758 8.508  -29.749 1.00 23.73 ? 148 VAL A CA  1 
ATOM   1187 C C   . VAL A 1 170 ? -10.082 7.745  -30.867 1.00 29.58 ? 148 VAL A C   1 
ATOM   1188 O O   . VAL A 1 170 ? -10.631 7.643  -31.972 1.00 30.93 ? 148 VAL A O   1 
ATOM   1189 C CB  . VAL A 1 170 ? -12.095 7.840  -29.383 1.00 24.18 ? 148 VAL A CB  1 
ATOM   1190 C CG1 . VAL A 1 170 ? -11.849 6.388  -28.927 1.00 23.52 ? 148 VAL A CG1 1 
ATOM   1191 C CG2 . VAL A 1 170 ? -12.822 8.635  -28.325 1.00 22.14 ? 148 VAL A CG2 1 
ATOM   1192 N N   . ARG A 1 171 ? -8.896  7.216  -30.595 1.00 28.65 ? 149 ARG A N   1 
ATOM   1193 C CA  . ARG A 1 171 ? -8.219  6.368  -31.561 1.00 39.36 ? 149 ARG A CA  1 
ATOM   1194 C C   . ARG A 1 171 ? -7.800  5.084  -30.869 1.00 32.05 ? 149 ARG A C   1 
ATOM   1195 O O   . ARG A 1 171 ? -7.118  5.126  -29.840 1.00 30.50 ? 149 ARG A O   1 
ATOM   1196 C CB  . ARG A 1 171 ? -7.006  7.078  -32.174 1.00 40.63 ? 149 ARG A CB  1 
ATOM   1197 C CG  . ARG A 1 171 ? -6.593  6.491  -33.526 1.00 48.72 ? 149 ARG A CG  1 
ATOM   1198 C CD  . ARG A 1 171 ? -5.686  7.452  -34.294 1.00 52.74 ? 149 ARG A CD  1 
ATOM   1199 N NE  . ARG A 1 171 ? -4.927  6.773  -35.340 1.00 51.54 ? 149 ARG A NE  1 
ATOM   1200 C CZ  . ARG A 1 171 ? -3.959  7.341  -36.048 1.00 44.17 ? 149 ARG A CZ  1 
ATOM   1201 N NH1 . ARG A 1 171 ? -3.610  8.603  -35.852 1.00 41.42 ? 149 ARG A NH1 1 
ATOM   1202 N NH2 . ARG A 1 171 ? -3.326  6.624  -36.974 1.00 41.60 ? 149 ARG A NH2 1 
ATOM   1203 N N   . ASP A 1 172 ? -8.229  3.950  -31.422 1.00 36.68 ? 150 ASP A N   1 
ATOM   1204 C CA  . ASP A 1 172 ? -7.893  2.643  -30.872 1.00 36.73 ? 150 ASP A CA  1 
ATOM   1205 C C   . ASP A 1 172 ? -8.476  2.483  -29.470 1.00 36.17 ? 150 ASP A C   1 
ATOM   1206 O O   . ASP A 1 172 ? -7.864  1.873  -28.594 1.00 42.69 ? 150 ASP A O   1 
ATOM   1207 C CB  . ASP A 1 172 ? -6.374  2.439  -30.851 1.00 39.26 ? 150 ASP A CB  1 
ATOM   1208 C CG  . ASP A 1 172 ? -5.776  2.352  -32.252 1.00 58.31 ? 150 ASP A CG  1 
ATOM   1209 O OD1 . ASP A 1 172 ? -4.614  2.790  -32.422 1.00 53.26 ? 150 ASP A OD1 1 
ATOM   1210 O OD2 . ASP A 1 172 ? -6.466  1.870  -33.181 1.00 51.36 ? 150 ASP A OD2 1 
ATOM   1211 N N   . GLY A 1 173 ? -9.649  3.069  -29.246 1.00 29.17 ? 151 GLY A N   1 
ATOM   1212 C CA  . GLY A 1 173 ? -10.336 3.003  -27.973 1.00 33.19 ? 151 GLY A CA  1 
ATOM   1213 C C   . GLY A 1 173 ? -9.787  3.894  -26.878 1.00 29.94 ? 151 GLY A C   1 
ATOM   1214 O O   . GLY A 1 173 ? -10.228 3.773  -25.732 1.00 28.91 ? 151 GLY A O   1 
ATOM   1215 N N   . VAL A 1 174 ? -8.847  4.781  -27.181 1.00 25.53 ? 152 VAL A N   1 
ATOM   1216 C CA  . VAL A 1 174 ? -8.179  5.590  -26.170 1.00 22.16 ? 152 VAL A CA  1 
ATOM   1217 C C   . VAL A 1 174 ? -8.522  7.053  -26.403 1.00 20.82 ? 152 VAL A C   1 
ATOM   1218 O O   . VAL A 1 174 ? -8.229  7.601  -27.473 1.00 22.81 ? 152 VAL A O   1 
ATOM   1219 C CB  . VAL A 1 174 ? -6.654  5.396  -26.197 1.00 31.26 ? 152 VAL A CB  1 
ATOM   1220 C CG1 . VAL A 1 174 ? -5.992  6.348  -25.196 1.00 26.24 ? 152 VAL A CG1 1 
ATOM   1221 C CG2 . VAL A 1 174 ? -6.301  3.953  -25.880 1.00 33.26 ? 152 VAL A CG2 1 
ATOM   1222 N N   . LEU A 1 175 ? -9.115  7.693  -25.399 1.00 19.90 ? 153 LEU A N   1 
ATOM   1223 C CA  . LEU A 1 175 ? -9.379  9.120  -25.500 1.00 18.34 ? 153 LEU A CA  1 
ATOM   1224 C C   . LEU A 1 175 ? -8.062  9.891  -25.514 1.00 19.93 ? 153 LEU A C   1 
ATOM   1225 O O   . LEU A 1 175 ? -7.231  9.738  -24.613 1.00 18.11 ? 153 LEU A O   1 
ATOM   1226 C CB  . LEU A 1 175 ? -10.258 9.575  -24.338 1.00 19.27 ? 153 LEU A CB  1 
ATOM   1227 C CG  . LEU A 1 175 ? -10.587 11.060 -24.329 1.00 18.88 ? 153 LEU A CG  1 
ATOM   1228 C CD1 . LEU A 1 175 ? -11.230 11.528 -25.642 1.00 21.39 ? 153 LEU A CD1 1 
ATOM   1229 C CD2 . LEU A 1 175 ? -11.502 11.370 -23.142 1.00 21.58 ? 153 LEU A CD2 1 
ATOM   1230 N N   . THR A 1 176 ? -7.873  10.722 -26.542 1.00 17.67 ? 154 THR A N   1 
ATOM   1231 C CA  . THR A 1 176 ? -6.603  11.390 -26.798 1.00 15.36 ? 154 THR A CA  1 
ATOM   1232 C C   . THR A 1 176 ? -6.838  12.866 -27.046 1.00 17.47 ? 154 THR A C   1 
ATOM   1233 O O   . THR A 1 176 ? -7.790  13.240 -27.737 1.00 16.38 ? 154 THR A O   1 
ATOM   1234 C CB  . THR A 1 176 ? -5.886  10.814 -28.032 1.00 17.90 ? 154 THR A CB  1 
ATOM   1235 O OG1 . THR A 1 176 ? -5.753  9.396  -27.897 1.00 23.17 ? 154 THR A OG1 1 
ATOM   1236 C CG2 . THR A 1 176 ? -4.486  11.434 -28.168 1.00 20.27 ? 154 THR A CG2 1 
ATOM   1237 N N   . GLY A 1 177 ? -5.946  13.702 -26.514 1.00 18.53 ? 155 GLY A N   1 
ATOM   1238 C CA  . GLY A 1 177 ? -5.953  15.111 -26.864 1.00 16.05 ? 155 GLY A CA  1 
ATOM   1239 C C   . GLY A 1 177 ? -4.630  15.544 -27.471 1.00 16.90 ? 155 GLY A C   1 
ATOM   1240 O O   . GLY A 1 177 ? -3.577  15.339 -26.863 1.00 14.89 ? 155 GLY A O   1 
ATOM   1241 N N   . ASP A 1 178 ? -4.657  16.143 -28.655 1.00 16.57 ? 156 ASP A N   1 
ATOM   1242 C CA  . ASP A 1 178 ? -3.450  16.654 -29.302 1.00 13.73 ? 156 ASP A CA  1 
ATOM   1243 C C   . ASP A 1 178 ? -3.490  18.179 -29.304 1.00 16.92 ? 156 ASP A C   1 
ATOM   1244 O O   . ASP A 1 178 ? -4.538  18.778 -29.565 1.00 16.00 ? 156 ASP A O   1 
ATOM   1245 C CB  . ASP A 1 178 ? -3.332  16.153 -30.746 1.00 15.60 ? 156 ASP A CB  1 
ATOM   1246 C CG  . ASP A 1 178 ? -2.921  14.678 -30.847 1.00 22.52 ? 156 ASP A CG  1 
ATOM   1247 O OD1 . ASP A 1 178 ? -2.412  14.106 -29.874 1.00 19.50 ? 156 ASP A OD1 1 
ATOM   1248 O OD2 . ASP A 1 178 ? -3.079  14.096 -31.943 1.00 21.72 ? 156 ASP A OD2 1 
ATOM   1249 N N   . ILE A 1 179 ? -2.354  18.815 -29.014 1.00 17.91 ? 157 ILE A N   1 
ATOM   1250 C CA  . ILE A 1 179 ? -2.258  20.273 -29.068 1.00 14.95 ? 157 ILE A CA  1 
ATOM   1251 C C   . ILE A 1 179 ? -0.928  20.664 -29.687 1.00 20.38 ? 157 ILE A C   1 
ATOM   1252 O O   . ILE A 1 179 ? 0.115   20.097 -29.345 1.00 17.70 ? 157 ILE A O   1 
ATOM   1253 C CB  . ILE A 1 179 ? -2.399  20.949 -27.679 1.00 14.80 ? 157 ILE A CB  1 
ATOM   1254 C CG1 . ILE A 1 179 ? -3.313  20.152 -26.729 1.00 15.21 ? 157 ILE A CG1 1 
ATOM   1255 C CG2 . ILE A 1 179 ? -2.878  22.398 -27.852 1.00 20.69 ? 157 ILE A CG2 1 
ATOM   1256 C CD1 . ILE A 1 179 ? -3.351  20.701 -25.276 1.00 15.43 ? 157 ILE A CD1 1 
ATOM   1257 N N   . GLU A 1 180 ? -0.967  21.643 -30.602 1.00 17.87 ? 158 GLU A N   1 
ATOM   1258 C CA  . GLU A 1 180 ? 0.235   22.344 -31.059 1.00 20.13 ? 158 GLU A CA  1 
ATOM   1259 C C   . GLU A 1 180 ? 0.376   23.584 -30.187 1.00 21.67 ? 158 GLU A C   1 
ATOM   1260 O O   . GLU A 1 180 ? -0.296  24.590 -30.408 1.00 25.11 ? 158 GLU A O   1 
ATOM   1261 C CB  . GLU A 1 180 ? 0.125   22.719 -32.534 1.00 21.85 ? 158 GLU A CB  1 
ATOM   1262 C CG  . GLU A 1 180 ? 0.204   21.531 -33.467 1.00 32.35 ? 158 GLU A CG  1 
ATOM   1263 C CD  . GLU A 1 180 ? 0.204   21.937 -34.927 1.00 57.42 ? 158 GLU A CD  1 
ATOM   1264 O OE1 . GLU A 1 180 ? 0.733   21.160 -35.753 1.00 59.67 ? 158 GLU A OE1 1 
ATOM   1265 O OE2 . GLU A 1 180 ? -0.329  23.024 -35.246 1.00 51.52 ? 158 GLU A OE2 1 
ATOM   1266 N N   . MET A 1 181 ? 1.227   23.501 -29.181 1.00 16.02 ? 159 MET A N   1 
ATOM   1267 C CA  . MET A 1 181 ? 1.413   24.543 -28.185 1.00 18.35 ? 159 MET A CA  1 
ATOM   1268 C C   . MET A 1 181 ? 2.556   25.472 -28.593 1.00 22.00 ? 159 MET A C   1 
ATOM   1269 O O   . MET A 1 181 ? 3.455   25.096 -29.356 1.00 16.17 ? 159 MET A O   1 
ATOM   1270 C CB  . MET A 1 181 ? 1.748   23.887 -26.850 1.00 16.97 ? 159 MET A CB  1 
ATOM   1271 C CG  . MET A 1 181 ? 0.620   23.214 -26.066 1.00 21.39 ? 159 MET A CG  1 
ATOM   1272 S SD  . MET A 1 181 ? -0.748  24.209 -25.471 1.00 20.05 ? 159 MET A SD  1 
ATOM   1273 C CE  . MET A 1 181 ? -0.097  24.465 -23.834 1.00 18.74 ? 159 MET A CE  1 
ATOM   1274 N N   . ALA A 1 182 ? 2.554   26.682 -28.031 1.00 19.01 ? 160 ALA A N   1 
ATOM   1275 C CA  . ALA A 1 182 ? 3.665   27.596 -28.262 1.00 18.11 ? 160 ALA A CA  1 
ATOM   1276 C C   . ALA A 1 182 ? 3.916   28.432 -27.018 1.00 20.55 ? 160 ALA A C   1 
ATOM   1277 O O   . ALA A 1 182 ? 2.983   29.008 -26.457 1.00 15.92 ? 160 ALA A O   1 
ATOM   1278 C CB  . ALA A 1 182 ? 3.400   28.506 -29.471 1.00 21.84 ? 160 ALA A CB  1 
ATOM   1279 N N   . LEU A 1 183 ? 5.176   28.485 -26.594 1.00 18.18 ? 161 LEU A N   1 
ATOM   1280 C CA  . LEU A 1 183 ? 5.626   29.405 -25.556 1.00 17.92 ? 161 LEU A CA  1 
ATOM   1281 C C   . LEU A 1 183 ? 6.075   30.723 -26.175 1.00 21.82 ? 161 LEU A C   1 
ATOM   1282 O O   . LEU A 1 183 ? 6.945   30.740 -27.053 1.00 20.94 ? 161 LEU A O   1 
ATOM   1283 C CB  . LEU A 1 183 ? 6.796   28.814 -24.767 1.00 18.57 ? 161 LEU A CB  1 
ATOM   1284 C CG  . LEU A 1 183 ? 6.423   27.886 -23.615 1.00 20.64 ? 161 LEU A CG  1 
ATOM   1285 C CD1 . LEU A 1 183 ? 7.625   27.050 -23.215 1.00 21.64 ? 161 LEU A CD1 1 
ATOM   1286 C CD2 . LEU A 1 183 ? 5.863   28.692 -22.452 1.00 18.08 ? 161 LEU A CD2 1 
ATOM   1287 N N   . LEU A 1 184 ? 5.511   31.824 -25.687 1.00 15.82 ? 162 LEU A N   1 
ATOM   1288 C CA  . LEU A 1 184 ? 6.032   33.131 -26.034 1.00 19.08 ? 162 LEU A CA  1 
ATOM   1289 C C   . LEU A 1 184 ? 7.345   33.359 -25.289 1.00 24.92 ? 162 LEU A C   1 
ATOM   1290 O O   . LEU A 1 184 ? 7.435   33.102 -24.087 1.00 22.95 ? 162 LEU A O   1 
ATOM   1291 C CB  . LEU A 1 184 ? 5.002   34.210 -25.683 1.00 17.92 ? 162 LEU A CB  1 
ATOM   1292 C CG  . LEU A 1 184 ? 5.492   35.631 -25.979 1.00 23.37 ? 162 LEU A CG  1 
ATOM   1293 C CD1 . LEU A 1 184 ? 5.696   35.804 -27.479 1.00 36.68 ? 162 LEU A CD1 1 
ATOM   1294 C CD2 . LEU A 1 184 ? 4.523   36.667 -25.449 1.00 30.65 ? 162 LEU A CD2 1 
ATOM   1295 N N   . LEU A 1 185 ? 8.372   33.820 -26.003 1.00 22.34 ? 163 LEU A N   1 
ATOM   1296 C CA  . LEU A 1 185 ? 9.676   34.102 -25.420 1.00 28.09 ? 163 LEU A CA  1 
ATOM   1297 C C   . LEU A 1 185 ? 9.909   35.600 -25.350 1.00 31.79 ? 163 LEU A C   1 
ATOM   1298 O O   . LEU A 1 185 ? 9.284   36.384 -26.075 1.00 27.21 ? 163 LEU A O   1 
ATOM   1299 C CB  . LEU A 1 185 ? 10.820  33.485 -26.236 1.00 23.05 ? 163 LEU A CB  1 
ATOM   1300 C CG  . LEU A 1 185 ? 10.744  31.986 -26.514 1.00 24.40 ? 163 LEU A CG  1 
ATOM   1301 C CD1 . LEU A 1 185 ? 11.902  31.568 -27.389 1.00 24.68 ? 163 LEU A CD1 1 
ATOM   1302 C CD2 . LEU A 1 185 ? 10.708  31.204 -25.209 1.00 22.43 ? 163 LEU A CD2 1 
ATOM   1303 N N   . GLU A 1 186 ? 10.851  35.979 -24.491 1.00 31.93 ? 164 GLU A N   1 
ATOM   1304 C CA  . GLU A 1 186 ? 11.361  37.342 -24.517 1.00 35.18 ? 164 GLU A CA  1 
ATOM   1305 C C   . GLU A 1 186 ? 11.881  37.658 -25.916 1.00 45.40 ? 164 GLU A C   1 
ATOM   1306 O O   . GLU A 1 186 ? 12.505  36.817 -26.570 1.00 43.28 ? 164 GLU A O   1 
ATOM   1307 C CB  . GLU A 1 186 ? 12.473  37.522 -23.482 1.00 46.62 ? 164 GLU A CB  1 
ATOM   1308 C CG  . GLU A 1 186 ? 11.976  37.647 -22.048 1.00 53.89 ? 164 GLU A CG  1 
ATOM   1309 C CD  . GLU A 1 186 ? 13.080  37.431 -21.016 1.00 60.76 ? 164 GLU A CD  1 
ATOM   1310 O OE1 . GLU A 1 186 ? 14.269  37.613 -21.367 1.00 64.12 ? 164 GLU A OE1 1 
ATOM   1311 O OE2 . GLU A 1 186 ? 12.760  37.090 -19.854 1.00 52.41 ? 164 GLU A OE2 1 
ATOM   1312 N N   . GLY A 1 187 ? 11.606  38.872 -26.383 1.00 46.54 ? 165 GLY A N   1 
ATOM   1313 C CA  . GLY A 1 187 ? 11.856  39.220 -27.765 1.00 42.92 ? 165 GLY A CA  1 
ATOM   1314 C C   . GLY A 1 187 ? 10.729  38.880 -28.719 1.00 46.97 ? 165 GLY A C   1 
ATOM   1315 O O   . GLY A 1 187 ? 10.832  39.193 -29.911 1.00 46.95 ? 165 GLY A O   1 
ATOM   1316 N N   . ASN A 1 188 ? 9.667   38.239 -28.234 1.00 42.13 ? 166 ASN A N   1 
ATOM   1317 C CA  . ASN A 1 188 ? 8.438   37.917 -28.961 1.00 44.86 ? 166 ASN A CA  1 
ATOM   1318 C C   . ASN A 1 188 ? 8.574   36.767 -29.955 1.00 47.40 ? 166 ASN A C   1 
ATOM   1319 O O   . ASN A 1 188 ? 7.649   36.535 -30.746 1.00 47.89 ? 166 ASN A O   1 
ATOM   1320 C CB  . ASN A 1 188 ? 7.859   39.137 -29.682 1.00 49.52 ? 166 ASN A CB  1 
ATOM   1321 C CG  . ASN A 1 188 ? 6.633   39.682 -28.981 1.00 71.68 ? 166 ASN A CG  1 
ATOM   1322 O OD1 . ASN A 1 188 ? 6.610   39.801 -27.750 1.00 59.39 ? 166 ASN A OD1 1 
ATOM   1323 N ND2 . ASN A 1 188 ? 5.593   39.988 -29.755 1.00 74.01 ? 166 ASN A ND2 1 
ATOM   1324 N N   . ALA A 1 189 ? 9.680   36.030 -29.935 1.00 44.03 ? 167 ALA A N   1 
ATOM   1325 C CA  . ALA A 1 189 ? 9.737   34.780 -30.672 1.00 36.53 ? 167 ALA A CA  1 
ATOM   1326 C C   . ALA A 1 189 ? 8.797   33.757 -30.032 1.00 28.06 ? 167 ALA A C   1 
ATOM   1327 O O   . ALA A 1 189 ? 8.312   33.940 -28.912 1.00 27.28 ? 167 ALA A O   1 
ATOM   1328 C CB  . ALA A 1 189 ? 11.167  34.242 -30.701 1.00 34.70 ? 167 ALA A CB  1 
ATOM   1329 N N   . HIS A 1 190 ? 8.528   32.670 -30.754 1.00 26.70 ? 168 HIS A N   1 
ATOM   1330 C CA  . HIS A 1 190 ? 7.771   31.563 -30.186 1.00 24.06 ? 168 HIS A CA  1 
ATOM   1331 C C   . HIS A 1 190 ? 8.589   30.280 -30.220 1.00 23.02 ? 168 HIS A C   1 
ATOM   1332 O O   . HIS A 1 190 ? 9.493   30.109 -31.046 1.00 27.31 ? 168 HIS A O   1 
ATOM   1333 C CB  . HIS A 1 190 ? 6.428   31.360 -30.898 1.00 28.42 ? 168 HIS A CB  1 
ATOM   1334 C CG  . HIS A 1 190 ? 5.396   32.363 -30.484 1.00 33.17 ? 168 HIS A CG  1 
ATOM   1335 N ND1 . HIS A 1 190 ? 5.329   33.623 -31.039 1.00 28.69 ? 168 HIS A ND1 1 
ATOM   1336 C CD2 . HIS A 1 190 ? 4.430   32.317 -29.534 1.00 27.71 ? 168 HIS A CD2 1 
ATOM   1337 C CE1 . HIS A 1 190 ? 4.349   34.302 -30.469 1.00 34.34 ? 168 HIS A CE1 1 
ATOM   1338 N NE2 . HIS A 1 190 ? 3.786   33.533 -29.554 1.00 27.53 ? 168 HIS A NE2 1 
ATOM   1339 N N   . TYR A 1 191 ? 8.260   29.392 -29.291 1.00 21.05 ? 169 TYR A N   1 
ATOM   1340 C CA  . TYR A 1 191 ? 9.002   28.161 -29.026 1.00 23.24 ? 169 TYR A CA  1 
ATOM   1341 C C   . TYR A 1 191 ? 7.981   27.033 -28.979 1.00 21.09 ? 169 TYR A C   1 
ATOM   1342 O O   . TYR A 1 191 ? 7.196   26.950 -28.031 1.00 20.13 ? 169 TYR A O   1 
ATOM   1343 C CB  . TYR A 1 191 ? 9.767   28.294 -27.708 1.00 23.14 ? 169 TYR A CB  1 
ATOM   1344 C CG  . TYR A 1 191 ? 10.483  27.067 -27.178 1.00 23.55 ? 169 TYR A CG  1 
ATOM   1345 C CD1 . TYR A 1 191 ? 11.441  26.399 -27.940 1.00 22.87 ? 169 TYR A CD1 1 
ATOM   1346 C CD2 . TYR A 1 191 ? 10.249  26.628 -25.882 1.00 20.12 ? 169 TYR A CD2 1 
ATOM   1347 C CE1 . TYR A 1 191 ? 12.120  25.287 -27.426 1.00 27.49 ? 169 TYR A CE1 1 
ATOM   1348 C CE2 . TYR A 1 191 ? 10.917  25.534 -25.357 1.00 23.00 ? 169 TYR A CE2 1 
ATOM   1349 C CZ  . TYR A 1 191 ? 11.848  24.862 -26.132 1.00 23.92 ? 169 TYR A CZ  1 
ATOM   1350 O OH  . TYR A 1 191 ? 12.511  23.770 -25.583 1.00 20.95 ? 169 TYR A OH  1 
ATOM   1351 N N   . ARG A 1 192 ? 7.974   26.194 -30.014 1.00 19.09 ? 170 ARG A N   1 
ATOM   1352 C CA  . ARG A 1 192 ? 6.881   25.262 -30.272 1.00 19.39 ? 170 ARG A CA  1 
ATOM   1353 C C   . ARG A 1 192 ? 6.998   24.006 -29.416 1.00 18.78 ? 170 ARG A C   1 
ATOM   1354 O O   . ARG A 1 192 ? 8.091   23.516 -29.131 1.00 18.76 ? 170 ARG A O   1 
ATOM   1355 C CB  . ARG A 1 192 ? 6.872   24.847 -31.747 1.00 20.26 ? 170 ARG A CB  1 
ATOM   1356 C CG  . ARG A 1 192 ? 6.297   23.425 -31.991 1.00 36.61 ? 170 ARG A CG  1 
ATOM   1357 C CD  . ARG A 1 192 ? 6.218   23.012 -33.450 1.00 46.58 ? 170 ARG A CD  1 
ATOM   1358 N NE  . ARG A 1 192 ? 5.454   21.782 -33.659 1.00 38.49 ? 170 ARG A NE  1 
ATOM   1359 C CZ  . ARG A 1 192 ? 5.103   21.322 -34.855 1.00 46.09 ? 170 ARG A CZ  1 
ATOM   1360 N NH1 . ARG A 1 192 ? 5.453   21.950 -35.968 1.00 41.33 ? 170 ARG A NH1 1 
ATOM   1361 N NH2 . ARG A 1 192 ? 4.419   20.181 -34.941 1.00 42.02 ? 170 ARG A NH2 1 
ATOM   1362 N N   . CYS A 1 193 ? 5.849   23.469 -29.032 1.00 14.84 ? 171 CYS A N   1 
ATOM   1363 C CA  . CYS A 1 193 ? 5.811   22.217 -28.291 1.00 16.97 ? 171 CYS A CA  1 
ATOM   1364 C C   . CYS A 1 193 ? 4.573   21.445 -28.721 1.00 19.35 ? 171 CYS A C   1 
ATOM   1365 O O   . CYS A 1 193 ? 3.474   22.008 -28.716 1.00 24.84 ? 171 CYS A O   1 
ATOM   1366 C CB  . CYS A 1 193 ? 5.789   22.483 -26.783 1.00 16.98 ? 171 CYS A CB  1 
ATOM   1367 S SG  . CYS A 1 193 ? 5.774   20.968 -25.786 1.00 17.86 ? 171 CYS A SG  1 
ATOM   1368 N N   . ASP A 1 194 ? 4.746   20.187 -29.119 1.00 16.66 ? 172 ASP A N   1 
ATOM   1369 C CA  . ASP A 1 194 ? 3.606   19.312 -29.389 1.00 20.31 ? 172 ASP A CA  1 
ATOM   1370 C C   . ASP A 1 194 ? 3.221   18.524 -28.140 1.00 19.84 ? 172 ASP A C   1 
ATOM   1371 O O   . ASP A 1 194 ? 4.078   17.901 -27.505 1.00 16.77 ? 172 ASP A O   1 
ATOM   1372 C CB  . ASP A 1 194 ? 3.904   18.354 -30.540 1.00 22.46 ? 172 ASP A CB  1 
ATOM   1373 C CG  . ASP A 1 194 ? 4.387   19.074 -31.773 1.00 33.27 ? 172 ASP A CG  1 
ATOM   1374 O OD1 . ASP A 1 194 ? 3.631   19.945 -32.245 1.00 30.13 ? 172 ASP A OD1 1 
ATOM   1375 O OD2 . ASP A 1 194 ? 5.504   18.779 -32.263 1.00 35.46 ? 172 ASP A OD2 1 
ATOM   1376 N N   . PHE A 1 195 ? 1.932   18.570 -27.791 1.00 16.58 ? 173 PHE A N   1 
ATOM   1377 C CA  . PHE A 1 195 ? 1.339   17.804 -26.698 1.00 16.40 ? 173 PHE A CA  1 
ATOM   1378 C C   . PHE A 1 195 ? 0.563   16.625 -27.269 1.00 17.19 ? 173 PHE A C   1 
ATOM   1379 O O   . PHE A 1 195 ? -0.218  16.787 -28.215 1.00 14.83 ? 173 PHE A O   1 
ATOM   1380 C CB  . PHE A 1 195 ? 0.314   18.629 -25.898 1.00 15.41 ? 173 PHE A CB  1 
ATOM   1381 C CG  . PHE A 1 195 ? 0.893   19.555 -24.858 1.00 16.03 ? 173 PHE A CG  1 
ATOM   1382 C CD1 . PHE A 1 195 ? 2.169   20.083 -24.968 1.00 16.06 ? 173 PHE A CD1 1 
ATOM   1383 C CD2 . PHE A 1 195 ? 0.104   19.934 -23.776 1.00 15.23 ? 173 PHE A CD2 1 
ATOM   1384 C CE1 . PHE A 1 195 ? 2.661   20.982 -23.998 1.00 19.95 ? 173 PHE A CE1 1 
ATOM   1385 C CE2 . PHE A 1 195 ? 0.582   20.823 -22.796 1.00 16.62 ? 173 PHE A CE2 1 
ATOM   1386 C CZ  . PHE A 1 195 ? 1.871   21.339 -22.906 1.00 18.52 ? 173 PHE A CZ  1 
ATOM   1387 N N   . ARG A 1 196 ? 0.727   15.453 -26.664 1.00 20.43 ? 174 ARG A N   1 
ATOM   1388 C CA  . ARG A 1 196 ? -0.276  14.398 -26.801 1.00 20.86 ? 174 ARG A CA  1 
ATOM   1389 C C   . ARG A 1 196 ? -0.568  13.847 -25.417 1.00 16.12 ? 174 ARG A C   1 
ATOM   1390 O O   . ARG A 1 196 ? 0.356   13.449 -24.701 1.00 15.06 ? 174 ARG A O   1 
ATOM   1391 C CB  . ARG A 1 196 ? 0.168   13.278 -27.742 1.00 21.83 ? 174 ARG A CB  1 
ATOM   1392 C CG  . ARG A 1 196 ? -0.822  12.106 -27.713 1.00 22.10 ? 174 ARG A CG  1 
ATOM   1393 C CD  . ARG A 1 196 ? -0.617  11.150 -28.868 1.00 27.44 ? 174 ARG A CD  1 
ATOM   1394 N NE  . ARG A 1 196 ? -1.109  11.720 -30.115 1.00 18.62 ? 174 ARG A NE  1 
ATOM   1395 C CZ  . ARG A 1 196 ? -0.995  11.127 -31.290 1.00 23.67 ? 174 ARG A CZ  1 
ATOM   1396 N NH1 . ARG A 1 196 ? -0.429  9.934  -31.407 1.00 29.13 ? 174 ARG A NH1 1 
ATOM   1397 N NH2 . ARG A 1 196 ? -1.449  11.747 -32.377 1.00 26.69 ? 174 ARG A NH2 1 
ATOM   1398 N N   . THR A 1 197 ? -1.836  13.870 -25.030 1.00 18.82 ? 175 THR A N   1 
ATOM   1399 C CA  . THR A 1 197 ? -2.300  13.345 -23.752 1.00 18.47 ? 175 THR A CA  1 
ATOM   1400 C C   . THR A 1 197 ? -3.269  12.204 -24.006 1.00 20.10 ? 175 THR A C   1 
ATOM   1401 O O   . THR A 1 197 ? -4.144  12.316 -24.868 1.00 17.16 ? 175 THR A O   1 
ATOM   1402 C CB  . THR A 1 197 ? -3.017  14.423 -22.929 1.00 19.04 ? 175 THR A CB  1 
ATOM   1403 O OG1 . THR A 1 197 ? -2.243  15.623 -22.940 1.00 18.46 ? 175 THR A OG1 1 
ATOM   1404 C CG2 . THR A 1 197 ? -3.228  13.947 -21.473 1.00 14.68 ? 175 THR A CG2 1 
ATOM   1405 N N   . THR A 1 198 ? -3.124  11.108 -23.262 1.00 14.89 ? 176 THR A N   1 
ATOM   1406 C CA  . THR A 1 198 ? -4.146  10.071 -23.249 1.00 19.32 ? 176 THR A CA  1 
ATOM   1407 C C   . THR A 1 198 ? -4.826  10.105 -21.888 1.00 19.19 ? 176 THR A C   1 
ATOM   1408 O O   . THR A 1 198 ? -4.177  10.387 -20.874 1.00 18.27 ? 176 THR A O   1 
ATOM   1409 C CB  . THR A 1 198 ? -3.554  8.688  -23.539 1.00 22.04 ? 176 THR A CB  1 
ATOM   1410 O OG1 . THR A 1 198 ? -2.453  8.444  -22.656 1.00 18.76 ? 176 THR A OG1 1 
ATOM   1411 C CG2 . THR A 1 198 ? -3.065  8.594  -25.013 1.00 22.82 ? 176 THR A CG2 1 
ATOM   1412 N N   . TYR A 1 199 ? -6.135  9.843  -21.876 1.00 20.22 ? 177 TYR A N   1 
ATOM   1413 C CA  . TYR A 1 199 ? -6.980  10.000 -20.700 1.00 19.15 ? 177 TYR A CA  1 
ATOM   1414 C C   . TYR A 1 199 ? -7.720  8.695  -20.471 1.00 18.72 ? 177 TYR A C   1 
ATOM   1415 O O   . TYR A 1 199 ? -8.286  8.140  -21.415 1.00 18.32 ? 177 TYR A O   1 
ATOM   1416 C CB  . TYR A 1 199 ? -8.014  11.119 -20.886 1.00 16.80 ? 177 TYR A CB  1 
ATOM   1417 C CG  . TYR A 1 199 ? -7.460  12.488 -21.201 1.00 14.89 ? 177 TYR A CG  1 
ATOM   1418 C CD1 . TYR A 1 199 ? -7.101  13.366 -20.178 1.00 13.20 ? 177 TYR A CD1 1 
ATOM   1419 C CD2 . TYR A 1 199 ? -7.300  12.903 -22.518 1.00 17.70 ? 177 TYR A CD2 1 
ATOM   1420 C CE1 . TYR A 1 199 ? -6.623  14.620 -20.453 1.00 14.14 ? 177 TYR A CE1 1 
ATOM   1421 C CE2 . TYR A 1 199 ? -6.816  14.182 -22.808 1.00 17.16 ? 177 TYR A CE2 1 
ATOM   1422 C CZ  . TYR A 1 199 ? -6.491  15.024 -21.759 1.00 12.25 ? 177 TYR A CZ  1 
ATOM   1423 O OH  . TYR A 1 199 ? -5.994  16.284 -22.006 1.00 17.35 ? 177 TYR A OH  1 
ATOM   1424 N N   . LYS A 1 200 ? -7.772  8.233  -19.221 1.00 18.66 ? 178 LYS A N   1 
ATOM   1425 C CA  . LYS A 1 200 ? -8.410  6.953  -18.922 1.00 19.33 ? 178 LYS A CA  1 
ATOM   1426 C C   . LYS A 1 200 ? -9.112  6.984  -17.570 1.00 22.75 ? 178 LYS A C   1 
ATOM   1427 O O   . LYS A 1 200 ? -8.463  7.117  -16.525 1.00 21.52 ? 178 LYS A O   1 
ATOM   1428 C CB  . LYS A 1 200 ? -7.381  5.815  -18.949 1.00 26.56 ? 178 LYS A CB  1 
ATOM   1429 C CG  . LYS A 1 200 ? -7.993  4.409  -18.817 1.00 32.58 ? 178 LYS A CG  1 
ATOM   1430 C CD  . LYS A 1 200 ? -9.304  4.189  -19.597 1.00 48.66 ? 178 LYS A CD  1 
ATOM   1431 C CE  . LYS A 1 200 ? -9.055  4.018  -21.103 1.00 52.94 ? 178 LYS A CE  1 
ATOM   1432 N NZ  . LYS A 1 200 ? -10.280 4.088  -21.990 1.00 37.70 ? 178 LYS A NZ  1 
ATOM   1433 N N   . ALA A 1 201 ? -10.429 6.792  -17.591 1.00 21.09 ? 179 ALA A N   1 
ATOM   1434 C CA  . ALA A 1 201 ? -11.190 6.634  -16.362 1.00 22.70 ? 179 ALA A CA  1 
ATOM   1435 C C   . ALA A 1 201 ? -10.764 5.369  -15.629 1.00 25.09 ? 179 ALA A C   1 
ATOM   1436 O O   . ALA A 1 201 ? -10.400 4.362  -16.245 1.00 28.53 ? 179 ALA A O   1 
ATOM   1437 C CB  . ALA A 1 201 ? -12.685 6.564  -16.673 1.00 23.38 ? 179 ALA A CB  1 
ATOM   1438 N N   . LYS A 1 202 ? -10.830 5.427  -14.296 1.00 26.54 ? 180 LYS A N   1 
ATOM   1439 C CA  . LYS A 1 202 ? -10.520 4.254  -13.480 1.00 29.39 ? 180 LYS A CA  1 
ATOM   1440 C C   . LYS A 1 202 ? -11.648 3.232  -13.526 1.00 31.59 ? 180 LYS A C   1 
ATOM   1441 O O   . LYS A 1 202 ? -11.401 2.024  -13.474 1.00 34.44 ? 180 LYS A O   1 
ATOM   1442 C CB  . LYS A 1 202 ? -10.246 4.681  -12.037 1.00 31.99 ? 180 LYS A CB  1 
ATOM   1443 C CG  . LYS A 1 202 ? -8.920  5.412  -11.880 1.00 29.46 ? 180 LYS A CG  1 
ATOM   1444 C CD  . LYS A 1 202 ? -8.627  5.785  -10.431 1.00 46.88 ? 180 LYS A CD  1 
ATOM   1445 C CE  . LYS A 1 202 ? -7.937  7.148  -10.364 1.00 35.02 ? 180 LYS A CE  1 
ATOM   1446 N NZ  . LYS A 1 202 ? -6.462  6.984  -10.261 1.00 48.31 ? 180 LYS A NZ  1 
ATOM   1447 N N   . GLU A 1 203 ? -12.893 3.698  -13.589 1.00 31.23 ? 181 GLU A N   1 
ATOM   1448 C CA  . GLU A 1 203 ? -14.047 2.817  -13.612 1.00 35.68 ? 181 GLU A CA  1 
ATOM   1449 C C   . GLU A 1 203 ? -14.294 2.301  -15.023 1.00 36.87 ? 181 GLU A C   1 
ATOM   1450 O O   . GLU A 1 203 ? -14.191 3.053  -15.993 1.00 33.50 ? 181 GLU A O   1 
ATOM   1451 C CB  . GLU A 1 203 ? -15.279 3.569  -13.121 1.00 35.60 ? 181 GLU A CB  1 
ATOM   1452 C CG  . GLU A 1 203 ? -16.517 2.727  -13.006 1.00 42.76 ? 181 GLU A CG  1 
ATOM   1453 C CD  . GLU A 1 203 ? -17.645 3.485  -12.355 1.00 59.36 ? 181 GLU A CD  1 
ATOM   1454 O OE1 . GLU A 1 203 ? -17.959 3.201  -11.179 1.00 60.33 ? 181 GLU A OE1 1 
ATOM   1455 O OE2 . GLU A 1 203 ? -18.212 4.374  -13.034 1.00 50.02 ? 181 GLU A OE2 1 
ATOM   1456 N N   . LYS A 1 204 ? -14.628 1.016  -15.137 1.00 36.67 ? 182 LYS A N   1 
ATOM   1457 C CA  . LYS A 1 204 ? -14.890 0.450  -16.452 1.00 38.55 ? 182 LYS A CA  1 
ATOM   1458 C C   . LYS A 1 204 ? -16.204 0.991  -17.001 1.00 41.06 ? 182 LYS A C   1 
ATOM   1459 O O   . LYS A 1 204 ? -17.157 1.222  -16.255 1.00 42.95 ? 182 LYS A O   1 
ATOM   1460 C CB  . LYS A 1 204 ? -14.943 -1.081 -16.384 1.00 45.20 ? 182 LYS A CB  1 
ATOM   1461 C CG  . LYS A 1 204 ? -13.599 -1.735 -16.670 1.00 52.66 ? 182 LYS A CG  1 
ATOM   1462 C CD  . LYS A 1 204 ? -12.968 -1.181 -17.945 1.00 63.52 ? 182 LYS A CD  1 
ATOM   1463 C CE  . LYS A 1 204 ? -11.449 -1.312 -17.912 1.00 72.57 ? 182 LYS A CE  1 
ATOM   1464 N NZ  . LYS A 1 204 ? -10.859 -1.408 -19.276 1.00 78.51 ? 182 LYS A NZ  1 
ATOM   1465 N N   . GLY A 1 205 ? -16.250 1.213  -18.311 1.00 44.80 ? 183 GLY A N   1 
ATOM   1466 C CA  . GLY A 1 205 ? -17.513 1.494  -18.967 1.00 44.57 ? 183 GLY A CA  1 
ATOM   1467 C C   . GLY A 1 205 ? -17.954 2.941  -18.996 1.00 42.80 ? 183 GLY A C   1 
ATOM   1468 O O   . GLY A 1 205 ? -19.104 3.207  -19.374 1.00 37.11 ? 183 GLY A O   1 
ATOM   1469 N N   . VAL A 1 206 ? -17.097 3.881  -18.593 1.00 33.65 ? 184 VAL A N   1 
ATOM   1470 C CA  . VAL A 1 206 ? -17.402 5.299  -18.772 1.00 30.86 ? 184 VAL A CA  1 
ATOM   1471 C C   . VAL A 1 206 ? -17.497 5.588  -20.264 1.00 32.90 ? 184 VAL A C   1 
ATOM   1472 O O   . VAL A 1 206 ? -16.572 5.283  -21.031 1.00 29.02 ? 184 VAL A O   1 
ATOM   1473 C CB  . VAL A 1 206 ? -16.333 6.185  -18.109 1.00 32.09 ? 184 VAL A CB  1 
ATOM   1474 C CG1 . VAL A 1 206 ? -16.656 7.658  -18.335 1.00 27.71 ? 184 VAL A CG1 1 
ATOM   1475 C CG2 . VAL A 1 206 ? -16.200 5.889  -16.615 1.00 27.31 ? 184 VAL A CG2 1 
ATOM   1476 N N   . LYS A 1 207 ? -18.607 6.191  -20.679 1.00 28.71 ? 185 LYS A N   1 
ATOM   1477 C CA  . LYS A 1 207 ? -18.861 6.410  -22.097 1.00 31.09 ? 185 LYS A CA  1 
ATOM   1478 C C   . LYS A 1 207 ? -17.863 7.407  -22.688 1.00 29.70 ? 185 LYS A C   1 
ATOM   1479 O O   . LYS A 1 207 ? -17.679 8.509  -22.165 1.00 26.59 ? 185 LYS A O   1 
ATOM   1480 C CB  . LYS A 1 207 ? -20.292 6.901  -22.303 1.00 33.74 ? 185 LYS A CB  1 
ATOM   1481 C CG  . LYS A 1 207 ? -20.739 6.852  -23.756 1.00 44.69 ? 185 LYS A CG  1 
ATOM   1482 C CD  . LYS A 1 207 ? -22.109 7.480  -23.966 1.00 47.93 ? 185 LYS A CD  1 
ATOM   1483 C CE  . LYS A 1 207 ? -22.636 7.152  -25.367 1.00 51.85 ? 185 LYS A CE  1 
ATOM   1484 N NZ  . LYS A 1 207 ? -23.885 7.894  -25.692 1.00 49.61 ? 185 LYS A NZ  1 
ATOM   1485 N N   . LEU A 1 208 ? -17.226 7.019  -23.792 1.00 26.74 ? 186 LEU A N   1 
ATOM   1486 C CA  . LEU A 1 208 ? -16.295 7.913  -24.467 1.00 26.67 ? 186 LEU A CA  1 
ATOM   1487 C C   . LEU A 1 208 ? -17.045 9.001  -25.236 1.00 23.67 ? 186 LEU A C   1 
ATOM   1488 O O   . LEU A 1 208 ? -18.146 8.771  -25.740 1.00 25.06 ? 186 LEU A O   1 
ATOM   1489 C CB  . LEU A 1 208 ? -15.399 7.121  -25.419 1.00 26.90 ? 186 LEU A CB  1 
ATOM   1490 C CG  . LEU A 1 208 ? -14.474 6.156  -24.679 1.00 34.30 ? 186 LEU A CG  1 
ATOM   1491 C CD1 . LEU A 1 208 ? -14.022 5.022  -25.572 1.00 38.14 ? 186 LEU A CD1 1 
ATOM   1492 C CD2 . LEU A 1 208 ? -13.291 6.936  -24.194 1.00 29.02 ? 186 LEU A CD2 1 
ATOM   1493 N N   . PRO A 1 209 ? -16.456 10.189 -25.357 1.00 21.52 ? 187 PRO A N   1 
ATOM   1494 C CA  . PRO A 1 209 ? -17.117 11.284 -26.075 1.00 21.75 ? 187 PRO A CA  1 
ATOM   1495 C C   . PRO A 1 209 ? -16.891 11.148 -27.576 1.00 29.45 ? 187 PRO A C   1 
ATOM   1496 O O   . PRO A 1 209 ? -16.026 10.403 -28.037 1.00 23.68 ? 187 PRO A O   1 
ATOM   1497 C CB  . PRO A 1 209 ? -16.399 12.534 -25.548 1.00 19.91 ? 187 PRO A CB  1 
ATOM   1498 C CG  . PRO A 1 209 ? -14.969 12.026 -25.278 1.00 19.72 ? 187 PRO A CG  1 
ATOM   1499 C CD  . PRO A 1 209 ? -15.102 10.555 -24.896 1.00 21.18 ? 187 PRO A CD  1 
ATOM   1500 N N   . GLY A 1 210 ? -17.665 11.913 -28.336 1.00 23.74 ? 188 GLY A N   1 
ATOM   1501 C CA  . GLY A 1 210 ? -17.355 12.100 -29.739 1.00 26.93 ? 188 GLY A CA  1 
ATOM   1502 C C   . GLY A 1 210 ? -16.186 13.062 -29.906 1.00 22.62 ? 188 GLY A C   1 
ATOM   1503 O O   . GLY A 1 210 ? -15.726 13.688 -28.956 1.00 23.59 ? 188 GLY A O   1 
ATOM   1504 N N   . ALA A 1 211 ? -15.689 13.182 -31.138 1.00 23.28 ? 189 ALA A N   1 
ATOM   1505 C CA  . ALA A 1 211 ? -14.585 14.110 -31.378 1.00 22.49 ? 189 ALA A CA  1 
ATOM   1506 C C   . ALA A 1 211 ? -15.036 15.538 -31.072 1.00 21.82 ? 189 ALA A C   1 
ATOM   1507 O O   . ALA A 1 211 ? -16.162 15.925 -31.404 1.00 23.82 ? 189 ALA A O   1 
ATOM   1508 C CB  . ALA A 1 211 ? -14.115 14.002 -32.840 1.00 23.26 ? 189 ALA A CB  1 
ATOM   1509 N N   . HIS A 1 212 ? -14.160 16.321 -30.442 1.00 19.70 ? 190 HIS A N   1 
ATOM   1510 C CA  . HIS A 1 212 ? -14.497 17.700 -30.087 1.00 20.38 ? 190 HIS A CA  1 
ATOM   1511 C C   . HIS A 1 212 ? -13.203 18.459 -29.782 1.00 21.49 ? 190 HIS A C   1 
ATOM   1512 O O   . HIS A 1 212 ? -12.097 17.970 -30.042 1.00 17.62 ? 190 HIS A O   1 
ATOM   1513 C CB  . HIS A 1 212 ? -15.498 17.738 -28.921 1.00 18.26 ? 190 HIS A CB  1 
ATOM   1514 C CG  . HIS A 1 212 ? -14.950 17.223 -27.622 1.00 17.59 ? 190 HIS A CG  1 
ATOM   1515 N ND1 . HIS A 1 212 ? -14.846 15.877 -27.336 1.00 17.27 ? 190 HIS A ND1 1 
ATOM   1516 C CD2 . HIS A 1 212 ? -14.465 17.878 -26.536 1.00 16.82 ? 190 HIS A CD2 1 
ATOM   1517 C CE1 . HIS A 1 212 ? -14.327 15.725 -26.125 1.00 16.49 ? 190 HIS A CE1 1 
ATOM   1518 N NE2 . HIS A 1 212 ? -14.093 16.924 -25.616 1.00 16.81 ? 190 HIS A NE2 1 
ATOM   1519 N N   . PHE A 1 213 ? -13.341 19.679 -29.266 1.00 16.93 ? 191 PHE A N   1 
ATOM   1520 C CA  . PHE A 1 213 ? -12.198 20.541 -28.990 1.00 16.57 ? 191 PHE A CA  1 
ATOM   1521 C C   . PHE A 1 213 ? -12.339 21.160 -27.601 1.00 22.09 ? 191 PHE A C   1 
ATOM   1522 O O   . PHE A 1 213 ? -13.449 21.365 -27.100 1.00 18.37 ? 191 PHE A O   1 
ATOM   1523 C CB  . PHE A 1 213 ? -12.090 21.666 -30.050 1.00 17.56 ? 191 PHE A CB  1 
ATOM   1524 C CG  . PHE A 1 213 ? -12.004 21.158 -31.462 1.00 24.85 ? 191 PHE A CG  1 
ATOM   1525 C CD1 . PHE A 1 213 ? -10.772 20.818 -32.021 1.00 27.79 ? 191 PHE A CD1 1 
ATOM   1526 C CD2 . PHE A 1 213 ? -13.156 20.977 -32.223 1.00 32.52 ? 191 PHE A CD2 1 
ATOM   1527 C CE1 . PHE A 1 213 ? -10.690 20.339 -33.317 1.00 25.30 ? 191 PHE A CE1 1 
ATOM   1528 C CE2 . PHE A 1 213 ? -13.077 20.490 -33.526 1.00 37.12 ? 191 PHE A CE2 1 
ATOM   1529 C CZ  . PHE A 1 213 ? -11.843 20.172 -34.068 1.00 32.22 ? 191 PHE A CZ  1 
ATOM   1530 N N   . VAL A 1 214 ? -11.209 21.460 -26.973 1.00 15.09 ? 192 VAL A N   1 
ATOM   1531 C CA  . VAL A 1 214 ? -11.207 22.232 -25.728 1.00 15.12 ? 192 VAL A CA  1 
ATOM   1532 C C   . VAL A 1 214 ? -10.265 23.411 -25.897 1.00 15.44 ? 192 VAL A C   1 
ATOM   1533 O O   . VAL A 1 214 ? -9.062  23.222 -26.121 1.00 16.56 ? 192 VAL A O   1 
ATOM   1534 C CB  . VAL A 1 214 ? -10.788 21.408 -24.500 1.00 17.07 ? 192 VAL A CB  1 
ATOM   1535 C CG1 . VAL A 1 214 ? -10.822 22.300 -23.243 1.00 15.00 ? 192 VAL A CG1 1 
ATOM   1536 C CG2 . VAL A 1 214 ? -11.682 20.188 -24.305 1.00 18.53 ? 192 VAL A CG2 1 
ATOM   1537 N N   . ASP A 1 215 ? -10.801 24.625 -25.751 1.00 15.03 ? 193 ASP A N   1 
ATOM   1538 C CA  . ASP A 1 215 ? -9.986  25.838 -25.780 1.00 15.87 ? 193 ASP A CA  1 
ATOM   1539 C C   . ASP A 1 215 ? -9.405  26.075 -24.394 1.00 20.04 ? 193 ASP A C   1 
ATOM   1540 O O   . ASP A 1 215 ? -10.103 25.931 -23.393 1.00 17.71 ? 193 ASP A O   1 
ATOM   1541 C CB  . ASP A 1 215 ? -10.834 27.046 -26.192 1.00 15.80 ? 193 ASP A CB  1 
ATOM   1542 C CG  . ASP A 1 215 ? -11.230 27.031 -27.658 1.00 23.63 ? 193 ASP A CG  1 
ATOM   1543 O OD1 . ASP A 1 215 ? -10.628 26.294 -28.468 1.00 22.38 ? 193 ASP A OD1 1 
ATOM   1544 O OD2 . ASP A 1 215 ? -12.172 27.754 -28.004 1.00 25.60 ? 193 ASP A OD2 1 
ATOM   1545 N N   . HIS A 1 216 ? -8.119  26.420 -24.331 1.00 12.94 ? 194 HIS A N   1 
ATOM   1546 C CA  . HIS A 1 216 ? -7.426  26.582 -23.057 1.00 12.74 ? 194 HIS A CA  1 
ATOM   1547 C C   . HIS A 1 216 ? -6.710  27.923 -23.040 1.00 16.68 ? 194 HIS A C   1 
ATOM   1548 O O   . HIS A 1 216 ? -6.092  28.312 -24.034 1.00 15.67 ? 194 HIS A O   1 
ATOM   1549 C CB  . HIS A 1 216 ? -6.300  25.552 -22.839 1.00 15.38 ? 194 HIS A CB  1 
ATOM   1550 C CG  . HIS A 1 216 ? -6.730  24.127 -22.691 1.00 14.67 ? 194 HIS A CG  1 
ATOM   1551 N ND1 . HIS A 1 216 ? -7.036  23.560 -21.472 1.00 16.78 ? 194 HIS A ND1 1 
ATOM   1552 C CD2 . HIS A 1 216 ? -6.779  23.121 -23.600 1.00 15.44 ? 194 HIS A CD2 1 
ATOM   1553 C CE1 . HIS A 1 216 ? -7.314  22.277 -21.648 1.00 17.17 ? 194 HIS A CE1 1 
ATOM   1554 N NE2 . HIS A 1 216 ? -7.157  21.986 -22.931 1.00 14.73 ? 194 HIS A NE2 1 
ATOM   1555 N N   . CYS A 1 217 ? -6.701  28.576 -21.883 1.00 16.23 ? 195 CYS A N   1 
ATOM   1556 C CA  . CYS A 1 217 ? -5.679  29.579 -21.615 1.00 14.59 ? 195 CYS A CA  1 
ATOM   1557 C C   . CYS A 1 217 ? -5.136  29.317 -20.226 1.00 21.19 ? 195 CYS A C   1 
ATOM   1558 O O   . CYS A 1 217 ? -5.847  28.805 -19.360 1.00 16.69 ? 195 CYS A O   1 
ATOM   1559 C CB  . CYS A 1 217 ? -6.198  31.015 -21.782 1.00 20.68 ? 195 CYS A CB  1 
ATOM   1560 S SG  . CYS A 1 217 ? -7.407  31.567 -20.575 1.00 23.42 ? 195 CYS A SG  1 
ATOM   1561 N N   . ILE A 1 218 ? -3.847  29.593 -20.034 1.00 15.82 ? 196 ILE A N   1 
ATOM   1562 C CA  . ILE A 1 218 ? -3.209  29.338 -18.748 1.00 14.21 ? 196 ILE A CA  1 
ATOM   1563 C C   . ILE A 1 218 ? -2.287  30.513 -18.457 1.00 15.63 ? 196 ILE A C   1 
ATOM   1564 O O   . ILE A 1 218 ? -1.630  31.036 -19.368 1.00 16.82 ? 196 ILE A O   1 
ATOM   1565 C CB  . ILE A 1 218 ? -2.467  27.977 -18.745 1.00 12.17 ? 196 ILE A CB  1 
ATOM   1566 C CG1 . ILE A 1 218 ? -1.954  27.640 -17.335 1.00 14.35 ? 196 ILE A CG1 1 
ATOM   1567 C CG2 . ILE A 1 218 ? -1.321  27.976 -19.781 1.00 16.96 ? 196 ILE A CG2 1 
ATOM   1568 C CD1 . ILE A 1 218 ? -1.429  26.198 -17.165 1.00 12.43 ? 196 ILE A CD1 1 
ATOM   1569 N N   . GLU A 1 219 ? -2.272  30.961 -17.197 1.00 17.26 ? 197 GLU A N   1 
ATOM   1570 C CA  . GLU A 1 219 ? -1.614  32.219 -16.848 1.00 18.25 ? 197 GLU A CA  1 
ATOM   1571 C C   . GLU A 1 219 ? -0.920  32.116 -15.496 1.00 15.76 ? 197 GLU A C   1 
ATOM   1572 O O   . GLU A 1 219 ? -1.571  31.785 -14.498 1.00 16.12 ? 197 GLU A O   1 
ATOM   1573 C CB  . GLU A 1 219 ? -2.643  33.360 -16.793 1.00 18.60 ? 197 GLU A CB  1 
ATOM   1574 C CG  . GLU A 1 219 ? -2.081  34.711 -16.365 1.00 19.47 ? 197 GLU A CG  1 
ATOM   1575 C CD  . GLU A 1 219 ? -1.577  35.543 -17.536 1.00 29.69 ? 197 GLU A CD  1 
ATOM   1576 O OE1 . GLU A 1 219 ? -1.668  35.074 -18.691 1.00 34.53 ? 197 GLU A OE1 1 
ATOM   1577 O OE2 . GLU A 1 219 ? -1.129  36.684 -17.308 1.00 27.53 ? 197 GLU A OE2 1 
ATOM   1578 N N   . ILE A 1 220 ? 0.370   32.456 -15.436 1.00 12.92 ? 198 ILE A N   1 
ATOM   1579 C CA  . ILE A 1 220 ? 1.008   32.690 -14.139 1.00 11.76 ? 198 ILE A CA  1 
ATOM   1580 C C   . ILE A 1 220 ? 0.546   34.064 -13.635 1.00 18.56 ? 198 ILE A C   1 
ATOM   1581 O O   . ILE A 1 220 ? 0.874   35.095 -14.228 1.00 18.78 ? 198 ILE A O   1 
ATOM   1582 C CB  . ILE A 1 220 ? 2.539   32.608 -14.227 1.00 12.75 ? 198 ILE A CB  1 
ATOM   1583 C CG1 . ILE A 1 220 ? 2.945   31.144 -14.468 1.00 13.07 ? 198 ILE A CG1 1 
ATOM   1584 C CG2 . ILE A 1 220 ? 3.171   33.115 -12.920 1.00 15.05 ? 198 ILE A CG2 1 
ATOM   1585 C CD1 . ILE A 1 220 ? 4.464   30.852 -14.446 1.00 14.33 ? 198 ILE A CD1 1 
ATOM   1586 N N   . LEU A 1 221 ? -0.263  34.077 -12.564 1.00 17.71 ? 199 LEU A N   1 
ATOM   1587 C CA  . LEU A 1 221 ? -0.796  35.325 -12.013 1.00 18.63 ? 199 LEU A CA  1 
ATOM   1588 C C   . LEU A 1 221 ? 0.242   36.073 -11.192 1.00 19.42 ? 199 LEU A C   1 
ATOM   1589 O O   . LEU A 1 221 ? 0.237   37.317 -11.154 1.00 19.22 ? 199 LEU A O   1 
ATOM   1590 C CB  . LEU A 1 221 ? -2.010  35.025 -11.125 1.00 21.22 ? 199 LEU A CB  1 
ATOM   1591 C CG  . LEU A 1 221 ? -3.134  34.174 -11.726 1.00 21.28 ? 199 LEU A CG  1 
ATOM   1592 C CD1 . LEU A 1 221 ? -4.253  33.930 -10.718 1.00 24.64 ? 199 LEU A CD1 1 
ATOM   1593 C CD2 . LEU A 1 221 ? -3.717  34.801 -12.986 1.00 21.58 ? 199 LEU A CD2 1 
ATOM   1594 N N   . SER A 1 222 ? 1.119   35.334 -10.513 1.00 17.42 ? 200 SER A N   1 
ATOM   1595 C CA  . SER A 1 222 ? 2.084   35.918 -9.590  1.00 17.85 ? 200 SER A CA  1 
ATOM   1596 C C   . SER A 1 222 ? 3.174   34.893 -9.323  1.00 23.93 ? 200 SER A C   1 
ATOM   1597 O O   . SER A 1 222 ? 2.955   33.691 -9.478  1.00 19.41 ? 200 SER A O   1 
ATOM   1598 C CB  . SER A 1 222 ? 1.414   36.340 -8.276  1.00 22.76 ? 200 SER A CB  1 
ATOM   1599 O OG  . SER A 1 222 ? 2.245   37.227 -7.561  1.00 27.72 ? 200 SER A OG  1 
ATOM   1600 N N   . HIS A 1 223 ? 4.337   35.379 -8.882  1.00 21.45 ? 201 HIS A N   1 
ATOM   1601 C CA  . HIS A 1 223 ? 5.451   34.510 -8.522  1.00 22.76 ? 201 HIS A CA  1 
ATOM   1602 C C   . HIS A 1 223 ? 6.453   35.315 -7.705  1.00 26.62 ? 201 HIS A C   1 
ATOM   1603 O O   . HIS A 1 223 ? 6.518   36.543 -7.811  1.00 26.15 ? 201 HIS A O   1 
ATOM   1604 C CB  . HIS A 1 223 ? 6.134   33.932 -9.767  1.00 17.42 ? 201 HIS A CB  1 
ATOM   1605 C CG  . HIS A 1 223 ? 6.767   34.988 -10.613 1.00 21.32 ? 201 HIS A CG  1 
ATOM   1606 N ND1 . HIS A 1 223 ? 8.061   35.423 -10.417 1.00 24.42 ? 201 HIS A ND1 1 
ATOM   1607 C CD2 . HIS A 1 223 ? 6.254   35.758 -11.603 1.00 20.20 ? 201 HIS A CD2 1 
ATOM   1608 C CE1 . HIS A 1 223 ? 8.330   36.394 -11.274 1.00 23.27 ? 201 HIS A CE1 1 
ATOM   1609 N NE2 . HIS A 1 223 ? 7.251   36.618 -12.004 1.00 25.42 ? 201 HIS A NE2 1 
ATOM   1610 N N   . ASP A 1 224 ? 7.235   34.617 -6.885  1.00 22.74 ? 202 ASP A N   1 
ATOM   1611 C CA  . ASP A 1 224 ? 8.343   35.284 -6.223  1.00 24.18 ? 202 ASP A CA  1 
ATOM   1612 C C   . ASP A 1 224 ? 9.590   35.181 -7.102  1.00 22.74 ? 202 ASP A C   1 
ATOM   1613 O O   . ASP A 1 224 ? 9.564   34.584 -8.174  1.00 22.98 ? 202 ASP A O   1 
ATOM   1614 C CB  . ASP A 1 224 ? 8.554   34.727 -4.811  1.00 29.16 ? 202 ASP A CB  1 
ATOM   1615 C CG  . ASP A 1 224 ? 8.990   33.264 -4.789  1.00 26.15 ? 202 ASP A CG  1 
ATOM   1616 O OD1 . ASP A 1 224 ? 9.142   32.616 -5.851  1.00 24.66 ? 202 ASP A OD1 1 
ATOM   1617 O OD2 . ASP A 1 224 ? 9.187   32.757 -3.667  1.00 28.08 ? 202 ASP A OD2 1 
ATOM   1618 N N   . LYS A 1 225 ? 10.699  35.759 -6.635  1.00 25.75 ? 203 LYS A N   1 
ATOM   1619 C CA  . LYS A 1 225 ? 11.859  35.979 -7.502  1.00 28.35 ? 203 LYS A CA  1 
ATOM   1620 C C   . LYS A 1 225 ? 12.334  34.692 -8.171  1.00 28.77 ? 203 LYS A C   1 
ATOM   1621 O O   . LYS A 1 225 ? 12.562  34.658 -9.389  1.00 32.22 ? 203 LYS A O   1 
ATOM   1622 C CB  . LYS A 1 225 ? 12.996  36.604 -6.699  1.00 30.95 ? 203 LYS A CB  1 
ATOM   1623 C CG  . LYS A 1 225 ? 14.145  37.094 -7.579  1.00 35.66 ? 203 LYS A CG  1 
ATOM   1624 C CD  . LYS A 1 225 ? 15.361  37.475 -6.756  1.00 50.24 ? 203 LYS A CD  1 
ATOM   1625 C CE  . LYS A 1 225 ? 16.625  37.337 -7.590  1.00 63.08 ? 203 LYS A CE  1 
ATOM   1626 N NZ  . LYS A 1 225 ? 17.443  36.150 -7.187  1.00 65.70 ? 203 LYS A NZ  1 
ATOM   1627 N N   . ASP A 1 226 ? 12.490  33.622 -7.397  1.00 31.39 ? 204 ASP A N   1 
ATOM   1628 C CA  . ASP A 1 226 ? 13.053  32.380 -7.914  1.00 24.90 ? 204 ASP A CA  1 
ATOM   1629 C C   . ASP A 1 226 ? 11.985  31.383 -8.357  1.00 26.46 ? 204 ASP A C   1 
ATOM   1630 O O   . ASP A 1 226 ? 12.317  30.229 -8.647  1.00 26.06 ? 204 ASP A O   1 
ATOM   1631 C CB  . ASP A 1 226 ? 13.955  31.724 -6.859  1.00 30.53 ? 204 ASP A CB  1 
ATOM   1632 C CG  . ASP A 1 226 ? 15.243  32.498 -6.617  1.00 42.83 ? 204 ASP A CG  1 
ATOM   1633 O OD1 . ASP A 1 226 ? 15.890  32.915 -7.601  1.00 38.88 ? 204 ASP A OD1 1 
ATOM   1634 O OD2 . ASP A 1 226 ? 15.616  32.664 -5.439  1.00 40.24 ? 204 ASP A OD2 1 
ATOM   1635 N N   . TYR A 1 227 ? 10.721  31.799 -8.411  1.00 22.56 ? 205 TYR A N   1 
ATOM   1636 C CA  . TYR A 1 227 ? 9.599   30.909 -8.715  1.00 22.88 ? 205 TYR A CA  1 
ATOM   1637 C C   . TYR A 1 227 ? 9.503   29.753 -7.714  1.00 21.11 ? 205 TYR A C   1 
ATOM   1638 O O   . TYR A 1 227 ? 9.032   28.665 -8.055  1.00 22.90 ? 205 TYR A O   1 
ATOM   1639 C CB  . TYR A 1 227 ? 9.672   30.370 -10.154 1.00 21.12 ? 205 TYR A CB  1 
ATOM   1640 C CG  . TYR A 1 227 ? 9.389   31.407 -11.213 1.00 18.31 ? 205 TYR A CG  1 
ATOM   1641 C CD1 . TYR A 1 227 ? 10.343  32.363 -11.543 1.00 25.30 ? 205 TYR A CD1 1 
ATOM   1642 C CD2 . TYR A 1 227 ? 8.174   31.423 -11.901 1.00 24.43 ? 205 TYR A CD2 1 
ATOM   1643 C CE1 . TYR A 1 227 ? 10.094  33.321 -12.510 1.00 23.76 ? 205 TYR A CE1 1 
ATOM   1644 C CE2 . TYR A 1 227 ? 7.920   32.384 -12.880 1.00 22.07 ? 205 TYR A CE2 1 
ATOM   1645 C CZ  . TYR A 1 227 ? 8.892   33.330 -13.173 1.00 25.05 ? 205 TYR A CZ  1 
ATOM   1646 O OH  . TYR A 1 227 ? 8.678   34.288 -14.140 1.00 26.23 ? 205 TYR A OH  1 
ATOM   1647 N N   . ASN A 1 228 ? 9.939   29.968 -6.467  1.00 21.69 ? 206 ASN A N   1 
ATOM   1648 C CA  . ASN A 1 228 ? 9.631   29.007 -5.406  1.00 24.04 ? 206 ASN A CA  1 
ATOM   1649 C C   . ASN A 1 228 ? 8.152   29.043 -5.033  1.00 26.00 ? 206 ASN A C   1 
ATOM   1650 O O   . ASN A 1 228 ? 7.619   28.053 -4.523  1.00 22.45 ? 206 ASN A O   1 
ATOM   1651 C CB  . ASN A 1 228 ? 10.485  29.276 -4.160  1.00 28.84 ? 206 ASN A CB  1 
ATOM   1652 C CG  . ASN A 1 228 ? 11.958  28.954 -4.365  1.00 33.00 ? 206 ASN A CG  1 
ATOM   1653 O OD1 . ASN A 1 228 ? 12.307  27.919 -4.922  1.00 27.63 ? 206 ASN A OD1 1 
ATOM   1654 N ND2 . ASN A 1 228 ? 12.828  29.846 -3.911  1.00 34.59 ? 206 ASN A ND2 1 
ATOM   1655 N N   . LYS A 1 229 ? 7.482   30.163 -5.285  1.00 25.12 ? 207 LYS A N   1 
ATOM   1656 C CA  . LYS A 1 229 ? 6.056   30.323 -5.035  1.00 22.28 ? 207 LYS A CA  1 
ATOM   1657 C C   . LYS A 1 229 ? 5.451   30.914 -6.295  1.00 23.31 ? 207 LYS A C   1 
ATOM   1658 O O   . LYS A 1 229 ? 5.985   31.881 -6.847  1.00 22.14 ? 207 LYS A O   1 
ATOM   1659 C CB  . LYS A 1 229 ? 5.804   31.226 -3.817  1.00 25.63 ? 207 LYS A CB  1 
ATOM   1660 C CG  . LYS A 1 229 ? 6.322   30.621 -2.527  1.00 26.33 ? 207 LYS A CG  1 
ATOM   1661 C CD  . LYS A 1 229 ? 5.876   31.361 -1.270  1.00 35.68 ? 207 LYS A CD  1 
ATOM   1662 C CE  . LYS A 1 229 ? 5.228   30.406 -0.265  1.00 56.33 ? 207 LYS A CE  1 
ATOM   1663 N NZ  . LYS A 1 229 ? 4.508   31.116 0.843   1.00 58.41 ? 207 LYS A NZ  1 
ATOM   1664 N N   . VAL A 1 230 ? 4.377   30.299 -6.778  1.00 19.33 ? 208 VAL A N   1 
ATOM   1665 C CA  . VAL A 1 230 ? 3.732   30.685 -8.029  1.00 17.45 ? 208 VAL A CA  1 
ATOM   1666 C C   . VAL A 1 230 ? 2.232   30.547 -7.826  1.00 21.44 ? 208 VAL A C   1 
ATOM   1667 O O   . VAL A 1 230 ? 1.774   29.581 -7.204  1.00 21.28 ? 208 VAL A O   1 
ATOM   1668 C CB  . VAL A 1 230 ? 4.184   29.801 -9.221  1.00 17.60 ? 208 VAL A CB  1 
ATOM   1669 C CG1 . VAL A 1 230 ? 3.377   30.131 -10.511 1.00 15.36 ? 208 VAL A CG1 1 
ATOM   1670 C CG2 . VAL A 1 230 ? 5.702   29.910 -9.465  1.00 15.77 ? 208 VAL A CG2 1 
ATOM   1671 N N   . LYS A 1 231 ? 1.473   31.511 -8.348  1.00 16.17 ? 209 LYS A N   1 
ATOM   1672 C CA  . LYS A 1 231 ? 0.017   31.452 -8.406  1.00 18.76 ? 209 LYS A CA  1 
ATOM   1673 C C   . LYS A 1 231 ? -0.392  31.288 -9.866  1.00 19.06 ? 209 LYS A C   1 
ATOM   1674 O O   . LYS A 1 231 ? 0.078   32.035 -10.731 1.00 16.65 ? 209 LYS A O   1 
ATOM   1675 C CB  . LYS A 1 231 ? -0.605  32.717 -7.808  1.00 21.40 ? 209 LYS A CB  1 
ATOM   1676 C CG  . LYS A 1 231 ? -2.098  32.848 -8.061  1.00 36.91 ? 209 LYS A CG  1 
ATOM   1677 C CD  . LYS A 1 231 ? -2.920  32.669 -6.795  1.00 47.52 ? 209 LYS A CD  1 
ATOM   1678 C CE  . LYS A 1 231 ? -2.635  33.768 -5.768  1.00 43.25 ? 209 LYS A CE  1 
ATOM   1679 N NZ  . LYS A 1 231 ? -2.983  33.331 -4.387  1.00 42.80 ? 209 LYS A NZ  1 
ATOM   1680 N N   . LEU A 1 232 ? -1.251  30.307 -10.138 1.00 16.05 ? 210 LEU A N   1 
ATOM   1681 C CA  . LEU A 1 232 ? -1.526  29.839 -11.492 1.00 14.46 ? 210 LEU A CA  1 
ATOM   1682 C C   . LEU A 1 232 ? -3.031  29.795 -11.729 1.00 16.16 ? 210 LEU A C   1 
ATOM   1683 O O   . LEU A 1 232 ? -3.805  29.547 -10.800 1.00 18.91 ? 210 LEU A O   1 
ATOM   1684 C CB  . LEU A 1 232 ? -0.932  28.446 -11.715 1.00 17.51 ? 210 LEU A CB  1 
ATOM   1685 C CG  . LEU A 1 232 ? -0.921  27.810 -13.111 1.00 17.41 ? 210 LEU A CG  1 
ATOM   1686 C CD1 . LEU A 1 232 ? 0.038   28.559 -14.073 1.00 11.67 ? 210 LEU A CD1 1 
ATOM   1687 C CD2 . LEU A 1 232 ? -0.489  26.341 -12.990 1.00 12.35 ? 210 LEU A CD2 1 
ATOM   1688 N N   . TYR A 1 233 ? -3.441  30.012 -12.984 1.00 14.77 ? 211 TYR A N   1 
ATOM   1689 C CA  . TYR A 1 233 ? -4.857  30.039 -13.350 1.00 17.37 ? 211 TYR A CA  1 
ATOM   1690 C C   . TYR A 1 233 ? -5.067  29.423 -14.725 1.00 15.25 ? 211 TYR A C   1 
ATOM   1691 O O   . TYR A 1 233 ? -4.230  29.578 -15.606 1.00 15.17 ? 211 TYR A O   1 
ATOM   1692 C CB  . TYR A 1 233 ? -5.387  31.475 -13.356 1.00 16.16 ? 211 TYR A CB  1 
ATOM   1693 C CG  . TYR A 1 233 ? -6.782  31.646 -13.903 1.00 16.51 ? 211 TYR A CG  1 
ATOM   1694 C CD1 . TYR A 1 233 ? -7.893  31.330 -13.127 1.00 17.76 ? 211 TYR A CD1 1 
ATOM   1695 C CD2 . TYR A 1 233 ? -6.991  32.169 -15.187 1.00 17.97 ? 211 TYR A CD2 1 
ATOM   1696 C CE1 . TYR A 1 233 ? -9.175  31.518 -13.601 1.00 18.33 ? 211 TYR A CE1 1 
ATOM   1697 C CE2 . TYR A 1 233 ? -8.283  32.351 -15.684 1.00 21.03 ? 211 TYR A CE2 1 
ATOM   1698 C CZ  . TYR A 1 233 ? -9.370  32.015 -14.880 1.00 24.96 ? 211 TYR A CZ  1 
ATOM   1699 O OH  . TYR A 1 233 ? -10.659 32.210 -15.330 1.00 18.73 ? 211 TYR A OH  1 
ATOM   1700 N N   . GLU A 1 234 ? -6.195  28.732 -14.906 1.00 14.59 ? 212 GLU A N   1 
ATOM   1701 C CA  . GLU A 1 234 ? -6.551  28.150 -16.198 1.00 15.73 ? 212 GLU A CA  1 
ATOM   1702 C C   . GLU A 1 234 ? -8.030  28.343 -16.441 1.00 14.76 ? 212 GLU A C   1 
ATOM   1703 O O   . GLU A 1 234 ? -8.832  28.223 -15.515 1.00 16.34 ? 212 GLU A O   1 
ATOM   1704 C CB  . GLU A 1 234 ? -6.226  26.655 -16.254 1.00 12.47 ? 212 GLU A CB  1 
ATOM   1705 C CG  . GLU A 1 234 ? -6.120  26.033 -17.650 1.00 16.59 ? 212 GLU A CG  1 
ATOM   1706 C CD  . GLU A 1 234 ? -6.744  24.647 -17.733 1.00 21.43 ? 212 GLU A CD  1 
ATOM   1707 O OE1 . GLU A 1 234 ? -6.671  23.920 -16.727 1.00 22.90 ? 212 GLU A OE1 1 
ATOM   1708 O OE2 . GLU A 1 234 ? -7.108  24.192 -18.840 1.00 22.84 ? 212 GLU A OE2 1 
ATOM   1709 N N   . HIS A 1 235 ? -8.386  28.593 -17.700 1.00 15.83 ? 213 HIS A N   1 
ATOM   1710 C CA  . HIS A 1 235 ? -9.773  28.690 -18.138 1.00 19.35 ? 213 HIS A CA  1 
ATOM   1711 C C   . HIS A 1 235 ? -9.902  27.818 -19.379 1.00 15.47 ? 213 HIS A C   1 
ATOM   1712 O O   . HIS A 1 235 ? -9.104  27.959 -20.313 1.00 15.67 ? 213 HIS A O   1 
ATOM   1713 C CB  . HIS A 1 235 ? -10.159 30.153 -18.430 1.00 18.87 ? 213 HIS A CB  1 
ATOM   1714 C CG  . HIS A 1 235 ? -11.592 30.354 -18.824 1.00 16.93 ? 213 HIS A CG  1 
ATOM   1715 N ND1 . HIS A 1 235 ? -12.024 31.487 -19.480 1.00 24.00 ? 213 HIS A ND1 1 
ATOM   1716 C CD2 . HIS A 1 235 ? -12.692 29.581 -18.653 1.00 17.74 ? 213 HIS A CD2 1 
ATOM   1717 C CE1 . HIS A 1 235 ? -13.327 31.404 -19.700 1.00 25.03 ? 213 HIS A CE1 1 
ATOM   1718 N NE2 . HIS A 1 235 ? -13.758 30.259 -19.202 1.00 19.96 ? 213 HIS A NE2 1 
ATOM   1719 N N   . ALA A 1 236 ? -10.867 26.893 -19.379 1.00 12.78 ? 214 ALA A N   1 
ATOM   1720 C CA  . ALA A 1 236 ? -11.002 25.926 -20.468 1.00 15.07 ? 214 ALA A CA  1 
ATOM   1721 C C   . ALA A 1 236 ? -12.468 25.744 -20.819 1.00 16.21 ? 214 ALA A C   1 
ATOM   1722 O O   . ALA A 1 236 ? -13.316 25.639 -19.928 1.00 18.11 ? 214 ALA A O   1 
ATOM   1723 C CB  . ALA A 1 236 ? -10.389 24.554 -20.093 1.00 13.55 ? 214 ALA A CB  1 
ATOM   1724 N N   . VAL A 1 237 ? -12.770 25.714 -22.121 1.00 15.53 ? 215 VAL A N   1 
ATOM   1725 C CA  . VAL A 1 237 ? -14.148 25.616 -22.598 1.00 16.97 ? 215 VAL A CA  1 
ATOM   1726 C C   . VAL A 1 237 ? -14.181 24.620 -23.752 1.00 16.06 ? 215 VAL A C   1 
ATOM   1727 O O   . VAL A 1 237 ? -13.439 24.767 -24.729 1.00 16.16 ? 215 VAL A O   1 
ATOM   1728 C CB  . VAL A 1 237 ? -14.690 26.988 -23.047 1.00 18.89 ? 215 VAL A CB  1 
ATOM   1729 C CG1 . VAL A 1 237 ? -16.099 26.842 -23.626 1.00 21.79 ? 215 VAL A CG1 1 
ATOM   1730 C CG2 . VAL A 1 237 ? -14.692 27.985 -21.869 1.00 20.93 ? 215 VAL A CG2 1 
ATOM   1731 N N   . ALA A 1 238 ? -15.033 23.612 -23.648 1.00 15.67 ? 216 ALA A N   1 
ATOM   1732 C CA  . ALA A 1 238 ? -15.165 22.631 -24.715 1.00 21.64 ? 216 ALA A CA  1 
ATOM   1733 C C   . ALA A 1 238 ? -16.147 23.126 -25.767 1.00 23.31 ? 216 ALA A C   1 
ATOM   1734 O O   . ALA A 1 238 ? -17.099 23.850 -25.463 1.00 20.74 ? 216 ALA A O   1 
ATOM   1735 C CB  . ALA A 1 238 ? -15.638 21.282 -24.159 1.00 16.07 ? 216 ALA A CB  1 
ATOM   1736 N N   . HIS A 1 239 ? -15.924 22.712 -27.015 1.00 23.13 ? 217 HIS A N   1 
ATOM   1737 C CA  . HIS A 1 239 ? -16.860 23.038 -28.083 1.00 28.54 ? 217 HIS A CA  1 
ATOM   1738 C C   . HIS A 1 239 ? -16.738 22.005 -29.195 1.00 23.02 ? 217 HIS A C   1 
ATOM   1739 O O   . HIS A 1 239 ? -15.776 21.240 -29.254 1.00 25.12 ? 217 HIS A O   1 
ATOM   1740 C CB  . HIS A 1 239 ? -16.628 24.464 -28.608 1.00 30.06 ? 217 HIS A CB  1 
ATOM   1741 C CG  . HIS A 1 239 ? -15.269 24.690 -29.196 1.00 29.96 ? 217 HIS A CG  1 
ATOM   1742 N ND1 . HIS A 1 239 ? -14.989 24.480 -30.534 1.00 32.69 ? 217 HIS A ND1 1 
ATOM   1743 C CD2 . HIS A 1 239 ? -14.113 25.119 -28.634 1.00 27.47 ? 217 HIS A CD2 1 
ATOM   1744 C CE1 . HIS A 1 239 ? -13.719 24.770 -30.766 1.00 31.70 ? 217 HIS A CE1 1 
ATOM   1745 N NE2 . HIS A 1 239 ? -13.164 25.154 -29.630 1.00 30.77 ? 217 HIS A NE2 1 
ATOM   1746 N N   . SER A 1 240 ? -17.747 21.970 -30.063 1.00 25.89 ? 218 SER A N   1 
ATOM   1747 C CA  . SER A 1 240 ? -17.683 21.142 -31.256 1.00 34.29 ? 218 SER A CA  1 
ATOM   1748 C C   . SER A 1 240 ? -17.077 21.940 -32.412 1.00 45.13 ? 218 SER A C   1 
ATOM   1749 O O   . SER A 1 240 ? -16.856 23.151 -32.322 1.00 50.51 ? 218 SER A O   1 
ATOM   1750 C CB  . SER A 1 240 ? -19.071 20.628 -31.619 1.00 38.44 ? 218 SER A CB  1 
ATOM   1751 O OG  . SER A 1 240 ? -19.940 21.724 -31.818 1.00 42.11 ? 218 SER A OG  1 
ATOM   1752 N N   . GLY A 1 241 ? -16.808 21.243 -33.510 1.00 54.49 ? 219 GLY A N   1 
ATOM   1753 C CA  . GLY A 1 241 ? -16.127 21.828 -34.658 1.00 53.40 ? 219 GLY A CA  1 
ATOM   1754 C C   . GLY A 1 241 ? -16.661 23.148 -35.179 1.00 53.21 ? 219 GLY A C   1 
ATOM   1755 O O   . GLY A 1 241 ? -17.853 23.288 -35.446 1.00 68.15 ? 219 GLY A O   1 
ATOM   1756 N N   . SER B 1 26  ? 11.985  54.822 -8.467  1.00 58.38 ? 2   SER B N   1 
ATOM   1757 C CA  . SER B 1 26  ? 12.425  54.415 -7.137  1.00 57.02 ? 2   SER B CA  1 
ATOM   1758 C C   . SER B 1 26  ? 11.218  54.083 -6.267  1.00 44.10 ? 2   SER B C   1 
ATOM   1759 O O   . SER B 1 26  ? 11.280  53.172 -5.437  1.00 51.90 ? 2   SER B O   1 
ATOM   1760 C CB  . SER B 1 26  ? 13.279  55.510 -6.483  1.00 53.32 ? 2   SER B CB  1 
ATOM   1761 O OG  . SER B 1 26  ? 13.814  55.092 -5.232  1.00 57.21 ? 2   SER B OG  1 
ATOM   1762 N N   . ALA B 1 27  ? 10.107  54.804 -6.469  1.00 31.33 ? 3   ALA B N   1 
ATOM   1763 C CA  . ALA B 1 27  ? 8.960   54.659 -5.577  1.00 28.70 ? 3   ALA B CA  1 
ATOM   1764 C C   . ALA B 1 27  ? 8.181   53.372 -5.803  1.00 33.39 ? 3   ALA B C   1 
ATOM   1765 O O   . ALA B 1 27  ? 7.426   52.958 -4.917  1.00 29.95 ? 3   ALA B O   1 
ATOM   1766 C CB  . ALA B 1 27  ? 8.011   55.853 -5.722  1.00 28.50 ? 3   ALA B CB  1 
ATOM   1767 N N   . ILE B 1 28  ? 8.335   52.732 -6.955  1.00 27.64 ? 4   ILE B N   1 
ATOM   1768 C CA  . ILE B 1 28  ? 7.547   51.555 -7.305  1.00 22.39 ? 4   ILE B CA  1 
ATOM   1769 C C   . ILE B 1 28  ? 8.375   50.314 -7.020  1.00 22.55 ? 4   ILE B C   1 
ATOM   1770 O O   . ILE B 1 28  ? 9.493   50.171 -7.534  1.00 28.05 ? 4   ILE B O   1 
ATOM   1771 C CB  . ILE B 1 28  ? 7.103   51.590 -8.772  1.00 24.78 ? 4   ILE B CB  1 
ATOM   1772 C CG1 . ILE B 1 28  ? 6.373   52.906 -9.071  1.00 23.12 ? 4   ILE B CG1 1 
ATOM   1773 C CG2 . ILE B 1 28  ? 6.230   50.385 -9.071  1.00 21.07 ? 4   ILE B CG2 1 
ATOM   1774 C CD1 . ILE B 1 28  ? 5.100   53.109 -8.293  1.00 22.36 ? 4   ILE B CD1 1 
ATOM   1775 N N   . LYS B 1 29  ? 7.840   49.429 -6.184  1.00 21.21 ? 5   LYS B N   1 
ATOM   1776 C CA  . LYS B 1 29  ? 8.519   48.191 -5.824  1.00 23.28 ? 5   LYS B CA  1 
ATOM   1777 C C   . LYS B 1 29  ? 8.010   47.060 -6.705  1.00 20.01 ? 5   LYS B C   1 
ATOM   1778 O O   . LYS B 1 29  ? 6.917   47.148 -7.272  1.00 22.24 ? 5   LYS B O   1 
ATOM   1779 C CB  . LYS B 1 29  ? 8.277   47.857 -4.344  1.00 25.45 ? 5   LYS B CB  1 
ATOM   1780 C CG  . LYS B 1 29  ? 9.189   48.589 -3.350  1.00 27.86 ? 5   LYS B CG  1 
ATOM   1781 C CD  . LYS B 1 29  ? 8.894   50.088 -3.264  1.00 27.65 ? 5   LYS B CD  1 
ATOM   1782 C CE  . LYS B 1 29  ? 7.569   50.338 -2.558  1.00 29.97 ? 5   LYS B CE  1 
ATOM   1783 N NZ  . LYS B 1 29  ? 7.199   51.789 -2.491  1.00 24.63 ? 5   LYS B NZ  1 
ATOM   1784 N N   . PRO B 1 30  ? 8.790   45.989 -6.880  1.00 25.49 ? 6   PRO B N   1 
ATOM   1785 C CA  . PRO B 1 30  ? 8.333   44.898 -7.759  1.00 19.94 ? 6   PRO B CA  1 
ATOM   1786 C C   . PRO B 1 30  ? 7.137   44.123 -7.228  1.00 23.69 ? 6   PRO B C   1 
ATOM   1787 O O   . PRO B 1 30  ? 6.444   43.479 -8.021  1.00 23.08 ? 6   PRO B O   1 
ATOM   1788 C CB  . PRO B 1 30  ? 9.572   43.995 -7.893  1.00 21.39 ? 6   PRO B CB  1 
ATOM   1789 C CG  . PRO B 1 30  ? 10.579  44.503 -6.963  1.00 28.28 ? 6   PRO B CG  1 
ATOM   1790 C CD  . PRO B 1 30  ? 10.199  45.851 -6.474  1.00 25.31 ? 6   PRO B CD  1 
ATOM   1791 N N   . ASP B 1 31  ? 6.884   44.134 -5.921  1.00 22.98 ? 7   ASP B N   1 
ATOM   1792 C CA  . ASP B 1 31  ? 5.698   43.510 -5.342  1.00 22.07 ? 7   ASP B CA  1 
ATOM   1793 C C   . ASP B 1 31  ? 5.006   44.563 -4.500  1.00 21.68 ? 7   ASP B C   1 
ATOM   1794 O O   . ASP B 1 31  ? 5.631   45.146 -3.616  1.00 23.87 ? 7   ASP B O   1 
ATOM   1795 C CB  . ASP B 1 31  ? 6.069   42.307 -4.477  1.00 24.20 ? 7   ASP B CB  1 
ATOM   1796 C CG  . ASP B 1 31  ? 6.601   41.160 -5.291  1.00 31.30 ? 7   ASP B CG  1 
ATOM   1797 O OD1 . ASP B 1 31  ? 5.797   40.521 -5.993  1.00 27.47 ? 7   ASP B OD1 1 
ATOM   1798 O OD2 . ASP B 1 31  ? 7.824   40.920 -5.247  1.00 30.12 ? 7   ASP B OD2 1 
ATOM   1799 N N   . MET B 1 32  ? 3.732   44.825 -4.777  1.00 19.71 ? 8   MET B N   1 
ATOM   1800 C CA  . MET B 1 32  ? 3.009   45.826 -4.004  1.00 23.02 ? 8   MET B CA  1 
ATOM   1801 C C   . MET B 1 32  ? 1.619   45.314 -3.658  1.00 23.27 ? 8   MET B C   1 
ATOM   1802 O O   . MET B 1 32  ? 1.066   44.427 -4.312  1.00 19.01 ? 8   MET B O   1 
ATOM   1803 C CB  . MET B 1 32  ? 2.942   47.174 -4.742  1.00 22.42 ? 8   MET B CB  1 
ATOM   1804 C CG  . MET B 1 32  ? 4.321   47.683 -5.133  1.00 29.66 ? 8   MET B CG  1 
ATOM   1805 S SD  . MET B 1 32  ? 4.559   49.447 -5.383  1.00 30.51 ? 8   MET B SD  1 
ATOM   1806 C CE  . MET B 1 32  ? 3.500   50.225 -4.149  1.00 26.26 ? 8   MET B CE  1 
ATOM   1807 N N   . LYS B 1 33  ? 1.064   45.902 -2.609  1.00 20.80 ? 9   LYS B N   1 
ATOM   1808 C CA  . LYS B 1 33  ? -0.270  45.593 -2.120  1.00 22.07 ? 9   LYS B CA  1 
ATOM   1809 C C   . LYS B 1 33  ? -1.224  46.683 -2.584  1.00 26.12 ? 9   LYS B C   1 
ATOM   1810 O O   . LYS B 1 33  ? -0.809  47.793 -2.915  1.00 20.98 ? 9   LYS B O   1 
ATOM   1811 C CB  . LYS B 1 33  ? -0.278  45.490 -0.596  1.00 20.55 ? 9   LYS B CB  1 
ATOM   1812 C CG  . LYS B 1 33  ? 0.655   44.430 -0.025  1.00 26.66 ? 9   LYS B CG  1 
ATOM   1813 C CD  . LYS B 1 33  ? 0.698   44.526 1.502   1.00 36.03 ? 9   LYS B CD  1 
ATOM   1814 C CE  . LYS B 1 33  ? 1.724   43.567 2.101   1.00 33.81 ? 9   LYS B CE  1 
ATOM   1815 N NZ  . LYS B 1 33  ? 1.841   43.719 3.577   1.00 46.77 ? 9   LYS B NZ  1 
ATOM   1816 N N   . ILE B 1 34  ? -2.515  46.355 -2.610  1.00 21.30 ? 10  ILE B N   1 
ATOM   1817 C CA  . ILE B 1 34  ? -3.532  47.247 -3.148  1.00 20.97 ? 10  ILE B CA  1 
ATOM   1818 C C   . ILE B 1 34  ? -4.703  47.247 -2.187  1.00 23.64 ? 10  ILE B C   1 
ATOM   1819 O O   . ILE B 1 34  ? -5.236  46.180 -1.861  1.00 20.26 ? 10  ILE B O   1 
ATOM   1820 C CB  . ILE B 1 34  ? -3.991  46.820 -4.557  1.00 23.25 ? 10  ILE B CB  1 
ATOM   1821 C CG1 . ILE B 1 34  ? -2.778  46.621 -5.476  1.00 25.56 ? 10  ILE B CG1 1 
ATOM   1822 C CG2 . ILE B 1 34  ? -4.949  47.862 -5.123  1.00 20.57 ? 10  ILE B CG2 1 
ATOM   1823 C CD1 . ILE B 1 34  ? -2.900  45.517 -6.471  1.00 29.34 ? 10  ILE B CD1 1 
ATOM   1824 N N   . LYS B 1 35  ? -5.089  48.435 -1.722  1.00 21.92 ? 11  LYS B N   1 
ATOM   1825 C CA  . LYS B 1 35  ? -6.265  48.618 -0.880  1.00 18.43 ? 11  LYS B CA  1 
ATOM   1826 C C   . LYS B 1 35  ? -7.251  49.518 -1.610  1.00 22.46 ? 11  LYS B C   1 
ATOM   1827 O O   . LYS B 1 35  ? -6.860  50.553 -2.161  1.00 19.33 ? 11  LYS B O   1 
ATOM   1828 C CB  . LYS B 1 35  ? -5.901  49.256 0.461   1.00 20.31 ? 11  LYS B CB  1 
ATOM   1829 C CG  . LYS B 1 35  ? -4.863  48.474 1.248   1.00 25.68 ? 11  LYS B CG  1 
ATOM   1830 C CD  . LYS B 1 35  ? -5.460  47.189 1.805   1.00 26.09 ? 11  LYS B CD  1 
ATOM   1831 C CE  . LYS B 1 35  ? -4.396  46.420 2.580   1.00 42.04 ? 11  LYS B CE  1 
ATOM   1832 N NZ  . LYS B 1 35  ? -4.855  45.094 3.072   1.00 33.70 ? 11  LYS B NZ  1 
ATOM   1833 N N   . LEU B 1 36  ? -8.530  49.148 -1.593  1.00 19.97 ? 12  LEU B N   1 
ATOM   1834 C CA  . LEU B 1 36  ? -9.495  49.831 -2.446  1.00 18.00 ? 12  LEU B CA  1 
ATOM   1835 C C   . LEU B 1 36  ? -10.860 49.866 -1.783  1.00 20.67 ? 12  LEU B C   1 
ATOM   1836 O O   . LEU B 1 36  ? -11.279 48.888 -1.153  1.00 22.20 ? 12  LEU B O   1 
ATOM   1837 C CB  . LEU B 1 36  ? -9.597  49.132 -3.815  1.00 18.94 ? 12  LEU B CB  1 
ATOM   1838 C CG  . LEU B 1 36  ? -10.563 49.726 -4.851  1.00 19.95 ? 12  LEU B CG  1 
ATOM   1839 C CD1 . LEU B 1 36  ? -10.035 49.538 -6.276  1.00 19.36 ? 12  LEU B CD1 1 
ATOM   1840 C CD2 . LEU B 1 36  ? -11.949 49.085 -4.715  1.00 17.12 ? 12  LEU B CD2 1 
ATOM   1841 N N   . ARG B 1 37  ? -11.557 50.991 -1.942  1.00 17.82 ? 13  ARG B N   1 
ATOM   1842 C CA  . ARG B 1 37  ? -12.973 51.058 -1.611  1.00 18.30 ? 13  ARG B CA  1 
ATOM   1843 C C   . ARG B 1 37  ? -13.676 51.789 -2.737  1.00 24.00 ? 13  ARG B C   1 
ATOM   1844 O O   . ARG B 1 37  ? -13.243 52.882 -3.128  1.00 22.69 ? 13  ARG B O   1 
ATOM   1845 C CB  . ARG B 1 37  ? -13.223 51.775 -0.275  1.00 20.24 ? 13  ARG B CB  1 
ATOM   1846 C CG  . ARG B 1 37  ? -14.710 52.080 -0.056  1.00 22.45 ? 13  ARG B CG  1 
ATOM   1847 C CD  . ARG B 1 37  ? -15.044 52.365 1.402   1.00 30.09 ? 13  ARG B CD  1 
ATOM   1848 N NE  . ARG B 1 37  ? -14.731 51.241 2.280   1.00 33.15 ? 13  ARG B NE  1 
ATOM   1849 C CZ  . ARG B 1 37  ? -14.300 51.374 3.529   1.00 54.19 ? 13  ARG B CZ  1 
ATOM   1850 N NH1 . ARG B 1 37  ? -14.135 52.566 4.080   1.00 46.31 ? 13  ARG B NH1 1 
ATOM   1851 N NH2 . ARG B 1 37  ? -14.042 50.284 4.250   1.00 42.17 ? 13  ARG B NH2 1 
ATOM   1852 N N   . MET B 1 38  ? -14.756 51.203 -3.255  1.00 20.62 ? 14  MET B N   1 
ATOM   1853 C CA  . MET B 1 38  ? -15.528 51.881 -4.284  1.00 23.84 ? 14  MET B CA  1 
ATOM   1854 C C   . MET B 1 38  ? -16.914 52.135 -3.709  1.00 22.71 ? 14  MET B C   1 
ATOM   1855 O O   . MET B 1 38  ? -17.510 51.251 -3.073  1.00 20.89 ? 14  MET B O   1 
ATOM   1856 C CB  . MET B 1 38  ? -15.614 51.085 -5.600  1.00 20.08 ? 14  MET B CB  1 
ATOM   1857 C CG  . MET B 1 38  ? -16.937 51.197 -6.360  1.00 18.27 ? 14  MET B CG  1 
ATOM   1858 S SD  . MET B 1 38  ? -17.269 49.981 -7.671  1.00 19.88 ? 14  MET B SD  1 
ATOM   1859 C CE  . MET B 1 38  ? -15.902 50.258 -8.806  1.00 16.41 ? 14  MET B CE  1 
ATOM   1860 N N   . GLU B 1 39  ? -17.392 53.361 -3.876  1.00 18.67 ? 15  GLU B N   1 
ATOM   1861 C CA  . GLU B 1 39  ? -18.767 53.729 -3.566  1.00 21.82 ? 15  GLU B CA  1 
ATOM   1862 C C   . GLU B 1 39  ? -19.471 53.995 -4.884  1.00 23.63 ? 15  GLU B C   1 
ATOM   1863 O O   . GLU B 1 39  ? -18.903 54.644 -5.769  1.00 21.56 ? 15  GLU B O   1 
ATOM   1864 C CB  . GLU B 1 39  ? -18.814 54.959 -2.668  1.00 21.13 ? 15  GLU B CB  1 
ATOM   1865 C CG  . GLU B 1 39  ? -20.198 55.374 -2.289  1.00 36.77 ? 15  GLU B CG  1 
ATOM   1866 C CD  . GLU B 1 39  ? -20.267 55.877 -0.866  1.00 54.05 ? 15  GLU B CD  1 
ATOM   1867 O OE1 . GLU B 1 39  ? -21.377 55.848 -0.284  1.00 51.39 ? 15  GLU B OE1 1 
ATOM   1868 O OE2 . GLU B 1 39  ? -19.205 56.286 -0.332  1.00 48.13 ? 15  GLU B OE2 1 
ATOM   1869 N N   . GLY B 1 40  ? -20.677 53.471 -5.037  1.00 24.73 ? 16  GLY B N   1 
ATOM   1870 C CA  . GLY B 1 40  ? -21.298 53.513 -6.348  1.00 22.96 ? 16  GLY B CA  1 
ATOM   1871 C C   . GLY B 1 40  ? -22.805 53.591 -6.293  1.00 26.97 ? 16  GLY B C   1 
ATOM   1872 O O   . GLY B 1 40  ? -23.433 53.323 -5.263  1.00 22.87 ? 16  GLY B O   1 
ATOM   1873 N N   . ASN B 1 41  ? -23.376 53.960 -7.434  1.00 23.87 ? 17  ASN B N   1 
ATOM   1874 C CA  . ASN B 1 41  ? -24.824 53.966 -7.614  1.00 22.24 ? 17  ASN B CA  1 
ATOM   1875 C C   . ASN B 1 41  ? -25.102 53.677 -9.081  1.00 29.53 ? 17  ASN B C   1 
ATOM   1876 O O   . ASN B 1 41  ? -24.669 54.443 -9.946  1.00 22.70 ? 17  ASN B O   1 
ATOM   1877 C CB  . ASN B 1 41  ? -25.415 55.308 -7.190  1.00 27.85 ? 17  ASN B CB  1 
ATOM   1878 C CG  . ASN B 1 41  ? -26.917 55.267 -7.074  1.00 33.78 ? 17  ASN B CG  1 
ATOM   1879 O OD1 . ASN B 1 41  ? -27.607 54.925 -8.027  1.00 34.52 ? 17  ASN B OD1 1 
ATOM   1880 N ND2 . ASN B 1 41  ? -27.434 55.604 -5.899  1.00 40.77 ? 17  ASN B ND2 1 
ATOM   1881 N N   . VAL B 1 42  ? -25.801 52.581 -9.367  1.00 23.73 ? 18  VAL B N   1 
ATOM   1882 C CA  . VAL B 1 42  ? -26.088 52.164 -10.739 1.00 22.38 ? 18  VAL B CA  1 
ATOM   1883 C C   . VAL B 1 42  ? -27.595 52.000 -10.876 1.00 27.25 ? 18  VAL B C   1 
ATOM   1884 O O   . VAL B 1 42  ? -28.192 51.165 -10.186 1.00 26.96 ? 18  VAL B O   1 
ATOM   1885 C CB  . VAL B 1 42  ? -25.368 50.854 -11.103 1.00 24.42 ? 18  VAL B CB  1 
ATOM   1886 C CG1 . VAL B 1 42  ? -25.902 50.307 -12.427 1.00 24.52 ? 18  VAL B CG1 1 
ATOM   1887 C CG2 . VAL B 1 42  ? -23.863 51.055 -11.170 1.00 20.03 ? 18  VAL B CG2 1 
ATOM   1888 N N   . ASN B 1 43  ? -28.207 52.776 -11.776 1.00 28.13 ? 19  ASN B N   1 
ATOM   1889 C CA  . ASN B 1 43  ? -29.661 52.733 -11.985 1.00 26.98 ? 19  ASN B CA  1 
ATOM   1890 C C   . ASN B 1 43  ? -30.399 52.925 -10.662 1.00 26.72 ? 19  ASN B C   1 
ATOM   1891 O O   . ASN B 1 43  ? -31.454 52.338 -10.413 1.00 29.20 ? 19  ASN B O   1 
ATOM   1892 C CB  . ASN B 1 43  ? -30.085 51.426 -12.662 1.00 26.93 ? 19  ASN B CB  1 
ATOM   1893 C CG  . ASN B 1 43  ? -30.150 51.535 -14.183 1.00 30.90 ? 19  ASN B CG  1 
ATOM   1894 O OD1 . ASN B 1 43  ? -29.276 52.133 -14.824 1.00 24.27 ? 19  ASN B OD1 1 
ATOM   1895 N ND2 . ASN B 1 43  ? -31.148 50.904 -14.767 1.00 27.80 ? 19  ASN B ND2 1 
ATOM   1896 N N   . GLY B 1 44  ? -29.829 53.751 -9.792  1.00 26.53 ? 20  GLY B N   1 
ATOM   1897 C CA  . GLY B 1 44  ? -30.449 54.034 -8.519  1.00 26.22 ? 20  GLY B CA  1 
ATOM   1898 C C   . GLY B 1 44  ? -30.023 53.139 -7.374  1.00 32.01 ? 20  GLY B C   1 
ATOM   1899 O O   . GLY B 1 44  ? -30.396 53.417 -6.230  1.00 33.34 ? 20  GLY B O   1 
ATOM   1900 N N   . HIS B 1 45  ? -29.254 52.079 -7.628  1.00 27.52 ? 21  HIS B N   1 
ATOM   1901 C CA  . HIS B 1 45  ? -28.883 51.134 -6.578  1.00 31.53 ? 21  HIS B CA  1 
ATOM   1902 C C   . HIS B 1 45  ? -27.516 51.491 -6.005  1.00 27.12 ? 21  HIS B C   1 
ATOM   1903 O O   . HIS B 1 45  ? -26.509 51.428 -6.710  1.00 25.33 ? 21  HIS B O   1 
ATOM   1904 C CB  . HIS B 1 45  ? -28.881 49.699 -7.104  1.00 29.39 ? 21  HIS B CB  1 
ATOM   1905 C CG  . HIS B 1 45  ? -28.731 48.673 -6.028  1.00 34.72 ? 21  HIS B CG  1 
ATOM   1906 N ND1 . HIS B 1 45  ? -29.795 48.209 -5.284  1.00 36.04 ? 21  HIS B ND1 1 
ATOM   1907 C CD2 . HIS B 1 45  ? -27.639 48.010 -5.579  1.00 39.81 ? 21  HIS B CD2 1 
ATOM   1908 C CE1 . HIS B 1 45  ? -29.363 47.309 -4.417  1.00 38.99 ? 21  HIS B CE1 1 
ATOM   1909 N NE2 . HIS B 1 45  ? -28.058 47.171 -4.577  1.00 33.84 ? 21  HIS B NE2 1 
ATOM   1910 N N   . HIS B 1 46  ? -27.487 51.852 -4.724  1.00 25.98 ? 22  HIS B N   1 
ATOM   1911 C CA  . HIS B 1 46  ? -26.237 52.202 -4.059  1.00 29.54 ? 22  HIS B CA  1 
ATOM   1912 C C   . HIS B 1 46  ? -25.508 50.948 -3.589  1.00 30.00 ? 22  HIS B C   1 
ATOM   1913 O O   . HIS B 1 46  ? -26.130 49.942 -3.226  1.00 26.88 ? 22  HIS B O   1 
ATOM   1914 C CB  . HIS B 1 46  ? -26.514 53.122 -2.867  1.00 30.41 ? 22  HIS B CB  1 
ATOM   1915 C CG  . HIS B 1 46  ? -25.301 53.443 -2.048  1.00 39.22 ? 22  HIS B CG  1 
ATOM   1916 N ND1 . HIS B 1 46  ? -25.037 52.836 -0.837  1.00 46.09 ? 22  HIS B ND1 1 
ATOM   1917 C CD2 . HIS B 1 46  ? -24.293 54.325 -2.254  1.00 35.90 ? 22  HIS B CD2 1 
ATOM   1918 C CE1 . HIS B 1 46  ? -23.912 53.322 -0.339  1.00 41.67 ? 22  HIS B CE1 1 
ATOM   1919 N NE2 . HIS B 1 46  ? -23.441 54.227 -1.179  1.00 39.78 ? 22  HIS B NE2 1 
ATOM   1920 N N   . PHE B 1 47  ? -24.176 51.015 -3.588  1.00 24.65 ? 23  PHE B N   1 
ATOM   1921 C CA  . PHE B 1 47  ? -23.378 49.895 -3.107  1.00 25.90 ? 23  PHE B CA  1 
ATOM   1922 C C   . PHE B 1 47  ? -22.015 50.404 -2.651  1.00 27.49 ? 23  PHE B C   1 
ATOM   1923 O O   . PHE B 1 47  ? -21.554 51.472 -3.067  1.00 23.06 ? 23  PHE B O   1 
ATOM   1924 C CB  . PHE B 1 47  ? -23.223 48.821 -4.198  1.00 26.25 ? 23  PHE B CB  1 
ATOM   1925 C CG  . PHE B 1 47  ? -22.711 49.367 -5.498  1.00 20.19 ? 23  PHE B CG  1 
ATOM   1926 C CD1 . PHE B 1 47  ? -23.587 49.902 -6.440  1.00 23.91 ? 23  PHE B CD1 1 
ATOM   1927 C CD2 . PHE B 1 47  ? -21.349 49.373 -5.771  1.00 22.96 ? 23  PHE B CD2 1 
ATOM   1928 C CE1 . PHE B 1 47  ? -23.108 50.423 -7.633  1.00 20.76 ? 23  PHE B CE1 1 
ATOM   1929 C CE2 . PHE B 1 47  ? -20.867 49.901 -6.961  1.00 26.07 ? 23  PHE B CE2 1 
ATOM   1930 C CZ  . PHE B 1 47  ? -21.743 50.427 -7.891  1.00 23.01 ? 23  PHE B CZ  1 
ATOM   1931 N N   . VAL B 1 48  ? -21.375 49.627 -1.778  1.00 25.39 ? 24  VAL B N   1 
ATOM   1932 C CA  . VAL B 1 48  ? -19.988 49.846 -1.377  1.00 20.93 ? 24  VAL B CA  1 
ATOM   1933 C C   . VAL B 1 48  ? -19.250 48.523 -1.529  1.00 22.48 ? 24  VAL B C   1 
ATOM   1934 O O   . VAL B 1 48  ? -19.753 47.477 -1.101  1.00 23.13 ? 24  VAL B O   1 
ATOM   1935 C CB  . VAL B 1 48  ? -19.874 50.366 0.070   1.00 26.22 ? 24  VAL B CB  1 
ATOM   1936 C CG1 . VAL B 1 48  ? -18.413 50.494 0.485   1.00 26.17 ? 24  VAL B CG1 1 
ATOM   1937 C CG2 . VAL B 1 48  ? -20.607 51.702 0.218   1.00 27.20 ? 24  VAL B CG2 1 
ATOM   1938 N N   . ILE B 1 49  ? -18.061 48.565 -2.127  1.00 21.07 ? 25  ILE B N   1 
ATOM   1939 C CA  . ILE B 1 49  ? -17.263 47.371 -2.380  1.00 17.36 ? 25  ILE B CA  1 
ATOM   1940 C C   . ILE B 1 49  ? -15.828 47.641 -1.937  1.00 20.71 ? 25  ILE B C   1 
ATOM   1941 O O   . ILE B 1 49  ? -15.217 48.631 -2.360  1.00 21.04 ? 25  ILE B O   1 
ATOM   1942 C CB  . ILE B 1 49  ? -17.301 46.963 -3.868  1.00 21.45 ? 25  ILE B CB  1 
ATOM   1943 C CG1 . ILE B 1 49  ? -18.747 46.733 -4.331  1.00 17.98 ? 25  ILE B CG1 1 
ATOM   1944 C CG2 . ILE B 1 49  ? -16.441 45.716 -4.105  1.00 20.89 ? 25  ILE B CG2 1 
ATOM   1945 C CD1 . ILE B 1 49  ? -18.897 46.557 -5.838  1.00 18.27 ? 25  ILE B CD1 1 
ATOM   1946 N N   . ASP B 1 50  ? -15.290 46.760 -1.099  1.00 22.65 ? 26  ASP B N   1 
ATOM   1947 C CA  . ASP B 1 50  ? -13.904 46.843 -0.663  1.00 20.52 ? 26  ASP B CA  1 
ATOM   1948 C C   . ASP B 1 50  ? -13.048 45.867 -1.458  1.00 21.84 ? 26  ASP B C   1 
ATOM   1949 O O   . ASP B 1 50  ? -13.498 44.776 -1.819  1.00 20.42 ? 26  ASP B O   1 
ATOM   1950 C CB  . ASP B 1 50  ? -13.775 46.521 0.825   1.00 29.41 ? 26  ASP B CB  1 
ATOM   1951 C CG  . ASP B 1 50  ? -14.300 47.633 1.708   1.00 33.52 ? 26  ASP B CG  1 
ATOM   1952 O OD1 . ASP B 1 50  ? -14.703 48.682 1.169   1.00 30.75 ? 26  ASP B OD1 1 
ATOM   1953 O OD2 . ASP B 1 50  ? -14.306 47.462 2.937   1.00 31.96 ? 26  ASP B OD2 1 
ATOM   1954 N N   . GLY B 1 51  ? -11.804 46.250 -1.694  1.00 21.50 ? 27  GLY B N   1 
ATOM   1955 C CA  . GLY B 1 51  ? -10.862 45.389 -2.394  1.00 23.18 ? 27  GLY B CA  1 
ATOM   1956 C C   . GLY B 1 51  ? -9.545  45.284 -1.660  1.00 22.81 ? 27  GLY B C   1 
ATOM   1957 O O   . GLY B 1 51  ? -9.074  46.248 -1.065  1.00 21.06 ? 27  GLY B O   1 
ATOM   1958 N N   . ASP B 1 52  ? -8.963  44.090 -1.699  1.00 18.58 ? 28  ASP B N   1 
ATOM   1959 C CA  . ASP B 1 52  ? -7.661  43.793 -1.105  1.00 18.22 ? 28  ASP B CA  1 
