data_9FD7
# 
_entry.id   9FD7 
# 
_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   9FD7         pdb_00009fd7 10.2210/pdb9fd7/pdb 
WWPDB D_1292138702 ?            ?                   
# 
loop_
_pdbx_audit_revision_history.ordinal 
_pdbx_audit_revision_history.data_content_type 
_pdbx_audit_revision_history.major_revision 
_pdbx_audit_revision_history.minor_revision 
_pdbx_audit_revision_history.revision_date 
_pdbx_audit_revision_history.part_number 
1 'Structure model' 1 0 2025-03-12 ? 
2 'Structure model' 1 1 2025-05-21 ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_audit_revision_group.ordinal             1 
_pdbx_audit_revision_group.revision_ordinal    2 
_pdbx_audit_revision_group.data_content_type   'Structure model' 
_pdbx_audit_revision_group.group               'Database references' 
# 
loop_
_pdbx_audit_revision_category.ordinal 
_pdbx_audit_revision_category.revision_ordinal 
_pdbx_audit_revision_category.data_content_type 
_pdbx_audit_revision_category.category 
1 2 'Structure model' citation        
2 2 'Structure model' citation_author 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume'          
2 2 'Structure model' '_citation_author.identifier_ORCID' 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9FD7 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-16 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              g.j.poelarends@rug.nl 
_pdbx_contact_author.name_first         Gerrit 
_pdbx_contact_author.name_last          Poelarends 
_pdbx_contact_author.name_mi            J. 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-6917-6368 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Thunnissen, A.M.W.H.' 1 0000-0002-1915-9850 
'Zhou, H.'             2 ?                   
'Frietema, H.O.T.'     3 ?                   
'Poelarends, G.J.'     4 0000-0002-6917-6368 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   GE 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Angew.Chem.Int.Ed.Engl. 
_citation.journal_id_ASTM           ACIEAY 
_citation.journal_id_CSD            0179 
_citation.journal_id_ISSN           1521-3773 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            64 
_citation.language                  ? 
_citation.page_first                e202503054 
_citation.page_last                 e202503054 
_citation.title                     
'Engineering 2-Deoxy-D-ribose-5-phosphate Aldolase for anti- and syn-Selective Epoxidations of alpha , beta-Unsaturated Aldehydes.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/anie.202503054 
_citation.pdbx_database_id_PubMed   39993220 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Zhou, H.'           1 ?                   
primary 'Kunzendorf, A.'     2 ?                   
primary 'Xu, G.'             3 ?                   
primary 'Frietema, H.O.T.'   4 ?                   
primary 'Thunnissen, A.W.H.' 5 ?                   
primary 'Poelarends, G.J.'   6 0000-0002-6917-6368 
# 
loop_
_entity.id 
_entity.type 
_entity.src_method 
_entity.pdbx_description 
_entity.formula_weight 
_entity.pdbx_number_of_molecules 
_entity.pdbx_ec 
_entity.pdbx_mutation 
_entity.pdbx_fragment 
_entity.details 
1 polymer     man 'Deoxyribose-phosphate aldolase' 28715.734 2   4.1.2.4 
'T18S, L20S, D22G, D24Y, C47S, I48V, F52S, K172R, T197S, P202V, A203T, R207S, G236S, S239GEs' ? ? 
2 non-polymer syn GLYCEROL                         92.094    5   ?       ? ? ? 
3 water       nat water                            18.015    207 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'DERA,2-deoxy-D-ribose 5-phosphate aldolase,Phosphodeoxyriboaldolase,Deoxyriboaldolase' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;MTDLKASSLRALKLMDLSTLNGDYTDEKVIALCHQAKTPVGNTAAISVYPRSIPIARKTLKEQGTPEIRIATVTNFPHGN
DDIEIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIK
AGADFIKTSTGRVAVNATPESARIMMEVIRDMGVEKSVGFKVTGGVSTAEDAQKYLAIADELFGADWADARHYRFSASGL
LASLLKALGHGDGKSASSYLEHHHHHH
;
_entity_poly.pdbx_seq_one_letter_code_can   
;MTDLKASSLRALKLMDLSTLNGDYTDEKVIALCHQAKTPVGNTAAISVYPRSIPIARKTLKEQGTPEIRIATVTNFPHGN
DDIEIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIK
AGADFIKTSTGRVAVNATPESARIMMEVIRDMGVEKSVGFKVTGGVSTAEDAQKYLAIADELFGADWADARHYRFSASGL
LASLLKALGHGDGKSASSYLEHHHHHH
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 GLYCEROL GOL 
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   THR n 
1 3   ASP n 
1 4   LEU n 
1 5   LYS n 
1 6   ALA n 
1 7   SER n 
1 8   SER n 
1 9   LEU n 
1 10  ARG n 
1 11  ALA n 
1 12  LEU n 
1 13  LYS n 
1 14  LEU n 
1 15  MET n 
1 16  ASP n 
1 17  LEU n 
1 18  SER n 
1 19  THR n 
1 20  LEU n 
1 21  ASN n 
1 22  GLY n 
1 23  ASP n 
1 24  TYR n 
1 25  THR n 
1 26  ASP n 
1 27  GLU n 
1 28  LYS n 
1 29  VAL n 
1 30  ILE n 
1 31  ALA n 
1 32  LEU n 
1 33  CYS n 
1 34  HIS n 
1 35  GLN n 
1 36  ALA n 
1 37  LYS n 
1 38  THR n 
1 39  PRO n 
1 40  VAL n 
1 41  GLY n 
1 42  ASN n 
1 43  THR n 
1 44  ALA n 
1 45  ALA n 
1 46  ILE n 
1 47  SER n 
1 48  VAL n 
1 49  TYR n 
1 50  PRO n 
1 51  ARG n 
1 52  SER n 
1 53  ILE n 
1 54  PRO n 
1 55  ILE n 
1 56  ALA n 
1 57  ARG n 
1 58  LYS n 
1 59  THR n 
1 60  LEU n 
1 61  LYS n 
1 62  GLU n 
1 63  GLN n 
1 64  GLY n 
1 65  THR n 
1 66  PRO n 
1 67  GLU n 
1 68  ILE n 
1 69  ARG n 
1 70  ILE n 
1 71  ALA n 
1 72  THR n 
1 73  VAL n 
1 74  THR n 
1 75  ASN n 
1 76  PHE n 
1 77  PRO n 
1 78  HIS n 
1 79  GLY n 
1 80  ASN n 
1 81  ASP n 
1 82  ASP n 
1 83  ILE n 
1 84  GLU n 
1 85  ILE n 
1 86  ALA n 
1 87  LEU n 
1 88  ALA n 
1 89  GLU n 
1 90  THR n 
1 91  ARG n 
1 92  ALA n 
1 93  ALA n 
1 94  ILE n 
1 95  ALA n 
1 96  TYR n 
1 97  GLY n 
1 98  ALA n 
1 99  ASP n 
1 100 GLU n 
1 101 VAL n 
1 102 ASP n 
1 103 VAL n 
1 104 VAL n 
1 105 PHE n 
1 106 PRO n 
1 107 TYR n 
1 108 ARG n 
1 109 ALA n 
1 110 LEU n 
1 111 MET n 
1 112 ALA n 
1 113 GLY n 
1 114 ASN n 
1 115 GLU n 
1 116 GLN n 
1 117 VAL n 
1 118 GLY n 
1 119 PHE n 
1 120 ASP n 
1 121 LEU n 
1 122 VAL n 
1 123 LYS n 
1 124 ALA n 
1 125 CYS n 
1 126 LYS n 
1 127 GLU n 
1 128 ALA n 
1 129 CYS n 
1 130 ALA n 
1 131 ALA n 
1 132 ALA n 
1 133 ASN n 
1 134 VAL n 
1 135 LEU n 
1 136 LEU n 
1 137 LYS n 
1 138 VAL n 
1 139 ILE n 
1 140 ILE n 
1 141 GLU n 
1 142 THR n 
1 143 GLY n 
1 144 GLU n 
1 145 LEU n 
1 146 LYS n 
1 147 ASP n 
1 148 GLU n 
1 149 ALA n 
1 150 LEU n 
1 151 ILE n 
1 152 ARG n 
1 153 LYS n 
1 154 ALA n 
1 155 SER n 
1 156 GLU n 
1 157 ILE n 
1 158 SER n 
1 159 ILE n 
1 160 LYS n 
1 161 ALA n 
1 162 GLY n 
1 163 ALA n 
1 164 ASP n 
1 165 PHE n 
1 166 ILE n 
1 167 LYS n 
1 168 THR n 
1 169 SER n 
1 170 THR n 
1 171 GLY n 
1 172 ARG n 
1 173 VAL n 
1 174 ALA n 
1 175 VAL n 
1 176 ASN n 
1 177 ALA n 
1 178 THR n 
1 179 PRO n 
1 180 GLU n 
1 181 SER n 
1 182 ALA n 
1 183 ARG n 
1 184 ILE n 
1 185 MET n 
1 186 MET n 
1 187 GLU n 
1 188 VAL n 
1 189 ILE n 
1 190 ARG n 
1 191 ASP n 
1 192 MET n 
1 193 GLY n 
1 194 VAL n 
1 195 GLU n 
1 196 LYS n 
1 197 SER n 
1 198 VAL n 
1 199 GLY n 
1 200 PHE n 
1 201 LYS n 
1 202 VAL n 
1 203 THR n 
1 204 GLY n 
1 205 GLY n 
1 206 VAL n 
1 207 SER n 
1 208 THR n 
1 209 ALA n 
1 210 GLU n 
1 211 ASP n 
1 212 ALA n 
1 213 GLN n 
1 214 LYS n 
1 215 TYR n 
1 216 LEU n 
1 217 ALA n 
1 218 ILE n 
1 219 ALA n 
1 220 ASP n 
1 221 GLU n 
1 222 LEU n 
1 223 PHE n 
1 224 GLY n 
1 225 ALA n 
1 226 ASP n 
1 227 TRP n 
1 228 ALA n 
1 229 ASP n 
1 230 ALA n 
1 231 ARG n 
1 232 HIS n 
1 233 TYR n 
1 234 ARG n 
1 235 PHE n 
1 236 SER n 
1 237 ALA n 
1 238 SER n 
1 239 GLY n 
1 240 LEU n 
1 241 LEU n 
1 242 ALA n 
1 243 SER n 
1 244 LEU n 
1 245 LEU n 
1 246 LYS n 
1 247 ALA n 
1 248 LEU n 
1 249 GLY n 
1 250 HIS n 
1 251 GLY n 
1 252 ASP n 
1 253 GLY n 
1 254 LYS n 
1 255 SER n 
1 256 ALA n 
1 257 SER n 
1 258 SER n 
1 259 TYR n 
1 260 LEU n 
1 261 GLU n 
1 262 HIS n 
1 263 HIS n 
1 264 HIS n 
1 265 HIS n 
1 266 HIS n 
1 267 HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   267 
_entity_src_gen.gene_src_common_name               ? 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'deoC, EcolC_3675' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     562 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ?                               'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ?                               'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ?                               'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?                               'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ?                               'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ?                               'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?                               'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ?                               'C2 H5 N O2'     75.067  
GOL non-polymer         . GLYCEROL        'GLYCERIN; PROPANE-1,2,3-TRIOL' 'C3 H8 O3'       92.094  
HIS 'L-peptide linking' y HISTIDINE       ?                               'C6 H10 N3 O2 1' 156.162 
HOH non-polymer         . WATER           ?                               'H2 O'           18.015  
ILE 'L-peptide linking' y ISOLEUCINE      ?                               'C6 H13 N O2'    131.173 
LEU 'L-peptide linking' y LEUCINE         ?                               'C6 H13 N O2'    131.173 
LYS 'L-peptide linking' y LYSINE          ?                               'C6 H15 N2 O2 1' 147.195 
MET 'L-peptide linking' y METHIONINE      ?                               'C5 H11 N O2 S'  149.211 
PHE 'L-peptide linking' y PHENYLALANINE   ?                               'C9 H11 N O2'    165.189 
PRO 'L-peptide linking' y PROLINE         ?                               'C5 H9 N O2'     115.130 
SER 'L-peptide linking' y SERINE          ?                               'C3 H7 N O3'     105.093 
THR 'L-peptide linking' y THREONINE       ?                               'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ?                               'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ?                               'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ?                               'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   MET 1   1   ?   ?   ?   A . n 
A 1 2   THR 2   2   ?   ?   ?   A . n 
A 1 3   ASP 3   3   ?   ?   ?   A . n 
A 1 4   LEU 4   4   4   LEU LEU A . n 
A 1 5   LYS 5   5   5   LYS LYS A . n 
A 1 6   ALA 6   6   6   ALA ALA A . n 
A 1 7   SER 7   7   7   SER SER A . n 
A 1 8   SER 8   8   8   SER SER A . n 
A 1 9   LEU 9   9   9   LEU LEU A . n 
A 1 10  ARG 10  10  10  ARG ARG A . n 
A 1 11  ALA 11  11  11  ALA ALA A . n 
A 1 12  LEU 12  12  12  LEU LEU A . n 
A 1 13  LYS 13  13  13  LYS LYS A . n 
A 1 14  LEU 14  14  14  LEU LEU A . n 
A 1 15  MET 15  15  15  MET MET A . n 
A 1 16  ASP 16  16  16  ASP ASP A . n 
A 1 17  LEU 17  17  17  LEU LEU A . n 
A 1 18  SER 18  18  18  SER SER A . n 
A 1 19  THR 19  19  ?   ?   ?   A . n 
A 1 20  LEU 20  20  ?   ?   ?   A . n 
A 1 21  ASN 21  21  ?   ?   ?   A . n 
A 1 22  GLY 22  22  ?   ?   ?   A . n 
A 1 23  ASP 23  23  ?   ?   ?   A . n 
A 1 24  TYR 24  24  ?   ?   ?   A . n 
A 1 25  THR 25  25  25  THR THR A . n 
A 1 26  ASP 26  26  26  ASP ASP A . n 
A 1 27  GLU 27  27  27  GLU GLU A . n 
A 1 28  LYS 28  28  28  LYS LYS A . n 
A 1 29  VAL 29  29  29  VAL VAL A . n 
A 1 30  ILE 30  30  30  ILE ILE A . n 
A 1 31  ALA 31  31  31  ALA ALA A . n 
A 1 32  LEU 32  32  32  LEU LEU A . n 
A 1 33  CYS 33  33  33  CYS CYS A . n 
A 1 34  HIS 34  34  34  HIS HIS A . n 
A 1 35  GLN 35  35  35  GLN GLN A . n 
A 1 36  ALA 36  36  36  ALA ALA A . n 
A 1 37  LYS 37  37  37  LYS LYS A . n 
A 1 38  THR 38  38  38  THR THR A . n 
A 1 39  PRO 39  39  39  PRO PRO A . n 
A 1 40  VAL 40  40  40  VAL VAL A . n 
A 1 41  GLY 41  41  41  GLY GLY A . n 
A 1 42  ASN 42  42  42  ASN ASN A . n 
A 1 43  THR 43  43  43  THR THR A . n 
A 1 44  ALA 44  44  44  ALA ALA A . n 
A 1 45  ALA 45  45  45  ALA ALA A . n 
A 1 46  ILE 46  46  46  ILE ILE A . n 
A 1 47  SER 47  47  47  SER SER A . n 
A 1 48  VAL 48  48  48  VAL VAL A . n 
A 1 49  TYR 49  49  49  TYR TYR A . n 
A 1 50  PRO 50  50  50  PRO PRO A . n 
A 1 51  ARG 51  51  51  ARG ARG A . n 
A 1 52  SER 52  52  52  SER SER A . n 
A 1 53  ILE 53  53  53  ILE ILE A . n 
A 1 54  PRO 54  54  54  PRO PRO A . n 
A 1 55  ILE 55  55  55  ILE ILE A . n 
A 1 56  ALA 56  56  56  ALA ALA A . n 
A 1 57  ARG 57  57  57  ARG ARG A . n 
A 1 58  LYS 58  58  58  LYS LYS A . n 
A 1 59  THR 59  59  59  THR THR A . n 
A 1 60  LEU 60  60  60  LEU LEU A . n 
A 1 61  LYS 61  61  61  LYS LYS A . n 
A 1 62  GLU 62  62  62  GLU GLU A . n 
A 1 63  GLN 63  63  63  GLN GLN A . n 
A 1 64  GLY 64  64  64  GLY GLY A . n 
A 1 65  THR 65  65  65  THR THR A . n 
A 1 66  PRO 66  66  66  PRO PRO A . n 
A 1 67  GLU 67  67  67  GLU GLU A . n 
A 1 68  ILE 68  68  68  ILE ILE A . n 
A 1 69  ARG 69  69  69  ARG ARG A . n 
A 1 70  ILE 70  70  70  ILE ILE A . n 
A 1 71  ALA 71  71  71  ALA ALA A . n 
A 1 72  THR 72  72  72  THR THR A . n 
A 1 73  VAL 73  73  73  VAL VAL A . n 
A 1 74  THR 74  74  74  THR THR A . n 
A 1 75  ASN 75  75  75  ASN ASN A . n 
A 1 76  PHE 76  76  76  PHE PHE A . n 
A 1 77  PRO 77  77  77  PRO PRO A . n 
A 1 78  HIS 78  78  78  HIS HIS A . n 
A 1 79  GLY 79  79  79  GLY GLY A . n 
A 1 80  ASN 80  80  80  ASN ASN A . n 
A 1 81  ASP 81  81  81  ASP ASP A . n 
A 1 82  ASP 82  82  82  ASP ASP A . n 
A 1 83  ILE 83  83  83  ILE ILE A . n 
A 1 84  GLU 84  84  84  GLU GLU A . n 
A 1 85  ILE 85  85  85  ILE ILE A . n 
A 1 86  ALA 86  86  86  ALA ALA A . n 
A 1 87  LEU 87  87  87  LEU LEU A . n 
A 1 88  ALA 88  88  88  ALA ALA A . n 
A 1 89  GLU 89  89  89  GLU GLU A . n 
A 1 90  THR 90  90  90  THR THR A . n 
A 1 91  ARG 91  91  91  ARG ARG A . n 
A 1 92  ALA 92  92  92  ALA ALA A . n 
A 1 93  ALA 93  93  93  ALA ALA A . n 
A 1 94  ILE 94  94  94  ILE ILE A . n 
A 1 95  ALA 95  95  95  ALA ALA A . n 
A 1 96  TYR 96  96  96  TYR TYR A . n 
A 1 97  GLY 97  97  97  GLY GLY A . n 
A 1 98  ALA 98  98  98  ALA ALA A . n 
A 1 99  ASP 99  99  99  ASP ASP A . n 
A 1 100 GLU 100 100 100 GLU GLU A . n 
A 1 101 VAL 101 101 101 VAL VAL A . n 
A 1 102 ASP 102 102 102 ASP ASP A . n 
A 1 103 VAL 103 103 103 VAL VAL A . n 
A 1 104 VAL 104 104 104 VAL VAL A . n 
A 1 105 PHE 105 105 105 PHE PHE A . n 
A 1 106 PRO 106 106 106 PRO PRO A . n 
A 1 107 TYR 107 107 107 TYR TYR A . n 
A 1 108 ARG 108 108 108 ARG ARG A . n 
A 1 109 ALA 109 109 109 ALA ALA A . n 
A 1 110 LEU 110 110 110 LEU LEU A . n 
A 1 111 MET 111 111 111 MET MET A . n 
A 1 112 ALA 112 112 112 ALA ALA A . n 
A 1 113 GLY 113 113 113 GLY GLY A . n 
A 1 114 ASN 114 114 114 ASN ASN A . n 
A 1 115 GLU 115 115 115 GLU GLU A . n 
A 1 116 GLN 116 116 116 GLN GLN A . n 
A 1 117 VAL 117 117 117 VAL VAL A . n 
A 1 118 GLY 118 118 118 GLY GLY A . n 
A 1 119 PHE 119 119 119 PHE PHE A . n 
A 1 120 ASP 120 120 120 ASP ASP A . n 
A 1 121 LEU 121 121 121 LEU LEU A . n 
A 1 122 VAL 122 122 122 VAL VAL A . n 
A 1 123 LYS 123 123 123 LYS LYS A . n 
A 1 124 ALA 124 124 124 ALA ALA A . n 
A 1 125 CYS 125 125 125 CYS CYS A . n 
A 1 126 LYS 126 126 126 LYS LYS A . n 
A 1 127 GLU 127 127 127 GLU GLU A . n 
A 1 128 ALA 128 128 128 ALA ALA A . n 
A 1 129 CYS 129 129 129 CYS CYS A . n 
A 1 130 ALA 130 130 130 ALA ALA A . n 
A 1 131 ALA 131 131 131 ALA ALA A . n 
A 1 132 ALA 132 132 132 ALA ALA A . n 
A 1 133 ASN 133 133 133 ASN ASN A . n 
A 1 134 VAL 134 134 134 VAL VAL A . n 
A 1 135 LEU 135 135 135 LEU LEU A . n 
A 1 136 LEU 136 136 136 LEU LEU A . n 
A 1 137 LYS 137 137 137 LYS LYS A . n 
A 1 138 VAL 138 138 138 VAL VAL A . n 
A 1 139 ILE 139 139 139 ILE ILE A . n 
A 1 140 ILE 140 140 140 ILE ILE A . n 
A 1 141 GLU 141 141 141 GLU GLU A . n 
A 1 142 THR 142 142 142 THR THR A . n 
A 1 143 GLY 143 143 143 GLY GLY A . n 
A 1 144 GLU 144 144 144 GLU GLU A . n 
A 1 145 LEU 145 145 145 LEU LEU A . n 
A 1 146 LYS 146 146 146 LYS LYS A . n 
A 1 147 ASP 147 147 147 ASP ASP A . n 
A 1 148 GLU 148 148 148 GLU GLU A . n 
A 1 149 ALA 149 149 149 ALA ALA A . n 
A 1 150 LEU 150 150 150 LEU LEU A . n 
A 1 151 ILE 151 151 151 ILE ILE A . n 
A 1 152 ARG 152 152 152 ARG ARG A . n 
A 1 153 LYS 153 153 153 LYS LYS A . n 
A 1 154 ALA 154 154 154 ALA ALA A . n 
A 1 155 SER 155 155 155 SER SER A . n 
A 1 156 GLU 156 156 156 GLU GLU A . n 
A 1 157 ILE 157 157 157 ILE ILE A . n 
A 1 158 SER 158 158 158 SER SER A . n 
A 1 159 ILE 159 159 159 ILE ILE A . n 
A 1 160 LYS 160 160 160 LYS LYS A . n 
A 1 161 ALA 161 161 161 ALA ALA A . n 
A 1 162 GLY 162 162 162 GLY GLY A . n 
A 1 163 ALA 163 163 163 ALA ALA A . n 
A 1 164 ASP 164 164 164 ASP ASP A . n 
A 1 165 PHE 165 165 165 PHE PHE A . n 
A 1 166 ILE 166 166 166 ILE ILE A . n 
A 1 167 LYS 167 167 167 LYS LYS A . n 
A 1 168 THR 168 168 168 THR THR A . n 
A 1 169 SER 169 169 169 SER SER A . n 
A 1 170 THR 170 170 170 THR THR A . n 
A 1 171 GLY 171 171 171 GLY GLY A . n 
A 1 172 ARG 172 172 172 ARG ARG A . n 
A 1 173 VAL 173 173 173 VAL VAL A . n 
A 1 174 ALA 174 174 174 ALA ALA A . n 
A 1 175 VAL 175 175 175 VAL VAL A . n 
A 1 176 ASN 176 176 176 ASN ASN A . n 
A 1 177 ALA 177 177 177 ALA ALA A . n 
A 1 178 THR 178 178 178 THR THR A . n 
A 1 179 PRO 179 179 179 PRO PRO A . n 
A 1 180 GLU 180 180 180 GLU GLU A . n 
A 1 181 SER 181 181 181 SER SER A . n 
A 1 182 ALA 182 182 182 ALA ALA A . n 
A 1 183 ARG 183 183 183 ARG ARG A . n 
A 1 184 ILE 184 184 184 ILE ILE A . n 
A 1 185 MET 185 185 185 MET MET A . n 
A 1 186 MET 186 186 186 MET MET A . n 
A 1 187 GLU 187 187 187 GLU GLU A . n 
A 1 188 VAL 188 188 188 VAL VAL A . n 
A 1 189 ILE 189 189 189 ILE ILE A . n 
A 1 190 ARG 190 190 190 ARG ARG A . n 
A 1 191 ASP 191 191 191 ASP ASP A . n 
A 1 192 MET 192 192 192 MET MET A . n 
A 1 193 GLY 193 193 193 GLY GLY A . n 
A 1 194 VAL 194 194 194 VAL VAL A . n 
A 1 195 GLU 195 195 195 GLU GLU A . n 
A 1 196 LYS 196 196 196 LYS LYS A . n 
A 1 197 SER 197 197 197 SER SER A . n 
A 1 198 VAL 198 198 198 VAL VAL A . n 
A 1 199 GLY 199 199 199 GLY GLY A . n 
A 1 200 PHE 200 200 200 PHE PHE A . n 
A 1 201 LYS 201 201 201 LYS LYS A . n 
A 1 202 VAL 202 202 202 VAL VAL A . n 
A 1 203 THR 203 203 203 THR THR A . n 
A 1 204 GLY 204 204 204 GLY GLY A . n 
A 1 205 GLY 205 205 205 GLY GLY A . n 
A 1 206 VAL 206 206 206 VAL VAL A . n 
A 1 207 SER 207 207 207 SER SER A . n 
A 1 208 THR 208 208 208 THR THR A . n 
A 1 209 ALA 209 209 209 ALA ALA A . n 
A 1 210 GLU 210 210 210 GLU GLU A . n 
A 1 211 ASP 211 211 211 ASP ASP A . n 
A 1 212 ALA 212 212 212 ALA ALA A . n 
A 1 213 GLN 213 213 213 GLN GLN A . n 
A 1 214 LYS 214 214 214 LYS LYS A . n 
A 1 215 TYR 215 215 215 TYR TYR A . n 
A 1 216 LEU 216 216 216 LEU LEU A . n 
A 1 217 ALA 217 217 217 ALA ALA A . n 
A 1 218 ILE 218 218 218 ILE ILE A . n 
A 1 219 ALA 219 219 219 ALA ALA A . n 
A 1 220 ASP 220 220 220 ASP ASP A . n 
A 1 221 GLU 221 221 221 GLU GLU A . n 
A 1 222 LEU 222 222 222 LEU LEU A . n 
A 1 223 PHE 223 223 223 PHE PHE A . n 
A 1 224 GLY 224 224 224 GLY GLY A . n 
A 1 225 ALA 225 225 225 ALA ALA A . n 
A 1 226 ASP 226 226 226 ASP ASP A . n 
A 1 227 TRP 227 227 227 TRP TRP A . n 
A 1 228 ALA 228 228 228 ALA ALA A . n 
A 1 229 ASP 229 229 229 ASP ASP A . n 
A 1 230 ALA 230 230 230 ALA ALA A . n 
A 1 231 ARG 231 231 231 ARG ARG A . n 
A 1 232 HIS 232 232 232 HIS HIS A . n 
A 1 233 TYR 233 233 233 TYR TYR A . n 
A 1 234 ARG 234 234 234 ARG ARG A . n 
A 1 235 PHE 235 235 235 PHE PHE A . n 
A 1 236 SER 236 236 236 SER SER A . n 
A 1 237 ALA 237 237 237 ALA ALA A . n 
A 1 238 SER 238 238 238 SER SER A . n 
A 1 239 GLY 239 239 239 GLY GLY A . n 
A 1 240 LEU 240 240 240 LEU LEU A . n 
A 1 241 LEU 241 241 241 LEU LEU A . n 
A 1 242 ALA 242 242 242 ALA ALA A . n 
A 1 243 SER 243 243 243 SER SER A . n 
A 1 244 LEU 244 244 244 LEU LEU A . n 
A 1 245 LEU 245 245 245 LEU LEU A . n 
A 1 246 LYS 246 246 246 LYS LYS A . n 
A 1 247 ALA 247 247 247 ALA ALA A . n 
A 1 248 LEU 248 248 248 LEU LEU A . n 
A 1 249 GLY 249 249 249 GLY GLY A . n 
A 1 250 HIS 250 250 250 HIS HIS A . n 
A 1 251 GLY 251 251 ?   ?   ?   A . n 
A 1 252 ASP 252 252 ?   ?   ?   A . n 
A 1 253 GLY 253 253 ?   ?   ?   A . n 
A 1 254 LYS 254 254 ?   ?   ?   A . n 
A 1 255 SER 255 255 ?   ?   ?   A . n 
A 1 256 ALA 256 256 ?   ?   ?   A . n 
A 1 257 SER 257 257 ?   ?   ?   A . n 
A 1 258 SER 258 258 ?   ?   ?   A . n 
A 1 259 TYR 259 259 ?   ?   ?   A . n 
A 1 260 LEU 260 260 ?   ?   ?   A . n 
A 1 261 GLU 261 261 ?   ?   ?   A . n 
A 1 262 HIS 262 262 ?   ?   ?   A . n 
A 1 263 HIS 263 263 ?   ?   ?   A . n 
A 1 264 HIS 264 264 ?   ?   ?   A . n 
A 1 265 HIS 265 265 ?   ?   ?   A . n 
A 1 266 HIS 266 266 ?   ?   ?   A . n 
A 1 267 HIS 267 267 ?   ?   ?   A . n 
B 1 1   MET 1   1   ?   ?   ?   B . n 
B 1 2   THR 2   2   ?   ?   ?   B . n 
B 1 3   ASP 3   3   3   ASP ASP B . n 
B 1 4   LEU 4   4   4   LEU LEU B . n 
B 1 5   LYS 5   5   5   LYS LYS B . n 
B 1 6   ALA 6   6   6   ALA ALA B . n 
B 1 7   SER 7   7   7   SER SER B . n 
B 1 8   SER 8   8   8   SER SER B . n 
B 1 9   LEU 9   9   9   LEU LEU B . n 
B 1 10  ARG 10  10  10  ARG ARG B . n 
B 1 11  ALA 11  11  11  ALA ALA B . n 
B 1 12  LEU 12  12  12  LEU LEU B . n 
B 1 13  LYS 13  13  13  LYS LYS B . n 
B 1 14  LEU 14  14  14  LEU LEU B . n 
B 1 15  MET 15  15  15  MET MET B . n 
B 1 16  ASP 16  16  16  ASP ASP B . n 
B 1 17  LEU 17  17  17  LEU LEU B . n 
B 1 18  SER 18  18  18  SER SER B . n 
B 1 19  THR 19  19  19  THR THR B . n 
B 1 20  LEU 20  20  ?   ?   ?   B . n 
B 1 21  ASN 21  21  ?   ?   ?   B . n 
B 1 22  GLY 22  22  22  GLY GLY B . n 
B 1 23  ASP 23  23  23  ASP ASP B . n 
B 1 24  TYR 24  24  24  TYR TYR B . n 
B 1 25  THR 25  25  25  THR THR B . n 
B 1 26  ASP 26  26  26  ASP ASP B . n 
B 1 27  GLU 27  27  27  GLU GLU B . n 
B 1 28  LYS 28  28  28  LYS LYS B . n 
B 1 29  VAL 29  29  29  VAL VAL B . n 
B 1 30  ILE 30  30  30  ILE ILE B . n 
B 1 31  ALA 31  31  31  ALA ALA B . n 
B 1 32  LEU 32  32  32  LEU LEU B . n 
B 1 33  CYS 33  33  33  CYS CYS B . n 
B 1 34  HIS 34  34  34  HIS HIS B . n 
B 1 35  GLN 35  35  35  GLN GLN B . n 
B 1 36  ALA 36  36  36  ALA ALA B . n 
B 1 37  LYS 37  37  37  LYS LYS B . n 
B 1 38  THR 38  38  38  THR THR B . n 
B 1 39  PRO 39  39  39  PRO PRO B . n 
B 1 40  VAL 40  40  40  VAL VAL B . n 
B 1 41  GLY 41  41  41  GLY GLY B . n 
B 1 42  ASN 42  42  42  ASN ASN B . n 
B 1 43  THR 43  43  43  THR THR B . n 
B 1 44  ALA 44  44  44  ALA ALA B . n 
B 1 45  ALA 45  45  45  ALA ALA B . n 
B 1 46  ILE 46  46  46  ILE ILE B . n 
B 1 47  SER 47  47  47  SER SER B . n 
B 1 48  VAL 48  48  48  VAL VAL B . n 
B 1 49  TYR 49  49  49  TYR TYR B . n 
B 1 50  PRO 50  50  50  PRO PRO B . n 
B 1 51  ARG 51  51  51  ARG ARG B . n 
B 1 52  SER 52  52  52  SER SER B . n 
B 1 53  ILE 53  53  53  ILE ILE B . n 
B 1 54  PRO 54  54  54  PRO PRO B . n 
B 1 55  ILE 55  55  55  ILE ILE B . n 
B 1 56  ALA 56  56  56  ALA ALA B . n 
B 1 57  ARG 57  57  57  ARG ARG B . n 
B 1 58  LYS 58  58  58  LYS LYS B . n 
B 1 59  THR 59  59  59  THR THR B . n 
B 1 60  LEU 60  60  60  LEU LEU B . n 
B 1 61  LYS 61  61  61  LYS LYS B . n 
B 1 62  GLU 62  62  62  GLU GLU B . n 
B 1 63  GLN 63  63  63  GLN GLN B . n 
B 1 64  GLY 64  64  64  GLY GLY B . n 
B 1 65  THR 65  65  65  THR THR B . n 
B 1 66  PRO 66  66  66  PRO PRO B . n 
B 1 67  GLU 67  67  67  GLU GLU B . n 
B 1 68  ILE 68  68  68  ILE ILE B . n 
B 1 69  ARG 69  69  69  ARG ARG B . n 
B 1 70  ILE 70  70  70  ILE ILE B . n 
B 1 71  ALA 71  71  71  ALA ALA B . n 
B 1 72  THR 72  72  72  THR THR B . n 
B 1 73  VAL 73  73  73  VAL VAL B . n 
B 1 74  THR 74  74  74  THR THR B . n 
B 1 75  ASN 75  75  75  ASN ASN B . n 
B 1 76  PHE 76  76  76  PHE PHE B . n 
B 1 77  PRO 77  77  77  PRO PRO B . n 
B 1 78  HIS 78  78  78  HIS HIS B C n 
B 1 79  GLY 79  79  79  GLY GLY B . n 
B 1 80  ASN 80  80  80  ASN ASN B . n 
B 1 81  ASP 81  81  81  ASP ASP B . n 
B 1 82  ASP 82  82  82  ASP ASP B . n 
B 1 83  ILE 83  83  83  ILE ILE B . n 
B 1 84  GLU 84  84  84  GLU GLU B . n 
B 1 85  ILE 85  85  85  ILE ILE B . n 
B 1 86  ALA 86  86  86  ALA ALA B . n 
B 1 87  LEU 87  87  87  LEU LEU B . n 
B 1 88  ALA 88  88  88  ALA ALA B . n 
B 1 89  GLU 89  89  89  GLU GLU B . n 
B 1 90  THR 90  90  90  THR THR B . n 
B 1 91  ARG 91  91  91  ARG ARG B . n 
B 1 92  ALA 92  92  92  ALA ALA B . n 
B 1 93  ALA 93  93  93  ALA ALA B . n 
B 1 94  ILE 94  94  94  ILE ILE B . n 
B 1 95  ALA 95  95  95  ALA ALA B . n 
B 1 96  TYR 96  96  96  TYR TYR B . n 
B 1 97  GLY 97  97  97  GLY GLY B . n 
B 1 98  ALA 98  98  98  ALA ALA B . n 
B 1 99  ASP 99  99  99  ASP ASP B . n 
B 1 100 GLU 100 100 100 GLU GLU B . n 
B 1 101 VAL 101 101 101 VAL VAL B . n 
B 1 102 ASP 102 102 102 ASP ASP B . n 
B 1 103 VAL 103 103 103 VAL VAL B . n 
B 1 104 VAL 104 104 104 VAL VAL B . n 
B 1 105 PHE 105 105 105 PHE PHE B . n 
B 1 106 PRO 106 106 106 PRO PRO B . n 
B 1 107 TYR 107 107 107 TYR TYR B . n 
B 1 108 ARG 108 108 108 ARG ARG B . n 
B 1 109 ALA 109 109 109 ALA ALA B . n 
B 1 110 LEU 110 110 110 LEU LEU B . n 
B 1 111 MET 111 111 111 MET MET B . n 
B 1 112 ALA 112 112 112 ALA ALA B . n 
B 1 113 GLY 113 113 113 GLY GLY B . n 
B 1 114 ASN 114 114 114 ASN ASN B . n 
B 1 115 GLU 115 115 115 GLU GLU B . n 
B 1 116 GLN 116 116 116 GLN GLN B . n 
B 1 117 VAL 117 117 117 VAL VAL B . n 
B 1 118 GLY 118 118 118 GLY GLY B . n 
B 1 119 PHE 119 119 119 PHE PHE B . n 
B 1 120 ASP 120 120 120 ASP ASP B . n 
B 1 121 LEU 121 121 121 LEU LEU B . n 
B 1 122 VAL 122 122 122 VAL VAL B . n 
B 1 123 LYS 123 123 123 LYS LYS B . n 
B 1 124 ALA 124 124 124 ALA ALA B . n 
B 1 125 CYS 125 125 125 CYS CYS B . n 
B 1 126 LYS 126 126 126 LYS LYS B . n 
B 1 127 GLU 127 127 127 GLU GLU B . n 
B 1 128 ALA 128 128 128 ALA ALA B . n 
B 1 129 CYS 129 129 129 CYS CYS B . n 
B 1 130 ALA 130 130 130 ALA ALA B . n 
B 1 131 ALA 131 131 131 ALA ALA B . n 
B 1 132 ALA 132 132 132 ALA ALA B . n 
B 1 133 ASN 133 133 133 ASN ASN B . n 
B 1 134 VAL 134 134 134 VAL VAL B . n 
B 1 135 LEU 135 135 135 LEU LEU B . n 
B 1 136 LEU 136 136 136 LEU LEU B . n 
B 1 137 LYS 137 137 137 LYS LYS B . n 
B 1 138 VAL 138 138 138 VAL VAL B . n 
B 1 139 ILE 139 139 139 ILE ILE B . n 
B 1 140 ILE 140 140 140 ILE ILE B . n 
B 1 141 GLU 141 141 141 GLU GLU B . n 
B 1 142 THR 142 142 142 THR THR B . n 
B 1 143 GLY 143 143 143 GLY GLY B . n 
B 1 144 GLU 144 144 144 GLU GLU B . n 
B 1 145 LEU 145 145 145 LEU LEU B . n 
B 1 146 LYS 146 146 146 LYS LYS B . n 
B 1 147 ASP 147 147 147 ASP ASP B . n 
B 1 148 GLU 148 148 148 GLU GLU B . n 
B 1 149 ALA 149 149 149 ALA ALA B . n 
B 1 150 LEU 150 150 150 LEU LEU B . n 
B 1 151 ILE 151 151 151 ILE ILE B . n 
B 1 152 ARG 152 152 152 ARG ARG B . n 
B 1 153 LYS 153 153 153 LYS LYS B . n 
B 1 154 ALA 154 154 154 ALA ALA B . n 
B 1 155 SER 155 155 155 SER SER B . n 
B 1 156 GLU 156 156 156 GLU GLU B . n 
B 1 157 ILE 157 157 157 ILE ILE B . n 
B 1 158 SER 158 158 158 SER SER B . n 
B 1 159 ILE 159 159 159 ILE ILE B . n 
B 1 160 LYS 160 160 160 LYS LYS B . n 
B 1 161 ALA 161 161 161 ALA ALA B . n 
B 1 162 GLY 162 162 162 GLY GLY B . n 
B 1 163 ALA 163 163 163 ALA ALA B . n 
B 1 164 ASP 164 164 164 ASP ASP B . n 
B 1 165 PHE 165 165 165 PHE PHE B . n 
B 1 166 ILE 166 166 166 ILE ILE B . n 
B 1 167 LYS 167 167 167 LYS LYS B . n 
B 1 168 THR 168 168 168 THR THR B . n 
B 1 169 SER 169 169 169 SER SER B . n 
B 1 170 THR 170 170 170 THR THR B . n 
B 1 171 GLY 171 171 171 GLY GLY B . n 
B 1 172 ARG 172 172 172 ARG ARG B . n 
B 1 173 VAL 173 173 173 VAL VAL B . n 
B 1 174 ALA 174 174 174 ALA ALA B . n 
B 1 175 VAL 175 175 175 VAL VAL B . n 
B 1 176 ASN 176 176 176 ASN ASN B . n 
B 1 177 ALA 177 177 177 ALA ALA B . n 
B 1 178 THR 178 178 178 THR THR B . n 
B 1 179 PRO 179 179 179 PRO PRO B . n 
B 1 180 GLU 180 180 180 GLU GLU B . n 
B 1 181 SER 181 181 181 SER SER B . n 
B 1 182 ALA 182 182 182 ALA ALA B . n 
B 1 183 ARG 183 183 183 ARG ARG B . n 
B 1 184 ILE 184 184 184 ILE ILE B . n 
B 1 185 MET 185 185 185 MET MET B . n 
B 1 186 MET 186 186 186 MET MET B . n 
B 1 187 GLU 187 187 187 GLU GLU B . n 
B 1 188 VAL 188 188 188 VAL VAL B . n 
B 1 189 ILE 189 189 189 ILE ILE B . n 
B 1 190 ARG 190 190 190 ARG ARG B . n 
B 1 191 ASP 191 191 191 ASP ASP B . n 
B 1 192 MET 192 192 192 MET MET B . n 
B 1 193 GLY 193 193 193 GLY GLY B . n 
B 1 194 VAL 194 194 194 VAL VAL B . n 
B 1 195 GLU 195 195 195 GLU GLU B . n 
B 1 196 LYS 196 196 196 LYS LYS B . n 
B 1 197 SER 197 197 197 SER SER B . n 
B 1 198 VAL 198 198 198 VAL VAL B . n 
B 1 199 GLY 199 199 199 GLY GLY B . n 
B 1 200 PHE 200 200 200 PHE PHE B . n 
B 1 201 LYS 201 201 201 LYS LYS B . n 
B 1 202 VAL 202 202 202 VAL VAL B . n 
B 1 203 THR 203 203 203 THR THR B . n 
B 1 204 GLY 204 204 204 GLY GLY B . n 
B 1 205 GLY 205 205 205 GLY GLY B . n 
B 1 206 VAL 206 206 206 VAL VAL B . n 
B 1 207 SER 207 207 207 SER SER B . n 
B 1 208 THR 208 208 208 THR THR B . n 
B 1 209 ALA 209 209 209 ALA ALA B . n 
B 1 210 GLU 210 210 210 GLU GLU B . n 
B 1 211 ASP 211 211 211 ASP ASP B . n 
B 1 212 ALA 212 212 212 ALA ALA B . n 
B 1 213 GLN 213 213 213 GLN GLN B . n 
B 1 214 LYS 214 214 214 LYS LYS B . n 
B 1 215 TYR 215 215 215 TYR TYR B . n 
B 1 216 LEU 216 216 216 LEU LEU B . n 
B 1 217 ALA 217 217 217 ALA ALA B . n 
B 1 218 ILE 218 218 218 ILE ILE B . n 
B 1 219 ALA 219 219 219 ALA ALA B . n 
B 1 220 ASP 220 220 220 ASP ASP B . n 
B 1 221 GLU 221 221 221 GLU GLU B . n 
B 1 222 LEU 222 222 222 LEU LEU B . n 
B 1 223 PHE 223 223 223 PHE PHE B . n 
B 1 224 GLY 224 224 224 GLY GLY B . n 
B 1 225 ALA 225 225 225 ALA ALA B . n 
B 1 226 ASP 226 226 226 ASP ASP B . n 
B 1 227 TRP 227 227 227 TRP TRP B . n 
B 1 228 ALA 228 228 228 ALA ALA B . n 
B 1 229 ASP 229 229 229 ASP ASP B . n 
B 1 230 ALA 230 230 230 ALA ALA B . n 
B 1 231 ARG 231 231 231 ARG ARG B . n 
B 1 232 HIS 232 232 232 HIS HIS B . n 
B 1 233 TYR 233 233 233 TYR TYR B . n 
B 1 234 ARG 234 234 234 ARG ARG B . n 
B 1 235 PHE 235 235 235 PHE PHE B . n 
B 1 236 SER 236 236 236 SER SER B . n 
B 1 237 ALA 237 237 237 ALA ALA B . n 
B 1 238 SER 238 238 238 SER SER B . n 
B 1 239 GLY 239 239 239 GLY GLY B . n 
B 1 240 LEU 240 240 240 LEU LEU B . n 
B 1 241 LEU 241 241 241 LEU LEU B . n 
B 1 242 ALA 242 242 242 ALA ALA B . n 
B 1 243 SER 243 243 243 SER SER B . n 
B 1 244 LEU 244 244 244 LEU LEU B . n 
B 1 245 LEU 245 245 245 LEU LEU B . n 
B 1 246 LYS 246 246 246 LYS LYS B . n 
B 1 247 ALA 247 247 247 ALA ALA B . n 
B 1 248 LEU 248 248 248 LEU LEU B . n 
B 1 249 GLY 249 249 249 GLY GLY B . n 
B 1 250 HIS 250 250 250 HIS HIS B . n 
B 1 251 GLY 251 251 ?   ?   ?   B . n 
B 1 252 ASP 252 252 ?   ?   ?   B . n 
B 1 253 GLY 253 253 ?   ?   ?   B . n 
B 1 254 LYS 254 254 ?   ?   ?   B . n 
B 1 255 SER 255 255 ?   ?   ?   B . n 
B 1 256 ALA 256 256 ?   ?   ?   B . n 
B 1 257 SER 257 257 ?   ?   ?   B . n 
B 1 258 SER 258 258 ?   ?   ?   B . n 
B 1 259 TYR 259 259 ?   ?   ?   B . n 
B 1 260 LEU 260 260 ?   ?   ?   B . n 
B 1 261 GLU 261 261 ?   ?   ?   B . n 
B 1 262 HIS 262 262 ?   ?   ?   B . n 
B 1 263 HIS 263 263 ?   ?   ?   B . n 
B 1 264 HIS 264 264 ?   ?   ?   B . n 
B 1 265 HIS 265 265 ?   ?   ?   B . n 
B 1 266 HIS 266 266 ?   ?   ?   B . n 
B 1 267 HIS 267 267 ?   ?   ?   B . n 
# 
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 GOL 1   301 1   GOL GOL A . 
D 2 GOL 1   301 1   GOL GOL B . 
E 2 GOL 1   302 2   GOL GOL B . 
F 2 GOL 1   303 3   GOL GOL B . 
G 2 GOL 1   304 4   GOL GOL B . 
H 3 HOH 1   401 45  HOH HOH A . 
H 3 HOH 2   402 137 HOH HOH A . 
H 3 HOH 3   403 87  HOH HOH A . 
H 3 HOH 4   404 66  HOH HOH A . 
H 3 HOH 5   405 69  HOH HOH A . 
H 3 HOH 6   406 192 HOH HOH A . 
H 3 HOH 7   407 140 HOH HOH A . 
H 3 HOH 8   408 187 HOH HOH A . 
H 3 HOH 9   409 65  HOH HOH A . 
H 3 HOH 10  410 85  HOH HOH A . 
H 3 HOH 11  411 171 HOH HOH A . 
H 3 HOH 12  412 177 HOH HOH A . 
H 3 HOH 13  413 60  HOH HOH A . 
H 3 HOH 14  414 127 HOH HOH A . 
H 3 HOH 15  415 158 HOH HOH A . 
H 3 HOH 16  416 43  HOH HOH A . 
H 3 HOH 17  417 61  HOH HOH A . 
H 3 HOH 18  418 167 HOH HOH A . 
H 3 HOH 19  419 18  HOH HOH A . 
H 3 HOH 20  420 79  HOH HOH A . 
H 3 HOH 21  421 190 HOH HOH A . 
H 3 HOH 22  422 170 HOH HOH A . 
H 3 HOH 23  423 126 HOH HOH A . 
H 3 HOH 24  424 81  HOH HOH A . 
H 3 HOH 25  425 141 HOH HOH A . 
H 3 HOH 26  426 31  HOH HOH A . 
H 3 HOH 27  427 36  HOH HOH A . 
H 3 HOH 28  428 15  HOH HOH A . 
H 3 HOH 29  429 35  HOH HOH A . 
H 3 HOH 30  430 21  HOH HOH A . 
H 3 HOH 31  431 176 HOH HOH A . 
H 3 HOH 32  432 86  HOH HOH A . 
H 3 HOH 33  433 183 HOH HOH A . 
H 3 HOH 34  434 92  HOH HOH A . 
H 3 HOH 35  435 110 HOH HOH A . 
H 3 HOH 36  436 138 HOH HOH A . 
H 3 HOH 37  437 123 HOH HOH A . 
H 3 HOH 38  438 179 HOH HOH A . 
H 3 HOH 39  439 29  HOH HOH A . 
H 3 HOH 40  440 55  HOH HOH A . 
H 3 HOH 41  441 8   HOH HOH A . 
H 3 HOH 42  442 178 HOH HOH A . 
H 3 HOH 43  443 26  HOH HOH A . 
H 3 HOH 44  444 136 HOH HOH A . 
H 3 HOH 45  445 6   HOH HOH A . 
H 3 HOH 46  446 84  HOH HOH A . 
H 3 HOH 47  447 104 HOH HOH A . 
H 3 HOH 48  448 78  HOH HOH A . 
H 3 HOH 49  449 96  HOH HOH A . 
H 3 HOH 50  450 71  HOH HOH A . 
H 3 HOH 51  451 181 HOH HOH A . 
H 3 HOH 52  452 9   HOH HOH A . 
H 3 HOH 53  453 115 HOH HOH A . 
H 3 HOH 54  454 163 HOH HOH A . 
H 3 HOH 55  455 168 HOH HOH A . 
H 3 HOH 56  456 30  HOH HOH A . 
H 3 HOH 57  457 97  HOH HOH A . 
H 3 HOH 58  458 58  HOH HOH A . 
H 3 HOH 59  459 53  HOH HOH A . 
H 3 HOH 60  460 180 HOH HOH A . 
H 3 HOH 61  461 59  HOH HOH A . 
H 3 HOH 62  462 113 HOH HOH A . 
H 3 HOH 63  463 139 HOH HOH A . 
H 3 HOH 64  464 161 HOH HOH A . 
H 3 HOH 65  465 188 HOH HOH A . 
H 3 HOH 66  466 173 HOH HOH A . 
H 3 HOH 67  467 73  HOH HOH A . 
H 3 HOH 68  468 24  HOH HOH A . 
H 3 HOH 69  469 7   HOH HOH A . 
H 3 HOH 70  470 182 HOH HOH A . 
H 3 HOH 71  471 49  HOH HOH A . 
H 3 HOH 72  472 38  HOH HOH A . 
H 3 HOH 73  473 74  HOH HOH A . 
H 3 HOH 74  474 209 HOH HOH A . 
H 3 HOH 75  475 124 HOH HOH A . 
H 3 HOH 76  476 193 HOH HOH A . 
H 3 HOH 77  477 12  HOH HOH A . 
H 3 HOH 78  478 112 HOH HOH A . 
H 3 HOH 79  479 130 HOH HOH A . 
H 3 HOH 80  480 165 HOH HOH A . 
H 3 HOH 81  481 39  HOH HOH A . 
H 3 HOH 82  482 90  HOH HOH A . 
H 3 HOH 83  483 114 HOH HOH A . 
H 3 HOH 84  484 37  HOH HOH A . 
H 3 HOH 85  485 132 HOH HOH A . 
H 3 HOH 86  486 156 HOH HOH A . 
H 3 HOH 87  487 185 HOH HOH A . 
H 3 HOH 88  488 107 HOH HOH A . 
H 3 HOH 89  489 88  HOH HOH A . 
H 3 HOH 90  490 23  HOH HOH A . 
H 3 HOH 91  491 189 HOH HOH A . 
H 3 HOH 92  492 57  HOH HOH A . 
H 3 HOH 93  493 101 HOH HOH A . 
H 3 HOH 94  494 122 HOH HOH A . 
H 3 HOH 95  495 200 HOH HOH A . 
H 3 HOH 96  496 184 HOH HOH A . 
H 3 HOH 97  497 91  HOH HOH A . 
H 3 HOH 98  498 169 HOH HOH A . 
H 3 HOH 99  499 162 HOH HOH A . 
H 3 HOH 100 500 105 HOH HOH A . 
H 3 HOH 101 501 68  HOH HOH A . 
H 3 HOH 102 502 72  HOH HOH A . 
H 3 HOH 103 503 186 HOH HOH A . 
H 3 HOH 104 504 194 HOH HOH A . 
H 3 HOH 105 505 125 HOH HOH A . 
H 3 HOH 106 506 128 HOH HOH A . 
H 3 HOH 107 507 54  HOH HOH A . 
H 3 HOH 108 508 145 HOH HOH A . 
H 3 HOH 109 509 135 HOH HOH A . 
H 3 HOH 110 510 208 HOH HOH A . 
H 3 HOH 111 511 196 HOH HOH A . 
H 3 HOH 112 512 133 HOH HOH A . 
I 3 HOH 1   401 204 HOH HOH B . 
I 3 HOH 2   402 109 HOH HOH B . 
I 3 HOH 3   403 195 HOH HOH B . 
I 3 HOH 4   404 131 HOH HOH B . 
I 3 HOH 5   405 160 HOH HOH B . 
I 3 HOH 6   406 152 HOH HOH B . 
I 3 HOH 7   407 129 HOH HOH B . 
I 3 HOH 8   408 93  HOH HOH B . 
I 3 HOH 9   409 118 HOH HOH B . 
I 3 HOH 10  410 102 HOH HOH B . 
I 3 HOH 11  411 34  HOH HOH B . 
I 3 HOH 12  412 151 HOH HOH B . 
I 3 HOH 13  413 149 HOH HOH B . 
I 3 HOH 14  414 142 HOH HOH B . 
I 3 HOH 15  415 207 HOH HOH B . 
I 3 HOH 16  416 76  HOH HOH B . 
I 3 HOH 17  417 10  HOH HOH B . 
I 3 HOH 18  418 41  HOH HOH B . 
I 3 HOH 19  419 11  HOH HOH B . 
I 3 HOH 20  420 52  HOH HOH B . 
I 3 HOH 21  421 13  HOH HOH B . 
I 3 HOH 22  422 94  HOH HOH B . 
I 3 HOH 23  423 206 HOH HOH B . 
I 3 HOH 24  424 111 HOH HOH B . 
I 3 HOH 25  425 164 HOH HOH B . 
I 3 HOH 26  426 103 HOH HOH B . 
I 3 HOH 27  427 67  HOH HOH B . 
I 3 HOH 28  428 80  HOH HOH B . 
I 3 HOH 29  429 64  HOH HOH B . 
I 3 HOH 30  430 146 HOH HOH B . 
I 3 HOH 31  431 153 HOH HOH B . 
I 3 HOH 32  432 191 HOH HOH B . 
I 3 HOH 33  433 120 HOH HOH B . 
I 3 HOH 34  434 166 HOH HOH B . 
I 3 HOH 35  435 116 HOH HOH B . 
I 3 HOH 36  436 2   HOH HOH B . 
I 3 HOH 37  437 33  HOH HOH B . 
I 3 HOH 38  438 148 HOH HOH B . 
I 3 HOH 39  439 154 HOH HOH B . 
I 3 HOH 40  440 4   HOH HOH B . 
I 3 HOH 41  441 117 HOH HOH B . 
I 3 HOH 42  442 32  HOH HOH B . 
I 3 HOH 43  443 3   HOH HOH B . 
I 3 HOH 44  444 1   HOH HOH B . 
I 3 HOH 45  445 77  HOH HOH B . 
I 3 HOH 46  446 46  HOH HOH B . 
I 3 HOH 47  447 205 HOH HOH B . 
I 3 HOH 48  448 48  HOH HOH B . 
I 3 HOH 49  449 70  HOH HOH B . 
I 3 HOH 50  450 150 HOH HOH B . 
I 3 HOH 51  451 16  HOH HOH B . 
I 3 HOH 52  452 42  HOH HOH B . 
I 3 HOH 53  453 203 HOH HOH B . 
I 3 HOH 54  454 28  HOH HOH B . 
I 3 HOH 55  455 155 HOH HOH B . 
I 3 HOH 56  456 19  HOH HOH B . 
I 3 HOH 57  457 143 HOH HOH B . 
I 3 HOH 58  458 98  HOH HOH B . 
I 3 HOH 59  459 47  HOH HOH B . 
I 3 HOH 60  460 20  HOH HOH B . 
I 3 HOH 61  461 44  HOH HOH B . 
I 3 HOH 62  462 40  HOH HOH B . 
I 3 HOH 63  463 159 HOH HOH B . 
I 3 HOH 64  464 99  HOH HOH B . 
I 3 HOH 65  465 63  HOH HOH B . 
I 3 HOH 66  466 198 HOH HOH B . 
I 3 HOH 67  467 14  HOH HOH B . 
I 3 HOH 68  468 144 HOH HOH B . 
I 3 HOH 69  469 5   HOH HOH B . 
I 3 HOH 70  470 147 HOH HOH B . 
I 3 HOH 71  471 106 HOH HOH B . 
I 3 HOH 72  472 108 HOH HOH B . 
I 3 HOH 73  473 56  HOH HOH B . 
I 3 HOH 74  474 62  HOH HOH B . 
I 3 HOH 75  475 119 HOH HOH B . 
I 3 HOH 76  476 51  HOH HOH B . 
I 3 HOH 77  477 134 HOH HOH B . 
I 3 HOH 78  478 201 HOH HOH B . 
I 3 HOH 79  479 121 HOH HOH B . 
I 3 HOH 80  480 175 HOH HOH B . 
I 3 HOH 81  481 27  HOH HOH B . 
I 3 HOH 82  482 22  HOH HOH B . 
I 3 HOH 83  483 202 HOH HOH B . 
I 3 HOH 84  484 25  HOH HOH B . 
I 3 HOH 85  485 197 HOH HOH B . 
I 3 HOH 86  486 50  HOH HOH B . 
I 3 HOH 87  487 17  HOH HOH B . 
I 3 HOH 88  488 157 HOH HOH B . 
I 3 HOH 89  489 82  HOH HOH B . 
I 3 HOH 90  490 95  HOH HOH B . 
I 3 HOH 91  491 100 HOH HOH B . 
I 3 HOH 92  492 83  HOH HOH B . 
I 3 HOH 93  493 172 HOH HOH B . 
I 3 HOH 94  494 75  HOH HOH B . 
I 3 HOH 95  495 89  HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? REFMAC  ? ? ? 5.8.0425 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .        2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .        3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .        4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   96.19 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9FD7 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     48.173 
_cell.length_a_esd                 ? 
_cell.length_b                     72.752 
_cell.length_b_esd                 ? 
_cell.length_c                     70.919 
_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                         9FD7 
_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                   9FD7 
_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             2.15 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          42.82 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;Protein was concentrated to 8 mg/mL in 20 mM potassium phosphate, pH 7. Crystallization conditions: 0-4% 2-propanol, 22-24% PEG 3350 in 0.1 M HEPES, pH 7.5.
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS PILATUS3 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-14 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.9655 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE MASSIF-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.9655 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   MASSIF-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9FD7 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.40 
_reflns.d_resolution_low                               72.75 
_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                                     91423 
_reflns.observed_criterion                             ? 
_reflns.observed_criterion_F_max                       ? 
_reflns.observed_criterion_F_min                       ? 
_reflns.observed_criterion_I_max                       ? 
_reflns.observed_criterion_I_min                       ? 
_reflns.observed_criterion_sigma_F                     ? 
_reflns.observed_criterion_sigma_I                     ? 
_reflns.percent_possible_obs                           95.7 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.6 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          16.9 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.97 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.064 
_reflns.pdbx_Rpim_I_all                                0.025 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       604885 
_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                              0.059 
_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                                    1.40 
_reflns_shell.d_res_low                                     1.42 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           ? 
_reflns_shell.number_measured_all                           20006 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             3626 
_reflns_shell.percent_possible_obs                          76.5 
_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                               5.5 
_reflns_shell.pdbx_chi_squared                              0.98 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     2.2 
_reflns_shell.pdbx_Rrim_I_all                               0.875 
_reflns_shell.pdbx_Rpim_I_all                               0.354 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.746 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.796 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            0.73 
_refine.aniso_B[1][2]                            0.00 
_refine.aniso_B[1][3]                            -1.22 
_refine.aniso_B[2][2]                            -1.35 
_refine.aniso_B[2][3]                            -0.00 
_refine.aniso_B[3][3]                            0.86 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               17.482 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               0.974 
_refine.correlation_coeff_Fo_to_Fc_free          0.969 
_refine.details                                  'HYDROGENS HAVE BEEN USED IF PRESENT IN THE INPUT' 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9FD7 
_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                            1.40 
_refine.ls_d_res_low                             50.68 
_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                     86934 
_refine.ls_number_reflns_R_free                  4462 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    95.48 
_refine.ls_percent_reflns_R_free                 4.9 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.13502 
_refine.ls_R_factor_R_free                       0.15708 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.13386 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    MASK 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          ? 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       'MAXIMUM LIKELIHOOD' 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       0.054 
_refine.pdbx_overall_ESU_R_Free                  0.048 
_refine.pdbx_solvent_vdw_probe_radii             1.20 
_refine.pdbx_solvent_ion_probe_radii             0.80 
_refine.pdbx_solvent_shrinkage_radii             0.80 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 ? 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             1.967 
_refine.overall_SU_ML                            0.034 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         1 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.40 
_refine_hist.d_res_low                        50.68 
_refine_hist.number_atoms_solvent             207 
_refine_hist.number_atoms_total               3888 
_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        3651 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         30 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.009  0.012  3780 ? r_bond_refined_d             ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.016  3754 ? r_bond_other_d               ? ? 
'X-RAY DIFFRACTION' ? 1.678  1.786  5112 ? r_angle_refined_deg          ? ? 
'X-RAY DIFFRACTION' ? 0.591  1.727  8652 ? r_angle_other_deg            ? ? 
'X-RAY DIFFRACTION' ? 6.290  5.000  500  ? r_dihedral_angle_1_deg       ? ? 
'X-RAY DIFFRACTION' ? 8.659  5.000  24   ? r_dihedral_angle_2_deg       ? ? 
'X-RAY DIFFRACTION' ? 11.334 10.000 670  ? r_dihedral_angle_3_deg       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_dihedral_angle_4_deg       ? ? 
'X-RAY DIFFRACTION' ? 0.097  0.200  612  ? r_chiral_restr               ? ? 
'X-RAY DIFFRACTION' ? 0.008  0.019  4395 ? r_gen_planes_refined         ? ? 
'X-RAY DIFFRACTION' ? 0.001  0.018  785  ? r_gen_planes_other           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_refined                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbd_other                  ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_refined              ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_nbtor_other                ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_refined        ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_xyhbond_nbd_other          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_refined          ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_metal_ion_other            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_refined       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_vdw_other         ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_refined     ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_hbond_other       ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_refined ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_symmetry_metal_ion_other   ? ? 
'X-RAY DIFFRACTION' ? 3.839  1.495  1971 ? r_mcbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 3.823  1.495  1971 ? r_mcbond_other               ? ? 
'X-RAY DIFFRACTION' ? 5.400  2.686  2465 ? r_mcangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 5.403  2.687  2466 ? r_mcangle_other              ? ? 
'X-RAY DIFFRACTION' ? 6.642  1.843  1809 ? r_scbond_it                  ? ? 
'X-RAY DIFFRACTION' ? 6.641  1.844  1810 ? r_scbond_other               ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_scangle_it                 ? ? 
'X-RAY DIFFRACTION' ? 9.499  3.218  2642 ? r_scangle_other              ? ? 
'X-RAY DIFFRACTION' ? 11.897 15.84  4253 ? r_long_range_B_refined       ? ? 
'X-RAY DIFFRACTION' ? 11.899 15.84  4254 ? r_long_range_B_other         ? ? 
'X-RAY DIFFRACTION' ? 4.118  3.000  7534 ? r_rigid_bond_restr           ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_free            ? ? 
'X-RAY DIFFRACTION' ? ?      ?      ?    ? r_sphericity_bonded          ? ? 
# 
_refine_ls_shell.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_ls_shell.d_res_high                       1.400 
_refine_ls_shell.d_res_low                        1.436 
_refine_ls_shell.number_reflns_all                ? 
_refine_ls_shell.number_reflns_obs                ? 
_refine_ls_shell.number_reflns_R_free             284 
_refine_ls_shell.number_reflns_R_work             5345 
_refine_ls_shell.percent_reflns_obs               79.89 
_refine_ls_shell.percent_reflns_R_free            ? 
_refine_ls_shell.R_factor_all                     ? 
_refine_ls_shell.R_factor_obs                     ? 
_refine_ls_shell.R_factor_R_free_error            ? 
_refine_ls_shell.R_factor_R_work                  0.239 
_refine_ls_shell.redundancy_reflns_all            ? 
_refine_ls_shell.redundancy_reflns_obs            ? 
_refine_ls_shell.wR_factor_all                    ? 
_refine_ls_shell.wR_factor_obs                    ? 
_refine_ls_shell.wR_factor_R_free                 ? 
_refine_ls_shell.wR_factor_R_work                 ? 
_refine_ls_shell.pdbx_R_complete                  ? 
_refine_ls_shell.pdbx_total_number_of_bins_used   20 
_refine_ls_shell.pdbx_phase_error                 ? 
_refine_ls_shell.pdbx_fsc_work                    ? 
_refine_ls_shell.pdbx_fsc_free                    ? 
_refine_ls_shell.R_factor_R_free                  0.274 
# 
_struct.entry_id                     9FD7 
_struct.title                        
'Re-engineered peroxygenase variant of 2-deoxy-D-ribose-5-phosphate aldolase in substrate-free 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        9FD7 
_struct_keywords.text            'protein engineering, directed evolution, aldolase, peroxygenase, Schiff base, LYASE' 
_struct_keywords.pdbx_keywords   LYASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 2 ? 
E N N 2 ? 
F N N 2 ? 
G N N 2 ? 
H N N 3 ? 
I N N 3 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    DEOC_ECOLC 
_struct_ref.pdbx_db_accession          B1IS38 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;MTDLKASSLRALKLMDLTTLNDDDTDEKVIALCHQAKTPVGNTAAICIYPRFIPIARKTLKEQGTPEIRIATVTNFPHGN
DDIEIALAETRAAIAYGADEVDVVFPYRALMAGNEQVGFDLVKACKEACAAANVLLKVIIETGELKDEALIRKASEISIK
AGADFIKTSTGKVAVNATPESARIMMEVIRDMGVEKTVGFKPAGGVRTAEDAQKYLAIADELFGADWADARHYRFGASSL
LASLLKALGHGDGKSASSY
;
_struct_ref.pdbx_align_begin           1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 9FD7 A 1 ? 259 ? B1IS38 1 ? 259 ? 1 259 
2 1 9FD7 B 1 ? 259 ? B1IS38 1 ? 259 ? 1 259 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 9FD7 SER A 18  ? UNP B1IS38 THR 18  'engineered mutation' 18  1  
1 9FD7 GLY A 22  ? UNP B1IS38 ASP 22  'engineered mutation' 22  2  
1 9FD7 TYR A 24  ? UNP B1IS38 ASP 24  'engineered mutation' 24  3  
1 9FD7 SER A 47  ? UNP B1IS38 CYS 47  'engineered mutation' 47  4  
1 9FD7 VAL A 48  ? UNP B1IS38 ILE 48  'engineered mutation' 48  5  
1 9FD7 SER A 52  ? UNP B1IS38 PHE 52  'engineered mutation' 52  6  
1 9FD7 ARG A 172 ? UNP B1IS38 LYS 172 'engineered mutation' 172 7  
1 9FD7 SER A 197 ? UNP B1IS38 THR 197 'engineered mutation' 197 8  
1 9FD7 VAL A 202 ? UNP B1IS38 PRO 202 'engineered mutation' 202 9  
1 9FD7 THR A 203 ? UNP B1IS38 ALA 203 'engineered mutation' 203 10 
1 9FD7 SER A 207 ? UNP B1IS38 ARG 207 'engineered mutation' 207 11 
1 9FD7 SER A 236 ? UNP B1IS38 GLY 236 'engineered mutation' 236 12 
1 9FD7 GLY A 239 ? UNP B1IS38 SER 239 'engineered mutation' 239 13 
1 9FD7 LEU A 260 ? UNP B1IS38 ?   ?   'expression tag'      260 14 
1 9FD7 GLU A 261 ? UNP B1IS38 ?   ?   'expression tag'      261 15 
1 9FD7 HIS A 262 ? UNP B1IS38 ?   ?   'expression tag'      262 16 
1 9FD7 HIS A 263 ? UNP B1IS38 ?   ?   'expression tag'      263 17 
1 9FD7 HIS A 264 ? UNP B1IS38 ?   ?   'expression tag'      264 18 
1 9FD7 HIS A 265 ? UNP B1IS38 ?   ?   'expression tag'      265 19 
1 9FD7 HIS A 266 ? UNP B1IS38 ?   ?   'expression tag'      266 20 
1 9FD7 HIS A 267 ? UNP B1IS38 ?   ?   'expression tag'      267 21 
2 9FD7 SER B 18  ? UNP B1IS38 THR 18  'engineered mutation' 18  22 
2 9FD7 GLY B 22  ? UNP B1IS38 ASP 22  'engineered mutation' 22  23 
2 9FD7 TYR B 24  ? UNP B1IS38 ASP 24  'engineered mutation' 24  24 
2 9FD7 SER B 47  ? UNP B1IS38 CYS 47  'engineered mutation' 47  25 
2 9FD7 VAL B 48  ? UNP B1IS38 ILE 48  'engineered mutation' 48  26 
2 9FD7 SER B 52  ? UNP B1IS38 PHE 52  'engineered mutation' 52  27 
2 9FD7 ARG B 172 ? UNP B1IS38 LYS 172 'engineered mutation' 172 28 
2 9FD7 SER B 197 ? UNP B1IS38 THR 197 'engineered mutation' 197 29 
2 9FD7 VAL B 202 ? UNP B1IS38 PRO 202 'engineered mutation' 202 30 
2 9FD7 THR B 203 ? UNP B1IS38 ALA 203 'engineered mutation' 203 31 
2 9FD7 SER B 207 ? UNP B1IS38 ARG 207 'engineered mutation' 207 32 
2 9FD7 SER B 236 ? UNP B1IS38 GLY 236 'engineered mutation' 236 33 
2 9FD7 GLY B 239 ? UNP B1IS38 SER 239 'engineered mutation' 239 34 
2 9FD7 LEU B 260 ? UNP B1IS38 ?   ?   'expression tag'      260 35 
2 9FD7 GLU B 261 ? UNP B1IS38 ?   ?   'expression tag'      261 36 
2 9FD7 HIS B 262 ? UNP B1IS38 ?   ?   'expression tag'      262 37 
2 9FD7 HIS B 263 ? UNP B1IS38 ?   ?   'expression tag'      263 38 
2 9FD7 HIS B 264 ? UNP B1IS38 ?   ?   'expression tag'      264 39 
2 9FD7 HIS B 265 ? UNP B1IS38 ?   ?   'expression tag'      265 40 
2 9FD7 HIS B 266 ? UNP B1IS38 ?   ?   'expression tag'      266 41 
2 9FD7 HIS B 267 ? UNP B1IS38 ?   ?   'expression tag'      267 42 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_defined_assembly ? monomeric 1 
2 author_defined_assembly ? monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,H       
2 1 B,D,E,F,G,I 
# 
loop_
_pdbx_struct_assembly_auth_evidence.id 
_pdbx_struct_assembly_auth_evidence.assembly_id 
_pdbx_struct_assembly_auth_evidence.experimental_support 
_pdbx_struct_assembly_auth_evidence.details 
1 1 'gel filtration' ? 
2 2 'gel filtration' ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 LEU A 4   ? LYS A 13  ? LEU A 4   LYS A 13  1 ? 10 
HELX_P HELX_P2  AA2 ASP A 26  ? ALA A 36  ? ASP A 26  ALA A 36  1 ? 11 
HELX_P HELX_P3  AA3 TYR A 49  ? ARG A 51  ? TYR A 49  ARG A 51  5 ? 3  
HELX_P HELX_P4  AA4 SER A 52  ? GLN A 63  ? SER A 52  GLN A 63  1 ? 12 
HELX_P HELX_P5  AA5 ASP A 82  ? GLY A 97  ? ASP A 82  GLY A 97  1 ? 16 
HELX_P HELX_P6  AA6 PRO A 106 ? ALA A 112 ? PRO A 106 ALA A 112 1 ? 7  
HELX_P HELX_P7  AA7 ASN A 114 ? ALA A 132 ? ASN A 114 ALA A 132 1 ? 19 
HELX_P HELX_P8  AA8 GLU A 141 ? LYS A 146 ? GLU A 141 LYS A 146 1 ? 6  
HELX_P HELX_P9  AA9 ASP A 147 ? ALA A 161 ? ASP A 147 ALA A 161 1 ? 15 
HELX_P HELX_P10 AB1 THR A 178 ? GLY A 193 ? THR A 178 GLY A 193 1 ? 16 
HELX_P HELX_P11 AB2 THR A 208 ? GLY A 224 ? THR A 208 GLY A 224 1 ? 17 
HELX_P HELX_P12 AB3 GLY A 239 ? LEU A 248 ? GLY A 239 LEU A 248 1 ? 10 
HELX_P HELX_P13 AB4 LEU B 4   ? LYS B 13  ? LEU B 4   LYS B 13  1 ? 10 
HELX_P HELX_P14 AB5 THR B 25  ? ALA B 36  ? THR B 25  ALA B 36  1 ? 12 
HELX_P HELX_P15 AB6 TYR B 49  ? ARG B 51  ? TYR B 49  ARG B 51  5 ? 3  
HELX_P HELX_P16 AB7 SER B 52  ? GLN B 63  ? SER B 52  GLN B 63  1 ? 12 
HELX_P HELX_P17 AB8 ASP B 82  ? GLY B 97  ? ASP B 82  GLY B 97  1 ? 16 
HELX_P HELX_P18 AB9 PRO B 106 ? ALA B 112 ? PRO B 106 ALA B 112 1 ? 7  
HELX_P HELX_P19 AC1 ASN B 114 ? ALA B 132 ? ASN B 114 ALA B 132 1 ? 19 
HELX_P HELX_P20 AC2 GLU B 141 ? LYS B 146 ? GLU B 141 LYS B 146 1 ? 6  
HELX_P HELX_P21 AC3 ASP B 147 ? ALA B 161 ? ASP B 147 ALA B 161 1 ? 15 
HELX_P HELX_P22 AC4 THR B 178 ? GLY B 193 ? THR B 178 GLY B 193 1 ? 16 
HELX_P HELX_P23 AC5 THR B 208 ? GLY B 224 ? THR B 208 GLY B 224 1 ? 17 
HELX_P HELX_P24 AC6 GLY B 239 ? LEU B 248 ? GLY B 239 LEU B 248 1 ? 10 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 76 A . ? PHE 76 A PRO 77 A ? PRO 77 A 1 -2.09 
2 PHE 76 B . ? PHE 76 B PRO 77 B ? PRO 77 B 1 -3.94 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 8 ? 
AA2 ? 2 ? 
AA3 ? 8 ? 
AA4 ? 2 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? parallel      
AA1 2 3 ? parallel      
AA1 3 4 ? parallel      
AA1 4 5 ? parallel      
AA1 5 6 ? parallel      
AA1 6 7 ? parallel      
AA1 7 8 ? parallel      
AA2 1 2 ? anti-parallel 
AA3 1 2 ? parallel      
AA3 2 3 ? parallel      
AA3 3 4 ? parallel      
AA3 4 5 ? parallel      
AA3 5 6 ? parallel      
AA3 6 7 ? parallel      
AA3 7 8 ? parallel      
AA4 1 2 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ASP A 16  ? LEU A 17  ? ASP A 16  LEU A 17  
AA1 2 ALA A 45  ? SER A 47  ? ALA A 45  SER A 47  
AA1 3 ARG A 69  ? THR A 74  ? ARG A 69  THR A 74  
AA1 4 GLU A 100 ? VAL A 104 ? GLU A 100 VAL A 104 
AA1 5 LEU A 135 ? ILE A 139 ? LEU A 135 ILE A 139 
AA1 6 PHE A 165 ? LYS A 167 ? PHE A 165 LYS A 167 
AA1 7 GLY A 199 ? THR A 203 ? GLY A 199 THR A 203 
AA1 8 TYR A 233 ? SER A 236 ? TYR A 233 SER A 236 
AA2 1 LYS A 37  ? THR A 38  ? LYS A 37  THR A 38  
AA2 2 GLY A 41  ? ASN A 42  ? GLY A 41  ASN A 42  
AA3 1 ASP B 16  ? LEU B 17  ? ASP B 16  LEU B 17  
AA3 2 ALA B 45  ? SER B 47  ? ALA B 45  SER B 47  
AA3 3 ARG B 69  ? THR B 74  ? ARG B 69  THR B 74  
AA3 4 GLU B 100 ? VAL B 104 ? GLU B 100 VAL B 104 
AA3 5 LEU B 135 ? ILE B 139 ? LEU B 135 ILE B 139 
AA3 6 PHE B 165 ? LYS B 167 ? PHE B 165 LYS B 167 
AA3 7 GLY B 199 ? THR B 203 ? GLY B 199 THR B 203 
AA3 8 TYR B 233 ? SER B 236 ? TYR B 233 SER B 236 
AA4 1 LYS B 37  ? THR B 38  ? LYS B 37  THR B 38  
AA4 2 GLY B 41  ? ASN B 42  ? GLY B 41  ASN B 42  
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N LEU A 17  ? N LEU A 17  O ALA A 45  ? O ALA A 45  
AA1 2 3 N ILE A 46  ? N ILE A 46  O ALA A 71  ? O ALA A 71  
AA1 3 4 N THR A 72  ? N THR A 72  O ASP A 102 ? O ASP A 102 
AA1 4 5 N VAL A 103 ? N VAL A 103 O ILE A 139 ? O ILE A 139 
AA1 5 6 N VAL A 138 ? N VAL A 138 O LYS A 167 ? O LYS A 167 
AA1 6 7 N ILE A 166 ? N ILE A 166 O GLY A 199 ? O GLY A 199 
AA1 7 8 N VAL A 202 ? N VAL A 202 O ARG A 234 ? O ARG A 234 
AA2 1 2 N THR A 38  ? N THR A 38  O GLY A 41  ? O GLY A 41  
AA3 1 2 N LEU B 17  ? N LEU B 17  O ALA B 45  ? O ALA B 45  
AA3 2 3 N ILE B 46  ? N ILE B 46  O ALA B 71  ? O ALA B 71  
AA3 3 4 N THR B 72  ? N THR B 72  O ASP B 102 ? O ASP B 102 
AA3 4 5 N VAL B 103 ? N VAL B 103 O ILE B 139 ? O ILE B 139 
AA3 5 6 N VAL B 138 ? N VAL B 138 O LYS B 167 ? O LYS B 167 
AA3 6 7 N ILE B 166 ? N ILE B 166 O GLY B 199 ? O GLY B 199 
AA3 7 8 N VAL B 202 ? N VAL B 202 O ARG B 234 ? O ARG B 234 
AA4 1 2 N THR B 38  ? N THR B 38  O GLY B 41  ? O GLY B 41  
# 
_pdbx_entry_details.entry_id                   9FD7 
_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     N 
_pdbx_entry_details.has_protein_modification   N 
# 
_pdbx_validate_rmsd_angle.id                         1 
_pdbx_validate_rmsd_angle.PDB_model_num              1 
_pdbx_validate_rmsd_angle.auth_atom_id_1             CG 
_pdbx_validate_rmsd_angle.auth_asym_id_1             B 
_pdbx_validate_rmsd_angle.auth_comp_id_1             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_1              111 
_pdbx_validate_rmsd_angle.PDB_ins_code_1             ? 
_pdbx_validate_rmsd_angle.label_alt_id_1             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_2             SD 
_pdbx_validate_rmsd_angle.auth_asym_id_2             B 
_pdbx_validate_rmsd_angle.auth_comp_id_2             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_2              111 
_pdbx_validate_rmsd_angle.PDB_ins_code_2             ? 
_pdbx_validate_rmsd_angle.label_alt_id_2             ? 
_pdbx_validate_rmsd_angle.auth_atom_id_3             CE 
_pdbx_validate_rmsd_angle.auth_asym_id_3             B 
_pdbx_validate_rmsd_angle.auth_comp_id_3             MET 
_pdbx_validate_rmsd_angle.auth_seq_id_3              111 
_pdbx_validate_rmsd_angle.PDB_ins_code_3             ? 
_pdbx_validate_rmsd_angle.label_alt_id_3             ? 