ATOM   1960 C C   . ASP B 1 52  ? -6.892  42.973 -2.125  1.00 23.69 ? 28  ASP B C   1 
ATOM   1961 O O   . ASP B 1 52  ? -7.332  41.876 -2.479  1.00 22.09 ? 28  ASP B O   1 
ATOM   1962 C CB  . ASP B 1 52  ? -7.817  43.012 0.207   1.00 20.05 ? 28  ASP B CB  1 
ATOM   1963 C CG  . ASP B 1 52  ? -6.544  42.982 1.032   1.00 33.62 ? 28  ASP B CG  1 
ATOM   1964 O OD1 . ASP B 1 52  ? -6.381  42.003 1.780   1.00 58.41 ? 28  ASP B OD1 1 
ATOM   1965 O OD2 . ASP B 1 52  ? -5.705  43.898 0.934   1.00 43.23 ? 28  ASP B OD2 1 
ATOM   1966 N N   . GLY B 1 53  ? -5.763  43.491 -2.608  1.00 21.73 ? 29  GLY B N   1 
ATOM   1967 C CA  . GLY B 1 53  ? -5.047  42.827 -3.678  1.00 23.50 ? 29  GLY B CA  1 
ATOM   1968 C C   . GLY B 1 53  ? -3.540  42.962 -3.579  1.00 26.21 ? 29  GLY B C   1 
ATOM   1969 O O   . GLY B 1 53  ? -2.999  43.584 -2.658  1.00 21.61 ? 29  GLY B O   1 
ATOM   1970 N N   . THR B 1 54  ? -2.870  42.336 -4.549  1.00 20.28 ? 30  THR B N   1 
ATOM   1971 C CA  . THR B 1 54  ? -1.421  42.401 -4.688  1.00 19.82 ? 30  THR B CA  1 
ATOM   1972 C C   . THR B 1 54  ? -1.098  42.410 -6.171  1.00 22.45 ? 30  THR B C   1 
ATOM   1973 O O   . THR B 1 54  ? -1.887  41.942 -6.994  1.00 22.07 ? 30  THR B O   1 
ATOM   1974 C CB  . THR B 1 54  ? -0.705  41.200 -4.052  1.00 27.50 ? 30  THR B CB  1 
ATOM   1975 O OG1 . THR B 1 54  ? -1.200  39.995 -4.651  1.00 26.95 ? 30  THR B OG1 1 
ATOM   1976 C CG2 . THR B 1 54  ? -0.955  41.137 -2.552  1.00 25.77 ? 30  THR B CG2 1 
ATOM   1977 N N   . GLY B 1 55  ? 0.094   42.898 -6.504  1.00 19.73 ? 31  GLY B N   1 
ATOM   1978 C CA  . GLY B 1 55  ? 0.427   43.020 -7.911  1.00 19.11 ? 31  GLY B CA  1 
ATOM   1979 C C   . GLY B 1 55  ? 1.916   43.144 -8.139  1.00 21.85 ? 31  GLY B C   1 
ATOM   1980 O O   . GLY B 1 55  ? 2.701   43.378 -7.213  1.00 21.18 ? 31  GLY B O   1 
ATOM   1981 N N   . LYS B 1 56  ? 2.282   43.020 -9.418  1.00 17.68 ? 32  LYS B N   1 
ATOM   1982 C CA  . LYS B 1 56  ? 3.669   43.077 -9.884  1.00 18.06 ? 32  LYS B CA  1 
ATOM   1983 C C   . LYS B 1 56  ? 3.733   44.216 -10.895 1.00 21.40 ? 32  LYS B C   1 
ATOM   1984 O O   . LYS B 1 56  ? 3.457   44.014 -12.086 1.00 18.01 ? 32  LYS B O   1 
ATOM   1985 C CB  . LYS B 1 56  ? 4.086   41.740 -10.497 1.00 22.82 ? 32  LYS B CB  1 
ATOM   1986 C CG  . LYS B 1 56  ? 4.169   40.629 -9.436  1.00 25.19 ? 32  LYS B CG  1 
ATOM   1987 C CD  . LYS B 1 56  ? 5.105   39.526 -9.838  1.00 36.40 ? 32  LYS B CD  1 
ATOM   1988 C CE  . LYS B 1 56  ? 6.505   39.808 -9.350  1.00 27.81 ? 32  LYS B CE  1 
ATOM   1989 N NZ  . LYS B 1 56  ? 6.843   39.211 -8.018  1.00 23.91 ? 32  LYS B NZ  1 
ATOM   1990 N N   . PRO B 1 57  ? 4.034   45.439 -10.455 1.00 22.15 ? 33  PRO B N   1 
ATOM   1991 C CA  . PRO B 1 57  ? 3.897   46.587 -11.374 1.00 16.64 ? 33  PRO B CA  1 
ATOM   1992 C C   . PRO B 1 57  ? 4.747   46.480 -12.633 1.00 21.92 ? 33  PRO B C   1 
ATOM   1993 O O   . PRO B 1 57  ? 4.303   46.913 -13.707 1.00 21.29 ? 33  PRO B O   1 
ATOM   1994 C CB  . PRO B 1 57  ? 4.325   47.773 -10.505 1.00 17.93 ? 33  PRO B CB  1 
ATOM   1995 C CG  . PRO B 1 57  ? 4.022   47.328 -9.085  1.00 19.91 ? 33  PRO B CG  1 
ATOM   1996 C CD  . PRO B 1 57  ? 4.360   45.862 -9.075  1.00 18.86 ? 33  PRO B CD  1 
ATOM   1997 N N   . PHE B 1 58  ? 5.957   45.913 -12.543 1.00 19.32 ? 34  PHE B N   1 
ATOM   1998 C CA  . PHE B 1 58  ? 6.823   45.848 -13.711 1.00 20.26 ? 34  PHE B CA  1 
ATOM   1999 C C   . PHE B 1 58  ? 6.481   44.686 -14.628 1.00 20.98 ? 34  PHE B C   1 
ATOM   2000 O O   . PHE B 1 58  ? 6.985   44.637 -15.755 1.00 20.46 ? 34  PHE B O   1 
ATOM   2001 C CB  . PHE B 1 58  ? 8.288   45.798 -13.267 1.00 21.66 ? 34  PHE B CB  1 
ATOM   2002 C CG  . PHE B 1 58  ? 8.695   47.006 -12.446 1.00 19.94 ? 34  PHE B CG  1 
ATOM   2003 C CD1 . PHE B 1 58  ? 8.959   48.231 -13.071 1.00 21.88 ? 34  PHE B CD1 1 
ATOM   2004 C CD2 . PHE B 1 58  ? 8.763   46.939 -11.058 1.00 22.91 ? 34  PHE B CD2 1 
ATOM   2005 C CE1 . PHE B 1 58  ? 9.311   49.358 -12.326 1.00 20.98 ? 34  PHE B CE1 1 
ATOM   2006 C CE2 . PHE B 1 58  ? 9.108   48.058 -10.305 1.00 24.98 ? 34  PHE B CE2 1 
ATOM   2007 C CZ  . PHE B 1 58  ? 9.389   49.275 -10.943 1.00 25.59 ? 34  PHE B CZ  1 
ATOM   2008 N N   . GLU B 1 59  ? 5.616   43.767 -14.192 1.00 18.11 ? 35  GLU B N   1 
ATOM   2009 C CA  . GLU B 1 59  ? 5.073   42.756 -15.091 1.00 21.20 ? 35  GLU B CA  1 
ATOM   2010 C C   . GLU B 1 59  ? 3.674   43.098 -15.595 1.00 19.54 ? 35  GLU B C   1 
ATOM   2011 O O   . GLU B 1 59  ? 3.146   42.378 -16.448 1.00 18.38 ? 35  GLU B O   1 
ATOM   2012 C CB  . GLU B 1 59  ? 5.043   41.393 -14.391 1.00 22.58 ? 35  GLU B CB  1 
ATOM   2013 C CG  . GLU B 1 59  ? 6.412   40.922 -13.932 1.00 25.26 ? 35  GLU B CG  1 
ATOM   2014 C CD  . GLU B 1 59  ? 6.421   39.450 -13.538 1.00 27.89 ? 35  GLU B CD  1 
ATOM   2015 O OE1 . GLU B 1 59  ? 5.345   38.813 -13.554 1.00 24.97 ? 35  GLU B OE1 1 
ATOM   2016 O OE2 . GLU B 1 59  ? 7.495   38.943 -13.192 1.00 26.73 ? 35  GLU B OE2 1 
ATOM   2017 N N   . GLY B 1 60  ? 3.061   44.166 -15.087 1.00 16.37 ? 36  GLY B N   1 
ATOM   2018 C CA  . GLY B 1 60  ? 1.717   44.513 -15.515 1.00 15.48 ? 36  GLY B CA  1 
ATOM   2019 C C   . GLY B 1 60  ? 0.647   43.549 -15.059 1.00 18.67 ? 36  GLY B C   1 
ATOM   2020 O O   . GLY B 1 60  ? -0.348  43.357 -15.769 1.00 18.02 ? 36  GLY B O   1 
ATOM   2021 N N   . LYS B 1 61  ? 0.812   42.942 -13.880 1.00 19.82 ? 37  LYS B N   1 
ATOM   2022 C CA  . LYS B 1 61  ? -0.102  41.920 -13.381 1.00 16.27 ? 37  LYS B CA  1 
ATOM   2023 C C   . LYS B 1 61  ? -0.596  42.285 -11.987 1.00 17.22 ? 37  LYS B C   1 
ATOM   2024 O O   . LYS B 1 61  ? 0.186   42.730 -11.145 1.00 18.40 ? 37  LYS B O   1 
ATOM   2025 C CB  . LYS B 1 61  ? 0.599   40.550 -13.339 1.00 16.62 ? 37  LYS B CB  1 
ATOM   2026 C CG  . LYS B 1 61  ? 1.046   40.052 -14.711 1.00 15.73 ? 37  LYS B CG  1 
ATOM   2027 C CD  . LYS B 1 61  ? 1.681   38.649 -14.644 1.00 17.06 ? 37  LYS B CD  1 
ATOM   2028 C CE  . LYS B 1 61  ? 1.762   38.044 -16.044 1.00 18.02 ? 37  LYS B CE  1 
ATOM   2029 N NZ  . LYS B 1 61  ? 2.297   36.627 -16.040 1.00 19.63 ? 37  LYS B NZ  1 
ATOM   2030 N N   . GLN B 1 62  ? -1.884  42.058 -11.727 1.00 15.84 ? 38  GLN B N   1 
ATOM   2031 C CA  . GLN B 1 62  ? -2.420  42.310 -10.393 1.00 14.59 ? 38  GLN B CA  1 
ATOM   2032 C C   . GLN B 1 62  ? -3.658  41.446 -10.185 1.00 18.68 ? 38  GLN B C   1 
ATOM   2033 O O   . GLN B 1 62  ? -4.369  41.122 -11.142 1.00 17.12 ? 38  GLN B O   1 
ATOM   2034 C CB  . GLN B 1 62  ? -2.761  43.793 -10.189 1.00 15.26 ? 38  GLN B CB  1 
ATOM   2035 C CG  . GLN B 1 62  ? -3.922  44.277 -11.052 1.00 20.22 ? 38  GLN B CG  1 
ATOM   2036 C CD  . GLN B 1 62  ? -4.308  45.721 -10.769 1.00 20.44 ? 38  GLN B CD  1 
ATOM   2037 O OE1 . GLN B 1 62  ? -4.425  46.141 -9.613  1.00 19.42 ? 38  GLN B OE1 1 
ATOM   2038 N NE2 . GLN B 1 62  ? -4.459  46.496 -11.823 1.00 19.45 ? 38  GLN B NE2 1 
ATOM   2039 N N   . SER B 1 63  ? -3.894  41.068 -8.924  1.00 16.50 ? 39  SER B N   1 
ATOM   2040 C CA  . SER B 1 63  ? -5.092  40.349 -8.511  1.00 18.85 ? 39  SER B CA  1 
ATOM   2041 C C   . SER B 1 63  ? -5.715  41.039 -7.309  1.00 24.04 ? 39  SER B C   1 
ATOM   2042 O O   . SER B 1 63  ? -5.021  41.664 -6.505  1.00 23.38 ? 39  SER B O   1 
ATOM   2043 C CB  . SER B 1 63  ? -4.800  38.891 -8.127  1.00 19.72 ? 39  SER B CB  1 
ATOM   2044 O OG  . SER B 1 63  ? -4.017  38.258 -9.112  1.00 28.50 ? 39  SER B OG  1 
ATOM   2045 N N   . MET B 1 64  ? -7.026  40.871 -7.156  1.00 18.13 ? 40  MET B N   1 
ATOM   2046 C CA  . MET B 1 64  ? -7.729  41.565 -6.092  1.00 17.74 ? 40  MET B CA  1 
ATOM   2047 C C   . MET B 1 64  ? -8.874  40.685 -5.604  1.00 23.05 ? 40  MET B C   1 
ATOM   2048 O O   . MET B 1 64  ? -9.572  40.073 -6.415  1.00 22.32 ? 40  MET B O   1 
ATOM   2049 C CB  . MET B 1 64  ? -8.262  42.898 -6.620  1.00 21.86 ? 40  MET B CB  1 
ATOM   2050 C CG  . MET B 1 64  ? -9.311  43.576 -5.763  1.00 32.55 ? 40  MET B CG  1 
ATOM   2051 S SD  . MET B 1 64  ? -9.282  45.371 -5.942  1.00 24.20 ? 40  MET B SD  1 
ATOM   2052 C CE  . MET B 1 64  ? -7.533  45.724 -5.944  1.00 32.64 ? 40  MET B CE  1 
ATOM   2053 N N   . ASP B 1 65  ? -9.045  40.605 -4.282  1.00 21.86 ? 41  ASP B N   1 
ATOM   2054 C CA  . ASP B 1 65  ? -10.242 40.027 -3.675  1.00 24.46 ? 41  ASP B CA  1 
ATOM   2055 C C   . ASP B 1 65  ? -11.230 41.148 -3.378  1.00 25.22 ? 41  ASP B C   1 
ATOM   2056 O O   . ASP B 1 65  ? -10.907 42.069 -2.620  1.00 23.49 ? 41  ASP B O   1 
ATOM   2057 C CB  . ASP B 1 65  ? -9.914  39.286 -2.376  1.00 23.09 ? 41  ASP B CB  1 
ATOM   2058 C CG  . ASP B 1 65  ? -9.046  38.079 -2.597  1.00 34.49 ? 41  ASP B CG  1 
ATOM   2059 O OD1 . ASP B 1 65  ? -9.402  37.268 -3.465  1.00 30.44 ? 41  ASP B OD1 1 
ATOM   2060 O OD2 . ASP B 1 65  ? -8.021  37.940 -1.895  1.00 41.96 ? 41  ASP B OD2 1 
ATOM   2061 N N   . LEU B 1 66  ? -12.438 41.059 -3.946  1.00 21.11 ? 42  LEU B N   1 
ATOM   2062 C CA  . LEU B 1 66  ? -13.466 42.077 -3.777  1.00 16.95 ? 42  LEU B CA  1 
ATOM   2063 C C   . LEU B 1 66  ? -14.593 41.559 -2.897  1.00 20.40 ? 42  LEU B C   1 
ATOM   2064 O O   . LEU B 1 66  ? -14.989 40.392 -2.998  1.00 21.57 ? 42  LEU B O   1 
ATOM   2065 C CB  . LEU B 1 66  ? -14.017 42.491 -5.141  1.00 24.76 ? 42  LEU B CB  1 
ATOM   2066 C CG  . LEU B 1 66  ? -12.924 43.113 -6.005  1.00 23.45 ? 42  LEU B CG  1 
ATOM   2067 C CD1 . LEU B 1 66  ? -13.232 42.898 -7.483  1.00 18.16 ? 42  LEU B CD1 1 
ATOM   2068 C CD2 . LEU B 1 66  ? -12.828 44.589 -5.672  1.00 20.00 ? 42  LEU B CD2 1 
ATOM   2069 N N   . GLU B 1 67  ? -15.115 42.417 -2.025  1.00 22.61 ? 43  GLU B N   1 
ATOM   2070 C CA  . GLU B 1 67  ? -16.258 42.019 -1.220  1.00 23.81 ? 43  GLU B CA  1 
ATOM   2071 C C   . GLU B 1 67  ? -17.262 43.164 -1.192  1.00 27.13 ? 43  GLU B C   1 
ATOM   2072 O O   . GLU B 1 67  ? -16.899 44.312 -0.911  1.00 25.32 ? 43  GLU B O   1 
ATOM   2073 C CB  . GLU B 1 67  ? -15.833 41.602 0.199   1.00 24.51 ? 43  GLU B CB  1 
ATOM   2074 C CG  . GLU B 1 67  ? -17.013 41.181 1.054   1.00 31.14 ? 43  GLU B CG  1 
ATOM   2075 C CD  . GLU B 1 67  ? -16.609 40.633 2.405   1.00 43.55 ? 43  GLU B CD  1 
ATOM   2076 O OE1 . GLU B 1 67  ? -15.405 40.674 2.732   1.00 43.48 ? 43  GLU B OE1 1 
ATOM   2077 O OE2 . GLU B 1 67  ? -17.506 40.154 3.134   1.00 44.72 ? 43  GLU B OE2 1 
ATOM   2078 N N   . VAL B 1 68  ? -18.505 42.855 -1.544  1.00 28.51 ? 44  VAL B N   1 
ATOM   2079 C CA  . VAL B 1 68  ? -19.598 43.819 -1.473  1.00 25.37 ? 44  VAL B CA  1 
ATOM   2080 C C   . VAL B 1 68  ? -19.958 44.028 -0.007  1.00 30.42 ? 44  VAL B C   1 
ATOM   2081 O O   . VAL B 1 68  ? -20.385 43.092 0.678   1.00 27.08 ? 44  VAL B O   1 
ATOM   2082 C CB  . VAL B 1 68  ? -20.813 43.335 -2.280  1.00 23.63 ? 44  VAL B CB  1 
ATOM   2083 C CG1 . VAL B 1 68  ? -21.954 44.361 -2.211  1.00 27.46 ? 44  VAL B CG1 1 
ATOM   2084 C CG2 . VAL B 1 68  ? -20.420 43.083 -3.737  1.00 25.41 ? 44  VAL B CG2 1 
ATOM   2085 N N   . LYS B 1 69  ? -19.769 45.253 0.486   1.00 26.09 ? 45  LYS B N   1 
ATOM   2086 C CA  . LYS B 1 69  ? -20.047 45.561 1.884   1.00 25.40 ? 45  LYS B CA  1 
ATOM   2087 C C   . LYS B 1 69  ? -21.444 46.130 2.098   1.00 26.59 ? 45  LYS B C   1 
ATOM   2088 O O   . LYS B 1 69  ? -22.024 45.943 3.172   1.00 29.01 ? 45  LYS B O   1 
ATOM   2089 C CB  . LYS B 1 69  ? -18.999 46.547 2.415   1.00 26.89 ? 45  LYS B CB  1 
ATOM   2090 C CG  . LYS B 1 69  ? -17.565 46.005 2.420   1.00 27.47 ? 45  LYS B CG  1 
ATOM   2091 C CD  . LYS B 1 69  ? -17.411 44.826 3.370   1.00 30.65 ? 45  LYS B CD  1 
ATOM   2092 C CE  . LYS B 1 69  ? -15.991 44.281 3.374   1.00 48.51 ? 45  LYS B CE  1 
ATOM   2093 N NZ  . LYS B 1 69  ? -15.018 45.227 3.990   1.00 51.63 ? 45  LYS B NZ  1 
ATOM   2094 N N   . GLU B 1 70  ? -22.003 46.812 1.098   1.00 24.69 ? 46  GLU B N   1 
ATOM   2095 C CA  . GLU B 1 70  ? -23.340 47.377 1.175   1.00 28.09 ? 46  GLU B CA  1 
ATOM   2096 C C   . GLU B 1 70  ? -23.992 47.225 -0.185  1.00 27.64 ? 46  GLU B C   1 
ATOM   2097 O O   . GLU B 1 70  ? -23.321 47.318 -1.216  1.00 26.68 ? 46  GLU B O   1 
ATOM   2098 C CB  . GLU B 1 70  ? -23.330 48.862 1.532   1.00 32.17 ? 46  GLU B CB  1 
ATOM   2099 C CG  . GLU B 1 70  ? -22.439 49.249 2.672   1.00 37.35 ? 46  GLU B CG  1 
ATOM   2100 C CD  . GLU B 1 70  ? -22.683 50.674 3.106   1.00 52.89 ? 46  GLU B CD  1 
ATOM   2101 O OE1 . GLU B 1 70  ? -21.846 51.214 3.863   1.00 45.21 ? 46  GLU B OE1 1 
ATOM   2102 O OE2 . GLU B 1 70  ? -23.702 51.256 2.661   1.00 50.03 ? 46  GLU B OE2 1 
ATOM   2103 N N   . GLY B 1 71  ? -25.305 47.012 -0.188  1.00 25.10 ? 47  GLY B N   1 
ATOM   2104 C CA  . GLY B 1 71  ? -26.034 46.949 -1.442  1.00 28.32 ? 47  GLY B CA  1 
ATOM   2105 C C   . GLY B 1 71  ? -26.036 45.606 -2.139  1.00 28.81 ? 47  GLY B C   1 
ATOM   2106 O O   . GLY B 1 71  ? -26.525 45.519 -3.272  1.00 30.32 ? 47  GLY B O   1 
ATOM   2107 N N   . GLY B 1 72  ? -25.496 44.561 -1.515  1.00 25.08 ? 48  GLY B N   1 
ATOM   2108 C CA  . GLY B 1 72  ? -25.577 43.225 -2.057  1.00 24.27 ? 48  GLY B CA  1 
ATOM   2109 C C   . GLY B 1 72  ? -26.931 42.602 -1.783  1.00 30.54 ? 48  GLY B C   1 
ATOM   2110 O O   . GLY B 1 72  ? -27.612 42.959 -0.818  1.00 31.23 ? 48  GLY B O   1 
ATOM   2111 N N   . PRO B 1 73  ? -27.370 41.670 -2.648  1.00 25.99 ? 49  PRO B N   1 
ATOM   2112 C CA  . PRO B 1 73  ? -26.731 41.221 -3.900  1.00 26.07 ? 49  PRO B CA  1 
ATOM   2113 C C   . PRO B 1 73  ? -26.879 42.255 -5.026  1.00 28.76 ? 49  PRO B C   1 
ATOM   2114 O O   . PRO B 1 73  ? -27.939 42.856 -5.163  1.00 26.18 ? 49  PRO B O   1 
ATOM   2115 C CB  . PRO B 1 73  ? -27.472 39.907 -4.203  1.00 30.06 ? 49  PRO B CB  1 
ATOM   2116 C CG  . PRO B 1 73  ? -28.870 40.145 -3.652  1.00 34.99 ? 49  PRO B CG  1 
ATOM   2117 C CD  . PRO B 1 73  ? -28.648 40.968 -2.393  1.00 26.78 ? 49  PRO B CD  1 
ATOM   2118 N N   . LEU B 1 74  ? -25.842 42.499 -5.832  1.00 25.19 ? 50  LEU B N   1 
ATOM   2119 C CA  . LEU B 1 74  ? -25.935 43.510 -6.885  1.00 29.86 ? 50  LEU B CA  1 
ATOM   2120 C C   . LEU B 1 74  ? -26.947 43.071 -7.937  1.00 24.56 ? 50  LEU B C   1 
ATOM   2121 O O   . LEU B 1 74  ? -26.926 41.909 -8.357  1.00 24.01 ? 50  LEU B O   1 
ATOM   2122 C CB  . LEU B 1 74  ? -24.566 43.756 -7.539  1.00 25.31 ? 50  LEU B CB  1 
ATOM   2123 C CG  . LEU B 1 74  ? -23.504 44.325 -6.592  1.00 28.45 ? 50  LEU B CG  1 
ATOM   2124 C CD1 . LEU B 1 74  ? -22.163 44.518 -7.322  1.00 23.43 ? 50  LEU B CD1 1 
ATOM   2125 C CD2 . LEU B 1 74  ? -23.991 45.629 -5.925  1.00 23.39 ? 50  LEU B CD2 1 
ATOM   2126 N N   . PRO B 1 75  ? -27.857 43.965 -8.377  1.00 28.02 ? 51  PRO B N   1 
ATOM   2127 C CA  . PRO B 1 75  ? -28.863 43.584 -9.377  1.00 28.04 ? 51  PRO B CA  1 
ATOM   2128 C C   . PRO B 1 75  ? -28.421 43.894 -10.803 1.00 27.06 ? 51  PRO B C   1 
ATOM   2129 O O   . PRO B 1 75  ? -29.250 43.983 -11.718 1.00 31.01 ? 51  PRO B O   1 
ATOM   2130 C CB  . PRO B 1 75  ? -30.072 44.435 -8.967  1.00 26.01 ? 51  PRO B CB  1 
ATOM   2131 C CG  . PRO B 1 75  ? -29.416 45.729 -8.531  1.00 26.80 ? 51  PRO B CG  1 
ATOM   2132 C CD  . PRO B 1 75  ? -28.130 45.303 -7.816  1.00 22.80 ? 51  PRO B CD  1 
ATOM   2133 N N   . PHE B 1 76  ? -27.116 44.065 -11.007 1.00 26.74 ? 52  PHE B N   1 
ATOM   2134 C CA  . PHE B 1 76  ? -26.564 44.328 -12.328 1.00 23.54 ? 52  PHE B CA  1 
ATOM   2135 C C   . PHE B 1 76  ? -25.290 43.514 -12.515 1.00 26.03 ? 52  PHE B C   1 
ATOM   2136 O O   . PHE B 1 76  ? -24.714 42.994 -11.558 1.00 25.23 ? 52  PHE B O   1 
ATOM   2137 C CB  . PHE B 1 76  ? -26.288 45.822 -12.536 1.00 22.89 ? 52  PHE B CB  1 
ATOM   2138 C CG  . PHE B 1 76  ? -25.379 46.420 -11.505 1.00 22.42 ? 52  PHE B CG  1 
ATOM   2139 C CD1 . PHE B 1 76  ? -23.995 46.324 -11.640 1.00 20.75 ? 52  PHE B CD1 1 
ATOM   2140 C CD2 . PHE B 1 76  ? -25.906 47.077 -10.392 1.00 24.38 ? 52  PHE B CD2 1 
ATOM   2141 C CE1 . PHE B 1 76  ? -23.150 46.875 -10.685 1.00 25.92 ? 52  PHE B CE1 1 
ATOM   2142 C CE2 . PHE B 1 76  ? -25.068 47.630 -9.429  1.00 26.48 ? 52  PHE B CE2 1 
ATOM   2143 C CZ  . PHE B 1 76  ? -23.687 47.528 -9.579  1.00 23.74 ? 52  PHE B CZ  1 
ATOM   2144 N N   . ALA B 1 77  ? -24.847 43.421 -13.773 1.00 24.12 ? 53  ALA B N   1 
ATOM   2145 C CA  . ALA B 1 77  ? -23.667 42.632 -14.123 1.00 19.61 ? 53  ALA B CA  1 
ATOM   2146 C C   . ALA B 1 77  ? -22.422 43.173 -13.428 1.00 24.92 ? 53  ALA B C   1 
ATOM   2147 O O   . ALA B 1 77  ? -22.050 44.338 -13.617 1.00 21.48 ? 53  ALA B O   1 
ATOM   2148 C CB  . ALA B 1 77  ? -23.475 42.641 -15.636 1.00 23.07 ? 53  ALA B CB  1 
ATOM   2149 N N   . PHE B 1 78  ? -21.763 42.320 -12.639 1.00 22.33 ? 54  PHE B N   1 
ATOM   2150 C CA  . PHE B 1 78  ? -20.538 42.737 -11.960 1.00 21.25 ? 54  PHE B CA  1 
ATOM   2151 C C   . PHE B 1 78  ? -19.502 43.270 -12.944 1.00 20.16 ? 54  PHE B C   1 
ATOM   2152 O O   . PHE B 1 78  ? -18.744 44.192 -12.613 1.00 17.72 ? 54  PHE B O   1 
ATOM   2153 C CB  . PHE B 1 78  ? -19.955 41.572 -11.150 1.00 17.44 ? 54  PHE B CB  1 
ATOM   2154 C CG  . PHE B 1 78  ? -19.007 42.010 -10.052 1.00 23.88 ? 54  PHE B CG  1 
ATOM   2155 C CD1 . PHE B 1 78  ? -17.666 42.239 -10.319 1.00 19.06 ? 54  PHE B CD1 1 
ATOM   2156 C CD2 . PHE B 1 78  ? -19.474 42.221 -8.758  1.00 20.79 ? 54  PHE B CD2 1 
ATOM   2157 C CE1 . PHE B 1 78  ? -16.791 42.645 -9.302  1.00 17.76 ? 54  PHE B CE1 1 
ATOM   2158 C CE2 . PHE B 1 78  ? -18.607 42.626 -7.737  1.00 19.05 ? 54  PHE B CE2 1 
ATOM   2159 C CZ  . PHE B 1 78  ? -17.266 42.843 -8.016  1.00 19.22 ? 54  PHE B CZ  1 
ATOM   2160 N N   . ASP B 1 79  ? -19.495 42.748 -14.174 1.00 21.52 ? 55  ASP B N   1 
ATOM   2161 C CA  . ASP B 1 79  ? -18.458 43.107 -15.142 1.00 16.47 ? 55  ASP B CA  1 
ATOM   2162 C C   . ASP B 1 79  ? -18.399 44.609 -15.428 1.00 18.84 ? 55  ASP B C   1 
ATOM   2163 O O   . ASP B 1 79  ? -17.348 45.110 -15.840 1.00 18.22 ? 55  ASP B O   1 
ATOM   2164 C CB  . ASP B 1 79  ? -18.683 42.356 -16.458 1.00 17.15 ? 55  ASP B CB  1 
ATOM   2165 C CG  . ASP B 1 79  ? -18.297 40.897 -16.374 1.00 22.13 ? 55  ASP B CG  1 
ATOM   2166 O OD1 . ASP B 1 79  ? -17.273 40.582 -15.718 1.00 19.35 ? 55  ASP B OD1 1 
ATOM   2167 O OD2 . ASP B 1 79  ? -19.011 40.070 -16.988 1.00 22.40 ? 55  ASP B OD2 1 
ATOM   2168 N N   . ILE B 1 80  ? -19.503 45.346 -15.275 1.00 19.23 ? 56  ILE B N   1 
ATOM   2169 C CA  . ILE B 1 80  ? -19.407 46.763 -15.634 1.00 16.87 ? 56  ILE B CA  1 
ATOM   2170 C C   . ILE B 1 80  ? -18.463 47.496 -14.692 1.00 16.94 ? 56  ILE B C   1 
ATOM   2171 O O   . ILE B 1 80  ? -17.914 48.547 -15.057 1.00 16.53 ? 56  ILE B O   1 
ATOM   2172 C CB  . ILE B 1 80  ? -20.777 47.474 -15.665 1.00 15.65 ? 56  ILE B CB  1 
ATOM   2173 C CG1 . ILE B 1 80  ? -21.383 47.622 -14.262 1.00 16.16 ? 56  ILE B CG1 1 
ATOM   2174 C CG2 . ILE B 1 80  ? -21.723 46.789 -16.651 1.00 20.46 ? 56  ILE B CG2 1 
ATOM   2175 C CD1 . ILE B 1 80  ? -22.587 48.605 -14.242 1.00 18.08 ? 56  ILE B CD1 1 
ATOM   2176 N N   . LEU B 1 81  ? -18.236 46.951 -13.492 1.00 14.74 ? 57  LEU B N   1 
ATOM   2177 C CA  . LEU B 1 81  ? -17.396 47.598 -12.493 1.00 14.31 ? 57  LEU B CA  1 
ATOM   2178 C C   . LEU B 1 81  ? -15.918 47.268 -12.621 1.00 18.78 ? 57  LEU B C   1 
ATOM   2179 O O   . LEU B 1 81  ? -15.094 47.990 -12.046 1.00 15.55 ? 57  LEU B O   1 
ATOM   2180 C CB  . LEU B 1 81  ? -17.821 47.168 -11.086 1.00 14.98 ? 57  LEU B CB  1 
ATOM   2181 C CG  . LEU B 1 81  ? -19.300 47.338 -10.737 1.00 17.68 ? 57  LEU B CG  1 
ATOM   2182 C CD1 . LEU B 1 81  ? -19.576 46.644 -9.404  1.00 20.53 ? 57  LEU B CD1 1 
ATOM   2183 C CD2 . LEU B 1 81  ? -19.633 48.801 -10.659 1.00 14.25 ? 57  LEU B CD2 1 
ATOM   2184 N N   . THR B 1 82  ? -15.555 46.192 -13.319 1.00 16.35 ? 58  THR B N   1 
ATOM   2185 C CA  . THR B 1 82  ? -14.261 45.568 -13.023 1.00 17.70 ? 58  THR B CA  1 
ATOM   2186 C C   . THR B 1 82  ? -13.071 46.393 -13.510 1.00 17.32 ? 58  THR B C   1 
ATOM   2187 O O   . THR B 1 82  ? -12.009 46.344 -12.881 1.00 16.11 ? 58  THR B O   1 
ATOM   2188 C CB  . THR B 1 82  ? -14.188 44.145 -13.589 1.00 15.77 ? 58  THR B CB  1 
ATOM   2189 O OG1 . THR B 1 82  ? -14.472 44.167 -14.989 1.00 15.72 ? 58  THR B OG1 1 
ATOM   2190 C CG2 . THR B 1 82  ? -15.184 43.204 -12.871 1.00 16.89 ? 58  THR B CG2 1 
ATOM   2191 N N   . THR B 1 83  ? -13.204 47.153 -14.605 1.00 15.34 ? 59  THR B N   1 
ATOM   2192 C CA  . THR B 1 83  ? -12.071 48.008 -14.985 1.00 16.20 ? 59  THR B CA  1 
ATOM   2193 C C   . THR B 1 83  ? -11.901 49.195 -14.051 1.00 17.25 ? 59  THR B C   1 
ATOM   2194 O O   . THR B 1 83  ? -10.856 49.860 -14.097 1.00 16.74 ? 59  THR B O   1 
ATOM   2195 C CB  . THR B 1 83  ? -12.188 48.524 -16.427 1.00 15.09 ? 59  THR B CB  1 
ATOM   2196 O OG1 . THR B 1 83  ? -13.268 49.462 -16.539 1.00 17.58 ? 59  THR B OG1 1 
ATOM   2197 C CG2 . THR B 1 83  ? -12.376 47.361 -17.419 1.00 15.76 ? 59  THR B CG2 1 
ATOM   2198 N N   . ALA B 1 84  ? -12.879 49.472 -13.194 1.00 16.18 ? 60  ALA B N   1 
ATOM   2199 C CA  . ALA B 1 84  ? -12.679 50.508 -12.191 1.00 18.38 ? 60  ALA B CA  1 
ATOM   2200 C C   . ALA B 1 84  ? -11.883 49.988 -10.997 1.00 18.97 ? 60  ALA B C   1 
ATOM   2201 O O   . ALA B 1 84  ? -11.249 50.786 -10.293 1.00 22.25 ? 60  ALA B O   1 
ATOM   2202 C CB  . ALA B 1 84  ? -14.027 51.072 -11.733 1.00 18.94 ? 60  ALA B CB  1 
ATOM   2203 N N   . PHE B 1 85  ? -11.891 48.676 -10.768 1.00 15.06 ? 61  PHE B N   1 
ATOM   2204 C CA  . PHE B 1 85  ? -11.043 48.058 -9.757  1.00 15.01 ? 61  PHE B CA  1 
ATOM   2205 C C   . PHE B 1 85  ? -9.632  47.898 -10.305 1.00 18.79 ? 61  PHE B C   1 
ATOM   2206 O O   . PHE B 1 85  ? -8.654  48.094 -9.569  1.00 17.48 ? 61  PHE B O   1 
ATOM   2207 C CB  . PHE B 1 85  ? -11.566 46.673 -9.344  1.00 17.31 ? 61  PHE B CB  1 
ATOM   2208 C CG  . PHE B 1 85  ? -12.957 46.690 -8.763  1.00 17.69 ? 61  PHE B CG  1 
ATOM   2209 C CD1 . PHE B 1 85  ? -13.263 47.490 -7.665  1.00 19.35 ? 61  PHE B CD1 1 
ATOM   2210 C CD2 . PHE B 1 85  ? -13.954 45.894 -9.311  1.00 19.14 ? 61  PHE B CD2 1 
ATOM   2211 C CE1 . PHE B 1 85  ? -14.552 47.494 -7.133  1.00 20.15 ? 61  PHE B CE1 1 
ATOM   2212 C CE2 . PHE B 1 85  ? -15.234 45.898 -8.787  1.00 18.45 ? 61  PHE B CE2 1 
ATOM   2213 C CZ  . PHE B 1 85  ? -15.532 46.705 -7.696  1.00 20.47 ? 61  PHE B CZ  1 
HETATM 2214 C C1  . 5SQ B 1 86  ? -8.279  48.323 -13.572 1.00 14.77 ? 64  5SQ B C1  1 
HETATM 2215 C C2  . 5SQ B 1 86  ? -8.066  50.452 -14.487 1.00 14.38 ? 64  5SQ B C2  1 
HETATM 2216 O O3  . 5SQ B 1 86  ? -7.017  52.341 -11.174 1.00 15.60 ? 64  5SQ B O3  1 
HETATM 2217 C C3  . 5SQ B 1 86  ? -6.870  51.310 -11.876 1.00 18.08 ? 64  5SQ B C3  1 
HETATM 2218 C CA3 . 5SQ B 1 86  ? -7.925  50.232 -11.900 1.00 20.53 ? 64  5SQ B CA3 1 
HETATM 2219 N N3  . 5SQ B 1 86  ? -8.074  49.677 -13.245 1.00 16.35 ? 64  5SQ B N3  1 
HETATM 2220 O O2  . 5SQ B 1 86  ? -7.947  51.605 -14.729 1.00 16.36 ? 64  5SQ B O2  1 
HETATM 2221 C CA1 . 5SQ B 1 86  ? -8.297  47.337 -12.363 1.00 17.44 ? 64  5SQ B CA1 1 
HETATM 2222 N N1  . 5SQ B 1 86  ? -9.523  47.516 -11.585 1.00 19.33 ? 64  5SQ B N1  1 
HETATM 2223 C CB1 . 5SQ B 1 86  ? -8.139  45.886 -12.852 1.00 16.30 ? 64  5SQ B CB1 1 
HETATM 2224 C CG1 . 5SQ B 1 86  ? -7.852  44.881 -11.701 1.00 14.71 ? 64  5SQ B CG1 1 
HETATM 2225 C C2H . 5SQ B 1 86  ? -7.835  43.520 -11.866 1.00 13.33 ? 64  5SQ B C2H 1 
HETATM 2226 N N2H . 5SQ B 1 86  ? -7.563  42.969 -10.689 1.00 22.64 ? 64  5SQ B N2H 1 
HETATM 2227 N N1H . 5SQ B 1 86  ? -7.575  45.140 -10.432 1.00 20.84 ? 64  5SQ B N1H 1 
HETATM 2228 C C1H . 5SQ B 1 86  ? -7.386  43.957 -9.787  1.00 14.77 ? 64  5SQ B C1H 1 
HETATM 2229 N N2  . 5SQ B 1 86  ? -8.406  48.080 -14.966 1.00 20.97 ? 64  5SQ B N2  1 
HETATM 2230 C CA2 . 5SQ B 1 86  ? -8.315  49.420 -15.614 1.00 18.31 ? 64  5SQ B CA2 1 
HETATM 2231 C CB2 . 5SQ B 1 86  ? -8.398  49.248 -16.930 1.00 19.84 ? 64  5SQ B CB2 1 
HETATM 2232 C CG2 . 5SQ B 1 86  ? -8.694  48.162 -17.934 1.00 18.62 ? 64  5SQ B CG2 1 
HETATM 2233 C CD2 . 5SQ B 1 86  ? -8.696  46.798 -17.723 1.00 18.61 ? 64  5SQ B CD2 1 
HETATM 2234 C CE2 . 5SQ B 1 86  ? -9.048  46.025 -18.816 1.00 14.92 ? 64  5SQ B CE2 1 
HETATM 2235 C CD1 . 5SQ B 1 86  ? -9.061  48.751 -19.141 1.00 16.64 ? 64  5SQ B CD1 1 
HETATM 2236 C CE1 . 5SQ B 1 86  ? -9.402  47.974 -20.224 1.00 15.75 ? 64  5SQ B CE1 1 
HETATM 2237 C CZ1 . 5SQ B 1 86  ? -9.401  46.605 -20.032 1.00 16.29 ? 64  5SQ B CZ1 1 
HETATM 2238 O OH  . 5SQ B 1 86  ? -9.742  45.792 -21.115 1.00 17.42 ? 64  5SQ B OH  1 
ATOM   2239 N N   . ASN B 1 87  ? -5.693  50.840 -12.273 1.00 13.98 ? 65  ASN B N   1 
ATOM   2240 C CA  . ASN B 1 87  ? -4.470  51.522 -11.893 1.00 19.39 ? 65  ASN B CA  1 
ATOM   2241 C C   . ASN B 1 87  ? -3.397  51.188 -12.908 1.00 16.51 ? 65  ASN B C   1 
ATOM   2242 O O   . ASN B 1 87  ? -2.815  50.107 -12.871 1.00 16.56 ? 65  ASN B O   1 
ATOM   2243 C CB  . ASN B 1 87  ? -4.038  51.112 -10.472 1.00 15.71 ? 65  ASN B CB  1 
ATOM   2244 C CG  . ASN B 1 87  ? -2.747  51.806 -10.021 1.00 16.88 ? 65  ASN B CG  1 
ATOM   2245 O OD1 . ASN B 1 87  ? -2.173  52.617 -10.751 1.00 17.22 ? 65  ASN B OD1 1 
ATOM   2246 N ND2 . ASN B 1 87  ? -2.291  51.488 -8.813  1.00 14.17 ? 65  ASN B ND2 1 
ATOM   2247 N N   . ARG B 1 88  ? -3.144  52.114 -13.833 1.00 16.46 ? 66  ARG B N   1 
ATOM   2248 C CA  . ARG B 1 88  ? -2.216  51.835 -14.932 1.00 18.29 ? 66  ARG B CA  1 
ATOM   2249 C C   . ARG B 1 88  ? -0.757  51.760 -14.491 1.00 15.67 ? 66  ARG B C   1 
ATOM   2250 O O   . ARG B 1 88  ? 0.119   51.507 -15.330 1.00 17.66 ? 66  ARG B O   1 
ATOM   2251 C CB  . ARG B 1 88  ? -2.414  52.871 -16.048 1.00 16.62 ? 66  ARG B CB  1 
ATOM   2252 C CG  . ARG B 1 88  ? -2.009  52.359 -17.453 1.00 21.26 ? 66  ARG B CG  1 
ATOM   2253 C CD  . ARG B 1 88  ? -3.028  51.392 -18.114 1.00 19.79 ? 66  ARG B CD  1 
ATOM   2254 N NE  . ARG B 1 88  ? -4.414  51.853 -18.069 1.00 16.38 ? 66  ARG B NE  1 
ATOM   2255 C CZ  . ARG B 1 88  ? -5.288  51.550 -17.118 1.00 20.40 ? 66  ARG B CZ  1 
ATOM   2256 N NH1 . ARG B 1 88  ? -5.015  50.656 -16.177 1.00 19.27 ? 66  ARG B NH1 1 
ATOM   2257 N NH2 . ARG B 1 88  ? -6.464  52.169 -17.099 1.00 18.64 ? 66  ARG B NH2 1 
ATOM   2258 N N   . VAL B 1 89  ? -0.467  51.912 -13.200 1.00 16.51 ? 67  VAL B N   1 
ATOM   2259 C CA  . VAL B 1 89  ? 0.826   51.477 -12.679 1.00 17.16 ? 67  VAL B CA  1 
ATOM   2260 C C   . VAL B 1 89  ? 1.051   50.004 -12.981 1.00 18.10 ? 67  VAL B C   1 
ATOM   2261 O O   . VAL B 1 89  ? 2.185   49.562 -13.209 1.00 18.38 ? 67  VAL B O   1 
ATOM   2262 C CB  . VAL B 1 89  ? 0.912   51.750 -11.165 1.00 18.23 ? 67  VAL B CB  1 
ATOM   2263 C CG1 . VAL B 1 89  ? 2.106   51.043 -10.551 1.00 29.15 ? 67  VAL B CG1 1 
ATOM   2264 C CG2 . VAL B 1 89  ? 1.035   53.227 -10.933 1.00 20.40 ? 67  VAL B CG2 1 
ATOM   2265 N N   . PHE B 1 90  ? -0.014  49.210 -12.952 1.00 15.47 ? 68  PHE B N   1 
ATOM   2266 C CA  . PHE B 1 90  ? 0.120   47.780 -13.218 1.00 16.95 ? 68  PHE B CA  1 
ATOM   2267 C C   . PHE B 1 90  ? 0.017   47.548 -14.725 1.00 19.11 ? 68  PHE B C   1 
ATOM   2268 O O   . PHE B 1 90  ? -0.956  47.002 -15.252 1.00 21.38 ? 68  PHE B O   1 
ATOM   2269 C CB  . PHE B 1 90  ? -0.911  46.995 -12.422 1.00 18.65 ? 68  PHE B CB  1 
ATOM   2270 C CG  . PHE B 1 90  ? -0.682  47.069 -10.941 1.00 19.49 ? 68  PHE B CG  1 
ATOM   2271 C CD1 . PHE B 1 90  ? 0.291   46.274 -10.346 1.00 21.31 ? 68  PHE B CD1 1 
ATOM   2272 C CD2 . PHE B 1 90  ? -1.366  47.984 -10.158 1.00 18.88 ? 68  PHE B CD2 1 
ATOM   2273 C CE1 . PHE B 1 90  ? 0.531   46.353 -8.970  1.00 22.68 ? 68  PHE B CE1 1 
ATOM   2274 C CE2 . PHE B 1 90  ? -1.131  48.065 -8.781  1.00 20.12 ? 68  PHE B CE2 1 
ATOM   2275 C CZ  . PHE B 1 90  ? -0.179  47.253 -8.194  1.00 22.06 ? 68  PHE B CZ  1 
ATOM   2276 N N   . ALA B 1 91  ? 1.073   47.983 -15.409 1.00 17.66 ? 69  ALA B N   1 
ATOM   2277 C CA  . ALA B 1 91  ? 1.242   47.786 -16.842 1.00 19.49 ? 69  ALA B CA  1 
ATOM   2278 C C   . ALA B 1 91  ? 2.736   47.695 -17.108 1.00 18.87 ? 69  ALA B C   1 
ATOM   2279 O O   . ALA B 1 91  ? 3.505   48.496 -16.572 1.00 17.99 ? 69  ALA B O   1 
ATOM   2280 C CB  . ALA B 1 91  ? 0.621   48.939 -17.639 1.00 16.95 ? 69  ALA B CB  1 
ATOM   2281 N N   . LYS B 1 92  ? 3.152   46.711 -17.902 1.00 17.79 ? 70  LYS B N   1 
ATOM   2282 C CA  . LYS B 1 92  ? 4.563   46.576 -18.253 1.00 18.40 ? 70  LYS B CA  1 
ATOM   2283 C C   . LYS B 1 92  ? 4.904   47.628 -19.301 1.00 20.84 ? 70  LYS B C   1 
ATOM   2284 O O   . LYS B 1 92  ? 4.420   47.553 -20.437 1.00 19.30 ? 70  LYS B O   1 
ATOM   2285 C CB  . LYS B 1 92  ? 4.849   45.180 -18.800 1.00 20.83 ? 70  LYS B CB  1 
ATOM   2286 C CG  . LYS B 1 92  ? 6.281   44.974 -19.275 1.00 22.35 ? 70  LYS B CG  1 
ATOM   2287 C CD  . LYS B 1 92  ? 6.727   43.575 -18.946 1.00 32.23 ? 70  LYS B CD  1 
ATOM   2288 C CE  . LYS B 1 92  ? 6.412   42.654 -20.127 1.00 38.19 ? 70  LYS B CE  1 
ATOM   2289 N NZ  . LYS B 1 92  ? 6.750   41.210 -19.893 1.00 54.54 ? 70  LYS B NZ  1 
ATOM   2290 N N   . TYR B 1 93  ? 5.770   48.588 -18.950 1.00 20.11 ? 71  TYR B N   1 
ATOM   2291 C CA  . TYR B 1 93  ? 6.205   49.594 -19.920 1.00 16.20 ? 71  TYR B CA  1 
ATOM   2292 C C   . TYR B 1 93  ? 7.592   49.242 -20.429 1.00 19.69 ? 71  TYR B C   1 
ATOM   2293 O O   . TYR B 1 93  ? 8.530   49.143 -19.621 1.00 21.64 ? 71  TYR B O   1 
ATOM   2294 C CB  . TYR B 1 93  ? 6.220   50.988 -19.294 1.00 21.12 ? 71  TYR B CB  1 
ATOM   2295 C CG  . TYR B 1 93  ? 4.922   51.740 -19.465 1.00 20.16 ? 71  TYR B CG  1 
ATOM   2296 C CD1 . TYR B 1 93  ? 3.818   51.442 -18.681 1.00 17.57 ? 71  TYR B CD1 1 
ATOM   2297 C CD2 . TYR B 1 93  ? 4.793   52.713 -20.455 1.00 17.74 ? 71  TYR B CD2 1 
ATOM   2298 C CE1 . TYR B 1 93  ? 2.613   52.117 -18.853 1.00 18.91 ? 71  TYR B CE1 1 
ATOM   2299 C CE2 . TYR B 1 93  ? 3.603   53.386 -20.645 1.00 18.50 ? 71  TYR B CE2 1 
ATOM   2300 C CZ  . TYR B 1 93  ? 2.519   53.094 -19.843 1.00 17.20 ? 71  TYR B CZ  1 
ATOM   2301 O OH  . TYR B 1 93  ? 1.337   53.769 -20.044 1.00 19.71 ? 71  TYR B OH  1 
ATOM   2302 N N   . PRO B 1 94  ? 7.787   49.053 -21.732 1.00 20.14 ? 72  PRO B N   1 
ATOM   2303 C CA  . PRO B 1 94  ? 9.150   48.979 -22.257 1.00 22.97 ? 72  PRO B CA  1 
ATOM   2304 C C   . PRO B 1 94  ? 9.860   50.311 -22.053 1.00 24.96 ? 72  PRO B C   1 
ATOM   2305 O O   . PRO B 1 94  ? 9.236   51.368 -21.898 1.00 27.69 ? 72  PRO B O   1 
ATOM   2306 C CB  . PRO B 1 94  ? 8.942   48.661 -23.745 1.00 28.40 ? 72  PRO B CB  1 
ATOM   2307 C CG  . PRO B 1 94  ? 7.612   49.254 -24.049 1.00 29.99 ? 72  PRO B CG  1 
ATOM   2308 C CD  . PRO B 1 94  ? 6.783   48.987 -22.808 1.00 26.96 ? 72  PRO B CD  1 
ATOM   2309 N N   . ASP B 1 95  ? 11.184  50.262 -22.060 1.00 23.35 ? 73  ASP B N   1 
ATOM   2310 C CA  . ASP B 1 95  ? 11.927  51.449 -21.663 1.00 24.42 ? 73  ASP B CA  1 
ATOM   2311 C C   . ASP B 1 95  ? 11.986  52.510 -22.760 1.00 27.56 ? 73  ASP B C   1 
ATOM   2312 O O   . ASP B 1 95  ? 12.544  53.580 -22.519 1.00 32.36 ? 73  ASP B O   1 
ATOM   2313 C CB  . ASP B 1 95  ? 13.333  51.060 -21.194 1.00 29.12 ? 73  ASP B CB  1 
ATOM   2314 C CG  . ASP B 1 95  ? 14.118  50.315 -22.244 1.00 40.62 ? 73  ASP B CG  1 
ATOM   2315 O OD1 . ASP B 1 95  ? 13.868  50.526 -23.451 1.00 31.94 ? 73  ASP B OD1 1 
ATOM   2316 O OD2 . ASP B 1 95  ? 15.009  49.524 -21.860 1.00 42.30 ? 73  ASP B OD2 1 
ATOM   2317 N N   . ASN B 1 96  ? 11.399  52.257 -23.935 1.00 27.02 ? 74  ASN B N   1 
ATOM   2318 C CA  . ASN B 1 96  ? 11.290  53.251 -25.001 1.00 27.38 ? 74  ASN B CA  1 
ATOM   2319 C C   . ASN B 1 96  ? 10.001  54.062 -24.922 1.00 29.19 ? 74  ASN B C   1 
ATOM   2320 O O   . ASN B 1 96  ? 9.724   54.857 -25.826 1.00 34.37 ? 74  ASN B O   1 
ATOM   2321 C CB  . ASN B 1 96  ? 11.379  52.575 -26.376 1.00 28.46 ? 74  ASN B CB  1 
ATOM   2322 C CG  . ASN B 1 96  ? 10.147  51.729 -26.698 1.00 28.07 ? 74  ASN B CG  1 
ATOM   2323 O OD1 . ASN B 1 96  ? 9.716   50.903 -25.895 1.00 34.77 ? 74  ASN B OD1 1 
ATOM   2324 N ND2 . ASN B 1 96  ? 9.582   51.931 -27.886 1.00 36.70 ? 74  ASN B ND2 1 
ATOM   2325 N N   . ILE B 1 97  ? 9.204   53.875 -23.876 1.00 23.84 ? 75  ILE B N   1 
ATOM   2326 C CA  . ILE B 1 97  ? 7.967   54.620 -23.677 1.00 24.94 ? 75  ILE B CA  1 
ATOM   2327 C C   . ILE B 1 97  ? 8.023   55.201 -22.273 1.00 21.88 ? 75  ILE B C   1 
ATOM   2328 O O   . ILE B 1 97  ? 8.303   54.472 -21.315 1.00 23.16 ? 75  ILE B O   1 
ATOM   2329 C CB  . ILE B 1 97  ? 6.735   53.710 -23.831 1.00 25.60 ? 75  ILE B CB  1 
ATOM   2330 C CG1 . ILE B 1 97  ? 6.692   53.085 -25.228 1.00 34.78 ? 75  ILE B CG1 1 
ATOM   2331 C CG2 . ILE B 1 97  ? 5.455   54.527 -23.605 1.00 22.62 ? 75  ILE B CG2 1 
ATOM   2332 C CD1 . ILE B 1 97  ? 5.484   52.165 -25.452 1.00 27.78 ? 75  ILE B CD1 1 
ATOM   2333 N N   . GLN B 1 98  ? 7.773   56.504 -22.143 1.00 20.74 ? 76  GLN B N   1 
ATOM   2334 C CA  . GLN B 1 98  ? 7.756   57.100 -20.815 1.00 19.22 ? 76  GLN B CA  1 
ATOM   2335 C C   . GLN B 1 98  ? 6.578   56.553 -20.019 1.00 19.96 ? 76  GLN B C   1 
ATOM   2336 O O   . GLN B 1 98  ? 5.467   56.438 -20.530 1.00 21.78 ? 76  GLN B O   1 
ATOM   2337 C CB  . GLN B 1 98  ? 7.691   58.626 -20.907 1.00 23.67 ? 76  GLN B CB  1 
ATOM   2338 C CG  . GLN B 1 98  ? 8.710   59.179 -21.890 1.00 39.01 ? 76  GLN B CG  1 
ATOM   2339 C CD  . GLN B 1 98  ? 8.890   60.691 -21.816 1.00 61.12 ? 76  GLN B CD  1 
ATOM   2340 O OE1 . GLN B 1 98  ? 7.957   61.457 -22.078 1.00 51.03 ? 76  GLN B OE1 1 
ATOM   2341 N NE2 . GLN B 1 98  ? 10.119  61.128 -21.523 1.00 60.76 ? 76  GLN B NE2 1 
ATOM   2342 N N   . ASP B 1 99  ? 6.835   56.223 -18.757 1.00 18.36 ? 77  ASP B N   1 
ATOM   2343 C CA  . ASP B 1 99  ? 5.871   55.556 -17.883 1.00 21.38 ? 77  ASP B CA  1 
ATOM   2344 C C   . ASP B 1 99  ? 5.352   56.616 -16.915 1.00 21.99 ? 77  ASP B C   1 
ATOM   2345 O O   . ASP B 1 99  ? 5.845   56.753 -15.797 1.00 23.46 ? 77  ASP B O   1 
ATOM   2346 C CB  . ASP B 1 99  ? 6.537   54.377 -17.175 1.00 19.35 ? 77  ASP B CB  1 
ATOM   2347 C CG  . ASP B 1 99  ? 5.563   53.535 -16.367 1.00 21.06 ? 77  ASP B CG  1 
ATOM   2348 O OD1 . ASP B 1 99  ? 4.448   54.007 -16.077 1.00 18.58 ? 77  ASP B OD1 1 
ATOM   2349 O OD2 . ASP B 1 99  ? 5.924   52.383 -16.037 1.00 18.05 ? 77  ASP B OD2 1 
ATOM   2350 N N   . TYR B 1 100 ? 4.332   57.357 -17.369 1.00 16.76 ? 78  TYR B N   1 
ATOM   2351 C CA  . TYR B 1 100 ? 3.714   58.433 -16.588 1.00 20.38 ? 78  TYR B CA  1 
ATOM   2352 C C   . TYR B 1 100 ? 3.262   57.961 -15.208 1.00 20.27 ? 78  TYR B C   1 
ATOM   2353 O O   . TYR B 1 100 ? 3.381   58.690 -14.214 1.00 20.45 ? 78  TYR B O   1 
ATOM   2354 C CB  . TYR B 1 100 ? 2.516   58.964 -17.372 1.00 16.30 ? 78  TYR B CB  1 
ATOM   2355 C CG  . TYR B 1 100 ? 1.852   60.222 -16.860 1.00 16.62 ? 78  TYR B CG  1 
ATOM   2356 C CD1 . TYR B 1 100 ? 2.443   61.478 -17.043 1.00 18.87 ? 78  TYR B CD1 1 
ATOM   2357 C CD2 . TYR B 1 100 ? 0.607   60.164 -16.237 1.00 16.87 ? 78  TYR B CD2 1 
ATOM   2358 C CE1 . TYR B 1 100 ? 1.820   62.636 -16.606 1.00 23.73 ? 78  TYR B CE1 1 
ATOM   2359 C CE2 . TYR B 1 100 ? -0.033  61.331 -15.803 1.00 18.90 ? 78  TYR B CE2 1 
ATOM   2360 C CZ  . TYR B 1 100 ? 0.583   62.554 -15.987 1.00 19.88 ? 78  TYR B CZ  1 
ATOM   2361 O OH  . TYR B 1 100 ? -0.033  63.705 -15.557 1.00 21.95 ? 78  TYR B OH  1 
ATOM   2362 N N   . PHE B 1 101 ? 2.745   56.739 -15.127 1.00 17.44 ? 79  PHE B N   1 
ATOM   2363 C CA  . PHE B 1 101 ? 2.087   56.291 -13.901 1.00 15.30 ? 79  PHE B CA  1 
ATOM   2364 C C   . PHE B 1 101 ? 3.096   55.915 -12.833 1.00 19.76 ? 79  PHE B C   1 
ATOM   2365 O O   . PHE B 1 101 ? 2.959   56.325 -11.673 1.00 20.00 ? 79  PHE B O   1 
ATOM   2366 C CB  . PHE B 1 101 ? 1.151   55.140 -14.247 1.00 20.84 ? 79  PHE B CB  1 
ATOM   2367 C CG  . PHE B 1 101 ? 0.229   55.480 -15.378 1.00 18.51 ? 79  PHE B CG  1 
ATOM   2368 C CD1 . PHE B 1 101 ? -0.866  56.308 -15.167 1.00 19.99 ? 79  PHE B CD1 1 
ATOM   2369 C CD2 . PHE B 1 101 ? 0.509   55.057 -16.669 1.00 15.21 ? 79  PHE B CD2 1 
ATOM   2370 C CE1 . PHE B 1 101 ? -1.700  56.671 -16.232 1.00 17.30 ? 79  PHE B CE1 1 
ATOM   2371 C CE2 . PHE B 1 101 ? -0.306  55.418 -17.735 1.00 15.12 ? 79  PHE B CE2 1 
ATOM   2372 C CZ  . PHE B 1 101 ? -1.421  56.225 -17.511 1.00 19.85 ? 79  PHE B CZ  1 
ATOM   2373 N N   . LYS B 1 102 ? 4.147   55.189 -13.208 1.00 18.98 ? 80  LYS B N   1 
ATOM   2374 C CA  . LYS B 1 102 ? 5.184   54.902 -12.230 1.00 22.50 ? 80  LYS B CA  1 
ATOM   2375 C C   . LYS B 1 102 ? 5.930   56.174 -11.831 1.00 23.26 ? 80  LYS B C   1 
ATOM   2376 O O   . LYS B 1 102 ? 6.344   56.304 -10.674 1.00 26.48 ? 80  LYS B O   1 
ATOM   2377 C CB  . LYS B 1 102 ? 6.117   53.818 -12.780 1.00 20.83 ? 80  LYS B CB  1 
ATOM   2378 C CG  . LYS B 1 102 ? 5.431   52.417 -12.756 1.00 22.16 ? 80  LYS B CG  1 
ATOM   2379 C CD  . LYS B 1 102 ? 6.394   51.254 -13.069 1.00 21.86 ? 80  LYS B CD  1 
ATOM   2380 C CE  . LYS B 1 102 ? 5.660   49.913 -13.263 1.00 18.98 ? 80  LYS B CE  1 
ATOM   2381 N NZ  . LYS B 1 102 ? 4.839   49.829 -14.559 1.00 15.26 ? 80  LYS B NZ  1 
ATOM   2382 N N   . GLN B 1 103 ? 6.076   57.142 -12.746 1.00 18.28 ? 81  GLN B N   1 
ATOM   2383 C CA  . GLN B 1 103 ? 6.690   58.408 -12.352 1.00 22.53 ? 81  GLN B CA  1 
ATOM   2384 C C   . GLN B 1 103 ? 5.774   59.299 -11.524 1.00 23.79 ? 81  GLN B C   1 
ATOM   2385 O O   . GLN B 1 103 ? 6.241   60.320 -11.008 1.00 25.36 ? 81  GLN B O   1 
ATOM   2386 C CB  . GLN B 1 103 ? 7.176   59.225 -13.555 1.00 24.10 ? 81  GLN B CB  1 
ATOM   2387 C CG  . GLN B 1 103 ? 7.757   58.452 -14.701 1.00 38.02 ? 81  GLN B CG  1 
ATOM   2388 C CD  . GLN B 1 103 ? 9.245   58.556 -14.766 1.00 53.21 ? 81  GLN B CD  1 
ATOM   2389 O OE1 . GLN B 1 103 ? 9.916   58.603 -13.733 1.00 61.99 ? 81  GLN B OE1 1 
ATOM   2390 N NE2 . GLN B 1 103 ? 9.786   58.598 -15.985 1.00 55.29 ? 81  GLN B NE2 1 
ATOM   2391 N N   . SER B 1 104 ? 4.493   58.969 -11.386 1.00 20.28 ? 82  SER B N   1 
ATOM   2392 C CA  A SER B 1 104 ? 3.597   59.803 -10.597 0.57 21.38 ? 82  SER B CA  1 
ATOM   2393 C CA  B SER B 1 104 ? 3.619   59.826 -10.590 0.43 21.39 ? 82  SER B CA  1 
ATOM   2394 C C   . SER B 1 104 ? 3.725   59.546 -9.099  1.00 26.88 ? 82  SER B C   1 
ATOM   2395 O O   . SER B 1 104 ? 3.119   60.277 -8.303  1.00 21.47 ? 82  SER B O   1 
ATOM   2396 C CB  A SER B 1 104 ? 2.156   59.573 -11.053 0.57 21.54 ? 82  SER B CB  1 
ATOM   2397 C CB  B SER B 1 104 ? 2.159   59.671 -11.012 0.43 21.48 ? 82  SER B CB  1 
ATOM   2398 O OG  A SER B 1 104 ? 1.941   60.153 -12.334 0.57 19.06 ? 82  SER B OG  1 
ATOM   2399 O OG  B SER B 1 104 ? 1.683   58.372 -10.718 0.43 19.73 ? 82  SER B OG  1 
ATOM   2400 N N   . PHE B 1 105 ? 4.481   58.539 -8.707  1.00 18.13 ? 83  PHE B N   1 
ATOM   2401 C CA  . PHE B 1 105 ? 4.540   58.227 -7.289  1.00 20.63 ? 83  PHE B CA  1 
ATOM   2402 C C   . PHE B 1 105 ? 5.864   58.673 -6.685  1.00 21.97 ? 83  PHE B C   1 
ATOM   2403 O O   . PHE B 1 105 ? 6.856   58.818 -7.398  1.00 25.21 ? 83  PHE B O   1 
ATOM   2404 C CB  . PHE B 1 105 ? 4.295   56.723 -7.093  1.00 24.25 ? 83  PHE B CB  1 
ATOM   2405 C CG  . PHE B 1 105 ? 2.863   56.358 -7.316  1.00 22.64 ? 83  PHE B CG  1 
ATOM   2406 C CD1 . PHE B 1 105 ? 2.394   56.039 -8.590  1.00 23.07 ? 83  PHE B CD1 1 
ATOM   2407 C CD2 . PHE B 1 105 ? 1.958   56.440 -6.274  1.00 18.82 ? 83  PHE B CD2 1 
ATOM   2408 C CE1 . PHE B 1 105 ? 1.050   55.755 -8.793  1.00 21.83 ? 83  PHE B CE1 1 
ATOM   2409 C CE2 . PHE B 1 105 ? 0.606   56.151 -6.479  1.00 18.75 ? 83  PHE B CE2 1 
ATOM   2410 C CZ  . PHE B 1 105 ? 0.158   55.814 -7.740  1.00 22.00 ? 83  PHE B CZ  1 
ATOM   2411 N N   . PRO B 1 106 ? 5.921   58.928 -5.372  1.00 25.65 ? 84  PRO B N   1 
ATOM   2412 C CA  . PRO B 1 106 ? 4.914   58.626 -4.331  1.00 20.46 ? 84  PRO B CA  1 
ATOM   2413 C C   . PRO B 1 106 ? 3.674   59.515 -4.261  1.00 25.52 ? 84  PRO B C   1 
ATOM   2414 O O   . PRO B 1 106 ? 2.722   59.091 -3.618  1.00 30.95 ? 84  PRO B O   1 
ATOM   2415 C CB  . PRO B 1 106 ? 5.740   58.757 -3.038  1.00 23.24 ? 84  PRO B CB  1 
ATOM   2416 C CG  . PRO B 1 106 ? 6.709   59.849 -3.367  1.00 25.09 ? 84  PRO B CG  1 
ATOM   2417 C CD  . PRO B 1 106 ? 7.134   59.523 -4.783  1.00 26.58 ? 84  PRO B CD  1 
ATOM   2418 N N   . LYS B 1 107 ? 3.599   60.705 -4.875  1.00 21.39 ? 85  LYS B N   1 
ATOM   2419 C CA  . LYS B 1 107 ? 2.420   61.547 -4.660  1.00 27.26 ? 85  LYS B CA  1 
ATOM   2420 C C   . LYS B 1 107 ? 1.165   60.928 -5.270  1.00 31.46 ? 85  LYS B C   1 
ATOM   2421 O O   . LYS B 1 107 ? 0.080   61.036 -4.686  1.00 32.58 ? 85  LYS B O   1 
ATOM   2422 C CB  . LYS B 1 107 ? 2.662   62.949 -5.216  1.00 24.89 ? 85  LYS B CB  1 
ATOM   2423 C CG  . LYS B 1 107 ? 3.514   63.827 -4.306  1.00 38.52 ? 85  LYS B CG  1 
ATOM   2424 C CD  . LYS B 1 107 ? 3.239   65.304 -4.503  1.00 44.90 ? 85  LYS B CD  1 
ATOM   2425 C CE  . LYS B 1 107 ? 3.946   66.142 -3.462  1.00 52.37 ? 85  LYS B CE  1 
ATOM   2426 N NZ  . LYS B 1 107 ? 5.413   66.207 -3.688  1.00 54.15 ? 85  LYS B NZ  1 
ATOM   2427 N N   . GLY B 1 108 ? 1.291   60.257 -6.411  1.00 20.82 ? 86  GLY B N   1 
ATOM   2428 C CA  . GLY B 1 108 ? 0.179   59.522 -7.005  1.00 24.37 ? 86  GLY B CA  1 
ATOM   2429 C C   . GLY B 1 108 ? -0.488  60.292 -8.130  1.00 18.72 ? 86  GLY B C   1 
ATOM   2430 O O   . GLY B 1 108 ? 0.009   61.310 -8.625  1.00 21.79 ? 86  GLY B O   1 
ATOM   2431 N N   . TYR B 1 109 ? -1.663  59.805 -8.513  1.00 22.45 ? 87  TYR B N   1 
ATOM   2432 C CA  . TYR B 1 109 ? -2.386  60.385 -9.636  1.00 18.73 ? 87  TYR B CA  1 
ATOM   2433 C C   . TYR B 1 109 ? -3.854  59.997 -9.521  1.00 20.01 ? 87  TYR B C   1 
ATOM   2434 O O   . TYR B 1 109 ? -4.249  59.213 -8.657  1.00 18.11 ? 87  TYR B O   1 
ATOM   2435 C CB  . TYR B 1 109 ? -1.785  59.933 -10.980 1.00 16.12 ? 87  TYR B CB  1 
ATOM   2436 C CG  . TYR B 1 109 ? -2.148  58.508 -11.361 1.00 15.27 ? 87  TYR B CG  1 
ATOM   2437 C CD1 . TYR B 1 109 ? -1.510  57.418 -10.766 1.00 19.14 ? 87  TYR B CD1 1 
ATOM   2438 C CD2 . TYR B 1 109 ? -3.159  58.254 -12.280 1.00 15.83 ? 87  TYR B CD2 1 
ATOM   2439 C CE1 . TYR B 1 109 ? -1.859  56.108 -11.100 1.00 18.93 ? 87  TYR B CE1 1 
ATOM   2440 C CE2 . TYR B 1 109 ? -3.516  56.945 -12.622 1.00 18.09 ? 87  TYR B CE2 1 
ATOM   2441 C CZ  . TYR B 1 109 ? -2.867  55.888 -12.029 1.00 19.28 ? 87  TYR B CZ  1 
ATOM   2442 O OH  . TYR B 1 109 ? -3.236  54.611 -12.370 1.00 16.59 ? 87  TYR B OH  1 
ATOM   2443 N N   . SER B 1 110 ? -4.667  60.554 -10.413 1.00 17.23 ? 88  SER B N   1 
ATOM   2444 C CA  A SER B 1 110 ? -6.072  60.186 -10.465 0.59 20.38 ? 88  SER B CA  1 
ATOM   2445 C CA  B SER B 1 110 ? -6.089  60.245 -10.462 0.41 20.38 ? 88  SER B CA  1 
ATOM   2446 C C   . SER B 1 110 ? -6.513  60.043 -11.913 1.00 18.13 ? 88  SER B C   1 
ATOM   2447 O O   . SER B 1 110 ? -5.893  60.574 -12.834 1.00 19.73 ? 88  SER B O   1 
ATOM   2448 C CB  A SER B 1 110 ? -6.938  61.214 -9.745  0.59 20.44 ? 88  SER B CB  1 
ATOM   2449 C CB  B SER B 1 110 ? -6.913  61.368 -9.826  0.41 20.64 ? 88  SER B CB  1 
ATOM   2450 O OG  A SER B 1 110 ? -6.850  62.465 -10.395 0.59 23.13 ? 88  SER B OG  1 
ATOM   2451 O OG  B SER B 1 110 ? -6.588  61.523 -8.454  0.41 23.66 ? 88  SER B OG  1 
ATOM   2452 N N   . TRP B 1 111 ? -7.600  59.300 -12.111 1.00 18.82 ? 89  TRP B N   1 
ATOM   2453 C CA  . TRP B 1 111 ? -8.186  59.190 -13.440 1.00 13.81 ? 89  TRP B CA  1 
ATOM   2454 C C   . TRP B 1 111 ? -9.697  59.346 -13.337 1.00 19.89 ? 89  TRP B C   1 
ATOM   2455 O O   . TRP B 1 111 ? -10.301 59.126 -12.277 1.00 18.64 ? 89  TRP B O   1 
ATOM   2456 C CB  . TRP B 1 111 ? -7.777  57.870 -14.147 1.00 13.79 ? 89  TRP B CB  1 
ATOM   2457 C CG  . TRP B 1 111 ? -8.130  56.571 -13.461 1.00 18.61 ? 89  TRP B CG  1 
ATOM   2458 C CD1 . TRP B 1 111 ? -7.262  55.727 -12.826 1.00 17.24 ? 89  TRP B CD1 1 
ATOM   2459 C CD2 . TRP B 1 111 ? -9.419  55.928 -13.414 1.00 17.21 ? 89  TRP B CD2 1 
ATOM   2460 N NE1 . TRP B 1 111 ? -7.932  54.632 -12.347 1.00 17.62 ? 89  TRP B NE1 1 
ATOM   2461 C CE2 . TRP B 1 111 ? -9.254  54.726 -12.694 1.00 19.41 ? 89  TRP B CE2 1 
ATOM   2462 C CE3 . TRP B 1 111 ? -10.701 56.269 -13.888 1.00 15.96 ? 89  TRP B CE3 1 
ATOM   2463 C CZ2 . TRP B 1 111 ? -10.309 53.854 -12.441 1.00 13.96 ? 89  TRP B CZ2 1 
ATOM   2464 C CZ3 . TRP B 1 111 ? -11.756 55.412 -13.624 1.00 15.65 ? 89  TRP B CZ3 1 
ATOM   2465 C CH2 . TRP B 1 111 ? -11.555 54.217 -12.899 1.00 17.45 ? 89  TRP B CH2 1 
ATOM   2466 N N   . GLU B 1 112 ? -10.300 59.785 -14.441 1.00 18.24 ? 90  GLU B N   1 
ATOM   2467 C CA  . GLU B 1 112 ? -11.749 59.842 -14.602 1.00 17.04 ? 90  GLU B CA  1 
ATOM   2468 C C   . GLU B 1 112 ? -12.102 59.205 -15.931 1.00 20.55 ? 90  GLU B C   1 
ATOM   2469 O O   . GLU B 1 112 ? -11.412 59.428 -16.927 1.00 18.11 ? 90  GLU B O   1 
ATOM   2470 C CB  . GLU B 1 112 ? -12.318 61.275 -14.563 1.00 23.54 ? 90  GLU B CB  1 
ATOM   2471 C CG  . GLU B 1 112 ? -11.742 62.114 -13.450 1.00 34.47 ? 90  GLU B CG  1 
ATOM   2472 C CD  . GLU B 1 112 ? -12.425 63.467 -13.307 1.00 50.69 ? 90  GLU B CD  1 
ATOM   2473 O OE1 . GLU B 1 112 ? -13.378 63.753 -14.065 1.00 43.51 ? 90  GLU B OE1 1 
ATOM   2474 O OE2 . GLU B 1 112 ? -12.015 64.230 -12.409 1.00 53.79 ? 90  GLU B OE2 1 
ATOM   2475 N N   . ARG B 1 113 ? -13.189 58.434 -15.947 1.00 16.54 ? 91  ARG B N   1 
ATOM   2476 C CA  . ARG B 1 113 ? -13.523 57.587 -17.084 1.00 18.87 ? 91  ARG B CA  1 
ATOM   2477 C C   . ARG B 1 113 ? -14.998 57.716 -17.418 1.00 19.37 ? 91  ARG B C   1 
ATOM   2478 O O   . ARG B 1 113 ? -15.842 57.720 -16.519 1.00 18.77 ? 91  ARG B O   1 
ATOM   2479 C CB  . ARG B 1 113 ? -13.222 56.111 -16.786 1.00 12.86 ? 91  ARG B CB  1 
ATOM   2480 C CG  . ARG B 1 113 ? -13.398 55.196 -18.002 1.00 14.37 ? 91  ARG B CG  1 
ATOM   2481 C CD  . ARG B 1 113 ? -12.906 53.781 -17.655 1.00 17.04 ? 91  ARG B CD  1 
ATOM   2482 N NE  . ARG B 1 113 ? -11.490 53.836 -17.308 1.00 14.72 ? 91  ARG B NE  1 
ATOM   2483 C CZ  . ARG B 1 113 ? -10.866 52.986 -16.502 1.00 19.20 ? 91  ARG B CZ  1 
ATOM   2484 N NH1 . ARG B 1 113 ? -11.486 51.934 -15.990 1.00 16.45 ? 91  ARG B NH1 1 
ATOM   2485 N NH2 . ARG B 1 113 ? -9.588  53.206 -16.196 1.00 16.61 ? 91  ARG B NH2 1 
ATOM   2486 N N   . SER B 1 114 ? -15.306 57.813 -18.711 1.00 15.79 ? 92  SER B N   1 
ATOM   2487 C CA  . SER B 1 114 ? -16.663 57.594 -19.190 1.00 18.33 ? 92  SER B CA  1 
ATOM   2488 C C   . SER B 1 114 ? -16.755 56.227 -19.861 1.00 16.27 ? 92  SER B C   1 
ATOM   2489 O O   . SER B 1 114 ? -15.857 55.825 -20.607 1.00 18.12 ? 92  SER B O   1 
ATOM   2490 C CB  . SER B 1 114 ? -17.101 58.699 -20.159 1.00 18.58 ? 92  SER B CB  1 
ATOM   2491 O OG  . SER B 1 114 ? -16.225 58.797 -21.273 1.00 22.05 ? 92  SER B OG  1 
ATOM   2492 N N   . LEU B 1 115 ? -17.847 55.520 -19.587 1.00 15.72 ? 93  LEU B N   1 
ATOM   2493 C CA  . LEU B 1 115 ? -18.146 54.213 -20.164 1.00 18.14 ? 93  LEU B CA  1 
ATOM   2494 C C   . LEU B 1 115 ? -19.456 54.393 -20.929 1.00 19.76 ? 93  LEU B C   1 
ATOM   2495 O O   . LEU B 1 115 ? -20.528 54.490 -20.319 1.00 21.22 ? 93  LEU B O   1 
ATOM   2496 C CB  . LEU B 1 115 ? -18.278 53.140 -19.088 1.00 18.62 ? 93  LEU B CB  1 
ATOM   2497 C CG  . LEU B 1 115 ? -17.040 52.800 -18.248 1.00 18.26 ? 93  LEU B CG  1 
ATOM   2498 C CD1 . LEU B 1 115 ? -16.858 53.806 -17.106 1.00 16.44 ? 93  LEU B CD1 1 
ATOM   2499 C CD2 . LEU B 1 115 ? -17.139 51.373 -17.687 1.00 20.03 ? 93  LEU B CD2 1 
ATOM   2500 N N   . THR B 1 116 ? -19.377 54.456 -22.249 1.00 17.27 ? 94  THR B N   1 
ATOM   2501 C CA  . THR B 1 116 ? -20.533 54.761 -23.093 1.00 18.73 ? 94  THR B CA  1 
ATOM   2502 C C   . THR B 1 116 ? -20.971 53.471 -23.775 1.00 14.76 ? 94  THR B C   1 
ATOM   2503 O O   . THR B 1 116 ? -20.390 53.070 -24.788 1.00 18.54 ? 94  THR B O   1 
ATOM   2504 C CB  . THR B 1 116 ? -20.194 55.855 -24.108 1.00 21.68 ? 94  THR B CB  1 
ATOM   2505 O OG1 . THR B 1 116 ? -19.804 57.049 -23.412 1.00 20.17 ? 94  THR B OG1 1 
ATOM   2506 C CG2 . THR B 1 116 ? -21.386 56.165 -25.008 1.00 29.32 ? 94  THR B CG2 1 
ATOM   2507 N N   . PHE B 1 117 ? -21.989 52.815 -23.211 1.00 18.12 ? 95  PHE B N   1 
ATOM   2508 C CA  . PHE B 1 117 ? -22.436 51.539 -23.752 1.00 19.00 ? 95  PHE B CA  1 
ATOM   2509 C C   . PHE B 1 117 ? -23.338 51.749 -24.964 1.00 25.29 ? 95  PHE B C   1 
ATOM   2510 O O   . PHE B 1 117 ? -24.039 52.763 -25.088 1.00 24.13 ? 95  PHE B O   1 
ATOM   2511 C CB  . PHE B 1 117 ? -23.168 50.716 -22.701 1.00 17.27 ? 95  PHE B CB  1 
ATOM   2512 C CG  . PHE B 1 117 ? -22.281 50.245 -21.581 1.00 19.71 ? 95  PHE B CG  1 
ATOM   2513 C CD1 . PHE B 1 117 ? -22.050 51.057 -20.483 1.00 16.93 ? 95  PHE B CD1 1 
ATOM   2514 C CD2 . PHE B 1 117 ? -21.684 48.991 -21.631 1.00 18.94 ? 95  PHE B CD2 1 
ATOM   2515 C CE1 . PHE B 1 117 ? -21.231 50.635 -19.442 1.00 18.81 ? 95  PHE B CE1 1 
ATOM   2516 C CE2 . PHE B 1 117 ? -20.865 48.553 -20.593 1.00 18.26 ? 95  PHE B CE2 1 
ATOM   2517 C CZ  . PHE B 1 117 ? -20.643 49.368 -19.497 1.00 17.37 ? 95  PHE B CZ  1 
ATOM   2518 N N   . GLU B 1 118 ? -23.316 50.762 -25.862 1.00 19.55 ? 96  GLU B N   1 
ATOM   2519 C CA  . GLU B 1 118 ? -23.940 50.939 -27.165 1.00 18.04 ? 96  GLU B CA  1 
ATOM   2520 C C   . GLU B 1 118 ? -25.454 51.095 -27.071 1.00 25.16 ? 96  GLU B C   1 
ATOM   2521 O O   . GLU B 1 118 ? -26.061 51.628 -28.004 1.00 23.32 ? 96  GLU B O   1 
ATOM   2522 C CB  . GLU B 1 118 ? -23.610 49.756 -28.075 1.00 23.32 ? 96  GLU B CB  1 
ATOM   2523 C CG  . GLU B 1 118 ? -24.296 48.471 -27.662 1.00 26.86 ? 96  GLU B CG  1 
ATOM   2524 C CD  . GLU B 1 118 ? -24.008 47.321 -28.610 1.00 34.32 ? 96  GLU B CD  1 
ATOM   2525 O OE1 . GLU B 1 118 ? -23.198 47.490 -29.544 1.00 32.84 ? 96  GLU B OE1 1 
ATOM   2526 O OE2 . GLU B 1 118 ? -24.671 46.276 -28.466 1.00 37.65 ? 96  GLU B OE2 1 
ATOM   2527 N N   . ASP B 1 119 ? -26.079 50.637 -25.987 1.00 20.22 ? 97  ASP B N   1 
ATOM   2528 C CA  . ASP B 1 119 ? -27.533 50.682 -25.880 1.00 21.93 ? 97  ASP B CA  1 
ATOM   2529 C C   . ASP B 1 119 ? -28.042 51.877 -25.075 1.00 24.24 ? 97  ASP B C   1 
ATOM   2530 O O   . ASP B 1 119 ? -29.233 51.932 -24.752 1.00 24.94 ? 97  ASP B O   1 
ATOM   2531 C CB  . ASP B 1 119 ? -28.073 49.368 -25.288 1.00 21.63 ? 97  ASP B CB  1 
ATOM   2532 C CG  . ASP B 1 119 ? -27.591 49.099 -23.853 1.00 24.09 ? 97  ASP B CG  1 
ATOM   2533 O OD1 . ASP B 1 119 ? -26.706 49.822 -23.336 1.00 25.25 ? 97  ASP B OD1 1 
ATOM   2534 O OD2 . ASP B 1 119 ? -28.117 48.144 -23.241 1.00 27.10 ? 97  ASP B OD2 1 
ATOM   2535 N N   . GLY B 1 120 ? -27.184 52.835 -24.755 1.00 22.94 ? 98  GLY B N   1 
ATOM   2536 C CA  . GLY B 1 120 ? -27.590 53.989 -23.986 1.00 27.61 ? 98  GLY B CA  1 
ATOM   2537 C C   . GLY B 1 120 ? -27.179 53.964 -22.526 1.00 25.07 ? 98  GLY B C   1 
ATOM   2538 O O   . GLY B 1 120 ? -27.219 55.015 -21.872 1.00 25.05 ? 98  GLY B O   1 
ATOM   2539 N N   . GLY B 1 121 ? -26.799 52.806 -21.993 1.00 21.04 ? 99  GLY B N   1 
ATOM   2540 C CA  . GLY B 1 121 ? -26.218 52.786 -20.659 1.00 20.75 ? 99  GLY B CA  1 
ATOM   2541 C C   . GLY B 1 121 ? -24.974 53.657 -20.603 1.00 20.86 ? 99  GLY B C   1 
ATOM   2542 O O   . GLY B 1 121 ? -24.147 53.651 -21.516 1.00 21.91 ? 99  GLY B O   1 
ATOM   2543 N N   . ILE B 1 122 ? -24.852 54.436 -19.531 1.00 22.91 ? 100 ILE B N   1 
ATOM   2544 C CA  . ILE B 1 122 ? -23.734 55.370 -19.371 1.00 21.90 ? 100 ILE B CA  1 
ATOM   2545 C C   . ILE B 1 122 ? -23.207 55.289 -17.942 1.00 25.82 ? 100 ILE B C   1 
ATOM   2546 O O   . ILE B 1 122 ? -23.980 55.356 -16.980 1.00 22.67 ? 100 ILE B O   1 
ATOM   2547 C CB  . ILE B 1 122 ? -24.144 56.816 -19.750 1.00 29.01 ? 100 ILE B CB  1 
ATOM   2548 C CG1 . ILE B 1 122 ? -22.976 57.791 -19.606 1.00 32.79 ? 100 ILE B CG1 1 
ATOM   2549 C CG2 . ILE B 1 122 ? -25.369 57.296 -18.988 1.00 32.92 ? 100 ILE B CG2 1 
ATOM   2550 C CD1 . ILE B 1 122 ? -22.162 57.963 -20.878 1.00 44.25 ? 100 ILE B CD1 1 
ATOM   2551 N N   . CYS B 1 123 ? -21.887 55.143 -17.801 1.00 19.49 ? 101 CYS B N   1 
ATOM   2552 C CA  . CYS B 1 123 ? -21.243 55.174 -16.500 1.00 19.80 ? 101 CYS B CA  1 
ATOM   2553 C C   . CYS B 1 123 ? -20.133 56.217 -16.480 1.00 25.85 ? 101 CYS B C   1 
ATOM   2554 O O   . CYS B 1 123 ? -19.539 56.546 -17.509 1.00 21.47 ? 101 CYS B O   1 
ATOM   2555 C CB  . CYS B 1 123 ? -20.669 53.804 -16.112 1.00 20.01 ? 101 CYS B CB  1 
ATOM   2556 S SG  . CYS B 1 123 ? -21.912 52.475 -16.018 1.00 21.82 ? 101 CYS B SG  1 
ATOM   2557 N N   . ASN B 1 124 ? -19.875 56.750 -15.293 1.00 21.37 ? 102 ASN B N   1 
ATOM   2558 C CA  . ASN B 1 124 ? -18.711 57.588 -15.034 1.00 16.46 ? 102 ASN B CA  1 
ATOM   2559 C C   . ASN B 1 124 ? -18.017 57.046 -13.801 1.00 19.49 ? 102 ASN B C   1 
ATOM   2560 O O   . ASN B 1 124 ? -18.678 56.740 -12.806 1.00 21.56 ? 102 ASN B O   1 
ATOM   2561 C CB  . ASN B 1 124 ? -19.089 59.065 -14.843 1.00 21.99 ? 102 ASN B CB  1 
ATOM   2562 C CG  . ASN B 1 124 ? -19.972 59.584 -15.959 1.00 42.63 ? 102 ASN B CG  1 
ATOM   2563 O OD1 . ASN B 1 124 ? -19.477 59.978 -17.023 1.00 42.19 ? 102 ASN B OD1 1 
ATOM   2564 N ND2 . ASN B 1 124 ? -21.285 59.583 -15.733 1.00 49.44 ? 102 ASN B ND2 1 
ATOM   2565 N N   . ALA B 1 125 ? -16.695 56.898 -13.874 1.00 18.89 ? 103 ALA B N   1 
ATOM   2566 C CA  . ALA B 1 125 ? -15.936 56.384 -12.745 1.00 18.80 ? 103 ALA B CA  1 
ATOM   2567 C C   . ALA B 1 125 ? -14.718 57.263 -12.518 1.00 22.42 ? 103 ALA B C   1 
ATOM   2568 O O   . ALA B 1 125 ? -14.254 57.974 -13.418 1.00 18.70 ? 103 ALA B O   1 
ATOM   2569 C CB  . ALA B 1 125 ? -15.517 54.920 -12.963 1.00 19.49 ? 103 ALA B CB  1 
ATOM   2570 N N   . ARG B 1 126 ? -14.219 57.226 -11.285 1.00 17.11 ? 104 ARG B N   1 
ATOM   2571 C CA  . ARG B 1 126 ? -13.035 57.987 -10.931 1.00 16.91 ? 104 ARG B CA  1 
ATOM   2572 C C   . ARG B 1 126 ? -12.284 57.222 -9.854  1.00 18.45 ? 104 ARG B C   1 
ATOM   2573 O O   . ARG B 1 126 ? -12.892 56.585 -8.993  1.00 20.17 ? 104 ARG B O   1 
ATOM   2574 C CB  . ARG B 1 126 ? -13.407 59.401 -10.448 1.00 21.80 ? 104 ARG B CB  1 
ATOM   2575 C CG  . ARG B 1 126 ? -12.230 60.191 -9.909  1.00 38.32 ? 104 ARG B CG  1 
ATOM   2576 C CD  . ARG B 1 126 ? -12.643 61.556 -9.367  1.00 38.64 ? 104 ARG B CD  1 
ATOM   2577 N NE  . ARG B 1 126 ? -11.531 62.205 -8.681  1.00 41.96 ? 104 ARG B NE  1 
ATOM   2578 C CZ  . ARG B 1 126 ? -10.878 63.263 -9.144  1.00 50.76 ? 104 ARG B CZ  1 
ATOM   2579 N NH1 . ARG B 1 126 ? -11.184 63.805 -10.312 1.00 55.99 ? 104 ARG B NH1 1 
ATOM   2580 N NH2 . ARG B 1 126 ? -9.898  63.793 -8.414  1.00 47.10 ? 104 ARG B NH2 1 
ATOM   2581 N N   . ASN B 1 127 ? -10.960 57.297 -9.905  1.00 18.42 ? 105 ASN B N   1 
ATOM   2582 C CA  . ASN B 1 127 ? -10.092 56.710 -8.887  1.00 17.42 ? 105 ASN B CA  1 
ATOM   2583 C C   . ASN B 1 127 ? -9.045  57.743 -8.507  1.00 20.44 ? 105 ASN B C   1 
ATOM   2584 O O   . ASN B 1 127 ? -8.396  58.312 -9.385  1.00 18.77 ? 105 ASN B O   1 
ATOM   2585 C CB  . ASN B 1 127 ? -9.415  55.425 -9.402  1.00 16.19 ? 105 ASN B CB  1 
ATOM   2586 C CG  . ASN B 1 127 ? -8.723  54.633 -8.302  1.00 18.34 ? 105 ASN B CG  1 
ATOM   2587 O OD1 . ASN B 1 127 ? -8.737  55.018 -7.133  1.00 18.08 ? 105 ASN B OD1 1 
ATOM   2588 N ND2 . ASN B 1 127 ? -8.114  53.514 -8.676  1.00 18.27 ? 105 ASN B ND2 1 
ATOM   2589 N N   . ASP B 1 128 ? -8.910  58.011 -7.210  1.00 18.02 ? 106 ASP B N   1 
ATOM   2590 C CA  . ASP B 1 128 ? -7.803  58.796 -6.671  1.00 18.78 ? 106 ASP B CA  1 
ATOM   2591 C C   . ASP B 1 128 ? -6.852  57.826 -5.982  1.00 21.37 ? 106 ASP B C   1 
ATOM   2592 O O   . ASP B 1 128 ? -7.262  57.103 -5.063  1.00 16.52 ? 106 ASP B O   1 
ATOM   2593 C CB  . ASP B 1 128 ? -8.292  59.853 -5.680  1.00 17.44 ? 106 ASP B CB  1 
ATOM   2594 C CG  . ASP B 1 128 ? -9.159  60.906 -6.329  1.00 33.81 ? 106 ASP B CG  1 
ATOM   2595 O OD1 . ASP B 1 128 ? -8.616  61.769 -7.055  1.00 40.51 ? 106 ASP B OD1 1 
ATOM   2596 O OD2 . ASP B 1 128 ? -10.392 60.875 -6.101  1.00 35.56 ? 106 ASP B OD2 1 
ATOM   2597 N N   . ILE B 1 129 ? -5.599  57.794 -6.431  1.00 18.03 ? 107 ILE B N   1 
ATOM   2598 C CA  . ILE B 1 129 ? -4.653  56.752 -6.045  1.00 18.14 ? 107 ILE B CA  1 
ATOM   2599 C C   . ILE B 1 129 ? -3.500  57.392 -5.285  1.00 22.90 ? 107 ILE B C   1 
ATOM   2600 O O   . ILE B 1 129 ? -2.889  58.350 -5.773  1.00 20.03 ? 107 ILE B O   1 
ATOM   2601 C CB  . ILE B 1 129 ? -4.130  55.980 -7.271  1.00 18.75 ? 107 ILE B CB  1 
ATOM   2602 C CG1 . ILE B 1 129 ? -5.298  55.457 -8.109  1.00 20.20 ? 107 ILE B CG1 1 
ATOM   2603 C CG2 . ILE B 1 129 ? -3.209  54.835 -6.833  1.00 19.90 ? 107 ILE B CG2 1 
ATOM   2604 C CD1 . ILE B 1 129 ? -4.854  54.633 -9.317  1.00 18.00 ? 107 ILE B CD1 1 
ATOM   2605 N N   . THR B 1 130 ? -3.205  56.857 -4.098  1.00 22.05 ? 108 THR B N   1 
ATOM   2606 C CA  . THR B 1 130 ? -2.084  57.291 -3.269  1.00 20.84 ? 108 THR B CA  1 
ATOM   2607 C C   . THR B 1 130 ? -1.263  56.065 -2.857  1.00 21.60 ? 108 THR B C   1 
ATOM   2608 O O   . THR B 1 130 ? -1.595  54.930 -3.197  1.00 21.53 ? 108 THR B O   1 
ATOM   2609 C CB  . THR B 1 130 ? -2.581  58.075 -2.047  1.00 25.71 ? 108 THR B CB  1 
ATOM   2610 O OG1 . THR B 1 130 ? -3.453  57.248 -1.268  1.00 24.14 ? 108 THR B OG1 1 
ATOM   2611 C CG2 . THR B 1 130 ? -3.343  59.339 -2.493  1.00 23.75 ? 108 THR B CG2 1 
ATOM   2612 N N   . MET B 1 131 ? -0.189  56.291 -2.099  1.00 24.18 ? 109 MET B N   1 
ATOM   2613 C CA  . MET B 1 131 ? 0.782   55.232 -1.843  1.00 23.36 ? 109 MET B CA  1 
ATOM   2614 C C   . MET B 1 131 ? 1.451   55.455 -0.491  1.00 23.93 ? 109 MET B C   1 
ATOM   2615 O O   . MET B 1 131 ? 1.833   56.576 -0.162  1.00 22.18 ? 109 MET B O   1 
ATOM   2616 C CB  . MET B 1 131 ? 1.806   55.192 -2.994  1.00 25.23 ? 109 MET B CB  1 
ATOM   2617 C CG  . MET B 1 131 ? 2.566   53.894 -3.231  1.00 28.73 ? 109 MET B CG  1 
ATOM   2618 S SD  . MET B 1 131 ? 4.321   54.062 -3.709  1.00 26.84 ? 109 MET B SD  1 
ATOM   2619 C CE  . MET B 1 131 ? 5.053   55.098 -2.426  1.00 24.40 ? 109 MET B CE  1 
ATOM   2620 N N   . GLU B 1 132 ? 1.566   54.385 0.300   1.00 22.09 ? 110 GLU B N   1 
ATOM   2621 C CA  . GLU B 1 132 ? 2.386   54.387 1.511   1.00 24.08 ? 110 GLU B CA  1 
ATOM   2622 C C   . GLU B 1 132 ? 3.235   53.127 1.468   1.00 28.29 ? 110 GLU B C   1 
ATOM   2623 O O   . GLU B 1 132 ? 2.696   52.021 1.542   1.00 23.18 ? 110 GLU B O   1 
ATOM   2624 C CB  . GLU B 1 132 ? 1.549   54.414 2.795   1.00 28.37 ? 110 GLU B CB  1 
ATOM   2625 C CG  . GLU B 1 132 ? 0.712   55.679 3.015   1.00 23.26 ? 110 GLU B CG  1 
ATOM   2626 C CD  . GLU B 1 132 ? 1.533   56.961 3.017   1.00 29.04 ? 110 GLU B CD  1 
ATOM   2627 O OE1 . GLU B 1 132 ? 2.682   56.931 3.483   1.00 25.43 ? 110 GLU B OE1 1 
ATOM   2628 O OE2 . GLU B 1 132 ? 1.014   58.002 2.554   1.00 27.69 ? 110 GLU B OE2 1 
ATOM   2629 N N   . GLY B 1 133 ? 4.551   53.293 1.346   1.00 25.34 ? 111 GLY B N   1 
ATOM   2630 C CA  . GLY B 1 133 ? 5.430   52.134 1.325   1.00 22.98 ? 111 GLY B CA  1 
ATOM   2631 C C   . GLY B 1 133 ? 5.034   51.196 0.198   1.00 25.83 ? 111 GLY B C   1 
ATOM   2632 O O   . GLY B 1 133 ? 5.003   51.574 -0.979  1.00 24.29 ? 111 GLY B O   1 
ATOM   2633 N N   . ASP B 1 134 ? 4.687   49.965 0.559   1.00 25.54 ? 112 ASP B N   1 
ATOM   2634 C CA  . ASP B 1 134 ? 4.434   48.901 -0.404  1.00 29.59 ? 112 ASP B CA  1 
ATOM   2635 C C   . ASP B 1 134 ? 2.994   48.869 -0.906  1.00 27.41 ? 112 ASP B C   1 
ATOM   2636 O O   . ASP B 1 134 ? 2.636   47.946 -1.641  1.00 22.21 ? 112 ASP B O   1 
ATOM   2637 C CB  . ASP B 1 134 ? 4.806   47.555 0.234   1.00 30.75 ? 112 ASP B CB  1 
ATOM   2638 C CG  . ASP B 1 134 ? 3.903   47.187 1.408   1.00 35.71 ? 112 ASP B CG  1 
ATOM   2639 O OD1 . ASP B 1 134 ? 3.062   48.016 1.827   1.00 29.77 ? 112 ASP B OD1 1 
ATOM   2640 O OD2 . ASP B 1 134 ? 4.090   46.093 1.980   1.00 34.31 ? 112 ASP B OD2 1 
ATOM   2641 N N   . THR B 1 135 ? 2.164   49.850 -0.543  1.00 22.59 ? 113 THR B N   1 
ATOM   2642 C CA  . THR B 1 135 ? 0.714   49.723 -0.686  1.00 20.73 ? 113 THR B CA  1 
ATOM   2643 C C   . THR B 1 135 ? 0.124   50.888 -1.467  1.00 21.59 ? 113 THR B C   1 
ATOM   2644 O O   . THR B 1 135 ? 0.417   52.049 -1.162  1.00 22.27 ? 113 THR B O   1 
ATOM   2645 C CB  . THR B 1 135 ? 0.044   49.638 0.698   1.00 22.07 ? 113 THR B CB  1 
ATOM   2646 O OG1 . THR B 1 135 ? 0.493   48.463 1.382   1.00 24.30 ? 113 THR B OG1 1 
ATOM   2647 C CG2 . THR B 1 135 ? -1.461  49.553 0.556   1.00 23.82 ? 113 THR B CG2 1 
ATOM   2648 N N   . PHE B 1 136 ? -0.704  50.580 -2.479  1.00 21.01 ? 114 PHE B N   1 
ATOM   2649 C CA  . PHE B 1 136 ? -1.529  51.590 -3.134  1.00 20.89 ? 114 PHE B CA  1 
ATOM   2650 C C   . PHE B 1 136 ? -2.892  51.649 -2.462  1.00 19.01 ? 114 PHE B C   1 
ATOM   2651 O O   . PHE B 1 136 ? -3.466  50.617 -2.126  1.00 20.61 ? 114 PHE B O   1 
ATOM   2652 C CB  . PHE B 1 136 ? -1.736  51.290 -4.624  1.00 19.91 ? 114 PHE B CB  1 
ATOM   2653 C CG  . PHE B 1 136 ? -0.472  51.364 -5.449  1.00 23.29 ? 114 PHE B CG  1 
ATOM   2654 C CD1 . PHE B 1 136 ? 0.159   52.576 -5.675  1.00 23.77 ? 114 PHE B CD1 1 
ATOM   2655 C CD2 . PHE B 1 136 ? 0.073   50.220 -5.998  1.00 18.54 ? 114 PHE B CD2 1 
ATOM   2656 C CE1 . PHE B 1 136 ? 1.325   52.644 -6.430  1.00 21.01 ? 114 PHE B CE1 1 
ATOM   2657 C CE2 . PHE B 1 136 ? 1.229   50.283 -6.766  1.00 19.84 ? 114 PHE B CE2 1 
ATOM   2658 C CZ  . PHE B 1 136 ? 1.858   51.495 -6.968  1.00 20.66 ? 114 PHE B CZ  1 
ATOM   2659 N N   . TYR B 1 137 ? -3.418  52.864 -2.295  1.00 20.00 ? 115 TYR B N   1 
ATOM   2660 C CA  . TYR B 1 137 ? -4.753  53.096 -1.750  1.00 22.63 ? 115 TYR B CA  1 
ATOM   2661 C C   . TYR B 1 137 ? -5.609  53.723 -2.837  1.00 22.91 ? 115 TYR B C   1 
ATOM   2662 O O   . TYR B 1 137 ? -5.147  54.620 -3.543  1.00 20.68 ? 115 TYR B O   1 
ATOM   2663 C CB  . TYR B 1 137 ? -4.692  54.014 -0.525  1.00 19.89 ? 115 TYR B CB  1 
ATOM   2664 C CG  . TYR B 1 137 ? -3.860  53.410 0.582   1.00 19.59 ? 115 TYR B CG  1 
ATOM   2665 C CD1 . TYR B 1 137 ? -4.428  52.560 1.523   1.00 21.22 ? 115 TYR B CD1 1 
ATOM   2666 C CD2 . TYR B 1 137 ? -2.477  53.602 0.617   1.00 22.67 ? 115 TYR B CD2 1 
ATOM   2667 C CE1 . TYR B 1 137 ? -3.647  51.975 2.524   1.00 22.08 ? 115 TYR B CE1 1 
ATOM   2668 C CE2 . TYR B 1 137 ? -1.699  53.019 1.606   1.00 21.58 ? 115 TYR B CE2 1 
ATOM   2669 C CZ  . TYR B 1 137 ? -2.286  52.211 2.548   1.00 23.46 ? 115 TYR B CZ  1 
ATOM   2670 O OH  . TYR B 1 137 ? -1.505  51.634 3.529   1.00 26.79 ? 115 TYR B OH  1 
ATOM   2671 N N   . ASN B 1 138 ? -6.853  53.254 -2.972  1.00 22.29 ? 116 ASN B N   1 
ATOM   2672 C CA  . ASN B 1 138 ? -7.702  53.603 -4.113  1.00 19.16 ? 116 ASN B CA  1 
ATOM   2673 C C   . ASN B 1 138 ? -9.073  54.036 -3.626  1.00 22.29 ? 116 ASN B C   1 
ATOM   2674 O O   . ASN B 1 138 ? -9.800  53.237 -3.027  1.00 23.97 ? 116 ASN B O   1 
ATOM   2675 C CB  . ASN B 1 138 ? -7.862  52.416 -5.071  1.00 16.58 ? 116 ASN B CB  1 
ATOM   2676 C CG  . ASN B 1 138 ? -6.552  51.938 -5.627  1.00 22.31 ? 116 ASN B CG  1 
ATOM   2677 O OD1 . ASN B 1 138 ? -6.238  52.182 -6.781  1.00 17.65 ? 116 ASN B OD1 1 
ATOM   2678 N ND2 . ASN B 1 138 ? -5.774  51.255 -4.806  1.00 17.75 ? 116 ASN B ND2 1 
ATOM   2679 N N   . LYS B 1 139 ? -9.431  55.287 -3.902  1.00 15.79 ? 117 LYS B N   1 
ATOM   2680 C CA  . LYS B 1 139 ? -10.740 55.834 -3.568  1.00 15.35 ? 117 LYS B CA  1 
ATOM   2681 C C   . LYS B 1 139 ? -11.515 55.913 -4.878  1.00 23.56 ? 117 LYS B C   1 
ATOM   2682 O O   . LYS B 1 139 ? -11.263 56.793 -5.705  1.00 18.92 ? 117 LYS B O   1 
ATOM   2683 C CB  . LYS B 1 139 ? -10.601 57.200 -2.893  1.00 19.78 ? 117 LYS B CB  1 
ATOM   2684 C CG  . LYS B 1 139 ? -11.911 57.958 -2.673  1.00 28.47 ? 117 LYS B CG  1 
ATOM   2685 C CD  . LYS B 1 139 ? -11.641 59.457 -2.396  1.00 30.81 ? 117 LYS B CD  1 
ATOM   2686 C CE  . LYS B 1 139 ? -12.930 60.255 -2.271  1.00 35.09 ? 117 LYS B CE  1 
ATOM   2687 N NZ  . LYS B 1 139 ? -12.666 61.699 -1.963  1.00 44.79 ? 117 LYS B NZ  1 
ATOM   2688 N N   . VAL B 1 140 ? -12.448 54.983 -5.071  1.00 16.76 ? 118 VAL B N   1 
ATOM   2689 C CA  . VAL B 1 140 ? -13.147 54.812 -6.346  1.00 17.22 ? 118 VAL B CA  1 
ATOM   2690 C C   . VAL B 1 140 ? -14.595 55.250 -6.197  1.00 19.52 ? 118 VAL B C   1 
ATOM   2691 O O   . VAL B 1 140 ? -15.240 54.943 -5.188  1.00 18.84 ? 118 VAL B O   1 
ATOM   2692 C CB  . VAL B 1 140 ? -13.078 53.346 -6.822  1.00 19.56 ? 118 VAL B CB  1 
ATOM   2693 C CG1 . VAL B 1 140 ? -13.740 53.187 -8.187  1.00 17.01 ? 118 VAL B CG1 1 
ATOM   2694 C CG2 . VAL B 1 140 ? -11.629 52.861 -6.881  1.00 18.41 ? 118 VAL B CG2 1 
ATOM   2695 N N   . ARG B 1 141 ? -15.102 55.977 -7.200  1.00 18.18 ? 119 ARG B N   1 
ATOM   2696 C CA  . ARG B 1 141 ? -16.519 56.301 -7.296  1.00 17.38 ? 119 ARG B CA  1 
ATOM   2697 C C   . ARG B 1 141 ? -17.023 55.822 -8.643  1.00 23.53 ? 119 ARG B C   1 
ATOM   2698 O O   . ARG B 1 141 ? -16.317 55.929 -9.650  1.00 23.17 ? 119 ARG B O   1 
ATOM   2699 C CB  . ARG B 1 141 ? -16.777 57.802 -7.141  1.00 21.81 ? 119 ARG B CB  1 
ATOM   2700 C CG  . ARG B 1 141 ? -16.245 58.410 -5.856  1.00 30.17 ? 119 ARG B CG  1 
ATOM   2701 C CD  . ARG B 1 141 ? -17.047 57.909 -4.660  1.00 32.61 ? 119 ARG B CD  1 
ATOM   2702 N NE  . ARG B 1 141 ? -16.531 58.388 -3.380  1.00 42.06 ? 119 ARG B NE  1 
ATOM   2703 C CZ  . ARG B 1 141 ? -15.860 57.646 -2.509  1.00 43.17 ? 119 ARG B CZ  1 
ATOM   2704 N NH1 . ARG B 1 141 ? -15.474 56.412 -2.803  1.00 31.65 ? 119 ARG B NH1 1 
ATOM   2705 N NH2 . ARG B 1 141 ? -15.550 58.161 -1.319  1.00 36.33 ? 119 ARG B NH2 1 
ATOM   2706 N N   . PHE B 1 142 ? -18.231 55.272 -8.661  1.00 20.42 ? 120 PHE B N   1 
ATOM   2707 C CA  . PHE B 1 142 ? -18.760 54.657 -9.874  1.00 17.37 ? 120 PHE B CA  1 
ATOM   2708 C C   . PHE B 1 142 ? -20.240 54.987 -9.980  1.00 20.09 ? 120 PHE B C   1 
ATOM   2709 O O   . PHE B 1 142 ? -21.016 54.638 -9.085  1.00 24.81 ? 120 PHE B O   1 
ATOM   2710 C CB  . PHE B 1 142 ? -18.531 53.136 -9.861  1.00 18.62 ? 120 PHE B CB  1 
ATOM   2711 C CG  . PHE B 1 142 ? -18.817 52.468 -11.185 1.00 20.32 ? 120 PHE B CG  1 
ATOM   2712 C CD1 . PHE B 1 142 ? -20.128 52.261 -11.610 1.00 20.63 ? 120 PHE B CD1 1 
ATOM   2713 C CD2 . PHE B 1 142 ? -17.780 52.041 -12.000 1.00 20.33 ? 120 PHE B CD2 1 
ATOM   2714 C CE1 . PHE B 1 142 ? -20.397 51.645 -12.827 1.00 19.02 ? 120 PHE B CE1 1 
ATOM   2715 C CE2 . PHE B 1 142 ? -18.037 51.425 -13.210 1.00 17.20 ? 120 PHE B CE2 1 
ATOM   2716 C CZ  . PHE B 1 142 ? -19.349 51.225 -13.630 1.00 18.98 ? 120 PHE B CZ  1 
ATOM   2717 N N   . TYR B 1 143 ? -20.636 55.666 -11.061 1.00 18.75 ? 121 TYR B N   1 
ATOM   2718 C CA  . TYR B 1 143 ? -22.027 56.054 -11.258 1.00 20.30 ? 121 TYR B CA  1 
ATOM   2719 C C   . TYR B 1 143 ? -22.505 55.533 -12.601 1.00 26.59 ? 121 TYR B C   1 
ATOM   2720 O O   . TYR B 1 143 ? -21.821 55.694 -13.612 1.00 23.64 ? 121 TYR B O   1 
ATOM   2721 C CB  . TYR B 1 143 ? -22.210 57.575 -11.195 1.00 25.58 ? 121 TYR B CB  1 
ATOM   2722 C CG  . TYR B 1 143 ? -23.580 58.038 -11.664 1.00 36.82 ? 121 TYR B CG  1 
ATOM   2723 C CD1 . TYR B 1 143 ? -23.757 58.582 -12.940 1.00 44.22 ? 121 TYR B CD1 1 
ATOM   2724 C CD2 . TYR B 1 143 ? -24.694 57.938 -10.836 1.00 44.61 ? 121 TYR B CD2 1 
ATOM   2725 C CE1 . TYR B 1 143 ? -25.001 59.009 -13.374 1.00 41.42 ? 121 TYR B CE1 1 
ATOM   2726 C CE2 . TYR B 1 143 ? -25.946 58.363 -11.262 1.00 47.49 ? 121 TYR B CE2 1 
ATOM   2727 C CZ  . TYR B 1 143 ? -26.092 58.896 -12.534 1.00 40.71 ? 121 TYR B CZ  1 
ATOM   2728 O OH  . TYR B 1 143 ? -27.329 59.323 -12.973 1.00 62.58 ? 121 TYR B OH  1 
ATOM   2729 N N   . GLY B 1 144 ? -23.673 54.914 -12.615 1.00 21.96 ? 122 GLY B N   1 
ATOM   2730 C CA  . GLY B 1 144 ? -24.195 54.406 -13.868 1.00 20.98 ? 122 GLY B CA  1 
ATOM   2731 C C   . GLY B 1 144 ? -25.685 54.611 -13.967 1.00 23.52 ? 122 GLY B C   1 
ATOM   2732 O O   . GLY B 1 144 ? -26.385 54.526 -12.951 1.00 23.00 ? 122 GLY B O   1 
ATOM   2733 N N   . THR B 1 145 ? -26.186 54.892 -15.169 1.00 23.63 ? 123 THR B N   1 
ATOM   2734 C CA  . THR B 1 145 ? -27.609 55.119 -15.341 1.00 26.06 ? 123 THR B CA  1 
ATOM   2735 C C   . THR B 1 145 ? -28.014 54.740 -16.757 1.00 23.66 ? 123 THR B C   1 
ATOM   2736 O O   . THR B 1 145 ? -27.171 54.458 -17.613 1.00 22.62 ? 123 THR B O   1 
ATOM   2737 C CB  . THR B 1 145 ? -27.973 56.572 -15.046 1.00 26.79 ? 123 THR B CB  1 
ATOM   2738 O OG1 . THR B 1 145 ? -29.389 56.673 -14.960 1.00 28.12 ? 123 THR B OG1 1 
ATOM   2739 C CG2 . THR B 1 145 ? -27.483 57.484 -16.148 1.00 29.68 ? 123 THR B CG2 1 
ATOM   2740 N N   . ASN B 1 146 ? -29.331 54.735 -16.984 1.00 26.08 ? 124 ASN B N   1 
ATOM   2741 C CA  . ASN B 1 146 ? -29.935 54.475 -18.293 1.00 27.73 ? 124 ASN B CA  1 
ATOM   2742 C C   . ASN B 1 146 ? -29.662 53.077 -18.823 1.00 26.71 ? 124 ASN B C   1 
ATOM   2743 O O   . ASN B 1 146 ? -29.754 52.858 -20.028 1.00 27.22 ? 124 ASN B O   1 
ATOM   2744 C CB  . ASN B 1 146 ? -29.506 55.513 -19.340 1.00 21.83 ? 124 ASN B CB  1 
ATOM   2745 C CG  . ASN B 1 146 ? -29.873 56.942 -18.946 1.00 44.09 ? 124 ASN B CG  1 
ATOM   2746 O OD1 . ASN B 1 146 ? -29.650 57.877 -19.713 1.00 55.87 ? 124 ASN B OD1 1 
ATOM   2747 N ND2 . ASN B 1 146 ? -30.531 57.102 -17.799 1.00 48.85 ? 124 ASN B ND2 1 
ATOM   2748 N N   . PHE B 1 147 ? -29.375 52.109 -17.963 1.00 23.95 ? 125 PHE B N   1 
ATOM   2749 C CA  . PHE B 1 147 ? -29.345 50.733 -18.442 1.00 24.69 ? 125 PHE B CA  1 
ATOM   2750 C C   . PHE B 1 147 ? -30.767 50.212 -18.627 1.00 25.48 ? 125 PHE B C   1 
ATOM   2751 O O   . PHE B 1 147 ? -31.583 50.311 -17.703 1.00 28.76 ? 125 PHE B O   1 
ATOM   2752 C CB  . PHE B 1 147 ? -28.581 49.844 -17.473 1.00 25.30 ? 125 PHE B CB  1 
ATOM   2753 C CG  . PHE B 1 147 ? -27.095 50.041 -17.523 1.00 19.06 ? 125 PHE B CG  1 
ATOM   2754 C CD1 . PHE B 1 147 ? -26.372 49.649 -18.645 1.00 19.87 ? 125 PHE B CD1 1 
ATOM   2755 C CD2 . PHE B 1 147 ? -26.412 50.596 -16.445 1.00 24.83 ? 125 PHE B CD2 1 
ATOM   2756 C CE1 . PHE B 1 147 ? -24.993 49.818 -18.697 1.00 20.45 ? 125 PHE B CE1 1 
ATOM   2757 C CE2 . PHE B 1 147 ? -25.024 50.766 -16.494 1.00 21.70 ? 125 PHE B CE2 1 
ATOM   2758 C CZ  . PHE B 1 147 ? -24.319 50.378 -17.621 1.00 21.62 ? 125 PHE B CZ  1 
ATOM   2759 N N   . PRO B 1 148 ? -31.103 49.669 -19.800 1.00 27.70 ? 126 PRO B N   1 
ATOM   2760 C CA  . PRO B 1 148 ? -32.448 49.108 -19.994 1.00 29.42 ? 126 PRO B CA  1 
ATOM   2761 C C   . PRO B 1 148 ? -32.678 47.930 -19.061 1.00 29.33 ? 126 PRO B C   1 
ATOM   2762 O O   . PRO B 1 148 ? -31.797 47.090 -18.870 1.00 31.60 ? 126 PRO B O   1 
ATOM   2763 C CB  . PRO B 1 148 ? -32.463 48.668 -21.463 1.00 31.60 ? 126 PRO B CB  1 
ATOM   2764 C CG  . PRO B 1 148 ? -31.161 49.077 -22.065 1.00 33.40 ? 126 PRO B CG  1 
ATOM   2765 C CD  . PRO B 1 148 ? -30.268 49.659 -21.015 1.00 26.18 ? 126 PRO B CD  1 
ATOM   2766 N N   . ALA B 1 149 ? -33.884 47.870 -18.491 1.00 32.02 ? 127 ALA B N   1 
ATOM   2767 C CA  . ALA B 1 149 ? -34.217 46.824 -17.525 1.00 27.39 ? 127 ALA B CA  1 
ATOM   2768 C C   . ALA B 1 149 ? -34.033 45.424 -18.106 1.00 41.40 ? 127 ALA B C   1 
ATOM   2769 O O   . ALA B 1 149 ? -33.643 44.498 -17.387 1.00 37.29 ? 127 ALA B O   1 
ATOM   2770 C CB  . ALA B 1 149 ? -35.659 47.007 -17.032 1.00 31.48 ? 127 ALA B CB  1 
ATOM   2771 N N   . ASN B 1 150 ? -34.295 45.244 -19.397 1.00 33.02 ? 128 ASN B N   1 
ATOM   2772 C CA  . ASN B 1 150 ? -34.187 43.940 -20.035 1.00 30.71 ? 128 ASN B CA  1 
ATOM   2773 C C   . ASN B 1 150 ? -32.861 43.733 -20.771 1.00 38.26 ? 128 ASN B C   1 
ATOM   2774 O O   . ASN B 1 150 ? -32.706 42.726 -21.468 1.00 34.54 ? 128 ASN B O   1 
ATOM   2775 C CB  . ASN B 1 150 ? -35.392 43.723 -20.966 1.00 38.26 ? 128 ASN B CB  1 
ATOM   2776 C CG  . ASN B 1 150 ? -35.171 44.273 -22.376 1.00 50.99 ? 128 ASN B CG  1 
ATOM   2777 O OD1 . ASN B 1 150 ? -34.349 45.171 -22.587 1.00 45.81 ? 128 ASN B OD1 1 
ATOM   2778 N ND2 . ASN B 1 150 ? -35.934 43.752 -23.346 1.00 45.83 ? 128 ASN B ND2 1 
ATOM   2779 N N   . GLY B 1 151 ? -31.893 44.648 -20.611 1.00 30.56 ? 129 GLY B N   1 
ATOM   2780 C CA  . GLY B 1 151 ? -30.605 44.537 -21.272 1.00 31.34 ? 129 GLY B CA  1 
ATOM   2781 C C   . GLY B 1 151 ? -29.663 43.610 -20.539 1.00 30.36 ? 129 GLY B C   1 
ATOM   2782 O O   . GLY B 1 151 ? -29.942 43.122 -19.432 1.00 29.16 ? 129 GLY B O   1 
ATOM   2783 N N   . PRO B 1 152 ? -28.498 43.358 -21.156 1.00 27.74 ? 130 PRO B N   1 
ATOM   2784 C CA  . PRO B 1 152 ? -27.566 42.379 -20.576 1.00 29.98 ? 130 PRO B CA  1 
ATOM   2785 C C   . PRO B 1 152 ? -26.990 42.791 -19.230 1.00 28.09 ? 130 PRO B C   1 
ATOM   2786 O O   . PRO B 1 152 ? -26.601 41.915 -18.450 1.00 31.02 ? 130 PRO B O   1 
ATOM   2787 C CB  . PRO B 1 152 ? -26.467 42.270 -21.646 1.00 29.42 ? 130 PRO B CB  1 
ATOM   2788 C CG  . PRO B 1 152 ? -26.517 43.571 -22.367 1.00 24.97 ? 130 PRO B CG  1 
ATOM   2789 C CD  . PRO B 1 152 ? -27.984 43.916 -22.419 1.00 23.78 ? 130 PRO B CD  1 
ATOM   2790 N N   . VAL B 1 153 ? -26.895 44.089 -18.940 1.00 25.86 ? 131 VAL B N   1 
ATOM   2791 C CA  . VAL B 1 153 ? -26.336 44.522 -17.660 1.00 20.66 ? 131 VAL B CA  1 
ATOM   2792 C C   . VAL B 1 153 ? -27.325 44.259 -16.524 1.00 24.15 ? 131 VAL B C   1 
ATOM   2793 O O   . VAL B 1 153 ? -27.006 43.565 -15.550 1.00 28.66 ? 131 VAL B O   1 
ATOM   2794 C CB  . VAL B 1 153 ? -25.923 46.005 -17.735 1.00 22.53 ? 131 VAL B CB  1 
ATOM   2795 C CG1 . VAL B 1 153 ? -25.594 46.548 -16.327 1.00 21.53 ? 131 VAL B CG1 1 
ATOM   2796 C CG2 . VAL B 1 153 ? -24.746 46.183 -18.687 1.00 19.69 ? 131 VAL B CG2 1 
ATOM   2797 N N   . MET B 1 154 ? -28.554 44.773 -16.644 1.00 23.96 ? 132 MET B N   1 
ATOM   2798 C CA  . MET B 1 154 ? -29.546 44.562 -15.592 1.00 29.13 ? 132 MET B CA  1 
ATOM   2799 C C   . MET B 1 154 ? -30.030 43.117 -15.518 1.00 35.97 ? 132 MET B C   1 
ATOM   2800 O O   . MET B 1 154 ? -30.519 42.697 -14.465 1.00 34.86 ? 132 MET B O   1 
ATOM   2801 C CB  . MET B 1 154 ? -30.731 45.513 -15.782 1.00 31.84 ? 132 MET B CB  1 
ATOM   2802 C CG  . MET B 1 154 ? -30.401 46.995 -15.648 1.00 31.31 ? 132 MET B CG  1 
ATOM   2803 S SD  . MET B 1 154 ? -29.256 47.392 -14.295 1.00 34.80 ? 132 MET B SD  1 
ATOM   2804 C CE  . MET B 1 154 ? -30.347 47.134 -12.905 1.00 33.57 ? 132 MET B CE  1 
ATOM   2805 N N   . GLN B 1 155 ? -29.905 42.348 -16.596 1.00 29.54 ? 133 GLN B N   1 
ATOM   2806 C CA  . GLN B 1 155 ? -30.285 40.941 -16.591 1.00 31.98 ? 133 GLN B CA  1 
ATOM   2807 C C   . GLN B 1 155 ? -29.107 40.014 -16.315 1.00 38.14 ? 133 GLN B C   1 
ATOM   2808 O O   . GLN B 1 155 ? -29.281 38.791 -16.333 1.00 31.66 ? 133 GLN B O   1 
ATOM   2809 C CB  . GLN B 1 155 ? -30.942 40.580 -17.927 1.00 33.19 ? 133 GLN B CB  1 
ATOM   2810 C CG  . GLN B 1 155 ? -32.382 41.088 -18.090 1.00 40.53 ? 133 GLN B CG  1 
ATOM   2811 C CD  . GLN B 1 155 ? -33.249 40.927 -16.838 1.00 51.19 ? 133 GLN B CD  1 
ATOM   2812 O OE1 . GLN B 1 155 ? -33.376 39.828 -16.304 1.00 45.46 ? 133 GLN B OE1 1 
ATOM   2813 N NE2 . GLN B 1 155 ? -33.863 42.018 -16.384 1.00 42.20 ? 133 GLN B NE2 1 
ATOM   2814 N N   . LYS B 1 156 ? -27.919 40.568 -16.072 1.00 31.39 ? 134 LYS B N   1 
ATOM   2815 C CA  . LYS B 1 156 ? -26.734 39.807 -15.663 1.00 32.22 ? 134 LYS B CA  1 
ATOM   2816 C C   . LYS B 1 156 ? -26.400 38.707 -16.674 1.00 33.72 ? 134 LYS B C   1 
ATOM   2817 O O   . LYS B 1 156 ? -26.280 37.523 -16.342 1.00 29.67 ? 134 LYS B O   1 
ATOM   2818 C CB  . LYS B 1 156 ? -26.916 39.229 -14.258 1.00 39.47 ? 134 LYS B CB  1 
ATOM   2819 C CG  . LYS B 1 156 ? -26.848 40.260 -13.144 1.00 36.57 ? 134 LYS B CG  1 
ATOM   2820 C CD  . LYS B 1 156 ? -27.532 39.732 -11.884 1.00 38.92 ? 134 LYS B CD  1 
ATOM   2821 C CE  . LYS B 1 156 ? -26.498 39.211 -10.912 1.00 47.64 ? 134 LYS B CE  1 
ATOM   2822 N NZ  . LYS B 1 156 ? -27.033 38.213 -9.918  1.00 44.49 ? 134 LYS B NZ  1 
ATOM   2823 N N   . LYS B 1 157 ? -26.240 39.128 -17.927 1.00 31.94 ? 135 LYS B N   1 
ATOM   2824 C CA  . LYS B 1 157 ? -26.010 38.213 -19.037 1.00 32.88 ? 135 LYS B CA  1 
ATOM   2825 C C   . LYS B 1 157 ? -24.595 38.309 -19.599 1.00 30.02 ? 135 LYS B C   1 
ATOM   2826 O O   . LYS B 1 157 ? -24.329 37.754 -20.669 1.00 33.10 ? 135 LYS B O   1 
ATOM   2827 C CB  . LYS B 1 157 ? -27.036 38.472 -20.142 1.00 34.47 ? 135 LYS B CB  1 
ATOM   2828 C CG  . LYS B 1 157 ? -28.486 38.144 -19.766 1.00 38.65 ? 135 LYS B CG  1 
ATOM   2829 C CD  . LYS B 1 157 ? -28.658 36.678 -19.377 1.00 41.08 ? 135 LYS B CD  1 
ATOM   2830 C CE  . LYS B 1 157 ? -29.988 36.451 -18.655 1.00 53.07 ? 135 LYS B CE  1 
ATOM   2831 N NZ  . LYS B 1 157 ? -29.989 35.218 -17.811 1.00 62.12 ? 135 LYS B NZ  1 
ATOM   2832 N N   . THR B 1 158 ? -23.684 38.992 -18.912 1.00 25.36 ? 136 THR B N   1 
ATOM   2833 C CA  . THR B 1 158 ? -22.325 39.163 -19.413 1.00 24.22 ? 136 THR B CA  1 
ATOM   2834 C C   . THR B 1 158 ? -21.434 38.008 -18.958 1.00 27.76 ? 136 THR B C   1 
ATOM   2835 O O   . THR B 1 158 ? -21.646 37.407 -17.902 1.00 23.70 ? 136 THR B O   1 
ATOM   2836 C CB  . THR B 1 158 ? -21.727 40.493 -18.942 1.00 22.66 ? 136 THR B CB  1 
ATOM   2837 O OG1 . THR B 1 158 ? -21.506 40.447 -17.530 1.00 21.65 ? 136 THR B OG1 1 
ATOM   2838 C CG2 . THR B 1 158 ? -22.675 41.647 -19.254 1.00 21.69 ? 136 THR B CG2 1 
ATOM   2839 N N   . LEU B 1 159 ? -20.432 37.697 -19.774 1.00 23.93 ? 137 LEU B N   1 
ATOM   2840 C CA  . LEU B 1 159 ? -19.475 36.644 -19.456 1.00 24.39 ? 137 LEU B CA  1 
ATOM   2841 C C   . LEU B 1 159 ? -18.075 37.171 -19.175 1.00 22.20 ? 137 LEU B C   1 
ATOM   2842 O O   . LEU B 1 159 ? -17.444 36.725 -18.210 1.00 22.91 ? 137 LEU B O   1 
ATOM   2843 C CB  . LEU B 1 159 ? -19.405 35.631 -20.603 1.00 19.89 ? 137 LEU B CB  1 
ATOM   2844 C CG  . LEU B 1 159 ? -20.613 34.726 -20.857 1.00 22.08 ? 137 LEU B CG  1 
ATOM   2845 C CD1 . LEU B 1 159 ? -20.295 33.742 -21.967 1.00 26.65 ? 137 LEU B CD1 1 
ATOM   2846 C CD2 . LEU B 1 159 ? -21.036 34.001 -19.582 1.00 26.57 ? 137 LEU B CD2 1 
ATOM   2847 N N   . LYS B 1 160 ? -17.580 38.116 -19.975 1.00 20.45 ? 138 LYS B N   1 
ATOM   2848 C CA  . LYS B 1 160 ? -16.242 38.677 -19.785 1.00 18.07 ? 138 LYS B CA  1 
ATOM   2849 C C   . LYS B 1 160 ? -16.046 39.857 -20.726 1.00 24.83 ? 138 LYS B C   1 
ATOM   2850 O O   . LYS B 1 160 ? -16.744 39.996 -21.736 1.00 21.95 ? 138 LYS B O   1 
ATOM   2851 C CB  . LYS B 1 160 ? -15.136 37.645 -20.039 1.00 24.78 ? 138 LYS B CB  1 
ATOM   2852 C CG  . LYS B 1 160 ? -15.003 37.207 -21.486 1.00 23.60 ? 138 LYS B CG  1 
ATOM   2853 C CD  . LYS B 1 160 ? -13.626 36.570 -21.758 1.00 32.99 ? 138 LYS B CD  1 
ATOM   2854 C CE  . LYS B 1 160 ? -13.336 36.520 -23.260 1.00 39.18 ? 138 LYS B CE  1 
ATOM   2855 N NZ  . LYS B 1 160 ? -12.244 35.575 -23.628 1.00 46.33 ? 138 LYS B NZ  1 
ATOM   2856 N N   . TRP B 1 161 ? -15.075 40.703 -20.383 1.00 15.80 ? 139 TRP B N   1 
ATOM   2857 C CA  . TRP B 1 161 ? -14.571 41.692 -21.319 1.00 14.06 ? 139 TRP B CA  1 
ATOM   2858 C C   . TRP B 1 161 ? -13.597 41.006 -22.271 1.00 14.82 ? 139 TRP B C   1 
ATOM   2859 O O   . TRP B 1 161 ? -12.748 40.232 -21.831 1.00 17.69 ? 139 TRP B O   1 
ATOM   2860 C CB  . TRP B 1 161 ? -13.845 42.823 -20.580 1.00 20.10 ? 139 TRP B CB  1 
ATOM   2861 C CG  . TRP B 1 161 ? -14.707 43.751 -19.766 1.00 21.39 ? 139 TRP B CG  1 
ATOM   2862 C CD1 . TRP B 1 161 ? -14.838 43.769 -18.398 1.00 19.37 ? 139 TRP B CD1 1 
ATOM   2863 C CD2 . TRP B 1 161 ? -15.516 44.829 -20.262 1.00 18.81 ? 139 TRP B CD2 1 
ATOM   2864 N NE1 . TRP B 1 161 ? -15.694 44.787 -18.016 1.00 19.26 ? 139 TRP B NE1 1 
ATOM   2865 C CE2 . TRP B 1 161 ? -16.130 45.444 -19.143 1.00 16.39 ? 139 TRP B CE2 1 
ATOM   2866 C CE3 . TRP B 1 161 ? -15.800 45.317 -21.545 1.00 14.06 ? 139 TRP B CE3 1 
ATOM   2867 C CZ2 . TRP B 1 161 ? -17.003 46.536 -19.268 1.00 20.11 ? 139 TRP B CZ2 1 
ATOM   2868 C CZ3 . TRP B 1 161 ? -16.676 46.408 -21.674 1.00 18.05 ? 139 TRP B CZ3 1 
ATOM   2869 C CH2 . TRP B 1 161 ? -17.251 47.014 -20.539 1.00 14.49 ? 139 TRP B CH2 1 
ATOM   2870 N N   . GLU B 1 162 ? -13.703 41.298 -23.562 1.00 16.90 ? 140 GLU B N   1 
ATOM   2871 C CA  . GLU B 1 162 ? -12.706 40.827 -24.510 1.00 20.76 ? 140 GLU B CA  1 
ATOM   2872 C C   . GLU B 1 162 ? -11.383 41.557 -24.292 1.00 18.46 ? 140 GLU B C   1 
ATOM   2873 O O   . GLU B 1 162 ? -11.369 42.708 -23.849 1.00 17.89 ? 140 GLU B O   1 
ATOM   2874 C CB  . GLU B 1 162 ? -13.184 41.051 -25.942 1.00 18.59 ? 140 GLU B CB  1 
ATOM   2875 C CG  . GLU B 1 162 ? -14.429 40.217 -26.288 1.00 24.15 ? 140 GLU B CG  1 
ATOM   2876 C CD  . GLU B 1 162 ? -14.118 38.730 -26.429 1.00 26.68 ? 140 GLU B CD  1 
ATOM   2877 O OE1 . GLU B 1 162 ? -12.939 38.339 -26.253 1.00 25.36 ? 140 GLU B OE1 1 
ATOM   2878 O OE2 . GLU B 1 162 ? -15.063 37.946 -26.678 1.00 25.18 ? 140 GLU B OE2 1 
ATOM   2879 N N   . PRO B 1 163 ? -10.252 40.920 -24.608 1.00 20.47 ? 141 PRO B N   1 
ATOM   2880 C CA  . PRO B 1 163 ? -8.975  41.646 -24.560 1.00 17.40 ? 141 PRO B CA  1 
ATOM   2881 C C   . PRO B 1 163 ? -9.027  42.905 -25.425 1.00 21.77 ? 141 PRO B C   1 
ATOM   2882 O O   . PRO B 1 163 ? -9.699  42.944 -26.457 1.00 21.54 ? 141 PRO B O   1 
ATOM   2883 C CB  . PRO B 1 163 ? -7.960  40.628 -25.095 1.00 20.03 ? 141 PRO B CB  1 
ATOM   2884 C CG  . PRO B 1 163 ? -8.602  39.299 -24.895 1.00 26.89 ? 141 PRO B CG  1 
ATOM   2885 C CD  . PRO B 1 163 ? -10.085 39.505 -24.982 1.00 22.10 ? 141 PRO B CD  1 
ATOM   2886 N N   . SER B 1 164 ? -8.338  43.961 -24.974 1.00 19.42 ? 142 SER B N   1 
ATOM   2887 C CA  . SER B 1 164 ? -8.489  45.286 -25.576 1.00 16.15 ? 142 SER B CA  1 
ATOM   2888 C C   . SER B 1 164 ? -7.128  45.930 -25.782 1.00 16.38 ? 142 SER B C   1 
ATOM   2889 O O   . SER B 1 164 ? -6.113  45.465 -25.260 1.00 18.57 ? 142 SER B O   1 
ATOM   2890 C CB  . SER B 1 164 ? -9.352  46.205 -24.708 1.00 17.72 ? 142 SER B CB  1 
ATOM   2891 O OG  . SER B 1 164 ? -8.625  46.577 -23.528 1.00 17.80 ? 142 SER B OG  1 
ATOM   2892 N N   . THR B 1 165 ? -7.123  47.030 -26.545 1.00 15.80 ? 143 THR B N   1 
ATOM   2893 C CA  . THR B 1 165 ? -5.946  47.879 -26.702 1.00 15.42 ? 143 THR B CA  1 
ATOM   2894 C C   . THR B 1 165 ? -6.349  49.321 -26.430 1.00 18.70 ? 143 THR B C   1 
ATOM   2895 O O   . THR B 1 165 ? -7.200  49.879 -27.134 1.00 18.24 ? 143 THR B O   1 
ATOM   2896 C CB  . THR B 1 165 ? -5.321  47.750 -28.098 1.00 18.91 ? 143 THR B CB  1 
ATOM   2897 O OG1 . THR B 1 165 ? -4.879  46.402 -28.316 1.00 27.42 ? 143 THR B OG1 1 
ATOM   2898 C CG2 . THR B 1 165 ? -4.141  48.709 -28.234 1.00 19.72 ? 143 THR B CG2 1 
ATOM   2899 N N   . GLU B 1 166 ? -5.750  49.915 -25.406 1.00 13.50 ? 144 GLU B N   1 
ATOM   2900 C CA  . GLU B 1 166 ? -6.024  51.293 -25.024 1.00 13.59 ? 144 GLU B CA  1 
ATOM   2901 C C   . GLU B 1 166 ? -5.106  52.215 -25.812 1.00 15.32 ? 144 GLU B C   1 
ATOM   2902 O O   . GLU B 1 166 ? -3.890  52.030 -25.809 1.00 16.32 ? 144 GLU B O   1 
ATOM   2903 C CB  . GLU B 1 166 ? -5.810  51.486 -23.516 1.00 14.90 ? 144 GLU B CB  1 
ATOM   2904 C CG  . GLU B 1 166 ? -6.093  52.913 -23.018 1.00 14.68 ? 144 GLU B CG  1 
ATOM   2905 C CD  . GLU B 1 166 ? -6.061  53.012 -21.505 1.00 14.53 ? 144 GLU B CD  1 
ATOM   2906 O OE1 . GLU B 1 166 ? -5.501  52.096 -20.866 1.00 18.63 ? 144 GLU B OE1 1 
ATOM   2907 O OE2 . GLU B 1 166 ? -6.624  53.999 -20.955 1.00 17.88 ? 144 GLU B OE2 1 
ATOM   2908 N N   . LYS B 1 167 ? -5.687  53.190 -26.503 1.00 15.05 ? 145 LYS B N   1 
ATOM   2909 C CA  . LYS B 1 167 ? -4.902  54.152 -27.271 1.00 18.03 ? 145 LYS B CA  1 
ATOM   2910 C C   . LYS B 1 167 ? -4.585  55.333 -26.359 1.00 18.53 ? 145 LYS B C   1 
ATOM   2911 O O   . LYS B 1 167 ? -5.495  56.048 -25.919 1.00 17.67 ? 145 LYS B O   1 
ATOM   2912 C CB  . LYS B 1 167 ? -5.661  54.576 -28.526 1.00 17.64 ? 145 LYS B CB  1 
ATOM   2913 C CG  . LYS B 1 167 ? -5.120  55.832 -29.188 1.00 23.90 ? 145 LYS B CG  1 
ATOM   2914 C CD  . LYS B 1 167 ? -5.964  56.171 -30.406 1.00 36.11 ? 145 LYS B CD  1 
ATOM   2915 C CE  . LYS B 1 167 ? -5.735  57.594 -30.872 1.00 32.73 ? 145 LYS B CE  1 
ATOM   2916 N NZ  . LYS B 1 167 ? -6.897  58.079 -31.675 1.00 34.68 ? 145 LYS B NZ  1 
ATOM   2917 N N   . MET B 1 168 ? -3.300  55.513 -26.043 1.00 17.03 ? 146 MET B N   1 
ATOM   2918 C CA  . MET B 1 168 ? -2.837  56.582 -25.159 1.00 16.66 ? 146 MET B CA  1 
ATOM   2919 C C   . MET B 1 168 ? -2.300  57.738 -25.994 1.00 15.34 ? 146 MET B C   1 
ATOM   2920 O O   . MET B 1 168 ? -1.449  57.533 -26.869 1.00 16.45 ? 146 MET B O   1 
ATOM   2921 C CB  . MET B 1 168 ? -1.741  56.070 -24.214 1.00 16.93 ? 146 MET B CB  1 
ATOM   2922 C CG  . MET B 1 168 ? -2.226  54.981 -23.256 1.00 17.05 ? 146 MET B CG  1 
ATOM   2923 S SD  . MET B 1 168 ? -3.245  55.689 -21.944 1.00 19.52 ? 146 MET B SD  1 
ATOM   2924 C CE  . MET B 1 168 ? -2.965  54.468 -20.641 1.00 19.25 ? 146 MET B CE  1 
ATOM   2925 N N   . TYR B 1 169 ? -2.768  58.949 -25.703 1.00 16.41 ? 147 TYR B N   1 
ATOM   2926 C CA  . TYR B 1 169 ? -2.370  60.113 -26.484 1.00 16.80 ? 147 TYR B CA  1 
ATOM   2927 C C   . TYR B 1 169 ? -2.660  61.364 -25.663 1.00 16.70 ? 147 TYR B C   1 
ATOM   2928 O O   . TYR B 1 169 ? -3.327  61.306 -24.634 1.00 19.05 ? 147 TYR B O   1 
ATOM   2929 C CB  . TYR B 1 169 ? -3.093  60.143 -27.837 1.00 17.06 ? 147 TYR B CB  1 
ATOM   2930 C CG  . TYR B 1 169 ? -4.601  60.328 -27.758 1.00 17.89 ? 147 TYR B CG  1 
ATOM   2931 C CD1 . TYR B 1 169 ? -5.442  59.288 -27.338 1.00 17.27 ? 147 TYR B CD1 1 
ATOM   2932 C CD2 . TYR B 1 169 ? -5.176  61.559 -28.069 1.00 23.23 ? 147 TYR B CD2 1 
ATOM   2933 C CE1 . TYR B 1 169 ? -6.821  59.474 -27.274 1.00 16.29 ? 147 TYR B CE1 1 
ATOM   2934 C CE2 . TYR B 1 169 ? -6.542  61.756 -28.007 1.00 22.13 ? 147 TYR B CE2 1 
ATOM   2935 C CZ  . TYR B 1 169 ? -7.359  60.715 -27.606 1.00 19.53 ? 147 TYR B CZ  1 
ATOM   2936 O OH  . TYR B 1 169 ? -8.724  60.923 -27.540 1.00 23.08 ? 147 TYR B OH  1 
ATOM   2937 N N   . VAL B 1 170 ? -2.153  62.498 -26.127 1.00 17.36 ? 148 VAL B N   1 
ATOM   2938 C CA  . VAL B 1 170 ? -2.341  63.766 -25.428 1.00 20.57 ? 148 VAL B CA  1 
ATOM   2939 C C   . VAL B 1 170 ? -3.446  64.536 -26.139 1.00 24.61 ? 148 VAL B C   1 
ATOM   2940 O O   . VAL B 1 170 ? -3.360  64.795 -27.349 1.00 20.50 ? 148 VAL B O   1 
ATOM   2941 C CB  . VAL B 1 170 ? -1.038  64.584 -25.360 1.00 23.92 ? 148 VAL B CB  1 
ATOM   2942 C CG1 . VAL B 1 170 ? -1.287  65.930 -24.669 1.00 21.13 ? 148 VAL B CG1 1 
ATOM   2943 C CG2 . VAL B 1 170 ? 0.051   63.797 -24.629 1.00 25.05 ? 148 VAL B CG2 1 
ATOM   2944 N N   . ARG B 1 171 ? -4.484  64.895 -25.381 1.00 22.76 ? 149 ARG B N   1 
ATOM   2945 C CA  . ARG B 1 171 ? -5.640  65.624 -25.886 1.00 22.95 ? 149 ARG B CA  1 
ATOM   2946 C C   . ARG B 1 171 ? -5.809  66.875 -25.045 1.00 24.04 ? 149 ARG B C   1 
ATOM   2947 O O   . ARG B 1 171 ? -6.064  66.775 -23.841 1.00 28.02 ? 149 ARG B O   1 
ATOM   2948 C CB  . ARG B 1 171 ? -6.904  64.759 -25.814 1.00 22.56 ? 149 ARG B CB  1 
ATOM   2949 C CG  . ARG B 1 171 ? -8.156  65.401 -26.462 1.00 35.53 ? 149 ARG B CG  1 
ATOM   2950 C CD  . ARG B 1 171 ? -9.402  64.528 -26.231 1.00 32.49 ? 149 ARG B CD  1 
ATOM   2951 N NE  . ARG B 1 171 ? -10.480 64.827 -27.170 1.00 44.08 ? 149 ARG B NE  1 
ATOM   2952 C CZ  . ARG B 1 171 ? -10.646 64.219 -28.339 1.00 60.95 ? 149 ARG B CZ  1 
ATOM   2953 N NH1 . ARG B 1 171 ? -9.840  63.241 -28.735 1.00 48.95 ? 149 ARG B NH1 1 
ATOM   2954 N NH2 . ARG B 1 171 ? -11.651 64.592 -29.131 1.00 62.95 ? 149 ARG B NH2 1 
ATOM   2955 N N   . ASP B 1 172 ? -5.669  68.043 -25.671 1.00 30.41 ? 150 ASP B N   1 
ATOM   2956 C CA  . ASP B 1 172 ? -5.807  69.318 -24.972 1.00 36.60 ? 150 ASP B CA  1 
ATOM   2957 C C   . ASP B 1 172 ? -4.943  69.348 -23.713 1.00 42.54 ? 150 ASP B C   1 
ATOM   2958 O O   . ASP B 1 172 ? -5.377  69.786 -22.646 1.00 32.05 ? 150 ASP B O   1 
ATOM   2959 C CB  . ASP B 1 172 ? -7.277  69.588 -24.642 1.00 46.95 ? 150 ASP B CB  1 
ATOM   2960 C CG  . ASP B 1 172 ? -8.137  69.728 -25.889 1.00 53.08 ? 150 ASP B CG  1 
ATOM   2961 O OD1 . ASP B 1 172 ? -9.370  69.550 -25.798 1.00 59.71 ? 150 ASP B OD1 1 
ATOM   2962 O OD2 . ASP B 1 172 ? -7.572  70.034 -26.962 1.00 62.51 ? 150 ASP B OD2 1 
ATOM   2963 N N   . GLY B 1 173 ? -3.716  68.839 -23.832 1.00 25.65 ? 151 GLY B N   1 
ATOM   2964 C CA  . GLY B 1 173 ? -2.770  68.881 -22.735 1.00 29.08 ? 151 GLY B CA  1 
ATOM   2965 C C   . GLY B 1 173 ? -2.986  67.843 -21.655 1.00 28.96 ? 151 GLY B C   1 
ATOM   2966 O O   . GLY B 1 173 ? -2.353  67.933 -20.594 1.00 29.90 ? 151 GLY B O   1 
ATOM   2967 N N   . VAL B 1 174 ? -3.851  66.860 -21.886 1.00 21.80 ? 152 VAL B N   1 
ATOM   2968 C CA  . VAL B 1 174 ? -4.219  65.875 -20.876 1.00 20.48 ? 152 VAL B CA  1 
ATOM   2969 C C   . VAL B 1 174 ? -3.961  64.487 -21.439 1.00 21.67 ? 152 VAL B C   1 
ATOM   2970 O O   . VAL B 1 174 ? -4.379  64.183 -22.561 1.00 20.22 ? 152 VAL B O   1 
ATOM   2971 C CB  . VAL B 1 174 ? -5.692  66.038 -20.445 1.00 20.94 ? 152 VAL B CB  1 
ATOM   2972 C CG1 . VAL B 1 174 ? -6.081  64.969 -19.431 1.00 27.40 ? 152 VAL B CG1 1 
ATOM   2973 C CG2 . VAL B 1 174 ? -5.939  67.437 -19.872 1.00 24.45 ? 152 VAL B CG2 1 
ATOM   2974 N N   . LEU B 1 175 ? -3.250  63.654 -20.671 1.00 21.34 ? 153 LEU B N   1 
ATOM   2975 C CA  . LEU B 1 175 ? -3.054  62.265 -21.073 1.00 19.51 ? 153 LEU B CA  1 
ATOM   2976 C C   . LEU B 1 175 ? -4.400  61.556 -21.087 1.00 16.25 ? 153 LEU B C   1 
ATOM   2977 O O   . LEU B 1 175 ? -5.138  61.584 -20.101 1.00 18.30 ? 153 LEU B O   1 
ATOM   2978 C CB  . LEU B 1 175 ? -2.086  61.556 -20.123 1.00 18.83 ? 153 LEU B CB  1 
ATOM   2979 C CG  . LEU B 1 175 ? -1.793  60.099 -20.501 1.00 21.12 ? 153 LEU B CG  1 
ATOM   2980 C CD1 . LEU B 1 175 ? -1.196  60.007 -21.906 1.00 18.90 ? 153 LEU B CD1 1 
ATOM   2981 C CD2 . LEU B 1 175 ? -0.885  59.434 -19.476 1.00 18.77 ? 153 LEU B CD2 1 
ATOM   2982 N N   . THR B 1 176 ? -4.728  60.951 -22.230 1.00 15.27 ? 154 THR B N   1 
ATOM   2983 C CA  . THR B 1 176 ? -6.055  60.407 -22.487 1.00 16.47 ? 154 THR B CA  1 
ATOM   2984 C C   . THR B 1 176 ? -5.902  59.002 -23.042 1.00 19.60 ? 154 THR B C   1 
ATOM   2985 O O   . THR B 1 176 ? -5.003  58.754 -23.846 1.00 18.03 ? 154 THR B O   1 
ATOM   2986 C CB  . THR B 1 176 ? -6.823  61.301 -23.477 1.00 16.47 ? 154 THR B CB  1 
ATOM   2987 O OG1 . THR B 1 176 ? -6.910  62.620 -22.933 1.00 20.87 ? 154 THR B OG1 1 
ATOM   2988 C CG2 . THR B 1 176 ? -8.237  60.781 -23.736 1.00 15.76 ? 154 THR B CG2 1 
ATOM   2989 N N   . GLY B 1 177 ? -6.763  58.082 -22.592 1.00 15.35 ? 155 GLY B N   1 
ATOM   2990 C CA  . GLY B 1 177 ? -6.780  56.731 -23.138 1.00 13.81 ? 155 GLY B CA  1 
ATOM   2991 C C   . GLY B 1 177 ? -8.150  56.382 -23.697 1.00 18.50 ? 155 GLY B C   1 
ATOM   2992 O O   . GLY B 1 177 ? -9.148  56.488 -22.971 1.00 16.25 ? 155 GLY B O   1 
ATOM   2993 N N   . ASP B 1 178 ? -8.227  56.031 -24.988 1.00 18.17 ? 156 ASP B N   1 
ATOM   2994 C CA  . ASP B 1 178 ? -9.477  55.654 -25.643 1.00 15.06 ? 156 ASP B CA  1 
ATOM   2995 C C   . ASP B 1 178 ? -9.469  54.147 -25.899 1.00 18.11 ? 156 ASP B C   1 
ATOM   2996 O O   . ASP B 1 178 ? -8.450  53.589 -26.316 1.00 16.85 ? 156 ASP B O   1 
ATOM   2997 C CB  . ASP B 1 178 ? -9.679  56.405 -26.976 1.00 15.55 ? 156 ASP B CB  1 
ATOM   2998 C CG  . ASP B 1 178 ? -10.084 57.860 -26.786 1.00 23.75 ? 156 ASP B CG  1 
ATOM   2999 O OD1 . ASP B 1 178 ? -10.411 58.260 -25.652 1.00 20.28 ? 156 ASP B OD1 1 
ATOM   3000 O OD2 . ASP B 1 178 ? -10.088 58.614 -27.783 1.00 18.70 ? 156 ASP B OD2 1 
ATOM   3001 N N   . ILE B 1 179 ? -10.598 53.480 -25.638 1.00 18.33 ? 157 ILE B N   1 
ATOM   3002 C CA  . ILE B 1 179 ? -10.723 52.038 -25.874 1.00 17.93 ? 157 ILE B CA  1 
ATOM   3003 C C   . ILE B 1 179 ? -12.090 51.723 -26.467 1.00 20.77 ? 157 ILE B C   1 
ATOM   3004 O O   . ILE B 1 179 ? -13.120 52.173 -25.952 1.00 18.35 ? 157 ILE B O   1 
ATOM   3005 C CB  . ILE B 1 179 ? -10.523 51.185 -24.604 1.00 14.73 ? 157 ILE B CB  1 
ATOM   3006 C CG1 . ILE B 1 179 ? -9.512  51.805 -23.636 1.00 13.58 ? 157 ILE B CG1 1 
ATOM   3007 C CG2 . ILE B 1 179 ? -10.125 49.729 -24.993 1.00 13.79 ? 157 ILE B CG2 1 
ATOM   3008 C CD1 . ILE B 1 179 ? -9.277  50.936 -22.370 1.00 14.63 ? 157 ILE B CD1 1 
ATOM   3009 N N   . GLU B 1 180 ? -12.106 50.920 -27.530 1.00 16.75 ? 158 GLU B N   1 
ATOM   3010 C CA  . GLU B 1 180 ? -13.324 50.236 -27.953 1.00 21.73 ? 158 GLU B CA  1 
ATOM   3011 C C   . GLU B 1 180 ? -13.362 48.904 -27.216 1.00 25.97 ? 158 GLU B C   1 
ATOM   3012 O O   . GLU B 1 180 ? -12.555 48.008 -27.487 1.00 23.05 ? 158 GLU B O   1 
ATOM   3013 C CB  . GLU B 1 180 ? -13.372 50.035 -29.467 1.00 22.73 ? 158 GLU B CB  1 
ATOM   3014 C CG  . GLU B 1 180 ? -13.181 51.293 -30.283 1.00 34.13 ? 158 GLU B CG  1 
ATOM   3015 C CD  . GLU B 1 180 ? -13.394 51.042 -31.772 1.00 40.55 ? 158 GLU B CD  1 
ATOM   3016 O OE1 . GLU B 1 180 ? -14.041 50.029 -32.123 1.00 43.47 ? 158 GLU B OE1 1 
ATOM   3017 O OE2 . GLU B 1 180 ? -12.915 51.848 -32.583 1.00 43.03 ? 158 GLU B OE2 1 
ATOM   3018 N N   . MET B 1 181 ? -14.270 48.786 -26.256 1.00 17.80 ? 159 MET B N   1 
ATOM   3019 C CA  . MET B 1 181 ? -14.372 47.608 -25.418 1.00 16.80 ? 159 MET B CA  1 
ATOM   3020 C C   . MET B 1 181 ? -15.556 46.760 -25.870 1.00 15.85 ? 159 MET B C   1 
ATOM   3021 O O   . MET B 1 181 ? -16.454 47.238 -26.560 1.00 17.43 ? 159 MET B O   1 
ATOM   3022 C CB  . MET B 1 181 ? -14.562 48.009 -23.952 1.00 16.87 ? 159 MET B CB  1 
ATOM   3023 C CG  . MET B 1 181 ? -13.379 48.717 -23.299 1.00 17.60 ? 159 MET B CG  1 
ATOM   3024 S SD  . MET B 1 181 ? -12.066 47.607 -22.836 1.00 19.42 ? 159 MET B SD  1 
ATOM   3025 C CE  . MET B 1 181 ? -12.650 47.136 -21.207 1.00 20.06 ? 159 MET B CE  1 
ATOM   3026 N N   . ALA B 1 182 ? -15.548 45.486 -25.476 1.00 17.19 ? 160 ALA B N   1 
ATOM   3027 C CA  . ALA B 1 182 ? -16.664 44.608 -25.820 1.00 17.36 ? 160 ALA B CA  1 
ATOM   3028 C C   . ALA B 1 182 ? -16.873 43.583 -24.722 1.00 19.81 ? 160 ALA B C   1 
ATOM   3029 O O   . ALA B 1 182 ? -15.924 42.897 -24.328 1.00 19.03 ? 160 ALA B O   1 
ATOM   3030 C CB  . ALA B 1 182 ? -16.430 43.897 -27.154 1.00 18.80 ? 160 ALA B CB  1 
ATOM   3031 N N   . LEU B 1 183 ? -18.112 43.481 -24.239 1.00 16.56 ? 161 LEU B N   1 
ATOM   3032 C CA  . LEU B 1 183 ? -18.511 42.419 -23.322 1.00 21.25 ? 161 LEU B CA  1 
ATOM   3033 C C   . LEU B 1 183 ? -19.007 41.235 -24.137 1.00 25.14 ? 161 LEU B C   1 
ATOM   3034 O O   . LEU B 1 183 ? -19.901 41.390 -24.972 1.00 22.22 ? 161 LEU B O   1 
ATOM   3035 C CB  . LEU B 1 183 ? -19.606 42.895 -22.363 1.00 19.25 ? 161 LEU B CB  1 
ATOM   3036 C CG  . LEU B 1 183 ? -19.123 43.704 -21.161 1.00 24.08 ? 161 LEU B CG  1 
ATOM   3037 C CD1 . LEU B 1 183 ? -20.265 44.482 -20.529 1.00 17.90 ? 161 LEU B CD1 1 
ATOM   3038 C CD2 . LEU B 1 183 ? -18.473 42.782 -20.133 1.00 23.55 ? 161 LEU B CD2 1 
ATOM   3039 N N   . LEU B 1 184 ? -18.390 40.070 -23.938 1.00 22.46 ? 162 LEU B N   1 
ATOM   3040 C CA  . LEU B 1 184 ? -18.965 38.830 -24.439 1.00 22.69 ? 162 LEU B CA  1 
ATOM   3041 C C   . LEU B 1 184 ? -20.198 38.506 -23.615 1.00 24.76 ? 162 LEU B C   1 
ATOM   3042 O O   . LEU B 1 184 ? -20.145 38.523 -22.379 1.00 26.21 ? 162 LEU B O   1 
ATOM   3043 C CB  . LEU B 1 184 ? -17.960 37.678 -24.336 1.00 23.71 ? 162 LEU B CB  1 
ATOM   3044 C CG  . LEU B 1 184 ? -18.464 36.321 -24.852 1.00 30.58 ? 162 LEU B CG  1 
ATOM   3045 C CD1 . LEU B 1 184 ? -18.721 36.351 -26.362 1.00 30.84 ? 162 LEU B CD1 1 
ATOM   3046 C CD2 . LEU B 1 184 ? -17.518 35.180 -24.484 1.00 23.80 ? 162 LEU B CD2 1 
ATOM   3047 N N   . LEU B 1 185 ? -21.300 38.214 -24.292 1.00 31.17 ? 163 LEU B N   1 
ATOM   3048 C CA  . LEU B 1 185 ? -22.569 37.901 -23.662 1.00 25.12 ? 163 LEU B CA  1 
ATOM   3049 C C   . LEU B 1 185 ? -22.859 36.414 -23.752 1.00 27.99 ? 163 LEU B C   1 
ATOM   3050 O O   . LEU B 1 185 ? -22.272 35.686 -24.561 1.00 32.80 ? 163 LEU B O   1 
ATOM   3051 C CB  . LEU B 1 185 ? -23.711 38.669 -24.326 1.00 32.17 ? 163 LEU B CB  1 
ATOM   3052 C CG  . LEU B 1 185 ? -23.645 40.186 -24.285 1.00 28.88 ? 163 LEU B CG  1 
ATOM   3053 C CD1 . LEU B 1 185 ? -24.931 40.755 -24.873 1.00 31.39 ? 163 LEU B CD1 1 
ATOM   3054 C CD2 . LEU B 1 185 ? -23.390 40.679 -22.855 1.00 27.02 ? 163 LEU B CD2 1 
ATOM   3055 N N   . GLU B 1 186 ? -23.792 35.970 -22.917 1.00 36.10 ? 164 GLU B N   1 
ATOM   3056 C CA  . GLU B 1 186 ? -24.343 34.635 -23.085 1.00 42.34 ? 164 GLU B CA  1 
ATOM   3057 C C   . GLU B 1 186 ? -24.999 34.535 -24.457 1.00 54.71 ? 164 GLU B C   1 
ATOM   3058 O O   . GLU B 1 186 ? -25.690 35.457 -24.899 1.00 54.34 ? 164 GLU B O   1 
ATOM   3059 C CB  . GLU B 1 186 ? -25.363 34.334 -21.987 1.00 49.22 ? 164 GLU B CB  1 
ATOM   3060 C CG  . GLU B 1 186 ? -24.734 33.887 -20.683 1.00 54.33 ? 164 GLU B CG  1 
ATOM   3061 C CD  . GLU B 1 186 ? -25.699 33.949 -19.513 1.00 68.51 ? 164 GLU B CD  1 
ATOM   3062 O OE1 . GLU B 1 186 ? -26.929 33.977 -19.749 1.00 63.00 ? 164 GLU B OE1 1 
ATOM   3063 O OE2 . GLU B 1 186 ? -25.220 34.011 -18.357 1.00 61.31 ? 164 GLU B OE2 1 
ATOM   3064 N N   . GLY B 1 187 ? -24.767 33.416 -25.140 1.00 51.06 ? 165 GLY B N   1 
ATOM   3065 C CA  . GLY B 1 187 ? -25.212 33.269 -26.508 1.00 49.09 ? 165 GLY B CA  1 
ATOM   3066 C C   . GLY B 1 187 ? -24.223 33.722 -27.563 1.00 48.42 ? 165 GLY B C   1 
ATOM   3067 O O   . GLY B 1 187 ? -24.546 33.656 -28.757 1.00 54.18 ? 165 GLY B O   1 
ATOM   3068 N N   . ASN B 1 188 ? -23.047 34.202 -27.161 1.00 48.20 ? 166 ASN B N   1 
ATOM   3069 C CA  . ASN B 1 188 ? -21.865 34.498 -27.978 1.00 52.38 ? 166 ASN B CA  1 
ATOM   3070 C C   . ASN B 1 188 ? -21.999 35.889 -28.616 1.00 45.46 ? 166 ASN B C   1 
ATOM   3071 O O   . ASN B 1 188 ? -21.083 36.311 -29.327 1.00 50.53 ? 166 ASN B O   1 
ATOM   3072 C CB  . ASN B 1 188 ? -21.615 33.406 -29.044 1.00 53.09 ? 166 ASN B CB  1 
ATOM   3073 C CG  . ASN B 1 188 ? -20.421 33.689 -29.981 1.00 55.88 ? 166 ASN B CG  1 
ATOM   3074 O OD1 . ASN B 1 188 ? -20.134 32.883 -30.867 1.00 70.38 ? 166 ASN B OD1 1 
ATOM   3075 N ND2 . ASN B 1 188 ? -19.671 34.755 -29.722 1.00 63.88 ? 166 ASN B ND2 1 
ATOM   3076 N N   . ALA B 1 189 ? -23.070 36.635 -28.363 1.00 39.71 ? 167 ALA B N   1 
ATOM   3077 C CA  . ALA B 1 189 ? -23.118 37.989 -28.897 1.00 40.85 ? 167 ALA B CA  1 
ATOM   3078 C C   . ALA B 1 189 ? -22.180 38.904 -28.109 1.00 37.87 ? 167 ALA B C   1 
ATOM   3079 O O   . ALA B 1 189 ? -21.674 38.555 -27.038 1.00 38.01 ? 167 ALA B O   1 
ATOM   3080 C CB  . ALA B 1 189 ? -24.544 38.536 -28.873 1.00 39.44 ? 167 ALA B CB  1 
ATOM   3081 N N   . HIS B 1 190 ? -21.937 40.092 -28.656 1.00 30.45 ? 168 HIS B N   1 
ATOM   3082 C CA  . HIS B 1 190 ? -21.101 41.080 -27.997 1.00 27.58 ? 168 HIS B CA  1 
ATOM   3083 C C   . HIS B 1 190 ? -21.891 42.358 -27.752 1.00 32.44 ? 168 HIS B C   1 
ATOM   3084 O O   . HIS B 1 190 ? -22.875 42.658 -28.436 1.00 33.10 ? 168 HIS B O   1 
ATOM   3085 C CB  . HIS B 1 190 ? -19.845 41.393 -28.813 1.00 27.96 ? 168 HIS B CB  1 
ATOM   3086 C CG  . HIS B 1 190 ? -18.778 40.354 -28.684 1.00 28.25 ? 168 HIS B CG  1 
ATOM   3087 N ND1 . HIS B 1 190 ? -18.688 39.277 -29.534 1.00 30.29 ? 168 HIS B ND1 1 
ATOM   3088 C CD2 . HIS B 1 190 ? -17.746 40.236 -27.813 1.00 27.67 ? 168 HIS B CD2 1 
ATOM   3089 C CE1 . HIS B 1 190 ? -17.659 38.526 -29.185 1.00 37.23 ? 168 HIS B CE1 1 
ATOM   3090 N NE2 . HIS B 1 190 ? -17.072 39.084 -28.141 1.00 28.42 ? 168 HIS B NE2 1 
ATOM   3091 N N   . TYR B 1 191 ? -21.425 43.107 -26.762 1.00 26.90 ? 169 TYR B N   1 
ATOM   3092 C CA  . TYR B 1 191 ? -22.102 44.302 -26.268 1.00 27.05 ? 169 TYR B CA  1 
ATOM   3093 C C   . TYR B 1 191 ? -21.012 45.353 -26.130 1.00 23.92 ? 169 TYR B C   1 
ATOM   3094 O O   . TYR B 1 191 ? -20.127 45.217 -25.274 1.00 23.05 ? 169 TYR B O   1 
ATOM   3095 C CB  . TYR B 1 191 ? -22.803 43.996 -24.941 1.00 27.52 ? 169 TYR B CB  1 
ATOM   3096 C CG  . TYR B 1 191 ? -23.408 45.145 -24.157 1.00 22.32 ? 169 TYR B CG  1 
ATOM   3097 C CD1 . TYR B 1 191 ? -24.350 45.993 -24.731 1.00 27.28 ? 169 TYR B CD1 1 
ATOM   3098 C CD2 . TYR B 1 191 ? -23.098 45.324 -22.812 1.00 21.35 ? 169 TYR B CD2 1 
ATOM   3099 C CE1 . TYR B 1 191 ? -24.925 47.028 -24.000 1.00 26.39 ? 169 TYR B CE1 1 
ATOM   3100 C CE2 . TYR B 1 191 ? -23.675 46.342 -22.067 1.00 21.16 ? 169 TYR B CE2 1 
ATOM   3101 C CZ  . TYR B 1 191 ? -24.584 47.197 -22.668 1.00 26.67 ? 169 TYR B CZ  1 
ATOM   3102 O OH  . TYR B 1 191 ? -25.159 48.207 -21.929 1.00 21.83 ? 169 TYR B OH  1 
ATOM   3103 N N   . ARG B 1 192 ? -21.041 46.354 -27.010 1.00 20.57 ? 170 ARG B N   1 
ATOM   3104 C CA  . ARG B 1 192 ? -19.940 47.296 -27.164 1.00 21.15 ? 170 ARG B CA  1 
ATOM   3105 C C   . ARG B 1 192 ? -20.022 48.418 -26.132 1.00 21.24 ? 170 ARG B C   1 
ATOM   3106 O O   . ARG B 1 192 ? -21.106 48.874 -25.759 1.00 22.47 ? 170 ARG B O   1 
ATOM   3107 C CB  . ARG B 1 192 ? -19.958 47.904 -28.569 1.00 26.34 ? 170 ARG B CB  1 
ATOM   3108 C CG  . ARG B 1 192 ? -19.354 49.327 -28.697 1.00 29.53 ? 170 ARG B CG  1 
ATOM   3109 C CD  . ARG B 1 192 ? -18.817 49.600 -30.127 1.00 44.26 ? 170 ARG B CD  1 
ATOM   3110 N NE  . ARG B 1 192 ? -18.174 50.908 -30.269 1.00 42.99 ? 170 ARG B NE  1 
ATOM   3111 C CZ  . ARG B 1 192 ? -17.822 51.451 -31.431 1.00 36.18 ? 170 ARG B CZ  1 
ATOM   3112 N NH1 . ARG B 1 192 ? -18.053 50.839 -32.582 1.00 37.20 ? 170 ARG B NH1 1 
ATOM   3113 N NH2 . ARG B 1 192 ? -17.219 52.638 -31.439 1.00 27.77 ? 170 ARG B NH2 1 
ATOM   3114 N N   . CYS B 1 193 ? -18.850 48.876 -25.690 1.00 17.94 ? 171 CYS B N   1 
ATOM   3115 C CA  . CYS B 1 193 ? -18.739 50.047 -24.833 1.00 17.21 ? 171 CYS B CA  1 
ATOM   3116 C C   . CYS B 1 193 ? -17.528 50.851 -25.280 1.00 23.70 ? 171 CYS B C   1 
ATOM   3117 O O   . CYS B 1 193 ? -16.465 50.279 -25.534 1.00 21.90 ? 171 CYS B O   1 
ATOM   3118 C CB  . CYS B 1 193 ? -18.591 49.633 -23.366 1.00 16.49 ? 171 CYS B CB  1 
ATOM   3119 S SG  . CYS B 1 193 ? -18.547 51.015 -22.177 1.00 20.59 ? 171 CYS B SG  1 
ATOM   3120 N N   . ASP B 1 194 ? -17.673 52.172 -25.361 1.00 19.56 ? 172 ASP B N   1 
ATOM   3121 C CA  . ASP B 1 194 ? -16.538 53.045 -25.643 1.00 17.80 ? 172 ASP B CA  1 
ATOM   3122 C C   . ASP B 1 194 ? -16.057 53.681 -24.348 1.00 17.56 ? 172 ASP B C   1 
ATOM   3123 O O   . ASP B 1 194 ? -16.854 54.289 -23.628 1.00 18.20 ? 172 ASP B O   1 
ATOM   3124 C CB  . ASP B 1 194 ? -16.924 54.132 -26.653 1.00 19.38 ? 172 ASP B CB  1 
ATOM   3125 C CG  . ASP B 1 194 ? -17.210 53.560 -28.022 1.00 29.62 ? 172 ASP B CG  1 
ATOM   3126 O OD1 . ASP B 1 194 ? -16.269 53.073 -28.657 1.00 26.14 ? 172 ASP B OD1 1 
ATOM   3127 O OD2 . ASP B 1 194 ? -18.389 53.540 -28.433 1.00 35.81 ? 172 ASP B OD2 1 
ATOM   3128 N N   . PHE B 1 195 ? -14.755 53.548 -24.073 1.00 17.01 ? 173 PHE B N   1 
ATOM   3129 C CA  . PHE B 1 195 ? -14.090 54.119 -22.900 1.00 20.64 ? 173 PHE B CA  1 
ATOM   3130 C C   . PHE B 1 195 ? -13.316 55.366 -23.310 1.00 20.97 ? 173 PHE B C   1 
ATOM   3131 O O   . PHE B 1 195 ? -12.618 55.368 -24.332 1.00 16.95 ? 173 PHE B O   1 
ATOM   3132 C CB  . PHE B 1 195 ? -13.048 53.170 -22.273 1.00 15.60 ? 173 PHE B CB  1 
ATOM   3133 C CG  . PHE B 1 195 ? -13.593 52.063 -21.389 1.00 14.35 ? 173 PHE B CG  1 
ATOM   3134 C CD1 . PHE B 1 195 ? -14.919 51.644 -21.444 1.00 20.98 ? 173 PHE B CD1 1 
ATOM   3135 C CD2 . PHE B 1 195 ? -12.733 51.441 -20.491 1.00 15.20 ? 173 PHE B CD2 1 
ATOM   3136 C CE1 . PHE B 1 195 ? -15.368 50.602 -20.623 1.00 22.28 ? 173 PHE B CE1 1 
ATOM   3137 C CE2 . PHE B 1 195 ? -13.165 50.394 -19.673 1.00 15.58 ? 173 PHE B CE2 1 
ATOM   3138 C CZ  . PHE B 1 195 ? -14.494 49.983 -19.735 1.00 17.83 ? 173 PHE B CZ  1 
ATOM   3139 N N   . ARG B 1 196 ? -13.394 56.409 -22.486 1.00 19.24 ? 174 ARG B N   1 
ATOM   3140 C CA  . ARG B 1 196 ? -12.389 57.466 -22.512 1.00 22.42 ? 174 ARG B CA  1 
ATOM   3141 C C   . ARG B 1 196 ? -11.973 57.744 -21.077 1.00 17.69 ? 174 ARG B C   1 
ATOM   3142 O O   . ARG B 1 196 ? -12.822 58.029 -20.232 1.00 16.88 ? 174 ARG B O   1 
ATOM   3143 C CB  . ARG B 1 196 ? -12.887 58.751 -23.177 1.00 17.13 ? 174 ARG B CB  1 
ATOM   3144 C CG  . ARG B 1 196 ? -11.881 59.906 -22.978 1.00 18.70 ? 174 ARG B CG  1 
ATOM   3145 C CD  . ARG B 1 196 ? -12.121 61.068 -23.958 1.00 20.28 ? 174 ARG B CD  1 
ATOM   3146 N NE  . ARG B 1 196 ? -11.883 60.650 -25.334 1.00 18.81 ? 174 ARG B NE  1 
ATOM   3147 C CZ  . ARG B 1 196 ? -12.269 61.345 -26.392 1.00 23.32 ? 174 ARG B CZ  1 
ATOM   3148 N NH1 . ARG B 1 196 ? -12.876 62.511 -26.262 1.00 25.45 ? 174 ARG B NH1 1 
ATOM   3149 N NH2 . ARG B 1 196 ? -12.020 60.871 -27.609 1.00 23.58 ? 174 ARG B NH2 1 
ATOM   3150 N N   . THR B 1 197 ? -10.675 57.653 -20.808 1.00 16.25 ? 175 THR B N   1 
ATOM   3151 C CA  . THR B 1 197 ? -10.110 57.935 -19.488 1.00 14.49 ? 175 THR B CA  1 
ATOM   3152 C C   . THR B 1 197 ? -9.124  59.090 -19.604 1.00 21.05 ? 175 THR B C   1 
ATOM   3153 O O   . THR B 1 197 ? -8.289  59.102 -20.516 1.00 18.59 ? 175 THR B O   1 
ATOM   3154 C CB  . THR B 1 197 ? -9.378  56.711 -18.945 1.00 17.66 ? 175 THR B CB  1 
ATOM   3155 O OG1 . THR B 1 197 ? -10.216 55.559 -19.091 1.00 18.56 ? 175 THR B OG1 1 
ATOM   3156 C CG2 . THR B 1 197 ? -9.027  56.905 -17.464 1.00 13.74 ? 175 THR B CG2 1 
ATOM   3157 N N   . THR B 1 198 ? -9.199  60.040 -18.680 1.00 17.36 ? 176 THR B N   1 
ATOM   3158 C CA  . THR B 1 198 ? -8.163  61.051 -18.539 1.00 18.09 ? 176 THR B CA  1 
ATOM   3159 C C   . THR B 1 198 ? -7.378  60.760 -17.266 1.00 20.85 ? 176 THR B C   1 
ATOM   3160 O O   . THR B 1 198 ? -7.953  60.335 -16.258 1.00 17.19 ? 176 THR B O   1 
ATOM   3161 C CB  . THR B 1 198 ? -8.736  62.468 -18.503 1.00 22.14 ? 176 THR B CB  1 
ATOM   3162 O OG1 . THR B 1 198 ? -9.718  62.584 -17.465 1.00 22.84 ? 176 THR B OG1 1 
ATOM   3163 C CG2 . THR B 1 198 ? -9.372  62.811 -19.853 1.00 24.85 ? 176 THR B CG2 1 
ATOM   3164 N N   . TYR B 1 199 ? -6.059  60.950 -17.342 1.00 18.68 ? 177 TYR B N   1 
ATOM   3165 C CA  . TYR B 1 199 ? -5.112  60.619 -16.285 1.00 19.80 ? 177 TYR B CA  1 
ATOM   3166 C C   . TYR B 1 199 ? -4.329  61.877 -15.927 1.00 20.67 ? 177 TYR B C   1 
ATOM   3167 O O   . TYR B 1 199 ? -3.837  62.569 -16.822 1.00 18.79 ? 177 TYR B O   1 
ATOM   3168 C CB  . TYR B 1 199 ? -4.133  59.543 -16.769 1.00 22.16 ? 177 TYR B CB  1 
ATOM   3169 C CG  . TYR B 1 199 ? -4.739  58.238 -17.271 1.00 17.56 ? 177 TYR B CG  1 
ATOM   3170 C CD1 . TYR B 1 199 ? -5.039  57.208 -16.388 1.00 16.81 ? 177 TYR B CD1 1 
ATOM   3171 C CD2 . TYR B 1 199 ? -4.991  58.044 -18.632 1.00 20.01 ? 177 TYR B CD2 1 
ATOM   3172 C CE1 . TYR B 1 199 ? -5.575  55.994 -16.838 1.00 15.05 ? 177 TYR B CE1 1 
ATOM   3173 C CE2 . TYR B 1 199 ? -5.535  56.836 -19.110 1.00 16.82 ? 177 TYR B CE2 1 
ATOM   3174 C CZ  . TYR B 1 199 ? -5.821  55.823 -18.201 1.00 19.32 ? 177 TYR B CZ  1 
ATOM   3175 O OH  . TYR B 1 199 ? -6.355  54.626 -18.627 1.00 17.83 ? 177 TYR B OH  1 
ATOM   3176 N N   . LYS B 1 200 ? -4.191  62.175 -14.632 1.00 20.66 ? 178 LYS B N   1 
ATOM   3177 C CA  . LYS B 1 200 ? -3.460  63.368 -14.211 1.00 18.23 ? 178 LYS B CA  1 
ATOM   3178 C C   . LYS B 1 200 ? -2.639  63.080 -12.962 1.00 19.81 ? 178 LYS B C   1 
ATOM   3179 O O   . LYS B 1 200 ? -3.203  62.762 -11.911 1.00 22.92 ? 178 LYS B O   1 
ATOM   3180 C CB  . LYS B 1 200 ? -4.400  64.561 -13.956 1.00 26.88 ? 178 LYS B CB  1 
ATOM   3181 C CG  . LYS B 1 200 ? -5.596  64.694 -14.900 1.00 41.12 ? 178 LYS B CG  1 
ATOM   3182 C CD  . LYS B 1 200 ? -6.419  65.952 -14.583 1.00 50.04 ? 178 LYS B CD  1 
ATOM   3183 C CE  . LYS B 1 200 ? -7.347  66.330 -15.737 1.00 48.33 ? 178 LYS B CE  1 
ATOM   3184 N NZ  . LYS B 1 200 ? -7.731  67.780 -15.704 1.00 56.71 ? 178 LYS B NZ  1 
ATOM   3185 N N   . ALA B 1 201 ? -1.316  63.258 -13.068 1.00 19.90 ? 179 ALA B N   1 
ATOM   3186 C CA  . ALA B 1 201 ? -0.442  63.169 -11.902 1.00 21.10 ? 179 ALA B CA  1 
ATOM   3187 C C   . ALA B 1 201 ? -0.778  64.255 -10.892 1.00 26.89 ? 179 ALA B C   1 
ATOM   3188 O O   . ALA B 1 201 ? -1.098  65.389 -11.258 1.00 27.59 ? 179 ALA B O   1 
ATOM   3189 C CB  . ALA B 1 201 ? 1.026   63.298 -12.317 1.00 22.03 ? 179 ALA B CB  1 
ATOM   3190 N N   . LYS B 1 202 ? -0.676  63.914 -9.606  1.00 25.29 ? 180 LYS B N   1 
ATOM   3191 C CA  . LYS B 1 202 ? -0.950  64.903 -8.565  1.00 29.10 ? 180 LYS B CA  1 
ATOM   3192 C C   . LYS B 1 202 ? 0.148   65.958 -8.499  1.00 37.19 ? 180 LYS B C   1 
ATOM   3193 O O   . LYS B 1 202 ? -0.124  67.138 -8.240  1.00 32.36 ? 180 LYS B O   1 
ATOM   3194 C CB  . LYS B 1 202 ? -1.118  64.207 -7.213  1.00 35.80 ? 180 LYS B CB  1 
ATOM   3195 C CG  . LYS B 1 202 ? -1.326  65.141 -6.005  1.00 48.68 ? 180 LYS B CG  1 
ATOM   3196 C CD  . LYS B 1 202 ? -2.366  66.243 -6.265  1.00 47.05 ? 180 LYS B CD  1 
ATOM   3197 C CE  . LYS B 1 202 ? -3.450  66.273 -5.185  1.00 56.06 ? 180 LYS B CE  1 
ATOM   3198 N NZ  . LYS B 1 202 ? -2.959  66.820 -3.887  1.00 52.77 ? 180 LYS B NZ  1 
ATOM   3199 N N   . GLU B 1 203 ? 1.397   65.564 -8.713  1.00 30.34 ? 181 GLU B N   1 
ATOM   3200 C CA  . GLU B 1 203 ? 2.475   66.528 -8.601  1.00 36.77 ? 181 GLU B CA  1 
ATOM   3201 C C   . GLU B 1 203 ? 2.554   67.350 -9.881  1.00 41.16 ? 181 GLU B C   1 
ATOM   3202 O O   . GLU B 1 203 ? 2.386   66.827 -10.985 1.00 35.20 ? 181 GLU B O   1 
ATOM   3203 C CB  . GLU B 1 203 ? 3.796   65.820 -8.295  1.00 36.47 ? 181 GLU B CB  1 
ATOM   3204 C CG  . GLU B 1 203 ? 5.033   66.377 -8.953  1.00 45.11 ? 181 GLU B CG  1 
ATOM   3205 C CD  . GLU B 1 203 ? 6.275   65.607 -8.540  1.00 50.48 ? 181 GLU B CD  1 
ATOM   3206 O OE1 . GLU B 1 203 ? 6.683   65.733 -7.364  1.00 63.08 ? 181 GLU B OE1 1 
ATOM   3207 O OE2 . GLU B 1 203 ? 6.834   64.866 -9.380  1.00 51.88 ? 181 GLU B OE2 1 
ATOM   3208 N N   . LYS B 1 204 ? 2.751   68.657 -9.722  1.00 44.31 ? 182 LYS B N   1 
ATOM   3209 C CA  . LYS B 1 204 ? 2.847   69.534 -10.880 1.00 54.38 ? 182 LYS B CA  1 
ATOM   3210 C C   . LYS B 1 204 ? 4.148   69.285 -11.629 1.00 49.00 ? 182 LYS B C   1 
ATOM   3211 O O   . LYS B 1 204 ? 5.207   69.105 -11.024 1.00 47.80 ? 182 LYS B O   1 
ATOM   3212 C CB  . LYS B 1 204 ? 2.758   71.002 -10.458 1.00 52.67 ? 182 LYS B CB  1 
ATOM   3213 C CG  . LYS B 1 204 ? 1.340   71.509 -10.168 1.00 65.99 ? 182 LYS B CG  1 
ATOM   3214 C CD  . LYS B 1 204 ? 0.895   71.253 -8.734  1.00 71.90 ? 182 LYS B CD  1 
ATOM   3215 C CE  . LYS B 1 204 ? -0.623  71.116 -8.649  1.00 77.02 ? 182 LYS B CE  1 
ATOM   3216 N NZ  . LYS B 1 204 ? -1.048  70.088 -7.660  1.00 71.19 ? 182 LYS B NZ  1 
ATOM   3217 N N   . GLY B 1 205 ? 4.062   69.254 -12.954 1.00 43.65 ? 183 GLY B N   1 
ATOM   3218 C CA  . GLY B 1 205 ? 5.250   69.196 -13.777 1.00 40.92 ? 183 GLY B CA  1 
ATOM   3219 C C   . GLY B 1 205 ? 5.748   67.814 -14.130 1.00 43.24 ? 183 GLY B C   1 
ATOM   3220 O O   . GLY B 1 205 ? 6.871   67.691 -14.631 1.00 40.19 ? 183 GLY B O   1 
ATOM   3221 N N   . VAL B 1 206 ? 4.973   66.764 -13.865 1.00 35.03 ? 184 VAL B N   1 
ATOM   3222 C CA  . VAL B 1 206 ? 5.319   65.461 -14.410 1.00 34.47 ? 184 VAL B CA  1 
ATOM   3223 C C   . VAL B 1 206 ? 5.121   65.513 -15.916 1.00 35.68 ? 184 VAL B C   1 
ATOM   3224 O O   . VAL B 1 206 ? 4.060   65.927 -16.409 1.00 32.49 ? 184 VAL B O   1 
ATOM   3225 C CB  . VAL B 1 206 ? 4.485   64.347 -13.764 1.00 31.56 ? 184 VAL B CB  1 
ATOM   3226 C CG1 . VAL B 1 206 ? 4.814   63.005 -14.419 1.00 31.81 ? 184 VAL B CG1 1 
ATOM   3227 C CG2 . VAL B 1 206 ? 4.743   64.269 -12.264 1.00 35.37 ? 184 VAL B CG2 1 
ATOM   3228 N N   . LYS B 1 207 ? 6.154   65.122 -16.654 1.00 31.88 ? 185 LYS B N   1 
ATOM   3229 C CA  . LYS B 1 207 ? 6.129   65.254 -18.100 1.00 39.30 ? 185 LYS B CA  1 
ATOM   3230 C C   . LYS B 1 207 ? 5.162   64.240 -18.697 1.00 24.23 ? 185 LYS B C   1 
ATOM   3231 O O   . LYS B 1 207 ? 5.118   63.081 -18.277 1.00 24.89 ? 185 LYS B O   1 
ATOM   3232 C CB  . LYS B 1 207 ? 7.540   65.066 -18.663 1.00 38.54 ? 185 LYS B CB  1 
ATOM   3233 C CG  . LYS B 1 207 ? 7.670   65.305 -20.154 1.00 42.94 ? 185 LYS B CG  1 
ATOM   3234 C CD  . LYS B 1 207 ? 8.993   64.739 -20.676 1.00 41.36 ? 185 LYS B CD  1 
ATOM   3235 C CE  . LYS B 1 207 ? 9.132   64.928 -22.182 1.00 50.54 ? 185 LYS B CE  1 
ATOM   3236 N NZ  . LYS B 1 207 ? 10.547  65.152 -22.569 1.00 49.86 ? 185 LYS B NZ  1 
ATOM   3237 N N   . LEU B 1 208 ? 4.358   64.690 -19.660 1.00 30.04 ? 186 LEU B N   1 
ATOM   3238 C CA  . LEU B 1 208 ? 3.460   63.781 -20.355 1.00 25.12 ? 186 LEU B CA  1 
ATOM   3239 C C   . LEU B 1 208 ? 4.267   62.809 -21.211 1.00 20.71 ? 186 LEU B C   1 
ATOM   3240 O O   . LEU B 1 208 ? 5.303   63.178 -21.776 1.00 24.25 ? 186 LEU B O   1 
ATOM   3241 C CB  . LEU B 1 208 ? 2.478   64.557 -21.237 1.00 25.22 ? 186 LEU B CB  1 
ATOM   3242 C CG  . LEU B 1 208 ? 1.521   65.507 -20.513 1.00 33.21 ? 186 LEU B CG  1 
ATOM   3243 C CD1 . LEU B 1 208 ? 0.664   66.261 -21.509 1.00 35.28 ? 186 LEU B CD1 1 
ATOM   3244 C CD2 . LEU B 1 208 ? 0.642   64.733 -19.547 1.00 32.26 ? 186 LEU B CD2 1 
ATOM   3245 N N   . PRO B 1 209 ? 3.815   61.565 -21.331 1.00 20.26 ? 187 PRO B N   1 
ATOM   3246 C CA  . PRO B 1 209 ? 4.495   60.610 -22.207 1.00 22.66 ? 187 PRO B CA  1 
ATOM   3247 C C   . PRO B 1 209 ? 4.130   60.875 -23.661 1.00 21.95 ? 187 PRO B C   1 
ATOM   3248 O O   . PRO B 1 209 ? 3.202   61.626 -23.980 1.00 22.48 ? 187 PRO B O   1 
ATOM   3249 C CB  . PRO B 1 209 ? 3.933   59.260 -21.749 1.00 21.41 ? 187 PRO B CB  1 
ATOM   3250 C CG  . PRO B 1 209 ? 2.500   59.608 -21.317 1.00 20.53 ? 187 PRO B CG  1 
ATOM   3251 C CD  . PRO B 1 209 ? 2.549   61.025 -20.792 1.00 16.98 ? 187 PRO B CD  1 
ATOM   3252 N N   . GLY B 1 210 ? 4.891   60.251 -24.551 1.00 22.81 ? 188 GLY B N   1 
ATOM   3253 C CA  . GLY B 1 210 ? 4.493   60.226 -25.937 1.00 20.68 ? 188 GLY B CA  1 
ATOM   3254 C C   . GLY B 1 210 ? 3.312   59.292 -26.116 1.00 20.87 ? 188 GLY B C   1 
ATOM   3255 O O   . GLY B 1 210 ? 2.913   58.559 -25.210 1.00 17.90 ? 188 GLY B O   1 
ATOM   3256 N N   . ALA B 1 211 ? 2.740   59.312 -27.310 1.00 20.38 ? 189 ALA B N   1 
ATOM   3257 C CA  . ALA B 1 211 ? 1.596   58.450 -27.569 1.00 22.21 ? 189 ALA B CA  1 
ATOM   3258 C C   . ALA B 1 211 ? 2.047   56.995 -27.640 1.00 17.99 ? 189 ALA B C   1 
ATOM   3259 O O   . ALA B 1 211 ? 3.180   56.692 -28.038 1.00 20.21 ? 189 ALA B O   1 
ATOM   3260 C CB  . ALA B 1 211 ? 0.897   58.870 -28.869 1.00 19.41 ? 189 ALA B CB  1 
ATOM   3261 N N   . HIS B 1 212 ? 1.157   56.089 -27.238 1.00 18.34 ? 190 HIS B N   1 
ATOM   3262 C CA  . HIS B 1 212 ? 1.474   54.660 -27.212 1.00 18.60 ? 190 HIS B CA  1 
ATOM   3263 C C   . HIS B 1 212 ? 0.164   53.887 -27.038 1.00 17.73 ? 190 HIS B C   1 
ATOM   3264 O O   . HIS B 1 212 ? -0.934  54.455 -27.136 1.00 18.14 ? 190 HIS B O   1 
ATOM   3265 C CB  . HIS B 1 212 ? 2.486   54.310 -26.105 1.00 16.45 ? 190 HIS B CB  1 
ATOM   3266 C CG  . HIS B 1 212 ? 2.046   54.695 -24.719 1.00 19.26 ? 190 HIS B CG  1 
ATOM   3267 N ND1 . HIS B 1 212 ? 2.128   55.984 -24.228 1.00 18.54 ? 190 HIS B ND1 1 
ATOM   3268 C CD2 . HIS B 1 212 ? 1.461   53.957 -23.738 1.00 18.73 ? 190 HIS B CD2 1 
ATOM   3269 C CE1 . HIS B 1 212 ? 1.642   56.018 -22.998 1.00 19.36 ? 190 HIS B CE1 1 
ATOM   3270 N NE2 . HIS B 1 212 ? 1.226   54.799 -22.679 1.00 14.77 ? 190 HIS B NE2 1 
ATOM   3271 N N   . PHE B 1 213 ? 0.281   52.579 -26.800 1.00 18.26 ? 191 PHE B N   1 
ATOM   3272 C CA  . PHE B 1 213 ? -0.862  51.699 -26.606 1.00 16.98 ? 191 PHE B CA  1 
ATOM   3273 C C   . PHE B 1 213 ? -0.638  50.863 -25.361 1.00 18.55 ? 191 PHE B C   1 
ATOM   3274 O O   . PHE B 1 213 ? 0.505   50.622 -24.969 1.00 18.15 ? 191 PHE B O   1 
ATOM   3275 C CB  . PHE B 1 213 ? -1.066  50.774 -27.807 1.00 18.55 ? 191 PHE B CB  1 
ATOM   3276 C CG  . PHE B 1 213 ? -1.312  51.510 -29.081 1.00 19.60 ? 191 PHE B CG  1 
ATOM   3277 C CD1 . PHE B 1 213 ? -2.596  51.909 -29.426 1.00 22.02 ? 191 PHE B CD1 1 
ATOM   3278 C CD2 . PHE B 1 213 ? -0.257  51.854 -29.910 1.00 23.45 ? 191 PHE B CD2 1 
ATOM   3279 C CE1 . PHE B 1 213 ? -2.818  52.610 -30.595 1.00 26.24 ? 191 PHE B CE1 1 
ATOM   3280 C CE2 . PHE B 1 213 ? -0.473  52.554 -31.073 1.00 27.49 ? 191 PHE B CE2 1 
ATOM   3281 C CZ  . PHE B 1 213 ? -1.754  52.934 -31.419 1.00 29.26 ? 191 PHE B CZ  1 
ATOM   3282 N N   . VAL B 1 214 ? -1.732  50.428 -24.736 1.00 15.97 ? 192 VAL B N   1 
ATOM   3283 C CA  . VAL B 1 214 ? -1.664  49.462 -23.640 1.00 16.11 ? 192 VAL B CA  1 
ATOM   3284 C C   . VAL B 1 214 ? -2.652  48.341 -23.941 1.00 22.12 ? 192 VAL B C   1 
ATOM   3285 O O   . VAL B 1 214 ? -3.863  48.581 -24.048 1.00 17.47 ? 192 VAL B O   1 
ATOM   3286 C CB  . VAL B 1 214 ? -1.949  50.098 -22.269 1.00 15.82 ? 192 VAL B CB  1 
ATOM   3287 C CG1 . VAL B 1 214 ? -1.836  49.040 -21.149 1.00 14.88 ? 192 VAL B CG1 1 
ATOM   3288 C CG2 . VAL B 1 214 ? -0.974  51.246 -21.989 1.00 17.27 ? 192 VAL B CG2 1 
ATOM   3289 N N   . ASP B 1 215 ? -2.132  47.124 -24.115 1.00 17.88 ? 193 ASP B N   1 
ATOM   3290 C CA  . ASP B 1 215 ? -2.979  45.944 -24.271 1.00 16.01 ? 193 ASP B CA  1 
ATOM   3291 C C   . ASP B 1 215 ? -3.447  45.499 -22.895 1.00 18.12 ? 193 ASP B C   1 
ATOM   3292 O O   . ASP B 1 215 ? -2.635  45.412 -21.970 1.00 18.71 ? 193 ASP B O   1 
ATOM   3293 C CB  . ASP B 1 215 ? -2.212  44.801 -24.948 1.00 17.01 ? 193 ASP B CB  1 
ATOM   3294 C CG  . ASP B 1 215 ? -1.924  45.063 -26.406 1.00 29.09 ? 193 ASP B CG  1 
ATOM   3295 O OD1 . ASP B 1 215 ? -2.540  45.983 -26.982 1.00 21.07 ? 193 ASP B OD1 1 
ATOM   3296 O OD2 . ASP B 1 215 ? -1.082  44.337 -26.983 1.00 23.08 ? 193 ASP B OD2 1 
ATOM   3297 N N   . HIS B 1 216 ? -4.747  45.223 -22.751 1.00 16.40 ? 194 HIS B N   1 
ATOM   3298 C CA  . HIS B 1 216 ? -5.314  44.772 -21.481 1.00 13.95 ? 194 HIS B CA  1 
ATOM   3299 C C   . HIS B 1 216 ? -6.041  43.447 -21.649 1.00 19.59 ? 194 HIS B C   1 
ATOM   3300 O O   . HIS B 1 216 ? -6.718  43.221 -22.659 1.00 18.80 ? 194 HIS B O   1 
ATOM   3301 C CB  . HIS B 1 216 ? -6.374  45.730 -20.910 1.00 12.86 ? 194 HIS B CB  1 
ATOM   3302 C CG  . HIS B 1 216 ? -5.898  47.117 -20.609 1.00 13.60 ? 194 HIS B CG  1 
ATOM   3303 N ND1 . HIS B 1 216 ? -5.438  47.498 -19.366 1.00 15.10 ? 194 HIS B ND1 1 
ATOM   3304 C CD2 . HIS B 1 216 ? -5.918  48.242 -21.362 1.00 19.48 ? 194 HIS B CD2 1 
ATOM   3305 C CE1 . HIS B 1 216 ? -5.136  48.785 -19.384 1.00 15.40 ? 194 HIS B CE1 1 
ATOM   3306 N NE2 . HIS B 1 216 ? -5.432  49.265 -20.581 1.00 17.73 ? 194 HIS B NE2 1 
ATOM   3307 N N   . CYS B 1 217 ? -5.963  42.606 -20.625 1.00 17.40 ? 195 CYS B N   1 
ATOM   3308 C CA  . CYS B 1 217 ? -6.955  41.557 -20.446 1.00 16.91 ? 195 CYS B CA  1 
ATOM   3309 C C   . CYS B 1 217 ? -7.340  41.549 -18.974 1.00 17.04 ? 195 CYS B C   1 
ATOM   3310 O O   . CYS B 1 217 ? -6.520  41.870 -18.104 1.00 15.91 ? 195 CYS B O   1 
ATOM   3311 C CB  . CYS B 1 217 ? -6.449  40.183 -20.937 1.00 21.52 ? 195 CYS B CB  1 
ATOM   3312 S SG  . CYS B 1 217 ? -5.126  39.432 -19.983 1.00 24.72 ? 195 CYS B SG  1 
ATOM   3313 N N   . ILE B 1 218 ? -8.609  41.258 -18.708 1.00 17.24 ? 196 ILE B N   1 
ATOM   3314 C CA  . ILE B 1 218 ? -9.152  41.269 -17.354 1.00 18.48 ? 196 ILE B CA  1 
ATOM   3315 C C   . ILE B 1 218 ? -10.090 40.074 -17.216 1.00 17.95 ? 196 ILE B C   1 
ATOM   3316 O O   . ILE B 1 218 ? -10.839 39.748 -18.142 1.00 18.81 ? 196 ILE B O   1 
ATOM   3317 C CB  . ILE B 1 218 ? -9.862  42.611 -17.042 1.00 14.75 ? 196 ILE B CB  1 
ATOM   3318 C CG1 . ILE B 1 218 ? -10.253 42.702 -15.564 1.00 16.90 ? 196 ILE B CG1 1 
ATOM   3319 C CG2 . ILE B 1 218 ? -11.081 42.852 -17.975 1.00 15.74 ? 196 ILE B CG2 1 
ATOM   3320 C CD1 . ILE B 1 218 ? -10.747 44.111 -15.180 1.00 17.51 ? 196 ILE B CD1 1 
ATOM   3321 N N   . GLU B 1 219 ? -10.040 39.413 -16.058 1.00 16.10 ? 197 GLU B N   1 
ATOM   3322 C CA  . GLU B 1 219 ? -10.684 38.112 -15.901 1.00 15.65 ? 197 GLU B CA  1 
ATOM   3323 C C   . GLU B 1 219 ? -11.210 37.994 -14.482 1.00 17.94 ? 197 GLU B C   1 
ATOM   3324 O O   . GLU B 1 219 ? -10.460 38.218 -13.523 1.00 17.79 ? 197 GLU B O   1 
ATOM   3325 C CB  . GLU B 1 219 ? -9.681  36.978 -16.188 1.00 19.14 ? 197 GLU B CB  1 
ATOM   3326 C CG  . GLU B 1 219 ? -10.230 35.555 -15.994 1.00 26.95 ? 197 GLU B CG  1 
ATOM   3327 C CD  . GLU B 1 219 ? -10.881 34.964 -17.245 1.00 31.26 ? 197 GLU B CD  1 
ATOM   3328 O OE1 . GLU B 1 219 ? -10.958 35.659 -18.279 1.00 37.19 ? 197 GLU B OE1 1 
ATOM   3329 O OE2 . GLU B 1 219 ? -11.296 33.787 -17.188 1.00 24.50 ? 197 GLU B OE2 1 
ATOM   3330 N N   . ILE B 1 220 ? -12.480 37.630 -14.338 1.00 15.87 ? 198 ILE B N   1 
ATOM   3331 C CA  . ILE B 1 220 ? -12.947 37.158 -13.041 1.00 14.80 ? 198 ILE B CA  1 
ATOM   3332 C C   . ILE B 1 220 ? -12.480 35.719 -12.875 1.00 18.96 ? 198 ILE B C   1 
ATOM   3333 O O   . ILE B 1 220 ? -12.857 34.825 -13.648 1.00 19.79 ? 198 ILE B O   1 
ATOM   3334 C CB  . ILE B 1 220 ? -14.473 37.291 -12.908 1.00 18.07 ? 198 ILE B CB  1 
ATOM   3335 C CG1 . ILE B 1 220 ? -14.848 38.783 -12.862 1.00 19.14 ? 198 ILE B CG1 1 
ATOM   3336 C CG2 . ILE B 1 220 ? -14.981 36.518 -11.674 1.00 20.47 ? 198 ILE B CG2 1 
ATOM   3337 C CD1 . ILE B 1 220 ? -16.369 39.072 -12.607 1.00 17.56 ? 198 ILE B CD1 1 
ATOM   3338 N N   . LEU B 1 221 ? -11.615 35.501 -11.883 1.00 21.34 ? 199 LEU B N   1 
ATOM   3339 C CA  . LEU B 1 221 ? -11.068 34.172 -11.624 1.00 18.67 ? 199 LEU B CA  1 
ATOM   3340 C C   . LEU B 1 221 ? -12.046 33.295 -10.860 1.00 23.55 ? 199 LEU B C   1 
ATOM   3341 O O   . LEU B 1 221 ? -12.079 32.066 -11.061 1.00 21.93 ? 199 LEU B O   1 
ATOM   3342 C CB  . LEU B 1 221 ? -9.788  34.307 -10.808 1.00 18.77 ? 199 LEU B CB  1 
ATOM   3343 C CG  . LEU B 1 221 ? -8.742  35.276 -11.343 1.00 22.28 ? 199 LEU B CG  1 
ATOM   3344 C CD1 . LEU B 1 221 ? -7.531  35.235 -10.419 1.00 23.40 ? 199 LEU B CD1 1 
ATOM   3345 C CD2 . LEU B 1 221 ? -8.357  34.915 -12.784 1.00 23.62 ? 199 LEU B CD2 1 
ATOM   3346 N N   . SER B 1 222 ? -12.817 33.908 -9.964  1.00 19.42 ? 200 SER B N   1 
ATOM   3347 C CA  . SER B 1 222 ? -13.697 33.203 -9.043  1.00 23.25 ? 200 SER B CA  1 
ATOM   3348 C C   . SER B 1 222 ? -14.753 34.176 -8.545  1.00 22.49 ? 200 SER B C   1 
ATOM   3349 O O   . SER B 1 222 ? -14.544 35.388 -8.536  1.00 21.33 ? 200 SER B O   1 
ATOM   3350 C CB  . SER B 1 222 ? -12.916 32.627 -7.859  1.00 25.87 ? 200 SER B CB  1 
ATOM   3351 O OG  . SER B 1 222 ? -13.650 31.583 -7.247  1.00 30.81 ? 200 SER B OG  1 
ATOM   3352 N N   . HIS B 1 223 ? -15.882 33.627 -8.106  1.00 23.21 ? 201 HIS B N   1 
ATOM   3353 C CA  . HIS B 1 223 ? -16.958 34.435 -7.542  1.00 21.77 ? 201 HIS B CA  1 
ATOM   3354 C C   . HIS B 1 223 ? -17.863 33.502 -6.760  1.00 26.92 ? 201 HIS B C   1 
ATOM   3355 O O   . HIS B 1 223 ? -17.913 32.312 -7.051  1.00 30.05 ? 201 HIS B O   1 
ATOM   3356 C CB  . HIS B 1 223 ? -17.759 35.138 -8.646  1.00 20.23 ? 201 HIS B CB  1 
ATOM   3357 C CG  . HIS B 1 223 ? -18.460 34.178 -9.556  1.00 27.75 ? 201 HIS B CG  1 
ATOM   3358 N ND1 . HIS B 1 223 ? -19.750 33.751 -9.331  1.00 29.37 ? 201 HIS B ND1 1 
ATOM   3359 C CD2 . HIS B 1 223 ? -18.033 33.519 -10.661 1.00 25.82 ? 201 HIS B CD2 1 
ATOM   3360 C CE1 . HIS B 1 223 ? -20.097 32.887 -10.269 1.00 31.67 ? 201 HIS B CE1 1 
ATOM   3361 N NE2 . HIS B 1 223 ? -19.072 32.729 -11.090 1.00 32.65 ? 201 HIS B NE2 1 
ATOM   3362 N N   . ASP B 1 224 ? -18.579 34.041 -5.773  1.00 25.69 ? 202 ASP B N   1 
ATOM   3363 C CA  . ASP B 1 224 ? -19.616 33.272 -5.105  1.00 24.33 ? 202 ASP B CA  1 
ATOM   3364 C C   . ASP B 1 224 ? -20.929 33.494 -5.860  1.00 26.28 ? 202 ASP B C   1 
ATOM   3365 O O   . ASP B 1 224 ? -20.969 34.176 -6.886  1.00 27.49 ? 202 ASP B O   1 
ATOM   3366 C CB  . ASP B 1 224 ? -19.680 33.628 -3.616  1.00 25.65 ? 202 ASP B CB  1 
ATOM   3367 C CG  . ASP B 1 224 ? -20.178 35.048 -3.347  1.00 33.43 ? 202 ASP B CG  1 
ATOM   3368 O OD1 . ASP B 1 224 ? -20.447 35.810 -4.301  1.00 27.60 ? 202 ASP B OD1 1 
ATOM   3369 O OD2 . ASP B 1 224 ? -20.291 35.398 -2.147  1.00 34.74 ? 202 ASP B OD2 1 
ATOM   3370 N N   . LYS B 1 225 ? -22.024 32.963 -5.328  1.00 29.17 ? 203 LYS B N   1 
ATOM   3371 C CA  . LYS B 1 225 ? -23.245 32.804 -6.115  1.00 27.95 ? 203 LYS B CA  1 
ATOM   3372 C C   . LYS B 1 225 ? -23.797 34.155 -6.556  1.00 30.30 ? 203 LYS B C   1 
ATOM   3373 O O   . LYS B 1 225 ? -24.149 34.343 -7.726  1.00 32.15 ? 203 LYS B O   1 
ATOM   3374 C CB  . LYS B 1 225 ? -24.310 32.042 -5.314  1.00 34.54 ? 203 LYS B CB  1 
ATOM   3375 C CG  . LYS B 1 225 ? -23.850 31.148 -4.120  1.00 63.02 ? 203 LYS B CG  1 
ATOM   3376 C CD  . LYS B 1 225 ? -22.485 30.427 -4.234  1.00 45.81 ? 203 LYS B CD  1 
ATOM   3377 C CE  . LYS B 1 225 ? -22.028 29.964 -2.855  1.00 65.86 ? 203 LYS B CE  1 
ATOM   3378 N NZ  . LYS B 1 225 ? -21.804 31.114 -1.925  1.00 52.13 ? 203 LYS B NZ  1 
ATOM   3379 N N   . ASP B 1 226 ? -23.879 35.109 -5.630  1.00 31.48 ? 204 ASP B N   1 
ATOM   3380 C CA  . ASP B 1 226 ? -24.432 36.426 -5.922  1.00 35.55 ? 204 ASP B CA  1 
ATOM   3381 C C   . ASP B 1 226 ? -23.368 37.466 -6.247  1.00 26.78 ? 204 ASP B C   1 
ATOM   3382 O O   . ASP B 1 226 ? -23.682 38.658 -6.313  1.00 27.12 ? 204 ASP B O   1 
ATOM   3383 C CB  . ASP B 1 226 ? -25.282 36.912 -4.749  1.00 34.23 ? 204 ASP B CB  1 
ATOM   3384 C CG  . ASP B 1 226 ? -26.503 36.049 -4.524  1.00 44.65 ? 204 ASP B CG  1 
ATOM   3385 O OD1 . ASP B 1 226 ? -27.167 35.700 -5.519  1.00 43.18 ? 204 ASP B OD1 1 
ATOM   3386 O OD2 . ASP B 1 226 ? -26.810 35.744 -3.356  1.00 43.49 ? 204 ASP B OD2 1 
ATOM   3387 N N   . TYR B 1 227 ? -22.119 37.054 -6.435  1.00 25.89 ? 205 TYR B N   1 
ATOM   3388 C CA  . TYR B 1 227 ? -21.029 37.995 -6.688  1.00 21.04 ? 205 TYR B CA  1 
ATOM   3389 C C   . TYR B 1 227 ? -20.864 38.974 -5.530  1.00 25.26 ? 205 TYR B C   1 
ATOM   3390 O O   . TYR B 1 227 ? -20.482 40.132 -5.722  1.00 24.53 ? 205 TYR B O   1 
ATOM   3391 C CB  . TYR B 1 227 ? -21.239 38.757 -8.005  1.00 23.71 ? 205 TYR B CB  1 
ATOM   3392 C CG  . TYR B 1 227 ? -21.093 37.896 -9.242  1.00 24.67 ? 205 TYR B CG  1 
ATOM   3393 C CD1 . TYR B 1 227 ? -22.074 36.976 -9.588  1.00 26.78 ? 205 TYR B CD1 1 
ATOM   3394 C CD2 . TYR B 1 227 ? -19.986 38.019 -10.075 1.00 28.62 ? 205 TYR B CD2 1 
ATOM   3395 C CE1 . TYR B 1 227 ? -21.951 36.184 -10.724 1.00 32.65 ? 205 TYR B CE1 1 
ATOM   3396 C CE2 . TYR B 1 227 ? -19.854 37.234 -11.210 1.00 25.92 ? 205 TYR B CE2 1 
ATOM   3397 C CZ  . TYR B 1 227 ? -20.840 36.324 -11.528 1.00 31.97 ? 205 TYR B CZ  1 
ATOM   3398 O OH  . TYR B 1 227 ? -20.714 35.534 -12.650 1.00 33.40 ? 205 TYR B OH  1 
ATOM   3399 N N   . ASN B 1 228 ? -21.179 38.541 -4.310  1.00 22.08 ? 206 ASN B N   1 
ATOM   3400 C CA  . ASN B 1 228 ? -20.773 39.342 -3.164  1.00 23.12 ? 206 ASN B CA  1 
ATOM   3401 C C   . ASN B 1 228 ? -19.267 39.241 -2.938  1.00 22.20 ? 206 ASN B C   1 
ATOM   3402 O O   . ASN B 1 228 ? -18.683 40.125 -2.308  1.00 24.11 ? 206 ASN B O   1 
ATOM   3403 C CB  . ASN B 1 228 ? -21.532 38.913 -1.899  1.00 28.67 ? 206 ASN B CB  1 
ATOM   3404 C CG  . ASN B 1 228 ? -23.022 39.263 -1.958  1.00 35.14 ? 206 ASN B CG  1 
ATOM   3405 O OD1 . ASN B 1 228 ? -23.399 40.357 -2.367  1.00 30.31 ? 206 ASN B OD1 1 
ATOM   3406 N ND2 . ASN B 1 228 ? -23.864 38.339 -1.529  1.00 32.31 ? 206 ASN B ND2 1 
ATOM   3407 N N   . LYS B 1 229 ? -18.643 38.166 -3.411  1.00 21.59 ? 207 LYS B N   1 
ATOM   3408 C CA  . LYS B 1 229 ? -17.197 37.989 -3.350  1.00 22.89 ? 207 LYS B CA  1 
ATOM   3409 C C   . LYS B 1 229 ? -16.711 37.630 -4.745  1.00 21.16 ? 207 LYS B C   1 
ATOM   3410 O O   . LYS B 1 229 ? -17.300 36.771 -5.409  1.00 22.98 ? 207 LYS B O   1 
ATOM   3411 C CB  . LYS B 1 229 ? -16.796 36.904 -2.337  1.00 23.57 ? 207 LYS B CB  1 
ATOM   3412 C CG  . LYS B 1 229 ? -17.132 37.262 -0.889  1.00 28.69 ? 207 LYS B CG  1 
ATOM   3413 C CD  . LYS B 1 229 ? -16.865 36.080 0.040   1.00 35.65 ? 207 LYS B CD  1 
ATOM   3414 C CE  . LYS B 1 229 ? -17.330 36.356 1.456   1.00 56.00 ? 207 LYS B CE  1 
ATOM   3415 N NZ  . LYS B 1 229 ? -16.227 36.895 2.297   1.00 60.65 ? 207 LYS B NZ  1 
ATOM   3416 N N   . VAL B 1 230 ? -15.662 38.315 -5.197  1.00 19.07 ? 208 VAL B N   1 
ATOM   3417 C CA  . VAL B 1 230 ? -15.129 38.153 -6.544  1.00 17.79 ? 208 VAL B CA  1 
ATOM   3418 C C   . VAL B 1 230 ? -13.610 38.222 -6.456  1.00 22.06 ? 208 VAL B C   1 
ATOM   3419 O O   . VAL B 1 230 ? -13.064 39.054 -5.726  1.00 21.62 ? 208 VAL B O   1 
ATOM   3420 C CB  . VAL B 1 230 ? -15.664 39.237 -7.519  1.00 16.30 ? 208 VAL B CB  1 
ATOM   3421 C CG1 . VAL B 1 230 ? -14.996 39.096 -8.874  1.00 17.51 ? 208 VAL B CG1 1 
ATOM   3422 C CG2 . VAL B 1 230 ? -17.201 39.141 -7.684  1.00 17.80 ? 208 VAL B CG2 1 
ATOM   3423 N N   . LYS B 1 231 ? -12.928 37.326 -7.172  1.00 17.96 ? 209 LYS B N   1 
ATOM   3424 C CA  . LYS B 1 231 ? -11.490 37.424 -7.393  1.00 18.35 ? 209 LYS B CA  1 
ATOM   3425 C C   . LYS B 1 231 ? -11.245 37.859 -8.829  1.00 21.08 ? 209 LYS B C   1 
ATOM   3426 O O   . LYS B 1 231 ? -11.772 37.246 -9.763  1.00 18.40 ? 209 LYS B O   1 
ATOM   3427 C CB  . LYS B 1 231 ? -10.783 36.096 -7.097  1.00 22.49 ? 209 LYS B CB  1 
ATOM   3428 C CG  . LYS B 1 231 ? -9.283  36.137 -7.417  1.00 34.50 ? 209 LYS B CG  1 
ATOM   3429 C CD  . LYS B 1 231 ? -8.392  36.099 -6.194  1.00 39.37 ? 209 LYS B CD  1 
ATOM   3430 C CE  . LYS B 1 231 ? -8.673  34.901 -5.303  1.00 47.06 ? 209 LYS B CE  1 
ATOM   3431 N NZ  . LYS B 1 231 ? -7.999  35.091 -3.990  1.00 45.27 ? 209 LYS B NZ  1 
ATOM   3432 N N   . LEU B 1 232 ? -10.450 38.923 -8.996  1.00 18.30 ? 210 LEU B N   1 
ATOM   3433 C CA  . LEU B 1 232 ? -10.271 39.613 -10.265 1.00 15.43 ? 210 LEU B CA  1 
ATOM   3434 C C   . LEU B 1 232 ? -8.788  39.664 -10.606 1.00 15.02 ? 210 LEU B C   1 
ATOM   3435 O O   . LEU B 1 232 ? -7.945  39.756 -9.710  1.00 18.65 ? 210 LEU B O   1 
ATOM   3436 C CB  . LEU B 1 232 ? -10.838 41.048 -10.180 1.00 16.19 ? 210 LEU B CB  1 
ATOM   3437 C CG  . LEU B 1 232 ? -10.935 41.856 -11.473 1.00 18.27 ? 210 LEU B CG  1 
ATOM   3438 C CD1 . LEU B 1 232 ? -11.962 41.236 -12.388 1.00 18.18 ? 210 LEU B CD1 1 
ATOM   3439 C CD2 . LEU B 1 232 ? -11.285 43.308 -11.164 1.00 17.76 ? 210 LEU B CD2 1 
ATOM   3440 N N   . TYR B 1 233 ? -8.468  39.601 -11.904 1.00 14.64 ? 211 TYR B N   1 
ATOM   3441 C CA  . TYR B 1 233 ? -7.085  39.648 -12.382 1.00 15.69 ? 211 TYR B CA  1 
ATOM   3442 C C   . TYR B 1 233 ? -6.978  40.530 -13.620 1.00 18.06 ? 211 TYR B C   1 
ATOM   3443 O O   . TYR B 1 233 ? -7.867  40.515 -14.471 1.00 18.93 ? 211 TYR B O   1 
ATOM   3444 C CB  . TYR B 1 233 ? -6.577  38.246 -12.743 1.00 19.31 ? 211 TYR B CB  1 
ATOM   3445 C CG  . TYR B 1 233 ? -5.203  38.189 -13.394 1.00 15.62 ? 211 TYR B CG  1 
ATOM   3446 C CD1 . TYR B 1 233 ? -4.033  38.373 -12.648 1.00 20.20 ? 211 TYR B CD1 1 
ATOM   3447 C CD2 . TYR B 1 233 ? -5.078  37.925 -14.758 1.00 17.85 ? 211 TYR B CD2 1 
ATOM   3448 C CE1 . TYR B 1 233 ? -2.772  38.286 -13.257 1.00 22.57 ? 211 TYR B CE1 1 
ATOM   3449 C CE2 . TYR B 1 233 ? -3.834  37.849 -15.382 1.00 17.74 ? 211 TYR B CE2 1 
ATOM   3450 C CZ  . TYR B 1 233 ? -2.684  38.033 -14.625 1.00 23.44 ? 211 TYR B CZ  1 
ATOM   3451 O OH  . TYR B 1 233 ? -1.449  37.933 -15.235 1.00 23.70 ? 211 TYR B OH  1 
ATOM   3452 N N   . GLU B 1 234 ? -5.863  41.252 -13.758 1.00 13.31 ? 212 GLU B N   1 
ATOM   3453 C CA  . GLU B 1 234 ? -5.631  42.007 -14.987 1.00 15.08 ? 212 GLU B CA  1 
ATOM   3454 C C   . GLU B 1 234 ? -4.173  41.866 -15.380 1.00 19.30 ? 212 GLU B C   1 
ATOM   3455 O O   . GLU B 1 234 ? -3.293  41.794 -14.513 1.00 17.27 ? 212 GLU B O   1 
ATOM   3456 C CB  . GLU B 1 234 ? -6.038  43.491 -14.803 1.00 15.73 ? 212 GLU B CB  1 
ATOM   3457 C CG  . GLU B 1 234 ? -6.162  44.368 -16.048 1.00 21.82 ? 212 GLU B CG  1 
ATOM   3458 C CD  . GLU B 1 234 ? -5.488  45.739 -15.890 1.00 26.14 ? 212 GLU B CD  1 
ATOM   3459 O OE1 . GLU B 1 234 ? -5.513  46.270 -14.758 1.00 24.24 ? 212 GLU B OE1 1 
ATOM   3460 O OE2 . GLU B 1 234 ? -5.071  46.355 -16.891 1.00 25.57 ? 212 GLU B OE2 1 
ATOM   3461 N N   . HIS B 1 235 ? -3.934  41.786 -16.693 1.00 17.48 ? 213 HIS B N   1 
ATOM   3462 C CA  . HIS B 1 235 ? -2.588  41.778 -17.266 1.00 17.76 ? 213 HIS B CA  1 
ATOM   3463 C C   . HIS B 1 235 ? -2.533  42.872 -18.328 1.00 14.78 ? 213 HIS B C   1 
ATOM   3464 O O   . HIS B 1 235 ? -3.365  42.888 -19.237 1.00 17.51 ? 213 HIS B O   1 
ATOM   3465 C CB  . HIS B 1 235 ? -2.252  40.406 -17.864 1.00 21.23 ? 213 HIS B CB  1 
ATOM   3466 C CG  . HIS B 1 235 ? -0.857  40.301 -18.404 1.00 21.35 ? 213 HIS B CG  1 
ATOM   3467 N ND1 . HIS B 1 235 ? -0.499  39.380 -19.367 1.00 22.47 ? 213 HIS B ND1 1 
ATOM   3468 C CD2 . HIS B 1 235 ? 0.263   41.014 -18.130 1.00 19.50 ? 213 HIS B CD2 1 
ATOM   3469 C CE1 . HIS B 1 235 ? 0.789   39.516 -19.648 1.00 24.06 ? 213 HIS B CE1 1 
ATOM   3470 N NE2 . HIS B 1 235 ? 1.275   40.501 -18.910 1.00 23.52 ? 213 HIS B NE2 1 
ATOM   3471 N N   . ALA B 1 236 ? -1.584  43.805 -18.202 1.00 16.36 ? 214 ALA B N   1 
ATOM   3472 C CA  . ALA B 1 236 ? -1.491  44.931 -19.130 1.00 12.95 ? 214 ALA B CA  1 
ATOM   3473 C C   . ALA B 1 236 ? -0.049  45.133 -19.559 1.00 13.71 ? 214 ALA B C   1 
ATOM   3474 O O   . ALA B 1 236 ? 0.856   45.094 -18.721 1.00 17.77 ? 214 ALA B O   1 
ATOM   3475 C CB  . ALA B 1 236 ? -2.020  46.233 -18.492 1.00 15.14 ? 214 ALA B CB  1 
ATOM   3476 N N   . VAL B 1 237 ? 0.158   45.384 -20.861 1.00 15.77 ? 215 VAL B N   1 
ATOM   3477 C CA  . VAL B 1 237 ? 1.488   45.574 -21.442 1.00 15.58 ? 215 VAL B CA  1 
ATOM   3478 C C   . VAL B 1 237 ? 1.424   46.751 -22.402 1.00 17.22 ? 215 VAL B C   1 
ATOM   3479 O O   . VAL B 1 237 ? 0.596   46.756 -23.324 1.00 19.53 ? 215 VAL B O   1 
ATOM   3480 C CB  . VAL B 1 237 ? 1.980   44.319 -22.195 1.00 17.35 ? 215 VAL B CB  1 
ATOM   3481 C CG1 . VAL B 1 237 ? 3.357   44.569 -22.845 1.00 17.83 ? 215 VAL B CG1 1 
ATOM   3482 C CG2 . VAL B 1 237 ? 2.005   43.082 -21.280 1.00 20.28 ? 215 VAL B CG2 1 
ATOM   3483 N N   . ALA B 1 238 ? 2.313   47.728 -22.213 1.00 17.20 ? 216 ALA B N   1 
ATOM   3484 C CA  . ALA B 1 238 ? 2.387   48.871 -23.117 1.00 19.83 ? 216 ALA B CA  1 
ATOM   3485 C C   . ALA B 1 238 ? 3.258   48.532 -24.317 1.00 21.82 ? 216 ALA B C   1 
ATOM   3486 O O   . ALA B 1 238 ? 4.205   47.747 -24.216 1.00 22.09 ? 216 ALA B O   1 
ATOM   3487 C CB  . ALA B 1 238 ? 2.948   50.105 -22.400 1.00 16.57 ? 216 ALA B CB  1 
ATOM   3488 N N   . HIS B 1 239 ? 2.931   49.128 -25.463 1.00 17.82 ? 217 HIS B N   1 
ATOM   3489 C CA  . HIS B 1 239 ? 3.740   48.956 -26.663 1.00 19.13 ? 217 HIS B CA  1 
ATOM   3490 C C   . HIS B 1 239 ? 3.572   50.192 -27.538 1.00 17.97 ? 217 HIS B C   1 
ATOM   3491 O O   . HIS B 1 239 ? 2.585   50.919 -27.432 1.00 20.42 ? 217 HIS B O   1 
ATOM   3492 C CB  . HIS B 1 239 ? 3.369   47.665 -27.421 1.00 21.93 ? 217 HIS B CB  1 
ATOM   3493 C CG  . HIS B 1 239 ? 1.933   47.586 -27.852 1.00 24.07 ? 217 HIS B CG  1 
ATOM   3494 N ND1 . HIS B 1 239 ? 1.521   47.925 -29.126 1.00 28.56 ? 217 HIS B ND1 1 
ATOM   3495 C CD2 . HIS B 1 239 ? 0.817   47.193 -27.187 1.00 22.79 ? 217 HIS B CD2 1 
ATOM   3496 C CE1 . HIS B 1 239 ? 0.214   47.742 -29.227 1.00 24.29 ? 217 HIS B CE1 1 
ATOM   3497 N NE2 . HIS B 1 239 ? -0.238  47.307 -28.062 1.00 26.83 ? 217 HIS B NE2 1 
ATOM   3498 N N   . SER B 1 240 ? 4.562   50.445 -28.392 1.00 21.34 ? 218 SER B N   1 
ATOM   3499 C CA  . SER B 1 240 ? 4.617   51.713 -29.106 1.00 31.36 ? 218 SER B CA  1 
ATOM   3500 C C   . SER B 1 240 ? 4.046   51.652 -30.513 1.00 35.68 ? 218 SER B C   1 
ATOM   3501 O O   . SER B 1 240 ? 3.593   52.683 -31.028 1.00 39.88 ? 218 SER B O   1 
ATOM   3502 C CB  . SER B 1 240 ? 6.066   52.211 -29.182 1.00 30.22 ? 218 SER B CB  1 
ATOM   3503 O OG  . SER B 1 240 ? 6.840   51.303 -29.941 1.00 38.82 ? 218 SER B OG  1 
ATOM   3504 N N   . GLY B 1 241 ? 4.081   50.492 -31.157 1.00 32.72 ? 219 GLY B N   1 
ATOM   3505 C CA  . GLY B 1 241 ? 3.629   50.382 -32.536 1.00 51.34 ? 219 GLY B CA  1 
ATOM   3506 C C   . GLY B 1 241 ? 2.136   50.142 -32.630 1.00 45.17 ? 219 GLY B C   1 