_pdbx_validate_rmsd_angle.angle_value                88.60 
_pdbx_validate_rmsd_angle.angle_target_value         100.20 
_pdbx_validate_rmsd_angle.angle_deviation            -11.60 
_pdbx_validate_rmsd_angle.angle_standard_deviation   1.60 
_pdbx_validate_rmsd_angle.linker_flag                N 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 GLU A 141 ? ? 65.68   63.30   
2 1 LYS A 146 ? ? 72.14   -54.25  
3 1 ASN A 176 ? ? -109.28 -140.06 
4 1 GLU B 141 ? ? 67.12   62.36   
5 1 LYS B 146 ? ? 72.15   -54.14  
6 1 ASN B 176 ? ? -113.18 -144.13 
# 
loop_
_pdbx_validate_planes.id 
_pdbx_validate_planes.PDB_model_num 
_pdbx_validate_planes.auth_comp_id 
_pdbx_validate_planes.auth_asym_id 
_pdbx_validate_planes.auth_seq_id 
_pdbx_validate_planes.PDB_ins_code 
_pdbx_validate_planes.label_alt_id 
_pdbx_validate_planes.rmsd 
_pdbx_validate_planes.type 
1 1 ARG A 234 ? ? 0.078 'SIDE CHAIN' 
2 1 ARG B 172 ? ? 0.111 'SIDE CHAIN' 
3 1 ARG B 234 ? ? 0.079 'SIDE CHAIN' 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A MET 1   ? A MET 1   
2  1 Y 1 A THR 2   ? A THR 2   
3  1 Y 1 A ASP 3   ? A ASP 3   
4  1 Y 1 A THR 19  ? A THR 19  
5  1 Y 1 A LEU 20  ? A LEU 20  
6  1 Y 1 A ASN 21  ? A ASN 21  
7  1 Y 1 A GLY 22  ? A GLY 22  
8  1 Y 1 A ASP 23  ? A ASP 23  
9  1 Y 1 A TYR 24  ? A TYR 24  
10 1 Y 1 A GLY 251 ? A GLY 251 
11 1 Y 1 A ASP 252 ? A ASP 252 
12 1 Y 1 A GLY 253 ? A GLY 253 
13 1 Y 1 A LYS 254 ? A LYS 254 
14 1 Y 1 A SER 255 ? A SER 255 
15 1 Y 1 A ALA 256 ? A ALA 256 
16 1 Y 1 A SER 257 ? A SER 257 
17 1 Y 1 A SER 258 ? A SER 258 
18 1 Y 1 A TYR 259 ? A TYR 259 
19 1 Y 1 A LEU 260 ? A LEU 260 
20 1 Y 1 A GLU 261 ? A GLU 261 
21 1 Y 1 A HIS 262 ? A HIS 262 
22 1 Y 1 A HIS 263 ? A HIS 263 
23 1 Y 1 A HIS 264 ? A HIS 264 
24 1 Y 1 A HIS 265 ? A HIS 265 
25 1 Y 1 A HIS 266 ? A HIS 266 
26 1 Y 1 A HIS 267 ? A HIS 267 
27 1 Y 1 B MET 1   ? B MET 1   
28 1 Y 1 B THR 2   ? B THR 2   
29 1 Y 1 B LEU 20  ? B LEU 20  
30 1 Y 1 B ASN 21  ? B ASN 21  
31 1 Y 1 B GLY 251 ? B GLY 251 
32 1 Y 1 B ASP 252 ? B ASP 252 
33 1 Y 1 B GLY 253 ? B GLY 253 
34 1 Y 1 B LYS 254 ? B LYS 254 
35 1 Y 1 B SER 255 ? B SER 255 
36 1 Y 1 B ALA 256 ? B ALA 256 
37 1 Y 1 B SER 257 ? B SER 257 
38 1 Y 1 B SER 258 ? B SER 258 
39 1 Y 1 B TYR 259 ? B TYR 259 
40 1 Y 1 B LEU 260 ? B LEU 260 
41 1 Y 1 B GLU 261 ? B GLU 261 
42 1 Y 1 B HIS 262 ? B HIS 262 
43 1 Y 1 B HIS 263 ? B HIS 263 
44 1 Y 1 B HIS 264 ? B HIS 264 
45 1 Y 1 B HIS 265 ? B HIS 265 
46 1 Y 1 B HIS 266 ? B HIS 266 
47 1 Y 1 B HIS 267 ? B HIS 267 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
GOL C1   C N N 137 
GOL O1   O N N 138 
GOL C2   C N N 139 
GOL O2   O N N 140 
GOL C3   C N N 141 
GOL O3   O N N 142 
GOL H11  H N N 143 
GOL H12  H N N 144 
GOL HO1  H N N 145 
GOL H2   H N N 146 
GOL HO2  H N N 147 
GOL H31  H N N 148 
GOL H32  H N N 149 
GOL HO3  H N N 150 
HIS N    N N N 151 
HIS CA   C N S 152 
HIS C    C N N 153 
HIS O    O N N 154 
HIS CB   C N N 155 
HIS CG   C Y N 156 
HIS ND1  N Y N 157 
HIS CD2  C Y N 158 
HIS CE1  C Y N 159 
HIS NE2  N Y N 160 
HIS OXT  O N N 161 
HIS H    H N N 162 
HIS H2   H N N 163 
HIS HA   H N N 164 
HIS HB2  H N N 165 
HIS HB3  H N N 166 
HIS HD1  H N N 167 
HIS HD2  H N N 168 
HIS HE1  H N N 169 
HIS HE2  H N N 170 
HIS HXT  H N N 171 
HOH O    O N N 172 
HOH H1   H N N 173 
HOH H2   H N N 174 
ILE N    N N N 175 
ILE CA   C N S 176 
ILE C    C N N 177 
ILE O    O N N 178 
ILE CB   C N S 179 
ILE CG1  C N N 180 
ILE CG2  C N N 181 
ILE CD1  C N N 182 
ILE OXT  O N N 183 
ILE H    H N N 184 
ILE H2   H N N 185 
ILE HA   H N N 186 
ILE HB   H N N 187 
ILE HG12 H N N 188 
ILE HG13 H N N 189 
ILE HG21 H N N 190 
ILE HG22 H N N 191 
ILE HG23 H N N 192 
ILE HD11 H N N 193 
ILE HD12 H N N 194 
ILE HD13 H N N 195 
ILE HXT  H N N 196 
LEU N    N N N 197 
LEU CA   C N S 198 
LEU C    C N N 199 
LEU O    O N N 200 
LEU CB   C N N 201 
LEU CG   C N N 202 
LEU CD1  C N N 203 
LEU CD2  C N N 204 
LEU OXT  O N N 205 
LEU H    H N N 206 
LEU H2   H N N 207 
LEU HA   H N N 208 
LEU HB2  H N N 209 
LEU HB3  H N N 210 
LEU HG   H N N 211 
LEU HD11 H N N 212 
LEU HD12 H N N 213 
LEU HD13 H N N 214 
LEU HD21 H N N 215 
LEU HD22 H N N 216 
LEU HD23 H N N 217 
LEU HXT  H N N 218 
LYS N    N N N 219 
LYS CA   C N S 220 
LYS C    C N N 221 
LYS O    O N N 222 
LYS CB   C N N 223 
LYS CG   C N N 224 
LYS CD   C N N 225 
LYS CE   C N N 226 
LYS NZ   N N N 227 
LYS OXT  O N N 228 
LYS H    H N N 229 
LYS H2   H N N 230 
LYS HA   H N N 231 
LYS HB2  H N N 232 
LYS HB3  H N N 233 
LYS HG2  H N N 234 
LYS HG3  H N N 235 
LYS HD2  H N N 236 
LYS HD3  H N N 237 
LYS HE2  H N N 238 
LYS HE3  H N N 239 
LYS HZ1  H N N 240 
LYS HZ2  H N N 241 
LYS HZ3  H N N 242 
LYS HXT  H N N 243 
MET N    N N N 244 
MET CA   C N S 245 
MET C    C N N 246 
MET O    O N N 247 
MET CB   C N N 248 
MET CG   C N N 249 
MET SD   S N N 250 
MET CE   C N N 251 
MET OXT  O N N 252 
MET H    H N N 253 
MET H2   H N N 254 
MET HA   H N N 255 
MET HB2  H N N 256 
MET HB3  H N N 257 
MET HG2  H N N 258 
MET HG3  H N N 259 
MET HE1  H N N 260 
MET HE2  H N N 261 
MET HE3  H N N 262 
MET HXT  H N N 263 
PHE N    N N N 264 
PHE CA   C N S 265 
PHE C    C N N 266 
PHE O    O N N 267 
PHE CB   C N N 268 
PHE CG   C Y N 269 
PHE CD1  C Y N 270 
PHE CD2  C Y N 271 
PHE CE1  C Y N 272 
PHE CE2  C Y N 273 
PHE CZ   C Y N 274 
PHE OXT  O N N 275 
PHE H    H N N 276 
PHE H2   H N N 277 
PHE HA   H N N 278 
PHE HB2  H N N 279 
PHE HB3  H N N 280 
PHE HD1  H N N 281 
PHE HD2  H N N 282 
PHE HE1  H N N 283 
PHE HE2  H N N 284 
PHE HZ   H N N 285 
PHE HXT  H N N 286 
PRO N    N N N 287 
PRO CA   C N S 288 
PRO C    C N N 289 
PRO O    O N N 290 
PRO CB   C N N 291 
PRO CG   C N N 292 
PRO CD   C N N 293 
PRO OXT  O N N 294 
PRO H    H N N 295 
PRO HA   H N N 296 
PRO HB2  H N N 297 
PRO HB3  H N N 298 
PRO HG2  H N N 299 
PRO HG3  H N N 300 
PRO HD2  H N N 301 
PRO HD3  H N N 302 
PRO HXT  H N N 303 
SER N    N N N 304 
SER CA   C N S 305 
SER C    C N N 306 
SER O    O N N 307 
SER CB   C N N 308 
SER OG   O N N 309 
SER OXT  O N N 310 
SER H    H N N 311 
SER H2   H N N 312 
SER HA   H N N 313 
SER HB2  H N N 314 
SER HB3  H N N 315 
SER HG   H N N 316 
SER HXT  H N N 317 
THR N    N N N 318 
THR CA   C N S 319 
THR C    C N N 320 
THR O    O N N 321 
THR CB   C N R 322 
THR OG1  O N N 323 
THR CG2  C N N 324 
THR OXT  O N N 325 
THR H    H N N 326 
THR H2   H N N 327 
THR HA   H N N 328 
THR HB   H N N 329 
THR HG1  H N N 330 
THR HG21 H N N 331 
THR HG22 H N N 332 
THR HG23 H N N 333 
THR HXT  H N N 334 
TRP N    N N N 335 
TRP CA   C N S 336 
TRP C    C N N 337 
TRP O    O N N 338 
TRP CB   C N N 339 
TRP CG   C Y N 340 
TRP CD1  C Y N 341 
TRP CD2  C Y N 342 
TRP NE1  N Y N 343 
TRP CE2  C Y N 344 
TRP CE3  C Y N 345 
TRP CZ2  C Y N 346 
TRP CZ3  C Y N 347 
TRP CH2  C Y N 348 
TRP OXT  O N N 349 
TRP H    H N N 350 
TRP H2   H N N 351 
TRP HA   H N N 352 
TRP HB2  H N N 353 
TRP HB3  H N N 354 
TRP HD1  H N N 355 
TRP HE1  H N N 356 
TRP HE3  H N N 357 
TRP HZ2  H N N 358 
TRP HZ3  H N N 359 
TRP HH2  H N N 360 
TRP HXT  H N N 361 
TYR N    N N N 362 
TYR CA   C N S 363 
TYR C    C N N 364 
TYR O    O N N 365 
TYR CB   C N N 366 
TYR CG   C Y N 367 
TYR CD1  C Y N 368 
TYR CD2  C Y N 369 
TYR CE1  C Y N 370 
TYR CE2  C Y N 371 
TYR CZ   C Y N 372 
TYR OH   O N N 373 
TYR OXT  O N N 374 
TYR H    H N N 375 
TYR H2   H N N 376 
TYR HA   H N N 377 
TYR HB2  H N N 378 
TYR HB3  H N N 379 
TYR HD1  H N N 380 
TYR HD2  H N N 381 
TYR HE1  H N N 382 
TYR HE2  H N N 383 
TYR HH   H N N 384 
TYR HXT  H N N 385 
VAL N    N N N 386 
VAL CA   C N S 387 
VAL C    C N N 388 
VAL O    O N N 389 
VAL CB   C N N 390 
VAL CG1  C N N 391 
VAL CG2  C N N 392 
VAL OXT  O N N 393 
VAL H    H N N 394 
VAL H2   H N N 395 
VAL HA   H N N 396 
VAL HB   H N N 397 
VAL HG11 H N N 398 
VAL HG12 H N N 399 
VAL HG13 H N N 400 
VAL HG21 H N N 401 
VAL HG22 H N N 402 
VAL HG23 H N N 403 
VAL HXT  H N N 404 
# 
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 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
GOL C1  O1   sing N N 129 
GOL C1  C2   sing N N 130 
GOL C1  H11  sing N N 131 
GOL C1  H12  sing N N 132 
GOL O1  HO1  sing N N 133 
GOL C2  O2   sing N N 134 
GOL C2  C3   sing N N 135 
GOL C2  H2   sing N N 136 
GOL O2  HO2  sing N N 137 
GOL C3  O3   sing N N 138 
GOL C3  H31  sing N N 139 
GOL C3  H32  sing N N 140 
GOL O3  HO3  sing N N 141 
HIS N   CA   sing N N 142 
HIS N   H    sing N N 143 
HIS N   H2   sing N N 144 
HIS CA  C    sing N N 145 
HIS CA  CB   sing N N 146 
HIS CA  HA   sing N N 147 
HIS C   O    doub N N 148 
HIS C   OXT  sing N N 149 
HIS CB  CG   sing N N 150 
HIS CB  HB2  sing N N 151 
HIS CB  HB3  sing N N 152 
HIS CG  ND1  sing Y N 153 
HIS CG  CD2  doub Y N 154 
HIS ND1 CE1  doub Y N 155 
HIS ND1 HD1  sing N N 156 
HIS CD2 NE2  sing Y N 157 
HIS CD2 HD2  sing N N 158 
HIS CE1 NE2  sing Y N 159 
HIS CE1 HE1  sing N N 160 
HIS NE2 HE2  sing N N 161 
HIS OXT HXT  sing N N 162 
HOH O   H1   sing N N 163 
HOH O   H2   sing N N 164 
ILE N   CA   sing N N 165 
ILE N   H    sing N N 166 
ILE N   H2   sing N N 167 
ILE CA  C    sing N N 168 
ILE CA  CB   sing N N 169 
ILE CA  HA   sing N N 170 
ILE C   O    doub N N 171 
ILE C   OXT  sing N N 172 
ILE CB  CG1  sing N N 173 
ILE CB  CG2  sing N N 174 
ILE CB  HB   sing N N 175 
ILE CG1 CD1  sing N N 176 
ILE CG1 HG12 sing N N 177 
ILE CG1 HG13 sing N N 178 
ILE CG2 HG21 sing N N 179 
ILE CG2 HG22 sing N N 180 
ILE CG2 HG23 sing N N 181 
ILE CD1 HD11 sing N N 182 
ILE CD1 HD12 sing N N 183 
ILE CD1 HD13 sing N N 184 
ILE OXT HXT  sing N N 185 
LEU N   CA   sing N N 186 
LEU N   H    sing N N 187 
LEU N   H2   sing N N 188 
LEU CA  C    sing N N 189 
LEU CA  CB   sing N N 190 
LEU CA  HA   sing N N 191 
LEU C   O    doub N N 192 
LEU C   OXT  sing N N 193 
LEU CB  CG   sing N N 194 
LEU CB  HB2  sing N N 195 
LEU CB  HB3  sing N N 196 
LEU CG  CD1  sing N N 197 
LEU CG  CD2  sing N N 198 
LEU CG  HG   sing N N 199 
LEU CD1 HD11 sing N N 200 
LEU CD1 HD12 sing N N 201 
LEU CD1 HD13 sing N N 202 
LEU CD2 HD21 sing N N 203 
LEU CD2 HD22 sing N N 204 
LEU CD2 HD23 sing N N 205 
LEU OXT HXT  sing N N 206 
LYS N   CA   sing N N 207 
LYS N   H    sing N N 208 
LYS N   H2   sing N N 209 
LYS CA  C    sing N N 210 
LYS CA  CB   sing N N 211 
LYS CA  HA   sing N N 212 
LYS C   O    doub N N 213 
LYS C   OXT  sing N N 214 
LYS CB  CG   sing N N 215 
LYS CB  HB2  sing N N 216 
LYS CB  HB3  sing N N 217 
LYS CG  CD   sing N N 218 
LYS CG  HG2  sing N N 219 
LYS CG  HG3  sing N N 220 
LYS CD  CE   sing N N 221 
LYS CD  HD2  sing N N 222 
LYS CD  HD3  sing N N 223 
LYS CE  NZ   sing N N 224 
LYS CE  HE2  sing N N 225 
LYS CE  HE3  sing N N 226 
LYS NZ  HZ1  sing N N 227 
LYS NZ  HZ2  sing N N 228 
LYS NZ  HZ3  sing N N 229 
LYS OXT HXT  sing N N 230 
MET N   CA   sing N N 231 
MET N   H    sing N N 232 
MET N   H2   sing N N 233 
MET CA  C    sing N N 234 
MET CA  CB   sing N N 235 
MET CA  HA   sing N N 236 
MET C   O    doub N N 237 
MET C   OXT  sing N N 238 
MET CB  CG   sing N N 239 
MET CB  HB2  sing N N 240 
MET CB  HB3  sing N N 241 
MET CG  SD   sing N N 242 
MET CG  HG2  sing N N 243 
MET CG  HG3  sing N N 244 
MET SD  CE   sing N N 245 
MET CE  HE1  sing N N 246 
MET CE  HE2  sing N N 247 
MET CE  HE3  sing N N 248 
MET OXT HXT  sing N N 249 
PHE N   CA   sing N N 250 
PHE N   H    sing N N 251 
PHE N   H2   sing N N 252 
PHE CA  C    sing N N 253 
PHE CA  CB   sing N N 254 
PHE CA  HA   sing N N 255 
PHE C   O    doub N N 256 
PHE C   OXT  sing N N 257 
PHE CB  CG   sing N N 258 
PHE CB  HB2  sing N N 259 
PHE CB  HB3  sing N N 260 
PHE CG  CD1  doub Y N 261 
PHE CG  CD2  sing Y N 262 
PHE CD1 CE1  sing Y N 263 
PHE CD1 HD1  sing N N 264 
PHE CD2 CE2  doub Y N 265 
PHE CD2 HD2  sing N N 266 
PHE CE1 CZ   doub Y N 267 
PHE CE1 HE1  sing N N 268 
PHE CE2 CZ   sing Y N 269 
PHE CE2 HE2  sing N N 270 
PHE CZ  HZ   sing N N 271 
PHE OXT HXT  sing N N 272 
PRO N   CA   sing N N 273 
PRO N   CD   sing N N 274 
PRO N   H    sing N N 275 
PRO CA  C    sing N N 276 
PRO CA  CB   sing N N 277 
PRO CA  HA   sing N N 278 
PRO C   O    doub N N 279 
PRO C   OXT  sing N N 280 
PRO CB  CG   sing N N 281 
PRO CB  HB2  sing N N 282 
PRO CB  HB3  sing N N 283 
PRO CG  CD   sing N N 284 
PRO CG  HG2  sing N N 285 
PRO CG  HG3  sing N N 286 
PRO CD  HD2  sing N N 287 
PRO CD  HD3  sing N N 288 
PRO OXT HXT  sing N N 289 
SER N   CA   sing N N 290 
SER N   H    sing N N 291 
SER N   H2   sing N N 292 
SER CA  C    sing N N 293 
SER CA  CB   sing N N 294 
SER CA  HA   sing N N 295 
SER C   O    doub N N 296 
SER C   OXT  sing N N 297 
SER CB  OG   sing N N 298 
SER CB  HB2  sing N N 299 
SER CB  HB3  sing N N 300 
SER OG  HG   sing N N 301 
SER OXT HXT  sing N N 302 
THR N   CA   sing N N 303 
THR N   H    sing N N 304 
THR N   H2   sing N N 305 
THR CA  C    sing N N 306 
THR CA  CB   sing N N 307 
THR CA  HA   sing N N 308 
THR C   O    doub N N 309 
THR C   OXT  sing N N 310 
THR CB  OG1  sing N N 311 
THR CB  CG2  sing N N 312 
THR CB  HB   sing N N 313 
THR OG1 HG1  sing N N 314 
THR CG2 HG21 sing N N 315 
THR CG2 HG22 sing N N 316 
THR CG2 HG23 sing N N 317 
THR OXT HXT  sing N N 318 
TRP N   CA   sing N N 319 
TRP N   H    sing N N 320 
TRP N   H2   sing N N 321 
TRP CA  C    sing N N 322 
TRP CA  CB   sing N N 323 
TRP CA  HA   sing N N 324 
TRP C   O    doub N N 325 
TRP C   OXT  sing N N 326 
TRP CB  CG   sing N N 327 
TRP CB  HB2  sing N N 328 
TRP CB  HB3  sing N N 329 
TRP CG  CD1  doub Y N 330 
TRP CG  CD2  sing Y N 331 
TRP CD1 NE1  sing Y N 332 
TRP CD1 HD1  sing N N 333 
TRP CD2 CE2  doub Y N 334 
TRP CD2 CE3  sing Y N 335 
TRP NE1 CE2  sing Y N 336 
TRP NE1 HE1  sing N N 337 
TRP CE2 CZ2  sing Y N 338 
TRP CE3 CZ3  doub Y N 339 
TRP CE3 HE3  sing N N 340 
TRP CZ2 CH2  doub Y N 341 
TRP CZ2 HZ2  sing N N 342 
TRP CZ3 CH2  sing Y N 343 
TRP CZ3 HZ3  sing N N 344 
TRP CH2 HH2  sing N N 345 
TRP OXT HXT  sing N N 346 
TYR N   CA   sing N N 347 
TYR N   H    sing N N 348 
TYR N   H2   sing N N 349 
TYR CA  C    sing N N 350 
TYR CA  CB   sing N N 351 
TYR CA  HA   sing N N 352 
TYR C   O    doub N N 353 
TYR C   OXT  sing N N 354 
TYR CB  CG   sing N N 355 
TYR CB  HB2  sing N N 356 
TYR CB  HB3  sing N N 357 
TYR CG  CD1  doub Y N 358 
TYR CG  CD2  sing Y N 359 
TYR CD1 CE1  sing Y N 360 
TYR CD1 HD1  sing N N 361 
TYR CD2 CE2  doub Y N 362 
TYR CD2 HD2  sing N N 363 
TYR CE1 CZ   doub Y N 364 
TYR CE1 HE1  sing N N 365 
TYR CE2 CZ   sing Y N 366 
TYR CE2 HE2  sing N N 367 
TYR CZ  OH   sing N N 368 
TYR OH  HH   sing N N 369 
TYR OXT HXT  sing N N 370 
VAL N   CA   sing N N 371 
VAL N   H    sing N N 372 
VAL N   H2   sing N N 373 
VAL CA  C    sing N N 374 
VAL CA  CB   sing N N 375 
VAL CA  HA   sing N N 376 
VAL C   O    doub N N 377 
VAL C   OXT  sing N N 378 
VAL CB  CG1  sing N N 379 
VAL CB  CG2  sing N N 380 
VAL CB  HB   sing N N 381 
VAL CG1 HG11 sing N N 382 
VAL CG1 HG12 sing N N 383 
VAL CG1 HG13 sing N N 384 
VAL CG2 HG21 sing N N 385 
VAL CG2 HG22 sing N N 386 
VAL CG2 HG23 sing N N 387 
VAL OXT HXT  sing N N 388 
# 
_pdbx_audit_support.funding_organization   'Netherlands Organisation for Scientific Research (NWO)' 
_pdbx_audit_support.country                Netherlands 
_pdbx_audit_support.grant_number           724.016.002 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7P75 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9FD7 
_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]   0.020759 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.002251 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.013745 
_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]   0.014183 
_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   . LEU A 1 4   ? -16.661 -21.501 -53.769 1.00 35.11 ? 4   LEU A N   1 
ATOM   2    C CA  . LEU A 1 4   ? -16.006 -20.555 -52.829 1.00 35.27 ? 4   LEU A CA  1 
ATOM   3    C C   . LEU A 1 4   ? -16.770 -20.507 -51.514 1.00 30.22 ? 4   LEU A C   1 
ATOM   4    O O   . LEU A 1 4   ? -16.153 -20.386 -50.455 1.00 29.68 ? 4   LEU A O   1 
ATOM   5    C CB  . LEU A 1 4   ? -15.897 -19.165 -53.445 1.00 37.64 ? 4   LEU A CB  1 
ATOM   6    C CG  . LEU A 1 4   ? -15.129 -18.124 -52.626 1.00 37.45 ? 4   LEU A CG  1 
ATOM   7    C CD1 . LEU A 1 4   ? -13.671 -18.536 -52.398 1.00 39.19 ? 4   LEU A CD1 1 
ATOM   8    C CD2 . LEU A 1 4   ? -15.219 -16.754 -53.317 1.00 40.34 ? 4   LEU A CD2 1 
ATOM   9    N N   . LYS A 1 5   ? -18.110 -20.577 -51.559 1.00 29.81 ? 5   LYS A N   1 
ATOM   10   C CA  . LYS A 1 5   ? -18.867 -20.633 -50.321 1.00 30.92 ? 5   LYS A CA  1 
ATOM   11   C C   . LYS A 1 5   ? -18.504 -21.889 -49.530 1.00 28.85 ? 5   LYS A C   1 
ATOM   12   O O   . LYS A 1 5   ? -18.267 -21.812 -48.328 1.00 27.66 ? 5   LYS A O   1 
ATOM   13   C CB  . LYS A 1 5   ? -20.366 -20.524 -50.607 1.00 33.86 ? 5   LYS A CB  1 
ATOM   14   C CG  . LYS A 1 5   ? -20.837 -19.106 -50.915 1.00 38.78 ? 5   LYS A CG  1 
ATOM   15   C CD  . LYS A 1 5   ? -22.339 -18.925 -50.762 1.00 45.24 ? 5   LYS A CD  1 
ATOM   16   C CE  . LYS A 1 5   ? -22.782 -17.490 -50.799 1.00 50.45 ? 5   LYS A CE  1 
ATOM   17   N NZ  . LYS A 1 5   ? -23.520 -17.173 -52.020 1.00 51.66 ? 5   LYS A NZ  1 
ATOM   18   N N   . ALA A 1 6   ? -18.454 -23.046 -50.193 1.00 27.56 ? 6   ALA A N   1 
ATOM   19   C CA  . ALA A 1 6   ? -18.116 -24.285 -49.502 1.00 26.08 ? 6   ALA A CA  1 
ATOM   20   C C   . ALA A 1 6   ? -16.694 -24.230 -48.938 1.00 24.00 ? 6   ALA A C   1 
ATOM   21   O O   . ALA A 1 6   ? -16.482 -24.667 -47.799 1.00 24.67 ? 6   ALA A O   1 
ATOM   22   C CB  . ALA A 1 6   ? -18.293 -25.463 -50.434 1.00 29.57 ? 6   ALA A CB  1 
ATOM   23   N N   . SER A 1 7   ? -15.720 -23.710 -49.710 1.00 24.68 ? 7   SER A N   1 
ATOM   24   C CA  . SER A 1 7   ? -14.361 -23.636 -49.194 1.00 23.14 ? 7   SER A CA  1 
ATOM   25   C C   . SER A 1 7   ? -14.291 -22.643 -48.033 1.00 21.55 ? 7   SER A C   1 
ATOM   26   O O   . SER A 1 7   ? -13.537 -22.848 -47.096 1.00 20.93 ? 7   SER A O   1 
ATOM   27   C CB  . SER A 1 7   ? -13.321 -23.306 -50.233 1.00 24.96 ? 7   SER A CB  1 
ATOM   28   O OG  . SER A 1 7   ? -13.657 -22.100 -50.894 1.00 29.74 ? 7   SER A OG  1 
ATOM   29   N N   . SER A 1 8   ? -15.111 -21.580 -48.068 1.00 20.08 ? 8   SER A N   1 
ATOM   30   C CA  . SER A 1 8   ? -15.028 -20.548 -47.046 1.00 19.55 ? 8   SER A CA  1 
ATOM   31   C C   . SER A 1 8   ? -15.584 -21.050 -45.721 1.00 17.60 ? 8   SER A C   1 
ATOM   32   O O   . SER A 1 8   ? -15.031 -20.769 -44.660 1.00 18.19 ? 8   SER A O   1 
ATOM   33   C CB  . SER A 1 8   ? -15.737 -19.302 -47.472 1.00 21.51 ? 8   SER A CB  1 
ATOM   34   O OG  . SER A 1 8   ? -15.123 -18.739 -48.616 1.00 22.75 ? 8   SER A OG  1 
ATOM   35   N N   . LEU A 1 9   ? -16.684 -21.798 -45.784 1.00 18.86 ? 9   LEU A N   1 
ATOM   36   C CA  . LEU A 1 9   ? -17.226 -22.395 -44.581 1.00 19.19 ? 9   LEU A CA  1 
ATOM   37   C C   . LEU A 1 9   ? -16.239 -23.395 -43.983 1.00 17.58 ? 9   LEU A C   1 
ATOM   38   O O   . LEU A 1 9   ? -16.031 -23.448 -42.771 1.00 17.01 ? 9   LEU A O   1 
ATOM   39   C CB  . LEU A 1 9   ? -18.541 -23.079 -44.928 1.00 21.50 ? 9   LEU A CB  1 
ATOM   40   C CG  . LEU A 1 9   ? -19.276 -23.665 -43.731 1.00 24.47 ? 9   LEU A CG  1 
ATOM   41   C CD1 . LEU A 1 9   ? -19.639 -22.555 -42.776 1.00 27.43 ? 9   LEU A CD1 1 
ATOM   42   C CD2 . LEU A 1 9   ? -20.553 -24.388 -44.156 1.00 26.02 ? 9   LEU A CD2 1 
ATOM   43   N N   . ARG A 1 10  ? -15.625 -24.183 -44.859 1.00 18.01 ? 10  ARG A N   1 
ATOM   44   C CA  . ARG A 1 10  ? -14.649 -25.151 -44.436 1.00 17.70 ? 10  ARG A CA  1 
ATOM   45   C C   . ARG A 1 10  ? -13.472 -24.457 -43.740 1.00 16.30 ? 10  ARG A C   1 
ATOM   46   O O   . ARG A 1 10  ? -13.076 -24.840 -42.632 1.00 16.67 ? 10  ARG A O   1 
ATOM   47   C CB  . ARG A 1 10  ? -14.229 -25.929 -45.673 1.00 20.01 ? 10  ARG A CB  1 
ATOM   48   C CG  . ARG A 1 10  ? -13.330 -27.093 -45.347 1.00 23.14 ? 10  ARG A CG  1 
ATOM   49   C CD  . ARG A 1 10  ? -13.072 -27.729 -46.691 1.00 26.17 ? 10  ARG A CD  1 
ATOM   50   N NE  . ARG A 1 10  ? -12.179 -28.818 -46.489 1.00 29.09 ? 10  ARG A NE  1 
ATOM   51   C CZ  . ARG A 1 10  ? -11.385 -29.312 -47.429 1.00 28.86 ? 10  ARG A CZ  1 
ATOM   52   N NH1 . ARG A 1 10  ? -11.289 -28.721 -48.611 1.00 32.76 ? 10  ARG A NH1 1 
ATOM   53   N NH2 . ARG A 1 10  ? -10.693 -30.395 -47.181 1.00 31.52 ? 10  ARG A NH2 1 
ATOM   54   N N   . ALA A 1 11  ? -12.955 -23.378 -44.339 1.00 15.81 ? 11  ALA A N   1 
ATOM   55   C CA  . ALA A 1 11  ? -11.811 -22.672 -43.784 1.00 15.06 ? 11  ALA A CA  1 
ATOM   56   C C   . ALA A 1 11  ? -12.157 -22.030 -42.435 1.00 14.34 ? 11  ALA A C   1 
ATOM   57   O O   . ALA A 1 11  ? -11.352 -22.004 -41.527 1.00 14.11 ? 11  ALA A O   1 
ATOM   58   C CB  . ALA A 1 11  ? -11.335 -21.635 -44.765 1.00 16.04 ? 11  ALA A CB  1 
ATOM   59   N N   . LEU A 1 12  ? -13.353 -21.450 -42.337 1.00 14.18 ? 12  LEU A N   1 
ATOM   60   C CA  . LEU A 1 12  ? -13.762 -20.771 -41.118 1.00 14.80 ? 12  LEU A CA  1 
ATOM   61   C C   . LEU A 1 12  ? -13.683 -21.756 -39.949 1.00 14.42 ? 12  LEU A C   1 
ATOM   62   O O   . LEU A 1 12  ? -13.217 -21.397 -38.868 1.00 14.35 ? 12  LEU A O   1 
ATOM   63   C CB  . LEU A 1 12  ? -15.166 -20.204 -41.327 1.00 15.93 ? 12  LEU A CB  1 
ATOM   64   C CG  . LEU A 1 12  ? -15.737 -19.442 -40.122 1.00 17.38 ? 12  LEU A CG  1 
ATOM   65   C CD1 . LEU A 1 12  ? -16.716 -18.392 -40.611 1.00 18.52 ? 12  LEU A CD1 1 
ATOM   66   C CD2 . LEU A 1 12  ? -16.474 -20.334 -39.117 1.00 17.73 ? 12  LEU A CD2 1 
ATOM   67   N N   . LYS A 1 13  ? -14.182 -22.982 -40.170 1.00 14.03 ? 13  LYS A N   1 
ATOM   68   C CA  . LYS A 1 13  ? -14.230 -24.005 -39.141 1.00 14.22 ? 13  LYS A CA  1 
ATOM   69   C C   . LYS A 1 13  ? -12.870 -24.592 -38.808 1.00 13.53 ? 13  LYS A C   1 
ATOM   70   O O   . LYS A 1 13  ? -12.739 -25.391 -37.905 1.00 15.45 ? 13  LYS A O   1 
ATOM   71   C CB  . LYS A 1 13  ? -15.214 -25.097 -39.554 1.00 15.72 ? 13  LYS A CB  1 
ATOM   72   C CG  . LYS A 1 13  ? -16.654 -24.581 -39.545 1.00 18.60 ? 13  LYS A CG  1 
ATOM   73   C CD  . LYS A 1 13  ? -17.640 -25.640 -40.013 1.00 21.76 ? 13  LYS A CD  1 
ATOM   74   C CE  . LYS A 1 13  ? -18.972 -25.001 -40.041 1.00 23.89 ? 13  LYS A CE  1 
ATOM   75   N NZ  . LYS A 1 13  ? -20.020 -25.951 -40.381 1.00 29.23 ? 13  LYS A NZ  1 
ATOM   76   N N   . LEU A 1 14  ? -11.843 -24.182 -39.563 1.00 12.30 ? 14  LEU A N   1 
ATOM   77   C CA  . LEU A 1 14  ? -10.451 -24.570 -39.342 1.00 12.00 ? 14  LEU A CA  1 
ATOM   78   C C   . LEU A 1 14  ? -9.621  -23.411 -38.791 1.00 11.64 ? 14  LEU A C   1 
ATOM   79   O O   . LEU A 1 14  ? -8.389  -23.525 -38.712 1.00 11.87 ? 14  LEU A O   1 
ATOM   80   C CB  . LEU A 1 14  ? -9.833  -25.085 -40.646 1.00 12.87 ? 14  LEU A CB  1 
ATOM   81   C CG  . LEU A 1 14  ? -10.523 -26.304 -41.259 1.00 13.64 ? 14  LEU A CG  1 
ATOM   82   C CD1 . LEU A 1 14  ? -9.978  -26.571 -42.629 1.00 15.60 ? 14  LEU A CD1 1 
ATOM   83   C CD2 . LEU A 1 14  ? -10.388 -27.515 -40.358 1.00 14.66 ? 14  LEU A CD2 1 
ATOM   84   N N   . MET A 1 15  ? -10.241 -22.277 -38.463 1.00 11.81 ? 15  MET A N   1 
ATOM   85   C CA  . MET A 1 15  ? -9.451  -21.144 -38.005 1.00 11.83 ? 15  MET A CA  1 
ATOM   86   C C   . MET A 1 15  ? -9.050  -21.269 -36.539 1.00 12.14 ? 15  MET A C   1 
ATOM   87   O O   . MET A 1 15  ? -9.855  -21.684 -35.689 1.00 12.14 ? 15  MET A O   1 
ATOM   88   C CB  . MET A 1 15  ? -10.194 -19.820 -38.185 1.00 13.61 ? 15  MET A CB  1 
ATOM   89   C CG  . MET A 1 15  ? -10.251 -19.340 -39.597 1.00 17.30 ? 15  MET A CG  1 
ATOM   90   S SD  . MET A 1 15  ? -10.715 -17.601 -39.757 1.00 23.84 ? 15  MET A SD  1 
ATOM   91   C CE  . MET A 1 15  ? -9.222  -16.828 -39.091 1.00 27.22 ? 15  MET A CE  1 
ATOM   92   N N   . ASP A 1 16  ? -7.800  -20.848 -36.249 1.00 12.26 ? 16  ASP A N   1 
ATOM   93   C CA  . ASP A 1 16  ? -7.394  -20.445 -34.905 1.00 12.21 ? 16  ASP A CA  1 
ATOM   94   C C   . ASP A 1 16  ? -7.473  -18.929 -34.873 1.00 12.57 ? 16  ASP A C   1 
ATOM   95   O O   . ASP A 1 16  ? -6.616  -18.222 -35.389 1.00 14.87 ? 16  ASP A O   1 
ATOM   96   C CB  . ASP A 1 16  ? -5.982  -20.856 -34.548 1.00 13.39 ? 16  ASP A CB  1 
ATOM   97   C CG  . ASP A 1 16  ? -5.719  -22.337 -34.340 1.00 13.93 ? 16  ASP A CG  1 
ATOM   98   O OD1 . ASP A 1 16  ? -6.590  -23.166 -34.652 1.00 15.10 ? 16  ASP A OD1 1 
ATOM   99   O OD2 . ASP A 1 16  ? -4.624  -22.652 -33.828 1.00 17.55 ? 16  ASP A OD2 1 
ATOM   100  N N   . LEU A 1 17  ? -8.571  -18.408 -34.305 1.00 12.81 ? 17  LEU A N   1 
ATOM   101  C CA  . LEU A 1 17  ? -8.819  -16.986 -34.402 1.00 13.36 ? 17  LEU A CA  1 
ATOM   102  C C   . LEU A 1 17  ? -7.999  -16.260 -33.346 1.00 13.82 ? 17  LEU A C   1 
ATOM   103  O O   . LEU A 1 17  ? -8.081  -16.610 -32.166 1.00 14.50 ? 17  LEU A O   1 
ATOM   104  C CB  . LEU A 1 17  ? -10.305 -16.732 -34.185 1.00 13.89 ? 17  LEU A CB  1 
ATOM   105  C CG  . LEU A 1 17  ? -10.778 -15.315 -34.459 1.00 16.13 ? 17  LEU A CG  1 
ATOM   106  C CD1 . LEU A 1 17  ? -10.648 -15.047 -35.933 1.00 17.91 ? 17  LEU A CD1 1 
ATOM   107  C CD2 . LEU A 1 17  ? -12.221 -15.149 -33.993 1.00 16.45 ? 17  LEU A CD2 1 
ATOM   108  N N   . SER A 1 18  ? -7.229  -15.246 -33.742 1.00 18.29 ? 18  SER A N   1 
ATOM   109  C CA  . SER A 1 18  ? -6.302  -14.586 -32.827 1.00 22.40 ? 18  SER A CA  1 
ATOM   110  C C   . SER A 1 18  ? -6.545  -13.065 -32.813 1.00 25.81 ? 18  SER A C   1 
ATOM   111  O O   . SER A 1 18  ? -7.305  -12.583 -33.681 1.00 32.95 ? 18  SER A O   1 
ATOM   112  C CB  . SER A 1 18  ? -4.887  -14.898 -33.199 1.00 25.80 ? 18  SER A CB  1 
ATOM   113  O OG  . SER A 1 18  ? -4.663  -14.336 -34.469 1.00 32.75 ? 18  SER A OG  1 
ATOM   114  N N   . THR A 1 25  ? -6.013  -6.605  -23.537 1.00 31.69 ? 25  THR A N   1 
ATOM   115  C CA  . THR A 1 25  ? -6.945  -6.426  -22.398 1.00 30.05 ? 25  THR A CA  1 
ATOM   116  C C   . THR A 1 25  ? -7.919  -7.604  -22.354 1.00 27.80 ? 25  THR A C   1 
ATOM   117  O O   . THR A 1 25  ? -8.188  -8.249  -23.356 1.00 27.55 ? 25  THR A O   1 
ATOM   118  C CB  . THR A 1 25  ? -7.735  -5.120  -22.520 1.00 31.97 ? 25  THR A CB  1 
ATOM   119  O OG1 . THR A 1 25  ? -8.582  -5.274  -23.663 1.00 33.32 ? 25  THR A OG1 1 
ATOM   120  C CG2 . THR A 1 25  ? -6.863  -3.883  -22.631 1.00 33.99 ? 25  THR A CG2 1 
ATOM   121  N N   . ASP A 1 26  ? -8.482  -7.840  -21.179 1.00 27.43 ? 26  ASP A N   1 
ATOM   122  C CA  . ASP A 1 26  ? -9.528  -8.838  -21.016 1.00 25.42 ? 26  ASP A CA  1 
ATOM   123  C C   . ASP A 1 26  ? -10.727 -8.554  -21.922 1.00 23.97 ? 26  ASP A C   1 
ATOM   124  O O   . ASP A 1 26  ? -11.298 -9.477  -22.499 1.00 21.08 ? 26  ASP A O   1 
ATOM   125  C CB  . ASP A 1 26  ? -9.989  -8.911  -19.575 1.00 27.10 ? 26  ASP A CB  1 
ATOM   126  C CG  . ASP A 1 26  ? -9.074  -9.647  -18.613 1.00 30.12 ? 26  ASP A CG  1 
ATOM   127  O OD1 . ASP A 1 26  ? -8.068  -10.195 -19.063 1.00 34.29 ? 26  ASP A OD1 1 
ATOM   128  O OD2 . ASP A 1 26  ? -9.398  -9.673  -17.419 1.00 37.67 ? 26  ASP A OD2 1 
ATOM   129  N N   . GLU A 1 27  ? -11.100 -7.282  -22.078 1.00 25.41 ? 27  GLU A N   1 
ATOM   130  C CA  . GLU A 1 27  ? -12.227 -6.934  -22.934 1.00 26.32 ? 27  GLU A CA  1 
ATOM   131  C C   . GLU A 1 27  ? -11.982 -7.421  -24.372 1.00 24.30 ? 27  GLU A C   1 
ATOM   132  O O   . GLU A 1 27  ? -12.875 -7.920  -25.052 1.00 25.03 ? 27  GLU A O   1 
ATOM   133  C CB  . GLU A 1 27  ? -12.435 -5.424  -22.857 1.00 31.81 ? 27  GLU A CB  1 
ATOM   134  C CG  . GLU A 1 27  ? -12.882 -4.913  -21.485 1.00 38.59 ? 27  GLU A CG  1 
ATOM   135  C CD  . GLU A 1 27  ? -12.012 -5.160  -20.244 1.00 44.32 ? 27  GLU A CD  1 
ATOM   136  O OE1 . GLU A 1 27  ? -10.760 -5.011  -20.253 1.00 40.80 ? 27  GLU A OE1 1 
ATOM   137  O OE2 . GLU A 1 27  ? -12.645 -5.489  -19.207 1.00 55.01 ? 27  GLU A OE2 1 
ATOM   138  N N   . LYS A 1 28  ? -10.748 -7.302  -24.849 1.00 22.64 ? 28  LYS A N   1 
ATOM   139  C CA  . LYS A 1 28  ? -10.432 -7.728  -26.210 1.00 24.00 ? 28  LYS A CA  1 
ATOM   140  C C   . LYS A 1 28  ? -10.459 -9.250  -26.313 1.00 19.74 ? 28  LYS A C   1 
ATOM   141  O O   . LYS A 1 28  ? -10.861 -9.785  -27.335 1.00 20.24 ? 28  LYS A O   1 
ATOM   142  C CB  . LYS A 1 28  ? -9.046  -7.241  -26.641 1.00 25.45 ? 28  LYS A CB  1 
ATOM   143  C CG  . LYS A 1 28  ? -8.927  -5.741  -26.764 1.00 31.94 ? 28  LYS A CG  1 
ATOM   144  C CD  . LYS A 1 28  ? -9.634  -5.146  -27.971 1.00 39.35 ? 28  LYS A CD  1 
ATOM   145  C CE  . LYS A 1 28  ? -9.813  -3.671  -27.804 1.00 44.06 ? 28  LYS A CE  1 
ATOM   146  N NZ  . LYS A 1 28  ? -10.639 -3.179  -28.901 1.00 48.29 ? 28  LYS A NZ  1 
ATOM   147  N N   . VAL A 1 29  ? -10.011 -9.961  -25.262 1.00 17.26 ? 29  VAL A N   1 
ATOM   148  C CA  . VAL A 1 29  ? -10.077 -11.410 -25.265 1.00 17.37 ? 29  VAL A CA  1 
ATOM   149  C C   . VAL A 1 29  ? -11.536 -11.862 -25.302 1.00 17.23 ? 29  VAL A C   1 
ATOM   150  O O   . VAL A 1 29  ? -11.907 -12.791 -26.011 1.00 17.32 ? 29  VAL A O   1 
ATOM   151  C CB  . VAL A 1 29  ? -9.317  -12.005 -24.065 1.00 16.98 ? 29  VAL A CB  1 
ATOM   152  C CG1 . VAL A 1 29  ? -9.570  -13.505 -23.915 1.00 17.64 ? 29  VAL A CG1 1 
ATOM   153  C CG2 . VAL A 1 29  ? -7.825  -11.700 -24.162 1.00 19.32 ? 29  VAL A CG2 1 
ATOM   154  N N   . ILE A 1 30  ? -12.373 -11.231 -24.483 1.00 18.26 ? 30  ILE A N   1 
ATOM   155  C CA  . ILE A 1 30  ? -13.782 -11.578 -24.439 1.00 18.84 ? 30  ILE A CA  1 
ATOM   156  C C   . ILE A 1 30  ? -14.415 -11.361 -25.815 1.00 18.96 ? 30  ILE A C   1 
ATOM   157  O O   . ILE A 1 30  ? -15.128 -12.230 -26.311 1.00 19.76 ? 30  ILE A O   1 
ATOM   158  C CB  . ILE A 1 30  ? -14.469 -10.786 -23.316 1.00 20.46 ? 30  ILE A CB  1 
ATOM   159  C CG1 . ILE A 1 30  ? -13.956 -11.227 -21.961 1.00 21.32 ? 30  ILE A CG1 1 
ATOM   160  C CG2 . ILE A 1 30  ? -15.981 -10.915 -23.424 1.00 21.46 ? 30  ILE A CG2 1 
ATOM   161  C CD1 . ILE A 1 30  ? -14.294 -10.289 -20.811 1.00 23.86 ? 30  ILE A CD1 1 
ATOM   162  N N   . ALA A 1 31  ? -14.108 -10.224 -26.442 1.00 20.17 ? 31  ALA A N   1 
ATOM   163  C CA  . ALA A 1 31  ? -14.606 -9.936  -27.790 1.00 20.76 ? 31  ALA A CA  1 
ATOM   164  C C   . ALA A 1 31  ? -14.151 -10.991 -28.797 1.00 20.60 ? 31  ALA A C   1 
ATOM   165  O O   . ALA A 1 31  ? -14.898 -11.387 -29.663 1.00 20.23 ? 31  ALA A O   1 
ATOM   166  C CB  . ALA A 1 31  ? -14.155 -8.573  -28.252 1.00 22.06 ? 31  ALA A CB  1 
ATOM   167  N N   . LEU A 1 32  ? -12.902 -11.437 -28.679 1.00 18.46 ? 32  LEU A N   1 
ATOM   168  C CA  . LEU A 1 32  ? -12.379 -12.471 -29.550 1.00 17.54 ? 32  LEU A CA  1 
ATOM   169  C C   . LEU A 1 32  ? -13.210 -13.741 -29.422 1.00 15.51 ? 32  LEU A C   1 
ATOM   170  O O   . LEU A 1 32  ? -13.546 -14.402 -30.396 1.00 16.67 ? 32  LEU A O   1 
ATOM   171  C CB  . LEU A 1 32  ? -10.924 -12.745 -29.181 1.00 17.86 ? 32  LEU A CB  1 
ATOM   172  C CG  . LEU A 1 32  ? -10.253 -13.883 -29.955 1.00 18.17 ? 32  LEU A CG  1 
ATOM   173  C CD1 . LEU A 1 32  ? -10.063 -13.533 -31.418 1.00 20.31 ? 32  LEU A CD1 1 
ATOM   174  C CD2 . LEU A 1 32  ? -8.923  -14.268 -29.377 1.00 17.70 ? 32  LEU A CD2 1 
ATOM   175  N N   . CYS A 1 33  ? -13.499 -14.129 -28.183 1.00 15.29 ? 33  CYS A N   1 
ATOM   176  C CA  . CYS A 1 33  ? -14.286 -15.326 -27.965 1.00 16.11 ? 33  CYS A CA  1 
ATOM   177  C C   . CYS A 1 33  ? -15.666 -15.171 -28.595 1.00 17.03 ? 33  CYS A C   1 
ATOM   178  O O   . CYS A 1 33  ? -16.169 -16.101 -29.221 1.00 17.06 ? 33  CYS A O   1 
ATOM   179  C CB  . CYS A 1 33  ? -14.470 -15.566 -26.482 1.00 16.91 ? 33  CYS A CB  1 
ATOM   180  S SG  . CYS A 1 33  ? -12.937 -16.043 -25.674 1.00 20.16 ? 33  CYS A SG  1 
ATOM   181  N N   . HIS A 1 34  ? -16.268 -13.985 -28.451 1.00 17.23 ? 34  HIS A N   1 
ATOM   182  C CA  . HIS A 1 34  ? -17.550 -13.729 -29.084 1.00 19.30 ? 34  HIS A CA  1 
ATOM   183  C C   . HIS A 1 34  ? -17.481 -13.852 -30.606 1.00 18.86 ? 34  HIS A C   1 
ATOM   184  O O   . HIS A 1 34  ? -18.369 -14.439 -31.229 1.00 19.09 ? 34  HIS A O   1 
ATOM   185  C CB  . HIS A 1 34  ? -18.111 -12.373 -28.643 1.00 20.48 ? 34  HIS A CB  1 
ATOM   186  C CG  . HIS A 1 34  ? -18.434 -12.274 -27.192 1.00 21.89 ? 34  HIS A CG  1 
ATOM   187  N ND1 . HIS A 1 34  ? -18.650 -11.079 -26.547 1.00 26.49 ? 34  HIS A ND1 1 
ATOM   188  C CD2 . HIS A 1 34  ? -18.591 -13.214 -26.275 1.00 21.37 ? 34  HIS A CD2 1 
ATOM   189  C CE1 . HIS A 1 34  ? -18.909 -11.300 -25.260 1.00 24.84 ? 34  HIS A CE1 1 
ATOM   190  N NE2 . HIS A 1 34  ? -18.883 -12.603 -25.062 1.00 24.20 ? 34  HIS A NE2 1 
ATOM   191  N N   . GLN A 1 35  ? -16.395 -13.345 -31.192 1.00 17.92 ? 35  GLN A N   1 
ATOM   192  C CA  . GLN A 1 35  ? -16.220 -13.348 -32.638 1.00 18.48 ? 35  GLN A CA  1 
ATOM   193  C C   . GLN A 1 35  ? -16.017 -14.760 -33.174 1.00 16.62 ? 35  GLN A C   1 
ATOM   194  O O   . GLN A 1 35  ? -16.391 -15.019 -34.305 1.00 18.61 ? 35  GLN A O   1 
ATOM   195  C CB  . GLN A 1 35  ? -15.026 -12.488 -33.035 1.00 22.13 ? 35  GLN A CB  1 
ATOM   196  C CG  . GLN A 1 35  ? -15.288 -11.002 -32.835 1.00 27.19 ? 35  GLN A CG  1 
ATOM   197  C CD  . GLN A 1 35  ? -14.014 -10.188 -32.808 1.00 34.50 ? 35  GLN A CD  1 
ATOM   198  O OE1 . GLN A 1 35  ? -12.896 -10.703 -32.943 1.00 39.35 ? 35  GLN A OE1 1 
ATOM   199  N NE2 . GLN A 1 35  ? -14.173 -8.892  -32.591 1.00 42.94 ? 35  GLN A NE2 1 
ATOM   200  N N   . ALA A 1 36  ? -15.466 -15.669 -32.357 1.00 15.30 ? 36  ALA A N   1 
ATOM   201  C CA  . ALA A 1 36  ? -15.264 -17.055 -32.757 1.00 15.06 ? 36  ALA A CA  1 
ATOM   202  C C   . ALA A 1 36  ? -16.569 -17.825 -32.944 1.00 14.99 ? 36  ALA A C   1 
ATOM   203  O O   . ALA A 1 36  ? -16.575 -18.874 -33.598 1.00 15.77 ? 36  ALA A O   1 
ATOM   204  C CB  . ALA A 1 36  ? -14.370 -17.757 -31.772 1.00 14.82 ? 36  ALA A CB  1 
ATOM   205  N N   . LYS A 1 37  ? -17.642 -17.340 -32.298 1.00 15.38 ? 37  LYS A N   1 
ATOM   206  C CA  . LYS A 1 37  ? -18.963 -17.938 -32.396 1.00 15.75 ? 37  LYS A CA  1 
ATOM   207  C C   . LYS A 1 37  ? -19.719 -17.201 -33.496 1.00 17.10 ? 37  LYS A C   1 
ATOM   208  O O   . LYS A 1 37  ? -20.366 -16.199 -33.236 1.00 19.13 ? 37  LYS A O   1 
ATOM   209  C CB  . LYS A 1 37  ? -19.642 -17.865 -31.029 1.00 16.45 ? 37  LYS A CB  1 
ATOM   210  C CG  . LYS A 1 37  ? -21.040 -18.457 -30.999 1.00 17.21 ? 37  LYS A CG  1 
ATOM   211  C CD  . LYS A 1 37  ? -21.719 -18.212 -29.660 1.00 19.22 ? 37  LYS A CD  1 
ATOM   212  C CE  . LYS A 1 37  ? -23.023 -18.958 -29.528 1.00 20.99 ? 37  LYS A CE  1 
ATOM   213  N NZ  . LYS A 1 37  ? -23.768 -18.628 -28.318 1.00 23.72 ? 37  LYS A NZ  1 
ATOM   214  N N   . THR A 1 38  ? -19.519 -17.627 -34.746 1.00 17.21 ? 38  THR A N   1 
ATOM   215  C CA  . THR A 1 38  ? -19.989 -16.876 -35.891 1.00 17.34 ? 38  THR A CA  1 
ATOM   216  C C   . THR A 1 38  ? -21.371 -17.358 -36.304 1.00 17.69 ? 38  THR A C   1 
ATOM   217  O O   . THR A 1 38  ? -21.836 -18.450 -35.916 1.00 16.66 ? 38  THR A O   1 
ATOM   218  C CB  . THR A 1 38  ? -19.034 -16.991 -37.094 1.00 17.80 ? 38  THR A CB  1 
ATOM   219  O OG1 . THR A 1 38  ? -19.424 -18.060 -37.955 1.00 17.45 ? 38  THR A OG1 1 
ATOM   220  C CG2 . THR A 1 38  ? -17.575 -17.115 -36.693 1.00 18.16 ? 38  THR A CG2 1 
ATOM   221  N N   . PRO A 1 39  ? -22.066 -16.558 -37.141 1.00 18.61 ? 39  PRO A N   1 
ATOM   222  C CA  . PRO A 1 39  ? -23.413 -16.941 -37.576 1.00 18.34 ? 39  PRO A CA  1 
ATOM   223  C C   . PRO A 1 39  ? -23.451 -18.234 -38.386 1.00 19.07 ? 39  PRO A C   1 
ATOM   224  O O   . PRO A 1 39  ? -24.513 -18.804 -38.583 1.00 18.48 ? 39  PRO A O   1 
ATOM   225  C CB  . PRO A 1 39  ? -23.911 -15.748 -38.382 1.00 21.01 ? 39  PRO A CB  1 
ATOM   226  C CG  . PRO A 1 39  ? -23.034 -14.587 -37.935 1.00 23.05 ? 39  PRO A CG  1 
ATOM   227  C CD  . PRO A 1 39  ? -21.706 -15.193 -37.558 1.00 20.97 ? 39  PRO A CD  1 
ATOM   228  N N   . VAL A 1 40  ? -22.294 -18.651 -38.947 1.00 17.33 ? 40  VAL A N   1 
ATOM   229  C CA  . VAL A 1 40  ? -22.259 -19.849 -39.779 1.00 16.86 ? 40  VAL A CA  1 
ATOM   230  C C   . VAL A 1 40  ? -21.510 -21.005 -39.112 1.00 16.63 ? 40  VAL A C   1 
ATOM   231  O O   . VAL A 1 40  ? -21.345 -22.061 -39.721 1.00 17.61 ? 40  VAL A O   1 
ATOM   232  C CB  . VAL A 1 40  ? -21.638 -19.556 -41.156 1.00 18.93 ? 40  VAL A CB  1 
ATOM   233  C CG1 . VAL A 1 40  ? -22.407 -18.435 -41.865 1.00 22.35 ? 40  VAL A CG1 1 
ATOM   234  C CG2 . VAL A 1 40  ? -20.152 -19.238 -41.051 1.00 19.32 ? 40  VAL A CG2 1 
ATOM   235  N N   . GLY A 1 41  ? -21.112 -20.839 -37.846 1.00 16.00 ? 41  GLY A N   1 
ATOM   236  C CA  . GLY A 1 41  ? -20.407 -21.881 -37.131 1.00 15.45 ? 41  GLY A CA  1 
ATOM   237  C C   . GLY A 1 41  ? -19.248 -21.297 -36.330 1.00 14.55 ? 41  GLY A C   1 
ATOM   238  O O   . GLY A 1 41  ? -19.004 -20.098 -36.335 1.00 15.53 ? 41  GLY A O   1 
ATOM   239  N N   . ASN A 1 42  ? -18.649 -22.167 -35.538 1.00 15.06 ? 42  ASN A N   1 
ATOM   240  C CA  . ASN A 1 42  ? -17.560 -21.815 -34.659 1.00 14.94 ? 42  ASN A CA  1 
ATOM   241  C C   . ASN A 1 42  ? -16.227 -22.038 -35.349 1.00 14.17 ? 42  ASN A C   1 
ATOM   242  O O   . ASN A 1 42  ? -16.074 -22.969 -36.135 1.00 14.54 ? 42  ASN A O   1 
ATOM   243  C CB  . ASN A 1 42  ? -17.611 -22.670 -33.409 1.00 15.88 ? 42  ASN A CB  1 
ATOM   244  C CG  . ASN A 1 42  ? -18.851 -22.422 -32.589 1.00 17.57 ? 42  ASN A CG  1 
ATOM   245  O OD1 . ASN A 1 42  ? -19.438 -21.342 -32.664 1.00 18.76 ? 42  ASN A OD1 1 
ATOM   246  N ND2 . ASN A 1 42  ? -19.196 -23.381 -31.740 1.00 20.78 ? 42  ASN A ND2 1 
ATOM   247  N N   . THR A 1 43  ? -15.269 -21.183 -35.033 1.00 13.80 ? 43  THR A N   1 
ATOM   248  C CA  . THR A 1 43  ? -13.902 -21.471 -35.466 1.00 13.01 ? 43  THR A CA  1 
ATOM   249  C C   . THR A 1 43  ? -13.419 -22.696 -34.702 1.00 13.52 ? 43  THR A C   1 
ATOM   250  O O   . THR A 1 43  ? -14.016 -23.091 -33.706 1.00 14.17 ? 43  THR A O   1 
ATOM   251  C CB  . THR A 1 43  ? -13.006 -20.258 -35.246 1.00 13.96 ? 43  THR A CB  1 
ATOM   252  O OG1 . THR A 1 43  ? -12.923 -19.927 -33.866 1.00 14.00 ? 43  THR A OG1 1 
ATOM   253  C CG2 . THR A 1 43  ? -13.455 -19.063 -36.057 1.00 14.29 ? 43  THR A CG2 1 
ATOM   254  N N   . ALA A 1 44  ? -12.297 -23.284 -35.134 1.00 13.07 ? 44  ALA A N   1 
ATOM   255  C CA  . ALA A 1 44  ? -11.760 -24.452 -34.457 1.00 12.24 ? 44  ALA A CA  1 
ATOM   256  C C   . ALA A 1 44  ? -11.239 -24.088 -33.070 1.00 12.11 ? 44  ALA A C   1 
ATOM   257  O O   . ALA A 1 44  ? -11.329 -24.881 -32.119 1.00 13.02 ? 44  ALA A O   1 
ATOM   258  C CB  . ALA A 1 44  ? -10.623 -25.035 -35.277 1.00 12.56 ? 44  ALA A CB  1 
ATOM   259  N N   . ALA A 1 45  ? -10.652 -22.896 -32.999 1.00 11.56 ? 45  ALA A N   1 
ATOM   260  C CA  . ALA A 1 45  ? -9.911  -22.460 -31.839 1.00 11.86 ? 45  ALA A CA  1 
ATOM   261  C C   . ALA A 1 45  ? -9.892  -20.949 -31.776 1.00 11.30 ? 45  ALA A C   1 
ATOM   262  O O   . ALA A 1 45  ? -10.191 -20.256 -32.748 1.00 11.53 ? 45  ALA A O   1 
ATOM   263  C CB  . ALA A 1 45  ? -8.482  -22.997 -31.842 1.00 11.91 ? 45  ALA A CB  1 
ATOM   264  N N   . ILE A 1 46  ? -9.548  -20.461 -30.582 1.00 11.62 ? 46  ILE A N   1 
ATOM   265  C CA  . ILE A 1 46  ? -9.019  -19.115 -30.416 1.00 12.77 ? 46  ILE A CA  1 
ATOM   266  C C   . ILE A 1 46  ? -7.554  -19.259 -29.998 1.00 12.17 ? 46  ILE A C   1 
ATOM   267  O O   . ILE A 1 46  ? -7.188  -20.275 -29.409 1.00 13.87 ? 46  ILE A O   1 
ATOM   268  C CB  . ILE A 1 46  ? -9.834  -18.294 -29.409 1.00 14.22 ? 46  ILE A CB  1 
ATOM   269  C CG1 . ILE A 1 46  ? -9.892  -18.939 -28.045 1.00 16.73 ? 46  ILE A CG1 1 
ATOM   270  C CG2 . ILE A 1 46  ? -11.222 -18.015 -29.975 1.00 14.28 ? 46  ILE A CG2 1 
ATOM   271  C CD1 . ILE A 1 46  ? -10.365 -17.998 -26.986 1.00 22.25 ? 46  ILE A CD1 1 
ATOM   272  N N   . SER A 1 47  ? -6.776  -18.210 -30.247 1.00 11.43 ? 47  SER A N   1 
ATOM   273  C CA  . SER A 1 47  ? -5.367  -18.211 -29.910 1.00 12.00 ? 47  SER A CA  1 
ATOM   274  C C   . SER A 1 47  ? -5.079  -16.921 -29.156 1.00 12.68 ? 47  SER A C   1 
ATOM   275  O O   . SER A 1 47  ? -5.361  -15.839 -29.646 1.00 13.92 ? 47  SER A O   1 
ATOM   276  C CB  . SER A 1 47  ? -4.494  -18.314 -31.160 1.00 14.13 ? 47  SER A CB  1 
ATOM   277  O OG  . SER A 1 47  ? -3.132  -18.412 -30.780 1.00 18.75 ? 47  SER A OG  1 
ATOM   278  N N   . VAL A 1 48  ? -4.595  -17.070 -27.919 1.00 11.85 ? 48  VAL A N   1 
ATOM   279  C CA  . VAL A 1 48  ? -4.340  -15.958 -27.025 1.00 11.74 ? 48  VAL A CA  1 
ATOM   280  C C   . VAL A 1 48  ? -2.983  -16.185 -26.365 1.00 11.98 ? 48  VAL A C   1 
ATOM   281  O O   . VAL A 1 48  ? -2.490  -17.299 -26.343 1.00 12.88 ? 48  VAL A O   1 
ATOM   282  C CB  . VAL A 1 48  ? -5.462  -15.798 -25.977 1.00 13.44 ? 48  VAL A CB  1 
ATOM   283  C CG1 . VAL A 1 48  ? -6.802  -15.485 -26.637 1.00 14.78 ? 48  VAL A CG1 1 
ATOM   284  C CG2 . VAL A 1 48  ? -5.588  -17.035 -25.130 1.00 14.45 ? 48  VAL A CG2 1 
ATOM   285  N N   . TYR A 1 49  ? -2.470  -15.137 -25.728 1.00 12.09 ? 49  TYR A N   1 
ATOM   286  C CA  . TYR A 1 49  ? -1.319  -15.307 -24.871 1.00 13.50 ? 49  TYR A CA  1 
ATOM   287  C C   . TYR A 1 49  ? -1.691  -16.119 -23.632 1.00 12.05 ? 49  TYR A C   1 
ATOM   288  O O   . TYR A 1 49  ? -2.845  -16.136 -23.201 1.00 12.50 ? 49  TYR A O   1 
ATOM   289  C CB  . TYR A 1 49  ? -0.669  -13.984 -24.474 1.00 14.96 ? 49  TYR A CB  1 
ATOM   290  C CG  . TYR A 1 49  ? 0.074   -13.287 -25.600 1.00 18.12 ? 49  TYR A CG  1 
ATOM   291  C CD1 . TYR A 1 49  ? 1.157   -13.879 -26.208 1.00 21.54 ? 49  TYR A CD1 1 
ATOM   292  C CD2 . TYR A 1 49  ? -0.346  -12.059 -26.073 1.00 23.23 ? 49  TYR A CD2 1 
ATOM   293  C CE1 . TYR A 1 49  ? 1.845   -13.243 -27.224 1.00 22.79 ? 49  TYR A CE1 1 
ATOM   294  C CE2 . TYR A 1 49  ? 0.333   -11.401 -27.076 1.00 26.01 ? 49  TYR A CE2 1 
ATOM   295  C CZ  . TYR A 1 49  ? 1.418   -12.009 -27.670 1.00 25.60 ? 49  TYR A CZ  1 
ATOM   296  O OH  . TYR A 1 49  ? 2.087   -11.387 -28.675 1.00 33.19 ? 49  TYR A OH  1 
ATOM   297  N N   . PRO A 1 50  ? -0.723  -16.836 -23.026 1.00 12.04 ? 50  PRO A N   1 
ATOM   298  C CA  . PRO A 1 50  ? -1.049  -17.743 -21.922 1.00 11.99 ? 50  PRO A CA  1 
ATOM   299  C C   . PRO A 1 50  ? -1.879  -17.129 -20.796 1.00 11.82 ? 50  PRO A C   1 
ATOM   300  O O   . PRO A 1 50  ? -2.829  -17.748 -20.311 1.00 12.22 ? 50  PRO A O   1 
ATOM   301  C CB  . PRO A 1 50  ? 0.293   -18.218 -21.452 1.00 11.98 ? 50  PRO A CB  1 
ATOM   302  C CG  . PRO A 1 50  ? 1.138   -18.181 -22.724 1.00 11.94 ? 50  PRO A CG  1 
ATOM   303  C CD  . PRO A 1 50  ? 0.686   -16.961 -23.455 1.00 12.07 ? 50  PRO A CD  1 
ATOM   304  N N   . ARG A 1 51  ? -1.531  -15.900 -20.416 1.00 12.18 ? 51  ARG A N   1 
ATOM   305  C CA  . ARG A 1 51  ? -2.189  -15.262 -19.288 1.00 13.03 ? 51  ARG A CA  1 
ATOM   306  C C   . ARG A 1 51  ? -3.683  -15.051 -19.526 1.00 12.82 ? 51  ARG A C   1 
ATOM   307  O O   . ARG A 1 51  ? -4.446  -14.867 -18.548 1.00 14.60 ? 51  ARG A O   1 
ATOM   308  C CB  . ARG A 1 51  ? -1.550  -13.915 -18.974 1.00 15.79 ? 51  ARG A CB  1 
ATOM   309  C CG  . ARG A 1 51  ? -1.616  -12.868 -20.068 1.00 19.97 ? 51  ARG A CG  1 
ATOM   310  C CD  . ARG A 1 51  ? -0.836  -11.650 -19.590 1.00 24.36 ? 51  ARG A CD  1 
ATOM   311  N NE  . ARG A 1 51  ? -0.681  -10.681 -20.647 1.00 30.88 ? 51  ARG A NE  1 
ATOM   312  C CZ  . ARG A 1 51  ? 0.215   -10.740 -21.643 1.00 33.39 ? 51  ARG A CZ  1 
ATOM   313  N NH1 . ARG A 1 51  ? 1.178   -11.656 -21.664 1.00 33.86 ? 51  ARG A NH1 1 
ATOM   314  N NH2 . ARG A 1 51  ? 0.142   -9.863  -22.620 1.00 39.79 ? 51  ARG A NH2 1 
ATOM   315  N N   . SER A 1 52  ? -4.106  -15.062 -20.792 1.00 11.91 ? 52  SER A N   1 
ATOM   316  C CA  . SER A 1 52  ? -5.487  -14.821 -21.164 1.00 13.20 ? 52  SER A CA  1 
ATOM   317  C C   . SER A 1 52  ? -6.309  -16.087 -21.201 1.00 12.58 ? 52  SER A C   1 
ATOM   318  O O   . SER A 1 52  ? -7.525  -16.002 -21.446 1.00 12.55 ? 52  SER A O   1 
ATOM   319  C CB  . SER A 1 52  ? -5.557  -14.123 -22.509 1.00 15.30 ? 52  SER A CB  1 
ATOM   320  O OG  . SER A 1 52  ? -4.894  -12.870 -22.482 1.00 18.13 ? 52  SER A OG  1 
ATOM   321  N N   . ILE A 1 53  ? -5.701  -17.249 -21.016 1.00 12.32 ? 53  ILE A N   1 
ATOM   322  C CA  . ILE A 1 53  ? -6.436  -18.498 -21.164 1.00 12.04 ? 53  ILE A CA  1 
ATOM   323  C C   . ILE A 1 53  ? -7.589  -18.604 -20.171 1.00 12.32 ? 53  ILE A C   1 
ATOM   324  O O   . ILE A 1 53  ? -8.675  -18.998 -20.591 1.00 13.07 ? 53  ILE A O   1 
ATOM   325  C CB  . ILE A 1 53  ? -5.478  -19.701 -21.109 1.00 12.54 ? 53  ILE A CB  1 
ATOM   326  C CG1 . ILE A 1 53  ? -4.566  -19.709 -22.335 1.00 12.74 ? 53  ILE A CG1 1 
ATOM   327  C CG2 . ILE A 1 53  ? -6.248  -21.014 -20.978 1.00 14.01 ? 53  ILE A CG2 1 
ATOM   328  C CD1 . ILE A 1 53  ? -3.382  -20.649 -22.199 1.00 13.57 ? 53  ILE A CD1 1 
ATOM   329  N N   . PRO A 1 54  ? -7.414  -18.286 -18.879 1.00 12.54 ? 54  PRO A N   1 
ATOM   330  C CA  . PRO A 1 54  ? -8.534  -18.482 -17.936 1.00 12.77 ? 54  PRO A CA  1 
ATOM   331  C C   . PRO A 1 54  ? -9.763  -17.659 -18.310 1.00 13.53 ? 54  PRO A C   1 
ATOM   332  O O   . PRO A 1 54  ? -10.889 -18.167 -18.255 1.00 14.05 ? 54  PRO A O   1 
ATOM   333  C CB  . PRO A 1 54  ? -7.909  -18.115 -16.605 1.00 13.62 ? 54  PRO A CB  1 
ATOM   334  C CG  . PRO A 1 54  ? -6.439  -18.422 -16.773 1.00 12.73 ? 54  PRO A CG  1 
ATOM   335  C CD  . PRO A 1 54  ? -6.155  -17.989 -18.189 1.00 12.09 ? 54  PRO A CD  1 
ATOM   336  N N   . ILE A 1 55  ? -9.592  -16.378 -18.631 1.00 13.17 ? 55  ILE A N   1 
ATOM   337  C CA  . ILE A 1 55  ? -10.759 -15.557 -18.940 1.00 14.34 ? 55  ILE A CA  1 
ATOM   338  C C   . ILE A 1 55  ? -11.391 -16.018 -20.248 1.00 13.45 ? 55  ILE A C   1 
ATOM   339  O O   . ILE A 1 55  ? -12.607 -15.977 -20.422 1.00 14.91 ? 55  ILE A O   1 
ATOM   340  C CB  . ILE A 1 55  ? -10.475 -14.045 -18.913 1.00 16.08 ? 55  ILE A CB  1 
ATOM   341  C CG1 . ILE A 1 55  ? -11.777 -13.209 -18.897 1.00 19.63 ? 55  ILE A CG1 1 
ATOM   342  C CG2 . ILE A 1 55  ? -9.593  -13.590 -20.060 1.00 16.72 ? 55  ILE A CG2 1 
ATOM   343  C CD1 . ILE A 1 55  ? -12.688 -13.494 -17.743 1.00 23.89 ? 55  ILE A CD1 1 
ATOM   344  N N   . ALA A 1 56  ? -10.562 -16.463 -21.192 1.00 12.64 ? 56  ALA A N   1 
ATOM   345  C CA  . ALA A 1 56  ? -11.101 -17.005 -22.421 1.00 13.38 ? 56  ALA A CA  1 
ATOM   346  C C   . ALA A 1 56  ? -11.946 -18.242 -22.178 1.00 13.77 ? 56  ALA A C   1 
ATOM   347  O O   . ALA A 1 56  ? -13.034 -18.369 -22.734 1.00 14.21 ? 56  ALA A O   1 
ATOM   348  C CB  . ALA A 1 56  ? -9.974  -17.332 -23.363 1.00 14.03 ? 56  ALA A CB  1 
ATOM   349  N N   . ARG A 1 57  ? -11.457 -19.154 -21.339 1.00 13.39 ? 57  ARG A N   1 
ATOM   350  C CA  . ARG A 1 57  ? -12.203 -20.364 -21.056 1.00 14.79 ? 57  ARG A CA  1 
ATOM   351  C C   . ARG A 1 57  ? -13.543 -20.010 -20.414 1.00 14.50 ? 57  ARG A C   1 
ATOM   352  O O   . ARG A 1 57  ? -14.563 -20.587 -20.786 1.00 16.19 ? 57  ARG A O   1 
ATOM   353  C CB  . ARG A 1 57  ? -11.420 -21.297 -20.135 1.00 16.19 ? 57  ARG A CB  1 
ATOM   354  C CG  . ARG A 1 57  ? -12.126 -22.625 -19.873 1.00 17.21 ? 57  ARG A CG  1 
ATOM   355  C CD  . ARG A 1 57  ? -12.096 -23.561 -21.051 1.00 19.36 ? 57  ARG A CD  1 
ATOM   356  N NE  . ARG A 1 57  ? -10.744 -24.075 -21.172 1.00 18.47 ? 57  ARG A NE  1 
ATOM   357  C CZ  . ARG A 1 57  ? -10.283 -24.746 -22.219 1.00 18.87 ? 57  ARG A CZ  1 
ATOM   358  N NH1 . ARG A 1 57  ? -11.050 -24.963 -23.277 1.00 19.94 ? 57  ARG A NH1 1 
ATOM   359  N NH2 . ARG A 1 57  ? -9.050  -25.210 -22.200 1.00 18.16 ? 57  ARG A NH2 1 
ATOM   360  N N   . LYS A 1 58  ? -13.527 -19.060 -19.477 1.00 15.11 ? 58  LYS A N   1 
ATOM   361  C CA  . LYS A 1 58  ? -14.768 -18.676 -18.826 1.00 15.47 ? 58  LYS A CA  1 
ATOM   362  C C   . LYS A 1 58  ? -15.765 -18.150 -19.852 1.00 16.13 ? 58  LYS A C   1 
ATOM   363  O O   . LYS A 1 58  ? -16.969 -18.439 -19.803 1.00 17.49 ? 58  LYS A O   1 
ATOM   364  C CB  . LYS A 1 58  ? -14.460 -17.601 -17.791 1.00 16.17 ? 58  LYS A CB  1 
ATOM   365  C CG  . LYS A 1 58  ? -15.667 -17.219 -16.946 1.00 17.13 ? 58  LYS A CG  1 
ATOM   366  C CD  . LYS A 1 58  ? -15.250 -16.284 -15.809 1.00 18.45 ? 58  LYS A CD  1 
ATOM   367  C CE  . LYS A 1 58  ? -16.366 -15.874 -14.956 1.00 21.36 ? 58  LYS A CE  1 
ATOM   368  N NZ  . LYS A 1 58  ? -15.982 -15.203 -13.713 1.00 23.82 ? 58  LYS A NZ  1 
ATOM   369  N N   . THR A 1 59  ? -15.263 -17.319 -20.772 1.00 15.14 ? 59  THR A N   1 
ATOM   370  C CA  . THR A 1 59  ? -16.113 -16.702 -21.765 1.00 16.32 ? 59  THR A CA  1 
ATOM   371  C C   . THR A 1 59  ? -16.687 -17.752 -22.714 1.00 16.82 ? 59  THR A C   1 
ATOM   372  O O   . THR A 1 59  ? -17.868 -17.701 -23.040 1.00 16.22 ? 59  THR A O   1 
ATOM   373  C CB  . THR A 1 59  ? -15.351 -15.624 -22.520 1.00 16.71 ? 59  THR A CB  1 
ATOM   374  O OG1 . THR A 1 59  ? -14.795 -14.714 -21.584 1.00 17.62 ? 59  THR A OG1 1 
ATOM   375  C CG2 . THR A 1 59  ? -16.261 -14.869 -23.467 1.00 18.15 ? 59  THR A CG2 1 
ATOM   376  N N   . LEU A 1 60  ? -15.839 -18.656 -23.222 1.00 16.52 ? 60  LEU A N   1 
ATOM   377  C CA  . LEU A 1 60  ? -16.299 -19.696 -24.133 1.00 16.34 ? 60  LEU A CA  1 
ATOM   378  C C   . LEU A 1 60  ? -17.363 -20.554 -23.464 1.00 17.31 ? 60  LEU A C   1 
ATOM   379  O O   . LEU A 1 60  ? -18.351 -20.902 -24.099 1.00 18.78 ? 60  LEU A O   1 
ATOM   380  C CB  . LEU A 1 60  ? -15.129 -20.555 -24.596 1.00 16.11 ? 60  LEU A CB  1 
ATOM   381  C CG  . LEU A 1 60  ? -14.127 -19.800 -25.482 1.00 15.71 ? 60  LEU A CG  1 
ATOM   382  C CD1 . LEU A 1 60  ? -12.886 -20.642 -25.672 1.00 16.16 ? 60  LEU A CD1 1 
ATOM   383  C CD2 . LEU A 1 60  ? -14.681 -19.386 -26.839 1.00 15.96 ? 60  LEU A CD2 1 
ATOM   384  N N   . LYS A 1 61  ? -17.171 -20.900 -22.184 1.00 17.67 ? 61  LYS A N   1 
ATOM   385  C CA  . LYS A 1 61  ? -18.180 -21.683 -21.480 1.00 19.15 ? 61  LYS A CA  1 
ATOM   386  C C   . LYS A 1 61  ? -19.478 -20.893 -21.326 1.00 18.82 ? 61  LYS A C   1 
ATOM   387  O O   . LYS A 1 61  ? -20.580 -21.428 -21.548 1.00 20.99 ? 61  LYS A O   1 
ATOM   388  C CB  . LYS A 1 61  ? -17.662 -22.111 -20.104 1.00 20.76 ? 61  LYS A CB  1 
ATOM   389  C CG  . LYS A 1 61  ? -16.549 -23.169 -20.115 1.00 26.27 ? 61  LYS A CG  1 
ATOM   390  C CD  . LYS A 1 61  ? -16.021 -23.402 -18.705 1.00 31.00 ? 61  LYS A CD  1 
ATOM   391  C CE  . LYS A 1 61  ? -14.975 -24.457 -18.590 1.00 36.76 ? 61  LYS A CE  1 
ATOM   392  N NZ  . LYS A 1 61  ? -14.217 -24.323 -17.331 1.00 40.79 ? 61  LYS A NZ  1 
ATOM   393  N N   . GLU A 1 62  ? -19.368 -19.601 -20.971 1.00 19.63 ? 62  GLU A N   1 
ATOM   394  C CA  . GLU A 1 62  ? -20.562 -18.805 -20.698 1.00 20.93 ? 62  GLU A CA  1 
ATOM   395  C C   . GLU A 1 62  ? -21.421 -18.608 -21.944 1.00 21.14 ? 62  GLU A C   1 
ATOM   396  O O   . GLU A 1 62  ? -22.642 -18.545 -21.863 1.00 23.26 ? 62  GLU A O   1 
ATOM   397  C CB  . GLU A 1 62  ? -20.173 -17.457 -20.101 1.00 23.60 ? 62  GLU A CB  1 
ATOM   398  C CG  . GLU A 1 62  ? -19.914 -17.574 -18.602 1.00 30.24 ? 62  GLU A CG  1 
ATOM   399  C CD  . GLU A 1 62  ? -19.667 -16.283 -17.838 1.00 35.55 ? 62  GLU A CD  1 
ATOM   400  O OE1 . GLU A 1 62  ? -19.904 -15.183 -18.386 1.00 43.24 ? 62  GLU A OE1 1 
ATOM   401  O OE2 . GLU A 1 62  ? -19.251 -16.404 -16.668 1.00 40.03 ? 62  GLU A OE2 1 
ATOM   402  N N   . GLN A 1 63  ? -20.793 -18.528 -23.117 1.00 20.02 ? 63  GLN A N   1 
ATOM   403  C CA  . GLN A 1 63  ? -21.522 -18.355 -24.362 1.00 20.95 ? 63  GLN A CA  1 
ATOM   404  C C   . GLN A 1 63  ? -21.923 -19.691 -24.991 1.00 20.30 ? 63  GLN A C   1 
ATOM   405  O O   . GLN A 1 63  ? -22.469 -19.710 -26.084 1.00 23.29 ? 63  GLN A O   1 
ATOM   406  C CB  . GLN A 1 63  ? -20.764 -17.506 -25.378 1.00 19.75 ? 63  GLN A CB  1 
ATOM   407  C CG  . GLN A 1 63  ? -19.527 -18.197 -25.954 1.00 18.02 ? 63  GLN A CG  1 
ATOM   408  C CD  . GLN A 1 63  ? -18.817 -17.314 -26.937 1.00 18.71 ? 63  GLN A CD  1 
ATOM   409  O OE1 . GLN A 1 63  ? -19.032 -16.102 -26.972 1.00 22.89 ? 63  GLN A OE1 1 
ATOM   410  N NE2 . GLN A 1 63  ? -17.944 -17.920 -27.725 1.00 17.44 ? 63  GLN A NE2 1 
ATOM   411  N N   . GLY A 1 64  ? -21.675 -20.809 -24.326 1.00 21.09 ? 64  GLY A N   1 
ATOM   412  C CA  . GLY A 1 64  ? -22.158 -22.085 -24.816 1.00 21.47 ? 64  GLY A CA  1 
ATOM   413  C C   . GLY A 1 64  ? -21.338 -22.655 -25.965 1.00 20.75 ? 64  GLY A C   1 
ATOM   414  O O   . GLY A 1 64  ? -21.859 -23.457 -26.726 1.00 23.21 ? 64  GLY A O   1 
ATOM   415  N N   . THR A 1 65  ? -20.040 -22.320 -26.015 1.00 19.14 ? 65  THR A N   1 
ATOM   416  C CA  . THR A 1 65  ? -19.158 -22.886 -27.030 1.00 19.16 ? 65  THR A CA  1 
ATOM   417  C C   . THR A 1 65  ? -17.947 -23.498 -26.353 1.00 17.74 ? 65  THR A C   1 
ATOM   418  O O   . THR A 1 65  ? -16.805 -23.139 -26.656 1.00 16.93 ? 65  THR A O   1 
ATOM   419  C CB  . THR A 1 65  ? -18.746 -21.842 -28.066 1.00 18.56 ? 65  THR A CB  1 
ATOM   420  O OG1 . THR A 1 65  ? -17.930 -20.834 -27.453 1.00 19.14 ? 65  THR A OG1 1 
ATOM   421  C CG2 . THR A 1 65  ? -19.959 -21.262 -28.774 1.00 20.55 ? 65  THR A CG2 1 
ATOM   422  N N   . PRO A 1 66  ? -18.146 -24.466 -25.435 1.00 19.12 ? 66  PRO A N   1 
ATOM   423  C CA  . PRO A 1 66  ? -17.012 -25.043 -24.719 1.00 19.81 ? 66  PRO A CA  1 
ATOM   424  C C   . PRO A 1 66  ? -16.069 -25.890 -25.578 1.00 20.65 ? 66  PRO A C   1 
ATOM   425  O O   . PRO A 1 66  ? -14.983 -26.215 -25.134 1.00 21.54 ? 66  PRO A O   1 
ATOM   426  C CB  . PRO A 1 66  ? -17.693 -25.852 -23.608 1.00 22.12 ? 66  PRO A CB  1 
ATOM   427  C CG  . PRO A 1 66  ? -18.972 -26.286 -24.266 1.00 22.48 ? 66  PRO A CG  1 
ATOM   428  C CD  . PRO A 1 66  ? -19.433 -25.064 -25.042 1.00 21.14 ? 66  PRO A CD  1 
ATOM   429  N N   . GLU A 1 67  ? -16.494 -26.222 -26.801 1.00 20.31 ? 67  GLU A N   1 
ATOM   430  C CA  . GLU A 1 67  ? -15.736 -27.105 -27.667 1.00 21.77 ? 67  GLU A CA  1 
ATOM   431  C C   . GLU A 1 67  ? -14.790 -26.281 -28.535 1.00 19.04 ? 67  GLU A C   1 
ATOM   432  O O   . GLU A 1 67  ? -13.922 -26.864 -29.159 1.00 21.41 ? 67  GLU A O   1 
ATOM   433  C CB  . GLU A 1 67  ? -16.609 -28.009 -28.543 1.00 26.39 ? 67  GLU A CB  1 
ATOM   434  C CG  . GLU A 1 67  ? -17.409 -29.028 -27.737 1.00 33.17 ? 67  GLU A CG  1 
ATOM   435  C CD  . GLU A 1 67  ? -18.182 -30.050 -28.547 1.00 41.47 ? 67  GLU A CD  1 
ATOM   436  O OE1 . GLU A 1 67  ? -18.174 -30.000 -29.795 1.00 51.44 ? 67  GLU A OE1 1 
ATOM   437  O OE2 . GLU A 1 67  ? -18.807 -30.913 -27.913 1.00 50.99 ? 67  GLU A OE2 1 
ATOM   438  N N   . ILE A 1 68  ? -14.893 -24.943 -28.530 1.00 15.79 ? 68  ILE A N   1 
ATOM   439  C CA  . ILE A 1 68  ? -13.859 -24.139 -29.171 1.00 14.50 ? 68  ILE A CA  1 
ATOM   440  C C   . ILE A 1 68  ? -12.564 -24.284 -28.376 1.00 14.07 ? 68  ILE A C   1 
ATOM   441  O O   . ILE A 1 68  ? -12.530 -24.074 -27.172 1.00 15.46 ? 68  ILE A O   1 
ATOM   442  C CB  . ILE A 1 68  ? -14.262 -22.662 -29.337 1.00 14.14 ? 68  ILE A CB  1 
ATOM   443  C CG1 . ILE A 1 68  ? -15.537 -22.537 -30.180 1.00 14.61 ? 68  ILE A CG1 1 
ATOM   444  C CG2 . ILE A 1 68  ? -13.099 -21.823 -29.860 1.00 14.75 ? 68  ILE A CG2 1 
ATOM   445  C CD1 . ILE A 1 68  ? -15.999 -21.105 -30.381 1.00 14.74 ? 68  ILE A CD1 1 
ATOM   446  N N   . ARG A 1 69  ? -11.487 -24.683 -29.060 1.00 12.47 ? 69  ARG A N   1 
ATOM   447  C CA  . ARG A 1 69  ? -10.239 -24.967 -28.393 1.00 12.74 ? 69  ARG A CA  1 
ATOM   448  C C   . ARG A 1 69  ? -9.532  -23.663 -28.053 1.00 11.94 ? 69  ARG A C   1 
ATOM   449  O O   . ARG A 1 69  ? -9.692  -22.644 -28.739 1.00 12.47 ? 69  ARG A O   1 
ATOM   450  C CB  . ARG A 1 69  ? -9.352  -25.822 -29.298 1.00 14.74 ? 69  ARG A CB  1 
ATOM   451  C CG  . ARG A 1 69  ? -10.009 -27.085 -29.858 1.00 17.95 ? 69  ARG A CG  1 
ATOM   452  C CD  . ARG A 1 69  ? -9.360  -27.456 -31.199 1.00 23.84 ? 69  ARG A CD  1 
ATOM   453  N NE  . ARG A 1 69  ? -9.871  -28.678 -31.810 1.00 29.89 ? 69  ARG A NE  1 
ATOM   454  C CZ  . ARG A 1 69  ? -10.956 -28.752 -32.566 1.00 33.65 ? 69  ARG A CZ  1 
ATOM   455  N NH1 . ARG A 1 69  ? -11.669 -27.664 -32.812 1.00 34.78 ? 69  ARG A NH1 1 
ATOM   456  N NH2 . ARG A 1 69  ? -11.323 -29.921 -33.078 1.00 37.23 ? 69  ARG A NH2 1 
ATOM   457  N N   . ILE A 1 70  ? -8.700  -23.727 -27.007 1.00 11.68 ? 70  ILE A N   1 
ATOM   458  C CA  . ILE A 1 70  ? -7.866  -22.594 -26.687 1.00 11.45 ? 70  ILE A CA  1 
ATOM   459  C C   . ILE A 1 70  ? -6.404  -22.967 -26.967 1.00 11.00 ? 70  ILE A C   1 
ATOM   460  O O   . ILE A 1 70  ? -5.843  -23.866 -26.356 1.00 11.67 ? 70  ILE A O   1 
ATOM   461  C CB  . ILE A 1 70  ? -8.016  -22.148 -25.239 1.00 12.40 ? 70  ILE A CB  1 
ATOM   462  C CG1 . ILE A 1 70  ? -9.467  -21.790 -24.938 1.00 13.16 ? 70  ILE A CG1 1 
ATOM   463  C CG2 . ILE A 1 70  ? -7.052  -20.986 -24.978 1.00 14.25 ? 70  ILE A CG2 1 
ATOM   464  C CD1 . ILE A 1 70  ? -9.739  -21.426 -23.489 1.00 13.94 ? 70  ILE A CD1 1 
ATOM   465  N N   . ALA A 1 71  ? -5.836  -22.261 -27.935 1.00 10.51 ? 71  ALA A N   1 
ATOM   466  C CA  . ALA A 1 71  ? -4.435  -22.378 -28.315 1.00 10.57 ? 71  ALA A CA  1 
ATOM   467  C C   . ALA A 1 71  ? -3.690  -21.185 -27.763 1.00 10.71 ? 71  ALA A C   1 
ATOM   468  O O   . ALA A 1 71  ? -4.240  -20.104 -27.558 1.00 11.87 ? 71  ALA A O   1 
ATOM   469  C CB  . ALA A 1 71  ? -4.328  -22.454 -29.796 1.00 11.43 ? 71  ALA A CB  1 
ATOM   470  N N   . THR A 1 72  ? -2.407  -21.411 -27.509 1.00 10.71 ? 72  THR A N   1 
ATOM   471  C CA  . THR A 1 72  ? -1.565  -20.315 -27.088 1.00 10.57 ? 72  THR A CA  1 
ATOM   472  C C   . THR A 1 72  ? -0.186  -20.521 -27.728 1.00 10.89 ? 72  THR A C   1 
ATOM   473  O O   . THR A 1 72  ? -0.004  -21.430 -28.539 1.00 12.58 ? 72  THR A O   1 
ATOM   474  C CB  . THR A 1 72  ? -1.497  -20.240 -25.564 1.00 10.86 ? 72  THR A CB  1 
ATOM   475  O OG1 . THR A 1 72  ? -0.898  -19.018 -25.179 1.00 11.56 ? 72  THR A OG1 1 
ATOM   476  C CG2 . THR A 1 72  ? -0.817  -21.448 -24.964 1.00 12.11 ? 72  THR A CG2 1 
ATOM   477  N N   . VAL A 1 73  ? 0.752   -19.650 -27.364 1.00 10.70 ? 73  VAL A N   1 
ATOM   478  C CA  . VAL A 1 73  ? 2.078   -19.623 -27.966 1.00 10.58 ? 73  VAL A CA  1 
ATOM   479  C C   . VAL A 1 73  ? 3.127   -19.605 -26.878 1.00 10.78 ? 73  VAL A C   1 
ATOM   480  O O   . VAL A 1 73  ? 2.962   -18.985 -25.840 1.00 11.43 ? 73  VAL A O   1 
ATOM   481  C CB  . VAL A 1 73  ? 2.263   -18.406 -28.882 1.00 11.34 ? 73  VAL A CB  1 
ATOM   482  C CG1 . VAL A 1 73  ? 1.432   -18.530 -30.144 1.00 12.11 ? 73  VAL A CG1 1 
ATOM   483  C CG2 . VAL A 1 73  ? 1.992   -17.083 -28.201 1.00 12.76 ? 73  VAL A CG2 1 
ATOM   484  N N   . THR A 1 74  ? 4.255   -20.288 -27.143 1.00 10.80 ? 74  THR A N   1 
ATOM   485  C CA  . THR A 1 74  ? 5.392   -20.270 -26.247 1.00 10.53 ? 74  THR A CA  1 
ATOM   486  C C   . THR A 1 74  ? 6.685   -20.192 -27.061 1.00 10.43 ? 74  THR A C   1 
ATOM   487  O O   . THR A 1 74  ? 6.706   -20.449 -28.262 1.00 10.19 ? 74  THR A O   1 
ATOM   488  C CB  . THR A 1 74  ? 5.410   -21.486 -25.347 1.00 10.69 ? 74  THR A CB  1 
ATOM   489  O OG1 . THR A 1 74  ? 5.517   -22.665 -26.114 1.00 11.89 ? 74  THR A OG1 1 
ATOM   490  C CG2 . THR A 1 74  ? 4.162   -21.576 -24.483 1.00 10.83 ? 74  THR A CG2 1 
ATOM   491  N N   . ASN A 1 75  ? 7.751   -19.849 -26.361 1.00 11.38 ? 75  ASN A N   1 
ATOM   492  C CA  . ASN A 1 75  ? 9.032   -19.565 -27.025 1.00 11.07 ? 75  ASN A CA  1 
ATOM   493  C C   . ASN A 1 75  ? 8.843   -18.520 -28.116 1.00 11.22 ? 75  ASN A C   1 
ATOM   494  O O   . ASN A 1 75  ? 9.536   -18.556 -29.155 1.00 11.61 ? 75  ASN A O   1 
ATOM   495  C CB  . ASN A 1 75  ? 9.697   -20.840 -27.521 1.00 11.22 ? 75  ASN A CB  1 
ATOM   496  C CG  . ASN A 1 75  ? 11.206  -20.709 -27.586 1.00 11.63 ? 75  ASN A CG  1 
ATOM   497  O OD1 . ASN A 1 75  ? 11.814  -20.075 -26.722 1.00 12.75 ? 75  ASN A OD1 1 
ATOM   498  N ND2 . ASN A 1 75  ? 11.809  -21.313 -28.604 1.00 11.75 ? 75  ASN A ND2 1 
ATOM   499  N N   . PHE A 1 76  ? 7.954   -17.565 -27.913 1.00 11.70 ? 76  PHE A N   1 
ATOM   500  C CA  . PHE A 1 76  ? 7.337   -16.796 -28.962 1.00 11.47 ? 76  PHE A CA  1 
ATOM   501  C C   . PHE A 1 76  ? 7.563   -15.306 -28.813 1.00 13.36 ? 76  PHE A C   1 
ATOM   502  O O   . PHE A 1 76  ? 7.431   -14.759 -27.710 1.00 15.23 ? 76  PHE A O   1 
ATOM   503  C CB  . PHE A 1 76  ? 5.843   -17.116 -28.964 1.00 11.73 ? 76  PHE A CB  1 
ATOM   504  C CG  . PHE A 1 76  ? 5.025   -16.377 -29.999 1.00 12.23 ? 76  PHE A CG  1 
ATOM   505  C CD1 . PHE A 1 76  ? 4.555   -15.081 -29.767 1.00 13.04 ? 76  PHE A CD1 1 
ATOM   506  C CD2 . PHE A 1 76  ? 4.658   -17.010 -31.179 1.00 13.13 ? 76  PHE A CD2 1 
ATOM   507  C CE1 . PHE A 1 76  ? 3.806   -14.437 -30.720 1.00 13.17 ? 76  PHE A CE1 1 
ATOM   508  C CE2 . PHE A 1 76  ? 3.877   -16.354 -32.112 1.00 13.73 ? 76  PHE A CE2 1 
ATOM   509  C CZ  . PHE A 1 76  ? 3.484   -15.064 -31.885 1.00 13.42 ? 76  PHE A CZ  1 
ATOM   510  N N   . PRO A 1 77  ? 7.815   -14.559 -29.918 1.00 13.59 ? 77  PRO A N   1 
ATOM   511  C CA  . PRO A 1 77  ? 7.934   -15.086 -31.283 1.00 13.41 ? 77  PRO A CA  1 
ATOM   512  C C   . PRO A 1 77  ? 9.359   -15.453 -31.674 1.00 12.89 ? 77  PRO A C   1 
ATOM   513  O O   . PRO A 1 77  ? 9.592   -15.880 -32.799 1.00 13.65 ? 77  PRO A O   1 
ATOM   514  C CB  . PRO A 1 77  ? 7.450   -13.886 -32.106 1.00 15.59 ? 77  PRO A CB  1 
ATOM   515  C CG  . PRO A 1 77  ? 7.977   -12.693 -31.366 1.00 15.28 ? 77  PRO A CG  1 
ATOM   516  C CD  . PRO A 1 77  ? 7.783   -13.093 -29.905 1.00 14.75 ? 77  PRO A CD  1 
ATOM   517  N N   . HIS A 1 78  ? 10.285  -15.314 -30.729 1.00 12.59 ? 78  HIS A N   1 
ATOM   518  C CA  . HIS A 1 78  ? 11.705  -15.322 -31.025 1.00 12.25 ? 78  HIS A CA  1 
ATOM   519  C C   . HIS A 1 78  ? 12.250  -16.666 -31.454 1.00 12.28 ? 78  HIS A C   1 
ATOM   520  O O   . HIS A 1 78  ? 13.246  -16.687 -32.207 1.00 13.57 ? 78  HIS A O   1 
ATOM   521  C CB  . HIS A 1 78  ? 12.461  -14.816 -29.810 1.00 13.75 ? 78  HIS A CB  1 
ATOM   522  C CG  . HIS A 1 78  ? 12.006  -15.418 -28.534 1.00 13.98 ? 78  HIS A CG  1 
ATOM   523  N ND1 . HIS A 1 78  ? 12.249  -16.724 -28.151 1.00 13.06 ? 78  HIS A ND1 1 
ATOM   524  C CD2 . HIS A 1 78  ? 11.218  -14.865 -27.562 1.00 15.31 ? 78  HIS A CD2 1 
ATOM   525  C CE1 . HIS A 1 78  ? 11.658  -16.936 -26.959 1.00 13.98 ? 78  HIS A CE1 1 
ATOM   526  N NE2 . HIS A 1 78  ? 11.038  -15.816 -26.593 1.00 15.48 ? 78  HIS A NE2 1 
ATOM   527  N N   . GLY A 1 79  ? 11.736  -17.791 -31.019 1.00 12.63 ? 79  GLY A N   1 
ATOM   528  C CA  . GLY A 1 79  ? 12.353  -19.070 -31.339 1.00 11.98 ? 79  GLY A CA  1 
ATOM   529  C C   . GLY A 1 79  ? 13.769  -19.165 -30.786 1.00 12.38 ? 79  GLY A C   1 
ATOM   530  O O   . GLY A 1 79  ? 14.665  -19.720 -31.427 1.00 13.01 ? 79  GLY A O   1 
ATOM   531  N N   . ASN A 1 80  ? 13.982  -18.669 -29.580 1.00 12.59 ? 80  ASN A N   1 
ATOM   532  C CA  . ASN A 1 80  ? 15.262  -18.829 -28.928 1.00 13.09 ? 80  ASN A CA  1 
ATOM   533  C C   . ASN A 1 80  ? 15.549  -20.310 -28.665 1.00 12.87 ? 80  ASN A C   1 
ATOM   534  O O   . ASN A 1 80  ? 14.677  -21.160 -28.717 1.00 13.38 ? 80  ASN A O   1 
ATOM   535  C CB  . ASN A 1 80  ? 15.318  -18.058 -27.613 1.00 13.10 ? 80  ASN A CB  1 
ATOM   536  C CG  . ASN A 1 80  ? 15.368  -16.563 -27.794 1.00 15.11 ? 80  ASN A CG  1 
ATOM   537  O OD1 . ASN A 1 80  ? 15.643  -16.034 -28.879 1.00 17.82 ? 80  ASN A OD1 1 
ATOM   538  N ND2 . ASN A 1 80  ? 15.090  -15.853 -26.717 1.00 17.34 ? 80  ASN A ND2 1 
ATOM   539  N N   . ASP A 1 81  ? 16.813  -20.632 -28.378 1.00 14.55 ? 81  ASP A N   1 
ATOM   540  C CA  . ASP A 1 81  ? 17.267  -22.011 -28.253 1.00 14.41 ? 81  ASP A CA  1 
ATOM   541  C C   . ASP A 1 81  ? 17.547  -22.403 -26.803 1.00 14.53 ? 81  ASP A C   1 
ATOM   542  O O   . ASP A 1 81  ? 18.328  -23.323 -26.561 1.00 16.86 ? 81  ASP A O   1 
ATOM   543  C CB  . ASP A 1 81  ? 18.467  -22.273 -29.146 1.00 16.87 ? 81  ASP A CB  1 
ATOM   544  C CG  . ASP A 1 81  ? 19.675  -21.422 -28.821 1.00 19.58 ? 81  ASP A CG  1 
ATOM   545  O OD1 . ASP A 1 81  ? 19.619  -20.628 -27.888 1.00 23.93 ? 81  ASP A OD1 1 
ATOM   546  O OD2 . ASP A 1 81  ? 20.699  -21.569 -29.487 1.00 24.88 ? 81  ASP A OD2 1 
ATOM   547  N N   . ASP A 1 82  ? 16.878  -21.727 -25.845 1.00 13.96 ? 82  ASP A N   1 
ATOM   548  C CA  . ASP A 1 82  ? 16.967  -22.089 -24.444 1.00 14.44 ? 82  ASP A CA  1 
ATOM   549  C C   . ASP A 1 82  ? 15.810  -23.029 -24.112 1.00 12.51 ? 82  ASP A C   1 
ATOM   550  O O   . ASP A 1 82  ? 14.646  -22.595 -24.023 1.00 12.99 ? 82  ASP A O   1 
ATOM   551  C CB  . ASP A 1 82  ? 16.965  -20.864 -23.547 1.00 14.88 ? 82  ASP A CB  1 
ATOM   552  C CG  . ASP A 1 82  ? 17.227  -21.177 -22.087 1.00 16.28 ? 82  ASP A CG  1 
ATOM   553  O OD1 . ASP A 1 82  ? 16.651  -22.190 -21.598 1.00 17.31 ? 82  ASP A OD1 1 
ATOM   554  O OD2 . ASP A 1 82  ? 17.937  -20.375 -21.454 1.00 20.93 ? 82  ASP A OD2 1 
ATOM   555  N N   . ILE A 1 83  ? 16.127  -24.310 -24.024 1.00 13.54 ? 83  ILE A N   1 
ATOM   556  C CA  . ILE A 1 83  ? 15.133  -25.348 -23.860 1.00 12.94 ? 83  ILE A CA  1 
ATOM   557  C C   . ILE A 1 83  ? 14.405  -25.151 -22.538 1.00 13.25 ? 83  ILE A C   1 
ATOM   558  O O   . ILE A 1 83  ? 13.192  -25.322 -22.444 1.00 14.96 ? 83  ILE A O   1 
ATOM   559  C CB  . ILE A 1 83  ? 15.724  -26.752 -23.981 1.00 14.78 ? 83  ILE A CB  1 
ATOM   560  C CG1 . ILE A 1 83  ? 16.282  -26.981 -25.374 1.00 15.94 ? 83  ILE A CG1 1 
ATOM   561  C CG2 . ILE A 1 83  ? 14.697  -27.817 -23.604 1.00 16.13 ? 83  ILE A CG2 1 
ATOM   562  C CD1 . ILE A 1 83  ? 17.100  -28.246 -25.472 1.00 19.29 ? 83  ILE A CD1 1 
ATOM   563  N N   . GLU A 1 84  ? 15.145  -24.866 -21.471 1.00 14.52 ? 84  GLU A N   1 
ATOM   564  C CA  . GLU A 1 84  ? 14.538  -24.732 -20.157 1.00 15.38 ? 84  GLU A CA  1 
ATOM   565  C C   . GLU A 1 84  ? 13.521  -23.597 -20.120 1.00 14.36 ? 84  GLU A C   1 
ATOM   566  O O   . GLU A 1 84  ? 12.448  -23.740 -19.505 1.00 15.72 ? 84  GLU A O   1 
ATOM   567  C CB  . GLU A 1 84  ? 15.592  -24.504 -19.085 1.00 17.55 ? 84  GLU A CB  1 
ATOM   568  C CG  . GLU A 1 84  ? 16.464  -25.737 -18.871 1.00 22.76 ? 84  GLU A CG  1 
ATOM   569  C CD  . GLU A 1 84  ? 17.724  -25.506 -18.046 1.00 33.80 ? 84  GLU A CD  1 
ATOM   570  O OE1 . GLU A 1 84  ? 17.808  -25.978 -16.901 1.00 43.78 ? 84  GLU A OE1 1 
ATOM   571  O OE2 . GLU A 1 84  ? 18.658  -24.861 -18.575 1.00 46.21 ? 84  GLU A OE2 1 
ATOM   572  N N   . ILE A 1 85  ? 13.791  -22.491 -20.816 1.00 13.33 ? 85  ILE A N   1 
ATOM   573  C CA  . ILE A 1 85  ? 12.810  -21.419 -20.847 1.00 13.48 ? 85  ILE A CA  1 
ATOM   574  C C   . ILE A 1 85  ? 11.596  -21.838 -21.667 1.00 13.34 ? 85  ILE A C   1 
ATOM   575  O O   . ILE A 1 85  ? 10.457  -21.614 -21.258 1.00 13.63 ? 85  ILE A O   1 
ATOM   576  C CB  . ILE A 1 85  ? 13.444  -20.111 -21.326 1.00 14.43 ? 85  ILE A CB  1 
ATOM   577  C CG1 . ILE A 1 85  ? 14.426  -19.590 -20.300 1.00 14.99 ? 85  ILE A CG1 1 
ATOM   578  C CG2 . ILE A 1 85  ? 12.405  -19.067 -21.712 1.00 16.01 ? 85  ILE A CG2 1 
ATOM   579  C CD1 . ILE A 1 85  ? 15.096  -18.281 -20.688 1.00 17.70 ? 85  ILE A CD1 1 
ATOM   580  N N   . ALA A 1 86  ? 11.811  -22.424 -22.854 1.00 12.55 ? 86  ALA A N   1 
ATOM   581  C CA  . ALA A 1 86  ? 10.689  -22.853 -23.666 1.00 12.49 ? 86  ALA A CA  1 
ATOM   582  C C   . ALA A 1 86  ? 9.822   -23.846 -22.908 1.00 11.69 ? 86  ALA A C   1 
ATOM   583  O O   . ALA A 1 86  ? 8.594   -23.806 -22.998 1.00 12.50 ? 86  ALA A O   1 
ATOM   584  C CB  . ALA A 1 86  ? 11.197  -23.443 -24.969 1.00 13.35 ? 86  ALA A CB  1 
ATOM   585  N N   . LEU A 1 87  ? 10.446  -24.762 -22.197 1.00 12.26 ? 87  LEU A N   1 
ATOM   586  C CA  . LEU A 1 87  ? 9.721   -25.767 -21.429 1.00 12.53 ? 87  LEU A CA  1 
ATOM   587  C C   . LEU A 1 87  ? 8.937   -25.133 -20.281 1.00 12.04 ? 87  LEU A C   1 
ATOM   588  O O   . LEU A 1 87  ? 7.796   -25.507 -20.080 1.00 12.05 ? 87  LEU A O   1 
ATOM   589  C CB  . LEU A 1 87  ? 10.708  -26.821 -20.920 1.00 14.00 ? 87  LEU A CB  1 
ATOM   590  C CG  . LEU A 1 87  ? 10.098  -27.970 -20.108 1.00 14.36 ? 87  LEU A CG  1 
ATOM   591  C CD1 . LEU A 1 87  ? 9.029   -28.699 -20.854 1.00 14.84 ? 87  LEU A CD1 1 
ATOM   592  C CD2 . LEU A 1 87  ? 11.199  -28.918 -19.665 1.00 16.78 ? 87  LEU A CD2 1 
ATOM   593  N N   . ALA A 1 88  ? 9.538   -24.199 -19.544 1.00 12.11 ? 88  ALA A N   1 
ATOM   594  C CA  . ALA A 1 88  ? 8.827   -23.535 -18.459 1.00 12.04 ? 88  ALA A CA  1 
ATOM   595  C C   . ALA A 1 88  ? 7.590   -22.827 -18.992 1.00 11.59 ? 88  ALA A C   1 
ATOM   596  O O   . ALA A 1 88  ? 6.506   -22.907 -18.417 1.00 12.39 ? 88  ALA A O   1 
ATOM   597  C CB  . ALA A 1 88  ? 9.756   -22.574 -17.768 1.00 12.74 ? 88  ALA A CB  1 
ATOM   598  N N   . GLU A 1 89  ? 7.739   -22.152 -20.130 1.00 11.32 ? 89  GLU A N   1 
ATOM   599  C CA  . GLU A 1 89  ? 6.631   -21.420 -20.711 1.00 10.85 ? 89  GLU A CA  1 
ATOM   600  C C   . GLU A 1 89  ? 5.534   -22.404 -21.139 1.00 11.07 ? 89  GLU A C   1 
ATOM   601  O O   . GLU A 1 89  ? 4.335   -22.152 -20.971 1.00 11.44 ? 89  GLU A O   1 
ATOM   602  C CB  . GLU A 1 89  ? 7.078   -20.584 -21.903 1.00 11.52 ? 89  GLU A CB  1 
ATOM   603  C CG  . GLU A 1 89  ? 7.982   -19.427 -21.508 1.00 12.90 ? 89  GLU A CG  1 
ATOM   604  C CD  . GLU A 1 89  ? 8.354   -18.487 -22.646 1.00 14.60 ? 89  GLU A CD  1 
ATOM   605  O OE1 . GLU A 1 89  ? 8.146   -18.899 -23.812 1.00 18.45 ? 89  GLU A OE1 1 
ATOM   606  O OE2 . GLU A 1 89  ? 8.870   -17.391 -22.394 1.00 16.02 ? 89  GLU A OE2 1 
ATOM   607  N N   . THR A 1 90  ? 5.919   -23.536 -21.717 1.00 10.53 ? 90  THR A N   1 
ATOM   608  C CA  . THR A 1 90  ? 4.997   -24.561 -22.157 1.00 10.94 ? 90  THR A CA  1 
ATOM   609  C C   . THR A 1 90  ? 4.259   -25.138 -20.947 1.00 11.14 ? 90  THR A C   1 
ATOM   610  O O   . THR A 1 90  ? 3.037   -25.317 -21.006 1.00 11.34 ? 90  THR A O   1 
ATOM   611  C CB  . THR A 1 90  ? 5.732   -25.609 -22.997 1.00 11.73 ? 90  THR A CB  1 
ATOM   612  O OG1 . THR A 1 90  ? 6.207   -24.942 -24.164 1.00 12.27 ? 90  THR A OG1 1 
ATOM   613  C CG2 . THR A 1 90  ? 4.791   -26.728 -23.414 1.00 11.72 ? 90  THR A CG2 1 
ATOM   614  N N   . ARG A 1 91  ? 4.976   -25.461 -19.882 1.00 11.02 ? 91  ARG A N   1 
ATOM   615  C CA  . ARG A 1 91  ? 4.346   -25.975 -18.671 1.00 11.55 ? 91  ARG A CA  1 
ATOM   616  C C   . ARG A 1 91  ? 3.372   -24.950 -18.129 1.00 10.86 ? 91  ARG A C   1 
ATOM   617  O O   . ARG A 1 91  ? 2.284   -25.320 -17.668 1.00 11.38 ? 91  ARG A O   1 
ATOM   618  C CB  . ARG A 1 91  ? 5.426   -26.344 -17.660 1.00 12.28 ? 91  ARG A CB  1 
ATOM   619  C CG  . ARG A 1 91  ? 6.192   -27.599 -18.065 1.00 14.31 ? 91  ARG A CG  1 
ATOM   620  C CD  . ARG A 1 91  ? 7.286   -27.876 -17.052 1.00 17.87 ? 91  ARG A CD  1 
ATOM   621  N NE  . ARG A 1 91  ? 7.881   -29.183 -17.207 1.00 20.00 ? 91  ARG A NE  1 
ATOM   622  C CZ  . ARG A 1 91  ? 9.074   -29.551 -16.737 1.00 23.89 ? 91  ARG A CZ  1 
ATOM   623  N NH1 . ARG A 1 91  ? 9.858   -28.691 -16.112 1.00 30.11 ? 91  ARG A NH1 1 
ATOM   624  N NH2 . ARG A 1 91  ? 9.470   -30.791 -16.901 1.00 27.53 ? 91  ARG A NH2 1 
ATOM   625  N N   . ALA A 1 92  ? 3.720   -23.672 -18.155 1.00 10.51 ? 92  ALA A N   1 
ATOM   626  C CA  . ALA A 1 92  ? 2.806   -22.634 -17.680 1.00 10.78 ? 92  ALA A CA  1 
ATOM   627  C C   . ALA A 1 92  ? 1.556   -22.568 -18.543 1.00 10.24 ? 92  ALA A C   1 
ATOM   628  O O   . ALA A 1 92  ? 0.432   -22.480 -18.033 1.00 11.30 ? 92  ALA A O   1 
ATOM   629  C CB  . ALA A 1 92  ? 3.455   -21.292 -17.611 1.00 11.31 ? 92  ALA A CB  1 
ATOM   630  N N   . ALA A 1 93  ? 1.699   -22.627 -19.868 1.00 10.64 ? 93  ALA A N   1 
ATOM   631  C CA  . ALA A 1 93  ? 0.561   -22.611 -20.763 1.00 10.68 ? 93  ALA A CA  1 
ATOM   632  C C   . ALA A 1 93  ? -0.371  -23.764 -20.422 1.00 10.59 ? 93  ALA A C   1 
ATOM   633  O O   . ALA A 1 93  ? -1.594  -23.607 -20.415 1.00 11.58 ? 93  ALA A O   1 
ATOM   634  C CB  . ALA A 1 93  ? 1.047   -22.710 -22.202 1.00 10.76 ? 93  ALA A CB  1 
ATOM   635  N N   . ILE A 1 94  ? 0.185   -24.954 -20.219 1.00 10.47 ? 94  ILE A N   1 
ATOM   636  C CA  . ILE A 1 94  ? -0.613  -26.113 -19.849 1.00 11.33 ? 94  ILE A CA  1 
ATOM   637  C C   . ILE A 1 94  ? -1.346  -25.820 -18.532 1.00 10.90 ? 94  ILE A C   1 
ATOM   638  O O   . ILE A 1 94  ? -2.563  -26.070 -18.391 1.00 12.15 ? 94  ILE A O   1 
ATOM   639  C CB  . ILE A 1 94  ? 0.278   -27.354 -19.728 1.00 12.23 ? 94  ILE A CB  1 
ATOM   640  C CG1 . ILE A 1 94  ? 0.812   -27.742 -21.087 1.00 12.19 ? 94  ILE A CG1 1 
ATOM   641  C CG2 . ILE A 1 94  ? -0.471  -28.512 -19.062 1.00 13.24 ? 94  ILE A CG2 1 
ATOM   642  C CD1 . ILE A 1 94  ? 1.953   -28.740 -21.022 1.00 13.85 ? 94  ILE A CD1 1 
ATOM   643  N N   . ALA A 1 95  ? -0.630  -25.285 -17.544 1.00 11.39 ? 95  ALA A N   1 
ATOM   644  C CA  . ALA A 1 95  ? -1.204  -25.047 -16.220 1.00 12.00 ? 95  ALA A CA  1 
ATOM   645  C C   . ALA A 1 95  ? -2.304  -24.001 -16.289 1.00 12.53 ? 95  ALA A C   1 
ATOM   646  O O   . ALA A 1 95  ? -3.279  -24.072 -15.514 1.00 13.81 ? 95  ALA A O   1 
ATOM   647  C CB  . ALA A 1 95  ? -0.130  -24.624 -15.267 1.00 12.41 ? 95  ALA A CB  1 
ATOM   648  N N   . TYR A 1 96  ? -2.202  -23.015 -17.146 1.00 12.51 ? 96  TYR A N   1 
ATOM   649  C CA  . TYR A 1 96  ? -3.240  -22.016 -17.344 1.00 11.89 ? 96  TYR A CA  1 
ATOM   650  C C   . TYR A 1 96  ? -4.516  -22.638 -17.906 1.00 12.65 ? 96  TYR A C   1 
ATOM   651  O O   . TYR A 1 96  ? -5.593  -22.087 -17.711 1.00 14.71 ? 96  TYR A O   1 
ATOM   652  C CB  . TYR A 1 96  ? -2.854  -20.899 -18.299 1.00 11.39 ? 96  TYR A CB  1 
ATOM   653  C CG  . TYR A 1 96  ? -2.035  -19.753 -17.745 1.00 11.25 ? 96  TYR A CG  1 
ATOM   654  C CD1 . TYR A 1 96  ? -2.541  -18.861 -16.814 1.00 11.65 ? 96  TYR A CD1 1 
ATOM   655  C CD2 . TYR A 1 96  ? -0.759  -19.481 -18.238 1.00 11.66 ? 96  TYR A CD2 1 
ATOM   656  C CE1 . TYR A 1 96  ? -1.824  -17.772 -16.378 1.00 11.67 ? 96  TYR A CE1 1 
ATOM   657  C CE2 . TYR A 1 96  ? -0.056  -18.375 -17.834 1.00 11.33 ? 96  TYR A CE2 1 
ATOM   658  C CZ  . TYR A 1 96  ? -0.558  -17.515 -16.885 1.00 11.47 ? 96  TYR A CZ  1 
ATOM   659  O OH  . TYR A 1 96  ? 0.151   -16.425 -16.470 1.00 13.00 ? 96  TYR A OH  1 
ATOM   660  N N   . GLY A 1 97  ? -4.393  -23.761 -18.611 1.00 11.81 ? 97  GLY A N   1 
ATOM   661  C CA  . GLY A 1 97  ? -5.520  -24.478 -19.187 1.00 12.11 ? 97  GLY A CA  1 
ATOM   662  C C   . GLY A 1 97  ? -5.508  -24.596 -20.705 1.00 12.28 ? 97  GLY A C   1 
ATOM   663  O O   . GLY A 1 97  ? -6.546  -24.894 -21.268 1.00 12.70 ? 97  GLY A O   1 
ATOM   664  N N   . ALA A 1 98  ? -4.365  -24.387 -21.378 1.00 11.48 ? 98  ALA A N   1 
ATOM   665  C CA  . ALA A 1 98  ? -4.373  -24.493 -22.827 1.00 10.75 ? 98  ALA A CA  1 
ATOM   666  C C   . ALA A 1 98  ? -4.885  -25.861 -23.266 1.00 10.75 ? 98  ALA A C   1 
ATOM   667  O O   . ALA A 1 98  ? -4.532  -26.895 -22.704 1.00 11.84 ? 98  ALA A O   1 
ATOM   668  C CB  . ALA A 1 98  ? -2.980  -24.276 -23.365 1.00 11.29 ? 98  ALA A CB  1 
ATOM   669  N N   . ASP A 1 99  ? -5.560  -25.879 -24.409 1.00 10.91 ? 99  ASP A N   1 
ATOM   670  C CA  . ASP A 1 99  ? -5.804  -27.120 -25.137 1.00 10.94 ? 99  ASP A CA  1 
ATOM   671  C C   . ASP A 1 99  ? -4.667  -27.447 -26.114 1.00 10.55 ? 99  ASP A C   1 
ATOM   672  O O   . ASP A 1 99  ? -4.475  -28.608 -26.427 1.00 11.63 ? 99  ASP A O   1 
ATOM   673  C CB  . ASP A 1 99  ? -7.111  -27.054 -25.918 1.00 11.52 ? 99  ASP A CB  1 
ATOM   674  C CG  . ASP A 1 99  ? -8.334  -26.849 -25.030 1.00 12.36 ? 99  ASP A CG  1 
ATOM   675  O OD1 . ASP A 1 99  ? -8.431  -27.579 -24.016 1.00 14.97 ? 99  ASP A OD1 1 
ATOM   676  O OD2 . ASP A 1 99  ? -9.113  -25.930 -25.337 1.00 13.64 ? 99  ASP A OD2 1 
ATOM   677  N N   . GLU A 1 100 ? -4.030  -26.389 -26.591 1.00 10.57 ? 100 GLU A N   1 
ATOM   678  C CA  . GLU A 1 100 ? -2.980  -26.530 -27.609 1.00 10.62 ? 100 GLU A CA  1 
ATOM   679  C C   . GLU A 1 100 ? -1.938  -25.471 -27.318 1.00 10.03 ? 100 GLU A C   1 
ATOM   680  O O   . GLU A 1 100 ? -2.241  -24.349 -26.954 1.00 9.92  ? 100 GLU A O   1 
ATOM   681  C CB  . GLU A 1 100 ? -3.537  -26.294 -29.001 1.00 11.18 ? 100 GLU A CB  1 
ATOM   682  C CG  . GLU A 1 100 ? -4.778  -27.133 -29.295 1.00 12.50 ? 100 GLU A CG  1 
ATOM   683  C CD  . GLU A 1 100 ? -5.340  -27.018 -30.699 1.00 13.78 ? 100 GLU A CD  1 
ATOM   684  O OE1 . GLU A 1 100 ? -4.981  -26.054 -31.429 1.00 14.10 ? 100 GLU A OE1 1 
ATOM   685  O OE2 . GLU A 1 100 ? -6.213  -27.860 -31.031 1.00 16.22 ? 100 GLU A OE2 1 
ATOM   686  N N   . VAL A 1 101 ? -0.678  -25.833 -27.593 1.00 9.71  ? 101 VAL A N   1 
ATOM   687  C CA  . VAL A 1 101 ? 0.445   -24.929 -27.464 1.00 10.18 ? 101 VAL A CA  1 
ATOM   688  C C   . VAL A 1 101 ? 1.194   -24.901 -28.790 1.00 10.50 ? 101 VAL A C   1 
ATOM   689  O O   . VAL A 1 101 ? 1.508   -25.976 -29.307 1.00 10.90 ? 101 VAL A O   1 
ATOM   690  C CB  . VAL A 1 101 ? 1.390   -25.392 -26.359 1.00 10.70 ? 101 VAL A CB  1 
ATOM   691  C CG1 . VAL A 1 101 ? 2.673   -24.564 -26.316 1.00 12.69 ? 101 VAL A CG1 1 
ATOM   692  C CG2 . VAL A 1 101 ? 0.709   -25.336 -25.030 1.00 10.31 ? 101 VAL A CG2 1 
ATOM   693  N N   . ASP A 1 102 ? 1.407   -23.681 -29.275 1.00 10.86 ? 102 ASP A N   1 
ATOM   694  C CA  . ASP A 1 102 ? 2.185   -23.488 -30.512 1.00 11.09 ? 102 ASP A CA  1 
ATOM   695  C C   . ASP A 1 102 ? 3.538   -22.929 -30.079 1.00 10.76 ? 102 ASP A C   1 
ATOM   696  O O   . ASP A 1 102 ? 3.649   -21.771 -29.696 1.00 10.95 ? 102 ASP A O   1 
ATOM   697  C CB  . ASP A 1 102 ? 1.480   -22.509 -31.437 1.00 11.14 ? 102 ASP A CB  1 
ATOM   698  C CG  . ASP A 1 102 ? 0.074   -22.870 -31.931 1.00 12.26 ? 102 ASP A CG  1 
ATOM   699  O OD1 . ASP A 1 102 ? -0.537  -23.852 -31.422 1.00 13.15 ? 102 ASP A OD1 1 
ATOM   700  O OD2 . ASP A 1 102 ? -0.415  -22.148 -32.827 1.00 15.05 ? 102 ASP A OD2 1 
ATOM   701  N N   . VAL A 1 103 ? 4.568   -23.770 -30.142 1.00 10.46 ? 103 VAL A N   1 
ATOM   702  C CA  . VAL A 1 103 ? 5.918   -23.388 -29.725 1.00 10.63 ? 103 VAL A CA  1 
ATOM   703  C C   . VAL A 1 103 ? 6.744   -22.999 -30.950 1.00 9.77  ? 103 VAL A C   1 
ATOM   704  O O   . VAL A 1 103 ? 6.590   -23.630 -31.992 1.00 10.66 ? 103 VAL A O   1 
ATOM   705  C CB  . VAL A 1 103 ? 6.596   -24.528 -28.943 1.00 10.71 ? 103 VAL A CB  1 
ATOM   706  C CG1 . VAL A 1 103 ? 6.874   -25.763 -29.790 1.00 12.13 ? 103 VAL A CG1 1 
ATOM   707  C CG2 . VAL A 1 103 ? 7.867   -24.044 -28.291 1.00 11.67 ? 103 VAL A CG2 1 
ATOM   708  N N   . VAL A 1 104 ? 7.584   -21.976 -30.787 1.00 10.42 ? 104 VAL A N   1 
ATOM   709  C CA  . VAL A 1 104 ? 8.476   -21.612 -31.904 1.00 10.70 ? 104 VAL A CA  1 
ATOM   710  C C   . VAL A 1 104 ? 9.714   -22.494 -31.841 1.00 10.22 ? 104 VAL A C   1 
ATOM   711  O O   . VAL A 1 104 ? 10.455  -22.494 -30.885 1.00 11.13 ? 104 VAL A O   1 
ATOM   712  C CB  . VAL A 1 104 ? 8.817   -20.112 -31.927 1.00 10.68 ? 104 VAL A CB  1 
ATOM   713  C CG1 . VAL A 1 104 ? 9.586   -19.769 -33.211 1.00 11.37 ? 104 VAL A CG1 1 
ATOM   714  C CG2 . VAL A 1 104 ? 7.559   -19.269 -31.817 1.00 10.66 ? 104 VAL A CG2 1 
ATOM   715  N N   . PHE A 1 105 ? 9.981   -23.143 -32.994 1.00 11.16 ? 105 PHE A N   1 
ATOM   716  C CA  . PHE A 1 105 ? 11.194  -23.916 -33.230 1.00 11.05 ? 105 PHE A CA  1 
ATOM   717  C C   . PHE A 1 105 ? 12.398  -22.980 -33.195 1.00 11.45 ? 105 PHE A C   1 
ATOM   718  O O   . PHE A 1 105 ? 12.306  -21.832 -33.628 1.00 11.74 ? 105 PHE A O   1 
ATOM   719  C CB  . PHE A 1 105 ? 11.070  -24.514 -34.636 1.00 11.58 ? 105 PHE A CB  1 
ATOM   720  C CG  . PHE A 1 105 ? 12.156  -25.506 -34.992 1.00 11.69 ? 105 PHE A CG  1 
ATOM   721  C CD1 . PHE A 1 105 ? 11.998  -26.841 -34.734 1.00 12.98 ? 105 PHE A CD1 1 
ATOM   722  C CD2 . PHE A 1 105 ? 13.323  -25.097 -35.633 1.00 13.41 ? 105 PHE A CD2 1 
ATOM   723  C CE1 . PHE A 1 105 ? 12.986  -27.745 -35.026 1.00 13.75 ? 105 PHE A CE1 1 
ATOM   724  C CE2 . PHE A 1 105 ? 14.297  -26.021 -35.967 1.00 14.40 ? 105 PHE A CE2 1 
ATOM   725  C CZ  . PHE A 1 105 ? 14.124  -27.330 -35.660 1.00 13.96 ? 105 PHE A CZ  1 
ATOM   726  N N   . PRO A 1 106 ? 13.560  -23.464 -32.708 1.00 12.05 ? 106 PRO A N   1 
ATOM   727  C CA  . PRO A 1 106 ? 14.778  -22.656 -32.707 1.00 12.53 ? 106 PRO A CA  1 
ATOM   728  C C   . PRO A 1 106 ? 15.391  -22.634 -34.097 1.00 12.20 ? 106 PRO A C   1 
ATOM   729  O O   . PRO A 1 106 ? 16.406  -23.289 -34.370 1.00 12.83 ? 106 PRO A O   1 
ATOM   730  C CB  . PRO A 1 106 ? 15.646  -23.327 -31.653 1.00 12.70 ? 106 PRO A CB  1 
ATOM   731  C CG  . PRO A 1 106 ? 15.233  -24.777 -31.686 1.00 12.56 ? 106 PRO A CG  1 
ATOM   732  C CD  . PRO A 1 106 ? 13.740  -24.735 -31.994 1.00 12.01 ? 106 PRO A CD  1 
ATOM   733  N N   . TYR A 1 107 ? 14.788  -21.820 -34.943 1.00 12.36 ? 107 TYR A N   1 
ATOM   734  C CA  . TYR A 1 107 ? 15.134  -21.817 -36.360 1.00 12.45 ? 107 TYR A CA  1 
ATOM   735  C C   . TYR A 1 107 ? 16.492  -21.175 -36.560 1.00 13.33 ? 107 TYR A C   1 
ATOM   736  O O   . TYR A 1 107 ? 17.221  -21.587 -37.476 1.00 14.63 ? 107 TYR A O   1 
ATOM   737  C CB  . TYR A 1 107 ? 14.016  -21.183 -37.181 1.00 12.32 ? 107 TYR A CB  1 
ATOM   738  C CG  . TYR A 1 107 ? 13.697  -19.740 -36.833 1.00 11.96 ? 107 TYR A CG  1 
ATOM   739  C CD1 . TYR A 1 107 ? 14.402  -18.703 -37.430 1.00 13.32 ? 107 TYR A CD1 1 
ATOM   740  C CD2 . TYR A 1 107 ? 12.656  -19.410 -35.968 1.00 12.01 ? 107 TYR A CD2 1 
ATOM   741  C CE1 . TYR A 1 107 ? 14.132  -17.380 -37.164 1.00 13.38 ? 107 TYR A CE1 1 
ATOM   742  C CE2 . TYR A 1 107 ? 12.361  -18.081 -35.729 1.00 12.88 ? 107 TYR A CE2 1 
ATOM   743  C CZ  . TYR A 1 107 ? 13.097  -17.063 -36.305 1.00 13.07 ? 107 TYR A CZ  1 
ATOM   744  O OH  . TYR A 1 107 ? 12.826  -15.747 -36.042 1.00 15.01 ? 107 TYR A OH  1 
ATOM   745  N N   . ARG A 1 108 ? 16.860  -20.161 -35.778 1.00 13.84 ? 108 ARG A N   1 
ATOM   746  C CA  . ARG A 1 108 ? 18.181  -19.566 -35.940 1.00 14.21 ? 108 ARG A CA  1 
ATOM   747  C C   . ARG A 1 108 ? 19.231  -20.589 -35.592 1.00 14.61 ? 108 ARG A C   1 
ATOM   748  O O   . ARG A 1 108 ? 20.290  -20.609 -36.239 1.00 15.18 ? 108 ARG A O   1 
ATOM   749  C CB  . ARG A 1 108 ? 18.378  -18.295 -35.122 1.00 15.60 ? 108 ARG A CB  1 
ATOM   750  C CG  . ARG A 1 108 ? 17.627  -17.113 -35.683 1.00 16.68 ? 108 ARG A CG  1 
ATOM   751  C CD  . ARG A 1 108 ? 17.917  -15.847 -34.908 1.00 19.89 ? 108 ARG A CD  1 
ATOM   752  N NE  . ARG A 1 108 ? 17.569  -15.967 -33.516 1.00 22.97 ? 108 ARG A NE  1 
ATOM   753  C CZ  . ARG A 1 108 ? 16.353  -15.940 -33.047 1.00 23.32 ? 108 ARG A CZ  1 
ATOM   754  N NH1 . ARG A 1 108 ? 15.350  -15.620 -33.851 1.00 26.81 ? 108 ARG A NH1 1 
ATOM   755  N NH2 . ARG A 1 108 ? 16.127  -16.240 -31.772 1.00 21.95 ? 108 ARG A NH2 1 
ATOM   756  N N   . ALA A 1 109 ? 18.991  -21.418 -34.576 1.00 13.78 ? 109 ALA A N   1 
ATOM   757  C CA  . ALA A 1 109 ? 19.973  -22.449 -34.250 1.00 13.74 ? 109 ALA A CA  1 
ATOM   758  C C   . ALA A 1 109 ? 20.144  -23.434 -35.402 1.00 13.73 ? 109 ALA A C   1 
ATOM   759  O O   . ALA A 1 109 ? 21.258  -23.859 -35.696 1.00 15.04 ? 109 ALA A O   1 
ATOM   760  C CB  . ALA A 1 109 ? 19.601  -23.138 -32.974 1.00 15.06 ? 109 ALA A CB  1 
ATOM   761  N N   . LEU A 1 110 ? 19.053  -23.789 -36.073 1.00 13.86 ? 110 LEU A N   1 
ATOM   762  C CA  . LEU A 1 110 ? 19.129  -24.700 -37.207 1.00 14.07 ? 110 LEU A CA  1 
ATOM   763  C C   . LEU A 1 110 ? 19.916  -24.073 -38.354 1.00 14.51 ? 110 LEU A C   1 
ATOM   764  O O   . LEU A 1 110 ? 20.742  -24.747 -38.971 1.00 16.18 ? 110 LEU A O   1 
ATOM   765  C CB  . LEU A 1 110 ? 17.732  -25.040 -37.694 1.00 14.68 ? 110 LEU A CB  1 
ATOM   766  C CG  . LEU A 1 110 ? 17.678  -25.895 -38.965 1.00 15.62 ? 110 LEU A CG  1 
ATOM   767  C CD1 . LEU A 1 110 ? 18.316  -27.251 -38.742 1.00 16.44 ? 110 LEU A CD1 1 
ATOM   768  C CD2 . LEU A 1 110 ? 16.249  -26.081 -39.437 1.00 16.26 ? 110 LEU A CD2 1 
ATOM   769  N N   . MET A 1 111 ? 19.708  -22.772 -38.560 1.00 14.84 ? 111 MET A N   1 
ATOM   770  C CA  . MET A 1 111 ? 20.404  -22.064 -39.613 1.00 16.31 ? 111 MET A CA  1 
ATOM   771  C C   . MET A 1 111 ? 21.894  -21.981 -39.277 1.00 16.02 ? 111 MET A C   1 
ATOM   772  O O   . MET A 1 111 ? 22.732  -21.839 -40.189 1.00 18.28 ? 111 MET A O   1 
ATOM   773  C CB  . MET A 1 111 ? 19.799  -20.691 -39.879 1.00 18.47 ? 111 MET A CB  1 
ATOM   774  C CG  . MET A 1 111 ? 18.404  -20.756 -40.471 1.00 20.03 ? 111 MET A CG  1 
ATOM   775  S SD  . MET A 1 111 ? 17.481  -19.202 -40.380 1.00 28.51 ? 111 MET A SD  1 
ATOM   776  C CE  . MET A 1 111 ? 18.198  -18.603 -41.902 1.00 28.71 ? 111 MET A CE  1 
ATOM   777  N N   . ALA A 1 112 ? 22.256  -22.111 -37.997 1.00 15.91 ? 112 ALA A N   1 
ATOM   778  C CA  . ALA A 1 112 ? 23.643  -22.153 -37.553 1.00 16.14 ? 112 ALA A CA  1 
ATOM   779  C C   . ALA A 1 112 ? 24.167  -23.593 -37.432 1.00 17.13 ? 112 ALA A C   1 
ATOM   780  O O   . ALA A 1 112 ? 25.213  -23.826 -36.838 1.00 19.82 ? 112 ALA A O   1 
ATOM   781  C CB  . ALA A 1 112 ? 23.780  -21.397 -36.247 1.00 17.00 ? 112 ALA A CB  1 
ATOM   782  N N   . GLY A 1 113 ? 23.437  -24.568 -37.972 1.00 17.50 ? 113 GLY A N   1 
ATOM   783  C CA  . GLY A 1 113 ? 23.884  -25.944 -38.074 1.00 18.79 ? 113 GLY A CA  1 
ATOM   784  C C   . GLY A 1 113 ? 23.580  -26.828 -36.874 1.00 19.04 ? 113 GLY A C   1 
ATOM   785  O O   . GLY A 1 113 ? 24.016  -27.967 -36.830 1.00 22.09 ? 113 GLY A O   1 
ATOM   786  N N   . ASN A 1 114 ? 22.778  -26.327 -35.927 1.00 16.74 ? 114 ASN A N   1 
ATOM   787  C CA  . ASN A 1 114 ? 22.441  -27.092 -34.747 1.00 16.72 ? 114 ASN A CA  1 
ATOM   788  C C   . ASN A 1 114 ? 21.043  -27.682 -34.905 1.00 15.88 ? 114 ASN A C   1 
ATOM   789  O O   . ASN A 1 114 ? 20.058  -27.027 -34.602 1.00 17.58 ? 114 ASN A O   1 
ATOM   790  C CB  . ASN A 1 114 ? 22.549  -26.218 -33.501 1.00 17.50 ? 114 ASN A CB  1 
ATOM   791  C CG  . ASN A 1 114 ? 22.390  -27.035 -32.244 1.00 17.97 ? 114 ASN A CG  1 
ATOM   792  O OD1 . ASN A 1 114 ? 21.894  -28.169 -32.279 1.00 18.60 ? 114 ASN A OD1 1 
ATOM   793  N ND2 . ASN A 1 114 ? 22.813  -26.471 -31.133 1.00 22.23 ? 114 ASN A ND2 1 
ATOM   794  N N   . GLU A 1 115 ? 20.979  -28.935 -35.356 1.00 16.89 ? 115 GLU A N   1 
ATOM   795  C CA  . GLU A 1 115 ? 19.726  -29.644 -35.520 1.00 17.08 ? 115 GLU A CA  1 
ATOM   796  C C   . GLU A 1 115 ? 19.262  -30.214 -34.188 1.00 16.76 ? 115 GLU A C   1 
ATOM   797  O O   . GLU A 1 115 ? 18.065  -30.335 -33.951 1.00 16.64 ? 115 GLU A O   1 
ATOM   798  C CB  . GLU A 1 115 ? 19.893  -30.777 -36.525 1.00 19.25 ? 115 GLU A CB  1 
ATOM   799  C CG  . GLU A 1 115 ? 20.213  -30.312 -37.938 1.00 21.31 ? 115 GLU A CG  1 
ATOM   800  C CD  . GLU A 1 115 ? 20.289  -31.468 -38.917 1.00 24.50 ? 115 GLU A CD  1 
ATOM   801  O OE1 . GLU A 1 115 ? 20.045  -32.632 -38.531 1.00 29.01 ? 115 GLU A OE1 1 
ATOM   802  O OE2 . GLU A 1 115 ? 20.580  -31.181 -40.086 1.00 29.32 ? 115 GLU A OE2 1 
ATOM   803  N N   . GLN A 1 116 ? 20.192  -30.579 -33.323 1.00 16.97 ? 116 GLN A N   1 
ATOM   804  C CA  . GLN A 1 116 ? 19.866  -31.326 -32.130 1.00 17.81 ? 116 GLN A CA  1 
ATOM   805  C C   . GLN A 1 116 ? 19.044  -30.471 -31.170 1.00 16.43 ? 116 GLN A C   1 
ATOM   806  O O   . GLN A 1 116 ? 18.145  -30.991 -30.516 1.00 17.39 ? 116 GLN A O   1 
ATOM   807  C CB  . GLN A 1 116 ? 21.141  -31.794 -31.423 1.00 18.79 ? 116 GLN A CB  1 
ATOM   808  C CG  . GLN A 1 116 ? 20.854  -32.740 -30.253 1.00 21.34 ? 116 GLN A CG  1 
ATOM   809  C CD  . GLN A 1 116 ? 20.217  -34.027 -30.733 1.00 24.96 ? 116 GLN A CD  1 
ATOM   810  O OE1 . GLN A 1 116 ? 20.674  -34.637 -31.707 1.00 29.78 ? 116 GLN A OE1 1 
ATOM   811  N NE2 . GLN A 1 116 ? 19.168  -34.483 -30.076 1.00 28.51 ? 116 GLN A NE2 1 
ATOM   812  N N   . VAL A 1 117 ? 19.359  -29.184 -31.062 1.00 16.00 ? 117 VAL A N   1 
ATOM   813  C CA  . VAL A 1 117 ? 18.660  -28.386 -30.067 1.00 15.55 ? 117 VAL A CA  1 
ATOM   814  C C   . VAL A 1 117 ? 17.186  -28.268 -30.462 1.00 14.61 ? 117 VAL A C   1 
ATOM   815  O O   . VAL A 1 117 ? 16.312  -28.247 -29.593 1.00 14.80 ? 117 VAL A O   1 
ATOM   816  C CB  . VAL A 1 117 ? 19.293  -27.014 -29.822 1.00 15.12 ? 117 VAL A CB  1 
ATOM   817  C CG1 . VAL A 1 117 ? 19.217  -26.102 -31.029 1.00 15.57 ? 117 VAL A CG1 1 
ATOM   818  C CG2 . VAL A 1 117 ? 18.695  -26.323 -28.600 1.00 16.21 ? 117 VAL A CG2 1 
ATOM   819  N N   . GLY A 1 118 ? 16.879  -28.157 -31.757 1.00 14.54 ? 118 GLY A N   1 
ATOM   820  C CA  . GLY A 1 118 ? 15.493  -28.130 -32.209 1.00 14.01 ? 118 GLY A CA  1 
ATOM   821  C C   . GLY A 1 118 ? 14.763  -29.418 -31.843 1.00 13.79 ? 118 GLY A C   1 
ATOM   822  O O   . GLY A 1 118 ? 13.615  -29.382 -31.374 1.00 14.64 ? 118 GLY A O   1 
ATOM   823  N N   . PHE A 1 119 ? 15.408  -30.558 -32.066 1.00 13.10 ? 119 PHE A N   1 
ATOM   824  C CA  . PHE A 1 119 ? 14.827  -31.837 -31.692 1.00 12.81 ? 119 PHE A CA  1 
ATOM   825  C C   . PHE A 1 119 ? 14.553  -31.856 -30.190 1.00 13.63 ? 119 PHE A C   1 
ATOM   826  O O   . PHE A 1 119 ? 13.450  -32.222 -29.748 1.00 14.10 ? 119 PHE A O   1 
ATOM   827  C CB  . PHE A 1 119 ? 15.776  -32.957 -32.111 1.00 13.87 ? 119 PHE A CB  1 
ATOM   828  C CG  . PHE A 1 119 ? 15.214  -34.314 -31.754 1.00 15.70 ? 119 PHE A CG  1 
ATOM   829  C CD1 . PHE A 1 119 ? 15.468  -34.881 -30.507 1.00 17.15 ? 119 PHE A CD1 1 
ATOM   830  C CD2 . PHE A 1 119 ? 14.406  -35.007 -32.639 1.00 17.07 ? 119 PHE A CD2 1 
ATOM   831  C CE1 . PHE A 1 119 ? 14.913  -36.097 -30.164 1.00 18.33 ? 119 PHE A CE1 1 
ATOM   832  C CE2 . PHE A 1 119 ? 13.870  -36.239 -32.293 1.00 19.01 ? 119 PHE A CE2 1 
ATOM   833  C CZ  . PHE A 1 119 ? 14.090  -36.762 -31.054 1.00 19.40 ? 119 PHE A CZ  1 
ATOM   834  N N   . ASP A 1 120 ? 15.553  -31.465 -29.409 1.00 13.95 ? 120 ASP A N   1 
ATOM   835  C CA  . ASP A 1 120 ? 15.448  -31.569 -27.964 1.00 14.39 ? 120 ASP A CA  1 
ATOM   836  C C   . ASP A 1 120 ? 14.371  -30.627 -27.431 1.00 13.87 ? 120 ASP A C   1 
ATOM   837  O O   . ASP A 1 120 ? 13.638  -30.980 -26.484 1.00 14.80 ? 120 ASP A O   1 
ATOM   838  C CB  . ASP A 1 120 ? 16.791  -31.305 -27.317 1.00 16.39 ? 120 ASP A CB  1 
ATOM   839  C CG  . ASP A 1 120 ? 17.824  -32.404 -27.512 1.00 19.43 ? 120 ASP A CG  1 
ATOM   840  O OD1 . ASP A 1 120 ? 17.436  -33.517 -27.903 1.00 21.91 ? 120 ASP A OD1 1 
ATOM   841  O OD2 . ASP A 1 120 ? 18.998  -32.148 -27.230 1.00 23.93 ? 120 ASP A OD2 1 
ATOM   842  N N   . LEU A 1 121 ? 14.305  -29.423 -27.995 1.00 12.65 ? 121 LEU A N   1 
ATOM   843  C CA  . LEU A 1 121 ? 13.342  -28.428 -27.543 1.00 12.72 ? 121 LEU A CA  1 
ATOM   844  C C   . LEU A 1 121 ? 11.922  -28.922 -27.825 1.00 12.51 ? 121 LEU A C   1 
ATOM   845  O O   . LEU A 1 121 ? 11.032  -28.893 -26.984 1.00 13.19 ? 121 LEU A O   1 
ATOM   846  C CB  . LEU A 1 121 ? 13.637  -27.071 -28.183 1.00 13.31 ? 121 LEU A CB  1 
ATOM   847  C CG  . LEU A 1 121 ? 12.877  -25.864 -27.633 1.00 13.74 ? 121 LEU A CG  1 
ATOM   848  C CD1 . LEU A 1 121 ? 13.691  -24.613 -27.774 1.00 14.65 ? 121 LEU A CD1 1 
ATOM   849  C CD2 . LEU A 1 121 ? 11.516  -25.667 -28.266 1.00 14.18 ? 121 LEU A CD2 1 
ATOM   850  N N   . VAL A 1 122 ? 11.665  -29.342 -29.055 1.00 11.82 ? 122 VAL A N   1 
ATOM   851  C CA  . VAL A 1 122 ? 10.363  -29.841 -29.439 1.00 11.78 ? 122 VAL A CA  1 
ATOM   852  C C   . VAL A 1 122 ? 10.004  -31.058 -28.584 1.00 12.84 ? 122 VAL A C   1 
ATOM   853  O O   . VAL A 1 122 ? 8.874   -31.147 -28.081 1.00 13.00 ? 122 VAL A O   1 
ATOM   854  C CB  . VAL A 1 122 ? 10.219  -30.155 -30.928 1.00 12.85 ? 122 VAL A CB  1 
ATOM   855  C CG1 . VAL A 1 122 ? 8.898   -30.835 -31.235 1.00 12.86 ? 122 VAL A CG1 1 
ATOM   856  C CG2 . VAL A 1 122 ? 10.396  -28.874 -31.731 1.00 12.93 ? 122 VAL A CG2 1 
ATOM   857  N N   . LYS A 1 123 ? 10.940  -31.989 -28.432 1.00 13.04 ? 123 LYS A N   1 
ATOM   858  C CA  . LYS A 1 123 ? 10.663  -33.191 -27.667 1.00 14.26 ? 123 LYS A CA  1 
ATOM   859  C C   . LYS A 1 123 ? 10.277  -32.858 -26.220 1.00 14.25 ? 123 LYS A C   1 
ATOM   860  O O   . LYS A 1 123 ? 9.346   -33.446 -25.695 1.00 15.06 ? 123 LYS A O   1 
ATOM   861  C CB  . LYS A 1 123 ? 11.849  -34.163 -27.675 1.00 16.07 ? 123 LYS A CB  1 
ATOM   862  C CG  . LYS A 1 123 ? 11.576  -35.491 -26.959 1.00 19.80 ? 123 LYS A CG  1 
ATOM   863  C CD  . LYS A 1 123 ? 12.568  -36.586 -27.276 1.00 25.93 ? 123 LYS A CD  1 
ATOM   864  C CE  . LYS A 1 123 ? 12.273  -37.827 -26.503 1.00 31.56 ? 123 LYS A CE  1 
ATOM   865  N NZ  . LYS A 1 123 ? 12.809  -37.751 -25.139 1.00 38.24 ? 123 LYS A NZ  1 
ATOM   866  N N   . ALA A 1 124 ? 11.014  -31.950 -25.582 1.00 13.63 ? 124 ALA A N   1 
ATOM   867  C CA  . ALA A 1 124 ? 10.740  -31.604 -24.199 1.00 13.99 ? 124 ALA A CA  1 
ATOM   868  C C   . ALA A 1 124 ? 9.312   -31.056 -24.107 1.00 12.82 ? 124 ALA A C   1 
ATOM   869  O O   . ALA A 1 124 ? 8.553   -31.372 -23.183 1.00 14.78 ? 124 ALA A O   1 
ATOM   870  C CB  . ALA A 1 124 ? 11.758  -30.608 -23.681 1.00 15.97 ? 124 ALA A CB  1 
ATOM   871  N N   . CYS A 1 125 ? 8.972   -30.136 -25.017 1.00 13.74 ? 125 CYS A N   1 
ATOM   872  C CA  . CYS A 1 125 ? 7.660   -29.517 -25.016 1.00 12.70 ? 125 CYS A CA  1 
ATOM   873  C C   . CYS A 1 125 ? 6.573   -30.551 -25.302 1.00 12.67 ? 125 CYS A C   1 
ATOM   874  O O   . CYS A 1 125 ? 5.512   -30.519 -24.674 1.00 13.16 ? 125 CYS A O   1 
ATOM   875  C CB  . CYS A 1 125 ? 7.612   -28.315 -25.951 1.00 12.62 ? 125 CYS A CB  1 
ATOM   876  S SG  . CYS A 1 125 ? 8.677   -26.940 -25.411 1.00 15.83 ? 125 CYS A SG  1 
ATOM   877  N N   . LYS A 1 126 ? 6.822   -31.467 -26.246 1.00 13.09 ? 126 LYS A N   1 
ATOM   878  C CA  . LYS A 1 126 ? 5.848   -32.507 -26.569 1.00 13.17 ? 126 LYS A CA  1 
ATOM   879  C C   . LYS A 1 126 ? 5.608   -33.421 -25.371 1.00 14.45 ? 126 LYS A C   1 
ATOM   880  O O   . LYS A 1 126 ? 4.463   -33.795 -25.091 1.00 15.13 ? 126 LYS A O   1 
ATOM   881  C CB  . LYS A 1 126 ? 6.316   -33.365 -27.744 1.00 14.13 ? 126 LYS A CB  1 
ATOM   882  C CG  . LYS A 1 126 ? 5.450   -34.573 -28.050 1.00 16.10 ? 126 LYS A CG  1 
ATOM   883  C CD  . LYS A 1 126 ? 3.991   -34.244 -28.352 1.00 17.19 ? 126 LYS A CD  1 
ATOM   884  C CE  . LYS A 1 126 ? 3.139   -35.447 -28.568 1.00 20.47 ? 126 LYS A CE  1 
ATOM   885  N NZ  . LYS A 1 126 ? 3.281   -36.045 -29.874 1.00 23.85 ? 126 LYS A NZ  1 
ATOM   886  N N   . GLU A 1 127 ? 6.660   -33.764 -24.625 1.00 15.17 ? 127 GLU A N   1 
ATOM   887  C CA  . GLU A 1 127 ? 6.477   -34.642 -23.480 1.00 16.17 ? 127 GLU A CA  1 
ATOM   888  C C   . GLU A 1 127 ? 5.572   -33.997 -22.443 1.00 14.30 ? 127 GLU A C   1 
ATOM   889  O O   . GLU A 1 127 ? 4.663   -34.667 -21.903 1.00 16.56 ? 127 GLU A O   1 
ATOM   890  C CB  . GLU A 1 127 ? 7.827   -35.022 -22.894 1.00 19.22 ? 127 GLU A CB  1 
ATOM   891  C CG  . GLU A 1 127 ? 8.584   -35.998 -23.783 1.00 23.50 ? 127 GLU A CG  1 
ATOM   892  C CD  . GLU A 1 127 ? 10.030  -36.219 -23.371 1.00 30.06 ? 127 GLU A CD  1 
ATOM   893  O OE1 . GLU A 1 127 ? 10.557  -35.495 -22.470 1.00 35.20 ? 127 GLU A OE1 1 
ATOM   894  O OE2 . GLU A 1 127 ? 10.609  -37.172 -23.939 1.00 34.87 ? 127 GLU A OE2 1 
ATOM   895  N N   . ALA A 1 128 ? 5.778   -32.700 -22.217 1.00 13.75 ? 128 ALA A N   1 
ATOM   896  C CA  . ALA A 1 128 ? 4.932   -31.978 -21.270 1.00 12.96 ? 128 ALA A CA  1 
ATOM   897  C C   . ALA A 1 128 ? 3.493   -31.951 -21.772 1.00 12.38 ? 128 ALA A C   1 
ATOM   898  O O   . ALA A 1 128 ? 2.530   -32.196 -21.030 1.00 14.26 ? 128 ALA A O   1 
ATOM   899  C CB  . ALA A 1 128 ? 5.461   -30.568 -21.094 1.00 13.84 ? 128 ALA A CB  1 
ATOM   900  N N   . CYS A 1 129 ? 3.308   -31.627 -23.042 1.00 12.31 ? 129 CYS A N   1 
ATOM   901  C CA  . CYS A 1 129 ? 1.989   -31.501 -23.606 1.00 12.02 ? 129 CYS A CA  1 
ATOM   902  C C   . CYS A 1 129 ? 1.282   -32.852 -23.587 1.00 13.99 ? 129 CYS A C   1 
ATOM   903  O O   . CYS A 1 129 ? 0.095   -32.939 -23.226 1.00 13.95 ? 129 CYS A O   1 
ATOM   904  C CB  . CYS A 1 129 ? 1.998   -30.923 -25.007 1.00 12.27 ? 129 CYS A CB  1 
ATOM   905  S SG  . CYS A 1 129 ? 2.399   -29.156 -25.064 1.00 13.84 ? 129 CYS A SG  1 
ATOM   906  N N   . ALA A 1 130 ? 1.968   -33.904 -24.022 1.00 14.24 ? 130 ALA A N   1 
ATOM   907  C CA  . ALA A 1 130 ? 1.332   -35.203 -24.107 1.00 16.22 ? 130 ALA A CA  1 
ATOM   908  C C   . ALA A 1 130 ? 0.844   -35.671 -22.742 1.00 15.78 ? 130 ALA A C   1 
ATOM   909  O O   . ALA A 1 130 ? -0.230  -36.289 -22.633 1.00 17.22 ? 130 ALA A O   1 
ATOM   910  C CB  . ALA A 1 130 ? 2.277   -36.207 -24.674 1.00 16.36 ? 130 ALA A CB  1 
ATOM   911  N N   . ALA A 1 131 ? 1.631   -35.406 -21.697 1.00 15.54 ? 131 ALA A N   1 
ATOM   912  C CA  . ALA A 1 131 ? 1.249   -35.822 -20.351 1.00 17.18 ? 131 ALA A CA  1 
ATOM   913  C C   . ALA A 1 131 ? -0.071  -35.168 -19.934 1.00 16.58 ? 131 ALA A C   1 
ATOM   914  O O   . ALA A 1 131 ? -0.746  -35.688 -19.046 1.00 19.89 ? 131 ALA A O   1 
ATOM   915  C CB  . ALA A 1 131 ? 2.345   -35.453 -19.377 1.00 18.48 ? 131 ALA A CB  1 
ATOM   916  N N   . ALA A 1 132 ? -0.411  -34.015 -20.524 1.00 15.41 ? 132 ALA A N   1 
ATOM   917  C CA  . ALA A 1 132 ? -1.604  -33.255 -20.181 1.00 15.32 ? 132 ALA A CA  1 
ATOM   918  C C   . ALA A 1 132 ? -2.704  -33.323 -21.239 1.00 15.47 ? 132 ALA A C   1 
ATOM   919  O O   . ALA A 1 132 ? -3.705  -32.596 -21.144 1.00 16.96 ? 132 ALA A O   1 
ATOM   920  C CB  . ALA A 1 132 ? -1.206  -31.811 -19.954 1.00 17.54 ? 132 ALA A CB  1 
ATOM   921  N N   . ASN A 1 133 ? -2.531  -34.178 -22.250 1.00 15.84 ? 133 ASN A N   1 
ATOM   922  C CA  . ASN A 1 133 ? -3.481  -34.316 -23.354 1.00 17.89 ? 133 ASN A CA  1 
ATOM   923  C C   . ASN A 1 133 ? -3.633  -33.000 -24.114 1.00 15.66 ? 133 ASN A C   1 
ATOM   924  O O   . ASN A 1 133 ? -4.716  -32.652 -24.564 1.00 18.50 ? 133 ASN A O   1 
ATOM   925  C CB  . ASN A 1 133 ? -4.827  -34.857 -22.857 1.00 21.77 ? 133 ASN A CB  1 
ATOM   926  C CG  . ASN A 1 133 ? -5.626  -35.491 -23.963 1.00 29.52 ? 133 ASN A CG  1 
ATOM   927  O OD1 . ASN A 1 133 ? -5.102  -35.777 -25.045 1.00 37.77 ? 133 ASN A OD1 1 
ATOM   928  N ND2 . ASN A 1 133 ? -6.898  -35.744 -23.702 1.00 35.86 ? 133 ASN A ND2 1 
ATOM   929  N N   . VAL A 1 134 ? -2.523  -32.265 -24.262 1.00 13.54 ? 134 VAL A N   1 
ATOM   930  C CA  . VAL A 1 134 ? -2.472  -30.993 -24.962 1.00 12.58 ? 134 VAL A CA  1 
ATOM   931  C C   . VAL A 1 134 ? -1.762  -31.221 -26.292 1.00 12.26 ? 134 VAL A C   1 
ATOM   932  O O   . VAL A 1 134 ? -0.738  -31.899 -26.322 1.00 13.79 ? 134 VAL A O   1 
ATOM   933  C CB  . VAL A 1 134 ? -1.745  -29.959 -24.073 1.00 11.98 ? 134 VAL A CB  1 
ATOM   934  C CG1 . VAL A 1 134 ? -1.322  -28.698 -24.819 1.00 12.06 ? 134 VAL A CG1 1 
ATOM   935  C CG2 . VAL A 1 134 ? -2.606  -29.603 -22.877 1.00 13.70 ? 134 VAL A CG2 1 
ATOM   936  N N   . LEU A 1 135 ? -2.294  -30.627 -27.361 1.00 12.32 ? 135 LEU A N   1 
ATOM   937  C CA  . LEU A 1 135 ? -1.662  -30.753 -28.663 1.00 12.75 ? 135 LEU A CA  1 
ATOM   938  C C   . LEU A 1 135 ? -0.526  -29.748 -28.791 1.00 11.76 ? 135 LEU A C   1 
ATOM   939  O O   . LEU A 1 135 ? -0.652  -28.608 -28.347 1.00 12.35 ? 135 LEU A O   1 
ATOM   940  C CB  . LEU A 1 135 ? -2.775  -30.475 -29.668 1.00 16.68 ? 135 LEU A CB  1 
ATOM   941  C CG  . LEU A 1 135 ? -2.544  -30.595 -31.157 1.00 22.14 ? 135 LEU A CG  1 
ATOM   942  C CD1 . LEU A 1 135 ? -3.796  -31.284 -31.691 1.00 27.15 ? 135 LEU A CD1 1 
ATOM   943  C CD2 . LEU A 1 135 ? -2.354  -29.227 -31.742 1.00 28.45 ? 135 LEU A CD2 1 
ATOM   944  N N   . LEU A 1 136 ? 0.576   -30.170 -29.428 1.00 12.14 ? 136 LEU A N   1 
ATOM   945  C CA  . LEU A 1 136 ? 1.704   -29.278 -29.686 1.00 11.33 ? 136 LEU A CA  1 
ATOM   946  C C   . LEU A 1 136 ? 1.813   -28.971 -31.176 1.00 10.45 ? 136 LEU A C   1 
ATOM   947  O O   . LEU A 1 136 ? 1.992   -29.882 -31.978 1.00 11.89 ? 136 LEU A O   1 
ATOM   948  C CB  . LEU A 1 136 ? 3.002   -29.930 -29.237 1.00 12.00 ? 136 LEU A CB  1 
ATOM   949  C CG  . LEU A 1 136 ? 4.240   -29.032 -29.367 1.00 12.84 ? 136 LEU A CG  1 
ATOM   950  C CD1 . LEU A 1 136 ? 4.243   -27.916 -28.345 1.00 14.01 ? 136 LEU A CD1 1 
ATOM   951  C CD2 . LEU A 1 136 ? 5.486   -29.879 -29.228 1.00 14.26 ? 136 LEU A CD2 1 
ATOM   952  N N   . LYS A 1 137 ? 1.771   -27.683 -31.491 1.00 10.58 ? 137 LYS A N   1 
ATOM   953  C CA  . LYS A 1 137 ? 2.098   -27.237 -32.841 1.00 10.50 ? 137 LYS A CA  1 
ATOM   954  C C   . LYS A 1 137 ? 3.479   -26.631 -32.762 1.00 10.68 ? 137 LYS A C   1 
ATOM   955  O O   . LYS A 1 137 ? 3.868   -26.005 -31.805 1.00 11.52 ? 137 LYS A O   1 
ATOM   956  C CB  . LYS A 1 137 ? 1.137   -26.172 -33.371 1.00 10.95 ? 137 LYS A CB  1 
ATOM   957  C CG  . LYS A 1 137 ? -0.371  -26.474 -33.128 1.00 11.41 ? 137 LYS A CG  1 
ATOM   958  C CD  . LYS A 1 137 ? -1.203  -25.612 -34.066 1.00 12.04 ? 137 LYS A CD  1 
ATOM   959  C CE  . LYS A 1 137 ? -2.690  -25.564 -33.731 1.00 12.72 ? 137 LYS A CE  1 
ATOM   960  N NZ  . LYS A 1 137 ? -3.008  -24.636 -32.630 1.00 13.43 ? 137 LYS A NZ  1 
ATOM   961  N N   . VAL A 1 138 ? 4.258   -26.803 -33.842 1.00 9.64  ? 138 VAL A N   1 
ATOM   962  C CA  . VAL A 1 138 ? 5.621   -26.270 -33.891 1.00 10.15 ? 138 VAL A CA  1 
ATOM   963  C C   . VAL A 1 138 ? 5.726   -25.277 -35.035 1.00 10.01 ? 138 VAL A C   1 
ATOM   964  O O   . VAL A 1 138 ? 5.509   -25.653 -36.205 1.00 10.91 ? 138 VAL A O   1 
ATOM   965  C CB  . VAL A 1 138 ? 6.666   -27.375 -34.024 1.00 9.92  ? 138 VAL A CB  1 
ATOM   966  C CG1 . VAL A 1 138 ? 8.037   -26.761 -34.157 1.00 10.83 ? 138 VAL A CG1 1 
ATOM   967  C CG2 . VAL A 1 138 ? 6.632   -28.331 -32.858 1.00 11.06 ? 138 VAL A CG2 1 
ATOM   968  N N   . ILE A 1 139 ? 6.035   -24.024 -34.695 1.00 10.49 ? 139 ILE A N   1 
ATOM   969  C CA  . ILE A 1 139 ? 6.186   -22.954 -35.668 1.00 10.30 ? 139 ILE A CA  1 
ATOM   970  C C   . ILE A 1 139 ? 7.627   -22.998 -36.166 1.00 10.79 ? 139 ILE A C   1 
ATOM   971  O O   . ILE A 1 139 ? 8.543   -22.751 -35.395 1.00 11.35 ? 139 ILE A O   1 
ATOM   972  C CB  . ILE A 1 139 ? 5.890   -21.580 -35.044 1.00 10.56 ? 139 ILE A CB  1 
ATOM   973  C CG1 . ILE A 1 139 ? 4.464   -21.534 -34.494 1.00 11.30 ? 139 ILE A CG1 1 
ATOM   974  C CG2 . ILE A 1 139 ? 6.157   -20.483 -36.070 1.00 11.02 ? 139 ILE A CG2 1 
ATOM   975  C CD1 . ILE A 1 139 ? 4.231   -20.380 -33.533 1.00 12.39 ? 139 ILE A CD1 1 
ATOM   976  N N   . ILE A 1 140 ? 7.818   -23.213 -37.470 1.00 10.87 ? 140 ILE A N   1 
ATOM   977  C CA  . ILE A 1 140 ? 9.194   -23.287 -37.966 1.00 11.66 ? 140 ILE A CA  1 
ATOM   978  C C   . ILE A 1 140 ? 9.697   -21.963 -38.549 1.00 11.46 ? 140 ILE A C   1 
ATOM   979  O O   . ILE A 1 140 ? 10.907  -21.822 -38.759 1.00 12.47 ? 140 ILE A O   1 
ATOM   980  C CB  . ILE A 1 140 ? 9.384   -24.459 -38.939 1.00 12.35 ? 140 ILE A CB  1 
ATOM   981  C CG1 . ILE A 1 140 ? 8.583   -24.299 -40.212 1.00 13.09 ? 140 ILE A CG1 1 
ATOM   982  C CG2 . ILE A 1 140 ? 9.111   -25.790 -38.209 1.00 13.19 ? 140 ILE A CG2 1 
ATOM   983  C CD1 . ILE A 1 140 ? 9.003   -25.267 -41.318 1.00 13.92 ? 140 ILE A CD1 1 
ATOM   984  N N   . GLU A 1 141 ? 8.825   -20.996 -38.793 1.00 11.92 ? 141 GLU A N   1 
ATOM   985  C CA  . GLU A 1 141 ? 9.206   -19.671 -39.296 1.00 11.57 ? 141 GLU A CA  1 
ATOM   986  C C   . GLU A 1 141 ? 9.780   -19.765 -40.704 1.00 11.88 ? 141 GLU A C   1 
ATOM   987  O O   . GLU A 1 141 ? 10.931  -19.368 -40.950 1.00 13.11 ? 141 GLU A O   1 
ATOM   988  C CB  . GLU A 1 141 ? 10.089  -18.860 -38.350 1.00 12.37 ? 141 GLU A CB  1 
ATOM   989  C CG  . GLU A 1 141 ? 9.930   -17.358 -38.530 1.00 13.14 ? 141 GLU A CG  1 
ATOM   990  C CD  . GLU A 1 141 ? 8.606   -16.762 -38.062 1.00 12.99 ? 141 GLU A CD  1 
ATOM   991  O OE1 . GLU A 1 141 ? 7.568   -17.003 -38.710 1.00 12.70 ? 141 GLU A OE1 1 
ATOM   992  O OE2 . GLU A 1 141 ? 8.625   -16.067 -37.023 1.00 14.14 ? 141 GLU A OE2 1 
ATOM   993  N N   . THR A 1 142 ? 8.936   -20.208 -41.631 1.00 11.72 ? 142 THR A N   1 
ATOM   994  C CA  . THR A 1 142 ? 9.402   -20.425 -43.006 1.00 12.50 ? 142 THR A CA  1 
ATOM   995  C C   . THR A 1 142 ? 9.940   -19.151 -43.656 1.00 13.88 ? 142 THR A C   1 
ATOM   996  O O   . THR A 1 142 ? 10.807  -19.197 -44.545 1.00 15.05 ? 142 THR A O   1 
ATOM   997  C CB  . THR A 1 142 ? 8.247   -20.959 -43.839 1.00 12.52 ? 142 THR A CB  1 
ATOM   998  O OG1 . THR A 1 142 ? 7.111   -20.104 -43.745 1.00 13.27 ? 142 THR A OG1 1 
ATOM   999  C CG2 . THR A 1 142 ? 7.848   -22.362 -43.420 1.00 13.08 ? 142 THR A CG2 1 
ATOM   1000 N N   . GLY A 1 143 ? 9.402   -17.999 -43.285 1.00 13.44 ? 143 GLY A N   1 
ATOM   1001 C CA  . GLY A 1 143 ? 9.819   -16.716 -43.813 1.00 14.22 ? 143 GLY A CA  1 
ATOM   1002 C C   . GLY A 1 143 ? 11.220  -16.307 -43.382 1.00 16.40 ? 143 GLY A C   1 
ATOM   1003 O O   . GLY A 1 143 ? 11.803  -15.423 -44.006 1.00 22.21 ? 143 GLY A O   1 
ATOM   1004 N N   . GLU A 1 144 ? 11.748  -16.906 -42.302 1.00 14.86 ? 144 GLU A N   1 
ATOM   1005 C CA  . GLU A 1 144 ? 13.138  -16.658 -41.908 1.00 15.09 ? 144 GLU A CA  1 
ATOM   1006 C C   . GLU A 1 144 ? 14.027  -17.776 -42.441 1.00 15.68 ? 144 GLU A C   1 
ATOM   1007 O O   . GLU A 1 144 ? 15.177  -17.509 -42.765 1.00 17.51 ? 144 GLU A O   1 
ATOM   1008 C CB  . GLU A 1 144 ? 13.238  -16.503 -40.398 1.00 17.27 ? 144 GLU A CB  1 
ATOM   1009 C CG  . GLU A 1 144 ? 12.546  -15.247 -39.887 1.00 18.30 ? 144 GLU A CG  1 
ATOM   1010 C CD  . GLU A 1 144 ? 13.166  -13.962 -40.373 1.00 20.98 ? 144 GLU A CD  1 
ATOM   1011 O OE1 . GLU A 1 144 ? 14.399  -13.891 -40.495 1.00 24.03 ? 144 GLU A OE1 1 
ATOM   1012 O OE2 . GLU A 1 144 ? 12.424  -13.029 -40.694 1.00 24.10 ? 144 GLU A OE2 1 
ATOM   1013 N N   . LEU A 1 145 ? 13.536  -19.021 -42.474 1.00 15.05 ? 145 LEU A N   1 
ATOM   1014 C CA  . LEU A 1 145 ? 14.336  -20.104 -43.019 1.00 15.37 ? 145 LEU A CA  1 
ATOM   1015 C C   . LEU A 1 145 ? 14.617  -19.873 -44.506 1.00 17.44 ? 145 LEU A C   1 
ATOM   1016 O O   . LEU A 1 145 ? 15.755  -20.098 -44.964 1.00 19.67 ? 145 LEU A O   1 
ATOM   1017 C CB  . LEU A 1 145 ? 13.634  -21.436 -42.815 1.00 16.00 ? 145 LEU A CB  1 
ATOM   1018 C CG  . LEU A 1 145 ? 13.523  -21.925 -41.370 1.00 15.52 ? 145 LEU A CG  1 
ATOM   1019 C CD1 . LEU A 1 145 ? 12.623  -23.131 -41.297 1.00 17.79 ? 145 LEU A CD1 1 
ATOM   1020 C CD2 . LEU A 1 145 ? 14.852  -22.223 -40.746 1.00 17.14 ? 145 LEU A CD2 1 
ATOM   1021 N N   . LYS A 1 146 ? 13.567  -19.501 -45.262 1.00 17.75 ? 146 LYS A N   1 
ATOM   1022 C CA  . LYS A 1 146 ? 13.627  -19.130 -46.674 1.00 20.35 ? 146 LYS A CA  1 
ATOM   1023 C C   . LYS A 1 146 ? 13.875  -20.337 -47.599 1.00 21.07 ? 146 LYS A C   1 
ATOM   1024 O O   . LYS A 1 146 ? 13.138  -20.603 -48.535 1.00 27.55 ? 146 LYS A O   1 
ATOM   1025 C CB  . LYS A 1 146 ? 14.594  -17.950 -46.812 1.00 23.94 ? 146 LYS A CB  1 
ATOM   1026 C CG  . LYS A 1 146 ? 14.106  -16.681 -46.105 1.00 29.53 ? 146 LYS A CG  1 
ATOM   1027 C CD  . LYS A 1 146 ? 15.056  -15.498 -46.265 1.00 35.66 ? 146 LYS A CD  1 
ATOM   1028 C CE  . LYS A 1 146 ? 14.545  -14.221 -45.669 1.00 40.97 ? 146 LYS A CE  1 
ATOM   1029 N NZ  . LYS A 1 146 ? 15.239  -13.880 -44.428 1.00 46.69 ? 146 LYS A NZ  1 
ATOM   1030 N N   . ASP A 1 147 ? 14.914  -21.079 -47.343 1.00 22.65 ? 147 ASP A N   1 
ATOM   1031 C CA  . ASP A 1 147 ? 15.361  -22.128 -48.226 1.00 20.15 ? 147 ASP A CA  1 
ATOM   1032 C C   . ASP A 1 147 ? 14.503  -23.393 -48.087 1.00 18.13 ? 147 ASP A C   1 
ATOM   1033 O O   . ASP A 1 147 ? 14.199  -23.815 -46.978 1.00 18.28 ? 147 ASP A O   1 
ATOM   1034 C CB  . ASP A 1 147 ? 16.784  -22.403 -47.814 1.00 25.14 ? 147 ASP A CB  1 
ATOM   1035 C CG  . ASP A 1 147 ? 17.356  -23.611 -48.498 1.00 30.37 ? 147 ASP A CG  1 
ATOM   1036 O OD1 . ASP A 1 147 ? 17.629  -23.505 -49.691 1.00 37.14 ? 147 ASP A OD1 1 
ATOM   1037 O OD2 . ASP A 1 147 ? 17.451  -24.638 -47.812 1.00 37.28 ? 147 ASP A OD2 1 
ATOM   1038 N N   . GLU A 1 148 ? 14.129  -24.017 -49.215 1.00 18.29 ? 148 GLU A N   1 
ATOM   1039 C CA  . GLU A 1 148 ? 13.370  -25.251 -49.236 1.00 17.77 ? 148 GLU A CA  1 
ATOM   1040 C C   . GLU A 1 148 ? 14.004  -26.316 -48.340 1.00 16.79 ? 148 GLU A C   1 
ATOM   1041 O O   . GLU A 1 148 ? 13.327  -26.986 -47.551 1.00 17.20 ? 148 GLU A O   1 
ATOM   1042 C CB  . GLU A 1 148 ? 13.104  -25.729 -50.658 1.00 18.81 ? 148 GLU A CB  1 
ATOM   1043 C CG  . GLU A 1 148 ? 12.491  -27.124 -50.707 1.00 21.68 ? 148 GLU A CG  1 
ATOM   1044 C CD  . GLU A 1 148 ? 12.078  -27.634 -52.066 1.00 26.38 ? 148 GLU A CD  1 
ATOM   1045 O OE1 . GLU A 1 148 ? 12.252  -26.911 -53.055 1.00 30.51 ? 148 GLU A OE1 1 
ATOM   1046 O OE2 . GLU A 1 148 ? 11.593  -28.785 -52.136 1.00 32.00 ? 148 GLU A OE2 1 
ATOM   1047 N N   . ALA A 1 149 ? 15.313  -26.528 -48.472 1.00 17.43 ? 149 ALA A N   1 
ATOM   1048 C CA  . ALA A 1 149 ? 15.976  -27.572 -47.716 1.00 17.89 ? 149 ALA A CA  1 
ATOM   1049 C C   . ALA A 1 149 ? 15.840  -27.338 -46.206 1.00 17.19 ? 149 ALA A C   1 
ATOM   1050 O O   . ALA A 1 149 ? 15.691  -28.289 -45.441 1.00 17.37 ? 149 ALA A O   1 
ATOM   1051 C CB  . ALA A 1 149 ? 17.424  -27.696 -48.141 1.00 18.27 ? 149 ALA A CB  1 
ATOM   1052 N N   . LEU A 1 150 ? 15.969  -26.082 -45.765 1.00 15.82 ? 150 LEU A N   1 
ATOM   1053 C CA  . LEU A 1 150 ? 15.844  -25.760 -44.347 1.00 15.89 ? 150 LEU A CA  1 
ATOM   1054 C C   . LEU A 1 150 ? 14.399  -25.919 -43.889 1.00 14.71 ? 150 LEU A C   1 
ATOM   1055 O O   . LEU A 1 150 ? 14.192  -26.352 -42.776 1.00 14.54 ? 150 LEU A O   1 
ATOM   1056 C CB  . LEU A 1 150 ? 16.324  -24.351 -44.049 1.00 16.09 ? 150 LEU A CB  1 
ATOM   1057 C CG  . LEU A 1 150 ? 17.844  -24.168 -44.031 1.00 18.34 ? 150 LEU A CG  1 
ATOM   1058 C CD1 . LEU A 1 150 ? 18.208  -22.699 -44.061 1.00 19.46 ? 150 LEU A CD1 1 
ATOM   1059 C CD2 . LEU A 1 150 ? 18.407  -24.814 -42.784 1.00 21.77 ? 150 LEU A CD2 1 
ATOM   1060 N N   . ILE A 1 151 ? 13.426  -25.556 -44.723 1.00 13.94 ? 151 ILE A N   1 
ATOM   1061 C CA  . ILE A 1 151 ? 12.029  -25.726 -44.355 1.00 13.75 ? 151 ILE A CA  1 
ATOM   1062 C C   . ILE A 1 151 ? 11.743  -27.215 -44.181 1.00 13.84 ? 151 ILE A C   1 
ATOM   1063 O O   . ILE A 1 151 ? 11.093  -27.619 -43.212 1.00 13.41 ? 151 ILE A O   1 
ATOM   1064 C CB  . ILE A 1 151 ? 11.132  -25.054 -45.386 1.00 14.36 ? 151 ILE A CB  1 
ATOM   1065 C CG1 . ILE A 1 151 ? 11.307  -23.560 -45.318 1.00 14.10 ? 151 ILE A CG1 1 
ATOM   1066 C CG2 . ILE A 1 151 ? 9.687   -25.495 -45.220 1.00 14.13 ? 151 ILE A CG2 1 
ATOM   1067 C CD1 . ILE A 1 151 ? 10.661  -22.790 -46.461 1.00 15.32 ? 151 ILE A CD1 1 
ATOM   1068 N N   . ARG A 1 152 ? 12.222  -28.041 -45.114 1.00 13.83 ? 152 ARG A N   1 
ATOM   1069 C CA  . ARG A 1 152 ? 12.044  -29.478 -44.990 1.00 14.14 ? 152 ARG A CA  1 
ATOM   1070 C C   . ARG A 1 152 ? 12.705  -30.000 -43.712 1.00 14.14 ? 152 ARG A C   1 
ATOM   1071 O O   . ARG A 1 152 ? 12.105  -30.798 -42.987 1.00 14.90 ? 152 ARG A O   1 
ATOM   1072 C CB  . ARG A 1 152 ? 12.555  -30.269 -46.188 1.00 15.36 ? 152 ARG A CB  1 
ATOM   1073 C CG  . ARG A 1 152 ? 11.726  -30.051 -47.428 1.00 17.86 ? 152 ARG A CG  1 
ATOM   1074 C CD  . ARG A 1 152 ? 12.117  -31.013 -48.528 1.00 20.30 ? 152 ARG A CD  1 
ATOM   1075 N NE  . ARG A 1 152 ? 11.510  -30.639 -49.803 1.00 22.17 ? 152 ARG A NE  1 
ATOM   1076 C CZ  . ARG A 1 152 ? 10.252  -30.896 -50.146 1.00 24.94 ? 152 ARG A CZ  1 
ATOM   1077 N NH1 . ARG A 1 152 ? 9.503   -31.704 -49.401 1.00 26.42 ? 152 ARG A NH1 1 
ATOM   1078 N NH2 . ARG A 1 152 ? 9.751   -30.345 -51.233 1.00 28.41 ? 152 ARG A NH2 1 
ATOM   1079 N N   . LYS A 1 153 ? 13.938  -29.574 -43.451 1.00 14.00 ? 153 LYS A N   1 
ATOM   1080 C CA  . LYS A 1 153 ? 14.690  -30.070 -42.316 1.00 14.71 ? 153 LYS A CA  1 
ATOM   1081 C C   . LYS A 1 153 ? 13.983  -29.711 -41.002 1.00 13.76 ? 153 LYS A C   1 
ATOM   1082 O O   . LYS A 1 153 ? 13.842  -30.560 -40.129 1.00 14.01 ? 153 LYS A O   1 
ATOM   1083 C CB  . LYS A 1 153 ? 16.118  -29.518 -42.326 1.00 15.90 ? 153 LYS A CB  1 
ATOM   1084 C CG  . LYS A 1 153 ? 16.987  -30.100 -41.227 1.00 19.02 ? 153 LYS A CG  1 
ATOM   1085 C CD  . LYS A 1 153 ? 17.059  -31.624 -41.157 1.00 23.66 ? 153 LYS A CD  1 
ATOM   1086 C CE  . LYS A 1 153 ? 17.611  -32.175 -42.430 1.00 27.04 ? 153 LYS A CE  1 
ATOM   1087 N NZ  . LYS A 1 153 ? 17.703  -33.637 -42.443 1.00 30.92 ? 153 LYS A NZ  1 
ATOM   1088 N N   . ALA A 1 154 ? 13.563  -28.449 -40.858 1.00 13.10 ? 154 ALA A N   1 
ATOM   1089 C CA  . ALA A 1 154 ? 12.871  -28.040 -39.649 1.00 12.15 ? 154 ALA A CA  1 
ATOM   1090 C C   . ALA A 1 154 ? 11.572  -28.842 -39.466 1.00 12.59 ? 154 ALA A C   1 
ATOM   1091 O O   . ALA A 1 154 ? 11.229  -29.244 -38.360 1.00 12.44 ? 154 ALA A O   1 
ATOM   1092 C CB  . ALA A 1 154 ? 12.625  -26.558 -39.681 1.00 12.68 ? 154 ALA A CB  1 
ATOM   1093 N N   . SER A 1 155 ? 10.858  -29.074 -40.559 1.00 12.05 ? 155 SER A N   1 
ATOM   1094 C CA  . SER A 1 155 ? 9.645   -29.865 -40.533 1.00 11.92 ? 155 SER A CA  1 
ATOM   1095 C C   . SER A 1 155 ? 9.925   -31.299 -40.072 1.00 12.45 ? 155 SER A C   1 
ATOM   1096 O O   . SER A 1 155 ? 9.252   -31.855 -39.200 1.00 13.50 ? 155 SER A O   1 
ATOM   1097 C CB  . SER A 1 155 ? 8.973   -29.851 -41.881 1.00 12.48 ? 155 SER A CB  1 
ATOM   1098 O OG  . SER A 1 155 ? 8.605   -28.546 -42.277 1.00 13.13 ? 155 SER A OG  1 
ATOM   1099 N N   . GLU A 1 156 ? 10.970  -31.890 -40.655 1.00 13.19 ? 156 GLU A N   1 
ATOM   1100 C CA  . GLU A 1 156 ? 11.343  -33.264 -40.370 1.00 14.52 ? 156 GLU A CA  1 
ATOM   1101 C C   . GLU A 1 156 ? 11.732  -33.410 -38.896 1.00 13.79 ? 156 GLU A C   1 
ATOM   1102 O O   . GLU A 1 156 ? 11.314  -34.358 -38.229 1.00 14.66 ? 156 GLU A O   1 
ATOM   1103 C CB  . GLU A 1 156 ? 12.541  -33.638 -41.253 1.00 16.73 ? 156 GLU A CB  1 
ATOM   1104 C CG  . GLU A 1 156 ? 13.101  -35.023 -40.996 1.00 22.38 ? 156 GLU A CG  1 
ATOM   1105 C CD  . GLU A 1 156 ? 14.413  -35.212 -41.758 1.00 28.89 ? 156 GLU A CD  1 
ATOM   1106 O OE1 . GLU A 1 156 ? 14.837  -34.312 -42.553 1.00 31.71 ? 156 GLU A OE1 1 
ATOM   1107 O OE2 . GLU A 1 156 ? 15.041  -36.281 -41.541 1.00 37.25 ? 156 GLU A OE2 1 
ATOM   1108 N N   . ILE A 1 157 ? 12.605  -32.521 -38.410 1.00 13.15 ? 157 ILE A N   1 
ATOM   1109 C CA  . ILE A 1 157 ? 13.057  -32.594 -37.029 1.00 13.07 ? 157 ILE A CA  1 
ATOM   1110 C C   . ILE A 1 157 ? 11.853  -32.465 -36.100 1.00 12.27 ? 157 ILE A C   1 
ATOM   1111 O O   . ILE A 1 157 ? 11.737  -33.206 -35.130 1.00 13.79 ? 157 ILE A O   1 
ATOM   1112 C CB  . ILE A 1 157 ? 14.082  -31.493 -36.731 1.00 13.55 ? 157 ILE A CB  1 
ATOM   1113 C CG1 . ILE A 1 157 ? 15.387  -31.748 -37.496 1.00 14.25 ? 157 ILE A CG1 1 
ATOM   1114 C CG2 . ILE A 1 157 ? 14.341  -31.361 -35.237 1.00 13.86 ? 157 ILE A CG2 1 
ATOM   1115 C CD1 . ILE A 1 157 ? 16.266  -30.514 -37.560 1.00 15.51 ? 157 ILE A CD1 1 
ATOM   1116 N N   . SER A 1 158 ? 10.979  -31.498 -36.381 1.00 11.74 ? 158 SER A N   1 
ATOM   1117 C CA  . SER A 1 158 ? 9.805   -31.271 -35.536 1.00 12.00 ? 158 SER A CA  1 
ATOM   1118 C C   . SER A 1 158 ? 8.945   -32.522 -35.459 1.00 12.73 ? 158 SER A C   1 
ATOM   1119 O O   . SER A 1 158 ? 8.445   -32.904 -34.391 1.00 13.38 ? 158 SER A O   1 
ATOM   1120 C CB  . SER A 1 158 ? 9.030   -30.091 -36.055 1.00 12.04 ? 158 SER A CB  1 
ATOM   1121 O OG  . SER A 1 158 ? 9.780   -28.890 -35.977 1.00 13.42 ? 158 SER A OG  1 
ATOM   1122 N N   . ILE A 1 159 ? 8.707   -33.142 -36.611 1.00 12.86 ? 159 ILE A N   1 
ATOM   1123 C CA  . ILE A 1 159 ? 7.909   -34.353 -36.678 1.00 13.28 ? 159 ILE A CA  1 
ATOM   1124 C C   . ILE A 1 159 ? 8.558   -35.486 -35.892 1.00 13.27 ? 159 ILE A C   1 
ATOM   1125 O O   . ILE A 1 159 ? 7.897   -36.185 -35.104 1.00 14.38 ? 159 ILE A O   1 
ATOM   1126 C CB  . ILE A 1 159 ? 7.631   -34.724 -38.139 1.00 13.67 ? 159 ILE A CB  1 
ATOM   1127 C CG1 . ILE A 1 159 ? 6.596   -33.740 -38.712 1.00 13.70 ? 159 ILE A CG1 1 
ATOM   1128 C CG2 . ILE A 1 159 ? 7.172   -36.176 -38.275 1.00 14.54 ? 159 ILE A CG2 1 
ATOM   1129 C CD1 . ILE A 1 159 ? 6.466   -33.774 -40.226 1.00 14.64 ? 159 ILE A CD1 1 
ATOM   1130 N N   . LYS A 1 160 ? 9.849   -35.694 -36.096 1.00 14.00 ? 160 LYS A N   1 
ATOM   1131 C CA  . LYS A 1 160 ? 10.546  -36.752 -35.398 1.00 14.82 ? 160 LYS A CA  1 