ATOM   3507 O O   . GLY B 1 241 ? 1.519   49.722 -31.644 1.00 41.44 ? 219 GLY B O   1 
HETATM 3508 S S1  . DTT C 2 .   ? -6.415  32.082 -18.901 1.00 23.48 ? 301 DTT B S1  1 
HETATM 3509 C C1  . DTT C 2 .   ? -6.532  33.905 -18.691 1.00 30.84 ? 301 DTT B C1  1 
HETATM 3510 C C2  . DTT C 2 .   ? -6.169  34.748 -19.915 1.00 45.03 ? 301 DTT B C2  1 
HETATM 3511 O O2  . DTT C 2 .   ? -4.812  34.578 -20.236 1.00 43.80 ? 301 DTT B O2  1 
HETATM 3512 C C3  . DTT C 2 .   ? -6.410  36.251 -19.723 1.00 33.42 ? 301 DTT B C3  1 
HETATM 3513 O O3  . DTT C 2 .   ? -7.775  36.456 -19.467 1.00 50.68 ? 301 DTT B O3  1 
HETATM 3514 C C4  . DTT C 2 .   ? -5.598  36.851 -18.587 1.00 39.89 ? 301 DTT B C4  1 
HETATM 3515 S S4  . DTT C 2 .   ? -5.966  38.623 -18.350 1.00 25.77 ? 301 DTT B S4  1 
HETATM 3516 O O   . HOH D 3 .   ? -2.547  18.781 -33.386 1.00 47.59 ? 301 HOH A O   1 
HETATM 3517 O O   . HOH D 3 .   ? 1.555   39.484 -7.187  1.00 30.00 ? 302 HOH A O   1 
HETATM 3518 O O   . HOH D 3 .   ? -4.362  28.361 -1.516  1.00 41.17 ? 303 HOH A O   1 
HETATM 3519 O O   . HOH D 3 .   ? -2.954  35.552 -24.049 1.00 40.93 ? 304 HOH A O   1 
HETATM 3520 O O   . HOH D 3 .   ? -6.749  21.475 -16.372 1.00 14.81 ? 305 HOH A O   1 
HETATM 3521 O O   . HOH D 3 .   ? 14.046  33.826 -11.765 1.00 39.04 ? 306 HOH A O   1 
HETATM 3522 O O   . HOH D 3 .   ? -2.577  28.155 -23.208 1.00 16.85 ? 307 HOH A O   1 
HETATM 3523 O O   . HOH D 3 .   ? -16.196 29.544 -18.866 1.00 28.96 ? 308 HOH A O   1 
HETATM 3524 O O   . HOH D 3 .   ? -20.731 25.660 -3.927  1.00 37.38 ? 309 HOH A O   1 
HETATM 3525 O O   . HOH D 3 .   ? 9.011   28.150 -33.493 1.00 40.63 ? 310 HOH A O   1 
HETATM 3526 O O   . HOH D 3 .   ? 3.641   21.734 1.466   1.00 47.82 ? 311 HOH A O   1 
HETATM 3527 O O   . HOH D 3 .   ? -9.152  6.244  -22.934 1.00 28.79 ? 312 HOH A O   1 
HETATM 3528 O O   . HOH D 3 .   ? 3.206   17.910 -35.187 1.00 44.85 ? 313 HOH A O   1 
HETATM 3529 O O   . HOH D 3 .   ? 12.053  29.777 -31.402 1.00 46.02 ? 314 HOH A O   1 
HETATM 3530 O O   . HOH D 3 .   ? -11.509 11.599 2.830   1.00 43.35 ? 315 HOH A O   1 
HETATM 3531 O O   . HOH D 3 .   ? -7.725  24.068 -1.419  1.00 31.32 ? 316 HOH A O   1 
HETATM 3532 O O   . HOH D 3 .   ? 3.727   27.880 2.666   1.00 48.21 ? 317 HOH A O   1 
HETATM 3533 O O   . HOH D 3 .   ? -13.955 6.466  -13.300 1.00 24.49 ? 318 HOH A O   1 
HETATM 3534 O O   . HOH D 3 .   ? -2.239  33.296 -20.576 1.00 27.52 ? 319 HOH A O   1 
HETATM 3535 O O   . HOH D 3 .   ? -5.979  4.393  -35.766 1.00 41.83 ? 320 HOH A O   1 
HETATM 3536 O O   . HOH D 3 .   ? -3.202  17.235 -24.801 1.00 20.29 ? 321 HOH A O   1 
HETATM 3537 O O   . HOH D 3 .   ? 2.604   29.695 -3.447  1.00 27.80 ? 322 HOH A O   1 
HETATM 3538 O O   . HOH D 3 .   ? -18.888 6.816  -27.371 1.00 34.27 ? 323 HOH A O   1 
HETATM 3539 O O   . HOH D 3 .   ? 14.866  25.030 -24.524 1.00 21.20 ? 324 HOH A O   1 
HETATM 3540 O O   . HOH D 3 .   ? -14.506 27.658 -5.842  1.00 28.37 ? 325 HOH A O   1 
HETATM 3541 O O   . HOH D 3 .   ? -22.099 17.337 -21.126 1.00 31.96 ? 326 HOH A O   1 
HETATM 3542 O O   . HOH D 3 .   ? -1.257  36.195 -26.871 1.00 36.81 ? 327 HOH A O   1 
HETATM 3543 O O   . HOH D 3 .   ? 11.436  35.040 -18.778 1.00 33.04 ? 328 HOH A O   1 
HETATM 3544 O O   . HOH D 3 .   ? -7.014  18.618 -10.173 1.00 17.74 ? 329 HOH A O   1 
HETATM 3545 O O   . HOH D 3 .   ? -20.448 18.846 -17.877 1.00 27.45 ? 330 HOH A O   1 
HETATM 3546 O O   . HOH D 3 .   ? 16.775  24.784 -22.618 1.00 20.09 ? 331 HOH A O   1 
HETATM 3547 O O   . HOH D 3 .   ? 18.767  12.143 -21.940 1.00 46.69 ? 332 HOH A O   1 
HETATM 3548 O O   . HOH D 3 .   ? -11.585 8.905  -6.085  1.00 27.56 ? 333 HOH A O   1 
HETATM 3549 O O   . HOH D 3 .   ? 11.103  9.979  -22.787 1.00 51.01 ? 334 HOH A O   1 
HETATM 3550 O O   . HOH D 3 .   ? -7.030  30.482 -5.072  1.00 52.64 ? 335 HOH A O   1 
HETATM 3551 O O   . HOH D 3 .   ? 13.584  29.379 -10.862 1.00 23.90 ? 336 HOH A O   1 
HETATM 3552 O O   . HOH D 3 .   ? -13.144 4.611  -21.063 1.00 37.30 ? 337 HOH A O   1 
HETATM 3553 O O   . HOH D 3 .   ? 4.381   32.545 -17.383 1.00 19.16 ? 338 HOH A O   1 
HETATM 3554 O O   . HOH D 3 .   ? -5.945  20.733 -11.618 1.00 19.03 ? 339 HOH A O   1 
HETATM 3555 O O   . HOH D 3 .   ? -11.933 1.817  -25.016 1.00 43.18 ? 340 HOH A O   1 
HETATM 3556 O O   . HOH D 3 .   ? 16.050  14.337 -16.140 1.00 26.85 ? 341 HOH A O   1 
HETATM 3557 O O   . HOH D 3 .   ? -10.636 33.645 -20.313 1.00 28.75 ? 342 HOH A O   1 
HETATM 3558 O O   . HOH D 3 .   ? -14.945 18.406 -17.624 1.00 18.52 ? 343 HOH A O   1 
HETATM 3559 O O   . HOH D 3 .   ? 18.616  24.588 -7.293  1.00 39.37 ? 344 HOH A O   1 
HETATM 3560 O O   . HOH D 3 .   ? -10.513 29.646 -7.565  1.00 33.01 ? 345 HOH A O   1 
HETATM 3561 O O   . HOH D 3 .   ? -13.860 3.217  -18.682 1.00 37.96 ? 346 HOH A O   1 
HETATM 3562 O O   . HOH D 3 .   ? 15.655  15.079 -28.454 1.00 23.93 ? 347 HOH A O   1 
HETATM 3563 O O   . HOH D 3 .   ? -14.073 34.851 -17.976 1.00 22.16 ? 348 HOH A O   1 
HETATM 3564 O O   . HOH D 3 .   ? 7.550   32.762 -17.511 1.00 24.95 ? 349 HOH A O   1 
HETATM 3565 O O   . HOH D 3 .   ? 1.574   36.934 -28.294 1.00 37.54 ? 350 HOH A O   1 
HETATM 3566 O O   . HOH D 3 .   ? 14.358  25.641 -32.105 1.00 24.75 ? 351 HOH A O   1 
HETATM 3567 O O   . HOH D 3 .   ? 0.096   8.359  -23.616 1.00 39.01 ? 352 HOH A O   1 
HETATM 3568 O O   . HOH D 3 .   ? -18.907 25.867 -25.776 1.00 42.54 ? 353 HOH A O   1 
HETATM 3569 O O   . HOH D 3 .   ? -8.112  9.415  -2.905  1.00 27.78 ? 354 HOH A O   1 
HETATM 3570 O O   . HOH D 3 .   ? 8.091   12.788 -27.216 1.00 32.70 ? 355 HOH A O   1 
HETATM 3571 O O   . HOH D 3 .   ? 18.115  14.114 -18.099 1.00 34.24 ? 356 HOH A O   1 
HETATM 3572 O O   . HOH D 3 .   ? -3.677  15.443 -34.246 1.00 30.78 ? 357 HOH A O   1 
HETATM 3573 O O   . HOH D 3 .   ? -16.863 6.941  -13.349 1.00 29.84 ? 358 HOH A O   1 
HETATM 3574 O O   . HOH D 3 .   ? -9.148  19.716 1.113   1.00 38.92 ? 359 HOH A O   1 
HETATM 3575 O O   . HOH D 3 .   ? -19.884 12.972 -11.644 1.00 51.63 ? 360 HOH A O   1 
HETATM 3576 O O   . HOH D 3 .   ? 3.329   22.684 -19.407 1.00 17.43 ? 361 HOH A O   1 
HETATM 3577 O O   . HOH D 3 .   ? 0.148   27.097 -26.494 1.00 19.79 ? 362 HOH A O   1 
HETATM 3578 O O   . HOH D 3 .   ? -9.905  14.358 2.155   1.00 34.26 ? 363 HOH A O   1 
HETATM 3579 O O   . HOH D 3 .   ? 4.420   15.135 -27.880 1.00 19.59 ? 364 HOH A O   1 
HETATM 3580 O O   . HOH D 3 .   ? -12.999 28.526 -30.520 1.00 40.97 ? 365 HOH A O   1 
HETATM 3581 O O   . HOH D 3 .   ? -15.190 14.490 -22.846 1.00 17.09 ? 366 HOH A O   1 
HETATM 3582 O O   . HOH D 3 .   ? -3.746  7.743  -28.844 1.00 34.12 ? 367 HOH A O   1 
HETATM 3583 O O   . HOH D 3 .   ? 8.376   19.835 -31.322 1.00 17.61 ? 368 HOH A O   1 
HETATM 3584 O O   . HOH D 3 .   ? 5.626   11.108 -6.258  1.00 41.96 ? 369 HOH A O   1 
HETATM 3585 O O   . HOH D 3 .   ? -8.988  22.069 -18.451 1.00 18.66 ? 370 HOH A O   1 
HETATM 3586 O O   . HOH D 3 .   ? 12.307  27.522 -7.703  1.00 25.01 ? 371 HOH A O   1 
HETATM 3587 O O   . HOH D 3 .   ? -16.814 18.472 -33.279 1.00 43.34 ? 372 HOH A O   1 
HETATM 3588 O O   . HOH D 3 .   ? 15.416  17.708 -4.592  1.00 41.69 ? 373 HOH A O   1 
HETATM 3589 O O   . HOH D 3 .   ? -22.133 24.035 -19.735 1.00 31.50 ? 374 HOH A O   1 
HETATM 3590 O O   . HOH D 3 .   ? -6.917  5.300  -15.080 1.00 25.74 ? 375 HOH A O   1 
HETATM 3591 O O   . HOH D 3 .   ? 11.309  31.203 -18.213 1.00 21.18 ? 376 HOH A O   1 
HETATM 3592 O O   . HOH D 3 .   ? -18.636 25.167 -11.172 1.00 20.97 ? 377 HOH A O   1 
HETATM 3593 O O   . HOH D 3 .   ? 2.427   28.991 -17.659 1.00 17.55 ? 378 HOH A O   1 
HETATM 3594 O O   . HOH D 3 .   ? -29.491 19.811 -21.547 1.00 42.77 ? 379 HOH A O   1 
HETATM 3595 O O   . HOH D 3 .   ? -10.244 5.652  -7.019  1.00 46.28 ? 380 HOH A O   1 
HETATM 3596 O O   . HOH D 3 .   ? -16.958 33.472 -14.142 1.00 36.55 ? 381 HOH A O   1 
HETATM 3597 O O   . HOH D 3 .   ? 17.186  26.053 -28.106 1.00 25.88 ? 382 HOH A O   1 
HETATM 3598 O O   . HOH D 3 .   ? 7.723   11.024 -25.093 1.00 44.24 ? 383 HOH A O   1 
HETATM 3599 O O   . HOH D 3 .   ? 17.601  18.847 -6.481  1.00 47.99 ? 384 HOH A O   1 
HETATM 3600 O O   . HOH D 3 .   ? -3.260  31.391 -29.845 1.00 38.61 ? 385 HOH A O   1 
HETATM 3601 O O   . HOH D 3 .   ? -16.764 6.843  -10.445 1.00 27.72 ? 386 HOH A O   1 
HETATM 3602 O O   . HOH D 3 .   ? -6.150  24.613 -9.443  1.00 26.91 ? 387 HOH A O   1 
HETATM 3603 O O   . HOH D 3 .   ? -21.230 29.231 -11.289 1.00 45.77 ? 388 HOH A O   1 
HETATM 3604 O O   . HOH D 3 .   ? 18.483  26.339 -2.352  1.00 51.56 ? 389 HOH A O   1 
HETATM 3605 O O   . HOH D 3 .   ? -4.478  8.051  -5.993  1.00 33.98 ? 390 HOH A O   1 
HETATM 3606 O O   . HOH D 3 .   ? -7.959  29.094 -26.746 1.00 26.48 ? 391 HOH A O   1 
HETATM 3607 O O   . HOH D 3 .   ? -7.257  32.905 -7.681  1.00 38.19 ? 392 HOH A O   1 
HETATM 3608 O O   . HOH D 3 .   ? -4.367  11.087 -34.718 1.00 45.11 ? 393 HOH A O   1 
HETATM 3609 O O   . HOH D 3 .   ? -3.646  22.548 -31.403 1.00 22.29 ? 394 HOH A O   1 
HETATM 3610 O O   . HOH D 3 .   ? -3.417  6.925  -20.459 1.00 38.48 ? 395 HOH A O   1 
HETATM 3611 O O   . HOH D 3 .   ? 12.607  28.184 -34.113 1.00 50.54 ? 396 HOH A O   1 
HETATM 3612 O O   . HOH D 3 .   ? 6.078   34.431 -15.281 1.00 26.23 ? 397 HOH A O   1 
HETATM 3613 O O   . HOH D 3 .   ? 11.768  36.703 -11.205 1.00 39.41 ? 398 HOH A O   1 
HETATM 3614 O O   . HOH D 3 .   ? -3.167  7.064  -17.902 1.00 35.97 ? 399 HOH A O   1 
HETATM 3615 O O   . HOH D 3 .   ? -15.257 32.170 -11.613 1.00 41.43 ? 400 HOH A O   1 
HETATM 3616 O O   . HOH D 3 .   ? 11.588  28.777 -12.766 1.00 26.64 ? 401 HOH A O   1 
HETATM 3617 O O   . HOH D 3 .   ? 1.802   33.173 -17.806 1.00 16.51 ? 402 HOH A O   1 
HETATM 3618 O O   . HOH D 3 .   ? -22.373 19.497 -19.534 1.00 32.61 ? 403 HOH A O   1 
HETATM 3619 O O   . HOH D 3 .   ? 4.947   36.390 -17.830 1.00 34.54 ? 404 HOH A O   1 
HETATM 3620 O O   . HOH D 3 .   ? -2.714  30.828 -22.382 1.00 22.38 ? 405 HOH A O   1 
HETATM 3621 O O   . HOH D 3 .   ? 2.806   10.750 -27.626 1.00 40.15 ? 406 HOH A O   1 
HETATM 3622 O O   . HOH D 3 .   ? -9.401  25.097 -15.721 1.00 21.26 ? 407 HOH A O   1 
HETATM 3623 O O   . HOH D 3 .   ? -20.597 7.333  -18.917 1.00 38.12 ? 408 HOH A O   1 
HETATM 3624 O O   . HOH D 3 .   ? 1.256   30.821 -19.388 1.00 16.27 ? 409 HOH A O   1 
HETATM 3625 O O   . HOH D 3 .   ? -16.127 11.171 -1.239  1.00 48.36 ? 410 HOH A O   1 
HETATM 3626 O O   . HOH D 3 .   ? 0.796   8.057  -29.563 1.00 31.85 ? 411 HOH A O   1 
HETATM 3627 O O   . HOH D 3 .   ? -21.001 23.369 -17.389 1.00 24.54 ? 412 HOH A O   1 
HETATM 3628 O O   . HOH D 3 .   ? -19.737 13.726 -27.408 1.00 25.29 ? 413 HOH A O   1 
HETATM 3629 O O   . HOH D 3 .   ? -3.602  25.363 -30.322 1.00 21.81 ? 414 HOH A O   1 
HETATM 3630 O O   . HOH D 3 .   ? 14.874  34.893 -16.229 1.00 52.43 ? 415 HOH A O   1 
HETATM 3631 O O   . HOH D 3 .   ? -4.816  10.838 -6.454  1.00 22.46 ? 416 HOH A O   1 
HETATM 3632 O O   . HOH D 3 .   ? -6.558  28.414 -30.047 1.00 33.92 ? 417 HOH A O   1 
HETATM 3633 O O   . HOH D 3 .   ? 21.892  25.753 -18.588 1.00 41.58 ? 418 HOH A O   1 
HETATM 3634 O O   . HOH D 3 .   ? -7.842  22.871 3.007   1.00 40.19 ? 419 HOH A O   1 
HETATM 3635 O O   . HOH D 3 .   ? 18.883  17.083 -8.292  1.00 36.08 ? 420 HOH A O   1 
HETATM 3636 O O   . HOH D 3 .   ? 10.613  37.441 -4.246  1.00 30.95 ? 421 HOH A O   1 
HETATM 3637 O O   . HOH D 3 .   ? -13.978 29.156 -26.176 1.00 31.44 ? 422 HOH A O   1 
HETATM 3638 O O   . HOH D 3 .   ? -19.254 21.361 -17.641 1.00 21.71 ? 423 HOH A O   1 
HETATM 3639 O O   . HOH D 3 .   ? 19.772  15.913 -21.092 1.00 47.63 ? 424 HOH A O   1 
HETATM 3640 O O   . HOH D 3 .   ? 17.816  31.120 -25.160 1.00 46.00 ? 425 HOH A O   1 
HETATM 3641 O O   . HOH D 3 .   ? -21.835 14.569 -20.059 1.00 29.37 ? 426 HOH A O   1 
HETATM 3642 O O   . HOH D 3 .   ? -4.265  5.287  -29.105 1.00 52.29 ? 427 HOH A O   1 
HETATM 3643 O O   . HOH D 3 .   ? -21.904 14.905 -17.449 1.00 46.96 ? 428 HOH A O   1 
HETATM 3644 O O   . HOH D 3 .   ? -17.799 4.371  -24.971 1.00 35.59 ? 429 HOH A O   1 
HETATM 3645 O O   . HOH D 3 .   ? -24.814 23.697 -22.777 1.00 36.61 ? 430 HOH A O   1 
HETATM 3646 O O   . HOH D 3 .   ? -2.968  37.287 -22.770 1.00 36.46 ? 431 HOH A O   1 
HETATM 3647 O O   . HOH D 3 .   ? 17.700  22.662 -3.036  1.00 43.73 ? 432 HOH A O   1 
HETATM 3648 O O   . HOH D 3 .   ? 10.754  30.522 -14.717 1.00 24.42 ? 433 HOH A O   1 
HETATM 3649 O O   . HOH D 3 .   ? 8.618   30.322 -16.553 1.00 21.30 ? 434 HOH A O   1 
HETATM 3650 O O   . HOH D 3 .   ? 2.981   23.492 -31.867 1.00 39.45 ? 435 HOH A O   1 
HETATM 3651 O O   . HOH D 3 .   ? 0.595   16.173 -31.057 1.00 36.11 ? 436 HOH A O   1 
HETATM 3652 O O   . HOH D 3 .   ? -11.280 16.622 -32.621 1.00 30.47 ? 437 HOH A O   1 
HETATM 3653 O O   . HOH D 3 .   ? 13.444  23.836 -2.153  1.00 33.91 ? 438 HOH A O   1 
HETATM 3654 O O   . HOH D 3 .   ? -4.977  6.019  -7.808  1.00 48.49 ? 439 HOH A O   1 
HETATM 3655 O O   . HOH D 3 .   ? -20.784 8.551  -11.638 1.00 47.56 ? 440 HOH A O   1 
HETATM 3656 O O   . HOH D 3 .   ? 9.455   32.589 -33.654 1.00 38.18 ? 441 HOH A O   1 
HETATM 3657 O O   . HOH D 3 .   ? 12.497  33.649 -4.337  1.00 39.63 ? 442 HOH A O   1 
HETATM 3658 O O   . HOH D 3 .   ? -1.203  27.344 -29.381 1.00 35.02 ? 443 HOH A O   1 
HETATM 3659 O O   . HOH D 3 .   ? -19.989 23.909 -29.241 1.00 37.42 ? 444 HOH A O   1 
HETATM 3660 O O   . HOH D 3 .   ? 3.825   11.825 -7.476  1.00 37.94 ? 445 HOH A O   1 
HETATM 3661 O O   . HOH D 3 .   ? -8.949  7.269  -0.251  1.00 40.59 ? 446 HOH A O   1 
HETATM 3662 O O   . HOH D 3 .   ? -5.411  29.555 -5.298  1.00 40.38 ? 447 HOH A O   1 
HETATM 3663 O O   . HOH D 3 .   ? -19.597 24.703 -31.073 1.00 49.31 ? 448 HOH A O   1 
HETATM 3664 O O   . HOH D 3 .   ? 21.301  21.297 -17.971 1.00 48.21 ? 449 HOH A O   1 
HETATM 3665 O O   . HOH D 3 .   ? -13.690 25.881 -3.965  1.00 39.36 ? 450 HOH A O   1 
HETATM 3666 O O   . HOH D 3 .   ? 3.913   35.520 -5.571  1.00 38.61 ? 451 HOH A O   1 
HETATM 3667 O O   . HOH D 3 .   ? 19.142  22.075 -29.380 1.00 41.31 ? 452 HOH A O   1 
HETATM 3668 O O   . HOH D 3 .   ? 3.430   12.927 -6.064  1.00 36.74 ? 453 HOH A O   1 
HETATM 3669 O O   . HOH D 3 .   ? 20.385  26.217 -15.920 1.00 42.19 ? 454 HOH A O   1 
HETATM 3670 O O   . HOH D 3 .   ? 19.794  25.749 -28.594 1.00 46.82 ? 455 HOH A O   1 
HETATM 3671 O O   . HOH D 3 .   ? 7.700   15.577 0.062   1.00 44.05 ? 456 HOH A O   1 
HETATM 3672 O O   . HOH D 3 .   ? -21.246 29.612 -8.790  1.00 47.12 ? 457 HOH A O   1 
HETATM 3673 O O   . HOH D 3 .   ? -16.175 17.050 1.778   1.00 45.77 ? 458 HOH A O   1 
HETATM 3674 O O   . HOH D 3 .   ? 1.201   31.678 -4.177  1.00 41.50 ? 459 HOH A O   1 
HETATM 3675 O O   . HOH D 3 .   ? 16.102  20.512 -1.453  1.00 47.21 ? 460 HOH A O   1 
HETATM 3676 O O   . HOH D 3 .   ? 8.823   11.720 -0.464  1.00 43.48 ? 461 HOH A O   1 
HETATM 3677 O O   . HOH D 3 .   ? -14.478 -1.014 -12.678 1.00 48.07 ? 462 HOH A O   1 
HETATM 3678 O O   . HOH D 3 .   ? 19.082  29.161 -14.906 1.00 38.58 ? 463 HOH A O   1 
HETATM 3679 O O   . HOH D 3 .   ? 11.118  33.134 -15.912 1.00 30.71 ? 464 HOH A O   1 
HETATM 3680 O O   . HOH D 3 .   ? 6.348   23.417 5.177   1.00 51.31 ? 465 HOH A O   1 
HETATM 3681 O O   . HOH D 3 .   ? -8.506  30.581 -24.308 1.00 26.68 ? 466 HOH A O   1 
HETATM 3682 O O   . HOH D 3 .   ? -6.903  28.794 -4.316  1.00 39.92 ? 467 HOH A O   1 
HETATM 3683 O O   . HOH D 3 .   ? -9.692  32.082 -6.433  1.00 40.99 ? 468 HOH A O   1 
HETATM 3684 O O   . HOH D 3 .   ? 9.582   9.591  -24.757 1.00 44.31 ? 469 HOH A O   1 
HETATM 3685 O O   . HOH D 3 .   ? -19.321 15.729 -29.935 1.00 44.18 ? 470 HOH A O   1 
HETATM 3686 O O   . HOH D 3 .   ? 0.965   9.987  -24.456 1.00 36.16 ? 471 HOH A O   1 
HETATM 3687 O O   . HOH D 3 .   ? 1.579   38.782 -23.316 1.00 40.37 ? 472 HOH A O   1 
HETATM 3688 O O   . HOH D 3 .   ? 3.233   24.469 -34.297 1.00 46.26 ? 473 HOH A O   1 
HETATM 3689 O O   . HOH D 3 .   ? -20.218 23.409 -3.683  1.00 35.25 ? 474 HOH A O   1 
HETATM 3690 O O   . HOH D 3 .   ? -15.459 18.575 -35.445 1.00 43.47 ? 475 HOH A O   1 
HETATM 3691 O O   . HOH D 3 .   ? -10.414 7.824  -3.739  1.00 34.22 ? 476 HOH A O   1 
HETATM 3692 O O   . HOH D 3 .   ? -12.083 15.919 2.511   1.00 47.76 ? 477 HOH A O   1 
HETATM 3693 O O   . HOH D 3 .   ? 20.059  21.054 -13.968 1.00 44.27 ? 478 HOH A O   1 
HETATM 3694 O O   . HOH D 3 .   ? 6.317   10.207 -16.243 1.00 40.08 ? 479 HOH A O   1 
HETATM 3695 O O   . HOH D 3 .   ? 21.047  17.390 -8.847  1.00 47.39 ? 480 HOH A O   1 
HETATM 3696 O O   . HOH D 3 .   ? -2.035  39.557 -23.856 1.00 34.65 ? 481 HOH A O   1 
HETATM 3697 O O   . HOH D 3 .   ? 5.106   21.066 3.964   1.00 45.42 ? 482 HOH A O   1 
HETATM 3698 O O   . HOH D 3 .   ? 18.758  22.215 -5.302  1.00 44.29 ? 483 HOH A O   1 
HETATM 3699 O O   . HOH D 3 .   ? -0.310  28.399 -30.991 1.00 42.60 ? 484 HOH A O   1 
HETATM 3700 O O   . HOH D 3 .   ? 21.327  16.541 -18.852 1.00 48.30 ? 485 HOH A O   1 
HETATM 3701 O O   . HOH D 3 .   ? -1.362  39.141 -26.444 1.00 48.07 ? 486 HOH A O   1 
HETATM 3702 O O   . HOH D 3 .   ? 13.251  34.457 -14.718 1.00 39.78 ? 487 HOH A O   1 
HETATM 3703 O O   . HOH D 3 .   ? -15.528 33.687 -20.236 1.00 26.71 ? 488 HOH A O   1 
HETATM 3704 O O   . HOH D 3 .   ? 2.191   33.934 -5.196  1.00 43.00 ? 489 HOH A O   1 
HETATM 3705 O O   . HOH D 3 .   ? -8.029  30.083 -29.133 1.00 50.58 ? 490 HOH A O   1 
HETATM 3706 O O   . HOH D 3 .   ? 21.737  21.217 -15.894 1.00 55.48 ? 491 HOH A O   1 
HETATM 3707 O O   . HOH D 3 .   ? -16.617 31.640 -21.897 1.00 51.61 ? 492 HOH A O   1 
HETATM 3708 O O   . HOH D 3 .   ? 2.911   9.359  -23.841 1.00 48.05 ? 493 HOH A O   1 
HETATM 3709 O O   . HOH D 3 .   ? -9.191  25.834 0.292   1.00 48.37 ? 494 HOH A O   1 
HETATM 3710 O O   . HOH D 3 .   ? -12.568 30.112 -23.459 1.00 34.80 ? 495 HOH A O   1 
HETATM 3711 O O   . HOH D 3 .   ? -4.577  27.661 -31.831 1.00 47.27 ? 496 HOH A O   1 
HETATM 3712 O O   . HOH D 3 .   ? 15.556  32.209 -25.966 1.00 38.40 ? 497 HOH A O   1 
HETATM 3713 O O   . HOH D 3 .   ? -21.830 17.283 -15.967 1.00 38.36 ? 498 HOH A O   1 
HETATM 3714 O O   . HOH D 3 .   ? 13.539  29.169 -29.624 1.00 47.09 ? 499 HOH A O   1 
HETATM 3715 O O   . HOH D 3 .   ? 15.771  30.998 -27.804 1.00 44.97 ? 500 HOH A O   1 
HETATM 3716 O O   . HOH D 3 .   ? 14.905  27.198 -30.018 1.00 46.79 ? 501 HOH A O   1 
HETATM 3717 O O   . HOH D 3 .   ? 1.097   9.402  -26.392 1.00 43.58 ? 502 HOH A O   1 
HETATM 3718 O O   . HOH D 3 .   ? -22.724 28.795 -7.177  1.00 54.75 ? 503 HOH A O   1 
HETATM 3719 O O   . HOH D 3 .   ? -20.977 26.701 -11.477 1.00 30.04 ? 504 HOH A O   1 
HETATM 3720 O O   . HOH D 3 .   ? -24.811 23.959 -19.715 1.00 41.60 ? 505 HOH A O   1 
HETATM 3721 O O   . HOH D 3 .   ? -5.076  4.790  -21.833 1.00 46.50 ? 506 HOH A O   1 
HETATM 3722 O O   . HOH D 3 .   ? -20.764 25.821 -27.741 1.00 51.32 ? 507 HOH A O   1 
HETATM 3723 O O   . HOH D 3 .   ? -18.023 15.026 2.337   1.00 50.24 ? 508 HOH A O   1 
HETATM 3724 O O   . HOH D 3 .   ? -23.470 23.133 -15.583 1.00 43.19 ? 509 HOH A O   1 
HETATM 3725 O O   . HOH D 3 .   ? -11.689 27.072 -0.011  1.00 46.06 ? 510 HOH A O   1 
HETATM 3726 O O   . HOH D 3 .   ? 6.811   7.087  -13.430 1.00 42.18 ? 511 HOH A O   1 
HETATM 3727 O O   . HOH D 3 .   ? 13.174  10.044 -12.341 1.00 44.45 ? 512 HOH A O   1 
HETATM 3728 O O   . HOH D 3 .   ? 14.069  8.569  -14.485 1.00 47.35 ? 513 HOH A O   1 
HETATM 3729 O O   . HOH D 3 .   ? -5.053  38.548 -24.250 1.00 41.14 ? 514 HOH A O   1 
HETATM 3730 O O   . HOH D 3 .   ? -23.778 25.938 -23.578 1.00 49.03 ? 515 HOH A O   1 
HETATM 3731 O O   . HOH D 3 .   ? -24.138 22.513 -11.281 1.00 53.70 ? 516 HOH A O   1 
HETATM 3732 O O   . HOH D 3 .   ? 6.635   8.164  -15.118 1.00 41.01 ? 517 HOH A O   1 
HETATM 3733 O O   . HOH D 3 .   ? -23.276 25.483 -11.126 1.00 42.54 ? 518 HOH A O   1 
HETATM 3734 O O   . HOH D 3 .   ? -5.230  38.403 -26.843 1.00 45.73 ? 519 HOH A O   1 
HETATM 3735 O O   . HOH D 3 .   ? -7.518  34.255 -27.586 1.00 46.58 ? 520 HOH A O   1 
HETATM 3736 O O   . HOH D 3 .   ? -24.633 22.977 -13.062 1.00 49.27 ? 521 HOH A O   1 
HETATM 3737 O O   . HOH D 3 .   ? 7.880   5.033  -13.608 1.00 48.24 ? 522 HOH A O   1 
HETATM 3738 O O   . HOH D 3 .   ? 8.549   4.470  -11.624 1.00 46.48 ? 523 HOH A O   1 
HETATM 3739 O O   . HOH E 3 .   ? -30.945 58.457 -16.227 1.00 47.61 ? 401 HOH B O   1 
HETATM 3740 O O   . HOH E 3 .   ? -15.401 48.442 -31.565 1.00 43.43 ? 402 HOH B O   1 
HETATM 3741 O O   . HOH E 3 .   ? -13.734 63.884 -29.156 1.00 40.15 ? 403 HOH B O   1 
HETATM 3742 O O   . HOH E 3 .   ? 10.477  53.276 -9.011  1.00 34.26 ? 404 HOH B O   1 
HETATM 3743 O O   . HOH E 3 .   ? -25.792 36.483 -26.931 1.00 47.19 ? 405 HOH B O   1 
HETATM 3744 O O   . HOH E 3 .   ? -0.925  58.149 1.365   1.00 29.08 ? 406 HOH B O   1 
HETATM 3745 O O   . HOH E 3 .   ? -5.212  48.610 -13.996 1.00 15.22 ? 407 HOH B O   1 
HETATM 3746 O O   . HOH E 3 .   ? -10.132 43.325 -21.451 1.00 19.44 ? 408 HOH B O   1 
HETATM 3747 O O   . HOH E 3 .   ? 1.630   67.318 -13.345 1.00 42.18 ? 409 HOH B O   1 
HETATM 3748 O O   . HOH E 3 .   ? 2.898   45.904 4.304   1.00 40.43 ? 410 HOH B O   1 
HETATM 3749 O O   . HOH E 3 .   ? -1.013  38.944 -6.960  1.00 39.33 ? 411 HOH B O   1 
HETATM 3750 O O   . HOH E 3 .   ? -29.305 46.565 -18.815 1.00 24.95 ? 412 HOH B O   1 
HETATM 3751 O O   . HOH E 3 .   ? -1.012  44.362 -29.531 1.00 40.23 ? 413 HOH B O   1 
HETATM 3752 O O   . HOH E 3 .   ? -9.407  54.423 -21.237 1.00 16.18 ? 414 HOH B O   1 
HETATM 3753 O O   . HOH E 3 .   ? -10.303 37.526 -19.914 1.00 28.72 ? 415 HOH B O   1 
HETATM 3754 O O   . HOH E 3 .   ? -13.053 29.102 -7.583  1.00 25.73 ? 416 HOH B O   1 
HETATM 3755 O O   . HOH E 3 .   ? 1.348   65.880 -15.736 1.00 27.25 ? 417 HOH B O   1 
HETATM 3756 O O   . HOH E 3 .   ? 7.373   40.273 -17.566 1.00 46.45 ? 418 HOH B O   1 
HETATM 3757 O O   . HOH E 3 .   ? -12.421 59.288 -6.335  1.00 25.53 ? 419 HOH B O   1 
HETATM 3758 O O   . HOH E 3 .   ? 3.279   40.776 -5.447  1.00 25.58 ? 420 HOH B O   1 
HETATM 3759 O O   . HOH E 3 .   ? 8.356   51.492 -16.335 1.00 25.62 ? 421 HOH B O   1 
HETATM 3760 O O   . HOH E 3 .   ? -10.232 68.513 -23.560 1.00 49.98 ? 422 HOH B O   1 
HETATM 3761 O O   . HOH E 3 .   ? -26.683 56.664 -3.631  1.00 46.95 ? 423 HOH B O   1 
HETATM 3762 O O   . HOH E 3 .   ? -9.270  57.959 -30.179 1.00 30.46 ? 424 HOH B O   1 
HETATM 3763 O O   . HOH E 3 .   ? -26.968 45.101 -28.894 1.00 41.79 ? 425 HOH B O   1 
HETATM 3764 O O   . HOH E 3 .   ? -19.925 37.906 -15.834 1.00 28.19 ? 426 HOH B O   1 
HETATM 3765 O O   . HOH E 3 .   ? -0.827  47.584 3.468   1.00 38.06 ? 427 HOH B O   1 
HETATM 3766 O O   . HOH E 3 .   ? -16.663 51.741 -34.616 1.00 44.38 ? 428 HOH B O   1 
HETATM 3767 O O   . HOH E 3 .   ? -1.819  37.344 -20.386 1.00 31.65 ? 429 HOH B O   1 
HETATM 3768 O O   . HOH E 3 .   ? -11.791 35.967 -26.299 1.00 39.87 ? 430 HOH B O   1 
HETATM 3769 O O   . HOH E 3 .   ? -27.463 46.917 -20.997 1.00 20.99 ? 431 HOH B O   1 
HETATM 3770 O O   . HOH E 3 .   ? 10.163  53.523 -29.913 1.00 45.03 ? 432 HOH B O   1 
HETATM 3771 O O   . HOH E 3 .   ? -2.462  64.527 -17.952 1.00 26.10 ? 433 HOH B O   1 
HETATM 3772 O O   . HOH E 3 .   ? -25.037 39.852 -8.247  1.00 25.10 ? 434 HOH B O   1 
HETATM 3773 O O   . HOH E 3 .   ? -14.787 35.491 -27.652 1.00 40.98 ? 435 HOH B O   1 
HETATM 3774 O O   . HOH E 3 .   ? -1.516  39.021 -9.599  1.00 27.38 ? 436 HOH B O   1 
HETATM 3775 O O   . HOH E 3 .   ? -4.407  62.568 -7.342  1.00 38.88 ? 437 HOH B O   1 
HETATM 3776 O O   . HOH E 3 .   ? 9.566   40.071 -11.946 1.00 43.96 ? 438 HOH B O   1 
HETATM 3777 O O   . HOH E 3 .   ? -17.323 54.816 0.864   1.00 41.49 ? 439 HOH B O   1 
HETATM 3778 O O   . HOH E 3 .   ? 9.851   51.197 -18.539 1.00 30.44 ? 440 HOH B O   1 
HETATM 3779 O O   . HOH E 3 .   ? -5.704  48.405 -8.989  1.00 19.46 ? 441 HOH B O   1 
HETATM 3780 O O   . HOH E 3 .   ? 3.895   41.015 -18.709 1.00 24.92 ? 442 HOH B O   1 
HETATM 3781 O O   . HOH E 3 .   ? 9.508   42.063 -3.507  1.00 35.23 ? 443 HOH B O   1 
HETATM 3782 O O   . HOH E 3 .   ? -22.103 49.062 -31.430 1.00 34.90 ? 444 HOH B O   1 
HETATM 3783 O O   . HOH E 3 .   ? -13.035 44.778 -24.275 1.00 22.02 ? 445 HOH B O   1 
HETATM 3784 O O   . HOH E 3 .   ? -5.481  60.067 -32.816 1.00 30.66 ? 446 HOH B O   1 
HETATM 3785 O O   . HOH E 3 .   ? 2.999   51.891 -15.251 1.00 16.72 ? 447 HOH B O   1 
HETATM 3786 O O   . HOH E 3 .   ? -35.668 49.771 -19.184 1.00 41.86 ? 448 HOH B O   1 
HETATM 3787 O O   . HOH E 3 .   ? -35.806 44.989 -25.742 1.00 48.81 ? 449 HOH B O   1 
HETATM 3788 O O   . HOH E 3 .   ? -16.656 37.960 -15.941 1.00 19.98 ? 450 HOH B O   1 
HETATM 3789 O O   . HOH E 3 .   ? -23.581 41.365 -4.884  1.00 26.19 ? 451 HOH B O   1 
HETATM 3790 O O   . HOH E 3 .   ? 10.027  53.718 -19.372 1.00 34.21 ? 452 HOH B O   1 
HETATM 3791 O O   . HOH E 3 .   ? -27.638 55.645 -10.636 1.00 35.71 ? 453 HOH B O   1 
HETATM 3792 O O   . HOH E 3 .   ? -24.670 55.143 -23.957 1.00 29.04 ? 454 HOH B O   1 
HETATM 3793 O O   . HOH E 3 .   ? 0.361   59.034 -2.283  1.00 33.67 ? 455 HOH B O   1 
HETATM 3794 O O   . HOH E 3 .   ? -4.423  50.259 -7.391  1.00 18.68 ? 456 HOH B O   1 
HETATM 3795 O O   . HOH E 3 .   ? -15.569 47.987 -16.318 1.00 19.55 ? 457 HOH B O   1 
HETATM 3796 O O   . HOH E 3 .   ? -17.079 57.097 -23.260 1.00 20.37 ? 458 HOH B O   1 
HETATM 3797 O O   . HOH E 3 .   ? 7.410   45.237 -1.543  1.00 40.37 ? 459 HOH B O   1 
HETATM 3798 O O   . HOH E 3 .   ? 5.827   45.710 -25.052 1.00 36.06 ? 460 HOH B O   1 
HETATM 3799 O O   . HOH E 3 .   ? 6.874   43.805 -10.709 1.00 18.80 ? 461 HOH B O   1 
HETATM 3800 O O   . HOH E 3 .   ? -16.980 37.572 4.847   1.00 47.37 ? 462 HOH B O   1 
HETATM 3801 O O   . HOH E 3 .   ? 8.420   56.472 -8.884  1.00 40.67 ? 463 HOH B O   1 
HETATM 3802 O O   . HOH E 3 .   ? -2.693  49.464 4.726   1.00 33.38 ? 464 HOH B O   1 
HETATM 3803 O O   . HOH E 3 .   ? -10.080 40.505 -21.174 1.00 22.16 ? 465 HOH B O   1 
HETATM 3804 O O   . HOH E 3 .   ? 2.832   56.530 -19.688 1.00 19.48 ? 466 HOH B O   1 
HETATM 3805 O O   . HOH E 3 .   ? -5.344  44.332 -7.722  1.00 26.57 ? 467 HOH B O   1 
HETATM 3806 O O   . HOH E 3 .   ? 5.175   36.538 -15.136 1.00 37.16 ? 468 HOH B O   1 
HETATM 3807 O O   . HOH E 3 .   ? -3.259  48.367 -16.276 1.00 17.10 ? 469 HOH B O   1 
HETATM 3808 O O   . HOH E 3 .   ? -29.968 43.978 -3.630  1.00 40.70 ? 470 HOH B O   1 
HETATM 3809 O O   . HOH E 3 .   ? -23.737 35.845 -16.871 1.00 40.50 ? 471 HOH B O   1 
HETATM 3810 O O   . HOH E 3 .   ? -13.842 54.406 -28.286 1.00 35.90 ? 472 HOH B O   1 
HETATM 3811 O O   . HOH E 3 .   ? -19.523 33.492 -0.251  1.00 45.90 ? 473 HOH B O   1 
HETATM 3812 O O   . HOH E 3 .   ? -10.239 41.311 -28.666 1.00 40.47 ? 474 HOH B O   1 
HETATM 3813 O O   . HOH E 3 .   ? -25.626 35.796 -9.772  1.00 47.00 ? 475 HOH B O   1 
HETATM 3814 O O   . HOH E 3 .   ? 3.808   63.979 -25.375 1.00 24.21 ? 476 HOH B O   1 
HETATM 3815 O O   . HOH E 3 .   ? -14.615 41.468 -15.782 1.00 18.15 ? 477 HOH B O   1 
HETATM 3816 O O   . HOH E 3 .   ? -3.122  43.145 0.149   1.00 30.53 ? 478 HOH B O   1 
HETATM 3817 O O   . HOH E 3 .   ? 5.766   57.239 -27.098 1.00 35.56 ? 479 HOH B O   1 
HETATM 3818 O O   . HOH E 3 .   ? 5.671   65.281 -23.598 1.00 33.16 ? 480 HOH B O   1 
HETATM 3819 O O   . HOH E 3 .   ? -5.010  42.892 -25.554 1.00 22.46 ? 481 HOH B O   1 
HETATM 3820 O O   . HOH E 3 .   ? 2.400   62.886 -9.086  1.00 22.49 ? 482 HOH B O   1 
HETATM 3821 O O   . HOH E 3 .   ? -24.209 44.009 0.931   1.00 33.10 ? 483 HOH B O   1 
HETATM 3822 O O   . HOH E 3 .   ? -3.194  61.147 -5.571  1.00 36.47 ? 484 HOH B O   1 
HETATM 3823 O O   . HOH E 3 .   ? -13.639 39.926 -17.843 1.00 15.97 ? 485 HOH B O   1 
HETATM 3824 O O   . HOH E 3 .   ? -5.341  65.444 -29.252 1.00 39.34 ? 486 HOH B O   1 
HETATM 3825 O O   . HOH E 3 .   ? 9.415   39.686 -9.084  1.00 50.56 ? 487 HOH B O   1 
HETATM 3826 O O   . HOH E 3 .   ? -4.184  36.015 -7.400  1.00 39.04 ? 488 HOH B O   1 
HETATM 3827 O O   . HOH E 3 .   ? -23.585 39.368 -15.941 1.00 26.86 ? 489 HOH B O   1 
HETATM 3828 O O   . HOH E 3 .   ? -17.090 46.749 -29.276 1.00 39.81 ? 490 HOH B O   1 
HETATM 3829 O O   . HOH E 3 .   ? -3.412  33.759 -22.562 1.00 36.08 ? 491 HOH B O   1 
HETATM 3830 O O   . HOH E 3 .   ? 8.635   46.754 -16.674 1.00 26.49 ? 492 HOH B O   1 
HETATM 3831 O O   . HOH E 3 .   ? -21.100 32.749 -25.695 1.00 48.73 ? 493 HOH B O   1 
HETATM 3832 O O   . HOH E 3 .   ? -14.015 55.128 -0.734  1.00 33.70 ? 494 HOH B O   1 
HETATM 3833 O O   . HOH E 3 .   ? 0.810   42.850 -25.475 1.00 35.30 ? 495 HOH B O   1 
HETATM 3834 O O   . HOH E 3 .   ? -9.091  64.422 -23.185 1.00 31.48 ? 496 HOH B O   1 
HETATM 3835 O O   . HOH E 3 .   ? -20.604 59.783 -23.306 1.00 46.70 ? 497 HOH B O   1 
HETATM 3836 O O   . HOH E 3 .   ? -23.458 40.917 -10.063 1.00 27.49 ? 498 HOH B O   1 
HETATM 3837 O O   . HOH E 3 .   ? -28.405 49.594 -1.542  1.00 41.90 ? 499 HOH B O   1 
HETATM 3838 O O   . HOH E 3 .   ? -6.469  57.463 -2.347  1.00 26.26 ? 500 HOH B O   1 
HETATM 3839 O O   . HOH E 3 .   ? -29.638 46.038 -24.421 1.00 37.52 ? 501 HOH B O   1 
HETATM 3840 O O   . HOH E 3 .   ? 5.516   62.064 -6.500  1.00 29.13 ? 502 HOH B O   1 
HETATM 3841 O O   . HOH E 3 .   ? -8.686  63.510 -14.967 1.00 39.59 ? 503 HOH B O   1 
HETATM 3842 O O   . HOH E 3 .   ? 5.287   62.466 -9.274  1.00 33.87 ? 504 HOH B O   1 
HETATM 3843 O O   . HOH E 3 .   ? -17.409 34.146 -16.971 1.00 36.91 ? 505 HOH B O   1 
HETATM 3844 O O   . HOH E 3 .   ? -21.086 52.961 -27.565 1.00 21.80 ? 506 HOH B O   1 
HETATM 3845 O O   . HOH E 3 .   ? -26.638 38.153 -0.829  1.00 44.46 ? 507 HOH B O   1 
HETATM 3846 O O   . HOH E 3 .   ? -5.584  68.134 -28.537 1.00 34.44 ? 508 HOH B O   1 
HETATM 3847 O O   . HOH E 3 .   ? -9.580  50.283 -28.733 1.00 21.75 ? 509 HOH B O   1 
HETATM 3848 O O   . HOH E 3 .   ? -2.690  44.931 -14.264 1.00 25.29 ? 510 HOH B O   1 
HETATM 3849 O O   . HOH E 3 .   ? 6.848   58.128 -24.470 1.00 27.80 ? 511 HOH B O   1 
HETATM 3850 O O   . HOH E 3 .   ? -10.224 30.056 -10.118 1.00 27.24 ? 512 HOH B O   1 
HETATM 3851 O O   . HOH E 3 .   ? -0.438  70.028 -20.024 1.00 56.05 ? 513 HOH B O   1 
HETATM 3852 O O   . HOH E 3 .   ? -14.088 37.499 -16.745 1.00 17.05 ? 514 HOH B O   1 
HETATM 3853 O O   . HOH E 3 .   ? -13.571 56.464 -26.842 1.00 33.40 ? 515 HOH B O   1 
HETATM 3854 O O   . HOH E 3 .   ? -22.582 35.730 -0.400  1.00 48.54 ? 516 HOH B O   1 
HETATM 3855 O O   . HOH E 3 .   ? -13.429 38.188 -1.928  1.00 24.90 ? 517 HOH B O   1 
HETATM 3856 O O   . HOH E 3 .   ? 1.484   35.853 -18.722 1.00 18.61 ? 518 HOH B O   1 
HETATM 3857 O O   . HOH E 3 .   ? -15.440 55.033 3.245   1.00 48.85 ? 519 HOH B O   1 
HETATM 3858 O O   . HOH E 3 .   ? -31.793 54.601 -15.412 1.00 42.53 ? 520 HOH B O   1 
HETATM 3859 O O   . HOH E 3 .   ? -1.741  56.258 -29.486 1.00 23.46 ? 521 HOH B O   1 
HETATM 3860 O O   . HOH E 3 .   ? -7.821  56.392 -33.880 1.00 43.93 ? 522 HOH B O   1 
HETATM 3861 O O   . HOH E 3 .   ? 14.542  54.215 -2.527  1.00 48.68 ? 523 HOH B O   1 
HETATM 3862 O O   . HOH E 3 .   ? -2.553  68.905 -26.528 1.00 33.21 ? 524 HOH B O   1 
HETATM 3863 O O   . HOH E 3 .   ? 9.675   56.041 -18.004 1.00 27.59 ? 525 HOH B O   1 
HETATM 3864 O O   . HOH E 3 .   ? -23.153 40.601 -31.289 1.00 36.88 ? 526 HOH B O   1 
HETATM 3865 O O   . HOH E 3 .   ? -21.953 45.122 -30.777 1.00 39.59 ? 527 HOH B O   1 
HETATM 3866 O O   . HOH E 3 .   ? 14.897  52.684 -25.174 1.00 36.80 ? 528 HOH B O   1 
HETATM 3867 O O   . HOH E 3 .   ? 9.670   46.469 -19.133 1.00 37.01 ? 529 HOH B O   1 
HETATM 3868 O O   . HOH E 3 .   ? -4.530  64.148 -9.673  1.00 35.60 ? 530 HOH B O   1 
HETATM 3869 O O   . HOH E 3 .   ? -15.607 61.533 -22.187 1.00 40.67 ? 531 HOH B O   1 
HETATM 3870 O O   . HOH E 3 .   ? -20.743 40.067 -14.260 1.00 24.44 ? 532 HOH B O   1 
HETATM 3871 O O   . HOH E 3 .   ? 13.151  49.632 -26.181 1.00 43.24 ? 533 HOH B O   1 
HETATM 3872 O O   . HOH E 3 .   ? -8.274  63.156 -12.898 1.00 36.38 ? 534 HOH B O   1 
HETATM 3873 O O   . HOH E 3 .   ? 5.707   49.209 3.245   1.00 29.95 ? 535 HOH B O   1 
HETATM 3874 O O   . HOH E 3 .   ? -25.848 42.751 -28.224 1.00 44.76 ? 536 HOH B O   1 
HETATM 3875 O O   . HOH E 3 .   ? -23.740 34.474 -2.719  1.00 42.84 ? 537 HOH B O   1 
HETATM 3876 O O   . HOH E 3 .   ? -9.663  47.342 -28.085 1.00 20.76 ? 538 HOH B O   1 
HETATM 3877 O O   . HOH E 3 .   ? -13.896 64.021 -23.893 1.00 37.87 ? 539 HOH B O   1 
HETATM 3878 O O   . HOH E 3 .   ? 7.126   48.900 -16.292 1.00 21.65 ? 540 HOH B O   1 
HETATM 3879 O O   . HOH E 3 .   ? -19.739 56.172 -27.927 1.00 38.67 ? 541 HOH B O   1 
HETATM 3880 O O   . HOH E 3 .   ? -32.197 44.115 -12.340 1.00 36.77 ? 542 HOH B O   1 
HETATM 3881 O O   . HOH E 3 .   ? -29.969 51.374 -3.077  1.00 34.09 ? 543 HOH B O   1 
HETATM 3882 O O   . HOH E 3 .   ? -18.125 35.796 -14.222 1.00 32.66 ? 544 HOH B O   1 
HETATM 3883 O O   . HOH E 3 .   ? 7.739   55.318 -28.102 1.00 41.12 ? 545 HOH B O   1 
HETATM 3884 O O   . HOH E 3 .   ? -6.702  43.980 -28.745 1.00 42.84 ? 546 HOH B O   1 
HETATM 3885 O O   . HOH E 3 .   ? -23.317 32.557 -10.084 1.00 49.07 ? 547 HOH B O   1 
HETATM 3886 O O   . HOH E 3 .   ? -9.588  34.214 -22.882 1.00 41.98 ? 548 HOH B O   1 
HETATM 3887 O O   . HOH E 3 .   ? 4.457   67.641 -20.537 1.00 34.10 ? 549 HOH B O   1 
HETATM 3888 O O   . HOH E 3 .   ? -22.665 39.339 -12.473 1.00 28.85 ? 550 HOH B O   1 
HETATM 3889 O O   . HOH E 3 .   ? -22.336 32.970 -13.401 1.00 46.50 ? 551 HOH B O   1 
HETATM 3890 O O   . HOH E 3 .   ? -11.955 44.935 -27.539 1.00 37.20 ? 552 HOH B O   1 
HETATM 3891 O O   . HOH E 3 .   ? 8.952   42.392 -16.743 1.00 49.55 ? 553 HOH B O   1 
HETATM 3892 O O   . HOH E 3 .   ? 7.090   48.601 -27.998 1.00 34.77 ? 554 HOH B O   1 
HETATM 3893 O O   . HOH E 3 .   ? -10.272 48.537 1.816   1.00 45.09 ? 555 HOH B O   1 
HETATM 3894 O O   . HOH E 3 .   ? -15.252 62.354 -0.274  1.00 50.84 ? 556 HOH B O   1 
HETATM 3895 O O   . HOH E 3 .   ? -12.332 36.152 -3.066  1.00 39.69 ? 557 HOH B O   1 
HETATM 3896 O O   . HOH E 3 .   ? -15.191 32.967 -4.776  1.00 41.06 ? 558 HOH B O   1 
HETATM 3897 O O   . HOH E 3 .   ? -1.092  69.303 -3.009  1.00 55.83 ? 559 HOH B O   1 
HETATM 3898 O O   . HOH E 3 .   ? -11.825 38.913 -29.265 1.00 48.26 ? 560 HOH B O   1 
HETATM 3899 O O   . HOH E 3 .   ? -23.300 37.256 -13.810 1.00 41.89 ? 561 HOH B O   1 
HETATM 3900 O O   . HOH E 3 .   ? -11.808 42.436 0.610   1.00 40.14 ? 562 HOH B O   1 
HETATM 3901 O O   . HOH E 3 .   ? -4.204  41.062 -23.537 1.00 25.12 ? 563 HOH B O   1 
HETATM 3902 O O   . HOH E 3 .   ? -9.505  37.732 -22.169 1.00 37.10 ? 564 HOH B O   1 
HETATM 3903 O O   . HOH E 3 .   ? -25.907 35.613 -13.484 1.00 44.12 ? 565 HOH B O   1 
HETATM 3904 O O   . HOH E 3 .   ? 2.491   41.688 -2.691  1.00 39.93 ? 566 HOH B O   1 
HETATM 3905 O O   . HOH E 3 .   ? 8.064   63.105 -5.524  1.00 47.17 ? 567 HOH B O   1 
HETATM 3906 O O   . HOH E 3 .   ? -19.015 45.023 -29.555 1.00 39.65 ? 568 HOH B O   1 
HETATM 3907 O O   . HOH E 3 .   ? 9.340   44.673 -3.395  1.00 38.75 ? 569 HOH B O   1 
HETATM 3908 O O   . HOH E 3 .   ? 14.700  55.673 -24.456 1.00 48.36 ? 570 HOH B O   1 
HETATM 3909 O O   . HOH E 3 .   ? 5.614   37.346 -4.252  1.00 44.64 ? 571 HOH B O   1 
HETATM 3910 O O   . HOH E 3 .   ? -22.503 31.034 -23.606 1.00 49.67 ? 572 HOH B O   1 
HETATM 3911 O O   . HOH E 3 .   ? 4.208   39.863 -22.144 1.00 48.95 ? 573 HOH B O   1 
HETATM 3912 O O   . HOH E 3 .   ? -14.397 32.711 -22.748 1.00 39.16 ? 574 HOH B O   1 
HETATM 3913 O O   . HOH E 3 .   ? -1.767  49.420 -33.484 1.00 57.44 ? 575 HOH B O   1 
HETATM 3914 O O   . HOH E 3 .   ? -16.604 30.888 -3.756  1.00 52.72 ? 576 HOH B O   1 
HETATM 3915 O O   . HOH E 3 .   ? 9.982   54.838 -14.785 1.00 44.53 ? 577 HOH B O   1 
HETATM 3916 O O   . HOH E 3 .   ? -9.441  50.508 1.959   1.00 42.55 ? 578 HOH B O   1 
HETATM 3917 O O   . HOH E 3 .   ? -13.673 34.436 -4.523  1.00 36.88 ? 579 HOH B O   1 
HETATM 3918 O O   . HOH E 3 .   ? -13.160 44.438 -29.128 1.00 43.12 ? 580 HOH B O   1 
HETATM 3919 O O   . HOH E 3 .   ? -14.382 61.113 -5.777  1.00 42.82 ? 581 HOH B O   1 
HETATM 3920 O O   . HOH E 3 .   ? -5.491  42.341 -28.300 1.00 46.99 ? 582 HOH B O   1 
HETATM 3921 O O   . HOH E 3 .   ? -0.437  41.244 -23.055 1.00 33.72 ? 583 HOH B O   1 
HETATM 3922 O O   . HOH E 3 .   ? 3.120   37.457 -21.100 1.00 28.83 ? 584 HOH B O   1 
HETATM 3923 O O   . HOH E 3 .   ? 10.547  42.508 -15.080 1.00 56.64 ? 585 HOH B O   1 
HETATM 3924 O O   . HOH E 3 .   ? 12.106  49.781 -17.488 1.00 52.38 ? 586 HOH B O   1 
HETATM 3925 O O   . HOH E 3 .   ? -16.134 57.740 -25.941 1.00 33.54 ? 587 HOH B O   1 
HETATM 3926 O O   . HOH E 3 .   ? -27.060 43.252 -26.677 1.00 49.57 ? 588 HOH B O   1 
HETATM 3927 O O   . HOH E 3 .   ? 9.207   55.744 -29.994 1.00 42.15 ? 589 HOH B O   1 
HETATM 3928 O O   . HOH E 3 .   ? -10.762 40.433 1.369   1.00 55.06 ? 590 HOH B O   1 
HETATM 3929 O O   . HOH E 3 .   ? 9.214   42.538 -11.471 1.00 31.11 ? 591 HOH B O   1 
HETATM 3930 O O   . HOH E 3 .   ? -10.936 31.446 -24.012 1.00 38.33 ? 592 HOH B O   1 
HETATM 3931 O O   . HOH E 3 .   ? -28.549 57.307 -25.381 1.00 43.24 ? 593 HOH B O   1 
HETATM 3932 O O   . HOH E 3 .   ? 10.003  52.559 -14.404 1.00 39.58 ? 594 HOH B O   1 
HETATM 3933 O O   . HOH E 3 .   ? -22.756 30.512 -9.428  1.00 57.64 ? 595 HOH B O   1 
HETATM 3934 O O   . HOH E 3 .   ? 3.347   43.997 -26.748 1.00 43.15 ? 596 HOH B O   1 
HETATM 3935 O O   . HOH E 3 .   ? -6.345  65.887 -6.687  1.00 54.05 ? 597 HOH B O   1 
HETATM 3936 O O   . HOH E 3 .   ? -30.101 47.899 -0.664  1.00 48.17 ? 598 HOH B O   1 
HETATM 3937 O O   . HOH E 3 .   ? -17.288 43.280 -30.990 1.00 47.05 ? 599 HOH B O   1 
HETATM 3938 O O   . HOH E 3 .   ? 11.347  40.063 -7.955  1.00 49.37 ? 600 HOH B O   1 
HETATM 3939 O O   . HOH E 3 .   ? -2.770  48.325 -32.163 1.00 55.16 ? 601 HOH B O   1 
HETATM 3940 O O   . HOH E 3 .   ? -25.043 57.766 -24.772 1.00 33.25 ? 602 HOH B O   1 
HETATM 3941 O O   . HOH E 3 .   ? 3.197   42.059 -0.939  1.00 40.25 ? 603 HOH B O   1 
HETATM 3942 O O   . HOH E 3 .   ? -12.011 64.094 -21.900 1.00 37.20 ? 604 HOH B O   1 
HETATM 3943 O O   . HOH E 3 .   ? -1.644  41.398 1.319   1.00 45.59 ? 605 HOH B O   1 
HETATM 3944 O O   . HOH E 3 .   ? 11.820  45.751 -3.109  1.00 50.55 ? 606 HOH B O   1 
HETATM 3945 O O   . HOH E 3 .   ? -7.828  33.274 -24.569 1.00 36.68 ? 607 HOH B O   1 
HETATM 3946 O O   . HOH E 3 .   ? 12.692  50.303 -14.742 1.00 49.60 ? 608 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   . SER A 26  ? 0.6120 0.8418 0.9971 -0.1066 0.0621  0.0537  2   SER A N   
2    C CA  . SER A 26  ? 0.5069 0.7548 0.8850 -0.1107 0.0820  0.0740  2   SER A CA  
3    C C   . SER A 26  ? 0.4226 0.6486 0.7659 -0.1080 0.0879  0.0895  2   SER A C   
4    O O   . SER A 26  ? 0.5430 0.7866 0.8620 -0.1024 0.1026  0.0992  2   SER A O   
5    C CB  . SER A 26  ? 0.4707 0.7239 0.8803 -0.1265 0.0855  0.0849  2   SER A CB  
6    O OG  . SER A 26  ? 0.5272 0.7959 0.9273 -0.1304 0.1046  0.1063  2   SER A OG  
7    N N   . ALA A 27  ? 0.4641 0.6528 0.8034 -0.1107 0.0756  0.0899  3   ALA A N   
8    C CA  . ALA A 27  ? 0.2984 0.4665 0.6070 -0.1077 0.0789  0.1050  3   ALA A CA  
9    C C   . ALA A 27  ? 0.3332 0.5048 0.6092 -0.0945 0.0802  0.0974  3   ALA A C   
10   O O   . ALA A 27  ? 0.5115 0.6871 0.7565 -0.0895 0.0892  0.1099  3   ALA A O   
11   C CB  . ALA A 27  ? 0.3331 0.4619 0.6501 -0.1123 0.0652  0.1049  3   ALA A CB  
12   N N   . ILE A 28  ? 0.2759 0.4469 0.5585 -0.0880 0.0704  0.0767  4   ILE A N   
13   C CA  . ILE A 28  ? 0.2922 0.4562 0.5329 -0.0717 0.0671  0.0626  4   ILE A CA  
14   C C   . ILE A 28  ? 0.2007 0.3981 0.4359 -0.0624 0.0781  0.0562  4   ILE A C   
15   O O   . ILE A 28  ? 0.2432 0.4604 0.5062 -0.0619 0.0767  0.0467  4   ILE A O   
16   C CB  . ILE A 28  ? 0.3554 0.4956 0.5922 -0.0655 0.0485  0.0409  4   ILE A CB  
17   C CG1 . ILE A 28  ? 0.4348 0.5507 0.6934 -0.0762 0.0375  0.0415  4   ILE A CG1 
18   C CG2 . ILE A 28  ? 0.3389 0.4630 0.5327 -0.0519 0.0451  0.0321  4   ILE A CG2 
19   C CD1 . ILE A 28  ? 0.2569 0.3446 0.4915 -0.0754 0.0358  0.0500  4   ILE A CD1 
20   N N   . LYS A 29  ? 0.2995 0.5045 0.4997 -0.0537 0.0881  0.0591  5   LYS A N   
21   C CA  . LYS A 29  ? 0.3084 0.5424 0.5018 -0.0419 0.0977  0.0475  5   LYS A CA  
22   C C   . LYS A 29  ? 0.2686 0.4832 0.4442 -0.0272 0.0855  0.0247  5   LYS A C   
23   O O   . LYS A 29  ? 0.2247 0.4068 0.3814 -0.0257 0.0733  0.0208  5   LYS A O   
24   C CB  . LYS A 29  ? 0.2748 0.5295 0.4392 -0.0385 0.1136  0.0567  5   LYS A CB  
25   C CG  . LYS A 29  ? 0.4163 0.6803 0.5797 -0.0512 0.1241  0.0853  5   LYS A CG  
26   C CD  . LYS A 29  ? 0.5439 0.8010 0.7447 -0.0668 0.1220  0.0989  5   LYS A CD  
27   C CE  . LYS A 29  ? 0.6514 0.8930 0.8395 -0.0752 0.1234  0.1226  5   LYS A CE  
28   N NZ  . LYS A 29  ? 0.3833 0.5886 0.5623 -0.0758 0.1096  0.1251  5   LYS A NZ  
29   N N   . PRO A 30  ? 0.2381 0.4730 0.4220 -0.0158 0.0888  0.0105  6   PRO A N   
30   C CA  . PRO A 30  ? 0.2303 0.4452 0.4003 -0.0013 0.0777  -0.0079 6   PRO A CA  
31   C C   . PRO A 30  ? 0.1731 0.3671 0.3046 0.0052  0.0775  -0.0131 6   PRO A C   
32   O O   . PRO A 30  ? 0.2086 0.3773 0.3286 0.0131  0.0665  -0.0235 6   PRO A O   
33   C CB  . PRO A 30  ? 0.1958 0.4412 0.3864 0.0103  0.0846  -0.0195 6   PRO A CB  
34   C CG  . PRO A 30  ? 0.3472 0.6313 0.5605 0.0016  0.1004  -0.0085 6   PRO A CG  
35   C CD  . PRO A 30  ? 0.1879 0.4638 0.4037 -0.0166 0.1010  0.0118  6   PRO A CD  
36   N N   . ASP A 31  ? 0.1845 0.3908 0.2969 0.0019  0.0889  -0.0054 7   ASP A N   
37   C CA  . ASP A 31  ? 0.2166 0.4072 0.2938 0.0068  0.0875  -0.0112 7   ASP A CA  
38   C C   . ASP A 31  ? 0.2287 0.4162 0.2916 -0.0045 0.0894  0.0085  7   ASP A C   
39   O O   . ASP A 31  ? 0.2418 0.4566 0.3083 -0.0107 0.1019  0.0237  7   ASP A O   
40   C CB  . ASP A 31  ? 0.2214 0.4370 0.2861 0.0183  0.0990  -0.0263 7   ASP A CB  
41   C CG  . ASP A 31  ? 0.2791 0.4916 0.3590 0.0322  0.0956  -0.0471 7   ASP A CG  
42   O OD1 . ASP A 31  ? 0.3023 0.4835 0.3749 0.0379  0.0838  -0.0573 7   ASP A OD1 
43   O OD2 . ASP A 31  ? 0.3020 0.5440 0.4039 0.0374  0.1048  -0.0516 7   ASP A OD2 
44   N N   . MET A 32  ? 0.2725 0.4284 0.3213 -0.0070 0.0776  0.0102  8   MET A N   
45   C CA  . MET A 32  ? 0.2462 0.3952 0.2852 -0.0160 0.0768  0.0291  8   MET A CA  
46   C C   . MET A 32  ? 0.2702 0.4067 0.2774 -0.0109 0.0716  0.0229  8   MET A C   
47   O O   . MET A 32  ? 0.2455 0.3645 0.2447 -0.0041 0.0639  0.0053  8   MET A O   
48   C CB  . MET A 32  ? 0.1856 0.3096 0.2452 -0.0247 0.0665  0.0374  8   MET A CB  
49   C CG  . MET A 32  ? 0.2438 0.3801 0.3392 -0.0318 0.0692  0.0423  8   MET A CG  
50   S SD  . MET A 32  ? 0.3291 0.4914 0.4388 -0.0438 0.0841  0.0701  8   MET A SD  
51   C CE  . MET A 32  ? 0.2697 0.3995 0.3801 -0.0522 0.0745  0.0867  8   MET A CE  
52   N N   . LYS A 33  ? 0.2371 0.3842 0.2284 -0.0147 0.0754  0.0388  9   LYS A N   
53   C CA  . LYS A 33  ? 0.2321 0.3683 0.1972 -0.0117 0.0678  0.0359  9   LYS A CA  
54   C C   . LYS A 33  ? 0.2833 0.3907 0.2568 -0.0175 0.0569  0.0471  9   LYS A C   
55   O O   . LYS A 33  ? 0.2500 0.3492 0.2468 -0.0247 0.0567  0.0607  9   LYS A O   
56   C CB  . LYS A 33  ? 0.2505 0.4174 0.1916 -0.0108 0.0759  0.0473  9   LYS A CB  
57   C CG  . LYS A 33  ? 0.3477 0.5484 0.2795 -0.0040 0.0882  0.0339  9   LYS A CG  
58   C CD  . LYS A 33  ? 0.4254 0.6572 0.3395 -0.0051 0.0969  0.0514  9   LYS A CD  
59   C CE  . LYS A 33  ? 0.4719 0.7284 0.3756 0.0033  0.1045  0.0323  9   LYS A CE  
60   N NZ  . LYS A 33  ? 0.4684 0.7463 0.3490 0.0043  0.1061  0.0431  9   LYS A NZ  
61   N N   . ILE A 34  ? 0.2390 0.3319 0.1958 -0.0141 0.0478  0.0394  10  ILE A N   
62   C CA  . ILE A 34  ? 0.2565 0.3230 0.2213 -0.0171 0.0374  0.0447  10  ILE A CA  
63   C C   . ILE A 34  ? 0.2913 0.3615 0.2359 -0.0150 0.0323  0.0501  10  ILE A C   
64   O O   . ILE A 34  ? 0.3023 0.3801 0.2280 -0.0101 0.0302  0.0353  10  ILE A O   
65   C CB  . ILE A 34  ? 0.2869 0.3308 0.2585 -0.0145 0.0301  0.0265  10  ILE A CB  
66   C CG1 . ILE A 34  ? 0.2819 0.3287 0.2696 -0.0140 0.0341  0.0190  10  ILE A CG1 
67   C CG2 . ILE A 34  ? 0.2943 0.3161 0.2767 -0.0174 0.0217  0.0313  10  ILE A CG2 
68   C CD1 . ILE A 34  ? 0.2481 0.2802 0.2362 -0.0088 0.0286  0.0024  10  ILE A CD1 
69   N N   . LYS A 35  ? 0.2378 0.3038 0.1890 -0.0183 0.0296  0.0710  11  LYS A N   
70   C CA  . LYS A 35  ? 0.2923 0.3618 0.2286 -0.0154 0.0225  0.0785  11  LYS A CA  
71   C C   . LYS A 35  ? 0.2722 0.3150 0.2265 -0.0161 0.0132  0.0812  11  LYS A C   
72   O O   . LYS A 35  ? 0.2776 0.3050 0.2558 -0.0202 0.0139  0.0894  11  LYS A O   
73   C CB  . LYS A 35  ? 0.2532 0.3458 0.1804 -0.0162 0.0274  0.1046  11  LYS A CB  
74   C CG  . LYS A 35  ? 0.4330 0.5586 0.3423 -0.0153 0.0392  0.1046  11  LYS A CG  
75   C CD  . LYS A 35  ? 0.4243 0.5691 0.3040 -0.0083 0.0365  0.0828  11  LYS A CD  
76   C CE  . LYS A 35  ? 0.4302 0.6093 0.2945 -0.0060 0.0496  0.0786  11  LYS A CE  
77   N NZ  . LYS A 35  ? 0.6105 0.8045 0.4522 0.0012  0.0457  0.0520  11  LYS A NZ  
78   N N   . LEU A 36  ? 0.2653 0.3047 0.2104 -0.0121 0.0046  0.0728  12  LEU A N   
79   C CA  . LEU A 36  ? 0.2417 0.2590 0.2044 -0.0114 -0.0029 0.0705  12  LEU A CA  
80   C C   . LEU A 36  ? 0.2769 0.3006 0.2328 -0.0069 -0.0117 0.0751  12  LEU A C   
81   O O   . LEU A 36  ? 0.2499 0.2910 0.1861 -0.0047 -0.0144 0.0672  12  LEU A O   
82   C CB  . LEU A 36  ? 0.2531 0.2567 0.2192 -0.0116 -0.0035 0.0481  12  LEU A CB  
83   C CG  . LEU A 36  ? 0.3102 0.2957 0.2921 -0.0104 -0.0091 0.0428  12  LEU A CG  
84   C CD1 . LEU A 36  ? 0.3046 0.2779 0.2944 -0.0119 -0.0068 0.0292  12  LEU A CD1 
85   C CD2 . LEU A 36  ? 0.2644 0.2541 0.2392 -0.0074 -0.0152 0.0355  12  LEU A CD2 
86   N N   . ARG A 37  ? 0.2286 0.2391 0.2038 -0.0050 -0.0169 0.0858  13  ARG A N   
87   C CA  . ARG A 37  ? 0.2321 0.2472 0.2078 0.0005  -0.0264 0.0873  13  ARG A CA  
88   C C   . ARG A 37  ? 0.2827 0.2774 0.2814 0.0024  -0.0295 0.0770  13  ARG A C   
89   O O   . ARG A 37  ? 0.2887 0.2658 0.3082 0.0015  -0.0276 0.0812  13  ARG A O   
90   C CB  . ARG A 37  ? 0.2717 0.2972 0.2484 0.0044  -0.0306 0.1146  13  ARG A CB  
91   C CG  . ARG A 37  ? 0.3299 0.3643 0.3094 0.0118  -0.0423 0.1176  13  ARG A CG  
92   C CD  . ARG A 37  ? 0.3222 0.3751 0.2937 0.0165  -0.0471 0.1471  13  ARG A CD  
93   N NE  . ARG A 37  ? 0.3764 0.4419 0.3515 0.0249  -0.0599 0.1522  13  ARG A NE  
94   C CZ  . ARG A 37  ? 0.3425 0.3919 0.3471 0.0309  -0.0660 0.1564  13  ARG A CZ  
95   N NH1 . ARG A 37  ? 0.3124 0.3319 0.3439 0.0293  -0.0608 0.1530  13  ARG A NH1 
96   N NH2 . ARG A 37  ? 0.3621 0.4276 0.3705 0.0394  -0.0777 0.1619  13  ARG A NH2 
97   N N   . MET A 38  ? 0.2007 0.2000 0.1975 0.0046  -0.0340 0.0627  14  MET A N   
98   C CA  . MET A 38  ? 0.3224 0.3096 0.3391 0.0076  -0.0359 0.0530  14  MET A CA  
99   C C   . MET A 38  ? 0.2692 0.2675 0.2950 0.0143  -0.0446 0.0583  14  MET A C   
100  O O   . MET A 38  ? 0.2743 0.2916 0.2875 0.0143  -0.0493 0.0557  14  MET A O   
101  C CB  . MET A 38  ? 0.2449 0.2298 0.2560 0.0040  -0.0317 0.0326  14  MET A CB  
102  C CG  . MET A 38  ? 0.2285 0.2063 0.2573 0.0072  -0.0314 0.0223  14  MET A CG  
103  S SD  . MET A 38  ? 0.2435 0.2274 0.2652 0.0032  -0.0274 0.0055  14  MET A SD  
104  C CE  . MET A 38  ? 0.2224 0.1913 0.2419 0.0014  -0.0208 -0.0009 14  MET A CE  
105  N N   . GLU A 39  ? 0.2361 0.2235 0.2862 0.0204  -0.0475 0.0642  15  GLU A N   
106  C CA  . GLU A 39  ? 0.2697 0.2670 0.3353 0.0287  -0.0556 0.0668  15  GLU A CA  
107  C C   . GLU A 39  ? 0.3005 0.2909 0.3847 0.0314  -0.0525 0.0481  15  GLU A C   
108  O O   . GLU A 39  ? 0.2185 0.1907 0.3151 0.0319  -0.0480 0.0420  15  GLU A O   
109  C CB  . GLU A 39  ? 0.2549 0.2468 0.3370 0.0360  -0.0618 0.0905  15  GLU A CB  
110  C CG  . GLU A 39  ? 0.3604 0.3644 0.4608 0.0465  -0.0716 0.0947  15  GLU A CG  
111  C CD  . GLU A 39  ? 0.5151 0.5239 0.6203 0.0534  -0.0801 0.1240  15  GLU A CD  
112  O OE1 . GLU A 39  ? 0.4544 0.4479 0.5609 0.0507  -0.0766 0.1419  15  GLU A OE1 
113  O OE2 . GLU A 39  ? 0.3810 0.4099 0.4914 0.0616  -0.0904 0.1305  15  GLU A OE2 
114  N N   . GLY A 40  ? 0.2336 0.2413 0.3198 0.0326  -0.0544 0.0377  16  GLY A N   
115  C CA  . GLY A 40  ? 0.2675 0.2751 0.3652 0.0334  -0.0484 0.0198  16  GLY A CA  
116  C C   . GLY A 40  ? 0.2024 0.2286 0.3215 0.0409  -0.0529 0.0163  16  GLY A C   
117  O O   . GLY A 40  ? 0.2218 0.2644 0.3434 0.0437  -0.0619 0.0254  16  GLY A O   
118  N N   . ASN A 41  ? 0.2096 0.2368 0.3437 0.0445  -0.0464 0.0019  17  ASN A N   
119  C CA  . ASN A 41  ? 0.1790 0.2288 0.3344 0.0503  -0.0473 -0.0050 17  ASN A CA  
120  C C   . ASN A 41  ? 0.1950 0.2513 0.3505 0.0474  -0.0351 -0.0218 17  ASN A C   
121  O O   . ASN A 41  ? 0.2390 0.2837 0.3979 0.0519  -0.0293 -0.0311 17  ASN A O   
122  C CB  . ASN A 41  ? 0.2124 0.2605 0.3980 0.0651  -0.0538 -0.0011 17  ASN A CB  
123  C CG  . ASN A 41  ? 0.3469 0.4236 0.5557 0.0718  -0.0577 -0.0041 17  ASN A CG  
124  O OD1 . ASN A 41  ? 0.3133 0.4034 0.5371 0.0750  -0.0497 -0.0192 17  ASN A OD1 
125  N ND2 . ASN A 41  ? 0.4892 0.5791 0.7017 0.0747  -0.0703 0.0103  17  ASN A ND2 
126  N N   . VAL A 42  ? 0.1821 0.2586 0.3352 0.0397  -0.0313 -0.0255 18  VAL A N   
127  C CA  . VAL A 42  ? 0.1667 0.2525 0.3172 0.0352  -0.0184 -0.0362 18  VAL A CA  
128  C C   . VAL A 42  ? 0.1651 0.2820 0.3405 0.0369  -0.0158 -0.0406 18  VAL A C   
129  O O   . VAL A 42  ? 0.1726 0.3040 0.3549 0.0309  -0.0220 -0.0359 18  VAL A O   
130  C CB  . VAL A 42  ? 0.1738 0.2514 0.2990 0.0215  -0.0139 -0.0334 18  VAL A CB  
131  C CG1 . VAL A 42  ? 0.1572 0.2482 0.2819 0.0167  -0.0009 -0.0390 18  VAL A CG1 
132  C CG2 . VAL A 42  ? 0.1571 0.2080 0.2612 0.0210  -0.0152 -0.0305 18  VAL A CG2 
133  N N   . ASN A 43  ? 0.1878 0.3178 0.3781 0.0452  -0.0068 -0.0513 19  ASN A N   
134  C CA  . ASN A 43  ? 0.1507 0.3142 0.3697 0.0491  -0.0027 -0.0565 19  ASN A CA  
135  C C   . ASN A 43  ? 0.2280 0.4017 0.4704 0.0553  -0.0172 -0.0502 19  ASN A C   
136  O O   . ASN A 43  ? 0.2117 0.4130 0.4727 0.0511  -0.0189 -0.0494 19  ASN A O   
137  C CB  . ASN A 43  ? 0.1950 0.3785 0.4114 0.0346  0.0075  -0.0546 19  ASN A CB  
138  C CG  . ASN A 43  ? 0.2326 0.4265 0.4406 0.0345  0.0248  -0.0614 19  ASN A CG  
139  O OD1 . ASN A 43  ? 0.1722 0.3505 0.3632 0.0409  0.0279  -0.0679 19  ASN A OD1 
140  N ND2 . ASN A 43  ? 0.1811 0.4046 0.4021 0.0268  0.0362  -0.0598 19  ASN A ND2 
141  N N   . GLY A 44  ? 0.1597 0.3123 0.4019 0.0647  -0.0285 -0.0440 20  GLY A N   
142  C CA  . GLY A 44  ? 0.2454 0.4083 0.5079 0.0729  -0.0434 -0.0347 20  GLY A CA  
143  C C   . GLY A 44  ? 0.2067 0.3691 0.4510 0.0631  -0.0552 -0.0222 20  GLY A C   
144  O O   . GLY A 44  ? 0.2699 0.4430 0.5261 0.0703  -0.0693 -0.0124 20  GLY A O   
145  N N   . HIS A 45  ? 0.2380 0.3894 0.4537 0.0483  -0.0506 -0.0224 21  HIS A N   
146  C CA  . HIS A 45  ? 0.2416 0.3952 0.4399 0.0394  -0.0610 -0.0154 21  HIS A CA  
147  C C   . HIS A 45  ? 0.2649 0.3907 0.4365 0.0405  -0.0647 -0.0048 21  HIS A C   
148  O O   . HIS A 45  ? 0.2422 0.3457 0.3954 0.0354  -0.0555 -0.0073 21  HIS A O   
149  C CB  . HIS A 45  ? 0.2200 0.3794 0.4092 0.0228  -0.0542 -0.0233 21  HIS A CB  
150  C CG  . HIS A 45  ? 0.3695 0.5313 0.5424 0.0141  -0.0648 -0.0217 21  HIS A CG  
151  N ND1 . HIS A 45  ? 0.3340 0.5238 0.5231 0.0092  -0.0747 -0.0265 21  HIS A ND1 
152  C CD2 . HIS A 45  ? 0.3584 0.5012 0.5017 0.0099  -0.0673 -0.0182 21  HIS A CD2 
153  C CE1 . HIS A 45  ? 0.3745 0.5619 0.5427 0.0028  -0.0835 -0.0277 21  HIS A CE1 
154  N NE2 . HIS A 45  ? 0.3279 0.4875 0.4678 0.0035  -0.0783 -0.0225 21  HIS A NE2 
155  N N   . HIS A 46  ? 0.2025 0.3329 0.3729 0.0472  -0.0782 0.0084  22  HIS A N   
156  C CA  . HIS A 46  ? 0.2477 0.3567 0.3956 0.0482  -0.0811 0.0221  22  HIS A CA  
157  C C   . HIS A 46  ? 0.2858 0.3962 0.4028 0.0363  -0.0821 0.0208  22  HIS A C   
158  O O   . HIS A 46  ? 0.2812 0.4139 0.3966 0.0307  -0.0884 0.0140  22  HIS A O   
159  C CB  . HIS A 46  ? 0.2830 0.3982 0.4421 0.0611  -0.0943 0.0409  22  HIS A CB  
160  C CG  . HIS A 46  ? 0.4717 0.5713 0.6079 0.0608  -0.0970 0.0593  22  HIS A CG  
161  N ND1 . HIS A 46  ? 0.4318 0.5474 0.5421 0.0567  -0.1047 0.0679  22  HIS A ND1 
162  C CD2 . HIS A 46  ? 0.5332 0.6049 0.6700 0.0634  -0.0921 0.0701  22  HIS A CD2 
163  C CE1 . HIS A 46  ? 0.4906 0.5907 0.5851 0.0571  -0.1030 0.0853  22  HIS A CE1 
164  N NE2 . HIS A 46  ? 0.4568 0.5289 0.5688 0.0604  -0.0956 0.0877  22  HIS A NE2 
165  N N   . PHE A 47  ? 0.2216 0.3096 0.3168 0.0327  -0.0762 0.0258  23  PHE A N   
166  C CA  . PHE A 47  ? 0.2399 0.3290 0.3070 0.0234  -0.0760 0.0232  23  PHE A CA  
167  C C   . PHE A 47  ? 0.2427 0.3146 0.2916 0.0244  -0.0729 0.0366  23  PHE A C   
168  O O   . PHE A 47  ? 0.2164 0.2697 0.2758 0.0291  -0.0690 0.0448  23  PHE A O   
169  C CB  . PHE A 47  ? 0.2122 0.2948 0.2751 0.0125  -0.0665 0.0060  23  PHE A CB  
170  C CG  . PHE A 47  ? 0.1914 0.2517 0.2576 0.0122  -0.0544 0.0030  23  PHE A CG  
171  C CD1 . PHE A 47  ? 0.2540 0.3171 0.3416 0.0160  -0.0498 -0.0025 23  PHE A CD1 
172  C CD2 . PHE A 47  ? 0.2742 0.3152 0.3223 0.0086  -0.0480 0.0042  23  PHE A CD2 
173  C CE1 . PHE A 47  ? 0.1962 0.2436 0.2839 0.0166  -0.0397 -0.0074 23  PHE A CE1 
174  C CE2 . PHE A 47  ? 0.3041 0.3288 0.3548 0.0087  -0.0390 0.0002  23  PHE A CE2 
175  C CZ  . PHE A 47  ? 0.2137 0.2419 0.2825 0.0127  -0.0352 -0.0062 23  PHE A CZ  
176  N N   . VAL A 48  ? 0.2404 0.3207 0.2640 0.0196  -0.0748 0.0374  24  VAL A N   
177  C CA  . VAL A 48  ? 0.2796 0.3494 0.2843 0.0185  -0.0697 0.0488  24  VAL A CA  
178  C C   . VAL A 48  ? 0.2449 0.3158 0.2286 0.0101  -0.0642 0.0337  24  VAL A C   
179  O O   . VAL A 48  ? 0.2603 0.3492 0.2359 0.0072  -0.0699 0.0215  24  VAL A O   
180  C CB  . VAL A 48  ? 0.2630 0.3495 0.2572 0.0249  -0.0779 0.0708  24  VAL A CB  
181  C CG1 . VAL A 48  ? 0.3319 0.4112 0.3074 0.0220  -0.0699 0.0832  24  VAL A CG1 
182  C CG2 . VAL A 48  ? 0.2493 0.3324 0.2688 0.0348  -0.0845 0.0879  24  VAL A CG2 
183  N N   . ILE A 49  ? 0.2228 0.2752 0.2004 0.0066  -0.0542 0.0333  25  ILE A N   
184  C CA  . ILE A 49  ? 0.2121 0.2626 0.1739 0.0005  -0.0482 0.0196  25  ILE A CA  
185  C C   . ILE A 49  ? 0.2957 0.3442 0.2435 0.0008  -0.0420 0.0310  25  ILE A C   
186  O O   . ILE A 49  ? 0.2752 0.3092 0.2335 0.0017  -0.0377 0.0430  25  ILE A O   
187  C CB  . ILE A 49  ? 0.2376 0.2690 0.2105 -0.0039 -0.0413 0.0066  25  ILE A CB  
188  C CG1 . ILE A 49  ? 0.2134 0.2508 0.2017 -0.0054 -0.0455 -0.0026 25  ILE A CG1 
189  C CG2 . ILE A 49  ? 0.2526 0.2780 0.2131 -0.0084 -0.0352 -0.0048 25  ILE A CG2 
190  C CD1 . ILE A 49  ? 0.1968 0.2189 0.1959 -0.0089 -0.0376 -0.0101 25  ILE A CD1 
191  N N   . ASP A 50  ? 0.2349 0.3001 0.1617 -0.0001 -0.0414 0.0259  26  ASP A N   
192  C CA  . ASP A 50  ? 0.2236 0.2927 0.1371 -0.0002 -0.0333 0.0350  26  ASP A CA  
193  C C   . ASP A 50  ? 0.2766 0.3356 0.1881 -0.0037 -0.0253 0.0173  26  ASP A C   
194  O O   . ASP A 50  ? 0.2640 0.3214 0.1751 -0.0055 -0.0275 -0.0024 26  ASP A O   
195  C CB  . ASP A 50  ? 0.2476 0.3480 0.1369 0.0030  -0.0366 0.0415  26  ASP A CB  
196  C CG  . ASP A 50  ? 0.3251 0.4367 0.2157 0.0078  -0.0436 0.0675  26  ASP A CG  
197  O OD1 . ASP A 50  ? 0.3804 0.4722 0.2935 0.0087  -0.0443 0.0807  26  ASP A OD1 
198  O OD2 . ASP A 50  ? 0.3682 0.5094 0.2379 0.0116  -0.0489 0.0742  26  ASP A OD2 
199  N N   . GLY A 51  ? 0.2709 0.3232 0.1844 -0.0048 -0.0164 0.0250  27  GLY A N   
200  C CA  . GLY A 51  ? 0.2691 0.3136 0.1829 -0.0063 -0.0092 0.0105  27  GLY A CA  
201  C C   . GLY A 51  ? 0.3051 0.3664 0.2079 -0.0054 -0.0006 0.0153  27  GLY A C   
202  O O   . GLY A 51  ? 0.2375 0.3073 0.1402 -0.0060 0.0028  0.0358  27  GLY A O   
203  N N   . ASP A 52  ? 0.2834 0.3499 0.1795 -0.0039 0.0035  -0.0032 28  ASP A N   
204  C CA  . ASP A 52  ? 0.2940 0.3799 0.1816 -0.0019 0.0134  -0.0024 28  ASP A CA  
205  C C   . ASP A 52  ? 0.3335 0.4060 0.2326 -0.0004 0.0178  -0.0197 28  ASP A C   
206  O O   . ASP A 52  ? 0.2869 0.3503 0.1869 0.0013  0.0136  -0.0393 28  ASP A O   
207  C CB  . ASP A 52  ? 0.3096 0.4267 0.1719 0.0020  0.0129  -0.0099 28  ASP A CB  
208  C CG  . ASP A 52  ? 0.5040 0.6469 0.3554 0.0054  0.0249  -0.0130 28  ASP A CG  
209  O OD1 . ASP A 52  ? 0.4830 0.6190 0.3474 0.0063  0.0324  -0.0210 28  ASP A OD1 
210  O OD2 . ASP A 52  ? 0.7180 0.8916 0.5481 0.0079  0.0267  -0.0068 28  ASP A OD2 
211  N N   . GLY A 53  ? 0.3040 0.3751 0.2154 -0.0012 0.0253  -0.0118 29  GLY A N   
212  C CA  . GLY A 53  ? 0.3023 0.3609 0.2273 0.0013  0.0275  -0.0252 29  GLY A CA  
213  C C   . GLY A 53  ? 0.2292 0.3028 0.1634 0.0025  0.0374  -0.0206 29  GLY A C   
214  O O   . GLY A 53  ? 0.2156 0.3105 0.1454 0.0002  0.0443  -0.0066 29  GLY A O   
215  N N   . THR A 54  ? 0.2253 0.2892 0.1743 0.0061  0.0383  -0.0310 30  THR A N   
216  C CA  . THR A 54  ? 0.2476 0.3265 0.2111 0.0078  0.0465  -0.0288 30  THR A CA  
217  C C   . THR A 54  ? 0.2597 0.3193 0.2429 0.0088  0.0411  -0.0306 30  THR A C   
218  O O   . THR A 54  ? 0.2507 0.2880 0.2332 0.0105  0.0333  -0.0369 30  THR A O   
219  C CB  . THR A 54  ? 0.2613 0.3614 0.2206 0.0163  0.0547  -0.0457 30  THR A CB  
220  O OG1 . THR A 54  ? 0.3165 0.3970 0.2775 0.0225  0.0485  -0.0650 30  THR A OG1 
221  C CG2 . THR A 54  ? 0.2704 0.3985 0.2061 0.0165  0.0609  -0.0452 30  THR A CG2 
222  N N   . GLY A 55  ? 0.2126 0.2840 0.2141 0.0077  0.0453  -0.0246 31  GLY A N   
223  C CA  . GLY A 55  ? 0.2240 0.2824 0.2425 0.0102  0.0387  -0.0277 31  GLY A CA  
224  C C   . GLY A 55  ? 0.1786 0.2576 0.2198 0.0110  0.0436  -0.0259 31  GLY A C   
225  O O   . GLY A 55  ? 0.2039 0.3069 0.2500 0.0076  0.0534  -0.0197 31  GLY A O   
226  N N   . LYS A 56  ? 0.1768 0.2487 0.2326 0.0154  0.0364  -0.0299 32  LYS A N   
227  C CA  . LYS A 56  ? 0.1798 0.2720 0.2616 0.0167  0.0378  -0.0296 32  LYS A CA  
228  C C   . LYS A 56  ? 0.2034 0.2885 0.2970 0.0099  0.0276  -0.0238 32  LYS A C   
229  O O   . LYS A 56  ? 0.1876 0.2592 0.2795 0.0148  0.0172  -0.0273 32  LYS A O   
230  C CB  . LYS A 56  ? 0.2225 0.3171 0.3138 0.0303  0.0363  -0.0407 32  LYS A CB  
231  C CG  . LYS A 56  ? 0.3137 0.4205 0.4001 0.0380  0.0470  -0.0513 32  LYS A CG  
232  C CD  . LYS A 56  ? 0.3741 0.4894 0.4815 0.0518  0.0466  -0.0616 32  LYS A CD  
233  C CE  . LYS A 56  ? 0.3788 0.5054 0.4828 0.0609  0.0570  -0.0767 32  LYS A CE  
234  N NZ  . LYS A 56  ? 0.2778 0.4438 0.3895 0.0588  0.0716  -0.0764 32  LYS A NZ  
235  N N   . PRO A 57  ? 0.1751 0.2686 0.2808 -0.0014 0.0300  -0.0150 33  PRO A N   
236  C CA  . PRO A 57  ? 0.1589 0.2431 0.2764 -0.0082 0.0192  -0.0139 33  PRO A CA  
237  C C   . PRO A 57  ? 0.1767 0.2708 0.3120 -0.0030 0.0096  -0.0218 33  PRO A C   
238  O O   . PRO A 57  ? 0.1773 0.2603 0.3088 -0.0025 -0.0021 -0.0260 33  PRO A O   
239  C CB  . PRO A 57  ? 0.1434 0.2378 0.2796 -0.0210 0.0255  -0.0030 33  PRO A CB  
240  C CG  . PRO A 57  ? 0.1599 0.2597 0.2785 -0.0209 0.0380  0.0054  33  PRO A CG  
241  C CD  . PRO A 57  ? 0.1659 0.2759 0.2739 -0.0087 0.0425  -0.0048 33  PRO A CD  
242  N N   . PHE A 58  ? 0.1697 0.2873 0.3236 0.0023  0.0140  -0.0244 34  PHE A N   
243  C CA  . PHE A 58  ? 0.1370 0.2687 0.3117 0.0073  0.0034  -0.0305 34  PHE A CA  
244  C C   . PHE A 58  ? 0.1986 0.3201 0.3589 0.0222  -0.0043 -0.0346 34  PHE A C   
245  O O   . PHE A 58  ? 0.1828 0.3141 0.3545 0.0279  -0.0160 -0.0376 34  PHE A O   
246  C CB  . PHE A 58  ? 0.1628 0.3281 0.3704 0.0062  0.0108  -0.0307 34  PHE A CB  
247  C CG  . PHE A 58  ? 0.1806 0.3570 0.4074 -0.0099 0.0187  -0.0228 34  PHE A CG  
248  C CD1 . PHE A 58  ? 0.1370 0.3164 0.3880 -0.0211 0.0091  -0.0243 34  PHE A CD1 
249  C CD2 . PHE A 58  ? 0.2760 0.4593 0.4964 -0.0141 0.0353  -0.0136 34  PHE A CD2 
250  C CE1 . PHE A 58  ? 0.2892 0.4744 0.5627 -0.0370 0.0162  -0.0151 34  PHE A CE1 
251  C CE2 . PHE A 58  ? 0.2367 0.4291 0.4753 -0.0293 0.0431  -0.0014 34  PHE A CE2 
252  C CZ  . PHE A 58  ? 0.2322 0.4234 0.4998 -0.0413 0.0337  -0.0012 34  PHE A CZ  
253  N N   . GLU A 59  ? 0.1650 0.2678 0.3024 0.0282  0.0012  -0.0341 35  GLU A N   
254  C CA  . GLU A 59  ? 0.1554 0.2412 0.2795 0.0398  -0.0058 -0.0347 35  GLU A CA  
255  C C   . GLU A 59  ? 0.1833 0.2450 0.2826 0.0354  -0.0116 -0.0308 35  GLU A C   
256  O O   . GLU A 59  ? 0.2337 0.2820 0.3222 0.0430  -0.0174 -0.0278 35  GLU A O   
257  C CB  . GLU A 59  ? 0.1909 0.2697 0.3106 0.0489  0.0031  -0.0389 35  GLU A CB  
258  C CG  . GLU A 59  ? 0.2162 0.3204 0.3615 0.0576  0.0093  -0.0451 35  GLU A CG  
259  C CD  . GLU A 59  ? 0.2975 0.3924 0.4419 0.0704  0.0150  -0.0536 35  GLU A CD  
260  O OE1 . GLU A 59  ? 0.3428 0.4106 0.4680 0.0709  0.0141  -0.0544 35  GLU A OE1 
261  O OE2 . GLU A 59  ? 0.2829 0.3986 0.4489 0.0799  0.0207  -0.0612 35  GLU A OE2 
262  N N   . GLY A 60  ? 0.1713 0.2284 0.2639 0.0237  -0.0097 -0.0297 36  GLY A N   
263  C CA  . GLY A 60  ? 0.1993 0.2363 0.2704 0.0204  -0.0136 -0.0276 36  GLY A CA  
264  C C   . GLY A 60  ? 0.2383 0.2560 0.2906 0.0234  -0.0086 -0.0257 36  GLY A C   
265  O O   . GLY A 60  ? 0.2034 0.2072 0.2413 0.0248  -0.0128 -0.0229 36  GLY A O   
266  N N   . LYS A 61  ? 0.1902 0.2094 0.2428 0.0238  0.0006  -0.0281 37  LYS A N   
267  C CA  . LYS A 61  ? 0.1999 0.2029 0.2382 0.0261  0.0042  -0.0302 37  LYS A CA  
268  C C   . LYS A 61  ? 0.2263 0.2314 0.2547 0.0190  0.0113  -0.0309 37  LYS A C   
269  O O   . LYS A 61  ? 0.2058 0.2283 0.2410 0.0162  0.0175  -0.0302 37  LYS A O   
270  C CB  . LYS A 61  ? 0.1788 0.1825 0.2266 0.0367  0.0068  -0.0365 37  LYS A CB  
271  C CG  . LYS A 61  ? 0.2286 0.2283 0.2863 0.0458  -0.0012 -0.0323 37  LYS A CG  
272  C CD  . LYS A 61  ? 0.2278 0.2242 0.2998 0.0581  0.0007  -0.0383 37  LYS A CD  
273  C CE  . LYS A 61  ? 0.2391 0.2256 0.3180 0.0671  -0.0086 -0.0287 37  LYS A CE  
274  N NZ  . LYS A 61  ? 0.2438 0.2184 0.3391 0.0795  -0.0079 -0.0327 37  LYS A NZ  
275  N N   . GLN A 62  ? 0.1654 0.1555 0.1788 0.0163  0.0105  -0.0311 38  GLN A N   
276  C CA  . GLN A 62  ? 0.2091 0.2039 0.2118 0.0113  0.0154  -0.0313 38  GLN A CA  
277  C C   . GLN A 62  ? 0.2581 0.2390 0.2493 0.0115  0.0137  -0.0367 38  GLN A C   
278  O O   . GLN A 62  ? 0.2108 0.1761 0.2020 0.0119  0.0089  -0.0354 38  GLN A O   
279  C CB  . GLN A 62  ? 0.2166 0.2135 0.2187 0.0032  0.0141  -0.0217 38  GLN A CB  
280  C CG  . GLN A 62  ? 0.2154 0.1967 0.2131 0.0010  0.0073  -0.0196 38  GLN A CG  
281  C CD  . GLN A 62  ? 0.2500 0.2310 0.2504 -0.0052 0.0058  -0.0130 38  GLN A CD  
282  O OE1 . GLN A 62  ? 0.2014 0.1874 0.1985 -0.0083 0.0091  -0.0073 38  GLN A OE1 
283  N NE2 . GLN A 62  ? 0.2190 0.1951 0.2260 -0.0061 0.0004  -0.0138 38  GLN A NE2 
284  N N   . SER A 63  ? 0.2584 0.2479 0.2403 0.0109  0.0176  -0.0424 39  SER A N   
285  C CA  A SER A 63  ? 0.2673 0.2478 0.2404 0.0096  0.0149  -0.0500 39  SER A CA  
286  C CA  B SER A 63  ? 0.2664 0.2474 0.2395 0.0098  0.0151  -0.0505 39  SER A CA  
287  C C   . SER A 63  ? 0.3160 0.3095 0.2753 0.0050  0.0153  -0.0465 39  SER A C   
288  O O   . SER A 63  ? 0.2982 0.3097 0.2533 0.0044  0.0203  -0.0405 39  SER A O   
289  C CB  A SER A 63  ? 0.3268 0.3053 0.3045 0.0161  0.0167  -0.0665 39  SER A CB  
290  C CB  B SER A 63  ? 0.3300 0.3120 0.3062 0.0163  0.0175  -0.0675 39  SER A CB  
291  O OG  A SER A 63  ? 0.3243 0.3249 0.2940 0.0189  0.0226  -0.0755 39  SER A OG  
292  O OG  B SER A 63  ? 0.2973 0.2632 0.2887 0.0217  0.0157  -0.0700 39  SER A OG  
293  N N   . MET A 64  ? 0.2656 0.2513 0.2195 0.0015  0.0100  -0.0483 40  MET A N   
294  C CA  . MET A 64  ? 0.2572 0.2556 0.1993 -0.0017 0.0081  -0.0432 40  MET A CA  
295  C C   . MET A 64  ? 0.3165 0.3145 0.2538 -0.0030 0.0027  -0.0558 40  MET A C   
296  O O   . MET A 64  ? 0.2993 0.2807 0.2466 -0.0051 -0.0007 -0.0605 40  MET A O   
297  C CB  . MET A 64  ? 0.2792 0.2708 0.2255 -0.0056 0.0048  -0.0285 40  MET A CB  
298  C CG  . MET A 64  ? 0.2945 0.2985 0.2321 -0.0073 0.0021  -0.0197 40  MET A CG  
299  S SD  . MET A 64  ? 0.2916 0.2882 0.2403 -0.0096 0.0004  -0.0022 40  MET A SD  
300  C CE  . MET A 64  ? 0.3695 0.3714 0.3255 -0.0103 0.0077  0.0057  40  MET A CE  
301  N N   . ASP A 65  ? 0.2678 0.2866 0.1907 -0.0022 0.0017  -0.0601 41  ASP A N   
302  C CA  . ASP A 65  ? 0.3051 0.3294 0.2235 -0.0043 -0.0060 -0.0712 41  ASP A CA  
303  C C   . ASP A 65  ? 0.3084 0.3388 0.2234 -0.0072 -0.0115 -0.0557 41  ASP A C   
304  O O   . ASP A 65  ? 0.2923 0.3366 0.1978 -0.0057 -0.0097 -0.0404 41  ASP A O   
305  C CB  . ASP A 65  ? 0.3236 0.3717 0.2262 -0.0005 -0.0057 -0.0875 41  ASP A CB  
306  C CG  . ASP A 65  ? 0.4955 0.5379 0.4050 0.0041  -0.0006 -0.1069 41  ASP A CG  
307  O OD1 . ASP A 65  ? 0.4985 0.5176 0.4258 0.0026  -0.0034 -0.1177 41  ASP A OD1 
308  O OD2 . ASP A 65  ? 0.4725 0.5342 0.3715 0.0096  0.0068  -0.1104 41  ASP A OD2 
309  N N   . LEU A 66  ? 0.2858 0.3071 0.2115 -0.0110 -0.0179 -0.0587 42  LEU A N   
310  C CA  . LEU A 66  ? 0.2646 0.2899 0.1933 -0.0124 -0.0231 -0.0454 42  LEU A CA  
311  C C   . LEU A 66  ? 0.2481 0.2892 0.1754 -0.0142 -0.0327 -0.0558 42  LEU A C   
312  O O   . LEU A 66  ? 0.2655 0.3038 0.1993 -0.0174 -0.0354 -0.0743 42  LEU A O   
313  C CB  . LEU A 66  ? 0.2697 0.2751 0.2153 -0.0149 -0.0214 -0.0393 42  LEU A CB  
314  C CG  . LEU A 66  ? 0.2103 0.2028 0.1584 -0.0131 -0.0145 -0.0302 42  LEU A CG  
315  C CD1 . LEU A 66  ? 0.2689 0.2450 0.2292 -0.0150 -0.0126 -0.0310 42  LEU A CD1 
316  C CD2 . LEU A 66  ? 0.2466 0.2437 0.1942 -0.0111 -0.0144 -0.0143 42  LEU A CD2 
317  N N   . GLU A 67  ? 0.2605 0.3184 0.1823 -0.0119 -0.0388 -0.0439 43  GLU A N   
318  C CA  . GLU A 67  ? 0.3057 0.3844 0.2262 -0.0127 -0.0500 -0.0529 43  GLU A CA  
319  C C   . GLU A 67  ? 0.3554 0.4393 0.2859 -0.0107 -0.0559 -0.0364 43  GLU A C   
320  O O   . GLU A 67  ? 0.2694 0.3559 0.1942 -0.0058 -0.0545 -0.0166 43  GLU A O   
321  C CB  . GLU A 67  ? 0.2908 0.3975 0.1863 -0.0086 -0.0535 -0.0587 43  GLU A CB  
322  C CG  . GLU A 67  ? 0.4579 0.5912 0.3505 -0.0087 -0.0677 -0.0689 43  GLU A CG  
323  C CD  . GLU A 67  ? 0.4845 0.6384 0.3566 -0.0048 -0.0681 -0.0777 43  GLU A CD  
324  O OE1 . GLU A 67  ? 0.6177 0.7690 0.4782 -0.0025 -0.0581 -0.0812 43  GLU A OE1 
325  O OE2 . GLU A 67  ? 0.5263 0.6993 0.3963 -0.0036 -0.0777 -0.0808 43  GLU A OE2 
326  N N   . VAL A 68  ? 0.2848 0.3703 0.2339 -0.0145 -0.0619 -0.0444 44  VAL A N   
327  C CA  . VAL A 68  ? 0.3322 0.4273 0.2946 -0.0112 -0.0685 -0.0322 44  VAL A CA  
328  C C   . VAL A 68  ? 0.3129 0.4386 0.2612 -0.0059 -0.0805 -0.0277 44  VAL A C   
329  O O   . VAL A 68  ? 0.3016 0.4472 0.2449 -0.0086 -0.0892 -0.0447 44  VAL A O   
330  C CB  . VAL A 68  ? 0.2950 0.3882 0.2835 -0.0174 -0.0703 -0.0427 44  VAL A CB  
331  C CG1 . VAL A 68  ? 0.3173 0.4236 0.3226 -0.0124 -0.0765 -0.0317 44  VAL A CG1 
332  C CG2 . VAL A 68  ? 0.2489 0.3152 0.2470 -0.0222 -0.0581 -0.0446 44  VAL A CG2 
333  N N   . LYS A 69  ? 0.2449 0.3751 0.1876 0.0017  -0.0817 -0.0047 45  LYS A N   
334  C CA  . LYS A 69  ? 0.2725 0.4330 0.1990 0.0084  -0.0927 0.0067  45  LYS A CA  
335  C C   . LYS A 69  ? 0.2683 0.4443 0.2140 0.0135  -0.1052 0.0144  45  LYS A C   
336  O O   . LYS A 69  ? 0.3370 0.5435 0.2726 0.0180  -0.1180 0.0165  45  LYS A O   
337  C CB  . LYS A 69  ? 0.3394 0.4962 0.2509 0.0138  -0.0864 0.0326  45  LYS A CB  
338  C CG  . LYS A 69  ? 0.3173 0.4649 0.2109 0.0100  -0.0737 0.0279  45  LYS A CG  
339  C CD  . LYS A 69  ? 0.4047 0.5702 0.2801 0.0069  -0.0757 0.0016  45  LYS A CD  
340  C CE  . LYS A 69  ? 0.4975 0.6913 0.3529 0.0118  -0.0816 0.0055  45  LYS A CE  
341  N NZ  . LYS A 69  ? 0.7569 0.9592 0.5985 0.0096  -0.0783 -0.0200 45  LYS A NZ  