ATOM   1132 C C   . LYS A 1 160 ? 10.504  -36.559 -33.880 1.00 14.93 ? 160 LYS A C   1 
ATOM   1133 O O   . LYS A 1 160 ? 10.471  -37.545 -33.139 1.00 17.76 ? 160 LYS A O   1 
ATOM   1134 C CB  . LYS A 1 160 ? 11.999  -36.823 -35.878 1.00 16.69 ? 160 LYS A CB  1 
ATOM   1135 C CG  . LYS A 1 160 ? 12.126  -37.406 -37.262 1.00 19.19 ? 160 LYS A CG  1 
ATOM   1136 C CD  . LYS A 1 160 ? 13.580  -37.458 -37.687 1.00 22.99 ? 160 LYS A CD  1 
ATOM   1137 C CE  . LYS A 1 160 ? 13.609  -38.068 -39.027 1.00 29.58 ? 160 LYS A CE  1 
ATOM   1138 N NZ  . LYS A 1 160 ? 14.976  -38.167 -39.507 1.00 33.78 ? 160 LYS A NZ  1 
ATOM   1139 N N   . ALA A 1 161 ? 10.531  -35.297 -33.438 1.00 14.46 ? 161 ALA A N   1 
ATOM   1140 C CA  . ALA A 1 161 ? 10.477  -34.974 -32.018 1.00 15.30 ? 161 ALA A CA  1 
ATOM   1141 C C   . ALA A 1 161 ? 9.060   -35.035 -31.439 1.00 15.78 ? 161 ALA A C   1 
ATOM   1142 O O   . ALA A 1 161 ? 8.906   -34.898 -30.223 1.00 17.36 ? 161 ALA A O   1 
ATOM   1143 C CB  . ALA A 1 161 ? 11.052  -33.598 -31.800 1.00 15.53 ? 161 ALA A CB  1 
ATOM   1144 N N   . GLY A 1 162 ? 8.041   -35.212 -32.286 1.00 14.89 ? 162 GLY A N   1 
ATOM   1145 C CA  . GLY A 1 162 ? 6.689   -35.530 -31.851 1.00 15.36 ? 162 GLY A CA  1 
ATOM   1146 C C   . GLY A 1 162 ? 5.673   -34.411 -32.069 1.00 15.04 ? 162 GLY A C   1 
ATOM   1147 O O   . GLY A 1 162 ? 4.589   -34.459 -31.485 1.00 16.39 ? 162 GLY A O   1 
ATOM   1148 N N   . ALA A 1 163 ? 5.974   -33.413 -32.904 1.00 13.61 ? 163 ALA A N   1 
ATOM   1149 C CA  . ALA A 1 163 ? 5.000   -32.365 -33.191 1.00 12.74 ? 163 ALA A CA  1 
ATOM   1150 C C   . ALA A 1 163 ? 3.682   -32.982 -33.639 1.00 12.97 ? 163 ALA A C   1 
ATOM   1151 O O   . ALA A 1 163 ? 3.645   -33.881 -34.477 1.00 13.81 ? 163 ALA A O   1 
ATOM   1152 C CB  . ALA A 1 163 ? 5.513   -31.473 -34.310 1.00 14.08 ? 163 ALA A CB  1 
ATOM   1153 N N   . ASP A 1 164 ? 2.578   -32.424 -33.159 1.00 11.66 ? 164 ASP A N   1 
ATOM   1154 C CA  . ASP A 1 164 ? 1.260   -32.816 -33.618 1.00 11.83 ? 164 ASP A CA  1 
ATOM   1155 C C   . ASP A 1 164 ? 0.808   -31.980 -34.808 1.00 11.21 ? 164 ASP A C   1 
ATOM   1156 O O   . ASP A 1 164 ? -0.098  -32.384 -35.524 1.00 12.47 ? 164 ASP A O   1 
ATOM   1157 C CB  . ASP A 1 164 ? 0.268   -32.679 -32.482 1.00 12.94 ? 164 ASP A CB  1 
ATOM   1158 C CG  . ASP A 1 164 ? 0.614   -33.503 -31.251 1.00 14.14 ? 164 ASP A CG  1 
ATOM   1159 O OD1 . ASP A 1 164 ? 0.876   -34.715 -31.405 1.00 15.68 ? 164 ASP A OD1 1 
ATOM   1160 O OD2 . ASP A 1 164 ? 0.625   -32.923 -30.127 1.00 15.68 ? 164 ASP A OD2 1 
ATOM   1161 N N   . PHE A 1 165 ? 1.410   -30.808 -34.974 1.00 11.44 ? 165 PHE A N   1 
ATOM   1162 C CA  . PHE A 1 165 ? 1.193   -29.947 -36.130 1.00 10.72 ? 165 PHE A CA  1 
ATOM   1163 C C   . PHE A 1 165 ? 2.522   -29.275 -36.453 1.00 10.36 ? 165 PHE A C   1 
ATOM   1164 O O   . PHE A 1 165 ? 3.294   -28.997 -35.533 1.00 10.58 ? 165 PHE A O   1 
ATOM   1165 C CB  . PHE A 1 165 ? 0.267   -28.748 -35.874 1.00 11.79 ? 165 PHE A CB  1 
ATOM   1166 C CG  . PHE A 1 165 ? -1.227  -28.929 -36.118 1.00 12.33 ? 165 PHE A CG  1 
ATOM   1167 C CD1 . PHE A 1 165 ? -2.013  -29.636 -35.249 1.00 14.07 ? 165 PHE A CD1 1 
ATOM   1168 C CD2 . PHE A 1 165 ? -1.814  -28.383 -37.256 1.00 13.39 ? 165 PHE A CD2 1 
ATOM   1169 C CE1 . PHE A 1 165 ? -3.379  -29.746 -35.503 1.00 15.98 ? 165 PHE A CE1 1 
ATOM   1170 C CE2 . PHE A 1 165 ? -3.149  -28.498 -37.503 1.00 15.72 ? 165 PHE A CE2 1 
ATOM   1171 C CZ  . PHE A 1 165 ? -3.930  -29.185 -36.623 1.00 15.37 ? 165 PHE A CZ  1 
ATOM   1172 N N   . ILE A 1 166 ? 2.759   -29.011 -37.740 1.00 10.92 ? 166 ILE A N   1 
ATOM   1173 C CA  . ILE A 1 166 ? 3.799   -28.062 -38.102 1.00 10.81 ? 166 ILE A CA  1 
ATOM   1174 C C   . ILE A 1 166 ? 3.128   -26.820 -38.693 1.00 10.36 ? 166 ILE A C   1 
ATOM   1175 O O   . ILE A 1 166 ? 2.144   -26.918 -39.432 1.00 11.31 ? 166 ILE A O   1 
ATOM   1176 C CB  . ILE A 1 166 ? 4.841   -28.716 -39.046 1.00 11.96 ? 166 ILE A CB  1 
ATOM   1177 C CG1 . ILE A 1 166 ? 4.239   -29.342 -40.302 1.00 13.05 ? 166 ILE A CG1 1 
ATOM   1178 C CG2 . ILE A 1 166 ? 5.627   -29.756 -38.238 1.00 12.89 ? 166 ILE A CG2 1 
ATOM   1179 C CD1 . ILE A 1 166 ? 5.277   -29.896 -41.272 1.00 13.56 ? 166 ILE A CD1 1 
ATOM   1180 N N   . LYS A 1 167 ? 3.643   -25.649 -38.320 1.00 10.56 ? 167 LYS A N   1 
ATOM   1181 C CA  . LYS A 1 167 ? 3.007   -24.368 -38.544 1.00 10.30 ? 167 LYS A CA  1 
ATOM   1182 C C   . LYS A 1 167 ? 3.988   -23.435 -39.241 1.00 10.21 ? 167 LYS A C   1 
ATOM   1183 O O   . LYS A 1 167 ? 5.173   -23.375 -38.876 1.00 10.58 ? 167 LYS A O   1 
ATOM   1184 C CB  . LYS A 1 167 ? 2.548   -23.824 -37.182 1.00 11.58 ? 167 LYS A CB  1 
ATOM   1185 C CG  . LYS A 1 167 ? 2.058   -22.374 -37.179 1.00 12.18 ? 167 LYS A CG  1 
ATOM   1186 C CD  . LYS A 1 167 ? 1.350   -22.014 -35.881 1.00 12.11 ? 167 LYS A CD  1 
ATOM   1187 C CE  . LYS A 1 167 ? 1.147   -20.527 -35.742 1.00 13.86 ? 167 LYS A CE  1 
ATOM   1188 N NZ  . LYS A 1 167 ? 0.234   -20.284 -34.623 1.00 15.74 ? 167 LYS A NZ  1 
ATOM   1189 N N   . THR A 1 168 ? 3.484   -22.669 -40.211 1.00 10.67 ? 168 THR A N   1 
ATOM   1190 C CA  . THR A 1 168 ? 4.438   -21.938 -41.045 1.00 10.84 ? 168 THR A CA  1 
ATOM   1191 C C   . THR A 1 168 ? 5.196   -20.862 -40.270 1.00 10.89 ? 168 THR A C   1 
ATOM   1192 O O   . THR A 1 168 ? 6.390   -20.689 -40.428 1.00 11.72 ? 168 THR A O   1 
ATOM   1193 C CB  . THR A 1 168 ? 3.780   -21.301 -42.252 1.00 11.22 ? 168 THR A CB  1 
ATOM   1194 O OG1 . THR A 1 168 ? 2.837   -20.333 -41.858 1.00 11.26 ? 168 THR A OG1 1 
ATOM   1195 C CG2 . THR A 1 168 ? 3.169   -22.333 -43.182 1.00 11.86 ? 168 THR A CG2 1 
ATOM   1196 N N   . SER A 1 169 ? 4.497   -20.076 -39.445 1.00 10.89 ? 169 SER A N   1 
ATOM   1197 C CA  . SER A 1 169 ? 4.930   -18.742 -39.111 1.00 11.07 ? 169 SER A CA  1 
ATOM   1198 C C   . SER A 1 169 ? 4.385   -18.241 -37.784 1.00 11.13 ? 169 SER A C   1 
ATOM   1199 O O   . SER A 1 169 ? 3.320   -18.678 -37.342 1.00 11.64 ? 169 SER A O   1 
ATOM   1200 C CB  . SER A 1 169 ? 4.533   -17.767 -40.216 1.00 11.58 ? 169 SER A CB  1 
ATOM   1201 O OG  . SER A 1 169 ? 4.784   -18.243 -41.533 1.00 12.44 ? 169 SER A OG  1 
ATOM   1202 N N   . THR A 1 170 ? 5.070   -17.232 -37.261 1.00 11.47 ? 170 THR A N   1 
ATOM   1203 C CA  . THR A 1 170 ? 4.595   -16.524 -36.082 1.00 11.83 ? 170 THR A CA  1 
ATOM   1204 C C   . THR A 1 170 ? 3.576   -15.431 -36.400 1.00 13.05 ? 170 THR A C   1 
ATOM   1205 O O   . THR A 1 170 ? 2.857   -14.974 -35.492 1.00 14.51 ? 170 THR A O   1 
ATOM   1206 C CB  . THR A 1 170 ? 5.740   -15.896 -35.304 1.00 12.43 ? 170 THR A CB  1 
ATOM   1207 O OG1 . THR A 1 170 ? 6.399   -14.953 -36.159 1.00 13.12 ? 170 THR A OG1 1 
ATOM   1208 C CG2 . THR A 1 170 ? 6.651   -16.946 -34.705 1.00 11.90 ? 170 THR A CG2 1 
ATOM   1209 N N   . GLY A 1 171 ? 3.617   -14.908 -37.616 1.00 13.72 ? 171 GLY A N   1 
ATOM   1210 C CA  . GLY A 1 171 ? 2.904   -13.695 -37.951 1.00 14.89 ? 171 GLY A CA  1 
ATOM   1211 C C   . GLY A 1 171 ? 3.624   -12.431 -37.490 1.00 16.05 ? 171 GLY A C   1 
ATOM   1212 O O   . GLY A 1 171 ? 3.073   -11.346 -37.640 1.00 22.00 ? 171 GLY A O   1 
ATOM   1213 N N   . ARG A 1 172 ? 4.862   -12.558 -36.975 1.00 15.53 ? 172 ARG A N   1 
ATOM   1214 C CA  . ARG A 1 172 ? 5.547   -11.426 -36.367 1.00 18.28 ? 172 ARG A CA  1 
ATOM   1215 C C   . ARG A 1 172 ? 6.797   -11.033 -37.145 1.00 18.45 ? 172 ARG A C   1 
ATOM   1216 O O   . ARG A 1 172 ? 7.542   -10.175 -36.714 1.00 22.23 ? 172 ARG A O   1 
ATOM   1217 C CB  . ARG A 1 172 ? 5.918   -11.725 -34.917 1.00 17.83 ? 172 ARG A CB  1 
ATOM   1218 C CG  . ARG A 1 172 ? 4.724   -11.998 -34.026 1.00 19.07 ? 172 ARG A CG  1 
ATOM   1219 C CD  . ARG A 1 172 ? 3.712   -10.884 -33.915 1.00 22.69 ? 172 ARG A CD  1 
ATOM   1220 N NE  . ARG A 1 172 ? 2.686   -11.165 -32.911 1.00 27.47 ? 172 ARG A NE  1 
ATOM   1221 C CZ  . ARG A 1 172 ? 1.626   -11.965 -33.085 1.00 32.51 ? 172 ARG A CZ  1 
ATOM   1222 N NH1 . ARG A 1 172 ? 1.446   -12.638 -34.229 1.00 34.29 ? 172 ARG A NH1 1 
ATOM   1223 N NH2 . ARG A 1 172 ? 0.746   -12.091 -32.101 1.00 38.21 ? 172 ARG A NH2 1 
ATOM   1224 N N   . VAL A 1 173 ? 7.019   -11.679 -38.288 1.00 17.42 ? 173 VAL A N   1 
ATOM   1225 C CA  . VAL A 1 173 ? 8.137   -11.340 -39.150 1.00 17.44 ? 173 VAL A CA  1 
ATOM   1226 C C   . VAL A 1 173 ? 7.586   -10.857 -40.486 1.00 18.74 ? 173 VAL A C   1 
ATOM   1227 O O   . VAL A 1 173 ? 6.381   -10.924 -40.755 1.00 19.93 ? 173 VAL A O   1 
ATOM   1228 C CB  . VAL A 1 173 ? 9.096   -12.530 -39.312 1.00 17.90 ? 173 VAL A CB  1 
ATOM   1229 C CG1 . VAL A 1 173 ? 9.814   -12.849 -38.003 1.00 18.09 ? 173 VAL A CG1 1 
ATOM   1230 C CG2 . VAL A 1 173 ? 8.397   -13.754 -39.880 1.00 18.21 ? 173 VAL A CG2 1 
ATOM   1231 N N   . ALA A 1 174 ? 8.491   -10.374 -41.345 1.00 20.72 ? 174 ALA A N   1 
ATOM   1232 C CA  . ALA A 1 174 ? 8.096   -9.741  -42.586 1.00 21.06 ? 174 ALA A CA  1 
ATOM   1233 C C   . ALA A 1 174 ? 7.371   -10.705 -43.528 1.00 19.42 ? 174 ALA A C   1 
ATOM   1234 O O   . ALA A 1 174 ? 6.412   -10.310 -44.195 1.00 22.76 ? 174 ALA A O   1 
ATOM   1235 C CB  . ALA A 1 174 ? 9.305   -9.164  -43.264 1.00 22.32 ? 174 ALA A CB  1 
ATOM   1236 N N   . VAL A 1 175 ? 7.849   -11.953 -43.590 1.00 18.27 ? 175 VAL A N   1 
ATOM   1237 C CA  . VAL A 1 175 ? 7.307   -12.929 -44.517 1.00 16.23 ? 175 VAL A CA  1 
ATOM   1238 C C   . VAL A 1 175 ? 6.755   -14.085 -43.712 1.00 14.50 ? 175 VAL A C   1 
ATOM   1239 O O   . VAL A 1 175 ? 7.460   -14.697 -42.923 1.00 14.10 ? 175 VAL A O   1 
ATOM   1240 C CB  . VAL A 1 175 ? 8.345   -13.428 -45.534 1.00 17.27 ? 175 VAL A CB  1 
ATOM   1241 C CG1 . VAL A 1 175 ? 7.735   -14.449 -46.474 1.00 18.69 ? 175 VAL A CG1 1 
ATOM   1242 C CG2 . VAL A 1 175 ? 8.944   -12.273 -46.301 1.00 19.14 ? 175 VAL A CG2 1 
ATOM   1243 N N   . ASN A 1 176 ? 5.474   -14.366 -43.949 1.00 14.67 ? 176 ASN A N   1 
ATOM   1244 C CA  . ASN A 1 176 ? 4.764   -15.449 -43.271 1.00 13.66 ? 176 ASN A CA  1 
ATOM   1245 C C   . ASN A 1 176 ? 4.520   -16.547 -44.305 1.00 13.52 ? 176 ASN A C   1 
ATOM   1246 O O   . ASN A 1 176 ? 5.382   -16.791 -45.136 1.00 15.40 ? 176 ASN A O   1 
ATOM   1247 C CB  . ASN A 1 176 ? 3.582   -14.877 -42.515 1.00 14.75 ? 176 ASN A CB  1 
ATOM   1248 C CG  . ASN A 1 176 ? 4.061   -13.895 -41.469 1.00 16.99 ? 176 ASN A CG  1 
ATOM   1249 O OD1 . ASN A 1 176 ? 3.994   -12.669 -41.635 1.00 24.33 ? 176 ASN A OD1 1 
ATOM   1250 N ND2 . ASN A 1 176 ? 4.671   -14.418 -40.443 1.00 15.25 ? 176 ASN A ND2 1 
ATOM   1251 N N   . ALA A 1 177 ? 3.376   -17.195 -44.321 1.00 12.51 ? 177 ALA A N   1 
ATOM   1252 C CA  . ALA A 1 177 ? 3.177   -18.321 -45.216 1.00 12.60 ? 177 ALA A CA  1 
ATOM   1253 C C   . ALA A 1 177 ? 3.176   -17.874 -46.669 1.00 11.92 ? 177 ALA A C   1 
ATOM   1254 O O   . ALA A 1 177 ? 2.784   -16.757 -46.968 1.00 13.37 ? 177 ALA A O   1 
ATOM   1255 C CB  . ALA A 1 177 ? 1.856   -18.994 -44.928 1.00 13.03 ? 177 ALA A CB  1 
ATOM   1256 N N   . THR A 1 178 ? 3.622   -18.793 -47.537 1.00 12.53 ? 178 THR A N   1 
ATOM   1257 C CA  . THR A 1 178 ? 3.397   -18.718 -48.973 1.00 12.72 ? 178 THR A CA  1 
ATOM   1258 C C   . THR A 1 178 ? 2.812   -20.044 -49.410 1.00 12.52 ? 178 THR A C   1 
ATOM   1259 O O   . THR A 1 178 ? 2.964   -21.044 -48.720 1.00 12.18 ? 178 THR A O   1 
ATOM   1260 C CB  . THR A 1 178 ? 4.673   -18.415 -49.769 1.00 13.78 ? 178 THR A CB  1 
ATOM   1261 O OG1 . THR A 1 178 ? 5.515   -19.571 -49.742 1.00 14.66 ? 178 THR A OG1 1 
ATOM   1262 C CG2 . THR A 1 178 ? 5.376   -17.179 -49.258 1.00 14.16 ? 178 THR A CG2 1 
ATOM   1263 N N   . PRO A 1 179 ? 2.178   -20.117 -50.594 1.00 13.22 ? 179 PRO A N   1 
ATOM   1264 C CA  . PRO A 1 179 ? 1.717   -21.411 -51.079 1.00 12.95 ? 179 PRO A CA  1 
ATOM   1265 C C   . PRO A 1 179 ? 2.845   -22.415 -51.224 1.00 13.04 ? 179 PRO A C   1 
ATOM   1266 O O   . PRO A 1 179 ? 2.646   -23.601 -51.017 1.00 14.23 ? 179 PRO A O   1 
ATOM   1267 C CB  . PRO A 1 179 ? 0.996   -21.105 -52.381 1.00 15.02 ? 179 PRO A CB  1 
ATOM   1268 C CG  . PRO A 1 179 ? 0.600   -19.658 -52.228 1.00 16.01 ? 179 PRO A CG  1 
ATOM   1269 C CD  . PRO A 1 179 ? 1.735   -18.990 -51.428 1.00 14.45 ? 179 PRO A CD  1 
ATOM   1270 N N   . GLU A 1 180 ? 4.030   -21.937 -51.625 1.00 13.02 ? 180 GLU A N   1 
ATOM   1271 C CA  . GLU A 1 180 ? 5.148   -22.849 -51.779 1.00 14.77 ? 180 GLU A CA  1 
ATOM   1272 C C   . GLU A 1 180 ? 5.615   -23.404 -50.441 1.00 13.03 ? 180 GLU A C   1 
ATOM   1273 O O   . GLU A 1 180 ? 5.876   -24.594 -50.334 1.00 13.00 ? 180 GLU A O   1 
ATOM   1274 C CB  . GLU A 1 180 ? 6.261   -22.152 -52.560 1.00 16.68 ? 180 GLU A CB  1 
ATOM   1275 C CG  . GLU A 1 180 ? 5.859   -21.883 -54.010 1.00 21.73 ? 180 GLU A CG  1 
ATOM   1276 C CD  . GLU A 1 180 ? 5.272   -23.092 -54.717 1.00 25.76 ? 180 GLU A CD  1 
ATOM   1277 O OE1 . GLU A 1 180 ? 5.995   -24.125 -54.668 1.00 28.12 ? 180 GLU A OE1 1 
ATOM   1278 O OE2 . GLU A 1 180 ? 4.102   -23.001 -55.232 1.00 32.41 ? 180 GLU A OE2 1 
ATOM   1279 N N   . SER A 1 181 ? 5.734   -22.553 -49.423 1.00 13.17 ? 181 SER A N   1 
ATOM   1280 C CA  . SER A 1 181 ? 6.164   -23.073 -48.133 1.00 13.96 ? 181 SER A CA  1 
ATOM   1281 C C   . SER A 1 181 ? 5.105   -24.033 -47.558 1.00 13.04 ? 181 SER A C   1 
ATOM   1282 O O   . SER A 1 181 ? 5.453   -25.056 -46.981 1.00 13.34 ? 181 SER A O   1 
ATOM   1283 C CB  . SER A 1 181 ? 6.641   -21.976 -47.211 1.00 16.13 ? 181 SER A CB  1 
ATOM   1284 O OG  . SER A 1 181 ? 5.589   -21.103 -46.886 1.00 18.54 ? 181 SER A OG  1 
ATOM   1285 N N   . ALA A 1 182 ? 3.818   -23.768 -47.794 1.00 12.41 ? 182 ALA A N   1 
ATOM   1286 C CA  . ALA A 1 182 ? 2.759   -24.692 -47.390 1.00 13.50 ? 182 ALA A CA  1 
ATOM   1287 C C   . ALA A 1 182 ? 2.891   -26.043 -48.088 1.00 13.45 ? 182 ALA A C   1 
ATOM   1288 O O   . ALA A 1 182 ? 2.832   -27.090 -47.445 1.00 14.19 ? 182 ALA A O   1 
ATOM   1289 C CB  . ALA A 1 182 ? 1.391   -24.080 -47.663 1.00 14.30 ? 182 ALA A CB  1 
ATOM   1290 N N   . ARG A 1 183 ? 3.143   -26.012 -49.411 1.00 13.55 ? 183 ARG A N   1 
ATOM   1291 C CA  . ARG A 1 183 ? 3.275   -27.239 -50.168 1.00 14.58 ? 183 ARG A CA  1 
ATOM   1292 C C   . ARG A 1 183 ? 4.466   -28.038 -49.646 1.00 13.83 ? 183 ARG A C   1 
ATOM   1293 O O   . ARG A 1 183 ? 4.387   -29.255 -49.461 1.00 14.58 ? 183 ARG A O   1 
ATOM   1294 C CB  . ARG A 1 183 ? 3.479   -26.937 -51.652 1.00 16.99 ? 183 ARG A CB  1 
ATOM   1295 C CG  . ARG A 1 183 ? 3.688   -28.179 -52.492 1.00 19.61 ? 183 ARG A CG  1 
ATOM   1296 C CD  . ARG A 1 183 ? 4.086   -27.900 -53.936 1.00 24.12 ? 183 ARG A CD  1 
ATOM   1297 N NE  . ARG A 1 183 ? 5.285   -27.055 -54.068 1.00 29.63 ? 183 ARG A NE  1 
ATOM   1298 C CZ  . ARG A 1 183 ? 6.563   -27.478 -54.023 1.00 33.43 ? 183 ARG A CZ  1 
ATOM   1299 N NH1 . ARG A 1 183 ? 6.849   -28.762 -53.914 1.00 36.73 ? 183 ARG A NH1 1 
ATOM   1300 N NH2 . ARG A 1 183 ? 7.553   -26.604 -54.099 1.00 37.19 ? 183 ARG A NH2 1 
ATOM   1301 N N   . ILE A 1 184 ? 5.596   -27.347 -49.432 1.00 13.37 ? 184 ILE A N   1 
ATOM   1302 C CA  . ILE A 1 184 ? 6.786   -28.037 -48.964 1.00 13.14 ? 184 ILE A CA  1 
ATOM   1303 C C   . ILE A 1 184 ? 6.516   -28.763 -47.645 1.00 12.78 ? 184 ILE A C   1 
ATOM   1304 O O   . ILE A 1 184 ? 6.859   -29.928 -47.455 1.00 14.31 ? 184 ILE A O   1 
ATOM   1305 C CB  . ILE A 1 184 ? 7.966   -27.065 -48.849 1.00 15.29 ? 184 ILE A CB  1 
ATOM   1306 C CG1 . ILE A 1 184 ? 8.390   -26.573 -50.211 1.00 16.52 ? 184 ILE A CG1 1 
ATOM   1307 C CG2 . ILE A 1 184 ? 9.149   -27.704 -48.124 1.00 15.04 ? 184 ILE A CG2 1 
ATOM   1308 C CD1 . ILE A 1 184 ? 9.238   -25.310 -50.204 1.00 16.78 ? 184 ILE A CD1 1 
ATOM   1309 N N   . MET A 1 185 ? 5.888   -28.050 -46.703 1.00 12.57 ? 185 MET A N   1 
ATOM   1310 C CA  . MET A 1 185 ? 5.653   -28.628 -45.391 1.00 12.36 ? 185 MET A CA  1 
ATOM   1311 C C   . MET A 1 185 ? 4.688   -29.815 -45.471 1.00 12.51 ? 185 MET A C   1 
ATOM   1312 O O   . MET A 1 185 ? 4.878   -30.839 -44.814 1.00 12.93 ? 185 MET A O   1 
ATOM   1313 C CB  . MET A 1 185 ? 5.130   -27.532 -44.460 1.00 12.04 ? 185 MET A CB  1 
ATOM   1314 C CG  . MET A 1 185 ? 6.179   -26.532 -44.123 1.00 12.80 ? 185 MET A CG  1 
ATOM   1315 S SD  . MET A 1 185 ? 5.663   -25.178 -43.071 1.00 13.13 ? 185 MET A SD  1 
ATOM   1316 C CE  . MET A 1 185 ? 5.433   -26.026 -41.502 1.00 15.00 ? 185 MET A CE  1 
ATOM   1317 N N   . MET A 1 186 ? 3.631   -29.680 -46.277 1.00 12.65 ? 186 MET A N   1 
ATOM   1318 C CA  . MET A 1 186 ? 2.709   -30.786 -46.412 1.00 13.23 ? 186 MET A CA  1 
ATOM   1319 C C   . MET A 1 186 ? 3.339   -31.972 -47.143 1.00 13.18 ? 186 MET A C   1 
ATOM   1320 O O   . MET A 1 186 ? 3.038   -33.118 -46.830 1.00 14.20 ? 186 MET A O   1 
ATOM   1321 C CB  . MET A 1 186 ? 1.406   -30.339 -47.065 1.00 13.57 ? 186 MET A CB  1 
ATOM   1322 C CG  . MET A 1 186 ? 0.519   -29.616 -46.076 1.00 14.87 ? 186 MET A CG  1 
ATOM   1323 S SD  . MET A 1 186 ? -1.083  -29.169 -46.741 1.00 17.18 ? 186 MET A SD  1 
ATOM   1324 C CE  . MET A 1 186 ? -0.723  -27.542 -47.424 1.00 18.55 ? 186 MET A CE  1 
ATOM   1325 N N   . GLU A 1 187 ? 4.265   -31.708 -48.086 1.00 14.03 ? 187 GLU A N   1 
ATOM   1326 C CA  . GLU A 1 187 ? 4.991   -32.794 -48.706 1.00 14.78 ? 187 GLU A CA  1 
ATOM   1327 C C   . GLU A 1 187 ? 5.840   -33.549 -47.687 1.00 14.55 ? 187 GLU A C   1 
ATOM   1328 O O   . GLU A 1 187 ? 5.977   -34.762 -47.791 1.00 16.70 ? 187 GLU A O   1 
ATOM   1329 C CB  . GLU A 1 187 ? 5.887   -32.280 -49.830 1.00 16.35 ? 187 GLU A CB  1 
ATOM   1330 C CG  . GLU A 1 187 ? 5.132   -31.864 -51.076 1.00 18.57 ? 187 GLU A CG  1 
ATOM   1331 C CD  . GLU A 1 187 ? 6.018   -31.302 -52.173 1.00 22.47 ? 187 GLU A CD  1 
ATOM   1332 O OE1 . GLU A 1 187 ? 7.230   -31.118 -51.953 1.00 29.60 ? 187 GLU A OE1 1 
ATOM   1333 O OE2 . GLU A 1 187 ? 5.461   -31.036 -53.244 1.00 26.51 ? 187 GLU A OE2 1 
ATOM   1334 N N   . VAL A 1 188 ? 6.425   -32.844 -46.711 1.00 14.26 ? 188 VAL A N   1 
ATOM   1335 C CA  . VAL A 1 188 ? 7.180   -33.552 -45.686 1.00 14.88 ? 188 VAL A CA  1 
ATOM   1336 C C   . VAL A 1 188 ? 6.268   -34.498 -44.897 1.00 14.46 ? 188 VAL A C   1 
ATOM   1337 O O   . VAL A 1 188 ? 6.620   -35.643 -44.640 1.00 15.76 ? 188 VAL A O   1 
ATOM   1338 C CB  . VAL A 1 188 ? 7.896   -32.576 -44.732 1.00 15.10 ? 188 VAL A CB  1 
ATOM   1339 C CG1 . VAL A 1 188 ? 8.551   -33.330 -43.588 1.00 14.61 ? 188 VAL A CG1 1 
ATOM   1340 C CG2 . VAL A 1 188 ? 8.922   -31.713 -45.466 1.00 15.52 ? 188 VAL A CG2 1 
ATOM   1341 N N   . ILE A 1 189 ? 5.084   -34.009 -44.516 1.00 13.68 ? 189 ILE A N   1 
ATOM   1342 C CA  . ILE A 1 189 ? 4.123   -34.853 -43.817 1.00 13.88 ? 189 ILE A CA  1 
ATOM   1343 C C   . ILE A 1 189 ? 3.822   -36.107 -44.631 1.00 14.12 ? 189 ILE A C   1 
ATOM   1344 O O   . ILE A 1 189 ? 3.858   -37.224 -44.126 1.00 15.83 ? 189 ILE A O   1 
ATOM   1345 C CB  . ILE A 1 189 ? 2.840   -34.053 -43.526 1.00 13.48 ? 189 ILE A CB  1 
ATOM   1346 C CG1 . ILE A 1 189 ? 3.088   -32.958 -42.487 1.00 13.95 ? 189 ILE A CG1 1 
ATOM   1347 C CG2 . ILE A 1 189 ? 1.698   -34.966 -43.066 1.00 14.12 ? 189 ILE A CG2 1 
ATOM   1348 C CD1 . ILE A 1 189 ? 1.919   -32.002 -42.294 1.00 13.07 ? 189 ILE A CD1 1 
ATOM   1349 N N   . ARG A 1 190 ? 3.546   -35.904 -45.930 1.00 15.51 ? 190 ARG A N   1 
ATOM   1350 C CA  . ARG A 1 190 ? 3.217   -37.015 -46.795 1.00 17.04 ? 190 ARG A CA  1 
ATOM   1351 C C   . ARG A 1 190 ? 4.409   -37.968 -46.920 1.00 18.11 ? 190 ARG A C   1 
ATOM   1352 O O   . ARG A 1 190 ? 4.252   -39.180 -46.785 1.00 19.79 ? 190 ARG A O   1 
ATOM   1353 C CB  . ARG A 1 190 ? 2.822   -36.458 -48.157 1.00 18.55 ? 190 ARG A CB  1 
ATOM   1354 C CG  . ARG A 1 190 ? 2.340   -37.540 -49.100 1.00 20.66 ? 190 ARG A CG  1 
ATOM   1355 C CD  . ARG A 1 190 ? 2.343   -37.062 -50.513 1.00 23.58 ? 190 ARG A CD  1 
ATOM   1356 N NE  . ARG A 1 190 ? 3.712   -36.764 -50.928 1.00 25.36 ? 190 ARG A NE  1 
ATOM   1357 C CZ  . ARG A 1 190 ? 4.022   -36.204 -52.082 1.00 28.81 ? 190 ARG A CZ  1 
ATOM   1358 N NH1 . ARG A 1 190 ? 3.069   -35.957 -52.952 1.00 28.39 ? 190 ARG A NH1 1 
ATOM   1359 N NH2 . ARG A 1 190 ? 5.280   -35.894 -52.360 1.00 30.70 ? 190 ARG A NH2 1 
ATOM   1360 N N   . ASP A 1 191 ? 5.604   -37.407 -47.178 1.00 19.25 ? 191 ASP A N   1 
ATOM   1361 C CA  . ASP A 1 191 ? 6.772   -38.224 -47.476 1.00 21.19 ? 191 ASP A CA  1 
ATOM   1362 C C   . ASP A 1 191 ? 7.181   -39.052 -46.261 1.00 19.35 ? 191 ASP A C   1 
ATOM   1363 O O   . ASP A 1 191 ? 7.639   -40.182 -46.380 1.00 21.15 ? 191 ASP A O   1 
ATOM   1364 C CB  . ASP A 1 191 ? 7.927   -37.366 -47.969 1.00 22.33 ? 191 ASP A CB  1 
ATOM   1365 C CG  . ASP A 1 191 ? 7.715   -36.750 -49.345 1.00 24.08 ? 191 ASP A CG  1 
ATOM   1366 O OD1 . ASP A 1 191 ? 6.749   -37.158 -50.046 1.00 27.15 ? 191 ASP A OD1 1 
ATOM   1367 O OD2 . ASP A 1 191 ? 8.481   -35.833 -49.681 1.00 26.40 ? 191 ASP A OD2 1 
ATOM   1368 N N   . MET A 1 192 ? 7.026   -38.472 -45.073 1.00 18.35 ? 192 MET A N   1 
ATOM   1369 C CA  . MET A 1 192 ? 7.355   -39.164 -43.843 1.00 19.17 ? 192 MET A CA  1 
ATOM   1370 C C   . MET A 1 192 ? 6.289   -40.169 -43.421 1.00 19.84 ? 192 MET A C   1 
ATOM   1371 O O   . MET A 1 192 ? 6.505   -40.913 -42.471 1.00 21.39 ? 192 MET A O   1 
ATOM   1372 C CB  . MET A 1 192 ? 7.596   -38.135 -42.747 1.00 19.04 ? 192 MET A CB  1 
ATOM   1373 C CG  . MET A 1 192 ? 8.852   -37.350 -42.994 1.00 19.96 ? 192 MET A CG  1 
ATOM   1374 S SD  . MET A 1 192 ? 9.251   -36.251 -41.632 1.00 20.50 ? 192 MET A SD  1 
ATOM   1375 C CE  . MET A 1 192 ? 9.880   -37.373 -40.389 1.00 21.76 ? 192 MET A CE  1 
ATOM   1376 N N   . GLY A 1 193 ? 5.126   -40.156 -44.084 1.00 20.84 ? 193 GLY A N   1 
ATOM   1377 C CA  . GLY A 1 193 ? 4.066   -41.112 -43.808 1.00 20.59 ? 193 GLY A CA  1 
ATOM   1378 C C   . GLY A 1 193 ? 3.301   -40.813 -42.513 1.00 20.28 ? 193 GLY A C   1 
ATOM   1379 O O   . GLY A 1 193 ? 2.756   -41.734 -41.886 1.00 22.27 ? 193 GLY A O   1 
ATOM   1380 N N   . VAL A 1 194 ? 3.278   -39.532 -42.116 1.00 17.50 ? 194 VAL A N   1 
ATOM   1381 C CA  . VAL A 1 194 ? 2.755   -39.140 -40.819 1.00 16.30 ? 194 VAL A CA  1 
ATOM   1382 C C   . VAL A 1 194 ? 1.444   -38.370 -40.945 1.00 15.30 ? 194 VAL A C   1 
ATOM   1383 O O   . VAL A 1 194 ? 1.049   -37.688 -40.014 1.00 16.66 ? 194 VAL A O   1 
ATOM   1384 C CB  . VAL A 1 194 ? 3.781   -38.380 -39.972 1.00 15.86 ? 194 VAL A CB  1 
ATOM   1385 C CG1 . VAL A 1 194 ? 4.959   -39.285 -39.624 1.00 17.47 ? 194 VAL A CG1 1 
ATOM   1386 C CG2 . VAL A 1 194 ? 4.181   -37.055 -40.592 1.00 15.69 ? 194 VAL A CG2 1 
ATOM   1387 N N   . GLU A 1 195 ? 0.759   -38.471 -42.083 1.00 16.54 ? 195 GLU A N   1 
ATOM   1388 C CA  . GLU A 1 195 ? -0.450  -37.699 -42.307 1.00 16.68 ? 195 GLU A CA  1 
ATOM   1389 C C   . GLU A 1 195 ? -1.538  -38.029 -41.284 1.00 17.03 ? 195 GLU A C   1 
ATOM   1390 O O   . GLU A 1 195 ? -2.389  -37.194 -41.049 1.00 18.35 ? 195 GLU A O   1 
ATOM   1391 C CB  . GLU A 1 195 ? -0.930  -37.824 -43.753 1.00 18.97 ? 195 GLU A CB  1 
ATOM   1392 C CG  . GLU A 1 195 ? -1.515  -39.188 -44.102 1.00 21.98 ? 195 GLU A CG  1 
ATOM   1393 C CD  . GLU A 1 195 ? -0.551  -40.326 -44.375 1.00 27.68 ? 195 GLU A CD  1 
ATOM   1394 O OE1 . GLU A 1 195 ? 0.680   -40.108 -44.376 1.00 29.00 ? 195 GLU A OE1 1 
ATOM   1395 O OE2 . GLU A 1 195 ? -1.076  -41.441 -44.607 1.00 35.04 ? 195 GLU A OE2 1 
ATOM   1396 N N   . LYS A 1 196 ? -1.536  -39.212 -40.679 1.00 17.55 ? 196 LYS A N   1 
ATOM   1397 C CA  . LYS A 1 196 ? -2.570  -39.511 -39.699 1.00 19.11 ? 196 LYS A CA  1 
ATOM   1398 C C   . LYS A 1 196 ? -2.351  -38.713 -38.420 1.00 18.17 ? 196 LYS A C   1 
ATOM   1399 O O   . LYS A 1 196 ? -3.328  -38.300 -37.791 1.00 20.23 ? 196 LYS A O   1 
ATOM   1400 C CB  . LYS A 1 196 ? -2.658  -41.002 -39.400 1.00 22.56 ? 196 LYS A CB  1 
ATOM   1401 C CG  . LYS A 1 196 ? -3.318  -41.779 -40.501 1.00 29.22 ? 196 LYS A CG  1 
ATOM   1402 C CD  . LYS A 1 196 ? -3.430  -43.265 -40.171 1.00 36.33 ? 196 LYS A CD  1 
ATOM   1403 C CE  . LYS A 1 196 ? -4.569  -43.928 -40.862 1.00 41.43 ? 196 LYS A CE  1 
ATOM   1404 N NZ  . LYS A 1 196 ? -4.473  -43.751 -42.308 1.00 44.22 ? 196 LYS A NZ  1 
ATOM   1405 N N   . SER A 1 197 ? -1.093  -38.440 -38.071 1.00 16.64 ? 197 SER A N   1 
ATOM   1406 C CA  . SER A 1 197 ? -0.742  -37.929 -36.748 1.00 17.41 ? 197 SER A CA  1 
ATOM   1407 C C   . SER A 1 197 ? -0.261  -36.476 -36.746 1.00 15.69 ? 197 SER A C   1 
ATOM   1408 O O   . SER A 1 197 ? -0.124  -35.882 -35.669 1.00 16.69 ? 197 SER A O   1 
ATOM   1409 C CB  . SER A 1 197 ? 0.300   -38.811 -36.106 1.00 20.53 ? 197 SER A CB  1 
ATOM   1410 O OG  . SER A 1 197 ? 1.480   -38.882 -36.894 1.00 21.36 ? 197 SER A OG  1 
ATOM   1411 N N   . VAL A 1 198 ? 0.009   -35.890 -37.918 1.00 14.23 ? 198 VAL A N   1 
ATOM   1412 C CA  . VAL A 1 198 ? 0.583   -34.555 -37.973 1.00 13.53 ? 198 VAL A CA  1 
ATOM   1413 C C   . VAL A 1 198 ? -0.287  -33.684 -38.870 1.00 13.40 ? 198 VAL A C   1 
ATOM   1414 O O   . VAL A 1 198 ? -0.527  -34.012 -40.030 1.00 14.41 ? 198 VAL A O   1 
ATOM   1415 C CB  . VAL A 1 198 ? 2.043   -34.576 -38.492 1.00 14.15 ? 198 VAL A CB  1 
ATOM   1416 C CG1 . VAL A 1 198 ? 2.619   -33.161 -38.515 1.00 14.21 ? 198 VAL A CG1 1 
ATOM   1417 C CG2 . VAL A 1 198 ? 2.891   -35.495 -37.611 1.00 15.20 ? 198 VAL A CG2 1 
ATOM   1418 N N   . GLY A 1 199 ? -0.696  -32.536 -38.337 1.00 12.25 ? 199 GLY A N   1 
ATOM   1419 C CA  . GLY A 1 199 ? -1.414  -31.541 -39.081 1.00 11.57 ? 199 GLY A CA  1 
ATOM   1420 C C   . GLY A 1 199 ? -0.508  -30.421 -39.588 1.00 10.55 ? 199 GLY A C   1 
ATOM   1421 O O   . GLY A 1 199 ? 0.672   -30.326 -39.229 1.00 10.65 ? 199 GLY A O   1 
ATOM   1422 N N   . PHE A 1 200 ? -1.116  -29.547 -40.374 1.00 10.73 ? 200 PHE A N   1 
ATOM   1423 C CA  . PHE A 1 200 ? -0.462  -28.401 -40.965 1.00 10.80 ? 200 PHE A CA  1 
ATOM   1424 C C   . PHE A 1 200 ? -1.245  -27.136 -40.631 1.00 10.62 ? 200 PHE A C   1 
ATOM   1425 O O   . PHE A 1 200 ? -2.485  -27.145 -40.743 1.00 11.43 ? 200 PHE A O   1 
ATOM   1426 C CB  . PHE A 1 200 ? -0.391  -28.580 -42.485 1.00 11.66 ? 200 PHE A CB  1 
ATOM   1427 C CG  . PHE A 1 200 ? 0.094   -27.326 -43.188 1.00 11.55 ? 200 PHE A CG  1 
ATOM   1428 C CD1 . PHE A 1 200 ? 1.409   -26.905 -43.071 1.00 12.64 ? 200 PHE A CD1 1 
ATOM   1429 C CD2 . PHE A 1 200 ? -0.794  -26.496 -43.854 1.00 13.10 ? 200 PHE A CD2 1 
ATOM   1430 C CE1 . PHE A 1 200 ? 1.811   -25.712 -43.618 1.00 13.14 ? 200 PHE A CE1 1 
ATOM   1431 C CE2 . PHE A 1 200 ? -0.366  -25.326 -44.442 1.00 14.46 ? 200 PHE A CE2 1 
ATOM   1432 C CZ  . PHE A 1 200 ? 0.946   -24.930 -44.307 1.00 13.49 ? 200 PHE A CZ  1 
ATOM   1433 N N   A LYS A 1 201 ? -0.552  -26.065 -40.229 0.50 11.13 ? 201 LYS A N   1 
ATOM   1434 N N   B LYS A 1 201 ? -0.550  -26.067 -40.235 0.50 10.97 ? 201 LYS A N   1 
ATOM   1435 C CA  A LYS A 1 201 ? -1.203  -24.796 -39.951 0.50 11.39 ? 201 LYS A CA  1 
ATOM   1436 C CA  B LYS A 1 201 ? -1.201  -24.801 -39.958 0.50 11.12 ? 201 LYS A CA  1 
ATOM   1437 C C   A LYS A 1 201 ? -0.553  -23.669 -40.740 0.50 11.48 ? 201 LYS A C   1 
ATOM   1438 C C   B LYS A 1 201 ? -0.552  -23.669 -40.742 0.50 11.37 ? 201 LYS A C   1 
ATOM   1439 O O   A LYS A 1 201 ? 0.671   -23.483 -40.694 0.50 12.55 ? 201 LYS A O   1 
ATOM   1440 O O   B LYS A 1 201 ? 0.671   -23.482 -40.694 0.50 12.44 ? 201 LYS A O   1 
ATOM   1441 C CB  A LYS A 1 201 ? -1.232  -24.468 -38.452 0.50 12.00 ? 201 LYS A CB  1 
ATOM   1442 C CB  B LYS A 1 201 ? -1.214  -24.494 -38.458 0.50 11.31 ? 201 LYS A CB  1 
ATOM   1443 C CG  A LYS A 1 201 ? -1.798  -23.091 -38.147 0.50 12.61 ? 201 LYS A CG  1 
ATOM   1444 C CG  B LYS A 1 201 ? -1.776  -23.130 -38.166 0.50 11.76 ? 201 LYS A CG  1 
ATOM   1445 C CD  A LYS A 1 201 ? -2.182  -22.902 -36.679 0.50 13.07 ? 201 LYS A CD  1 
ATOM   1446 C CD  B LYS A 1 201 ? -2.187  -22.949 -36.712 0.50 12.08 ? 201 LYS A CD  1 
ATOM   1447 C CE  A LYS A 1 201 ? -2.447  -21.465 -36.317 0.50 14.09 ? 201 LYS A CE  1 
ATOM   1448 C CE  B LYS A 1 201 ? -3.046  -21.743 -36.642 0.50 13.22 ? 201 LYS A CE  1 
ATOM   1449 N NZ  A LYS A 1 201 ? -2.631  -21.300 -34.874 0.50 14.52 ? 201 LYS A NZ  1 
ATOM   1450 N NZ  B LYS A 1 201 ? -2.239  -20.529 -36.542 0.50 13.35 ? 201 LYS A NZ  1 
ATOM   1451 N N   . VAL A 1 202 ? -1.380  -22.932 -41.471 1.00 11.82 ? 202 VAL A N   1 
ATOM   1452 C CA  . VAL A 1 202 ? -0.955  -21.757 -42.225 1.00 12.21 ? 202 VAL A CA  1 
ATOM   1453 C C   . VAL A 1 202 ? -1.170  -20.514 -41.380 1.00 11.57 ? 202 VAL A C   1 
ATOM   1454 O O   . VAL A 1 202 ? -2.294  -20.289 -40.924 1.00 13.22 ? 202 VAL A O   1 
ATOM   1455 C CB  . VAL A 1 202 ? -1.636  -21.641 -43.594 1.00 15.65 ? 202 VAL A CB  1 
ATOM   1456 C CG1 . VAL A 1 202 ? -3.098  -21.875 -43.620 1.00 19.27 ? 202 VAL A CG1 1 
ATOM   1457 C CG2 . VAL A 1 202 ? -1.304  -20.329 -44.299 1.00 17.76 ? 202 VAL A CG2 1 
ATOM   1458 N N   . THR A 1 203 ? -0.112  -19.726 -41.178 1.00 11.93 ? 203 THR A N   1 
ATOM   1459 C CA  . THR A 1 203 ? -0.217  -18.438 -40.542 1.00 12.66 ? 203 THR A CA  1 
ATOM   1460 C C   . THR A 1 203 ? 0.266   -17.378 -41.497 1.00 12.84 ? 203 THR A C   1 
ATOM   1461 O O   . THR A 1 203 ? 1.415   -17.470 -41.970 1.00 13.33 ? 203 THR A O   1 
ATOM   1462 C CB  . THR A 1 203 ? 0.526   -18.404 -39.212 1.00 14.31 ? 203 THR A CB  1 
ATOM   1463 O OG1 . THR A 1 203 ? -0.227  -19.184 -38.288 1.00 17.74 ? 203 THR A OG1 1 
ATOM   1464 C CG2 . THR A 1 203 ? 0.640   -16.989 -38.670 1.00 14.53 ? 203 THR A CG2 1 
ATOM   1465 N N   . GLY A 1 204 ? -0.569  -16.370 -41.717 1.00 14.39 ? 204 GLY A N   1 
ATOM   1466 C CA  . GLY A 1 204 ? -0.261  -15.321 -42.664 1.00 17.06 ? 204 GLY A CA  1 
ATOM   1467 C C   . GLY A 1 204 ? -0.462  -15.794 -44.099 1.00 18.75 ? 204 GLY A C   1 
ATOM   1468 O O   . GLY A 1 204 ? -0.698  -16.959 -44.366 1.00 19.44 ? 204 GLY A O   1 
ATOM   1469 N N   . GLY A 1 205 ? -0.380  -14.856 -45.038 1.00 22.35 ? 205 GLY A N   1 
ATOM   1470 C CA  . GLY A 1 205 ? -0.480  -15.152 -46.452 1.00 23.83 ? 205 GLY A CA  1 
ATOM   1471 C C   . GLY A 1 205 ? -1.887  -15.550 -46.911 1.00 25.47 ? 205 GLY A C   1 
ATOM   1472 O O   . GLY A 1 205 ? -2.084  -15.824 -48.088 1.00 32.18 ? 205 GLY A O   1 
ATOM   1473 N N   . VAL A 1 206 ? -2.903  -15.492 -46.051 1.00 28.23 ? 206 VAL A N   1 
ATOM   1474 C CA  . VAL A 1 206 ? -4.232  -15.944 -46.419 1.00 29.44 ? 206 VAL A CA  1 
ATOM   1475 C C   . VAL A 1 206 ? -5.212  -14.830 -46.059 1.00 30.09 ? 206 VAL A C   1 
ATOM   1476 O O   . VAL A 1 206 ? -5.914  -14.873 -45.041 1.00 32.40 ? 206 VAL A O   1 
ATOM   1477 C CB  . VAL A 1 206 ? -4.671  -17.270 -45.764 1.00 29.39 ? 206 VAL A CB  1 
ATOM   1478 C CG1 . VAL A 1 206 ? -5.964  -17.801 -46.377 1.00 30.13 ? 206 VAL A CG1 1 
ATOM   1479 C CG2 . VAL A 1 206 ? -3.626  -18.357 -45.844 1.00 31.03 ? 206 VAL A CG2 1 
ATOM   1480 N N   . SER A 1 207 ? -5.250  -13.822 -46.922 1.00 30.65 ? 207 SER A N   1 
ATOM   1481 C CA  . SER A 1 207 ? -5.975  -12.602 -46.648 1.00 33.07 ? 207 SER A CA  1 
ATOM   1482 C C   . SER A 1 207 ? -7.432  -12.783 -47.041 1.00 31.20 ? 207 SER A C   1 
ATOM   1483 O O   . SER A 1 207 ? -8.286  -12.163 -46.445 1.00 32.60 ? 207 SER A O   1 
ATOM   1484 C CB  . SER A 1 207 ? -5.387  -11.436 -47.373 1.00 35.79 ? 207 SER A CB  1 
ATOM   1485 O OG  . SER A 1 207 ? -3.975  -11.455 -47.260 1.00 40.17 ? 207 SER A OG  1 
ATOM   1486 N N   . THR A 1 208 ? -7.696  -13.612 -48.057 1.00 27.55 ? 208 THR A N   1 
ATOM   1487 C CA  . THR A 1 208 ? -9.019  -13.683 -48.633 1.00 27.29 ? 208 THR A CA  1 
ATOM   1488 C C   . THR A 1 208 ? -9.527  -15.114 -48.643 1.00 24.37 ? 208 THR A C   1 
ATOM   1489 O O   . THR A 1 208 ? -8.771  -16.078 -48.569 1.00 21.63 ? 208 THR A O   1 
ATOM   1490 C CB  . THR A 1 208 ? -8.988  -13.125 -50.057 1.00 27.75 ? 208 THR A CB  1 
ATOM   1491 O OG1 . THR A 1 208 ? -8.258  -14.050 -50.863 1.00 26.92 ? 208 THR A OG1 1 
ATOM   1492 C CG2 . THR A 1 208 ? -8.418  -11.719 -50.120 1.00 29.50 ? 208 THR A CG2 1 
ATOM   1493 N N   . ALA A 1 209 ? -10.836 -15.209 -48.838 1.00 24.14 ? 209 ALA A N   1 
ATOM   1494 C CA  . ALA A 1 209 ? -11.520 -16.464 -49.063 1.00 24.64 ? 209 ALA A CA  1 
ATOM   1495 C C   . ALA A 1 209 ? -10.899 -17.202 -50.248 1.00 22.69 ? 209 ALA A C   1 
ATOM   1496 O O   . ALA A 1 209 ? -10.722 -18.420 -50.178 1.00 23.09 ? 209 ALA A O   1 
ATOM   1497 C CB  . ALA A 1 209 ? -12.993 -16.189 -49.284 1.00 24.71 ? 209 ALA A CB  1 
ATOM   1498 N N   . GLU A 1 210 ? -10.525 -16.474 -51.313 1.00 24.28 ? 210 GLU A N   1 
ATOM   1499 C CA  . GLU A 1 210 ? -9.897  -17.098 -52.473 1.00 22.98 ? 210 GLU A CA  1 
ATOM   1500 C C   . GLU A 1 210 ? -8.535  -17.708 -52.111 1.00 21.62 ? 210 GLU A C   1 
ATOM   1501 O O   . GLU A 1 210 ? -8.183  -18.800 -52.553 1.00 22.57 ? 210 GLU A O   1 
ATOM   1502 C CB  . GLU A 1 210 ? -9.741  -16.120 -53.641 1.00 25.64 ? 210 GLU A CB  1 
ATOM   1503 C CG  . GLU A 1 210 ? -11.093 -15.671 -54.202 1.00 29.66 ? 210 GLU A CG  1 
ATOM   1504 C CD  . GLU A 1 210 ? -11.785 -14.520 -53.497 1.00 32.27 ? 210 GLU A CD  1 
ATOM   1505 O OE1 . GLU A 1 210 ? -11.339 -14.019 -52.436 1.00 33.96 ? 210 GLU A OE1 1 
ATOM   1506 O OE2 . GLU A 1 210 ? -12.850 -14.136 -54.026 1.00 38.94 ? 210 GLU A OE2 1 
ATOM   1507 N N   . ASP A 1 211 ? -7.769  -17.002 -51.295 1.00 19.89 ? 211 ASP A N   1 
ATOM   1508 C CA  . ASP A 1 211 ? -6.519  -17.544 -50.794 1.00 19.93 ? 211 ASP A CA  1 
ATOM   1509 C C   . ASP A 1 211 ? -6.757  -18.823 -49.999 1.00 18.97 ? 211 ASP A C   1 
ATOM   1510 O O   . ASP A 1 211 ? -6.027  -19.799 -50.161 1.00 18.72 ? 211 ASP A O   1 
ATOM   1511 C CB  . ASP A 1 211 ? -5.788  -16.541 -49.918 1.00 21.52 ? 211 ASP A CB  1 
ATOM   1512 C CG  . ASP A 1 211 ? -5.318  -15.267 -50.602 1.00 24.96 ? 211 ASP A CG  1 
ATOM   1513 O OD1 . ASP A 1 211 ? -4.960  -15.333 -51.790 1.00 28.25 ? 211 ASP A OD1 1 
ATOM   1514 O OD2 . ASP A 1 211 ? -5.285  -14.224 -49.922 1.00 28.02 ? 211 ASP A OD2 1 
ATOM   1515 N N   . ALA A 1 212 ? -7.766  -18.810 -49.105 1.00 18.40 ? 212 ALA A N   1 
ATOM   1516 C CA  . ALA A 1 212 ? -8.002  -19.971 -48.270 1.00 17.89 ? 212 ALA A CA  1 
ATOM   1517 C C   . ALA A 1 212 ? -8.310  -21.190 -49.148 1.00 18.41 ? 212 ALA A C   1 
ATOM   1518 O O   . ALA A 1 212 ? -7.883  -22.313 -48.854 1.00 18.49 ? 212 ALA A O   1 
ATOM   1519 C CB  . ALA A 1 212 ? -9.121  -19.674 -47.317 1.00 18.71 ? 212 ALA A CB  1 
ATOM   1520 N N   . GLN A 1 213 ? -9.095  -20.959 -50.207 1.00 18.81 ? 213 GLN A N   1 
ATOM   1521 C CA  . GLN A 1 213 ? -9.463  -22.041 -51.099 1.00 19.97 ? 213 GLN A CA  1 
ATOM   1522 C C   . GLN A 1 213 ? -8.209  -22.674 -51.698 1.00 18.97 ? 213 GLN A C   1 
ATOM   1523 O O   . GLN A 1 213 ? -8.126  -23.894 -51.831 1.00 19.94 ? 213 GLN A O   1 
ATOM   1524 C CB  . GLN A 1 213 ? -10.433 -21.485 -52.133 1.00 23.13 ? 213 GLN A CB  1 
ATOM   1525 C CG  . GLN A 1 213 ? -10.906 -22.530 -53.124 1.00 24.90 ? 213 GLN A CG  1 
ATOM   1526 C CD  . GLN A 1 213 ? -11.843 -21.922 -54.132 1.00 29.50 ? 213 GLN A CD  1 
ATOM   1527 O OE1 . GLN A 1 213 ? -11.459 -21.047 -54.913 1.00 36.27 ? 213 GLN A OE1 1 
ATOM   1528 N NE2 . GLN A 1 213 ? -13.100 -22.333 -54.087 1.00 33.42 ? 213 GLN A NE2 1 
ATOM   1529 N N   . LYS A 1 214 ? -7.234  -21.839 -52.084 1.00 19.31 ? 214 LYS A N   1 
ATOM   1530 C CA  . LYS A 1 214 ? -6.027  -22.344 -52.708 1.00 19.20 ? 214 LYS A CA  1 
ATOM   1531 C C   . LYS A 1 214 ? -5.212  -23.164 -51.714 1.00 18.04 ? 214 LYS A C   1 
ATOM   1532 O O   . LYS A 1 214 ? -4.729  -24.236 -52.036 1.00 19.75 ? 214 LYS A O   1 
ATOM   1533 C CB  . LYS A 1 214 ? -5.191  -21.181 -53.240 1.00 22.18 ? 214 LYS A CB  1 
ATOM   1534 C CG  . LYS A 1 214 ? -3.985  -21.673 -53.927 1.00 26.24 ? 214 LYS A CG  1 
ATOM   1535 C CD  . LYS A 1 214 ? -3.256  -20.528 -54.594 1.00 30.48 ? 214 LYS A CD  1 
ATOM   1536 C CE  . LYS A 1 214 ? -2.822  -19.461 -53.634 1.00 32.21 ? 214 LYS A CE  1 
ATOM   1537 N NZ  . LYS A 1 214 ? -2.128  -18.443 -54.434 1.00 35.29 ? 214 LYS A NZ  1 
ATOM   1538 N N   . TYR A 1 215 ? -5.079  -22.677 -50.478 1.00 16.86 ? 215 TYR A N   1 
ATOM   1539 C CA  . TYR A 1 215 ? -4.310  -23.413 -49.483 1.00 15.39 ? 215 TYR A CA  1 
ATOM   1540 C C   . TYR A 1 215 ? -4.965  -24.750 -49.157 1.00 15.52 ? 215 TYR A C   1 
ATOM   1541 O O   . TYR A 1 215 ? -4.278  -25.752 -48.952 1.00 16.02 ? 215 TYR A O   1 
ATOM   1542 C CB  . TYR A 1 215 ? -4.116  -22.569 -48.222 1.00 14.99 ? 215 TYR A CB  1 
ATOM   1543 C CG  . TYR A 1 215 ? -2.978  -21.562 -48.320 1.00 14.93 ? 215 TYR A CG  1 
ATOM   1544 C CD1 . TYR A 1 215 ? -1.695  -21.900 -47.953 1.00 14.84 ? 215 TYR A CD1 1 
ATOM   1545 C CD2 . TYR A 1 215 ? -3.193  -20.251 -48.712 1.00 18.68 ? 215 TYR A CD2 1 
ATOM   1546 C CE1 . TYR A 1 215 ? -0.651  -20.998 -48.047 1.00 14.84 ? 215 TYR A CE1 1 
ATOM   1547 C CE2 . TYR A 1 215 ? -2.154  -19.336 -48.814 1.00 19.00 ? 215 TYR A CE2 1 
ATOM   1548 C CZ  . TYR A 1 215 ? -0.878  -19.702 -48.446 1.00 16.51 ? 215 TYR A CZ  1 
ATOM   1549 O OH  . TYR A 1 215 ? 0.126   -18.785 -48.457 1.00 16.81 ? 215 TYR A OH  1 
ATOM   1550 N N   . LEU A 1 216 ? -6.302  -24.768 -49.078 1.00 15.65 ? 216 LEU A N   1 
ATOM   1551 C CA  . LEU A 1 216 ? -7.006  -26.024 -48.860 1.00 16.64 ? 216 LEU A CA  1 
ATOM   1552 C C   . LEU A 1 216 ? -6.806  -26.975 -50.028 1.00 16.19 ? 216 LEU A C   1 
ATOM   1553 O O   . LEU A 1 216 ? -6.666  -28.170 -49.835 1.00 16.70 ? 216 LEU A O   1 
ATOM   1554 C CB  . LEU A 1 216 ? -8.485  -25.783 -48.576 1.00 18.19 ? 216 LEU A CB  1 
ATOM   1555 C CG  . LEU A 1 216 ? -8.790  -25.409 -47.128 1.00 20.79 ? 216 LEU A CG  1 
ATOM   1556 C CD1 . LEU A 1 216 ? -10.201 -24.883 -47.057 1.00 21.64 ? 216 LEU A CD1 1 
ATOM   1557 C CD2 . LEU A 1 216 ? -8.566  -26.611 -46.229 1.00 20.47 ? 216 LEU A CD2 1 
ATOM   1558 N N   . ALA A 1 217 ? -6.766  -26.427 -51.247 1.00 16.79 ? 217 ALA A N   1 
ATOM   1559 C CA  . ALA A 1 217 ? -6.628  -27.278 -52.421 1.00 17.76 ? 217 ALA A CA  1 
ATOM   1560 C C   . ALA A 1 217 ? -5.286  -28.006 -52.421 1.00 17.71 ? 217 ALA A C   1 
ATOM   1561 O O   . ALA A 1 217 ? -5.208  -29.127 -52.909 1.00 17.85 ? 217 ALA A O   1 
ATOM   1562 C CB  . ALA A 1 217 ? -6.818  -26.468 -53.676 1.00 19.82 ? 217 ALA A CB  1 
ATOM   1563 N N   . ILE A 1 218 ? -4.250  -27.393 -51.837 1.00 16.20 ? 218 ILE A N   1 
ATOM   1564 C CA  . ILE A 1 218 ? -2.961  -28.064 -51.741 1.00 16.11 ? 218 ILE A CA  1 
ATOM   1565 C C   . ILE A 1 218 ? -3.106  -29.334 -50.912 1.00 14.95 ? 218 ILE A C   1 
ATOM   1566 O O   . ILE A 1 218 ? -2.668  -30.401 -51.296 1.00 15.98 ? 218 ILE A O   1 
ATOM   1567 C CB  . ILE A 1 218 ? -1.875  -27.137 -51.185 1.00 17.03 ? 218 ILE A CB  1 
ATOM   1568 C CG1 . ILE A 1 218 ? -1.696  -25.890 -52.050 1.00 19.25 ? 218 ILE A CG1 1 
ATOM   1569 C CG2 . ILE A 1 218 ? -0.594  -27.927 -50.948 1.00 17.78 ? 218 ILE A CG2 1 
ATOM   1570 C CD1 . ILE A 1 218 ? -0.897  -24.787 -51.384 1.00 20.02 ? 218 ILE A CD1 1 
ATOM   1571 N N   . ALA A 1 219 ? -3.765  -29.221 -49.756 1.00 15.95 ? 219 ALA A N   1 
ATOM   1572 C CA  . ALA A 1 219 ? -3.991  -30.385 -48.904 1.00 16.12 ? 219 ALA A CA  1 
ATOM   1573 C C   . ALA A 1 219 ? -4.832  -31.443 -49.620 1.00 16.17 ? 219 ALA A C   1 
ATOM   1574 O O   . ALA A 1 219 ? -4.547  -32.635 -49.560 1.00 16.34 ? 219 ALA A O   1 
ATOM   1575 C CB  . ALA A 1 219 ? -4.681  -29.946 -47.642 1.00 16.55 ? 219 ALA A CB  1 
ATOM   1576 N N   . ASP A 1 220 ? -5.908  -31.003 -50.278 1.00 17.38 ? 220 ASP A N   1 
ATOM   1577 C CA  . ASP A 1 220 ? -6.796  -31.923 -50.959 1.00 18.37 ? 220 ASP A CA  1 
ATOM   1578 C C   . ASP A 1 220 ? -6.059  -32.692 -52.051 1.00 18.19 ? 220 ASP A C   1 
ATOM   1579 O O   . ASP A 1 220 ? -6.236  -33.890 -52.185 1.00 20.21 ? 220 ASP A O   1 
ATOM   1580 C CB  . ASP A 1 220 ? -8.015  -31.205 -51.512 1.00 19.98 ? 220 ASP A CB  1 
ATOM   1581 C CG  . ASP A 1 220 ? -8.979  -30.587 -50.509 1.00 21.01 ? 220 ASP A CG  1 
ATOM   1582 O OD1 . ASP A 1 220 ? -8.848  -30.863 -49.288 1.00 22.73 ? 220 ASP A OD1 1 
ATOM   1583 O OD2 . ASP A 1 220 ? -9.905  -29.867 -50.968 1.00 24.31 ? 220 ASP A OD2 1 
ATOM   1584 N N   . GLU A 1 221 ? -5.171  -32.003 -52.766 1.00 18.71 ? 221 GLU A N   1 
ATOM   1585 C CA  . GLU A 1 221 ? -4.407  -32.636 -53.824 1.00 20.67 ? 221 GLU A CA  1 
ATOM   1586 C C   . GLU A 1 221 ? -3.389  -33.634 -53.271 1.00 19.02 ? 221 GLU A C   1 
ATOM   1587 O O   . GLU A 1 221 ? -3.174  -34.679 -53.867 1.00 20.00 ? 221 GLU A O   1 
ATOM   1588 C CB  . GLU A 1 221 ? -3.712  -31.544 -54.632 1.00 23.80 ? 221 GLU A CB  1 
ATOM   1589 C CG  . GLU A 1 221 ? -4.694  -30.714 -55.454 1.00 32.75 ? 221 GLU A CG  1 
ATOM   1590 C CD  . GLU A 1 221 ? -4.098  -29.443 -56.071 1.00 42.73 ? 221 GLU A CD  1 
ATOM   1591 O OE1 . GLU A 1 221 ? -2.844  -29.249 -56.060 1.00 49.50 ? 221 GLU A OE1 1 
ATOM   1592 O OE2 . GLU A 1 221 ? -4.911  -28.630 -56.587 1.00 53.31 ? 221 GLU A OE2 1 
ATOM   1593 N N   . LEU A 1 222 ? -2.756  -33.304 -52.134 1.00 16.80 ? 222 LEU A N   1 
ATOM   1594 C CA  . LEU A 1 222 ? -1.724  -34.167 -51.593 1.00 16.83 ? 222 LEU A CA  1 
ATOM   1595 C C   . LEU A 1 222 ? -2.294  -35.401 -50.915 1.00 17.16 ? 222 LEU A C   1 
ATOM   1596 O O   . LEU A 1 222 ? -1.706  -36.478 -51.015 1.00 18.87 ? 222 LEU A O   1 
ATOM   1597 C CB  . LEU A 1 222 ? -0.818  -33.393 -50.644 1.00 17.99 ? 222 LEU A CB  1 
ATOM   1598 C CG  . LEU A 1 222 ? 0.166   -32.438 -51.316 1.00 19.94 ? 222 LEU A CG  1 
ATOM   1599 C CD1 . LEU A 1 222 ? 0.831   -31.603 -50.264 1.00 19.59 ? 222 LEU A CD1 1 
ATOM   1600 C CD2 . LEU A 1 222 ? 1.209   -33.142 -52.134 1.00 21.97 ? 222 LEU A CD2 1 
ATOM   1601 N N   . PHE A 1 223 ? -3.379  -35.209 -50.148 1.00 16.85 ? 223 PHE A N   1 
ATOM   1602 C CA  . PHE A 1 223 ? -3.835  -36.265 -49.262 1.00 16.22 ? 223 PHE A CA  1 
ATOM   1603 C C   . PHE A 1 223 ? -5.220  -36.804 -49.562 1.00 17.51 ? 223 PHE A C   1 
ATOM   1604 O O   . PHE A 1 223 ? -5.551  -37.856 -49.016 1.00 20.80 ? 223 PHE A O   1 
ATOM   1605 C CB  . PHE A 1 223 ? -3.873  -35.725 -47.840 1.00 15.79 ? 223 PHE A CB  1 
ATOM   1606 C CG  . PHE A 1 223 ? -2.546  -35.232 -47.324 1.00 16.23 ? 223 PHE A CG  1 
ATOM   1607 C CD1 . PHE A 1 223 ? -1.553  -36.145 -47.056 1.00 17.95 ? 223 PHE A CD1 1 
ATOM   1608 C CD2 . PHE A 1 223 ? -2.306  -33.882 -47.114 1.00 15.76 ? 223 PHE A CD2 1 
ATOM   1609 C CE1 . PHE A 1 223 ? -0.340  -35.716 -46.573 1.00 17.59 ? 223 PHE A CE1 1 
ATOM   1610 C CE2 . PHE A 1 223 ? -1.075  -33.465 -46.665 1.00 16.25 ? 223 PHE A CE2 1 
ATOM   1611 C CZ  . PHE A 1 223 ? -0.103  -34.387 -46.385 1.00 18.22 ? 223 PHE A CZ  1 
ATOM   1612 N N   . GLY A 1 224 ? -5.988  -36.098 -50.383 1.00 17.87 ? 224 GLY A N   1 
ATOM   1613 C CA  . GLY A 1 224 ? -7.394  -36.410 -50.536 1.00 19.16 ? 224 GLY A CA  1 
ATOM   1614 C C   . GLY A 1 224 ? -8.218  -35.398 -49.756 1.00 19.63 ? 224 GLY A C   1 
ATOM   1615 O O   . GLY A 1 224 ? -7.753  -34.857 -48.750 1.00 19.66 ? 224 GLY A O   1 
ATOM   1616 N N   . ALA A 1 225 ? -9.456  -35.192 -50.216 1.00 20.53 ? 225 ALA A N   1 
ATOM   1617 C CA  . ALA A 1 225 ? -10.266 -34.076 -49.760 1.00 23.26 ? 225 ALA A CA  1 
ATOM   1618 C C   . ALA A 1 225 ? -10.757 -34.245 -48.319 1.00 22.08 ? 225 ALA A C   1 
ATOM   1619 O O   . ALA A 1 225 ? -11.200 -33.276 -47.724 1.00 24.52 ? 225 ALA A O   1 
ATOM   1620 C CB  . ALA A 1 225 ? -11.426 -33.887 -50.716 1.00 26.63 ? 225 ALA A CB  1 
ATOM   1621 N N   . ASP A 1 226 ? -10.693 -35.450 -47.742 1.00 20.18 ? 226 ASP A N   1 
ATOM   1622 C CA  . ASP A 1 226 ? -11.180 -35.672 -46.380 1.00 22.25 ? 226 ASP A CA  1 
ATOM   1623 C C   . ASP A 1 226 ? -10.096 -35.428 -45.324 1.00 20.17 ? 226 ASP A C   1 
ATOM   1624 O O   . ASP A 1 226 ? -10.400 -35.415 -44.126 1.00 21.31 ? 226 ASP A O   1 
ATOM   1625 C CB  . ASP A 1 226 ? -11.775 -37.060 -46.236 1.00 28.10 ? 226 ASP A CB  1 
ATOM   1626 C CG  . ASP A 1 226 ? -13.090 -37.267 -46.973 1.00 33.57 ? 226 ASP A CG  1 
ATOM   1627 O OD1 . ASP A 1 226 ? -13.828 -36.273 -47.193 1.00 40.62 ? 226 ASP A OD1 1 
ATOM   1628 O OD2 . ASP A 1 226 ? -13.355 -38.413 -47.353 1.00 42.42 ? 226 ASP A OD2 1 
ATOM   1629 N N   . TRP A 1 227 ? -8.840  -35.220 -45.742 1.00 18.64 ? 227 TRP A N   1 
ATOM   1630 C CA  . TRP A 1 227 ? -7.760  -35.139 -44.777 1.00 16.74 ? 227 TRP A CA  1 
ATOM   1631 C C   . TRP A 1 227 ? -7.864  -33.910 -43.868 1.00 16.06 ? 227 TRP A C   1 
ATOM   1632 O O   . TRP A 1 227 ? -7.603  -34.002 -42.661 1.00 17.07 ? 227 TRP A O   1 
ATOM   1633 C CB  . TRP A 1 227 ? -6.418  -35.161 -45.517 1.00 15.89 ? 227 TRP A CB  1 
ATOM   1634 C CG  . TRP A 1 227 ? -5.257  -35.125 -44.582 1.00 16.37 ? 227 TRP A CG  1 
ATOM   1635 C CD1 . TRP A 1 227 ? -4.767  -36.158 -43.854 1.00 17.96 ? 227 TRP A CD1 1 
ATOM   1636 C CD2 . TRP A 1 227 ? -4.430  -33.980 -44.289 1.00 15.54 ? 227 TRP A CD2 1 
ATOM   1637 N NE1 . TRP A 1 227 ? -3.699  -35.727 -43.108 1.00 18.49 ? 227 TRP A NE1 1 
ATOM   1638 C CE2 . TRP A 1 227 ? -3.451  -34.404 -43.370 1.00 15.89 ? 227 TRP A CE2 1 
ATOM   1639 C CE3 . TRP A 1 227 ? -4.416  -32.648 -44.705 1.00 15.27 ? 227 TRP A CE3 1 
ATOM   1640 C CZ2 . TRP A 1 227 ? -2.474  -33.544 -42.877 1.00 15.05 ? 227 TRP A CZ2 1 
ATOM   1641 C CZ3 . TRP A 1 227 ? -3.447  -31.798 -44.225 1.00 15.93 ? 227 TRP A CZ3 1 
ATOM   1642 C CH2 . TRP A 1 227 ? -2.446  -32.262 -43.376 1.00 15.09 ? 227 TRP A CH2 1 
ATOM   1643 N N   . ALA A 1 228 ? -8.138  -32.750 -44.459 1.00 15.25 ? 228 ALA A N   1 
ATOM   1644 C CA  . ALA A 1 228 ? -8.039  -31.467 -43.770 1.00 16.30 ? 228 ALA A CA  1 
ATOM   1645 C C   . ALA A 1 228 ? -9.225  -31.170 -42.838 1.00 16.14 ? 228 ALA A C   1 
ATOM   1646 O O   . ALA A 1 228 ? -9.944  -30.191 -43.024 1.00 18.42 ? 228 ALA A O   1 
ATOM   1647 C CB  . ALA A 1 228 ? -7.851  -30.354 -44.762 1.00 16.93 ? 228 ALA A CB  1 
ATOM   1648 N N   . ASP A 1 229 ? -9.322  -31.947 -41.771 1.00 15.47 ? 229 ASP A N   1 
ATOM   1649 C CA  . ASP A 1 229 ? -10.234 -31.662 -40.668 1.00 15.18 ? 229 ASP A CA  1 
ATOM   1650 C C   . ASP A 1 229 ? -9.490  -30.845 -39.621 1.00 14.15 ? 229 ASP A C   1 
ATOM   1651 O O   . ASP A 1 229 ? -8.308  -30.514 -39.803 1.00 13.80 ? 229 ASP A O   1 
ATOM   1652 C CB  . ASP A 1 229 ? -10.824 -32.958 -40.169 1.00 16.60 ? 229 ASP A CB  1 
ATOM   1653 C CG  . ASP A 1 229 ? -9.839  -33.901 -39.499 1.00 18.58 ? 229 ASP A CG  1 
ATOM   1654 O OD1 . ASP A 1 229 ? -8.693  -33.483 -39.249 1.00 15.94 ? 229 ASP A OD1 1 
ATOM   1655 O OD2 . ASP A 1 229 ? -10.262 -35.036 -39.187 1.00 25.05 ? 229 ASP A OD2 1 
ATOM   1656 N N   . ALA A 1 230 ? -10.170 -30.514 -38.519 1.00 14.42 ? 230 ALA A N   1 
ATOM   1657 C CA  . ALA A 1 230 ? -9.562  -29.617 -37.543 1.00 15.26 ? 230 ALA A CA  1 
ATOM   1658 C C   . ALA A 1 230 ? -8.349  -30.243 -36.841 1.00 13.14 ? 230 ALA A C   1 
ATOM   1659 O O   . ALA A 1 230 ? -7.534  -29.504 -36.301 1.00 14.93 ? 230 ALA A O   1 
ATOM   1660 C CB  . ALA A 1 230 ? -10.582 -29.092 -36.558 1.00 16.77 ? 230 ALA A CB  1 
ATOM   1661 N N   . ARG A 1 231 ? -8.200  -31.578 -36.862 1.00 13.70 ? 231 ARG A N   1 
ATOM   1662 C CA  . ARG A 1 231 ? -7.024  -32.204 -36.280 1.00 13.67 ? 231 ARG A CA  1 
ATOM   1663 C C   . ARG A 1 231 ? -5.841  -32.121 -37.245 1.00 13.13 ? 231 ARG A C   1 
ATOM   1664 O O   . ARG A 1 231 ? -4.692  -32.326 -36.836 1.00 14.52 ? 231 ARG A O   1 
ATOM   1665 C CB  . ARG A 1 231 ? -7.328  -33.652 -35.895 1.00 14.94 ? 231 ARG A CB  1 
ATOM   1666 C CG  . ARG A 1 231 ? -6.149  -34.463 -35.372 1.00 15.81 ? 231 ARG A CG  1 
ATOM   1667 C CD  . ARG A 1 231 ? -5.469  -33.834 -34.177 1.00 15.29 ? 231 ARG A CD  1 
ATOM   1668 N NE  . ARG A 1 231 ? -4.349  -34.637 -33.738 1.00 15.80 ? 231 ARG A NE  1 
ATOM   1669 C CZ  . ARG A 1 231 ? -3.099  -34.520 -34.211 1.00 15.02 ? 231 ARG A CZ  1 
ATOM   1670 N NH1 . ARG A 1 231 ? -2.831  -33.663 -35.179 1.00 15.54 ? 231 ARG A NH1 1 
ATOM   1671 N NH2 . ARG A 1 231 ? -2.124  -35.262 -33.710 1.00 17.29 ? 231 ARG A NH2 1 
ATOM   1672 N N   . HIS A 1 232 ? -6.103  -31.804 -38.511 1.00 12.71 ? 232 HIS A N   1 
ATOM   1673 C CA  . HIS A 1 232 ? -5.025  -31.831 -39.492 1.00 13.31 ? 232 HIS A CA  1 
ATOM   1674 C C   . HIS A 1 232 ? -4.771  -30.520 -40.211 1.00 11.81 ? 232 HIS A C   1 
ATOM   1675 O O   . HIS A 1 232 ? -3.780  -30.434 -40.933 1.00 12.00 ? 232 HIS A O   1 
ATOM   1676 C CB  . HIS A 1 232 ? -5.251  -32.954 -40.505 1.00 14.15 ? 232 HIS A CB  1 
ATOM   1677 C CG  . HIS A 1 232 ? -5.251  -34.290 -39.843 1.00 15.97 ? 232 HIS A CG  1 
ATOM   1678 N ND1 . HIS A 1 232 ? -6.340  -34.851 -39.219 1.00 17.57 ? 232 HIS A ND1 1 
ATOM   1679 C CD2 . HIS A 1 232 ? -4.240  -35.136 -39.633 1.00 17.31 ? 232 HIS A CD2 1 
ATOM   1680 C CE1 . HIS A 1 232 ? -5.997  -36.012 -38.687 1.00 18.46 ? 232 HIS A CE1 1 
ATOM   1681 N NE2 . HIS A 1 232 ? -4.709  -36.216 -38.932 1.00 18.01 ? 232 HIS A NE2 1 
ATOM   1682 N N   . TYR A 1 233 ? -5.612  -29.507 -40.089 1.00 12.05 ? 233 TYR A N   1 
ATOM   1683 C CA  . TYR A 1 233 ? -5.430  -28.286 -40.854 1.00 11.49 ? 233 TYR A CA  1 
ATOM   1684 C C   . TYR A 1 233 ? -5.968  -27.119 -40.036 1.00 11.27 ? 233 TYR A C   1 
ATOM   1685 O O   . TYR A 1 233 ? -7.095  -27.204 -39.528 1.00 12.93 ? 233 TYR A O   1 
ATOM   1686 C CB  . TYR A 1 233 ? -6.113  -28.379 -42.216 1.00 12.45 ? 233 TYR A CB  1 
ATOM   1687 C CG  . TYR A 1 233 ? -5.540  -27.459 -43.267 1.00 12.84 ? 233 TYR A CG  1 
ATOM   1688 C CD1 . TYR A 1 233 ? -5.762  -26.086 -43.264 1.00 14.30 ? 233 TYR A CD1 1 
ATOM   1689 C CD2 . TYR A 1 233 ? -4.746  -27.993 -44.266 1.00 14.57 ? 233 TYR A CD2 1 
ATOM   1690 C CE1 . TYR A 1 233 ? -5.161  -25.253 -44.197 1.00 15.79 ? 233 TYR A CE1 1 
ATOM   1691 C CE2 . TYR A 1 233 ? -4.171  -27.176 -45.227 1.00 15.27 ? 233 TYR A CE2 1 
ATOM   1692 C CZ  . TYR A 1 233 ? -4.386  -25.813 -45.198 1.00 15.76 ? 233 TYR A CZ  1 
ATOM   1693 O OH  . TYR A 1 233 ? -3.774  -25.019 -46.143 1.00 18.39 ? 233 TYR A OH  1 
ATOM   1694 N N   . ARG A 1 234 ? -5.215  -26.026 -39.997 1.00 10.57 ? 234 ARG A N   1 
ATOM   1695 C CA  . ARG A 1 234 ? -5.670  -24.791 -39.394 1.00 10.38 ? 234 ARG A CA  1 
ATOM   1696 C C   . ARG A 1 234 ? -5.217  -23.593 -40.198 1.00 11.12 ? 234 ARG A C   1 
ATOM   1697 O O   . ARG A 1 234 ? -4.178  -23.626 -40.864 1.00 11.27 ? 234 ARG A O   1 
ATOM   1698 C CB  . ARG A 1 234 ? -5.171  -24.609 -37.960 1.00 11.24 ? 234 ARG A CB  1 
ATOM   1699 C CG  . ARG A 1 234 ? -5.582  -25.697 -36.989 1.00 11.11 ? 234 ARG A CG  1 
ATOM   1700 C CD  . ARG A 1 234 ? -7.048  -25.665 -36.602 1.00 11.01 ? 234 ARG A CD  1 
ATOM   1701 N NE  . ARG A 1 234 ? -7.317  -26.785 -35.707 1.00 11.52 ? 234 ARG A NE  1 
ATOM   1702 C CZ  . ARG A 1 234 ? -6.929  -26.843 -34.436 1.00 11.99 ? 234 ARG A CZ  1 
ATOM   1703 N NH1 . ARG A 1 234 ? -6.532  -25.759 -33.807 1.00 12.78 ? 234 ARG A NH1 1 
ATOM   1704 N NH2 . ARG A 1 234 ? -6.936  -27.998 -33.809 1.00 13.55 ? 234 ARG A NH2 1 
ATOM   1705 N N   . PHE A 1 235 ? -5.925  -22.488 -40.013 1.00 11.93 ? 235 PHE A N   1 
ATOM   1706 C CA  . PHE A 1 235 ? -5.616  -21.186 -40.554 1.00 11.81 ? 235 PHE A CA  1 
ATOM   1707 C C   . PHE A 1 235 ? -5.559  -20.127 -39.474 1.00 12.59 ? 235 PHE A C   1 
ATOM   1708 O O   . PHE A 1 235 ? -6.442  -20.076 -38.608 1.00 13.18 ? 235 PHE A O   1 
ATOM   1709 C CB  . PHE A 1 235 ? -6.710  -20.657 -41.488 1.00 12.95 ? 235 PHE A CB  1 
ATOM   1710 C CG  . PHE A 1 235 ? -6.827  -21.354 -42.821 1.00 15.07 ? 235 PHE A CG  1 
ATOM   1711 C CD1 . PHE A 1 235 ? -6.062  -20.890 -43.869 1.00 16.45 ? 235 PHE A CD1 1 
ATOM   1712 C CD2 . PHE A 1 235 ? -7.742  -22.365 -43.069 1.00 16.19 ? 235 PHE A CD2 1 
ATOM   1713 C CE1 . PHE A 1 235 ? -6.160  -21.460 -45.128 1.00 18.33 ? 235 PHE A CE1 1 
ATOM   1714 C CE2 . PHE A 1 235 ? -7.839  -22.925 -44.339 1.00 17.47 ? 235 PHE A CE2 1 
ATOM   1715 C CZ  . PHE A 1 235 ? -7.034  -22.473 -45.359 1.00 18.11 ? 235 PHE A CZ  1 
ATOM   1716 N N   . SER A 1 236 ? -4.653  -19.171 -39.619 1.00 13.65 ? 236 SER A N   1 
ATOM   1717 C CA  A SER A 1 236 ? -4.749  -17.895 -38.927 0.25 13.54 ? 236 SER A CA  1 
ATOM   1718 C CA  B SER A 1 236 ? -4.741  -17.898 -38.920 0.25 13.97 ? 236 SER A CA  1 
ATOM   1719 C CA  C SER A 1 236 ? -4.713  -17.901 -38.905 0.50 15.16 ? 236 SER A CA  1 
ATOM   1720 C C   . SER A 1 236 ? -4.178  -16.795 -39.811 1.00 14.17 ? 236 SER A C   1 
ATOM   1721 O O   . SER A 1 236 ? -3.069  -16.905 -40.290 1.00 15.47 ? 236 SER A O   1 
ATOM   1722 C CB  A SER A 1 236 ? -4.040  -17.903 -37.610 0.25 13.23 ? 236 SER A CB  1 
ATOM   1723 C CB  B SER A 1 236 ? -4.038  -17.934 -37.584 0.25 14.27 ? 236 SER A CB  1 
ATOM   1724 C CB  C SER A 1 236 ? -3.903  -17.932 -37.635 0.50 17.86 ? 236 SER A CB  1 
ATOM   1725 O OG  A SER A 1 236 ? -4.213  -16.641 -36.976 0.25 11.89 ? 236 SER A OG  1 
ATOM   1726 O OG  B SER A 1 236 ? -2.634  -18.127 -37.693 0.25 14.45 ? 236 SER A OG  1 
ATOM   1727 O OG  C SER A 1 236 ? -4.480  -18.693 -36.585 0.50 21.90 ? 236 SER A OG  1 
ATOM   1728 N N   . ALA A 1 237 ? -4.930  -15.713 -39.993 1.00 17.13 ? 237 ALA A N   1 
ATOM   1729 C CA  . ALA A 1 237 ? -4.395  -14.563 -40.697 1.00 18.42 ? 237 ALA A CA  1 
ATOM   1730 C C   . ALA A 1 237 ? -5.253  -13.348 -40.407 1.00 22.15 ? 237 ALA A C   1 
ATOM   1731 O O   . ALA A 1 237 ? -6.482  -13.472 -40.294 1.00 22.31 ? 237 ALA A O   1 
ATOM   1732 C CB  . ALA A 1 237 ? -4.371  -14.811 -42.183 1.00 21.12 ? 237 ALA A CB  1 
ATOM   1733 N N   . SER A 1 238 ? -4.600  -12.184 -40.405 1.00 26.00 ? 238 SER A N   1 
ATOM   1734 C CA  . SER A 1 238 ? -5.312  -10.914 -40.317 1.00 29.65 ? 238 SER A CA  1 
ATOM   1735 C C   . SER A 1 238 ? -6.305  -10.801 -41.464 1.00 30.55 ? 238 SER A C   1 
ATOM   1736 O O   . SER A 1 238 ? -5.952  -11.022 -42.620 1.00 32.54 ? 238 SER A O   1 
ATOM   1737 C CB  . SER A 1 238 ? -4.368  -9.732  -40.356 1.00 34.47 ? 238 SER A CB  1 
ATOM   1738 O OG  . SER A 1 238 ? -3.543  -9.721  -39.209 1.00 42.68 ? 238 SER A OG  1 
ATOM   1739 N N   . GLY A 1 239 ? -7.554  -10.485 -41.122 1.00 29.17 ? 239 GLY A N   1 
ATOM   1740 C CA  . GLY A 1 239 ? -8.551  -10.134 -42.113 1.00 28.22 ? 239 GLY A CA  1 
ATOM   1741 C C   . GLY A 1 239 ? -9.297  -11.351 -42.653 1.00 25.98 ? 239 GLY A C   1 
ATOM   1742 O O   . GLY A 1 239 ? -10.303 -11.188 -43.333 1.00 28.43 ? 239 GLY A O   1 
ATOM   1743 N N   . LEU A 1 240 ? -8.834  -12.568 -42.344 1.00 23.94 ? 240 LEU A N   1 
ATOM   1744 C CA  . LEU A 1 240 ? -9.384  -13.732 -43.015 1.00 20.03 ? 240 LEU A CA  1 
ATOM   1745 C C   . LEU A 1 240 ? -10.824 -13.994 -42.574 1.00 19.77 ? 240 LEU A C   1 
ATOM   1746 O O   . LEU A 1 240 ? -11.667 -14.302 -43.405 1.00 21.11 ? 240 LEU A O   1 
ATOM   1747 C CB  . LEU A 1 240 ? -8.500  -14.952 -42.796 1.00 18.96 ? 240 LEU A CB  1 
ATOM   1748 C CG  . LEU A 1 240 ? -9.001  -16.236 -43.454 1.00 19.20 ? 240 LEU A CG  1 
ATOM   1749 C CD1 . LEU A 1 240 ? -9.164  -16.072 -44.954 1.00 20.87 ? 240 LEU A CD1 1 
ATOM   1750 C CD2 . LEU A 1 240 ? -8.038  -17.371 -43.118 1.00 20.30 ? 240 LEU A CD2 1 
ATOM   1751 N N   . LEU A 1 241 ? -11.108 -13.922 -41.271 1.00 19.50 ? 241 LEU A N   1 
ATOM   1752 C CA  . LEU A 1 241 ? -12.455 -14.235 -40.829 1.00 19.78 ? 241 LEU A CA  1 
ATOM   1753 C C   . LEU A 1 241 ? -13.450 -13.310 -41.533 1.00 21.12 ? 241 LEU A C   1 
ATOM   1754 O O   . LEU A 1 241 ? -14.490 -13.760 -41.997 1.00 21.20 ? 241 LEU A O   1 
ATOM   1755 C CB  . LEU A 1 241 ? -12.608 -14.143 -39.316 1.00 19.62 ? 241 LEU A CB  1 
ATOM   1756 C CG  . LEU A 1 241 ? -14.014 -14.474 -38.803 1.00 20.32 ? 241 LEU A CG  1 
ATOM   1757 C CD1 . LEU A 1 241 ? -14.441 -15.886 -39.194 1.00 22.51 ? 241 LEU A CD1 1 
ATOM   1758 C CD2 . LEU A 1 241 ? -14.028 -14.276 -37.318 1.00 22.09 ? 241 LEU A CD2 1 
ATOM   1759 N N   . ALA A 1 242 ? -13.138 -12.010 -41.598 1.00 22.88 ? 242 ALA A N   1 
ATOM   1760 C CA  . ALA A 1 242 ? -14.036 -11.065 -42.238 1.00 25.03 ? 242 ALA A CA  1 
ATOM   1761 C C   . ALA A 1 242 ? -14.245 -11.433 -43.705 1.00 25.61 ? 242 ALA A C   1 
ATOM   1762 O O   . ALA A 1 242 ? -15.360 -11.348 -44.212 1.00 26.77 ? 242 ALA A O   1 
ATOM   1763 C CB  . ALA A 1 242 ? -13.500 -9.663  -42.092 1.00 26.46 ? 242 ALA A CB  1 
ATOM   1764 N N   . SER A 1 243 ? -13.174 -11.855 -44.386 1.00 25.73 ? 243 SER A N   1 
ATOM   1765 C CA  . SER A 1 243 ? -13.286 -12.194 -45.791 1.00 26.03 ? 243 SER A CA  1 
ATOM   1766 C C   . SER A 1 243 ? -14.153 -13.441 -45.959 1.00 24.23 ? 243 SER A C   1 
ATOM   1767 O O   . SER A 1 243 ? -14.987 -13.525 -46.865 1.00 25.79 ? 243 SER A O   1 
ATOM   1768 C CB  . SER A 1 243 ? -11.919 -12.387 -46.390 1.00 26.66 ? 243 SER A CB  1 
ATOM   1769 O OG  . SER A 1 243 ? -12.000 -12.621 -47.794 1.00 28.82 ? 243 SER A OG  1 
ATOM   1770 N N   . LEU A 1 244 ? -13.954 -14.417 -45.072 1.00 22.44 ? 244 LEU A N   1 
ATOM   1771 C CA  . LEU A 1 244 ? -14.739 -15.639 -45.142 1.00 21.92 ? 244 LEU A CA  1 
ATOM   1772 C C   . LEU A 1 244 ? -16.214 -15.320 -44.909 1.00 22.10 ? 244 LEU A C   1 
ATOM   1773 O O   . LEU A 1 244 ? -17.073 -15.803 -45.638 1.00 22.93 ? 244 LEU A O   1 
ATOM   1774 C CB  . LEU A 1 244 ? -14.233 -16.684 -44.153 1.00 19.38 ? 244 LEU A CB  1 
ATOM   1775 C CG  . LEU A 1 244 ? -12.810 -17.191 -44.422 1.00 19.21 ? 244 LEU A CG  1 
ATOM   1776 C CD1 . LEU A 1 244 ? -12.384 -18.089 -43.289 1.00 20.16 ? 244 LEU A CD1 1 
ATOM   1777 C CD2 . LEU A 1 244 ? -12.691 -17.918 -45.744 1.00 21.41 ? 244 LEU A CD2 1 
ATOM   1778 N N   . LEU A 1 245 ? -16.496 -14.516 -43.882 1.00 22.30 ? 245 LEU A N   1 
ATOM   1779 C CA  . LEU A 1 245 ? -17.870 -14.176 -43.584 1.00 23.96 ? 245 LEU A CA  1 
ATOM   1780 C C   . LEU A 1 245 ? -18.510 -13.406 -44.733 1.00 26.18 ? 245 LEU A C   1 
ATOM   1781 O O   . LEU A 1 245 ? -19.675 -13.646 -45.036 1.00 27.72 ? 245 LEU A O   1 
ATOM   1782 C CB  . LEU A 1 245 ? -17.987 -13.440 -42.256 1.00 23.62 ? 245 LEU A CB  1 
ATOM   1783 C CG  . LEU A 1 245 ? -17.809 -14.335 -41.029 1.00 24.45 ? 245 LEU A CG  1 
ATOM   1784 C CD1 . LEU A 1 245 ? -17.634 -13.480 -39.787 1.00 26.69 ? 245 LEU A CD1 1 
ATOM   1785 C CD2 . LEU A 1 245 ? -18.968 -15.333 -40.879 1.00 24.11 ? 245 LEU A CD2 1 