342  N N   . GLU A 70  ? 0.2593 0.4166 0.2326 0.0139  -0.1014 0.0178  46  GLU A N   
343  C CA  . GLU A 70  ? 0.3051 0.4755 0.3028 0.0201  -0.1112 0.0243  46  GLU A CA  
344  C C   . GLU A 70  ? 0.2522 0.4088 0.2779 0.0148  -0.1044 0.0105  46  GLU A C   
345  O O   . GLU A 70  ? 0.2300 0.3598 0.2576 0.0113  -0.0914 0.0085  46  GLU A O   
346  C CB  . GLU A 70  ? 0.3112 0.4742 0.3153 0.0311  -0.1121 0.0518  46  GLU A CB  
347  C CG  . GLU A 70  ? 0.4145 0.5923 0.3920 0.0363  -0.1171 0.0721  46  GLU A CG  
348  C CD  . GLU A 70  ? 0.4342 0.6018 0.4247 0.0465  -0.1185 0.1022  46  GLU A CD  
349  O OE1 . GLU A 70  ? 0.5319 0.6967 0.5524 0.0535  -0.1239 0.1056  46  GLU A OE1 
350  O OE2 . GLU A 70  ? 0.4563 0.6149 0.4298 0.0467  -0.1119 0.1195  46  GLU A OE2 
351  N N   . GLY A 71  ? 0.2958 0.4743 0.3432 0.0143  -0.1133 0.0016  47  GLY A N   
352  C CA  . GLY A 71  ? 0.3320 0.5037 0.4079 0.0098  -0.1059 -0.0082 47  GLY A CA  
353  C C   . GLY A 71  ? 0.3450 0.5096 0.4228 -0.0041 -0.0988 -0.0273 47  GLY A C   
354  O O   . GLY A 71  ? 0.3177 0.4733 0.4147 -0.0087 -0.0888 -0.0316 47  GLY A O   
355  N N   . GLY A 72  ? 0.2954 0.4644 0.3546 -0.0105 -0.1034 -0.0386 48  GLY A N   
356  C CA  . GLY A 72  ? 0.2938 0.4561 0.3610 -0.0235 -0.0993 -0.0574 48  GLY A CA  
357  C C   . GLY A 72  ? 0.3430 0.5325 0.4378 -0.0301 -0.1099 -0.0706 48  GLY A C   
358  O O   . GLY A 72  ? 0.2870 0.5060 0.3849 -0.0243 -0.1245 -0.0696 48  GLY A O   
359  N N   . PRO A 73  ? 0.2523 0.4338 0.3703 -0.0427 -0.1032 -0.0819 49  PRO A N   
360  C CA  . PRO A 73  ? 0.2423 0.3920 0.3599 -0.0493 -0.0870 -0.0807 49  PRO A CA  
361  C C   . PRO A 73  ? 0.2861 0.4272 0.4122 -0.0443 -0.0743 -0.0651 49  PRO A C   
362  O O   . PRO A 73  ? 0.1795 0.3407 0.3288 -0.0419 -0.0757 -0.0618 49  PRO A O   
363  C CB  . PRO A 73  ? 0.2305 0.3830 0.3761 -0.0648 -0.0882 -0.0969 49  PRO A CB  
364  C CG  . PRO A 73  ? 0.2737 0.4561 0.4411 -0.0648 -0.0974 -0.0975 49  PRO A CG  
365  C CD  . PRO A 73  ? 0.3188 0.5202 0.4638 -0.0514 -0.1106 -0.0933 49  PRO A CD  
366  N N   . LEU A 74  ? 0.2414 0.3559 0.3502 -0.0417 -0.0624 -0.0574 50  LEU A N   
367  C CA  . LEU A 74  ? 0.2205 0.3293 0.3346 -0.0358 -0.0515 -0.0463 50  LEU A CA  
368  C C   . LEU A 74  ? 0.2265 0.3431 0.3674 -0.0448 -0.0424 -0.0477 50  LEU A C   
369  O O   . LEU A 74  ? 0.2144 0.3222 0.3620 -0.0564 -0.0386 -0.0521 50  LEU A O   
370  C CB  . LEU A 74  ? 0.2042 0.2855 0.2944 -0.0323 -0.0423 -0.0401 50  LEU A CB  
371  C CG  . LEU A 74  ? 0.2445 0.3176 0.3097 -0.0248 -0.0479 -0.0359 50  LEU A CG  
372  C CD1 . LEU A 74  ? 0.2441 0.2927 0.2926 -0.0237 -0.0383 -0.0319 50  LEU A CD1 
373  C CD2 . LEU A 74  ? 0.2386 0.3230 0.3071 -0.0137 -0.0542 -0.0266 50  LEU A CD2 
374  N N   . PRO A 75  ? 0.1971 0.3308 0.3559 -0.0393 -0.0382 -0.0433 51  PRO A N   
375  C CA  . PRO A 75  ? 0.2083 0.3557 0.3934 -0.0480 -0.0275 -0.0429 51  PRO A CA  
376  C C   . PRO A 75  ? 0.2087 0.3422 0.3827 -0.0469 -0.0109 -0.0350 51  PRO A C   
377  O O   . PRO A 75  ? 0.2414 0.3910 0.4333 -0.0503 0.0005  -0.0315 51  PRO A O   
378  C CB  . PRO A 75  ? 0.2084 0.3872 0.4188 -0.0404 -0.0319 -0.0440 51  PRO A CB  
379  C CG  . PRO A 75  ? 0.1924 0.3612 0.3838 -0.0239 -0.0362 -0.0396 51  PRO A CG  
380  C CD  . PRO A 75  ? 0.2230 0.3692 0.3847 -0.0251 -0.0443 -0.0393 51  PRO A CD  
381  N N   . PHE A 76  ? 0.2126 0.3200 0.3575 -0.0421 -0.0094 -0.0321 52  PHE A N   
382  C CA  . PHE A 76  ? 0.1935 0.2900 0.3248 -0.0400 0.0037  -0.0258 52  PHE A CA  
383  C C   . PHE A 76  ? 0.3019 0.3707 0.4116 -0.0441 0.0040  -0.0231 52  PHE A C   
384  O O   . PHE A 76  ? 0.1909 0.2479 0.2922 -0.0453 -0.0054 -0.0278 52  PHE A O   
385  C CB  . PHE A 76  ? 0.1725 0.2701 0.2945 -0.0256 0.0049  -0.0268 52  PHE A CB  
386  C CG  . PHE A 76  ? 0.1838 0.2648 0.2898 -0.0183 -0.0059 -0.0278 52  PHE A CG  
387  C CD1 . PHE A 76  ? 0.2188 0.2764 0.3012 -0.0183 -0.0053 -0.0257 52  PHE A CD1 
388  C CD2 . PHE A 76  ? 0.1962 0.2875 0.3126 -0.0115 -0.0164 -0.0290 52  PHE A CD2 
389  C CE1 . PHE A 76  ? 0.2013 0.2468 0.2714 -0.0129 -0.0133 -0.0246 52  PHE A CE1 
390  C CE2 . PHE A 76  ? 0.1894 0.2672 0.2915 -0.0055 -0.0250 -0.0256 52  PHE A CE2 
391  C CZ  . PHE A 76  ? 0.2471 0.3024 0.3263 -0.0069 -0.0226 -0.0234 52  PHE A CZ  
392  N N   . ALA A 77  ? 0.2275 0.2892 0.3281 -0.0451 0.0151  -0.0155 53  ALA A N   
393  C CA  . ALA A 77  ? 0.1893 0.2264 0.2725 -0.0474 0.0159  -0.0113 53  ALA A CA  
394  C C   . ALA A 77  ? 0.2104 0.2324 0.2728 -0.0392 0.0082  -0.0162 53  ALA A C   
395  O O   . ALA A 77  ? 0.1989 0.2226 0.2513 -0.0301 0.0086  -0.0168 53  ALA A O   
396  C CB  . ALA A 77  ? 0.2542 0.2919 0.3281 -0.0464 0.0279  -0.0004 53  ALA A CB  
397  N N   . PHE A 78  ? 0.1995 0.2071 0.2573 -0.0426 0.0019  -0.0201 54  PHE A N   
398  C CA  . PHE A 78  ? 0.2233 0.2196 0.2624 -0.0359 -0.0035 -0.0230 54  PHE A CA  
399  C C   . PHE A 78  ? 0.2262 0.2119 0.2502 -0.0304 0.0018  -0.0176 54  PHE A C   
400  O O   . PHE A 78  ? 0.1798 0.1620 0.1931 -0.0240 -0.0011 -0.0186 54  PHE A O   
401  C CB  . PHE A 78  ? 0.2419 0.2286 0.2792 -0.0402 -0.0091 -0.0303 54  PHE A CB  
402  C CG  . PHE A 78  ? 0.2139 0.1991 0.2346 -0.0341 -0.0150 -0.0340 54  PHE A CG  
403  C CD1 . PHE A 78  ? 0.2318 0.2044 0.2384 -0.0297 -0.0122 -0.0315 54  PHE A CD1 
404  C CD2 . PHE A 78  ? 0.2561 0.2557 0.2764 -0.0328 -0.0233 -0.0385 54  PHE A CD2 
405  C CE1 . PHE A 78  ? 0.2283 0.2030 0.2219 -0.0251 -0.0156 -0.0329 54  PHE A CE1 
406  C CE2 . PHE A 78  ? 0.2120 0.2137 0.2159 -0.0276 -0.0272 -0.0383 54  PHE A CE2 
407  C CZ  . PHE A 78  ? 0.2344 0.2237 0.2257 -0.0243 -0.0225 -0.0353 54  PHE A CZ  
408  N N   . ASP A 79  ? 0.1682 0.1506 0.1925 -0.0329 0.0091  -0.0106 55  ASP A N   
409  C CA  . ASP A 79  ? 0.1958 0.1721 0.2050 -0.0273 0.0124  -0.0057 55  ASP A CA  
410  C C   . ASP A 79  ? 0.2545 0.2405 0.2571 -0.0196 0.0126  -0.0095 55  ASP A C   
411  O O   . ASP A 79  ? 0.2140 0.1950 0.2050 -0.0146 0.0115  -0.0103 55  ASP A O   
412  C CB  . ASP A 79  ? 0.2100 0.1872 0.2203 -0.0306 0.0202  0.0057  55  ASP A CB  
413  C CG  . ASP A 79  ? 0.2855 0.2453 0.3033 -0.0364 0.0195  0.0105  55  ASP A CG  
414  O OD1 . ASP A 79  ? 0.2370 0.1832 0.2504 -0.0339 0.0139  0.0043  55  ASP A OD1 
415  O OD2 . ASP A 79  ? 0.2561 0.2162 0.2861 -0.0431 0.0253  0.0207  55  ASP A OD2 
416  N N   . ILE A 80  ? 0.1983 0.1991 0.2112 -0.0182 0.0137  -0.0131 56  ILE A N   
417  C CA  . ILE A 80  ? 0.1777 0.1849 0.1879 -0.0097 0.0135  -0.0194 56  ILE A CA  
418  C C   . ILE A 80  ? 0.1761 0.1707 0.1840 -0.0060 0.0057  -0.0230 56  ILE A C   
419  O O   . ILE A 80  ? 0.1966 0.1894 0.2028 -0.0004 0.0044  -0.0284 56  ILE A O   
420  C CB  . ILE A 80  ? 0.2228 0.2490 0.2483 -0.0067 0.0165  -0.0240 56  ILE A CB  
421  C CG1 . ILE A 80  ? 0.1898 0.2169 0.2300 -0.0068 0.0090  -0.0255 56  ILE A CG1 
422  C CG2 . ILE A 80  ? 0.2115 0.2549 0.2414 -0.0114 0.0266  -0.0185 56  ILE A CG2 
423  C CD1 . ILE A 80  ? 0.1931 0.2398 0.2524 -0.0006 0.0106  -0.0310 56  ILE A CD1 
424  N N   . LEU A 81  ? 0.1986 0.1860 0.2073 -0.0095 0.0006  -0.0205 57  LEU A N   
425  C CA  . LEU A 81  ? 0.2204 0.1998 0.2272 -0.0070 -0.0053 -0.0200 57  LEU A CA  
426  C C   . LEU A 81  ? 0.2089 0.1773 0.2043 -0.0080 -0.0052 -0.0186 57  LEU A C   
427  O O   . LEU A 81  ? 0.2198 0.1834 0.2153 -0.0062 -0.0081 -0.0171 57  LEU A O   
428  C CB  . LEU A 81  ? 0.1573 0.1410 0.1670 -0.0095 -0.0106 -0.0178 57  LEU A CB  
429  C CG  . LEU A 81  ? 0.2116 0.2098 0.2355 -0.0089 -0.0131 -0.0188 57  LEU A CG  
430  C CD1 . LEU A 81  ? 0.2222 0.2269 0.2449 -0.0118 -0.0202 -0.0182 57  LEU A CD1 
431  C CD2 . LEU A 81  ? 0.1799 0.1809 0.2154 -0.0007 -0.0148 -0.0185 57  LEU A CD2 
432  N N   . THR A 82  ? 0.2103 0.1750 0.1990 -0.0107 -0.0020 -0.0176 58  THR A N   
433  C CA  . THR A 82  ? 0.2213 0.1777 0.2031 -0.0112 -0.0029 -0.0168 58  THR A CA  
434  C C   . THR A 82  ? 0.2186 0.1727 0.1980 -0.0077 -0.0037 -0.0174 58  THR A C   
435  O O   . THR A 82  ? 0.1908 0.1422 0.1693 -0.0077 -0.0048 -0.0166 58  THR A O   
436  C CB  . THR A 82  ? 0.1899 0.1406 0.1700 -0.0138 -0.0002 -0.0151 58  THR A CB  
437  O OG1 . THR A 82  ? 0.1843 0.1381 0.1629 -0.0129 0.0035  -0.0108 58  THR A OG1 
438  C CG2 . THR A 82  ? 0.1594 0.1106 0.1463 -0.0190 -0.0011 -0.0176 58  THR A CG2 
439  N N   . THR A 83  ? 0.1822 0.1404 0.1618 -0.0048 -0.0031 -0.0201 59  THR A N   
440  C CA  . THR A 83  ? 0.1816 0.1389 0.1627 -0.0025 -0.0059 -0.0238 59  THR A CA  
441  C C   . THR A 83  ? 0.2452 0.1991 0.2381 -0.0027 -0.0089 -0.0250 59  THR A C   
442  O O   . THR A 83  ? 0.2207 0.1726 0.2204 -0.0029 -0.0113 -0.0274 59  THR A O   
443  C CB  . THR A 83  ? 0.2116 0.1771 0.1882 0.0013  -0.0060 -0.0297 59  THR A CB  
444  O OG1 . THR A 83  ? 0.2222 0.1932 0.2049 0.0037  -0.0052 -0.0364 59  THR A OG1 
445  C CG2 . THR A 83  ? 0.2173 0.1871 0.1822 0.0016  -0.0023 -0.0228 59  THR A CG2 
446  N N   . ALA A 84  ? 0.2228 0.1767 0.2213 -0.0027 -0.0092 -0.0223 60  ALA A N   
447  C CA  . ALA A 84  ? 0.2292 0.1783 0.2399 -0.0026 -0.0123 -0.0183 60  ALA A CA  
448  C C   . ALA A 84  ? 0.2447 0.1939 0.2506 -0.0060 -0.0117 -0.0087 60  ALA A C   
449  O O   . ALA A 84  ? 0.2519 0.1982 0.2672 -0.0072 -0.0127 -0.0017 60  ALA A O   
450  C CB  . ALA A 84  ? 0.1970 0.1479 0.2179 0.0008  -0.0142 -0.0175 60  ALA A CB  
451  N N   . PHE A 85  ? 0.1637 0.2006 0.2042 -0.0069 -0.0258 -0.0068 61  PHE A N   
452  C CA  . PHE A 85  ? 0.2096 0.2343 0.2272 -0.0066 -0.0307 -0.0074 61  PHE A CA  
453  C C   . PHE A 85  ? 0.2085 0.2190 0.2120 -0.0051 -0.0214 -0.0075 61  PHE A C   
454  O O   . PHE A 85  ? 0.2076 0.2123 0.1961 -0.0014 -0.0202 -0.0062 61  PHE A O   
455  C CB  . PHE A 85  ? 0.1807 0.2047 0.1960 -0.0147 -0.0381 -0.0145 61  PHE A CB  
456  C CG  . PHE A 85  ? 0.1887 0.2311 0.2214 -0.0177 -0.0494 -0.0156 61  PHE A CG  
457  C CD1 . PHE A 85  ? 0.2423 0.2944 0.2745 -0.0108 -0.0595 -0.0106 61  PHE A CD1 
458  C CD2 . PHE A 85  ? 0.1574 0.2081 0.2090 -0.0280 -0.0508 -0.0205 61  PHE A CD2 
459  C CE1 . PHE A 85  ? 0.2324 0.3049 0.2846 -0.0121 -0.0726 -0.0115 61  PHE A CE1 
460  C CE2 . PHE A 85  ? 0.1610 0.2340 0.2344 -0.0315 -0.0617 -0.0227 61  PHE A CE2 
461  C CZ  . PHE A 85  ? 0.2082 0.2936 0.2830 -0.0226 -0.0737 -0.0188 61  PHE A CZ  
462  C C1  . 5SQ A 86  ? 0.2023 0.2068 0.2107 -0.0055 -0.0029 -0.0042 64  5SQ A C1  
463  C C2  . 5SQ A 86  ? 0.1893 0.2041 0.2066 -0.0015 0.0044  -0.0054 64  5SQ A C2  
464  O O3  . 5SQ A 86  ? 0.1962 0.1974 0.2087 0.0081  -0.0030 0.0053  64  5SQ A O3  
465  C C3  . 5SQ A 86  ? 0.1694 0.1731 0.1783 0.0055  -0.0009 0.0008  64  5SQ A C3  
466  C CA3 . 5SQ A 86  ? 0.2291 0.2370 0.2391 0.0029  -0.0051 -0.0015 64  5SQ A CA3 
467  N N3  . 5SQ A 86  ? 0.2064 0.2157 0.2188 -0.0009 -0.0013 -0.0038 64  5SQ A N3  
468  O O2  . 5SQ A 86  ? 0.1865 0.2041 0.2096 0.0010  0.0072  -0.0079 64  5SQ A O2  
469  C CA1 . 5SQ A 86  ? 0.2196 0.2173 0.2210 -0.0061 -0.0090 -0.0072 64  5SQ A CA1 
470  N N1  . 5SQ A 86  ? 0.2001 0.2074 0.2092 -0.0083 -0.0153 -0.0081 64  5SQ A N1  
471  C CB1 . 5SQ A 86  ? 0.1899 0.1746 0.1881 -0.0098 -0.0100 -0.0092 64  5SQ A CB1 
472  C CG1 . 5SQ A 86  ? 0.2101 0.1856 0.1994 -0.0091 -0.0147 -0.0173 64  5SQ A CG1 
473  C C2H . 5SQ A 86  ? 0.1770 0.1366 0.1660 -0.0120 -0.0174 -0.0227 64  5SQ A C2H 
474  N N2H . 5SQ A 86  ? 0.2830 0.2394 0.2616 -0.0103 -0.0205 -0.0331 64  5SQ A N2H 
475  N N1H . 5SQ A 86  ? 0.2720 0.2520 0.2508 -0.0061 -0.0167 -0.0210 64  5SQ A N1H 
476  C C1H . 5SQ A 86  ? 0.2027 0.1730 0.1725 -0.0070 -0.0199 -0.0312 64  5SQ A C1H 
477  N N2  . 5SQ A 86  ? 0.2089 0.2142 0.2178 -0.0097 0.0011  -0.0020 64  5SQ A N2  
478  C CA2 . 5SQ A 86  ? 0.2083 0.2230 0.2206 -0.0075 0.0061  -0.0036 64  5SQ A CA2 
479  C CB2 . 5SQ A 86  ? 0.1722 0.1899 0.1792 -0.0121 0.0097  -0.0015 64  5SQ A CB2 
480  C CG2 . 5SQ A 86  ? 0.2117 0.2254 0.2111 -0.0196 0.0102  0.0055  64  5SQ A CG2 
481  C CD2 . 5SQ A 86  ? 0.1968 0.1964 0.1947 -0.0230 0.0056  0.0105  64  5SQ A CD2 
482  C CE2 . 5SQ A 86  ? 0.2162 0.2105 0.2074 -0.0316 0.0068  0.0199  64  5SQ A CE2 
483  C CD1 . 5SQ A 86  ? 0.1806 0.2063 0.1742 -0.0241 0.0166  0.0058  64  5SQ A CD1 
484  C CE1 . 5SQ A 86  ? 0.2107 0.2352 0.1933 -0.0330 0.0187  0.0150  64  5SQ A CE1 
485  C CZ1 . 5SQ A 86  ? 0.2129 0.2202 0.1951 -0.0369 0.0134  0.0239  64  5SQ A CZ1 
486  O OH  . 5SQ A 86  ? 0.2476 0.2494 0.2184 -0.0474 0.0150  0.0369  64  5SQ A OH  
487  N N   . ASN A 87  ? 0.1954 0.1965 0.1975 0.0046  0.0029  -0.0007 65  ASN A N   
488  C CA  . ASN A 87  ? 0.2005 0.2001 0.2014 0.0047  0.0069  0.0013  65  ASN A CA  
489  C C   . ASN A 87  ? 0.2142 0.2175 0.2175 0.0044  0.0098  -0.0024 65  ASN A C   
490  O O   . ASN A 87  ? 0.1833 0.1869 0.1828 0.0064  0.0099  -0.0043 65  ASN A O   
491  C CB  . ASN A 87  ? 0.2156 0.2134 0.2037 0.0047  0.0073  0.0050  65  ASN A CB  
492  C CG  . ASN A 87  ? 0.2240 0.2229 0.2116 0.0021  0.0140  0.0086  65  ASN A CG  
493  O OD1 . ASN A 87  ? 0.2268 0.2268 0.2268 0.0001  0.0166  0.0077  65  ASN A OD1 
494  N ND2 . ASN A 87  ? 0.2082 0.2086 0.1812 0.0005  0.0173  0.0123  65  ASN A ND2 
495  N N   . ARG A 88  ? 0.2156 0.2220 0.2268 0.0027  0.0107  -0.0046 66  ARG A N   
496  C CA  . ARG A 88  ? 0.2190 0.2320 0.2327 0.0024  0.0099  -0.0075 66  ARG A CA  
497  C C   . ARG A 88  ? 0.2459 0.2654 0.2661 0.0027  0.0126  -0.0077 66  ARG A C   
498  O O   . ARG A 88  ? 0.2177 0.2463 0.2448 0.0037  0.0100  -0.0100 66  ARG A O   
499  C CB  . ARG A 88  ? 0.1792 0.1960 0.1964 -0.0008 0.0091  -0.0123 66  ARG A CB  
500  C CG  . ARG A 88  ? 0.2117 0.2359 0.2234 -0.0013 0.0046  -0.0134 66  ARG A CG  
501  C CD  . ARG A 88  ? 0.1742 0.1949 0.1752 -0.0007 0.0031  -0.0082 66  ARG A CD  
502  N NE  . ARG A 88  ? 0.1662 0.1870 0.1660 -0.0033 0.0075  -0.0108 66  ARG A NE  
503  C CZ  . ARG A 88  ? 0.2132 0.2297 0.2175 -0.0022 0.0092  -0.0093 66  ARG A CZ  
504  N NH1 . ARG A 88  ? 0.1864 0.1962 0.1901 0.0001  0.0070  -0.0056 66  ARG A NH1 
505  N NH2 . ARG A 88  ? 0.1945 0.2158 0.2049 -0.0029 0.0128  -0.0133 66  ARG A NH2 
506  N N   . VAL A 89  ? 0.1657 0.1837 0.1839 0.0016  0.0177  -0.0049 67  VAL A N   
507  C CA  . VAL A 89  ? 0.1565 0.1848 0.1795 0.0023  0.0233  -0.0063 67  VAL A CA  
508  C C   . VAL A 89  ? 0.2387 0.2688 0.2612 0.0100  0.0209  -0.0107 67  VAL A C   
509  O O   . VAL A 89  ? 0.2230 0.2650 0.2584 0.0139  0.0225  -0.0147 67  VAL A O   
510  C CB  . VAL A 89  ? 0.2211 0.2476 0.2341 -0.0011 0.0304  -0.0013 67  VAL A CB  
511  C CG1 . VAL A 89  ? 0.3245 0.3642 0.3378 0.0013  0.0387  -0.0060 67  VAL A CG1 
512  C CG2 . VAL A 89  ? 0.2917 0.3163 0.3120 -0.0093 0.0336  0.0047  67  VAL A CG2 
513  N N   . PHE A 90  ? 0.1996 0.2176 0.2109 0.0124  0.0166  -0.0105 68  PHE A N   
514  C CA  . PHE A 90  ? 0.2198 0.2327 0.2315 0.0190  0.0138  -0.0147 68  PHE A CA  
515  C C   . PHE A 90  ? 0.2690 0.2791 0.2861 0.0206  0.0058  -0.0109 68  PHE A C   
516  O O   . PHE A 90  ? 0.2361 0.2349 0.2460 0.0187  0.0012  -0.0073 68  PHE A O   
517  C CB  . PHE A 90  ? 0.2034 0.2042 0.2013 0.0183  0.0126  -0.0169 68  PHE A CB  
518  C CG  . PHE A 90  ? 0.2495 0.2549 0.2365 0.0173  0.0193  -0.0206 68  PHE A CG  
519  C CD1 . PHE A 90  ? 0.1605 0.1713 0.1481 0.0225  0.0259  -0.0300 68  PHE A CD1 
520  C CD2 . PHE A 90  ? 0.2464 0.2520 0.2225 0.0117  0.0192  -0.0143 68  PHE A CD2 
521  C CE1 . PHE A 90  ? 0.2194 0.2374 0.1917 0.0201  0.0339  -0.0334 68  PHE A CE1 
522  C CE2 . PHE A 90  ? 0.2231 0.2330 0.1837 0.0096  0.0244  -0.0144 68  PHE A CE2 
523  C CZ  . PHE A 90  ? 0.2803 0.2974 0.2364 0.0127  0.0327  -0.0240 68  PHE A CZ  
524  N N   . ALA A 91  ? 0.1811 0.2043 0.2107 0.0223  0.0042  -0.0110 69  ALA A N   
525  C CA  . ALA A 91  ? 0.1857 0.2104 0.2183 0.0242  -0.0052 -0.0064 69  ALA A CA  
526  C C   . ALA A 91  ? 0.2019 0.2436 0.2548 0.0307  -0.0077 -0.0095 69  ALA A C   
527  O O   . ALA A 91  ? 0.2108 0.2683 0.2750 0.0273  -0.0014 -0.0142 69  ALA A O   
528  C CB  . ALA A 91  ? 0.1874 0.2159 0.2116 0.0160  -0.0072 -0.0043 69  ALA A CB  
529  N N   . LYS A 92  ? 0.1701 0.2094 0.2305 0.0395  -0.0172 -0.0058 70  LYS A N   
530  C CA  . LYS A 92  ? 0.1611 0.2204 0.2469 0.0479  -0.0218 -0.0089 70  LYS A CA  
531  C C   . LYS A 92  ? 0.2007 0.2771 0.2886 0.0419  -0.0312 -0.0058 70  LYS A C   
532  O O   . LYS A 92  ? 0.2162 0.2859 0.2894 0.0409  -0.0427 0.0028  70  LYS A O   
533  C CB  . LYS A 92  ? 0.1834 0.2312 0.2795 0.0620  -0.0308 -0.0056 70  LYS A CB  
534  C CG  . LYS A 92  ? 0.2381 0.3096 0.3668 0.0739  -0.0380 -0.0087 70  LYS A CG  
535  C CD  . LYS A 92  ? 0.2582 0.3131 0.3975 0.0894  -0.0507 -0.0023 70  LYS A CD  
536  C CE  . LYS A 92  ? 0.4747 0.5568 0.6530 0.1040  -0.0593 -0.0060 70  LYS A CE  
537  N NZ  . LYS A 92  ? 0.5709 0.6664 0.7767 0.1138  -0.0441 -0.0237 70  LYS A NZ  
538  N N   . TYR A 93  ? 0.2002 0.2989 0.3046 0.0363  -0.0261 -0.0132 71  TYR A N   
539  C CA  . TYR A 93  ? 0.1473 0.2635 0.2562 0.0289  -0.0355 -0.0143 71  TYR A CA  
540  C C   . TYR A 93  ? 0.2401 0.3836 0.3806 0.0369  -0.0457 -0.0164 71  TYR A C   
541  O O   . TYR A 93  ? 0.1680 0.3278 0.3357 0.0412  -0.0368 -0.0228 71  TYR A O   
542  C CB  . TYR A 93  ? 0.1436 0.2645 0.2539 0.0152  -0.0251 -0.0213 71  TYR A CB  
543  C CG  . TYR A 93  ? 0.1888 0.2908 0.2723 0.0067  -0.0235 -0.0207 71  TYR A CG  
544  C CD1 . TYR A 93  ? 0.1909 0.2716 0.2570 0.0073  -0.0146 -0.0174 71  TYR A CD1 
545  C CD2 . TYR A 93  ? 0.2030 0.3112 0.2802 -0.0013 -0.0313 -0.0256 71  TYR A CD2 
546  C CE1 . TYR A 93  ? 0.1982 0.2660 0.2460 0.0012  -0.0128 -0.0182 71  TYR A CE1 
547  C CE2 . TYR A 93  ? 0.1703 0.2637 0.2260 -0.0074 -0.0280 -0.0284 71  TYR A CE2 
548  C CZ  . TYR A 93  ? 0.1588 0.2332 0.2022 -0.0054 -0.0184 -0.0242 71  TYR A CZ  
549  O OH  . TYR A 93  ? 0.2039 0.2680 0.2322 -0.0098 -0.0147 -0.0282 71  TYR A OH  
550  N N   . PRO A 94  ? 0.2423 0.3950 0.3812 0.0388  -0.0642 -0.0114 72  PRO A N   
551  C CA  . PRO A 94  ? 0.2270 0.4114 0.4008 0.0461  -0.0770 -0.0138 72  PRO A CA  
552  C C   . PRO A 94  ? 0.1997 0.4120 0.3957 0.0325  -0.0726 -0.0256 72  PRO A C   
553  O O   . PRO A 94  ? 0.2270 0.4303 0.4061 0.0175  -0.0650 -0.0304 72  PRO A O   
554  C CB  . PRO A 94  ? 0.2599 0.4424 0.4153 0.0494  -0.1001 -0.0026 72  PRO A CB  
555  C CG  . PRO A 94  ? 0.2596 0.4229 0.3740 0.0354  -0.0956 -0.0017 72  PRO A CG  
556  C CD  . PRO A 94  ? 0.1566 0.2950 0.2608 0.0333  -0.0744 -0.0037 72  PRO A CD  
557  N N   . ASP A 95  ? 0.2182 0.4649 0.4565 0.0381  -0.0778 -0.0307 73  ASP A N   
558  C CA  . ASP A 95  ? 0.2308 0.5024 0.4941 0.0232  -0.0699 -0.0405 73  ASP A CA  
559  C C   . ASP A 95  ? 0.2767 0.5530 0.5281 0.0074  -0.0829 -0.0446 73  ASP A C   
560  O O   . ASP A 95  ? 0.3227 0.6075 0.5871 -0.0087 -0.0750 -0.0524 73  ASP A O   
561  C CB  . ASP A 95  ? 0.1526 0.4511 0.4530 0.0310  -0.0692 -0.0405 73  ASP A CB  
562  C CG  . ASP A 95  ? 0.2991 0.6083 0.6051 0.0425  -0.0933 -0.0325 73  ASP A CG  
563  O OD1 . ASP A 95  ? 0.4243 0.7207 0.7017 0.0416  -0.1107 -0.0261 73  ASP A OD1 
564  O OD2 . ASP A 95  ? 0.3583 0.6902 0.6962 0.0520  -0.0947 -0.0320 73  ASP A OD2 
565  N N   . ASN A 96  ? 0.2705 0.5390 0.4946 0.0106  -0.1020 -0.0394 74  ASN A N   
566  C CA  . ASN A 96  ? 0.2547 0.5270 0.4621 -0.0039 -0.1144 -0.0453 74  ASN A CA  
567  C C   . ASN A 96  ? 0.2781 0.5256 0.4459 -0.0128 -0.1094 -0.0503 74  ASN A C   
568  O O   . ASN A 96  ? 0.2778 0.5240 0.4212 -0.0216 -0.1201 -0.0555 74  ASN A O   
569  C CB  . ASN A 96  ? 0.2854 0.5690 0.4859 0.0034  -0.1385 -0.0356 74  ASN A CB  
570  C CG  . ASN A 96  ? 0.4017 0.6642 0.5650 0.0142  -0.1476 -0.0217 74  ASN A CG  
571  O OD1 . ASN A 96  ? 0.3662 0.6106 0.5241 0.0243  -0.1376 -0.0163 74  ASN A OD1 
572  N ND2 . ASN A 96  ? 0.6197 0.8834 0.7571 0.0118  -0.1673 -0.0143 74  ASN A ND2 
573  N N   . ILE A 97  ? 0.2323 0.4514 0.3867 -0.0108 -0.0895 -0.0460 75  ILE A N   
574  C CA  . ILE A 97  ? 0.2421 0.4336 0.3648 -0.0197 -0.0789 -0.0501 75  ILE A CA  
575  C C   . ILE A 97  ? 0.2200 0.3998 0.3580 -0.0264 -0.0590 -0.0538 75  ILE A C   
576  O O   . ILE A 97  ? 0.2155 0.3937 0.3661 -0.0194 -0.0482 -0.0470 75  ILE A O   
577  C CB  . ILE A 97  ? 0.2577 0.4250 0.3445 -0.0111 -0.0771 -0.0384 75  ILE A CB  
578  C CG1 . ILE A 97  ? 0.2745 0.4515 0.3430 -0.0056 -0.0973 -0.0299 75  ILE A CG1 
579  C CG2 . ILE A 97  ? 0.2575 0.4023 0.3182 -0.0195 -0.0654 -0.0449 75  ILE A CG2 
580  C CD1 . ILE A 97  ? 0.2949 0.4489 0.3357 0.0029  -0.0955 -0.0139 75  ILE A CD1 
581  N N   . GLN A 98  ? 0.1887 0.3596 0.3248 -0.0401 -0.0546 -0.0648 76  GLN A N   
582  C CA  . GLN A 98  ? 0.1877 0.3426 0.3351 -0.0475 -0.0375 -0.0651 76  GLN A CA  
583  C C   . GLN A 98  ? 0.2010 0.3306 0.3268 -0.0382 -0.0256 -0.0544 76  GLN A C   
584  O O   . GLN A 98  ? 0.2320 0.3458 0.3315 -0.0342 -0.0269 -0.0541 76  GLN A O   
585  C CB  . GLN A 98  ? 0.1704 0.3124 0.3166 -0.0617 -0.0376 -0.0788 76  GLN A CB  
586  C CG  . GLN A 98  ? 0.2952 0.4098 0.4451 -0.0677 -0.0221 -0.0759 76  GLN A CG  
587  C CD  . GLN A 98  ? 0.4658 0.5891 0.6447 -0.0760 -0.0122 -0.0688 76  GLN A CD  
588  O OE1 . GLN A 98  ? 0.4916 0.6431 0.6891 -0.0739 -0.0130 -0.0655 76  GLN A OE1 
589  N NE2 . GLN A 98  ? 0.5659 0.6645 0.7485 -0.0850 -0.0017 -0.0653 76  GLN A NE2 
590  N N   . ASP A 99  ? 0.1940 0.3228 0.3309 -0.0358 -0.0136 -0.0465 77  ASP A N   
591  C CA  . ASP A 99  ? 0.1920 0.2997 0.3097 -0.0282 -0.0038 -0.0375 77  ASP A CA  
592  C C   . ASP A 99  ? 0.2162 0.3030 0.3314 -0.0369 0.0061  -0.0360 77  ASP A C   
593  O O   . ASP A 99  ? 0.2089 0.2961 0.3341 -0.0422 0.0163  -0.0302 77  ASP A O   
594  C CB  . ASP A 99  ? 0.1847 0.3044 0.3118 -0.0195 0.0020  -0.0318 77  ASP A CB  
595  C CG  . ASP A 99  ? 0.1892 0.2890 0.2948 -0.0119 0.0093  -0.0250 77  ASP A CG  
596  O OD1 . ASP A 99  ? 0.1881 0.2670 0.2758 -0.0143 0.0112  -0.0226 77  ASP A OD1 
597  O OD2 . ASP A 99  ? 0.1760 0.2825 0.2851 -0.0028 0.0123  -0.0237 77  ASP A OD2 
598  N N   . TYR A 100 ? 0.2013 0.2699 0.3028 -0.0381 0.0033  -0.0407 78  TYR A N   
599  C CA  . TYR A 100 ? 0.2686 0.3141 0.3711 -0.0439 0.0096  -0.0397 78  TYR A CA  
600  C C   . TYR A 100 ? 0.2177 0.2511 0.3111 -0.0392 0.0180  -0.0259 78  TYR A C   
601  O O   . TYR A 100 ? 0.2360 0.2559 0.3345 -0.0457 0.0240  -0.0187 78  TYR A O   
602  C CB  . TYR A 100 ? 0.2011 0.2329 0.2917 -0.0414 0.0056  -0.0496 78  TYR A CB  
603  C CG  . TYR A 100 ? 0.2849 0.2908 0.3814 -0.0443 0.0095  -0.0519 78  TYR A CG  
604  C CD1 . TYR A 100 ? 0.2241 0.2211 0.3375 -0.0552 0.0080  -0.0625 78  TYR A CD1 
605  C CD2 . TYR A 100 ? 0.2456 0.2355 0.3332 -0.0356 0.0130  -0.0447 78  TYR A CD2 
606  C CE1 . TYR A 100 ? 0.2360 0.2044 0.3576 -0.0562 0.0105  -0.0649 78  TYR A CE1 
607  C CE2 . TYR A 100 ? 0.2218 0.1873 0.3187 -0.0354 0.0144  -0.0462 78  TYR A CE2 
608  C CZ  . TYR A 100 ? 0.2755 0.2283 0.3893 -0.0449 0.0134  -0.0560 78  TYR A CZ  
609  O OH  . TYR A 100 ? 0.2644 0.1882 0.3904 -0.0431 0.0138  -0.0576 78  TYR A OH  
610  N N   . PHE A 101 ? 0.2193 0.2561 0.2976 -0.0289 0.0175  -0.0216 79  PHE A N   
611  C CA  . PHE A 101 ? 0.1952 0.2211 0.2607 -0.0242 0.0228  -0.0114 79  PHE A CA  
612  C C   . PHE A 101 ? 0.2246 0.2598 0.2935 -0.0278 0.0313  -0.0044 79  PHE A C   
613  O O   . PHE A 101 ? 0.2621 0.2863 0.3240 -0.0316 0.0370  0.0053  79  PHE A O   
614  C CB  . PHE A 101 ? 0.1773 0.2035 0.2280 -0.0144 0.0188  -0.0119 79  PHE A CB  
615  C CG  . PHE A 101 ? 0.1735 0.1954 0.2199 -0.0129 0.0135  -0.0184 79  PHE A CG  
616  C CD1 . PHE A 101 ? 0.1866 0.1948 0.2324 -0.0125 0.0144  -0.0193 79  PHE A CD1 
617  C CD2 . PHE A 101 ? 0.2057 0.2389 0.2495 -0.0120 0.0077  -0.0238 79  PHE A CD2 
618  C CE1 . PHE A 101 ? 0.1917 0.1999 0.2352 -0.0112 0.0125  -0.0284 79  PHE A CE1 
619  C CE2 . PHE A 101 ? 0.2262 0.2582 0.2616 -0.0124 0.0051  -0.0304 79  PHE A CE2 
620  C CZ  . PHE A 101 ? 0.2301 0.2510 0.2661 -0.0122 0.0090  -0.0342 79  PHE A CZ  
621  N N   . LYS A 102 ? 0.2234 0.2804 0.3034 -0.0264 0.0326  -0.0089 80  LYS A N   
622  C CA  . LYS A 102 ? 0.1978 0.2690 0.2842 -0.0304 0.0440  -0.0051 80  LYS A CA  
623  C C   . LYS A 102 ? 0.2198 0.2918 0.3215 -0.0457 0.0503  -0.0008 80  LYS A C   
624  O O   . LYS A 102 ? 0.2388 0.3128 0.3366 -0.0528 0.0619  0.0083  80  LYS A O   
625  C CB  . LYS A 102 ? 0.2476 0.3439 0.3487 -0.0227 0.0439  -0.0129 80  LYS A CB  
626  C CG  . LYS A 102 ? 0.2293 0.3184 0.3137 -0.0090 0.0407  -0.0146 80  LYS A CG  
627  C CD  . LYS A 102 ? 0.1939 0.3037 0.2959 0.0010  0.0407  -0.0220 80  LYS A CD  
628  C CE  . LYS A 102 ? 0.1592 0.2551 0.2474 0.0137  0.0350  -0.0242 80  LYS A CE  
629  N NZ  . LYS A 102 ? 0.1768 0.2606 0.2598 0.0169  0.0205  -0.0215 80  LYS A NZ  
630  N N   . GLN A 103 ? 0.2081 0.2768 0.3249 -0.0524 0.0430  -0.0068 81  GLN A N   
631  C CA  . GLN A 103 ? 0.2377 0.3025 0.3721 -0.0690 0.0479  -0.0037 81  GLN A CA  
632  C C   . GLN A 103 ? 0.1994 0.2304 0.3204 -0.0732 0.0496  0.0080  81  GLN A C   
633  O O   . GLN A 103 ? 0.2619 0.2826 0.3957 -0.0877 0.0542  0.0144  81  GLN A O   
634  C CB  . GLN A 103 ? 0.2761 0.3478 0.4317 -0.0754 0.0378  -0.0175 81  GLN A CB  
635  C CG  . GLN A 103 ? 0.3048 0.4133 0.4813 -0.0740 0.0340  -0.0266 81  GLN A CG  
636  C CD  . GLN A 103 ? 0.3678 0.5009 0.5687 -0.0850 0.0466  -0.0223 81  GLN A CD  
637  O OE1 . GLN A 103 ? 0.5264 0.6837 0.7323 -0.0771 0.0532  -0.0218 81  GLN A OE1 
638  N NE2 . GLN A 103 ? 0.4144 0.5416 0.6327 -0.1039 0.0511  -0.0202 81  GLN A NE2 
639  N N   . SER A 104 ? 0.2168 0.2306 0.3158 -0.0611 0.0448  0.0112  82  SER A N   
640  C CA  A SER A 104 ? 0.2923 0.2758 0.3809 -0.0610 0.0432  0.0227  82  SER A CA  
641  C CA  B SER A 104 ? 0.2914 0.2747 0.3811 -0.0618 0.0435  0.0228  82  SER A CA  
642  C C   . SER A 104 ? 0.3145 0.2945 0.3863 -0.0651 0.0516  0.0417  82  SER A C   
643  O O   . SER A 104 ? 0.3193 0.2739 0.3829 -0.0663 0.0491  0.0559  82  SER A O   
644  C CB  A SER A 104 ? 0.2670 0.2415 0.3426 -0.0462 0.0346  0.0174  82  SER A CB  
645  C CB  B SER A 104 ? 0.2683 0.2396 0.3470 -0.0477 0.0343  0.0173  82  SER A CB  
646  O OG  A SER A 104 ? 0.2388 0.2058 0.3267 -0.0449 0.0281  0.0033  82  SER A OG  
647  O OG  B SER A 104 ? 0.2819 0.2655 0.3424 -0.0378 0.0342  0.0187  82  SER A OG  
648  N N   . PHE A 105 ? 0.2688 0.2739 0.3346 -0.0663 0.0609  0.0421  83  PHE A N   
649  C CA  . PHE A 105 ? 0.2716 0.2784 0.3147 -0.0699 0.0702  0.0572  83  PHE A CA  
650  C C   . PHE A 105 ? 0.3412 0.3630 0.3960 -0.0871 0.0852  0.0645  83  PHE A C   
651  O O   . PHE A 105 ? 0.3022 0.3429 0.3857 -0.0935 0.0884  0.0536  83  PHE A O   
652  C CB  . PHE A 105 ? 0.3085 0.3328 0.3334 -0.0574 0.0712  0.0490  83  PHE A CB  
653  C CG  . PHE A 105 ? 0.2821 0.2904 0.2926 -0.0445 0.0581  0.0469  83  PHE A CG  
654  C CD1 . PHE A 105 ? 0.2814 0.2745 0.2676 -0.0426 0.0537  0.0602  83  PHE A CD1 
655  C CD2 . PHE A 105 ? 0.2810 0.2904 0.3035 -0.0355 0.0493  0.0330  83  PHE A CD2 
656  C CE1 . PHE A 105 ? 0.2375 0.2203 0.2168 -0.0315 0.0411  0.0575  83  PHE A CE1 
657  C CE2 . PHE A 105 ? 0.2914 0.2893 0.3043 -0.0259 0.0391  0.0314  83  PHE A CE2 
658  C CZ  . PHE A 105 ? 0.2879 0.2737 0.2820 -0.0238 0.0351  0.0427  83  PHE A CZ  
659  N N   . PRO A 106 ? 0.3394 0.3554 0.3723 -0.0964 0.0945  0.0839  84  PRO A N   
660  C CA  . PRO A 106 ? 0.3674 0.3687 0.3624 -0.0897 0.0904  0.0975  84  PRO A CA  
661  C C   . PRO A 106 ? 0.4320 0.3963 0.4202 -0.0841 0.0740  0.1099  84  PRO A C   
662  O O   . PRO A 106 ? 0.3877 0.3461 0.3489 -0.0750 0.0666  0.1165  84  PRO A O   
663  C CB  . PRO A 106 ? 0.3779 0.3890 0.3545 -0.1051 0.1075  0.1145  84  PRO A CB  
664  C CG  . PRO A 106 ? 0.3787 0.3841 0.3862 -0.1195 0.1137  0.1163  84  PRO A CG  
665  C CD  . PRO A 106 ? 0.3523 0.3799 0.3962 -0.1169 0.1107  0.0948  84  PRO A CD  
666  N N   . LYS A 107 ? 0.3640 0.3042 0.3770 -0.0879 0.0672  0.1116  85  LYS A N   
667  C CA  . LYS A 107 ? 0.3688 0.2740 0.3776 -0.0811 0.0530  0.1245  85  LYS A CA  
668  C C   . LYS A 107 ? 0.3750 0.2814 0.3816 -0.0614 0.0399  0.1105  85  LYS A C   
669  O O   . LYS A 107 ? 0.4370 0.3292 0.4298 -0.0524 0.0289  0.1220  85  LYS A O   
670  C CB  . LYS A 107 ? 0.3498 0.2270 0.3888 -0.0891 0.0498  0.1255  85  LYS A CB  
671  C CG  . LYS A 107 ? 0.4690 0.3294 0.4976 -0.1042 0.0556  0.1412  85  LYS A CG  
672  C CD  . LYS A 107 ? 0.6573 0.5120 0.7159 -0.1180 0.0588  0.1298  85  LYS A CD  
673  C CE  . LYS A 107 ? 0.7290 0.5495 0.7825 -0.1290 0.0588  0.1456  85  LYS A CE  
674  N NZ  . LYS A 107 ? 0.7145 0.5367 0.7918 -0.1484 0.0650  0.1365  85  LYS A NZ  
675  N N   . GLY A 108 ? 0.3142 0.2386 0.3353 -0.0554 0.0401  0.0874  86  GLY A N   
676  C CA  . GLY A 108 ? 0.2929 0.2219 0.3115 -0.0398 0.0305  0.0748  86  GLY A CA  
677  C C   . GLY A 108 ? 0.2740 0.1906 0.3168 -0.0340 0.0236  0.0613  86  GLY A C   
678  O O   . GLY A 108 ? 0.3161 0.2210 0.3785 -0.0416 0.0253  0.0573  86  GLY A O   
679  N N   . TYR A 109 ? 0.2252 0.2553 0.2255 -0.0767 -0.0272 0.0026  87  TYR A N   
680  C CA  . TYR A 109 ? 0.2458 0.2673 0.2368 -0.0903 -0.0164 -0.0134 87  TYR A CA  
681  C C   . TYR A 109 ? 0.2484 0.2432 0.2514 -0.0647 -0.0164 -0.0059 87  TYR A C   
682  O O   . TYR A 109 ? 0.2419 0.2378 0.2561 -0.0436 -0.0268 0.0100  87  TYR A O   
683  C CB  . TYR A 109 ? 0.2486 0.3338 0.2311 -0.1075 -0.0264 -0.0146 87  TYR A CB  
684  C CG  . TYR A 109 ? 0.1992 0.3117 0.1956 -0.0786 -0.0399 0.0061  87  TYR A CG  
685  C CD1 . TYR A 109 ? 0.1935 0.3216 0.2029 -0.0562 -0.0451 0.0286  87  TYR A CD1 
686  C CD2 . TYR A 109 ? 0.1970 0.3103 0.1914 -0.0747 -0.0393 0.0023  87  TYR A CD2 
687  C CE1 . TYR A 109 ? 0.1962 0.3325 0.2142 -0.0314 -0.0427 0.0460  87  TYR A CE1 
688  C CE2 . TYR A 109 ? 0.1934 0.3229 0.1982 -0.0490 -0.0438 0.0207  87  TYR A CE2 
689  C CZ  . TYR A 109 ? 0.1984 0.3350 0.2140 -0.0279 -0.0421 0.0420  87  TYR A CZ  
690  O OH  . TYR A 109 ? 0.1845 0.3203 0.2062 -0.0046 -0.0324 0.0581  87  TYR A OH  
691  N N   . SER A 110 ? 0.2467 0.2217 0.2441 -0.0724 -0.0019 -0.0189 88  SER A N   
692  C CA  A SER A 110 ? 0.2404 0.1998 0.2511 -0.0496 -0.0012 -0.0102 88  SER A CA  
693  C CA  B SER A 110 ? 0.2414 0.1996 0.2520 -0.0498 -0.0005 -0.0104 88  SER A CA  
694  C C   . SER A 110 ? 0.2387 0.2099 0.2389 -0.0600 -0.0007 -0.0240 88  SER A C   
695  O O   . SER A 110 ? 0.2645 0.2497 0.2450 -0.0902 0.0064  -0.0421 88  SER A O   
696  C CB  A SER A 110 ? 0.2967 0.2098 0.3215 -0.0370 0.0260  -0.0009 88  SER A CB  
697  C CB  B SER A 110 ? 0.2985 0.2085 0.3220 -0.0387 0.0285  -0.0028 88  SER A CB  
698  O OG  A SER A 110 ? 0.3185 0.1882 0.3290 -0.0579 0.0610  -0.0221 88  SER A OG  
699  O OG  B SER A 110 ? 0.2992 0.2076 0.3357 -0.0258 0.0279  0.0173  88  SER A OG  
700  N N   . TRP A 111 ? 0.2191 0.1926 0.2297 -0.0401 -0.0080 -0.0155 89  TRP A N   
701  C CA  . TRP A 111 ? 0.2509 0.2308 0.2528 -0.0476 -0.0055 -0.0273 89  TRP A CA  
702  C C   . TRP A 111 ? 0.2261 0.1797 0.2424 -0.0291 0.0045  -0.0217 89  TRP A C   
703  O O   . TRP A 111 ? 0.2310 0.1865 0.2655 -0.0091 0.0002  -0.0022 89  TRP A O   
704  C CB  . TRP A 111 ? 0.1949 0.2222 0.1929 -0.0437 -0.0245 -0.0197 89  TRP A CB  
705  C CG  . TRP A 111 ? 0.1699 0.1991 0.1775 -0.0204 -0.0333 -0.0042 89  TRP A CG  
706  C CD1 . TRP A 111 ? 0.1880 0.2303 0.1966 -0.0135 -0.0370 0.0082  89  TRP A CD1 
707  C CD2 . TRP A 111 ? 0.1869 0.2039 0.1985 -0.0083 -0.0326 -0.0027 89  TRP A CD2 
708  N NE1 . TRP A 111 ? 0.2075 0.2371 0.2149 -0.0029 -0.0335 0.0127  89  TRP A NE1 
709  C CE2 . TRP A 111 ? 0.1978 0.2175 0.2063 -0.0017 -0.0331 0.0057  89  TRP A CE2 
710  C CE3 . TRP A 111 ? 0.2027 0.2065 0.2186 -0.0056 -0.0274 -0.0085 89  TRP A CE3 
711  C CZ2 . TRP A 111 ? 0.1930 0.2063 0.1969 -0.0007 -0.0292 0.0044  89  TRP A CZ2 
712  C CZ3 . TRP A 111 ? 0.1835 0.1899 0.2019 0.0022  -0.0291 -0.0040 89  TRP A CZ3 
713  C CH2 . TRP A 111 ? 0.1946 0.2076 0.2043 0.0008  -0.0303 0.0002  89  TRP A CH2 
714  N N   . GLU A 112 ? 0.2468 0.1858 0.2543 -0.0397 0.0188  -0.0368 90  GLU A N   
715  C CA  . GLU A 112 ? 0.2509 0.1709 0.2730 -0.0224 0.0302  -0.0307 90  GLU A CA  
716  C C   . GLU A 112 ? 0.2400 0.1789 0.2490 -0.0301 0.0207  -0.0432 90  GLU A C   
717  O O   . GLU A 112 ? 0.2529 0.2071 0.2394 -0.0561 0.0210  -0.0600 90  GLU A O   
718  C CB  . GLU A 112 ? 0.3255 0.1890 0.3528 -0.0242 0.0735  -0.0345 90  GLU A CB  
719  C CG  . GLU A 112 ? 0.5083 0.3613 0.5634 0.0044  0.0886  -0.0134 90  GLU A CG  
720  C CD  . GLU A 112 ? 0.6540 0.4472 0.7251 0.0157  0.1428  -0.0025 90  GLU A CD  
721  O OE1 . GLU A 112 ? 0.7155 0.5081 0.8176 0.0450  0.1604  0.0249  90  GLU A OE1 
722  O OE2 . GLU A 112 ? 0.6820 0.4301 0.7364 -0.0035 0.1724  -0.0175 90  GLU A OE2 
723  N N   . ARG A 113 ? 0.2427 0.1904 0.2646 -0.0110 0.0127  -0.0327 91  ARG A N   
724  C CA  . ARG A 113 ? 0.2060 0.1718 0.2168 -0.0138 0.0035  -0.0405 91  ARG A CA  
725  C C   . ARG A 113 ? 0.2317 0.1819 0.2542 -0.0026 0.0143  -0.0394 91  ARG A C   
726  O O   . ARG A 113 ? 0.2208 0.1742 0.2652 0.0144  0.0160  -0.0215 91  ARG A O   
727  C CB  . ARG A 113 ? 0.1767 0.1708 0.1857 -0.0041 -0.0149 -0.0293 91  ARG A CB  
728  C CG  . ARG A 113 ? 0.1848 0.1923 0.1846 -0.0013 -0.0164 -0.0311 91  ARG A CG  
729  C CD  . ARG A 113 ? 0.1959 0.2142 0.1919 0.0090  -0.0174 -0.0185 91  ARG A CD  
730  N NE  . ARG A 113 ? 0.1862 0.2229 0.1823 0.0075  -0.0206 -0.0084 91  ARG A NE  
731  C CZ  . ARG A 113 ? 0.2261 0.2596 0.2222 0.0154  -0.0153 0.0028  91  ARG A CZ  
732  N NH1 . ARG A 113 ? 0.2106 0.2202 0.1998 0.0189  -0.0027 0.0014  91  ARG A NH1 
733  N NH2 . ARG A 113 ? 0.1894 0.2430 0.1889 0.0144  -0.0184 0.0133  91  ARG A NH2 
734  N N   . SER A 114 ? 0.2317 0.1763 0.2406 -0.0137 0.0215  -0.0550 92  SER A N   
735  C CA  . SER A 114 ? 0.2524 0.1891 0.2708 -0.0025 0.0281  -0.0540 92  SER A CA  
736  C C   . SER A 114 ? 0.2472 0.2112 0.2547 -0.0005 0.0103  -0.0546 92  SER A C   
737  O O   . SER A 114 ? 0.2285 0.2130 0.2191 -0.0106 0.0033  -0.0581 92  SER A O   
738  C CB  . SER A 114 ? 0.3009 0.2011 0.3097 -0.0174 0.0572  -0.0725 92  SER A CB  
739  O OG  . SER A 114 ? 0.3311 0.2466 0.3079 -0.0484 0.0540  -0.0933 92  SER A OG  
740  N N   . LEU A 115 ? 0.2356 0.2060 0.2538 0.0120  0.0071  -0.0468 93  LEU A N   
741  C CA  . LEU A 115 ? 0.1736 0.1545 0.1797 0.0133  0.0021  -0.0492 93  LEU A CA  
742  C C   . LEU A 115 ? 0.2307 0.2043 0.2425 0.0158  0.0103  -0.0547 93  LEU A C   
743  O O   . LEU A 115 ? 0.2531 0.2366 0.2828 0.0217  0.0123  -0.0455 93  LEU A O   
744  C CB  . LEU A 115 ? 0.1947 0.1866 0.1984 0.0137  -0.0021 -0.0417 93  LEU A CB  
745  C CG  . LEU A 115 ? 0.2025 0.1975 0.2008 0.0119  -0.0059 -0.0353 93  LEU A CG  
746  C CD1 . LEU A 115 ? 0.2025 0.2058 0.2171 0.0117  -0.0125 -0.0266 93  LEU A CD1 
747  C CD2 . LEU A 115 ? 0.2335 0.2237 0.2150 0.0047  0.0044  -0.0368 93  LEU A CD2 
748  N N   . THR A 116 ? 0.2434 0.2103 0.2417 0.0103  0.0153  -0.0660 94  THR A N   
749  C CA  . THR A 116 ? 0.2664 0.2207 0.2686 0.0111  0.0261  -0.0737 94  THR A CA  
750  C C   . THR A 116 ? 0.2638 0.2260 0.2535 0.0135  0.0236  -0.0757 94  THR A C   
751  O O   . THR A 116 ? 0.2482 0.2188 0.2215 0.0103  0.0234  -0.0764 94  THR A O   
752  C CB  . THR A 116 ? 0.3000 0.2352 0.2903 -0.0050 0.0407  -0.0894 94  THR A CB  
753  O OG1 . THR A 116 ? 0.3203 0.2366 0.3170 -0.0102 0.0524  -0.0896 94  THR A OG1 
754  C CG2 . THR A 116 ? 0.3528 0.2650 0.3480 -0.0040 0.0593  -0.0981 94  THR A CG2 
755  N N   . PHE A 117 ? 0.2382 0.2049 0.2355 0.0171  0.0249  -0.0732 95  PHE A N   
756  C CA  . PHE A 117 ? 0.2471 0.2104 0.2284 0.0154  0.0312  -0.0782 95  PHE A CA  
757  C C   . PHE A 117 ? 0.2665 0.2218 0.2476 0.0161  0.0380  -0.0868 95  PHE A C   
758  O O   . PHE A 117 ? 0.2373 0.1913 0.2357 0.0179  0.0412  -0.0878 95  PHE A O   
759  C CB  . PHE A 117 ? 0.2345 0.2103 0.2130 0.0049  0.0338  -0.0780 95  PHE A CB  
760  C CG  . PHE A 117 ? 0.2324 0.2115 0.2038 -0.0013 0.0321  -0.0730 95  PHE A CG  
761  C CD1 . PHE A 117 ? 0.2519 0.2541 0.2414 -0.0011 0.0189  -0.0620 95  PHE A CD1 
762  C CD2 . PHE A 117 ? 0.3067 0.2607 0.2535 -0.0059 0.0508  -0.0770 95  PHE A CD2 
763  C CE1 . PHE A 117 ? 0.1815 0.1870 0.1625 -0.0089 0.0174  -0.0586 95  PHE A CE1 
764  C CE2 . PHE A 117 ? 0.2212 0.1712 0.1592 -0.0136 0.0557  -0.0741 95  PHE A CE2 
765  C CZ  . PHE A 117 ? 0.2438 0.2221 0.1975 -0.0169 0.0355  -0.0667 95  PHE A CZ  
766  N N   . GLU A 118 ? 0.2489 0.1984 0.2122 0.0177  0.0419  -0.0826 96  GLU A N   
767  C CA  . GLU A 118 ? 0.2679 0.2142 0.2277 0.0175  0.0433  -0.0842 96  GLU A CA  
768  C C   . GLU A 118 ? 0.2854 0.2315 0.2563 0.0152  0.0451  -0.0865 96  GLU A C   
769  O O   . GLU A 118 ? 0.3037 0.2450 0.2769 0.0148  0.0475  -0.0887 96  GLU A O   
770  C CB  . GLU A 118 ? 0.2864 0.2334 0.2316 0.0237  0.0522  -0.0793 96  GLU A CB  
771  C CG  . GLU A 118 ? 0.2903 0.2284 0.2335 0.0239  0.0609  -0.0734 96  GLU A CG  
772  C CD  . GLU A 118 ? 0.4517 0.3829 0.3879 0.0299  0.0769  -0.0653 96  GLU A CD  
773  O OE1 . GLU A 118 ? 0.4450 0.3774 0.3811 0.0281  0.0744  -0.0694 96  GLU A OE1 
774  O OE2 . GLU A 118 ? 0.3535 0.2753 0.2842 0.0396  0.0955  -0.0495 96  GLU A OE2 
775  N N   . ASP A 119 ? 0.2839 0.2416 0.2612 0.0096  0.0486  -0.0900 97  ASP A N   
776  C CA  . ASP A 119 ? 0.3031 0.2798 0.2960 0.0048  0.0566  -0.0984 97  ASP A CA  
777  C C   . ASP A 119 ? 0.2685 0.2733 0.2977 0.0146  0.0545  -0.0824 97  ASP A C   
778  O O   . ASP A 119 ? 0.2343 0.2802 0.2864 0.0147  0.0566  -0.0686 97  ASP A O   
779  C CB  . ASP A 119 ? 0.2656 0.2599 0.2414 -0.0167 0.0625  -0.1053 97  ASP A CB  
780  C CG  . ASP A 119 ? 0.2981 0.3188 0.2696 -0.0320 0.0581  -0.1022 97  ASP A CG  
781  O OD1 . ASP A 119 ? 0.2715 0.2904 0.2540 -0.0202 0.0480  -0.0916 97  ASP A OD1 
782  O OD2 . ASP A 119 ? 0.2790 0.3237 0.2318 -0.0619 0.0659  -0.1108 97  ASP A OD2 
783  N N   . GLY A 120 ? 0.2312 0.2191 0.2681 0.0239  0.0536  -0.0769 98  GLY A N   
784  C CA  . GLY A 120 ? 0.2238 0.2232 0.2960 0.0388  0.0623  -0.0549 98  GLY A CA  
785  C C   . GLY A 120 ? 0.1911 0.2316 0.2788 0.0400  0.0509  -0.0328 98  GLY A C   
786  O O   . GLY A 120 ? 0.1986 0.2485 0.3187 0.0576  0.0624  -0.0073 98  GLY A O   
787  N N   . GLY A 121 ? 0.2302 0.2914 0.2949 0.0216  0.0351  -0.0403 99  GLY A N   
788  C CA  . GLY A 121 ? 0.2595 0.3579 0.3323 0.0171  0.0246  -0.0230 99  GLY A CA  
789  C C   . GLY A 121 ? 0.1966 0.2542 0.2690 0.0285  0.0255  -0.0244 99  GLY A C   
790  O O   . GLY A 121 ? 0.2377 0.2519 0.2858 0.0254  0.0263  -0.0454 99  GLY A O   
791  N N   . ILE A 122 ? 0.1799 0.2594 0.2809 0.0414  0.0280  0.0022  100 ILE A N   
792  C CA  . ILE A 122 ? 0.2144 0.2533 0.3155 0.0493  0.0347  0.0005  100 ILE A CA  
793  C C   . ILE A 122 ? 0.1985 0.2746 0.3063 0.0468  0.0216  0.0193  100 ILE A C   
794  O O   . ILE A 122 ? 0.1719 0.3093 0.3077 0.0530  0.0199  0.0522  100 ILE A O   
795  C CB  . ILE A 122 ? 0.3421 0.3483 0.4711 0.0699  0.0665  0.0146  100 ILE A CB  
796  C CG1 . ILE A 122 ? 0.3615 0.3259 0.4801 0.0674  0.0849  -0.0069 100 ILE A CG1 
797  C CG2 . ILE A 122 ? 0.3669 0.3290 0.4875 0.0679  0.0782  0.0074  100 ILE A CG2 
798  C CD1 . ILE A 122 ? 0.4993 0.4419 0.5760 0.0449  0.0698  -0.0424 100 ILE A CD1 
799  N N   . CYS A 123 ? 0.1885 0.2377 0.2735 0.0378  0.0134  0.0034  101 CYS A N   
800  C CA  . CYS A 123 ? 0.1689 0.2444 0.2585 0.0352  0.0037  0.0188  101 CYS A CA  
801  C C   . CYS A 123 ? 0.2142 0.2472 0.3053 0.0428  0.0130  0.0162  101 CYS A C   
802  O O   . CYS A 123 ? 0.2396 0.2297 0.3129 0.0373  0.0202  -0.0068 101 CYS A O   
803  C CB  . CYS A 123 ? 0.1927 0.2777 0.2501 0.0122  -0.0101 0.0026  101 CYS A CB  
804  S SG  . CYS A 123 ? 0.1973 0.3272 0.2398 -0.0127 -0.0117 -0.0025 101 CYS A SG  
805  N N   . ASN A 124 ? 0.1803 0.2341 0.2900 0.0506  0.0135  0.0404  102 ASN A N   
806  C CA  . ASN A 124 ? 0.2266 0.2422 0.3337 0.0527  0.0233  0.0369  102 ASN A CA  
807  C C   . ASN A 124 ? 0.1788 0.2268 0.2802 0.0448  0.0036  0.0458  102 ASN A C   
808  O O   . ASN A 124 ? 0.1891 0.2952 0.3043 0.0445  -0.0059 0.0706  102 ASN A O   
809  C CB  . ASN A 124 ? 0.3101 0.3027 0.4499 0.0757  0.0586  0.0623  102 ASN A CB  
810  C CG  . ASN A 124 ? 0.4509 0.3908 0.5878 0.0770  0.0891  0.0452  102 ASN A CG  
811  O OD1 . ASN A 124 ? 0.5224 0.4263 0.6259 0.0541  0.0883  0.0080  102 ASN A OD1 
812  N ND2 . ASN A 124 ? 0.6457 0.5897 0.8190 0.1030  0.1183  0.0766  102 ASN A ND2 
813  N N   . ALA A 125 ? 0.1782 0.1987 0.2588 0.0344  -0.0016 0.0276  103 ALA A N   
814  C CA  . ALA A 125 ? 0.1751 0.2192 0.2483 0.0262  -0.0164 0.0341  103 ALA A CA  
815  C C   . ALA A 125 ? 0.2108 0.2251 0.2823 0.0268  -0.0100 0.0310  103 ALA A C   
816  O O   . ALA A 125 ? 0.2226 0.2005 0.2855 0.0223  0.0024  0.0138  103 ALA A O   
817  C CB  . ALA A 125 ? 0.1556 0.2029 0.1996 0.0093  -0.0275 0.0151  103 ALA A CB  
818  N N   . ARG A 126 ? 0.2113 0.2462 0.2870 0.0258  -0.0173 0.0459  104 ARG A N   
819  C CA  . ARG A 126 ? 0.1857 0.1937 0.2590 0.0246  -0.0107 0.0431  104 ARG A CA  
820  C C   . ARG A 126 ? 0.2100 0.2424 0.2731 0.0152  -0.0272 0.0473  104 ARG A C   
821  O O   . ARG A 126 ? 0.1934 0.2664 0.2566 0.0093  -0.0370 0.0599  104 ARG A O   
822  C CB  . ARG A 126 ? 0.3054 0.2955 0.4059 0.0427  0.0164  0.0663  104 ARG A CB  
823  C CG  . ARG A 126 ? 0.5373 0.4845 0.6335 0.0387  0.0363  0.0606  104 ARG A CG  
824  C CD  . ARG A 126 ? 0.4768 0.4277 0.6056 0.0635  0.0594  0.1018  104 ARG A CD  
825  N NE  . ARG A 126 ? 0.6351 0.5696 0.7576 0.0578  0.0634  0.1022  104 ARG A NE  
826  C CZ  . ARG A 126 ? 0.7775 0.6489 0.8863 0.0462  0.0950  0.0819  104 ARG A CZ  
827  N NH1 . ARG A 126 ? 0.7355 0.5552 0.8295 0.0326  0.1249  0.0551  104 ARG A NH1 
828  N NH2 . ARG A 126 ? 0.7125 0.5725 0.8180 0.0422  0.1000  0.0859  104 ARG A NH2 
829  N N   . ASN A 127 ? 0.1783 0.1904 0.2291 0.0079  -0.0281 0.0353  105 ASN A N   
830  C CA  . ASN A 127 ? 0.2069 0.2330 0.2480 -0.0002 -0.0381 0.0385  105 ASN A CA  
831  C C   . ASN A 127 ? 0.2136 0.2210 0.2579 -0.0004 -0.0322 0.0396  105 ASN A C   
832  O O   . ASN A 127 ? 0.2313 0.2179 0.2692 -0.0068 -0.0245 0.0245  105 ASN A O   
833  C CB  . ASN A 127 ? 0.2151 0.2384 0.2354 -0.0084 -0.0410 0.0239  105 ASN A CB  
834  C CG  . ASN A 127 ? 0.1834 0.2120 0.1909 -0.0185 -0.0411 0.0263  105 ASN A CG  
835  O OD1 . ASN A 127 ? 0.2523 0.2958 0.2640 -0.0235 -0.0457 0.0374  105 ASN A OD1 
836  N ND2 . ASN A 127 ? 0.2078 0.2232 0.2001 -0.0208 -0.0303 0.0192  105 ASN A ND2 
837  N N   . ASP A 128 ? 0.1828 0.2040 0.2349 0.0016  -0.0340 0.0576  106 ASP A N   
838  C CA  . ASP A 128 ? 0.2042 0.2073 0.2575 0.0001  -0.0274 0.0595  106 ASP A CA  
839  C C   . ASP A 128 ? 0.2200 0.2374 0.2576 -0.0115 -0.0408 0.0549  106 ASP A C   
840  O O   . ASP A 128 ? 0.2024 0.2470 0.2361 -0.0172 -0.0480 0.0658  106 ASP A O   
841  C CB  . ASP A 128 ? 0.2432 0.2512 0.3202 0.0158  -0.0136 0.0903  106 ASP A CB  
842  C CG  . ASP A 128 ? 0.5662 0.5444 0.6613 0.0317  0.0147  0.0982  106 ASP A CG  
843  O OD1 . ASP A 128 ? 0.6741 0.6820 0.7901 0.0477  0.0172  0.1229  106 ASP A OD1 
844  O OD2 . ASP A 128 ? 0.6680 0.5937 0.7537 0.0237  0.0387  0.0779  106 ASP A OD2 
845  N N   . ILE A 129 ? 0.2125 0.2182 0.2397 -0.0186 -0.0407 0.0404  107 ILE A N   
846  C CA  . ILE A 129 ? 0.2414 0.2556 0.2572 -0.0242 -0.0447 0.0391  107 ILE A CA  
847  C C   . ILE A 129 ? 0.2314 0.2413 0.2484 -0.0290 -0.0440 0.0420  107 ILE A C   
848  O O   . ILE A 129 ? 0.2383 0.2416 0.2569 -0.0346 -0.0394 0.0351  107 ILE A O   
849  C CB  . ILE A 129 ? 0.2001 0.2211 0.2108 -0.0219 -0.0416 0.0332  107 ILE A CB  
850  C CG1 . ILE A 129 ? 0.2173 0.2371 0.2260 -0.0170 -0.0398 0.0291  107 ILE A CG1 
851  C CG2 . ILE A 129 ? 0.2153 0.2368 0.2194 -0.0205 -0.0325 0.0396  107 ILE A CG2 
852  C CD1 . ILE A 129 ? 0.2005 0.2340 0.2090 -0.0101 -0.0341 0.0309  107 ILE A CD1 
853  N N   . THR A 130 ? 0.2528 0.2671 0.2640 -0.0332 -0.0457 0.0492  108 THR A N   
854  C CA  . THR A 130 ? 0.3214 0.3317 0.3322 -0.0378 -0.0449 0.0521  108 THR A CA  
855  C C   . THR A 130 ? 0.2955 0.3066 0.2943 -0.0425 -0.0394 0.0510  108 THR A C   
856  O O   . THR A 130 ? 0.2677 0.2743 0.2557 -0.0440 -0.0303 0.0476  108 THR A O   
857  C CB  . THR A 130 ? 0.3085 0.3221 0.3255 -0.0375 -0.0458 0.0675  108 THR A CB  
858  O OG1 . THR A 130 ? 0.2558 0.2960 0.2653 -0.0448 -0.0511 0.0767  108 THR A OG1 
859  C CG2 . THR A 130 ? 0.2750 0.2735 0.3088 -0.0262 -0.0352 0.0753  108 THR A CG2 
860  N N   . MET A 131 ? 0.2666 0.2769 0.2663 -0.0455 -0.0378 0.0537  109 MET A N   
861  C CA  . MET A 131 ? 0.3356 0.3404 0.3272 -0.0476 -0.0249 0.0563  109 MET A CA  
862  C C   . MET A 131 ? 0.2951 0.2945 0.2792 -0.0590 -0.0264 0.0586  109 MET A C   
863  O O   . MET A 131 ? 0.3017 0.3046 0.2946 -0.0591 -0.0351 0.0617  109 MET A O   
864  C CB  . MET A 131 ? 0.3212 0.3444 0.3259 -0.0380 -0.0186 0.0648  109 MET A CB  
865  C CG  . MET A 131 ? 0.2912 0.3062 0.2955 -0.0264 0.0085  0.0764  109 MET A CG  
866  S SD  . MET A 131 ? 0.3715 0.4426 0.4037 -0.0098 0.0128  0.1033  109 MET A SD  
867  C CE  . MET A 131 ? 0.3744 0.4504 0.4056 -0.0250 0.0023  0.0994  109 MET A CE  
868  N N   . GLU A 132 ? 0.3383 0.3247 0.3027 -0.0719 -0.0116 0.0554  110 GLU A N   
869  C CA  . GLU A 132 ? 0.3861 0.3689 0.3388 -0.0866 -0.0086 0.0568  110 GLU A CA  
870  C C   . GLU A 132 ? 0.3699 0.3231 0.3079 -0.0910 0.0239  0.0519  110 GLU A C   
871  O O   . GLU A 132 ? 0.3504 0.2811 0.2655 -0.1048 0.0482  0.0412  110 GLU A O   
872  C CB  . GLU A 132 ? 0.3793 0.3849 0.3156 -0.1089 -0.0186 0.0590  110 GLU A CB  
873  C CG  . GLU A 132 ? 0.3394 0.3730 0.2985 -0.0954 -0.0397 0.0760  110 GLU A CG  
874  C CD  . GLU A 132 ? 0.4092 0.4917 0.3601 -0.1131 -0.0486 0.0923  110 GLU A CD  
875  O OE1 . GLU A 132 ? 0.3882 0.4869 0.3113 -0.1440 -0.0433 0.0877  110 GLU A OE1 
876  O OE2 . GLU A 132 ? 0.3330 0.4445 0.3059 -0.0979 -0.0579 0.1132  110 GLU A OE2 
877  N N   . GLY A 133 ? 0.3517 0.4594 0.3659 -0.0543 0.0300  0.0520  111 GLY A N   
878  C CA  . GLY A 133 ? 0.2847 0.4148 0.3046 -0.0436 0.0363  0.0627  111 GLY A CA  
879  C C   . GLY A 133 ? 0.2751 0.4341 0.3039 -0.0307 0.0326  0.0673  111 GLY A C   
880  O O   . GLY A 133 ? 0.3264 0.5237 0.3705 -0.0369 0.0236  0.0635  111 GLY A O   
881  N N   . ASP A 134 ? 0.2702 0.4088 0.2862 -0.0145 0.0436  0.0748  112 ASP A N   
882  C CA  . ASP A 134 ? 0.2585 0.4124 0.2798 0.0024  0.0495  0.0830  112 ASP A CA  
883  C C   . ASP A 134 ? 0.2619 0.3897 0.2666 0.0016  0.0400  0.0704  112 ASP A C   
884  O O   . ASP A 134 ? 0.2833 0.4065 0.2843 0.0156  0.0513  0.0754  112 ASP A O   
885  C CB  . ASP A 134 ? 0.3022 0.4381 0.3172 0.0200  0.0793  0.0976  112 ASP A CB  
886  C CG  . ASP A 134 ? 0.4008 0.4766 0.3798 0.0115  0.0918  0.0845  112 ASP A CG  
887  O OD1 . ASP A 134 ? 0.4573 0.5187 0.4207 -0.0049 0.0735  0.0700  112 ASP A OD1 
888  O OD2 . ASP A 134 ? 0.5287 0.5753 0.4941 0.0202  0.1237  0.0901  112 ASP A OD2 
889  N N   . THR A 135 ? 0.2515 0.3628 0.2474 -0.0122 0.0237  0.0570  113 THR A N   
890  C CA  . THR A 135 ? 0.2758 0.3678 0.2573 -0.0129 0.0153  0.0470  113 THR A CA  
891  C C   . THR A 135 ? 0.3019 0.4067 0.2959 -0.0194 -0.0008 0.0396  113 THR A C   
892  O O   . THR A 135 ? 0.2327 0.3375 0.2336 -0.0302 -0.0037 0.0369  113 THR A O   
893  C CB  . THR A 135 ? 0.2778 0.3441 0.2352 -0.0202 0.0151  0.0427  113 THR A CB  
894  O OG1 . THR A 135 ? 0.2761 0.3273 0.2162 -0.0211 0.0345  0.0447  113 THR A OG1 
895  C CG2 . THR A 135 ? 0.2554 0.3162 0.2000 -0.0224 0.0070  0.0337  113 THR A CG2 
896  N N   . PHE A 136 ? 0.2572 0.3668 0.2515 -0.0145 -0.0057 0.0351  114 PHE A N   
897  C CA  . PHE A 136 ? 0.2003 0.3111 0.1999 -0.0218 -0.0176 0.0253  114 PHE A CA  
898  C C   . PHE A 136 ? 0.1965 0.2802 0.1819 -0.0206 -0.0218 0.0213  114 PHE A C   
899  O O   . PHE A 136 ? 0.2746 0.3503 0.2448 -0.0166 -0.0187 0.0202  114 PHE A O   
900  C CB  . PHE A 136 ? 0.2137 0.3483 0.2203 -0.0168 -0.0209 0.0240  114 PHE A CB  
901  C CG  . PHE A 136 ? 0.2106 0.3972 0.2349 -0.0199 -0.0206 0.0314  114 PHE A CG  
902  C CD1 . PHE A 136 ? 0.1957 0.4061 0.2294 -0.0429 -0.0248 0.0216  114 PHE A CD1 
903  C CD2 . PHE A 136 ? 0.1532 0.3700 0.1842 -0.0008 -0.0115 0.0494  114 PHE A CD2 
904  C CE1 . PHE A 136 ? 0.2234 0.5016 0.2727 -0.0523 -0.0260 0.0270  114 PHE A CE1 
905  C CE2 . PHE A 136 ? 0.1638 0.4501 0.2145 -0.0010 -0.0124 0.0629  114 PHE A CE2 
906  C CZ  . PHE A 136 ? 0.2384 0.5629 0.2982 -0.0298 -0.0227 0.0502  114 PHE A CZ  
907  N N   . TYR A 137 ? 0.2229 0.2953 0.2123 -0.0250 -0.0242 0.0203  115 TYR A N   
908  C CA  . TYR A 137 ? 0.2613 0.3237 0.2439 -0.0190 -0.0278 0.0235  115 TYR A CA  
909  C C   . TYR A 137 ? 0.2325 0.2895 0.2237 -0.0197 -0.0303 0.0155  115 TYR A C   
910  O O   . TYR A 137 ? 0.2352 0.2866 0.2355 -0.0296 -0.0246 0.0081  115 TYR A O   
911  C CB  . TYR A 137 ? 0.2474 0.2997 0.2290 -0.0149 -0.0208 0.0380  115 TYR A CB  
912  C CG  . TYR A 137 ? 0.2289 0.2898 0.1970 -0.0151 -0.0197 0.0460  115 TYR A CG  
913  C CD1 . TYR A 137 ? 0.2455 0.3249 0.1960 -0.0159 -0.0251 0.0473  115 TYR A CD1 
914  C CD2 . TYR A 137 ? 0.2759 0.3288 0.2465 -0.0195 -0.0109 0.0491  115 TYR A CD2 
915  C CE1 . TYR A 137 ? 0.2860 0.3728 0.2189 -0.0221 -0.0206 0.0509  115 TYR A CE1 
916  C CE2 . TYR A 137 ? 0.2904 0.3480 0.2468 -0.0207 -0.0077 0.0555  115 TYR A CE2 
917  C CZ  . TYR A 137 ? 0.3089 0.3818 0.2451 -0.0226 -0.0120 0.0558  115 TYR A CZ  
918  O OH  . TYR A 137 ? 0.3077 0.3847 0.2249 -0.0296 -0.0055 0.0587  115 TYR A OH  
919  N N   . ASN A 138 ? 0.2160 0.2769 0.2023 -0.0137 -0.0367 0.0145  116 ASN A N   
920  C CA  . ASN A 138 ? 0.2347 0.2901 0.2276 -0.0137 -0.0387 0.0059  116 ASN A CA  
921  C C   . ASN A 138 ? 0.1991 0.2561 0.1943 -0.0033 -0.0385 0.0164  116 ASN A C   
922  O O   . ASN A 138 ? 0.2345 0.3147 0.2207 -0.0009 -0.0457 0.0201  116 ASN A O   
923  C CB  . ASN A 138 ? 0.1875 0.2522 0.1744 -0.0147 -0.0443 -0.0050 116 ASN A CB  
924  C CG  . ASN A 138 ? 0.2164 0.2925 0.2049 -0.0172 -0.0417 -0.0061 116 ASN A CG  
925  O OD1 . ASN A 138 ? 0.2155 0.3043 0.2114 -0.0218 -0.0431 -0.0110 116 ASN A OD1 
926  N ND2 . ASN A 138 ? 0.2060 0.2846 0.1876 -0.0143 -0.0361 0.0006  116 ASN A ND2 
927  N N   . LYS A 139 ? 0.2034 0.2392 0.2096 0.0013  -0.0262 0.0217  117 LYS A N   
928  C CA  . LYS A 139 ? 0.2136 0.2544 0.2278 0.0178  -0.0210 0.0383  117 LYS A CA  
929  C C   . LYS A 139 ? 0.2112 0.2405 0.2303 0.0145  -0.0208 0.0237  117 LYS A C   
930  O O   . LYS A 139 ? 0.2234 0.2192 0.2464 0.0065  -0.0055 0.0136  117 LYS A O   
931  C CB  . LYS A 139 ? 0.2492 0.2634 0.2723 0.0309  0.0040  0.0595  117 LYS A CB  
932  C CG  . LYS A 139 ? 0.2488 0.2718 0.2665 0.0356  0.0064  0.0761  117 LYS A CG  
933  C CD  . LYS A 139 ? 0.3130 0.2950 0.3381 0.0488  0.0406  0.0960  117 LYS A CD  
934  C CE  . LYS A 139 ? 0.3058 0.2944 0.3242 0.0540  0.0445  0.1133  117 LYS A CE  
935  N NZ  . LYS A 139 ? 0.3798 0.3148 0.4020 0.0629  0.0853  0.1282  117 LYS A NZ  
936  N N   . VAL A 140 ? 0.1961 0.2527 0.2123 0.0162  -0.0349 0.0199  118 VAL A N   
937  C CA  . VAL A 140 ? 0.1840 0.2312 0.2021 0.0117  -0.0366 0.0040  118 VAL A CA  
938  C C   . VAL A 140 ? 0.2055 0.2665 0.2364 0.0271  -0.0319 0.0187  118 VAL A C   
939  O O   . VAL A 140 ? 0.1952 0.3000 0.2282 0.0360  -0.0388 0.0356  118 VAL A O   
940  C CB  . VAL A 140 ? 0.2288 0.2901 0.2328 0.0012  -0.0497 -0.0132 118 VAL A CB  
941  C CG1 . VAL A 140 ? 0.1960 0.2481 0.2008 -0.0013 -0.0502 -0.0272 118 VAL A CG1 
942  C CG2 . VAL A 140 ? 0.2108 0.2649 0.2073 -0.0071 -0.0501 -0.0197 118 VAL A CG2 
943  N N   . ARG A 141 ? 0.2022 0.2330 0.2413 0.0287  -0.0186 0.0129  119 ARG A N   
944  C CA  . ARG A 141 ? 0.1964 0.2383 0.2502 0.0446  -0.0113 0.0260  119 ARG A CA  
945  C C   . ARG A 141 ? 0.2479 0.2811 0.2967 0.0326  -0.0181 0.0016  119 ARG A C   
946  O O   . ARG A 141 ? 0.2377 0.2391 0.2767 0.0167  -0.0156 -0.0199 119 ARG A O   
947  C CB  . ARG A 141 ? 0.2855 0.2871 0.3535 0.0607  0.0219  0.0446  119 ARG A CB  
948  C CG  . ARG A 141 ? 0.3502 0.3564 0.4235 0.0778  0.0350  0.0744  119 ARG A CG  
949  C CD  . ARG A 141 ? 0.6414 0.5773 0.7123 0.0729  0.0717  0.0710  119 ARG A CD  
950  N NE  . ARG A 141 ? 0.8018 0.7355 0.8706 0.0808  0.0810  0.0902  119 ARG A NE  
951  C CZ  . ARG A 141 ? 0.8055 0.7294 0.8599 0.0581  0.0724  0.0711  119 ARG A CZ  
952  N NH1 . ARG A 141 ? 0.4133 0.3385 0.4555 0.0285  0.0528  0.0363  119 ARG A NH1 
953  N NH2 . ARG A 141 ? 0.7049 0.6227 0.7585 0.0677  0.0854  0.0910  119 ARG A NH2 
954  N N   . PHE A 142 ? 0.2055 0.2747 0.2602 0.0386  -0.0264 0.0053  120 PHE A N   
955  C CA  . PHE A 142 ? 0.1890 0.2498 0.2378 0.0280  -0.0313 -0.0172 120 PHE A CA  
956  C C   . PHE A 142 ? 0.1872 0.2665 0.2553 0.0428  -0.0230 -0.0038 120 PHE A C   
957  O O   . PHE A 142 ? 0.2073 0.3426 0.2874 0.0545  -0.0276 0.0181  120 PHE A O   
958  C CB  . PHE A 142 ? 0.1818 0.2676 0.2120 0.0128  -0.0475 -0.0339 120 PHE A CB  
959  C CG  . PHE A 142 ? 0.1751 0.2387 0.1942 0.0027  -0.0474 -0.0570 120 PHE A CG  
960  C CD1 . PHE A 142 ? 0.1875 0.2626 0.2124 0.0031  -0.0456 -0.0622 120 PHE A CD1 
961  C CD2 . PHE A 142 ? 0.2072 0.2455 0.2111 -0.0051 -0.0475 -0.0693 120 PHE A CD2 
962  C CE1 . PHE A 142 ? 0.2004 0.2506 0.2133 -0.0047 -0.0416 -0.0796 120 PHE A CE1 
963  C CE2 . PHE A 142 ? 0.2198 0.2376 0.2127 -0.0088 -0.0371 -0.0686 120 PHE A CE2 
964  C CZ  . PHE A 142 ? 0.2397 0.2582 0.2357 -0.0086 -0.0336 -0.0727 120 PHE A CZ  
965  N N   . TYR A 143 ? 0.1915 0.2321 0.2627 0.0417  -0.0100 -0.0152 121 TYR A N   
966  C CA  . TYR A 143 ? 0.1849 0.2388 0.2763 0.0574  0.0016  -0.0021 121 TYR A CA  
967  C C   . TYR A 143 ? 0.2479 0.2837 0.3292 0.0425  -0.0024 -0.0298 121 TYR A C   
968  O O   . TYR A 143 ? 0.2518 0.2426 0.3167 0.0274  0.0011  -0.0516 121 TYR A O   
969  C CB  . TYR A 143 ? 0.2238 0.2339 0.3317 0.0764  0.0360  0.0180  121 TYR A CB  
970  C CG  . TYR A 143 ? 0.3536 0.3694 0.4841 0.0958  0.0547  0.0333  121 TYR A CG  
971  C CD1 . TYR A 143 ? 0.2596 0.3421 0.4178 0.1251  0.0570  0.0727  121 TYR A CD1 
972  C CD2 . TYR A 143 ? 0.2995 0.2631 0.4239 0.0846  0.0703  0.0104  121 TYR A CD2 
973  C CE1 . TYR A 143 ? 0.2543 0.3506 0.4377 0.1464  0.0761  0.0917  121 TYR A CE1 
974  C CE2 . TYR A 143 ? 0.3201 0.2860 0.4665 0.1037  0.0908  0.0253  121 TYR A CE2 
975  C CZ  . TYR A 143 ? 0.3673 0.3997 0.5448 0.1359  0.0937  0.0668  121 TYR A CZ  
976  O OH  . TYR A 143 ? 0.4102 0.4510 0.6055 0.1517  0.1117  0.0834  121 TYR A OH  
977  N N   . GLY A 144 ? 0.1648 0.2418 0.2556 0.0456  -0.0082 -0.0278 122 GLY A N   
978  C CA  . GLY A 144 ? 0.2070 0.2657 0.2882 0.0329  -0.0091 -0.0527 122 GLY A CA  
979  C C   . GLY A 144 ? 0.1846 0.2710 0.2902 0.0468  0.0009  -0.0396 122 GLY A C   
980  O O   . GLY A 144 ? 0.1888 0.3400 0.3158 0.0609  -0.0015 -0.0136 122 GLY A O   
981  N N   . THR A 145 ? 0.2344 0.2797 0.3371 0.0425  0.0123  -0.0559 123 THR A N   
982  C CA  . THR A 145 ? 0.1948 0.2616 0.3223 0.0567  0.0252  -0.0436 123 THR A CA  
983  C C   . THR A 145 ? 0.2151 0.2452 0.3276 0.0410  0.0281  -0.0732 123 THR A C   
984  O O   . THR A 145 ? 0.2909 0.2776 0.3752 0.0232  0.0233  -0.0980 123 THR A O   
985  C CB  . THR A 145 ? 0.2741 0.3155 0.4267 0.0843  0.0562  -0.0132 123 THR A CB  
986  O OG1 . THR A 145 ? 0.3017 0.3884 0.4862 0.1062  0.0682  0.0110  123 THR A OG1 
987  C CG2 . THR A 145 ? 0.3384 0.2887 0.4733 0.0728  0.0802  -0.0344 123 THR A CG2 
988  N N   . ASN A 146 ? 0.1842 0.3411 0.4300 0.0627  0.0368  -0.0283 124 ASN A N   
989  C CA  . ASN A 146 ? 0.1632 0.3177 0.4074 0.0568  0.0526  -0.0375 124 ASN A CA  
990  C C   . ASN A 146 ? 0.2036 0.3601 0.4364 0.0455  0.0556  -0.0407 124 ASN A C   
991  O O   . ASN A 146 ? 0.1852 0.3346 0.4071 0.0396  0.0693  -0.0462 124 ASN A O   
992  C CB  . ASN A 146 ? 0.2398 0.3730 0.4680 0.0591  0.0641  -0.0439 124 ASN A CB  
993  C CG  . ASN A 146 ? 0.3556 0.4864 0.5998 0.0684  0.0663  -0.0446 124 ASN A CG  
994  O OD1 . ASN A 146 ? 0.3607 0.5056 0.6283 0.0742  0.0592  -0.0386 124 ASN A OD1 
995  N ND2 . ASN A 146 ? 0.4082 0.5214 0.6400 0.0695  0.0759  -0.0524 124 ASN A ND2 
996  N N   . PHE A 147 ? 0.1789 0.3448 0.4129 0.0417  0.0435  -0.0374 125 PHE A N   
997  C CA  . PHE A 147 ? 0.1144 0.2823 0.3433 0.0302  0.0472  -0.0415 125 PHE A CA  
998  C C   . PHE A 147 ? 0.1741 0.3587 0.4251 0.0247  0.0523  -0.0434 125 PHE A C   
999  O O   . PHE A 147 ? 0.1771 0.3799 0.4493 0.0279  0.0432  -0.0408 125 PHE A O   
1000 C CB  . PHE A 147 ? 0.1045 0.2744 0.3237 0.0266  0.0323  -0.0395 125 PHE A CB  
1001 C CG  . PHE A 147 ? 0.1069 0.2537 0.2929 0.0282  0.0285  -0.0360 125 PHE A CG  
1002 C CD1 . PHE A 147 ? 0.1283 0.2550 0.2893 0.0221  0.0367  -0.0373 125 PHE A CD1 
1003 C CD2 . PHE A 147 ? 0.1651 0.3119 0.3465 0.0357  0.0167  -0.0301 125 PHE A CD2 
1004 C CE1 . PHE A 147 ? 0.1574 0.2656 0.2914 0.0235  0.0323  -0.0341 125 PHE A CE1 
1005 C CE2 . PHE A 147 ? 0.1926 0.3199 0.3465 0.0364  0.0140  -0.0269 125 PHE A CE2 
1006 C CZ  . PHE A 147 ? 0.1682 0.2768 0.2995 0.0304  0.0215  -0.0297 125 PHE A CZ  
1007 N N   . PRO A 148 ? 0.2104 0.3901 0.4572 0.0163  0.0667  -0.0467 126 PRO A N   
1008 C CA  . PRO A 148 ? 0.1844 0.3800 0.4536 0.0099  0.0720  -0.0480 126 PRO A CA  
1009 C C   . PRO A 148 ? 0.1484 0.3575 0.4316 0.0024  0.0595  -0.0487 126 PRO A C   
1010 O O   . PRO A 148 ? 0.1262 0.3276 0.3968 -0.0028 0.0534  -0.0501 126 PRO A O   
1011 C CB  . PRO A 148 ? 0.1916 0.3752 0.4463 0.0017  0.0898  -0.0489 126 PRO A CB  
1012 C CG  . PRO A 148 ? 0.2313 0.3938 0.4548 0.0048  0.0936  -0.0486 126 PRO A CG  
1013 C CD  . PRO A 148 ? 0.1503 0.3102 0.3701 0.0119  0.0782  -0.0478 126 PRO A CD  
1014 N N   . ALA A 149 ? 0.1269 0.3568 0.4366 0.0016  0.0556  -0.0489 127 ALA A N   
1015 C CA  . ALA A 149 ? 0.1635 0.4079 0.4866 -0.0064 0.0428  -0.0514 127 ALA A CA  
1016 C C   . ALA A 149 ? 0.2216 0.4549 0.5390 -0.0202 0.0494  -0.0555 127 ALA A C   
1017 O O   . ALA A 149 ? 0.2238 0.4570 0.5384 -0.0265 0.0386  -0.0596 127 ALA A O   
1018 C CB  . ALA A 149 ? 0.2119 0.4811 0.5656 -0.0060 0.0400  -0.0509 127 ALA A CB  
1019 N N   . ASN A 150 ? 0.1376 0.3609 0.4521 -0.0251 0.0674  -0.0540 128 ASN A N   
1020 C CA  . ASN A 150 ? 0.2291 0.4401 0.5397 -0.0382 0.0755  -0.0545 128 ASN A CA  
1021 C C   . ASN A 150 ? 0.2879 0.4745 0.5693 -0.0389 0.0819  -0.0515 128 ASN A C   
1022 O O   . ASN A 150 ? 0.2390 0.4120 0.5149 -0.0488 0.0909  -0.0486 128 ASN A O   
1023 C CB  . ASN A 150 ? 0.2629 0.4786 0.5871 -0.0443 0.0915  -0.0518 128 ASN A CB  
1024 C CG  . ASN A 150 ? 0.3544 0.5656 0.6654 -0.0367 0.1060  -0.0482 128 ASN A CG  
1025 O OD1 . ASN A 150 ? 0.2841 0.4853 0.5747 -0.0277 0.1048  -0.0478 128 ASN A OD1 
1026 N ND2 . ASN A 150 ? 0.3783 0.5972 0.7007 -0.0406 0.1199  -0.0464 128 ASN A ND2 
1027 N N   . GLY A 151 ? 0.1951 0.3756 0.4585 -0.0289 0.0773  -0.0509 129 GLY A N   
1028 C CA  . GLY A 151 ? 0.2319 0.3884 0.4637 -0.0286 0.0807  -0.0469 129 GLY A CA  
1029 C C   . GLY A 151 ? 0.2024 0.3471 0.4228 -0.0324 0.0676  -0.0481 129 GLY A C   
1030 O O   . GLY A 151 ? 0.2147 0.3730 0.4533 -0.0358 0.0563  -0.0547 129 GLY A O   
1031 N N   . PRO A 152 ? 0.1744 0.2943 0.3642 -0.0319 0.0688  -0.0426 130 PRO A N   
1032 C CA  . PRO A 152 ? 0.2027 0.3099 0.3834 -0.0351 0.0586  -0.0445 130 PRO A CA  
1033 C C   . PRO A 152 ? 0.1994 0.3139 0.3747 -0.0277 0.0424  -0.0495 130 PRO A C   
1034 O O   . PRO A 152 ? 0.1891 0.3011 0.3640 -0.0312 0.0338  -0.0550 130 PRO A O   
1035 C CB  . PRO A 152 ? 0.2143 0.2958 0.3657 -0.0342 0.0645  -0.0354 130 PRO A CB  
1036 C CG  . PRO A 152 ? 0.2563 0.3385 0.3943 -0.0283 0.0731  -0.0308 130 PRO A CG  
1037 C CD  . PRO A 152 ? 0.1685 0.2727 0.3334 -0.0296 0.0804  -0.0351 130 PRO A CD  
1038 N N   . VAL A 153 ? 0.1863 0.3090 0.3574 -0.0178 0.0388  -0.0476 131 VAL A N   
1039 C CA  . VAL A 153 ? 0.1824 0.3122 0.3473 -0.0110 0.0241  -0.0492 131 VAL A CA  
1040 C C   . VAL A 153 ? 0.1462 0.3027 0.3366 -0.0131 0.0143  -0.0556 131 VAL A C   
1041 O O   . VAL A 153 ? 0.1384 0.3005 0.3260 -0.0157 0.0032  -0.0612 131 VAL A O   
1042 C CB  . VAL A 153 ? 0.1967 0.3232 0.3498 0.0001  0.0239  -0.0433 131 VAL A CB  
1043 C CG1 . VAL A 153 ? 0.1372 0.2749 0.2890 0.0071  0.0094  -0.0421 131 VAL A CG1 
1044 C CG2 . VAL A 153 ? 0.1462 0.2480 0.2714 0.0013  0.0297  -0.0386 131 VAL A CG2 
1045 N N   . MET A 154 ? 0.1191 0.2944 0.3350 -0.0119 0.0179  -0.0556 132 MET A N   
1046 C CA  . MET A 154 ? 0.1025 0.3065 0.3461 -0.0147 0.0075  -0.0613 132 MET A CA  
1047 C C   . MET A 154 ? 0.1589 0.3656 0.4153 -0.0286 0.0073  -0.0708 132 MET A C   
1048 O O   . MET A 154 ? 0.1845 0.4066 0.4485 -0.0318 -0.0054 -0.0764 132 MET A O   
1049 C CB  . MET A 154 ? 0.1429 0.3629 0.4104 -0.0097 0.0122  -0.0574 132 MET A CB  
1050 C CG  . MET A 154 ? 0.1344 0.3533 0.3966 0.0043  0.0114  -0.0495 132 MET A CG  
1051 S SD  . MET A 154 ? 0.2224 0.4404 0.4637 0.0126  -0.0055 -0.0450 132 MET A SD  
1052 C CE  . MET A 154 ? 0.1931 0.4377 0.4486 0.0108  -0.0227 -0.0438 132 MET A CE  
1053 N N   . GLN A 155 ? 0.1291 0.3161 0.3823 -0.0364 0.0209  -0.0702 133 GLN A N   
1054 C CA  . GLN A 155 ? 0.1776 0.3639 0.4466 -0.0501 0.0218  -0.0787 133 GLN A CA  
1055 C C   . GLN A 155 ? 0.2119 0.3780 0.4594 -0.0528 0.0162  -0.0836 133 GLN A C   
1056 O O   . GLN A 155 ? 0.2119 0.3742 0.4727 -0.0640 0.0164  -0.0925 133 GLN A O   
1057 C CB  . GLN A 155 ? 0.1778 0.3531 0.4578 -0.0580 0.0400  -0.0736 133 GLN A CB  
1058 C CG  . GLN A 155 ? 0.2349 0.4266 0.5333 -0.0564 0.0461  -0.0697 133 GLN A CG  
1059 C CD  . GLN A 155 ? 0.3324 0.5463 0.6527 -0.0597 0.0339  -0.0764 133 GLN A CD  
1060 O OE1 . GLN A 155 ? 0.3708 0.6047 0.6990 -0.0518 0.0257  -0.0749 133 GLN A OE1 
1061 N NE2 . GLN A 155 ? 0.2060 0.4157 0.5364 -0.0714 0.0324  -0.0832 133 GLN A NE2 
1062 N N   . LYS A 156 ? 0.1922 0.3456 0.4099 -0.0432 0.0119  -0.0787 134 LYS A N   
1063 C CA  . LYS A 156 ? 0.2138 0.3510 0.4122 -0.0439 0.0067  -0.0838 134 LYS A CA  
1064 C C   . LYS A 156 ? 0.2064 0.3177 0.4057 -0.0516 0.0178  -0.0829 134 LYS A C   
1065 O O   . LYS A 156 ? 0.2140 0.3188 0.4212 -0.0593 0.0157  -0.0934 134 LYS A O   
1066 C CB  . LYS A 156 ? 0.1782 0.3353 0.3838 -0.0478 -0.0075 -0.0980 134 LYS A CB  
1067 C CG  . LYS A 156 ? 0.2432 0.4234 0.4409 -0.0381 -0.0201 -0.0948 134 LYS A CG  
1068 C CD  . LYS A 156 ? 0.2949 0.4989 0.4977 -0.0421 -0.0347 -0.1063 134 LYS A CD  
1069 C CE  . LYS A 156 ? 0.4187 0.6110 0.6036 -0.0460 -0.0377 -0.1184 134 LYS A CE  
1070 N NZ  . LYS A 156 ? 0.4283 0.6348 0.6110 -0.0504 -0.0480 -0.1289 134 LYS A NZ  
1071 N N   . LYS A 157 ? 0.2257 0.3219 0.4167 -0.0495 0.0297  -0.0702 135 LYS A N   
1072 C CA  . LYS A 157 ? 0.2312 0.3034 0.4223 -0.0558 0.0407  -0.0643 135 LYS A CA  
1073 C C   . LYS A 157 ? 0.2375 0.2870 0.4000 -0.0482 0.0419  -0.0548 135 LYS A C   
1074 O O   . LYS A 157 ? 0.2544 0.2848 0.4126 -0.0508 0.0511  -0.0446 135 LYS A O   
1075 C CB  . LYS A 157 ? 0.2378 0.3134 0.4425 -0.0612 0.0544  -0.0559 135 LYS A CB  
1076 C CG  . LYS A 157 ? 0.3007 0.3989 0.5400 -0.0705 0.0546  -0.0650 135 LYS A CG  
1077 C CD  . LYS A 157 ? 0.5101 0.6122 0.7629 -0.0758 0.0706  -0.0560 135 LYS A CD  
1078 C CE  . LYS A 157 ? 0.5125 0.6344 0.7994 -0.0849 0.0706  -0.0637 135 LYS A CE  
1079 N NZ  . LYS A 157 ? 0.5013 0.6332 0.7945 -0.0843 0.0834  -0.0550 135 LYS A NZ  
1080 N N   . THR A 158 ? 0.1980 0.2503 0.3421 -0.0390 0.0325  -0.0566 136 THR A N   
1081 C CA  . THR A 158 ? 0.1630 0.1971 0.2830 -0.0318 0.0326  -0.0481 136 THR A CA  
1082 C C   . THR A 158 ? 0.2055 0.2265 0.3254 -0.0327 0.0289  -0.0544 136 THR A C   
1083 O O   . THR A 158 ? 0.2520 0.2819 0.3824 -0.0360 0.0230  -0.0682 136 THR A O   
1084 C CB  . THR A 158 ? 0.2007 0.2437 0.3031 -0.0219 0.0262  -0.0456 136 THR A CB  
1085 O OG1 . THR A 158 ? 0.2131 0.2684 0.3157 -0.0194 0.0157  -0.0550 136 THR A OG1 
1086 C CG2 . THR A 158 ? 0.1791 0.2362 0.2866 -0.0202 0.0298  -0.0425 136 THR A CG2 
1087 N N   . LEU A 159 ? 0.2320 0.2325 0.3406 -0.0296 0.0325  -0.0449 137 LEU A N   
1088 C CA  . LEU A 159 ? 0.2406 0.2263 0.3519 -0.0288 0.0308  -0.0496 137 LEU A CA  
1089 C C   . LEU A 159 ? 0.2223 0.2066 0.3145 -0.0190 0.0251  -0.0476 137 LEU A C   
1090 O O   . LEU A 159 ? 0.2102 0.1975 0.3032 -0.0170 0.0205  -0.0589 137 LEU A O   
1091 C CB  . LEU A 159 ? 0.2590 0.2220 0.3786 -0.0326 0.0393  -0.0388 137 LEU A CB  
1092 C CG  . LEU A 159 ? 0.2979 0.2578 0.4424 -0.0442 0.0463  -0.0417 137 LEU A CG  
1093 C CD1 . LEU A 159 ? 0.3435 0.2781 0.4959 -0.0467 0.0544  -0.0281 137 LEU A CD1 
1094 C CD2 . LEU A 159 ? 0.2968 0.2647 0.4595 -0.0496 0.0412  -0.0632 137 LEU A CD2 
1095 N N   . LYS A 160 ? 0.1896 0.1711 0.2649 -0.0133 0.0254  -0.0346 138 LYS A N   
1096 C CA  . LYS A 160 ? 0.1503 0.1309 0.2105 -0.0049 0.0202  -0.0317 138 LYS A CA  
1097 C C   . LYS A 160 ? 0.2328 0.2135 0.2765 -0.0013 0.0206  -0.0195 138 LYS A C   
1098 O O   . LYS A 160 ? 0.2197 0.1974 0.2617 -0.0049 0.0261  -0.0123 138 LYS A O   
1099 C CB  . LYS A 160 ? 0.2084 0.1725 0.2734 -0.0023 0.0211  -0.0300 138 LYS A CB  
1100 C CG  . LYS A 160 ? 0.2407 0.1881 0.3056 -0.0029 0.0257  -0.0145 138 LYS A CG  
1101 C CD  . LYS A 160 ? 0.3339 0.2675 0.4035 0.0028  0.0246  -0.0097 138 LYS A CD  
1102 C CE  . LYS A 160 ? 0.3327 0.2527 0.3987 0.0033  0.0269  0.0093  138 LYS A CE  
1103 N NZ  . LYS A 160 ? 0.5543 0.4621 0.6283 0.0103  0.0246  0.0159  138 LYS A NZ  
1104 N N   . TRP A 161 ? 0.2013 0.1857 0.2329 0.0051  0.0152  -0.0180 139 TRP A N   
1105 C CA  . TRP A 161 ? 0.2149 0.1966 0.2314 0.0083  0.0144  -0.0081 139 TRP A CA  
1106 C C   . TRP A 161 ? 0.2399 0.2080 0.2536 0.0101  0.0141  0.0015  139 TRP A C   
1107 O O   . TRP A 161 ? 0.2406 0.2041 0.2621 0.0131  0.0120  -0.0005 139 TRP A O   
1108 C CB  . TRP A 161 ? 0.1688 0.1596 0.1774 0.0135  0.0085  -0.0101 139 TRP A CB  
1109 C CG  . TRP A 161 ? 0.1672 0.1712 0.1781 0.0135  0.0076  -0.0156 139 TRP A CG  
1110 C CD1 . TRP A 161 ? 0.1999 0.2153 0.2161 0.0146  0.0039  -0.0222 139 TRP A CD1 
1111 C CD2 . TRP A 161 ? 0.2085 0.2167 0.2166 0.0131  0.0101  -0.0141 139 TRP A CD2 
1112 N NE1 . TRP A 161 ? 0.2039 0.2302 0.2225 0.0154  0.0029  -0.0229 139 TRP A NE1 
1113 C CE2 . TRP A 161 ? 0.1470 0.1684 0.1626 0.0148  0.0073  -0.0188 139 TRP A CE2 
1114 C CE3 . TRP A 161 ? 0.1897 0.1927 0.1896 0.0116  0.0150  -0.0097 139 TRP A CE3 
1115 C CZ2 . TRP A 161 ? 0.1873 0.2154 0.2068 0.0160  0.0094  -0.0191 139 TRP A CZ2 
1116 C CZ3 . TRP A 161 ? 0.2168 0.2267 0.2183 0.0121  0.0183  -0.0124 139 TRP A CZ3 
1117 C CH2 . TRP A 161 ? 0.1574 0.1789 0.1706 0.0148  0.0156  -0.0169 139 TRP A CH2 
1118 N N   . GLU A 162 ? 0.2260 0.1892 0.2285 0.0088  0.0163  0.0121  140 GLU A N   
1119 C CA  . GLU A 162 ? 0.2052 0.1586 0.2028 0.0116  0.0135  0.0238  140 GLU A CA  
1120 C C   . GLU A 162 ? 0.2079 0.1667 0.1993 0.0175  0.0054  0.0235  140 GLU A C   
1121 O O   . GLU A 162 ? 0.2578 0.2260 0.2425 0.0181  0.0032  0.0176  140 GLU A O   
1122 C CB  . GLU A 162 ? 0.2035 0.1536 0.1860 0.0083  0.0169  0.0358  140 GLU A CB  
1123 C CG  . GLU A 162 ? 0.2608 0.2052 0.2511 0.0016  0.0266  0.0392  140 GLU A CG  
1124 C CD  . GLU A 162 ? 0.3447 0.2743 0.3517 0.0011  0.0283  0.0467  140 GLU A CD  
1125 O OE1 . GLU A 162 ? 0.3214 0.2453 0.3343 0.0071  0.0222  0.0490  140 GLU A OE1 
1126 O OE2 . GLU A 162 ? 0.3224 0.2457 0.3393 -0.0052 0.0365  0.0501  140 GLU A OE2 
1127 N N   . PRO A 163 ? 0.2519 0.2050 0.2487 0.0219  0.0013  0.0304  141 PRO A N   
1128 C CA  . PRO A 163 ? 0.2390 0.1988 0.2319 0.0266  -0.0063 0.0317  141 PRO A CA  
1129 C C   . PRO A 163 ? 0.2502 0.2156 0.2234 0.0243  -0.0096 0.0355  141 PRO A C   
1130 O O   . PRO A 163 ? 0.2559 0.2179 0.2169 0.0208  -0.0071 0.0421  141 PRO A O   
1131 C CB  . PRO A 163 ? 0.2492 0.2015 0.2530 0.0314  -0.0094 0.0418  141 PRO A CB  
1132 C CG  . PRO A 163 ? 0.3838 0.3250 0.4037 0.0303  -0.0024 0.0388  141 PRO A CG  
1133 C CD  . PRO A 163 ? 0.2901 0.2302 0.3006 0.0229  0.0036  0.0377  141 PRO A CD  
1134 N N   . SER A 164 ? 0.2250 0.1988 0.1953 0.0258  -0.0146 0.0306  142 SER A N   
1135 C CA  . SER A 164 ? 0.2387 0.2174 0.1929 0.0229  -0.0170 0.0290  142 SER A CA  
1136 C C   . SER A 164 ? 0.2772 0.2621 0.2310 0.0247  -0.0262 0.0308  142 SER A C   
1137 O O   . SER A 164 ? 0.2365 0.2241 0.2045 0.0287  -0.0296 0.0324  142 SER A O   
1138 C CB  . SER A 164 ? 0.2583 0.2408 0.2134 0.0212  -0.0124 0.0185  142 SER A CB  
1139 O OG  . SER A 164 ? 0.2375 0.2252 0.2037 0.0241  -0.0151 0.0143  142 SER A OG  
1140 N N   . THR A 165 ? 0.2485 0.2369 0.1873 0.0214  -0.0297 0.0290  143 THR A N   
1141 C CA  . THR A 165 ? 0.2461 0.2418 0.1857 0.0211  -0.0387 0.0277  143 THR A CA  
1142 C C   . THR A 165 ? 0.2882 0.2852 0.2229 0.0175  -0.0367 0.0165  143 THR A C   
1143 O O   . THR A 165 ? 0.2788 0.2738 0.1977 0.0140  -0.0334 0.0121  143 THR A O   
1144 C CB  . THR A 165 ? 0.3344 0.3340 0.2612 0.0201  -0.0475 0.0363  143 THR A CB  
1145 O OG1 . THR A 165 ? 0.3281 0.3256 0.2651 0.0249  -0.0498 0.0484  143 THR A OG1 
1146 C CG2 . THR A 165 ? 0.3565 0.3658 0.2854 0.0181  -0.0578 0.0322  143 THR A CG2 
1147 N N   . GLU A 166 ? 0.2372 0.2372 0.1865 0.0184  -0.0377 0.0122  144 GLU A N   
1148 C CA  . GLU A 166 ? 0.2048 0.2039 0.1552 0.0156  -0.0359 0.0031  144 GLU A CA  
1149 C C   . GLU A 166 ? 0.2484 0.2516 0.1954 0.0114  -0.0444 -0.0005 144 GLU A C   
1150 O O   . GLU A 166 ? 0.2249 0.2350 0.1817 0.0117  -0.0518 0.0040  144 GLU A O   
1151 C CB  . GLU A 166 ? 0.1994 0.2001 0.1673 0.0183  -0.0326 0.0029  144 GLU A CB  
1152 C CG  . GLU A 166 ? 0.2254 0.2242 0.2000 0.0161  -0.0316 -0.0032 144 GLU A CG  
1153 C CD  . GLU A 166 ? 0.2516 0.2523 0.2399 0.0191  -0.0273 -0.0002 144 GLU A CD  
1154 O OE1 . GLU A 166 ? 0.1778 0.1845 0.1726 0.0216  -0.0274 0.0051  144 GLU A OE1 
1155 O OE2 . GLU A 166 ? 0.2210 0.2181 0.2142 0.0191  -0.0240 -0.0030 144 GLU A OE2 
1156 N N   . LYS A 167 ? 0.2271 0.2274 0.1613 0.0071  -0.0433 -0.0097 145 LYS A N   
1157 C CA  . LYS A 167 ? 0.2712 0.2754 0.2015 0.0016  -0.0516 -0.0168 145 LYS A CA  
1158 C C   . LYS A 167 ? 0.2860 0.2865 0.2351 -0.0003 -0.0502 -0.0241 145 LYS A C   
1159 O O   . LYS A 167 ? 0.2171 0.2095 0.1691 0.0002  -0.0423 -0.0309 145 LYS A O   
1160 C CB  . LYS A 167 ? 0.3176 0.3208 0.2230 -0.0026 -0.0505 -0.0252 145 LYS A CB  
1161 C CG  . LYS A 167 ? 0.5127 0.5194 0.3990 -0.0012 -0.0512 -0.0146 145 LYS A CG  
1162 C CD  . LYS A 167 ? 0.6597 0.6669 0.5180 -0.0055 -0.0474 -0.0217 145 LYS A CD  
1163 C CE  . LYS A 167 ? 0.6030 0.6079 0.4495 -0.0030 -0.0390 -0.0111 145 LYS A CE  
1164 N NZ  . LYS A 167 ? 0.8383 0.8367 0.6876 -0.0022 -0.0245 -0.0188 145 LYS A NZ  
1165 N N   . MET A 168 ? 0.2051 0.2120 0.1698 -0.0021 -0.0576 -0.0214 146 MET A N   
1166 C CA  . MET A 168 ? 0.2215 0.2251 0.2071 -0.0046 -0.0559 -0.0252 146 MET A CA  
1167 C C   . MET A 168 ? 0.2076 0.2116 0.1941 -0.0129 -0.0630 -0.0373 146 MET A C   
1168 O O   . MET A 168 ? 0.2557 0.2705 0.2388 -0.0165 -0.0737 -0.0373 146 MET A O   
1169 C CB  . MET A 168 ? 0.2342 0.2456 0.2401 -0.0023 -0.0570 -0.0146 146 MET A CB  
1170 C CG  . MET A 168 ? 0.2482 0.2602 0.2536 0.0050  -0.0504 -0.0054 146 MET A CG  
1171 S SD  . MET A 168 ? 0.2636 0.2670 0.2783 0.0070  -0.0403 -0.0054 146 MET A SD  
1172 C CE  . MET A 168 ? 0.2794 0.2901 0.2980 0.0136  -0.0353 0.0048  146 MET A CE  
1173 N N   . TYR A 169 ? 0.2213 0.2142 0.2149 -0.0157 -0.0576 -0.0478 147 TYR A N   
1174 C CA  . TYR A 169 ? 0.2830 0.2739 0.2783 -0.0244 -0.0633 -0.0630 147 TYR A CA  
1175 C C   . TYR A 169 ? 0.2603 0.2372 0.2788 -0.0260 -0.0561 -0.0686 147 TYR A C   
1176 O O   . TYR A 169 ? 0.2625 0.2326 0.2910 -0.0197 -0.0474 -0.0599 147 TYR A O   
1177 C CB  . TYR A 169 ? 0.3363 0.3272 0.3025 -0.0267 -0.0640 -0.0755 147 TYR A CB  
1178 C CG  . TYR A 169 ? 0.3046 0.2841 0.2625 -0.0218 -0.0510 -0.0804 147 TYR A CG  
1179 C CD1 . TYR A 169 ? 0.2935 0.2742 0.2426 -0.0144 -0.0446 -0.0686 147 TYR A CD1 
1180 C CD2 . TYR A 169 ? 0.3774 0.3454 0.3384 -0.0249 -0.0450 -0.0981 147 TYR A CD2 
1181 C CE1 . TYR A 169 ? 0.2762 0.2493 0.2210 -0.0103 -0.0331 -0.0730 147 TYR A CE1 
1182 C CE2 . TYR A 169 ? 0.3948 0.3543 0.3519 -0.0196 -0.0325 -0.1026 147 TYR A CE2 
1183 C CZ  . TYR A 169 ? 0.3125 0.2759 0.2618 -0.0125 -0.0269 -0.0897 147 TYR A CZ  
1184 O OH  . TYR A 169 ? 0.3248 0.2825 0.2734 -0.0076 -0.0149 -0.0942 147 TYR A OH  
1185 N N   . VAL A 170 ? 0.3011 0.2743 0.3298 -0.0348 -0.0607 -0.0825 148 VAL A N   
1186 C CA  . VAL A 170 ? 0.2966 0.2540 0.3509 -0.0374 -0.0545 -0.0886 148 VAL A CA  
1187 C C   . VAL A 170 ? 0.3778 0.3241 0.4220 -0.0412 -0.0515 -0.1112 148 VAL A C   
1188 O O   . VAL A 170 ? 0.3971 0.3497 0.4286 -0.0493 -0.0599 -0.1265 148 VAL A O   
1189 C CB  . VAL A 170 ? 0.2922 0.2528 0.3739 -0.0459 -0.0609 -0.0870 148 VAL A CB  
1190 C CG1 . VAL A 170 ? 0.2808 0.2218 0.3911 -0.0489 -0.0533 -0.0921 148 VAL A CG1 
1191 C CG2 . VAL A 170 ? 0.2587 0.2328 0.3497 -0.0422 -0.0624 -0.0662 148 VAL A CG2 
1192 N N   . ARG A 171 ? 0.3689 0.3005 0.4189 -0.0351 -0.0399 -0.1139 149 ARG A N   
1193 C CA  . ARG A 171 ? 0.5100 0.4296 0.5560 -0.0378 -0.0344 -0.1371 149 ARG A CA  
1194 C C   . ARG A 171 ? 0.4128 0.3122 0.4925 -0.0357 -0.0256 -0.1383 149 ARG A C   
1195 O O   . ARG A 171 ? 0.3904 0.2852 0.4831 -0.0267 -0.0188 -0.1221 149 ARG A O   
1196 C CB  . ARG A 171 ? 0.5342 0.4572 0.5523 -0.0313 -0.0271 -0.1410 149 ARG A CB  
1197 C CG  . ARG A 171 ? 0.6438 0.5633 0.6441 -0.0353 -0.0228 -0.1616 149 ARG A CG  
1198 C CD  . ARG A 171 ? 0.7026 0.6314 0.6697 -0.0313 -0.0177 -0.1625 149 ARG A CD  
1199 N NE  . ARG A 171 ? 0.6929 0.6163 0.6490 -0.0313 -0.0088 -0.1771 149 ARG A NE  
1200 C CZ  . ARG A 171 ? 0.6056 0.5347 0.5381 -0.0275 -0.0009 -0.1789 149 ARG A CZ  
1201 N NH1 . ARG A 171 ? 0.5725 0.5121 0.4892 -0.0239 -0.0005 -0.1664 149 ARG A NH1 
1202 N NH2 . ARG A 171 ? 0.5767 0.5012 0.5026 -0.0276 0.0073  -0.1933 149 ARG A NH2 
1203 N N   . ASP A 172 ? 0.4708 0.3627 0.5602 -0.0424 -0.0253 -0.1497 150 ASP A N   
1204 C CA  . ASP A 172 ? 0.4670 0.3414 0.5871 -0.0399 -0.0168 -0.1475 150 ASP A CA  
1205 C C   . ASP A 172 ? 0.4511 0.3226 0.6005 -0.0393 -0.0181 -0.1265 150 ASP A C   
1206 O O   . ASP A 172 ? 0.5300 0.3909 0.7010 -0.0322 -0.0104 -0.1141 150 ASP A O   
1207 C CB  . ASP A 172 ? 0.5019 0.3684 0.6216 -0.0291 -0.0048 -0.1484 150 ASP A CB  
1208 C CG  . ASP A 172 ? 0.7509 0.6190 0.8457 -0.0302 -0.0009 -0.1690 150 ASP A CG  
1209 O OD1 . ASP A 172 ? 0.6900 0.5606 0.7729 -0.0222 0.0068  -0.1693 150 ASP A OD1 
1210 O OD2 . ASP A 172 ? 0.6655 0.5338 0.7524 -0.0392 -0.0055 -0.1843 150 ASP A OD2 
1211 N N   . GLY A 173 ? 0.3584 0.2420 0.5081 -0.0462 -0.0281 -0.1204 151 GLY A N   
1212 C CA  . GLY A 173 ? 0.4005 0.2849 0.5758 -0.0470 -0.0290 -0.0996 151 GLY A CA  
1213 C C   . GLY A 173 ? 0.3591 0.2512 0.5274 -0.0363 -0.0255 -0.0768 151 GLY A C   
1214 O O   . GLY A 173 ? 0.3394 0.2338 0.5250 -0.0353 -0.0238 -0.0567 151 GLY A O   
1215 N N   . VAL A 174 ? 0.3100 0.2086 0.4514 -0.0283 -0.0237 -0.0782 152 VAL A N   
1216 C CA  . VAL A 174 ? 0.2673 0.1741 0.4007 -0.0179 -0.0200 -0.0583 152 VAL A CA  
1217 C C   . VAL A 174 ? 0.2530 0.1791 0.3588 -0.0171 -0.0261 -0.0549 152 VAL A C   
1218 O O   . VAL A 174 ? 0.2846 0.2146 0.3677 -0.0180 -0.0284 -0.0677 152 VAL A O   
1219 C CB  . VAL A 174 ? 0.3860 0.2839 0.5178 -0.0085 -0.0117 -0.0611 152 VAL A CB  
1220 C CG1 . VAL A 174 ? 0.3218 0.2317 0.4436 0.0008  -0.0100 -0.0423 152 VAL A CG1 
1221 C CG2 . VAL A 174 ? 0.4075 0.2851 0.5712 -0.0074 -0.0055 -0.0619 152 VAL A CG2 
1222 N N   . LEU A 175 ? 0.2366 0.1749 0.3447 -0.0153 -0.0278 -0.0373 153 LEU A N   
1223 C CA  . LEU A 175 ? 0.2187 0.1732 0.3049 -0.0130 -0.0323 -0.0330 153 LEU A CA  
1224 C C   . LEU A 175 ? 0.2449 0.2000 0.3124 -0.0047 -0.0277 -0.0320 153 LEU A C   
1225 O O   . LEU A 175 ? 0.2206 0.1729 0.2946 0.0017  -0.0218 -0.0229 153 LEU A O   
1226 C CB  . LEU A 175 ? 0.2233 0.1899 0.3189 -0.0122 -0.0330 -0.0162 153 LEU A CB  
1227 C CG  . LEU A 175 ? 0.2190 0.2010 0.2973 -0.0089 -0.0367 -0.0115 153 LEU A CG  
1228 C CD1 . LEU A 175 ? 0.2528 0.2406 0.3194 -0.0139 -0.0458 -0.0223 153 LEU A CD1 
1229 C CD2 . LEU A 175 ? 0.2450 0.2390 0.3359 -0.0083 -0.0352 0.0026  153 LEU A CD2 
1230 N N   . THR A 176 ? 0.2222 0.1822 0.2670 -0.0053 -0.0306 -0.0405 154 THR A N   
1231 C CA  . THR A 176 ? 0.1985 0.1583 0.2268 0.0006  -0.0254 -0.0420 154 THR A CA  
1232 C C   . THR A 176 ? 0.2278 0.1993 0.2368 0.0017  -0.0293 -0.0367 154 THR A C   
1233 O O   . THR A 176 ? 0.2145 0.1922 0.2155 -0.0028 -0.0369 -0.0389 154 THR A O   
1234 C CB  . THR A 176 ? 0.2364 0.1878 0.2559 -0.0016 -0.0219 -0.0595 154 THR A CB  
1235 O OG1 . THR A 176 ? 0.3003 0.2385 0.3415 -0.0028 -0.0181 -0.0665 154 THR A OG1 
1236 C CG2 . THR A 176 ? 0.2699 0.2225 0.2775 0.0046  -0.0143 -0.0595 154 THR A CG2 
1237 N N   . GLY A 177 ? 0.2421 0.2166 0.2452 0.0077  -0.0247 -0.0297 155 GLY A N   
1238 C CA  . GLY A 177 ? 0.2140 0.1957 0.2002 0.0089  -0.0267 -0.0258 155 GLY A CA  
1239 C C   . GLY A 177 ? 0.2299 0.2095 0.2028 0.0109  -0.0202 -0.0302 155 GLY A C   
1240 O O   . GLY A 177 ? 0.2024 0.1801 0.1832 0.0149  -0.0138 -0.0293 155 GLY A O   
1241 N N   . ASP A 178 ? 0.2316 0.2130 0.1850 0.0080  -0.0217 -0.0338 156 ASP A N   
1242 C CA  . ASP A 178 ? 0.2002 0.1811 0.1403 0.0089  -0.0141 -0.0367 156 ASP A CA  
1243 C C   . ASP A 178 ? 0.2421 0.2278 0.1728 0.0100  -0.0154 -0.0259 156 ASP A C   
1244 O O   . ASP A 178 ? 0.2312 0.2205 0.1563 0.0087  -0.0232 -0.0199 156 ASP A O   
1245 C CB  . ASP A 178 ? 0.2303 0.2099 0.1526 0.0041  -0.0127 -0.0489 156 ASP A CB  
1246 C CG  . ASP A 178 ? 0.3168 0.2888 0.2502 0.0036  -0.0078 -0.0630 156 ASP A CG  
1247 O OD1 . ASP A 178 ? 0.2730 0.2406 0.2275 0.0080  -0.0037 -0.0612 156 ASP A OD1 
1248 O OD2 . ASP A 178 ? 0.3113 0.2818 0.2320 -0.0012 -0.0078 -0.0763 156 ASP A OD2 
1249 N N   . ILE A 179 ? 0.2542 0.2401 0.1862 0.0124  -0.0079 -0.0233 157 ILE A N   
1250 C CA  . ILE A 179 ? 0.2182 0.2060 0.1439 0.0128  -0.0075 -0.0140 157 ILE A CA  
1251 C C   . ILE A 179 ? 0.2895 0.2772 0.2076 0.0115  0.0023  -0.0158 157 ILE A C   
1252 O O   . ILE A 179 ? 0.2519 0.2404 0.1801 0.0130  0.0093  -0.0218 157 ILE A O   
1253 C CB  . ILE A 179 ? 0.2105 0.1998 0.1520 0.0164  -0.0090 -0.0074 157 ILE A CB  
1254 C CG1 . ILE A 179 ? 0.2109 0.2020 0.1652 0.0182  -0.0144 -0.0076 157 ILE A CG1 
1255 C CG2 . ILE A 179 ? 0.2867 0.2754 0.2241 0.0165  -0.0115 0.0016  157 ILE A CG2 
1256 C CD1 . ILE A 179 ? 0.2081 0.2031 0.1753 0.0216  -0.0142 -0.0031 157 ILE A CD1 
1257 N N   . GLU A 180 ? 0.2630 0.2509 0.1652 0.0088  0.0032  -0.0093 158 GLU A N   
1258 C CA  . GLU A 180 ? 0.2929 0.2814 0.1906 0.0069  0.0135  -0.0071 158 GLU A CA  
1259 C C   . GLU A 180 ? 0.3084 0.2950 0.2199 0.0082  0.0133  0.0019  158 GLU A C   
1260 O O   . GLU A 180 ? 0.3546 0.3380 0.2616 0.0079  0.0091  0.0120  158 GLU A O   
1261 C CB  . GLU A 180 ? 0.3229 0.3127 0.1948 0.0026  0.0153  -0.0030 158 GLU A CB  
1262 C CG  . GLU A 180 ? 0.4600 0.4528 0.3163 0.0002  0.0178  -0.0157 158 GLU A CG  
1263 C CD  . GLU A 180 ? 0.7861 0.7830 0.6125 -0.0047 0.0205  -0.0119 158 GLU A CD  
1264 O OE1 . GLU A 180 ? 0.8181 0.8186 0.6304 -0.0073 0.0281  -0.0240 158 GLU A OE1 
1265 O OE2 . GLU A 180 ? 0.7146 0.7114 0.5316 -0.0055 0.0153  0.0034  158 GLU A OE2 
1266 N N   . MET A 181 ? 0.2300 0.2189 0.1597 0.0099  0.0173  -0.0024 159 MET A N   
1267 C CA  . MET A 181 ? 0.2549 0.2430 0.1994 0.0106  0.0167  0.0017  159 MET A CA  
1268 C C   . MET A 181 ? 0.3002 0.2882 0.2475 0.0065  0.0260  0.0045  159 MET A C   
1269 O O   . MET A 181 ? 0.2268 0.2185 0.1691 0.0040  0.0343  0.0016  159 MET A O   
1270 C CB  . MET A 181 ? 0.2299 0.2237 0.1912 0.0139  0.0148  -0.0048 159 MET A CB  
1271 C CG  . MET A 181 ? 0.2849 0.2792 0.2488 0.0175  0.0065  -0.0051 159 MET A CG  
1272 S SD  . MET A 181 ? 0.2682 0.2595 0.2340 0.0191  -0.0002 0.0008  159 MET A SD  
1273 C CE  . MET A 181 ? 0.2442 0.2425 0.2255 0.0207  0.0006  -0.0037 159 MET A CE  
1274 N N   . ALA A 182 ? 0.2601 0.2441 0.2182 0.0054  0.0255  0.0091  160 ALA A N   
1275 C CA  . ALA A 182 ? 0.2461 0.2297 0.2125 0.0003  0.0344  0.0115  160 ALA A CA  
1276 C C   . ALA A 182 ? 0.2701 0.2533 0.2574 -0.0003 0.0326  0.0078  160 ALA A C   
1277 O O   . ALA A 182 ? 0.2125 0.1894 0.2028 0.0021  0.0266  0.0096  160 ALA A O   
1278 C CB  . ALA A 182 ? 0.3005 0.2758 0.2535 -0.0031 0.0382  0.0243  160 ALA A CB  
1279 N N   . LEU A 183 ? 0.2323 0.2235 0.2348 -0.0036 0.0377  0.0016  161 LEU A N   
1280 C CA  . LEU A 183 ? 0.2220 0.2143 0.2444 -0.0066 0.0368  -0.0035 161 LEU A CA  
1281 C C   . LEU A 183 ? 0.2720 0.2549 0.3021 -0.0136 0.0445  0.0031  161 LEU A C   
1282 O O   . LEU A 183 ? 0.2599 0.2457 0.2900 -0.0182 0.0537  0.0072  161 LEU A O   
1283 C CB  . LEU A 183 ? 0.2198 0.2283 0.2575 -0.0074 0.0367  -0.0133 161 LEU A CB  
1284 C CG  . LEU A 183 ? 0.2429 0.2606 0.2807 -0.0013 0.0274  -0.0194 161 LEU A CG  
1285 C CD1 . LEU A 183 ? 0.2456 0.2801 0.2964 -0.0006 0.0277  -0.0248 161 LEU A CD1 
1286 C CD2 . LEU A 183 ? 0.2092 0.2253 0.2524 -0.0016 0.0213  -0.0243 161 LEU A CD2 
1287 N N   . LEU A 184 ? 0.1968 0.1686 0.2357 -0.0144 0.0420  0.0039  162 LEU A N   
1288 C CA  . LEU A 184 ? 0.2367 0.1983 0.2901 -0.0216 0.0493  0.0090  162 LEU A CA  
1289 C C   . LEU A 184 ? 0.2994 0.2719 0.3756 -0.0284 0.0522  -0.0028 162 LEU A C   
1290 O O   . LEU A 184 ? 0.2685 0.2509 0.3528 -0.0269 0.0452  -0.0159 162 LEU A O   
1291 C CB  . LEU A 184 ? 0.2252 0.1703 0.2852 -0.0194 0.0457  0.0118  162 LEU A CB  
1292 C CG  . LEU A 184 ? 0.2927 0.2233 0.3721 -0.0270 0.0535  0.0174  162 LEU A CG  
1293 C CD1 . LEU A 184 ? 0.4672 0.3918 0.5348 -0.0300 0.0615  0.0366  162 LEU A CD1 
1294 C CD2 . LEU A 184 ? 0.3863 0.3002 0.4780 -0.0238 0.0502  0.0167  162 LEU A CD2 
1295 N N   . LEU A 185 ? 0.2631 0.2362 0.3496 -0.0363 0.0624  0.0022  163 LEU A N   
1296 C CA  . LEU A 185 ? 0.3232 0.3086 0.4354 -0.0441 0.0655  -0.0082 163 LEU A CA  
1297 C C   . LEU A 185 ? 0.3676 0.3386 0.5018 -0.0530 0.0704  -0.0071 163 LEU A C   
1298 O O   . LEU A 185 ? 0.3176 0.2691 0.4471 -0.0535 0.0748  0.0063  163 LEU A O   
1299 C CB  . LEU A 185 ? 0.2539 0.2536 0.3683 -0.0476 0.0752  -0.0049 163 LEU A CB  
1300 C CG  . LEU A 185 ? 0.2730 0.2850 0.3691 -0.0394 0.0733  -0.0061 163 LEU A CG  
1301 C CD1 . LEU A 185 ? 0.2704 0.2951 0.3722 -0.0432 0.0858  -0.0039 163 LEU A CD1 
1302 C CD2 . LEU A 185 ? 0.2419 0.2670 0.3435 -0.0336 0.0612  -0.0187 163 LEU A CD2 
1303 N N   . GLU A 186 ? 0.4340 0.2985 0.4805 -0.2039 0.0290  -0.0441 164 GLU A N   
1304 C CA  . GLU A 186 ? 0.4817 0.3181 0.5370 -0.2205 0.0300  -0.0426 164 GLU A CA  
1305 C C   . GLU A 186 ? 0.6106 0.4451 0.6692 -0.2310 0.0365  -0.0147 164 GLU A C   
1306 O O   . GLU A 186 ? 0.5693 0.4480 0.6273 -0.2343 0.0405  -0.0038 164 GLU A O   
1307 C CB  . GLU A 186 ? 0.6127 0.4829 0.6758 -0.2389 0.0243  -0.0602 164 GLU A CB  
1308 C CG  . GLU A 186 ? 0.7107 0.5729 0.7640 -0.2341 0.0187  -0.0867 164 GLU A CG  
1309 C CD  . GLU A 186 ? 0.7810 0.6913 0.8363 -0.2510 0.0100  -0.0996 164 GLU A CD  
1310 O OE1 . GLU A 186 ? 0.8093 0.7471 0.8799 -0.2689 0.0087  -0.0906 164 GLU A OE1 
1311 O OE2 . GLU A 186 ? 0.6757 0.5982 0.7173 -0.2466 0.0043  -0.1168 164 GLU A OE2 
1312 N N   . GLY A 187 ? 0.6397 0.4253 0.7033 -0.2353 0.0378  -0.0024 165 GLY A N   
1313 C CA  . GLY A 187 ? 0.5966 0.3755 0.6588 -0.2427 0.0435  0.0285  165 GLY A CA  
1314 C C   . GLY A 187 ? 0.6605 0.4177 0.7065 -0.2236 0.0431  0.0511  165 GLY A C   
1315 O O   . GLY A 187 ? 0.6642 0.4166 0.7029 -0.2289 0.0469  0.0791  165 GLY A O   
1316 N N   . ASN A 188 ? 0.6050 0.3525 0.6434 -0.2020 0.0386  0.0402  166 ASN A N   
1317 C CA  . ASN A 188 ? 0.6509 0.3776 0.6761 -0.1804 0.0341  0.0597  166 ASN A CA  
1318 C C   . ASN A 188 ? 0.6738 0.4489 0.6784 -0.1738 0.0345  0.0743  166 ASN A C   
1319 O O   . ASN A 188 ? 0.6870 0.4541 0.6786 -0.1583 0.0284  0.0938  166 ASN A O   
1320 C CB  . ASN A 188 ? 0.7216 0.4012 0.7586 -0.1760 0.0323  0.0854  166 ASN A CB  
1321 C CG  . ASN A 188 ? 1.0179 0.6489 1.0569 -0.1555 0.0275  0.0729  166 ASN A CG  
1322 O OD1 . ASN A 188 ? 0.8569 0.4872 0.9125 -0.1527 0.0232  0.0436  166 ASN A OD1 
1323 N ND2 . ASN A 188 ? 1.0548 0.6638 1.0933 -0.1355 0.0231  0.0968  166 ASN A ND2 
1324 N N   . ALA A 189 ? 0.6144 0.4406 0.6178 -0.1853 0.0417  0.0644  167 ALA A N   
1325 C CA  . ALA A 189 ? 0.5095 0.3806 0.4977 -0.1749 0.0451  0.0683  167 ALA A CA  
1326 C C   . ALA A 189 ? 0.3991 0.2798 0.3871 -0.1456 0.0377  0.0522  167 ALA A C   
1327 O O   . ALA A 189 ? 0.3911 0.2543 0.3910 -0.1360 0.0319  0.0357  167 ALA A O   
1328 C CB  . ALA A 189 ? 0.4653 0.3891 0.4639 -0.1910 0.0566  0.0591  167 ALA A CB  
1329 N N   . HIS A 190 ? 0.3778 0.2859 0.3506 -0.1337 0.0395  0.0558  168 HIS A N   
1330 C CA  . HIS A 190 ? 0.3397 0.2611 0.3135 -0.1093 0.0341  0.0409  168 HIS A CA  
1331 C C   . HIS A 190 ? 0.3088 0.2782 0.2877 -0.1064 0.0426  0.0285  168 HIS A C   
1332 O O   . HIS A 190 ? 0.3556 0.3502 0.3318 -0.1196 0.0545  0.0331  168 HIS A O   
1333 C CB  . HIS A 190 ? 0.4066 0.3106 0.3626 -0.0943 0.0260  0.0542  168 HIS A CB  
1334 C CG  . HIS A 190 ? 0.4781 0.3384 0.4437 -0.0861 0.0160  0.0612  168 HIS A CG  
1335 N ND1 . HIS A 190 ? 0.4329 0.2581 0.3990 -0.0975 0.0135  0.0832  168 HIS A ND1 
1336 C CD2 . HIS A 190 ? 0.4092 0.2550 0.3886 -0.0678 0.0101  0.0484  168 HIS A CD2 
1337 C CE1 . HIS A 190 ? 0.5105 0.2996 0.4947 -0.0838 0.0064  0.0829  168 HIS A CE1 
1338 N NE2 . HIS A 190 ? 0.4170 0.2200 0.4089 -0.0661 0.0054  0.0604  168 HIS A NE2 
1339 N N   . TYR A 191 ? 0.2762 0.2579 0.2656 -0.0891 0.0375  0.0131  169 TYR A N   
1340 C CA  . TYR A 191 ? 0.2851 0.3079 0.2900 -0.0823 0.0429  0.0016  169 TYR A CA  
1341 C C   . TYR A 191 ? 0.2611 0.2823 0.2579 -0.0609 0.0388  -0.0036 169 TYR A C   
1342 O O   . TYR A 191 ? 0.2527 0.2607 0.2513 -0.0501 0.0288  -0.0089 169 TYR A O   
1343 C CB  . TYR A 191 ? 0.2700 0.3098 0.2995 -0.0873 0.0375  -0.0085 169 TYR A CB  
1344 C CG  . TYR A 191 ? 0.2529 0.3347 0.3071 -0.0775 0.0378  -0.0159 169 TYR A CG  
1345 C CD1 . TYR A 191 ? 0.2269 0.3432 0.2988 -0.0779 0.0510  -0.0153 169 TYR A CD1 
1346 C CD2 . TYR A 191 ? 0.2046 0.2927 0.2671 -0.0690 0.0256  -0.0224 169 TYR A CD2 
1347 C CE1 . TYR A 191 ? 0.2622 0.4157 0.3667 -0.0659 0.0509  -0.0199 169 TYR A CE1 
1348 C CE2 . TYR A 191 ? 0.2198 0.3453 0.3086 -0.0598 0.0228  -0.0233 169 TYR A CE2 
1349 C CZ  . TYR A 191 ? 0.2128 0.3697 0.3262 -0.0565 0.0349  -0.0214 169 TYR A CZ  
1350 O OH  . TYR A 191 ? 0.1515 0.3443 0.3004 -0.0442 0.0314  -0.0201 169 TYR A OH  
1351 N N   . ARG A 192 ? 0.2349 0.2693 0.2213 -0.0574 0.0478  -0.0035 170 ARG A N   
1352 C CA  . ARG A 192 ? 0.2458 0.2726 0.2183 -0.0426 0.0443  -0.0071 170 ARG A CA  
1353 C C   . ARG A 192 ? 0.2253 0.2687 0.2194 -0.0271 0.0437  -0.0195 170 ARG A C   
1354 O O   . ARG A 192 ? 0.2079 0.2776 0.2271 -0.0264 0.0507  -0.0248 170 ARG A O   
1355 C CB  . ARG A 192 ? 0.2624 0.2965 0.2111 -0.0495 0.0553  -0.0055 170 ARG A CB  
1356 C CG  . ARG A 192 ? 0.4691 0.5088 0.4130 -0.0368 0.0583  -0.0184 170 ARG A CG  
1357 C CD  . ARG A 192 ? 0.6032 0.6497 0.5168 -0.0476 0.0699  -0.0216 170 ARG A CD  
1358 N NE  . ARG A 192 ? 0.5042 0.5483 0.4099 -0.0385 0.0702  -0.0351 170 ARG A NE  
1359 C CZ  . ARG A 192 ? 0.6103 0.6574 0.4835 -0.0492 0.0773  -0.0415 170 ARG A CZ  
1360 N NH1 . ARG A 192 ? 0.5573 0.6128 0.4003 -0.0693 0.0849  -0.0337 170 ARG A NH1 
1361 N NH2 . ARG A 192 ? 0.5616 0.6042 0.4307 -0.0426 0.0774  -0.0564 170 ARG A NH2 
1362 N N   . CYS A 193 ? 0.1825 0.2118 0.1696 -0.0148 0.0350  -0.0216 171 CYS A N   
1363 C CA  . CYS A 193 ? 0.2002 0.2400 0.2045 -0.0013 0.0337  -0.0294 171 CYS A CA  
1364 C C   . CYS A 193 ? 0.2404 0.2663 0.2285 0.0063  0.0313  -0.0324 171 CYS A C   
1365 O O   . CYS A 193 ? 0.3205 0.3295 0.2937 0.0062  0.0223  -0.0270 171 CYS A O   
1366 C CB  . CYS A 193 ? 0.1956 0.2366 0.2130 0.0014  0.0224  -0.0284 171 CYS A CB  
1367 S SG  . CYS A 193 ? 0.1956 0.2499 0.2332 0.0156  0.0179  -0.0302 171 CYS A SG  
1368 N N   . ASP A 194 ? 0.2018 0.2348 0.1963 0.0124  0.0399  -0.0414 172 ASP A N   
1369 C CA  . ASP A 194 ? 0.2564 0.2766 0.2386 0.0173  0.0372  -0.0464 172 ASP A CA  
1370 C C   . ASP A 194 ? 0.2451 0.2626 0.2460 0.0286  0.0296  -0.0458 172 ASP A C   
1371 O O   . ASP A 194 ? 0.1940 0.2223 0.2209 0.0354  0.0323  -0.0459 172 ASP A O   
1372 C CB  . ASP A 194 ? 0.2847 0.3083 0.2606 0.0146  0.0524  -0.0601 172 ASP A CB  
1373 C CG  . ASP A 194 ? 0.4266 0.4580 0.3796 -0.0001 0.0620  -0.0602 172 ASP A CG  
1374 O OD1 . ASP A 194 ? 0.3985 0.4218 0.3246 -0.0093 0.0520  -0.0491 172 ASP A OD1 
1375 O OD2 . ASP A 194 ? 0.4454 0.4923 0.4094 -0.0027 0.0797  -0.0697 172 ASP A OD2 
1376 N N   . PHE A 195 ? 0.2115 0.2172 0.2012 0.0297  0.0197  -0.0428 173 PHE A N   
1377 C CA  . PHE A 195 ? 0.2066 0.2093 0.2073 0.0366  0.0135  -0.0410 173 PHE A CA  
1378 C C   . PHE A 195 ? 0.2212 0.2141 0.2177 0.0372  0.0162  -0.0481 173 PHE A C   
1379 O O   . PHE A 195 ? 0.1993 0.1876 0.1766 0.0307  0.0151  -0.0517 173 PHE A O   
1380 C CB  . PHE A 195 ? 0.1975 0.1966 0.1912 0.0357  0.0040  -0.0357 173 PHE A CB  
1381 C CG  . PHE A 195 ? 0.2017 0.2070 0.2006 0.0338  0.0010  -0.0325 173 PHE A CG  
1382 C CD1 . PHE A 195 ? 0.1970 0.2110 0.2022 0.0297  0.0039  -0.0318 173 PHE A CD1 
1383 C CD2 . PHE A 195 ? 0.1926 0.1969 0.1893 0.0335  -0.0036 -0.0325 173 PHE A CD2 
1384 C CE1 . PHE A 195 ? 0.2435 0.2633 0.2511 0.0238  0.0000  -0.0311 173 PHE A CE1 
1385 C CE2 . PHE A 195 ? 0.2087 0.2176 0.2052 0.0281  -0.0052 -0.0342 173 PHE A CE2 
1386 C CZ  . PHE A 195 ? 0.2288 0.2447 0.2300 0.0224  -0.0046 -0.0335 173 PHE A CZ  
1387 N N   . ARG A 196 ? 0.2575 0.2467 0.2721 0.0435  0.0179  -0.0483 174 ARG A N   
1388 C CA  . ARG A 196 ? 0.2682 0.2439 0.2804 0.0419  0.0175  -0.0530 174 ARG A CA  
1389 C C   . ARG A 196 ? 0.2037 0.1783 0.2303 0.0460  0.0107  -0.0413 174 ARG A C   
1390 O O   . ARG A 196 ? 0.1822 0.1610 0.2290 0.0528  0.0105  -0.0331 174 ARG A O   
1391 C CB  . ARG A 196 ? 0.2822 0.2464 0.3009 0.0421  0.0305  -0.0677 174 ARG A CB  
1392 C CG  . ARG A 196 ? 0.2913 0.2374 0.3111 0.0384  0.0298  -0.0728 174 ARG A CG  
1393 C CD  . ARG A 196 ? 0.3649 0.2974 0.3804 0.0330  0.0422  -0.0902 174 ARG A CD  
1394 N NE  . ARG A 196 ? 0.2619 0.2011 0.2444 0.0192  0.0425  -0.1011 174 ARG A NE  
1395 C CZ  . ARG A 196 ? 0.3322 0.2665 0.3008 0.0100  0.0510  -0.1150 174 ARG A CZ  
1396 N NH1 . ARG A 196 ? 0.3997 0.3201 0.3870 0.0143  0.0617  -0.1231 174 ARG A NH1 
1397 N NH2 . ARG A 196 ? 0.3777 0.3226 0.3138 -0.0043 0.0482  -0.1202 174 ARG A NH2 
1398 N N   . THR A 197 ? 0.2416 0.2148 0.2588 0.0408  0.0046  -0.0386 175 THR A N   
1399 C CA  . THR A 197 ? 0.2345 0.2085 0.2590 0.0403  -0.0003 -0.0272 175 THR A CA  
1400 C C   . THR A 197 ? 0.2591 0.2188 0.2858 0.0346  0.0011  -0.0303 175 THR A C   
1401 O O   . THR A 197 ? 0.2256 0.1847 0.2418 0.0279  0.0010  -0.0400 175 THR A O   
1402 C CB  . THR A 197 ? 0.2404 0.2288 0.2542 0.0368  -0.0052 -0.0233 175 THR A CB  
1403 O OG1 . THR A 197 ? 0.2318 0.2282 0.2413 0.0391  -0.0056 -0.0249 175 THR A OG1 
1404 C CG2 . THR A 197 ? 0.1824 0.1770 0.1984 0.0333  -0.0083 -0.0111 175 THR A CG2 
1405 N N   . THR A 198 ? 0.1917 0.1409 0.2331 0.0354  0.0009  -0.0200 176 THR A N   
1406 C CA  . THR A 198 ? 0.2517 0.1865 0.2960 0.0265  0.0017  -0.0201 176 THR A CA  
1407 C C   . THR A 198 ? 0.2469 0.1939 0.2882 0.0203  -0.0036 -0.0035 176 THR A C   
1408 O O   . THR A 198 ? 0.2315 0.1895 0.2731 0.0238  -0.0077 0.0106  176 THR A O   
1409 C CB  . THR A 198 ? 0.2885 0.1950 0.3537 0.0302  0.0078  -0.0213 176 THR A CB  
1410 O OG1 . THR A 198 ? 0.2401 0.1476 0.3249 0.0413  0.0047  -0.0031 176 THR A OG1 
1411 C CG2 . THR A 198 ? 0.3027 0.1980 0.3664 0.0322  0.0179  -0.0450 176 THR A CG2 
1412 N N   . TYR A 199 ? 0.2605 0.2099 0.2980 0.0087  -0.0033 -0.0058 177 TYR A N   
1413 C CA  . TYR A 199 ? 0.2426 0.2097 0.2752 0.0000  -0.0043 0.0057  177 TYR A CA  
1414 C C   . TYR A 199 ? 0.2392 0.1915 0.2805 -0.0128 -0.0029 0.0135  177 TYR A C   
1415 O O   . TYR A 199 ? 0.2366 0.1761 0.2834 -0.0192 -0.0013 0.0014  177 TYR A O   
1416 C CB  . TYR A 199 ? 0.2066 0.1986 0.2333 -0.0025 -0.0033 -0.0050 177 TYR A CB  
1417 C CG  . TYR A 199 ? 0.1812 0.1831 0.2013 0.0083  -0.0044 -0.0128 177 TYR A CG  
1418 C CD1 . TYR A 199 ? 0.1578 0.1734 0.1703 0.0107  -0.0029 -0.0095 177 TYR A CD1 
1419 C CD2 . TYR A 199 ? 0.2189 0.2157 0.2379 0.0130  -0.0066 -0.0235 177 TYR A CD2 
1420 C CE1 . TYR A 199 ? 0.1696 0.1897 0.1780 0.0184  -0.0032 -0.0173 177 TYR A CE1 
1421 C CE2 . TYR A 199 ? 0.2118 0.2150 0.2254 0.0210  -0.0076 -0.0275 177 TYR A CE2 
1422 C CZ  . TYR A 199 ? 0.1474 0.1602 0.1581 0.0240  -0.0056 -0.0246 177 TYR A CZ  
1423 O OH  . TYR A 199 ? 0.2125 0.2269 0.2198 0.0300  -0.0059 -0.0291 177 TYR A OH  
1424 N N   . LYS A 200 ? 0.2379 0.1932 0.2778 -0.0197 -0.0037 0.0340  178 LYS A N   
1425 C CA  . LYS A 200 ? 0.2492 0.1869 0.2982 -0.0339 -0.0022 0.0460  178 LYS A CA  
1426 C C   . LYS A 200 ? 0.2888 0.2493 0.3263 -0.0486 -0.0005 0.0637  178 LYS A C   
1427 O O   . LYS A 200 ? 0.2740 0.2433 0.3003 -0.0480 -0.0043 0.0822  178 LYS A O   
1428 C CB  . LYS A 200 ? 0.3472 0.2485 0.4134 -0.0269 -0.0049 0.0595  178 LYS A CB  
1429 C CG  . LYS A 200 ? 0.4287 0.3002 0.5088 -0.0416 -0.0028 0.0708  178 LYS A CG  
1430 C CD  . LYS A 200 ? 0.6325 0.5039 0.7124 -0.0581 0.0026  0.0507  178 LYS A CD  
1431 C CE  . LYS A 200 ? 0.6918 0.5415 0.7782 -0.0526 0.0058  0.0221  178 LYS A CE  
1432 N NZ  . LYS A 200 ? 0.4965 0.3580 0.5778 -0.0693 0.0067  0.0006  178 LYS A NZ  
1433 N N   . ALA A 201 ? 0.2628 0.2354 0.3032 -0.0642 0.0052  0.0587  179 ALA A N   
1434 C CA  . ALA A 201 ? 0.2791 0.2735 0.3101 -0.0820 0.0107  0.0748  179 ALA A CA  
1435 C C   . ALA A 201 ? 0.3180 0.2858 0.3494 -0.0920 0.0065  0.1049  179 ALA A C   
1436 O O   . ALA A 201 ? 0.3686 0.2972 0.4181 -0.0894 0.0027  0.1089  179 ALA A O   
1437 C CB  . ALA A 201 ? 0.2771 0.2913 0.3200 -0.0972 0.0183  0.0632  179 ALA A CB  
1438 N N   . LYS A 202 ? 0.3360 0.3248 0.3475 -0.1046 0.0079  0.1264  180 LYS A N   
1439 C CA  . LYS A 202 ? 0.3798 0.3470 0.3899 -0.1170 0.0019  0.1623  180 LYS A CA  
1440 C C   . LYS A 202 ? 0.4079 0.3620 0.4302 -0.1393 0.0089  0.1696  180 LYS A C   
1441 O O   . LYS A 202 ? 0.4524 0.3674 0.4888 -0.1449 0.0036  0.1924  180 LYS A O   
1442 C CB  . LYS A 202 ? 0.4130 0.4120 0.3905 -0.1280 0.0000  0.1842  180 LYS A CB  
1443 C CG  . LYS A 202 ? 0.3819 0.3878 0.3498 -0.1099 -0.0112 0.1848  180 LYS A CG  
1444 C CD  . LYS A 202 ? 0.6036 0.6424 0.5352 -0.1241 -0.0151 0.2033  180 LYS A CD  
1445 C CE  . LYS A 202 ? 0.4507 0.5152 0.3647 -0.1143 -0.0165 0.1838  180 LYS A CE  
1446 N NZ  . LYS A 202 ? 0.6194 0.6747 0.5416 -0.1000 -0.0361 0.2013  180 LYS A NZ  
1447 N N   . GLU A 203 ? 0.3930 0.3798 0.4139 -0.1524 0.0210  0.1512  181 GLU A N   
1448 C CA  . GLU A 203 ? 0.4461 0.4291 0.4804 -0.1770 0.0283  0.1564  181 GLU A CA  
1449 C C   . GLU A 203 ? 0.4623 0.4147 0.5241 -0.1731 0.0255  0.1348  181 GLU A C   
1450 O O   . GLU A 203 ? 0.4149 0.3753 0.4825 -0.1562 0.0234  0.1071  181 GLU A O   
1451 C CB  . GLU A 203 ? 0.4287 0.4670 0.4571 -0.1919 0.0433  0.1440  181 GLU A CB  
1452 C CG  . GLU A 203 ? 0.5130 0.5560 0.5558 -0.2138 0.0518  0.1461  181 GLU A CG  
1453 C CD  . GLU A 203 ? 0.7051 0.8048 0.7457 -0.2220 0.0679  0.1333  181 GLU A CD  
1454 O OE1 . GLU A 203 ? 0.7195 0.8317 0.7412 -0.2336 0.0756  0.1477  181 GLU A OE1 
1455 O OE2 . GLU A 203 ? 0.5697 0.7012 0.6298 -0.2153 0.0727  0.1082  181 GLU A OE2 
1456 N N   . LYS A 204 ? 0.4667 0.3832 0.5435 -0.1912 0.0255  0.1476  182 LYS A N   
1457 C CA  . LYS A 204 ? 0.4933 0.3792 0.5924 -0.1930 0.0240  0.1240  182 LYS A CA  
1458 C C   . LYS A 204 ? 0.5077 0.4376 0.6148 -0.2061 0.0290  0.0994  182 LYS A C   
1459 O O   . LYS A 204 ? 0.5181 0.4895 0.6244 -0.2224 0.0372  0.1066  182 LYS A O   
1460 C CB  . LYS A 204 ? 0.5907 0.4272 0.6995 -0.2027 0.0267  0.1343  182 LYS A CB  
1461 C CG  . LYS A 204 ? 0.7015 0.4840 0.8155 -0.1809 0.0210  0.1393  182 LYS A CG  
1462 C CD  . LYS A 204 ? 0.8395 0.6116 0.9625 -0.1632 0.0175  0.1101  182 LYS A CD  
1463 C CE  . LYS A 204 ? 0.9621 0.7063 1.0891 -0.1340 0.0126  0.1183  182 LYS A CE  
1464 N NZ  . LYS A 204 ? 1.0429 0.7603 1.1799 -0.1192 0.0150  0.0856  182 LYS A NZ  
1465 N N   . GLY A 205 ? 0.5538 0.4788 0.6698 -0.1983 0.0240  0.0702  183 GLY A N   
1466 C CA  . GLY A 205 ? 0.5334 0.4965 0.6634 -0.2136 0.0242  0.0505  183 GLY A CA  
1467 C C   . GLY A 205 ? 0.4913 0.5133 0.6218 -0.1994 0.0244  0.0390  183 GLY A C   
1468 O O   . GLY A 205 ? 0.3992 0.4620 0.5489 -0.2117 0.0240  0.0283  183 GLY A O   
1469 N N   . VAL A 206 ? 0.3786 0.4070 0.4929 -0.1745 0.0247  0.0416  184 VAL A N   
1470 C CA  . VAL A 206 ? 0.3269 0.4006 0.4449 -0.1580 0.0249  0.0279  184 VAL A CA  
1471 C C   . VAL A 206 ? 0.3503 0.4234 0.4764 -0.1514 0.0130  0.0072  184 VAL A C   
1472 O O   . VAL A 206 ? 0.3182 0.3525 0.4317 -0.1430 0.0066  0.0001  184 VAL A O   
1473 C CB  . VAL A 206 ? 0.3501 0.4221 0.4469 -0.1353 0.0270  0.0327  184 VAL A CB  
1474 C CG1 . VAL A 206 ? 0.2791 0.3903 0.3836 -0.1184 0.0283  0.0174  184 VAL A CG1 
1475 C CG2 . VAL A 206 ? 0.2934 0.3694 0.3747 -0.1458 0.0366  0.0546  184 VAL A CG2 
1476 N N   . LYS A 207 ? 0.2745 0.3937 0.4228 -0.1554 0.0103  -0.0018 185 LYS A N   
1477 C CA  . LYS A 207 ? 0.3002 0.4262 0.4548 -0.1550 -0.0041 -0.0172 185 LYS A CA  
1478 C C   . LYS A 207 ? 0.2920 0.4072 0.4292 -0.1284 -0.0104 -0.0237 185 LYS A C   
1479 O O   . LYS A 207 ? 0.2455 0.3800 0.3847 -0.1092 -0.0061 -0.0205 185 LYS A O   
1480 C CB  . LYS A 207 ? 0.3025 0.4880 0.4916 -0.1637 -0.0080 -0.0196 185 LYS A CB  
1481 C CG  . LYS A 207 ? 0.4351 0.6324 0.6304 -0.1730 -0.0268 -0.0312 185 LYS A CG  
1482 C CD  . LYS A 207 ? 0.4432 0.7007 0.6772 -0.1731 -0.0339 -0.0286 185 LYS A CD  
1483 C CE  . LYS A 207 ? 0.4929 0.7525 0.7244 -0.1836 -0.0540 -0.0358 185 LYS A CE  
1484 N NZ  . LYS A 207 ? 0.4339 0.7473 0.7038 -0.1769 -0.0644 -0.0299 185 LYS A NZ  
1485 N N   . LEU A 208 ? 0.2707 0.3547 0.3907 -0.1295 -0.0189 -0.0347 186 LEU A N   
1486 C CA  . LEU A 208 ? 0.2784 0.3540 0.3810 -0.1084 -0.0243 -0.0405 186 LEU A CA  
1487 C C   . LEU A 208 ? 0.2218 0.3403 0.3373 -0.1034 -0.0368 -0.0426 186 LEU A C   
1488 O O   . LEU A 208 ? 0.2238 0.3717 0.3568 -0.1203 -0.0461 -0.0446 186 LEU A O   
1489 C CB  . LEU A 208 ? 0.3033 0.3353 0.3837 -0.1132 -0.0258 -0.0537 186 LEU A CB  
1490 C CG  . LEU A 208 ? 0.4137 0.4003 0.4891 -0.1110 -0.0144 -0.0483 186 LEU A CG  
1491 C CD1 . LEU A 208 ? 0.4794 0.4233 0.5463 -0.1228 -0.0122 -0.0649 186 LEU A CD1 
1492 C CD2 . LEU A 208 ? 0.3525 0.3321 0.4181 -0.0860 -0.0107 -0.0409 186 LEU A CD2 
1493 N N   . PRO A 209 ? 0.1951 0.3179 0.3046 -0.0813 -0.0387 -0.0401 187 PRO A N   
1494 C CA  . PRO A 209 ? 0.1803 0.3401 0.3060 -0.0739 -0.0520 -0.0369 187 PRO A CA  
1495 C C   . PRO A 209 ? 0.2876 0.4407 0.3907 -0.0836 -0.0675 -0.0436 187 PRO A C   
1496 O O   . PRO A 209 ? 0.2366 0.3532 0.3099 -0.0910 -0.0637 -0.0546 187 PRO A O   
1497 C CB  . PRO A 209 ? 0.1590 0.3142 0.2834 -0.0482 -0.0456 -0.0319 187 PRO A CB  
1498 C CG  . PRO A 209 ? 0.1823 0.2925 0.2745 -0.0449 -0.0364 -0.0362 187 PRO A CG  
1499 C CD  . PRO A 209 ? 0.2077 0.3001 0.2969 -0.0633 -0.0303 -0.0387 187 PRO A CD  
1500 N N   . GLY A 210 ? 0.1976 0.3882 0.3161 -0.0833 -0.0845 -0.0362 188 GLY A N   
1501 C CA  . GLY A 210 ? 0.2478 0.4369 0.3385 -0.0909 -0.1004 -0.0383 188 GLY A CA  
1502 C C   . GLY A 210 ? 0.2077 0.3744 0.2774 -0.0703 -0.0967 -0.0341 188 GLY A C   
1503 O O   . GLY A 210 ? 0.2197 0.3760 0.3006 -0.0499 -0.0845 -0.0295 188 GLY A O   
1504 N N   . ALA A 211 ? 0.2293 0.3896 0.2656 -0.0788 -0.1067 -0.0366 189 ALA A N   
1505 C CA  . ALA A 211 ? 0.2321 0.3736 0.2487 -0.0625 -0.1031 -0.0312 189 ALA A CA  
1506 C C   . ALA A 211 ? 0.2054 0.3696 0.2539 -0.0418 -0.1114 -0.0100 189 ALA A C   
1507 O O   . ALA A 211 ? 0.2094 0.4106 0.2851 -0.0438 -0.1287 0.0035  189 ALA A O   
1508 C CB  . ALA A 211 ? 0.2575 0.3955 0.2309 -0.0798 -0.1122 -0.0365 189 ALA A CB  
1509 N N   . HIS A 212 ? 0.2611 0.2871 0.2004 -0.0599 -0.0475 -0.0599 190 HIS A N   
1510 C CA  . HIS A 212 ? 0.2663 0.2974 0.2106 -0.0531 -0.0562 -0.0387 190 HIS A CA  
1511 C C   . HIS A 212 ? 0.2889 0.3130 0.2146 -0.0475 -0.0426 -0.0312 190 HIS A C   
1512 O O   . HIS A 212 ? 0.2470 0.2680 0.1544 -0.0504 -0.0279 -0.0433 190 HIS A O   
1513 C CB  . HIS A 212 ? 0.2215 0.2607 0.2117 -0.0449 -0.0568 -0.0329 190 HIS A CB  
1514 C CG  . HIS A 212 ? 0.2098 0.2422 0.2165 -0.0390 -0.0361 -0.0338 190 HIS A CG  
1515 N ND1 . HIS A 212 ? 0.2063 0.2287 0.2212 -0.0447 -0.0284 -0.0437 190 HIS A ND1 
1516 C CD2 . HIS A 212 ? 0.1977 0.2292 0.2123 -0.0294 -0.0249 -0.0248 190 HIS A CD2 
1517 C CE1 . HIS A 212 ? 0.1956 0.2104 0.2204 -0.0396 -0.0150 -0.0375 190 HIS A CE1 
1518 N NE2 . HIS A 212 ? 0.1976 0.2201 0.2209 -0.0306 -0.0116 -0.0272 190 HIS A NE2 
1519 N N   . PHE A 213 ? 0.2283 0.2518 0.1632 -0.0396 -0.0485 -0.0142 191 PHE A N   
1520 C CA  . PHE A 213 ? 0.2314 0.2477 0.1505 -0.0363 -0.0389 -0.0056 191 PHE A CA  
1521 C C   . PHE A 213 ? 0.2906 0.3061 0.2425 -0.0217 -0.0339 0.0014  191 PHE A C   
1522 O O   . PHE A 213 ? 0.2304 0.2540 0.2136 -0.0154 -0.0426 0.0027  191 PHE A O   
1523 C CB  . PHE A 213 ? 0.2569 0.2682 0.1421 -0.0470 -0.0563 0.0099  191 PHE A CB  
1524 C CG  . PHE A 213 ? 0.3612 0.3778 0.2052 -0.0661 -0.0618 0.0031  191 PHE A CG  
1525 C CD1 . PHE A 213 ? 0.4075 0.4302 0.2181 -0.0781 -0.0427 -0.0087 191 PHE A CD1 
1526 C CD2 . PHE A 213 ? 0.4582 0.4783 0.2989 -0.0730 -0.0851 0.0046  191 PHE A CD2 
1527 C CE1 . PHE A 213 ? 0.3833 0.4151 0.1629 -0.0941 -0.0428 -0.0194 191 PHE A CE1 
1528 C CE2 . PHE A 213 ? 0.5284 0.5549 0.3273 -0.0923 -0.0896 -0.0039 191 PHE A CE2 
1529 C CZ  . PHE A 213 ? 0.4729 0.5048 0.2464 -0.1001 -0.0648 -0.0164 191 PHE A CZ  
1530 N N   . VAL A 214 ? 0.2056 0.2155 0.1521 -0.0173 -0.0193 0.0029  192 VAL A N   
1531 C CA  . VAL A 214 ? 0.1985 0.2079 0.1681 -0.0058 -0.0154 0.0083  192 VAL A CA  
1532 C C   . VAL A 214 ? 0.2117 0.2111 0.1639 -0.0068 -0.0171 0.0183  192 VAL A C   
1533 O O   . VAL A 214 ? 0.2331 0.2310 0.1650 -0.0125 -0.0053 0.0160  192 VAL A O   
1534 C CB  . VAL A 214 ? 0.2181 0.2293 0.2011 -0.0010 0.0021  0.0015  192 VAL A CB  
1535 C CG1 . VAL A 214 ? 0.1850 0.1995 0.1855 0.0079  0.0060  0.0048  192 VAL A CG1 
1536 C CG2 . VAL A 214 ? 0.2296 0.2464 0.2280 -0.0048 0.0032  -0.0052 192 VAL A CG2 
1537 N N   . ASP A 215 ? 0.2040 0.1974 0.1698 -0.0013 -0.0324 0.0276  193 ASP A N   
1538 C CA  . ASP A 215 ? 0.2233 0.2021 0.1776 -0.0031 -0.0370 0.0388  193 ASP A CA  
1539 C C   . ASP A 215 ? 0.2693 0.2503 0.2421 0.0072  -0.0220 0.0317  193 ASP A C   
1540 O O   . ASP A 215 ? 0.2269 0.2182 0.2279 0.0178  -0.0178 0.0223  193 ASP A O   
1541 C CB  . ASP A 215 ? 0.2229 0.1878 0.1896 -0.0002 -0.0654 0.0512  193 ASP A CB  
1542 C CG  . ASP A 215 ? 0.3340 0.2919 0.2718 -0.0149 -0.0863 0.0644  193 ASP A CG  
1543 O OD1 . ASP A 215 ? 0.3288 0.2927 0.2287 -0.0307 -0.0760 0.0635  193 ASP A OD1 
1544 O OD2 . ASP A 215 ? 0.3567 0.3046 0.3114 -0.0105 -0.1149 0.0739  193 ASP A OD2 
1545 N N   . HIS A 216 ? 0.1870 0.1621 0.1428 0.0016  -0.0132 0.0352  194 HIS A N   
1546 C CA  . HIS A 216 ? 0.1791 0.1569 0.1479 0.0092  -0.0007 0.0284  194 HIS A CA  
1547 C C   . HIS A 216 ? 0.2352 0.1982 0.2005 0.0056  -0.0077 0.0368  194 HIS A C   
1548 O O   . HIS A 216 ? 0.2329 0.1879 0.1744 -0.0088 -0.0121 0.0481  194 HIS A O   
1549 C CB  . HIS A 216 ? 0.2128 0.2000 0.1716 0.0062  0.0168  0.0215  194 HIS A CB  
1550 C CG  . HIS A 216 ? 0.1994 0.1948 0.1632 0.0089  0.0234  0.0133  194 HIS A CG  
1551 N ND1 . HIS A 216 ? 0.2200 0.2193 0.1984 0.0155  0.0287  0.0092  194 HIS A ND1 
1552 C CD2 . HIS A 216 ? 0.2112 0.2099 0.1654 0.0031  0.0253  0.0081  194 HIS A CD2 
1553 C CE1 . HIS A 216 ? 0.2242 0.2248 0.2035 0.0134  0.0313  0.0051  194 HIS A CE1 
1554 N NE2 . HIS A 216 ? 0.1974 0.1975 0.1648 0.0076  0.0293  0.0022  194 HIS A NE2 
1555 N N   . CYS A 217 ? 0.2231 0.1842 0.2095 0.0156  -0.0070 0.0301  195 CYS A N   
1556 C CA  . CYS A 217 ? 0.2072 0.1564 0.1909 0.0110  -0.0085 0.0339  195 CYS A CA  
1557 C C   . CYS A 217 ? 0.2834 0.2448 0.2771 0.0184  0.0051  0.0205  195 CYS A C   
1558 O O   . CYS A 217 ? 0.2182 0.1920 0.2240 0.0274  0.0109  0.0099  195 CYS A O   
1559 C CB  . CYS A 217 ? 0.2874 0.2125 0.2860 0.0133  -0.0307 0.0406  195 CYS A CB  
1560 S SG  . CYS A 217 ? 0.3058 0.2351 0.3490 0.0348  -0.0368 0.0200  195 CYS A SG  
1561 N N   . ILE A 218 ? 0.2180 0.1788 0.2042 0.0114  0.0103  0.0219  196 ILE A N   
1562 C CA  . ILE A 218 ? 0.1920 0.1638 0.1842 0.0165  0.0192  0.0113  196 ILE A CA  
1563 C C   . ILE A 218 ? 0.2118 0.1738 0.2082 0.0110  0.0142  0.0113  196 ILE A C   
1564 O O   . ILE A 218 ? 0.2324 0.1860 0.2208 -0.0019 0.0108  0.0219  196 ILE A O   
1565 C CB  . ILE A 218 ? 0.1636 0.1508 0.1481 0.0151  0.0302  0.0100  196 ILE A CB  
1566 C CG1 . ILE A 218 ? 0.1871 0.1825 0.1758 0.0201  0.0331  0.0030  196 ILE A CG1 
1567 C CG2 . ILE A 218 ? 0.2251 0.2170 0.2023 0.0035  0.0342  0.0140  196 ILE A CG2 
1568 C CD1 . ILE A 218 ? 0.1601 0.1644 0.1479 0.0219  0.0369  0.0030  196 ILE A CD1 
1569 N N   . GLU A 219 ? 0.2284 0.1921 0.2354 0.0176  0.0137  -0.0010 197 GLU A N   
1570 C CA  . GLU A 219 ? 0.2424 0.1929 0.2580 0.0132  0.0057  -0.0043 197 GLU A CA  
1571 C C   . GLU A 219 ? 0.2062 0.1703 0.2224 0.0152  0.0105  -0.0176 197 GLU A C   
1572 O O   . GLU A 219 ? 0.2072 0.1826 0.2228 0.0229  0.0147  -0.0298 197 GLU A O   
1573 C CB  . GLU A 219 ? 0.2472 0.1775 0.2821 0.0206  -0.0080 -0.0108 197 GLU A CB  
1574 C CG  . GLU A 219 ? 0.2602 0.1707 0.3089 0.0172  -0.0194 -0.0173 197 GLU A CG  
1575 C CD  . GLU A 219 ? 0.4003 0.2827 0.4452 0.0017  -0.0334 0.0039  197 GLU A CD  
1576 O OE1 . GLU A 219 ? 0.4676 0.3493 0.4949 -0.0070 -0.0330 0.0228  197 GLU A OE1 
1577 O OE2 . GLU A 219 ? 0.3762 0.2361 0.4337 -0.0040 -0.0458 0.0019  197 GLU A OE2 
1578 N N   . ILE A 220 ? 0.1696 0.1349 0.1863 0.0058  0.0091  -0.0157 198 ILE A N   
1579 C CA  . ILE A 220 ? 0.1513 0.1253 0.1703 0.0064  0.0074  -0.0290 198 ILE A CA  
1580 C C   . ILE A 220 ? 0.2390 0.1950 0.2710 0.0085  -0.0018 -0.0430 198 ILE A C   
1581 O O   . ILE A 220 ? 0.2453 0.1798 0.2883 0.0009  -0.0113 -0.0380 198 ILE A O   
1582 C CB  . ILE A 220 ? 0.1587 0.1438 0.1817 -0.0039 0.0070  -0.0250 198 ILE A CB  
1583 C CG1 . ILE A 220 ? 0.1574 0.1627 0.1766 -0.0007 0.0141  -0.0190 198 ILE A CG1 
1584 C CG2 . ILE A 220 ? 0.1851 0.1755 0.2113 -0.0051 0.0001  -0.0390 198 ILE A CG2 
1585 C CD1 . ILE A 220 ? 0.1618 0.1870 0.1956 -0.0068 0.0132  -0.0205 198 ILE A CD1 
1586 N N   . LEU A 221 ? 0.2254 0.1901 0.2573 0.0175  0.0009  -0.0618 199 LEU A N   
1587 C CA  . LEU A 221 ? 0.2350 0.1869 0.2861 0.0226  -0.0066 -0.0838 199 LEU A CA  
1588 C C   . LEU A 221 ? 0.2452 0.1948 0.2979 0.0151  -0.0131 -0.0967 199 LEU A C   
1589 O O   . LEU A 221 ? 0.2430 0.1700 0.3173 0.0152  -0.0247 -0.1092 199 LEU A O   
1590 C CB  . LEU A 221 ? 0.2607 0.2334 0.3123 0.0323  0.0032  -0.1056 199 LEU A CB  
1591 C CG  . LEU A 221 ? 0.2581 0.2402 0.3101 0.0386  0.0107  -0.0968 199 LEU A CG  
1592 C CD1 . LEU A 221 ? 0.2921 0.3019 0.3423 0.0400  0.0216  -0.1125 199 LEU A CD1 
1593 C CD2 . LEU A 221 ? 0.2624 0.2190 0.3387 0.0447  -0.0020 -0.0870 199 LEU A CD2 
1594 N N   . SER A 222 ? 0.2195 0.1902 0.2523 0.0087  -0.0089 -0.0942 200 SER A N   
1595 C CA  . SER A 222 ? 0.2239 0.1983 0.2559 0.0010  -0.0164 -0.1081 200 SER A CA  
1596 C C   . SER A 222 ? 0.2994 0.2945 0.3154 -0.0055 -0.0166 -0.0943 200 SER A C   
1597 O O   . SER A 222 ? 0.2426 0.2499 0.2450 -0.0019 -0.0103 -0.0806 200 SER A O   
1598 C CB  . SER A 222 ? 0.2847 0.2699 0.3103 0.0047  -0.0141 -0.1395 200 SER A CB  
1599 O OG  . SER A 222 ? 0.3472 0.3284 0.3776 -0.0029 -0.0245 -0.1569 200 SER A OG  
1600 N N   . HIS A 223 ? 0.2648 0.2631 0.2870 -0.0146 -0.0266 -0.0996 201 HIS A N   
1601 C CA  . HIS A 223 ? 0.2762 0.2958 0.2926 -0.0191 -0.0323 -0.0902 201 HIS A CA  
1602 C C   . HIS A 223 ? 0.3214 0.3454 0.3445 -0.0290 -0.0458 -0.1049 201 HIS A C   
1603 O O   . HIS A 223 ? 0.3159 0.3227 0.3550 -0.0347 -0.0496 -0.1173 201 HIS A O   
1604 C CB  . HIS A 223 ? 0.2009 0.2254 0.2355 -0.0206 -0.0284 -0.0706 201 HIS A CB  
1605 C CG  . HIS A 223 ? 0.2462 0.2599 0.3041 -0.0324 -0.0295 -0.0691 201 HIS A CG  
1606 N ND1 . HIS A 223 ? 0.2751 0.3010 0.3519 -0.0445 -0.0377 -0.0733 201 HIS A ND1 
1607 C CD2 . HIS A 223 ? 0.2379 0.2278 0.3020 -0.0370 -0.0260 -0.0626 201 HIS A CD2 
1608 C CE1 . HIS A 223 ? 0.2604 0.2711 0.3525 -0.0583 -0.0366 -0.0687 201 HIS A CE1 
1609 N NE2 . HIS A 223 ? 0.2990 0.2853 0.3815 -0.0543 -0.0311 -0.0606 201 HIS A NE2 
1610 N N   . ASP A 224 ? 0.2688 0.3136 0.2814 -0.0316 -0.0564 -0.1030 202 ASP A N   
1611 C CA  . ASP A 224 ? 0.2809 0.3338 0.3041 -0.0422 -0.0719 -0.1151 202 ASP A CA  
1612 C C   . ASP A 224 ? 0.2464 0.3110 0.3065 -0.0475 -0.0753 -0.1034 202 ASP A C   
1613 O O   . ASP A 224 ? 0.2443 0.3116 0.3173 -0.0432 -0.0643 -0.0884 202 ASP A O   
1614 C CB  . ASP A 224 ? 0.3487 0.4186 0.3405 -0.0449 -0.0861 -0.1203 202 ASP A CB  
1615 C CG  . ASP A 224 ? 0.3074 0.3918 0.2945 -0.0395 -0.0949 -0.0977 202 ASP A CG  
1616 O OD1 . ASP A 224 ? 0.2802 0.3653 0.2916 -0.0317 -0.0877 -0.0825 202 ASP A OD1 
1617 O OD2 . ASP A 224 ? 0.3382 0.4324 0.2964 -0.0441 -0.1113 -0.0959 202 ASP A OD2 
1618 N N   . LYS A 225 ? 0.2747 0.3508 0.3530 -0.0585 -0.0896 -0.1134 203 LYS A N   
1619 C CA  . LYS A 225 ? 0.2888 0.3798 0.4085 -0.0688 -0.0893 -0.1083 203 LYS A CA  
1620 C C   . LYS A 225 ? 0.2795 0.3958 0.4178 -0.0602 -0.0846 -0.0942 203 LYS A C   
1621 O O   . LYS A 225 ? 0.3136 0.4366 0.4740 -0.0649 -0.0695 -0.0871 203 LYS A O   
1622 C CB  . LYS A 225 ? 0.3105 0.4169 0.4486 -0.0814 -0.1085 -0.1226 203 LYS A CB  
1623 C CG  . LYS A 225 ? 0.3491 0.4727 0.5330 -0.0979 -0.1054 -0.1210 203 LYS A CG  
1624 C CD  . LYS A 225 ? 0.5239 0.6643 0.7208 -0.1060 -0.1214 -0.1273 203 LYS A CD  
1625 C CE  . LYS A 225 ? 0.6610 0.8336 0.9020 -0.1155 -0.1151 -0.1209 203 LYS A CE  
1626 N NZ  . LYS A 225 ? 0.6760 0.8837 0.9366 -0.1019 -0.1267 -0.1191 203 LYS A NZ  
1627 N N   . ASP A 226 ? 0.3111 0.4410 0.4405 -0.0489 -0.0986 -0.0907 204 ASP A N   
1628 C CA  . ASP A 226 ? 0.2122 0.3647 0.3692 -0.0382 -0.1001 -0.0818 204 ASP A CA  
1629 C C   . ASP A 226 ? 0.2448 0.3819 0.3788 -0.0247 -0.0883 -0.0688 204 ASP A C   
1630 O O   . ASP A 226 ? 0.2286 0.3786 0.3829 -0.0133 -0.0928 -0.0630 204 ASP A O   
1631 C CB  . ASP A 226 ? 0.2729 0.4452 0.4419 -0.0333 -0.1298 -0.0828 204 ASP A CB  
1632 C CG  . ASP A 226 ? 0.4092 0.6046 0.6135 -0.0455 -0.1408 -0.0950 204 ASP A CG  
1633 O OD1 . ASP A 226 ? 0.3414 0.5532 0.5827 -0.0535 -0.1245 -0.0993 204 ASP A OD1 
1634 O OD2 . ASP A 226 ? 0.3830 0.5769 0.5690 -0.0489 -0.1613 -0.0959 204 ASP A OD2 
1635 N N   . TYR A 227 ? 0.2161 0.3268 0.3142 -0.0252 -0.0751 -0.0665 205 TYR A N   
1636 C CA  . TYR A 227 ? 0.2327 0.3293 0.3072 -0.0145 -0.0649 -0.0552 205 TYR A CA  
1637 C C   . TYR A 227 ? 0.2169 0.3140 0.2711 -0.0073 -0.0826 -0.0459 205 TYR A C   
1638 O O   . TYR A 227 ? 0.2428 0.3340 0.2931 0.0016  -0.0801 -0.0343 205 TYR A O   
1639 C CB  . TYR A 227 ? 0.2000 0.3033 0.2992 -0.0103 -0.0491 -0.0498 205 TYR A CB  
1640 C CG  . TYR A 227 ? 0.1664 0.2607 0.2687 -0.0209 -0.0316 -0.0512 205 TYR A CG  
1641 C CD1 . TYR A 227 ? 0.2430 0.3485 0.3696 -0.0359 -0.0310 -0.0576 205 TYR A CD1 
1642 C CD2 . TYR A 227 ? 0.2577 0.3315 0.3391 -0.0182 -0.0183 -0.0442 205 TYR A CD2 
1643 C CE1 . TYR A 227 ? 0.2286 0.3204 0.3536 -0.0499 -0.0191 -0.0536 205 TYR A CE1 
1644 C CE2 . TYR A 227 ? 0.2319 0.2928 0.3140 -0.0294 -0.0084 -0.0412 205 TYR A CE2 
1645 C CZ  . TYR A 227 ? 0.2607 0.3285 0.3624 -0.0461 -0.0095 -0.0444 205 TYR A CZ  
1646 O OH  . TYR A 227 ? 0.2825 0.3327 0.3812 -0.0615 -0.0035 -0.0365 205 TYR A OH  
1647 N N   . ASN A 228 ? 0.2279 0.3298 0.2663 -0.0134 -0.1028 -0.0495 206 ASN A N   
1648 C CA  . ASN A 228 ? 0.2713 0.3676 0.2743 -0.0130 -0.1208 -0.0364 206 ASN A CA  
1649 C C   . ASN A 228 ? 0.3174 0.3986 0.2717 -0.0178 -0.1049 -0.0349 206 ASN A C   
1650 O O   . ASN A 228 ? 0.2850 0.3589 0.2092 -0.0193 -0.1118 -0.0191 206 ASN A O   
1651 C CB  . ASN A 228 ? 0.3322 0.4392 0.3242 -0.0220 -0.1485 -0.0403 206 ASN A CB  
1652 C CG  . ASN A 228 ? 0.3607 0.4873 0.4058 -0.0158 -0.1704 -0.0401 206 ASN A CG  
1653 O OD1 . ASN A 228 ? 0.2810 0.4106 0.3582 -0.0029 -0.1771 -0.0302 206 ASN A OD1 
1654 N ND2 . ASN A 228 ? 0.3708 0.5131 0.4305 -0.0246 -0.1822 -0.0544 206 ASN A ND2 
1655 N N   . LYS A 229 ? 0.3090 0.3860 0.2593 -0.0210 -0.0852 -0.0515 207 LYS A N   
1656 C CA  . LYS A 229 ? 0.2864 0.3561 0.2041 -0.0236 -0.0677 -0.0570 207 LYS A CA  
1657 C C   . LYS A 229 ? 0.2942 0.3535 0.2381 -0.0159 -0.0476 -0.0624 207 LYS A C   
1658 O O   . LYS A 229 ? 0.2715 0.3273 0.2425 -0.0166 -0.0467 -0.0715 207 LYS A O   
1659 C CB  . LYS A 229 ? 0.3365 0.4134 0.2239 -0.0354 -0.0693 -0.0786 207 LYS A CB  
1660 C CG  . LYS A 229 ? 0.3544 0.4416 0.2043 -0.0475 -0.0913 -0.0705 207 LYS A CG  
1661 C CD  . LYS A 229 ? 0.4831 0.5752 0.2972 -0.0594 -0.0866 -0.0905 207 LYS A CD  
1662 C CE  . LYS A 229 ? 0.7598 0.8514 0.5291 -0.0680 -0.0853 -0.0737 207 LYS A CE  
1663 N NZ  . LYS A 229 ? 0.7922 0.8921 0.5352 -0.0775 -0.0705 -0.0944 207 LYS A NZ  
1664 N N   . VAL A 230 ? 0.2485 0.3018 0.1840 -0.0108 -0.0342 -0.0543 208 VAL A N   
1665 C CA  . VAL A 230 ? 0.2213 0.2638 0.1780 -0.0038 -0.0193 -0.0550 208 VAL A CA  
1666 C C   . VAL A 230 ? 0.2781 0.3200 0.2165 -0.0024 -0.0061 -0.0599 208 VAL A C   
1667 O O   . VAL A 230 ? 0.2822 0.3312 0.1950 -0.0065 -0.0054 -0.0516 208 VAL A O   
1668 C CB  . VAL A 230 ? 0.2167 0.2577 0.1942 0.0023  -0.0181 -0.0383 208 VAL A CB  
1669 C CG1 . VAL A 230 ? 0.1882 0.2181 0.1771 0.0061  -0.0041 -0.0367 208 VAL A CG1 
1670 C CG2 . VAL A 230 ? 0.1812 0.2324 0.1856 0.0003  -0.0284 -0.0380 208 VAL A CG2 
1671 N N   . LYS A 231 ? 0.2088 0.2424 0.1632 0.0022  0.0026  -0.0729 209 LYS A N   
1672 C CA  . LYS A 231 ? 0.2414 0.2782 0.1933 0.0063  0.0152  -0.0804 209 LYS A CA  
1673 C C   . LYS A 231 ? 0.2429 0.2660 0.2152 0.0139  0.0184  -0.0670 209 LYS A C   
1674 O O   . LYS A 231 ? 0.2111 0.2188 0.2028 0.0153  0.0131  -0.0641 209 LYS A O   
1675 C CB  . LYS A 231 ? 0.2707 0.3100 0.2325 0.0079  0.0186  -0.1104 209 LYS A CB  
1676 C CG  . LYS A 231 ? 0.4606 0.5045 0.4373 0.0151  0.0293  -0.1194 209 LYS A CG  
1677 C CD  . LYS A 231 ? 0.5923 0.6595 0.5537 0.0073  0.0384  -0.1286 209 LYS A CD  
1678 C CE  . LYS A 231 ? 0.5355 0.6081 0.4996 0.0040  0.0353  -0.1517 209 LYS A CE  
1679 N NZ  . LYS A 231 ? 0.5311 0.6291 0.4661 -0.0093 0.0435  -0.1573 209 LYS A NZ  
1680 N N   . LEU A 232 ? 0.2054 0.2341 0.1703 0.0156  0.0261  -0.0579 210 LEU A N   
1681 C CA  . LEU A 232 ? 0.1847 0.2034 0.1614 0.0204  0.0276  -0.0433 210 LEU A CA  
1682 C C   . LEU A 232 ? 0.2022 0.2256 0.1862 0.0249  0.0353  -0.0495 210 LEU A C   
1683 O O   . LEU A 232 ? 0.2343 0.2752 0.2091 0.0217  0.0433  -0.0603 210 LEU A O   
1684 C CB  . LEU A 232 ? 0.2261 0.2467 0.1926 0.0183  0.0260  -0.0258 210 LEU A CB  
1685 C CG  . LEU A 232 ? 0.2237 0.2374 0.2002 0.0215  0.0278  -0.0143 210 LEU A CG  
1686 C CD1 . LEU A 232 ? 0.1484 0.1564 0.1387 0.0197  0.0252  -0.0130 210 LEU A CD1 
1687 C CD2 . LEU A 232 ? 0.1609 0.1766 0.1316 0.0214  0.0246  -0.0037 210 LEU A CD2 
1688 N N   . TYR A 233 ? 0.1835 0.1945 0.1834 0.0299  0.0324  -0.0428 211 TYR A N   
1689 C CA  . TYR A 233 ? 0.2098 0.2256 0.2246 0.0357  0.0353  -0.0488 211 TYR A CA  
1690 C C   . TYR A 233 ? 0.1861 0.1923 0.2013 0.0359  0.0321  -0.0316 211 TYR A C   
1691 O O   . TYR A 233 ? 0.1911 0.1832 0.2020 0.0327  0.0264  -0.0197 211 TYR A O   
1692 C CB  . TYR A 233 ? 0.1879 0.1955 0.2305 0.0438  0.0276  -0.0660 211 TYR A CB  
1693 C CG  . TYR A 233 ? 0.1837 0.1942 0.2496 0.0508  0.0239  -0.0696 211 TYR A CG  
1694 C CD1 . TYR A 233 ? 0.1900 0.2251 0.2596 0.0485  0.0327  -0.0801 211 TYR A CD1 
1695 C CD2 . TYR A 233 ? 0.2040 0.1915 0.2874 0.0566  0.0082  -0.0596 211 TYR A CD2 
1696 C CE1 . TYR A 233 ? 0.1866 0.2281 0.2818 0.0540  0.0279  -0.0851 211 TYR A CE1 
1697 C CE2 . TYR A 233 ? 0.2343 0.2257 0.3390 0.0618  0.0004  -0.0612 211 TYR A CE2 
1698 C CZ  . TYR A 233 ? 0.2714 0.2919 0.3851 0.0616  0.0112  -0.0762 211 TYR A CZ  
1699 O OH  . TYR A 233 ? 0.1808 0.2089 0.3219 0.0670  0.0031  -0.0817 211 TYR A OH  
1700 N N   . GLU A 234 ? 0.1724 0.1896 0.1923 0.0373  0.0367  -0.0322 212 GLU A N   
1701 C CA  . GLU A 234 ? 0.1892 0.1992 0.2091 0.0368  0.0325  -0.0194 212 GLU A CA  
1702 C C   . GLU A 234 ? 0.1661 0.1854 0.2091 0.0424  0.0297  -0.0277 212 GLU A C   
1703 O O   . GLU A 234 ? 0.1752 0.2164 0.2294 0.0432  0.0388  -0.0424 212 GLU A O   
1704 C CB  . GLU A 234 ? 0.1524 0.1665 0.1547 0.0306  0.0392  -0.0097 212 GLU A CB  
1705 C CG  . GLU A 234 ? 0.2092 0.2145 0.2066 0.0284  0.0355  0.0003  212 GLU A CG  
1706 C CD  . GLU A 234 ? 0.2695 0.2805 0.2643 0.0252  0.0396  0.0026  212 GLU A CD  
1707 O OE1 . GLU A 234 ? 0.2886 0.3041 0.2775 0.0217  0.0444  0.0033  212 GLU A OE1 
1708 O OE2 . GLU A 234 ? 0.2886 0.2961 0.2829 0.0235  0.0363  0.0054  212 GLU A OE2 
1709 N N   . HIS A 235 ? 0.1818 0.1881 0.2314 0.0443  0.0170  -0.0187 213 HIS A N   
1710 C CA  . HIS A 235 ? 0.2149 0.2298 0.2905 0.0502  0.0089  -0.0244 213 HIS A CA  
1711 C C   . HIS A 235 ? 0.1730 0.1820 0.2325 0.0435  0.0038  -0.0092 213 HIS A C   
1712 O O   . HIS A 235 ? 0.1890 0.1797 0.2268 0.0373  -0.0031 0.0048  213 HIS A O   
1713 C CB  . HIS A 235 ? 0.2042 0.2040 0.3087 0.0605  -0.0107 -0.0295 213 HIS A CB  
1714 C CG  . HIS A 235 ? 0.1651 0.1752 0.3031 0.0680  -0.0230 -0.0370 213 HIS A CG  
1715 N ND1 . HIS A 235 ? 0.2556 0.2457 0.4104 0.0718  -0.0467 -0.0329 213 HIS A ND1 
1716 C CD2 . HIS A 235 ? 0.1610 0.1992 0.3138 0.0674  -0.0150 -0.0463 213 HIS A CD2 
1717 C CE1 . HIS A 235 ? 0.2545 0.2605 0.4360 0.0759  -0.0537 -0.0413 213 HIS A CE1 
1718 N NE2 . HIS A 235 ? 0.1802 0.2166 0.3617 0.0732  -0.0340 -0.0500 213 HIS A NE2 
1719 N N   . ALA A 236 ? 0.1300 0.1572 0.1985 0.0418  0.0087  -0.0136 214 ALA A N   
1720 C CA  . ALA A 236 ? 0.1655 0.1886 0.2184 0.0343  0.0049  -0.0035 214 ALA A CA  
1721 C C   . ALA A 236 ? 0.1655 0.2045 0.2458 0.0366  -0.0036 -0.0096 214 ALA A C   
1722 O O   . ALA A 236 ? 0.1727 0.2360 0.2795 0.0390  0.0051  -0.0235 214 ALA A O   
1723 C CB  . ALA A 236 ? 0.1524 0.1778 0.1846 0.0262  0.0202  -0.0013 214 ALA A CB  
1724 N N   . VAL A 237 ? 0.1624 0.1916 0.2360 0.0337  -0.0206 -0.0004 215 VAL A N   
1725 C CA  . VAL A 237 ? 0.1661 0.2101 0.2687 0.0362  -0.0346 -0.0054 215 VAL A CA  
1726 C C   . VAL A 237 ? 0.1649 0.2036 0.2415 0.0244  -0.0401 0.0026  215 VAL A C   
1727 O O   . VAL A 237 ? 0.1839 0.2034 0.2266 0.0174  -0.0481 0.0144  215 VAL A O   
1728 C CB  . VAL A 237 ? 0.1846 0.2192 0.3141 0.0473  -0.0614 -0.0034 215 VAL A CB  
1729 C CG1 . VAL A 237 ? 0.2040 0.2559 0.3682 0.0507  -0.0804 -0.0086 215 VAL A CG1 
1730 C CG2 . VAL A 237 ? 0.1976 0.2383 0.3594 0.0605  -0.0558 -0.0185 215 VAL A CG2 
1731 N N   . ALA A 238 ? 0.1487 0.2062 0.2405 0.0195  -0.0349 -0.0055 216 ALA A N   
1732 C CA  . ALA A 238 ? 0.2325 0.2857 0.3039 0.0083  -0.0412 -0.0027 216 ALA A CA  
1733 C C   . ALA A 238 ? 0.2482 0.3049 0.3327 0.0091  -0.0693 0.0006  216 ALA A C   
1734 O O   . ALA A 238 ? 0.1967 0.2680 0.3234 0.0194  -0.0818 -0.0045 216 ALA A O   
1735 C CB  . ALA A 238 ? 0.1537 0.2209 0.2362 0.0000  -0.0265 -0.0114 216 ALA A CB  
1736 N N   . HIS A 239 ? 0.2614 0.3065 0.3112 -0.0022 -0.0806 0.0070  217 HIS A N   
1737 C CA  . HIS A 239 ? 0.3273 0.3747 0.3824 -0.0051 -0.1112 0.0123  217 HIS A CA  
1738 C C   . HIS A 239 ? 0.2708 0.3156 0.2882 -0.0219 -0.1138 0.0100  217 HIS A C   
1739 O O   . HIS A 239 ? 0.3100 0.3477 0.2968 -0.0295 -0.0933 0.0044  217 HIS A O   
1740 C CB  . HIS A 239 ? 0.3569 0.3840 0.4012 -0.0013 -0.1360 0.0301  217 HIS A CB  
1741 C CG  . HIS A 239 ? 0.3822 0.3869 0.3693 -0.0139 -0.1292 0.0430  217 HIS A CG  
1742 N ND1 . HIS A 239 ? 0.4361 0.4328 0.3731 -0.0331 -0.1412 0.0523  217 HIS A ND1 
1743 C CD2 . HIS A 239 ? 0.3591 0.3526 0.3319 -0.0124 -0.1110 0.0462  217 HIS A CD2 
1744 C CE1 . HIS A 239 ? 0.4413 0.4259 0.3372 -0.0437 -0.1279 0.0598  217 HIS A CE1 
1745 N NE2 . HIS A 239 ? 0.4228 0.4046 0.3418 -0.0307 -0.1104 0.0566  217 HIS A NE2 
1746 N N   . SER A 240 ? 0.3024 0.3548 0.3266 -0.0270 -0.1406 0.0113  218 SER A N   
1747 C CA  . SER A 240 ? 0.4229 0.4733 0.4068 -0.0449 -0.1476 0.0076  218 SER A CA  
1748 C C   . SER A 240 ? 0.5843 0.6169 0.5133 -0.0571 -0.1661 0.0254  218 SER A C   
1749 O O   . SER A 240 ? 0.6571 0.6753 0.5866 -0.0504 -0.1750 0.0426  218 SER A O   
1750 C CB  . SER A 240 ? 0.4584 0.5280 0.4742 -0.0478 -0.1683 -0.0006 218 SER A CB  
1751 O OG  . SER A 240 ? 0.4944 0.5671 0.5383 -0.0377 -0.1963 0.0110  218 SER A OG  
1752 N N   . GLY A 241 ? 0.7176 0.7507 0.6022 -0.0745 -0.1639 0.0185  219 GLY A N   
1753 C CA  . GLY A 241 ? 0.7249 0.7457 0.5584 -0.0872 -0.1638 0.0307  219 GLY A CA  
1754 C C   . GLY A 241 ? 0.7267 0.7326 0.5625 -0.0854 -0.1898 0.0553  219 GLY A C   
1755 O O   . GLY A 241 ? 0.9059 0.9156 0.7679 -0.0799 -0.2139 0.0582  219 GLY A O   
1756 N N   . SER B 26  ? 0.6640 0.7196 0.8347 -0.0574 -0.0525 -0.0561 2   SER B N   
1757 C CA  . SER B 26  ? 0.6436 0.7206 0.8023 -0.0556 -0.0635 -0.0722 2   SER B CA  
1758 C C   . SER B 26  ? 0.4924 0.5618 0.6214 -0.0493 -0.0652 -0.0799 2   SER B C   
1759 O O   . SER B 26  ? 0.5931 0.6801 0.6986 -0.0419 -0.0715 -0.0804 2   SER B O   
1760 C CB  . SER B 26  ? 0.5808 0.6730 0.7722 -0.0679 -0.0702 -0.0931 2   SER B CB  
1761 O OG  . SER B 26  ? 0.6239 0.7466 0.8032 -0.0660 -0.0819 -0.1082 2   SER B OG  
1762 N N   . ALA B 27  ? 0.3377 0.3830 0.4695 -0.0515 -0.0591 -0.0832 3   ALA B N   
1763 C CA  . ALA B 27  ? 0.3140 0.3549 0.4217 -0.0467 -0.0602 -0.0932 3   ALA B CA  
1764 C C   . ALA B 27  ? 0.3867 0.4210 0.4610 -0.0355 -0.0569 -0.0755 3   ALA B C   
1765 O O   . ALA B 27  ? 0.3491 0.3883 0.4005 -0.0304 -0.0589 -0.0804 3   ALA B O   
1766 C CB  . ALA B 27  ? 0.3132 0.3308 0.4390 -0.0518 -0.0542 -0.1028 3   ALA B CB  
1767 N N   . ILE B 28  ? 0.3170 0.3431 0.3902 -0.0319 -0.0513 -0.0563 4   ILE B N   
1768 C CA  . ILE B 28  ? 0.2615 0.2788 0.3102 -0.0226 -0.0471 -0.0425 4   ILE B CA  
1769 C C   . ILE B 28  ? 0.2605 0.2955 0.3009 -0.0156 -0.0516 -0.0350 4   ILE B C   
1770 O O   . ILE B 28  ? 0.3216 0.3676 0.3767 -0.0164 -0.0524 -0.0308 4   ILE B O   
1771 C CB  . ILE B 28  ? 0.2954 0.2967 0.3493 -0.0226 -0.0379 -0.0294 4   ILE B CB  
1772 C CG1 . ILE B 28  ? 0.2745 0.2605 0.3434 -0.0288 -0.0335 -0.0326 4   ILE B CG1 
1773 C CG2 . ILE B 28  ? 0.2585 0.2522 0.2901 -0.0143 -0.0341 -0.0203 4   ILE B CG2 
1774 C CD1 . ILE B 28  ? 0.2732 0.2479 0.3285 -0.0267 -0.0333 -0.0413 4   ILE B CD1 
1775 N N   . LYS B 29  ? 0.2488 0.2882 0.2688 -0.0084 -0.0540 -0.0316 5   LYS B N   
1776 C CA  . LYS B 29  ? 0.2710 0.3264 0.2871 -0.0002 -0.0578 -0.0207 5   LYS B CA  
1777 C C   . LYS B 29  ? 0.2365 0.2748 0.2490 0.0067  -0.0503 -0.0075 5   LYS B C   
1778 O O   . LYS B 29  ? 0.2738 0.2923 0.2791 0.0057  -0.0437 -0.0073 5   LYS B O   
1779 C CB  . LYS B 29  ? 0.2971 0.3726 0.2971 0.0039  -0.0647 -0.0211 5   LYS B CB  
1780 C CG  . LYS B 29  ? 0.3154 0.4223 0.3208 -0.0009 -0.0748 -0.0350 5   LYS B CG  
1781 C CD  . LYS B 29  ? 0.3120 0.4130 0.3256 -0.0118 -0.0748 -0.0576 5   LYS B CD  
1782 C CE  . LYS B 29  ? 0.3492 0.4454 0.3442 -0.0110 -0.0725 -0.0652 5   LYS B CE  
1783 N NZ  . LYS B 29  ? 0.2800 0.3674 0.2885 -0.0203 -0.0712 -0.0886 5   LYS B NZ  
1784 N N   . PRO B 30  ? 0.3003 0.3470 0.3211 0.0139  -0.0508 0.0021  6   PRO B N   
1785 C CA  . PRO B 30  ? 0.2346 0.2653 0.2579 0.0200  -0.0431 0.0097  6   PRO B CA  
1786 C C   . PRO B 30  ? 0.2903 0.3089 0.3010 0.0246  -0.0407 0.0169  6   PRO B C   
1787 O O   . PRO B 30  ? 0.2875 0.2894 0.3002 0.0264  -0.0337 0.0181  6   PRO B O   
1788 C CB  . PRO B 30  ? 0.2422 0.2871 0.2835 0.0273  -0.0446 0.0163  6   PRO B CB  
1789 C CG  . PRO B 30  ? 0.3199 0.3899 0.3648 0.0258  -0.0541 0.0156  6   PRO B CG  
1790 C CD  . PRO B 30  ? 0.2853 0.3570 0.3194 0.0159  -0.0578 0.0038  6   PRO B CD  
1791 N N   . ASP B 31  ? 0.2812 0.3116 0.2805 0.0262  -0.0463 0.0215  7   ASP B N   
1792 C CA  . ASP B 31  ? 0.2762 0.2986 0.2638 0.0296  -0.0435 0.0303  7   ASP B CA  
1793 C C   . ASP B 31  ? 0.2750 0.3046 0.2441 0.0241  -0.0463 0.0212  7   ASP B C   
1794 O O   . ASP B 31  ? 0.2960 0.3497 0.2612 0.0226  -0.0537 0.0157  7   ASP B O   
1795 C CB  . ASP B 31  ? 0.2961 0.3330 0.2905 0.0390  -0.0463 0.0495  7   ASP B CB  
1796 C CG  . ASP B 31  ? 0.3817 0.4075 0.4002 0.0456  -0.0419 0.0571  7   ASP B CG  
1797 O OD1 . ASP B 31  ? 0.3384 0.3417 0.3635 0.0461  -0.0341 0.0570  7   ASP B OD1 
1798 O OD2 . ASP B 31  ? 0.3567 0.3981 0.3898 0.0500  -0.0460 0.0610  7   ASP B OD2 
1799 N N   . MET B 32  ? 0.2591 0.2708 0.2190 0.0212  -0.0404 0.0174  8   MET B N   
1800 C CA  . MET B 32  ? 0.3037 0.3218 0.2492 0.0170  -0.0418 0.0066  8   MET B CA  
1801 C C   . MET B 32  ? 0.3133 0.3239 0.2470 0.0194  -0.0364 0.0143  8   MET B C   
1802 O O   . MET B 32  ? 0.2633 0.2567 0.2023 0.0217  -0.0307 0.0241  8   MET B O   
1803 C CB  . MET B 32  ? 0.2981 0.3037 0.2499 0.0092  -0.0402 -0.0098 8   MET B CB  
1804 C CG  . MET B 32  ? 0.3819 0.3956 0.3495 0.0057  -0.0446 -0.0156 8   MET B CG  
1805 S SD  . MET B 32  ? 0.3890 0.3992 0.3711 -0.0043 -0.0454 -0.0342 8   MET B SD  
1806 C CE  . MET B 32  ? 0.3373 0.3532 0.3074 -0.0059 -0.0464 -0.0497 8   MET B CE  
1807 N N   . LYS B 33  ? 0.2815 0.3079 0.2010 0.0184  -0.0381 0.0077  9   LYS B N   
1808 C CA  . LYS B 33  ? 0.3019 0.3273 0.2094 0.0202  -0.0328 0.0138  9   LYS B CA  
1809 C C   . LYS B 33  ? 0.3591 0.3681 0.2650 0.0151  -0.0284 -0.0024 9   LYS B C   
1810 O O   . LYS B 33  ? 0.2930 0.2978 0.2064 0.0105  -0.0304 -0.0184 9   LYS B O   
1811 C CB  . LYS B 33  ? 0.2757 0.3372 0.1680 0.0236  -0.0369 0.0179  9   LYS B CB  
1812 C CG  . LYS B 33  ? 0.3445 0.4282 0.2402 0.0300  -0.0418 0.0387  9   LYS B CG  
1813 C CD  . LYS B 33  ? 0.4536 0.5835 0.3319 0.0330  -0.0468 0.0417  9   LYS B CD  
1814 C CE  . LYS B 33  ? 0.4143 0.5726 0.2979 0.0402  -0.0529 0.0652  9   LYS B CE  
1815 N NZ  . LYS B 33  ? 0.5663 0.7794 0.4312 0.0432  -0.0588 0.0683  9   LYS B NZ  
1816 N N   . ILE B 34  ? 0.3031 0.3031 0.2032 0.0161  -0.0219 0.0033  10  ILE B N   
1817 C CA  . ILE B 34  ? 0.3036 0.2878 0.2052 0.0128  -0.0170 -0.0080 10  ILE B CA  
1818 C C   . ILE B 34  ? 0.3374 0.3345 0.2261 0.0148  -0.0131 -0.0080 10  ILE B C   
1819 O O   . ILE B 34  ? 0.2947 0.2966 0.1785 0.0177  -0.0100 0.0087  10  ILE B O   
1820 C CB  . ILE B 34  ? 0.3373 0.2971 0.2490 0.0115  -0.0121 -0.0013 10  ILE B CB  
1821 C CG1 . ILE B 34  ? 0.3647 0.3183 0.2881 0.0105  -0.0151 0.0001  10  ILE B CG1 
1822 C CG2 . ILE B 34  ? 0.3060 0.2543 0.2214 0.0089  -0.0080 -0.0107 10  ILE B CG2 
1823 C CD1 . ILE B 34  ? 0.4138 0.3559 0.3451 0.0116  -0.0115 0.0092  10  ILE B CD1 
1824 N N   . LYS B 35  ? 0.3140 0.3180 0.2008 0.0133  -0.0126 -0.0267 11  LYS B N   
1825 C CA  . LYS B 35  ? 0.2687 0.2867 0.1447 0.0154  -0.0077 -0.0309 11  LYS B CA  
1826 C C   . LYS B 35  ? 0.3231 0.3202 0.2102 0.0139  -0.0022 -0.0411 11  LYS B C   
1827 O O   . LYS B 35  ? 0.2828 0.2668 0.1850 0.0112  -0.0036 -0.0543 11  LYS B O   
1828 C CB  . LYS B 35  ? 0.2846 0.3366 0.1505 0.0163  -0.0115 -0.0482 11  LYS B CB  
1829 C CG  . LYS B 35  ? 0.3466 0.4272 0.2018 0.0185  -0.0182 -0.0370 11  LYS B CG  
1830 C CD  . LYS B 35  ? 0.3506 0.4468 0.1939 0.0231  -0.0145 -0.0102 11  LYS B CD  
1831 C CE  . LYS B 35  ? 0.5445 0.6717 0.3810 0.0267  -0.0213 0.0054  11  LYS B CE  
1832 N NZ  . LYS B 35  ? 0.4358 0.5767 0.2680 0.0316  -0.0173 0.0376  11  LYS B NZ  
1833 N N   . LEU B 36  ? 0.2934 0.2893 0.1762 0.0157  0.0044  -0.0335 12  LEU B N   
1834 C CA  . LEU B 36  ? 0.2706 0.2474 0.1660 0.0152  0.0093  -0.0380 12  LEU B CA  
1835 C C   . LEU B 36  ? 0.3023 0.2916 0.1915 0.0181  0.0161  -0.0397 12  LEU B C   
1836 O O   . LEU B 36  ? 0.3207 0.3253 0.1974 0.0194  0.0185  -0.0268 12  LEU B O   
1837 C CB  . LEU B 36  ? 0.2868 0.2429 0.1899 0.0132  0.0100  -0.0226 12  LEU B CB  
1838 C CG  . LEU B 36  ? 0.3000 0.2420 0.2160 0.0129  0.0141  -0.0228 12  LEU B CG  
1839 C CD1 . LEU B 36  ? 0.2937 0.2224 0.2193 0.0103  0.0120  -0.0150 12  LEU B CD1 
1840 C CD2 . LEU B 36  ? 0.2638 0.2111 0.1754 0.0141  0.0198  -0.0150 12  LEU B CD2 
1841 N N   . ARG B 37  ? 0.2641 0.2474 0.1657 0.0194  0.0198  -0.0539 13  ARG B N   
1842 C CA  . ARG B 37  ? 0.2677 0.2594 0.1683 0.0225  0.0272  -0.0545 13  ARG B CA  
1843 C C   . ARG B 37  ? 0.3400 0.3106 0.2615 0.0232  0.0301  -0.0544 13  ARG B C   
1844 O O   . ARG B 37  ? 0.3214 0.2797 0.2611 0.0233  0.0286  -0.0655 13  ARG B O   
1845 C CB  . ARG B 37  ? 0.2854 0.3032 0.1805 0.0259  0.0300  -0.0757 13  ARG B CB  
1846 C CG  . ARG B 37  ? 0.3094 0.3347 0.2091 0.0300  0.0387  -0.0795 13  ARG B CG  
1847 C CD  . ARG B 37  ? 0.3980 0.4598 0.2855 0.0336  0.0428  -0.0971 13  ARG B CD  
1848 N NE  . ARG B 37  ? 0.4356 0.5264 0.2976 0.0330  0.0414  -0.0822 13  ARG B NE  
1849 C CZ  . ARG B 37  ? 0.6946 0.8233 0.5409 0.0347  0.0402  -0.0955 13  ARG B CZ  
1850 N NH1 . ARG B 37  ? 0.5883 0.7298 0.4417 0.0365  0.0403  -0.1290 13  ARG B NH1 
1851 N NH2 . ARG B 37  ? 0.5399 0.6970 0.3653 0.0348  0.0392  -0.0749 13  ARG B NH2 
1852 N N   . MET B 38  ? 0.2976 0.2664 0.2196 0.0235  0.0341  -0.0409 14  MET B N   
1853 C CA  . MET B 38  ? 0.3360 0.2923 0.2774 0.0251  0.0366  -0.0386 14  MET B CA  
1854 C C   . MET B 38  ? 0.3163 0.2860 0.2608 0.0296  0.0440  -0.0431 14  MET B C   
1855 O O   . MET B 38  ? 0.2926 0.2780 0.2231 0.0290  0.0473  -0.0369 14  MET B O   
1856 C CB  . MET B 38  ? 0.2908 0.2380 0.2340 0.0215  0.0343  -0.0211 14  MET B CB  
1857 C CG  . MET B 38  ? 0.2631 0.2129 0.2181 0.0232  0.0380  -0.0138 14  MET B CG  
1858 S SD  . MET B 38  ? 0.2833 0.2345 0.2374 0.0178  0.0357  0.0013  14  MET B SD  
1859 C CE  . MET B 38  ? 0.2415 0.1824 0.1996 0.0156  0.0294  0.0041  14  MET B CE  
1860 N N   . GLU B 39  ? 0.2597 0.2242 0.2256 0.0343  0.0471  -0.0533 15  GLU B N   
1861 C CA  . GLU B 39  ? 0.2927 0.2684 0.2681 0.0397  0.0545  -0.0572 15  GLU B CA  
1862 C C   . GLU B 39  ? 0.3123 0.2780 0.3074 0.0413  0.0547  -0.0427 15  GLU B C   
1863 O O   . GLU B 39  ? 0.2857 0.2363 0.2972 0.0413  0.0512  -0.0383 15  GLU B O   
1864 C CB  . GLU B 39  ? 0.2774 0.2579 0.2674 0.0454  0.0588  -0.0824 15  GLU B CB  
1865 C CG  . GLU B 39  ? 0.4671 0.4611 0.4690 0.0522  0.0674  -0.0888 15  GLU B CG  
1866 C CD  . GLU B 39  ? 0.6800 0.6955 0.6782 0.0561  0.0726  -0.1163 15  GLU B CD  
1867 O OE1 . GLU B 39  ? 0.6394 0.6759 0.6371 0.0609  0.0805  -0.1210 15  GLU B OE1 
1868 O OE2 . GLU B 39  ? 0.6057 0.6211 0.6018 0.0541  0.0689  -0.1341 15  GLU B OE2 
1869 N N   . GLY B 40  ? 0.3224 0.3005 0.3168 0.0422  0.0585  -0.0334 16  GLY B N   
1870 C CA  . GLY B 40  ? 0.2958 0.2718 0.3050 0.0426  0.0570  -0.0178 16  GLY B CA  
1871 C C   . GLY B 40  ? 0.3374 0.3294 0.3578 0.0471  0.0629  -0.0149 16  GLY B C   
1872 O O   . GLY B 40  ? 0.2835 0.2894 0.2962 0.0485  0.0689  -0.0225 16  GLY B O   
1873 N N   . ASN B 41  ? 0.2913 0.2854 0.3305 0.0497  0.0614  -0.0022 17  ASN B N   
1874 C CA  . ASN B 41  ? 0.2602 0.2725 0.3123 0.0536  0.0656  0.0038  17  ASN B CA  
1875 C C   . ASN B 41  ? 0.3473 0.3686 0.4062 0.0510  0.0597  0.0217  17  ASN B C   
1876 O O   . ASN B 41  ? 0.2576 0.2735 0.3313 0.0544  0.0562  0.0306  17  ASN B O   
1877 C CB  . ASN B 41  ? 0.3221 0.3341 0.4020 0.0649  0.0721  -0.0045 17  ASN B CB  
1878 C CG  . ASN B 41  ? 0.3860 0.4196 0.4779 0.0698  0.0779  -0.0013 17  ASN B CG  
1879 O OD1 . ASN B 41  ? 0.3887 0.4360 0.4871 0.0686  0.0748  0.0145  17  ASN B OD1 
1880 N ND2 . ASN B 41  ? 0.4709 0.5123 0.5660 0.0752  0.0863  -0.0176 17  ASN B ND2 
1881 N N   . VAL B 42  ? 0.2712 0.3092 0.3213 0.0447  0.0586  0.0269  18  VAL B N   
1882 C CA  . VAL B 42  ? 0.2473 0.3014 0.3017 0.0408  0.0523  0.0392  18  VAL B CA  
1883 C C   . VAL B 42  ? 0.2959 0.3756 0.3637 0.0424  0.0550  0.0438  18  VAL B C   
1884 O O   . VAL B 42  ? 0.2922 0.3785 0.3535 0.0373  0.0589  0.0384  18  VAL B O   
1885 C CB  . VAL B 42  ? 0.2805 0.3320 0.3153 0.0294  0.0472  0.0370  18  VAL B CB  
1886 C CG1 . VAL B 42  ? 0.2716 0.3482 0.3118 0.0246  0.0416  0.0437  18  VAL B CG1 
1887 C CG2 . VAL B 42  ? 0.2356 0.2659 0.2596 0.0285  0.0438  0.0346  18  VAL B CG2 
1888 N N   . ASN B 43  ? 0.2945 0.3913 0.3829 0.0493  0.0529  0.0559  19  ASN B N   
1889 C CA  . ASN B 43  ? 0.2649 0.3904 0.3697 0.0519  0.0547  0.0616  19  ASN B CA  
1890 C C   . ASN B 43  ? 0.2608 0.3833 0.3710 0.0567  0.0644  0.0519  19  ASN B C   
1891 O O   . ASN B 43  ? 0.2843 0.4268 0.3982 0.0537  0.0675  0.0512  19  ASN B O   
1892 C CB  . ASN B 43  ? 0.2596 0.4079 0.3557 0.0400  0.0494  0.0611  19  ASN B CB  
1893 C CG  . ASN B 43  ? 0.2984 0.4744 0.4013 0.0396  0.0406  0.0729  19  ASN B CG  
1894 O OD1 . ASN B 43  ? 0.2167 0.3872 0.3182 0.0432  0.0368  0.0811  19  ASN B OD1 
1895 N ND2 . ASN B 43  ? 0.2455 0.4553 0.3556 0.0344  0.0374  0.0735  19  ASN B ND2 
1896 N N   . GLY B 44  ? 0.2654 0.3656 0.3772 0.0636  0.0696  0.0429  20  GLY B N   
1897 C CA  . GLY B 44  ? 0.2593 0.3614 0.3757 0.0692  0.0794  0.0306  20  GLY B CA  
1898 C C   . GLY B 44  ? 0.3435 0.4398 0.4331 0.0615  0.0831  0.0189  20  GLY B C   
1899 O O   . GLY B 44  ? 0.3583 0.4602 0.4483 0.0664  0.0916  0.0073  20  GLY B O   
1900 N N   . HIS B 45  ? 0.2964 0.3847 0.3646 0.0503  0.0774  0.0218  21  HIS B N   
1901 C CA  . HIS B 45  ? 0.3553 0.4411 0.4017 0.0433  0.0808  0.0164  21  HIS B CA  
1902 C C   . HIS B 45  ? 0.3116 0.3762 0.3427 0.0446  0.0792  0.0070  21  HIS B C   
1903 O O   . HIS B 45  ? 0.2962 0.3444 0.3218 0.0412  0.0719  0.0097  21  HIS B O   
1904 C CB  . HIS B 45  ? 0.3295 0.4189 0.3682 0.0308  0.0765  0.0249  21  HIS B CB  
1905 C CG  . HIS B 45  ? 0.4013 0.4920 0.4258 0.0243  0.0814  0.0255  21  HIS B CG  
1906 N ND1 . HIS B 45  ? 0.4092 0.5210 0.4391 0.0227  0.0896  0.0293  21  HIS B ND1 
1907 C CD2 . HIS B 45  ? 0.4763 0.5527 0.4837 0.0194  0.0795  0.0260  21  HIS B CD2 
1908 C CE1 . HIS B 45  ? 0.4512 0.5622 0.4681 0.0171  0.0928  0.0340  21  HIS B CE1 
1909 N NE2 . HIS B 45  ? 0.3976 0.4871 0.4010 0.0154  0.0865  0.0321  21  HIS B NE2 
1910 N N   . HIS B 46  ? 0.2977 0.3671 0.3223 0.0492  0.0861  -0.0052 22  HIS B N   
1911 C CA  . HIS B 46  ? 0.3520 0.4077 0.3628 0.0500  0.0844  -0.0170 22  HIS B CA  
1912 C C   . HIS B 46  ? 0.3660 0.4218 0.3520 0.0412  0.0820  -0.0107 22  HIS B C   
1913 O O   . HIS B 46  ? 0.3232 0.3942 0.3037 0.0363  0.0859  -0.0009 22  HIS B O   
1914 C CB  . HIS B 46  ? 0.3575 0.4253 0.3725 0.0588  0.0926  -0.0364 22  HIS B CB  
1915 C CG  . HIS B 46  ? 0.4759 0.5376 0.4767 0.0588  0.0908  -0.0523 22  HIS B CG  
1916 N ND1 . HIS B 46  ? 0.5642 0.6461 0.5410 0.0565  0.0939  -0.0571 22  HIS B ND1 
1917 C CD2 . HIS B 46  ? 0.4378 0.4794 0.4469 0.0607  0.0862  -0.0639 22  HIS B CD2 
1918 C CE1 . HIS B 46  ? 0.5127 0.5890 0.4817 0.0571  0.0905  -0.0727 22  HIS B CE1 
1919 N NE2 . HIS B 46  ? 0.4905 0.5408 0.4801 0.0591  0.0859  -0.0781 22  HIS B NE2 
1920 N N   . PHE B 47  ? 0.3074 0.3467 0.2824 0.0392  0.0761  -0.0148 23  PHE B N   
1921 C CA  . PHE B 47  ? 0.3299 0.3694 0.2848 0.0326  0.0737  -0.0077 23  PHE B CA  
1922 C C   . PHE B 47  ? 0.3567 0.3868 0.3009 0.0341  0.0693  -0.0192 23  PHE B C   
1923 O O   . PHE B 47  ? 0.3016 0.3179 0.2568 0.0377  0.0664  -0.0299 23  PHE B O   
1924 C CB  . PHE B 47  ? 0.3373 0.3652 0.2948 0.0244  0.0682  0.0069  23  PHE B CB  