ATOM   1786 N N   . LYS A 1 246 ? -17.758 -12.501 -45.375 1.00 27.67 ? 246 LYS A N   1 
ATOM   1787 C CA  . LYS A 1 246 ? -18.265 -11.747 -46.515 1.00 30.05 ? 246 LYS A CA  1 
ATOM   1788 C C   . LYS A 1 246 ? -18.647 -12.699 -47.643 1.00 28.69 ? 246 LYS A C   1 
ATOM   1789 O O   . LYS A 1 246 ? -19.705 -12.555 -48.237 1.00 32.88 ? 246 LYS A O   1 
ATOM   1790 C CB  . LYS A 1 246 ? -17.209 -10.738 -46.974 1.00 35.48 ? 246 LYS A CB  1 
ATOM   1791 C CG  . LYS A 1 246 ? -17.550 -9.832  -48.163 1.00 40.53 ? 246 LYS A CG  1 
ATOM   1792 C CD  . LYS A 1 246 ? -16.360 -8.924  -48.486 1.00 46.06 ? 246 LYS A CD  1 
ATOM   1793 C CE  . LYS A 1 246 ? -16.639 -7.554  -49.032 1.00 51.92 ? 246 LYS A CE  1 
ATOM   1794 N NZ  . LYS A 1 246 ? -17.283 -7.576  -50.344 1.00 54.38 ? 246 LYS A NZ  1 
ATOM   1795 N N   . ALA A 1 247 ? -17.792 -13.691 -47.917 1.00 28.63 ? 247 ALA A N   1 
ATOM   1796 C CA  . ALA A 1 247 ? -18.063 -14.669 -48.960 1.00 30.13 ? 247 ALA A CA  1 
ATOM   1797 C C   . ALA A 1 247 ? -19.344 -15.442 -48.654 1.00 31.62 ? 247 ALA A C   1 
ATOM   1798 O O   . ALA A 1 247 ? -20.026 -15.901 -49.562 1.00 34.08 ? 247 ALA A O   1 
ATOM   1799 C CB  . ALA A 1 247 ? -16.890 -15.602 -49.119 1.00 29.52 ? 247 ALA A CB  1 
ATOM   1800 N N   . LEU A 1 248 ? -19.647 -15.607 -47.362 1.00 28.60 ? 248 LEU A N   1 
ATOM   1801 C CA  . LEU A 1 248 ? -20.799 -16.378 -46.921 1.00 30.12 ? 248 LEU A CA  1 
ATOM   1802 C C   . LEU A 1 248 ? -22.045 -15.519 -46.719 1.00 32.59 ? 248 LEU A C   1 
ATOM   1803 O O   . LEU A 1 248 ? -23.062 -16.057 -46.311 1.00 35.83 ? 248 LEU A O   1 
ATOM   1804 C CB  . LEU A 1 248 ? -20.398 -17.135 -45.654 1.00 28.57 ? 248 LEU A CB  1 
ATOM   1805 C CG  . LEU A 1 248 ? -19.356 -18.234 -45.911 1.00 26.80 ? 248 LEU A CG  1 
ATOM   1806 C CD1 . LEU A 1 248 ? -18.691 -18.689 -44.637 1.00 25.87 ? 248 LEU A CD1 1 
ATOM   1807 C CD2 . LEU A 1 248 ? -19.983 -19.430 -46.627 1.00 28.57 ? 248 LEU A CD2 1 
ATOM   1808 N N   . GLY A 1 249 ? -21.954 -14.209 -46.972 1.00 32.70 ? 249 GLY A N   1 
ATOM   1809 C CA  . GLY A 1 249 ? -23.114 -13.336 -46.934 1.00 33.47 ? 249 GLY A CA  1 
ATOM   1810 C C   . GLY A 1 249 ? -23.288 -12.602 -45.606 1.00 35.44 ? 249 GLY A C   1 
ATOM   1811 O O   . GLY A 1 249 ? -24.362 -12.075 -45.355 1.00 40.65 ? 249 GLY A O   1 
ATOM   1812 N N   . HIS A 1 250 ? -22.230 -12.513 -44.790 1.00 35.74 ? 250 HIS A N   1 
ATOM   1813 C CA  . HIS A 1 250 ? -22.291 -11.809 -43.522 1.00 34.52 ? 250 HIS A CA  1 
ATOM   1814 C C   . HIS A 1 250 ? -21.414 -10.551 -43.563 1.00 42.78 ? 250 HIS A C   1 
ATOM   1815 O O   . HIS A 1 250 ? -20.205 -10.729 -43.393 1.00 47.05 ? 250 HIS A O   1 
ATOM   1816 C CB  . HIS A 1 250 ? -21.958 -12.800 -42.415 1.00 34.32 ? 250 HIS A CB  1 
ATOM   1817 C CG  . HIS A 1 250 ? -23.122 -13.702 -42.191 1.00 38.49 ? 250 HIS A CG  1 
ATOM   1818 N ND1 . HIS A 1 250 ? -23.239 -14.946 -42.778 1.00 39.96 ? 250 HIS A ND1 1 
ATOM   1819 C CD2 . HIS A 1 250 ? -24.254 -13.498 -41.506 1.00 38.04 ? 250 HIS A CD2 1 
ATOM   1820 C CE1 . HIS A 1 250 ? -24.386 -15.491 -42.396 1.00 39.15 ? 250 HIS A CE1 1 
ATOM   1821 N NE2 . HIS A 1 250 ? -25.026 -14.620 -41.639 1.00 38.11 ? 250 HIS A NE2 1 
ATOM   1822 N N   . ASP B 1 3   ? 19.718  2.120   15.897  1.00 38.93 ? 3   ASP B N   1 
ATOM   1823 C CA  . ASP B 1 3   ? 20.848  2.058   14.933  1.00 35.61 ? 3   ASP B CA  1 
ATOM   1824 C C   . ASP B 1 3   ? 20.269  1.936   13.524  1.00 31.08 ? 3   ASP B C   1 
ATOM   1825 O O   . ASP B 1 3   ? 19.850  0.863   13.096  1.00 28.06 ? 3   ASP B O   1 
ATOM   1826 C CB  . ASP B 1 3   ? 21.824  0.972   15.354  1.00 40.35 ? 3   ASP B CB  1 
ATOM   1827 C CG  . ASP B 1 3   ? 23.004  0.736   14.429  1.00 43.85 ? 3   ASP B CG  1 
ATOM   1828 O OD1 . ASP B 1 3   ? 22.989  1.259   13.295  1.00 43.20 ? 3   ASP B OD1 1 
ATOM   1829 O OD2 . ASP B 1 3   ? 23.933  0.024   14.862  1.00 51.11 ? 3   ASP B OD2 1 
ATOM   1830 N N   . LEU B 1 4   ? 20.219  3.075   12.830  1.00 27.61 ? 4   LEU B N   1 
ATOM   1831 C CA  . LEU B 1 4   ? 19.611  3.153   11.516  1.00 26.87 ? 4   LEU B CA  1 
ATOM   1832 C C   . LEU B 1 4   ? 20.389  2.320   10.495  1.00 25.79 ? 4   LEU B C   1 
ATOM   1833 O O   . LEU B 1 4   ? 19.799  1.743   9.581   1.00 25.57 ? 4   LEU B O   1 
ATOM   1834 C CB  . LEU B 1 4   ? 19.512  4.607   11.070  1.00 29.27 ? 4   LEU B CB  1 
ATOM   1835 C CG  . LEU B 1 4   ? 18.731  4.866   9.777   1.00 29.67 ? 4   LEU B CG  1 
ATOM   1836 C CD1 . LEU B 1 4   ? 17.288  4.367   9.849   1.00 30.10 ? 4   LEU B CD1 1 
ATOM   1837 C CD2 . LEU B 1 4   ? 18.771  6.363   9.455   1.00 34.29 ? 4   LEU B CD2 1 
ATOM   1838 N N   . LYS B 1 5   ? 21.716  2.263   10.609  1.00 25.60 ? 5   LYS B N   1 
ATOM   1839 C CA  . LYS B 1 5   ? 22.473  1.449   9.665   1.00 26.76 ? 5   LYS B CA  1 
ATOM   1840 C C   . LYS B 1 5   ? 22.109  -0.027  9.837   1.00 23.64 ? 5   LYS B C   1 
ATOM   1841 O O   . LYS B 1 5   ? 21.903  -0.757  8.869   1.00 23.83 ? 5   LYS B O   1 
ATOM   1842 C CB  . LYS B 1 5   ? 23.974  1.708   9.805   1.00 30.93 ? 5   LYS B CB  1 
ATOM   1843 C CG  . LYS B 1 5   ? 24.439  3.007   9.148   1.00 34.90 ? 5   LYS B CG  1 
ATOM   1844 C CD  . LYS B 1 5   ? 25.951  3.064   8.926   1.00 39.99 ? 5   LYS B CD  1 
ATOM   1845 C CE  . LYS B 1 5   ? 26.374  4.120   7.962   1.00 48.26 ? 5   LYS B CE  1 
ATOM   1846 N NZ  . LYS B 1 5   ? 27.096  5.212   8.615   1.00 53.97 ? 5   LYS B NZ  1 
ATOM   1847 N N   . ALA B 1 6   ? 22.053  -0.490  11.080  1.00 24.02 ? 6   ALA B N   1 
ATOM   1848 C CA  . ALA B 1 6   ? 21.721  -1.874  11.367  1.00 23.06 ? 6   ALA B CA  1 
ATOM   1849 C C   . ALA B 1 6   ? 20.309  -2.196  10.883  1.00 20.27 ? 6   ALA B C   1 
ATOM   1850 O O   . ALA B 1 6   ? 20.105  -3.253  10.305  1.00 20.49 ? 6   ALA B O   1 
ATOM   1851 C CB  . ALA B 1 6   ? 21.865  -2.140  12.846  1.00 25.04 ? 6   ALA B CB  1 
ATOM   1852 N N   . SER B 1 7   ? 19.339  -1.301  11.129  1.00 20.16 ? 7   SER B N   1 
ATOM   1853 C CA  . SER B 1 7   ? 17.975  -1.559  10.689  1.00 19.17 ? 7   SER B CA  1 
ATOM   1854 C C   . SER B 1 7   ? 17.906  -1.556  9.169   1.00 17.94 ? 7   SER B C   1 
ATOM   1855 O O   . SER B 1 7   ? 17.149  -2.319  8.589   1.00 16.75 ? 7   SER B O   1 
ATOM   1856 C CB  . SER B 1 7   ? 16.937  -0.635  11.260  1.00 22.91 ? 7   SER B CB  1 
ATOM   1857 O OG  . SER B 1 7   ? 17.284  0.710   11.005  1.00 28.71 ? 7   SER B OG  1 
ATOM   1858 N N   . SER B 1 8   ? 18.738  -0.731  8.519   1.00 16.82 ? 8   SER B N   1 
ATOM   1859 C CA  . SER B 1 8   ? 18.665  -0.602  7.071   1.00 16.28 ? 8   SER B CA  1 
ATOM   1860 C C   . SER B 1 8   ? 19.229  -1.840  6.388   1.00 15.76 ? 8   SER B C   1 
ATOM   1861 O O   . SER B 1 8   ? 18.667  -2.301  5.405   1.00 15.66 ? 8   SER B O   1 
ATOM   1862 C CB  . SER B 1 8   ? 19.373  0.636   6.618   1.00 17.47 ? 8   SER B CB  1 
ATOM   1863 O OG  . SER B 1 8   ? 18.738  1.788   7.158   1.00 19.42 ? 8   SER B OG  1 
ATOM   1864 N N   . LEU B 1 9   ? 20.336  -2.366  6.907   1.00 16.08 ? 9   LEU B N   1 
ATOM   1865 C CA  . LEU B 1 9   ? 20.860  -3.612  6.381   1.00 16.39 ? 9   LEU B CA  1 
ATOM   1866 C C   . LEU B 1 9   ? 19.875  -4.762  6.562   1.00 15.96 ? 9   LEU B C   1 
ATOM   1867 O O   . LEU B 1 9   ? 19.661  -5.600  5.690   1.00 16.14 ? 9   LEU B O   1 
ATOM   1868 C CB  . LEU B 1 9   ? 22.180  -3.931  7.072   1.00 18.94 ? 9   LEU B CB  1 
ATOM   1869 C CG  . LEU B 1 9   ? 22.898  -5.160  6.530   1.00 22.01 ? 9   LEU B CG  1 
ATOM   1870 C CD1 . LEU B 1 9   ? 23.272  -4.920  5.056   1.00 24.70 ? 9   LEU B CD1 1 
ATOM   1871 C CD2 . LEU B 1 9   ? 24.158  -5.454  7.315   1.00 25.61 ? 9   LEU B CD2 1 
ATOM   1872 N N   . ARG B 1 10  ? 19.247  -4.779  7.724   1.00 16.12 ? 10  ARG B N   1 
ATOM   1873 C CA  . ARG B 1 10  ? 18.276  -5.800  8.018   1.00 15.97 ? 10  ARG B CA  1 
ATOM   1874 C C   . ARG B 1 10  ? 17.100  -5.709  7.036   1.00 13.75 ? 10  ARG B C   1 
ATOM   1875 O O   . ARG B 1 10  ? 16.702  -6.714  6.450   1.00 14.02 ? 10  ARG B O   1 
ATOM   1876 C CB  . ARG B 1 10  ? 17.901  -5.591  9.478   1.00 18.54 ? 10  ARG B CB  1 
ATOM   1877 C CG  . ARG B 1 10  ? 16.959  -6.648  9.969   1.00 21.61 ? 10  ARG B CG  1 
ATOM   1878 C CD  . ARG B 1 10  ? 16.675  -6.202  11.391  1.00 23.18 ? 10  ARG B CD  1 
ATOM   1879 N NE  . ARG B 1 10  ? 15.777  -7.150  11.914  1.00 23.41 ? 10  ARG B NE  1 
ATOM   1880 C CZ  . ARG B 1 10  ? 15.013  -6.954  12.970  1.00 24.64 ? 10  ARG B CZ  1 
ATOM   1881 N NH1 . ARG B 1 10  ? 14.931  -5.764  13.538  1.00 26.71 ? 10  ARG B NH1 1 
ATOM   1882 N NH2 . ARG B 1 10  ? 14.337  -7.960  13.437  1.00 26.62 ? 10  ARG B NH2 1 
ATOM   1883 N N   . ALA B 1 11  ? 16.575  -4.489  6.816   1.00 13.65 ? 11  ALA B N   1 
ATOM   1884 C CA  . ALA B 1 11  ? 15.444  -4.312  5.913   1.00 12.99 ? 11  ALA B CA  1 
ATOM   1885 C C   . ALA B 1 11  ? 15.807  -4.676  4.466   1.00 12.66 ? 11  ALA B C   1 
ATOM   1886 O O   . ALA B 1 11  ? 14.998  -5.251  3.738   1.00 12.50 ? 11  ALA B O   1 
ATOM   1887 C CB  . ALA B 1 11  ? 14.964  -2.897  6.001   1.00 13.42 ? 11  ALA B CB  1 
ATOM   1888 N N   . LEU B 1 12  ? 17.027  -4.312  4.028   1.00 12.11 ? 12  LEU B N   1 
ATOM   1889 C CA  . LEU B 1 12  ? 17.415  -4.594  2.662   1.00 12.01 ? 12  LEU B CA  1 
ATOM   1890 C C   . LEU B 1 12  ? 17.333  -6.089  2.407   1.00 11.84 ? 12  LEU B C   1 
ATOM   1891 O O   . LEU B 1 12  ? 16.876  -6.529  1.349   1.00 11.89 ? 12  LEU B O   1 
ATOM   1892 C CB  . LEU B 1 12  ? 18.810  -4.012  2.492   1.00 13.19 ? 12  LEU B CB  1 
ATOM   1893 C CG  . LEU B 1 12  ? 19.403  -4.189  1.082   1.00 13.95 ? 12  LEU B CG  1 
ATOM   1894 C CD1 . LEU B 1 12  ? 20.342  -3.022  0.815   1.00 15.25 ? 12  LEU B CD1 1 
ATOM   1895 C CD2 . LEU B 1 12  ? 20.150  -5.513  0.887   1.00 14.87 ? 12  LEU B CD2 1 
ATOM   1896 N N   . LYS B 1 13  ? 17.833  -6.878  3.357   1.00 11.99 ? 13  LYS B N   1 
ATOM   1897 C CA  . LYS B 1 13  ? 17.887  -8.321  3.223   1.00 12.05 ? 13  LYS B CA  1 
ATOM   1898 C C   . LYS B 1 13  ? 16.520  -8.983  3.356   1.00 10.96 ? 13  LYS B C   1 
ATOM   1899 O O   . LYS B 1 13  ? 16.401  -10.190 3.167   1.00 12.79 ? 13  LYS B O   1 
ATOM   1900 C CB  . LYS B 1 13  ? 18.886  -8.908  4.203   1.00 13.11 ? 13  LYS B CB  1 
ATOM   1901 C CG  . LYS B 1 13  ? 20.307  -8.475  3.878   1.00 14.98 ? 13  LYS B CG  1 
ATOM   1902 C CD  . LYS B 1 13  ? 21.317  -9.013  4.861   1.00 17.80 ? 13  LYS B CD  1 
ATOM   1903 C CE  . LYS B 1 13  ? 22.645  -8.539  4.453   1.00 21.11 ? 13  LYS B CE  1 
ATOM   1904 N NZ  . LYS B 1 13  ? 23.673  -9.040  5.371   1.00 25.08 ? 13  LYS B NZ  1 
ATOM   1905 N N   . LEU B 1 14  ? 15.499  -8.174  3.677   1.00 10.74 ? 14  LEU B N   1 
ATOM   1906 C CA  . LEU B 1 14  ? 14.110  -8.613  3.732   1.00 11.02 ? 14  LEU B CA  1 
ATOM   1907 C C   . LEU B 1 14  ? 13.289  -8.088  2.568   1.00 10.71 ? 14  LEU B C   1 
ATOM   1908 O O   . LEU B 1 14  ? 12.071  -8.230  2.539   1.00 11.43 ? 14  LEU B O   1 
ATOM   1909 C CB  . LEU B 1 14  ? 13.468  -8.192  5.062   1.00 11.68 ? 14  LEU B CB  1 
ATOM   1910 C CG  . LEU B 1 14  ? 14.155  -8.735  6.302   1.00 12.00 ? 14  LEU B CG  1 
ATOM   1911 C CD1 . LEU B 1 14  ? 13.572  -8.056  7.536   1.00 12.69 ? 14  LEU B CD1 1 
ATOM   1912 C CD2 . LEU B 1 14  ? 14.013  -10.239 6.383   1.00 12.17 ? 14  LEU B CD2 1 
ATOM   1913 N N   . MET B 1 15  ? 13.908  -7.464  1.580   1.00 11.38 ? 15  MET B N   1 
ATOM   1914 C CA  . MET B 1 15  ? 13.116  -6.880  0.506   1.00 11.11 ? 15  MET B CA  1 
ATOM   1915 C C   . MET B 1 15  ? 12.728  -7.919  -0.544  1.00 10.88 ? 15  MET B C   1 
ATOM   1916 O O   . MET B 1 15  ? 13.541  -8.783  -0.920  1.00 11.27 ? 15  MET B O   1 
ATOM   1917 C CB  . MET B 1 15  ? 13.829  -5.729  -0.220  1.00 13.19 ? 15  MET B CB  1 
ATOM   1918 C CG  . MET B 1 15  ? 13.878  -4.450  0.542   1.00 15.75 ? 15  MET B CG  1 
ATOM   1919 S SD  . MET B 1 15  ? 14.338  -3.039  -0.481  1.00 19.65 ? 15  MET B SD  1 
ATOM   1920 C CE  . MET B 1 15  ? 12.822  -2.853  -1.457  1.00 21.00 ? 15  MET B CE  1 
ATOM   1921 N N   . ASP B 1 16  ? 11.486  -7.767  -1.032  1.00 11.11 ? 16  ASP B N   1 
ATOM   1922 C CA  . ASP B 1 16  ? 11.071  -8.329  -2.301  1.00 11.02 ? 16  ASP B CA  1 
ATOM   1923 C C   . ASP B 1 16  ? 11.157  -7.177  -3.296  1.00 11.45 ? 16  ASP B C   1 
ATOM   1924 O O   . ASP B 1 16  ? 10.282  -6.320  -3.365  1.00 13.14 ? 16  ASP B O   1 
ATOM   1925 C CB  . ASP B 1 16  ? 9.639   -8.863  -2.273  1.00 11.52 ? 16  ASP B CB  1 
ATOM   1926 C CG  . ASP B 1 16  ? 9.395   -10.155 -1.527  1.00 11.85 ? 16  ASP B CG  1 
ATOM   1927 O OD1 . ASP B 1 16  ? 10.276  -10.607 -0.806  1.00 13.09 ? 16  ASP B OD1 1 
ATOM   1928 O OD2 . ASP B 1 16  ? 8.258   -10.693 -1.651  1.00 15.29 ? 16  ASP B OD2 1 
ATOM   1929 N N   . LEU B 1 17  ? 12.247  -7.136  -4.064  1.00 11.42 ? 17  LEU B N   1 
ATOM   1930 C CA  . LEU B 1 17  ? 12.474  -5.985  -4.918  1.00 11.98 ? 17  LEU B CA  1 
ATOM   1931 C C   . LEU B 1 17  ? 11.653  -6.095  -6.201  1.00 11.75 ? 17  LEU B C   1 
ATOM   1932 O O   . LEU B 1 17  ? 11.680  -7.141  -6.847  1.00 12.78 ? 17  LEU B O   1 
ATOM   1933 C CB  . LEU B 1 17  ? 13.967  -5.964  -5.246  1.00 12.47 ? 17  LEU B CB  1 
ATOM   1934 C CG  . LEU B 1 17  ? 14.444  -4.670  -5.900  1.00 13.67 ? 17  LEU B CG  1 
ATOM   1935 C CD1 . LEU B 1 17  ? 14.341  -3.507  -4.960  1.00 15.61 ? 17  LEU B CD1 1 
ATOM   1936 C CD2 . LEU B 1 17  ? 15.856  -4.820  -6.418  1.00 14.51 ? 17  LEU B CD2 1 
ATOM   1937 N N   . SER B 1 18  ? 10.918  -5.028  -6.538  1.00 14.32 ? 18  SER B N   1 
ATOM   1938 C CA  . SER B 1 18  ? 10.096  -5.033  -7.746  1.00 19.49 ? 18  SER B CA  1 
ATOM   1939 C C   . SER B 1 18  ? 10.379  -3.776  -8.574  1.00 24.34 ? 18  SER B C   1 
ATOM   1940 O O   . SER B 1 18  ? 11.050  -2.869  -8.082  1.00 26.27 ? 18  SER B O   1 
ATOM   1941 C CB  . SER B 1 18  ? 8.640   -5.156  -7.383  1.00 24.38 ? 18  SER B CB  1 
ATOM   1942 O OG  . SER B 1 18  ? 8.276   -3.956  -6.749  1.00 29.86 ? 18  SER B OG  1 
ATOM   1943 N N   . THR B 1 19  ? 9.988   -3.779  -9.864  1.00 29.19 ? 19  THR B N   1 
ATOM   1944 C CA  . THR B 1 19  ? 9.892   -2.571  -10.689 1.00 32.59 ? 19  THR B CA  1 
ATOM   1945 C C   . THR B 1 19  ? 8.654   -1.756  -10.312 1.00 34.10 ? 19  THR B C   1 
ATOM   1946 O O   . THR B 1 19  ? 7.745   -2.306  -9.576  1.00 38.68 ? 19  THR B O   1 
ATOM   1947 C CB  . THR B 1 19  ? 9.828   -2.944  -12.169 1.00 33.26 ? 19  THR B CB  1 
ATOM   1948 O OG1 . THR B 1 19  ? 8.664   -3.760  -12.283 1.00 35.20 ? 19  THR B OG1 1 
ATOM   1949 C CG2 . THR B 1 19  ? 11.048  -3.710  -12.636 1.00 29.91 ? 19  THR B CG2 1 
ATOM   1950 N N   . GLY B 1 22  ? 6.470   -1.636  -13.743 1.00 43.30 ? 22  GLY B N   1 
ATOM   1951 C CA  . GLY B 1 22  ? 6.324   -3.077  -14.006 1.00 36.15 ? 22  GLY B CA  1 
ATOM   1952 C C   . GLY B 1 22  ? 7.321   -3.554  -15.067 1.00 38.25 ? 22  GLY B C   1 
ATOM   1953 O O   . GLY B 1 22  ? 7.857   -2.778  -15.855 1.00 43.13 ? 22  GLY B O   1 
ATOM   1954 N N   . ASP B 1 23  ? 7.512   -4.872  -15.092 1.00 33.46 ? 23  ASP B N   1 
ATOM   1955 C CA  . ASP B 1 23  ? 8.458   -5.567  -15.955 1.00 30.84 ? 23  ASP B CA  1 
ATOM   1956 C C   . ASP B 1 23  ? 7.751   -5.982  -17.241 1.00 31.79 ? 23  ASP B C   1 
ATOM   1957 O O   . ASP B 1 23  ? 7.012   -6.956  -17.253 1.00 37.49 ? 23  ASP B O   1 
ATOM   1958 C CB  . ASP B 1 23  ? 8.958   -6.822  -15.254 1.00 29.28 ? 23  ASP B CB  1 
ATOM   1959 C CG  . ASP B 1 23  ? 7.904   -7.565  -14.441 1.00 28.27 ? 23  ASP B CG  1 
ATOM   1960 O OD1 . ASP B 1 23  ? 7.254   -6.896  -13.611 1.00 34.38 ? 23  ASP B OD1 1 
ATOM   1961 O OD2 . ASP B 1 23  ? 7.761   -8.786  -14.604 1.00 20.76 ? 23  ASP B OD2 1 
ATOM   1962 N N   . TYR B 1 24  ? 7.969   -5.235  -18.321 1.00 28.58 ? 24  TYR B N   1 
ATOM   1963 C CA  . TYR B 1 24  ? 7.348   -5.557  -19.599 1.00 29.13 ? 24  TYR B CA  1 
ATOM   1964 C C   . TYR B 1 24  ? 8.398   -5.882  -20.643 1.00 27.61 ? 24  TYR B C   1 
ATOM   1965 O O   . TYR B 1 24  ? 8.048   -6.180  -21.793 1.00 31.12 ? 24  TYR B O   1 
ATOM   1966 C CB  . TYR B 1 24  ? 6.544   -4.362  -20.125 1.00 28.68 ? 24  TYR B CB  1 
ATOM   1967 C CG  . TYR B 1 24  ? 5.240   -4.217  -19.371 1.00 28.68 ? 24  TYR B CG  1 
ATOM   1968 C CD1 . TYR B 1 24  ? 5.229   -3.706  -18.079 1.00 29.18 ? 24  TYR B CD1 1 
ATOM   1969 C CD2 . TYR B 1 24  ? 4.032   -4.598  -19.945 1.00 30.61 ? 24  TYR B CD2 1 
ATOM   1970 C CE1 . TYR B 1 24  ? 4.051   -3.577  -17.371 1.00 31.53 ? 24  TYR B CE1 1 
ATOM   1971 C CE2 . TYR B 1 24  ? 2.842   -4.455  -19.255 1.00 33.26 ? 24  TYR B CE2 1 
ATOM   1972 C CZ  . TYR B 1 24  ? 2.856   -3.966  -17.956 1.00 33.49 ? 24  TYR B CZ  1 
ATOM   1973 O OH  . TYR B 1 24  ? 1.703   -3.818  -17.230 1.00 37.37 ? 24  TYR B OH  1 
ATOM   1974 N N   . THR B 1 25  ? 9.667   -5.714  -20.264 1.00 24.18 ? 25  THR B N   1 
ATOM   1975 C CA  . THR B 1 25  ? 10.741  -6.028  -21.184 1.00 22.68 ? 25  THR B CA  1 
ATOM   1976 C C   . THR B 1 25  ? 11.747  -6.868  -20.420 1.00 20.25 ? 25  THR B C   1 
ATOM   1977 O O   . THR B 1 25  ? 11.907  -6.740  -19.196 1.00 20.33 ? 25  THR B O   1 
ATOM   1978 C CB  . THR B 1 25  ? 11.408  -4.781  -21.772 1.00 22.23 ? 25  THR B CB  1 
ATOM   1979 O OG1 . THR B 1 25  ? 12.132  -4.106  -20.737 1.00 21.05 ? 25  THR B OG1 1 
ATOM   1980 C CG2 . THR B 1 25  ? 10.418  -3.864  -22.473 1.00 22.76 ? 25  THR B CG2 1 
ATOM   1981 N N   . ASP B 1 26  ? 12.486  -7.665  -21.195 1.00 21.81 ? 26  ASP B N   1 
ATOM   1982 C CA  . ASP B 1 26  ? 13.558  -8.453  -20.630 1.00 20.24 ? 26  ASP B CA  1 
ATOM   1983 C C   . ASP B 1 26  ? 14.594  -7.536  -19.982 1.00 18.39 ? 26  ASP B C   1 
ATOM   1984 O O   . ASP B 1 26  ? 15.105  -7.864  -18.920 1.00 17.17 ? 26  ASP B O   1 
ATOM   1985 C CB  . ASP B 1 26  ? 14.207  -9.349  -21.667 1.00 24.27 ? 26  ASP B CB  1 
ATOM   1986 C CG  . ASP B 1 26  ? 13.389  -10.560 -22.094 1.00 28.20 ? 26  ASP B CG  1 
ATOM   1987 O OD1 . ASP B 1 26  ? 12.374  -10.869 -21.438 1.00 27.80 ? 26  ASP B OD1 1 
ATOM   1988 O OD2 . ASP B 1 26  ? 13.798  -11.202 -23.070 1.00 35.07 ? 26  ASP B OD2 1 
ATOM   1989 N N   . GLU B 1 27  ? 14.910  -6.392  -20.610 1.00 18.53 ? 27  GLU B N   1 
ATOM   1990 C CA  . GLU B 1 27  ? 15.921  -5.501  -20.069 1.00 18.91 ? 27  GLU B CA  1 
ATOM   1991 C C   . GLU B 1 27  ? 15.523  -5.066  -18.657 1.00 17.29 ? 27  GLU B C   1 
ATOM   1992 O O   . GLU B 1 27  ? 16.363  -5.002  -17.766 1.00 18.54 ? 27  GLU B O   1 
ATOM   1993 C CB  . GLU B 1 27  ? 16.107  -4.288  -20.972 1.00 22.08 ? 27  GLU B CB  1 
ATOM   1994 C CG  . GLU B 1 27  ? 17.185  -3.330  -20.467 1.00 26.52 ? 27  GLU B CG  1 
ATOM   1995 C CD  . GLU B 1 27  ? 17.542  -2.161  -21.377 1.00 29.35 ? 27  GLU B CD  1 
ATOM   1996 O OE1 . GLU B 1 27  ? 16.891  -1.877  -22.429 1.00 36.06 ? 27  GLU B OE1 1 
ATOM   1997 O OE2 . GLU B 1 27  ? 18.516  -1.502  -20.969 1.00 38.74 ? 27  GLU B OE2 1 
ATOM   1998 N N   . LYS B 1 28  ? 14.231  -4.789  -18.434 1.00 15.77 ? 28  LYS B N   1 
ATOM   1999 C CA  . LYS B 1 28  ? 13.795  -4.339  -17.124 1.00 16.93 ? 28  LYS B CA  1 
ATOM   2000 C C   . LYS B 1 28  ? 13.916  -5.451  -16.085 1.00 14.12 ? 28  LYS B C   1 
ATOM   2001 O O   . LYS B 1 28  ? 14.320  -5.195  -14.956 1.00 15.63 ? 28  LYS B O   1 
ATOM   2002 C CB  . LYS B 1 28  ? 12.342  -3.880  -17.165 1.00 18.79 ? 28  LYS B CB  1 
ATOM   2003 C CG  . LYS B 1 28  ? 12.098  -2.602  -17.893 1.00 24.12 ? 28  LYS B CG  1 
ATOM   2004 C CD  . LYS B 1 28  ? 12.436  -1.362  -17.106 1.00 25.55 ? 28  LYS B CD  1 
ATOM   2005 C CE  . LYS B 1 28  ? 11.478  -1.236  -15.929 1.00 26.13 ? 28  LYS B CE  1 
ATOM   2006 N NZ  . LYS B 1 28  ? 11.918  -0.233  -14.963 1.00 30.40 ? 28  LYS B NZ  1 
ATOM   2007 N N   . VAL B 1 29  ? 13.590  -6.686  -16.473 1.00 14.00 ? 29  VAL B N   1 
ATOM   2008 C CA  . VAL B 1 29  ? 13.729  -7.805  -15.557 1.00 13.68 ? 29  VAL B CA  1 
ATOM   2009 C C   . VAL B 1 29  ? 15.200  -8.034  -15.223 1.00 12.49 ? 29  VAL B C   1 
ATOM   2010 O O   . VAL B 1 29  ? 15.566  -8.250  -14.065 1.00 12.91 ? 29  VAL B O   1 
ATOM   2011 C CB  . VAL B 1 29  ? 13.142  -9.084  -16.168 1.00 14.72 ? 29  VAL B CB  1 
ATOM   2012 C CG1 . VAL B 1 29  ? 13.418  -10.264 -15.270 1.00 14.15 ? 29  VAL B CG1 1 
ATOM   2013 C CG2 . VAL B 1 29  ? 11.665  -8.960  -16.487 1.00 16.54 ? 29  VAL B CG2 1 
ATOM   2014 N N   . ILE B 1 30  ? 16.072  -7.993  -16.247 1.00 13.49 ? 30  ILE B N   1 
ATOM   2015 C CA  . ILE B 1 30  ? 17.479  -8.248  -16.037 1.00 14.84 ? 30  ILE B CA  1 
ATOM   2016 C C   . ILE B 1 30  ? 18.051  -7.186  -15.112 1.00 14.25 ? 30  ILE B C   1 
ATOM   2017 O O   . ILE B 1 30  ? 18.781  -7.515  -14.166 1.00 15.71 ? 30  ILE B O   1 
ATOM   2018 C CB  . ILE B 1 30  ? 18.188  -8.327  -17.396 1.00 16.77 ? 30  ILE B CB  1 
ATOM   2019 C CG1 . ILE B 1 30  ? 17.715  -9.544  -18.179 1.00 17.81 ? 30  ILE B CG1 1 
ATOM   2020 C CG2 . ILE B 1 30  ? 19.703  -8.333  -17.204 1.00 18.11 ? 30  ILE B CG2 1 
ATOM   2021 C CD1 . ILE B 1 30  ? 18.138  -9.521  -19.641 1.00 19.68 ? 30  ILE B CD1 1 
ATOM   2022 N N   . ALA B 1 31  ? 17.673  -5.927  -15.341 1.00 14.86 ? 31  ALA B N   1 
ATOM   2023 C CA  . ALA B 1 31  ? 18.139  -4.829  -14.502 1.00 15.49 ? 31  ALA B CA  1 
ATOM   2024 C C   . ALA B 1 31  ? 17.694  -5.011  -13.053 1.00 14.97 ? 31  ALA B C   1 
ATOM   2025 O O   . ALA B 1 31  ? 18.424  -4.718  -12.133 1.00 15.15 ? 31  ALA B O   1 
ATOM   2026 C CB  . ALA B 1 31  ? 17.658  -3.502  -15.039 1.00 17.02 ? 31  ALA B CB  1 
ATOM   2027 N N   . LEU B 1 32  ? 16.462  -5.479  -12.884 1.00 13.40 ? 32  LEU B N   1 
ATOM   2028 C CA  . LEU B 1 32  ? 15.939  -5.720  -11.557 1.00 12.90 ? 32  LEU B CA  1 
ATOM   2029 C C   . LEU B 1 32  ? 16.804  -6.755  -10.838 1.00 12.63 ? 32  LEU B C   1 
ATOM   2030 O O   . LEU B 1 32  ? 17.143  -6.616  -9.658  1.00 12.90 ? 32  LEU B O   1 
ATOM   2031 C CB  . LEU B 1 32  ? 14.501  -6.229  -11.637 1.00 13.05 ? 32  LEU B CB  1 
ATOM   2032 C CG  . LEU B 1 32  ? 13.835  -6.546  -10.297 1.00 13.93 ? 32  LEU B CG  1 
ATOM   2033 C CD1 . LEU B 1 32  ? 13.662  -5.313  -9.436  1.00 16.24 ? 32  LEU B CD1 1 
ATOM   2034 C CD2 . LEU B 1 32  ? 12.500  -7.212  -10.551 1.00 13.64 ? 32  LEU B CD2 1 
ATOM   2035 N N   . CYS B 1 33  ? 17.089  -7.864  -11.528 1.00 12.45 ? 33  CYS B N   1 
ATOM   2036 C CA  . CYS B 1 33  ? 17.930  -8.883  -10.945 1.00 12.76 ? 33  CYS B CA  1 
ATOM   2037 C C   . CYS B 1 33  ? 19.295  -8.302  -10.541 1.00 13.14 ? 33  CYS B C   1 
ATOM   2038 O O   . CYS B 1 33  ? 19.818  -8.604  -9.470  1.00 13.49 ? 33  CYS B O   1 
ATOM   2039 C CB  . CYS B 1 33  ? 18.155  -10.035 -11.910 1.00 13.99 ? 33  CYS B CB  1 
ATOM   2040 S SG  . CYS B 1 33  ? 16.663  -10.955 -12.289 1.00 17.12 ? 33  CYS B SG  1 
ATOM   2041 N N   . HIS B 1 34  ? 19.890  -7.474  -11.416 1.00 13.60 ? 34  HIS B N   1 
ATOM   2042 C CA  . HIS B 1 34  ? 21.166  -6.862  -11.089 1.00 14.91 ? 34  HIS B CA  1 
ATOM   2043 C C   . HIS B 1 34  ? 21.076  -5.978  -9.848  1.00 14.75 ? 34  HIS B C   1 
ATOM   2044 O O   . HIS B 1 34  ? 21.968  -5.971  -8.997  1.00 15.99 ? 34  HIS B O   1 
ATOM   2045 C CB  . HIS B 1 34  ? 21.706  -6.081  -12.290 1.00 17.11 ? 34  HIS B CB  1 
ATOM   2046 C CG  . HIS B 1 34  ? 22.073  -6.943  -13.452 1.00 18.38 ? 34  HIS B CG  1 
ATOM   2047 N ND1 . HIS B 1 34  ? 22.312  -6.414  -14.697 1.00 22.51 ? 34  HIS B ND1 1 
ATOM   2048 C CD2 . HIS B 1 34  ? 22.219  -8.263  -13.580 1.00 20.52 ? 34  HIS B CD2 1 
ATOM   2049 C CE1 . HIS B 1 34  ? 22.623  -7.401  -15.529 1.00 22.44 ? 34  HIS B CE1 1 
ATOM   2050 N NE2 . HIS B 1 34  ? 22.592  -8.530  -14.883 1.00 22.20 ? 34  HIS B NE2 1 
ATOM   2051 N N   A GLN B 1 35  ? 19.967  -5.233  -9.730  0.50 14.20 ? 35  GLN B N   1 
ATOM   2052 N N   B GLN B 1 35  ? 19.955  -5.269  -9.737  0.50 14.58 ? 35  GLN B N   1 
ATOM   2053 C CA  A GLN B 1 35  ? 19.790  -4.316  -8.617  0.50 14.38 ? 35  GLN B CA  1 
ATOM   2054 C CA  B GLN B 1 35  ? 19.769  -4.328  -8.654  0.50 14.90 ? 35  GLN B CA  1 
ATOM   2055 C C   A GLN B 1 35  ? 19.641  -5.049  -7.289  0.50 14.13 ? 35  GLN B C   1 
ATOM   2056 C C   B GLN B 1 35  ? 19.605  -5.031  -7.307  0.50 14.59 ? 35  GLN B C   1 
ATOM   2057 O O   A GLN B 1 35  ? 20.030  -4.505  -6.254  0.50 15.01 ? 35  GLN B O   1 
ATOM   2058 O O   B GLN B 1 35  ? 19.904  -4.431  -6.273  0.50 15.47 ? 35  GLN B O   1 
ATOM   2059 C CB  A GLN B 1 35  ? 18.595  -3.399  -8.848  0.50 15.11 ? 35  GLN B CB  1 
ATOM   2060 C CB  B GLN B 1 35  ? 18.531  -3.514  -8.997  0.50 16.53 ? 35  GLN B CB  1 
ATOM   2061 C CG  A GLN B 1 35  ? 18.901  -2.355  -9.912  0.50 17.24 ? 35  GLN B CG  1 
ATOM   2062 C CG  B GLN B 1 35  ? 18.259  -2.371  -8.037  0.50 18.99 ? 35  GLN B CG  1 
ATOM   2063 C CD  A GLN B 1 35  ? 17.675  -1.719  -10.512 0.50 21.12 ? 35  GLN B CD  1 
ATOM   2064 C CD  B GLN B 1 35  ? 17.071  -1.561  -8.496  0.50 22.61 ? 35  GLN B CD  1 
ATOM   2065 O OE1 A GLN B 1 35  ? 16.545  -1.933  -10.069 0.50 24.76 ? 35  GLN B OE1 1 
ATOM   2066 O OE1 B GLN B 1 35  ? 16.086  -2.094  -9.028  0.50 25.80 ? 35  GLN B OE1 1 
ATOM   2067 N NE2 A GLN B 1 35  ? 17.909  -0.907  -11.531 0.50 23.84 ? 35  GLN B NE2 1 
ATOM   2068 N NE2 B GLN B 1 35  ? 17.182  -0.254  -8.325  0.50 26.62 ? 35  GLN B NE2 1 
ATOM   2069 N N   . ALA B 1 36  ? 19.094  -6.270  -7.338  1.00 12.53 ? 36  ALA B N   1 
ATOM   2070 C CA  . ALA B 1 36  ? 18.893  -7.071  -6.147  1.00 12.82 ? 36  ALA B CA  1 
ATOM   2071 C C   . ALA B 1 36  ? 20.199  -7.535  -5.514  1.00 12.32 ? 36  ALA B C   1 
ATOM   2072 O O   . ALA B 1 36  ? 20.218  -7.901  -4.342  1.00 12.63 ? 36  ALA B O   1 
ATOM   2073 C CB  . ALA B 1 36  ? 18.023  -8.252  -6.453  1.00 12.52 ? 36  ALA B CB  1 
ATOM   2074 N N   . LYS B 1 37  ? 21.270  -7.568  -6.313  1.00 12.86 ? 37  LYS B N   1 
ATOM   2075 C CA  . LYS B 1 37  ? 22.603  -7.960  -5.860  1.00 13.08 ? 37  LYS B CA  1 
ATOM   2076 C C   . LYS B 1 37  ? 23.338  -6.673  -5.508  1.00 13.22 ? 37  LYS B C   1 
ATOM   2077 O O   . LYS B 1 37  ? 24.010  -6.065  -6.354  1.00 15.44 ? 37  LYS B O   1 
ATOM   2078 C CB  . LYS B 1 37  ? 23.293  -8.741  -6.997  1.00 13.93 ? 37  LYS B CB  1 
ATOM   2079 C CG  . LYS B 1 37  ? 24.678  -9.243  -6.637  1.00 13.58 ? 37  LYS B CG  1 
ATOM   2080 C CD  . LYS B 1 37  ? 25.337  -9.921  -7.839  1.00 15.62 ? 37  LYS B CD  1 
ATOM   2081 C CE  . LYS B 1 37  ? 26.635  -10.575 -7.449  1.00 18.72 ? 37  LYS B CE  1 
ATOM   2082 N NZ  . LYS B 1 37  ? 27.393  -11.053 -8.607  1.00 20.94 ? 37  LYS B NZ  1 
ATOM   2083 N N   . THR B 1 38  ? 23.192  -6.236  -4.262  1.00 13.28 ? 38  THR B N   1 
ATOM   2084 C CA  . THR B 1 38  ? 23.631  -4.912  -3.869  1.00 13.16 ? 38  THR B CA  1 
ATOM   2085 C C   . THR B 1 38  ? 25.016  -5.010  -3.254  1.00 13.12 ? 38  THR B C   1 
ATOM   2086 O O   . THR B 1 38  ? 25.476  -6.091  -2.875  1.00 13.32 ? 38  THR B O   1 
ATOM   2087 C CB  . THR B 1 38  ? 22.673  -4.252  -2.864  1.00 14.16 ? 38  THR B CB  1 
ATOM   2088 O OG1 . THR B 1 38  ? 23.077  -4.492  -1.520  1.00 13.96 ? 38  THR B OG1 1 
ATOM   2089 C CG2 . THR B 1 38  ? 21.212  -4.602  -3.058  1.00 15.44 ? 38  THR B CG2 1 
ATOM   2090 N N   . PRO B 1 39  ? 25.719  -3.859  -3.133  1.00 15.08 ? 39  PRO B N   1 
ATOM   2091 C CA  . PRO B 1 39  ? 27.055  -3.883  -2.544  1.00 15.00 ? 39  PRO B CA  1 
ATOM   2092 C C   . PRO B 1 39  ? 27.105  -4.347  -1.095  1.00 13.86 ? 39  PRO B C   1 
ATOM   2093 O O   . PRO B 1 39  ? 28.171  -4.652  -0.597  1.00 15.02 ? 39  PRO B O   1 
ATOM   2094 C CB  . PRO B 1 39  ? 27.538  -2.428  -2.668  1.00 17.85 ? 39  PRO B CB  1 
ATOM   2095 C CG  . PRO B 1 39  ? 26.690  -1.838  -3.766  1.00 19.87 ? 39  PRO B CG  1 
ATOM   2096 C CD  . PRO B 1 39  ? 25.341  -2.525  -3.639  1.00 17.97 ? 39  PRO B CD  1 
ATOM   2097 N N   . VAL B 1 40  ? 25.955  -4.340  -0.392  1.00 13.84 ? 40  VAL B N   1 
ATOM   2098 C CA  . VAL B 1 40  ? 25.943  -4.723  1.009   1.00 13.80 ? 40  VAL B CA  1 
ATOM   2099 C C   . VAL B 1 40  ? 25.209  -6.048  1.229   1.00 13.09 ? 40  VAL B C   1 
ATOM   2100 O O   . VAL B 1 40  ? 25.009  -6.459  2.381   1.00 13.98 ? 40  VAL B O   1 
ATOM   2101 C CB  . VAL B 1 40  ? 25.307  -3.635  1.894   1.00 16.34 ? 40  VAL B CB  1 
ATOM   2102 C CG1 . VAL B 1 40  ? 26.065  -2.330  1.743   1.00 18.40 ? 40  VAL B CG1 1 
ATOM   2103 C CG2 . VAL B 1 40  ? 23.810  -3.471  1.636   1.00 17.52 ? 40  VAL B CG2 1 
ATOM   2104 N N   . GLY B 1 41  ? 24.766  -6.697  0.163   1.00 13.23 ? 41  GLY B N   1 
ATOM   2105 C CA  . GLY B 1 41  ? 24.066  -7.960  0.276   1.00 13.35 ? 41  GLY B CA  1 
ATOM   2106 C C   . GLY B 1 41  ? 22.923  -8.042  -0.721  1.00 12.31 ? 41  GLY B C   1 
ATOM   2107 O O   . GLY B 1 41  ? 22.638  -7.099  -1.447  1.00 13.52 ? 41  GLY B O   1 
ATOM   2108 N N   . ASN B 1 42  ? 22.317  -9.217  -0.743  1.00 12.63 ? 42  ASN B N   1 
ATOM   2109 C CA  . ASN B 1 42  ? 21.208  -9.508  -1.636  1.00 12.44 ? 42  ASN B CA  1 
ATOM   2110 C C   . ASN B 1 42  ? 19.876  -9.240  -0.957  1.00 12.27 ? 42  ASN B C   1 
ATOM   2111 O O   . ASN B 1 42  ? 19.725  -9.461  0.239   1.00 12.89 ? 42  ASN B O   1 
ATOM   2112 C CB  . ASN B 1 42  ? 21.252  -10.959 -2.077  1.00 12.96 ? 42  ASN B CB  1 
ATOM   2113 C CG  . ASN B 1 42  ? 22.511  -11.281 -2.868  1.00 13.95 ? 42  ASN B CG  1 
ATOM   2114 O OD1 . ASN B 1 42  ? 23.098  -10.408 -3.507  1.00 15.82 ? 42  ASN B OD1 1 
ATOM   2115 N ND2 . ASN B 1 42  ? 22.857  -12.550 -2.903  1.00 16.75 ? 42  ASN B ND2 1 
ATOM   2116 N N   . THR B 1 43  ? 18.925  -8.753  -1.742  1.00 11.98 ? 43  THR B N   1 
ATOM   2117 C CA  . THR B 1 43  ? 17.564  -8.751  -1.235  1.00 11.62 ? 43  THR B CA  1 
ATOM   2118 C C   . THR B 1 43  ? 17.078  -10.186 -1.060  1.00 11.24 ? 43  THR B C   1 
ATOM   2119 O O   . THR B 1 43  ? 17.680  -11.127 -1.541  1.00 11.81 ? 43  THR B O   1 
ATOM   2120 C CB  . THR B 1 43  ? 16.660  -7.955  -2.167  1.00 11.78 ? 43  THR B CB  1 
ATOM   2121 O OG1 . THR B 1 43  ? 16.581  -8.583  -3.436  1.00 12.76 ? 43  THR B OG1 1 
ATOM   2122 C CG2 . THR B 1 43  ? 17.110  -6.508  -2.316  1.00 12.04 ? 43  THR B CG2 1 
ATOM   2123 N N   . ALA B 1 44  ? 15.954  -10.347 -0.302  1.00 11.47 ? 44  ALA B N   1 
ATOM   2124 C CA  . ALA B 1 44  ? 15.413  -11.679 -0.096  1.00 10.89 ? 44  ALA B CA  1 
ATOM   2125 C C   . ALA B 1 44  ? 14.902  -12.295 -1.395  1.00 10.47 ? 44  ALA B C   1 
ATOM   2126 O O   . ALA B 1 44  ? 14.996  -13.506 -1.604  1.00 10.67 ? 44  ALA B O   1 
ATOM   2127 C CB  . ALA B 1 44  ? 14.276  -11.605 0.922   1.00 11.78 ? 44  ALA B CB  1 
ATOM   2128 N N   . ALA B 1 45  ? 14.293  -11.434 -2.198  1.00 10.37 ? 45  ALA B N   1 
ATOM   2129 C CA  . ALA B 1 45  ? 13.589  -11.862 -3.395  1.00 10.31 ? 45  ALA B CA  1 
ATOM   2130 C C   . ALA B 1 45  ? 13.557  -10.725 -4.400  1.00 10.64 ? 45  ALA B C   1 
ATOM   2131 O O   . ALA B 1 45  ? 13.847  -9.566  -4.103  1.00 11.06 ? 45  ALA B O   1 
ATOM   2132 C CB  . ALA B 1 45  ? 12.162  -12.275 -3.004  1.00 10.89 ? 45  ALA B CB  1 
ATOM   2133 N N   . ILE B 1 46  ? 13.155  -11.109 -5.605  1.00 10.44 ? 46  ILE B N   1 
ATOM   2134 C CA  . ILE B 1 46  ? 12.651  -10.172 -6.601  1.00 10.92 ? 46  ILE B CA  1 
ATOM   2135 C C   . ILE B 1 46  ? 11.191  -10.573 -6.833  1.00 10.84 ? 46  ILE B C   1 
ATOM   2136 O O   . ILE B 1 46  ? 10.834  -11.739 -6.650  1.00 12.70 ? 46  ILE B O   1 
ATOM   2137 C CB  . ILE B 1 46  ? 13.474  -10.171 -7.908  1.00 12.16 ? 46  ILE B CB  1 
ATOM   2138 C CG1 . ILE B 1 46  ? 13.512  -11.555 -8.517  1.00 15.02 ? 46  ILE B CG1 1 
ATOM   2139 C CG2 . ILE B 1 46  ? 14.884  -9.619  -7.657  1.00 12.71 ? 46  ILE B CG2 1 
ATOM   2140 C CD1 . ILE B 1 46  ? 13.997  -11.613 -9.925  1.00 19.06 ? 46  ILE B CD1 1 
ATOM   2141 N N   . SER B 1 47  ? 10.398  -9.614  -7.288  1.00 10.39 ? 47  SER B N   1 
ATOM   2142 C CA  . SER B 1 47  ? 9.011   -9.855  -7.629  1.00 11.34 ? 47  SER B CA  1 
ATOM   2143 C C   . SER B 1 47  ? 8.790   -9.388  -9.062  1.00 11.14 ? 47  SER B C   1 
ATOM   2144 O O   . SER B 1 47  ? 9.090   -8.247  -9.383  1.00 13.26 ? 47  SER B O   1 
ATOM   2145 C CB  . SER B 1 47  ? 8.122   -9.113  -6.663  1.00 13.93 ? 47  SER B CB  1 
ATOM   2146 O OG  . SER B 1 47  ? 6.751   -9.389  -6.905  1.00 19.31 ? 47  SER B OG  1 
ATOM   2147 N N   . VAL B 1 48  ? 8.247   -10.301 -9.857  1.00 11.09 ? 48  VAL B N   1 
ATOM   2148 C CA  . VAL B 1 48  ? 8.037   -10.071 -11.271 1.00 11.14 ? 48  VAL B CA  1 
ATOM   2149 C C   . VAL B 1 48  ? 6.697   -10.683 -11.668 1.00 11.49 ? 48  VAL B C   1 
ATOM   2150 O O   . VAL B 1 48  ? 6.162   -11.513 -10.947 1.00 12.96 ? 48  VAL B O   1 
ATOM   2151 C CB  . VAL B 1 48  ? 9.166   -10.661 -12.139 1.00 12.75 ? 48  VAL B CB  1 
ATOM   2152 C CG1 . VAL B 1 48  ? 10.481  -9.965  -11.899 1.00 13.62 ? 48  VAL B CG1 1 
ATOM   2153 C CG2 . VAL B 1 48  ? 9.289   -12.153 -11.967 1.00 12.73 ? 48  VAL B CG2 1 
ATOM   2154 N N   . TYR B 1 49  ? 6.194   -10.309 -12.853 1.00 11.37 ? 49  TYR B N   1 
ATOM   2155 C CA  . TYR B 1 49  ? 5.007   -10.985 -13.367 1.00 11.81 ? 49  TYR B CA  1 
ATOM   2156 C C   . TYR B 1 49  ? 5.376   -12.402 -13.783 1.00 11.50 ? 49  TYR B C   1 
ATOM   2157 O O   . TYR B 1 49  ? 6.543   -12.718 -14.071 1.00 11.63 ? 49  TYR B O   1 
ATOM   2158 C CB  . TYR B 1 49  ? 4.410   -10.232 -14.549 1.00 13.65 ? 49  TYR B CB  1 
ATOM   2159 C CG  . TYR B 1 49  ? 3.691   -8.951  -14.199 1.00 15.97 ? 49  TYR B CG  1 
ATOM   2160 C CD1 . TYR B 1 49  ? 2.581   -8.985  -13.372 1.00 18.81 ? 49  TYR B CD1 1 
ATOM   2161 C CD2 . TYR B 1 49  ? 4.138   -7.721  -14.645 1.00 18.58 ? 49  TYR B CD2 1 
ATOM   2162 C CE1 . TYR B 1 49  ? 1.882   -7.834  -13.053 1.00 19.86 ? 49  TYR B CE1 1 
ATOM   2163 C CE2 . TYR B 1 49  ? 3.458   -6.554  -14.322 1.00 21.71 ? 49  TYR B CE2 1 
ATOM   2164 C CZ  . TYR B 1 49  ? 2.319   -6.617  -13.530 1.00 21.76 ? 49  TYR B CZ  1 
ATOM   2165 O OH  . TYR B 1 49  ? 1.598   -5.516  -13.159 1.00 27.29 ? 49  TYR B OH  1 
ATOM   2166 N N   . PRO B 1 50  ? 4.425   -13.341 -13.796 1.00 11.34 ? 50  PRO B N   1 
ATOM   2167 C CA  . PRO B 1 50  ? 4.742   -14.746 -14.015 1.00 11.61 ? 50  PRO B CA  1 
ATOM   2168 C C   . PRO B 1 50  ? 5.575   -15.014 -15.270 1.00 11.49 ? 50  PRO B C   1 
ATOM   2169 O O   . PRO B 1 50  ? 6.523   -15.805 -15.232 1.00 11.56 ? 50  PRO B O   1 
ATOM   2170 C CB  . PRO B 1 50  ? 3.383   -15.413 -14.097 1.00 12.69 ? 50  PRO B CB  1 
ATOM   2171 C CG  . PRO B 1 50  ? 2.572   -14.587 -13.128 1.00 12.59 ? 50  PRO B CG  1 
ATOM   2172 C CD  . PRO B 1 50  ? 3.010   -13.155 -13.404 1.00 11.68 ? 50  PRO B CD  1 
ATOM   2173 N N   . ARG B 1 51  ? 5.241   -14.328 -16.367 1.00 11.55 ? 51  ARG B N   1 
ATOM   2174 C CA  . ARG B 1 51  ? 5.910   -14.601 -17.633 1.00 12.65 ? 51  ARG B CA  1 
ATOM   2175 C C   . ARG B 1 51  ? 7.385   -14.249 -17.575 1.00 12.72 ? 51  ARG B C   1 
ATOM   2176 O O   . ARG B 1 51  ? 8.170   -14.683 -18.443 1.00 13.60 ? 51  ARG B O   1 
ATOM   2177 C CB  . ARG B 1 51  ? 5.218   -13.827 -18.744 1.00 13.91 ? 51  ARG B CB  1 
ATOM   2178 C CG  . ARG B 1 51  ? 5.195   -12.326 -18.575 1.00 17.48 ? 51  ARG B CG  1 
ATOM   2179 C CD  . ARG B 1 51  ? 4.493   -11.701 -19.758 1.00 24.16 ? 51  ARG B CD  1 
ATOM   2180 N NE  . ARG B 1 51  ? 4.440   -10.263 -19.582 1.00 31.35 ? 51  ARG B NE  1 
ATOM   2181 C CZ  . ARG B 1 51  ? 3.552   -9.590  -18.854 1.00 36.73 ? 51  ARG B CZ  1 
ATOM   2182 N NH1 . ARG B 1 51  ? 2.588   -10.222 -18.179 1.00 40.21 ? 51  ARG B NH1 1 
ATOM   2183 N NH2 . ARG B 1 51  ? 3.638   -8.268  -18.806 1.00 40.94 ? 51  ARG B NH2 1 
ATOM   2184 N N   . SER B 1 52  ? 7.785   -13.427 -16.604 1.00 11.89 ? 52  SER B N   1 
ATOM   2185 C CA  . SER B 1 52  ? 9.163   -12.972 -16.470 1.00 11.72 ? 52  SER B CA  1 
ATOM   2186 C C   . SER B 1 52  ? 10.024  -13.932 -15.658 1.00 10.91 ? 52  SER B C   1 
ATOM   2187 O O   . SER B 1 52  ? 11.241  -13.732 -15.566 1.00 11.54 ? 52  SER B O   1 
ATOM   2188 C CB  . SER B 1 52  ? 9.215   -11.594 -15.804 1.00 13.25 ? 52  SER B CB  1 
ATOM   2189 O OG  . SER B 1 52  ? 8.525   -10.653 -16.613 1.00 16.62 ? 52  SER B OG  1 
ATOM   2190 N N   . ILE B 1 53  ? 9.410   -14.942 -15.044 1.00 10.93 ? 53  ILE B N   1 
ATOM   2191 C CA  . ILE B 1 53  ? 10.138  -15.791 -14.122 1.00 11.10 ? 53  ILE B CA  1 
ATOM   2192 C C   . ILE B 1 53  ? 11.288  -16.506 -14.825 1.00 11.47 ? 53  ILE B C   1 
ATOM   2193 O O   . ILE B 1 53  ? 12.387  -16.537 -14.273 1.00 11.81 ? 53  ILE B O   1 
ATOM   2194 C CB  . ILE B 1 53  ? 9.211   -16.771 -13.402 1.00 11.74 ? 53  ILE B CB  1 
ATOM   2195 C CG1 . ILE B 1 53  ? 8.311   -15.977 -12.478 1.00 11.94 ? 53  ILE B CG1 1 
ATOM   2196 C CG2 . ILE B 1 53  ? 9.992   -17.836 -12.633 1.00 12.39 ? 53  ILE B CG2 1 
ATOM   2197 C CD1 . ILE B 1 53  ? 7.154   -16.758 -11.891 1.00 13.57 ? 53  ILE B CD1 1 
ATOM   2198 N N   . PRO B 1 54  ? 11.117  -17.126 -16.016 1.00 12.61 ? 54  PRO B N   1 
ATOM   2199 C CA  . PRO B 1 54  ? 12.240  -17.873 -16.605 1.00 12.70 ? 54  PRO B CA  1 
ATOM   2200 C C   . PRO B 1 54  ? 13.474  -17.027 -16.869 1.00 12.42 ? 54  PRO B C   1 
ATOM   2201 O O   . PRO B 1 54  ? 14.601  -17.474 -16.543 1.00 13.36 ? 54  PRO B O   1 
ATOM   2202 C CB  . PRO B 1 54  ? 11.590  -18.465 -17.840 1.00 13.32 ? 54  PRO B CB  1 
ATOM   2203 C CG  . PRO B 1 54  ? 10.133  -18.610 -17.471 1.00 13.21 ? 54  PRO B CG  1 
ATOM   2204 C CD  . PRO B 1 54  ? 9.851   -17.311 -16.753 1.00 12.91 ? 54  PRO B CD  1 
ATOM   2205 N N   . ILE B 1 55  ? 13.297  -15.832 -17.440 1.00 12.30 ? 55  ILE B N   1 
ATOM   2206 C CA  . ILE B 1 55  ? 14.470  -15.002 -17.719 1.00 13.07 ? 55  ILE B CA  1 
ATOM   2207 C C   . ILE B 1 55  ? 15.089  -14.493 -16.426 1.00 12.01 ? 55  ILE B C   1 
ATOM   2208 O O   . ILE B 1 55  ? 16.297  -14.371 -16.280 1.00 12.78 ? 55  ILE B O   1 
ATOM   2209 C CB  . ILE B 1 55  ? 14.208  -13.874 -18.729 1.00 15.61 ? 55  ILE B CB  1 
ATOM   2210 C CG1 . ILE B 1 55  ? 15.512  -13.347 -19.278 1.00 18.98 ? 55  ILE B CG1 1 
ATOM   2211 C CG2 . ILE B 1 55  ? 13.356  -12.753 -18.171 1.00 16.70 ? 55  ILE B CG2 1 
ATOM   2212 C CD1 . ILE B 1 55  ? 16.225  -14.363 -20.130 1.00 24.10 ? 55  ILE B CD1 1 
ATOM   2213 N N   . ALA B 1 56  ? 14.262  -14.230 -15.424 1.00 11.50 ? 56  ALA B N   1 
ATOM   2214 C CA  . ALA B 1 56  ? 14.766  -13.816 -14.114 1.00 11.46 ? 56  ALA B CA  1 
ATOM   2215 C C   . ALA B 1 56  ? 15.620  -14.918 -13.505 1.00 11.38 ? 56  ALA B C   1 
ATOM   2216 O O   . ALA B 1 56  ? 16.695  -14.655 -12.986 1.00 11.88 ? 56  ALA B O   1 
ATOM   2217 C CB  . ALA B 1 56  ? 13.621  -13.446 -13.192 1.00 11.51 ? 56  ALA B CB  1 
ATOM   2218 N N   . ARG B 1 57  ? 15.143  -16.163 -13.555 1.00 11.86 ? 57  ARG B N   1 
ATOM   2219 C CA  . ARG B 1 57  ? 15.895  -17.251 -12.968 1.00 12.45 ? 57  ARG B CA  1 
ATOM   2220 C C   . ARG B 1 57  ? 17.241  -17.384 -13.676 1.00 12.46 ? 57  ARG B C   1 
ATOM   2221 O O   . ARG B 1 57  ? 18.268  -17.572 -13.033 1.00 13.57 ? 57  ARG B O   1 
ATOM   2222 C CB  . ARG B 1 57  ? 15.124  -18.563 -13.049 1.00 13.49 ? 57  ARG B CB  1 
ATOM   2223 C CG  . ARG B 1 57  ? 15.819  -19.713 -12.348 1.00 14.90 ? 57  ARG B CG  1 
ATOM   2224 C CD  . ARG B 1 57  ? 15.825  -19.635 -10.857 1.00 17.13 ? 57  ARG B CD  1 
ATOM   2225 N NE  . ARG B 1 57  ? 14.466  -19.973 -10.425 1.00 16.03 ? 57  ARG B NE  1 
ATOM   2226 C CZ  . ARG B 1 57  ? 13.989  -19.795 -9.206  1.00 15.97 ? 57  ARG B CZ  1 
ATOM   2227 N NH1 . ARG B 1 57  ? 14.737  -19.251 -8.265  1.00 18.58 ? 57  ARG B NH1 1 
ATOM   2228 N NH2 . ARG B 1 57  ? 12.758  -20.158 -8.942  1.00 16.64 ? 57  ARG B NH2 1 
ATOM   2229 N N   . LYS B 1 58  ? 17.227  -17.302 -15.001 1.00 12.62 ? 58  LYS B N   1 
ATOM   2230 C CA  . LYS B 1 58  ? 18.473  -17.415 -15.768 1.00 13.79 ? 58  LYS B CA  1 
ATOM   2231 C C   . LYS B 1 58  ? 19.452  -16.336 -15.321 1.00 13.52 ? 58  LYS B C   1 
ATOM   2232 O O   . LYS B 1 58  ? 20.655  -16.594 -15.173 1.00 15.09 ? 58  LYS B O   1 
ATOM   2233 C CB  . LYS B 1 58  ? 18.166  -17.282 -17.262 1.00 14.15 ? 58  LYS B CB  1 
ATOM   2234 C CG  . LYS B 1 58  ? 19.385  -17.524 -18.128 1.00 16.14 ? 58  LYS B CG  1 
ATOM   2235 C CD  . LYS B 1 58  ? 19.002  -17.616 -19.598 1.00 18.26 ? 58  LYS B CD  1 
ATOM   2236 C CE  . LYS B 1 58  ? 20.108  -18.010 -20.483 1.00 20.19 ? 58  LYS B CE  1 
ATOM   2237 N NZ  . LYS B 1 58  ? 19.635  -18.261 -21.851 1.00 24.13 ? 58  LYS B NZ  1 
ATOM   2238 N N   . THR B 1 59  ? 18.954  -15.106 -15.180 1.00 12.89 ? 59  THR B N   1 
ATOM   2239 C CA  . THR B 1 59  ? 19.801  -13.979 -14.850 1.00 13.25 ? 59  THR B CA  1 
ATOM   2240 C C   . THR B 1 59  ? 20.357  -14.141 -13.436 1.00 13.25 ? 59  THR B C   1 
ATOM   2241 O O   . THR B 1 59  ? 21.536  -13.882 -13.194 1.00 14.52 ? 59  THR B O   1 
ATOM   2242 C CB  . THR B 1 59  ? 19.033  -12.665 -14.980 1.00 13.69 ? 59  THR B CB  1 
ATOM   2243 O OG1 . THR B 1 59  ? 18.473  -12.568 -16.275 1.00 14.83 ? 59  THR B OG1 1 
ATOM   2244 C CG2 . THR B 1 59  ? 19.886  -11.443 -14.698 1.00 14.77 ? 59  THR B CG2 1 
ATOM   2245 N N   . LEU B 1 60  ? 19.507  -14.502 -12.449 1.00 12.75 ? 60  LEU B N   1 
ATOM   2246 C CA  . LEU B 1 60  ? 19.988  -14.688 -11.094 1.00 12.89 ? 60  LEU B CA  1 
ATOM   2247 C C   . LEU B 1 60  ? 21.058  -15.773 -11.032 1.00 13.84 ? 60  LEU B C   1 
ATOM   2248 O O   . LEU B 1 60  ? 22.031  -15.620 -10.302 1.00 15.21 ? 60  LEU B O   1 
ATOM   2249 C CB  . LEU B 1 60  ? 18.818  -15.045 -10.181 1.00 12.39 ? 60  LEU B CB  1 
ATOM   2250 C CG  . LEU B 1 60  ? 17.780  -13.942 -9.987  1.00 12.67 ? 60  LEU B CG  1 
ATOM   2251 C CD1 . LEU B 1 60  ? 16.581  -14.487 -9.287  1.00 14.16 ? 60  LEU B CD1 1 
ATOM   2252 C CD2 . LEU B 1 60  ? 18.378  -12.761 -9.233  1.00 12.74 ? 60  LEU B CD2 1 
ATOM   2253 N N   . LYS B 1 61  ? 20.882  -16.868 -11.780 1.00 14.41 ? 61  LYS B N   1 
ATOM   2254 C CA  . LYS B 1 61  ? 21.910  -17.908 -11.829 1.00 14.90 ? 61  LYS B CA  1 
ATOM   2255 C C   . LYS B 1 61  ? 23.199  -17.360 -12.440 1.00 16.33 ? 61  LYS B C   1 
ATOM   2256 O O   . LYS B 1 61  ? 24.288  -17.610 -11.924 1.00 18.38 ? 61  LYS B O   1 
ATOM   2257 C CB  . LYS B 1 61  ? 21.379  -19.151 -12.547 1.00 17.85 ? 61  LYS B CB  1 
ATOM   2258 C CG  . LYS B 1 61  ? 20.317  -19.931 -11.762 1.00 22.52 ? 61  LYS B CG  1 
ATOM   2259 C CD  . LYS B 1 61  ? 19.710  -21.035 -12.625 1.00 27.97 ? 61  LYS B CD  1 
ATOM   2260 C CE  . LYS B 1 61  ? 18.714  -21.932 -12.014 1.00 33.40 ? 61  LYS B CE  1 
ATOM   2261 N NZ  . LYS B 1 61  ? 18.142  -22.740 -13.098 1.00 37.46 ? 61  LYS B NZ  1 
ATOM   2262 N N   . GLU B 1 62  ? 23.079  -16.613 -13.536 1.00 16.63 ? 62  GLU B N   1 
ATOM   2263 C CA  . GLU B 1 62  ? 24.264  -16.174 -14.259 1.00 17.91 ? 62  GLU B CA  1 
ATOM   2264 C C   . GLU B 1 62  ? 25.107  -15.193 -13.436 1.00 16.83 ? 62  GLU B C   1 
ATOM   2265 O O   . GLU B 1 62  ? 26.326  -15.140 -13.534 1.00 19.87 ? 62  GLU B O   1 
ATOM   2266 C CB  . GLU B 1 62  ? 23.897  -15.571 -15.615 1.00 20.95 ? 62  GLU B CB  1 
ATOM   2267 C CG  . GLU B 1 62  ? 23.580  -16.642 -16.652 1.00 25.86 ? 62  GLU B CG  1 
ATOM   2268 C CD  . GLU B 1 62  ? 23.371  -16.134 -18.069 1.00 31.50 ? 62  GLU B CD  1 
ATOM   2269 O OE1 . GLU B 1 62  ? 23.665  -14.936 -18.314 1.00 38.63 ? 62  GLU B OE1 1 
ATOM   2270 O OE2 . GLU B 1 62  ? 22.958  -16.935 -18.944 1.00 34.81 ? 62  GLU B OE2 1 
ATOM   2271 N N   . GLN B 1 63  ? 24.452  -14.391 -12.597 1.00 16.14 ? 63  GLN B N   1 
ATOM   2272 C CA  . GLN B 1 63  ? 25.165  -13.440 -11.755 1.00 16.36 ? 63  GLN B CA  1 
ATOM   2273 C C   . GLN B 1 63  ? 25.594  -14.054 -10.426 1.00 16.48 ? 63  GLN B C   1 
ATOM   2274 O O   . GLN B 1 63  ? 26.144  -13.363 -9.577  1.00 19.37 ? 63  GLN B O   1 
ATOM   2275 C CB  . GLN B 1 63  ? 24.380  -12.154 -11.539 1.00 16.55 ? 63  GLN B CB  1 
ATOM   2276 C CG  . GLN B 1 63  ? 23.155  -12.327 -10.674 1.00 16.13 ? 63  GLN B CG  1 
ATOM   2277 C CD  . GLN B 1 63  ? 22.426  -11.022 -10.455 1.00 15.91 ? 63  GLN B CD  1 
ATOM   2278 O OE1 . GLN B 1 63  ? 22.611  -10.051 -11.203 1.00 19.72 ? 63  GLN B OE1 1 
ATOM   2279 N NE2 . GLN B 1 63  ? 21.574  -10.991 -9.435  1.00 14.11 ? 63  GLN B NE2 1 
ATOM   2280 N N   . GLY B 1 64  ? 25.368  -15.348 -10.228 1.00 17.09 ? 64  GLY B N   1 
ATOM   2281 C CA  . GLY B 1 64  ? 25.863  -15.980 -9.014  1.00 17.09 ? 64  GLY B CA  1 
ATOM   2282 C C   . GLY B 1 64  ? 25.023  -15.693 -7.775  1.00 16.61 ? 64  GLY B C   1 
ATOM   2283 O O   . GLY B 1 64  ? 25.533  -15.809 -6.682  1.00 18.61 ? 64  GLY B O   1 
ATOM   2284 N N   . THR B 1 65  ? 23.735  -15.418 -7.946  1.00 15.43 ? 65  THR B N   1 
ATOM   2285 C CA  . THR B 1 65  ? 22.848  -15.219 -6.801  1.00 14.75 ? 65  THR B CA  1 
ATOM   2286 C C   . THR B 1 65  ? 21.640  -16.137 -6.905  1.00 14.76 ? 65  THR B C   1 
ATOM   2287 O O   . THR B 1 65  ? 20.497  -15.679 -6.934  1.00 14.53 ? 65  THR B O   1 
ATOM   2288 C CB  . THR B 1 65  ? 22.408  -13.768 -6.667  1.00 14.79 ? 65  THR B CB  1 
ATOM   2289 O OG1 . THR B 1 65  ? 21.621  -13.400 -7.796  1.00 14.98 ? 65  THR B OG1 1 
ATOM   2290 C CG2 . THR B 1 65  ? 23.604  -12.850 -6.502  1.00 15.91 ? 65  THR B CG2 1 
ATOM   2291 N N   . PRO B 1 66  ? 21.849  -17.462 -6.967  1.00 16.52 ? 66  PRO B N   1 
ATOM   2292 C CA  . PRO B 1 66  ? 20.726  -18.380 -7.154  1.00 17.49 ? 66  PRO B CA  1 
ATOM   2293 C C   . PRO B 1 66  ? 19.825  -18.486 -5.940  1.00 18.44 ? 66  PRO B C   1 
ATOM   2294 O O   . PRO B 1 66  ? 18.744  -19.041 -6.067  1.00 20.98 ? 66  PRO B O   1 
ATOM   2295 C CB  . PRO B 1 66  ? 21.427  -19.699 -7.473  1.00 21.29 ? 66  PRO B CB  1 
ATOM   2296 C CG  . PRO B 1 66  ? 22.726  -19.582 -6.749  1.00 19.70 ? 66  PRO B CG  1 
ATOM   2297 C CD  . PRO B 1 66  ? 23.154  -18.147 -6.904  1.00 19.01 ? 66  PRO B CD  1 
ATOM   2298 N N   . GLU B 1 67  ? 20.250  -17.924 -4.797  1.00 18.44 ? 67  GLU B N   1 
ATOM   2299 C CA  . GLU B 1 67  ? 19.464  -18.030 -3.574  1.00 19.58 ? 67  GLU B CA  1 
ATOM   2300 C C   . GLU B 1 67  ? 18.474  -16.871 -3.447  1.00 15.66 ? 67  GLU B C   1 
ATOM   2301 O O   . GLU B 1 67  ? 17.627  -16.889 -2.535  1.00 17.80 ? 67  GLU B O   1 
ATOM   2302 C CB  . GLU B 1 67  ? 20.373  -18.100 -2.344  1.00 24.18 ? 67  GLU B CB  1 
ATOM   2303 C CG  . GLU B 1 67  ? 21.086  -16.787 -2.009  1.00 29.58 ? 67  GLU B CG  1 
ATOM   2304 C CD  . GLU B 1 67  ? 22.382  -16.437 -2.739  1.00 34.07 ? 67  GLU B CD  1 
ATOM   2305 O OE1 . GLU B 1 67  ? 22.349  -16.291 -3.948  1.00 29.33 ? 67  GLU B OE1 1 
ATOM   2306 O OE2 . GLU B 1 67  ? 23.438  -16.236 -2.088  1.00 44.57 ? 67  GLU B OE2 1 
ATOM   2307 N N   . ILE B 1 68  ? 18.543  -15.875 -4.345  1.00 13.11 ? 68  ILE B N   1 
ATOM   2308 C CA  . ILE B 1 68  ? 17.517  -14.831 -4.353  1.00 12.27 ? 68  ILE B CA  1 
ATOM   2309 C C   . ILE B 1 68  ? 16.225  -15.480 -4.844  1.00 12.43 ? 68  ILE B C   1 
ATOM   2310 O O   . ILE B 1 68  ? 16.194  -16.098 -5.906  1.00 13.45 ? 68  ILE B O   1 
ATOM   2311 C CB  . ILE B 1 68  ? 17.926  -13.607 -5.193  1.00 12.31 ? 68  ILE B CB  1 
ATOM   2312 C CG1 . ILE B 1 68  ? 19.202  -12.965 -4.630  1.00 12.00 ? 68  ILE B CG1 1 
ATOM   2313 C CG2 . ILE B 1 68  ? 16.773  -12.619 -5.367  1.00 12.75 ? 68  ILE B CG2 1 
ATOM   2314 C CD1 . ILE B 1 68  ? 19.674  -11.737 -5.410  1.00 13.06 ? 68  ILE B CD1 1 
ATOM   2315 N N   . ARG B 1 69  ? 15.138  -15.320 -4.073  1.00 11.40 ? 69  ARG B N   1 
ATOM   2316 C CA  . ARG B 1 69  ? 13.884  -15.967 -4.398  1.00 11.44 ? 69  ARG B CA  1 
ATOM   2317 C C   . ARG B 1 69  ? 13.192  -15.187 -5.503  1.00 10.47 ? 69  ARG B C   1 
ATOM   2318 O O   . ARG B 1 69  ? 13.336  -13.972 -5.597  1.00 11.30 ? 69  ARG B O   1 
ATOM   2319 C CB  . ARG B 1 69  ? 13.023  -16.046 -3.131  1.00 12.90 ? 69  ARG B CB  1 
ATOM   2320 C CG  . ARG B 1 69  ? 13.699  -16.700 -1.931  1.00 15.56 ? 69  ARG B CG  1 
ATOM   2321 C CD  . ARG B 1 69  ? 13.047  -16.180 -0.637  1.00 20.50 ? 69  ARG B CD  1 
ATOM   2322 N NE  . ARG B 1 69  ? 13.637  -16.650 0.612   1.00 24.90 ? 69  ARG B NE  1 
ATOM   2323 C CZ  . ARG B 1 69  ? 14.781  -16.206 1.156   1.00 27.24 ? 69  ARG B CZ  1 
ATOM   2324 N NH1 . ARG B 1 69  ? 15.423  -15.172 0.643   1.00 29.25 ? 69  ARG B NH1 1 
ATOM   2325 N NH2 . ARG B 1 69  ? 15.273  -16.798 2.223   1.00 30.54 ? 69  ARG B NH2 1 
ATOM   2326 N N   . ILE B 1 70  ? 12.380  -15.910 -6.265  1.00 10.30 ? 70  ILE B N   1 
ATOM   2327 C CA  . ILE B 1 70  ? 11.512  -15.278 -7.236  1.00 10.06 ? 70  ILE B CA  1 
ATOM   2328 C C   . ILE B 1 70  ? 10.061  -15.384 -6.743  1.00 9.89  ? 70  ILE B C   1 
ATOM   2329 O O   . ILE B 1 70  ? 9.502   -16.472 -6.671  1.00 10.79 ? 70  ILE B O   1 
ATOM   2330 C CB  . ILE B 1 70  ? 11.679  -15.866 -8.632  1.00 11.22 ? 70  ILE B CB  1 
ATOM   2331 C CG1 . ILE B 1 70  ? 13.144  -15.785 -9.097  1.00 11.96 ? 70  ILE B CG1 1 
ATOM   2332 C CG2 . ILE B 1 70  ? 10.736  -15.136 -9.584  1.00 12.23 ? 70  ILE B CG2 1 
ATOM   2333 C CD1 . ILE B 1 70  ? 13.401  -16.468 -10.412 1.00 13.36 ? 70  ILE B CD1 1 
ATOM   2334 N N   . ALA B 1 71  ? 9.512   -14.212 -6.472  1.00 9.71  ? 71  ALA B N   1 
ATOM   2335 C CA  . ALA B 1 71  ? 8.106   -14.091 -6.121  1.00 10.18 ? 71  ALA B CA  1 
ATOM   2336 C C   . ALA B 1 71  ? 7.355   -13.542 -7.319  1.00 10.61 ? 71  ALA B C   1 
ATOM   2337 O O   . ALA B 1 71  ? 7.903   -12.828 -8.149  1.00 11.11 ? 71  ALA B O   1 
ATOM   2338 C CB  . ALA B 1 71  ? 7.961   -13.170 -4.942  1.00 11.01 ? 71  ALA B CB  1 
ATOM   2339 N N   . THR B 1 72  ? 6.058   -13.877 -7.392  1.00 11.40 ? 72  THR B N   1 
ATOM   2340 C CA  . THR B 1 72  ? 5.194   -13.317 -8.408  1.00 11.10 ? 72  THR B CA  1 
ATOM   2341 C C   . THR B 1 72  ? 3.815   -13.042 -7.787  1.00 11.21 ? 72  THR B C   1 
ATOM   2342 O O   . THR B 1 72  ? 3.658   -13.143 -6.571  1.00 12.42 ? 72  THR B O   1 
ATOM   2343 C CB  . THR B 1 72  ? 5.173   -14.237 -9.622  1.00 11.58 ? 72  THR B CB  1 
ATOM   2344 O OG1 . THR B 1 72  ? 4.565   -13.582 -10.724 1.00 11.71 ? 72  THR B OG1 1 
ATOM   2345 C CG2 . THR B 1 72  ? 4.492   -15.552 -9.326  1.00 12.10 ? 72  THR B CG2 1 
ATOM   2346 N N   . VAL B 1 73  ? 2.904   -12.595 -8.630  1.00 10.85 ? 73  VAL B N   1 
ATOM   2347 C CA  . VAL B 1 73  ? 1.575   -12.156 -8.240  1.00 10.50 ? 73  VAL B CA  1 
ATOM   2348 C C   . VAL B 1 73  ? 0.550   -12.886 -9.062  1.00 10.44 ? 73  VAL B C   1 
ATOM   2349 O O   . VAL B 1 73  ? 0.708   -13.068 -10.260 1.00 11.81 ? 73  VAL B O   1 
ATOM   2350 C CB  . VAL B 1 73  ? 1.402   -10.642 -8.346  1.00 11.31 ? 73  VAL B CB  1 
ATOM   2351 C CG1 . VAL B 1 73  ? 2.228   -9.930  -7.281  1.00 12.29 ? 73  VAL B CG1 1 
ATOM   2352 C CG2 . VAL B 1 73  ? 1.737   -10.110 -9.729  1.00 11.38 ? 73  VAL B CG2 1 
ATOM   2353 N N   . THR B 1 74  ? -0.557  -13.245 -8.396  1.00 10.05 ? 74  THR B N   1 
ATOM   2354 C CA  . THR B 1 74  ? -1.713  -13.806 -9.055  1.00 9.98  ? 74  THR B CA  1 
ATOM   2355 C C   . THR B 1 74  ? -3.004  -13.215 -8.488  1.00 10.11 ? 74  THR B C   1 
ATOM   2356 O O   . THR B 1 74  ? -3.012  -12.588 -7.434  1.00 10.62 ? 74  THR B O   1 
ATOM   2357 C CB  . THR B 1 74  ? -1.735  -15.328 -8.981  1.00 10.87 ? 74  THR B CB  1 
ATOM   2358 O OG1 . THR B 1 74  ? -1.867  -15.726 -7.625  1.00 11.01 ? 74  THR B OG1 1 
ATOM   2359 C CG2 . THR B 1 74  ? -0.476  -15.930 -9.581  1.00 11.41 ? 74  THR B CG2 1 
ATOM   2360 N N   . ASN B 1 75  ? -4.084  -13.407 -9.245  1.00 9.64  ? 75  ASN B N   1 
ATOM   2361 C CA  . ASN B 1 75  ? -5.359  -12.752 -8.978  1.00 9.75  ? 75  ASN B CA  1 
ATOM   2362 C C   . ASN B 1 75  ? -5.181  -11.244 -8.830  1.00 10.02 ? 75  ASN B C   1 
ATOM   2363 O O   . ASN B 1 75  ? -5.841  -10.584 -8.014  1.00 10.78 ? 75  ASN B O   1 
ATOM   2364 C CB  . ASN B 1 75  ? -6.045  -13.364 -7.765  1.00 10.01 ? 75  ASN B CB  1 
ATOM   2365 C CG  . ASN B 1 75  ? -7.556  -13.227 -7.808  1.00 10.09 ? 75  ASN B CG  1 
ATOM   2366 O OD1 . ASN B 1 75  ? -8.161  -13.301 -8.890  1.00 11.13 ? 75  ASN B OD1 1 
ATOM   2367 N ND2 . ASN B 1 75  ? -8.170  -13.063 -6.638  1.00 10.15 ? 75  ASN B ND2 1 
ATOM   2368 N N   . PHE B 1 76  ? -4.270  -10.663 -9.623  1.00 10.47 ? 76  PHE B N   1 
ATOM   2369 C CA  . PHE B 1 76  ? -3.672  -9.387  -9.307  1.00 10.84 ? 76  PHE B CA  1 
ATOM   2370 C C   . PHE B 1 76  ? -3.917  -8.353  -10.397 1.00 11.55 ? 76  PHE B C   1 
ATOM   2371 O O   . PHE B 1 76  ? -3.763  -8.675  -11.585 1.00 13.27 ? 76  PHE B O   1 
ATOM   2372 C CB  . PHE B 1 76  ? -2.179  -9.638  -9.122  1.00 11.25 ? 76  PHE B CB  1 
ATOM   2373 C CG  . PHE B 1 76  ? -1.352  -8.398  -8.833  1.00 11.99 ? 76  PHE B CG  1 
ATOM   2374 C CD1 . PHE B 1 76  ? -0.901  -7.570  -9.868  1.00 12.72 ? 76  PHE B CD1 1 
ATOM   2375 C CD2 . PHE B 1 76  ? -1.013  -8.087  -7.511  1.00 12.32 ? 76  PHE B CD2 1 
ATOM   2376 C CE1 . PHE B 1 76  ? -0.162  -6.450  -9.557  1.00 12.83 ? 76  PHE B CE1 1 
ATOM   2377 C CE2 . PHE B 1 76  ? -0.233  -6.984  -7.238  1.00 13.84 ? 76  PHE B CE2 1 
ATOM   2378 C CZ  . PHE B 1 76  ? 0.161   -6.163  -8.256  1.00 13.80 ? 76  PHE B CZ  1 
ATOM   2379 N N   . PRO B 1 77  ? -4.144  -7.068  -10.043 1.00 12.25 ? 77  PRO B N   1 
ATOM   2380 C CA  . PRO B 1 77  ? -4.258  -6.580  -8.653  1.00 12.74 ? 77  PRO B CA  1 
ATOM   2381 C C   . PRO B 1 77  ? -5.685  -6.579  -8.119  1.00 11.89 ? 77  PRO B C   1 
ATOM   2382 O O   . PRO B 1 77  ? -5.894  -6.150  -6.964  1.00 13.34 ? 77  PRO B O   1 
ATOM   2383 C CB  . PRO B 1 77  ? -3.766  -5.128  -8.765  1.00 14.31 ? 77  PRO B CB  1 
ATOM   2384 C CG  . PRO B 1 77  ? -4.253  -4.710  -10.151 1.00 14.71 ? 77  PRO B CG  1 
ATOM   2385 C CD  . PRO B 1 77  ? -4.145  -5.963  -11.006 1.00 14.36 ? 77  PRO B CD  1 
ATOM   2386 N N   . HIS B 1 78  C -6.624  -7.097  -8.922  1.00 11.29 ? 78  HIS B N   1 
ATOM   2387 C CA  . HIS B 1 78  C -8.043  -6.891  -8.677  1.00 12.03 ? 78  HIS B CA  1 
ATOM   2388 C C   . HIS B 1 78  C -8.596  -7.651  -7.481  1.00 11.76 ? 78  HIS B C   1 
ATOM   2389 O O   . HIS B 1 78  C -9.594  -7.183  -6.908  1.00 12.77 ? 78  HIS B O   1 
ATOM   2390 C CB  . HIS B 1 78  C -8.832  -7.306  -9.916  1.00 13.07 ? 78  HIS B CB  1 
ATOM   2391 C CG  . HIS B 1 78  C -8.346  -8.612  -10.499 1.00 13.49 ? 78  HIS B CG  1 
ATOM   2392 N ND1 . HIS B 1 78  C -8.568  -9.864  -9.953  1.00 13.18 ? 78  HIS B ND1 1 
ATOM   2393 C CD2 . HIS B 1 78  C -7.551  -8.826  -11.597 1.00 14.63 ? 78  HIS B CD2 1 
ATOM   2394 C CE1 . HIS B 1 78  C -8.011  -10.799 -10.718 1.00 14.82 ? 78  HIS B CE1 1 
ATOM   2395 N NE2 . HIS B 1 78  C -7.382  -10.182 -11.733 1.00 15.54 ? 78  HIS B NE2 1 
ATOM   2396 N N   . GLY B 1 79  ? -8.062  -8.809  -7.121  1.00 10.58 ? 79  GLY B N   1 
ATOM   2397 C CA  . GLY B 1 79  ? -8.680  -9.566  -6.044  1.00 10.64 ? 79  GLY B CA  1 
ATOM   2398 C C   . GLY B 1 79  ? -10.112 -9.965  -6.390  1.00 10.48 ? 79  GLY B C   1 
ATOM   2399 O O   . GLY B 1 79  ? -11.012 -9.977  -5.529  1.00 11.31 ? 79  GLY B O   1 
ATOM   2400 N N   . ASN B 1 80  ? -10.317 -10.408 -7.629  1.00 10.34 ? 80  ASN B N   1 
ATOM   2401 C CA  . ASN B 1 80  ? -11.601 -10.932 -8.038  1.00 10.96 ? 80  ASN B CA  1 
ATOM   2402 C C   . ASN B 1 80  ? -11.892 -12.238 -7.301  1.00 11.40 ? 80  ASN B C   1 
ATOM   2403 O O   . ASN B 1 80  ? -11.032 -12.842 -6.671  1.00 12.51 ? 80  ASN B O   1 
ATOM   2404 C CB  . ASN B 1 80  ? -11.640 -11.188 -9.532  1.00 12.23 ? 80  ASN B CB  1 
ATOM   2405 C CG  . ASN B 1 80  ? -11.683 -9.924  -10.350 1.00 13.77 ? 80  ASN B CG  1 
ATOM   2406 O OD1 . ASN B 1 80  ? -11.978 -8.826  -9.857  1.00 15.58 ? 80  ASN B OD1 1 
ATOM   2407 N ND2 . ASN B 1 80  ? -11.419 -10.091 -11.633 1.00 16.01 ? 80  ASN B ND2 1 
ATOM   2408 N N   . ASP B 1 81  ? -13.176 -12.636 -7.311  1.00 12.62 ? 81  ASP B N   1 
ATOM   2409 C CA  . ASP B 1 81  ? -13.619 -13.780 -6.520  1.00 12.96 ? 81  ASP B CA  1 
ATOM   2410 C C   . ASP B 1 81  ? -13.892 -15.022 -7.361  1.00 13.91 ? 81  ASP B C   1 
ATOM   2411 O O   . ASP B 1 81  ? -14.624 -15.914 -6.944  1.00 16.15 ? 81  ASP B O   1 
ATOM   2412 C CB  . ASP B 1 81  ? -14.822 -13.454 -5.646  1.00 14.81 ? 81  ASP B CB  1 
ATOM   2413 C CG  . ASP B 1 81  ? -16.012 -12.970 -6.421  1.00 17.66 ? 81  ASP B CG  1 
ATOM   2414 O OD1 . ASP B 1 81  ? -15.968 -12.979 -7.651  1.00 21.55 ? 81  ASP B OD1 1 
ATOM   2415 O OD2 . ASP B 1 81  ? -17.005 -12.639 -5.765  1.00 24.49 ? 81  ASP B OD2 1 
ATOM   2416 N N   . ASP B 1 82  ? -13.195 -15.148 -8.496  1.00 12.50 ? 82  ASP B N   1 
ATOM   2417 C CA  . ASP B 1 82  ? -13.275 -16.333 -9.338  1.00 12.98 ? 82  ASP B CA  1 
ATOM   2418 C C   . ASP B 1 82  ? -12.141 -17.265 -8.974  1.00 11.84 ? 82  ASP B C   1 
ATOM   2419 O O   . ASP B 1 82  ? -10.970 -17.019 -9.315  1.00 12.46 ? 82  ASP B O   1 
ATOM   2420 C CB  . ASP B 1 82  ? -13.260 -15.998 -10.820 1.00 13.25 ? 82  ASP B CB  1 
ATOM   2421 C CG  . ASP B 1 82  ? -13.514 -17.183 -11.733 1.00 14.78 ? 82  ASP B CG  1 
ATOM   2422 O OD1 . ASP B 1 82  ? -12.947 -18.243 -11.473 1.00 15.77 ? 82  ASP B OD1 1 
ATOM   2423 O OD2 . ASP B 1 82  ? -14.275 -17.043 -12.708 1.00 20.43 ? 82  ASP B OD2 1 
ATOM   2424 N N   . ILE B 1 83  ? -12.450 -18.309 -8.222  1.00 12.15 ? 83  ILE B N   1 
ATOM   2425 C CA  . ILE B 1 83  ? -11.442 -19.196 -7.682  1.00 12.54 ? 83  ILE B CA  1 
ATOM   2426 C C   . ILE B 1 83  ? -10.717 -19.896 -8.823  1.00 12.05 ? 83  ILE B C   1 
ATOM   2427 O O   . ILE B 1 83  ? -9.508  -20.068 -8.759  1.00 13.26 ? 83  ILE B O   1 
ATOM   2428 C CB  . ILE B 1 83  ? -12.054 -20.202 -6.704  1.00 13.52 ? 83  ILE B CB  1 
ATOM   2429 C CG1 . ILE B 1 83  ? -12.571 -19.495 -5.496  1.00 15.38 ? 83  ILE B CG1 1 
ATOM   2430 C CG2 . ILE B 1 83  ? -11.014 -21.253 -6.316  1.00 14.83 ? 83  ILE B CG2 1 
ATOM   2431 C CD1 . ILE B 1 83  ? -13.369 -20.380 -4.582  1.00 17.85 ? 83  ILE B CD1 1 
ATOM   2432 N N   . GLU B 1 84  ? -11.439 -20.350 -9.837  1.00 12.92 ? 84  GLU B N   1 
ATOM   2433 C CA  . GLU B 1 84  ? -10.826 -21.107 -10.914 1.00 14.49 ? 84  GLU B CA  1 
ATOM   2434 C C   . GLU B 1 84  ? -9.797  -20.266 -11.647 1.00 13.12 ? 84  GLU B C   1 
ATOM   2435 O O   . GLU B 1 84  ? -8.717  -20.766 -12.026 1.00 14.56 ? 84  GLU B O   1 
ATOM   2436 C CB  . GLU B 1 84  ? -11.878 -21.633 -11.870 1.00 16.66 ? 84  GLU B CB  1 
ATOM   2437 C CG  . GLU B 1 84  ? -12.663 -22.773 -11.247 1.00 22.37 ? 84  GLU B CG  1 
ATOM   2438 C CD  . GLU B 1 84  ? -11.974 -24.132 -11.212 1.00 30.26 ? 84  GLU B CD  1 
ATOM   2439 O OE1 . GLU B 1 84  ? -10.819 -24.254 -11.711 1.00 38.07 ? 84  GLU B OE1 1 
ATOM   2440 O OE2 . GLU B 1 84  ? -12.650 -25.094 -10.731 1.00 41.24 ? 84  GLU B OE2 1 
ATOM   2441 N N   . ILE B 1 85  ? -10.082 -18.975 -11.861 1.00 12.55 ? 85  ILE B N   1 
ATOM   2442 C CA  . ILE B 1 85  ? -9.085  -18.131 -12.511 1.00 11.98 ? 85  ILE B CA  1 
ATOM   2443 C C   . ILE B 1 85  ? -7.884  -17.927 -11.601 1.00 11.28 ? 85  ILE B C   1 
ATOM   2444 O O   . ILE B 1 85  ? -6.742  -18.014 -12.029 1.00 11.61 ? 85  ILE B O   1 
ATOM   2445 C CB  . ILE B 1 85  ? -9.733  -16.815 -12.968 1.00 13.31 ? 85  ILE B CB  1 
ATOM   2446 C CG1 . ILE B 1 85  ? -10.731 -17.098 -14.093 1.00 13.67 ? 85  ILE B CG1 1 
ATOM   2447 C CG2 . ILE B 1 85  ? -8.690  -15.772 -13.359 1.00 14.01 ? 85  ILE B CG2 1 
ATOM   2448 C CD1 . ILE B 1 85  ? -11.374 -15.862 -14.684 1.00 14.87 ? 85  ILE B CD1 1 
ATOM   2449 N N   . ALA B 1 86  ? -8.094  -17.601 -10.333 1.00 11.14 ? 86  ALA B N   1 
ATOM   2450 C CA  . ALA B 1 86  ? -6.974  -17.386 -9.424  1.00 11.03 ? 86  ALA B CA  1 
ATOM   2451 C C   . ALA B 1 86  ? -6.108  -18.637 -9.339  1.00 10.45 ? 86  ALA B C   1 
ATOM   2452 O O   . ALA B 1 86  ? -4.864  -18.559 -9.293  1.00 11.11 ? 86  ALA B O   1 
ATOM   2453 C CB  . ALA B 1 86  ? -7.494  -17.007 -8.073  1.00 11.82 ? 86  ALA B CB  1 
ATOM   2454 N N   . LEU B 1 87  ? -6.751  -19.802 -9.303  1.00 10.92 ? 87  LEU B N   1 
ATOM   2455 C CA  . LEU B 1 87  ? -6.022  -21.058 -9.196  1.00 10.94 ? 87  LEU B CA  1 
ATOM   2456 C C   . LEU B 1 87  ? -5.226  -21.329 -10.474 1.00 10.94 ? 87  LEU B C   1 
ATOM   2457 O O   . LEU B 1 87  ? -4.093  -21.781 -10.376 1.00 11.18 ? 87  LEU B O   1 
ATOM   2458 C CB  . LEU B 1 87  ? -7.006  -22.185 -8.910  1.00 11.45 ? 87  LEU B CB  1 
ATOM   2459 C CG  . LEU B 1 87  ? -6.435  -23.602 -8.802  1.00 12.71 ? 87  LEU B CG  1 
ATOM   2460 C CD1 . LEU B 1 87  ? -5.355  -23.707 -7.757  1.00 13.64 ? 87  LEU B CD1 1 
ATOM   2461 C CD2 . LEU B 1 87  ? -7.555  -24.583 -8.547  1.00 14.49 ? 87  LEU B CD2 1 
ATOM   2462 N N   . ALA B 1 88  ? -5.820  -21.109 -11.647 1.00 11.25 ? 88  ALA B N   1 
ATOM   2463 C CA  . ALA B 1 88  ? -5.119  -21.355 -12.899 1.00 10.79 ? 88  ALA B CA  1 
ATOM   2464 C C   . ALA B 1 88  ? -3.883  -20.473 -12.938 1.00 10.40 ? 88  ALA B C   1 
ATOM   2465 O O   . ALA B 1 88  ? -2.802  -20.921 -13.326 1.00 11.56 ? 88  ALA B O   1 
ATOM   2466 C CB  . ALA B 1 88  ? -6.035  -21.049 -14.054 1.00 11.42 ? 88  ALA B CB  1 
ATOM   2467 N N   . GLU B 1 89  ? -4.014  -19.217 -12.535 1.00 10.36 ? 89  GLU B N   1 
ATOM   2468 C CA  . GLU B 1 89  ? -2.899  -18.294 -12.548 1.00 10.44 ? 89  GLU B CA  1 
ATOM   2469 C C   . GLU B 1 89  ? -1.812  -18.767 -11.599 1.00 10.16 ? 89  GLU B C   1 
ATOM   2470 O O   . GLU B 1 89  ? -0.610  -18.676 -11.884 1.00 10.85 ? 89  GLU B O   1 
ATOM   2471 C CB  . GLU B 1 89  ? -3.360  -16.878 -12.215 1.00 11.39 ? 89  GLU B CB  1 
ATOM   2472 C CG  . GLU B 1 89  ? -4.240  -16.229 -13.267 1.00 12.35 ? 89  GLU B CG  1 
ATOM   2473 C CD  . GLU B 1 89  ? -4.609  -14.783 -12.986 1.00 12.93 ? 89  GLU B CD  1 
ATOM   2474 O OE1 . GLU B 1 89  ? -4.319  -14.303 -11.885 1.00 18.37 ? 89  GLU B OE1 1 
ATOM   2475 O OE2 . GLU B 1 89  ? -5.111  -14.105 -13.890 1.00 15.88 ? 89  GLU B OE2 1 
ATOM   2476 N N   . THR B 1 90  ? -2.204  -19.223 -10.416 1.00 10.00 ? 90  THR B N   1 
ATOM   2477 C CA  . THR B 1 90  ? -1.280  -19.723 -9.421  1.00 10.06 ? 90  THR B CA  1 
ATOM   2478 C C   . THR B 1 90  ? -0.555  -20.963 -9.944  1.00 9.76  ? 90  THR B C   1 
ATOM   2479 O O   . THR B 1 90  ? 0.675   -21.066 -9.792  1.00 10.71 ? 90  THR B O   1 
ATOM   2480 C CB  . THR B 1 90  ? -2.018  -19.959 -8.091  1.00 10.84 ? 90  THR B CB  1 
ATOM   2481 O OG1 . THR B 1 90  ? -2.520  -18.704 -7.650  1.00 11.32 ? 90  THR B OG1 1 
ATOM   2482 C CG2 . THR B 1 90  ? -1.081  -20.539 -7.043  1.00 11.59 ? 90  THR B CG2 1 
ATOM   2483 N N   . ARG B 1 91  ? -1.275  -21.900 -10.543 1.00 10.70 ? 91  ARG B N   1 
ATOM   2484 C CA  . ARG B 1 91  ? -0.653  -23.083 -11.123 1.00 10.93 ? 91  ARG B CA  1 
ATOM   2485 C C   . ARG B 1 91  ? 0.349   -22.669 -12.192 1.00 10.53 ? 91  ARG B C   1 
ATOM   2486 O O   . ARG B 1 91  ? 1.432   -23.272 -12.283 1.00 11.23 ? 91  ARG B O   1 
ATOM   2487 C CB  . ARG B 1 91  ? -1.724  -24.000 -11.697 1.00 12.00 ? 91  ARG B CB  1 
ATOM   2488 C CG  . ARG B 1 91  ? -2.531  -24.685 -10.608 1.00 13.23 ? 91  ARG B CG  1 
ATOM   2489 C CD  . ARG B 1 91  ? -3.613  -25.520 -11.231 1.00 16.23 ? 91  ARG B CD  1 
ATOM   2490 N NE  . ARG B 1 91  ? -4.318  -26.376 -10.289 1.00 18.13 ? 91  ARG B NE  1 
ATOM   2491 C CZ  . ARG B 1 91  ? -5.497  -26.932 -10.517 1.00 20.81 ? 91  ARG B CZ  1 
ATOM   2492 N NH1 . ARG B 1 91  ? -6.189  -26.627 -11.606 1.00 25.67 ? 91  ARG B NH1 1 
ATOM   2493 N NH2 . ARG B 1 91  ? -5.980  -27.788 -9.647  1.00 24.04 ? 91  ARG B NH2 1 
ATOM   2494 N N   . ALA B 1 92  ? -0.004  -21.680 -13.015 1.00 10.46 ? 92  ALA B N   1 
ATOM   2495 C CA  . ALA B 1 92  ? 0.921   -21.232 -14.065 1.00 10.39 ? 92  ALA B CA  1 
ATOM   2496 C C   . ALA B 1 92  ? 2.163   -20.605 -13.442 1.00 10.08 ? 92  ALA B C   1 
ATOM   2497 O O   . ALA B 1 92  ? 3.288   -20.867 -13.903 1.00 10.74 ? 92  ALA B O   1 
ATOM   2498 C CB  . ALA B 1 92  ? 0.233   -20.237 -14.971 1.00 10.91 ? 92  ALA B CB  1 
ATOM   2499 N N   . ALA B 1 93  ? 2.004   -19.771 -12.424 1.00 9.90  ? 93  ALA B N   1 
ATOM   2500 C CA  . ALA B 1 93  ? 3.145   -19.175 -11.749 1.00 9.60  ? 93  ALA B CA  1 
ATOM   2501 C C   . ALA B 1 93  ? 4.092   -20.259 -11.253 1.00 9.53  ? 93  ALA B C   1 
ATOM   2502 O O   . ALA B 1 93  ? 5.321   -20.144 -11.361 1.00 10.32 ? 93  ALA B O   1 
ATOM   2503 C CB  . ALA B 1 93  ? 2.698   -18.322 -10.594 1.00 10.60 ? 93  ALA B CB  1 
ATOM   2504 N N   . ILE B 1 94  ? 3.529   -21.300 -10.623 1.00 9.65  ? 94  ILE B N   1 
ATOM   2505 C CA  . ILE B 1 94  ? 4.324   -22.406 -10.142 1.00 10.17 ? 94  ILE B CA  1 
ATOM   2506 C C   . ILE B 1 94  ? 5.070   -23.044 -11.327 1.00 10.35 ? 94  ILE B C   1 
ATOM   2507 O O   . ILE B 1 94  ? 6.270   -23.321 -11.263 1.00 11.98 ? 94  ILE B O   1 
ATOM   2508 C CB  . ILE B 1 94  ? 3.459   -23.435 -9.424  1.00 10.91 ? 94  ILE B CB  1 
ATOM   2509 C CG1 . ILE B 1 94  ? 2.902   -22.839 -8.118  1.00 11.30 ? 94  ILE B CG1 1 
ATOM   2510 C CG2 . ILE B 1 94  ? 4.213   -24.722 -9.171  1.00 12.09 ? 94  ILE B CG2 1 
ATOM   2511 C CD1 . ILE B 1 94  ? 1.683   -23.559 -7.570  1.00 12.75 ? 94  ILE B CD1 1 
ATOM   2512 N N   . ALA B 1 95  ? 4.361   -23.309 -12.418 1.00 10.65 ? 95  ALA B N   1 
ATOM   2513 C CA  . ALA B 1 95  ? 4.934   -23.973 -13.592 1.00 11.11 ? 95  ALA B CA  1 
ATOM   2514 C C   . ALA B 1 95  ? 6.055   -23.149 -14.227 1.00 10.80 ? 95  ALA B C   1 
ATOM   2515 O O   . ALA B 1 95  ? 7.049   -23.713 -14.743 1.00 12.68 ? 95  ALA B O   1 
ATOM   2516 C CB  . ALA B 1 95  ? 3.862   -24.288 -14.575 1.00 11.52 ? 95  ALA B CB  1 
ATOM   2517 N N   . TYR B 1 96  ? 5.911   -21.834 -14.199 1.00 10.95 ? 96  TYR B N   1 
ATOM   2518 C CA  . TYR B 1 96  ? 6.965   -20.970 -14.719 1.00 11.07 ? 96  TYR B CA  1 
ATOM   2519 C C   . TYR B 1 96  ? 8.239   -21.063 -13.875 1.00 11.84 ? 96  TYR B C   1 
ATOM   2520 O O   . TYR B 1 96  ? 9.326   -20.741 -14.381 1.00 14.07 ? 96  TYR B O   1 
ATOM   2521 C CB  . TYR B 1 96  ? 6.596   -19.507 -14.732 1.00 11.25 ? 96  TYR B CB  1 
ATOM   2522 C CG  . TYR B 1 96  ? 5.757   -18.992 -15.878 1.00 10.92 ? 96  TYR B CG  1 
ATOM   2523 C CD1 . TYR B 1 96  ? 6.257   -18.949 -17.164 1.00 11.34 ? 96  TYR B CD1 1 
ATOM   2524 C CD2 . TYR B 1 96  ? 4.489   -18.470 -15.694 1.00 11.90 ? 96  TYR B CD2 1 
ATOM   2525 C CE1 . TYR B 1 96  ? 5.528   -18.448 -18.216 1.00 11.39 ? 96  TYR B CE1 1 
ATOM   2526 C CE2 . TYR B 1 96  ? 3.771   -17.912 -16.714 1.00 11.97 ? 96  TYR B CE2 1 
ATOM   2527 C CZ  . TYR B 1 96  ? 4.282   -17.904 -17.994 1.00 11.23 ? 96  TYR B CZ  1 
ATOM   2528 O OH  . TYR B 1 96  ? 3.552   -17.377 -19.023 1.00 13.02 ? 96  TYR B OH  1 
ATOM   2529 N N   . GLY B 1 97  ? 8.109   -21.450 -12.609 1.00 11.77 ? 97  GLY B N   1 
ATOM   2530 C CA  . GLY B 1 97  ? 9.224   -21.611 -11.688 1.00 11.75 ? 97  GLY B CA  1 
ATOM   2531 C C   . GLY B 1 97  ? 9.212   -20.698 -10.463 1.00 11.79 ? 97  GLY B C   1 
ATOM   2532 O O   . GLY B 1 97  ? 10.258  -20.525 -9.851  1.00 12.27 ? 97  GLY B O   1 
ATOM   2533 N N   . ALA B 1 98  ? 8.077   -20.107 -10.102 1.00 10.90 ? 98  ALA B N   1 
ATOM   2534 C CA  . ALA B 1 98  ? 8.083   -19.242 -8.940  1.00 10.57 ? 98  ALA B CA  1 
ATOM   2535 C C   . ALA B 1 98  ? 8.516   -19.983 -7.675  1.00 10.63 ? 98  ALA B C   1 
ATOM   2536 O O   . ALA B 1 98  ? 8.194   -21.142 -7.482  1.00 10.40 ? 98  ALA B O   1 
ATOM   2537 C CB  . ALA B 1 98  ? 6.661   -18.742 -8.646  1.00 11.41 ? 98  ALA B CB  1 
ATOM   2538 N N   . ASP B 1 99  ? 9.230   -19.258 -6.811  1.00 9.84  ? 99  ASP B N   1 
ATOM   2539 C CA  . ASP B 1 99  ? 9.479   -19.718 -5.455  1.00 9.95  ? 99  ASP B CA  1 
ATOM   2540 C C   . ASP B 1 99  ? 8.349   -19.341 -4.511  1.00 9.54  ? 99  ASP B C   1 
ATOM   2541 O O   . ASP B 1 99  ? 8.153   -20.039 -3.525  1.00 10.16 ? 99  ASP B O   1 
ATOM   2542 C CB  . ASP B 1 99  ? 10.784  -19.156 -4.917  1.00 10.28 ? 99  ASP B CB  1 
ATOM   2543 C CG  . ASP B 1 99  ? 12.019  -19.588 -5.703  1.00 11.35 ? 99  ASP B CG  1 
ATOM   2544 O OD1 . ASP B 1 99  ? 12.124  -20.795 -5.923  1.00 13.81 ? 99  ASP B OD1 1 
ATOM   2545 O OD2 . ASP B 1 99  ? 12.758  -18.683 -6.114  1.00 12.64 ? 99  ASP B OD2 1 
ATOM   2546 N N   . GLU B 1 100 ? 7.699   -18.235 -4.841  1.00 9.85  ? 100 GLU B N   1 
ATOM   2547 C CA  . GLU B 1 100 ? 6.649   -17.694 -3.979  1.00 9.65  ? 100 GLU B CA  1 
ATOM   2548 C C   . GLU B 1 100 ? 5.600   -17.052 -4.852  1.00 9.49  ? 100 GLU B C   1 
ATOM   2549 O O   . GLU B 1 100 ? 5.881   -16.441 -5.876  1.00 10.12 ? 100 GLU B O   1 
ATOM   2550 C CB  . GLU B 1 100 ? 7.215   -16.613 -3.061  1.00 10.47 ? 100 GLU B CB  1 
ATOM   2551 C CG  . GLU B 1 100 ? 8.423   -17.075 -2.263  1.00 11.70 ? 100 GLU B CG  1 
ATOM   2552 C CD  . GLU B 1 100 ? 8.992   -16.074 -1.290  1.00 12.84 ? 100 GLU B CD  1 
ATOM   2553 O OE1 . GLU B 1 100 ? 8.640   -14.880 -1.367  1.00 13.61 ? 100 GLU B OE1 1 
ATOM   2554 O OE2 . GLU B 1 100 ? 9.861   -16.512 -0.484  1.00 15.53 ? 100 GLU B OE2 1 
ATOM   2555 N N   . VAL B 1 101 ? 4.342   -17.176 -4.454  1.00 9.76  ? 101 VAL B N   1 
ATOM   2556 C CA  . VAL B 1 101 ? 3.220   -16.568 -5.129  1.00 9.56  ? 101 VAL B CA  1 
ATOM   2557 C C   . VAL B 1 101 ? 2.482   -15.677 -4.154  1.00 9.67  ? 101 VAL B C   1 
ATOM   2558 O O   . VAL B 1 101 ? 2.135   -16.163 -3.071  1.00 11.17 ? 101 VAL B O   1 
ATOM   2559 C CB  . VAL B 1 101 ? 2.263   -17.627 -5.684  1.00 9.84  ? 101 VAL B CB  1 
ATOM   2560 C CG1 . VAL B 1 101 ? 1.010   -16.989 -6.263  1.00 11.88 ? 101 VAL B CG1 1 
ATOM   2561 C CG2 . VAL B 1 101 ? 2.968   -18.485 -6.717  1.00 10.08 ? 101 VAL B CG2 1 
ATOM   2562 N N   . ASP B 1 102 ? 2.240   -14.433 -4.538  1.00 9.89  ? 102 ASP B N   1 
ATOM   2563 C CA  . ASP B 1 102 ? 1.468   -13.479 -3.748  1.00 10.07 ? 102 ASP B CA  1 
ATOM   2564 C C   . ASP B 1 102 ? 0.135   -13.348 -4.451  1.00 9.99  ? 102 ASP B C   1 
ATOM   2565 O O   . ASP B 1 102 ? 0.045   -12.724 -5.512  1.00 10.78 ? 102 ASP B O   1 
ATOM   2566 C CB  . ASP B 1 102 ? 2.185   -12.142 -3.682  1.00 10.34 ? 102 ASP B CB  1 
ATOM   2567 C CG  . ASP B 1 102 ? 3.583   -12.085 -3.061  1.00 11.52 ? 102 ASP B CG  1 
ATOM   2568 O OD1 . ASP B 1 102 ? 4.186   -13.153 -2.805  1.00 12.56 ? 102 ASP B OD1 1 
ATOM   2569 O OD2 . ASP B 1 102 ? 4.029   -10.956 -2.789  1.00 15.00 ? 102 ASP B OD2 1 
ATOM   2570 N N   . VAL B 1 103 ? -0.931  -13.936 -3.861  1.00 10.05 ? 103 VAL B N   1 
ATOM   2571 C CA  . VAL B 1 103 ? -2.265  -13.914 -4.417  1.00 10.00 ? 103 VAL B CA  1 
ATOM   2572 C C   . VAL B 1 103 ? -3.093  -12.827 -3.739  1.00 9.36  ? 103 VAL B C   1 
ATOM   2573 O O   . VAL B 1 103 ? -2.941  -12.625 -2.538  1.00 9.74  ? 103 VAL B O   1 
ATOM   2574 C CB  . VAL B 1 103 ? -2.935  -15.285 -4.308  1.00 10.32 ? 103 VAL B CB  1 
ATOM   2575 C CG1 . VAL B 1 103 ? -3.247  -15.667 -2.862  1.00 11.29 ? 103 VAL B CG1 1 
ATOM   2576 C CG2 . VAL B 1 103 ? -4.200  -15.335 -5.144  1.00 11.21 ? 103 VAL B CG2 1 
ATOM   2577 N N   . VAL B 1 104 ? -3.906  -12.135 -4.509  1.00 9.80  ? 104 VAL B N   1 
ATOM   2578 C CA  . VAL B 1 104 ? -4.829  -11.143 -3.928  1.00 9.35  ? 104 VAL B CA  1 
ATOM   2579 C C   . VAL B 1 104 ? -6.090  -11.831 -3.425  1.00 9.15  ? 104 VAL B C   1 
ATOM   2580 O O   . VAL B 1 104 ? -6.806  -12.491 -4.144  1.00 10.35 ? 104 VAL B O   1 
ATOM   2581 C CB  . VAL B 1 104 ? -5.157  -9.995  -4.885  1.00 9.36  ? 104 VAL B CB  1 
ATOM   2582 C CG1 . VAL B 1 104 ? -5.894  -8.890  -4.181  1.00 9.92  ? 104 VAL B CG1 1 
ATOM   2583 C CG2 . VAL B 1 104 ? -3.906  -9.429  -5.530  1.00 9.46  ? 104 VAL B CG2 1 
ATOM   2584 N N   . PHE B 1 105 ? -6.306  -11.616 -2.114  1.00 9.55  ? 105 PHE B N   1 
ATOM   2585 C CA  . PHE B 1 105 ? -7.549  -12.026 -1.461  1.00 9.62  ? 105 PHE B CA  1 
ATOM   2586 C C   . PHE B 1 105 ? -8.750  -11.347 -2.108  1.00 9.30  ? 105 PHE B C   1 
ATOM   2587 O O   . PHE B 1 105 ? -8.675  -10.182 -2.512  1.00 10.49 ? 105 PHE B O   1 
ATOM   2588 C CB  . PHE B 1 105 ? -7.419  -11.598 0.000   1.00 9.59  ? 105 PHE B CB  1 
ATOM   2589 C CG  . PHE B 1 105 ? -8.520  -12.115 0.906   1.00 10.04 ? 105 PHE B CG  1 
ATOM   2590 C CD1 . PHE B 1 105 ? -8.373  -13.315 1.556   1.00 10.62 ? 105 PHE B CD1 1 
ATOM   2591 C CD2 . PHE B 1 105 ? -9.678  -11.380 1.131   1.00 10.80 ? 105 PHE B CD2 1 
ATOM   2592 C CE1 . PHE B 1 105 ? -9.366  -13.793 2.383   1.00 11.81 ? 105 PHE B CE1 1 
ATOM   2593 C CE2 . PHE B 1 105 ? -10.631 -11.844 2.015   1.00 12.40 ? 105 PHE B CE2 1 
ATOM   2594 C CZ  . PHE B 1 105 ? -10.496 -13.056 2.571   1.00 11.49 ? 105 PHE B CZ  1 
ATOM   2595 N N   . PRO B 1 106 ? -9.903  -12.055 -2.166  1.00 10.27 ? 106 PRO B N   1 
ATOM   2596 C CA  . PRO B 1 106 ? -11.132 -11.424 -2.675  1.00 10.77 ? 106 PRO B CA  1 
ATOM   2597 C C   . PRO B 1 106 ? -11.724 -10.498 -1.618  1.00 10.77 ? 106 PRO B C   1 
ATOM   2598 O O   . PRO B 1 106 ? -12.735 -10.809 -0.986  1.00 11.92 ? 106 PRO B O   1 
ATOM   2599 C CB  . PRO B 1 106 ? -11.947 -12.606 -3.080  1.00 11.29 ? 106 PRO B CB  1 
ATOM   2600 C CG  . PRO B 1 106 ? -11.571 -13.692 -2.093  1.00 11.24 ? 106 PRO B CG  1 
ATOM   2601 C CD  . PRO B 1 106 ? -10.058 -13.492 -1.902  1.00 10.63 ? 106 PRO B CD  1 
ATOM   2602 N N   . TYR B 1 107 ? -11.113 -9.334  -1.486  1.00 10.28 ? 107 TYR B N   1 
ATOM   2603 C CA  . TYR B 1 107 ? -11.473 -8.399  -0.443  1.00 10.72 ? 107 TYR B CA  1 
ATOM   2604 C C   . TYR B 1 107 ? -12.836 -7.791  -0.719  1.00 11.03 ? 107 TYR B C   1 
ATOM   2605 O O   . TYR B 1 107 ? -13.556 -7.520  0.256   1.00 11.18 ? 107 TYR B O   1 
ATOM   2606 C CB  . TYR B 1 107 ? -10.376 -7.374  -0.191  1.00 11.51 ? 107 TYR B CB  1 
ATOM   2607 C CG  . TYR B 1 107 ? -10.038 -6.484  -1.373  1.00 11.32 ? 107 TYR B CG  1 
ATOM   2608 C CD1 . TYR B 1 107 ? -10.758 -5.329  -1.625  1.00 12.59 ? 107 TYR B CD1 1 
ATOM   2609 C CD2 . TYR B 1 107 ? -9.017  -6.815  -2.255  1.00 11.39 ? 107 TYR B CD2 1 
ATOM   2610 C CE1 . TYR B 1 107 ? -10.510 -4.510  -2.715  1.00 12.26 ? 107 TYR B CE1 1 
ATOM   2611 C CE2 . TYR B 1 107 ? -8.718  -5.990  -3.325  1.00 11.35 ? 107 TYR B CE2 1 
ATOM   2612 C CZ  . TYR B 1 107 ? -9.434  -4.823  -3.538  1.00 11.91 ? 107 TYR B CZ  1 
ATOM   2613 O OH  . TYR B 1 107 ? -9.159  -4.020  -4.598  1.00 14.39 ? 107 TYR B OH  1 
ATOM   2614 N N   . ARG B 1 108 ? -13.211 -7.520  -1.958  1.00 11.44 ? 108 ARG B N   1 
ATOM   2615 C CA  . ARG B 1 108 ? -14.542 -6.973  -2.194  1.00 11.19 ? 108 ARG B CA  1 
ATOM   2616 C C   . ARG B 1 108 ? -15.603 -7.980  -1.815  1.00 11.70 ? 108 ARG B C   1 
ATOM   2617 O O   . ARG B 1 108 ? -16.662 -7.575  -1.289  1.00 12.99 ? 108 ARG B O   1 
ATOM   2618 C CB  . ARG B 1 108 ? -14.714 -6.549  -3.651  1.00 12.04 ? 108 ARG B CB  1 
ATOM   2619 C CG  . ARG B 1 108 ? -13.989 -5.248  -3.963  1.00 13.85 ? 108 ARG B CG  1 
ATOM   2620 C CD  . ARG B 1 108 ? -14.239 -4.740  -5.372  1.00 16.95 ? 108 ARG B CD  1 
ATOM   2621 N NE  . ARG B 1 108 ? -13.931 -5.751  -6.332  1.00 20.28 ? 108 ARG B NE  1 
ATOM   2622 C CZ  . ARG B 1 108 ? -12.721 -6.075  -6.712  1.00 19.45 ? 108 ARG B CZ  1 
ATOM   2623 N NH1 . ARG B 1 108 ? -11.699 -5.312  -6.349  1.00 23.22 ? 108 ARG B NH1 1 
ATOM   2624 N NH2 . ARG B 1 108 ? -12.529 -7.148  -7.475  1.00 18.00 ? 108 ARG B NH2 1 
ATOM   2625 N N   . ALA B 1 109 ? -15.349 -9.265  -2.040  1.00 11.40 ? 109 ALA B N   1 
ATOM   2626 C CA  . ALA B 1 109 ? -16.333 -10.255 -1.640  1.00 10.94 ? 109 ALA B CA  1 
ATOM   2627 C C   . ALA B 1 109 ? -16.494 -10.254 -0.120  1.00 10.91 ? 109 ALA B C   1 
ATOM   2628 O O   . ALA B 1 109 ? -17.612 -10.389 0.394   1.00 12.12 ? 109 ALA B O   1 
ATOM   2629 C CB  . ALA B 1 109 ? -15.976 -11.613 -2.159  1.00 12.05 ? 109 ALA B CB  1 
ATOM   2630 N N   . LEU B 1 110 ? -15.403 -10.112 0.617   1.00 11.55 ? 110 LEU B N   1 
ATOM   2631 C CA  . LEU B 1 110 ? -15.469 -10.070 2.072   1.00 11.35 ? 110 LEU B CA  1 
ATOM   2632 C C   . LEU B 1 110 ? -16.258 -8.848  2.530   1.00 11.63 ? 110 LEU B C   1 
ATOM   2633 O O   . LEU B 1 110 ? -17.101 -8.925  3.469   1.00 13.79 ? 110 LEU B O   1 
ATOM   2634 C CB  . LEU B 1 110 ? -14.072 -10.012 2.681   1.00 11.28 ? 110 LEU B CB  1 
ATOM   2635 C CG  . LEU B 1 110 ? -14.050 -9.838  4.201   1.00 12.01 ? 110 LEU B CG  1 
ATOM   2636 C CD1 . LEU B 1 110 ? -14.726 -11.019 4.899   1.00 13.25 ? 110 LEU B CD1 1 
ATOM   2637 C CD2 . LEU B 1 110 ? -12.633 -9.717  4.703   1.00 12.83 ? 110 LEU B CD2 1 
ATOM   2638 N N   . MET B 1 111 ? -16.042 -7.717  1.870   1.00 11.80 ? 111 MET B N   1 
ATOM   2639 C CA  . MET B 1 111 ? -16.746 -6.490  2.205   1.00 12.75 ? 111 MET B CA  1 
ATOM   2640 C C   . MET B 1 111 ? -18.243 -6.647  1.926   1.00 12.92 ? 111 MET B C   1 
ATOM   2641 O O   . MET B 1 111 ? -19.073 -5.932  2.509   1.00 15.00 ? 111 MET B O   1 
ATOM   2642 C CB  . MET B 1 111 ? -16.144 -5.302  1.455   1.00 14.61 ? 111 MET B CB  1 
ATOM   2643 C CG  . MET B 1 111 ? -14.745 -4.981  1.935   1.00 18.04 ? 111 MET B CG  1 
ATOM   2644 S SD  . MET B 1 111 ? -13.801 -3.877  0.860   1.00 24.54 ? 111 MET B SD  1 
ATOM   2645 C CE  . MET B 1 111 ? -14.506 -2.486  1.743   1.00 23.81 ? 111 MET B CE  1 
ATOM   2646 N N   . ALA B 1 112 ? -18.591 -7.563  1.024   1.00 12.98 ? 112 ALA B N   1 
ATOM   2647 C CA  . ALA B 1 112 ? -19.970 -7.882  0.708   1.00 13.22 ? 112 ALA B CA  1 
ATOM   2648 C C   . ALA B 1 112 ? -20.495 -9.067  1.535   1.00 14.41 ? 112 ALA B C   1 
ATOM   2649 O O   . ALA B 1 112 ? -21.562 -9.596  1.236   1.00 16.35 ? 112 ALA B O   1 
ATOM   2650 C CB  . ALA B 1 112 ? -20.138 -8.149  -0.756  1.00 13.95 ? 112 ALA B CB  1 
ATOM   2651 N N   . GLY B 1 113 ? -19.770 -9.449  2.588   1.00 14.66 ? 113 GLY B N   1 
ATOM   2652 C CA  . GLY B 1 113 ? -20.207 -10.442 3.537   1.00 14.96 ? 113 GLY B CA  1 
ATOM   2653 C C   . GLY B 1 113 ? -19.930 -11.887 3.191   1.00 15.55 ? 113 GLY B C   1 
ATOM   2654 O O   . GLY B 1 113 ? -20.381 -12.785 3.897   1.00 19.17 ? 113 GLY B O   1 
ATOM   2655 N N   . ASN B 1 114 ? -19.117 -12.124 2.139   1.00 14.39 ? 114 ASN B N   1 
ATOM   2656 C CA  . ASN B 1 114 ? -18.803 -13.479 1.743   1.00 14.98 ? 114 ASN B CA  1 
ATOM   2657 C C   . ASN B 1 114 ? -17.397 -13.813 2.234   1.00 14.36 ? 114 ASN B C   1 
ATOM   2658 O O   . ASN B 1 114 ? -16.402 -13.506 1.571   1.00 15.72 ? 114 ASN B O   1 
ATOM   2659 C CB  . ASN B 1 114 ? -18.914 -13.615 0.239   1.00 15.25 ? 114 ASN B CB  1 
ATOM   2660 C CG  . ASN B 1 114 ? -18.753 -15.046 -0.213  1.00 16.08 ? 114 ASN B CG  1 
ATOM   2661 O OD1 . ASN B 1 114 ? -18.251 -15.901 0.525   1.00 15.75 ? 114 ASN B OD1 1 
ATOM   2662 N ND2 . ASN B 1 114 ? -19.165 -15.318 -1.440  1.00 19.88 ? 114 ASN B ND2 1 
ATOM   2663 N N   . GLU B 1 115 ? -17.333 -14.455 3.392   1.00 14.47 ? 115 GLU B N   1 
ATOM   2664 C CA  . GLU B 1 115 ? -16.090 -14.909 3.977   1.00 14.44 ? 115 GLU B CA  1 
ATOM   2665 C C   . GLU B 1 115 ? -15.654 -16.207 3.322   1.00 14.25 ? 115 GLU B C   1 
ATOM   2666 O O   . GLU B 1 115 ? -14.463 -16.480 3.230   1.00 15.15 ? 115 GLU B O   1 
ATOM   2667 C CB  . GLU B 1 115 ? -16.277 -15.145 5.478   1.00 16.05 ? 115 GLU B CB  1 
ATOM   2668 C CG  . GLU B 1 115 ? -16.628 -13.885 6.259   1.00 16.33 ? 115 GLU B CG  1 
ATOM   2669 C CD  . GLU B 1 115 ? -16.661 -14.110 7.758   1.00 19.30 ? 115 GLU B CD  1 
ATOM   2670 O OE1 . GLU B 1 115 ? -16.425 -15.245 8.201   1.00 24.03 ? 115 GLU B OE1 1 
ATOM   2671 O OE2 . GLU B 1 115 ? -16.941 -13.126 8.461   1.00 22.88 ? 115 GLU B OE2 1 
ATOM   2672 N N   . GLN B 1 116 ? -16.592 -17.028 2.889   1.00 13.76 ? 116 GLN B N   1 
ATOM   2673 C CA  . GLN B 1 116 ? -16.275 -18.375 2.454   1.00 14.67 ? 116 GLN B CA  1 
ATOM   2674 C C   . GLN B 1 116 ? -15.431 -18.362 1.175   1.00 13.64 ? 116 GLN B C   1 
ATOM   2675 O O   . GLN B 1 116 ? -14.514 -19.175 1.019   1.00 13.87 ? 116 GLN B O   1 
ATOM   2676 C CB  . GLN B 1 116 ? -17.546 -19.187 2.227   1.00 16.65 ? 116 GLN B CB  1 
ATOM   2677 C CG  . GLN B 1 116 ? -17.284 -20.663 1.984   1.00 19.81 ? 116 GLN B CG  1 
ATOM   2678 C CD  . GLN B 1 116 ? -16.646 -21.339 3.183   1.00 23.70 ? 116 GLN B CD  1 
ATOM   2679 O OE1 . GLN B 1 116 ? -17.065 -21.152 4.320   1.00 29.13 ? 116 GLN B OE1 1 
ATOM   2680 N NE2 . GLN B 1 116 ? -15.605 -22.121 2.980   1.00 26.39 ? 116 GLN B NE2 1 
ATOM   2681 N N   . VAL B 1 117 ? -15.728 -17.447 0.251   1.00 12.99 ? 117 VAL B N   1 
ATOM   2682 C CA  . VAL B 1 117 ? -14.992 -17.474 -1.005  1.00 12.54 ? 117 VAL B CA  1 
ATOM   2683 C C   . VAL B 1 117 ? -13.526 -17.119 -0.749  1.00 13.20 ? 117 VAL B C   1 
ATOM   2684 O O   . VAL B 1 117 ? -12.663 -17.678 -1.420  1.00 12.87 ? 117 VAL B O   1 
ATOM   2685 C CB  . VAL B 1 117 ? -15.605 -16.579 -2.094  1.00 12.86 ? 117 VAL B CB  1 
ATOM   2686 C CG1 . VAL B 1 117 ? -15.541 -15.108 -1.753  1.00 13.88 ? 117 VAL B CG1 1 
ATOM   2687 C CG2 . VAL B 1 117 ? -14.978 -16.875 -3.449  1.00 14.17 ? 117 VAL B CG2 1 
ATOM   2688 N N   . GLY B 1 118 ? -13.246 -16.211 0.196   1.00 12.06 ? 118 GLY B N   1 
ATOM   2689 C CA  . GLY B 1 118 ? -11.863 -15.900 0.531   1.00 11.89 ? 118 GLY B CA  1 
ATOM   2690 C C   . GLY B 1 118 ? -11.133 -17.129 1.066   1.00 11.59 ? 118 GLY B C   1 
ATOM   2691 O O   . GLY B 1 118 ? -9.999  -17.427 0.701   1.00 12.11 ? 118 GLY B O   1 
ATOM   2692 N N   . PHE B 1 119 ? -11.807 -17.860 1.952   1.00 11.44 ? 119 PHE B N   1 
ATOM   2693 C CA  . PHE B 1 119 ? -11.233 -19.077 2.494   1.00 11.72 ? 119 PHE B CA  1 
ATOM   2694 C C   . PHE B 1 119 ? -10.924 -20.049 1.354   1.00 11.54 ? 119 PHE B C   1 
ATOM   2695 O O   . PHE B 1 119 ? -9.840  -20.613 1.249   1.00 12.32 ? 119 PHE B O   1 
ATOM   2696 C CB  . PHE B 1 119 ? -12.202 -19.664 3.519   1.00 12.59 ? 119 PHE B CB  1 
ATOM   2697 C CG  . PHE B 1 119 ? -11.635 -20.931 4.117   1.00 13.16 ? 119 PHE B CG  1 
ATOM   2698 C CD1 . PHE B 1 119 ? -10.820 -20.888 5.238   1.00 14.02 ? 119 PHE B CD1 1 
ATOM   2699 C CD2 . PHE B 1 119 ? -11.861 -22.158 3.527   1.00 14.13 ? 119 PHE B CD2 1 
ATOM   2700 C CE1 . PHE B 1 119 ? -10.269 -22.037 5.758   1.00 15.11 ? 119 PHE B CE1 1 
ATOM   2701 C CE2 . PHE B 1 119 ? -11.305 -23.314 4.063   1.00 15.73 ? 119 PHE B CE2 1 
ATOM   2702 C CZ  . PHE B 1 119 ? -10.507 -23.239 5.178   1.00 15.48 ? 119 PHE B CZ  1 
ATOM   2703 N N   . ASP B 1 120 ? -11.920 -20.277 0.520   1.00 11.78 ? 120 ASP B N   1 
ATOM   2704 C CA  . ASP B 1 120 ? -11.820 -21.289 -0.509  1.00 11.58 ? 120 ASP B CA  1 
ATOM   2705 C C   . ASP B 1 120 ? -10.740 -20.906 -1.534  1.00 11.46 ? 120 ASP B C   1 
ATOM   2706 O O   . ASP B 1 120 ? -10.024 -21.785 -2.038  1.00 12.94 ? 120 ASP B O   1 
ATOM   2707 C CB  . ASP B 1 120 ? -13.170 -21.528 -1.151  1.00 13.18 ? 120 ASP B CB  1 
ATOM   2708 C CG  . ASP B 1 120 ? -14.224 -22.204 -0.280  1.00 16.07 ? 120 ASP B CG  1 
ATOM   2709 O OD1 . ASP B 1 120 ? -13.849 -22.789 0.733   1.00 19.45 ? 120 ASP B OD1 1 
ATOM   2710 O OD2 . ASP B 1 120 ? -15.388 -22.166 -0.657  1.00 20.04 ? 120 ASP B OD2 1 
ATOM   2711 N N   . LEU B 1 121 ? -10.651 -19.617 -1.867  1.00 11.87 ? 121 LEU B N   1 
ATOM   2712 C CA  . LEU B 1 121 ? -9.692  -19.181 -2.888  1.00 11.64 ? 121 LEU B CA  1 
ATOM   2713 C C   . LEU B 1 121 ? -8.300  -19.352 -2.327  1.00 11.49 ? 121 LEU B C   1 
ATOM   2714 O O   . LEU B 1 121 ? -7.415  -19.884 -3.013  1.00 12.48 ? 121 LEU B O   1 
ATOM   2715 C CB  . LEU B 1 121 ? -9.998  -17.738 -3.280  1.00 12.31 ? 121 LEU B CB  1 
ATOM   2716 C CG  . LEU B 1 121 ? -9.217  -17.186 -4.466  1.00 12.31 ? 121 LEU B CG  1 
ATOM   2717 C CD1 . LEU B 1 121 ? -10.046 -16.120 -5.200  1.00 13.53 ? 121 LEU B CD1 1 
ATOM   2718 C CD2 . LEU B 1 121 ? -7.863  -16.602 -4.092  1.00 12.75 ? 121 LEU B CD2 1 
ATOM   2719 N N   . VAL B 1 122 ? -8.041  -18.868 -1.114  1.00 11.03 ? 122 VAL B N   1 
ATOM   2720 C CA  . VAL B 1 122 ? -6.726  -19.011 -0.527  1.00 11.14 ? 122 VAL B CA  1 
ATOM   2721 C C   . VAL B 1 122 ? -6.392  -20.480 -0.389  1.00 10.97 ? 122 VAL B C   1 
ATOM   2722 O O   . VAL B 1 122 ? -5.254  -20.881 -0.698  1.00 11.28 ? 122 VAL B O   1 
ATOM   2723 C CB  . VAL B 1 122 ? -6.617  -18.272 0.814   1.00 10.43 ? 122 VAL B CB  1 
ATOM   2724 C CG1 . VAL B 1 122 ? -5.307  -18.610 1.514   1.00 10.79 ? 122 VAL B CG1 1 
ATOM   2725 C CG2 . VAL B 1 122 ? -6.755  -16.781 0.605   1.00 10.96 ? 122 VAL B CG2 1 
ATOM   2726 N N   . LYS B 1 123 ? -7.331  -21.295 0.093   1.00 10.94 ? 123 LYS B N   1 
ATOM   2727 C CA  . LYS B 1 123 ? -7.045  -22.699 0.302   1.00 12.00 ? 123 LYS B CA  1 
ATOM   2728 C C   . LYS B 1 123 ? -6.642  -23.373 -1.020  1.00 12.04 ? 123 LYS B C   1 
ATOM   2729 O O   . LYS B 1 123 ? -5.674  -24.148 -1.051  1.00 12.60 ? 123 LYS B O   1 
ATOM   2730 C CB  . LYS B 1 123 ? -8.232  -23.425 0.949   1.00 13.95 ? 123 LYS B CB  1 
ATOM   2731 C CG  . LYS B 1 123 ? -7.962  -24.868 1.267   1.00 16.90 ? 123 LYS B CG  1 
ATOM   2732 C CD  . LYS B 1 123 ? -9.010  -25.456 2.184   1.00 20.53 ? 123 LYS B CD  1 
ATOM   2733 C CE  . LYS B 1 123 ? -8.833  -26.908 2.445   1.00 27.98 ? 123 LYS B CE  1 
ATOM   2734 N NZ  . LYS B 1 123 ? -9.324  -27.615 1.266   1.00 33.19 ? 123 LYS B NZ  1 
ATOM   2735 N N   . ALA B 1 124 ? -7.392  -23.105 -2.096  1.00 11.67 ? 124 ALA B N   1 
ATOM   2736 C CA  . ALA B 1 124 ? -7.071  -23.725 -3.379  1.00 12.21 ? 124 ALA B CA  1 
ATOM   2737 C C   . ALA B 1 124 ? -5.644  -23.360 -3.814  1.00 11.59 ? 124 ALA B C   1 
ATOM   2738 O O   . ALA B 1 124 ? -4.866  -24.219 -4.238  1.00 11.82 ? 124 ALA B O   1 
ATOM   2739 C CB  . ALA B 1 124 ? -8.085  -23.331 -4.419  1.00 13.70 ? 124 ALA B CB  1 
ATOM   2740 N N   . CYS B 1 125 ? -5.302  -22.078 -3.708  1.00 10.45 ? 125 CYS B N   1 
ATOM   2741 C CA  . CYS B 1 125 ? -3.995  -21.600 -4.122  1.00 10.55 ? 125 CYS B CA  1 
ATOM   2742 C C   . CYS B 1 125 ? -2.911  -22.165 -3.214  1.00 10.59 ? 125 CYS B C   1 
ATOM   2743 O O   . CYS B 1 125 ? -1.835  -22.525 -3.688  1.00 11.24 ? 125 CYS B O   1 
ATOM   2744 C CB  . CYS B 1 125 ? -3.975  -20.093 -4.171  1.00 11.35 ? 125 CYS B CB  1 
ATOM   2745 S SG  . CYS B 1 125 ? -5.035  -19.399 -5.461  1.00 13.95 ? 125 CYS B SG  1 
ATOM   2746 N N   . LYS B 1 126 ? -3.171  -22.239 -1.899  1.00 10.61 ? 126 LYS B N   1 
ATOM   2747 C CA  . LYS B 1 126 ? -2.200  -22.802 -0.974  1.00 11.31 ? 126 LYS B CA  1 
ATOM   2748 C C   . LYS B 1 126 ? -1.951  -24.271 -1.294  1.00 11.77 ? 126 LYS B C   1 
ATOM   2749 O O   . LYS B 1 126 ? -0.809  -24.727 -1.272  1.00 12.82 ? 126 LYS B O   1 
ATOM   2750 C CB  . LYS B 1 126 ? -2.660  -22.672 0.476   1.00 12.37 ? 126 LYS B CB  1 
ATOM   2751 C CG  . LYS B 1 126 ? -1.788  -23.438 1.473   1.00 13.40 ? 126 LYS B CG  1 
ATOM   2752 C CD  . LYS B 1 126 ? -0.332  -23.011 1.503   1.00 14.96 ? 126 LYS B CD  1 
ATOM   2753 C CE  . LYS B 1 126 ? 0.474   -23.835 2.463   1.00 17.46 ? 126 LYS B CE  1 
ATOM   2754 N NZ  . LYS B 1 126 ? 0.335   -23.461 3.837   1.00 22.28 ? 126 LYS B NZ  1 
ATOM   2755 N N   . GLU B 1 127 ? -2.997  -25.042 -1.603  1.00 12.42 ? 127 GLU B N   1 
ATOM   2756 C CA  . GLU B 1 127 ? -2.783  -26.450 -1.907  1.00 14.22 ? 127 GLU B CA  1 
ATOM   2757 C C   . GLU B 1 127 ? -1.873  -26.619 -3.112  1.00 13.26 ? 127 GLU B C   1 
ATOM   2758 O O   . GLU B 1 127 ? -1.002  -27.497 -3.113  1.00 14.97 ? 127 GLU B O   1 
ATOM   2759 C CB  . GLU B 1 127 ? -4.106  -27.180 -2.039  1.00 17.04 ? 127 GLU B CB  1 
ATOM   2760 C CG  . GLU B 1 127 ? -4.711  -27.269 -0.635  1.00 21.03 ? 127 GLU B CG  1 
ATOM   2761 C CD  . GLU B 1 127 ? -6.092  -27.814 -0.475  1.00 26.70 ? 127 GLU B CD  1 
ATOM   2762 O OE1 . GLU B 1 127 ? -6.738  -28.016 -1.508  1.00 37.79 ? 127 GLU B OE1 1 
ATOM   2763 O OE2 . GLU B 1 127 ? -6.497  -28.043 0.686   1.00 32.22 ? 127 GLU B OE2 1 
ATOM   2764 N N   . ALA B 1 128 ? -2.109  -25.794 -4.138  1.00 12.38 ? 128 ALA B N   1 
ATOM   2765 C CA  . ALA B 1 128 ? -1.262  -25.855 -5.326  1.00 12.26 ? 128 ALA B CA  1 
ATOM   2766 C C   . ALA B 1 128 ? 0.187   -25.513 -4.971  1.00 11.65 ? 128 ALA B C   1 
ATOM   2767 O O   . ALA B 1 128 ? 1.147   -26.179 -5.385  1.00 13.09 ? 128 ALA B O   1 
ATOM   2768 C CB  . ALA B 1 128 ? -1.798  -24.913 -6.359  1.00 12.66 ? 128 ALA B CB  1 
ATOM   2769 N N   . CYS B 1 129 ? 0.367   -24.435 -4.220  1.00 11.15 ? 129 CYS B N   1 
ATOM   2770 C CA  . CYS B 1 129 ? 1.695   -24.008 -3.842  1.00 10.56 ? 129 CYS B CA  1 
ATOM   2771 C C   . CYS B 1 129 ? 2.401   -25.057 -2.987  1.00 11.53 ? 129 CYS B C   1 
ATOM   2772 O O   . CYS B 1 129 ? 3.574   -25.389 -3.186  1.00 12.84 ? 129 CYS B O   1 
ATOM   2773 C CB  . CYS B 1 129 ? 1.669   -22.674 -3.134  1.00 11.17 ? 129 CYS B CB  1 
ATOM   2774 S SG  . CYS B 1 129 ? 1.305   -21.291 -4.234  1.00 12.29 ? 129 CYS B SG  1 
ATOM   2775 N N   . ALA B 1 130 ? 1.686   -25.587 -1.991  1.00 12.18 ? 130 ALA B N   1 
ATOM   2776 C CA  . ALA B 1 130 ? 2.301   -26.525 -1.082  1.00 13.18 ? 130 ALA B CA  1 
ATOM   2777 C C   . ALA B 1 130 ? 2.793   -27.763 -1.805  1.00 14.34 ? 130 ALA B C   1 
ATOM   2778 O O   . ALA B 1 130 ? 3.844   -28.296 -1.455  1.00 15.32 ? 130 ALA B O   1 
ATOM   2779 C CB  . ALA B 1 130 ? 1.326   -26.881 0.009   1.00 14.61 ? 130 ALA B CB  1 
ATOM   2780 N N   . ALA B 1 131 ? 2.027   -28.209 -2.810  1.00 15.08 ? 131 ALA B N   1 
ATOM   2781 C CA  . ALA B 1 131 ? 2.406   -29.396 -3.561  1.00 15.98 ? 131 ALA B CA  1 
ATOM   2782 C C   . ALA B 1 131 ? 3.723   -29.186 -4.319  1.00 15.62 ? 131 ALA B C   1 
ATOM   2783 O O   . ALA B 1 131 ? 4.370   -30.160 -4.688  1.00 19.00 ? 131 ALA B O   1 
ATOM   2784 C CB  . ALA B 1 131 ? 1.303   -29.752 -4.511  1.00 18.93 ? 131 ALA B CB  1 
ATOM   2785 N N   . ALA B 1 132 ? 4.089   -27.928 -4.536  1.00 13.10 ? 132 ALA B N   1 
ATOM   2786 C CA  . ALA B 1 132 ? 5.298   -27.578 -5.266  1.00 14.51 ? 132 ALA B CA  1 
ATOM   2787 C C   . ALA B 1 132 ? 6.401   -26.990 -4.382  1.00 14.27 ? 132 ALA B C   1 
ATOM   2788 O O   . ALA B 1 132 ? 7.415   -26.504 -4.892  1.00 16.19 ? 132 ALA B O   1 
ATOM   2789 C CB  . ALA B 1 132 ? 4.938   -26.605 -6.381  1.00 16.13 ? 132 ALA B CB  1 
ATOM   2790 N N   . ASN B 1 133 ? 6.225   -27.025 -3.052  1.00 14.32 ? 133 ASN B N   1 
ATOM   2791 C CA  . ASN B 1 133 ? 7.160   -26.392 -2.119  1.00 14.39 ? 133 ASN B CA  1 
ATOM   2792 C C   . ASN B 1 133 ? 7.317   -24.891 -2.398  1.00 13.78 ? 133 ASN B C   1 
ATOM   2793 O O   . ASN B 1 133 ? 8.405   -24.330 -2.274  1.00 16.60 ? 133 ASN B O   1 
ATOM   2794 C CB  . ASN B 1 133 ? 8.510   -27.110 -2.119  1.00 17.91 ? 133 ASN B CB  1 
ATOM   2795 C CG  . ASN B 1 133 ? 8.404   -28.539 -1.642  1.00 24.36 ? 133 ASN B CG  1 
ATOM   2796 O OD1 . ASN B 1 133 ? 8.731   -29.472 -2.378  1.00 32.25 ? 133 ASN B OD1 1 
ATOM   2797 N ND2 . ASN B 1 133 ? 7.920   -28.752 -0.432  1.00 26.71 ? 133 ASN B ND2 1 
ATOM   2798 N N   . VAL B 1 134 ? 6.218   -24.241 -2.774  1.00 11.40 ? 134 VAL B N   1 
ATOM   2799 C CA  . VAL B 1 134 ? 6.160   -22.819 -3.044  1.00 10.71 ? 134 VAL B CA  1 
ATOM   2800 C C   . VAL B 1 134 ? 5.448   -22.132 -1.890  1.00 11.04 ? 134 VAL B C   1 
ATOM   2801 O O   . VAL B 1 134 ? 4.419   -22.638 -1.463  1.00 11.87 ? 134 VAL B O   1 
ATOM   2802 C CB  . VAL B 1 134 ? 5.454   -22.609 -4.412  1.00 10.83 ? 134 VAL B CB  1 
ATOM   2803 C CG1 . VAL B 1 134 ? 5.031   -21.175 -4.654  1.00 11.14 ? 134 VAL B CG1 1 
ATOM   2804 C CG2 . VAL B 1 134 ? 6.338   -23.123 -5.548  1.00 12.07 ? 134 VAL B CG2 1 
ATOM   2805 N N   . LEU B 1 135 ? 5.951   -20.973 -1.463  1.00 10.71 ? 135 LEU B N   1 
ATOM   2806 C CA  . LEU B 1 135 ? 5.292   -20.229 -0.404  1.00 11.87 ? 135 LEU B CA  1 
ATOM   2807 C C   . LEU B 1 135 ? 4.170   -19.376 -0.987  1.00 10.98 ? 135 LEU B C   1 
ATOM   2808 O O   . LEU B 1 135 ? 4.307   -18.807 -2.068  1.00 11.81 ? 135 LEU B O   1 
ATOM   2809 C CB  . LEU B 1 135 ? 6.308   -19.362 0.310   1.00 15.91 ? 135 LEU B CB  1 
ATOM   2810 C CG  . LEU B 1 135 ? 7.269   -20.059 1.267   1.00 19.99 ? 135 LEU B CG  1 
ATOM   2811 C CD1 . LEU B 1 135 ? 7.880   -18.919 2.028   1.00 23.75 ? 135 LEU B CD1 1 
ATOM   2812 C CD2 . LEU B 1 135 ? 6.677   -21.074 2.210   1.00 22.62 ? 135 LEU B CD2 1 
ATOM   2813 N N   . LEU B 1 136 ? 3.060   -19.281 -0.235  1.00 11.18 ? 136 LEU B N   1 
ATOM   2814 C CA  . LEU B 1 136 ? 1.933   -18.455 -0.621  1.00 10.75 ? 136 LEU B CA  1 
ATOM   2815 C C   . LEU B 1 136 ? 1.844   -17.247 0.298   1.00 9.68  ? 136 LEU B C   1 
ATOM   2816 O O   . LEU B 1 136 ? 1.646   -17.413 1.519   1.00 10.75 ? 136 LEU B O   1 
ATOM   2817 C CB  . LEU B 1 136 ? 0.619   -19.211 -0.571  1.00 11.13 ? 136 LEU B CB  1 
ATOM   2818 C CG  . LEU B 1 136 ? -0.590  -18.422 -1.082  1.00 11.61 ? 136 LEU B CG  1 
ATOM   2819 C CD1 . LEU B 1 136 ? -0.594  -18.258 -2.584  1.00 12.18 ? 136 LEU B CD1 1 
ATOM   2820 C CD2 . LEU B 1 136 ? -1.887  -19.057 -0.624  1.00 13.18 ? 136 LEU B CD2 1 
ATOM   2821 N N   . LYS B 1 137 ? 1.922   -16.046 -0.261  1.00 9.45  ? 137 LYS B N   1 
ATOM   2822 C CA  . LYS B 1 137 ? 1.565   -14.832 0.450   1.00 9.26  ? 137 LYS B CA  1 
ATOM   2823 C C   . LYS B 1 137 ? 0.170   -14.437 0.002   1.00 9.93  ? 137 LYS B C   1 
ATOM   2824 O O   . LYS B 1 137 ? -0.193  -14.593 -1.139  1.00 11.09 ? 137 LYS B O   1 
ATOM   2825 C CB  . LYS B 1 137 ? 2.505   -13.654 0.170   1.00 9.56  ? 137 LYS B CB  1 
ATOM   2826 C CG  . LYS B 1 137 ? 3.989   -14.040 0.230   1.00 9.89  ? 137 LYS B CG  1 
ATOM   2827 C CD  . LYS B 1 137 ? 4.882   -12.825 0.385   1.00 10.67 ? 137 LYS B CD  1 
ATOM   2828 C CE  . LYS B 1 137 ? 6.336   -13.016 0.078   1.00 11.60 ? 137 LYS B CE  1 
ATOM   2829 N NZ  . LYS B 1 137 ? 6.658   -13.007 -1.366  1.00 11.67 ? 137 LYS B NZ  1 
ATOM   2830 N N   . VAL B 1 138 ? -0.650  -13.890 0.924   1.00 9.16  ? 138 VAL B N   1 
ATOM   2831 C CA  . VAL B 1 138 ? -1.985  -13.419 0.615   1.00 9.01  ? 138 VAL B CA  1 
ATOM   2832 C C   . VAL B 1 138 ? -2.076  -11.927 0.851   1.00 9.03  ? 138 VAL B C   1 
ATOM   2833 O O   . VAL B 1 138 ? -1.853  -11.458 1.973   1.00 9.59  ? 138 VAL B O   1 
ATOM   2834 C CB  . VAL B 1 138 ? -3.037  -14.169 1.433   1.00 10.01 ? 138 VAL B CB  1 
ATOM   2835 C CG1 . VAL B 1 138 ? -4.398  -13.625 1.096   1.00 10.68 ? 138 VAL B CG1 1 
ATOM   2836 C CG2 . VAL B 1 138 ? -2.981  -15.650 1.156   1.00 10.40 ? 138 VAL B CG2 1 
ATOM   2837 N N   . ILE B 1 139 ? -2.374  -11.197 -0.231  1.00 9.49  ? 139 ILE B N   1 
ATOM   2838 C CA  . ILE B 1 139 ? -2.544  -9.755  -0.178  1.00 9.13  ? 139 ILE B CA  1 
ATOM   2839 C C   . ILE B 1 139 ? -3.986  -9.450  0.204   1.00 9.17  ? 139 ILE B C   1 
ATOM   2840 O O   . ILE B 1 139 ? -4.879  -9.749  -0.544  1.00 10.30 ? 139 ILE B O   1 
ATOM   2841 C CB  . ILE B 1 139 ? -2.212  -9.125  -1.549  1.00 9.34  ? 139 ILE B CB  1 
ATOM   2842 C CG1 . ILE B 1 139 ? -0.794  -9.434  -1.972  1.00 10.27 ? 139 ILE B CG1 1 
ATOM   2843 C CG2 . ILE B 1 139 ? -2.467  -7.629  -1.503  1.00 10.45 ? 139 ILE B CG2 1 
ATOM   2844 C CD1 . ILE B 1 139 ? -0.577  -9.239  -3.460  1.00 10.39 ? 139 ILE B CD1 1 
ATOM   2845 N N   . ILE B 1 140 ? -4.172  -8.791  1.349   1.00 9.90  ? 140 ILE B N   1 
ATOM   2846 C CA  . ILE B 1 140 ? -5.550  -8.540  1.778   1.00 10.11 ? 140 ILE B CA  1 
ATOM   2847 C C   . ILE B 1 140 ? -6.057  -7.161  1.364   1.00 9.94  ? 140 ILE B C   1 
ATOM   2848 O O   . ILE B 1 140 ? -7.253  -6.922  1.389   1.00 11.37 ? 140 ILE B O   1 
ATOM   2849 C CB  . ILE B 1 140 ? -5.715  -8.791  3.275   1.00 10.81 ? 140 ILE B CB  1 
ATOM   2850 C CG1 . ILE B 1 140 ? -4.912  -7.826  4.122   1.00 11.36 ? 140 ILE B CG1 1 
ATOM   2851 C CG2 . ILE B 1 140 ? -5.450  -10.267 3.583   1.00 11.78 ? 140 ILE B CG2 1 
ATOM   2852 C CD1 . ILE B 1 140 ? -5.360  -7.887  5.580   1.00 12.51 ? 140 ILE B CD1 1 
ATOM   2853 N N   . GLU B 1 141 ? -5.178  -6.236  0.955   1.00 10.29 ? 141 GLU B N   1 
ATOM   2854 C CA  . GLU B 1 141 ? -5.557  -4.921  0.479   1.00 10.38 ? 141 GLU B CA  1 
ATOM   2855 C C   . GLU B 1 141 ? -6.152  -4.090  1.607   1.00 10.09 ? 141 GLU B C   1 
ATOM   2856 O O   . GLU B 1 141 ? -7.294  -3.636  1.537   1.00 10.38 ? 141 GLU B O   1 
ATOM   2857 C CB  . GLU B 1 141 ? -6.399  -4.932  -0.798  1.00 10.87 ? 141 GLU B CB  1 
ATOM   2858 C CG  . GLU B 1 141 ? -6.251  -3.651  -1.621  1.00 11.30 ? 141 GLU B CG  1 
ATOM   2859 C CD  . GLU B 1 141 ? -4.916  -3.510  -2.339  1.00 10.71 ? 141 GLU B CD  1 
ATOM   2860 O OE1 . GLU B 1 141 ? -4.939  -3.665  -3.583  1.00 11.92 ? 141 GLU B OE1 1 
ATOM   2861 O OE2 . GLU B 1 141 ? -3.894  -3.283  -1.673  1.00 11.22 ? 141 GLU B OE2 1 
ATOM   2862 N N   . THR B 1 142 ? -5.333  -3.840  2.618   1.00 10.05 ? 142 THR B N   1 
ATOM   2863 C CA  . THR B 1 142 ? -5.763  -3.110  3.800   1.00 10.60 ? 142 THR B CA  1 
ATOM   2864 C C   . THR B 1 142 ? -6.321  -1.738  3.449   1.00 11.02 ? 142 THR B C   1 
ATOM   2865 O O   . THR B 1 142 ? -7.192  -1.210  4.155   1.00 11.90 ? 142 THR B O   1 
ATOM   2866 C CB  . THR B 1 142 ? -4.616  -2.966  4.789   1.00 11.90 ? 142 THR B CB  1 
ATOM   2867 O OG1 . THR B 1 142 ? -3.490  -2.376  4.150   1.00 12.21 ? 142 THR B OG1 1 
ATOM   2868 C CG2 . THR B 1 142 ? -4.208  -4.292  5.368   1.00 11.66 ? 142 THR B CG2 1 
ATOM   2869 N N   . GLY B 1 143 ? -5.767  -1.084  2.433   1.00 11.60 ? 143 GLY B N   1 
ATOM   2870 C CA  . GLY B 1 143 ? -6.194  0.251   2.077   1.00 12.06 ? 143 GLY B CA  1 
ATOM   2871 C C   . GLY B 1 143 ? -7.572  0.303   1.422   1.00 12.60 ? 143 GLY B C   1 
ATOM   2872 O O   . GLY B 1 143 ? -8.108  1.395   1.292   1.00 16.24 ? 143 GLY B O   1 
ATOM   2873 N N   . GLU B 1 144 ? -8.097  -0.849  0.974   1.00 11.25 ? 144 GLU B N   1 
ATOM   2874 C CA  . GLU B 1 144 ? -9.470  -0.918  0.498   1.00 12.67 ? 144 GLU B CA  1 
ATOM   2875 C C   . GLU B 1 144 ? -10.365 -1.423  1.613   1.00 12.88 ? 144 GLU B C   1 
ATOM   2876 O O   . GLU B 1 144 ? -11.508 -0.947  1.731   1.00 14.53 ? 144 GLU B O   1 
ATOM   2877 C CB  . GLU B 1 144 ? -9.580  -1.793  -0.747  1.00 12.94 ? 144 GLU B CB  1 
ATOM   2878 C CG  . GLU B 1 144 ? -8.875  -1.177  -1.951  1.00 13.69 ? 144 GLU B CG  1 
ATOM   2879 C CD  . GLU B 1 144 ? -9.491  0.138   -2.397  1.00 16.69 ? 144 GLU B CD  1 
ATOM   2880 O OE1 . GLU B 1 144 ? -10.746 0.212   -2.392  1.00 20.18 ? 144 GLU B OE1 1 
ATOM   2881 O OE2 . GLU B 1 144 ? -8.759  1.102   -2.707  1.00 19.48 ? 144 GLU B OE2 1 
ATOM   2882 N N   . LEU B 1 145 ? -9.898  -2.389  2.400   1.00 11.63 ? 145 LEU B N   1 
ATOM   2883 C CA  . LEU B 1 145 ? -10.721 -2.843  3.533   1.00 12.13 ? 145 LEU B CA  1 
ATOM   2884 C C   . LEU B 1 145 ? -10.991 -1.716  4.528   1.00 12.56 ? 145 LEU B C   1 
ATOM   2885 O O   . LEU B 1 145 ? -12.105 -1.601  5.040   1.00 14.46 ? 145 LEU B O   1 
ATOM   2886 C CB  . LEU B 1 145 ? -10.016 -3.999  4.231   1.00 12.21 ? 145 LEU B CB  1 
ATOM   2887 C CG  . LEU B 1 145 ? -9.923  -5.315  3.459   1.00 12.79 ? 145 LEU B CG  1 
ATOM   2888 C CD1 . LEU B 1 145 ? -9.010  -6.298  4.131   1.00 13.78 ? 145 LEU B CD1 1 
ATOM   2889 C CD2 . LEU B 1 145 ? -11.260 -5.934  3.188   1.00 13.64 ? 145 LEU B CD2 1 
ATOM   2890 N N   . LYS B 1 146 ? -9.937  -0.985  4.895   1.00 14.41 ? 146 LYS B N   1 
ATOM   2891 C CA  . LYS B 1 146 ? -9.958  0.213   5.731   1.00 16.15 ? 146 LYS B CA  1 
ATOM   2892 C C   . LYS B 1 146 ? -10.247 -0.059  7.210   1.00 17.27 ? 146 LYS B C   1 
ATOM   2893 O O   . LYS B 1 146 ? -9.484  0.337   8.083   1.00 18.60 ? 146 LYS B O   1 
ATOM   2894 C CB  . LYS B 1 146 ? -10.876 1.278   5.136   1.00 18.89 ? 146 LYS B CB  1 
ATOM   2895 C CG  . LYS B 1 146 ? -10.368 1.799   3.788   1.00 23.15 ? 146 LYS B CG  1 
ATOM   2896 C CD  . LYS B 1 146 ? -11.161 2.981   3.243   1.00 28.88 ? 146 LYS B CD  1 
ATOM   2897 C CE  . LYS B 1 146 ? -10.726 3.499   1.893   1.00 30.82 ? 146 LYS B CE  1 
ATOM   2898 N NZ  . LYS B 1 146 ? -9.316  3.920   1.836   1.00 35.25 ? 146 LYS B NZ  1 
ATOM   2899 N N   . ASP B 1 147 ? -11.339 -0.740  7.492   1.00 16.82 ? 147 ASP B N   1 
ATOM   2900 C CA  A ASP B 1 147 ? -11.811 -0.959  8.836   0.50 16.66 ? 147 ASP B CA  1 
ATOM   2901 C CA  B ASP B 1 147 ? -11.784 -0.932  8.867   0.50 16.63 ? 147 ASP B CA  1 
ATOM   2902 C C   . ASP B 1 147 ? -10.949 -2.013  9.535   1.00 15.80 ? 147 ASP B C   1 
ATOM   2903 O O   . ASP B 1 147 ? -10.673 -3.063  8.957   1.00 15.46 ? 147 ASP B O   1 
ATOM   2904 C CB  A ASP B 1 147 ? -13.242 -1.421  8.688   0.50 18.97 ? 147 ASP B CB  1 
ATOM   2905 C CB  B ASP B 1 147 ? -13.238 -1.357  8.952   0.50 18.95 ? 147 ASP B CB  1 
ATOM   2906 C CG  A ASP B 1 147 ? -13.815 -1.913  9.991   0.50 21.18 ? 147 ASP B CG  1 
ATOM   2907 C CG  B ASP B 1 147 ? -14.233 -0.311  8.492   0.50 21.52 ? 147 ASP B CG  1 
ATOM   2908 O OD1 A ASP B 1 147 ? -14.098 -1.053  10.828  0.50 25.61 ? 147 ASP B OD1 1 
ATOM   2909 O OD1 B ASP B 1 147 ? -13.874 0.882   8.467   0.50 25.42 ? 147 ASP B OD1 1 
ATOM   2910 O OD2 A ASP B 1 147 ? -13.896 -3.138  10.146  0.50 25.42 ? 147 ASP B OD2 1 
ATOM   2911 O OD2 B ASP B 1 147 ? -15.342 -0.718  8.152   0.50 26.60 ? 147 ASP B OD2 1 
ATOM   2912 N N   . GLU B 1 148 ? -10.588 -1.757  10.790  1.00 15.98 ? 148 GLU B N   1 
ATOM   2913 C CA  . GLU B 1 148 ? -9.801  -2.687  11.562  1.00 15.68 ? 148 GLU B CA  1 
ATOM   2914 C C   . GLU B 1 148 ? -10.429 -4.078  11.595  1.00 14.36 ? 148 GLU B C   1 
ATOM   2915 O O   . GLU B 1 148 ? -9.735  -5.080  11.435  1.00 14.99 ? 148 GLU B O   1 
ATOM   2916 C CB  . GLU B 1 148 ? -9.585  -2.134  12.968  1.00 17.65 ? 148 GLU B CB  1 
ATOM   2917 C CG  . GLU B 1 148 ? -8.876  -3.118  13.879  1.00 19.45 ? 148 GLU B CG  1 
ATOM   2918 C CD  . GLU B 1 148 ? -8.378  -2.544  15.178  1.00 23.78 ? 148 GLU B CD  1 
ATOM   2919 O OE1 . GLU B 1 148 ? -8.445  -1.319  15.404  1.00 28.54 ? 148 GLU B OE1 1 
ATOM   2920 O OE2 . GLU B 1 148 ? -7.840  -3.380  15.918  1.00 29.78 ? 148 GLU B OE2 1 
ATOM   2921 N N   . ALA B 1 149 ? -11.742 -4.146  11.859  1.00 15.63 ? 149 ALA B N   1 
ATOM   2922 C CA  . ALA B 1 149 ? -12.397 -5.445  11.948  1.00 15.40 ? 149 ALA B CA  1 
ATOM   2923 C C   . ALA B 1 149 ? -12.264 -6.234  10.639  1.00 13.88 ? 149 ALA B C   1 
ATOM   2924 O O   . ALA B 1 149 ? -12.123 -7.459  10.666  1.00 14.50 ? 149 ALA B O   1 
ATOM   2925 C CB  . ALA B 1 149 ? -13.863 -5.294  12.328  1.00 16.34 ? 149 ALA B CB  1 
ATOM   2926 N N   . LEU B 1 150 ? -12.376 -5.558  9.486   1.00 13.35 ? 150 LEU B N   1 
ATOM   2927 C CA  . LEU B 1 150 ? -12.242 -6.235  8.203   1.00 12.79 ? 150 LEU B CA  1 
ATOM   2928 C C   . LEU B 1 150 ? -10.808 -6.659  7.939   1.00 11.38 ? 150 LEU B C   1 
ATOM   2929 O O   . LEU B 1 150 ? -10.616 -7.728  7.407   1.00 11.83 ? 150 LEU B O   1 
ATOM   2930 C CB  . LEU B 1 150 ? -12.744 -5.353  7.069   1.00 14.34 ? 150 LEU B CB  1 
ATOM   2931 C CG  . LEU B 1 150 ? -14.265 -5.235  6.944   1.00 15.94 ? 150 LEU B CG  1 
ATOM   2932 C CD1 . LEU B 1 150 ? -14.638 -4.136  6.013   1.00 17.30 ? 150 LEU B CD1 1 
ATOM   2933 C CD2 . LEU B 1 150 ? -14.850 -6.524  6.422   1.00 20.00 ? 150 LEU B CD2 1 
ATOM   2934 N N   . ILE B 1 151 ? -9.832  -5.832  8.339   1.00 11.47 ? 151 ILE B N   1 
ATOM   2935 C CA  . ILE B 1 151 ? -8.435  -6.216  8.192   1.00 11.39 ? 151 ILE B CA  1 
ATOM   2936 C C   . ILE B 1 151 ? -8.161  -7.466  9.006   1.00 11.20 ? 151 ILE B C   1 
ATOM   2937 O O   . ILE B 1 151 ? -7.514  -8.397  8.558   1.00 11.85 ? 151 ILE B O   1 
ATOM   2938 C CB  . ILE B 1 151 ? -7.541  -5.043  8.557   1.00 11.69 ? 151 ILE B CB  1 
ATOM   2939 C CG1 . ILE B 1 151 ? -7.734  -3.949  7.515   1.00 12.25 ? 151 ILE B CG1 1 
ATOM   2940 C CG2 . ILE B 1 151 ? -6.091  -5.486  8.690   1.00 11.68 ? 151 ILE B CG2 1 
ATOM   2941 C CD1 . ILE B 1 151 ? -7.111  -2.635  7.881   1.00 14.03 ? 151 ILE B CD1 1 
ATOM   2942 N N   . ARG B 1 152 ? -8.675  -7.490  10.246  1.00 11.95 ? 152 ARG B N   1 
ATOM   2943 C CA  . ARG B 1 152 ? -8.466  -8.656  11.085  1.00 11.92 ? 152 ARG B CA  1 
ATOM   2944 C C   . ARG B 1 152 ? -9.131  -9.884  10.484  1.00 12.08 ? 152 ARG B C   1 
ATOM   2945 O O   . ARG B 1 152 ? -8.541  -10.967 10.466  1.00 13.88 ? 152 ARG B O   1 
ATOM   2946 C CB  . ARG B 1 152 ? -8.972  -8.435  12.509  1.00 12.75 ? 152 ARG B CB  1 
ATOM   2947 C CG  . ARG B 1 152 ? -8.145  -7.434  13.289  1.00 14.55 ? 152 ARG B CG  1 
ATOM   2948 C CD  . ARG B 1 152 ? -8.561  -7.395  14.753  1.00 17.17 ? 152 ARG B CD  1 
ATOM   2949 N NE  . ARG B 1 152 ? -7.901  -6.317  15.449  1.00 21.65 ? 152 ARG B NE  1 
ATOM   2950 C CZ  . ARG B 1 152 ? -6.654  -6.329  15.906  1.00 22.95 ? 152 ARG B CZ  1 
ATOM   2951 N NH1 . ARG B 1 152 ? -5.961  -7.451  15.958  1.00 29.05 ? 152 ARG B NH1 1 
ATOM   2952 N NH2 . ARG B 1 152 ? -6.121  -5.211  16.347  1.00 25.99 ? 152 ARG B NH2 1 
ATOM   2953 N N   . LYS B 1 153 ? -10.387 -9.721  10.023  1.00 12.18 ? 153 LYS B N   1 
ATOM   2954 C CA  . LYS B 1 153 ? -11.100 -10.856 9.466   1.00 12.18 ? 153 LYS B CA  1 
ATOM   2955 C C   . LYS B 1 153 ? -10.388 -11.424 8.220   1.00 11.15 ? 153 LYS B C   1 
ATOM   2956 O O   . LYS B 1 153 ? -10.262 -12.625 8.072   1.00 12.27 ? 153 LYS B O   1 
ATOM   2957 C CB  . LYS B 1 153 ? -12.533 -10.454 9.130   1.00 13.61 ? 153 LYS B CB  1 
ATOM   2958 C CG  . LYS B 1 153 ? -13.369 -11.601 8.644   1.00 15.89 ? 153 LYS B CG  1 
ATOM   2959 C CD  . LYS B 1 153 ? -13.449 -12.798 9.574   1.00 18.58 ? 153 LYS B CD  1 
ATOM   2960 C CE  . LYS B 1 153 ? -13.995 -12.445 10.928  1.00 21.09 ? 153 LYS B CE  1 
ATOM   2961 N NZ  . LYS B 1 153 ? -14.077 -13.601 11.827  1.00 24.82 ? 153 LYS B NZ  1 
ATOM   2962 N N   . ALA B 1 154 ? -9.957  -10.552 7.304   1.00 10.82 ? 154 ALA B N   1 
ATOM   2963 C CA  . ALA B 1 154 ? -9.267  -11.031 6.104   1.00 10.88 ? 154 ALA B CA  1 
ATOM   2964 C C   . ALA B 1 154 ? -7.963  -11.737 6.473   1.00 10.57 ? 154 ALA B C   1 
ATOM   2965 O O   . ALA B 1 154 ? -7.647  -12.776 5.897   1.00 11.14 ? 154 ALA B O   1 
ATOM   2966 C CB  . ALA B 1 154 ? -9.012  -9.885  5.168   1.00 10.93 ? 154 ALA B CB  1 
ATOM   2967 N N   . SER B 1 155 ? -7.290  -11.217 7.477   1.00 10.81 ? 155 SER B N   1 
ATOM   2968 C CA  . SER B 1 155 ? -6.046  -11.822 7.959   1.00 10.79 ? 155 SER B CA  1 
ATOM   2969 C C   . SER B 1 155 ? -6.316  -13.217 8.517   1.00 10.88 ? 155 SER B C   1 
ATOM   2970 O O   . SER B 1 155 ? -5.661  -14.200 8.216   1.00 11.25 ? 155 SER B O   1 
ATOM   2971 C CB  . SER B 1 155 ? -5.370  -10.950 8.964   1.00 10.93 ? 155 SER B CB  1 
ATOM   2972 O OG  . SER B 1 155 ? -5.013  -9.685  8.441   1.00 11.09 ? 155 SER B OG  1 
ATOM   2973 N N   . GLU B 1 156 ? -7.372  -13.286 9.341   1.00 11.42 ? 156 GLU B N   1 
ATOM   2974 C CA  . GLU B 1 156 ? -7.745  -14.530 9.994   1.00 12.26 ? 156 GLU B CA  1 
ATOM   2975 C C   . GLU B 1 156 ? -8.141  -15.598 8.973   1.00 11.72 ? 156 GLU B C   1 
ATOM   2976 O O   . GLU B 1 156 ? -7.733  -16.749 9.064   1.00 11.81 ? 156 GLU B O   1 
ATOM   2977 C CB  . GLU B 1 156 ? -8.929  -14.271 10.937  1.00 14.69 ? 156 GLU B CB  1 
ATOM   2978 C CG  . GLU B 1 156 ? -9.465  -15.521 11.611  1.00 18.59 ? 156 GLU B CG  1 
ATOM   2979 C CD  . GLU B 1 156 ? -10.772 -15.269 12.324  1.00 23.43 ? 156 GLU B CD  1 
ATOM   2980 O OE1 . GLU B 1 156 ? -11.505 -14.293 12.078  1.00 30.76 ? 156 GLU B OE1 1 
ATOM   2981 O OE2 . GLU B 1 156 ? -10.985 -16.085 13.215  1.00 34.33 ? 156 GLU B OE2 1 
ATOM   2982 N N   . ILE B 1 157 ? -9.023  -15.239 8.029   1.00 11.36 ? 157 ILE B N   1 
ATOM   2983 C CA  . ILE B 1 157 ? -9.457  -16.201 7.024   1.00 11.23 ? 157 ILE B CA  1 
ATOM   2984 C C   . ILE B 1 157 ? -8.252  -16.695 6.205   1.00 11.03 ? 157 ILE B C   1 
ATOM   2985 O O   . ILE B 1 157 ? -8.120  -17.884 5.965   1.00 11.73 ? 157 ILE B O   1 
ATOM   2986 C CB  . ILE B 1 157 ? -10.476 -15.542 6.085   1.00 11.90 ? 157 ILE B CB  1 
ATOM   2987 C CG1 . ILE B 1 157 ? -11.775 -15.199 6.849   1.00 12.47 ? 157 ILE B CG1 1 
ATOM   2988 C CG2 . ILE B 1 157 ? -10.766 -16.418 4.879   1.00 12.32 ? 157 ILE B CG2 1 
ATOM   2989 C CD1 . ILE B 1 157 ? -12.662 -14.247 6.075   1.00 13.20 ? 157 ILE B CD1 1 
ATOM   2990 N N   . SER B 1 158 ? -7.368  -15.765 5.840   1.00 11.04 ? 158 SER B N   1 
ATOM   2991 C CA  . SER B 1 158 ? -6.184  -16.139 5.067   1.00 10.90 ? 158 SER B CA  1 
ATOM   2992 C C   . SER B 1 158 ? -5.313  -17.148 5.805   1.00 10.91 ? 158 SER B C   1 
ATOM   2993 O O   . SER B 1 158 ? -4.850  -18.138 5.255   1.00 11.35 ? 158 SER B O   1 
ATOM   2994 C CB  . SER B 1 158 ? -5.401  -14.908 4.694   1.00 10.94 ? 158 SER B CB  1 
ATOM   2995 O OG  . SER B 1 158 ? -6.148  -14.053 3.852   1.00 11.59 ? 158 SER B OG  1 
ATOM   2996 N N   . ILE B 1 159 ? -5.094  -16.879 7.091   1.00 10.99 ? 159 ILE B N   1 
ATOM   2997 C CA  . ILE B 1 159 ? -4.337  -17.761 7.942   1.00 10.68 ? 159 ILE B CA  1 
ATOM   2998 C C   . ILE B 1 159 ? -4.981  -19.130 8.046   1.00 10.93 ? 159 ILE B C   1 
ATOM   2999 O O   . ILE B 1 159 ? -4.353  -20.154 7.928   1.00 11.84 ? 159 ILE B O   1 
ATOM   3000 C CB  . ILE B 1 159 ? -4.057  -17.100 9.289   1.00 11.61 ? 159 ILE B CB  1 
ATOM   3001 C CG1 . ILE B 1 159 ? -3.055  -15.949 9.111   1.00 12.65 ? 159 ILE B CG1 1 
ATOM   3002 C CG2 . ILE B 1 159 ? -3.539  -18.128 10.304  1.00 11.98 ? 159 ILE B CG2 1 
ATOM   3003 C CD1 . ILE B 1 159 ? -3.019  -14.992 10.293  1.00 14.05 ? 159 ILE B CD1 1 
ATOM   3004 N N   . LYS B 1 160 ? -6.271  -19.145 8.377   1.00 11.37 ? 160 LYS B N   1 
ATOM   3005 C CA  . LYS B 1 160 ? -6.982  -20.404 8.508   1.00 13.03 ? 160 LYS B CA  1 
ATOM   3006 C C   . LYS B 1 160 ? -6.926  -21.249 7.236   1.00 11.66 ? 160 LYS B C   1 
ATOM   3007 O O   . LYS B 1 160 ? -6.896  -22.474 7.299   1.00 14.13 ? 160 LYS B O   1 
ATOM   3008 C CB  . LYS B 1 160 ? -8.463  -20.171 8.851   1.00 14.27 ? 160 LYS B CB  1 
ATOM   3009 C CG  . LYS B 1 160 ? -8.669  -19.657 10.242  1.00 17.61 ? 160 LYS B CG  1 
ATOM   3010 C CD  . LYS B 1 160 ? -10.150 -19.486 10.561  1.00 21.95 ? 160 LYS B CD  1 
ATOM   3011 C CE  . LYS B 1 160 ? -10.325 -19.160 11.978  1.00 27.44 ? 160 LYS B CE  1 
ATOM   3012 N NZ  . LYS B 1 160 ? -11.742 -18.928 12.259  1.00 31.87 ? 160 LYS B NZ  1 
ATOM   3013 N N   . ALA B 1 161 ? -6.905  -20.581 6.082   1.00 11.98 ? 161 ALA B N   1 
ATOM   3014 C CA  . ALA B 1 161 ? -6.850  -21.264 4.784   1.00 12.56 ? 161 ALA B CA  1 
ATOM   3015 C C   . ALA B 1 161 ? -5.439  -21.710 4.410   1.00 12.88 ? 161 ALA B C   1 
ATOM   3016 O O   . ALA B 1 161 ? -5.278  -22.340 3.375   1.00 14.98 ? 161 ALA B O   1 
ATOM   3017 C CB  . ALA B 1 161 ? -7.396  -20.362 3.730   1.00 13.69 ? 161 ALA B CB  1 
ATOM   3018 N N   . GLY B 1 162 ? -4.426  -21.295 5.170   1.00 12.36 ? 162 GLY B N   1 
ATOM   3019 C CA  . GLY B 1 162 ? -3.079  -21.804 4.994   1.00 12.79 ? 162 GLY B CA  1 
ATOM   3020 C C   . GLY B 1 162 ? -2.065  -20.791 4.477   1.00 12.41 ? 162 GLY B C   1 
ATOM   3021 O O   . GLY B 1 162 ? -0.965  -21.220 4.107   1.00 14.22 ? 162 GLY B O   1 
ATOM   3022 N N   . ALA B 1 163 ? -2.371  -19.494 4.488   1.00 10.60 ? 163 ALA B N   1 
ATOM   3023 C CA  . ALA B 1 163 ? -1.399  -18.503 4.035   1.00 10.85 ? 163 ALA B CA  1 
ATOM   3024 C C   . ALA B 1 163 ? -0.088  -18.685 4.785   1.00 10.09 ? 163 ALA B C   1 
ATOM   3025 O O   . ALA B 1 163 ? -0.043  -18.851 5.999   1.00 10.97 ? 163 ALA B O   1 
ATOM   3026 C CB  . ALA B 1 163 ? -1.890  -17.113 4.290   1.00 11.70 ? 163 ALA B CB  1 
ATOM   3027 N N   . ASP B 1 164 ? 1.032   -18.594 4.055   1.00 10.34 ? 164 ASP B N   1 
ATOM   3028 C CA  . ASP B 1 164 ? 2.346   -18.599 4.666   1.00 10.48 ? 164 ASP B CA  1 
ATOM   3029 C C   . ASP B 1 164 ? 2.802   -17.198 5.055   1.00 10.34 ? 164 ASP B C   1 
ATOM   3030 O O   . ASP B 1 164 ? 3.707   -17.047 5.863   1.00 11.01 ? 164 ASP B O   1 
ATOM   3031 C CB  . ASP B 1 164 ? 3.341   -19.214 3.712   1.00 10.50 ? 164 ASP B CB  1 
ATOM   3032 C CG  . ASP B 1 164 ? 2.985   -20.638 3.299   1.00 12.41 ? 164 ASP B CG  1 
ATOM   3033 O OD1 . ASP B 1 164 ? 2.739   -21.473 4.203   1.00 14.85 ? 164 ASP B OD1 1 
ATOM   3034 O OD2 . ASP B 1 164 ? 3.015   -20.934 2.070   1.00 13.87 ? 164 ASP B OD2 1 
ATOM   3035 N N   . PHE B 1 165 ? 2.225   -16.192 4.414   1.00 10.28 ? 165 PHE B N   1 
ATOM   3036 C CA  . PHE B 1 165 ? 2.418   -14.785 4.727   1.00 9.77  ? 165 PHE B CA  1 
ATOM   3037 C C   . PHE B 1 165 ? 1.093   -14.075 4.525   1.00 9.63  ? 165 PHE B C   1 
ATOM   3038 O O   . PHE B 1 165 ? 0.352   -14.472 3.637   1.00 10.20 ? 165 PHE B O   1 
ATOM   3039 C CB  . PHE B 1 165 ? 3.357   -14.070 3.738   1.00 10.65 ? 165 PHE B CB  1 
ATOM   3040 C CG  . PHE B 1 165 ? 4.848   -14.045 4.045   1.00 11.38 ? 165 PHE B CG  1 
ATOM   3041 C CD1 . PHE B 1 165 ? 5.627   -15.160 3.853   1.00 13.28 ? 165 PHE B CD1 1 
ATOM   3042 C CD2 . PHE B 1 165 ? 5.419   -12.909 4.581   1.00 12.16 ? 165 PHE B CD2 1 
ATOM   3043 C CE1 . PHE B 1 165 ? 7.022   -15.086 4.065   1.00 14.79 ? 165 PHE B CE1 1 
ATOM   3044 C CE2 . PHE B 1 165 ? 6.765   -12.843 4.848   1.00 13.09 ? 165 PHE B CE2 1 
ATOM   3045 C CZ  . PHE B 1 165 ? 7.563   -13.933 4.575   1.00 13.80 ? 165 PHE B CZ  1 
ATOM   3046 N N   . ILE B 1 166 ? 0.861   -13.019 5.313   1.00 9.28  ? 166 ILE B N   1 
ATOM   3047 C CA  . ILE B 1 166 ? -0.171  -12.062 5.005   1.00 9.21  ? 166 ILE B CA  1 
ATOM   3048 C C   . ILE B 1 166 ? 0.509   -10.740 4.658   1.00 9.13  ? 166 ILE B C   1 
ATOM   3049 O O   . ILE B 1 166 ? 1.503   -10.354 5.272   1.00 10.20 ? 166 ILE B O   1 
ATOM   3050 C CB  . ILE B 1 166 ? -1.213  -11.956 6.140   1.00 10.40 ? 166 ILE B CB  1 
ATOM   3051 C CG1 . ILE B 1 166 ? -0.618  -11.650 7.498   1.00 10.38 ? 166 ILE B CG1 1 
ATOM   3052 C CG2 . ILE B 1 166 ? -1.989  -13.266 6.148   1.00 11.48 ? 166 ILE B CG2 1 
ATOM   3053 C CD1 . ILE B 1 166 ? -1.661  -11.412 8.601   1.00 11.48 ? 166 ILE B CD1 1 
ATOM   3054 N N   . LYS B 1 167 ? -0.009  -10.114 3.602   1.00 9.66  ? 167 LYS B N   1 
ATOM   3055 C CA  . LYS B 1 167 ? 0.636   -8.976  2.969   1.00 9.74  ? 167 LYS B CA  1 
ATOM   3056 C C   . LYS B 1 167 ? -0.358  -7.823  2.893   1.00 9.15  ? 167 LYS B C   1 
ATOM   3057 O O   . LYS B 1 167 ? -1.529  -8.035  2.550   1.00 9.72  ? 167 LYS B O   1 
ATOM   3058 C CB  . LYS B 1 167 ? 1.100   -9.433  1.584   1.00 10.17 ? 167 LYS B CB  1 
ATOM   3059 C CG  . LYS B 1 167 ? 1.617   -8.343  0.637   1.00 11.20 ? 167 LYS B CG  1 
ATOM   3060 C CD  . LYS B 1 167 ? 2.307   -8.932  -0.599  1.00 12.11 ? 167 LYS B CD  1 
ATOM   3061 C CE  . LYS B 1 167 ? 2.487   -7.898  -1.690  1.00 14.55 ? 167 LYS B CE  1 
ATOM   3062 N NZ  . LYS B 1 167 ? 3.434   -8.362  -2.710  1.00 17.48 ? 167 LYS B NZ  1 
ATOM   3063 N N   . THR B 1 168 ? 0.112   -6.604  3.138   1.00 9.25  ? 168 THR B N   1 
ATOM   3064 C CA  . THR B 1 168 ? -0.820  -5.504  3.274   1.00 9.91  ? 168 THR B CA  1 
ATOM   3065 C C   . THR B 1 168 ? -1.563  -5.200  1.983   1.00 9.55  ? 168 THR B C   1 
ATOM   3066 O O   . THR B 1 168 ? -2.761  -4.976  1.977   1.00 11.12 ? 168 THR B O   1 
ATOM   3067 C CB  . THR B 1 168 ? -0.147  -4.232  3.766   1.00 10.06 ? 168 THR B CB  1 
ATOM   3068 O OG1 . THR B 1 168 ? 0.851   -3.793  2.847   1.00 10.51 ? 168 THR B OG1 1 
ATOM   3069 C CG2 . THR B 1 168 ? 0.489   -4.427  5.128   1.00 10.63 ? 168 THR B CG2 1 
ATOM   3070 N N   . SER B 1 169 ? -0.818  -5.131  0.865   1.00 9.50  ? 169 SER B N   1 
ATOM   3071 C CA  . SER B 1 169 ? -1.268  -4.330  -0.254  1.00 9.82  ? 169 SER B CA  1 
ATOM   3072 C C   . SER B 1 169 ? -0.707  -4.801  -1.590  1.00 10.05 ? 169 SER B C   1 
ATOM   3073 O O   . SER B 1 169 ? 0.360   -5.423  -1.646  1.00 10.68 ? 169 SER B O   1 
ATOM   3074 C CB  . SER B 1 169 ? -0.875  -2.869  -0.048  1.00 10.78 ? 169 SER B CB  1 
ATOM   3075 O OG  . SER B 1 169 ? -1.116  -2.394  1.277   1.00 11.83 ? 169 SER B OG  1 
ATOM   3076 N N   . THR B 1 170 ? -1.388  -4.373  -2.647  1.00 10.05 ? 170 THR B N   1 
ATOM   3077 C CA  . THR B 1 170 ? -0.910  -4.614  -4.004  1.00 10.55 ? 170 THR B CA  1 
ATOM   3078 C C   . THR B 1 170 ? 0.104   -3.564  -4.439  1.00 12.10 ? 170 THR B C   1 
ATOM   3079 O O   . THR B 1 170 ? 0.847   -3.823  -5.385  1.00 14.43 ? 170 THR B O   1 
ATOM   3080 C CB  . THR B 1 170 ? -2.051  -4.617  -5.004  1.00 10.70 ? 170 THR B CB  1 
ATOM   3081 O OG1 . THR B 1 170 ? -2.695  -3.351  -4.976  1.00 11.39 ? 170 THR B OG1 1 
ATOM   3082 C CG2 . THR B 1 170 ? -2.984  -5.795  -4.838  1.00 11.07 ? 170 THR B CG2 1 
ATOM   3083 N N   . GLY B 1 171 ? 0.048   -2.371  -3.852  1.00 12.10 ? 171 GLY B N   1 
ATOM   3084 C CA  . GLY B 1 171 ? 0.779   -1.226  -4.366  1.00 13.61 ? 171 GLY B CA  1 
ATOM   3085 C C   . GLY B 1 171 ? 0.078   -0.565  -5.546  1.00 14.46 ? 171 GLY B C   1 
ATOM   3086 O O   . GLY B 1 171 ? 0.644   0.355   -6.123  1.00 19.19 ? 171 GLY B O   1 
ATOM   3087 N N   . ARG B 1 172 ? -1.156  -0.982  -5.874  1.00 13.71 ? 172 ARG B N   1 
ATOM   3088 C CA  . ARG B 1 172 ? -1.849  -0.488  -7.053  1.00 15.58 ? 172 ARG B CA  1 
ATOM   3089 C C   . ARG B 1 172 ? -3.083  0.335   -6.704  1.00 16.30 ? 172 ARG B C   1 
ATOM   3090 O O   . ARG B 1 172 ? -3.838  0.714   -7.580  1.00 20.78 ? 172 ARG B O   1 
ATOM   3091 C CB  . ARG B 1 172 ? -2.214  -1.666  -7.965  1.00 16.97 ? 172 ARG B CB  1 
ATOM   3092 C CG  . ARG B 1 172 ? -1.001  -2.435  -8.472  1.00 18.53 ? 172 ARG B CG  1 
ATOM   3093 C CD  . ARG B 1 172 ? -0.174  -1.615  -9.445  1.00 22.26 ? 172 ARG B CD  1 
ATOM   3094 N NE  . ARG B 1 172 ? -0.950  -1.488  -10.678 1.00 29.85 ? 172 ARG B NE  1 