1925 C CG  . PHE B 47  ? 0.2632 0.2740 0.2300 0.0245  0.0613  0.0058  23  PHE B CG  
1926 C CD1 . PHE B 47  ? 0.3031 0.3182 0.2872 0.0270  0.0612  0.0085  23  PHE B CD1 
1927 C CD2 . PHE B 47  ? 0.3062 0.3010 0.2653 0.0227  0.0551  0.0040  23  PHE B CD2 
1928 C CE1 . PHE B 47  ? 0.2634 0.2693 0.2561 0.0277  0.0552  0.0114  23  PHE B CE1 
1929 C CE2 . PHE B 47  ? 0.3463 0.3300 0.3143 0.0229  0.0496  0.0052  23  PHE B CE2 
1930 C CZ  . PHE B 47  ? 0.2999 0.2901 0.2842 0.0254  0.0498  0.0098  23  PHE B CZ  
1931 N N   . VAL B 48  ? 0.3331 0.3730 0.2586 0.0312  0.0688  -0.0152 24  VAL B N   
1932 C CA  . VAL B 48  ? 0.2821 0.3168 0.1962 0.0311  0.0631  -0.0232 24  VAL B CA  
1933 C C   . VAL B 48  ? 0.3068 0.3362 0.2113 0.0251  0.0587  -0.0054 24  VAL B C   
1934 O O   . VAL B 48  ? 0.3119 0.3543 0.2126 0.0225  0.0628  0.0100  24  VAL B O   
1935 C CB  . VAL B 48  ? 0.3442 0.4059 0.2460 0.0358  0.0669  -0.0391 24  VAL B CB  
1936 C CG1 . VAL B 48  ? 0.3475 0.4088 0.2379 0.0346  0.0598  -0.0472 24  VAL B CG1 
1937 C CG2 . VAL B 48  ? 0.3501 0.4157 0.2678 0.0425  0.0722  -0.0608 24  VAL B CG2 
1938 N N   . ILE B 49  ? 0.2952 0.3059 0.1995 0.0230  0.0513  -0.0068 25  ILE B N   
1939 C CA  . ILE B 49  ? 0.2521 0.2552 0.1523 0.0184  0.0471  0.0079  25  ILE B CA  
1940 C C   . ILE B 49  ? 0.2979 0.3009 0.1883 0.0195  0.0409  0.0013  25  ILE B C   
1941 O O   . ILE B 49  ? 0.3041 0.2957 0.1994 0.0204  0.0370  -0.0123 25  ILE B O   
1942 C CB  . ILE B 49  ? 0.3065 0.2885 0.2202 0.0141  0.0440  0.0134  25  ILE B CB  
1943 C CG1 . ILE B 49  ? 0.2571 0.2438 0.1821 0.0124  0.0491  0.0180  25  ILE B CG1 
1944 C CG2 . ILE B 49  ? 0.3020 0.2757 0.2160 0.0100  0.0406  0.0247  25  ILE B CG2 
1945 C CD1 . ILE B 49  ? 0.2605 0.2354 0.1984 0.0087  0.0456  0.0189  25  ILE B CD1 
1946 N N   . ASP B 50  ? 0.3212 0.3386 0.2008 0.0192  0.0401  0.0129  26  ASP B N   
1947 C CA  . ASP B 50  ? 0.2955 0.3176 0.1665 0.0202  0.0335  0.0094  26  ASP B CA  
1948 C C   . ASP B 50  ? 0.3160 0.3191 0.1945 0.0172  0.0290  0.0229  26  ASP B C   
1949 O O   . ASP B 50  ? 0.2974 0.2935 0.1850 0.0148  0.0319  0.0386  26  ASP B O   
1950 C CB  . ASP B 50  ? 0.4017 0.4595 0.2562 0.0232  0.0349  0.0152  26  ASP B CB  
1951 C CG  . ASP B 50  ? 0.4485 0.5309 0.2942 0.0267  0.0384  -0.0060 26  ASP B CG  
1952 O OD1 . ASP B 50  ? 0.4151 0.4820 0.2714 0.0272  0.0396  -0.0248 26  ASP B OD1 
1953 O OD2 . ASP B 50  ? 0.4215 0.5411 0.2518 0.0295  0.0402  -0.0038 26  ASP B OD2 
1954 N N   . GLY B 51  ? 0.3142 0.3106 0.1922 0.0172  0.0222  0.0152  27  GLY B N   
1955 C CA  . GLY B 51  ? 0.3377 0.3194 0.2236 0.0155  0.0181  0.0253  27  GLY B CA  
1956 C C   . GLY B 51  ? 0.3308 0.3265 0.2094 0.0178  0.0121  0.0270  27  GLY B C   
1957 O O   . GLY B 51  ? 0.3068 0.3162 0.1770 0.0188  0.0086  0.0123  27  GLY B O   
1958 N N   . ASP B 52  ? 0.2756 0.2693 0.1610 0.0186  0.0108  0.0445  28  ASP B N   
1959 C CA  . ASP B 52  ? 0.2673 0.2753 0.1496 0.0216  0.0046  0.0508  28  ASP B CA  
1960 C C   . ASP B 52  ? 0.3380 0.3240 0.2381 0.0210  0.0029  0.0575  28  ASP B C   
1961 O O   . ASP B 52  ? 0.3166 0.2910 0.2315 0.0207  0.0073  0.0710  28  ASP B O   
1962 C CB  . ASP B 52  ? 0.2829 0.3208 0.1581 0.0256  0.0063  0.0718  28  ASP B CB  
1963 C CG  . ASP B 52  ? 0.4484 0.5128 0.3161 0.0296  -0.0012 0.0765  28  ASP B CG  
1964 O OD1 . ASP B 52  ? 0.7550 0.8394 0.6249 0.0338  -0.0007 0.1019  28  ASP B OD1 
1965 O OD2 . ASP B 52  ? 0.5710 0.6380 0.4337 0.0285  -0.0076 0.0570  28  ASP B OD2 
1966 N N   . GLY B 53  ? 0.3142 0.2954 0.2162 0.0206  -0.0029 0.0466  29  GLY B N   
1967 C CA  . GLY B 53  ? 0.3370 0.3000 0.2560 0.0204  -0.0037 0.0488  29  GLY B CA  
1968 C C   . GLY B 53  ? 0.3677 0.3392 0.2889 0.0225  -0.0105 0.0472  29  GLY B C   
1969 O O   . GLY B 53  ? 0.3062 0.2990 0.2159 0.0237  -0.0157 0.0436  29  GLY B O   
1970 N N   . THR B 54  ? 0.2917 0.2493 0.2294 0.0231  -0.0104 0.0482  30  THR B N   
1971 C CA  . THR B 54  ? 0.2816 0.2457 0.2258 0.0251  -0.0160 0.0462  30  THR B CA  
1972 C C   . THR B 54  ? 0.3163 0.2639 0.2729 0.0226  -0.0138 0.0359  30  THR B C   
1973 O O   . THR B 54  ? 0.3137 0.2475 0.2774 0.0208  -0.0083 0.0337  30  THR B O   
1974 C CB  . THR B 54  ? 0.3715 0.3455 0.3281 0.0319  -0.0177 0.0654  30  THR B CB  
1975 O OG1 . THR B 54  ? 0.3638 0.3192 0.3408 0.0333  -0.0113 0.0736  30  THR B OG1 
1976 C CG2 . THR B 54  ? 0.3453 0.3450 0.2886 0.0352  -0.0201 0.0796  30  THR B CG2 
1977 N N   . GLY B 55  ? 0.2785 0.2322 0.2389 0.0223  -0.0180 0.0296  31  GLY B N   
1978 C CA  . GLY B 55  ? 0.2703 0.2155 0.2405 0.0199  -0.0153 0.0205  31  GLY B CA  
1979 C C   . GLY B 55  ? 0.2983 0.2537 0.2780 0.0213  -0.0192 0.0186  31  GLY B C   
1980 O O   . GLY B 55  ? 0.2859 0.2553 0.2635 0.0230  -0.0252 0.0220  31  GLY B O   
1981 N N   . LYS B 56  ? 0.2429 0.1956 0.2331 0.0204  -0.0157 0.0121  32  LYS B N   
1982 C CA  . LYS B 56  ? 0.2401 0.2039 0.2422 0.0217  -0.0175 0.0096  32  LYS B CA  
1983 C C   . LYS B 56  ? 0.2819 0.2494 0.2818 0.0153  -0.0156 0.0024  32  LYS B C   
1984 O O   . LYS B 56  ? 0.2376 0.2058 0.2410 0.0145  -0.0102 -0.0021 32  LYS B O   
1985 C CB  . LYS B 56  ? 0.2947 0.2568 0.3155 0.0276  -0.0136 0.0093  32  LYS B CB  
1986 C CG  . LYS B 56  ? 0.3224 0.2816 0.3531 0.0348  -0.0154 0.0219  32  LYS B CG  
1987 C CD  . LYS B 56  ? 0.4548 0.4161 0.5120 0.0421  -0.0131 0.0225  32  LYS B CD  
1988 C CE  . LYS B 56  ? 0.3383 0.3178 0.4006 0.0456  -0.0194 0.0280  32  LYS B CE  
1989 N NZ  . LYS B 56  ? 0.2842 0.2718 0.3525 0.0527  -0.0247 0.0468  32  LYS B NZ  
1990 N N   . PRO B 57  ? 0.2911 0.2631 0.2873 0.0106  -0.0196 0.0014  33  PRO B N   
1991 C CA  . PRO B 57  ? 0.2201 0.1933 0.2189 0.0045  -0.0166 -0.0008 33  PRO B CA  
1992 C C   . PRO B 57  ? 0.2786 0.2650 0.2892 0.0042  -0.0129 -0.0005 33  PRO B C   
1993 O O   . PRO B 57  ? 0.2691 0.2599 0.2798 0.0015  -0.0079 0.0011  33  PRO B O   
1994 C CB  . PRO B 57  ? 0.2346 0.2104 0.2364 -0.0001 -0.0219 -0.0038 33  PRO B CB  
1995 C CG  . PRO B 57  ? 0.2636 0.2389 0.2540 0.0032  -0.0268 -0.0050 33  PRO B CG  
1996 C CD  . PRO B 57  ? 0.2490 0.2271 0.2405 0.0104  -0.0265 0.0016  33  PRO B CD  
1997 N N   . PHE B 58  ? 0.2387 0.2358 0.2596 0.0076  -0.0148 -0.0010 34  PHE B N   
1998 C CA  . PHE B 58  ? 0.2411 0.2551 0.2737 0.0075  -0.0105 -0.0018 34  PHE B CA  
1999 C C   . PHE B 58  ? 0.2487 0.2661 0.2823 0.0126  -0.0044 -0.0077 34  PHE B C   
2000 O O   . PHE B 58  ? 0.2335 0.2699 0.2740 0.0126  0.0007  -0.0108 34  PHE B O   
2001 C CB  . PHE B 58  ? 0.2499 0.2768 0.2963 0.0090  -0.0148 -0.0011 34  PHE B CB  
2002 C CG  . PHE B 58  ? 0.2267 0.2547 0.2763 0.0023  -0.0209 0.0003  34  PHE B CG  
2003 C CD1 . PHE B 58  ? 0.2457 0.2800 0.3057 -0.0056 -0.0186 0.0030  34  PHE B CD1 
2004 C CD2 . PHE B 58  ? 0.2668 0.2920 0.3116 0.0036  -0.0287 -0.0014 34  PHE B CD2 
2005 C CE1 . PHE B 58  ? 0.2313 0.2648 0.3011 -0.0127 -0.0238 0.0008  34  PHE B CE1 
2006 C CE2 . PHE B 58  ? 0.2899 0.3196 0.3395 -0.0032 -0.0345 -0.0057 34  PHE B CE2 
2007 C CZ  . PHE B 58  ? 0.2922 0.3237 0.3565 -0.0118 -0.0320 -0.0063 34  PHE B CZ  
2008 N N   . GLU B 59  ? 0.2191 0.2212 0.2478 0.0163  -0.0042 -0.0105 35  GLU B N   
2009 C CA  . GLU B 59  ? 0.2563 0.2602 0.2892 0.0191  0.0018  -0.0201 35  GLU B CA  
2010 C C   . GLU B 59  ? 0.2407 0.2413 0.2603 0.0147  0.0043  -0.0218 35  GLU B C   
2011 O O   . GLU B 59  ? 0.2228 0.2301 0.2455 0.0155  0.0089  -0.0325 35  GLU B O   
2012 C CB  . GLU B 59  ? 0.2744 0.2642 0.3194 0.0259  0.0014  -0.0217 35  GLU B CB  
2013 C CG  . GLU B 59  ? 0.3007 0.2967 0.3625 0.0321  -0.0011 -0.0183 35  GLU B CG  
2014 C CD  . GLU B 59  ? 0.3308 0.3152 0.4136 0.0402  0.0007  -0.0186 35  GLU B CD  
2015 O OE1 . GLU B 59  ? 0.2981 0.2679 0.3828 0.0398  0.0038  -0.0218 35  GLU B OE1 
2016 O OE2 . GLU B 59  ? 0.3083 0.2985 0.4090 0.0469  -0.0009 -0.0144 35  GLU B OE2 
2017 N N   . GLY B 60  ? 0.2073 0.1997 0.2149 0.0103  0.0014  -0.0133 36  GLY B N   
2018 C CA  . GLY B 60  ? 0.2001 0.1905 0.1975 0.0072  0.0036  -0.0130 36  GLY B CA  
2019 C C   . GLY B 60  ? 0.2463 0.2217 0.2414 0.0088  0.0042  -0.0175 36  GLY B C   
2020 O O   . GLY B 60  ? 0.2374 0.2179 0.2293 0.0070  0.0072  -0.0227 36  GLY B O   
2021 N N   . LYS B 61  ? 0.2649 0.2250 0.2630 0.0121  0.0014  -0.0141 37  LYS B N   
2022 C CA  . LYS B 61  ? 0.2234 0.1698 0.2250 0.0136  0.0029  -0.0148 37  LYS B CA  
2023 C C   . LYS B 61  ? 0.2427 0.1779 0.2335 0.0137  -0.0006 -0.0039 37  LYS B C   
2024 O O   . LYS B 61  ? 0.2580 0.1957 0.2456 0.0152  -0.0051 0.0019  37  LYS B O   
2025 C CB  . LYS B 61  ? 0.2219 0.1650 0.2445 0.0191  0.0046  -0.0184 37  LYS B CB  
2026 C CG  . LYS B 61  ? 0.2016 0.1589 0.2373 0.0196  0.0091  -0.0343 37  LYS B CG  
2027 C CD  . LYS B 61  ? 0.2111 0.1623 0.2747 0.0259  0.0119  -0.0403 37  LYS B CD  
2028 C CE  . LYS B 61  ? 0.2134 0.1800 0.2913 0.0257  0.0177  -0.0630 37  LYS B CE  
2029 N NZ  . LYS B 61  ? 0.2250 0.1832 0.3378 0.0322  0.0217  -0.0728 37  LYS B NZ  
2030 N N   . GLN B 62  ? 0.2294 0.1565 0.2157 0.0120  0.0015  -0.0026 38  GLN B N   
2031 C CA  . GLN B 62  ? 0.2190 0.1406 0.1950 0.0126  -0.0006 0.0070  38  GLN B CA  
2032 C C   . GLN B 62  ? 0.2719 0.1853 0.2526 0.0119  0.0034  0.0098  38  GLN B C   
2033 O O   . GLN B 62  ? 0.2504 0.1629 0.2373 0.0089  0.0070  0.0015  38  GLN B O   
2034 C CB  . GLN B 62  ? 0.2313 0.1561 0.1925 0.0095  -0.0026 0.0058  38  GLN B CB  
2035 C CG  . GLN B 62  ? 0.2953 0.2197 0.2533 0.0061  0.0009  0.0018  38  GLN B CG  
2036 C CD  . GLN B 62  ? 0.3004 0.2254 0.2508 0.0043  -0.0001 0.0022  38  GLN B CD  
2037 O OE1 . GLN B 62  ? 0.2903 0.2134 0.2343 0.0052  -0.0020 0.0028  38  GLN B OE1 
2038 N NE2 . GLN B 62  ? 0.2850 0.2153 0.2388 0.0022  0.0013  0.0016  38  GLN B NE2 
2039 N N   . SER B 63  ? 0.2456 0.1571 0.2243 0.0144  0.0029  0.0221  39  SER B N   
2040 C CA  . SER B 63  ? 0.2755 0.1813 0.2596 0.0132  0.0071  0.0289  39  SER B CA  
2041 C C   . SER B 63  ? 0.3449 0.2582 0.3103 0.0135  0.0062  0.0372  39  SER B C   
2042 O O   . SER B 63  ? 0.3371 0.2609 0.2905 0.0160  0.0018  0.0398  39  SER B O   
2043 C CB  . SER B 63  ? 0.2806 0.1799 0.2887 0.0168  0.0095  0.0402  39  SER B CB  
2044 O OG  . SER B 63  ? 0.3869 0.2811 0.4149 0.0180  0.0104  0.0299  39  SER B OG  
2045 N N   . MET B 64  ? 0.2709 0.1822 0.2359 0.0109  0.0106  0.0398  40  MET B N   
2046 C CA  . MET B 64  ? 0.2681 0.1900 0.2158 0.0114  0.0110  0.0447  40  MET B CA  
2047 C C   . MET B 64  ? 0.3325 0.2546 0.2888 0.0102  0.0169  0.0569  40  MET B C   
2048 O O   . MET B 64  ? 0.3214 0.2333 0.2934 0.0063  0.0206  0.0533  40  MET B O   
2049 C CB  . MET B 64  ? 0.3241 0.2463 0.2602 0.0089  0.0106  0.0309  40  MET B CB  
2050 C CG  . MET B 64  ? 0.4605 0.3918 0.3844 0.0092  0.0131  0.0313  40  MET B CG  
2051 S SD  . MET B 64  ? 0.3571 0.2901 0.2721 0.0092  0.0109  0.0158  40  MET B SD  
2052 C CE  . MET B 64  ? 0.4637 0.3977 0.3789 0.0100  0.0041  0.0115  40  MET B CE  
2053 N N   . ASP B 65  ? 0.3153 0.2527 0.2628 0.0131  0.0178  0.0711  41  ASP B N   
2054 C CA  . ASP B 65  ? 0.3445 0.2878 0.2971 0.0117  0.0242  0.0846  41  ASP B CA  
2055 C C   . ASP B 65  ? 0.3569 0.3111 0.2904 0.0106  0.0260  0.0747  41  ASP B C   
2056 O O   . ASP B 65  ? 0.3361 0.3063 0.2503 0.0137  0.0232  0.0693  41  ASP B O   
2057 C CB  . ASP B 65  ? 0.3206 0.2818 0.2751 0.0163  0.0253  0.1094  41  ASP B CB  
2058 C CG  . ASP B 65  ? 0.4599 0.4097 0.4408 0.0186  0.0248  0.1230  41  ASP B CG  
2059 O OD1 . ASP B 65  ? 0.4068 0.3356 0.4141 0.0148  0.0286  0.1203  41  ASP B OD1 
2060 O OD2 . ASP B 65  ? 0.5510 0.5148 0.5285 0.0243  0.0206  0.1352  41  ASP B OD2 
2061 N N   . LEU B 66  ? 0.3042 0.2518 0.2460 0.0063  0.0308  0.0710  42  LEU B N   
2062 C CA  . LEU B 66  ? 0.2526 0.2096 0.1818 0.0061  0.0333  0.0619  42  LEU B CA  
2063 C C   . LEU B 66  ? 0.2905 0.2625 0.2221 0.0054  0.0405  0.0763  42  LEU B C   
2064 O O   . LEU B 66  ? 0.3004 0.2671 0.2522 0.0019  0.0445  0.0900  42  LEU B O   
2065 C CB  . LEU B 66  ? 0.3533 0.2974 0.2901 0.0024  0.0328  0.0479  42  LEU B CB  
2066 C CG  . LEU B 66  ? 0.3409 0.2754 0.2748 0.0033  0.0267  0.0361  42  LEU B CG  
2067 C CD1 . LEU B 66  ? 0.2723 0.1988 0.2189 -0.0008 0.0263  0.0283  42  LEU B CD1 
2068 C CD2 . LEU B 66  ? 0.2998 0.2402 0.2199 0.0065  0.0249  0.0262  42  LEU B CD2 
2069 N N   . GLU B 67  ? 0.3175 0.3096 0.2321 0.0085  0.0429  0.0726  43  GLU B N   
2070 C CA  . GLU B 67  ? 0.3257 0.3369 0.2420 0.0079  0.0507  0.0858  43  GLU B CA  
2071 C C   . GLU B 67  ? 0.3676 0.3880 0.2752 0.0094  0.0539  0.0700  43  GLU B C   
2072 O O   . GLU B 67  ? 0.3474 0.3741 0.2407 0.0136  0.0511  0.0535  43  GLU B O   
2073 C CB  . GLU B 67  ? 0.3289 0.3682 0.2342 0.0120  0.0524  0.1043  43  GLU B CB  
2074 C CG  . GLU B 67  ? 0.4038 0.4682 0.3111 0.0115  0.0617  0.1210  43  GLU B CG  
2075 C CD  . GLU B 67  ? 0.5527 0.6511 0.4510 0.0156  0.0638  0.1451  43  GLU B CD  
2076 O OE1 . GLU B 67  ? 0.5530 0.6567 0.4423 0.0193  0.0567  0.1454  43  GLU B OE1 
2077 O OE2 . GLU B 67  ? 0.5584 0.6760 0.4649 0.0144  0.0692  0.1574  43  GLU B OE2 
2078 N N   . VAL B 68  ? 0.3807 0.4011 0.3016 0.0057  0.0596  0.0737  44  VAL B N   
2079 C CA  . VAL B 68  ? 0.3383 0.3700 0.2556 0.0079  0.0638  0.0619  44  VAL B CA  
2080 C C   . VAL B 68  ? 0.3961 0.4609 0.2988 0.0124  0.0700  0.0668  44  VAL B C   
2081 O O   . VAL B 68  ? 0.3468 0.4287 0.2535 0.0105  0.0759  0.0874  44  VAL B O   
2082 C CB  . VAL B 68  ? 0.3113 0.3377 0.2488 0.0023  0.0676  0.0655  44  VAL B CB  
2083 C CG1 . VAL B 68  ? 0.3555 0.3957 0.2921 0.0060  0.0720  0.0546  44  VAL B CG1 
2084 C CG2 . VAL B 68  ? 0.3376 0.3396 0.2881 -0.0022 0.0612  0.0586  44  VAL B CG2 
2085 N N   . LYS B 69  ? 0.3422 0.4188 0.2304 0.0183  0.0692  0.0475  45  LYS B N   
2086 C CA  . LYS B 69  ? 0.3260 0.4406 0.1984 0.0232  0.0748  0.0460  45  LYS B CA  
2087 C C   . LYS B 69  ? 0.3340 0.4651 0.2112 0.0257  0.0835  0.0378  45  LYS B C   
2088 O O   . LYS B 69  ? 0.3555 0.5226 0.2241 0.0279  0.0912  0.0446  45  LYS B O   
2089 C CB  . LYS B 69  ? 0.3472 0.4703 0.2040 0.0279  0.0692  0.0248  45  LYS B CB  
2090 C CG  . LYS B 69  ? 0.3593 0.4748 0.2097 0.0264  0.0608  0.0335  45  LYS B CG  
2091 C CD  . LYS B 69  ? 0.3927 0.5362 0.2356 0.0264  0.0634  0.0613  45  LYS B CD  
2092 C CE  . LYS B 69  ? 0.6219 0.7594 0.4621 0.0263  0.0551  0.0714  45  LYS B CE  
2093 N NZ  . LYS B 69  ? 0.6607 0.8173 0.4836 0.0300  0.0486  0.0500  45  LYS B NZ  
2094 N N   . GLU B 70  ? 0.3123 0.4218 0.2041 0.0259  0.0828  0.0250  46  GLU B N   
2095 C CA  . GLU B 70  ? 0.3476 0.4710 0.2486 0.0291  0.0906  0.0176  46  GLU B CA  
2096 C C   . GLU B 70  ? 0.3431 0.4424 0.2649 0.0251  0.0886  0.0221  46  GLU B C   
2097 O O   . GLU B 70  ? 0.3382 0.4104 0.2652 0.0228  0.0807  0.0196  46  GLU B O   
2098 C CB  . GLU B 70  ? 0.3975 0.5275 0.2972 0.0372  0.0917  -0.0105 46  GLU B CB  
2099 C CG  . GLU B 70  ? 0.4623 0.6142 0.3428 0.0407  0.0906  -0.0241 46  GLU B CG  
2100 C CD  . GLU B 70  ? 0.6535 0.8161 0.5399 0.0483  0.0941  -0.0557 46  GLU B CD  
2101 O OE1 . GLU B 70  ? 0.5552 0.7322 0.4305 0.0507  0.0916  -0.0750 46  GLU B OE1 
2102 O OE2 . GLU B 70  ? 0.6129 0.7696 0.5183 0.0520  0.0993  -0.0622 46  GLU B OE2 
2103 N N   . GLY B 71  ? 0.3020 0.4160 0.2357 0.0243  0.0958  0.0283  47  GLY B N   
2104 C CA  . GLY B 71  ? 0.3409 0.4405 0.2947 0.0209  0.0936  0.0306  47  GLY B CA  
2105 C C   . GLY B 71  ? 0.3473 0.4357 0.3116 0.0106  0.0908  0.0468  47  GLY B C   
2106 O O   . GLY B 71  ? 0.3640 0.4438 0.3442 0.0069  0.0874  0.0457  47  GLY B O   
2107 N N   . GLY B 72  ? 0.3012 0.3916 0.2602 0.0060  0.0920  0.0612  48  GLY B N   
2108 C CA  . GLY B 72  ? 0.2885 0.3684 0.2652 -0.0038 0.0912  0.0757  48  GLY B CA  
2109 C C   . GLY B 72  ? 0.3552 0.4550 0.3503 -0.0090 0.0999  0.0877  48  GLY B C   
2110 O O   . GLY B 72  ? 0.3571 0.4836 0.3459 -0.0046 0.1081  0.0912  48  GLY B O   
2111 N N   . PRO B 73  ? 0.2924 0.3823 0.3128 -0.0188 0.0987  0.0922  49  PRO B N   
2112 C CA  . PRO B 73  ? 0.2982 0.3628 0.3294 -0.0245 0.0898  0.0839  49  PRO B CA  
2113 C C   . PRO B 73  ? 0.3349 0.3961 0.3619 -0.0208 0.0828  0.0653  49  PRO B C   
2114 O O   . PRO B 73  ? 0.2949 0.3727 0.3273 -0.0186 0.0853  0.0616  49  PRO B O   
2115 C CB  . PRO B 73  ? 0.3373 0.4030 0.4017 -0.0365 0.0935  0.0931  49  PRO B CB  
2116 C CG  . PRO B 73  ? 0.3882 0.4814 0.4600 -0.0367 0.1020  0.0995  49  PRO B CG  
2117 C CD  . PRO B 73  ? 0.2883 0.3973 0.3320 -0.0257 0.1071  0.1047  49  PRO B CD  
2118 N N   . LEU B 74  ? 0.2984 0.3412 0.3175 -0.0195 0.0744  0.0557  50  LEU B N   
2119 C CA  . LEU B 74  ? 0.3582 0.4018 0.3746 -0.0154 0.0683  0.0433  50  LEU B CA  
2120 C C   . LEU B 74  ? 0.2795 0.3362 0.3175 -0.0227 0.0665  0.0395  50  LEU B C   
2121 O O   . LEU B 74  ? 0.2684 0.3214 0.3227 -0.0325 0.0655  0.0385  50  LEU B O   
2122 C CB  . LEU B 74  ? 0.3104 0.3355 0.3157 -0.0136 0.0605  0.0366  50  LEU B CB  
2123 C CG  . LEU B 74  ? 0.3604 0.3752 0.3454 -0.0066 0.0607  0.0374  50  LEU B CG  
2124 C CD1 . LEU B 74  ? 0.3049 0.3029 0.2826 -0.0058 0.0532  0.0314  50  LEU B CD1 
2125 C CD2 . LEU B 74  ? 0.2954 0.3208 0.2726 0.0024  0.0645  0.0332  50  LEU B CD2 
2126 N N   . PRO B 75  ? 0.3162 0.3902 0.3581 -0.0181 0.0660  0.0365  51  PRO B N   
2127 C CA  . PRO B 75  ? 0.3031 0.3970 0.3655 -0.0248 0.0633  0.0326  51  PRO B CA  
2128 C C   . PRO B 75  ? 0.2897 0.3877 0.3508 -0.0248 0.0537  0.0240  51  PRO B C   
2129 O O   . PRO B 75  ? 0.3272 0.4499 0.4010 -0.0270 0.0499  0.0206  51  PRO B O   
2130 C CB  . PRO B 75  ? 0.2686 0.3834 0.3363 -0.0179 0.0684  0.0368  51  PRO B CB  
2131 C CG  . PRO B 75  ? 0.2884 0.3917 0.3383 -0.0051 0.0688  0.0363  51  PRO B CG  
2132 C CD  . PRO B 75  ? 0.2513 0.3311 0.2840 -0.0064 0.0692  0.0367  51  PRO B CD  
2133 N N   . PHE B 76  ? 0.2970 0.3760 0.3432 -0.0222 0.0497  0.0214  52  PHE B N   
2134 C CA  . PHE B 76  ? 0.2550 0.3411 0.2984 -0.0220 0.0415  0.0151  52  PHE B CA  
2135 C C   . PHE B 76  ? 0.2948 0.3616 0.3327 -0.0270 0.0390  0.0083  52  PHE B C   
2136 O O   . PHE B 76  ? 0.2931 0.3383 0.3272 -0.0279 0.0429  0.0116  52  PHE B O   
2137 C CB  . PHE B 76  ? 0.2498 0.3369 0.2832 -0.0104 0.0396  0.0215  52  PHE B CB  
2138 C CG  . PHE B 76  ? 0.2572 0.3183 0.2764 -0.0037 0.0429  0.0244  52  PHE B CG  
2139 C CD1 . PHE B 76  ? 0.2461 0.2889 0.2535 -0.0041 0.0395  0.0217  52  PHE B CD1 
2140 C CD2 . PHE B 76  ? 0.2830 0.3416 0.3018 0.0030  0.0494  0.0277  52  PHE B CD2 
2141 C CE1 . PHE B 76  ? 0.3222 0.3450 0.3178 0.0013  0.0417  0.0225  52  PHE B CE1 
2142 C CE2 . PHE B 76  ? 0.3199 0.3600 0.3262 0.0085  0.0520  0.0262  52  PHE B CE2 
2143 C CZ  . PHE B 76  ? 0.2949 0.3174 0.2898 0.0073  0.0476  0.0237  52  PHE B CZ  
2144 N N   . ALA B 77  ? 0.2665 0.3453 0.3046 -0.0294 0.0324  -0.0005 53  ALA B N   
2145 C CA  . ALA B 77  ? 0.2146 0.2797 0.2509 -0.0337 0.0301  -0.0100 53  ALA B CA  
2146 C C   . ALA B 77  ? 0.2965 0.3353 0.3149 -0.0266 0.0309  -0.0026 53  ALA B C   
2147 O O   . ALA B 77  ? 0.2564 0.2968 0.2630 -0.0189 0.0289  0.0034  53  ALA B O   
2148 C CB  . ALA B 77  ? 0.2492 0.3410 0.2864 -0.0360 0.0233  -0.0213 53  ALA B CB  
2149 N N   . PHE B 78  ? 0.2705 0.2871 0.2908 -0.0292 0.0339  -0.0023 54  PHE B N   
2150 C CA  . PHE B 78  ? 0.2690 0.2650 0.2733 -0.0231 0.0339  0.0035  54  PHE B CA  
2151 C C   . PHE B 78  ? 0.2573 0.2557 0.2528 -0.0204 0.0284  -0.0017 54  PHE B C   
2152 O O   . PHE B 78  ? 0.2338 0.2231 0.2164 -0.0141 0.0275  0.0038  54  PHE B O   
2153 C CB  . PHE B 78  ? 0.2245 0.2020 0.2361 -0.0264 0.0370  0.0063  54  PHE B CB  
2154 C CG  . PHE B 78  ? 0.3164 0.2793 0.3115 -0.0198 0.0378  0.0156  54  PHE B CG  
2155 C CD1 . PHE B 78  ? 0.2616 0.2151 0.2476 -0.0168 0.0337  0.0125  54  PHE B CD1 
2156 C CD2 . PHE B 78  ? 0.2790 0.2430 0.2679 -0.0169 0.0427  0.0264  54  PHE B CD2 
2157 C CE1 . PHE B 78  ? 0.2527 0.1971 0.2249 -0.0114 0.0335  0.0193  54  PHE B CE1 
2158 C CE2 . PHE B 78  ? 0.2643 0.2222 0.2374 -0.0112 0.0427  0.0322  54  PHE B CE2 
2159 C CZ  . PHE B 78  ? 0.2724 0.2202 0.2377 -0.0087 0.0376  0.0282  54  PHE B CZ  
2160 N N   . ASP B 79  ? 0.2664 0.2811 0.2702 -0.0253 0.0251  -0.0130 55  ASP B N   
2161 C CA  . ASP B 79  ? 0.2025 0.2248 0.1984 -0.0232 0.0209  -0.0175 55  ASP B CA  
2162 C C   . ASP B 79  ? 0.2331 0.2646 0.2179 -0.0159 0.0190  -0.0058 55  ASP B C   
2163 O O   . ASP B 79  ? 0.2281 0.2586 0.2057 -0.0129 0.0169  -0.0034 55  ASP B O   
2164 C CB  . ASP B 79  ? 0.1987 0.2477 0.2053 -0.0296 0.0180  -0.0340 55  ASP B CB  
2165 C CG  . ASP B 79  ? 0.2604 0.2966 0.2839 -0.0362 0.0199  -0.0491 55  ASP B CG  
2166 O OD1 . ASP B 79  ? 0.2341 0.2447 0.2563 -0.0338 0.0217  -0.0457 55  ASP B OD1 
2167 O OD2 . ASP B 79  ? 0.2521 0.3054 0.2935 -0.0438 0.0196  -0.0648 55  ASP B OD2 
2168 N N   . ILE B 80  ? 0.2339 0.2755 0.2214 -0.0129 0.0200  0.0025  56  ILE B N   
2169 C CA  . ILE B 80  ? 0.2023 0.2517 0.1870 -0.0055 0.0188  0.0149  56  ILE B CA  
2170 C C   . ILE B 80  ? 0.2146 0.2360 0.1929 -0.0005 0.0206  0.0198  56  ILE B C   
2171 O O   . ILE B 80  ? 0.2088 0.2310 0.1884 0.0042  0.0195  0.0283  56  ILE B O   
2172 C CB  . ILE B 80  ? 0.1782 0.2443 0.1720 -0.0016 0.0199  0.0236  56  ILE B CB  
2173 C CG1 . ILE B 80  ? 0.1908 0.2371 0.1861 0.0009  0.0253  0.0244  56  ILE B CG1 
2174 C CG2 . ILE B 80  ? 0.2254 0.3256 0.2266 -0.0071 0.0169  0.0177  56  ILE B CG2 
2175 C CD1 . ILE B 80  ? 0.2064 0.2671 0.2134 0.0076  0.0273  0.0338  56  ILE B CD1 
2176 N N   . LEU B 81  ? 0.1955 0.1953 0.1691 -0.0017 0.0234  0.0153  57  LEU B N   
2177 C CA  . LEU B 81  ? 0.1992 0.1784 0.1662 0.0024  0.0245  0.0168  57  LEU B CA  
2178 C C   . LEU B 81  ? 0.2613 0.2302 0.2221 0.0008  0.0217  0.0137  57  LEU B C   
2179 O O   . LEU B 81  ? 0.2255 0.1823 0.1830 0.0039  0.0212  0.0144  57  LEU B O   
2180 C CB  . LEU B 81  ? 0.2123 0.1816 0.1752 0.0024  0.0286  0.0150  57  LEU B CB  
2181 C CG  . LEU B 81  ? 0.2407 0.2209 0.2101 0.0038  0.0328  0.0172  57  LEU B CG  
2182 C CD1 . LEU B 81  ? 0.2800 0.2557 0.2444 0.0025  0.0375  0.0174  57  LEU B CD1 
2183 C CD2 . LEU B 81  ? 0.1948 0.1765 0.1700 0.0112  0.0341  0.0195  57  LEU B CD2 
2184 N N   . THR B 82  ? 0.2283 0.2027 0.1901 -0.0039 0.0200  0.0082  58  THR B N   
2185 C CA  . THR B 82  ? 0.2511 0.2123 0.2092 -0.0049 0.0187  0.0044  58  THR B CA  
2186 C C   . THR B 82  ? 0.2473 0.2086 0.2023 -0.0025 0.0161  0.0066  58  THR B C   
2187 O O   . THR B 82  ? 0.2375 0.1859 0.1888 -0.0015 0.0150  0.0059  58  THR B O   
2188 C CB  . THR B 82  ? 0.2227 0.1878 0.1888 -0.0101 0.0187  -0.0046 58  THR B CB  
2189 O OG1 . THR B 82  ? 0.2129 0.2016 0.1828 -0.0124 0.0169  -0.0106 58  THR B OG1 
2190 C CG2 . THR B 82  ? 0.2357 0.1957 0.2103 -0.0135 0.0222  -0.0048 58  THR B CG2 
2191 N N   . THR B 83  ? 0.2154 0.1938 0.1738 -0.0016 0.0150  0.0113  59  THR B N   
2192 C CA  . THR B 83  ? 0.2259 0.2044 0.1852 0.0003  0.0135  0.0169  59  THR B CA  
2193 C C   . THR B 83  ? 0.2435 0.2054 0.2066 0.0037  0.0143  0.0218  59  THR B C   
2194 O O   . THR B 83  ? 0.2372 0.1942 0.2046 0.0042  0.0133  0.0247  59  THR B O   
2195 C CB  . THR B 83  ? 0.2010 0.2073 0.1651 0.0006  0.0128  0.0251  59  THR B CB  
2196 O OG1 . THR B 83  ? 0.2274 0.2413 0.1992 0.0040  0.0138  0.0362  59  THR B OG1 
2197 C CG2 . THR B 83  ? 0.2026 0.2325 0.1636 -0.0032 0.0118  0.0147  59  THR B CG2 
2198 N N   . ALA B 84  ? 0.2321 0.1867 0.1959 0.0058  0.0165  0.0209  60  ALA B N   
2199 C CA  . ALA B 84  ? 0.2631 0.2034 0.2319 0.0089  0.0176  0.0191  60  ALA B CA  
2200 C C   . ALA B 84  ? 0.2779 0.2068 0.2360 0.0078  0.0163  0.0100  60  ALA B C   
2201 O O   . ALA B 84  ? 0.3208 0.2418 0.2826 0.0089  0.0156  0.0049  60  ALA B O   
2202 C CB  . ALA B 84  ? 0.2675 0.2091 0.2430 0.0127  0.0212  0.0196  60  ALA B CB  
2203 N N   . PHE B 85  ? 0.2314 0.1613 0.1795 0.0056  0.0160  0.0083  61  PHE B N   
2204 C CA  . PHE B 85  ? 0.2356 0.1595 0.1752 0.0053  0.0144  0.0048  61  PHE B CA  
2205 C C   . PHE B 85  ? 0.2834 0.2058 0.2249 0.0039  0.0108  0.0046  61  PHE B C   
2206 O O   . PHE B 85  ? 0.2687 0.1880 0.2075 0.0046  0.0082  0.0017  61  PHE B O   
2207 C CB  . PHE B 85  ? 0.2657 0.1908 0.2013 0.0039  0.0163  0.0074  61  PHE B CB  
2208 C CG  . PHE B 85  ? 0.2693 0.1989 0.2038 0.0046  0.0206  0.0089  61  PHE B CG  
2209 C CD1 . PHE B 85  ? 0.2912 0.2235 0.2204 0.0079  0.0224  0.0058  61  PHE B CD1 
2210 C CD2 . PHE B 85  ? 0.2841 0.2183 0.2249 0.0017  0.0230  0.0114  61  PHE B CD2 
2211 C CE1 . PHE B 85  ? 0.2989 0.2388 0.2278 0.0091  0.0272  0.0069  61  PHE B CE1 
2212 C CE2 . PHE B 85  ? 0.2730 0.2135 0.2148 0.0020  0.0273  0.0136  61  PHE B CE2 
2213 C CZ  . PHE B 85  ? 0.2996 0.2431 0.2348 0.0061  0.0298  0.0123  61  PHE B CZ  
2214 C C1  . 5SQ B 86  ? 0.2198 0.1651 0.1762 0.0007  0.0091  0.0119  64  5SQ B C1  
2215 C C2  . 5SQ B 86  ? 0.2059 0.1597 0.1809 0.0017  0.0102  0.0273  64  5SQ B C2  
2216 O O3  . 5SQ B 86  ? 0.2302 0.1435 0.2191 0.0020  0.0072  0.0058  64  5SQ B O3  
2217 C C3  . 5SQ B 86  ? 0.2623 0.1840 0.2405 0.0014  0.0067  0.0107  64  5SQ B C3  
2218 C CA3 . 5SQ B 86  ? 0.2967 0.2220 0.2614 0.0027  0.0081  0.0103  64  5SQ B CA3 
2219 N N3  . 5SQ B 86  ? 0.2391 0.1785 0.2035 0.0017  0.0090  0.0163  64  5SQ B N3  
2220 O O2  . 5SQ B 86  ? 0.2262 0.1801 0.2154 0.0023  0.0112  0.0362  64  5SQ B O2  
2221 C CA1 . 5SQ B 86  ? 0.2601 0.1932 0.2093 0.0011  0.0086  0.0060  64  5SQ B CA1 
2222 N N1  . 5SQ B 86  ? 0.2864 0.2155 0.2324 0.0021  0.0107  0.0065  64  5SQ B N1  
2223 C CB1 . 5SQ B 86  ? 0.2440 0.1808 0.1945 -0.0003 0.0091  0.0015  64  5SQ B CB1 
2224 C CG1 . 5SQ B 86  ? 0.2280 0.1534 0.1776 0.0008  0.0088  0.0014  64  5SQ B CG1 
2225 C C2H . 5SQ B 86  ? 0.2083 0.1316 0.1666 0.0001  0.0103  -0.0014 64  5SQ B C2H 
2226 N N2H . 5SQ B 86  ? 0.3289 0.2440 0.2873 0.0023  0.0100  0.0049  64  5SQ B N2H 
2227 N N1H . 5SQ B 86  ? 0.3096 0.2291 0.2532 0.0029  0.0074  0.0049  64  5SQ B N1H 
2228 C C1H . 5SQ B 86  ? 0.2329 0.1486 0.1796 0.0041  0.0078  0.0086  64  5SQ B C1H 
2229 N N2  . 5SQ B 86  ? 0.2909 0.2563 0.2496 -0.0005 0.0098  0.0141  64  5SQ B N2  
2230 C CA2 . 5SQ B 86  ? 0.2510 0.2257 0.2189 0.0005  0.0105  0.0264  64  5SQ B CA2 
2231 C CB2 . 5SQ B 86  ? 0.2615 0.2625 0.2297 -0.0002 0.0111  0.0307  64  5SQ B CB2 
2232 C CG2 . 5SQ B 86  ? 0.2398 0.2656 0.2021 -0.0020 0.0112  0.0223  64  5SQ B CG2 
2233 C CD2 . 5SQ B 86  ? 0.2427 0.2634 0.2011 -0.0039 0.0110  0.0059  64  5SQ B CD2 
2234 C CE2 . 5SQ B 86  ? 0.1867 0.2352 0.1449 -0.0061 0.0113  -0.0042 64  5SQ B CE2 
2235 C CD1 . 5SQ B 86  ? 0.2030 0.2611 0.1680 -0.0013 0.0117  0.0338  64  5SQ B CD1 
2236 C CE1 . 5SQ B 86  ? 0.1822 0.2737 0.1423 -0.0030 0.0115  0.0254  64  5SQ B CE1 
2237 C CZ1 . 5SQ B 86  ? 0.1923 0.2774 0.1494 -0.0058 0.0113  0.0036  64  5SQ B CZ1 
2238 O OH  . 5SQ B 86  ? 0.1954 0.3153 0.1513 -0.0084 0.0111  -0.0107 64  5SQ B OH  
2239 N N   . ASN B 87  ? 0.2091 0.1358 0.1861 -0.0005 0.0045  0.0114  65  ASN B N   
2240 C CA  . ASN B 87  ? 0.2752 0.1986 0.2629 -0.0027 0.0020  0.0082  65  ASN B CA  
2241 C C   . ASN B 87  ? 0.2337 0.1687 0.2250 -0.0045 0.0017  0.0145  65  ASN B C   
2242 O O   . ASN B 87  ? 0.2361 0.1753 0.2178 -0.0038 0.0000  0.0107  65  ASN B O   
2243 C CB  . ASN B 87  ? 0.2333 0.1524 0.2110 -0.0023 -0.0019 -0.0036 65  ASN B CB  
2244 C CG  . ASN B 87  ? 0.2438 0.1639 0.2336 -0.0055 -0.0056 -0.0100 65  ASN B CG  
2245 O OD1 . ASN B 87  ? 0.2418 0.1623 0.2502 -0.0085 -0.0046 -0.0049 65  ASN B OD1 
2246 N ND2 . ASN B 87  ? 0.2112 0.1351 0.1921 -0.0050 -0.0099 -0.0199 65  ASN B ND2 
2247 N N   . ARG B 88  ? 0.2230 0.2066 0.1958 -0.0083 -0.0220 -0.0111 66  ARG B N   
2248 C CA  . ARG B 88  ? 0.2471 0.2264 0.2215 -0.0132 -0.0252 -0.0136 66  ARG B CA  
2249 C C   . ARG B 88  ? 0.2217 0.1857 0.1881 -0.0042 -0.0273 -0.0040 66  ARG B C   
2250 O O   . ARG B 88  ? 0.2464 0.2087 0.2159 -0.0060 -0.0272 -0.0045 66  ARG B O   
2251 C CB  . ARG B 88  ? 0.2191 0.2184 0.1941 -0.0124 -0.0379 -0.0170 66  ARG B CB  
2252 C CG  . ARG B 88  ? 0.2751 0.2818 0.2509 -0.0201 -0.0370 -0.0242 66  ARG B CG  
2253 C CD  . ARG B 88  ? 0.2461 0.2740 0.2317 -0.0350 -0.0306 -0.0427 66  ARG B CD  
2254 N NE  . ARG B 88  ? 0.1871 0.2523 0.1828 -0.0352 -0.0367 -0.0482 66  ARG B NE  
2255 C CZ  . ARG B 88  ? 0.2321 0.3016 0.2413 -0.0403 -0.0285 -0.0504 66  ARG B CZ  
2256 N NH1 . ARG B 88  ? 0.2289 0.2638 0.2396 -0.0468 -0.0116 -0.0473 66  ARG B NH1 
2257 N NH2 . ARG B 88  ? 0.1923 0.3033 0.2126 -0.0351 -0.0350 -0.0526 66  ARG B NH2 
2258 N N   . VAL B 89  ? 0.2369 0.1971 0.1933 0.0068  -0.0288 0.0037  67  VAL B N   
2259 C CA  . VAL B 89  ? 0.2471 0.2064 0.1984 0.0182  -0.0294 0.0129  67  VAL B CA  
2260 C C   . VAL B 89  ? 0.2648 0.2047 0.2183 0.0213  -0.0098 0.0200  67  VAL B C   
2261 O O   . VAL B 89  ? 0.2671 0.2082 0.2232 0.0308  -0.0080 0.0265  67  VAL B O   
2262 C CB  . VAL B 89  ? 0.2637 0.2311 0.1978 0.0324  -0.0342 0.0187  67  VAL B CB  
2263 C CG1 . VAL B 89  ? 0.4008 0.3789 0.3280 0.0508  -0.0337 0.0317  67  VAL B CG1 
2264 C CG2 . VAL B 89  ? 0.2874 0.2678 0.2198 0.0277  -0.0519 0.0061  67  VAL B CG2 
2265 N N   . PHE B 90  ? 0.2374 0.1581 0.1922 0.0133  0.0086  0.0181  68  PHE B N   
2266 C CA  . PHE B 90  ? 0.2663 0.1545 0.2230 0.0131  0.0343  0.0218  68  PHE B CA  
2267 C C   . PHE B 90  ? 0.2898 0.1771 0.2593 -0.0060 0.0358  0.0016  68  PHE B C   
2268 O O   . PHE B 90  ? 0.3178 0.1976 0.2970 -0.0265 0.0483  -0.0152 68  PHE B O   
2269 C CB  . PHE B 90  ? 0.2969 0.1606 0.2512 0.0094  0.0590  0.0277  68  PHE B CB  
2270 C CG  . PHE B 90  ? 0.3147 0.1786 0.2473 0.0344  0.0612  0.0512  68  PHE B CG  
2271 C CD1 . PHE B 90  ? 0.3493 0.1947 0.2655 0.0618  0.0744  0.0748  68  PHE B CD1 
2272 C CD2 . PHE B 90  ? 0.3014 0.1892 0.2267 0.0355  0.0491  0.0500  68  PHE B CD2 
2273 C CE1 . PHE B 90  ? 0.3718 0.2283 0.2617 0.0897  0.0739  0.0972  68  PHE B CE1 
2274 C CE2 . PHE B 90  ? 0.3243 0.2174 0.2228 0.0602  0.0502  0.0688  68  PHE B CE2 
2275 C CZ  . PHE B 90  ? 0.3592 0.2402 0.2388 0.0872  0.0610  0.0923  68  PHE B CZ  
2276 N N   . ALA B 91  ? 0.2667 0.1678 0.2364 0.0004  0.0232  0.0018  69  ALA B N   
2277 C CA  . ALA B 91  ? 0.2878 0.1908 0.2618 -0.0112 0.0251  -0.0144 69  ALA B CA  
2278 C C   . ALA B 91  ? 0.2796 0.1840 0.2533 0.0054  0.0256  -0.0039 69  ALA B C   
2279 O O   . ALA B 91  ? 0.2598 0.1875 0.2363 0.0165  0.0105  0.0084  69  ALA B O   
2280 C CB  . ALA B 91  ? 0.2441 0.1806 0.2195 -0.0225 0.0050  -0.0253 69  ALA B CB  
2281 N N   . LYS B 92  ? 0.2737 0.1561 0.2463 0.0061  0.0446  -0.0115 70  LYS B N   
2282 C CA  . LYS B 92  ? 0.2780 0.1675 0.2537 0.0241  0.0482  -0.0017 70  LYS B CA  
2283 C C   . LYS B 92  ? 0.2966 0.2201 0.2753 0.0153  0.0323  -0.0085 70  LYS B C   
2284 O O   . LYS B 92  ? 0.2802 0.2028 0.2502 0.0021  0.0354  -0.0262 70  LYS B O   
2285 C CB  . LYS B 92  ? 0.3242 0.1722 0.2949 0.0303  0.0786  -0.0088 70  LYS B CB  
2286 C CG  . LYS B 92  ? 0.3381 0.1970 0.3139 0.0523  0.0861  0.0006  70  LYS B CG  
2287 C CD  . LYS B 92  ? 0.4806 0.2923 0.4517 0.0759  0.1187  0.0104  70  LYS B CD  
2288 C CE  . LYS B 92  ? 0.5745 0.3416 0.5349 0.0621  0.1452  -0.0179 70  LYS B CE  
2289 N NZ  . LYS B 92  ? 0.8040 0.5104 0.7580 0.0820  0.1836  -0.0109 70  LYS B NZ  
2290 N N   . TYR B 93  ? 0.2731 0.2280 0.2631 0.0222  0.0174  0.0047  71  TYR B N   
2291 C CA  . TYR B 93  ? 0.2140 0.1933 0.2081 0.0142  0.0098  0.0031  71  TYR B CA  
2292 C C   . TYR B 93  ? 0.2491 0.2434 0.2555 0.0265  0.0216  0.0095  71  TYR B C   
2293 O O   . TYR B 93  ? 0.2610 0.2758 0.2854 0.0402  0.0196  0.0212  71  TYR B O   
2294 C CB  . TYR B 93  ? 0.2667 0.2658 0.2698 0.0073  -0.0088 0.0094  71  TYR B CB  
2295 C CG  . TYR B 93  ? 0.2618 0.2526 0.2515 -0.0036 -0.0176 0.0037  71  TYR B CG  
2296 C CD1 . TYR B 93  ? 0.2353 0.2142 0.2181 -0.0048 -0.0211 -0.0008 71  TYR B CD1 
2297 C CD2 . TYR B 93  ? 0.2310 0.2282 0.2147 -0.0091 -0.0192 0.0056  71  TYR B CD2 
2298 C CE1 . TYR B 93  ? 0.2542 0.2353 0.2290 -0.0110 -0.0286 -0.0054 71  TYR B CE1 
2299 C CE2 . TYR B 93  ? 0.2456 0.2409 0.2165 -0.0113 -0.0263 0.0041  71  TYR B CE2 
2300 C CZ  . TYR B 93  ? 0.2313 0.2221 0.1999 -0.0121 -0.0322 -0.0025 71  TYR B CZ  
2301 O OH  . TYR B 93  ? 0.2635 0.2619 0.2235 -0.0107 -0.0389 -0.0032 71  TYR B OH  
2302 N N   . PRO B 94  ? 0.2584 0.2512 0.2557 0.0245  0.0337  0.0021  72  PRO B N   
2303 C CA  . PRO B 94  ? 0.2814 0.2972 0.2941 0.0358  0.0456  0.0100  72  PRO B CA  
2304 C C   . PRO B 94  ? 0.2861 0.3391 0.3230 0.0271  0.0339  0.0213  72  PRO B C   
2305 O O   . PRO B 94  ? 0.3228 0.3734 0.3559 0.0120  0.0208  0.0213  72  PRO B O   
2306 C CB  . PRO B 94  ? 0.3617 0.3669 0.3504 0.0328  0.0604  -0.0032 72  PRO B CB  
2307 C CG  . PRO B 94  ? 0.3911 0.3899 0.3584 0.0164  0.0465  -0.0127 72  PRO B CG  
2308 C CD  . PRO B 94  ? 0.3569 0.3379 0.3294 0.0126  0.0359  -0.0146 72  PRO B CD  
2309 N N   . ASP B 95  ? 0.2449 0.3326 0.3097 0.0363  0.0416  0.0296  73  ASP B N   
2310 C CA  . ASP B 95  ? 0.2346 0.3616 0.3318 0.0224  0.0317  0.0353  73  ASP B CA  
2311 C C   . ASP B 95  ? 0.2757 0.4008 0.3708 0.0047  0.0413  0.0385  73  ASP B C   
2312 O O   . ASP B 95  ? 0.3198 0.4667 0.4429 -0.0127 0.0390  0.0414  73  ASP B O   
2313 C CB  . ASP B 95  ? 0.2632 0.4439 0.3993 0.0370  0.0348  0.0418  73  ASP B CB  
2314 C CG  . ASP B 95  ? 0.4043 0.5948 0.5444 0.0538  0.0597  0.0465  73  ASP B CG  
2315 O OD1 . ASP B 95  ? 0.3083 0.4772 0.4281 0.0458  0.0742  0.0444  73  ASP B OD1 
2316 O OD2 . ASP B 95  ? 0.4074 0.6308 0.5690 0.0788  0.0657  0.0534  73  ASP B OD2 
2317 N N   . ASN B 96  ? 0.2887 0.3881 0.3497 0.0085  0.0534  0.0374  74  ASN B N   
2318 C CA  . ASN B 96  ? 0.2997 0.3938 0.3468 -0.0013 0.0640  0.0460  74  ASN B CA  
2319 C C   . ASN B 96  ? 0.3408 0.4062 0.3619 -0.0088 0.0511  0.0468  74  ASN B C   
2320 O O   . ASN B 96  ? 0.4163 0.4726 0.4169 -0.0097 0.0607  0.0582  74  ASN B O   
2321 C CB  . ASN B 96  ? 0.3236 0.4163 0.3413 0.0119  0.0836  0.0446  74  ASN B CB  
2322 C CG  . ASN B 96  ? 0.3409 0.4083 0.3173 0.0186  0.0763  0.0273  74  ASN B CG  
2323 O OD1 . ASN B 96  ? 0.4297 0.4826 0.4090 0.0208  0.0671  0.0152  74  ASN B OD1 
2324 N ND2 . ASN B 96  ? 0.4635 0.5296 0.4014 0.0216  0.0820  0.0258  74  ASN B ND2 
2325 N N   . ILE B 97  ? 0.2777 0.3305 0.2975 -0.0101 0.0322  0.0377  75  ILE B N   
2326 C CA  . ILE B 97  ? 0.3055 0.3366 0.3054 -0.0139 0.0204  0.0382  75  ILE B CA  
2327 C C   . ILE B 97  ? 0.2600 0.2882 0.2831 -0.0237 0.0070  0.0351  75  ILE B C   
2328 O O   . ILE B 97  ? 0.2676 0.3076 0.3047 -0.0207 -0.0015 0.0275  75  ILE B O   
2329 C CB  . ILE B 97  ? 0.3258 0.3487 0.2981 -0.0064 0.0122  0.0251  75  ILE B CB  
2330 C CG1 . ILE B 97  ? 0.4482 0.4793 0.3942 0.0010  0.0240  0.0199  75  ILE B CG1 
2331 C CG2 . ILE B 97  ? 0.2964 0.3092 0.2539 -0.0069 0.0000  0.0272  75  ILE B CG2 
2332 C CD1 . ILE B 97  ? 0.3674 0.3970 0.2910 0.0013  0.0168  -0.0013 75  ILE B CD1 
2333 N N   . GLN B 98  ? 0.2510 0.2620 0.2751 -0.0329 0.0076  0.0412  76  GLN B N   
2334 C CA  . GLN B 98  ? 0.2276 0.2337 0.2688 -0.0435 -0.0045 0.0320  76  GLN B CA  
2335 C C   . GLN B 98  ? 0.2462 0.2437 0.2687 -0.0336 -0.0201 0.0240  76  GLN B C   
2336 O O   . GLN B 98  ? 0.2814 0.2668 0.2795 -0.0244 -0.0208 0.0269  76  GLN B O   
2337 C CB  . GLN B 98  ? 0.2930 0.2694 0.3368 -0.0559 0.0057  0.0379  76  GLN B CB  
2338 C CG  . GLN B 98  ? 0.4816 0.4595 0.5410 -0.0663 0.0290  0.0506  76  GLN B CG  
2339 C CD  . GLN B 98  ? 0.7704 0.7107 0.8412 -0.0844 0.0463  0.0548  76  GLN B CD  
2340 O OE1 . GLN B 98  ? 0.6661 0.5634 0.7095 -0.0738 0.0540  0.0670  76  GLN B OE1 
2341 N NE2 . GLN B 98  ? 0.7460 0.7034 0.8593 -0.1114 0.0559  0.0450  76  GLN B NE2 
2342 N N   . ASP B 99  ? 0.2174 0.2281 0.2522 -0.0350 -0.0320 0.0141  77  ASP B N   
2343 C CA  . ASP B 99  ? 0.2627 0.2676 0.2819 -0.0251 -0.0422 0.0090  77  ASP B CA  
2344 C C   . ASP B 99  ? 0.2764 0.2673 0.2919 -0.0308 -0.0502 0.0016  77  ASP B C   
2345 O O   . ASP B 99  ? 0.2869 0.2931 0.3112 -0.0344 -0.0595 -0.0081 77  ASP B O   
2346 C CB  . ASP B 99  ? 0.2268 0.2541 0.2543 -0.0152 -0.0451 0.0084  77  ASP B CB  
2347 C CG  . ASP B 99  ? 0.2586 0.2731 0.2682 -0.0041 -0.0476 0.0080  77  ASP B CG  
2348 O OD1 . ASP B 99  ? 0.2370 0.2352 0.2336 -0.0069 -0.0512 0.0044  77  ASP B OD1 
2349 O OD2 . ASP B 99  ? 0.2190 0.2385 0.2285 0.0091  -0.0422 0.0133  77  ASP B OD2 
2350 N N   . TYR B 100 ? 0.2237 0.1891 0.2239 -0.0285 -0.0461 0.0057  78  TYR B N   
2351 C CA  . TYR B 100 ? 0.2795 0.2221 0.2728 -0.0299 -0.0484 -0.0007 78  TYR B CA  
2352 C C   . TYR B 100 ? 0.2773 0.2292 0.2635 -0.0245 -0.0595 -0.0113 78  TYR B C   
2353 O O   . TYR B 100 ? 0.2822 0.2276 0.2673 -0.0298 -0.0639 -0.0244 78  TYR B O   
2354 C CB  . TYR B 100 ? 0.2403 0.1632 0.2158 -0.0171 -0.0415 0.0108  78  TYR B CB  
2355 C CG  . TYR B 100 ? 0.2582 0.1484 0.2249 -0.0123 -0.0365 0.0091  78  TYR B CG  
2356 C CD1 . TYR B 100 ? 0.2970 0.1512 0.2688 -0.0218 -0.0223 0.0105  78  TYR B CD1 
2357 C CD2 . TYR B 100 ? 0.2650 0.1566 0.2195 0.0019  -0.0413 0.0064  78  TYR B CD2 
2358 C CE1 . TYR B 100 ? 0.3758 0.1884 0.3373 -0.0151 -0.0122 0.0085  78  TYR B CE1 
2359 C CE2 . TYR B 100 ? 0.3048 0.1635 0.2496 0.0114  -0.0332 0.0055  78  TYR B CE2 
2360 C CZ  . TYR B 100 ? 0.3311 0.1466 0.2777 0.0038  -0.0184 0.0061  78  TYR B CZ  
2361 O OH  . TYR B 100 ? 0.3757 0.1476 0.3108 0.0147  -0.0054 0.0042  78  TYR B OH  
2362 N N   . PHE B 101 ? 0.2394 0.2043 0.2188 -0.0147 -0.0612 -0.0070 79  PHE B N   
2363 C CA  . PHE B 101 ? 0.2151 0.1833 0.1830 -0.0065 -0.0654 -0.0111 79  PHE B CA  
2364 C C   . PHE B 101 ? 0.2638 0.2532 0.2336 -0.0046 -0.0731 -0.0155 79  PHE B C   
2365 O O   . PHE B 101 ? 0.2694 0.2629 0.2275 -0.0015 -0.0797 -0.0247 79  PHE B O   
2366 C CB  . PHE B 101 ? 0.2861 0.2561 0.2497 -0.0005 -0.0585 -0.0049 79  PHE B CB  
2367 C CG  . PHE B 101 ? 0.2572 0.2257 0.2205 -0.0012 -0.0553 -0.0033 79  PHE B CG  
2368 C CD1 . PHE B 101 ? 0.2790 0.2443 0.2364 0.0055  -0.0558 -0.0038 79  PHE B CD1 
2369 C CD2 . PHE B 101 ? 0.2120 0.1872 0.1787 -0.0049 -0.0518 -0.0009 79  PHE B CD2 
2370 C CE1 . PHE B 101 ? 0.2416 0.2176 0.1982 0.0114  -0.0547 0.0007  79  PHE B CE1 
2371 C CE2 . PHE B 101 ? 0.2091 0.1945 0.1709 -0.0015 -0.0516 0.0009  79  PHE B CE2 
2372 C CZ  . PHE B 101 ? 0.2693 0.2584 0.2267 0.0079  -0.0541 0.0030  79  PHE B CZ  
2373 N N   . LYS B 102 ? 0.2178 0.2845 0.2188 -0.0484 -0.0026 -0.0259 80  LYS B N   
2374 C CA  . LYS B 102 ? 0.2566 0.3345 0.2638 -0.0454 -0.0073 -0.0321 80  LYS B CA  
2375 C C   . LYS B 102 ? 0.2648 0.3435 0.2756 -0.0610 -0.0135 -0.0284 80  LYS B C   
2376 O O   . LYS B 102 ? 0.3076 0.3806 0.3178 -0.0594 -0.0198 -0.0334 80  LYS B O   
2377 C CB  . LYS B 102 ? 0.2192 0.3332 0.2389 -0.0380 -0.0044 -0.0390 80  LYS B CB  
2378 C CG  . LYS B 102 ? 0.2398 0.3436 0.2585 -0.0201 -0.0030 -0.0456 80  LYS B CG  
2379 C CD  . LYS B 102 ? 0.2208 0.3548 0.2552 -0.0082 -0.0036 -0.0564 80  LYS B CD  
2380 C CE  . LYS B 102 ? 0.1884 0.3082 0.2247 0.0077  -0.0042 -0.0631 80  LYS B CE  
2381 N NZ  . LYS B 102 ? 0.1420 0.2639 0.1739 0.0060  0.0023  -0.0653 80  LYS B NZ  
2382 N N   . GLN B 103 ? 0.1984 0.2833 0.2128 -0.0772 -0.0133 -0.0187 81  GLN B N   
2383 C CA  . GLN B 103 ? 0.2524 0.3312 0.2723 -0.0941 -0.0219 -0.0139 81  GLN B CA  
2384 C C   . GLN B 103 ? 0.2862 0.3203 0.2974 -0.0935 -0.0291 -0.0159 81  GLN B C   
2385 O O   . GLN B 103 ? 0.3081 0.3310 0.3244 -0.1054 -0.0387 -0.0161 81  GLN B O   
2386 C CB  . GLN B 103 ? 0.2627 0.3618 0.2914 -0.1148 -0.0218 0.0010  81  GLN B CB  
2387 C CG  . GLN B 103 ? 0.4209 0.5681 0.4556 -0.1150 -0.0124 0.0032  81  GLN B CG  
2388 C CD  . GLN B 103 ? 0.5936 0.7847 0.6434 -0.1268 -0.0136 0.0042  81  GLN B CD  
2389 O OE1 . GLN B 103 ? 0.7035 0.8930 0.7589 -0.1259 -0.0199 -0.0031 81  GLN B OE1 
2390 N NE2 . GLN B 103 ? 0.6026 0.8387 0.6594 -0.1384 -0.0075 0.0133  81  GLN B NE2 
2391 N N   . SER B 104 ? 0.2535 0.2637 0.2535 -0.0802 -0.0255 -0.0187 82  SER B N   
2392 C CA  A SER B 104 ? 0.2818 0.2555 0.2749 -0.0770 -0.0317 -0.0236 82  SER B CA  
2393 C CA  B SER B 104 ? 0.2819 0.2557 0.2752 -0.0773 -0.0320 -0.0236 82  SER B CA  
2394 C C   . SER B 104 ? 0.3550 0.3247 0.3415 -0.0672 -0.0355 -0.0374 82  SER B C   
2395 O O   . SER B 104 ? 0.2965 0.2420 0.2774 -0.0638 -0.0413 -0.0458 82  SER B O   
2396 C CB  A SER B 104 ? 0.2923 0.2490 0.2773 -0.0668 -0.0261 -0.0207 82  SER B CB  
2397 C CB  B SER B 104 ? 0.2920 0.2469 0.2772 -0.0674 -0.0268 -0.0209 82  SER B CB  
2398 O OG  A SER B 104 ? 0.2595 0.2153 0.2495 -0.0776 -0.0260 -0.0070 82  SER B OG  
2399 O OG  B SER B 104 ? 0.2694 0.2332 0.2472 -0.0525 -0.0192 -0.0257 82  SER B OG  
2400 N N   . PHE B 105 ? 0.2357 0.2302 0.2230 -0.0619 -0.0331 -0.0405 83  PHE B N   
2401 C CA  . PHE B 105 ? 0.2702 0.2643 0.2495 -0.0528 -0.0370 -0.0507 83  PHE B CA  
2402 C C   . PHE B 105 ? 0.2796 0.2889 0.2664 -0.0624 -0.0458 -0.0556 83  PHE B C   
2403 O O   . PHE B 105 ? 0.3097 0.3384 0.3098 -0.0739 -0.0466 -0.0499 83  PHE B O   
2404 C CB  . PHE B 105 ? 0.3132 0.3201 0.2880 -0.0386 -0.0308 -0.0488 83  PHE B CB  
2405 C CG  . PHE B 105 ? 0.3014 0.2914 0.2673 -0.0297 -0.0244 -0.0460 83  PHE B CG  
2406 C CD1 . PHE B 105 ? 0.3057 0.2949 0.2758 -0.0301 -0.0179 -0.0392 83  PHE B CD1 
2407 C CD2 . PHE B 105 ? 0.2610 0.2395 0.2144 -0.0219 -0.0251 -0.0508 83  PHE B CD2 
2408 C CE1 . PHE B 105 ? 0.2971 0.2720 0.2602 -0.0231 -0.0130 -0.0366 83  PHE B CE1 
2409 C CE2 . PHE B 105 ? 0.2662 0.2333 0.2131 -0.0148 -0.0191 -0.0477 83  PHE B CE2 
2410 C CZ  . PHE B 105 ? 0.3065 0.2704 0.2590 -0.0157 -0.0135 -0.0403 83  PHE B CZ  
2411 N N   . PRO B 106 ? 0.3303 0.3354 0.3090 -0.0587 -0.0528 -0.0666 84  PRO B N   
2412 C CA  . PRO B 106 ? 0.2733 0.2686 0.2354 -0.0448 -0.0516 -0.0739 84  PRO B CA  
2413 C C   . PRO B 106 ? 0.3493 0.3162 0.3040 -0.0416 -0.0516 -0.0806 84  PRO B C   
2414 O O   . PRO B 106 ? 0.4227 0.3888 0.3647 -0.0295 -0.0474 -0.0841 84  PRO B O   
2415 C CB  . PRO B 106 ? 0.3049 0.3153 0.2630 -0.0456 -0.0608 -0.0841 84  PRO B CB  
2416 C CG  . PRO B 106 ? 0.3245 0.3325 0.2963 -0.0624 -0.0697 -0.0875 84  PRO B CG  
2417 C CD  . PRO B 106 ? 0.3352 0.3530 0.3215 -0.0697 -0.0632 -0.0728 84  PRO B CD  
2418 N N   . LYS B 107 ? 0.3013 0.2464 0.2648 -0.0515 -0.0568 -0.0816 85  LYS B N   
2419 C CA  . LYS B 107 ? 0.3865 0.3043 0.3451 -0.0449 -0.0591 -0.0909 85  LYS B CA  
2420 C C   . LYS B 107 ? 0.4428 0.3565 0.3961 -0.0344 -0.0482 -0.0824 85  LYS B C   
2421 O O   . LYS B 107 ? 0.4621 0.3691 0.4066 -0.0223 -0.0462 -0.0914 85  LYS B O   
2422 C CB  . LYS B 107 ? 0.3605 0.2519 0.3332 -0.0582 -0.0702 -0.0915 85  LYS B CB  
2423 C CG  . LYS B 107 ? 0.5335 0.4198 0.5104 -0.0661 -0.0844 -0.1071 85  LYS B CG  
2424 C CD  . LYS B 107 ? 0.6202 0.4771 0.6087 -0.0708 -0.0911 -0.1087 85  LYS B CD  
2425 C CE  . LYS B 107 ? 0.7145 0.5706 0.7048 -0.0750 -0.1000 -0.1234 85  LYS B CE  
2426 N NZ  . LYS B 107 ? 0.7281 0.5994 0.7302 -0.0945 -0.1062 -0.1162 85  LYS B NZ  
2427 N N   . GLY B 108 ? 0.3033 0.2254 0.2623 -0.0385 -0.0411 -0.0667 86  GLY B N   
2428 C CA  . GLY B 108 ? 0.3500 0.2716 0.3045 -0.0296 -0.0314 -0.0590 86  GLY B CA  
2429 C C   . GLY B 108 ? 0.2825 0.1848 0.2439 -0.0340 -0.0319 -0.0515 86  GLY B C   
2430 O O   . GLY B 108 ? 0.3222 0.2122 0.2933 -0.0460 -0.0397 -0.0481 86  GLY B O   
2431 N N   . TYR B 109 ? 0.3319 0.2322 0.2890 -0.0250 -0.0248 -0.0474 87  TYR B N   
2432 C CA  . TYR B 109 ? 0.2876 0.1736 0.2506 -0.0278 -0.0252 -0.0382 87  TYR B CA  
2433 C C   . TYR B 109 ? 0.3065 0.1900 0.2637 -0.0144 -0.0194 -0.0400 87  TYR B C   
2434 O O   . TYR B 109 ? 0.2813 0.1766 0.2302 -0.0052 -0.0142 -0.0460 87  TYR B O   
2435 C CB  . TYR B 109 ? 0.2477 0.1489 0.2159 -0.0387 -0.0214 -0.0236 87  TYR B CB  
2436 C CG  . TYR B 109 ? 0.2322 0.1521 0.1957 -0.0317 -0.0115 -0.0208 87  TYR B CG  
2437 C CD1 . TYR B 109 ? 0.2765 0.2133 0.2375 -0.0275 -0.0084 -0.0255 87  TYR B CD1 
2438 C CD2 . TYR B 109 ? 0.2399 0.1588 0.2026 -0.0289 -0.0072 -0.0138 87  TYR B CD2 
2439 C CE1 . TYR B 109 ? 0.2704 0.2188 0.2301 -0.0210 -0.0021 -0.0235 87  TYR B CE1 
2440 C CE2 . TYR B 109 ? 0.2647 0.1980 0.2248 -0.0232 -0.0001 -0.0131 87  TYR B CE2 
2441 C CZ  . TYR B 109 ? 0.2759 0.2216 0.2352 -0.0193 0.0018  -0.0182 87  TYR B CZ  
2442 O OH  . TYR B 109 ? 0.2388 0.1933 0.1984 -0.0138 0.0061  -0.0179 87  TYR B OH  
2443 N N   . SER B 110 ? 0.2738 0.1445 0.2364 -0.0143 -0.0208 -0.0328 88  SER B N   
2444 C CA  A SER B 110 ? 0.3141 0.1865 0.2737 -0.0027 -0.0153 -0.0330 88  SER B CA  
2445 C CA  B SER B 110 ? 0.3144 0.1858 0.2743 -0.0026 -0.0157 -0.0332 88  SER B CA  
2446 C C   . SER B 110 ? 0.2837 0.1577 0.2476 -0.0078 -0.0133 -0.0180 88  SER B C   
2447 O O   . SER B 110 ? 0.3033 0.1734 0.2728 -0.0195 -0.0178 -0.0077 88  SER B O   
2448 C CB  A SER B 110 ? 0.3195 0.1755 0.2818 0.0085  -0.0211 -0.0454 88  SER B CB  
2449 C CB  B SER B 110 ? 0.3225 0.1756 0.2862 0.0078  -0.0224 -0.0450 88  SER B CB  
2450 O OG  A SER B 110 ? 0.3580 0.1891 0.3317 0.0032  -0.0319 -0.0413 88  SER B OG  
2451 O OG  B SER B 110 ? 0.3616 0.2176 0.3196 0.0135  -0.0243 -0.0619 88  SER B OG  
2452 N N   . TRP B 111 ? 0.2901 0.1737 0.2513 -0.0001 -0.0068 -0.0161 89  TRP B N   
2453 C CA  . TRP B 111 ? 0.2244 0.1115 0.1888 -0.0036 -0.0057 -0.0039 89  TRP B CA  
2454 C C   . TRP B 111 ? 0.3014 0.1862 0.2682 0.0080  -0.0050 -0.0055 89  TRP B C   
2455 O O   . TRP B 111 ? 0.2849 0.1742 0.2492 0.0182  -0.0019 -0.0156 89  TRP B O   
2456 C CB  . TRP B 111 ? 0.2184 0.1265 0.1791 -0.0090 0.0011  0.0008  89  TRP B CB  
2457 C CG  . TRP B 111 ? 0.2771 0.1963 0.2336 -0.0024 0.0074  -0.0049 89  TRP B CG  
2458 C CD1 . TRP B 111 ? 0.2582 0.1850 0.2121 -0.0029 0.0092  -0.0094 89  TRP B CD1 
2459 C CD2 . TRP B 111 ? 0.2576 0.1825 0.2140 0.0041  0.0111  -0.0040 89  TRP B CD2 
2460 N NE1 . TRP B 111 ? 0.2613 0.1948 0.2135 0.0023  0.0128  -0.0099 89  TRP B NE1 
2461 C CE2 . TRP B 111 ? 0.2833 0.2169 0.2371 0.0057  0.0144  -0.0066 89  TRP B CE2 
2462 C CE3 . TRP B 111 ? 0.2407 0.1654 0.2005 0.0082  0.0108  -0.0002 89  TRP B CE3 
2463 C CZ2 . TRP B 111 ? 0.2115 0.1529 0.1660 0.0089  0.0175  -0.0042 89  TRP B CZ2 
2464 C CZ3 . TRP B 111 ? 0.2328 0.1685 0.1933 0.0125  0.0149  0.0002  89  TRP B CZ3 
2465 C CH2 . TRP B 111 ? 0.2538 0.1977 0.2117 0.0118  0.0182  -0.0012 89  TRP B CH2 
2466 N N   . GLU B 112 ? 0.2797 0.1612 0.2520 0.0060  -0.0085 0.0053  90  GLU B N   
2467 C CA  . GLU B 112 ? 0.2621 0.1466 0.2388 0.0162  -0.0081 0.0061  90  GLU B CA  
2468 C C   . GLU B 112 ? 0.3019 0.2012 0.2777 0.0095  -0.0058 0.0186  90  GLU B C   
2469 O O   . GLU B 112 ? 0.2709 0.1713 0.2458 -0.0016 -0.0089 0.0291  90  GLU B O   
2470 C CB  . GLU B 112 ? 0.3479 0.2109 0.3356 0.0241  -0.0186 0.0053  90  GLU B CB  
2471 C CG  . GLU B 112 ? 0.4919 0.3362 0.4817 0.0286  -0.0243 -0.0087 90  GLU B CG  
2472 C CD  . GLU B 112 ? 0.7006 0.5213 0.7043 0.0401  -0.0363 -0.0142 90  GLU B CD  
2473 O OE1 . GLU B 112 ? 0.6071 0.4269 0.6192 0.0452  -0.0401 -0.0052 90  GLU B OE1 
2474 O OE2 . GLU B 112 ? 0.7444 0.5478 0.7516 0.0449  -0.0430 -0.0289 90  GLU B OE2 
2475 N N   . ARG B 113 ? 0.2461 0.1602 0.2223 0.0155  -0.0008 0.0173  91  ARG B N   
2476 C CA  . ARG B 113 ? 0.2705 0.2015 0.2449 0.0092  0.0016  0.0250  91  ARG B CA  
2477 C C   . ARG B 113 ? 0.2719 0.2107 0.2533 0.0164  -0.0001 0.0286  91  ARG B C   
2478 O O   . ARG B 113 ? 0.2618 0.2037 0.2477 0.0265  0.0022  0.0219  91  ARG B O   
2479 C CB  . ARG B 113 ? 0.1918 0.1357 0.1611 0.0062  0.0086  0.0188  91  ARG B CB  
2480 C CG  . ARG B 113 ? 0.2060 0.1659 0.1742 -0.0005 0.0094  0.0222  91  ARG B CG  
2481 C CD  . ARG B 113 ? 0.2384 0.2040 0.2049 -0.0026 0.0133  0.0145  91  ARG B CD  
2482 N NE  . ARG B 113 ? 0.2120 0.1724 0.1749 -0.0052 0.0140  0.0105  91  ARG B NE  
2483 C CZ  . ARG B 113 ? 0.2695 0.2280 0.2321 -0.0040 0.0157  0.0043  91  ARG B CZ  
2484 N NH1 . ARG B 113 ? 0.2332 0.1930 0.1988 -0.0019 0.0166  0.0029  91  ARG B NH1 
2485 N NH2 . ARG B 113 ? 0.2382 0.1943 0.1988 -0.0059 0.0155  0.0012  91  ARG B NH2 
2486 N N   . SER B 114 ? 0.2236 0.1705 0.2058 0.0110  -0.0040 0.0394  92  SER B N   
2487 C CA  . SER B 114 ? 0.2489 0.2104 0.2373 0.0156  -0.0051 0.0431  92  SER B CA  
2488 C C   . SER B 114 ? 0.2177 0.1993 0.2011 0.0075  -0.0008 0.0417  92  SER B C   
2489 O O   . SER B 114 ? 0.2419 0.2288 0.2177 -0.0018 -0.0004 0.0425  92  SER B O   
2490 C CB  . SER B 114 ? 0.2514 0.2091 0.2456 0.0163  -0.0150 0.0567  92  SER B CB  
2491 O OG  . SER B 114 ? 0.2965 0.2584 0.2829 0.0032  -0.0179 0.0676  92  SER B OG  
2492 N N   . LEU B 115 ? 0.2045 0.1991 0.1935 0.0111  0.0016  0.0386  93  LEU B N   
2493 C CA  . LEU B 115 ? 0.2300 0.2409 0.2182 0.0037  0.0031  0.0360  93  LEU B CA  
2494 C C   . LEU B 115 ? 0.2425 0.2702 0.2380 0.0053  -0.0015 0.0426  93  LEU B C   
2495 O O   . LEU B 115 ? 0.2552 0.2906 0.2606 0.0123  -0.0007 0.0429  93  LEU B O   
2496 C CB  . LEU B 115 ? 0.2351 0.2465 0.2258 0.0034  0.0083  0.0291  93  LEU B CB  
2497 C CG  . LEU B 115 ? 0.2374 0.2346 0.2218 0.0023  0.0118  0.0232  93  LEU B CG  
2498 C CD1 . LEU B 115 ? 0.2180 0.2048 0.2017 0.0107  0.0138  0.0221  93  LEU B CD1 
2499 C CD2 . LEU B 115 ? 0.2578 0.2578 0.2455 -0.0023 0.0134  0.0199  93  LEU B CD2 
2500 N N   . THR B 116 ? 0.2090 0.2474 0.2000 -0.0009 -0.0064 0.0479  94  THR B N   
2501 C CA  . THR B 116 ? 0.2196 0.2756 0.2167 0.0003  -0.0126 0.0562  94  THR B CA  
2502 C C   . THR B 116 ? 0.1626 0.2388 0.1593 -0.0081 -0.0133 0.0496  94  THR B C   
2503 O O   . THR B 116 ? 0.2103 0.2964 0.1975 -0.0160 -0.0153 0.0468  94  THR B O   
2504 C CB  . THR B 116 ? 0.2585 0.3146 0.2507 -0.0015 -0.0198 0.0696  94  THR B CB  
2505 O OG1 . THR B 116 ? 0.2461 0.2781 0.2420 0.0058  -0.0216 0.0747  94  THR B OG1 
2506 C CG2 . THR B 116 ? 0.3464 0.4225 0.3450 0.0001  -0.0279 0.0800  94  THR B CG2 
2507 N N   . PHE B 117 ? 0.1988 0.2833 0.2065 -0.0069 -0.0121 0.0464  95  PHE B N   
2508 C CA  . PHE B 117 ? 0.2040 0.3034 0.2144 -0.0162 -0.0146 0.0393  95  PHE B CA  
2509 C C   . PHE B 117 ? 0.2747 0.3987 0.2874 -0.0185 -0.0224 0.0449  95  PHE B C   
2510 O O   . PHE B 117 ? 0.2557 0.3872 0.2739 -0.0112 -0.0256 0.0561  95  PHE B O   
2511 C CB  . PHE B 117 ? 0.1774 0.2783 0.2002 -0.0177 -0.0117 0.0370  95  PHE B CB  
2512 C CG  . PHE B 117 ? 0.2163 0.2967 0.2361 -0.0179 -0.0057 0.0321  95  PHE B CG  
2513 C CD1 . PHE B 117 ? 0.1845 0.2553 0.2033 -0.0088 0.0001  0.0355  95  PHE B CD1 
2514 C CD2 . PHE B 117 ? 0.2098 0.2809 0.2287 -0.0262 -0.0074 0.0234  95  PHE B CD2 
2515 C CE1 . PHE B 117 ? 0.2148 0.2701 0.2298 -0.0093 0.0048  0.0319  95  PHE B CE1 
2516 C CE2 . PHE B 117 ? 0.2079 0.2608 0.2253 -0.0259 -0.0035 0.0211  95  PHE B CE2 
2517 C CZ  . PHE B 117 ? 0.1997 0.2463 0.2141 -0.0182 0.0029  0.0263  95  PHE B CZ  
2518 N N   . GLU B 118 ? 0.1990 0.3359 0.2081 -0.0281 -0.0266 0.0357  96  GLU B N   
2519 C CA  . GLU B 118 ? 0.1717 0.3352 0.1784 -0.0317 -0.0347 0.0395  96  GLU B CA  
2520 C C   . GLU B 118 ? 0.2506 0.4322 0.2731 -0.0293 -0.0391 0.0474  96  GLU B C   
2521 O O   . GLU B 118 ? 0.2202 0.4235 0.2424 -0.0288 -0.0464 0.0559  96  GLU B O   
2522 C CB  . GLU B 118 ? 0.2368 0.4122 0.2371 -0.0416 -0.0388 0.0228  96  GLU B CB  
2523 C CG  . GLU B 118 ? 0.2774 0.4511 0.2920 -0.0481 -0.0417 0.0119  96  GLU B CG  
2524 C CD  . GLU B 118 ? 0.3701 0.5529 0.3809 -0.0565 -0.0486 -0.0082 96  GLU B CD  
2525 O OE1 . GLU B 118 ? 0.3526 0.5472 0.3479 -0.0562 -0.0491 -0.0154 96  GLU B OE1 
2526 O OE2 . GLU B 118 ? 0.4081 0.5898 0.4325 -0.0638 -0.0545 -0.0167 96  GLU B OE2 
2527 N N   . ASP B 119 ? 0.1846 0.3623 0.2214 -0.0284 -0.0353 0.0460  97  ASP B N   
2528 C CA  . ASP B 119 ? 0.1923 0.3943 0.2465 -0.0272 -0.0388 0.0525  97  ASP B CA  
2529 C C   . ASP B 119 ? 0.2182 0.4210 0.2818 -0.0120 -0.0353 0.0628  97  ASP B C   
2530 O O   . ASP B 119 ? 0.2137 0.4397 0.2944 -0.0085 -0.0363 0.0669  97  ASP B O   
2531 C CB  . ASP B 119 ? 0.1828 0.3894 0.2497 -0.0382 -0.0383 0.0460  97  ASP B CB  
2532 C CG  . ASP B 119 ? 0.2201 0.4062 0.2891 -0.0366 -0.0291 0.0455  97  ASP B CG  
2533 O OD1 . ASP B 119 ? 0.2449 0.4109 0.3036 -0.0273 -0.0229 0.0462  97  ASP B OD1 
2534 O OD2 . ASP B 119 ? 0.2523 0.4439 0.3335 -0.0462 -0.0290 0.0456  97  ASP B OD2 
2535 N N   . GLY B 120 ? 0.2122 0.3922 0.2670 -0.0026 -0.0320 0.0657  98  GLY B N   
2536 C CA  . GLY B 120 ? 0.2692 0.4459 0.3340 0.0135  -0.0304 0.0713  98  GLY B CA  
2537 C C   . GLY B 120 ? 0.2419 0.4031 0.3076 0.0189  -0.0204 0.0645  98  GLY B C   
2538 O O   . GLY B 120 ? 0.2427 0.3957 0.3134 0.0335  -0.0193 0.0650  98  GLY B O   
2539 N N   . GLY B 121 ? 0.1935 0.3507 0.2551 0.0079  -0.0146 0.0580  99  GLY B N   
2540 C CA  . GLY B 121 ? 0.1958 0.3382 0.2545 0.0117  -0.0060 0.0533  99  GLY B CA  
2541 C C   . GLY B 121 ? 0.2114 0.3242 0.2570 0.0179  -0.0054 0.0515  99  GLY B C   
2542 O O   . GLY B 121 ? 0.2325 0.3329 0.2669 0.0117  -0.0091 0.0524  99  GLY B O   
2543 N N   . ILE B 122 ? 0.2394 0.3441 0.2870 0.0300  -0.0011 0.0483  100 ILE B N   
2544 C CA  . ILE B 122 ? 0.2393 0.3153 0.2776 0.0356  -0.0020 0.0464  100 ILE B CA  
2545 C C   . ILE B 122 ? 0.2930 0.3607 0.3274 0.0395  0.0058  0.0379  100 ILE B C   
2546 O O   . ILE B 122 ? 0.2443 0.3301 0.2871 0.0476  0.0103  0.0338  100 ILE B O   
2547 C CB  . ILE B 122 ? 0.3284 0.3988 0.3752 0.0492  -0.0101 0.0511  100 ILE B CB  
2548 C CG1 . ILE B 122 ? 0.3895 0.4275 0.4289 0.0522  -0.0132 0.0506  100 ILE B CG1 
2549 C CG2 . ILE B 122 ? 0.3655 0.4558 0.4294 0.0650  -0.0092 0.0464  100 ILE B CG2 
2550 C CD1 . ILE B 122 ? 0.5416 0.5687 0.5710 0.0407  -0.0195 0.0617  100 ILE B CD1 
2551 N N   . CYS B 123 ? 0.2246 0.2698 0.2462 0.0335  0.0073  0.0352  101 CYS B N   
2552 C CA  . CYS B 123 ? 0.2332 0.2697 0.2495 0.0371  0.0130  0.0277  101 CYS B CA  
2553 C C   . CYS B 123 ? 0.3211 0.3304 0.3308 0.0408  0.0095  0.0248  101 CYS B C   
2554 O O   . CYS B 123 ? 0.2710 0.2678 0.2771 0.0352  0.0042  0.0308  101 CYS B O   
2555 C CB  . CYS B 123 ? 0.2379 0.2750 0.2474 0.0251  0.0176  0.0274  101 CYS B CB  
2556 S SG  . CYS B 123 ? 0.2480 0.3135 0.2676 0.0164  0.0196  0.0331  101 CYS B SG  
2557 N N   . ASN B 124 ? 0.2666 0.2701 0.2754 0.0496  0.0120  0.0157  102 ASN B N   
2558 C CA  . ASN B 124 ? 0.2150 0.1925 0.2179 0.0509  0.0086  0.0112  102 ASN B CA  
2559 C C   . ASN B 124 ? 0.2558 0.2348 0.2498 0.0493  0.0149  0.0031  102 ASN B C   
2560 O O   . ASN B 124 ? 0.2749 0.2740 0.2701 0.0551  0.0204  -0.0022 102 ASN B O   
2561 C CB  . ASN B 124 ? 0.2859 0.2506 0.2988 0.0654  0.0012  0.0057  102 ASN B CB  
2562 C CG  . ASN B 124 ? 0.5430 0.5097 0.5672 0.0689  -0.0064 0.0156  102 ASN B CG  
2563 O OD1 . ASN B 124 ? 0.5429 0.4946 0.5657 0.0612  -0.0137 0.0272  102 ASN B OD1 
2564 N ND2 . ASN B 124 ? 0.6177 0.6074 0.6533 0.0802  -0.0050 0.0124  102 ASN B ND2 
2565 N N   . ALA B 125 ? 0.2567 0.2193 0.2419 0.0408  0.0141  0.0034  103 ALA B N   
2566 C CA  . ALA B 125 ? 0.2578 0.2218 0.2346 0.0391  0.0184  -0.0027 103 ALA B CA  
2567 C C   . ALA B 125 ? 0.3123 0.2547 0.2850 0.0386  0.0138  -0.0083 103 ALA B C   
2568 O O   . ALA B 125 ? 0.2697 0.1958 0.2451 0.0348  0.0077  -0.0037 103 ALA B O   
2569 C CB  . ALA B 125 ? 0.2658 0.2363 0.2382 0.0279  0.0217  0.0036  103 ALA B CB  
2570 N N   . ARG B 126 ? 0.2463 0.1911 0.2127 0.0415  0.0160  -0.0172 104 ARG B N   
2571 C CA  . ARG B 126 ? 0.2510 0.1776 0.2141 0.0400  0.0110  -0.0240 104 ARG B CA  
2572 C C   . ARG B 126 ? 0.2703 0.2069 0.2237 0.0372  0.0148  -0.0279 104 ARG B C   
2573 O O   . ARG B 126 ? 0.2867 0.2436 0.2362 0.0409  0.0201  -0.0290 104 ARG B O   
2574 C CB  . ARG B 126 ? 0.3148 0.2293 0.2840 0.0517  0.0047  -0.0363 104 ARG B CB  
2575 C CG  . ARG B 126 ? 0.5311 0.4268 0.4980 0.0495  -0.0020 -0.0456 104 ARG B CG  
2576 C CD  . ARG B 126 ? 0.5373 0.4182 0.5125 0.0626  -0.0103 -0.0616 104 ARG B CD  
2577 N NE  . ARG B 126 ? 0.5856 0.4506 0.5582 0.0597  -0.0173 -0.0731 104 ARG B NE  
2578 C CZ  . ARG B 126 ? 0.7041 0.5387 0.6859 0.0542  -0.0294 -0.0723 104 ARG B CZ  
2579 N NH1 . ARG B 126 ? 0.7725 0.5893 0.7654 0.0507  -0.0361 -0.0584 104 ARG B NH1 
2580 N NH2 . ARG B 126 ? 0.6607 0.4879 0.6413 0.0493  -0.0347 -0.0820 104 ARG B NH2 
2581 N N   . ASN B 127 ? 0.2749 0.2000 0.2251 0.0299  0.0115  -0.0282 105 ASN B N   
2582 C CA  . ASN B 127 ? 0.2621 0.1954 0.2043 0.0277  0.0127  -0.0317 105 ASN B CA  
2583 C C   . ASN B 127 ? 0.3054 0.2245 0.2469 0.0264  0.0060  -0.0412 105 ASN B C   
2584 O O   . ASN B 127 ? 0.2874 0.1913 0.2346 0.0193  0.0012  -0.0375 105 ASN B O   
2585 C CB  . ASN B 127 ? 0.2452 0.1830 0.1871 0.0192  0.0146  -0.0218 105 ASN B CB  
2586 C CG  . ASN B 127 ? 0.2710 0.2193 0.2064 0.0185  0.0149  -0.0222 105 ASN B CG  
2587 O OD1 . ASN B 127 ? 0.2675 0.2234 0.1961 0.0230  0.0146  -0.0293 105 ASN B OD1 
2588 N ND2 . ASN B 127 ? 0.2687 0.2187 0.2068 0.0135  0.0145  -0.0153 105 ASN B ND2 
2589 N N   . ASP B 128 ? 0.2744 0.2010 0.2091 0.0320  0.0051  -0.0531 106 ASP B N   
2590 C CA  . ASP B 128 ? 0.2880 0.2043 0.2214 0.0293  -0.0021 -0.0635 106 ASP B CA  
2591 C C   . ASP B 128 ? 0.3182 0.2502 0.2435 0.0244  -0.0005 -0.0604 106 ASP B C   
2592 O O   . ASP B 128 ? 0.2528 0.2055 0.1695 0.0288  0.0038  -0.0600 106 ASP B O   
2593 C CB  . ASP B 128 ? 0.2720 0.1868 0.2038 0.0405  -0.0063 -0.0830 106 ASP B CB  
2594 C CG  . ASP B 128 ? 0.4819 0.3774 0.4254 0.0475  -0.0109 -0.0873 106 ASP B CG  
2595 O OD1 . ASP B 128 ? 0.5724 0.4412 0.5255 0.0411  -0.0199 -0.0850 106 ASP B OD1 
2596 O OD2 . ASP B 128 ? 0.4993 0.4083 0.4436 0.0591  -0.0063 -0.0917 106 ASP B OD2 
2597 N N   . ILE B 129 ? 0.2770 0.2021 0.2061 0.0150  -0.0045 -0.0565 107 ILE B N   
2598 C CA  . ILE B 129 ? 0.2747 0.2143 0.2004 0.0110  -0.0039 -0.0511 107 ILE B CA  
2599 C C   . ILE B 129 ? 0.3354 0.2754 0.2592 0.0075  -0.0112 -0.0611 107 ILE B C   
2600 O O   . ILE B 129 ? 0.3013 0.2270 0.2326 0.0008  -0.0170 -0.0648 107 ILE B O   
2601 C CB  . ILE B 129 ? 0.2798 0.2188 0.2138 0.0045  -0.0019 -0.0396 107 ILE B CB  
2602 C CG1 . ILE B 129 ? 0.2979 0.2352 0.2342 0.0070  0.0037  -0.0319 107 ILE B CG1 
2603 C CG2 . ILE B 129 ? 0.2898 0.2429 0.2234 0.0037  -0.0029 -0.0356 107 ILE B CG2 
2604 C CD1 . ILE B 129 ? 0.2667 0.2068 0.2103 0.0021  0.0053  -0.0245 107 ILE B CD1 
2605 N N   . THR B 130 ? 0.3219 0.2798 0.2363 0.0106  -0.0120 -0.0638 108 THR B N   
2606 C CA  . THR B 130 ? 0.3054 0.2693 0.2170 0.0072  -0.0195 -0.0732 108 THR B CA  
2607 C C   . THR B 130 ? 0.3094 0.2922 0.2191 0.0058  -0.0201 -0.0631 108 THR B C   
2608 O O   . THR B 130 ? 0.3063 0.2937 0.2179 0.0077  -0.0156 -0.0499 108 THR B O   
2609 C CB  . THR B 130 ? 0.3687 0.3390 0.2693 0.0143  -0.0224 -0.0905 108 THR B CB  
2610 O OG1 . THR B 130 ? 0.3450 0.3383 0.2338 0.0216  -0.0159 -0.0858 108 THR B OG1 
2611 C CG2 . THR B 130 ? 0.3493 0.2968 0.2562 0.0180  -0.0245 -0.1025 108 THR B CG2 
2612 N N   . MET B 131 ? 0.3392 0.3325 0.2469 0.0027  -0.0273 -0.0695 109 MET B N   
2613 C CA  . MET B 131 ? 0.3226 0.3322 0.2329 0.0016  -0.0303 -0.0597 109 MET B CA  
2614 C C   . MET B 131 ? 0.3268 0.3553 0.2272 0.0017  -0.0380 -0.0676 109 MET B C   
2615 O O   . MET B 131 ? 0.3062 0.3312 0.2054 -0.0020 -0.0436 -0.0830 109 MET B O   
2616 C CB  . MET B 131 ? 0.3422 0.3471 0.2693 -0.0051 -0.0316 -0.0563 109 MET B CB  
2617 C CG  . MET B 131 ? 0.3791 0.3971 0.3154 -0.0026 -0.0328 -0.0457 109 MET B CG  
2618 S SD  . MET B 131 ? 0.3444 0.3778 0.2976 -0.0095 -0.0387 -0.0488 109 MET B SD  
2619 C CE  . MET B 131 ? 0.3128 0.3557 0.2585 -0.0155 -0.0483 -0.0603 109 MET B CE  
2620 N N   . GLU B 132 ? 0.2992 0.3473 0.1929 0.0054  -0.0397 -0.0565 110 GLU B N   
2621 C CA  . GLU B 132 ? 0.3195 0.3908 0.2047 0.0048  -0.0483 -0.0601 110 GLU B CA  
2622 C C   . GLU B 132 ? 0.3661 0.4477 0.2609 0.0059  -0.0531 -0.0433 110 GLU B C   
2623 O O   . GLU B 132 ? 0.3011 0.3846 0.1951 0.0099  -0.0513 -0.0267 110 GLU B O   
2624 C CB  . GLU B 132 ? 0.3738 0.4661 0.2379 0.0093  -0.0473 -0.0627 110 GLU B CB  
2625 C CG  . GLU B 132 ? 0.3140 0.4006 0.1693 0.0120  -0.0441 -0.0842 110 GLU B CG  
2626 C CD  . GLU B 132 ? 0.3892 0.4646 0.2497 0.0074  -0.0522 -0.1058 110 GLU B CD  
2627 O OE1 . GLU B 132 ? 0.3389 0.4259 0.2015 0.0025  -0.0605 -0.1064 110 GLU B OE1 
2628 O OE2 . GLU B 132 ? 0.3779 0.4298 0.2445 0.0078  -0.0505 -0.1184 110 GLU B OE2 
2629 N N   . GLY B 133 ? 0.3227 0.4112 0.2288 0.0023  -0.0603 -0.0475 111 GLY B N   
2630 C CA  . GLY B 133 ? 0.2849 0.3851 0.2032 0.0059  -0.0664 -0.0341 111 GLY B CA  
2631 C C   . GLY B 133 ? 0.3218 0.4054 0.2541 0.0104  -0.0609 -0.0236 111 GLY B C   
2632 O O   . GLY B 133 ? 0.3034 0.3736 0.2460 0.0078  -0.0547 -0.0297 111 GLY B O   
2633 N N   . ASP B 134 ? 0.3177 0.4024 0.2502 0.0164  -0.0640 -0.0071 112 ASP B N   
2634 C CA  . ASP B 134 ? 0.3689 0.4379 0.3173 0.0216  -0.0625 0.0017  112 ASP B CA  
2635 C C   . ASP B 134 ? 0.3496 0.4002 0.2915 0.0202  -0.0529 0.0048  112 ASP B C   
2636 O O   . ASP B 134 ? 0.2845 0.3211 0.2383 0.0237  -0.0526 0.0118  112 ASP B O   
2637 C CB  . ASP B 134 ? 0.3792 0.4541 0.3351 0.0282  -0.0741 0.0192  112 ASP B CB  
2638 C CG  . ASP B 134 ? 0.4459 0.5273 0.3836 0.0256  -0.0763 0.0361  112 ASP B CG  
2639 O OD1 . ASP B 134 ? 0.3753 0.4621 0.2936 0.0204  -0.0683 0.0308  112 ASP B OD1 
2640 O OD2 . ASP B 134 ? 0.4253 0.5100 0.3684 0.0289  -0.0871 0.0551  112 ASP B OD2 
2641 N N   . THR B 135 ? 0.2940 0.3452 0.2190 0.0158  -0.0462 -0.0018 113 THR B N   
2642 C CA  . THR B 135 ? 0.2761 0.3179 0.1936 0.0153  -0.0385 0.0038  113 THR B CA  
2643 C C   . THR B 135 ? 0.2919 0.3213 0.2073 0.0130  -0.0297 -0.0106 113 THR B C   
2644 O O   . THR B 135 ? 0.3016 0.3343 0.2104 0.0107  -0.0299 -0.0244 113 THR B O   
2645 C CB  . THR B 135 ? 0.2928 0.3543 0.1916 0.0144  -0.0393 0.0124  113 THR B CB  
2646 O OG1 . THR B 135 ? 0.3166 0.3883 0.2182 0.0153  -0.0490 0.0313  113 THR B OG1 
2647 C CG2 . THR B 135 ? 0.3180 0.3763 0.2107 0.0133  -0.0307 0.0179  113 THR B CG2 
2648 N N   . PHE B 136 ? 0.2874 0.3015 0.2095 0.0133  -0.0237 -0.0072 114 PHE B N   
2649 C CA  . PHE B 136 ? 0.2903 0.2936 0.2097 0.0118  -0.0162 -0.0166 114 PHE B CA  
2650 C C   . PHE B 136 ? 0.2683 0.2784 0.1756 0.0136  -0.0113 -0.0131 114 PHE B C   
2651 O O   . PHE B 136 ? 0.2866 0.3032 0.1932 0.0136  -0.0113 0.0012  114 PHE B O   
2652 C CB  . PHE B 136 ? 0.2786 0.2670 0.2108 0.0109  -0.0124 -0.0153 114 PHE B CB  
2653 C CG  . PHE B 136 ? 0.3172 0.3060 0.2617 0.0090  -0.0151 -0.0206 114 PHE B CG  
2654 C CD1 . PHE B 136 ? 0.3232 0.3122 0.2679 0.0036  -0.0155 -0.0300 114 PHE B CD1 
2655 C CD2 . PHE B 136 ? 0.2522 0.2427 0.2095 0.0124  -0.0180 -0.0167 114 PHE B CD2 
2656 C CE1 . PHE B 136 ? 0.2817 0.2783 0.2383 -0.0001 -0.0173 -0.0330 114 PHE B CE1 
2657 C CE2 . PHE B 136 ? 0.2619 0.2608 0.2312 0.0116  -0.0194 -0.0233 114 PHE B CE2 
2658 C CZ  . PHE B 136 ? 0.2706 0.2754 0.2390 0.0046  -0.0184 -0.0302 114 PHE B CZ  
2659 N N   . TYR B 137 ? 0.2834 0.2929 0.1835 0.0150  -0.0079 -0.0263 115 TYR B N   
2660 C CA  . TYR B 137 ? 0.3162 0.3370 0.2069 0.0188  -0.0021 -0.0274 115 TYR B CA  
2661 C C   . TYR B 137 ? 0.3229 0.3266 0.2210 0.0204  0.0029  -0.0325 115 TYR B C   
2662 O O   . TYR B 137 ? 0.2984 0.2846 0.2027 0.0192  0.0007  -0.0419 115 TYR B O   
2663 C CB  . TYR B 137 ? 0.2801 0.3184 0.1571 0.0226  -0.0040 -0.0426 115 TYR B CB  
2664 C CG  . TYR B 137 ? 0.2722 0.3318 0.1401 0.0205  -0.0098 -0.0363 115 TYR B CG  
2665 C CD1 . TYR B 137 ? 0.2874 0.3743 0.1447 0.0202  -0.0083 -0.0220 115 TYR B CD1 
2666 C CD2 . TYR B 137 ? 0.3117 0.3661 0.1834 0.0176  -0.0176 -0.0412 115 TYR B CD2 
2667 C CE1 . TYR B 137 ? 0.2941 0.4015 0.1432 0.0177  -0.0152 -0.0128 115 TYR B CE1 
2668 C CE2 . TYR B 137 ? 0.2934 0.3686 0.1580 0.0163  -0.0243 -0.0342 115 TYR B CE2 
2669 C CZ  . TYR B 137 ? 0.3126 0.4131 0.1655 0.0166  -0.0234 -0.0196 115 TYR B CZ  
2670 O OH  . TYR B 137 ? 0.3499 0.4722 0.1957 0.0148  -0.0316 -0.0098 115 TYR B OH  
2671 N N   . ASN B 138 ? 0.3127 0.3232 0.2111 0.0219  0.0087  -0.0245 116 ASN B N   
2672 C CA  . ASN B 138 ? 0.2749 0.2712 0.1821 0.0230  0.0126  -0.0255 116 ASN B CA  
2673 C C   . ASN B 138 ? 0.3105 0.3232 0.2134 0.0294  0.0181  -0.0299 116 ASN B C   
2674 O O   . ASN B 138 ? 0.3255 0.3607 0.2245 0.0283  0.0219  -0.0194 116 ASN B O   
2675 C CB  . ASN B 138 ? 0.2416 0.2302 0.1584 0.0179  0.0133  -0.0110 116 ASN B CB  
2676 C CG  . ASN B 138 ? 0.3157 0.2928 0.2392 0.0142  0.0083  -0.0093 116 ASN B CG  
2677 O OD1 . ASN B 138 ? 0.2584 0.2229 0.1895 0.0123  0.0082  -0.0123 116 ASN B OD1 
2678 N ND2 . ASN B 138 ? 0.2561 0.2414 0.1770 0.0134  0.0037  -0.0042 116 ASN B ND2 
2679 N N   . LYS B 139 ? 0.2304 0.2333 0.1361 0.0359  0.0178  -0.0447 117 LYS B N   
2680 C CA  . LYS B 139 ? 0.2197 0.2384 0.1252 0.0452  0.0224  -0.0527 117 LYS B CA  
2681 C C   . LYS B 139 ? 0.3245 0.3282 0.2424 0.0452  0.0239  -0.0466 117 LYS B C   
2682 O O   . LYS B 139 ? 0.2715 0.2505 0.1968 0.0463  0.0193  -0.0522 117 LYS B O   
2683 C CB  . LYS B 139 ? 0.2775 0.2943 0.1798 0.0551  0.0183  -0.0761 117 LYS B CB  
2684 C CG  . LYS B 139 ? 0.3816 0.4122 0.2878 0.0686  0.0214  -0.0897 117 LYS B CG  
2685 C CD  . LYS B 139 ? 0.4152 0.4268 0.3286 0.0752  0.0128  -0.1102 117 LYS B CD  
2686 C CE  . LYS B 139 ? 0.4625 0.4836 0.3871 0.0871  0.0135  -0.1201 117 LYS B CE  
2687 N NZ  . LYS B 139 ? 0.5892 0.5903 0.5225 0.0931  0.0034  -0.1382 117 LYS B NZ  
2688 N N   . VAL B 140 ? 0.2321 0.2520 0.1528 0.0425  0.0293  -0.0335 118 VAL B N   
2689 C CA  . VAL B 140 ? 0.2377 0.2471 0.1696 0.0403  0.0301  -0.0256 118 VAL B CA  
2690 C C   . VAL B 140 ? 0.2583 0.2882 0.1953 0.0494  0.0344  -0.0300 118 VAL B C   
2691 O O   . VAL B 140 ? 0.2405 0.3024 0.1728 0.0520  0.0396  -0.0300 118 VAL B O   
2692 C CB  . VAL B 140 ? 0.2662 0.2760 0.2009 0.0293  0.0306  -0.0084 118 VAL B CB  
2693 C CG1 . VAL B 140 ? 0.2335 0.2340 0.1788 0.0267  0.0304  -0.0030 118 VAL B CG1 
2694 C CG2 . VAL B 140 ? 0.2578 0.2520 0.1897 0.0232  0.0260  -0.0061 118 VAL B CG2 
2695 N N   . ARG B 141 ? 0.2427 0.2580 0.1899 0.0541  0.0320  -0.0329 119 ARG B N   
2696 C CA  . ARG B 141 ? 0.2233 0.2579 0.1793 0.0630  0.0351  -0.0353 119 ARG B CA  
2697 C C   . ARG B 141 ? 0.3007 0.3274 0.2661 0.0563  0.0340  -0.0220 119 ARG B C   
2698 O O   . ARG B 141 ? 0.3044 0.3050 0.2710 0.0503  0.0291  -0.0179 119 ARG B O   
2699 C CB  . ARG B 141 ? 0.2803 0.3063 0.2422 0.0788  0.0305  -0.0540 119 ARG B CB  
2700 C CG  . ARG B 141 ? 0.3871 0.4192 0.3400 0.0867  0.0297  -0.0723 119 ARG B CG  
2701 C CD  . ARG B 141 ? 0.4042 0.4840 0.3508 0.0916  0.0387  -0.0759 119 ARG B CD  
2702 N NE  . ARG B 141 ? 0.5237 0.6126 0.4619 0.0941  0.0365  -0.0898 119 ARG B NE  
2703 C CZ  . ARG B 141 ? 0.5372 0.6415 0.4615 0.0853  0.0389  -0.0838 119 ARG B CZ  
2704 N NH1 . ARG B 141 ? 0.3929 0.5001 0.3096 0.0738  0.0429  -0.0647 119 ARG B NH1 
2705 N NH2 . ARG B 141 ? 0.4482 0.5651 0.3669 0.0883  0.0362  -0.0966 119 ARG B NH2 
2706 N N   . PHE B 142 ? 0.2502 0.3037 0.2222 0.0561  0.0386  -0.0153 120 PHE B N   
2707 C CA  . PHE B 142 ? 0.2097 0.2601 0.1902 0.0481  0.0371  -0.0032 120 PHE B CA  
2708 C C   . PHE B 142 ? 0.2313 0.3082 0.2239 0.0565  0.0393  -0.0041 120 PHE B C   
2709 O O   . PHE B 142 ? 0.2791 0.3905 0.2731 0.0581  0.0455  -0.0035 120 PHE B O   
2710 C CB  . PHE B 142 ? 0.2249 0.2797 0.2029 0.0330  0.0384  0.0102  120 PHE B CB  
2711 C CG  . PHE B 142 ? 0.2467 0.2930 0.2324 0.0241  0.0348  0.0186  120 PHE B CG  
2712 C CD1 . PHE B 142 ? 0.2401 0.3071 0.2367 0.0232  0.0356  0.0239  120 PHE B CD1 
2713 C CD2 . PHE B 142 ? 0.2561 0.2779 0.2385 0.0171  0.0303  0.0196  120 PHE B CD2 
2714 C CE1 . PHE B 142 ? 0.2195 0.2806 0.2225 0.0148  0.0311  0.0296  120 PHE B CE1 
2715 C CE2 . PHE B 142 ? 0.2157 0.2337 0.2041 0.0099  0.0267  0.0238  120 PHE B CE2 