ATOM   3095 C CZ  . ARG B 1 172 ? -1.121  -2.456  -11.596 1.00 31.79 ? 172 ARG B CZ  1 
ATOM   3096 N NH1 . ARG B 1 172 ? -0.242  -3.434  -11.715 1.00 33.22 ? 172 ARG B NH1 1 
ATOM   3097 N NH2 . ARG B 1 172 ? -2.163  -2.415  -12.411 1.00 34.49 ? 172 ARG B NH2 1 
ATOM   3098 N N   . VAL B 1 173 ? -3.342  0.527   -5.412  1.00 14.81 ? 173 VAL B N   1 
ATOM   3099 C CA  . VAL B 1 173 ? -4.444  1.368   -4.974  1.00 15.72 ? 173 VAL B CA  1 
ATOM   3100 C C   . VAL B 1 173 ? -3.879  2.583   -4.236  1.00 14.79 ? 173 VAL B C   1 
ATOM   3101 O O   . VAL B 1 173 ? -2.692  2.664   -3.967  1.00 16.14 ? 173 VAL B O   1 
ATOM   3102 C CB  . VAL B 1 173 ? -5.444  0.574   -4.105  1.00 15.94 ? 173 VAL B CB  1 
ATOM   3103 C CG1 . VAL B 1 173 ? -6.079  -0.551  -4.917  1.00 17.03 ? 173 VAL B CG1 1 
ATOM   3104 C CG2 . VAL B 1 173 ? -4.783  -0.004  -2.859  1.00 16.58 ? 173 VAL B CG2 1 
ATOM   3105 N N   . ALA B 1 174 ? -4.735  3.529   -3.878  1.00 16.78 ? 174 ALA B N   1 
ATOM   3106 C CA  . ALA B 1 174 ? -4.290  4.775   -3.293  1.00 17.92 ? 174 ALA B CA  1 
ATOM   3107 C C   . ALA B 1 174 ? -3.638  4.599   -1.918  1.00 15.93 ? 174 ALA B C   1 
ATOM   3108 O O   . ALA B 1 174 ? -2.684  5.299   -1.591  1.00 17.15 ? 174 ALA B O   1 
ATOM   3109 C CB  . ALA B 1 174 ? -5.468  5.708   -3.186  1.00 19.94 ? 174 ALA B CB  1 
ATOM   3110 N N   . VAL B 1 175 ? -4.170  3.690   -1.111  1.00 14.15 ? 175 VAL B N   1 
ATOM   3111 C CA  . VAL B 1 175 ? -3.699  3.494   0.245   1.00 12.72 ? 175 VAL B CA  1 
ATOM   3112 C C   . VAL B 1 175 ? -3.106  2.099   0.332   1.00 11.95 ? 175 VAL B C   1 
ATOM   3113 O O   . VAL B 1 175 ? -3.774  1.102   0.089   1.00 13.09 ? 175 VAL B O   1 
ATOM   3114 C CB  . VAL B 1 175 ? -4.837  3.659   1.267   1.00 12.93 ? 175 VAL B CB  1 
ATOM   3115 C CG1 . VAL B 1 175 ? -4.344  3.367   2.686   1.00 12.71 ? 175 VAL B CG1 1 
ATOM   3116 C CG2 . VAL B 1 175 ? -5.446  5.045   1.162   1.00 14.06 ? 175 VAL B CG2 1 
ATOM   3117 N N   . ASN B 1 176 ? -1.834  2.064   0.724   1.00 12.42 ? 176 ASN B N   1 
ATOM   3118 C CA  . ASN B 1 176 ? -1.091  0.823   0.866   1.00 12.54 ? 176 ASN B CA  1 
ATOM   3119 C C   . ASN B 1 176 ? -0.808  0.668   2.351   1.00 12.64 ? 176 ASN B C   1 
ATOM   3120 O O   . ASN B 1 176 ? -1.645  1.046   3.170   1.00 14.05 ? 176 ASN B O   1 
ATOM   3121 C CB  . ASN B 1 176 ? 0.090   0.814   -0.091  1.00 13.61 ? 176 ASN B CB  1 
ATOM   3122 C CG  . ASN B 1 176 ? -0.403  0.897   -1.520  1.00 15.21 ? 176 ASN B CG  1 
ATOM   3123 O OD1 . ASN B 1 176 ? -0.409  1.975   -2.122  1.00 22.38 ? 176 ASN B OD1 1 
ATOM   3124 N ND2 . ASN B 1 176 ? -0.967  -0.184  -2.007  1.00 14.32 ? 176 ASN B ND2 1 
ATOM   3125 N N   . ALA B 1 177 ? 0.345   0.135   2.738   1.00 11.68 ? 177 ALA B N   1 
ATOM   3126 C CA  . ALA B 1 177 ? 0.595   -0.128  4.143   1.00 11.63 ? 177 ALA B CA  1 
ATOM   3127 C C   . ALA B 1 177 ? 0.628   1.166   4.928   1.00 11.76 ? 177 ALA B C   1 
ATOM   3128 O O   . ALA B 1 177 ? 1.024   2.211   4.443   1.00 13.17 ? 177 ALA B O   1 
ATOM   3129 C CB  . ALA B 1 177 ? 1.918   -0.819  4.315   1.00 12.26 ? 177 ALA B CB  1 
ATOM   3130 N N   . THR B 1 178 ? 0.233   1.047   6.204   1.00 11.74 ? 178 THR B N   1 
ATOM   3131 C CA  . THR B 1 178 ? 0.453   2.050   7.224   1.00 12.20 ? 178 THR B CA  1 
ATOM   3132 C C   . THR B 1 178 ? 0.982   1.314   8.441   1.00 12.64 ? 178 THR B C   1 
ATOM   3133 O O   . THR B 1 178 ? 0.788   0.111   8.580   1.00 11.23 ? 178 THR B O   1 
ATOM   3134 C CB  . THR B 1 178 ? -0.825  2.811   7.588   1.00 14.02 ? 178 THR B CB  1 
ATOM   3135 O OG1 . THR B 1 178 ? -1.704  1.935   8.291   1.00 16.05 ? 178 THR B OG1 1 
ATOM   3136 C CG2 . THR B 1 178 ? -1.470  3.420   6.361   1.00 15.44 ? 178 THR B CG2 1 
ATOM   3137 N N   . PRO B 1 179 ? 1.615   2.030   9.394   1.00 14.39 ? 179 PRO B N   1 
ATOM   3138 C CA  . PRO B 1 179 ? 2.044   1.387   10.636  1.00 13.49 ? 179 PRO B CA  1 
ATOM   3139 C C   . PRO B 1 179 ? 0.869   0.762   11.377  1.00 13.17 ? 179 PRO B C   1 
ATOM   3140 O O   . PRO B 1 179 ? 1.029   -0.305  11.951  1.00 13.79 ? 179 PRO B O   1 
ATOM   3141 C CB  . PRO B 1 179 ? 2.697   2.519   11.393  1.00 15.18 ? 179 PRO B CB  1 
ATOM   3142 C CG  . PRO B 1 179 ? 3.222   3.393   10.269  1.00 16.72 ? 179 PRO B CG  1 
ATOM   3143 C CD  . PRO B 1 179 ? 2.076   3.424   9.276   1.00 15.33 ? 179 PRO B CD  1 
ATOM   3144 N N   . GLU B 1 180 ? -0.302  1.406   11.305  1.00 13.95 ? 180 GLU B N   1 
ATOM   3145 C CA  . GLU B 1 180 ? -1.470  0.872   11.989  1.00 15.01 ? 180 GLU B CA  1 
ATOM   3146 C C   . GLU B 1 180 ? -1.922  -0.448  11.358  1.00 13.02 ? 180 GLU B C   1 
ATOM   3147 O O   . GLU B 1 180 ? -2.221  -1.422  12.048  1.00 13.48 ? 180 GLU B O   1 
ATOM   3148 C CB  . GLU B 1 180 ? -2.595  1.916   11.997  1.00 18.76 ? 180 GLU B CB  1 
ATOM   3149 C CG  . GLU B 1 180 ? -3.851  1.472   12.718  1.00 25.08 ? 180 GLU B CG  1 
ATOM   3150 C CD  . GLU B 1 180 ? -4.921  2.543   12.868  1.00 31.92 ? 180 GLU B CD  1 
ATOM   3151 O OE1 . GLU B 1 180 ? -4.844  3.640   12.253  1.00 41.82 ? 180 GLU B OE1 1 
ATOM   3152 O OE2 . GLU B 1 180 ? -5.854  2.263   13.646  1.00 37.93 ? 180 GLU B OE2 1 
ATOM   3153 N N   . SER B 1 181 ? -2.026  -0.501  10.031  1.00 13.17 ? 181 SER B N   1 
ATOM   3154 C CA  A SER B 1 181 ? -2.479  -1.741  9.426   0.50 12.53 ? 181 SER B CA  1 
ATOM   3155 C CA  B SER B 1 181 ? -2.395  -1.714  9.314   0.50 14.10 ? 181 SER B CA  1 
ATOM   3156 C C   . SER B 1 181 ? -1.426  -2.843  9.615   1.00 12.01 ? 181 SER B C   1 
ATOM   3157 O O   . SER B 1 181 ? -1.785  -3.998  9.793   1.00 12.41 ? 181 SER B O   1 
ATOM   3158 C CB  A SER B 1 181 ? -2.938  -1.548  7.976   0.50 12.14 ? 181 SER B CB  1 
ATOM   3159 C CB  B SER B 1 181 ? -2.422  -1.478  7.821   0.50 15.77 ? 181 SER B CB  1 
ATOM   3160 O OG  A SER B 1 181 ? -1.887  -1.067  7.143   0.50 11.82 ? 181 SER B OG  1 
ATOM   3161 O OG  B SER B 1 181 ? -3.580  -0.738  7.489   0.50 17.98 ? 181 SER B OG  1 
ATOM   3162 N N   . ALA B 1 182 ? -0.127  -2.509  9.611   1.00 12.32 ? 182 ALA B N   1 
ATOM   3163 C CA  . ALA B 1 182 ? 0.887   -3.504  9.910   1.00 12.70 ? 182 ALA B CA  1 
ATOM   3164 C C   . ALA B 1 182 ? 0.721   -4.053  11.329  1.00 12.33 ? 182 ALA B C   1 
ATOM   3165 O O   . ALA B 1 182 ? 0.770   -5.264  11.543  1.00 12.12 ? 182 ALA B O   1 
ATOM   3166 C CB  . ALA B 1 182 ? 2.255   -2.889  9.717   1.00 12.74 ? 182 ALA B CB  1 
ATOM   3167 N N   . ARG B 1 183 ? 0.510   -3.157  12.296  1.00 11.61 ? 183 ARG B N   1 
ATOM   3168 C CA  . ARG B 1 183 ? 0.330   -3.589  13.665  1.00 12.92 ? 183 ARG B CA  1 
ATOM   3169 C C   . ARG B 1 183 ? -0.888  -4.509  13.757  1.00 11.49 ? 183 ARG B C   1 
ATOM   3170 O O   . ARG B 1 183 ? -0.827  -5.554  14.393  1.00 12.07 ? 183 ARG B O   1 
ATOM   3171 C CB  . ARG B 1 183 ? 0.165   -2.377  14.569  1.00 14.17 ? 183 ARG B CB  1 
ATOM   3172 C CG  . ARG B 1 183 ? -0.096  -2.780  16.006  1.00 16.63 ? 183 ARG B CG  1 
ATOM   3173 C CD  . ARG B 1 183 ? -0.537  -1.630  16.897  1.00 20.74 ? 183 ARG B CD  1 
ATOM   3174 N NE  . ARG B 1 183 ? -1.691  -0.849  16.420  1.00 25.05 ? 183 ARG B NE  1 
ATOM   3175 C CZ  . ARG B 1 183 ? -2.981  -1.175  16.557  1.00 27.20 ? 183 ARG B CZ  1 
ATOM   3176 N NH1 . ARG B 1 183 ? -3.342  -2.298  17.141  1.00 30.33 ? 183 ARG B NH1 1 
ATOM   3177 N NH2 . ARG B 1 183 ? -3.917  -0.357  16.110  1.00 33.54 ? 183 ARG B NH2 1 
ATOM   3178 N N   . ILE B 1 184 ? -2.016  -4.090  13.159  1.00 11.28 ? 184 ILE B N   1 
ATOM   3179 C CA  . ILE B 1 184 ? -3.202  -4.925  13.206  1.00 11.43 ? 184 ILE B CA  1 
ATOM   3180 C C   . ILE B 1 184 ? -2.956  -6.330  12.705  1.00 11.23 ? 184 ILE B C   1 
ATOM   3181 O O   . ILE B 1 184 ? -3.317  -7.334  13.302  1.00 12.21 ? 184 ILE B O   1 
ATOM   3182 C CB  . ILE B 1 184 ? -4.369  -4.236  12.487  1.00 12.25 ? 184 ILE B CB  1 
ATOM   3183 C CG1 . ILE B 1 184 ? -4.778  -2.966  13.215  1.00 13.73 ? 184 ILE B CG1 1 
ATOM   3184 C CG2 . ILE B 1 184 ? -5.537  -5.189  12.297  1.00 12.54 ? 184 ILE B CG2 1 
ATOM   3185 C CD1 . ILE B 1 184 ? -5.578  -2.010  12.349  1.00 14.58 ? 184 ILE B CD1 1 
ATOM   3186 N N   . MET B 1 185 ? -2.301  -6.413  11.533  1.00 10.38 ? 185 MET B N   1 
ATOM   3187 C CA  . MET B 1 185 ? -2.070  -7.708  10.916  1.00 10.48 ? 185 MET B CA  1 
ATOM   3188 C C   . MET B 1 185 ? -1.132  -8.580  11.743  1.00 10.81 ? 185 MET B C   1 
ATOM   3189 O O   . MET B 1 185 ? -1.354  -9.777  11.912  1.00 11.09 ? 185 MET B O   1 
ATOM   3190 C CB  . MET B 1 185 ? -1.518  -7.514  9.493   1.00 10.61 ? 185 MET B CB  1 
ATOM   3191 C CG  . MET B 1 185 ? -2.599  -6.994  8.572   1.00 10.31 ? 185 MET B CG  1 
ATOM   3192 S SD  . MET B 1 185 ? -2.052  -6.645  6.901   1.00 11.55 ? 185 MET B SD  1 
ATOM   3193 C CE  . MET B 1 185 ? -1.806  -8.315  6.294   1.00 12.46 ? 185 MET B CE  1 
ATOM   3194 N N   . MET B 1 186 ? -0.078  -7.974  12.286  1.00 11.42 ? 186 MET B N   1 
ATOM   3195 C CA  . MET B 1 186 ? 0.812   -8.740  13.143  1.00 11.59 ? 186 MET B CA  1 
ATOM   3196 C C   . MET B 1 186 ? 0.155   -9.138  14.463  1.00 11.47 ? 186 MET B C   1 
ATOM   3197 O O   . MET B 1 186 ? 0.421   -10.223 14.960  1.00 11.55 ? 186 MET B O   1 
ATOM   3198 C CB  . MET B 1 186 ? 2.120   -7.978  13.367  1.00 12.46 ? 186 MET B CB  1 
ATOM   3199 C CG  . MET B 1 186 ? 3.036   -8.038  12.156  1.00 13.77 ? 186 MET B CG  1 
ATOM   3200 S SD  . MET B 1 186 ? 4.641   -7.285  12.414  1.00 16.40 ? 186 MET B SD  1 
ATOM   3201 C CE  . MET B 1 186 ? 4.265   -5.614  11.881  1.00 17.71 ? 186 MET B CE  1 
ATOM   3202 N N   . GLU B 1 187 ? -0.760  -8.310  14.967  1.00 11.76 ? 187 GLU B N   1 
ATOM   3203 C CA  . GLU B 1 187 ? -1.543  -8.705  16.131  1.00 12.44 ? 187 GLU B CA  1 
ATOM   3204 C C   . GLU B 1 187 ? -2.388  -9.939  15.839  1.00 12.09 ? 187 GLU B C   1 
ATOM   3205 O O   . GLU B 1 187 ? -2.561  -10.782 16.703  1.00 12.43 ? 187 GLU B O   1 
ATOM   3206 C CB  . GLU B 1 187 ? -2.383  -7.543  16.634  1.00 13.62 ? 187 GLU B CB  1 
ATOM   3207 C CG  . GLU B 1 187 ? -1.583  -6.464  17.347  1.00 15.21 ? 187 GLU B CG  1 
ATOM   3208 C CD  . GLU B 1 187 ? -2.464  -5.294  17.787  1.00 19.26 ? 187 GLU B CD  1 
ATOM   3209 O OE1 . GLU B 1 187 ? -3.680  -5.290  17.479  1.00 26.46 ? 187 GLU B OE1 1 
ATOM   3210 O OE2 . GLU B 1 187 ? -1.940  -4.369  18.408  1.00 23.20 ? 187 GLU B OE2 1 
ATOM   3211 N N   . VAL B 1 188 ? -2.935  -10.044 14.636  1.00 12.21 ? 188 VAL B N   1 
ATOM   3212 C CA  . VAL B 1 188 ? -3.700  -11.228 14.284  1.00 11.60 ? 188 VAL B CA  1 
ATOM   3213 C C   . VAL B 1 188 ? -2.811  -12.466 14.333  1.00 11.18 ? 188 VAL B C   1 
ATOM   3214 O O   . VAL B 1 188 ? -3.204  -13.505 14.868  1.00 12.01 ? 188 VAL B O   1 
ATOM   3215 C CB  . VAL B 1 188 ? -4.421  -11.109 12.943  1.00 12.03 ? 188 VAL B CB  1 
ATOM   3216 C CG1 . VAL B 1 188 ? -5.113  -12.410 12.585  1.00 12.29 ? 188 VAL B CG1 1 
ATOM   3217 C CG2 . VAL B 1 188 ? -5.404  -9.971  12.955  1.00 12.24 ? 188 VAL B CG2 1 
ATOM   3218 N N   . ILE B 1 189 ? -1.600  -12.367 13.751  1.00 10.94 ? 189 ILE B N   1 
ATOM   3219 C CA  . ILE B 1 189 ? -0.684  -13.483 13.796  1.00 11.38 ? 189 ILE B CA  1 
ATOM   3220 C C   . ILE B 1 189 ? -0.438  -13.898 15.251  1.00 11.46 ? 189 ILE B C   1 
ATOM   3221 O O   . ILE B 1 189 ? -0.448  -15.082 15.583  1.00 12.65 ? 189 ILE B O   1 
ATOM   3222 C CB  . ILE B 1 189 ? 0.628   -13.089 13.072  1.00 11.37 ? 189 ILE B CB  1 
ATOM   3223 C CG1 . ILE B 1 189 ? 0.435   -12.899 11.558  1.00 11.55 ? 189 ILE B CG1 1 
ATOM   3224 C CG2 . ILE B 1 189 ? 1.755   -14.076 13.373  1.00 12.18 ? 189 ILE B CG2 1 
ATOM   3225 C CD1 . ILE B 1 189 ? 1.638   -12.363 10.786  1.00 11.83 ? 189 ILE B CD1 1 
ATOM   3226 N N   . ARG B 1 190 ? -0.166  -12.915 16.110  1.00 11.96 ? 190 ARG B N   1 
ATOM   3227 C CA  . ARG B 1 190 ? 0.097   -13.219 17.507  1.00 13.14 ? 190 ARG B CA  1 
ATOM   3228 C C   . ARG B 1 190 ? -1.130  -13.815 18.194  1.00 13.00 ? 190 ARG B C   1 
ATOM   3229 O O   . ARG B 1 190 ? -1.000  -14.808 18.899  1.00 14.16 ? 190 ARG B O   1 
ATOM   3230 C CB  . ARG B 1 190 ? 0.544   -11.922 18.186  1.00 16.28 ? 190 ARG B CB  1 
ATOM   3231 C CG  . ARG B 1 190 ? 1.058   -12.174 19.590  1.00 21.62 ? 190 ARG B CG  1 
ATOM   3232 C CD  . ARG B 1 190 ? 0.751   -11.093 20.594  1.00 27.63 ? 190 ARG B CD  1 
ATOM   3233 N NE  . ARG B 1 190 ? -0.564  -10.469 20.506  1.00 29.06 ? 190 ARG B NE  1 
ATOM   3234 C CZ  . ARG B 1 190 ? -0.786  -9.207  20.818  1.00 34.33 ? 190 ARG B CZ  1 
ATOM   3235 N NH1 . ARG B 1 190 ? 0.166   -8.511  21.419  1.00 38.71 ? 190 ARG B NH1 1 
ATOM   3236 N NH2 . ARG B 1 190 ? -1.955  -8.647  20.545  1.00 35.37 ? 190 ARG B NH2 1 
ATOM   3237 N N   . ASP B 1 191 ? -2.292  -13.208 17.971  1.00 12.65 ? 191 ASP B N   1 
ATOM   3238 C CA  . ASP B 1 191 ? -3.506  -13.635 18.661  1.00 13.75 ? 191 ASP B CA  1 
ATOM   3239 C C   . ASP B 1 191 ? -3.904  -15.049 18.237  1.00 12.91 ? 191 ASP B C   1 
ATOM   3240 O O   . ASP B 1 191 ? -4.464  -15.813 19.002  1.00 14.07 ? 191 ASP B O   1 
ATOM   3241 C CB  . ASP B 1 191 ? -4.626  -12.658 18.395  1.00 14.48 ? 191 ASP B CB  1 
ATOM   3242 C CG  . ASP B 1 191 ? -4.479  -11.299 19.067  1.00 17.04 ? 191 ASP B CG  1 
ATOM   3243 O OD1 . ASP B 1 191 ? -3.564  -11.146 19.923  1.00 20.22 ? 191 ASP B OD1 1 
ATOM   3244 O OD2 . ASP B 1 191 ? -5.236  -10.389 18.688  1.00 21.18 ? 191 ASP B OD2 1 
ATOM   3245 N N   . MET B 1 192 ? -3.660  -15.405 16.967  1.00 12.69 ? 192 MET B N   1 
ATOM   3246 C CA  . MET B 1 192 ? -3.954  -16.735 16.475  1.00 12.73 ? 192 MET B CA  1 
ATOM   3247 C C   . MET B 1 192 ? -2.903  -17.766 16.904  1.00 12.12 ? 192 MET B C   1 
ATOM   3248 O O   . MET B 1 192 ? -3.136  -18.967 16.838  1.00 13.99 ? 192 MET B O   1 
ATOM   3249 C CB  . MET B 1 192 ? -4.094  -16.716 14.955  1.00 12.78 ? 192 MET B CB  1 
ATOM   3250 C CG  . MET B 1 192 ? -5.315  -15.932 14.547  1.00 13.55 ? 192 MET B CG  1 
ATOM   3251 S SD  . MET B 1 192 ? -5.661  -15.994 12.804  1.00 17.67 ? 192 MET B SD  1 
ATOM   3252 C CE  . MET B 1 192 ? -6.323  -17.661 12.647  1.00 16.66 ? 192 MET B CE  1 
ATOM   3253 N N   . GLY B 1 193 ? -1.753  -17.281 17.346  1.00 11.97 ? 193 GLY B N   1 
ATOM   3254 C CA  . GLY B 1 193 ? -0.674  -18.160 17.793  1.00 13.00 ? 193 GLY B CA  1 
ATOM   3255 C C   . GLY B 1 193 ? 0.164   -18.749 16.666  1.00 13.28 ? 193 GLY B C   1 
ATOM   3256 O O   . GLY B 1 193 ? 0.738   -19.811 16.862  1.00 14.19 ? 193 GLY B O   1 
ATOM   3257 N N   . VAL B 1 194 ? 0.190   -18.097 15.496  1.00 12.55 ? 194 VAL B N   1 
ATOM   3258 C CA  . VAL B 1 194 ? 0.720   -18.708 14.292  1.00 13.50 ? 194 VAL B CA  1 
ATOM   3259 C C   . VAL B 1 194 ? 2.042   -18.087 13.872  1.00 13.16 ? 194 VAL B C   1 
ATOM   3260 O O   . VAL B 1 194 ? 2.446   -18.243 12.723  1.00 13.11 ? 194 VAL B O   1 
ATOM   3261 C CB  . VAL B 1 194 ? -0.283  -18.714 13.138  1.00 12.78 ? 194 VAL B CB  1 
ATOM   3262 C CG1 . VAL B 1 194 ? -1.467  -19.590 13.475  1.00 13.89 ? 194 VAL B CG1 1 
ATOM   3263 C CG2 . VAL B 1 194 ? -0.675  -17.310 12.699  1.00 12.53 ? 194 VAL B CG2 1 
ATOM   3264 N N   . GLU B 1 195 ? 2.711   -17.365 14.743  1.00 13.65 ? 195 GLU B N   1 
ATOM   3265 C CA  . GLU B 1 195 ? 3.931   -16.655 14.375  1.00 13.61 ? 195 GLU B CA  1 
ATOM   3266 C C   . GLU B 1 195 ? 5.025   -17.604 13.902  1.00 14.17 ? 195 GLU B C   1 
ATOM   3267 O O   . GLU B 1 195 ? 5.891   -17.156 13.191  1.00 15.27 ? 195 GLU B O   1 
ATOM   3268 C CB  . GLU B 1 195 ? 4.385   -15.762 15.525  1.00 17.47 ? 195 GLU B CB  1 
ATOM   3269 C CG  . GLU B 1 195 ? 4.861   -16.506 16.760  1.00 19.31 ? 195 GLU B CG  1 
ATOM   3270 C CD  . GLU B 1 195 ? 3.804   -16.949 17.740  1.00 23.03 ? 195 GLU B CD  1 
ATOM   3271 O OE1 . GLU B 1 195 ? 2.607   -16.730 17.509  1.00 22.19 ? 195 GLU B OE1 1 
ATOM   3272 O OE2 . GLU B 1 195 ? 4.241   -17.466 18.788  1.00 31.24 ? 195 GLU B OE2 1 
ATOM   3273 N N   . LYS B 1 196 ? 5.015   -18.879 14.244  1.00 13.80 ? 196 LYS B N   1 
ATOM   3274 C CA  . LYS B 1 196 ? 6.033   -19.783 13.729  1.00 16.19 ? 196 LYS B CA  1 
ATOM   3275 C C   . LYS B 1 196 ? 5.867   -20.010 12.227  1.00 16.80 ? 196 LYS B C   1 
ATOM   3276 O O   . LYS B 1 196 ? 6.861   -20.118 11.485  1.00 18.11 ? 196 LYS B O   1 
ATOM   3277 C CB  . LYS B 1 196 ? 5.979   -21.145 14.427  1.00 19.93 ? 196 LYS B CB  1 
ATOM   3278 C CG  . LYS B 1 196 ? 6.885   -22.254 13.912  1.00 25.79 ? 196 LYS B CG  1 
ATOM   3279 C CD  . LYS B 1 196 ? 6.626   -23.615 14.570  1.00 32.01 ? 196 LYS B CD  1 
ATOM   3280 C CE  . LYS B 1 196 ? 6.163   -23.479 15.994  1.00 37.47 ? 196 LYS B CE  1 
ATOM   3281 N NZ  . LYS B 1 196 ? 5.905   -24.732 16.711  1.00 39.58 ? 196 LYS B NZ  1 
ATOM   3282 N N   . SER B 1 197 ? 4.621   -20.000 11.748  1.00 13.66 ? 197 SER B N   1 
ATOM   3283 C CA  . SER B 1 197 ? 4.311   -20.461 10.400  1.00 14.73 ? 197 SER B CA  1 
ATOM   3284 C C   . SER B 1 197 ? 3.838   -19.345 9.459   1.00 13.59 ? 197 SER B C   1 
ATOM   3285 O O   . SER B 1 197 ? 3.690   -19.596 8.246   1.00 15.05 ? 197 SER B O   1 
ATOM   3286 C CB  . SER B 1 197 ? 3.275   -21.551 10.427  1.00 16.71 ? 197 SER B CB  1 
ATOM   3287 O OG  . SER B 1 197 ? 2.070   -21.095 11.018  1.00 19.38 ? 197 SER B OG  1 
ATOM   3288 N N   . VAL B 1 198 ? 3.561   -18.143 9.971   1.00 11.65 ? 198 VAL B N   1 
ATOM   3289 C CA  . VAL B 1 198 ? 3.002   -17.083 9.155   1.00 11.02 ? 198 VAL B CA  1 
ATOM   3290 C C   . VAL B 1 198 ? 3.861   -15.847 9.294   1.00 11.07 ? 198 VAL B C   1 
ATOM   3291 O O   . VAL B 1 198 ? 4.088   -15.332 10.388  1.00 12.55 ? 198 VAL B O   1 
ATOM   3292 C CB  . VAL B 1 198 ? 1.550   -16.772 9.558   1.00 11.87 ? 198 VAL B CB  1 
ATOM   3293 C CG1 . VAL B 1 198 ? 0.953   -15.686 8.668   1.00 12.04 ? 198 VAL B CG1 1 
ATOM   3294 C CG2 . VAL B 1 198 ? 0.727   -18.025 9.426   1.00 12.78 ? 198 VAL B CG2 1 
ATOM   3295 N N   . GLY B 1 199 ? 4.293   -15.342 8.136   1.00 10.30 ? 199 GLY B N   1 
ATOM   3296 C CA  . GLY B 1 199 ? 5.015   -14.096 8.051   1.00 10.39 ? 199 GLY B CA  1 
ATOM   3297 C C   . GLY B 1 199 ? 4.116   -12.929 7.676   1.00 9.58  ? 199 GLY B C   1 
ATOM   3298 O O   . GLY B 1 199 ? 2.935   -13.086 7.341   1.00 9.40  ? 199 GLY B O   1 
ATOM   3299 N N   . PHE B 1 200 ? 4.722   -11.746 7.711   1.00 9.52  ? 200 PHE B N   1 
ATOM   3300 C CA  . PHE B 1 200 ? 4.089   -10.477 7.412   1.00 9.63  ? 200 PHE B CA  1 
ATOM   3301 C C   . PHE B 1 200 ? 4.891   -9.737  6.343   1.00 9.84  ? 200 PHE B C   1 
ATOM   3302 O O   . PHE B 1 200 ? 6.105   -9.656  6.446   1.00 10.37 ? 200 PHE B O   1 
ATOM   3303 C CB  . PHE B 1 200 ? 3.989   -9.650  8.692   1.00 10.38 ? 200 PHE B CB  1 
ATOM   3304 C CG  . PHE B 1 200 ? 3.480   -8.261  8.418   1.00 10.70 ? 200 PHE B CG  1 
ATOM   3305 C CD1 . PHE B 1 200 ? 2.166   -8.045  8.011   1.00 11.90 ? 200 PHE B CD1 1 
ATOM   3306 C CD2 . PHE B 1 200 ? 4.336   -7.183  8.472   1.00 12.09 ? 200 PHE B CD2 1 
ATOM   3307 C CE1 . PHE B 1 200 ? 1.734   -6.765  7.673   1.00 11.99 ? 200 PHE B CE1 1 
ATOM   3308 C CE2 . PHE B 1 200 ? 3.918   -5.922  8.113   1.00 12.77 ? 200 PHE B CE2 1 
ATOM   3309 C CZ  . PHE B 1 200 ? 2.629   -5.704  7.708   1.00 12.86 ? 200 PHE B CZ  1 
ATOM   3310 N N   . LYS B 1 201 ? 4.196   -9.182  5.346   1.00 9.93  ? 201 LYS B N   1 
ATOM   3311 C CA  A LYS B 1 201 ? 4.838   -8.377  4.317   0.50 10.31 ? 201 LYS B CA  1 
ATOM   3312 C CA  B LYS B 1 201 ? 4.838   -8.372  4.323   0.50 10.33 ? 201 LYS B CA  1 
ATOM   3313 C C   . LYS B 1 201 ? 4.177   -7.011  4.192   1.00 10.24 ? 201 LYS B C   1 
ATOM   3314 O O   . LYS B 1 201 ? 2.964   -6.900  4.031   1.00 10.66 ? 201 LYS B O   1 
ATOM   3315 C CB  A LYS B 1 201 ? 4.885   -9.109  2.973   0.50 10.73 ? 201 LYS B CB  1 
ATOM   3316 C CB  B LYS B 1 201 ? 4.862   -9.067  2.963   0.50 10.77 ? 201 LYS B CB  1 
ATOM   3317 C CG  A LYS B 1 201 ? 5.464   -8.271  1.837   0.50 11.33 ? 201 LYS B CG  1 
ATOM   3318 C CG  B LYS B 1 201 ? 5.418   -8.228  1.823   0.50 11.84 ? 201 LYS B CG  1 
ATOM   3319 C CD  A LYS B 1 201 ? 5.795   -9.095  0.609   0.50 12.00 ? 201 LYS B CD  1 
ATOM   3320 C CD  B LYS B 1 201 ? 5.849   -9.108  0.665   0.50 12.69 ? 201 LYS B CD  1 
ATOM   3321 C CE  A LYS B 1 201 ? 6.114   -8.243  -0.594  0.50 12.87 ? 201 LYS B CE  1 
ATOM   3322 C CE  B LYS B 1 201 ? 6.708   -8.313  -0.273  0.50 14.04 ? 201 LYS B CE  1 
ATOM   3323 N NZ  A LYS B 1 201 ? 6.286   -9.018  -1.830  0.50 13.96 ? 201 LYS B NZ  1 
ATOM   3324 N NZ  B LYS B 1 201 ? 5.894   -7.305  -0.940  0.50 15.37 ? 201 LYS B NZ  1 
ATOM   3325 N N   . VAL B 1 202 ? 5.010   -5.988  4.254   1.00 10.78 ? 202 VAL B N   1 
ATOM   3326 C CA  A VAL B 1 202 ? 4.687   -4.590  4.069   0.50 11.81 ? 202 VAL B CA  1 
ATOM   3327 C CA  B VAL B 1 202 ? 4.558   -4.636  4.053   0.50 11.59 ? 202 VAL B CA  1 
ATOM   3328 C C   . VAL B 1 202 ? 4.847   -4.237  2.604   1.00 11.54 ? 202 VAL B C   1 
ATOM   3329 O O   . VAL B 1 202 ? 5.955   -4.359  2.104   1.00 13.67 ? 202 VAL B O   1 
ATOM   3330 C CB  A VAL B 1 202 ? 5.732   -3.734  4.810   0.50 13.23 ? 202 VAL B CB  1 
ATOM   3331 C CB  B VAL B 1 202 ? 5.205   -3.718  5.111   0.50 12.46 ? 202 VAL B CB  1 
ATOM   3332 C CG1 A VAL B 1 202 ? 5.577   -2.245  4.505   0.50 14.10 ? 202 VAL B CG1 1 
ATOM   3333 C CG1 B VAL B 1 202 ? 6.719   -3.818  5.130   0.50 13.17 ? 202 VAL B CG1 1 
ATOM   3334 C CG2 A VAL B 1 202 ? 5.772   -4.021  6.298   0.50 13.19 ? 202 VAL B CG2 1 
ATOM   3335 C CG2 B VAL B 1 202 ? 4.781   -2.261  4.963   0.50 13.19 ? 202 VAL B CG2 1 
ATOM   3336 N N   . THR B 1 203 ? 3.807   -3.752  1.958   1.00 11.51 ? 203 THR B N   1 
ATOM   3337 C CA  . THR B 1 203 ? 3.897   -3.235  0.603   1.00 12.37 ? 203 THR B CA  1 
ATOM   3338 C C   . THR B 1 203 ? 3.416   -1.798  0.626   1.00 12.41 ? 203 THR B C   1 
ATOM   3339 O O   . THR B 1 203 ? 2.283   -1.551  1.045   1.00 12.31 ? 203 THR B O   1 
ATOM   3340 C CB  . THR B 1 203 ? 3.126   -4.073  -0.390  1.00 15.55 ? 203 THR B CB  1 
ATOM   3341 O OG1 . THR B 1 203 ? 3.886   -5.274  -0.512  1.00 19.46 ? 203 THR B OG1 1 
ATOM   3342 C CG2 . THR B 1 203 ? 3.051   -3.383  -1.739  1.00 15.81 ? 203 THR B CG2 1 
ATOM   3343 N N   . GLY B 1 204 ? 4.268   -0.897  0.126   1.00 13.40 ? 204 GLY B N   1 
ATOM   3344 C CA  . GLY B 1 204 ? 3.999   0.521   0.117   1.00 15.06 ? 204 GLY B CA  1 
ATOM   3345 C C   . GLY B 1 204 ? 4.126   1.100   1.524   1.00 16.30 ? 204 GLY B C   1 
ATOM   3346 O O   . GLY B 1 204 ? 4.390   0.373   2.477   1.00 17.93 ? 204 GLY B O   1 
ATOM   3347 N N   . GLY B 1 205 ? 4.017   2.424   1.627   1.00 19.24 ? 205 GLY B N   1 
ATOM   3348 C CA  . GLY B 1 205 ? 4.061   3.104   2.906   1.00 20.22 ? 205 GLY B CA  1 
ATOM   3349 C C   . GLY B 1 205 ? 5.424   3.056   3.595   1.00 21.56 ? 205 GLY B C   1 
ATOM   3350 O O   . GLY B 1 205 ? 5.548   3.375   4.765   1.00 27.75 ? 205 GLY B O   1 
ATOM   3351 N N   . VAL B 1 206 ? 6.471   2.617   2.905   1.00 20.81 ? 206 VAL B N   1 
ATOM   3352 C CA  . VAL B 1 206 ? 7.765   2.504   3.545   1.00 20.43 ? 206 VAL B CA  1 
ATOM   3353 C C   . VAL B 1 206 ? 8.801   3.064   2.573   1.00 20.89 ? 206 VAL B C   1 
ATOM   3354 O O   . VAL B 1 206 ? 9.512   2.343   1.919   1.00 20.80 ? 206 VAL B O   1 
ATOM   3355 C CB  . VAL B 1 206 ? 8.046   1.048   3.961   1.00 21.79 ? 206 VAL B CB  1 
ATOM   3356 C CG1 . VAL B 1 206 ? 7.943   0.069   2.800   1.00 24.70 ? 206 VAL B CG1 1 
ATOM   3357 C CG2 . VAL B 1 206 ? 9.362   0.920   4.710   1.00 22.48 ? 206 VAL B CG2 1 
ATOM   3358 N N   . SER B 1 207 ? 8.903   4.382   2.556   1.00 23.22 ? 207 SER B N   1 
ATOM   3359 C CA  . SER B 1 207 ? 9.677   5.079   1.554   1.00 26.40 ? 207 SER B CA  1 
ATOM   3360 C C   . SER B 1 207 ? 11.123  5.188   1.995   1.00 24.05 ? 207 SER B C   1 
ATOM   3361 O O   . SER B 1 207 ? 11.989  5.288   1.137   1.00 27.70 ? 207 SER B O   1 
ATOM   3362 C CB  . SER B 1 207 ? 9.115   6.440   1.272   1.00 29.69 ? 207 SER B CB  1 
ATOM   3363 O OG  . SER B 1 207 ? 7.948   6.276   0.493   1.00 38.35 ? 207 SER B OG  1 
ATOM   3364 N N   . THR B 1 208 ? 11.353  5.269   3.305   1.00 22.56 ? 208 THR B N   1 
ATOM   3365 C CA  . THR B 1 208 ? 12.670  5.608   3.802   1.00 21.50 ? 208 THR B CA  1 
ATOM   3366 C C   . THR B 1 208 ? 13.179  4.546   4.763   1.00 20.45 ? 208 THR B C   1 
ATOM   3367 O O   . THR B 1 208 ? 12.442  3.755   5.331   1.00 19.46 ? 208 THR B O   1 
ATOM   3368 C CB  . THR B 1 208 ? 12.652  6.976   4.489   1.00 23.58 ? 208 THR B CB  1 
ATOM   3369 O OG1 . THR B 1 208 ? 11.912  6.780   5.696   1.00 24.04 ? 208 THR B OG1 1 
ATOM   3370 C CG2 . THR B 1 208 ? 12.064  8.062   3.602   1.00 26.83 ? 208 THR B CG2 1 
ATOM   3371 N N   . ALA B 1 209 ? 14.480  4.601   4.983   1.00 21.83 ? 209 ALA B N   1 
ATOM   3372 C CA  . ALA B 1 209 ? 15.151  3.795   5.993   1.00 21.67 ? 209 ALA B CA  1 
ATOM   3373 C C   . ALA B 1 209 ? 14.521  4.007   7.369   1.00 20.65 ? 209 ALA B C   1 
ATOM   3374 O O   . ALA B 1 209 ? 14.319  3.040   8.105   1.00 21.04 ? 209 ALA B O   1 
ATOM   3375 C CB  . ALA B 1 209 ? 16.619  4.160   5.983   1.00 22.72 ? 209 ALA B CB  1 
ATOM   3376 N N   . GLU B 1 210 ? 14.158  5.256   7.671   1.00 20.68 ? 210 GLU B N   1 
ATOM   3377 C CA  . GLU B 1 210 ? 13.509  5.558   8.939   1.00 19.89 ? 210 GLU B CA  1 
ATOM   3378 C C   . GLU B 1 210 ? 12.153  4.844   9.067   1.00 18.81 ? 210 GLU B C   1 
ATOM   3379 O O   . GLU B 1 210 ? 11.779  4.318   10.120  1.00 19.61 ? 210 GLU B O   1 
ATOM   3380 C CB  . GLU B 1 210 ? 13.359  7.068   9.121   1.00 22.27 ? 210 GLU B CB  1 
ATOM   3381 C CG  . GLU B 1 210 ? 14.684  7.808   9.289   1.00 26.37 ? 210 GLU B CG  1 
ATOM   3382 C CD  . GLU B 1 210 ? 15.430  8.176   8.019   1.00 28.91 ? 210 GLU B CD  1 
ATOM   3383 O OE1 . GLU B 1 210 ? 14.990  7.855   6.891   1.00 30.48 ? 210 GLU B OE1 1 
ATOM   3384 O OE2 . GLU B 1 210 ? 16.489  8.830   8.169   1.00 35.15 ? 210 GLU B OE2 1 
ATOM   3385 N N   . ASP B 1 211 ? 11.390  4.848   7.983   1.00 17.19 ? 211 ASP B N   1 
ATOM   3386 C CA  . ASP B 1 211 ? 10.138  4.128   7.955   1.00 16.30 ? 211 ASP B CA  1 
ATOM   3387 C C   . ASP B 1 211 ? 10.353  2.639   8.196   1.00 15.67 ? 211 ASP B C   1 
ATOM   3388 O O   . ASP B 1 211 ? 9.613   2.004   8.948   1.00 16.06 ? 211 ASP B O   1 
ATOM   3389 C CB  . ASP B 1 211 ? 9.425   4.324   6.632   1.00 17.45 ? 211 ASP B CB  1 
ATOM   3390 C CG  . ASP B 1 211 ? 8.975   5.733   6.301   1.00 19.29 ? 211 ASP B CG  1 
ATOM   3391 O OD1 . ASP B 1 211 ? 8.606   6.462   7.245   1.00 23.31 ? 211 ASP B OD1 1 
ATOM   3392 O OD2 . ASP B 1 211 ? 8.963   6.066   5.079   1.00 21.66 ? 211 ASP B OD2 1 
ATOM   3393 N N   . ALA B 1 212 ? 11.328  2.058   7.515   1.00 15.86 ? 212 ALA B N   1 
ATOM   3394 C CA  . ALA B 1 212 ? 11.560  0.627   7.632   1.00 14.94 ? 212 ALA B CA  1 
ATOM   3395 C C   . ALA B 1 212 ? 11.878  0.267   9.084   1.00 15.27 ? 212 ALA B C   1 
ATOM   3396 O O   . ALA B 1 212 ? 11.467  -0.786  9.569   1.00 16.03 ? 212 ALA B O   1 
ATOM   3397 C CB  . ALA B 1 212 ? 12.643  0.190   6.680   1.00 14.82 ? 212 ALA B CB  1 
ATOM   3398 N N   . GLN B 1 213 ? 12.662  1.122   9.746   1.00 16.14 ? 213 GLN B N   1 
ATOM   3399 C CA  . GLN B 1 213 ? 13.025  0.864   11.119  1.00 17.33 ? 213 GLN B CA  1 
ATOM   3400 C C   . GLN B 1 213 ? 11.753  0.800   11.972  1.00 16.82 ? 213 GLN B C   1 
ATOM   3401 O O   . GLN B 1 213 ? 11.674  -0.031  12.862  1.00 18.24 ? 213 GLN B O   1 
ATOM   3402 C CB  . GLN B 1 213 ? 14.005  1.939   11.529  1.00 19.72 ? 213 GLN B CB  1 
ATOM   3403 C CG  . GLN B 1 213 ? 14.435  1.838   12.977  1.00 21.41 ? 213 GLN B CG  1 
ATOM   3404 C CD  . GLN B 1 213 ? 15.421  2.947   13.261  1.00 26.06 ? 213 GLN B CD  1 
ATOM   3405 O OE1 . GLN B 1 213 ? 15.098  4.132   13.119  1.00 31.53 ? 213 GLN B OE1 1 
ATOM   3406 N NE2 . GLN B 1 213 ? 16.648  2.569   13.580  1.00 31.19 ? 213 GLN B NE2 1 
ATOM   3407 N N   . LYS B 1 214 ? 10.777  1.684   11.722  1.00 16.13 ? 214 LYS B N   1 
ATOM   3408 C CA  . LYS B 1 214 ? 9.555   1.705   12.512  1.00 17.29 ? 214 LYS B CA  1 
ATOM   3409 C C   . LYS B 1 214 ? 8.752   0.424   12.306  1.00 17.54 ? 214 LYS B C   1 
ATOM   3410 O O   . LYS B 1 214 ? 8.254   -0.176  13.261  1.00 17.51 ? 214 LYS B O   1 
ATOM   3411 C CB  . LYS B 1 214 ? 8.703   2.908   12.139  1.00 19.91 ? 214 LYS B CB  1 
ATOM   3412 C CG  . LYS B 1 214 ? 7.341   2.939   12.795  1.00 23.16 ? 214 LYS B CG  1 
ATOM   3413 C CD  . LYS B 1 214 ? 6.766   4.332   12.683  1.00 29.44 ? 214 LYS B CD  1 
ATOM   3414 C CE  . LYS B 1 214 ? 6.530   4.669   11.262  1.00 33.70 ? 214 LYS B CE  1 
ATOM   3415 N NZ  . LYS B 1 214 ? 6.047   6.035   11.098  1.00 39.12 ? 214 LYS B NZ  1 
ATOM   3416 N N   . TYR B 1 215 ? 8.656   -0.038  11.055  1.00 14.63 ? 215 TYR B N   1 
ATOM   3417 C CA  . TYR B 1 215 ? 7.910   -1.256  10.792  1.00 13.57 ? 215 TYR B CA  1 
ATOM   3418 C C   . TYR B 1 215 ? 8.564   -2.458  11.455  1.00 12.79 ? 215 TYR B C   1 
ATOM   3419 O O   . TYR B 1 215 ? 7.897   -3.365  11.941  1.00 14.10 ? 215 TYR B O   1 
ATOM   3420 C CB  . TYR B 1 215 ? 7.756   -1.465  9.286   1.00 14.30 ? 215 TYR B CB  1 
ATOM   3421 C CG  . TYR B 1 215 ? 6.658   -0.632  8.652   1.00 14.44 ? 215 TYR B CG  1 
ATOM   3422 C CD1 . TYR B 1 215 ? 5.352   -1.040  8.662   1.00 14.26 ? 215 TYR B CD1 1 
ATOM   3423 C CD2 . TYR B 1 215 ? 6.926   0.567   8.025   1.00 18.56 ? 215 TYR B CD2 1 
ATOM   3424 C CE1 . TYR B 1 215 ? 4.366   -0.316  8.045   1.00 13.42 ? 215 TYR B CE1 1 
ATOM   3425 C CE2 . TYR B 1 215 ? 5.937   1.304   7.401   1.00 18.45 ? 215 TYR B CE2 1 
ATOM   3426 C CZ  . TYR B 1 215 ? 4.637   0.876   7.437   1.00 16.01 ? 215 TYR B CZ  1 
ATOM   3427 O OH  . TYR B 1 215 ? 3.691   1.609   6.808   1.00 17.92 ? 215 TYR B OH  1 
ATOM   3428 N N   . LEU B 1 216 ? 9.894   -2.522  11.392  1.00 12.90 ? 216 LEU B N   1 
ATOM   3429 C CA  . LEU B 1 216 ? 10.605  -3.610  12.032  1.00 13.53 ? 216 LEU B CA  1 
ATOM   3430 C C   . LEU B 1 216 ? 10.415  -3.545  13.545  1.00 13.97 ? 216 LEU B C   1 
ATOM   3431 O O   . LEU B 1 216 ? 10.318  -4.579  14.175  1.00 16.11 ? 216 LEU B O   1 
ATOM   3432 C CB  . LEU B 1 216 ? 12.088  -3.604  11.662  1.00 14.58 ? 216 LEU B CB  1 
ATOM   3433 C CG  . LEU B 1 216 ? 12.362  -4.210  10.294  1.00 16.95 ? 216 LEU B CG  1 
ATOM   3434 C CD1 . LEU B 1 216 ? 13.767  -3.823  9.916   1.00 19.24 ? 216 LEU B CD1 1 
ATOM   3435 C CD2 . LEU B 1 216 ? 12.144  -5.711  10.339  1.00 17.75 ? 216 LEU B CD2 1 
ATOM   3436 N N   . ALA B 1 217 ? 10.368  -2.341  14.112  1.00 14.34 ? 217 ALA B N   1 
ATOM   3437 C CA  . ALA B 1 217 ? 10.182  -2.204  15.549  1.00 15.10 ? 217 ALA B CA  1 
ATOM   3438 C C   . ALA B 1 217 ? 8.861   -2.819  16.015  1.00 15.81 ? 217 ALA B C   1 
ATOM   3439 O O   . ALA B 1 217 ? 8.785   -3.372  17.119  1.00 16.49 ? 217 ALA B O   1 
ATOM   3440 C CB  . ALA B 1 217 ? 10.330  -0.766  15.965  1.00 15.91 ? 217 ALA B CB  1 
ATOM   3441 N N   . ILE B 1 218 ? 7.829   -2.711  15.189  1.00 14.79 ? 218 ILE B N   1 
ATOM   3442 C CA  . ILE B 1 218 ? 6.547   -3.291  15.542  1.00 15.35 ? 218 ILE B CA  1 
ATOM   3443 C C   . ILE B 1 218 ? 6.708   -4.797  15.722  1.00 15.84 ? 218 ILE B C   1 
ATOM   3444 O O   . ILE B 1 218 ? 6.242   -5.392  16.685  1.00 16.59 ? 218 ILE B O   1 
ATOM   3445 C CB  . ILE B 1 218 ? 5.448   -2.951  14.522  1.00 16.63 ? 218 ILE B CB  1 
ATOM   3446 C CG1 . ILE B 1 218 ? 5.202   -1.437  14.467  1.00 18.57 ? 218 ILE B CG1 1 
ATOM   3447 C CG2 . ILE B 1 218 ? 4.155   -3.703  14.844  1.00 17.62 ? 218 ILE B CG2 1 
ATOM   3448 C CD1 . ILE B 1 218 ? 4.421   -0.959  13.266  1.00 19.70 ? 218 ILE B CD1 1 
ATOM   3449 N N   . ALA B 1 219 ? 7.327   -5.442  14.754  1.00 14.69 ? 219 ALA B N   1 
ATOM   3450 C CA  . ALA B 1 219 ? 7.562   -6.880  14.813  1.00 14.91 ? 219 ALA B CA  1 
ATOM   3451 C C   . ALA B 1 219 ? 8.415   -7.249  16.026  1.00 15.96 ? 219 ALA B C   1 
ATOM   3452 O O   . ALA B 1 219 ? 8.130   -8.228  16.689  1.00 16.21 ? 219 ALA B O   1 
ATOM   3453 C CB  . ALA B 1 219 ? 8.240   -7.337  13.541  1.00 15.44 ? 219 ALA B CB  1 
ATOM   3454 N N   . ASP B 1 220 ? 9.511   -6.500  16.238  1.00 15.58 ? 220 ASP B N   1 
ATOM   3455 C CA  . ASP B 1 220 ? 10.396  -6.782  17.352  1.00 16.19 ? 220 ASP B CA  1 
ATOM   3456 C C   . ASP B 1 220 ? 9.646   -6.700  18.688  1.00 16.95 ? 220 ASP B C   1 
ATOM   3457 O O   . ASP B 1 220 ? 9.833   -7.550  19.564  1.00 19.00 ? 220 ASP B O   1 
ATOM   3458 C CB  . ASP B 1 220 ? 11.611  -5.872  17.351  1.00 16.76 ? 220 ASP B CB  1 
ATOM   3459 C CG  . ASP B 1 220 ? 12.588  -6.045  16.184  1.00 18.67 ? 220 ASP B CG  1 
ATOM   3460 O OD1 . ASP B 1 220 ? 12.444  -7.026  15.417  1.00 19.68 ? 220 ASP B OD1 1 
ATOM   3461 O OD2 . ASP B 1 220 ? 13.469  -5.175  16.029  1.00 23.01 ? 220 ASP B OD2 1 
ATOM   3462 N N   . GLU B 1 221 ? 8.758   -5.704  18.814  1.00 16.52 ? 221 GLU B N   1 
ATOM   3463 C CA  . GLU B 1 221 ? 7.971   -5.557  20.036  1.00 17.27 ? 221 GLU B CA  1 
ATOM   3464 C C   . GLU B 1 221 ? 6.981   -6.709  20.241  1.00 17.08 ? 221 GLU B C   1 
ATOM   3465 O O   . GLU B 1 221 ? 6.775   -7.160  21.375  1.00 20.69 ? 221 GLU B O   1 
ATOM   3466 C CB  . GLU B 1 221 ? 7.278   -4.199  20.002  1.00 19.38 ? 221 GLU B CB  1 
ATOM   3467 C CG  . GLU B 1 221 ? 8.256   -3.033  20.095  1.00 25.32 ? 221 GLU B CG  1 
ATOM   3468 C CD  . GLU B 1 221 ? 7.751   -1.651  19.714  1.00 32.99 ? 221 GLU B CD  1 
ATOM   3469 O OE1 . GLU B 1 221 ? 6.574   -1.510  19.321  1.00 40.43 ? 221 GLU B OE1 1 
ATOM   3470 O OE2 . GLU B 1 221 ? 8.599   -0.724  19.725  1.00 40.78 ? 221 GLU B OE2 1 
ATOM   3471 N N   . LEU B 1 222 ? 6.346   -7.165  19.159  1.00 15.79 ? 222 LEU B N   1 
ATOM   3472 C CA  . LEU B 1 222 ? 5.334   -8.200  19.289  1.00 16.64 ? 222 LEU B CA  1 
ATOM   3473 C C   . LEU B 1 222 ? 5.942   -9.582  19.473  1.00 16.66 ? 222 LEU B C   1 
ATOM   3474 O O   . LEU B 1 222 ? 5.399   -10.405 20.195  1.00 20.04 ? 222 LEU B O   1 
ATOM   3475 C CB  . LEU B 1 222 ? 4.418   -8.173  18.075  1.00 16.23 ? 222 LEU B CB  1 
ATOM   3476 C CG  . LEU B 1 222 ? 3.425   -7.014  18.006  1.00 17.36 ? 222 LEU B CG  1 
ATOM   3477 C CD1 . LEU B 1 222 ? 2.756   -6.959  16.659  1.00 18.05 ? 222 LEU B CD1 1 
ATOM   3478 C CD2 . LEU B 1 222 ? 2.373   -7.112  19.110  1.00 19.34 ? 222 LEU B CD2 1 
ATOM   3479 N N   . PHE B 1 223 ? 7.048   -9.878  18.768  1.00 15.65 ? 223 PHE B N   1 
ATOM   3480 C CA  . PHE B 1 223 ? 7.505   -11.251 18.654  1.00 16.70 ? 223 PHE B CA  1 
ATOM   3481 C C   . PHE B 1 223 ? 8.934   -11.475 19.127  1.00 19.24 ? 223 PHE B C   1 
ATOM   3482 O O   . PHE B 1 223 ? 9.419   -12.617 19.113  1.00 22.17 ? 223 PHE B O   1 
ATOM   3483 C CB  . PHE B 1 223 ? 7.459   -11.640 17.185  1.00 15.82 ? 223 PHE B CB  1 
ATOM   3484 C CG  . PHE B 1 223 ? 6.070   -11.632 16.589  1.00 15.32 ? 223 PHE B CG  1 
ATOM   3485 C CD1 . PHE B 1 223 ? 5.081   -12.475 17.089  1.00 16.26 ? 223 PHE B CD1 1 
ATOM   3486 C CD2 . PHE B 1 223 ? 5.759   -10.762 15.561  1.00 15.72 ? 223 PHE B CD2 1 
ATOM   3487 C CE1 . PHE B 1 223 ? 3.805   -12.423 16.566  1.00 16.98 ? 223 PHE B CE1 1 
ATOM   3488 C CE2 . PHE B 1 223 ? 4.497   -10.738 15.028  1.00 16.49 ? 223 PHE B CE2 1 
ATOM   3489 C CZ  . PHE B 1 223 ? 3.519   -11.555 15.546  1.00 16.72 ? 223 PHE B CZ  1 
ATOM   3490 N N   . GLY B 1 224 ? 9.646   -10.397 19.451  1.00 19.80 ? 224 GLY B N   1 
ATOM   3491 C CA  . GLY B 1 224 ? 11.061  -10.489 19.775  1.00 20.60 ? 224 GLY B CA  1 
ATOM   3492 C C   . GLY B 1 224 ? 11.882  -10.194 18.535  1.00 20.71 ? 224 GLY B C   1 
ATOM   3493 O O   . GLY B 1 224 ? 11.429  -10.409 17.421  1.00 20.63 ? 224 GLY B O   1 
ATOM   3494 N N   . ALA B 1 225 ? 13.111  -9.756  18.770  1.00 22.54 ? 225 ALA B N   1 
ATOM   3495 C CA  . ALA B 1 225 ? 13.951  -9.196  17.725  1.00 23.43 ? 225 ALA B CA  1 
ATOM   3496 C C   . ALA B 1 225 ? 14.447  -10.256 16.743  1.00 22.75 ? 225 ALA B C   1 
ATOM   3497 O O   . ALA B 1 225 ? 14.909  -9.905  15.661  1.00 26.07 ? 225 ALA B O   1 
ATOM   3498 C CB  . ALA B 1 225 ? 15.113  -8.463  18.362  1.00 26.20 ? 225 ALA B CB  1 
ATOM   3499 N N   . ASP B 1 226 ? 14.355  -11.545 17.093  1.00 21.99 ? 226 ASP B N   1 
ATOM   3500 C CA  . ASP B 1 226 ? 14.817  -12.614 16.210  1.00 24.05 ? 226 ASP B CA  1 
ATOM   3501 C C   . ASP B 1 226 ? 13.752  -13.090 15.221  1.00 20.67 ? 226 ASP B C   1 
ATOM   3502 O O   . ASP B 1 226 ? 14.046  -13.840 14.293  1.00 22.58 ? 226 ASP B O   1 
ATOM   3503 C CB  . ASP B 1 226 ? 15.319  -13.793 17.024  1.00 27.39 ? 226 ASP B CB  1 
ATOM   3504 C CG  . ASP B 1 226 ? 16.637  -13.533 17.726  1.00 35.41 ? 226 ASP B CG  1 
ATOM   3505 O OD1 . ASP B 1 226 ? 17.404  -12.664 17.237  1.00 42.62 ? 226 ASP B OD1 1 
ATOM   3506 O OD2 . ASP B 1 226 ? 16.852  -14.160 18.778  1.00 46.73 ? 226 ASP B OD2 1 
ATOM   3507 N N   . TRP B 1 227 ? 12.509  -12.638 15.376  1.00 18.21 ? 227 TRP B N   1 
ATOM   3508 C CA  . TRP B 1 227 ? 11.414  -13.229 14.629  1.00 16.56 ? 227 TRP B CA  1 
ATOM   3509 C C   . TRP B 1 227 ? 11.496  -12.875 13.137  1.00 14.88 ? 227 TRP B C   1 
ATOM   3510 O O   . TRP B 1 227 ? 11.219  -13.711 12.277  1.00 15.22 ? 227 TRP B O   1 
ATOM   3511 C CB  . TRP B 1 227 ? 10.086  -12.779 15.220  1.00 15.65 ? 227 TRP B CB  1 
ATOM   3512 C CG  . TRP B 1 227 ? 8.913   -13.343 14.480  1.00 14.96 ? 227 TRP B CG  1 
ATOM   3513 C CD1 . TRP B 1 227 ? 8.413   -14.610 14.570  1.00 14.65 ? 227 TRP B CD1 1 
ATOM   3514 C CD2 . TRP B 1 227 ? 8.073   -12.634 13.538  1.00 14.07 ? 227 TRP B CD2 1 
ATOM   3515 N NE1 . TRP B 1 227 ? 7.329   -14.737 13.761  1.00 15.11 ? 227 TRP B NE1 1 
ATOM   3516 C CE2 . TRP B 1 227 ? 7.082   -13.547 13.130  1.00 14.16 ? 227 TRP B CE2 1 
ATOM   3517 C CE3 . TRP B 1 227 ? 8.042   -11.332 13.042  1.00 14.49 ? 227 TRP B CE3 1 
ATOM   3518 C CZ2 . TRP B 1 227 ? 6.091   -13.184 12.225  1.00 13.81 ? 227 TRP B CZ2 1 
ATOM   3519 C CZ3 . TRP B 1 227 ? 7.061   -10.985 12.148  1.00 14.83 ? 227 TRP B CZ3 1 
ATOM   3520 C CH2 . TRP B 1 227 ? 6.096   -11.896 11.759  1.00 14.57 ? 227 TRP B CH2 1 
ATOM   3521 N N   . ALA B 1 228 ? 11.769  -11.600 12.842  1.00 15.27 ? 228 ALA B N   1 
ATOM   3522 C CA  . ALA B 1 228 ? 11.663  -11.065 11.491  1.00 14.67 ? 228 ALA B CA  1 
ATOM   3523 C C   . ALA B 1 228 ? 12.841  -11.439 10.576  1.00 14.61 ? 228 ALA B C   1 
ATOM   3524 O O   . ALA B 1 228 ? 13.607  -10.585 10.116  1.00 17.69 ? 228 ALA B O   1 
ATOM   3525 C CB  . ALA B 1 228 ? 11.512  -9.568  11.538  1.00 15.78 ? 228 ALA B CB  1 
ATOM   3526 N N   . ASP B 1 229 ? 12.963  -12.725 10.299  1.00 14.59 ? 229 ASP B N   1 
ATOM   3527 C CA  . ASP B 1 229 ? 13.870  -13.226 9.292   1.00 13.93 ? 229 ASP B CA  1 
ATOM   3528 C C   . ASP B 1 229 ? 13.096  -13.283 7.972   1.00 12.68 ? 229 ASP B C   1 
ATOM   3529 O O   . ASP B 1 229 ? 11.930  -12.897 7.881   1.00 12.85 ? 229 ASP B O   1 
ATOM   3530 C CB  . ASP B 1 229 ? 14.431  -14.557 9.741   1.00 14.02 ? 229 ASP B CB  1 
ATOM   3531 C CG  . ASP B 1 229 ? 13.446  -15.709 9.808   1.00 15.85 ? 229 ASP B CG  1 
ATOM   3532 O OD1 . ASP B 1 229 ? 12.282  -15.533 9.376   1.00 15.66 ? 229 ASP B OD1 1 
ATOM   3533 O OD2 . ASP B 1 229 ? 13.832  -16.747 10.367  1.00 21.23 ? 229 ASP B OD2 1 
ATOM   3534 N N   . ALA B 1 230 ? 13.756  -13.722 6.912   1.00 13.32 ? 230 ALA B N   1 
ATOM   3535 C CA  . ALA B 1 230 ? 13.146  -13.679 5.605   1.00 12.25 ? 230 ALA B CA  1 
ATOM   3536 C C   . ALA B 1 230 ? 11.960  -14.624 5.451   1.00 11.71 ? 230 ALA B C   1 
ATOM   3537 O O   . ALA B 1 230 ? 11.119  -14.400 4.572   1.00 12.11 ? 230 ALA B O   1 
ATOM   3538 C CB  . ALA B 1 230 ? 14.174  -13.926 4.519   1.00 13.11 ? 230 ALA B CB  1 
ATOM   3539 N N   . ARG B 1 231 ? 11.807  -15.616 6.344   1.00 12.65 ? 231 ARG B N   1 
ATOM   3540 C CA  . ARG B 1 231 ? 10.622  -16.461 6.298   1.00 11.89 ? 231 ARG B CA  1 
ATOM   3541 C C   . ARG B 1 231 ? 9.439   -15.773 6.983   1.00 11.09 ? 231 ARG B C   1 
ATOM   3542 O O   . ARG B 1 231 ? 8.307   -16.215 6.795   1.00 12.36 ? 231 ARG B O   1 
ATOM   3543 C CB  . ARG B 1 231 ? 10.913  -17.823 6.911   1.00 12.42 ? 231 ARG B CB  1 
ATOM   3544 C CG  . ARG B 1 231 ? 9.733   -18.763 7.056   1.00 13.10 ? 231 ARG B CG  1 
ATOM   3545 C CD  . ARG B 1 231 ? 9.034   -19.060 5.761   1.00 13.00 ? 231 ARG B CD  1 
ATOM   3546 N NE  . ARG B 1 231 ? 7.894   -19.946 5.923   1.00 14.13 ? 231 ARG B NE  1 
ATOM   3547 C CZ  . ARG B 1 231 ? 6.660   -19.556 6.235   1.00 14.22 ? 231 ARG B CZ  1 
ATOM   3548 N NH1 . ARG B 1 231 ? 6.395   -18.280 6.427   1.00 13.44 ? 231 ARG B NH1 1 
ATOM   3549 N NH2 . ARG B 1 231 ? 5.695   -20.449 6.320   1.00 14.02 ? 231 ARG B NH2 1 
ATOM   3550 N N   . HIS B 1 232 ? 9.689   -14.700 7.729   1.00 10.60 ? 232 HIS B N   1 
ATOM   3551 C CA  . HIS B 1 232 ? 8.624   -14.093 8.503   1.00 10.79 ? 232 HIS B CA  1 
ATOM   3552 C C   . HIS B 1 232 ? 8.379   -12.621 8.213   1.00 10.45 ? 232 HIS B C   1 
ATOM   3553 O O   . HIS B 1 232 ? 7.392   -12.079 8.692   1.00 10.82 ? 232 HIS B O   1 
ATOM   3554 C CB  . HIS B 1 232 ? 8.845   -14.295 10.004  1.00 11.44 ? 232 HIS B CB  1 
ATOM   3555 C CG  . HIS B 1 232 ? 8.789   -15.736 10.344  1.00 13.03 ? 232 HIS B CG  1 
ATOM   3556 N ND1 . HIS B 1 232 ? 9.876   -16.570 10.236  1.00 14.69 ? 232 HIS B ND1 1 
ATOM   3557 C CD2 . HIS B 1 232 ? 7.773   -16.512 10.753  1.00 13.88 ? 232 HIS B CD2 1 
ATOM   3558 C CE1 . HIS B 1 232 ? 9.528   -17.805 10.568  1.00 15.41 ? 232 HIS B CE1 1 
ATOM   3559 N NE2 . HIS B 1 232 ? 8.244   -17.797 10.914  1.00 15.78 ? 232 HIS B NE2 1 
ATOM   3560 N N   . TYR B 1 233 ? 9.221   -11.946 7.418   1.00 9.95  ? 233 TYR B N   1 
ATOM   3561 C CA  . TYR B 1 233 ? 9.059   -10.521 7.233   1.00 10.11 ? 233 TYR B CA  1 
ATOM   3562 C C   . TYR B 1 233 ? 9.617   -10.151 5.859   1.00 10.13 ? 233 TYR B C   1 
ATOM   3563 O O   . TYR B 1 233 ? 10.721  -10.554 5.526   1.00 11.25 ? 233 TYR B O   1 
ATOM   3564 C CB  . TYR B 1 233 ? 9.741   -9.717  8.346   1.00 11.25 ? 233 TYR B CB  1 
ATOM   3565 C CG  . TYR B 1 233 ? 9.161   -8.344  8.595   1.00 11.81 ? 233 TYR B CG  1 
ATOM   3566 C CD1 . TYR B 1 233 ? 9.349   -7.287  7.709   1.00 13.45 ? 233 TYR B CD1 1 
ATOM   3567 C CD2 . TYR B 1 233 ? 8.330   -8.124  9.683   1.00 13.78 ? 233 TYR B CD2 1 
ATOM   3568 C CE1 . TYR B 1 233 ? 8.763   -6.050  7.909   1.00 15.15 ? 233 TYR B CE1 1 
ATOM   3569 C CE2 . TYR B 1 233 ? 7.753   -6.886  9.904   1.00 14.73 ? 233 TYR B CE2 1 
ATOM   3570 C CZ  . TYR B 1 233 ? 7.976   -5.842  9.033   1.00 16.07 ? 233 TYR B CZ  1 
ATOM   3571 O OH  . TYR B 1 233 ? 7.344   -4.648  9.323   1.00 18.52 ? 233 TYR B OH  1 
ATOM   3572 N N   . ARG B 1 234 ? 8.884   -9.334  5.139   1.00 9.45  ? 234 ARG B N   1 
ATOM   3573 C CA  . ARG B 1 234 ? 9.325   -8.765  3.887   1.00 9.63  ? 234 ARG B CA  1 
ATOM   3574 C C   . ARG B 1 234 ? 8.887   -7.330  3.737   1.00 10.07 ? 234 ARG B C   1 
ATOM   3575 O O   . ARG B 1 234 ? 7.847   -6.938  4.261   1.00 10.04 ? 234 ARG B O   1 
ATOM   3576 C CB  . ARG B 1 234 ? 8.831   -9.543  2.668   1.00 10.31 ? 234 ARG B CB  1 
ATOM   3577 C CG  . ARG B 1 234 ? 9.249   -11.001 2.614   1.00 9.59  ? 234 ARG B CG  1 
ATOM   3578 C CD  . ARG B 1 234 ? 10.722  -11.249 2.344   1.00 9.75  ? 234 ARG B CD  1 
ATOM   3579 N NE  . ARG B 1 234 ? 10.977  -12.667 2.347   1.00 10.20 ? 234 ARG B NE  1 
ATOM   3580 C CZ  . ARG B 1 234 ? 10.581  -13.532 1.429   1.00 10.27 ? 234 ARG B CZ  1 
ATOM   3581 N NH1 . ARG B 1 234 ? 10.182  -13.117 0.237   1.00 10.80 ? 234 ARG B NH1 1 
ATOM   3582 N NH2 . ARG B 1 234 ? 10.583  -14.822 1.693   1.00 11.52 ? 234 ARG B NH2 1 
ATOM   3583 N N   . PHE B 1 235 ? 9.622   -6.589  2.897   1.00 10.96 ? 235 PHE B N   1 
ATOM   3584 C CA  . PHE B 1 235 ? 9.298   -5.244  2.473   1.00 11.11 ? 235 PHE B CA  1 
ATOM   3585 C C   . PHE B 1 235 ? 9.270   -5.132  0.964   1.00 10.99 ? 235 PHE B C   1 
ATOM   3586 O O   . PHE B 1 235 ? 10.134  -5.678  0.289   1.00 12.21 ? 235 PHE B O   1 
ATOM   3587 C CB  . PHE B 1 235 ? 10.351  -4.215  2.878   1.00 11.54 ? 235 PHE B CB  1 
ATOM   3588 C CG  . PHE B 1 235 ? 10.458  -3.935  4.364   1.00 11.82 ? 235 PHE B CG  1 
ATOM   3589 C CD1 . PHE B 1 235 ? 9.652   -2.963  4.912   1.00 14.10 ? 235 PHE B CD1 1 
ATOM   3590 C CD2 . PHE B 1 235 ? 11.409  -4.526  5.180   1.00 13.93 ? 235 PHE B CD2 1 
ATOM   3591 C CE1 . PHE B 1 235 ? 9.708   -2.655  6.254   1.00 15.41 ? 235 PHE B CE1 1 
ATOM   3592 C CE2 . PHE B 1 235 ? 11.488  -4.188  6.520   1.00 16.31 ? 235 PHE B CE2 1 
ATOM   3593 C CZ  . PHE B 1 235 ? 10.629  -3.242  7.047   1.00 15.76 ? 235 PHE B CZ  1 
ATOM   3594 N N   A SER B 1 236 ? 8.357   -4.303  0.456   0.50 11.60 ? 236 SER B N   1 
ATOM   3595 N N   B SER B 1 236 ? 8.342   -4.337  0.446   0.50 12.08 ? 236 SER B N   1 
ATOM   3596 C CA  A SER B 1 236 ? 8.422   -3.829  -0.920  0.50 12.46 ? 236 SER B CA  1 
ATOM   3597 C CA  B SER B 1 236 ? 8.459   -3.819  -0.909  0.50 13.24 ? 236 SER B CA  1 
ATOM   3598 C C   A SER B 1 236 ? 7.868   -2.415  -1.007  0.50 12.58 ? 236 SER B C   1 
ATOM   3599 C C   B SER B 1 236 ? 7.922   -2.397  -0.915  0.50 13.27 ? 236 SER B C   1 
ATOM   3600 O O   A SER B 1 236 ? 6.728   -2.180  -0.623  0.50 13.16 ? 236 SER B O   1 
ATOM   3601 O O   B SER B 1 236 ? 6.899   -2.124  -0.292  0.50 14.66 ? 236 SER B O   1 
ATOM   3602 C CB  A SER B 1 236 ? 7.664   -4.731  -1.870  0.50 14.29 ? 236 SER B CB  1 
ATOM   3603 C CB  B SER B 1 236 ? 7.737   -4.689  -1.910  0.50 15.57 ? 236 SER B CB  1 
ATOM   3604 O OG  A SER B 1 236 ? 7.807   -4.237  -3.194  0.50 17.53 ? 236 SER B OG  1 
ATOM   3605 O OG  B SER B 1 236 ? 6.337   -4.585  -1.742  0.50 19.20 ? 236 SER B OG  1 
ATOM   3606 N N   . ALA B 1 237 ? 8.622   -1.495  -1.587  1.00 14.93 ? 237 ALA B N   1 
ATOM   3607 C CA  . ALA B 1 237 ? 8.149   -0.155  -1.827  1.00 16.16 ? 237 ALA B CA  1 
ATOM   3608 C C   . ALA B 1 237 ? 9.062   0.508   -2.840  1.00 17.02 ? 237 ALA B C   1 
ATOM   3609 O O   . ALA B 1 237 ? 10.284  0.375   -2.751  1.00 16.89 ? 237 ALA B O   1 
ATOM   3610 C CB  . ALA B 1 237 ? 8.124   0.671   -0.567  1.00 18.30 ? 237 ALA B CB  1 
ATOM   3611 N N   . SER B 1 238 ? 8.452   1.329   -3.681  1.00 19.99 ? 238 SER B N   1 
ATOM   3612 C CA  . SER B 1 238 ? 9.209   2.141   -4.610  1.00 20.53 ? 238 SER B CA  1 
ATOM   3613 C C   . SER B 1 238 ? 10.136  3.056   -3.813  1.00 22.51 ? 238 SER B C   1 
ATOM   3614 O O   . SER B 1 238 ? 9.704   3.714   -2.882  1.00 23.13 ? 238 SER B O   1 
ATOM   3615 C CB  . SER B 1 238 ? 8.263   2.929   -5.490  1.00 24.81 ? 238 SER B CB  1 
ATOM   3616 O OG  . SER B 1 238 ? 9.042   3.701   -6.390  1.00 34.17 ? 238 SER B OG  1 
ATOM   3617 N N   . GLY B 1 239 ? 11.409  3.117   -4.203  1.00 22.24 ? 239 GLY B N   1 
ATOM   3618 C CA  . GLY B 1 239 ? 12.341  4.065   -3.628  1.00 20.01 ? 239 GLY B CA  1 
ATOM   3619 C C   . GLY B 1 239 ? 13.043  3.559   -2.370  1.00 18.70 ? 239 GLY B C   1 
ATOM   3620 O O   . GLY B 1 239 ? 14.046  4.148   -1.946  1.00 18.87 ? 239 GLY B O   1 
ATOM   3621 N N   . LEU B 1 240 ? 12.543  2.468   -1.769  1.00 15.99 ? 240 LEU B N   1 
ATOM   3622 C CA  . LEU B 1 240 ? 13.080  2.046   -0.494  1.00 15.72 ? 240 LEU B CA  1 
ATOM   3623 C C   . LEU B 1 240 ? 14.521  1.558   -0.618  1.00 16.15 ? 240 LEU B C   1 
ATOM   3624 O O   . LEU B 1 240 ? 15.352  1.869   0.226   1.00 16.71 ? 240 LEU B O   1 
ATOM   3625 C CB  . LEU B 1 240 ? 12.165  0.996   0.137   1.00 15.97 ? 240 LEU B CB  1 
ATOM   3626 C CG  . LEU B 1 240 ? 12.679  0.394   1.450   1.00 15.79 ? 240 LEU B CG  1 
ATOM   3627 C CD1 . LEU B 1 240 ? 12.841  1.523   2.494   1.00 16.89 ? 240 LEU B CD1 1 
ATOM   3628 C CD2 . LEU B 1 240 ? 11.775  -0.716  1.966   1.00 16.68 ? 240 LEU B CD2 1 
ATOM   3629 N N   . LEU B 1 241 ? 14.816  0.744   -1.637  1.00 15.20 ? 241 LEU B N   1 
ATOM   3630 C CA  . LEU B 1 241 ? 16.175  0.222   -1.759  1.00 15.03 ? 241 LEU B CA  1 
ATOM   3631 C C   . LEU B 1 241 ? 17.191  1.368   -1.814  1.00 16.03 ? 241 LEU B C   1 
ATOM   3632 O O   . LEU B 1 241 ? 18.233  1.332   -1.144  1.00 15.44 ? 241 LEU B O   1 
ATOM   3633 C CB  . LEU B 1 241 ? 16.346  -0.697  -2.959  1.00 15.29 ? 241 LEU B CB  1 
ATOM   3634 C CG  . LEU B 1 241 ? 17.732  -1.314  -3.087  1.00 16.30 ? 241 LEU B CG  1 
ATOM   3635 C CD1 . LEU B 1 241 ? 18.165  -2.108  -1.928  1.00 17.71 ? 241 LEU B CD1 1 
ATOM   3636 C CD2 . LEU B 1 241 ? 17.766  -2.164  -4.307  1.00 18.50 ? 241 LEU B CD2 1 
ATOM   3637 N N   . ALA B 1 242 ? 16.886  2.398   -2.607  1.00 16.98 ? 242 ALA B N   1 
ATOM   3638 C CA  . ALA B 1 242 ? 17.788  3.536   -2.725  1.00 19.11 ? 242 ALA B CA  1 
ATOM   3639 C C   . ALA B 1 242 ? 17.989  4.212   -1.371  1.00 18.60 ? 242 ALA B C   1 
ATOM   3640 O O   . ALA B 1 242 ? 19.090  4.610   -1.020  1.00 20.94 ? 242 ALA B O   1 
ATOM   3641 C CB  . ALA B 1 242 ? 17.258  4.516   -3.741  1.00 20.96 ? 242 ALA B CB  1 
ATOM   3642 N N   . SER B 1 243 ? 16.910  4.331   -0.603  1.00 18.48 ? 243 SER B N   1 
ATOM   3643 C CA  . SER B 1 243 ? 16.998  4.988   0.690   1.00 19.77 ? 243 SER B CA  1 
ATOM   3644 C C   . SER B 1 243 ? 17.848  4.143   1.640   1.00 18.23 ? 243 SER B C   1 
ATOM   3645 O O   . SER B 1 243 ? 18.653  4.660   2.415   1.00 20.01 ? 243 SER B O   1 
ATOM   3646 C CB  . SER B 1 243 ? 15.617  5.235   1.253   1.00 20.40 ? 243 SER B CB  1 
ATOM   3647 O OG  . SER B 1 243 ? 15.688  5.906   2.507   1.00 21.92 ? 243 SER B OG  1 
ATOM   3648 N N   . LEU B 1 244 ? 17.651  2.823   1.600   1.00 17.49 ? 244 LEU B N   1 
ATOM   3649 C CA  . LEU B 1 244 ? 18.419  1.940   2.465   1.00 16.48 ? 244 LEU B CA  1 
ATOM   3650 C C   . LEU B 1 244 ? 19.896  2.031   2.117   1.00 17.81 ? 244 LEU B C   1 
ATOM   3651 O O   . LEU B 1 244 ? 20.739  2.120   3.002   1.00 18.44 ? 244 LEU B O   1 
ATOM   3652 C CB  . LEU B 1 244 ? 17.889  0.517   2.368   1.00 15.07 ? 244 LEU B CB  1 
ATOM   3653 C CG  . LEU B 1 244 ? 16.455  0.289   2.870   1.00 15.36 ? 244 LEU B CG  1 
ATOM   3654 C CD1 . LEU B 1 244 ? 16.051  -1.115  2.613   1.00 16.31 ? 244 LEU B CD1 1 
ATOM   3655 C CD2 . LEU B 1 244 ? 16.363  0.586   4.340   1.00 16.45 ? 244 LEU B CD2 1 
ATOM   3656 N N   . LEU B 1 245 ? 20.200  1.999   0.823   1.00 16.79 ? 245 LEU B N   1 
ATOM   3657 C CA  . LEU B 1 245 ? 21.580  2.063   0.389   1.00 18.21 ? 245 LEU B CA  1 
ATOM   3658 C C   . LEU B 1 245 ? 22.214  3.395   0.792   1.00 19.88 ? 245 LEU B C   1 
ATOM   3659 O O   . LEU B 1 245 ? 23.368  3.419   1.215   1.00 22.12 ? 245 LEU B O   1 
ATOM   3660 C CB  . LEU B 1 245 ? 21.708  1.782   -1.110  1.00 18.06 ? 245 LEU B CB  1 
ATOM   3661 C CG  . LEU B 1 245 ? 21.524  0.310   -1.475  1.00 19.06 ? 245 LEU B CG  1 
ATOM   3662 C CD1 . LEU B 1 245 ? 21.392  0.127   -2.968  1.00 20.15 ? 245 LEU B CD1 1 
ATOM   3663 C CD2 . LEU B 1 245 ? 22.626  -0.570  -0.917  1.00 19.27 ? 245 LEU B CD2 1 
ATOM   3664 N N   . LYS B 1 246 ? 21.464  4.489   0.667   1.00 21.67 ? 246 LYS B N   1 
ATOM   3665 C CA  . LYS B 1 246 ? 21.941  5.805   1.070   1.00 23.72 ? 246 LYS B CA  1 
ATOM   3666 C C   . LYS B 1 246 ? 22.268  5.810   2.563   1.00 24.31 ? 246 LYS B C   1 
ATOM   3667 O O   . LYS B 1 246 ? 23.272  6.357   2.968   1.00 26.37 ? 246 LYS B O   1 
ATOM   3668 C CB  . LYS B 1 246 ? 20.910  6.889   0.729   1.00 28.14 ? 246 LYS B CB  1 
ATOM   3669 C CG  . LYS B 1 246 ? 21.342  8.299   1.114   1.00 33.98 ? 246 LYS B CG  1 
ATOM   3670 C CD  . LYS B 1 246 ? 20.316  9.382   0.845   1.00 39.76 ? 246 LYS B CD  1 
ATOM   3671 C CE  . LYS B 1 246 ? 20.835  10.695  1.347   1.00 44.86 ? 246 LYS B CE  1 
ATOM   3672 N NZ  . LYS B 1 246 ? 19.762  11.681  1.274   1.00 48.54 ? 246 LYS B NZ  1 
ATOM   3673 N N   . ALA B 1 247 ? 21.385  5.221   3.389   1.00 23.02 ? 247 ALA B N   1 
ATOM   3674 C CA  . ALA B 1 247 ? 21.633  5.143   4.822   1.00 24.40 ? 247 ALA B CA  1 
ATOM   3675 C C   . ALA B 1 247 ? 22.936  4.395   5.109   1.00 25.10 ? 247 ALA B C   1 
ATOM   3676 O O   . ALA B 1 247 ? 23.590  4.652   6.118   1.00 28.72 ? 247 ALA B O   1 
ATOM   3677 C CB  . ALA B 1 247 ? 20.463  4.494   5.513   1.00 23.78 ? 247 ALA B CB  1 
ATOM   3678 N N   . LEU B 1 248 ? 23.267  3.433   4.240   1.00 24.62 ? 248 LEU B N   1 
ATOM   3679 C CA  . LEU B 1 248 ? 24.438  2.595   4.426   1.00 24.70 ? 248 LEU B CA  1 
ATOM   3680 C C   . LEU B 1 248 ? 25.688  3.152   3.744   1.00 27.24 ? 248 LEU B C   1 
ATOM   3681 O O   . LEU B 1 248 ? 26.721  2.508   3.825   1.00 32.06 ? 248 LEU B O   1 
ATOM   3682 C CB  . LEU B 1 248 ? 24.089  1.188   3.942   1.00 23.16 ? 248 LEU B CB  1 
ATOM   3683 C CG  . LEU B 1 248 ? 23.031  0.468   4.795   1.00 23.58 ? 248 LEU B CG  1 
ATOM   3684 C CD1 . LEU B 1 248 ? 22.439  -0.716  4.095   1.00 24.16 ? 248 LEU B CD1 1 
ATOM   3685 C CD2 . LEU B 1 248 ? 23.675  -0.016  6.079   1.00 26.46 ? 248 LEU B CD2 1 
ATOM   3686 N N   . GLY B 1 249 ? 25.588  4.308   3.078   1.00 30.85 ? 249 GLY B N   1 
ATOM   3687 C CA  . GLY B 1 249 ? 26.743  4.971   2.492   1.00 32.23 ? 249 GLY B CA  1 
ATOM   3688 C C   . GLY B 1 249 ? 26.988  4.629   1.017   1.00 31.95 ? 249 GLY B C   1 
ATOM   3689 O O   . GLY B 1 249 ? 28.083  4.837   0.499   1.00 37.66 ? 249 GLY B O   1 
ATOM   3690 N N   . HIS B 1 250 ? 25.938  4.172   0.326   1.00 33.47 ? 250 HIS B N   1 
ATOM   3691 C CA  . HIS B 1 250 ? 26.020  3.869   -1.097  1.00 32.07 ? 250 HIS B CA  1 
ATOM   3692 C C   . HIS B 1 250 ? 25.149  4.837   -1.902  1.00 35.64 ? 250 HIS B C   1 
ATOM   3693 O O   . HIS B 1 250 ? 23.933  4.590   -1.926  1.00 36.86 ? 250 HIS B O   1 
ATOM   3694 C CB  . HIS B 1 250 ? 25.694  2.394   -1.321  1.00 33.29 ? 250 HIS B CB  1 
ATOM   3695 C CG  . HIS B 1 250 ? 26.806  1.546   -0.830  1.00 35.22 ? 250 HIS B CG  1 
ATOM   3696 N ND1 . HIS B 1 250 ? 26.909  1.009   0.435   1.00 38.61 ? 250 HIS B ND1 1 
ATOM   3697 C CD2 . HIS B 1 250 ? 27.941  1.229   -1.463  1.00 34.17 ? 250 HIS B CD2 1 
ATOM   3698 C CE1 . HIS B 1 250 ? 28.045  0.338   0.526   1.00 35.09 ? 250 HIS B CE1 1 
ATOM   3699 N NE2 . HIS B 1 250 ? 28.688  0.468   -0.607  1.00 35.79 ? 250 HIS B NE2 1 
HETATM 3700 C C1  . GOL C 2 .   ? -1.400  -15.961 -30.279 1.00 34.14 ? 301 GOL A C1  1 
HETATM 3701 O O1  . GOL C 2 .   ? -1.424  -16.651 -31.532 1.00 30.40 ? 301 GOL A O1  1 
HETATM 3702 C C2  . GOL C 2 .   ? -1.151  -14.476 -30.437 1.00 38.10 ? 301 GOL A C2  1 
HETATM 3703 O O2  . GOL C 2 .   ? -1.935  -13.948 -31.500 1.00 36.61 ? 301 GOL A O2  1 
HETATM 3704 C C3  . GOL C 2 .   ? -1.416  -13.688 -29.175 1.00 37.59 ? 301 GOL A C3  1 
HETATM 3705 O O3  . GOL C 2 .   ? -2.521  -12.799 -29.311 1.00 38.80 ? 301 GOL A O3  1 
HETATM 3706 C C1  . GOL D 2 .   ? 1.054   6.518   0.177   1.00 33.02 ? 301 GOL B C1  1 
HETATM 3707 O O1  . GOL D 2 .   ? 2.162   5.888   -0.434  1.00 37.30 ? 301 GOL B O1  1 
HETATM 3708 C C2  . GOL D 2 .   ? 0.133   5.450   0.692   1.00 27.63 ? 301 GOL B C2  1 
HETATM 3709 O O2  . GOL D 2 .   ? -0.244  4.573   -0.373  1.00 25.30 ? 301 GOL B O2  1 
HETATM 3710 C C3  . GOL D 2 .   ? 0.790   4.635   1.784   1.00 26.87 ? 301 GOL B C3  1 
HETATM 3711 O O3  . GOL D 2 .   ? -0.175  3.763   2.339   1.00 26.25 ? 301 GOL B O3  1 
HETATM 3712 C C1  . GOL E 2 .   ? 5.155   -7.072  -10.847 1.00 35.32 ? 302 GOL B C1  1 
HETATM 3713 O O1  . GOL E 2 .   ? 6.123   -6.388  -11.626 1.00 37.89 ? 302 GOL B O1  1 
HETATM 3714 C C2  . GOL E 2 .   ? 5.488   -6.904  -9.389  1.00 34.86 ? 302 GOL B C2  1 
HETATM 3715 O O2  . GOL E 2 .   ? 5.211   -5.556  -9.008  1.00 39.93 ? 302 GOL B O2  1 
HETATM 3716 C C3  . GOL E 2 .   ? 4.731   -7.864  -8.516  1.00 38.35 ? 302 GOL B C3  1 
HETATM 3717 O O3  . GOL E 2 .   ? 5.147   -7.731  -7.161  1.00 35.12 ? 302 GOL B O3  1 
HETATM 3718 C C1  . GOL F 2 .   ? -7.162  1.566   10.217  1.00 40.63 ? 303 GOL B C1  1 
HETATM 3719 O O1  . GOL F 2 .   ? -8.045  0.589   10.762  1.00 46.90 ? 303 GOL B O1  1 
HETATM 3720 C C2  . GOL F 2 .   ? -6.382  1.025   9.036   1.00 38.95 ? 303 GOL B C2  1 
HETATM 3721 O O2  . GOL F 2 .   ? -7.025  1.470   7.842   1.00 37.46 ? 303 GOL B O2  1 
HETATM 3722 C C3  . GOL F 2 .   ? -4.915  1.402   9.080   1.00 37.00 ? 303 GOL B C3  1 
HETATM 3723 O O3  . GOL F 2 .   ? -4.552  2.457   8.190   1.00 38.41 ? 303 GOL B O3  1 
HETATM 3724 C C1  . GOL G 2 .   ? 3.047   -5.998  -5.191  1.00 30.40 ? 304 GOL B C1  1 
HETATM 3725 O O1  . GOL G 2 .   ? 3.520   -7.341  -5.238  1.00 33.98 ? 304 GOL B O1  1 
HETATM 3726 C C2  . GOL G 2 .   ? 4.086   -5.071  -4.585  1.00 33.73 ? 304 GOL B C2  1 
HETATM 3727 O O2  . GOL G 2 .   ? 4.612   -5.657  -3.394  1.00 33.88 ? 304 GOL B O2  1 
HETATM 3728 C C3  . GOL G 2 .   ? 5.240   -4.699  -5.490  1.00 38.07 ? 304 GOL B C3  1 
HETATM 3729 O O3  . GOL G 2 .   ? 5.888   -3.528  -4.991  1.00 41.53 ? 304 GOL B O3  1 
HETATM 3730 O O   . HOH H 3 .   ? -12.167 -10.502 -48.923 1.00 45.49 ? 401 HOH A O   1 
HETATM 3731 O O   A HOH H 3 .   ? -1.712  -20.370 -30.672 0.50 19.31 ? 402 HOH A O   1 
HETATM 3732 O O   B HOH H 3 .   ? -2.739  -20.773 -32.654 0.50 17.52 ? 402 HOH A O   1 
HETATM 3733 O O   . HOH H 3 .   ? 3.326   -31.426 -54.408 1.00 41.96 ? 403 HOH A O   1 
HETATM 3734 O O   . HOH H 3 .   ? -8.936  -36.572 -37.704 1.00 29.06 ? 404 HOH A O   1 
HETATM 3735 O O   . HOH H 3 .   ? -0.394  -16.588 -49.805 1.00 25.47 ? 405 HOH A O   1 
HETATM 3736 O O   . HOH H 3 .   ? -9.842  -28.488 -53.152 1.00 41.18 ? 406 HOH A O   1 
HETATM 3737 O O   . HOH H 3 .   ? 9.490   -15.699 -24.267 1.00 52.37 ? 407 HOH A O   1 
HETATM 3738 O O   . HOH H 3 .   ? -0.899  -17.513 -35.856 1.00 28.61 ? 408 HOH A O   1 
HETATM 3739 O O   . HOH H 3 .   ? -12.504 -20.034 -49.177 1.00 25.95 ? 409 HOH A O   1 
HETATM 3740 O O   . HOH H 3 .   ? -13.538 -21.891 -16.685 1.00 45.70 ? 410 HOH A O   1 
HETATM 3741 O O   . HOH H 3 .   ? 0.422   -33.909 -27.527 1.00 25.34 ? 411 HOH A O   1 
HETATM 3742 O O   . HOH H 3 .   ? 10.378  -15.214 -35.278 1.00 14.78 ? 412 HOH A O   1 
HETATM 3743 O O   . HOH H 3 .   ? -1.184  -14.742 -14.966 1.00 21.60 ? 413 HOH A O   1 
HETATM 3744 O O   . HOH H 3 .   ? -12.574 -12.305 -50.874 1.00 46.24 ? 414 HOH A O   1 
HETATM 3745 O O   . HOH H 3 .   ? 1.048   -36.611 -33.229 1.00 25.33 ? 415 HOH A O   1 
HETATM 3746 O O   . HOH H 3 .   ? -7.214  -29.863 -29.601 1.00 35.74 ? 416 HOH A O   1 
HETATM 3747 O O   . HOH H 3 .   ? -18.071 -26.478 -46.663 1.00 32.46 ? 417 HOH A O   1 
HETATM 3748 O O   . HOH H 3 .   ? -5.317  -13.203 -30.037 1.00 43.86 ? 418 HOH A O   1 
HETATM 3749 O O   . HOH H 3 .   ? -26.794 -18.365 -37.274 1.00 20.54 ? 419 HOH A O   1 