2716 C CZ  . PHE B 142 ? 0.2288 0.2652 0.2269 0.0084  0.0266  0.0286  120 PHE B CZ  
2717 N N   . TYR B 143 ? 0.2154 0.2800 0.2170 0.0615  0.0340  -0.0043 121 TYR B N   
2718 C CA  . TYR B 143 ? 0.2220 0.3115 0.2377 0.0712  0.0344  -0.0054 121 TYR B CA  
2719 C C   . TYR B 143 ? 0.2999 0.3876 0.3228 0.0619  0.0305  0.0071  121 TYR B C   
2720 O O   . TYR B 143 ? 0.2727 0.3335 0.2921 0.0567  0.0245  0.0111  121 TYR B O   
2721 C CB  . TYR B 143 ? 0.2899 0.3689 0.3132 0.0903  0.0290  -0.0194 121 TYR B CB  
2722 C CG  . TYR B 143 ? 0.4192 0.5194 0.4603 0.1020  0.0267  -0.0197 121 TYR B CG  
2723 C CD1 . TYR B 143 ? 0.5167 0.5970 0.5664 0.1034  0.0172  -0.0124 121 TYR B CD1 
2724 C CD2 . TYR B 143 ? 0.5002 0.6448 0.5499 0.1116  0.0337  -0.0264 121 TYR B CD2 
2725 C CE1 . TYR B 143 ? 0.4687 0.5693 0.5360 0.1149  0.0136  -0.0118 121 TYR B CE1 
2726 C CE2 . TYR B 143 ? 0.5227 0.6907 0.5911 0.1235  0.0313  -0.0274 121 TYR B CE2 
2727 C CZ  . TYR B 143 ? 0.4417 0.5858 0.5192 0.1256  0.0207  -0.0201 121 TYR B CZ  
2728 O OH  . TYR B 143 ? 0.7043 0.8721 0.8016 0.1383  0.0168  -0.0202 121 TYR B OH  
2729 N N   . GLY B 144 ? 0.2271 0.3474 0.2599 0.0591  0.0337  0.0132  122 GLY B N   
2730 C CA  . GLY B 144 ? 0.2118 0.3335 0.2518 0.0501  0.0290  0.0232  122 GLY B CA  
2731 C C   . GLY B 144 ? 0.2265 0.3839 0.2834 0.0574  0.0294  0.0246  122 GLY B C   
2732 O O   . GLY B 144 ? 0.2067 0.3978 0.2693 0.0622  0.0363  0.0217  122 GLY B O   
2733 N N   . THR B 145 ? 0.2257 0.3812 0.2909 0.0583  0.0222  0.0293  123 THR B N   
2734 C CA  . THR B 145 ? 0.2385 0.4297 0.3219 0.0661  0.0212  0.0308  123 THR B CA  
2735 C C   . THR B 145 ? 0.2064 0.3978 0.2946 0.0564  0.0133  0.0407  123 THR B C   
2736 O O   . THR B 145 ? 0.2062 0.3705 0.2829 0.0462  0.0087  0.0443  123 THR B O   
2737 C CB  . THR B 145 ? 0.2442 0.4364 0.3374 0.0902  0.0183  0.0201  123 THR B CB  
2738 O OG1 . THR B 145 ? 0.2399 0.4757 0.3527 0.0994  0.0193  0.0196  123 THR B OG1 
2739 C CG2 . THR B 145 ? 0.2930 0.4495 0.3853 0.0950  0.0068  0.0233  123 THR B CG2 
2740 N N   . ASN B 146 ? 0.2193 0.4468 0.3250 0.0601  0.0118  0.0439  124 ASN B N   
2741 C CA  . ASN B 146 ? 0.2349 0.4712 0.3476 0.0529  0.0032  0.0523  124 ASN B CA  
2742 C C   . ASN B 146 ? 0.2255 0.4581 0.3311 0.0296  0.0021  0.0577  124 ASN B C   
2743 O O   . ASN B 146 ? 0.2331 0.4634 0.3379 0.0222  -0.0060 0.0615  124 ASN B O   
2744 C CB  . ASN B 146 ? 0.1704 0.3800 0.2790 0.0615  -0.0070 0.0547  124 ASN B CB  
2745 C CG  . ASN B 146 ? 0.4486 0.6572 0.5694 0.0857  -0.0103 0.0495  124 ASN B CG  
2746 O OD1 . ASN B 146 ? 0.6046 0.7920 0.7261 0.0933  -0.0205 0.0543  124 ASN B OD1 
2747 N ND2 . ASN B 146 ? 0.4961 0.7314 0.6285 0.0978  -0.0030 0.0401  124 ASN B ND2 
2748 N N   . PHE B 147 ? 0.1914 0.4251 0.2933 0.0179  0.0088  0.0579  125 PHE B N   
2749 C CA  . PHE B 147 ? 0.2014 0.4333 0.3032 -0.0033 0.0050  0.0623  125 PHE B CA  
2750 C C   . PHE B 147 ? 0.1912 0.4642 0.3129 -0.0114 0.0024  0.0690  125 PHE B C   
2751 O O   . PHE B 147 ? 0.2173 0.5244 0.3512 -0.0078 0.0088  0.0723  125 PHE B O   
2752 C CB  . PHE B 147 ? 0.2168 0.4338 0.3109 -0.0138 0.0102  0.0632  125 PHE B CB  
2753 C CG  . PHE B 147 ? 0.1573 0.3338 0.2329 -0.0107 0.0105  0.0567  125 PHE B CG  
2754 C CD1 . PHE B 147 ? 0.1781 0.3311 0.2457 -0.0176 0.0036  0.0528  125 PHE B CD1 
2755 C CD2 . PHE B 147 ? 0.2367 0.4032 0.3034 -0.0013 0.0175  0.0534  125 PHE B CD2 
2756 C CE1 . PHE B 147 ? 0.2008 0.3229 0.2532 -0.0151 0.0044  0.0470  125 PHE B CE1 
2757 C CE2 . PHE B 147 ? 0.2137 0.3457 0.2651 0.0003  0.0173  0.0479  125 PHE B CE2 
2758 C CZ  . PHE B 147 ? 0.2219 0.3328 0.2669 -0.0067 0.0110  0.0454  125 PHE B CZ  
2759 N N   . PRO B 148 ? 0.2172 0.4926 0.3429 -0.0224 -0.0070 0.0702  126 PRO B N   
2760 C CA  . PRO B 148 ? 0.2188 0.5342 0.3649 -0.0326 -0.0109 0.0767  126 PRO B CA  
2761 C C   . PRO B 148 ? 0.2112 0.5375 0.3658 -0.0507 -0.0076 0.0838  126 PRO B C   
2762 O O   . PRO B 148 ? 0.2534 0.5484 0.3987 -0.0623 -0.0090 0.0831  126 PRO B O   
2763 C CB  . PRO B 148 ? 0.2496 0.5574 0.3936 -0.0424 -0.0230 0.0736  126 PRO B CB  
2764 C CG  . PRO B 148 ? 0.2926 0.5616 0.4148 -0.0361 -0.0244 0.0663  126 PRO B CG  
2765 C CD  . PRO B 148 ? 0.2122 0.4588 0.3237 -0.0249 -0.0146 0.0649  126 PRO B CD  
2766 N N   . ALA B 149 ? 0.2264 0.5936 0.3966 -0.0526 -0.0042 0.0909  127 ALA B N   
2767 C CA  . ALA B 149 ? 0.1662 0.5372 0.3374 -0.0687 -0.0015 0.0994  127 ALA B CA  
2768 C C   . ALA B 149 ? 0.3507 0.6974 0.5248 -0.0922 -0.0128 0.1024  127 ALA B C   
2769 O O   . ALA B 149 ? 0.3055 0.6346 0.4768 -0.1051 -0.0132 0.1090  127 ALA B O   
2770 C CB  . ALA B 149 ? 0.2008 0.6134 0.3820 -0.0657 0.0023  0.1040  127 ALA B CB  
2771 N N   . ASN B 150 ? 0.2437 0.5877 0.4230 -0.0970 -0.0232 0.0964  128 ASN B N   
2772 C CA  . ASN B 150 ? 0.2211 0.5414 0.4043 -0.1171 -0.0355 0.0941  128 ASN B CA  
2773 C C   . ASN B 150 ? 0.3321 0.6159 0.5056 -0.1184 -0.0423 0.0824  128 ASN B C   
2774 O O   . ASN B 150 ? 0.2912 0.5536 0.4675 -0.1316 -0.0541 0.0746  128 ASN B O   
2775 C CB  . ASN B 150 ? 0.3053 0.6483 0.5000 -0.1231 -0.0439 0.0924  128 ASN B CB  
2776 C CG  . ASN B 150 ? 0.4687 0.8104 0.6582 -0.1156 -0.0513 0.0804  128 ASN B CG  
2777 O OD1 . ASN B 150 ? 0.4091 0.7440 0.5876 -0.1017 -0.0480 0.0762  128 ASN B OD1 
2778 N ND2 . ASN B 150 ? 0.3979 0.7486 0.5948 -0.1250 -0.0619 0.0756  128 ASN B ND2 
2779 N N   . GLY B 151 ? 0.2446 0.5142 0.4023 -0.1019 -0.0346 0.0777  129 GLY B N   
2780 C CA  . GLY B 151 ? 0.2742 0.5028 0.4137 -0.0975 -0.0382 0.0639  129 GLY B CA  
2781 C C   . GLY B 151 ? 0.2740 0.4688 0.4106 -0.1057 -0.0389 0.0640  129 GLY B C   
2782 O O   . GLY B 151 ? 0.2535 0.4547 0.3997 -0.1148 -0.0361 0.0775  129 GLY B O   
2783 N N   . PRO B 152 ? 0.2566 0.4175 0.3799 -0.1022 -0.0431 0.0496  130 PRO B N   
2784 C CA  . PRO B 152 ? 0.2964 0.4230 0.4197 -0.1089 -0.0467 0.0479  130 PRO B CA  
2785 C C   . PRO B 152 ? 0.2772 0.3974 0.3928 -0.1017 -0.0356 0.0587  130 PRO B C   
2786 O O   . PRO B 152 ? 0.3185 0.4204 0.4396 -0.1107 -0.0390 0.0657  130 PRO B O   
2787 C CB  . PRO B 152 ? 0.3020 0.4038 0.4122 -0.1019 -0.0519 0.0270  130 PRO B CB  
2788 C CG  . PRO B 152 ? 0.2439 0.3648 0.3400 -0.0883 -0.0452 0.0238  130 PRO B CG  
2789 C CD  . PRO B 152 ? 0.2128 0.3692 0.3216 -0.0924 -0.0455 0.0349  130 PRO B CD  
2790 N N   . VAL B 153 ? 0.2486 0.3819 0.3520 -0.0857 -0.0239 0.0599  131 VAL B N   
2791 C CA  . VAL B 153 ? 0.1869 0.3161 0.2819 -0.0783 -0.0139 0.0669  131 VAL B CA  
2792 C C   . VAL B 153 ? 0.2168 0.3766 0.3244 -0.0872 -0.0097 0.0842  131 VAL B C   
2793 O O   . VAL B 153 ? 0.2757 0.4284 0.3849 -0.0959 -0.0098 0.0947  131 VAL B O   
2794 C CB  . VAL B 153 ? 0.2150 0.3461 0.2951 -0.0587 -0.0051 0.0605  131 VAL B CB  
2795 C CG1 . VAL B 153 ? 0.2032 0.3384 0.2766 -0.0507 0.0050  0.0660  131 VAL B CG1 
2796 C CG2 . VAL B 153 ? 0.1928 0.2959 0.2594 -0.0530 -0.0084 0.0472  131 VAL B CG2 
2797 N N   . MET B 154 ? 0.1982 0.3963 0.3159 -0.0857 -0.0066 0.0885  132 MET B N   
2798 C CA  . MET B 154 ? 0.2462 0.4837 0.3768 -0.0942 -0.0014 0.1046  132 MET B CA  
2799 C C   . MET B 154 ? 0.3317 0.5617 0.4734 -0.1154 -0.0119 0.1146  132 MET B C   
2800 O O   . MET B 154 ? 0.3129 0.5572 0.4545 -0.1207 -0.0094 0.1269  132 MET B O   
2801 C CB  . MET B 154 ? 0.2628 0.5447 0.4024 -0.0838 0.0041  0.1038  132 MET B CB  
2802 C CG  . MET B 154 ? 0.2601 0.5426 0.3870 -0.0581 0.0128  0.0925  132 MET B CG  
2803 S SD  . MET B 154 ? 0.3160 0.5819 0.4244 -0.0482 0.0227  0.0905  132 MET B SD  
2804 C CE  . MET B 154 ? 0.2816 0.5965 0.3975 -0.0531 0.0300  0.1022  132 MET B CE  
2805 N N   . GLN B 155 ? 0.2556 0.4619 0.4048 -0.1259 -0.0247 0.1078  133 GLN B N   
2806 C CA  . GLN B 155 ? 0.2887 0.4785 0.4479 -0.1431 -0.0366 0.1138  133 GLN B CA  
2807 C C   . GLN B 155 ? 0.3831 0.5274 0.5387 -0.1478 -0.0444 0.1128  133 GLN B C   
2808 O O   . GLN B 155 ? 0.3045 0.4287 0.4696 -0.1602 -0.0561 0.1164  133 GLN B O   
2809 C CB  . GLN B 155 ? 0.2999 0.4910 0.4703 -0.1502 -0.0474 0.1034  133 GLN B CB  
2810 C CG  . GLN B 155 ? 0.3751 0.6113 0.5536 -0.1496 -0.0434 0.1085  133 GLN B CG  
2811 C CD  . GLN B 155 ? 0.4997 0.7640 0.6814 -0.1541 -0.0366 0.1266  133 GLN B CD  
2812 O OE1 . GLN B 155 ? 0.4295 0.6813 0.6164 -0.1685 -0.0432 0.1375  133 GLN B OE1 
2813 N NE2 . GLN B 155 ? 0.3737 0.6773 0.5525 -0.1410 -0.0246 0.1290  133 GLN B NE2 
2814 N N   . LYS B 156 ? 0.3072 0.4347 0.4506 -0.1372 -0.0389 0.1075  134 LYS B N   
2815 C CA  . LYS B 156 ? 0.3326 0.4197 0.4718 -0.1380 -0.0452 0.1068  134 LYS B CA  
2816 C C   . LYS B 156 ? 0.3605 0.4115 0.5093 -0.1441 -0.0616 0.0926  134 LYS B C   
2817 O O   . LYS B 156 ? 0.3147 0.3418 0.4709 -0.1511 -0.0719 0.0974  134 LYS B O   
2818 C CB  . LYS B 156 ? 0.4231 0.5156 0.5611 -0.1433 -0.0440 0.1266  134 LYS B CB  
2819 C CG  . LYS B 156 ? 0.3811 0.5029 0.5053 -0.1334 -0.0286 0.1346  134 LYS B CG  
2820 C CD  . LYS B 156 ? 0.4027 0.5479 0.5281 -0.1414 -0.0282 0.1541  134 LYS B CD  
2821 C CE  . LYS B 156 ? 0.5229 0.6466 0.6407 -0.1411 -0.0316 0.1620  134 LYS B CE  
2822 N NZ  . LYS B 156 ? 0.4769 0.6125 0.6010 -0.1544 -0.0389 0.1829  134 LYS B NZ  
2823 N N   . LYS B 157 ? 0.3385 0.3883 0.4867 -0.1400 -0.0645 0.0736  135 LYS B N   
2824 C CA  . LYS B 157 ? 0.3567 0.3804 0.5121 -0.1428 -0.0791 0.0537  135 LYS B CA  
2825 C C   . LYS B 157 ? 0.3329 0.3287 0.4790 -0.1311 -0.0823 0.0328  135 LYS B C   
2826 O O   . LYS B 157 ? 0.3759 0.3575 0.5243 -0.1290 -0.0923 0.0104  135 LYS B O   
2827 C CB  . LYS B 157 ? 0.3662 0.4164 0.5270 -0.1473 -0.0823 0.0452  135 LYS B CB  
2828 C CG  . LYS B 157 ? 0.4065 0.4826 0.5795 -0.1592 -0.0820 0.0619  135 LYS B CG  
2829 C CD  . LYS B 157 ? 0.4418 0.4918 0.6271 -0.1709 -0.0933 0.0677  135 LYS B CD  
2830 C CE  . LYS B 157 ? 0.5807 0.6597 0.7759 -0.1832 -0.0910 0.0901  135 LYS B CE  
2831 N NZ  . LYS B 157 ? 0.6999 0.7568 0.9037 -0.1940 -0.0997 0.1052  135 LYS B NZ  
2832 N N   . THR B 158 ? 0.3309 0.3247 0.3082 -0.0947 0.0118  -0.0289 136 THR B N   
2833 C CA  . THR B 158 ? 0.3259 0.3070 0.2874 -0.0799 0.0009  -0.0175 136 THR B CA  
2834 C C   . THR B 158 ? 0.3879 0.3404 0.3265 -0.0842 -0.0008 -0.0048 136 THR B C   
2835 O O   . THR B 158 ? 0.3453 0.2861 0.2689 -0.1004 0.0040  0.0011  136 THR B O   
2836 C CB  . THR B 158 ? 0.3033 0.2924 0.2655 -0.0725 0.0020  -0.0155 136 THR B CB  
2837 O OG1 . THR B 158 ? 0.3013 0.2809 0.2404 -0.0885 0.0113  -0.0124 136 THR B OG1 
2838 C CG2 . THR B 158 ? 0.2698 0.2846 0.2697 -0.0680 0.0052  -0.0265 136 THR B CG2 
2839 N N   . LEU B 159 ? 0.3430 0.2832 0.2832 -0.0719 -0.0071 0.0002  137 LEU B N   
2840 C CA  . LEU B 159 ? 0.3577 0.2713 0.2977 -0.0716 -0.0095 0.0139  137 LEU B CA  
2841 C C   . LEU B 159 ? 0.3300 0.2398 0.2736 -0.0605 -0.0177 0.0278  137 LEU B C   
2842 O O   . LEU B 159 ? 0.3439 0.2401 0.2863 -0.0662 -0.0264 0.0479  137 LEU B O   
2843 C CB  . LEU B 159 ? 0.3013 0.2000 0.2544 -0.0694 -0.0034 0.0040  137 LEU B CB  
2844 C CG  . LEU B 159 ? 0.3308 0.2263 0.2819 -0.0840 0.0036  -0.0075 137 LEU B CG  
2845 C CD1 . LEU B 159 ? 0.3918 0.2677 0.3530 -0.0854 0.0134  -0.0199 137 LEU B CD1 
2846 C CD2 . LEU B 159 ? 0.3941 0.2765 0.3389 -0.0978 0.0041  0.0051  137 LEU B CD2 
2847 N N   . LYS B 160 ? 0.3022 0.2243 0.2505 -0.0475 -0.0176 0.0203  138 LYS B N   
2848 C CA  . LYS B 160 ? 0.2699 0.1913 0.2254 -0.0374 -0.0240 0.0311  138 LYS B CA  
2849 C C   . LYS B 160 ? 0.3512 0.2876 0.3047 -0.0274 -0.0213 0.0195  138 LYS B C   
2850 O O   . LYS B 160 ? 0.3140 0.2566 0.2634 -0.0283 -0.0174 0.0065  138 LYS B O   
2851 C CB  . LYS B 160 ? 0.3515 0.2524 0.3376 -0.0303 -0.0245 0.0397  138 LYS B CB  
2852 C CG  . LYS B 160 ? 0.3344 0.2274 0.3350 -0.0251 -0.0091 0.0194  138 LYS B CG  
2853 C CD  . LYS B 160 ? 0.4436 0.3201 0.4897 -0.0152 -0.0030 0.0227  138 LYS B CD  
2854 C CE  . LYS B 160 ? 0.5223 0.3934 0.5729 -0.0157 0.0194  -0.0047 138 LYS B CE  
2855 N NZ  . LYS B 160 ? 0.6010 0.4509 0.7086 -0.0099 0.0366  -0.0109 138 LYS B NZ  
2856 N N   . TRP B 161 ? 0.2345 0.1761 0.1896 -0.0210 -0.0260 0.0270  139 TRP B N   
2857 C CA  . TRP B 161 ? 0.2097 0.1594 0.1652 -0.0119 -0.0233 0.0192  139 TRP B CA  
2858 C C   . TRP B 161 ? 0.2179 0.1543 0.1911 -0.0065 -0.0154 0.0138  139 TRP B C   
2859 O O   . TRP B 161 ? 0.2489 0.1745 0.2487 -0.0031 -0.0163 0.0229  139 TRP B O   
2860 C CB  . TRP B 161 ? 0.2840 0.2430 0.2365 -0.0093 -0.0283 0.0268  139 TRP B CB  
2861 C CG  . TRP B 161 ? 0.3011 0.2719 0.2399 -0.0171 -0.0273 0.0242  139 TRP B CG  
2862 C CD1 . TRP B 161 ? 0.2800 0.2512 0.2048 -0.0316 -0.0282 0.0300  139 TRP B CD1 
2863 C CD2 . TRP B 161 ? 0.2631 0.2457 0.2058 -0.0140 -0.0229 0.0141  139 TRP B CD2 
2864 N NE1 . TRP B 161 ? 0.2762 0.2580 0.1977 -0.0381 -0.0178 0.0177  139 TRP B NE1 
2865 C CE2 . TRP B 161 ? 0.2309 0.2203 0.1715 -0.0244 -0.0158 0.0095  139 TRP B CE2 
2866 C CE3 . TRP B 161 ? 0.1994 0.1861 0.1487 -0.0068 -0.0253 0.0101  139 TRP B CE3 
2867 C CZ2 . TRP B 161 ? 0.2675 0.2683 0.2284 -0.0226 -0.0082 -0.0008 139 TRP B CZ2 
2868 C CZ3 . TRP B 161 ? 0.2406 0.2392 0.2059 -0.0054 -0.0258 0.0071  139 TRP B CZ3 
2869 C CH2 . TRP B 161 ? 0.1886 0.1944 0.1674 -0.0105 -0.0159 0.0009  139 TRP B CH2 
2870 N N   . GLU B 162 ? 0.2480 0.1845 0.2096 -0.0087 -0.0075 -0.0004 140 GLU B N   
2871 C CA  . GLU B 162 ? 0.2969 0.2202 0.2719 -0.0090 0.0080  -0.0123 140 GLU B CA  
2872 C C   . GLU B 162 ? 0.2600 0.1879 0.2535 0.0008  0.0085  -0.0068 140 GLU B C   
2873 O O   . GLU B 162 ? 0.2527 0.1941 0.2329 0.0044  -0.0020 0.0018  140 GLU B O   
2874 C CB  . GLU B 162 ? 0.2807 0.2022 0.2233 -0.0234 0.0157  -0.0285 140 GLU B CB  
2875 C CG  . GLU B 162 ? 0.3575 0.2755 0.2845 -0.0370 0.0148  -0.0355 140 GLU B CG  
2876 C CD  . GLU B 162 ? 0.3894 0.2856 0.3386 -0.0419 0.0339  -0.0486 140 GLU B CD  
2877 O OE1 . GLU B 162 ? 0.3642 0.2488 0.3504 -0.0327 0.0471  -0.0509 140 GLU B OE1 
2878 O OE2 . GLU B 162 ? 0.3759 0.2670 0.3138 -0.0547 0.0356  -0.0561 140 GLU B OE2 
2879 N N   . PRO B 163 ? 0.2764 0.1935 0.3077 0.0043  0.0230  -0.0136 141 PRO B N   
2880 C CA  . PRO B 163 ? 0.2275 0.1519 0.2816 0.0118  0.0252  -0.0110 141 PRO B CA  
2881 C C   . PRO B 163 ? 0.2945 0.2253 0.3072 0.0051  0.0297  -0.0204 141 PRO B C   
2882 O O   . PRO B 163 ? 0.3060 0.2305 0.2820 -0.0085 0.0373  -0.0332 141 PRO B O   
2883 C CB  . PRO B 163 ? 0.2470 0.1570 0.3570 0.0136  0.0481  -0.0248 141 PRO B CB  
2884 C CG  . PRO B 163 ? 0.3334 0.2281 0.4601 0.0117  0.0500  -0.0246 141 PRO B CG  
2885 C CD  . PRO B 163 ? 0.2924 0.1900 0.3573 0.0015  0.0402  -0.0251 141 PRO B CD  
2886 N N   . SER B 164 ? 0.2595 0.2023 0.2760 0.0115  0.0220  -0.0112 142 SER B N   
2887 C CA  . SER B 164 ? 0.2291 0.1768 0.2078 0.0061  0.0211  -0.0137 142 SER B CA  
2888 C C   . SER B 164 ? 0.2247 0.1756 0.2221 0.0080  0.0313  -0.0177 142 SER B C   
2889 O O   . SER B 164 ? 0.2351 0.1899 0.2806 0.0158  0.0342  -0.0154 142 SER B O   
2890 C CB  . SER B 164 ? 0.2513 0.2105 0.2115 0.0099  0.0018  0.0007  142 SER B CB  
2891 O OG  . SER B 164 ? 0.2423 0.2111 0.2228 0.0164  -0.0061 0.0115  142 SER B OG  
2892 N N   . THR B 165 ? 0.2293 0.1789 0.1923 -0.0003 0.0345  -0.0213 143 THR B N   
2893 C CA  . THR B 165 ? 0.2198 0.1731 0.1931 -0.0005 0.0434  -0.0244 143 THR B CA  
2894 C C   . THR B 165 ? 0.2689 0.2275 0.2143 0.0003  0.0287  -0.0119 143 THR B C   
2895 O O   . THR B 165 ? 0.2775 0.2291 0.1863 -0.0084 0.0229  -0.0085 143 THR B O   
2896 C CB  . THR B 165 ? 0.2730 0.2128 0.2329 -0.0179 0.0706  -0.0455 143 THR B CB  
2897 O OG1 . THR B 165 ? 0.3698 0.3028 0.3692 -0.0189 0.0913  -0.0623 143 THR B OG1 
2898 C CG2 . THR B 165 ? 0.2783 0.2226 0.2485 -0.0198 0.0809  -0.0489 143 THR B CG2 
2899 N N   . GLU B 166 ? 0.1918 0.1623 0.1588 0.0086  0.0214  -0.0040 144 GLU B N   
2900 C CA  . GLU B 166 ? 0.1976 0.1710 0.1476 0.0087  0.0129  0.0038  144 GLU B CA  
2901 C C   . GLU B 166 ? 0.2241 0.1924 0.1657 0.0016  0.0247  -0.0015 144 GLU B C   
2902 O O   . GLU B 166 ? 0.2263 0.2003 0.1936 0.0011  0.0357  -0.0086 144 GLU B O   
2903 C CB  . GLU B 166 ? 0.2038 0.1905 0.1718 0.0131  0.0024  0.0113  144 GLU B CB  
2904 C CG  . GLU B 166 ? 0.2051 0.1925 0.1601 0.0103  0.0003  0.0133  144 GLU B CG  
2905 C CD  . GLU B 166 ? 0.1981 0.1962 0.1577 0.0052  -0.0071 0.0167  144 GLU B CD  
2906 O OE1 . GLU B 166 ? 0.2424 0.2492 0.2163 0.0033  -0.0158 0.0232  144 GLU B OE1 
2907 O OE2 . GLU B 166 ? 0.2445 0.2405 0.1944 0.0001  -0.0038 0.0132  144 GLU B OE2 
2908 N N   . LYS B 167 ? 0.2344 0.1919 0.1455 -0.0051 0.0216  0.0036  145 LYS B N   
2909 C CA  . LYS B 167 ? 0.2803 0.2289 0.1759 -0.0157 0.0317  0.0015  145 LYS B CA  
2910 C C   . LYS B 167 ? 0.2798 0.2342 0.1899 -0.0096 0.0277  0.0067  145 LYS B C   
2911 O O   . LYS B 167 ? 0.2700 0.2216 0.1796 -0.0051 0.0171  0.0157  145 LYS B O   
2912 C CB  . LYS B 167 ? 0.2953 0.2262 0.1486 -0.0310 0.0260  0.0099  145 LYS B CB  
2913 C CG  . LYS B 167 ? 0.3863 0.3039 0.2179 -0.0438 0.0298  0.0157  145 LYS B CG  
2914 C CD  . LYS B 167 ? 0.5618 0.4614 0.3488 -0.0635 0.0157  0.0319  145 LYS B CD  
2915 C CE  . LYS B 167 ? 0.5298 0.4134 0.3004 -0.0740 0.0103  0.0478  145 LYS B CE  
2916 N NZ  . LYS B 167 ? 0.5646 0.4368 0.3163 -0.0852 -0.0180 0.0746  145 LYS B NZ  
2917 N N   . MET B 168 ? 0.2515 0.2146 0.1811 -0.0109 0.0380  -0.0008 146 MET B N   
2918 C CA  . MET B 168 ? 0.2409 0.2103 0.1817 -0.0104 0.0363  0.0008  146 MET B CA  
2919 C C   . MET B 168 ? 0.2346 0.1899 0.1585 -0.0208 0.0469  0.0001  146 MET B C   
2920 O O   . MET B 168 ? 0.2511 0.2032 0.1706 -0.0302 0.0613  -0.0080 146 MET B O   
2921 C CB  . MET B 168 ? 0.2255 0.2165 0.2012 -0.0088 0.0353  -0.0030 146 MET B CB  
2922 C CG  . MET B 168 ? 0.2185 0.2210 0.2084 -0.0025 0.0209  0.0032  146 MET B CG  
2923 S SD  . MET B 168 ? 0.2560 0.2589 0.2270 -0.0064 0.0106  0.0075  146 MET B SD  
2924 C CE  . MET B 168 ? 0.2406 0.2620 0.2287 -0.0104 -0.0073 0.0171  146 MET B CE  
2925 N N   . TYR B 169 ? 0.2533 0.1987 0.1717 -0.0210 0.0428  0.0069  147 TYR B N   
2926 C CA  . TYR B 169 ? 0.2697 0.1969 0.1719 -0.0317 0.0502  0.0106  147 TYR B CA  
2927 C C   . TYR B 169 ? 0.2655 0.1866 0.1824 -0.0292 0.0494  0.0129  147 TYR B C   
2928 O O   . TYR B 169 ? 0.2870 0.2159 0.2208 -0.0219 0.0451  0.0101  147 TYR B O   
2929 C CB  . TYR B 169 ? 0.2912 0.1972 0.1600 -0.0407 0.0436  0.0241  147 TYR B CB  
2930 C CG  . TYR B 169 ? 0.3020 0.2009 0.1766 -0.0321 0.0241  0.0406  147 TYR B CG  
2931 C CD1 . TYR B 169 ? 0.2866 0.1984 0.1712 -0.0219 0.0155  0.0388  147 TYR B CD1 
2932 C CD2 . TYR B 169 ? 0.3744 0.2538 0.2544 -0.0341 0.0145  0.0586  147 TYR B CD2 
2933 C CE1 . TYR B 169 ? 0.2704 0.1786 0.1700 -0.0147 -0.0008 0.0524  147 TYR B CE1 
2934 C CE2 . TYR B 169 ? 0.3540 0.2294 0.2575 -0.0251 -0.0034 0.0745  147 TYR B CE2 
2935 C CZ  . TYR B 169 ? 0.3123 0.2037 0.2262 -0.0156 -0.0102 0.0701  147 TYR B CZ  
2936 O OH  . TYR B 169 ? 0.3464 0.2369 0.2936 -0.0072 -0.0266 0.0845  147 TYR B OH  
2937 N N   . VAL B 170 ? 0.2815 0.1864 0.1915 -0.0386 0.0572  0.0158  148 VAL B N   
2938 C CA  . VAL B 170 ? 0.3195 0.2138 0.2482 -0.0386 0.0619  0.0148  148 VAL B CA  
2939 C C   . VAL B 170 ? 0.3780 0.2456 0.3113 -0.0357 0.0518  0.0350  148 VAL B C   
2940 O O   . VAL B 170 ? 0.3403 0.1898 0.2489 -0.0454 0.0455  0.0515  148 VAL B O   
2941 C CB  . VAL B 170 ? 0.3628 0.2559 0.2901 -0.0513 0.0768  0.0053  148 VAL B CB  
2942 C CG1 . VAL B 170 ? 0.3261 0.2036 0.2731 -0.0539 0.0854  0.0015  148 VAL B CG1 
2943 C CG2 . VAL B 170 ? 0.3637 0.2879 0.3002 -0.0544 0.0806  -0.0099 148 VAL B CG2 
2944 N N   . ARG B 171 ? 0.3439 0.2091 0.3118 -0.0255 0.0502  0.0344  149 ARG B N   
2945 C CA  . ARG B 171 ? 0.3439 0.1875 0.3408 -0.0193 0.0384  0.0553  149 ARG B CA  
2946 C C   . ARG B 171 ? 0.3471 0.1769 0.3896 -0.0176 0.0558  0.0447  149 ARG B C   
2947 O O   . ARG B 171 ? 0.3865 0.2284 0.4496 -0.0157 0.0714  0.0215  149 ARG B O   
2948 C CB  . ARG B 171 ? 0.3294 0.1847 0.3431 -0.0077 0.0237  0.0615  149 ARG B CB  
2949 C CG  . ARG B 171 ? 0.4855 0.3233 0.5411 -0.0011 0.0041  0.0892  149 ARG B CG  
2950 C CD  . ARG B 171 ? 0.4329 0.2876 0.5139 0.0098  -0.0077 0.0908  149 ARG B CD  
2951 N NE  . ARG B 171 ? 0.5727 0.4170 0.6850 0.0124  -0.0370 0.1248  149 ARG B NE  
2952 C CZ  . ARG B 171 ? 0.8001 0.6481 0.8675 0.0013  -0.0625 0.1449  149 ARG B CZ  
2953 N NH1 . ARG B 171 ? 0.6696 0.5213 0.6689 -0.0112 -0.0602 0.1384  149 ARG B NH1 
2954 N NH2 . ARG B 171 ? 0.8152 0.6694 0.9070 -0.0003 -0.0863 0.1645  149 ARG B NH2 
2955 N N   . ASP B 172 ? 0.4324 0.2346 0.4885 -0.0221 0.0551  0.0606  150 ASP B N   
2956 C CA  . ASP B 172 ? 0.5003 0.2835 0.6069 -0.0217 0.0755  0.0495  150 ASP B CA  
2957 C C   . ASP B 172 ? 0.5751 0.3735 0.6679 -0.0325 0.1032  0.0125  150 ASP B C   
2958 O O   . ASP B 172 ? 0.4309 0.2276 0.5592 -0.0344 0.1249  -0.0108 150 ASP B O   
2959 C CB  . ASP B 172 ? 0.6094 0.3872 0.7872 -0.0067 0.0736  0.0536  150 ASP B CB  
2960 C CG  . ASP B 172 ? 0.6840 0.4577 0.8750 0.0009  0.0376  0.0920  150 ASP B CG  
2961 O OD1 . ASP B 172 ? 0.7478 0.5368 0.9843 0.0129  0.0270  0.0963  150 ASP B OD1 
2962 O OD2 . ASP B 172 ? 0.8219 0.5789 0.9744 -0.0095 0.0212  0.1163  150 ASP B OD2 
2963 N N   . GLY B 173 ? 0.3724 0.1870 0.4150 -0.0433 0.1026  0.0066  151 GLY B N   
2964 C CA  . GLY B 173 ? 0.4148 0.2465 0.4436 -0.0578 0.1207  -0.0214 151 GLY B CA  
2965 C C   . GLY B 173 ? 0.4069 0.2675 0.4259 -0.0594 0.1199  -0.0377 151 GLY B C   
2966 O O   . GLY B 173 ? 0.4183 0.2923 0.4256 -0.0769 0.1315  -0.0586 151 GLY B O   
2967 N N   . VAL B 174 ? 0.3129 0.1827 0.3328 -0.0457 0.1047  -0.0271 152 VAL B N   
2968 C CA  . VAL B 174 ? 0.2914 0.1839 0.3028 -0.0483 0.1034  -0.0395 152 VAL B CA  
2969 C C   . VAL B 174 ? 0.3081 0.2200 0.2951 -0.0398 0.0821  -0.0255 152 VAL B C   
2970 O O   . VAL B 174 ? 0.2926 0.1967 0.2791 -0.0278 0.0698  -0.0078 152 VAL B O   
2971 C CB  . VAL B 174 ? 0.2883 0.1714 0.3362 -0.0414 0.1123  -0.0458 152 VAL B CB  
2972 C CG1 . VAL B 174 ? 0.3687 0.2731 0.3992 -0.0486 0.1119  -0.0581 152 VAL B CG1 
2973 C CG2 . VAL B 174 ? 0.3278 0.1885 0.4126 -0.0509 0.1408  -0.0649 152 VAL B CG2 
2974 N N   . LEU B 175 ? 0.3020 0.2381 0.2706 -0.0491 0.0772  -0.0325 153 LEU B N   
2975 C CA  . LEU B 175 ? 0.2766 0.2296 0.2350 -0.0405 0.0604  -0.0217 153 LEU B CA  
2976 C C   . LEU B 175 ? 0.2345 0.1855 0.1974 -0.0293 0.0539  -0.0169 153 LEU B C   
2977 O O   . LEU B 175 ? 0.2584 0.2110 0.2259 -0.0353 0.0601  -0.0269 153 LEU B O   
2978 C CB  . LEU B 175 ? 0.2617 0.2404 0.2134 -0.0529 0.0522  -0.0252 153 LEU B CB  
2979 C CG  . LEU B 175 ? 0.2838 0.2783 0.2403 -0.0429 0.0368  -0.0141 153 LEU B CG  
2980 C CD1 . LEU B 175 ? 0.2557 0.2443 0.2182 -0.0341 0.0413  -0.0103 153 LEU B CD1 
2981 C CD2 . LEU B 175 ? 0.2435 0.2632 0.2065 -0.0555 0.0226  -0.0107 153 LEU B CD2 
2982 N N   . THR B 176 ? 0.2245 0.1713 0.1843 -0.0173 0.0437  -0.0037 154 THR B N   
2983 C CA  . THR B 176 ? 0.2384 0.1820 0.2055 -0.0074 0.0357  0.0031  154 THR B CA  
2984 C C   . THR B 176 ? 0.2797 0.2335 0.2314 -0.0031 0.0247  0.0091  154 THR B C   
2985 O O   . THR B 176 ? 0.2639 0.2173 0.2037 -0.0055 0.0254  0.0112  154 THR B O   
2986 C CB  . THR B 176 ? 0.2402 0.1633 0.2223 -0.0016 0.0320  0.0165  154 THR B CB  
2987 O OG1 . THR B 176 ? 0.2914 0.2021 0.2995 -0.0047 0.0460  0.0091  154 THR B OG1 
2988 C CG2 . THR B 176 ? 0.2252 0.1492 0.2243 0.0074  0.0201  0.0256  154 THR B CG2 
2989 N N   . GLY B 177 ? 0.2223 0.1840 0.1771 0.0010  0.0187  0.0088  155 GLY B N   
2990 C CA  . GLY B 177 ? 0.2041 0.1715 0.1491 0.0049  0.0105  0.0131  155 GLY B CA  
2991 C C   . GLY B 177 ? 0.2647 0.2270 0.2114 0.0100  0.0021  0.0200  155 GLY B C   
2992 O O   . GLY B 177 ? 0.2296 0.1949 0.1931 0.0123  0.0023  0.0175  155 GLY B O   
2993 N N   . ASP B 178 ? 0.2686 0.2233 0.1986 0.0079  -0.0041 0.0276  156 ASP B N   
2994 C CA  . ASP B 178 ? 0.2306 0.1826 0.1591 0.0081  -0.0171 0.0370  156 ASP B CA  
2995 C C   . ASP B 178 ? 0.2727 0.2296 0.1859 0.0055  -0.0170 0.0311  156 ASP B C   
2996 O O   . ASP B 178 ? 0.2620 0.2167 0.1616 0.0003  -0.0073 0.0234  156 ASP B O   
2997 C CB  . ASP B 178 ? 0.2471 0.1844 0.1595 -0.0011 -0.0283 0.0533  156 ASP B CB  
2998 C CG  . ASP B 178 ? 0.3434 0.2728 0.2863 0.0037  -0.0329 0.0646  156 ASP B CG  
2999 O OD1 . ASP B 178 ? 0.2855 0.2210 0.2639 0.0134  -0.0238 0.0554  156 ASP B OD1 
3000 O OD2 . ASP B 178 ? 0.2881 0.2027 0.2198 -0.0053 -0.0445 0.0827  156 ASP B OD2 
3001 N N   . ILE B 179 ? 0.2703 0.2334 0.1930 0.0086  -0.0248 0.0326  157 ILE B N   
3002 C CA  . ILE B 179 ? 0.2684 0.2333 0.1795 0.0053  -0.0240 0.0267  157 ILE B CA  
3003 C C   . ILE B 179 ? 0.3046 0.2709 0.2135 0.0005  -0.0382 0.0343  157 ILE B C   
3004 O O   . ILE B 179 ? 0.2623 0.2362 0.1987 0.0067  -0.0461 0.0400  157 ILE B O   
3005 C CB  . ILE B 179 ? 0.2198 0.1932 0.1466 0.0116  -0.0184 0.0196  157 ILE B CB  
3006 C CG1 . ILE B 179 ? 0.2004 0.1784 0.1370 0.0141  -0.0126 0.0177  157 ILE B CG1 
3007 C CG2 . ILE B 179 ? 0.2107 0.1803 0.1328 0.0087  -0.0131 0.0132  157 ILE B CG2 
3008 C CD1 . ILE B 179 ? 0.2082 0.1939 0.1537 0.0134  -0.0141 0.0176  157 ILE B CD1 
3009 N N   . GLU B 180 ? 0.2656 0.2252 0.1457 -0.0131 -0.0396 0.0322  158 GLU B N   
3010 C CA  . GLU B 180 ? 0.3286 0.2923 0.2047 -0.0209 -0.0526 0.0363  158 GLU B CA  
3011 C C   . GLU B 180 ? 0.3780 0.3449 0.2638 -0.0155 -0.0413 0.0227  158 GLU B C   
3012 O O   . GLU B 180 ? 0.3481 0.3061 0.2216 -0.0206 -0.0264 0.0102  158 GLU B O   
3013 C CB  . GLU B 180 ? 0.3598 0.3128 0.1911 -0.0463 -0.0598 0.0399  158 GLU B CB  
3014 C CG  . GLU B 180 ? 0.5122 0.4577 0.3267 -0.0569 -0.0722 0.0569  158 GLU B CG  
3015 C CD  . GLU B 180 ? 0.6073 0.5461 0.3874 -0.0856 -0.0765 0.0581  158 GLU B CD  
3016 O OE1 . GLU B 180 ? 0.6467 0.5883 0.4165 -0.0974 -0.0782 0.0519  158 GLU B OE1 
3017 O OE2 . GLU B 180 ? 0.6481 0.5774 0.4096 -0.0995 -0.0779 0.0651  158 GLU B OE2 
3018 N N   . MET B 181 ? 0.2618 0.2397 0.1747 -0.0065 -0.0459 0.0246  159 MET B N   
3019 C CA  . MET B 181 ? 0.2461 0.2252 0.1669 -0.0035 -0.0377 0.0161  159 MET B CA  
3020 C C   . MET B 181 ? 0.2340 0.2163 0.1521 -0.0127 -0.0452 0.0150  159 MET B C   
3021 O O   . MET B 181 ? 0.2509 0.2404 0.1710 -0.0193 -0.0606 0.0236  159 MET B O   
3022 C CB  . MET B 181 ? 0.2368 0.2240 0.1801 0.0049  -0.0341 0.0163  159 MET B CB  
3023 C CG  . MET B 181 ? 0.2464 0.2320 0.1902 0.0096  -0.0275 0.0164  159 MET B CG  
3024 S SD  . MET B 181 ? 0.2723 0.2517 0.2140 0.0100  -0.0223 0.0157  159 MET B SD  
3025 C CE  . MET B 181 ? 0.2779 0.2620 0.2223 0.0041  -0.0244 0.0189  159 MET B CE  
3026 N N   . ALA B 182 ? 0.2528 0.2298 0.1705 -0.0144 -0.0366 0.0069  160 ALA B N   
3027 C CA  . ALA B 182 ? 0.2549 0.2345 0.1703 -0.0248 -0.0415 0.0037  160 ALA B CA  
3028 C C   . ALA B 182 ? 0.2826 0.2593 0.2109 -0.0217 -0.0332 -0.0004 160 ALA B C   
3029 O O   . ALA B 182 ? 0.2765 0.2404 0.2060 -0.0182 -0.0234 -0.0026 160 ALA B O   
3030 C CB  . ALA B 182 ? 0.2875 0.2547 0.1722 -0.0424 -0.0378 -0.0050 160 ALA B CB  
3031 N N   . LEU B 183 ? 0.2325 0.2211 0.1756 -0.0246 -0.0380 0.0002  161 LEU B N   
3032 C CA  . LEU B 183 ? 0.2919 0.2757 0.2398 -0.0284 -0.0307 -0.0032 161 LEU B CA  
3033 C C   . LEU B 183 ? 0.3467 0.3232 0.2852 -0.0403 -0.0300 -0.0106 161 LEU B C   
3034 O O   . LEU B 183 ? 0.3061 0.2942 0.2439 -0.0495 -0.0401 -0.0119 161 LEU B O   
3035 C CB  . LEU B 183 ? 0.2543 0.2538 0.2235 -0.0301 -0.0295 -0.0041 161 LEU B CB  
3036 C CG  . LEU B 183 ? 0.3143 0.3148 0.2858 -0.0268 -0.0217 -0.0026 161 LEU B CG  
3037 C CD1 . LEU B 183 ? 0.2207 0.2377 0.2216 -0.0308 -0.0140 -0.0105 161 LEU B CD1 
3038 C CD2 . LEU B 183 ? 0.3193 0.3045 0.2709 -0.0339 -0.0168 0.0020  161 LEU B CD2 
3039 N N   . LEU B 184 ? 0.3206 0.2772 0.2555 -0.0419 -0.0194 -0.0142 162 LEU B N   
3040 C CA  . LEU B 184 ? 0.3284 0.2748 0.2587 -0.0551 -0.0137 -0.0240 162 LEU B CA  
3041 C C   . LEU B 184 ? 0.3480 0.3043 0.2883 -0.0610 -0.0165 -0.0223 162 LEU B C   
3042 O O   . LEU B 184 ? 0.3648 0.3196 0.3115 -0.0574 -0.0141 -0.0148 162 LEU B O   
3043 C CB  . LEU B 184 ? 0.3474 0.2668 0.2867 -0.0533 0.0008  -0.0276 162 LEU B CB  
3044 C CG  . LEU B 184 ? 0.4402 0.3430 0.3787 -0.0683 0.0122  -0.0413 162 LEU B CG  
3045 C CD1 . LEU B 184 ? 0.4519 0.3558 0.3641 -0.0865 0.0166  -0.0590 162 LEU B CD1 
3046 C CD2 . LEU B 184 ? 0.3542 0.2285 0.3214 -0.0630 0.0265  -0.0409 162 LEU B CD2 
3047 N N   . LEU B 185 ? 0.4261 0.3928 0.3653 -0.0742 -0.0213 -0.0296 163 LEU B N   
3048 C CA  . LEU B 185 ? 0.3399 0.3194 0.2951 -0.0822 -0.0219 -0.0313 163 LEU B CA  
3049 C C   . LEU B 185 ? 0.3850 0.3459 0.3325 -0.0960 -0.0121 -0.0400 163 LEU B C   
3050 O O   . LEU B 185 ? 0.4572 0.3984 0.3905 -0.1018 -0.0052 -0.0480 163 LEU B O   
3051 C CB  . LEU B 185 ? 0.4129 0.4224 0.3869 -0.0879 -0.0380 -0.0307 163 LEU B CB  
3052 C CG  . LEU B 185 ? 0.3582 0.3860 0.3532 -0.0749 -0.0484 -0.0212 163 LEU B CG  
3053 C CD1 . LEU B 185 ? 0.3676 0.4254 0.3996 -0.0813 -0.0678 -0.0162 163 LEU B CD1 
3054 C CD2 . LEU B 185 ? 0.3306 0.3572 0.3390 -0.0643 -0.0339 -0.0213 163 LEU B CD2 
3055 N N   . GLU B 186 ? 0.4891 0.3528 0.5298 -0.2388 -0.0491 -0.0040 164 GLU B N   
3056 C CA  . GLU B 186 ? 0.5700 0.4116 0.6273 -0.2574 -0.0495 -0.0113 164 GLU B CA  
3057 C C   . GLU B 186 ? 0.7220 0.5834 0.7733 -0.2713 -0.0552 -0.0386 164 GLU B C   
3058 O O   . GLU B 186 ? 0.7037 0.6181 0.7430 -0.2742 -0.0596 -0.0392 164 GLU B O   
3059 C CB  . GLU B 186 ? 0.6448 0.5111 0.7141 -0.2722 -0.0495 0.0151  164 GLU B CB  
3060 C CG  . GLU B 186 ? 0.7164 0.5538 0.7940 -0.2630 -0.0437 0.0400  164 GLU B CG  
3061 C CD  . GLU B 186 ? 0.8815 0.7583 0.9634 -0.2737 -0.0436 0.0678  164 GLU B CD  
3062 O OE1 . GLU B 186 ? 0.7975 0.7138 0.8826 -0.2919 -0.0470 0.0663  164 GLU B OE1 
3063 O OE2 . GLU B 186 ? 0.7917 0.6650 0.8728 -0.2630 -0.0401 0.0909  164 GLU B OE2 
3064 N N   . GLY B 187 ? 0.6858 0.5072 0.7471 -0.2783 -0.0553 -0.0607 165 GLY B N   
3065 C CA  . GLY B 187 ? 0.6588 0.4960 0.7102 -0.2895 -0.0613 -0.0889 165 GLY B CA  
3066 C C   . GLY B 187 ? 0.6600 0.4885 0.6912 -0.2721 -0.0601 -0.1129 165 GLY B C   
3067 O O   . GLY B 187 ? 0.7313 0.5782 0.7491 -0.2804 -0.0642 -0.1358 165 GLY B O   
3068 N N   . ASN B 188 ? 0.6662 0.4720 0.6934 -0.2486 -0.0540 -0.1071 166 ASN B N   
3069 C CA  . ASN B 188 ? 0.7299 0.5188 0.7413 -0.2285 -0.0502 -0.1275 166 ASN B CA  
3070 C C   . ASN B 188 ? 0.6328 0.4752 0.6191 -0.2232 -0.0510 -0.1294 166 ASN B C   
3071 O O   . ASN B 188 ? 0.7031 0.5426 0.6743 -0.2071 -0.0468 -0.1441 166 ASN B O   
3072 C CB  . ASN B 188 ? 0.7495 0.5077 0.7601 -0.2332 -0.0519 -0.1577 166 ASN B CB  
3073 C CG  . ASN B 188 ? 0.7947 0.5432 0.7854 -0.2125 -0.0460 -0.1794 166 ASN B CG  
3074 O OD1 . ASN B 188 ? 0.9877 0.7139 0.9723 -0.2146 -0.0453 -0.2044 166 ASN B OD1 
3075 N ND2 . ASN B 188 ? 0.8945 0.6565 0.8761 -0.1926 -0.0405 -0.1695 166 ASN B ND2 
3076 N N   . ALA B 189 ? 0.5438 0.4373 0.5278 -0.2340 -0.0564 -0.1127 167 ALA B N   
3077 C CA  . ALA B 189 ? 0.5476 0.4908 0.5138 -0.2251 -0.0588 -0.1099 167 ALA B CA  
3078 C C   . ALA B 189 ? 0.5142 0.4470 0.4778 -0.2015 -0.0536 -0.0937 167 ALA B C   
3079 O O   . ALA B 189 ? 0.5240 0.4205 0.4995 -0.1929 -0.0489 -0.0800 167 ALA B O   
3080 C CB  . ALA B 189 ? 0.5077 0.5128 0.4782 -0.2381 -0.0668 -0.0944 167 ALA B CB  
3081 N N   . HIS B 190 ? 0.4125 0.3809 0.3637 -0.1835 -0.0538 -0.0907 168 HIS B N   
3082 C CA  . HIS B 190 ? 0.3772 0.3421 0.3286 -0.1541 -0.0481 -0.0731 168 HIS B CA  
3083 C C   . HIS B 190 ? 0.4202 0.4376 0.3749 -0.1451 -0.0517 -0.0517 168 HIS B C   
3084 O O   . HIS B 190 ? 0.4139 0.4763 0.3675 -0.1564 -0.0590 -0.0516 168 HIS B O   
3085 C CB  . HIS B 190 ? 0.3917 0.3422 0.3283 -0.1375 -0.0428 -0.0881 168 HIS B CB  
3086 C CG  . HIS B 190 ? 0.4130 0.3074 0.3532 -0.1343 -0.0357 -0.1036 168 HIS B CG  
3087 N ND1 . HIS B 190 ? 0.4479 0.3190 0.3841 -0.1501 -0.0345 -0.1329 168 HIS B ND1 
3088 C CD2 . HIS B 190 ? 0.4143 0.2729 0.3640 -0.1163 -0.0294 -0.0942 168 HIS B CD2 
3089 C CE1 . HIS B 190 ? 0.5495 0.3697 0.4955 -0.1398 -0.0270 -0.1404 168 HIS B CE1 
3090 N NE2 . HIS B 190 ? 0.4371 0.2511 0.3916 -0.1193 -0.0246 -0.1153 168 HIS B NE2 
3091 N N   . TYR B 191 ? 0.3500 0.3617 0.3103 -0.1242 -0.0465 -0.0341 169 TYR B N   
3092 C CA  . TYR B 191 ? 0.3358 0.3881 0.3040 -0.1124 -0.0470 -0.0148 169 TYR B CA  
3093 C C   . TYR B 191 ? 0.3021 0.3428 0.2640 -0.0866 -0.0415 -0.0099 169 TYR B C   
3094 O O   . TYR B 191 ? 0.3015 0.3101 0.2640 -0.0773 -0.0356 -0.0069 169 TYR B O   
3095 C CB  . TYR B 191 ? 0.3351 0.3921 0.3185 -0.1191 -0.0450 -0.0002 169 TYR B CB  
3096 C CG  . TYR B 191 ? 0.2534 0.3471 0.2476 -0.1047 -0.0419 0.0168  169 TYR B CG  
3097 C CD1 . TYR B 191 ? 0.2976 0.4397 0.2994 -0.1009 -0.0461 0.0219  169 TYR B CD1 
3098 C CD2 . TYR B 191 ? 0.2434 0.3259 0.2419 -0.0958 -0.0348 0.0274  169 TYR B CD2 
3099 C CE1 . TYR B 191 ? 0.2711 0.4446 0.2872 -0.0854 -0.0416 0.0351  169 TYR B CE1 
3100 C CE2 . TYR B 191 ? 0.2265 0.3425 0.2350 -0.0832 -0.0300 0.0380  169 TYR B CE2 
3101 C CZ  . TYR B 191 ? 0.2786 0.4376 0.2972 -0.0769 -0.0327 0.0408  169 TYR B CZ  
3102 O OH  . TYR B 191 ? 0.2023 0.3923 0.2348 -0.0618 -0.0264 0.0491  169 TYR B OH  
3103 N N   . ARG B 192 ? 0.2525 0.3201 0.2089 -0.0769 -0.0441 -0.0080 170 ARG B N   
3104 C CA  . ARG B 192 ? 0.2664 0.3217 0.2154 -0.0567 -0.0397 -0.0052 170 ARG B CA  
3105 C C   . ARG B 192 ? 0.2616 0.3233 0.2219 -0.0392 -0.0354 0.0107  170 ARG B C   
3106 O O   . ARG B 192 ? 0.2628 0.3546 0.2365 -0.0383 -0.0368 0.0208  170 ARG B O   
3107 C CB  . ARG B 192 ? 0.3266 0.4092 0.2652 -0.0558 -0.0447 -0.0067 170 ARG B CB  
3108 C CG  . ARG B 192 ? 0.3655 0.4529 0.3037 -0.0352 -0.0423 0.0066  170 ARG B CG  
3109 C CD  . ARG B 192 ? 0.5529 0.6543 0.4745 -0.0368 -0.0453 0.0027  170 ARG B CD  
3110 N NE  . ARG B 192 ? 0.5363 0.6386 0.4584 -0.0198 -0.0431 0.0175  170 ARG B NE  
3111 C CZ  . ARG B 192 ? 0.4474 0.5696 0.3579 -0.0197 -0.0460 0.0227  170 ARG B CZ  
3112 N NH1 . ARG B 192 ? 0.4570 0.6046 0.3519 -0.0351 -0.0511 0.0124  170 ARG B NH1 
3113 N NH2 . ARG B 192 ? 0.3412 0.4589 0.2551 -0.0055 -0.0437 0.0383  170 ARG B NH2 
3114 N N   . CYS B 193 ? 0.2303 0.2654 0.1860 -0.0254 -0.0295 0.0113  171 CYS B N   
3115 C CA  . CYS B 193 ? 0.2177 0.2550 0.1812 -0.0093 -0.0247 0.0216  171 CYS B CA  
3116 C C   . CYS B 193 ? 0.3079 0.3294 0.2632 0.0028  -0.0223 0.0214  171 CYS B C   
3117 O O   . CYS B 193 ? 0.2959 0.2949 0.2413 0.0009  -0.0207 0.0132  171 CYS B O   
3118 C CB  . CYS B 193 ? 0.2122 0.2345 0.1798 -0.0104 -0.0195 0.0231  171 CYS B CB  
3119 S SG  . CYS B 193 ? 0.2596 0.2876 0.2349 0.0062  -0.0121 0.0296  171 CYS B SG  
3120 N N   . ASP B 194 ? 0.2494 0.2823 0.2116 0.0155  -0.0214 0.0309  172 ASP B N   
3121 C CA  . ASP B 194 ? 0.2342 0.2511 0.1909 0.0253  -0.0187 0.0332  172 ASP B CA  
3122 C C   . ASP B 194 ? 0.2352 0.2343 0.1975 0.0340  -0.0121 0.0333  172 ASP B C   
3123 O O   . ASP B 194 ? 0.2359 0.2450 0.2106 0.0402  -0.0095 0.0366  172 ASP B O   
3124 C CB  . ASP B 194 ? 0.2460 0.2830 0.2075 0.0322  -0.0228 0.0456  172 ASP B CB  
3125 C CG  . ASP B 194 ? 0.3715 0.4312 0.3226 0.0214  -0.0299 0.0450  172 ASP B CG  
3126 O OD1 . ASP B 194 ? 0.3358 0.3859 0.2714 0.0157  -0.0289 0.0365  172 ASP B OD1 
3127 O OD2 . ASP B 194 ? 0.4372 0.5277 0.3958 0.0179  -0.0361 0.0514  172 ASP B OD2 
3128 N N   . PHE B 195 ? 0.2385 0.2152 0.1924 0.0343  -0.0091 0.0285  173 PHE B N   
3129 C CA  . PHE B 195 ? 0.2889 0.2509 0.2445 0.0394  -0.0039 0.0270  173 PHE B CA  
3130 C C   . PHE B 195 ? 0.2958 0.2487 0.2522 0.0464  -0.0023 0.0307  173 PHE B C   
3131 O O   . PHE B 195 ? 0.2476 0.1991 0.1975 0.0449  -0.0042 0.0332  173 PHE B O   
3132 C CB  . PHE B 195 ? 0.2325 0.1794 0.1807 0.0342  -0.0030 0.0220  173 PHE B CB  
3133 C CG  . PHE B 195 ? 0.2156 0.1647 0.1650 0.0268  -0.0035 0.0216  173 PHE B CG  
3134 C CD1 . PHE B 195 ? 0.2926 0.2574 0.2472 0.0214  -0.0052 0.0232  173 PHE B CD1 
3135 C CD2 . PHE B 195 ? 0.2310 0.1688 0.1777 0.0244  -0.0028 0.0223  173 PHE B CD2 
3136 C CE1 . PHE B 195 ? 0.3080 0.2745 0.2642 0.0120  -0.0056 0.0253  173 PHE B CE1 
3137 C CE2 . PHE B 195 ? 0.2348 0.1738 0.1834 0.0165  -0.0039 0.0264  173 PHE B CE2 
3138 C CZ  . PHE B 195 ? 0.2575 0.2096 0.2104 0.0095  -0.0050 0.0279  173 PHE B CZ  
3139 N N   . ARG B 196 ? 0.2734 0.2200 0.2376 0.0527  0.0020  0.0301  174 ARG B N   
3140 C CA  . ARG B 196 ? 0.3191 0.2491 0.2837 0.0554  0.0043  0.0310  174 ARG B CA  
3141 C C   . ARG B 196 ? 0.2625 0.1833 0.2263 0.0540  0.0093  0.0209  174 ARG B C   
3142 O O   . ARG B 196 ? 0.2483 0.1746 0.2185 0.0575  0.0133  0.0154  174 ARG B O   
3143 C CB  . ARG B 196 ? 0.2484 0.1766 0.2259 0.0639  0.0042  0.0407  174 ARG B CB  
3144 C CG  . ARG B 196 ? 0.2749 0.1805 0.2552 0.0644  0.0075  0.0406  174 ARG B CG  
3145 C CD  . ARG B 196 ? 0.2912 0.1944 0.2849 0.0681  0.0047  0.0541  174 ARG B CD  
3146 N NE  . ARG B 196 ? 0.2704 0.1888 0.2554 0.0638  -0.0010 0.0671  174 ARG B NE  
3147 C CZ  . ARG B 196 ? 0.3222 0.2492 0.3144 0.0648  -0.0058 0.0816  174 ARG B CZ  
3148 N NH1 . ARG B 196 ? 0.3465 0.2643 0.3563 0.0714  -0.0060 0.0858  174 ARG B NH1 
3149 N NH2 . ARG B 196 ? 0.3234 0.2692 0.3035 0.0593  -0.0101 0.0916  174 ARG B NH2 
3150 N N   . THR B 197 ? 0.2499 0.1617 0.2059 0.0483  0.0092  0.0181  175 THR B N   
3151 C CA  . THR B 197 ? 0.2300 0.1379 0.1826 0.0440  0.0124  0.0089  175 THR B CA  
3152 C C   . THR B 197 ? 0.3174 0.2102 0.2722 0.0418  0.0139  0.0072  175 THR B C   
3153 O O   . THR B 197 ? 0.2876 0.1775 0.2413 0.0396  0.0113  0.0147  175 THR B O   
3154 C CB  . THR B 197 ? 0.2705 0.1862 0.2142 0.0373  0.0094  0.0095  175 THR B CB  
3155 O OG1 . THR B 197 ? 0.2791 0.2035 0.2225 0.0375  0.0073  0.0133  175 THR B OG1 
3156 C CG2 . THR B 197 ? 0.2207 0.1422 0.1591 0.0312  0.0114  0.0019  175 THR B CG2 
3157 N N   . THR B 198 ? 0.2725 0.1568 0.2303 0.0408  0.0187  -0.0039 176 THR B N   
3158 C CA  . THR B 198 ? 0.2865 0.1552 0.2455 0.0340  0.0198  -0.0085 176 THR B CA  
3159 C C   . THR B 198 ? 0.3216 0.2011 0.2696 0.0230  0.0196  -0.0196 176 THR B C   
3160 O O   . THR B 198 ? 0.2727 0.1658 0.2147 0.0223  0.0217  -0.0276 176 THR B O   
3161 C CB  . THR B 198 ? 0.3406 0.1872 0.3133 0.0396  0.0255  -0.0149 176 THR B CB  
3162 O OG1 . THR B 198 ? 0.3471 0.1989 0.3217 0.0445  0.0318  -0.0299 176 THR B OG1 
3163 C CG2 . THR B 198 ? 0.3731 0.2128 0.3584 0.0500  0.0235  0.0022  176 THR B CG2 
3164 N N   . TYR B 199 ? 0.2950 0.1741 0.2406 0.0133  0.0166  -0.0179 177 TYR B N   
3165 C CA  . TYR B 199 ? 0.3066 0.2027 0.2428 0.0016  0.0138  -0.0239 177 TYR B CA  
3166 C C   . TYR B 199 ? 0.3212 0.2052 0.2591 -0.0107 0.0154  -0.0353 177 TYR B C   
3167 O O   . TYR B 199 ? 0.2999 0.1678 0.2464 -0.0125 0.0154  -0.0291 177 TYR B O   
3168 C CB  . TYR B 199 ? 0.3312 0.2440 0.2668 0.0009  0.0076  -0.0098 177 TYR B CB  
3169 C CG  . TYR B 199 ? 0.2706 0.1900 0.2064 0.0112  0.0059  0.0004  177 TYR B CG  
3170 C CD1 . TYR B 199 ? 0.2580 0.1923 0.1885 0.0110  0.0035  0.0024  177 TYR B CD1 
3171 C CD2 . TYR B 199 ? 0.3027 0.2142 0.2433 0.0188  0.0063  0.0081  177 TYR B CD2 
3172 C CE1 . TYR B 199 ? 0.2345 0.1701 0.1670 0.0181  0.0018  0.0110  177 TYR B CE1 
3173 C CE2 . TYR B 199 ? 0.2609 0.1770 0.2012 0.0256  0.0048  0.0136  177 TYR B CE2 
3174 C CZ  . TYR B 199 ? 0.2905 0.2157 0.2279 0.0251  0.0027  0.0145  177 TYR B CZ  
3175 O OH  . TYR B 199 ? 0.2712 0.1963 0.2100 0.0296  0.0012  0.0192  177 TYR B OH  
3176 N N   . LYS B 200 ? 0.3209 0.2142 0.2500 -0.0212 0.0168  -0.0519 178 LYS B N   
3177 C CA  . LYS B 200 ? 0.2939 0.1750 0.2238 -0.0361 0.0184  -0.0670 178 LYS B CA  
3178 C C   . LYS B 200 ? 0.3082 0.2205 0.2242 -0.0527 0.0139  -0.0762 178 LYS B C   
3179 O O   . LYS B 200 ? 0.3456 0.2757 0.2495 -0.0542 0.0159  -0.0868 178 LYS B O   
3180 C CB  . LYS B 200 ? 0.4115 0.2620 0.3480 -0.0324 0.0279  -0.0866 178 LYS B CB  
3181 C CG  . LYS B 200 ? 0.5939 0.4237 0.5446 -0.0124 0.0322  -0.0770 178 LYS B CG  
3182 C CD  . LYS B 200 ? 0.7130 0.5122 0.6760 -0.0068 0.0421  -0.0965 178 LYS B CD  
3183 C CE  . LYS B 200 ? 0.6912 0.4705 0.6745 0.0122  0.0431  -0.0799 178 LYS B CE  
3184 N NZ  . LYS B 200 ? 0.7997 0.5554 0.7996 0.0169  0.0442  -0.0868 178 LYS B NZ  
3185 N N   . ALA B 201 ? 0.3052 0.2279 0.2230 -0.0666 0.0079  -0.0716 179 ALA B N   
3186 C CA  . ALA B 201 ? 0.3132 0.2690 0.2193 -0.0853 0.0022  -0.0801 179 ALA B CA  
3187 C C   . ALA B 201 ? 0.3932 0.3385 0.2898 -0.0991 0.0083  -0.1108 179 ALA B C   
3188 O O   . ALA B 201 ? 0.4122 0.3183 0.3178 -0.0997 0.0156  -0.1249 179 ALA B O   
3189 C CB  . ALA B 201 ? 0.3175 0.2877 0.2319 -0.0980 -0.0050 -0.0696 179 ALA B CB  
3190 N N   . LYS B 202 ? 0.3669 0.3482 0.2458 -0.1109 0.0055  -0.1212 180 LYS B N   
3191 C CA  . LYS B 202 ? 0.4199 0.3975 0.2885 -0.1244 0.0123  -0.1531 180 LYS B CA  
3192 C C   . LYS B 202 ? 0.5226 0.4922 0.3982 -0.1429 0.0096  -0.1625 180 LYS B C   
3193 O O   . LYS B 202 ? 0.4687 0.4102 0.3507 -0.1447 0.0170  -0.1822 180 LYS B O   
3194 C CB  . LYS B 202 ? 0.4941 0.5199 0.3461 -0.1285 0.0097  -0.1527 180 LYS B CB  
3195 C CG  . LYS B 202 ? 0.6571 0.6889 0.5038 -0.1379 0.0166  -0.1776 180 LYS B CG  
3196 C CD  . LYS B 202 ? 0.6481 0.6336 0.5061 -0.1255 0.0297  -0.1986 180 LYS B CD  
3197 C CE  . LYS B 202 ? 0.7591 0.7618 0.6090 -0.1201 0.0386  -0.2134 180 LYS B CE  
3198 N NZ  . LYS B 202 ? 0.7127 0.7417 0.5509 -0.1393 0.0395  -0.2324 180 LYS B NZ  
3199 N N   . GLU B 203 ? 0.4269 0.4229 0.3031 -0.1567 -0.0013 -0.1478 181 GLU B N   
3200 C CA  . GLU B 203 ? 0.5066 0.5008 0.3898 -0.1761 -0.0041 -0.1554 181 GLU B CA  
3201 C C   . GLU B 203 ? 0.5723 0.5171 0.4746 -0.1744 -0.0001 -0.1524 181 GLU B C   
3202 O O   . GLU B 203 ? 0.4979 0.4304 0.4090 -0.1619 -0.0004 -0.1328 181 GLU B O   
3203 C CB  . GLU B 203 ? 0.4854 0.5338 0.3663 -0.1902 -0.0171 -0.1380 181 GLU B CB  
3204 C CG  . GLU B 203 ? 0.5901 0.6380 0.4858 -0.2057 -0.0222 -0.1310 181 GLU B CG  
3205 C CD  . GLU B 203 ? 0.6374 0.7466 0.5340 -0.2153 -0.0346 -0.1121 181 GLU B CD  
3206 O OE1 . GLU B 203 ? 0.7901 0.9307 0.6761 -0.2268 -0.0370 -0.1197 181 GLU B OE1 
3207 O OE2 . GLU B 203 ? 0.6446 0.7725 0.5543 -0.2100 -0.0413 -0.0886 181 GLU B OE2 
3208 N N   . LYS B 204 ? 0.6188 0.5354 0.5293 -0.1837 0.0039  -0.1684 182 LYS B N   
3209 C CA  . LYS B 204 ? 0.7549 0.6252 0.6859 -0.1825 0.0067  -0.1612 182 LYS B CA  
3210 C C   . LYS B 204 ? 0.6772 0.5682 0.6164 -0.1979 -0.0015 -0.1404 182 LYS B C   
3211 O O   . LYS B 204 ? 0.6498 0.5827 0.5838 -0.2156 -0.0092 -0.1404 182 LYS B O   
3212 C CB  . LYS B 204 ? 0.7424 0.5776 0.6811 -0.1891 0.0111  -0.1824 182 LYS B CB  
3213 C CG  . LYS B 204 ? 0.9217 0.7233 0.8622 -0.1687 0.0209  -0.1981 182 LYS B CG  
3214 C CD  . LYS B 204 ? 0.9932 0.8249 0.9139 -0.1698 0.0245  -0.2205 182 LYS B CD  
3215 C CE  . LYS B 204 ? 1.0627 0.8796 0.9842 -0.1447 0.0339  -0.2260 182 LYS B CE  
3216 N NZ  . LYS B 204 ? 0.9800 0.8434 0.8814 -0.1426 0.0349  -0.2305 182 LYS B NZ  
3217 N N   . GLY B 205 ? 0.6130 0.4795 0.5660 -0.1903 0.0005  -0.1202 183 GLY B N   
3218 C CA  . GLY B 205 ? 0.5686 0.4534 0.5328 -0.2046 -0.0051 -0.0992 183 GLY B CA  
3219 C C   . GLY B 205 ? 0.5814 0.5170 0.5446 -0.1925 -0.0113 -0.0749 183 GLY B C   
3220 O O   . GLY B 205 ? 0.5294 0.4944 0.5033 -0.2029 -0.0161 -0.0587 183 GLY B O   
3221 N N   . VAL B 206 ? 0.4764 0.4249 0.4298 -0.1699 -0.0111 -0.0715 184 VAL B N   
3222 C CA  . VAL B 206 ? 0.4557 0.4405 0.4134 -0.1529 -0.0152 -0.0471 184 VAL B CA  
3223 C C   . VAL B 206 ? 0.4746 0.4368 0.4444 -0.1391 -0.0099 -0.0287 184 VAL B C   
3224 O O   . VAL B 206 ? 0.4477 0.3694 0.4174 -0.1275 -0.0036 -0.0305 184 VAL B O   
3225 C CB  . VAL B 206 ? 0.4184 0.4169 0.3638 -0.1344 -0.0162 -0.0473 184 VAL B CB  
3226 C CG1 . VAL B 206 ? 0.4094 0.4361 0.3629 -0.1156 -0.0193 -0.0232 184 VAL B CG1 
3227 C CG2 . VAL B 206 ? 0.4610 0.4909 0.3921 -0.1501 -0.0221 -0.0622 184 VAL B CG2 
3228 N N   . LYS B 207 ? 0.4124 0.4053 0.3935 -0.1410 -0.0124 -0.0107 185 LYS B N   
3229 C CA  . LYS B 207 ? 0.5076 0.4875 0.4981 -0.1328 -0.0072 0.0065  185 LYS B CA  
3230 C C   . LYS B 207 ? 0.3201 0.2945 0.3058 -0.1052 -0.0040 0.0141  185 LYS B C   
3231 O O   . LYS B 207 ? 0.3217 0.3201 0.3040 -0.0924 -0.0068 0.0149  185 LYS B O   
3232 C CB  . LYS B 207 ? 0.4794 0.5017 0.4832 -0.1430 -0.0093 0.0212  185 LYS B CB  
3233 C CG  . LYS B 207 ? 0.5340 0.5514 0.5460 -0.1398 -0.0033 0.0390  185 LYS B CG  
3234 C CD  . LYS B 207 ? 0.4915 0.5631 0.5167 -0.1429 -0.0035 0.0523  185 LYS B CD  
3235 C CE  . LYS B 207 ? 0.6051 0.6796 0.6355 -0.1408 0.0037  0.0695  185 LYS B CE  
3236 N NZ  . LYS B 207 ? 0.5763 0.6958 0.6222 -0.1584 0.0044  0.0804  185 LYS B NZ  
3237 N N   . LEU B 208 ? 0.4042 0.3466 0.3906 -0.0970 0.0012  0.0206  186 LEU B N   
3238 C CA  . LEU B 208 ? 0.3442 0.2843 0.3260 -0.0740 0.0037  0.0277  186 LEU B CA  
3239 C C   . LEU B 208 ? 0.2744 0.2513 0.2611 -0.0671 0.0044  0.0404  186 LEU B C   
3240 O O   . LEU B 208 ? 0.3099 0.3064 0.3053 -0.0788 0.0055  0.0494  186 LEU B O   
3241 C CB  . LEU B 208 ? 0.3569 0.2613 0.3398 -0.0686 0.0077  0.0344  186 LEU B CB  
3242 C CG  . LEU B 208 ? 0.4716 0.3359 0.4544 -0.0698 0.0092  0.0211  186 LEU B CG  
3243 C CD1 . LEU B 208 ? 0.5057 0.3393 0.4955 -0.0625 0.0122  0.0337  186 LEU B CD1 
3244 C CD2 . LEU B 208 ? 0.4619 0.3288 0.4350 -0.0573 0.0089  0.0068  186 LEU B CD2 
3245 N N   . PRO B 209 ? 0.2666 0.2536 0.2495 -0.0487 0.0048  0.0405  187 PRO B N   
3246 C CA  . PRO B 209 ? 0.2847 0.3025 0.2738 -0.0395 0.0075  0.0484  187 PRO B CA  
3247 C C   . PRO B 209 ? 0.2788 0.2905 0.2648 -0.0364 0.0131  0.0572  187 PRO B C   
3248 O O   . PRO B 209 ? 0.2971 0.2800 0.2771 -0.0376 0.0135  0.0598  187 PRO B O   
3249 C CB  . PRO B 209 ? 0.2692 0.2889 0.2553 -0.0219 0.0059  0.0434  187 PRO B CB  
3250 C CG  . PRO B 209 ? 0.2736 0.2586 0.2480 -0.0193 0.0050  0.0368  187 PRO B CG  
3251 C CD  . PRO B 209 ? 0.2346 0.2024 0.2082 -0.0356 0.0039  0.0327  187 PRO B CD  
3252 N N   . GLY B 210 ? 0.2776 0.3206 0.2687 -0.0320 0.0177  0.0621  188 GLY B N   
3253 C CA  . GLY B 210 ? 0.2520 0.2977 0.2362 -0.0278 0.0231  0.0687  188 GLY B CA  
3254 C C   . GLY B 210 ? 0.2626 0.2935 0.2370 -0.0113 0.0231  0.0610  188 GLY B C   
3255 O O   . GLY B 210 ? 0.2283 0.2489 0.2030 -0.0026 0.0198  0.0520  188 GLY B O   
3256 N N   . ALA B 211 ? 0.2589 0.2917 0.2239 -0.0090 0.0263  0.0658  189 ALA B N   
3257 C CA  . ALA B 211 ? 0.2889 0.3107 0.2444 0.0035  0.0257  0.0580  189 ALA B CA  
3258 C C   . ALA B 211 ? 0.2284 0.2676 0.1877 0.0152  0.0298  0.0450  189 ALA B C   
3259 O O   . ALA B 211 ? 0.2442 0.3120 0.2115 0.0155  0.0356  0.0438  189 ALA B O   
3260 C CB  . ALA B 211 ? 0.2558 0.2819 0.1998 0.0009  0.0269  0.0674  189 ALA B CB  
3261 N N   . HIS B 212 ? 0.2545 0.2234 0.2189 -0.0407 0.0197  0.0653  190 HIS B N   
3262 C CA  . HIS B 212 ? 0.2606 0.2372 0.2088 -0.0396 0.0242  0.0490  190 HIS B CA  
3263 C C   . HIS B 212 ? 0.2558 0.2322 0.1856 -0.0360 0.0121  0.0437  190 HIS B C   
3264 O O   . HIS B 212 ? 0.2617 0.2372 0.1901 -0.0350 0.0004  0.0556  190 HIS B O   
3265 C CB  . HIS B 212 ? 0.2216 0.2047 0.1986 -0.0358 0.0279  0.0355  190 HIS B CB  
3266 C CG  . HIS B 212 ? 0.2510 0.2327 0.2481 -0.0323 0.0153  0.0286  190 HIS B CG  
3267 N ND1 . HIS B 212 ? 0.2374 0.2119 0.2552 -0.0371 0.0135  0.0310  190 HIS B ND1 
3268 C CD2 . HIS B 212 ? 0.2435 0.2279 0.2403 -0.0264 0.0064  0.0183  190 HIS B CD2 
3269 C CE1 . HIS B 212 ? 0.2454 0.2186 0.2717 -0.0357 0.0052  0.0195  190 HIS B CE1 
3270 N NE2 . HIS B 212 ? 0.1890 0.1699 0.2022 -0.0288 -0.0003 0.0134  190 HIS B NE2 
3271 N N   . PHE B 213 ? 0.2651 0.2430 0.1859 -0.0340 0.0168  0.0278  191 PHE B N   
3272 C CA  . PHE B 213 ? 0.2544 0.2313 0.1595 -0.0327 0.0082  0.0202  191 PHE B CA  
3273 C C   . PHE B 213 ? 0.2680 0.2441 0.1927 -0.0236 0.0089  0.0071  191 PHE B C   
3274 O O   . PHE B 213 ? 0.2553 0.2353 0.1992 -0.0199 0.0185  0.0040  191 PHE B O   
3275 C CB  . PHE B 213 ? 0.2870 0.2637 0.1539 -0.0441 0.0170  0.0140  191 PHE B CB  
3276 C CG  . PHE B 213 ? 0.3067 0.2910 0.1470 -0.0565 0.0143  0.0301  191 PHE B CG  
3277 C CD1 . PHE B 213 ? 0.3376 0.3332 0.1660 -0.0614 -0.0045 0.0449  191 PHE B CD1 
3278 C CD2 . PHE B 213 ? 0.3587 0.3427 0.1898 -0.0632 0.0302  0.0346  191 PHE B CD2 
3279 C CE1 . PHE B 213 ? 0.3942 0.4030 0.2000 -0.0730 -0.0094 0.0666  191 PHE B CE1 
3280 C CE2 . PHE B 213 ? 0.4156 0.4091 0.2198 -0.0756 0.0275  0.0535  191 PHE B CE2 
3281 C CZ  . PHE B 213 ? 0.4380 0.4450 0.2288 -0.0807 0.0065  0.0711  191 PHE B CZ  
3282 N N   . VAL B 214 ? 0.2365 0.2112 0.1591 -0.0203 -0.0015 0.0027  192 VAL B N   
3283 C CA  . VAL B 214 ? 0.2340 0.2086 0.1695 -0.0129 -0.0004 -0.0067 192 VAL B CA  
3284 C C   . VAL B 214 ? 0.3187 0.2871 0.2346 -0.0160 0.0003  -0.0148 192 VAL B C   
3285 O O   . VAL B 214 ? 0.2622 0.2329 0.1686 -0.0196 -0.0116 -0.0123 192 VAL B O   
3286 C CB  . VAL B 214 ? 0.2222 0.2013 0.1777 -0.0077 -0.0119 -0.0058 192 VAL B CB  
3287 C CG1 . VAL B 214 ? 0.2055 0.1892 0.1706 -0.0015 -0.0115 -0.0109 192 VAL B CG1 
3288 C CG2 . VAL B 214 ? 0.2329 0.2170 0.2062 -0.0100 -0.0115 -0.0017 192 VAL B CG2 
3289 N N   . ASP B 215 ? 0.2683 0.2289 0.1822 -0.0155 0.0163  -0.0240 193 ASP B N   
3290 C CA  . ASP B 215 ? 0.2530 0.2033 0.1520 -0.0205 0.0210  -0.0353 193 ASP B CA  
3291 C C   . ASP B 215 ? 0.2725 0.2241 0.1920 -0.0105 0.0138  -0.0336 193 ASP B C   
3292 O O   . ASP B 215 ? 0.2699 0.2271 0.2141 0.0002  0.0160  -0.0273 193 ASP B O   
3293 C CB  . ASP B 215 ? 0.2726 0.2074 0.1666 -0.0237 0.0475  -0.0474 193 ASP B CB  
3294 C CG  . ASP B 215 ? 0.4368 0.3689 0.2995 -0.0389 0.0581  -0.0534 193 ASP B CG  
3295 O OD1 . ASP B 215 ? 0.3385 0.2826 0.1794 -0.0485 0.0416  -0.0457 193 ASP B OD1 
3296 O OD2 . ASP B 215 ? 0.3658 0.2843 0.2270 -0.0412 0.0850  -0.0642 193 ASP B OD2 
3297 N N   . HIS B 216 ? 0.2543 0.2049 0.1639 -0.0154 0.0047  -0.0373 194 HIS B N   
3298 C CA  . HIS B 216 ? 0.2177 0.1692 0.1429 -0.0078 -0.0001 -0.0357 194 HIS B CA  
3299 C C   . HIS B 216 ? 0.2962 0.2345 0.2138 -0.0143 0.0091  -0.0460 194 HIS B C   
3300 O O   . HIS B 216 ? 0.2945 0.2298 0.1899 -0.0292 0.0093  -0.0552 194 HIS B O   
3301 C CB  . HIS B 216 ? 0.1991 0.1618 0.1276 -0.0072 -0.0174 -0.0302 194 HIS B CB  
3302 C CG  . HIS B 216 ? 0.2026 0.1733 0.1410 -0.0030 -0.0245 -0.0228 194 HIS B CG  
3303 N ND1 . HIS B 216 ? 0.2151 0.1909 0.1678 0.0030  -0.0264 -0.0212 194 HIS B ND1 
3304 C CD2 . HIS B 216 ? 0.2767 0.2507 0.2126 -0.0062 -0.0296 -0.0166 194 HIS B CD2 
3305 C CE1 . HIS B 216 ? 0.2161 0.1944 0.1747 0.0019  -0.0301 -0.0185 194 HIS B CE1 
3306 N NE2 . HIS B 216 ? 0.2487 0.2245 0.2002 -0.0018 -0.0315 -0.0139 194 HIS B NE2 
3307 N N   . CYS B 217 ? 0.2643 0.1970 0.1999 -0.0055 0.0157  -0.0430 195 CYS B N   
3308 C CA  . CYS B 217 ? 0.2625 0.1840 0.1963 -0.0114 0.0209  -0.0501 195 CYS B CA  
3309 C C   . CYS B 217 ? 0.2554 0.1861 0.2061 -0.0013 0.0131  -0.0388 195 CYS B C   
3310 O O   . CYS B 217 ? 0.2330 0.1741 0.1973 0.0097  0.0104  -0.0267 195 CYS B O   
3311 C CB  . CYS B 217 ? 0.3281 0.2241 0.2654 -0.0141 0.0471  -0.0600 195 CYS B CB  
3312 S SG  . CYS B 217 ? 0.3577 0.2481 0.3335 0.0070  0.0642  -0.0431 195 CYS B SG  
3313 N N   . ILE B 218 ? 0.2587 0.1896 0.2066 -0.0078 0.0086  -0.0425 196 ILE B N   
3314 C CA  . ILE B 218 ? 0.2679 0.2075 0.2268 -0.0013 0.0034  -0.0335 196 ILE B CA  
3315 C C   . ILE B 218 ? 0.2640 0.1912 0.2268 -0.0080 0.0129  -0.0379 196 ILE B C   
3316 O O   . ILE B 218 ? 0.2797 0.2015 0.2334 -0.0223 0.0139  -0.0504 196 ILE B O   
3317 C CB  . ILE B 218 ? 0.2154 0.1726 0.1723 -0.0016 -0.0121 -0.0323 196 ILE B CB  
3318 C CG1 . ILE B 218 ? 0.2377 0.2031 0.2016 0.0036  -0.0130 -0.0259 196 ILE B CG1 
3319 C CG2 . ILE B 218 ? 0.2276 0.1904 0.1802 -0.0128 -0.0194 -0.0383 196 ILE B CG2 
3320 C CD1 . ILE B 218 ? 0.2409 0.2180 0.2063 0.0042  -0.0211 -0.0276 196 ILE B CD1 
3321 N N   . GLU B 219 ? 0.2369 0.1621 0.2127 -0.0002 0.0194  -0.0265 197 GLU B N   
3322 C CA  . GLU B 219 ? 0.2341 0.1418 0.2186 -0.0055 0.0338  -0.0281 197 GLU B CA  
3323 C C   . GLU B 219 ? 0.2570 0.1754 0.2492 0.0000  0.0317  -0.0138 197 GLU B C   
3324 O O   . GLU B 219 ? 0.2500 0.1808 0.2452 0.0107  0.0286  0.0026  197 GLU B O   
3325 C CB  . GLU B 219 ? 0.2818 0.1650 0.2803 0.0000  0.0555  -0.0249 197 GLU B CB  
3326 C CG  . GLU B 219 ? 0.3843 0.2419 0.3977 -0.0049 0.0761  -0.0256 197 GLU B CG  
3327 C CD  . GLU B 219 ? 0.4501 0.2858 0.4517 -0.0263 0.0876  -0.0526 197 GLU B CD  
3328 O OE1 . GLU B 219 ? 0.5285 0.3763 0.5082 -0.0370 0.0761  -0.0669 197 GLU B OE1 
3329 O OE2 . GLU B 219 ? 0.3647 0.1874 0.3787 -0.0321 0.1033  -0.0539 197 GLU B OE2 
3330 N N   . ILE B 220 ? 0.2306 0.1476 0.2249 -0.0096 0.0336  -0.0193 198 ILE B N   
3331 C CA  . ILE B 220 ? 0.2131 0.1339 0.2153 -0.0061 0.0391  -0.0052 198 ILE B CA  
3332 C C   . ILE B 220 ? 0.2683 0.1653 0.2869 -0.0025 0.0587  0.0060  198 ILE B C   
3333 O O   . ILE B 220 ? 0.2845 0.1572 0.3104 -0.0127 0.0727  -0.0065 198 ILE B O   
3334 C CB  . ILE B 220 ? 0.2506 0.1803 0.2556 -0.0170 0.0366  -0.0132 198 ILE B CB  
3335 C CG1 . ILE B 220 ? 0.2586 0.2116 0.2570 -0.0154 0.0214  -0.0182 198 ILE B CG1 
3336 C CG2 . ILE B 220 ? 0.2787 0.2069 0.2920 -0.0159 0.0482  0.0010  198 ILE B CG2 
3337 C CD1 . ILE B 220 ? 0.2295 0.1974 0.2405 -0.0227 0.0206  -0.0220 198 ILE B CD1 
3338 N N   . LEU B 221 ? 0.2934 0.1980 0.3192 0.0107  0.0607  0.0306  199 LEU B N   
3339 C CA  . LEU B 221 ? 0.2581 0.1423 0.3089 0.0187  0.0806  0.0498  199 LEU B CA  
3340 C C   . LEU B 221 ? 0.3199 0.1952 0.3797 0.0137  0.0924  0.0599  199 LEU B C   
3341 O O   . LEU B 221 ? 0.3016 0.1466 0.3850 0.0135  0.1150  0.0646  199 LEU B O   
3342 C CB  . LEU B 221 ? 0.2492 0.1553 0.3087 0.0344  0.0745  0.0798  199 LEU B CB  
3343 C CG  . LEU B 221 ? 0.2906 0.2123 0.3434 0.0390  0.0614  0.0738  199 LEU B CG  
3344 C CD1 . LEU B 221 ? 0.2905 0.2403 0.3582 0.0518  0.0549  0.1080  199 LEU B CD1 
3345 C CD2 . LEU B 221 ? 0.3140 0.2064 0.3771 0.0380  0.0764  0.0544  199 LEU B CD2 
3346 N N   . SER B 222 ? 0.2651 0.1644 0.3086 0.0094  0.0809  0.0630  200 SER B N   
3347 C CA  . SER B 222 ? 0.3121 0.2095 0.3616 0.0051  0.0916  0.0766  200 SER B CA  
3348 C C   . SER B 222 ? 0.3014 0.2223 0.3308 -0.0037 0.0806  0.0644  200 SER B C   
3349 O O   . SER B 222 ? 0.2860 0.2272 0.2974 -0.0025 0.0651  0.0547  200 SER B O   
3350 C CB  . SER B 222 ? 0.3392 0.2473 0.3965 0.0172  0.0959  0.1157  200 SER B CB  
3351 O OG  . SER B 222 ? 0.4016 0.2959 0.4733 0.0137  0.1135  0.1316  200 SER B OG  
3352 N N   . HIS B 223 ? 0.3094 0.2261 0.3465 -0.0125 0.0919  0.0656  201 HIS B N   
3353 C CA  . HIS B 223 ? 0.2877 0.2260 0.3137 -0.0197 0.0878  0.0564  201 HIS B CA  
3354 C C   . HIS B 223 ? 0.3507 0.2839 0.3881 -0.0265 0.1052  0.0695  201 HIS B C   
3355 O O   . HIS B 223 ? 0.3919 0.3000 0.4500 -0.0292 0.1193  0.0764  201 HIS B O   
3356 C CB  . HIS B 223 ? 0.2646 0.2065 0.2974 -0.0281 0.0791  0.0287  201 HIS B CB  
3357 C CG  . HIS B 223 ? 0.3591 0.2822 0.4130 -0.0410 0.0877  0.0178  201 HIS B CG  
3358 N ND1 . HIS B 223 ? 0.3726 0.2999 0.4434 -0.0534 0.0967  0.0151  201 HIS B ND1 
3359 C CD2 . HIS B 223 ? 0.3404 0.2402 0.4002 -0.0465 0.0910  0.0073  201 HIS B CD2 
3360 C CE1 . HIS B 223 ? 0.4030 0.3118 0.4885 -0.0680 0.1028  0.0027  201 HIS B CE1 
3361 N NE2 . HIS B 223 ? 0.4246 0.3148 0.5013 -0.0647 0.1007  -0.0037 201 HIS B NE2 
3362 N N   . ASP B 224 ? 0.3323 0.2865 0.3571 -0.0302 0.1077  0.0717  202 ASP B N   
3363 C CA  . ASP B 224 ? 0.3119 0.2637 0.3489 -0.0388 0.1256  0.0812  202 ASP B CA  
3364 C C   . ASP B 224 ? 0.3278 0.2825 0.3884 -0.0503 0.1270  0.0571  202 ASP B C   
3365 O O   . ASP B 224 ? 0.3398 0.2989 0.4057 -0.0510 0.1132  0.0373  202 ASP B O   
3366 C CB  . ASP B 224 ? 0.3303 0.3043 0.3400 -0.0391 0.1311  0.0975  202 ASP B CB  
3367 C CG  . ASP B 224 ? 0.4270 0.4230 0.4201 -0.0420 0.1270  0.0757  202 ASP B CG  
3368 O OD1 . ASP B 224 ? 0.3484 0.3449 0.3554 -0.0408 0.1177  0.0528  202 ASP B OD1 
3369 O OD2 . ASP B 224 ? 0.4471 0.4597 0.4130 -0.0463 0.1352  0.0826  202 ASP B OD2 
3370 N N   . LYS B 225 ? 0.3582 0.3156 0.4346 -0.0600 0.1430  0.0618  203 LYS B N   
3371 C CA  . LYS B 225 ? 0.3307 0.2919 0.4393 -0.0739 0.1450  0.0445  203 LYS B CA  
3372 C C   . LYS B 225 ? 0.3492 0.3381 0.4640 -0.0725 0.1314  0.0268  203 LYS B C   
3373 O O   . LYS B 225 ? 0.3644 0.3597 0.4976 -0.0795 0.1186  0.0123  203 LYS B O   
3374 C CB  . LYS B 225 ? 0.4075 0.3704 0.5345 -0.0846 0.1665  0.0554  203 LYS B CB  
3375 C CG  . LYS B 225 ? 0.7785 0.7286 0.8873 -0.0784 0.1786  0.0823  203 LYS B CG  
3376 C CD  . LYS B 225 ? 0.5724 0.4979 0.6702 -0.0676 0.1749  0.0985  203 LYS B CD  
3377 C CE  . LYS B 225 ? 0.8314 0.7625 0.9085 -0.0599 0.1799  0.1290  203 LYS B CE  
3378 N NZ  . LYS B 225 ? 0.6596 0.6202 0.7009 -0.0577 0.1756  0.1340  203 LYS B NZ  
3379 N N   . ASP B 226 ? 0.3633 0.3692 0.4635 -0.0646 0.1357  0.0286  204 ASP B N   
3380 C CA  . ASP B 226 ? 0.4029 0.4313 0.5167 -0.0607 0.1294  0.0144  204 ASP B CA  
3381 C C   . ASP B 226 ? 0.3004 0.3269 0.3904 -0.0493 0.1138  0.0073  204 ASP B C   
3382 O O   . ASP B 226 ? 0.2968 0.3373 0.3962 -0.0438 0.1125  -0.0022 204 ASP B O   
3383 C CB  . ASP B 226 ? 0.3795 0.4237 0.4975 -0.0609 0.1507  0.0155  204 ASP B CB  
3384 C CG  . ASP B 226 ? 0.4979 0.5497 0.6488 -0.0727 0.1668  0.0216  204 ASP B CG  
3385 O OD1 . ASP B 226 ? 0.4644 0.5244 0.6518 -0.0812 0.1578  0.0174  204 ASP B OD1 
3386 O OD2 . ASP B 226 ? 0.4870 0.5392 0.6261 -0.0759 0.1884  0.0306  204 ASP B OD2 
3387 N N   . TYR B 227 ? 0.3034 0.3126 0.3678 -0.0453 0.1044  0.0129  205 TYR B N   
3388 C CA  . TYR B 227 ? 0.2496 0.2581 0.2918 -0.0360 0.0904  0.0074  205 TYR B CA  
3389 C C   . TYR B 227 ? 0.3076 0.3264 0.3257 -0.0332 0.0985  0.0047  205 TYR B C   
3390 O O   . TYR B 227 ? 0.2994 0.3218 0.3109 -0.0284 0.0920  -0.0068 205 TYR B O   
3391 C CB  . TYR B 227 ? 0.2745 0.2895 0.3367 -0.0346 0.0752  -0.0056 205 TYR B CB  
3392 C CG  . TYR B 227 ? 0.2872 0.2915 0.3587 -0.0416 0.0652  -0.0076 205 TYR B CG  
3393 C CD1 . TYR B 227 ? 0.3057 0.3111 0.4007 -0.0550 0.0707  -0.0084 205 TYR B CD1 
3394 C CD2 . TYR B 227 ? 0.3462 0.3392 0.4021 -0.0377 0.0527  -0.0110 205 TYR B CD2 
3395 C CE1 . TYR B 227 ? 0.3829 0.3763 0.4814 -0.0667 0.0646  -0.0156 205 TYR B CE1 
3396 C CE2 . TYR B 227 ? 0.3148 0.2955 0.3747 -0.0471 0.0483  -0.0171 205 TYR B CE2 
3397 C CZ  . TYR B 227 ? 0.3852 0.3652 0.4643 -0.0627 0.0545  -0.0209 205 TYR B CZ  
3398 O OH  . TYR B 227 ? 0.4086 0.3740 0.4866 -0.0771 0.0531  -0.0319 205 TYR B OH  
3399 N N   . ASN B 228 ? 0.2708 0.2937 0.2743 -0.0385 0.1150  0.0141  206 ASN B N   
3400 C CA  . ASN B 228 ? 0.2931 0.3248 0.2604 -0.0411 0.1226  0.0103  206 ASN B CA  
3401 C C   . ASN B 228 ? 0.2930 0.3248 0.2258 -0.0396 0.1072  0.0215  206 ASN B C   
3402 O O   . ASN B 228 ? 0.3245 0.3655 0.2262 -0.0440 0.1060  0.0133  206 ASN B O   
3403 C CB  . ASN B 228 ? 0.3649 0.4045 0.3198 -0.0504 0.1455  0.0179  206 ASN B CB  
3404 C CG  . ASN B 228 ? 0.4327 0.4778 0.4246 -0.0519 0.1645  0.0051  206 ASN B CG  
3405 O OD1 . ASN B 228 ? 0.3638 0.4119 0.3759 -0.0470 0.1667  -0.0126 206 ASN B OD1 
3406 N ND2 . ASN B 228 ? 0.3914 0.4391 0.3971 -0.0582 0.1797  0.0169  206 ASN B ND2 
3407 N N   . LYS B 229 ? 0.2855 0.3083 0.2265 -0.0348 0.0976  0.0400  207 LYS B N   
3408 C CA  . LYS B 229 ? 0.3071 0.3332 0.2294 -0.0304 0.0829  0.0551  207 LYS B CA  
3409 C C   . LYS B 229 ? 0.2822 0.2908 0.2307 -0.0214 0.0721  0.0526  207 LYS B C   
3410 O O   . LYS B 229 ? 0.3020 0.2943 0.2767 -0.0214 0.0785  0.0531  207 LYS B O   
3411 C CB  . LYS B 229 ? 0.3176 0.3517 0.2263 -0.0324 0.0877  0.0880  207 LYS B CB  
3412 C CG  . LYS B 229 ? 0.3877 0.4436 0.2587 -0.0453 0.0977  0.0919  207 LYS B CG  
3413 C CD  . LYS B 229 ? 0.4757 0.5419 0.3370 -0.0475 0.1022  0.1310  207 LYS B CD  
3414 C CE  . LYS B 229 ? 0.7415 0.8212 0.5651 -0.0610 0.1115  0.1283  207 LYS B CE  
3415 N NZ  . LYS B 229 ? 0.8053 0.9052 0.5938 -0.0659 0.0930  0.1305  207 LYS B NZ  
3416 N N   . VAL B 230 ? 0.2575 0.2696 0.1974 -0.0166 0.0576  0.0474  208 VAL B N   
3417 C CA  . VAL B 230 ? 0.2401 0.2369 0.1991 -0.0097 0.0490  0.0419  208 VAL B CA  
3418 C C   . VAL B 230 ? 0.2946 0.2998 0.2437 -0.0035 0.0379  0.0555  208 VAL B C   
3419 O O   . VAL B 230 ? 0.2900 0.3155 0.2158 -0.0074 0.0301  0.0556  208 VAL B O   
3420 C CB  . VAL B 230 ? 0.2191 0.2140 0.1864 -0.0107 0.0430  0.0169  208 VAL B CB  
3421 C CG1 . VAL B 230 ? 0.2350 0.2173 0.2129 -0.0064 0.0341  0.0122  208 VAL B CG1 
3422 C CG2 . VAL B 230 ? 0.2316 0.2259 0.2189 -0.0165 0.0523  0.0077  208 VAL B CG2 
3423 N N   . LYS B 231 ? 0.2410 0.2314 0.2099 0.0043  0.0391  0.0666  209 LYS B N   
3424 C CA  . LYS B 231 ? 0.2425 0.2408 0.2140 0.0122  0.0297  0.0780  209 LYS B CA  
3425 C C   . LYS B 231 ? 0.2793 0.2618 0.2598 0.0144  0.0263  0.0568  209 LYS B C   
3426 O O   . LYS B 231 ? 0.2485 0.2076 0.2431 0.0129  0.0355  0.0461  209 LYS B O   
3427 C CB  . LYS B 231 ? 0.2889 0.2831 0.2825 0.0217  0.0382  0.1103  209 LYS B CB  
3428 C CG  . LYS B 231 ? 0.4328 0.4377 0.4404 0.0319  0.0307  0.1248  209 LYS B CG  
3429 C CD  . LYS B 231 ? 0.4832 0.5267 0.4861 0.0336  0.0195  0.1595  209 LYS B CD  
3430 C CE  . LYS B 231 ? 0.5755 0.6205 0.5921 0.0361  0.0294  0.1856  209 LYS B CE  
3431 N NZ  . LYS B 231 ? 0.5425 0.6315 0.5461 0.0297  0.0134  0.2031  209 LYS B NZ  
3432 N N   . LEU B 232 ? 0.2429 0.2395 0.2129 0.0149  0.0136  0.0502  210 LEU B N   
3433 C CA  . LEU B 232 ? 0.2091 0.1956 0.1816 0.0150  0.0090  0.0308  210 LEU B CA  
3434 C C   . LEU B 232 ? 0.1991 0.1922 0.1795 0.0221  0.0044  0.0406  210 LEU B C   
3435 O O   . LEU B 232 ? 0.2379 0.2543 0.2162 0.0237  -0.0025 0.0584  210 LEU B O   
3436 C CB  . LEU B 232 ? 0.2207 0.2163 0.1783 0.0085  0.0012  0.0126  210 LEU B CB  
3437 C CG  . LEU B 232 ? 0.2485 0.2357 0.2100 0.0080  -0.0038 -0.0035 210 LEU B CG  
3438 C CD1 . LEU B 232 ? 0.2485 0.2220 0.2201 0.0045  0.0010  -0.0108 210 LEU B CD1 
3439 C CD2 . LEU B 232 ? 0.2416 0.2372 0.1959 0.0044  -0.0081 -0.0152 210 LEU B CD2 
3440 N N   . TYR B 233 ? 0.1970 0.1732 0.1862 0.0242  0.0084  0.0299  211 TYR B N   
3441 C CA  . TYR B 233 ? 0.2047 0.1854 0.2059 0.0312  0.0081  0.0374  211 TYR B CA  
3442 C C   . TYR B 233 ? 0.2402 0.2132 0.2329 0.0270  0.0045  0.0175  211 TYR B C   
3443 O O   . TYR B 233 ? 0.2591 0.2161 0.2440 0.0204  0.0076  0.0015  211 TYR B O   
3444 C CB  . TYR B 233 ? 0.2479 0.2101 0.2757 0.0402  0.0266  0.0501  211 TYR B CB  
3445 C CG  . TYR B 233 ? 0.1939 0.1576 0.2421 0.0489  0.0326  0.0568  211 TYR B CG  
3446 C CD1 . TYR B 233 ? 0.2356 0.2308 0.3011 0.0568  0.0239  0.0820  211 TYR B CD1 
3447 C CD2 . TYR B 233 ? 0.2303 0.1671 0.2807 0.0469  0.0479  0.0383  211 TYR B CD2 
3448 C CE1 . TYR B 233 ? 0.2553 0.2547 0.3475 0.0657  0.0314  0.0901  211 TYR B CE1 
3449 C CE2 . TYR B 233 ? 0.2223 0.1588 0.2931 0.0548  0.0583  0.0431  211 TYR B CE2 
3450 C CZ  . TYR B 233 ? 0.2757 0.2437 0.3711 0.0657  0.0504  0.0699  211 TYR B CZ  
3451 O OH  . TYR B 233 ? 0.2687 0.2396 0.3921 0.0744  0.0625  0.0768  211 TYR B OH  
3452 N N   . GLU B 234 ? 0.1743 0.1615 0.1700 0.0293  -0.0021 0.0211  212 GLU B N   
3453 C CA  . GLU B 234 ? 0.2015 0.1807 0.1907 0.0258  -0.0029 0.0065  212 GLU B CA  
3454 C C   . GLU B 234 ? 0.2469 0.2323 0.2540 0.0325  0.0027  0.0160  212 GLU B C   
3455 O O   . GLU B 234 ? 0.2085 0.2165 0.2313 0.0376  -0.0020 0.0342  212 GLU B O   
3456 C CB  . GLU B 234 ? 0.2113 0.2008 0.1856 0.0189  -0.0164 -0.0030 212 GLU B CB  
3457 C CG  . GLU B 234 ? 0.2935 0.2748 0.2607 0.0147  -0.0185 -0.0143 212 GLU B CG  
3458 C CD  . GLU B 234 ? 0.3446 0.3371 0.3117 0.0121  -0.0262 -0.0152 212 GLU B CD  
3459 O OE1 . GLU B 234 ? 0.3174 0.3213 0.2824 0.0091  -0.0314 -0.0153 212 GLU B OE1 
3460 O OE2 . GLU B 234 ? 0.3389 0.3274 0.3052 0.0104  -0.0259 -0.0177 212 GLU B OE2 
3461 N N   . HIS B 235 ? 0.2303 0.1985 0.2355 0.0309  0.0134  0.0049  213 HIS B N   
3462 C CA  . HIS B 235 ? 0.2265 0.1988 0.2494 0.0363  0.0226  0.0106  213 HIS B CA  
3463 C C   . HIS B 235 ? 0.1961 0.1657 0.1999 0.0277  0.0184  -0.0031 213 HIS B C   
3464 O O   . HIS B 235 ? 0.2434 0.1967 0.2252 0.0190  0.0210  -0.0175 213 HIS B O   
3465 C CB  . HIS B 235 ? 0.2720 0.2211 0.3134 0.0426  0.0488  0.0108  213 HIS B CB  
3466 C CG  . HIS B 235 ? 0.2635 0.2167 0.3309 0.0504  0.0637  0.0180  213 HIS B CG  
3467 N ND1 . HIS B 235 ? 0.2833 0.2089 0.3616 0.0523  0.0937  0.0088  213 HIS B ND1 
3468 C CD2 . HIS B 235 ? 0.2242 0.2062 0.3106 0.0550  0.0551  0.0321  213 HIS B CD2 
3469 C CE1 . HIS B 235 ? 0.2900 0.2276 0.3965 0.0607  0.1043  0.0189  213 HIS B CE1 
3470 N NE2 . HIS B 235 ? 0.2689 0.2430 0.3819 0.0622  0.0795  0.0344  213 HIS B NE2 
3471 N N   . ALA B 236 ? 0.2069 0.1956 0.2193 0.0281  0.0109  0.0034  214 ALA B N   
3472 C CA  . ALA B 236 ? 0.1694 0.1559 0.1668 0.0203  0.0075  -0.0053 214 ALA B CA  
3473 C C   . ALA B 236 ? 0.1689 0.1660 0.1861 0.0231  0.0161  0.0015  214 ALA B C   
3474 O O   . ALA B 236 ? 0.2039 0.2240 0.2473 0.0282  0.0122  0.0154  214 ALA B O   
3475 C CB  . ALA B 236 ? 0.1970 0.1932 0.1851 0.0144  -0.0104 -0.0073 214 ALA B CB  
3476 N N   . VAL B 237 ? 0.2033 0.1880 0.2078 0.0178  0.0271  -0.0064 215 VAL B N   
3477 C CA  . VAL B 237 ? 0.1921 0.1848 0.2150 0.0195  0.0399  -0.0014 215 VAL B CA  
3478 C C   . VAL B 237 ? 0.2215 0.2105 0.2222 0.0088  0.0367  -0.0065 215 VAL B C   
3479 O O   . VAL B 237 ? 0.2664 0.2396 0.2359 0.0008  0.0388  -0.0154 215 VAL B O   
3480 C CB  . VAL B 237 ? 0.2166 0.1929 0.2498 0.0247  0.0686  -0.0054 215 VAL B CB  
3481 C CG1 . VAL B 237 ? 0.2121 0.1978 0.2677 0.0267  0.0855  -0.0003 215 VAL B CG1 
3482 C CG2 . VAL B 237 ? 0.2441 0.2203 0.3060 0.0374  0.0752  0.0041  215 VAL B CG2 
3483 N N   . ALA B 238 ? 0.2100 0.2158 0.2277 0.0069  0.0316  0.0012  216 ALA B N   
3484 C CA  . ALA B 238 ? 0.2497 0.2513 0.2525 -0.0024 0.0314  0.0007  216 ALA B CA  
3485 C C   . ALA B 238 ? 0.2767 0.2739 0.2785 -0.0042 0.0544  -0.0001 216 ALA B C   
3486 O O   . ALA B 238 ? 0.2686 0.2729 0.2978 0.0032  0.0702  0.0026  216 ALA B O   
3487 C CB  . ALA B 238 ? 0.1966 0.2142 0.2188 -0.0068 0.0192  0.0068  216 ALA B CB  
3488 N N   . HIS B 239 ? 0.2393 0.2263 0.2113 -0.0144 0.0578  -0.0017 217 HIS B N   
3489 C CA  . HIS B 239 ? 0.2601 0.2430 0.2236 -0.0199 0.0815  -0.0037 217 HIS B CA  
3490 C C   . HIS B 239 ? 0.2532 0.2358 0.1936 -0.0314 0.0764  0.0046  217 HIS B C   
3491 O O   . HIS B 239 ? 0.2895 0.2703 0.2161 -0.0344 0.0571  0.0106  217 HIS B O   
3492 C CB  . HIS B 239 ? 0.3104 0.2752 0.2475 -0.0236 0.1013  -0.0191 217 HIS B CB  
3493 C CG  . HIS B 239 ? 0.3551 0.3105 0.2490 -0.0346 0.0880  -0.0258 217 HIS B CG  
3494 N ND1 . HIS B 239 ? 0.4273 0.3804 0.2773 -0.0518 0.0903  -0.0272 217 HIS B ND1 
3495 C CD2 . HIS B 239 ? 0.3414 0.2938 0.2309 -0.0323 0.0717  -0.0293 217 HIS B CD2 
3496 C CE1 . HIS B 239 ? 0.3823 0.3349 0.2055 -0.0599 0.0740  -0.0302 217 HIS B CE1 
3497 N NE2 . HIS B 239 ? 0.4069 0.3576 0.2550 -0.0477 0.0636  -0.0325 217 HIS B NE2 
3498 N N   . SER B 240 ? 0.2948 0.2800 0.2361 -0.0369 0.0957  0.0079  218 SER B N   
3499 C CA  . SER B 240 ? 0.4254 0.4124 0.3538 -0.0467 0.0921  0.0214  218 SER B CA  
3500 C C   . SER B 240 ? 0.4996 0.4799 0.3760 -0.0611 0.0992  0.0222  218 SER B C   
3501 O O   . SER B 240 ? 0.5572 0.5402 0.4179 -0.0684 0.0880  0.0392  218 SER B O   
3502 C CB  . SER B 240 ? 0.3961 0.3941 0.3578 -0.0470 0.1078  0.0280  218 SER B CB  
3503 O OG  . SER B 240 ? 0.5070 0.5034 0.4646 -0.0482 0.1372  0.0194  218 SER B OG  
3504 N N   . GLY B 241 ? 0.4737 0.4461 0.3235 -0.0671 0.1190  0.0054  219 GLY B N   
3505 C CA  . GLY B 241 ? 0.7294 0.6993 0.5220 -0.0871 0.1273  0.0030  219 GLY B CA  
3506 C C   . GLY B 241 ? 0.6600 0.6323 0.4239 -0.0931 0.1022  0.0017  219 GLY B C   
3507 O O   . GLY B 241 ? 0.6089 0.5774 0.3881 -0.0842 0.0902  -0.0041 219 GLY B O   
# 