HETATM 3750 O O   . HOH H 3 .   ? -12.499 -29.594 -43.517 1.00 35.75 ? 420 HOH A O   1 
HETATM 3751 O O   . HOH H 3 .   ? -17.889 -13.479 -35.902 1.00 43.02 ? 421 HOH A O   1 
HETATM 3752 O O   . HOH H 3 .   ? 3.934   -38.401 -35.933 1.00 30.43 ? 422 HOH A O   1 
HETATM 3753 O O   . HOH H 3 .   ? -4.608  -6.593  -25.818 1.00 52.72 ? 423 HOH A O   1 
HETATM 3754 O O   . HOH H 3 .   ? -10.878 -9.040  -44.844 1.00 44.61 ? 424 HOH A O   1 
HETATM 3755 O O   . HOH H 3 .   ? 7.316   -15.860 -20.814 1.00 19.19 ? 425 HOH A O   1 
HETATM 3756 O O   . HOH H 3 .   ? -22.506 -24.245 -40.790 1.00 46.11 ? 426 HOH A O   1 
HETATM 3757 O O   . HOH H 3 .   ? 0.265   -41.581 -40.866 1.00 24.12 ? 427 HOH A O   1 
HETATM 3758 O O   . HOH H 3 .   ? -8.288  -22.090 -17.594 1.00 25.70 ? 428 HOH A O   1 
HETATM 3759 O O   . HOH H 3 .   ? -6.602  -15.384 -36.916 1.00 29.06 ? 429 HOH A O   1 
HETATM 3760 O O   . HOH H 3 .   ? -3.025  -18.548 -34.307 1.00 21.49 ? 430 HOH A O   1 
HETATM 3761 O O   . HOH H 3 .   ? -6.084  -30.606 -27.301 1.00 34.15 ? 431 HOH A O   1 
HETATM 3762 O O   . HOH H 3 .   ? 16.522  -39.171 -37.512 1.00 47.15 ? 432 HOH A O   1 
HETATM 3763 O O   . HOH H 3 .   ? 14.161  -20.247 -25.360 1.00 14.30 ? 433 HOH A O   1 
HETATM 3764 O O   . HOH H 3 .   ? 1.928   -40.595 -46.743 1.00 38.22 ? 434 HOH A O   1 
HETATM 3765 O O   . HOH H 3 .   ? 23.002  -21.277 -28.069 1.00 53.50 ? 435 HOH A O   1 
HETATM 3766 O O   . HOH H 3 .   ? 4.327   -17.602 -23.936 1.00 27.58 ? 436 HOH A O   1 
HETATM 3767 O O   . HOH H 3 .   ? -17.414 -23.896 -54.823 1.00 51.45 ? 437 HOH A O   1 
HETATM 3768 O O   . HOH H 3 .   ? 7.040   -18.712 -46.131 1.00 16.01 ? 438 HOH A O   1 
HETATM 3769 O O   . HOH H 3 .   ? -21.625 -20.447 -34.071 1.00 17.86 ? 439 HOH A O   1 
HETATM 3770 O O   . HOH H 3 .   ? 0.192   -36.781 -52.956 1.00 26.23 ? 440 HOH A O   1 
HETATM 3771 O O   . HOH H 3 .   ? -7.692  -32.411 -47.352 1.00 19.24 ? 441 HOH A O   1 
HETATM 3772 O O   . HOH H 3 .   ? 7.439   -17.099 -41.441 1.00 13.89 ? 442 HOH A O   1 
HETATM 3773 O O   . HOH H 3 .   ? -15.024 -25.369 -32.574 1.00 21.92 ? 443 HOH A O   1 
HETATM 3774 O O   . HOH H 3 .   ? 22.217  -21.716 -42.876 1.00 41.62 ? 444 HOH A O   1 
HETATM 3775 O O   . HOH H 3 .   ? -4.021  -27.662 -20.079 1.00 14.95 ? 445 HOH A O   1 
HETATM 3776 O O   . HOH H 3 .   ? -17.431 -9.819  -43.265 1.00 38.43 ? 446 HOH A O   1 
HETATM 3777 O O   . HOH H 3 .   ? -13.396 -24.090 -24.426 1.00 22.74 ? 447 HOH A O   1 
HETATM 3778 O O   . HOH H 3 .   ? -6.206  -10.829 -20.979 1.00 42.37 ? 448 HOH A O   1 
HETATM 3779 O O   . HOH H 3 .   ? -9.006  -19.581 -55.058 1.00 43.85 ? 449 HOH A O   1 
HETATM 3780 O O   . HOH H 3 .   ? -21.022 -14.197 -30.541 1.00 35.27 ? 450 HOH A O   1 
HETATM 3781 O O   . HOH H 3 .   ? 15.178  -18.710 -33.938 1.00 13.67 ? 451 HOH A O   1 
HETATM 3782 O O   . HOH H 3 .   ? 5.152   -36.186 -34.836 1.00 17.48 ? 452 HOH A O   1 
HETATM 3783 O O   . HOH H 3 .   ? -6.733  -35.407 -54.435 1.00 39.63 ? 453 HOH A O   1 
HETATM 3784 O O   . HOH H 3 .   ? -7.610  -36.568 -41.593 1.00 28.32 ? 454 HOH A O   1 
HETATM 3785 O O   . HOH H 3 .   ? 1.339   -41.320 -38.223 1.00 30.02 ? 455 HOH A O   1 
HETATM 3786 O O   . HOH H 3 .   ? 2.484   -31.826 -18.273 1.00 30.46 ? 456 HOH A O   1 
HETATM 3787 O O   . HOH H 3 .   ? -10.220 -25.734 -51.891 1.00 40.17 ? 457 HOH A O   1 
HETATM 3788 O O   . HOH H 3 .   ? 4.700   -37.457 -21.919 1.00 33.62 ? 458 HOH A O   1 
HETATM 3789 O O   . HOH H 3 .   ? -17.580 -25.633 -31.418 1.00 31.86 ? 459 HOH A O   1 
HETATM 3790 O O   . HOH H 3 .   ? 17.329  -26.482 -34.334 1.00 18.65 ? 460 HOH A O   1 
HETATM 3791 O O   . HOH H 3 .   ? -20.766 -24.210 -21.900 1.00 33.91 ? 461 HOH A O   1 
HETATM 3792 O O   . HOH H 3 .   ? -18.669 -25.713 -28.518 1.00 30.99 ? 462 HOH A O   1 
HETATM 3793 O O   . HOH H 3 .   ? 6.680   -17.013 -25.306 1.00 17.86 ? 463 HOH A O   1 
HETATM 3794 O O   . HOH H 3 .   ? -12.980 -30.783 -38.419 1.00 27.49 ? 464 HOH A O   1 
HETATM 3795 O O   . HOH H 3 .   ? 1.830   -24.434 -54.304 1.00 50.97 ? 465 HOH A O   1 
HETATM 3796 O O   . HOH H 3 .   ? 3.287   -14.112 -46.019 1.00 32.66 ? 466 HOH A O   1 
HETATM 3797 O O   . HOH H 3 .   ? -23.686 -15.883 -27.535 1.00 41.30 ? 467 HOH A O   1 
HETATM 3798 O O   . HOH H 3 .   ? 2.176   -27.763 -16.184 1.00 26.88 ? 468 HOH A O   1 
HETATM 3799 O O   . HOH H 3 .   ? -7.249  -14.790 -17.982 1.00 17.60 ? 469 HOH A O   1 
HETATM 3800 O O   . HOH H 3 .   ? 17.286  -20.522 -32.282 1.00 15.41 ? 470 HOH A O   1 
HETATM 3801 O O   . HOH H 3 .   ? -9.113  -24.301 -18.817 1.00 24.87 ? 471 HOH A O   1 
HETATM 3802 O O   . HOH H 3 .   ? -11.643 -20.027 -16.187 1.00 25.63 ? 472 HOH A O   1 
HETATM 3803 O O   . HOH H 3 .   ? -9.150  -13.343 -39.212 1.00 26.34 ? 473 HOH A O   1 
HETATM 3804 O O   . HOH H 3 .   ? 3.784   -19.322 -21.190 1.00 34.88 ? 474 HOH A O   1 
HETATM 3805 O O   . HOH H 3 .   ? -3.809  -24.679 -54.750 1.00 57.85 ? 475 HOH A O   1 
HETATM 3806 O O   . HOH H 3 .   ? -14.757 -12.553 -49.588 1.00 42.63 ? 476 HOH A O   1 
HETATM 3807 O O   . HOH H 3 .   ? 1.228   -14.478 -20.967 1.00 19.96 ? 477 HOH A O   1 
HETATM 3808 O O   . HOH H 3 .   ? -3.920  -12.641 -25.364 1.00 27.88 ? 478 HOH A O   1 
HETATM 3809 O O   . HOH H 3 .   ? 3.661   -33.871 -54.893 1.00 49.17 ? 479 HOH A O   1 
HETATM 3810 O O   . HOH H 3 .   ? -0.041  -20.061 -55.661 1.00 30.17 ? 480 HOH A O   1 
HETATM 3811 O O   . HOH H 3 .   ? -10.003 -36.891 -52.518 1.00 38.30 ? 481 HOH A O   1 
HETATM 3812 O O   . HOH H 3 .   ? -21.382 -14.675 -27.997 1.00 36.23 ? 482 HOH A O   1 
HETATM 3813 O O   . HOH H 3 .   ? -12.267 -27.149 -25.743 1.00 46.40 ? 483 HOH A O   1 
HETATM 3814 O O   . HOH H 3 .   ? -13.831 -27.607 -41.964 1.00 23.28 ? 484 HOH A O   1 
HETATM 3815 O O   . HOH H 3 .   ? -18.231 -8.755  -28.309 1.00 49.99 ? 485 HOH A O   1 
HETATM 3816 O O   . HOH H 3 .   ? 0.399   -17.460 -33.778 1.00 38.36 ? 486 HOH A O   1 
HETATM 3817 O O   . HOH H 3 .   ? -7.532  -6.117  -18.970 1.00 46.50 ? 487 HOH A O   1 
HETATM 3818 O O   . HOH H 3 .   ? -19.863 -20.594 -53.942 1.00 44.88 ? 488 HOH A O   1 
HETATM 3819 O O   . HOH H 3 .   ? -24.834 -23.667 -26.695 1.00 50.90 ? 489 HOH A O   1 
HETATM 3820 O O   . HOH H 3 .   ? -7.906  -12.260 -16.907 1.00 32.87 ? 490 HOH A O   1 
HETATM 3821 O O   . HOH H 3 .   ? -6.322  -10.226 -32.122 1.00 59.59 ? 491 HOH A O   1 
HETATM 3822 O O   . HOH H 3 .   ? -1.355  -16.553 -52.237 1.00 49.81 ? 492 HOH A O   1 
HETATM 3823 O O   . HOH H 3 .   ? -12.133 -26.151 -49.985 1.00 43.04 ? 493 HOH A O   1 
HETATM 3824 O O   . HOH H 3 .   ? -17.257 -20.283 -56.504 1.00 50.55 ? 494 HOH A O   1 
HETATM 3825 O O   . HOH H 3 .   ? -4.455  -30.222 -19.368 1.00 32.74 ? 495 HOH A O   1 
HETATM 3826 O O   . HOH H 3 .   ? 14.602  -17.722 -24.322 1.00 21.66 ? 496 HOH A O   1 
HETATM 3827 O O   . HOH H 3 .   ? -15.273 -12.574 -15.154 1.00 52.66 ? 497 HOH A O   1 
HETATM 3828 O O   . HOH H 3 .   ? -10.870 -10.866 -39.815 1.00 31.05 ? 498 HOH A O   1 
HETATM 3829 O O   . HOH H 3 .   ? -7.128  -29.146 -21.648 1.00 69.69 ? 499 HOH A O   1 
HETATM 3830 O O   . HOH H 3 .   ? -19.612 -23.076 -53.116 1.00 38.26 ? 500 HOH A O   1 
HETATM 3831 O O   . HOH H 3 .   ? -21.514 -24.405 -29.748 1.00 35.94 ? 501 HOH A O   1 
HETATM 3832 O O   . HOH H 3 .   ? -13.748 -12.995 -13.123 1.00 35.18 ? 502 HOH A O   1 
HETATM 3833 O O   . HOH H 3 .   ? 3.675   -37.370 -32.782 1.00 36.54 ? 503 HOH A O   1 
HETATM 3834 O O   . HOH H 3 .   ? -19.545 -14.870 -22.866 1.00 40.17 ? 504 HOH A O   1 
HETATM 3835 O O   . HOH H 3 .   ? -25.905 -17.905 -41.360 1.00 69.02 ? 505 HOH A O   1 
HETATM 3836 O O   . HOH H 3 .   ? -18.067 -20.175 -17.237 1.00 46.70 ? 506 HOH A O   1 
HETATM 3837 O O   . HOH H 3 .   ? -2.160  -38.525 -19.993 1.00 45.10 ? 507 HOH A O   1 
HETATM 3838 O O   . HOH H 3 .   ? 13.243  -21.749 -16.749 1.00 31.68 ? 508 HOH A O   1 
HETATM 3839 O O   . HOH H 3 .   ? -16.905 -12.901 -17.393 1.00 60.97 ? 509 HOH A O   1 
HETATM 3840 O O   . HOH H 3 .   ? 3.463   -14.688 -22.657 1.00 35.08 ? 510 HOH A O   1 
HETATM 3841 O O   . HOH H 3 .   ? -20.297 -12.697 -35.211 1.00 54.12 ? 511 HOH A O   1 
HETATM 3842 O O   . HOH H 3 .   ? -5.680  -6.701  -28.779 1.00 51.74 ? 512 HOH A O   1 
HETATM 3843 O O   . HOH I 3 .   ? 6.348   -10.093 -3.853  1.00 26.30 ? 401 HOH B O   1 
HETATM 3844 O O   . HOH I 3 .   ? 4.154   4.321   6.428   1.00 32.75 ? 402 HOH B O   1 
HETATM 3845 O O   . HOH I 3 .   ? -8.637  -23.498 -12.488 1.00 38.46 ? 403 HOH B O   1 
HETATM 3846 O O   . HOH I 3 .   ? 14.722  -2.519  -23.512 1.00 51.04 ? 404 HOH B O   1 
HETATM 3847 O O   . HOH I 3 .   ? -5.795  1.356   5.564   1.00 26.65 ? 405 HOH B O   1 
HETATM 3848 O O   . HOH I 3 .   ? 2.574   -21.851 6.771   1.00 24.47 ? 406 HOH B O   1 
HETATM 3849 O O   . HOH I 3 .   ? -6.349  -30.314 -2.666  1.00 53.55 ? 407 HOH B O   1 
HETATM 3850 O O   . HOH I 3 .   ? 16.160  8.177   4.586   1.00 35.88 ? 408 HOH B O   1 
HETATM 3851 O O   . HOH I 3 .   ? 16.100  -9.797  10.146  1.00 34.28 ? 409 HOH B O   1 
HETATM 3852 O O   . HOH I 3 .   ? -6.705  -4.110  -5.501  1.00 13.88 ? 410 HOH B O   1 
HETATM 3853 O O   . HOH I 3 .   ? -5.962  -11.642 -13.635 1.00 31.63 ? 411 HOH B O   1 
HETATM 3854 O O   . HOH I 3 .   ? -0.379  -21.283 10.106  1.00 26.31 ? 412 HOH B O   1 
HETATM 3855 O O   . HOH I 3 .   ? 3.163   -23.347 0.749   1.00 23.20 ? 413 HOH B O   1 
HETATM 3856 O O   . HOH I 3 .   ? 4.898   -17.052 -21.273 1.00 24.16 ? 414 HOH B O   1 
HETATM 3857 O O   . HOH I 3 .   ? -3.404  0.214   5.023   1.00 14.80 ? 415 HOH B O   1 
HETATM 3858 O O   . HOH I 3 .   ? -17.110 -23.971 0.236   1.00 38.45 ? 416 HOH B O   1 
HETATM 3859 O O   . HOH I 3 .   ? 30.380  -5.168  -1.981  1.00 16.67 ? 417 HOH B O   1 
HETATM 3860 O O   . HOH I 3 .   ? -3.554  -14.049 -16.050 1.00 19.54 ? 418 HOH B O   1 
HETATM 3861 O O   . HOH I 3 .   ? -2.942  -12.022 -11.925 1.00 16.81 ? 419 HOH B O   1 
HETATM 3862 O O   . HOH I 3 .   ? 15.763  8.431   1.611   1.00 41.08 ? 420 HOH B O   1 
HETATM 3863 O O   . HOH I 3 .   ? -5.749  -15.273 21.294  1.00 17.40 ? 421 HOH B O   1 
HETATM 3864 O O   . HOH I 3 .   ? 4.180   -1.910  18.176  1.00 47.00 ? 422 HOH B O   1 
HETATM 3865 O O   . HOH I 3 .   ? 8.864   -6.139  -11.029 1.00 24.51 ? 423 HOH B O   1 
HETATM 3866 O O   . HOH I 3 .   ? -12.910 -6.534  -10.898 1.00 46.41 ? 424 HOH B O   1 
HETATM 3867 O O   . HOH I 3 .   ? 1.187   -27.720 -7.586  1.00 27.55 ? 425 HOH B O   1 
HETATM 3868 O O   . HOH I 3 .   ? -12.553 -1.588  -3.249  1.00 32.78 ? 426 HOH B O   1 
HETATM 3869 O O   . HOH I 3 .   ? 8.470   8.712   4.989   1.00 33.32 ? 427 HOH B O   1 
HETATM 3870 O O   . HOH I 3 .   ? -1.684  7.293   -3.103  1.00 50.49 ? 428 HOH B O   1 
HETATM 3871 O O   . HOH I 3 .   ? 12.465  5.184   12.586  1.00 33.64 ? 429 HOH B O   1 
HETATM 3872 O O   . HOH I 3 .   ? 12.027  -20.838 -14.302 1.00 25.97 ? 430 HOH B O   1 
HETATM 3873 O O   . HOH I 3 .   ? 3.195   -20.481 15.953  1.00 21.96 ? 431 HOH B O   1 
HETATM 3874 O O   . HOH I 3 .   ? -12.755 1.014   0.348   1.00 41.68 ? 432 HOH B O   1 
HETATM 3875 O O   . HOH I 3 .   ? 25.224  -8.785  -3.002  1.00 16.04 ? 433 HOH B O   1 
HETATM 3876 O O   . HOH I 3 .   ? 16.135  1.065   8.489   1.00 21.55 ? 434 HOH B O   1 
HETATM 3877 O O   . HOH I 3 .   ? -3.745  -1.616  0.460   1.00 11.16 ? 435 HOH B O   1 
HETATM 3878 O O   . HOH I 3 .   ? -10.501 -14.340 -9.784  1.00 12.64 ? 436 HOH B O   1 
HETATM 3879 O O   . HOH I 3 .   ? 14.685  6.777   -2.143  1.00 34.09 ? 437 HOH B O   1 
HETATM 3880 O O   . HOH I 3 .   ? 7.767   -23.409 -8.913  1.00 13.69 ? 438 HOH B O   1 
HETATM 3881 O O   . HOH I 3 .   ? 2.071   -21.896 13.617  1.00 27.06 ? 439 HOH B O   1 
HETATM 3882 O O   . HOH I 3 .   ? 1.854   -15.360 -18.346 1.00 14.40 ? 440 HOH B O   1 
HETATM 3883 O O   . HOH I 3 .   ? 11.269  -9.417  14.827  1.00 18.87 ? 441 HOH B O   1 
HETATM 3884 O O   . HOH I 3 .   ? -7.008  2.647   -1.293  1.00 19.60 ? 442 HOH B O   1 
HETATM 3885 O O   . HOH I 3 .   ? -11.543 -7.612  -4.271  1.00 12.09 ? 443 HOH B O   1 
HETATM 3886 O O   . HOH I 3 .   ? 8.574   6.908   9.947   1.00 46.69 ? 444 HOH B O   1 
HETATM 3887 O O   . HOH I 3 .   ? 21.147  5.117   -2.764  1.00 37.85 ? 445 HOH B O   1 
HETATM 3888 O O   . HOH I 3 .   ? -8.758  4.899   -0.670  1.00 36.03 ? 446 HOH B O   1 
HETATM 3889 O O   . HOH I 3 .   ? 6.744   -7.283  -4.051  1.00 30.31 ? 447 HOH B O   1 
HETATM 3890 O O   . HOH I 3 .   ? -5.612  -26.622 -5.394  1.00 30.44 ? 448 HOH B O   1 
HETATM 3891 O O   . HOH I 3 .   ? -16.621 -20.398 -2.396  1.00 33.24 ? 449 HOH B O   1 
HETATM 3892 O O   . HOH I 3 .   ? -1.571  -20.338 7.774   1.00 14.48 ? 450 HOH B O   1 
HETATM 3893 O O   . HOH I 3 .   ? 1.485   -26.007 -11.794 1.00 20.77 ? 451 HOH B O   1 
HETATM 3894 O O   . HOH I 3 .   ? -4.850  -20.384 15.168  1.00 23.76 ? 452 HOH B O   1 
HETATM 3895 O O   . HOH I 3 .   ? -13.683 -13.204 1.005   1.00 16.05 ? 453 HOH B O   1 
HETATM 3896 O O   . HOH I 3 .   ? -0.617  -13.215 -12.718 1.00 30.83 ? 454 HOH B O   1 
HETATM 3897 O O   . HOH I 3 .   ? 1.275   -16.030 19.977  1.00 23.89 ? 455 HOH B O   1 
HETATM 3898 O O   . HOH I 3 .   ? -10.915 -24.435 -2.237  1.00 23.99 ? 456 HOH B O   1 
HETATM 3899 O O   . HOH I 3 .   ? 10.918  -14.943 -18.933 1.00 17.24 ? 457 HOH B O   1 
HETATM 3900 O O   . HOH I 3 .   ? -0.049  -16.534 -13.611 1.00 37.92 ? 458 HOH B O   1 
HETATM 3901 O O   . HOH I 3 .   ? -8.963  -26.521 -2.345  1.00 28.15 ? 459 HOH B O   1 
HETATM 3902 O O   . HOH I 3 .   ? 12.870  -0.247  -3.699  1.00 20.37 ? 460 HOH B O   1 
HETATM 3903 O O   . HOH I 3 .   ? -13.735 -19.264 -14.372 1.00 27.44 ? 461 HOH B O   1 
HETATM 3904 O O   . HOH I 3 .   ? -11.053 0.814   11.919  1.00 31.19 ? 462 HOH B O   1 
HETATM 3905 O O   . HOH I 3 .   ? -15.206 -18.905 -7.814  1.00 28.86 ? 463 HOH B O   1 
HETATM 3906 O O   . HOH I 3 .   ? 22.628  6.042   8.422   1.00 49.05 ? 464 HOH B O   1 
HETATM 3907 O O   . HOH I 3 .   ? 1.853   4.782   5.418   1.00 26.76 ? 465 HOH B O   1 
HETATM 3908 O O   . HOH I 3 .   ? -1.257  -5.554  -13.576 1.00 57.08 ? 466 HOH B O   1 
HETATM 3909 O O   . HOH I 3 .   ? -11.340 -8.079  -13.701 1.00 41.40 ? 467 HOH B O   1 
HETATM 3910 O O   . HOH I 3 .   ? 15.394  -20.231 -16.873 1.00 27.53 ? 468 HOH B O   1 
HETATM 3911 O O   . HOH I 3 .   ? -13.682 -10.044 -4.367  1.00 13.34 ? 469 HOH B O   1 
HETATM 3912 O O   . HOH I 3 .   ? 12.891  -21.763 -12.101 1.00 27.49 ? 470 HOH B O   1 
HETATM 3913 O O   . HOH I 3 .   ? -11.514 -2.499  -5.590  1.00 35.75 ? 471 HOH B O   1 
HETATM 3914 O O   . HOH I 3 .   ? 12.166  1.655   -6.614  1.00 44.28 ? 472 HOH B O   1 
HETATM 3915 O O   . HOH I 3 .   ? 18.473  7.231   3.800   1.00 40.53 ? 473 HOH B O   1 
HETATM 3916 O O   . HOH I 3 .   ? -7.449  3.473   -4.984  1.00 36.83 ? 474 HOH B O   1 
HETATM 3917 O O   . HOH I 3 .   ? 17.494  -9.270  7.665   1.00 22.89 ? 475 HOH B O   1 
HETATM 3918 O O   . HOH I 3 .   ? -16.183 -9.821  -5.482  1.00 33.29 ? 476 HOH B O   1 
HETATM 3919 O O   . HOH I 3 .   ? 14.487  -5.850  -23.485 1.00 33.44 ? 477 HOH B O   1 
HETATM 3920 O O   . HOH I 3 .   ? -12.242 -25.196 0.095   1.00 46.86 ? 478 HOH B O   1 
HETATM 3921 O O   . HOH I 3 .   ? -0.777  4.306   10.775  1.00 29.28 ? 479 HOH B O   1 
HETATM 3922 O O   . HOH I 3 .   ? -14.431 -20.491 -10.036 1.00 34.29 ? 480 HOH B O   1 
HETATM 3923 O O   . HOH I 3 .   ? -11.044 -13.025 -12.260 1.00 19.26 ? 481 HOH B O   1 
HETATM 3924 O O   . HOH I 3 .   ? 14.754  2.111   -4.734  1.00 27.14 ? 482 HOH B O   1 
HETATM 3925 O O   . HOH I 3 .   ? -14.818 -10.443 -8.863  1.00 39.54 ? 483 HOH B O   1 
HETATM 3926 O O   . HOH I 3 .   ? 2.525   -13.023 -16.835 1.00 17.31 ? 484 HOH B O   1 
HETATM 3927 O O   . HOH I 3 .   ? -2.161  -28.138 -8.966  1.00 40.99 ? 485 HOH B O   1 
HETATM 3928 O O   . HOH I 3 .   ? -3.969  -27.624 -7.230  1.00 37.25 ? 486 HOH B O   1 
HETATM 3929 O O   . HOH I 3 .   ? 10.628  9.466   6.786   1.00 48.74 ? 487 HOH B O   1 
HETATM 3930 O O   . HOH I 3 .   ? 5.256   1.291   -3.418  1.00 37.38 ? 488 HOH B O   1 
HETATM 3931 O O   . HOH I 3 .   ? -18.881 -18.482 -1.972  1.00 37.78 ? 489 HOH B O   1 
HETATM 3932 O O   . HOH I 3 .   ? 16.800  7.813   -1.054  1.00 48.60 ? 490 HOH B O   1 
HETATM 3933 O O   . HOH I 3 .   ? -18.441 -8.400  -4.538  1.00 48.87 ? 491 HOH B O   1 
HETATM 3934 O O   . HOH I 3 .   ? 0.165   -12.129 -15.416 1.00 38.76 ? 492 HOH B O   1 
HETATM 3935 O O   . HOH I 3 .   ? 0.119   -26.767 -9.511  1.00 31.78 ? 493 HOH B O   1 
HETATM 3936 O O   . HOH I 3 .   ? -12.727 -24.392 -4.357  1.00 40.86 ? 494 HOH B O   1 
HETATM 3937 O O   . HOH I 3 .   ? -2.485  -11.535 -16.364 1.00 45.34 ? 495 HOH B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . LEU A 4   ? 0.2702 0.8543 0.2093 0.0462  0.0608  -0.0411 4   LEU A N   
2    C CA  . LEU A 4   ? 0.2754 0.8467 0.2180 0.0688  0.0684  -0.0056 4   LEU A CA  
3    C C   . LEU A 4   ? 0.2143 0.7709 0.1630 0.0728  0.0142  0.0121  4   LEU A C   
4    O O   . LEU A 4   ? 0.2363 0.7492 0.1423 0.0568  0.0011  0.0290  4   LEU A O   
5    C CB  . LEU A 4   ? 0.3094 0.8173 0.3035 0.0878  0.0362  0.0152  4   LEU A CB  
6    C CG  . LEU A 4   ? 0.3065 0.8307 0.2857 0.0968  0.0149  0.0146  4   LEU A CG  
7    C CD1 . LEU A 4   ? 0.3282 0.8306 0.3303 0.1114  0.0285  0.0280  4   LEU A CD1 
8    C CD2 . LEU A 4   ? 0.3424 0.8459 0.3446 0.0791  0.0230  0.0145  4   LEU A CD2 
9    N N   . LYS A 5   ? 0.2362 0.7306 0.1658 0.1112  0.0009  -0.0109 5   LYS A N   
10   C CA  . LYS A 5   ? 0.2701 0.7416 0.1630 0.0914  -0.0003 0.0101  5   LYS A CA  
11   C C   . LYS A 5   ? 0.2119 0.7132 0.1712 0.0888  -0.0064 -0.0058 5   LYS A C   
12   O O   . LYS A 5   ? 0.1643 0.7408 0.1458 0.0668  0.0290  -0.0022 5   LYS A O   
13   C CB  . LYS A 5   ? 0.2843 0.7519 0.2502 0.0937  -0.0227 0.0222  5   LYS A CB  
14   C CG  . LYS A 5   ? 0.3792 0.7775 0.3165 0.1060  -0.0448 0.0308  5   LYS A CG  
15   C CD  . LYS A 5   ? 0.4204 0.8186 0.4799 0.1209  -0.0796 0.0287  5   LYS A CD  
16   C CE  . LYS A 5   ? 0.5453 0.8272 0.5445 0.1068  -0.1193 0.0471  5   LYS A CE  
17   N NZ  . LYS A 5   ? 0.5806 0.8421 0.5400 0.0879  -0.1326 0.0396  5   LYS A NZ  
18   N N   . ALA A 6   ? 0.2022 0.6888 0.1562 0.0462  -0.0185 -0.0057 6   ALA A N   
19   C CA  . ALA A 6   ? 0.1963 0.6547 0.1400 0.0400  -0.0029 -0.0238 6   ALA A CA  
20   C C   . ALA A 6   ? 0.1719 0.6309 0.1090 0.0202  0.0336  -0.0303 6   ALA A C   
21   O O   . ALA A 6   ? 0.1851 0.6255 0.1269 0.0086  0.0405  -0.0301 6   ALA A O   
22   C CB  . ALA A 6   ? 0.2449 0.6610 0.2175 0.0452  0.0128  -0.0390 6   ALA A CB  
23   N N   . SER A 7   ? 0.1890 0.6074 0.1413 0.0172  0.0466  -0.0298 7   SER A N   
24   C CA  . SER A 7   ? 0.1872 0.5966 0.0952 0.0317  0.0610  -0.0069 7   SER A CA  
25   C C   . SER A 7   ? 0.1623 0.5519 0.1047 0.0467  0.0610  -0.0036 7   SER A C   
26   O O   . SER A 7   ? 0.1547 0.5390 0.1013 0.0433  0.0722  -0.0074 7   SER A O   
27   C CB  . SER A 7   ? 0.2639 0.6085 0.0762 0.0478  0.0886  -0.0002 7   SER A CB  
28   O OG  . SER A 7   ? 0.2572 0.6840 0.1886 0.0353  0.0811  0.0484  7   SER A OG  
29   N N   . SER A 8   ? 0.1287 0.5338 0.1006 0.0530  0.0582  -0.0077 8   SER A N   
30   C CA  . SER A 8   ? 0.1205 0.5211 0.1014 0.0493  0.0884  0.0036  8   SER A CA  
31   C C   . SER A 8   ? 0.0982 0.4819 0.0887 0.0389  0.0506  0.0093  8   SER A C   
32   O O   . SER A 8   ? 0.1324 0.4784 0.0804 0.0448  0.0404  0.0023  8   SER A O   
33   C CB  . SER A 8   ? 0.1475 0.5424 0.1272 0.0562  0.0744  0.0234  8   SER A CB  
34   O OG  . SER A 8   ? 0.1614 0.5773 0.1259 0.0410  0.0594  0.0372  8   SER A OG  
35   N N   . LEU A 9   ? 0.1094 0.4878 0.1194 0.0210  0.0669  -0.0065 9   LEU A N   
36   C CA  . LEU A 9   ? 0.1297 0.4951 0.1041 0.0127  0.0616  -0.0113 9   LEU A CA  
37   C C   . LEU A 9   ? 0.1295 0.4441 0.0943 0.0120  0.0708  -0.0221 9   LEU A C   
38   O O   . LEU A 9   ? 0.1219 0.4337 0.0906 0.0040  0.0682  -0.0044 9   LEU A O   
39   C CB  . LEU A 9   ? 0.1410 0.5247 0.1510 0.0036  0.0429  -0.0256 9   LEU A CB  
40   C CG  . LEU A 9   ? 0.1872 0.5497 0.1930 0.0039  0.0763  -0.0313 9   LEU A CG  
41   C CD1 . LEU A 9   ? 0.2417 0.5531 0.2473 0.0298  0.0919  -0.0574 9   LEU A CD1 
42   C CD2 . LEU A 9   ? 0.1425 0.5914 0.2548 -0.0141 0.0874  -0.0218 9   LEU A CD2 
43   N N   . ARG A 10  ? 0.1477 0.4350 0.1015 0.0180  0.0731  -0.0229 10  ARG A N   
44   C CA  . ARG A 10  ? 0.1458 0.4206 0.1060 0.0089  0.0964  -0.0154 10  ARG A CA  
45   C C   . ARG A 10  ? 0.1284 0.4043 0.0866 0.0153  0.0766  0.0016  10  ARG A C   
46   O O   . ARG A 10  ? 0.1254 0.3940 0.1138 0.0180  0.0701  0.0130  10  ARG A O   
47   C CB  . ARG A 10  ? 0.1552 0.4594 0.1459 0.0306  0.1088  -0.0454 10  ARG A CB  
48   C CG  . ARG A 10  ? 0.2005 0.4720 0.2066 0.0365  0.1327  -0.0670 10  ARG A CG  
49   C CD  . ARG A 10  ? 0.2244 0.4904 0.2794 0.0272  0.1505  -0.1109 10  ARG A CD  
50   N NE  . ARG A 10  ? 0.2367 0.5018 0.3669 0.0305  0.1238  -0.1437 10  ARG A NE  
51   C CZ  . ARG A 10  ? 0.1903 0.5137 0.3926 0.0271  0.1080  -0.1744 10  ARG A CZ  
52   N NH1 . ARG A 10  ? 0.2302 0.5637 0.4507 0.0306  0.1256  -0.2176 10  ARG A NH1 
53   N NH2 . ARG A 10  ? 0.2599 0.5124 0.4253 0.0351  0.0270  -0.1881 10  ARG A NH2 
54   N N   . ALA A 11  ? 0.0996 0.3955 0.1054 0.0121  0.0819  -0.0026 11  ALA A N   
55   C CA  . ALA A 11  ? 0.0899 0.4021 0.0802 0.0101  0.0785  0.0159  11  ALA A CA  
56   C C   . ALA A 11  ? 0.0761 0.3898 0.0790 0.0224  0.0712  0.0185  11  ALA A C   
57   O O   . ALA A 11  ? 0.0807 0.3704 0.0851 0.0064  0.0623  0.0015  11  ALA A O   
58   C CB  . ALA A 11  ? 0.1045 0.4044 0.1004 0.0076  0.0852  0.0294  11  ALA A CB  
59   N N   . LEU A 12  ? 0.0708 0.3874 0.0805 0.0235  0.0679  -0.0058 12  LEU A N   
60   C CA  . LEU A 12  ? 0.0817 0.3872 0.0933 0.0219  0.0803  0.0008  12  LEU A CA  
61   C C   . LEU A 12  ? 0.0859 0.3632 0.0990 0.0125  0.0778  -0.0052 12  LEU A C   
62   O O   . LEU A 12  ? 0.0793 0.3683 0.0976 0.0176  0.0798  -0.0191 12  LEU A O   
63   C CB  . LEU A 12  ? 0.0893 0.4090 0.1069 0.0390  0.0784  0.0031  12  LEU A CB  
64   C CG  . LEU A 12  ? 0.1165 0.4332 0.1107 0.0545  0.0756  -0.0010 12  LEU A CG  
65   C CD1 . LEU A 12  ? 0.1152 0.4524 0.1360 0.0563  0.0782  0.0152  12  LEU A CD1 
66   C CD2 . LEU A 12  ? 0.1254 0.4279 0.1202 0.0550  0.0737  -0.0087 12  LEU A CD2 
67   N N   . LYS A 13  ? 0.0805 0.3636 0.0891 -0.0009 0.0782  -0.0101 13  LYS A N   
68   C CA  . LYS A 13  ? 0.0831 0.3738 0.0834 -0.0110 0.0766  0.0037  13  LYS A CA  
69   C C   . LYS A 13  ? 0.0675 0.3501 0.0965 -0.0230 0.0720  0.0153  13  LYS A C   
70   O O   . LYS A 13  ? 0.0823 0.3856 0.1191 -0.0180 0.0655  0.0330  13  LYS A O   
71   C CB  . LYS A 13  ? 0.1147 0.3957 0.0870 -0.0172 0.0907  -0.0139 13  LYS A CB  
72   C CG  . LYS A 13  ? 0.1261 0.4183 0.1624 -0.0285 0.0718  -0.0053 13  LYS A CG  
73   C CD  . LYS A 13  ? 0.1395 0.4527 0.2347 -0.0372 0.0544  -0.0098 13  LYS A CD  
74   C CE  . LYS A 13  ? 0.1552 0.4818 0.2709 -0.0314 0.0457  -0.0313 13  LYS A CE  
75   N NZ  . LYS A 13  ? 0.2352 0.5185 0.3569 -0.0564 0.0316  -0.0483 13  LYS A NZ  
76   N N   . LEU A 14  ? 0.0562 0.3313 0.0797 -0.0149 0.0595  0.0095  14  LEU A N   
77   C CA  . LEU A 14  ? 0.0607 0.3174 0.0779 -0.0013 0.0506  -0.0185 14  LEU A CA  
78   C C   . LEU A 14  ? 0.0626 0.3023 0.0774 0.0036  0.0601  -0.0109 14  LEU A C   
79   O O   . LEU A 14  ? 0.0552 0.3034 0.0924 -0.0036 0.0517  -0.0039 14  LEU A O   
80   C CB  . LEU A 14  ? 0.0734 0.3223 0.0933 -0.0164 0.0741  -0.0210 14  LEU A CB  
81   C CG  . LEU A 14  ? 0.0944 0.3206 0.1034 -0.0139 0.0648  -0.0212 14  LEU A CG  
82   C CD1 . LEU A 14  ? 0.1416 0.3406 0.1104 0.0032  0.0683  -0.0382 14  LEU A CD1 
83   C CD2 . LEU A 14  ? 0.0901 0.3139 0.1531 -0.0162 0.0559  -0.0186 14  LEU A CD2 
84   N N   . MET A 15  ? 0.0749 0.3087 0.0651 0.0092  0.0621  -0.0194 15  MET A N   
85   C CA  . MET A 15  ? 0.0794 0.3029 0.0672 0.0065  0.0665  -0.0056 15  MET A CA  
86   C C   . MET A 15  ? 0.0773 0.3160 0.0678 -0.0051 0.0660  0.0028  15  MET A C   
87   O O   . MET A 15  ? 0.0675 0.3121 0.0816 -0.0086 0.0677  -0.0010 15  MET A O   
88   C CB  . MET A 15  ? 0.0921 0.3324 0.0926 0.0249  0.0680  0.0016  15  MET A CB  
89   C CG  . MET A 15  ? 0.1634 0.3768 0.1170 0.0534  0.0452  0.0007  15  MET A CG  
90   S SD  . MET A 15  ? 0.2359 0.4161 0.2538 0.0795  0.0334  0.0147  15  MET A SD  
91   C CE  . MET A 15  ? 0.3325 0.4384 0.2634 0.0437  0.0172  -0.0011 15  MET A CE  
92   N N   . ASP A 16  ? 0.0826 0.3146 0.0688 -0.0135 0.0686  0.0021  16  ASP A N   
93   C CA  . ASP A 16  ? 0.0741 0.3052 0.0845 -0.0015 0.0728  -0.0008 16  ASP A CA  
94   C C   . ASP A 16  ? 0.0728 0.3018 0.1029 -0.0033 0.0801  -0.0017 16  ASP A C   
95   O O   . ASP A 16  ? 0.0988 0.3189 0.1474 -0.0213 0.1055  0.0089  16  ASP A O   
96   C CB  . ASP A 16  ? 0.0678 0.3254 0.1154 -0.0012 0.0817  0.0096  16  ASP A CB  
97   C CG  . ASP A 16  ? 0.0783 0.3295 0.1215 0.0092  0.0910  0.0058  16  ASP A CG  
98   O OD1 . ASP A 16  ? 0.1366 0.3435 0.0935 0.0033  0.0665  -0.0126 16  ASP A OD1 
99   O OD2 . ASP A 16  ? 0.0809 0.3666 0.2192 0.0114  0.0744  0.0325  16  ASP A OD2 
100  N N   . LEU A 17  ? 0.0665 0.3163 0.1037 -0.0028 0.0765  -0.0005 17  LEU A N   
101  C CA  . LEU A 17  ? 0.0686 0.3101 0.1290 0.0142  0.0657  0.0076  17  LEU A CA  
102  C C   . LEU A 17  ? 0.0692 0.3210 0.1350 0.0148  0.0525  0.0132  17  LEU A C   
103  O O   . LEU A 17  ? 0.0995 0.3162 0.1351 0.0120  0.0425  0.0164  17  LEU A O   
104  C CB  . LEU A 17  ? 0.0703 0.3248 0.1325 0.0125  0.0659  0.0174  17  LEU A CB  
105  C CG  . LEU A 17  ? 0.0949 0.3414 0.1765 0.0342  0.0526  0.0128  17  LEU A CG  
106  C CD1 . LEU A 17  ? 0.1376 0.3558 0.1870 0.0445  0.0325  0.0367  17  LEU A CD1 
107  C CD2 . LEU A 17  ? 0.1043 0.3472 0.1735 0.0265  0.0634  -0.0035 17  LEU A CD2 
108  N N   . SER A 18  ? 0.1697 0.3410 0.1843 -0.0069 0.0608  0.0258  18  SER A N   
109  C CA  . SER A 18  ? 0.2013 0.4044 0.2453 -0.0400 0.0629  0.0328  18  SER A CA  
110  C C   . SER A 18  ? 0.2814 0.4055 0.2939 -0.0318 0.0367  0.0544  18  SER A C   
111  O O   . SER A 18  ? 0.4790 0.3640 0.4091 -0.0337 0.0004  0.0777  18  SER A O   
112  C CB  . SER A 18  ? 0.2186 0.4488 0.3131 -0.0487 0.0715  0.0746  18  SER A CB  
113  O OG  . SER A 18  ? 0.3059 0.5230 0.4155 -0.0512 0.0742  0.1259  18  SER A OG  
114  N N   . THR A 25  ? 0.3394 0.5891 0.2756 -0.1041 0.0598  -0.0247 25  THR A N   
115  C CA  . THR A 25  ? 0.3285 0.5366 0.2768 -0.0734 0.0638  -0.0084 25  THR A CA  
116  C C   . THR A 25  ? 0.2810 0.5040 0.2715 -0.0370 0.0598  -0.0294 25  THR A C   
117  O O   . THR A 25  ? 0.2501 0.5138 0.2828 0.0004  0.0549  -0.0322 25  THR A O   
118  C CB  . THR A 25  ? 0.3499 0.5257 0.3392 -0.0852 0.0544  -0.0242 25  THR A CB  
119  O OG1 . THR A 25  ? 0.3665 0.5282 0.3712 -0.0731 0.0341  -0.0102 25  THR A OG1 
120  C CG2 . THR A 25  ? 0.3366 0.5439 0.4111 -0.1004 0.0409  -0.0423 25  THR A CG2 
121  N N   . ASP A 26  ? 0.3406 0.4831 0.2184 -0.0098 0.0351  -0.0116 26  ASP A N   
122  C CA  . ASP A 26  ? 0.3033 0.4520 0.2107 -0.0100 0.0263  -0.0380 26  ASP A CA  
123  C C   . ASP A 26  ? 0.2700 0.4065 0.2343 0.0061  0.0422  -0.0400 26  ASP A C   
124  O O   . ASP A 26  ? 0.2242 0.3788 0.1978 0.0052  0.0769  -0.0429 26  ASP A O   
125  C CB  . ASP A 26  ? 0.3279 0.4889 0.2128 -0.0086 0.0396  -0.0284 26  ASP A CB  
126  C CG  . ASP A 26  ? 0.3904 0.5453 0.2086 -0.0057 0.0409  -0.0137 26  ASP A CG  
127  O OD1 . ASP A 26  ? 0.4110 0.5279 0.3639 0.0447  -0.0411 -0.0029 26  ASP A OD1 
128  O OD2 . ASP A 26  ? 0.5128 0.6977 0.2209 -0.0123 0.0695  -0.0241 26  ASP A OD2 
129  N N   . GLU A 27  ? 0.3032 0.4038 0.2585 0.0231  0.0519  -0.0601 27  GLU A N   
130  C CA  . GLU A 27  ? 0.2918 0.4253 0.2828 0.0371  0.0480  -0.0413 27  GLU A CA  
131  C C   . GLU A 27  ? 0.2652 0.3719 0.2862 0.0409  0.0292  -0.0308 27  GLU A C   
132  O O   . GLU A 27  ? 0.2464 0.3885 0.3160 0.0497  0.0005  -0.0592 27  GLU A O   
133  C CB  . GLU A 27  ? 0.3872 0.4702 0.3512 0.0397  0.0572  -0.0390 27  GLU A CB  
134  C CG  . GLU A 27  ? 0.4736 0.5803 0.4123 0.0454  0.0939  -0.0482 27  GLU A CG  
135  C CD  . GLU A 27  ? 0.5117 0.7140 0.4583 0.0097  0.1101  -0.0240 27  GLU A CD  
136  O OE1 . GLU A 27  ? 0.4366 0.6195 0.4939 -0.0458 0.1562  -0.0623 27  GLU A OE1 
137  O OE2 . GLU A 27  ? 0.7302 0.8274 0.5323 0.0033  0.1743  0.0064  27  GLU A OE2 
138  N N   . LYS A 28  ? 0.2618 0.3444 0.2542 0.0492  0.0616  -0.0256 28  LYS A N   
139  C CA  . LYS A 28  ? 0.2964 0.3606 0.2548 0.0400  0.0409  -0.0021 28  LYS A CA  
140  C C   . LYS A 28  ? 0.2046 0.3452 0.2000 0.0205  0.0519  -0.0149 28  LYS A C   
141  O O   . LYS A 28  ? 0.2081 0.3748 0.1860 0.0138  0.0456  0.0086  28  LYS A O   
142  C CB  . LYS A 28  ? 0.3100 0.3777 0.2793 0.0353  0.0489  0.0177  28  LYS A CB  
143  C CG  . LYS A 28  ? 0.4211 0.4192 0.3734 0.0352  0.0170  0.0034  28  LYS A CG  
144  C CD  . LYS A 28  ? 0.5361 0.4770 0.4819 0.0693  -0.0017 0.0480  28  LYS A CD  
145  C CE  . LYS A 28  ? 0.6226 0.5020 0.5495 0.0776  -0.0221 0.0559  28  LYS A CE  
146  N NZ  . LYS A 28  ? 0.6654 0.5805 0.5889 0.0825  -0.0548 0.0576  28  LYS A NZ  
147  N N   . VAL A 29  ? 0.1472 0.3076 0.2008 0.0251  0.0539  -0.0137 29  VAL A N   
148  C CA  . VAL A 29  ? 0.1612 0.3118 0.1869 0.0218  0.0518  -0.0168 29  VAL A CA  
149  C C   . VAL A 29  ? 0.1538 0.3153 0.1854 0.0331  0.0464  -0.0385 29  VAL A C   
150  O O   . VAL A 29  ? 0.1339 0.3399 0.1843 -0.0011 0.0493  -0.0444 29  VAL A O   
151  C CB  . VAL A 29  ? 0.1547 0.3159 0.1747 0.0096  0.0579  -0.0146 29  VAL A CB  
152  C CG1 . VAL A 29  ? 0.1691 0.3327 0.1685 0.0044  0.0478  -0.0136 29  VAL A CG1 
153  C CG2 . VAL A 29  ? 0.1690 0.3271 0.2377 -0.0270 0.0373  0.0066  29  VAL A CG2 
154  N N   . ILE A 30  ? 0.1521 0.3277 0.2139 0.0390  0.0500  -0.0568 30  ILE A N   
155  C CA  . ILE A 30  ? 0.1530 0.3487 0.2139 0.0359  0.0438  -0.0534 30  ILE A CA  
156  C C   . ILE A 30  ? 0.1531 0.3575 0.2099 0.0494  0.0534  -0.0482 30  ILE A C   
157  O O   . ILE A 30  ? 0.1524 0.3941 0.2043 0.0444  0.1014  -0.0616 30  ILE A O   
158  C CB  . ILE A 30  ? 0.1633 0.3722 0.2419 0.0481  0.0624  -0.0558 30  ILE A CB  
159  C CG1 . ILE A 30  ? 0.2007 0.3948 0.2144 0.0408  0.0726  -0.0498 30  ILE A CG1 
160  C CG2 . ILE A 30  ? 0.1491 0.3990 0.2671 0.0386  0.0877  -0.0454 30  ILE A CG2 
161  C CD1 . ILE A 30  ? 0.2614 0.4088 0.2362 0.0526  0.0525  -0.0657 30  ILE A CD1 
162  N N   . ALA A 31  ? 0.1559 0.3776 0.2328 0.0567  0.0544  -0.0460 31  ALA A N   
163  C CA  . ALA A 31  ? 0.1691 0.3733 0.2464 0.0542  0.0258  -0.0448 31  ALA A CA  
164  C C   . ALA A 31  ? 0.1837 0.3685 0.2306 0.0388  0.0022  -0.0515 31  ALA A C   
165  O O   . ALA A 31  ? 0.1903 0.3811 0.1972 0.0455  -0.0099 -0.0474 31  ALA A O   
166  C CB  . ALA A 31  ? 0.2080 0.3653 0.2648 0.0416  0.0156  -0.0533 31  ALA A CB  
167  N N   . LEU A 32  ? 0.1554 0.3557 0.1902 0.0363  0.0399  -0.0412 32  LEU A N   
168  C CA  . LEU A 32  ? 0.1536 0.3519 0.1609 0.0348  0.0308  -0.0277 32  LEU A CA  
169  C C   . LEU A 32  ? 0.0991 0.3627 0.1274 0.0307  0.0364  -0.0228 32  LEU A C   
170  O O   . LEU A 32  ? 0.1075 0.3820 0.1438 0.0281  0.0438  -0.0108 32  LEU A O   
171  C CB  . LEU A 32  ? 0.1546 0.3562 0.1678 0.0320  0.0351  -0.0199 32  LEU A CB  
172  C CG  . LEU A 32  ? 0.1575 0.3422 0.1906 0.0354  0.0331  -0.0275 32  LEU A CG  
173  C CD1 . LEU A 32  ? 0.2021 0.3716 0.1978 0.0526  0.0368  -0.0362 32  LEU A CD1 
174  C CD2 . LEU A 32  ? 0.1433 0.3347 0.1946 0.0179  0.0347  -0.0307 32  LEU A CD2 
175  N N   . CYS A 33  ? 0.1098 0.3525 0.1186 0.0327  0.0498  -0.0309 33  CYS A N   
176  C CA  . CYS A 33  ? 0.1369 0.3580 0.1173 0.0355  0.0691  -0.0305 33  CYS A CA  
177  C C   . CYS A 33  ? 0.1318 0.3680 0.1472 0.0373  0.0592  -0.0312 33  CYS A C   
178  O O   . CYS A 33  ? 0.0960 0.3980 0.1542 0.0218  0.0786  -0.0430 33  CYS A O   
179  C CB  . CYS A 33  ? 0.1930 0.3452 0.1045 0.0371  0.0510  -0.0480 33  CYS A CB  
180  S SG  . CYS A 33  ? 0.2190 0.3949 0.1521 0.0102  0.0229  -0.0008 33  CYS A SG  
181  N N   . HIS A 34  ? 0.1108 0.3831 0.1607 0.0480  0.0587  -0.0354 34  HIS A N   
182  C CA  . HIS A 34  ? 0.1323 0.4109 0.1902 0.0612  0.0364  -0.0429 34  HIS A CA  
183  C C   . HIS A 34  ? 0.1148 0.4058 0.1960 0.0635  0.0331  -0.0502 34  HIS A C   
184  O O   . HIS A 34  ? 0.0973 0.4451 0.1831 0.0609  0.0464  -0.0532 34  HIS A O   
185  C CB  . HIS A 34  ? 0.1295 0.4288 0.2199 0.0907  0.0352  -0.0624 34  HIS A CB  
186  C CG  . HIS A 34  ? 0.1343 0.4733 0.2240 0.0909  0.0313  -0.0866 34  HIS A CG  
187  N ND1 . HIS A 34  ? 0.2271 0.5073 0.2721 0.0921  0.0480  -0.1125 34  HIS A ND1 
188  C CD2 . HIS A 34  ? 0.1417 0.4857 0.1846 0.1092  0.0594  -0.0828 34  HIS A CD2 
189  C CE1 . HIS A 34  ? 0.1904 0.5021 0.2515 0.1140  0.0683  -0.1210 34  HIS A CE1 
190  N NE2 . HIS A 34  ? 0.1797 0.5133 0.2264 0.1291  0.0534  -0.1283 34  HIS A NE2 
191  N N   . GLN A 35  ? 0.1181 0.3936 0.1691 0.0473  0.0358  -0.0428 35  GLN A N   
192  C CA  . GLN A 35  ? 0.1226 0.4005 0.1792 0.0541  0.0190  -0.0269 35  GLN A CA  
193  C C   . GLN A 35  ? 0.0957 0.3898 0.1458 0.0459  0.0397  -0.0197 35  GLN A C   
194  O O   . GLN A 35  ? 0.1591 0.4094 0.1385 0.0538  0.0432  -0.0379 35  GLN A O   
195  C CB  . GLN A 35  ? 0.1624 0.4117 0.2668 0.0489  0.0283  -0.0264 35  GLN A CB  
196  C CG  . GLN A 35  ? 0.2638 0.4450 0.3243 0.0602  0.0499  -0.0304 35  GLN A CG  
197  C CD  . GLN A 35  ? 0.3294 0.4757 0.5057 0.0523  0.0348  -0.0364 35  GLN A CD  
198  O OE1 . GLN A 35  ? 0.2678 0.6019 0.6255 -0.0009 0.1007  0.0104  35  GLN A OE1 
199  N NE2 . GLN A 35  ? 0.4808 0.5031 0.6476 0.0410  0.0270  -0.0364 35  GLN A NE2 
200  N N   . ALA A 36  ? 0.0762 0.3743 0.1309 0.0437  0.0577  -0.0182 36  ALA A N   
201  C CA  . ALA A 36  ? 0.0763 0.3658 0.1299 0.0250  0.0619  -0.0235 36  ALA A CA  
202  C C   . ALA A 36  ? 0.0680 0.3765 0.1252 0.0367  0.0543  -0.0416 36  ALA A C   
203  O O   . ALA A 36  ? 0.0947 0.3804 0.1240 0.0214  0.0616  -0.0391 36  ALA A O   
204  C CB  . ALA A 36  ? 0.0883 0.3547 0.1201 0.0191  0.0560  -0.0243 36  ALA A CB  
205  N N   . LYS A 37  ? 0.0684 0.4079 0.1079 0.0372  0.0468  -0.0560 37  LYS A N   
206  C CA  . LYS A 37  ? 0.0650 0.4155 0.1179 0.0258  0.0585  -0.0438 37  LYS A CA  
207  C C   . LYS A 37  ? 0.0989 0.4224 0.1284 0.0307  0.0620  -0.0363 37  LYS A C   
208  O O   . LYS A 37  ? 0.1609 0.4321 0.1339 0.0502  0.0677  -0.0323 37  LYS A O   
209  C CB  . LYS A 37  ? 0.0792 0.4278 0.1179 0.0245  0.0589  -0.0436 37  LYS A CB  
210  C CG  . LYS A 37  ? 0.0770 0.4510 0.1258 0.0232  0.0606  -0.0482 37  LYS A CG  
211  C CD  . LYS A 37  ? 0.1042 0.4861 0.1400 0.0139  0.0883  -0.0443 37  LYS A CD  
212  C CE  . LYS A 37  ? 0.1561 0.5195 0.1220 -0.0235 0.0770  -0.0394 37  LYS A CE  
213  N NZ  . LYS A 37  ? 0.1566 0.5766 0.1679 -0.0185 0.1084  -0.0498 37  LYS A NZ  
214  N N   . THR A 38  ? 0.1162 0.4265 0.1112 0.0038  0.0781  -0.0213 38  THR A N   
215  C CA  . THR A 38  ? 0.1061 0.4349 0.1179 -0.0032 0.0797  -0.0142 38  THR A CA  
216  C C   . THR A 38  ? 0.1025 0.4484 0.1210 0.0032  0.0877  -0.0089 38  THR A C   
217  O O   . THR A 38  ? 0.0829 0.4375 0.1127 0.0033  0.0697  -0.0055 38  THR A O   
218  C CB  . THR A 38  ? 0.1035 0.4413 0.1314 -0.0171 0.0870  -0.0250 38  THR A CB  
219  O OG1 . THR A 38  ? 0.0605 0.4661 0.1363 -0.0207 0.0653  -0.0223 38  THR A OG1 
220  C CG2 . THR A 38  ? 0.1039 0.4274 0.1587 -0.0403 0.0826  -0.0265 38  THR A CG2 
221  N N   . PRO A 39  ? 0.0891 0.4655 0.1525 0.0134  0.0795  -0.0020 39  PRO A N   
222  C CA  . PRO A 39  ? 0.0814 0.4603 0.1550 0.0173  0.0637  0.0084  39  PRO A CA  
223  C C   . PRO A 39  ? 0.1100 0.4879 0.1266 0.0106  0.0693  0.0056  39  PRO A C   
224  O O   . PRO A 39  ? 0.1056 0.4661 0.1306 -0.0093 0.0779  0.0152  39  PRO A O   
225  C CB  . PRO A 39  ? 0.1408 0.4829 0.1747 0.0050  0.0557  0.0116  39  PRO A CB  
226  C CG  . PRO A 39  ? 0.1735 0.4875 0.2147 0.0085  0.0481  0.0099  39  PRO A CG  
227  C CD  . PRO A 39  ? 0.1491 0.4767 0.1711 0.0163  0.0645  0.0031  39  PRO A CD  
228  N N   . VAL A 40  ? 0.0701 0.4662 0.1220 0.0056  0.0470  -0.0030 40  VAL A N   
229  C CA  . VAL A 40  ? 0.0700 0.4678 0.1030 -0.0018 0.0640  -0.0083 40  VAL A CA  
230  C C   . VAL A 40  ? 0.0673 0.4492 0.1153 0.0004  0.0598  -0.0274 40  VAL A C   
231  O O   . VAL A 40  ? 0.0686 0.4568 0.1438 0.0049  0.0587  -0.0349 40  VAL A O   
232  C CB  . VAL A 40  ? 0.1082 0.5051 0.1058 -0.0006 0.0672  0.0085  40  VAL A CB  
233  C CG1 . VAL A 40  ? 0.1825 0.5267 0.1399 0.0153  0.0677  0.0137  40  VAL A CG1 
234  C CG2 . VAL A 40  ? 0.1226 0.4984 0.1128 -0.0175 0.0541  0.0218  40  VAL A CG2 
235  N N   . GLY A 41  ? 0.0599 0.4253 0.1226 0.0156  0.0450  -0.0194 41  GLY A N   
236  C CA  . GLY A 41  ? 0.0602 0.4114 0.1153 0.0092  0.0524  -0.0345 41  GLY A CA  
237  C C   . GLY A 41  ? 0.0515 0.3995 0.1019 0.0080  0.0641  -0.0314 41  GLY A C   
238  O O   . GLY A 41  ? 0.0577 0.4151 0.1172 0.0002  0.0574  -0.0347 41  GLY A O   
239  N N   . ASN A 42  ? 0.0462 0.3988 0.1271 0.0131  0.0659  -0.0463 42  ASN A N   
240  C CA  . ASN A 42  ? 0.0601 0.3785 0.1290 0.0111  0.0464  -0.0359 42  ASN A CA  
241  C C   . ASN A 42  ? 0.0717 0.3704 0.0962 0.0113  0.0490  -0.0307 42  ASN A C   
242  O O   . ASN A 42  ? 0.0689 0.3836 0.1000 0.0046  0.0720  -0.0423 42  ASN A O   
243  C CB  . ASN A 42  ? 0.0735 0.4050 0.1249 0.0171  0.0449  -0.0282 42  ASN A CB  
244  C CG  . ASN A 42  ? 0.1029 0.4324 0.1323 0.0097  0.0683  -0.0433 42  ASN A CG  
245  O OD1 . ASN A 42  ? 0.0743 0.4652 0.1731 0.0195  0.0667  -0.0612 42  ASN A OD1 
246  N ND2 . ASN A 42  ? 0.1258 0.4717 0.1920 -0.0037 0.1013  -0.0346 42  ASN A ND2 
247  N N   . THR A 43  ? 0.0443 0.3636 0.1166 0.0211  0.0612  -0.0292 43  THR A N   
248  C CA  . THR A 43  ? 0.0450 0.3496 0.0999 0.0199  0.0578  -0.0188 43  THR A CA  
249  C C   . THR A 43  ? 0.0618 0.3412 0.1108 0.0042  0.0759  -0.0088 43  THR A C   
250  O O   . THR A 43  ? 0.0688 0.3589 0.1108 -0.0170 0.0797  0.0096  43  THR A O   
251  C CB  . THR A 43  ? 0.0823 0.3461 0.1019 0.0292  0.0543  -0.0207 43  THR A CB  
252  O OG1 . THR A 43  ? 0.0732 0.3659 0.0928 0.0111  0.0663  -0.0261 43  THR A OG1 
253  C CG2 . THR A 43  ? 0.0709 0.3490 0.1232 0.0352  0.0621  -0.0117 43  THR A CG2 
254  N N   . ALA A 44  ? 0.0689 0.3279 0.0996 0.0083  0.0746  -0.0274 44  ALA A N   
255  C CA  . ALA A 44  ? 0.0762 0.3108 0.0780 -0.0023 0.0706  -0.0133 44  ALA A CA  
256  C C   . ALA A 44  ? 0.0784 0.2994 0.0823 0.0028  0.0736  -0.0112 44  ALA A C   
257  O O   . ALA A 44  ? 0.1003 0.3148 0.0795 -0.0193 0.0737  -0.0021 44  ALA A O   
258  C CB  . ALA A 44  ? 0.1010 0.3130 0.0633 -0.0030 0.0725  -0.0235 44  ALA A CB  
259  N N   . ALA A 45  ? 0.0719 0.2957 0.0718 -0.0043 0.0628  0.0041  45  ALA A N   
260  C CA  . ALA A 45  ? 0.0789 0.3043 0.0674 -0.0045 0.0665  0.0001  45  ALA A CA  
261  C C   . ALA A 45  ? 0.0667 0.2891 0.0737 0.0016  0.0638  0.0024  45  ALA A C   
262  O O   . ALA A 45  ? 0.0557 0.3063 0.0762 0.0150  0.0570  -0.0079 45  ALA A O   
263  C CB  . ALA A 45  ? 0.0822 0.3082 0.0620 -0.0072 0.0647  0.0071  45  ALA A CB  
264  N N   . ILE A 46  ? 0.0725 0.2976 0.0714 -0.0080 0.0656  -0.0031 46  ILE A N   
265  C CA  . ILE A 46  ? 0.0706 0.3057 0.1087 0.0012  0.0505  0.0024  46  ILE A CA  
266  C C   . ILE A 46  ? 0.0707 0.2910 0.1008 0.0114  0.0516  0.0009  46  ILE A C   
267  O O   . ILE A 46  ? 0.0732 0.3078 0.1460 0.0129  0.0368  0.0157  46  ILE A O   
268  C CB  . ILE A 46  ? 0.1120 0.3207 0.1076 0.0063  0.0498  -0.0022 46  ILE A CB  
269  C CG1 . ILE A 46  ? 0.1508 0.3580 0.1270 0.0119  0.0639  0.0038  46  ILE A CG1 
270  C CG2 . ILE A 46  ? 0.0882 0.3359 0.1183 -0.0037 0.0668  0.0024  46  ILE A CG2 
271  C CD1 . ILE A 46  ? 0.2476 0.3957 0.2021 0.0121  0.0826  0.0015  46  ILE A CD1 
272  N N   . SER A 47  ? 0.0599 0.2784 0.0959 0.0113  0.0503  -0.0017 47  SER A N   
273  C CA  . SER A 47  ? 0.0655 0.3004 0.0899 0.0019  0.0506  0.0002  47  SER A CA  
274  C C   . SER A 47  ? 0.0792 0.2882 0.1143 0.0066  0.0468  0.0016  47  SER A C   
275  O O   . SER A 47  ? 0.1261 0.2900 0.1129 -0.0060 0.0423  0.0002  47  SER A O   
276  C CB  . SER A 47  ? 0.0800 0.3479 0.1089 0.0033  0.0689  -0.0067 47  SER A CB  
277  O OG  . SER A 47  ? 0.1042 0.4276 0.1807 0.0091  0.0681  -0.0030 47  SER A OG  
278  N N   . VAL A 48  ? 0.0711 0.2728 0.1063 0.0031  0.0515  0.0038  48  VAL A N   
279  C CA  . VAL A 48  ? 0.0690 0.2713 0.1059 -0.0019 0.0589  0.0020  48  VAL A CA  
280  C C   . VAL A 48  ? 0.1070 0.2607 0.0875 0.0001  0.0483  0.0095  48  VAL A C   
281  O O   . VAL A 48  ? 0.1031 0.2702 0.1162 0.0024  0.0335  -0.0011 48  VAL A O   
282  C CB  . VAL A 48  ? 0.0883 0.3030 0.1194 0.0197  0.0650  -0.0220 48  VAL A CB  
283  C CG1 . VAL A 48  ? 0.0904 0.3134 0.1575 0.0170  0.0530  -0.0164 48  VAL A CG1 
284  C CG2 . VAL A 48  ? 0.1070 0.3167 0.1252 0.0032  0.0484  -0.0119 48  VAL A CG2 
285  N N   . TYR A 49  ? 0.1045 0.2575 0.0974 -0.0083 0.0586  0.0014  49  TYR A N   
286  C CA  . TYR A 49  ? 0.1268 0.2831 0.1029 0.0007  0.0537  0.0014  49  TYR A CA  
287  C C   . TYR A 49  ? 0.0793 0.2897 0.0888 0.0054  0.0676  -0.0076 49  TYR A C   
288  O O   . TYR A 49  ? 0.0828 0.3056 0.0864 0.0022  0.0707  -0.0137 49  TYR A O   
289  C CB  . TYR A 49  ? 0.1428 0.2888 0.1369 -0.0198 0.0664  0.0064  49  TYR A CB  
290  C CG  . TYR A 49  ? 0.2117 0.3030 0.1739 -0.0357 0.0871  0.0229  49  TYR A CG  
291  C CD1 . TYR A 49  ? 0.2796 0.3219 0.2169 -0.0457 0.1454  0.0333  49  TYR A CD1 
292  C CD2 . TYR A 49  ? 0.3082 0.3407 0.2337 -0.0225 0.1117  0.0343  49  TYR A CD2 
293  C CE1 . TYR A 49  ? 0.2715 0.3696 0.2248 -0.0401 0.1730  0.0418  49  TYR A CE1 
294  C CE2 . TYR A 49  ? 0.3249 0.3762 0.2873 -0.0200 0.1281  0.0728  49  TYR A CE2 
295  C CZ  . TYR A 49  ? 0.3137 0.3955 0.2636 -0.0352 0.1533  0.0507  49  TYR A CZ  
296  O OH  . TYR A 49  ? 0.4528 0.4701 0.3383 -0.0968 0.1521  0.1210  49  TYR A OH  
297  N N   . PRO A 50  ? 0.0725 0.3004 0.0847 0.0056  0.0649  0.0005  50  PRO A N   
298  C CA  . PRO A 50  ? 0.0842 0.2947 0.0765 0.0069  0.0615  -0.0055 50  PRO A CA  
299  C C   . PRO A 50  ? 0.0766 0.2895 0.0830 -0.0043 0.0698  -0.0064 50  PRO A C   
300  O O   . PRO A 50  ? 0.0786 0.3088 0.0771 -0.0079 0.0638  0.0134  50  PRO A O   
301  C CB  . PRO A 50  ? 0.0720 0.2874 0.0959 -0.0015 0.0647  0.0049  50  PRO A CB  
302  C CG  . PRO A 50  ? 0.0624 0.2948 0.0962 -0.0041 0.0615  -0.0003 50  PRO A CG  
303  C CD  . PRO A 50  ? 0.0633 0.2925 0.1029 0.0016  0.0542  -0.0017 50  PRO A CD  
304  N N   . ARG A 51  ? 0.0987 0.2974 0.0667 0.0080  0.0707  -0.0239 51  ARG A N   
305  C CA  . ARG A 51  ? 0.0955 0.3193 0.0801 0.0131  0.0781  -0.0292 51  ARG A CA  
306  C C   . ARG A 51  ? 0.0902 0.3172 0.0798 0.0079  0.0656  -0.0351 51  ARG A C   
307  O O   . ARG A 51  ? 0.1014 0.3469 0.1064 0.0121  0.0863  -0.0404 51  ARG A O   
308  C CB  . ARG A 51  ? 0.1375 0.3394 0.1229 0.0030  0.0697  -0.0427 51  ARG A CB  
309  C CG  . ARG A 51  ? 0.1768 0.3626 0.2195 -0.0179 0.0602  -0.0219 51  ARG A CG  
310  C CD  . ARG A 51  ? 0.2315 0.4048 0.2891 -0.0339 0.0885  -0.0327 51  ARG A CD  
311  N NE  . ARG A 51  ? 0.3525 0.4569 0.3639 -0.0257 0.0878  0.0257  51  ARG A NE  
312  C CZ  . ARG A 51  ? 0.4125 0.5034 0.3527 -0.0427 0.0999  0.0771  51  ARG A CZ  
313  N NH1 . ARG A 51  ? 0.3911 0.5089 0.3864 -0.0740 0.0729  0.0872  51  ARG A NH1 
314  N NH2 . ARG A 51  ? 0.5381 0.5361 0.4375 -0.0252 0.0720  0.1158  51  ARG A NH2 
315  N N   . SER A 52  ? 0.0753 0.2982 0.0791 0.0048  0.0684  -0.0328 52  SER A N   
316  C CA  . SER A 52  ? 0.0979 0.3014 0.1020 0.0129  0.0373  -0.0332 52  SER A CA  
317  C C   . SER A 52  ? 0.0957 0.3065 0.0758 0.0170  0.0481  -0.0071 52  SER A C   
318  O O   . SER A 52  ? 0.0781 0.3142 0.0846 0.0267  0.0541  -0.0250 52  SER A O   
319  C CB  . SER A 52  ? 0.1176 0.3072 0.1566 -0.0023 0.0279  0.0016  52  SER A CB  
320  O OG  . SER A 52  ? 0.1272 0.3139 0.2478 -0.0075 0.0269  0.0103  52  SER A OG  
321  N N   . ILE A 53  ? 0.0938 0.3101 0.0643 0.0047  0.0509  0.0002  53  ILE A N   
322  C CA  . ILE A 53  ? 0.0975 0.3041 0.0557 0.0022  0.0671  0.0075  53  ILE A CA  
323  C C   . ILE A 53  ? 0.0902 0.3173 0.0606 -0.0048 0.0674  -0.0021 53  ILE A C   
324  O O   . ILE A 53  ? 0.0910 0.3296 0.0761 0.0131  0.0748  -0.0228 53  ILE A O   
325  C CB  . ILE A 53  ? 0.1124 0.3098 0.0543 0.0028  0.0711  0.0096  53  ILE A CB  
326  C CG1 . ILE A 53  ? 0.1039 0.3183 0.0619 -0.0024 0.0730  0.0054  53  ILE A CG1 
327  C CG2 . ILE A 53  ? 0.1085 0.3230 0.1008 0.0039  0.0845  0.0103  53  ILE A CG2 
328  C CD1 . ILE A 53  ? 0.0905 0.3317 0.0933 -0.0092 0.0852  0.0061  53  ILE A CD1 
329  N N   . PRO A 54  ? 0.0773 0.3245 0.0747 -0.0048 0.0696  -0.0094 54  PRO A N   
330  C CA  . PRO A 54  ? 0.0729 0.3217 0.0906 -0.0071 0.0749  -0.0088 54  PRO A CA  
331  C C   . PRO A 54  ? 0.1032 0.3229 0.0878 0.0035  0.0789  -0.0197 54  PRO A C   
332  O O   . PRO A 54  ? 0.0871 0.3339 0.1129 -0.0046 0.0851  -0.0279 54  PRO A O   
333  C CB  . PRO A 54  ? 0.0927 0.3241 0.1008 0.0120  0.0673  -0.0129 54  PRO A CB  
334  C CG  . PRO A 54  ? 0.0886 0.3283 0.0667 0.0050  0.0703  -0.0065 54  PRO A CG  
335  C CD  . PRO A 54  ? 0.0877 0.3193 0.0525 -0.0006 0.0610  -0.0112 54  PRO A CD  
336  N N   . ILE A 55  ? 0.0855 0.3155 0.0996 0.0015  0.0759  -0.0067 55  ILE A N   
337  C CA  . ILE A 55  ? 0.0948 0.3401 0.1099 0.0239  0.0750  -0.0198 55  ILE A CA  
338  C C   . ILE A 55  ? 0.0716 0.3211 0.1184 0.0296  0.0737  -0.0298 55  ILE A C   
339  O O   . ILE A 55  ? 0.0681 0.3526 0.1459 0.0133  0.0683  -0.0411 55  ILE A O   
340  C CB  . ILE A 55  ? 0.1181 0.3403 0.1525 0.0155  0.0626  -0.0167 55  ILE A CB  
341  C CG1 . ILE A 55  ? 0.1600 0.3757 0.2103 0.0349  0.0284  -0.0266 55  ILE A CG1 
342  C CG2 . ILE A 55  ? 0.1428 0.3387 0.1539 0.0045  0.0561  -0.0215 55  ILE A CG2 
343  C CD1 . ILE A 55  ? 0.2350 0.4270 0.2457 0.0177  0.0381  -0.0009 55  ILE A CD1 
344  N N   . ALA A 56  ? 0.0667 0.3290 0.0846 0.0153  0.0669  -0.0196 56  ALA A N   
345  C CA  . ALA A 56  ? 0.1089 0.3250 0.0744 0.0178  0.0692  -0.0317 56  ALA A CA  
346  C C   . ALA A 56  ? 0.1041 0.3390 0.0801 0.0140  0.0721  -0.0367 56  ALA A C   
347  O O   . ALA A 56  ? 0.0992 0.3636 0.0773 0.0228  0.0749  -0.0425 56  ALA A O   
348  C CB  . ALA A 56  ? 0.1171 0.3407 0.0754 0.0243  0.0767  -0.0189 56  ALA A CB  
349  N N   . ARG A 57  ? 0.0762 0.3399 0.0926 -0.0071 0.0723  -0.0234 57  ARG A N   
350  C CA  . ARG A 57  ? 0.0975 0.3604 0.1042 -0.0149 0.0945  -0.0155 57  ARG A CA  
351  C C   . ARG A 57  ? 0.0728 0.3664 0.1119 -0.0199 0.0837  -0.0338 57  ARG A C   
352  O O   . ARG A 57  ? 0.0906 0.4011 0.1232 -0.0211 0.0929  -0.0387 57  ARG A O   
353  C CB  . ARG A 57  ? 0.0980 0.3748 0.1424 -0.0181 0.0922  -0.0078 57  ARG A CB  
354  C CG  . ARG A 57  ? 0.1060 0.3922 0.1558 -0.0272 0.1054  -0.0053 57  ARG A CG  
355  C CD  . ARG A 57  ? 0.1167 0.3993 0.2197 -0.0135 0.0785  -0.0106 57  ARG A CD  
356  N NE  . ARG A 57  ? 0.1133 0.3920 0.1965 -0.0144 0.0874  -0.0281 57  ARG A NE  
357  C CZ  . ARG A 57  ? 0.1189 0.3977 0.2004 -0.0106 0.0821  -0.0434 57  ARG A CZ  
358  N NH1 . ARG A 57  ? 0.1658 0.4045 0.1873 -0.0213 0.0724  -0.0413 57  ARG A NH1 
359  N NH2 . ARG A 57  ? 0.1192 0.3908 0.1799 0.0014  0.0879  -0.0578 57  ARG A NH2 
360  N N   . LYS A 58  ? 0.0765 0.3764 0.1212 -0.0095 0.0889  -0.0415 58  LYS A N   
361  C CA  . LYS A 58  ? 0.0749 0.3937 0.1193 0.0161  0.0848  -0.0360 58  LYS A CA  
362  C C   . LYS A 58  ? 0.0811 0.4006 0.1310 0.0162  0.0817  -0.0293 58  LYS A C   
363  O O   . LYS A 58  ? 0.0878 0.4628 0.1138 0.0278  0.0890  -0.0372 58  LYS A O   
364  C CB  . LYS A 58  ? 0.0791 0.3954 0.1399 0.0280  0.0770  -0.0442 58  LYS A CB  
365  C CG  . LYS A 58  ? 0.0924 0.4177 0.1406 0.0351  0.0838  -0.0482 58  LYS A CG  
366  C CD  . LYS A 58  ? 0.1220 0.4455 0.1334 0.0314  0.0923  -0.0557 58  LYS A CD  
367  C CE  . LYS A 58  ? 0.1455 0.4949 0.1714 0.0427  0.1158  -0.0622 58  LYS A CE  
368  N NZ  . LYS A 58  ? 0.2005 0.5350 0.1694 0.0261  0.1041  -0.0556 58  LYS A NZ  
369  N N   . THR A 59  ? 0.0835 0.3847 0.1070 0.0154  0.0841  -0.0414 59  THR A N   
370  C CA  . THR A 59  ? 0.1001 0.3838 0.1362 0.0276  0.0816  -0.0366 59  THR A CA  
371  C C   . THR A 59  ? 0.0927 0.4122 0.1342 0.0247  0.0653  -0.0313 59  THR A C   
372  O O   . THR A 59  ? 0.0771 0.4092 0.1298 0.0311  0.0818  -0.0364 59  THR A O   
373  C CB  . THR A 59  ? 0.1005 0.3678 0.1665 0.0232  0.0639  -0.0328 59  THR A CB  
374  O OG1 . THR A 59  ? 0.1188 0.3605 0.1900 0.0185  0.0575  -0.0339 59  THR A OG1 
375  C CG2 . THR A 59  ? 0.1213 0.3789 0.1895 0.0186  0.0361  -0.0377 59  THR A CG2 
376  N N   . LEU A 60  ? 0.0862 0.4225 0.1190 0.0170  0.0722  -0.0584 60  LEU A N   
377  C CA  . LEU A 60  ? 0.0775 0.4281 0.1151 0.0094  0.0829  -0.0359 60  LEU A CA  
378  C C   . LEU A 60  ? 0.0927 0.4594 0.1055 -0.0143 0.0892  -0.0356 60  LEU A C   
379  O O   . LEU A 60  ? 0.0874 0.4844 0.1419 0.0031  0.0771  -0.0455 60  LEU A O   
380  C CB  . LEU A 60  ? 0.0937 0.4159 0.1025 0.0132  0.0899  -0.0252 60  LEU A CB  
381  C CG  . LEU A 60  ? 0.0825 0.4045 0.1097 0.0075  0.0872  -0.0289 60  LEU A CG  
382  C CD1 . LEU A 60  ? 0.0770 0.4040 0.1331 0.0126  0.0922  -0.0283 60  LEU A CD1 
383  C CD2 . LEU A 60  ? 0.0915 0.4048 0.1100 0.0242  0.0875  -0.0378 60  LEU A CD2 
384  N N   . LYS A 61  ? 0.0851 0.4816 0.1047 -0.0321 0.0880  -0.0321 61  LYS A N   
385  C CA  . LYS A 61  ? 0.0775 0.4908 0.1592 -0.0368 0.0941  -0.0171 61  LYS A CA  
386  C C   . LYS A 61  ? 0.0888 0.4984 0.1279 -0.0285 0.1001  -0.0307 61  LYS A C   
387  O O   . LYS A 61  ? 0.1158 0.4980 0.1839 -0.0526 0.0997  -0.0256 61  LYS A O   
388  C CB  . LYS A 61  ? 0.1098 0.5210 0.1579 -0.0588 0.0983  0.0001  61  LYS A CB  
389  C CG  . LYS A 61  ? 0.1982 0.5313 0.2689 -0.0521 0.0709  0.0092  61  LYS A CG  
390  C CD  . LYS A 61  ? 0.2806 0.5776 0.3197 -0.0587 0.0340  0.0440  61  LYS A CD  
391  C CE  . LYS A 61  ? 0.3820 0.6291 0.3857 -0.0513 0.0479  0.0542  61  LYS A CE  
392  N NZ  . LYS A 61  ? 0.4616 0.6976 0.3906 -0.0679 0.0430  0.0742  61  LYS A NZ  
393  N N   . GLU A 62  ? 0.0719 0.5088 0.1651 -0.0102 0.1009  -0.0567 62  GLU A N   
394  C CA  . GLU A 62  ? 0.0711 0.5547 0.1694 0.0132  0.0981  -0.0694 62  GLU A CA  
395  C C   . GLU A 62  ? 0.0939 0.5510 0.1582 0.0091  0.0945  -0.0564 62  GLU A C   
396  O O   . GLU A 62  ? 0.0821 0.6130 0.1887 -0.0078 0.0752  -0.0748 62  GLU A O   
397  C CB  . GLU A 62  ? 0.1221 0.5703 0.2042 0.0548  0.1145  -0.0988 62  GLU A CB  
398  C CG  . GLU A 62  ? 0.2651 0.6473 0.2366 0.0542  0.1204  -0.0675 62  GLU A CG  
399  C CD  . GLU A 62  ? 0.3933 0.6910 0.2664 0.0655  0.0911  -0.0926 62  GLU A CD  
400  O OE1 . GLU A 62  ? 0.6062 0.6831 0.3534 0.0602  0.1246  -0.0534 62  GLU A OE1 
401  O OE2 . GLU A 62  ? 0.4054 0.8742 0.2412 0.0775  0.1321  -0.0722 62  GLU A OE2 
402  N N   . GLN A 63  ? 0.0793 0.5265 0.1548 0.0385  0.0883  -0.0894 63  GLN A N   
403  C CA  . GLN A 63  ? 0.0814 0.5174 0.1973 0.0321  0.0603  -0.0639 63  GLN A CA  
404  C C   . GLN A 63  ? 0.0720 0.5371 0.1622 0.0164  0.0760  -0.0665 63  GLN A C   
405  O O   . GLN A 63  ? 0.1147 0.5858 0.1843 -0.0428 0.0504  -0.0471 63  GLN A O   
406  C CB  . GLN A 63  ? 0.1241 0.4725 0.1537 0.0517  0.0680  -0.0724 63  GLN A CB  
407  C CG  . GLN A 63  ? 0.0859 0.4583 0.1403 0.0321  0.0722  -0.0357 63  GLN A CG  
408  C CD  . GLN A 63  ? 0.1172 0.4338 0.1599 0.0599  0.1020  -0.0446 63  GLN A CD  
409  O OE1 . GLN A 63  ? 0.1935 0.4398 0.2365 0.0583  0.1317  -0.0371 63  GLN A OE1 
410  N NE2 . GLN A 63  ? 0.0877 0.4409 0.1338 0.0341  0.0930  -0.0484 63  GLN A NE2 
411  N N   . GLY A 64  ? 0.0854 0.5484 0.1674 -0.0346 0.0924  -0.0414 64  GLY A N   
412  C CA  . GLY A 64  ? 0.1005 0.5679 0.1475 -0.0355 0.0950  -0.0268 64  GLY A CA  
413  C C   . GLY A 64  ? 0.0899 0.5313 0.1673 -0.0572 0.0839  -0.0523 64  GLY A C   
414  O O   . GLY A 64  ? 0.0796 0.5810 0.2212 -0.0414 0.0596  -0.0624 64  GLY A O   
415  N N   . THR A 65  ? 0.0780 0.4844 0.1649 -0.0385 0.0918  -0.0411 65  THR A N   
416  C CA  . THR A 65  ? 0.1087 0.4656 0.1537 -0.0176 0.0810  -0.0442 65  THR A CA  
417  C C   . THR A 65  ? 0.0824 0.4363 0.1554 -0.0399 0.0885  -0.0145 65  THR A C   
418  O O   . THR A 65  ? 0.0667 0.4091 0.1673 -0.0265 0.0783  -0.0123 65  THR A O   
419  C CB  . THR A 65  ? 0.0723 0.4708 0.1623 -0.0050 0.0839  -0.0385 65  THR A CB  
420  O OG1 . THR A 65  ? 0.0833 0.4865 0.1576 -0.0152 0.0988  -0.0414 65  THR A OG1 
421  C CG2 . THR A 65  ? 0.1151 0.5007 0.1648 0.0063  0.0713  -0.0201 65  THR A CG2 
422  N N   . PRO A 66  ? 0.0947 0.4570 0.1746 -0.0452 0.1000  0.0232  66  PRO A N   
423  C CA  . PRO A 66  ? 0.1013 0.4454 0.2059 -0.0397 0.0821  0.0295  66  PRO A CA  
424  C C   . PRO A 66  ? 0.1087 0.4266 0.2493 -0.0346 0.0801  0.0189  66  PRO A C   
425  O O   . PRO A 66  ? 0.1277 0.4263 0.2644 -0.0282 0.0470  0.0081  66  PRO A O   
426  C CB  . PRO A 66  ? 0.1436 0.4719 0.2250 -0.0272 0.0992  0.0515  66  PRO A CB  
427  C CG  . PRO A 66  ? 0.1476 0.4774 0.2290 -0.0598 0.1031  0.0650  66  PRO A CG  
428  C CD  . PRO A 66  ? 0.1133 0.4788 0.2113 -0.0483 0.1245  0.0431  66  PRO A CD  
429  N N   . GLU A 67  ? 0.1103 0.4038 0.2576 -0.0536 0.1036  0.0015  67  GLU A N   
430  C CA  . GLU A 67  ? 0.1517 0.4196 0.2560 -0.0526 0.1123  -0.0082 67  GLU A CA  
431  C C   . GLU A 67  ? 0.1126 0.3788 0.2320 -0.0292 0.0861  -0.0188 67  GLU A C   
432  O O   . GLU A 67  ? 0.1230 0.3932 0.2971 -0.0313 0.1171  -0.0536 67  GLU A O   
433  C CB  . GLU A 67  ? 0.1890 0.4798 0.3339 -0.0781 0.1355  -0.0341 67  GLU A CB  
434  C CG  . GLU A 67  ? 0.2965 0.5418 0.4220 -0.1026 0.1391  -0.0084 67  GLU A CG  
435  C CD  . GLU A 67  ? 0.4597 0.6419 0.4741 -0.1118 0.1058  -0.0236 67  GLU A CD  
436  O OE1 . GLU A 67  ? 0.6610 0.7935 0.4998 -0.0430 0.0673  -0.0246 67  GLU A OE1 
437  O OE2 . GLU A 67  ? 0.6176 0.7139 0.6058 -0.1321 0.1270  0.0397  67  GLU A OE2 
438  N N   . ILE A 68  ? 0.0693 0.3536 0.1770 -0.0329 0.0683  -0.0043 68  ILE A N   
439  C CA  . ILE A 68  ? 0.0658 0.3656 0.1195 -0.0228 0.0753  -0.0160 68  ILE A CA  
440  C C   . ILE A 68  ? 0.0632 0.3559 0.1155 -0.0212 0.0699  -0.0261 68  ILE A C   
441  O O   . ILE A 68  ? 0.0828 0.3952 0.1096 -0.0365 0.0762  -0.0294 68  ILE A O   
442  C CB  . ILE A 68  ? 0.0617 0.3736 0.1018 -0.0118 0.0727  -0.0158 68  ILE A CB  
443  C CG1 . ILE A 68  ? 0.0787 0.3770 0.0994 -0.0089 0.0638  -0.0173 68  ILE A CG1 
444  C CG2 . ILE A 68  ? 0.0710 0.3679 0.1215 -0.0225 0.0851  -0.0059 68  ILE A CG2 
445  C CD1 . ILE A 68  ? 0.0856 0.3828 0.0915 -0.0047 0.0684  -0.0194 68  ILE A CD1 
446  N N   . ARG A 69  ? 0.0611 0.3280 0.0847 -0.0191 0.0630  -0.0122 69  ARG A N   
447  C CA  . ARG A 69  ? 0.0775 0.3267 0.0798 -0.0109 0.0670  -0.0044 69  ARG A CA  
448  C C   . ARG A 69  ? 0.0642 0.3102 0.0795 -0.0003 0.0641  -0.0043 69  ARG A C   
449  O O   . ARG A 69  ? 0.0819 0.3149 0.0769 -0.0152 0.0583  0.0154  69  ARG A O   
450  C CB  . ARG A 69  ? 0.0974 0.3385 0.1242 -0.0093 0.0790  -0.0246 69  ARG A CB  
451  C CG  . ARG A 69  ? 0.1380 0.3653 0.1786 -0.0206 0.0752  -0.0289 69  ARG A CG  
452  C CD  . ARG A 69  ? 0.2469 0.4322 0.2267 -0.0081 0.0785  -0.0550 69  ARG A CD  
453  N NE  . ARG A 69  ? 0.3620 0.4767 0.2971 -0.0314 0.0601  -0.0527 69  ARG A NE  
454  C CZ  . ARG A 69  ? 0.4366 0.5464 0.2957 -0.0694 0.0307  -0.0377 69  ARG A CZ  
455  N NH1 . ARG A 69  ? 0.4943 0.5350 0.2922 -0.0771 0.0119  0.0042  69  ARG A NH1 
456  N NH2 . ARG A 69  ? 0.5080 0.5386 0.3679 -0.0826 0.0244  -0.0302 69  ARG A NH2 
457  N N   . ILE A 70  ? 0.0652 0.3107 0.0678 -0.0078 0.0602  -0.0052 70  ILE A N   
458  C CA  . ILE A 70  ? 0.0599 0.3034 0.0717 -0.0077 0.0550  -0.0068 70  ILE A CA  
459  C C   . ILE A 70  ? 0.0656 0.2828 0.0697 -0.0024 0.0577  0.0033  70  ILE A C   
460  O O   . ILE A 70  ? 0.0757 0.2928 0.0748 -0.0072 0.0680  0.0151  70  ILE A O   
461  C CB  . ILE A 70  ? 0.0500 0.3311 0.0901 -0.0134 0.0605  -0.0177 70  ILE A CB  
462  C CG1 . ILE A 70  ? 0.0643 0.3310 0.1048 -0.0020 0.0747  -0.0295 70  ILE A CG1 
463  C CG2 . ILE A 70  ? 0.1063 0.3360 0.0991 -0.0221 0.0570  -0.0288 70  ILE A CG2 
464  C CD1 . ILE A 70  ? 0.0972 0.3348 0.0975 -0.0094 0.0906  -0.0262 70  ILE A CD1 
465  N N   . ALA A 71  ? 0.0512 0.2740 0.0740 -0.0087 0.0524  0.0075  71  ALA A N   
466  C CA  . ALA A 71  ? 0.0611 0.2664 0.0743 -0.0039 0.0609  0.0046  71  ALA A CA  
467  C C   . ALA A 71  ? 0.0746 0.2603 0.0721 0.0065  0.0612  0.0036  71  ALA A C   
468  O O   . ALA A 71  ? 0.0703 0.2767 0.1040 0.0152  0.0697  0.0069  71  ALA A O   
469  C CB  . ALA A 71  ? 0.0845 0.2728 0.0769 -0.0069 0.0669  0.0000  71  ALA A CB  
470  N N   . THR A 72  ? 0.0679 0.2581 0.0810 0.0080  0.0671  -0.0027 72  THR A N   
471  C CA  . THR A 72  ? 0.0624 0.2569 0.0822 -0.0028 0.0652  -0.0029 72  THR A CA  
472  C C   . THR A 72  ? 0.0665 0.2446 0.1026 -0.0012 0.0758  -0.0148 72  THR A C   
473  O O   . THR A 72  ? 0.0745 0.2780 0.1254 0.0046  0.0887  -0.0259 72  THR A O   
474  C CB  . THR A 72  ? 0.0648 0.2648 0.0829 -0.0022 0.0669  -0.0055 72  THR A CB  
475  O OG1 . THR A 72  ? 0.0679 0.2792 0.0920 0.0008  0.0712  -0.0293 72  THR A OG1 
476  C CG2 . THR A 72  ? 0.0897 0.2920 0.0782 -0.0079 0.0692  0.0074  72  THR A CG2 
477  N N   . VAL A 73  ? 0.0572 0.2530 0.0961 -0.0002 0.0669  -0.0207 73  VAL A N   
478  C CA  . VAL A 73  ? 0.0566 0.2479 0.0974 -0.0006 0.0674  -0.0123 73  VAL A CA  
479  C C   . VAL A 73  ? 0.0637 0.2597 0.0861 -0.0006 0.0620  -0.0158 73  VAL A C   
480  O O   . VAL A 73  ? 0.0674 0.2815 0.0852 0.0066  0.0684  -0.0173 73  VAL A O   
481  C CB  . VAL A 73  ? 0.0569 0.2670 0.1070 -0.0119 0.0704  0.0079  73  VAL A CB  
482  C CG1 . VAL A 73  ? 0.0638 0.2815 0.1147 -0.0103 0.0640  0.0133  73  VAL A CG1 
483  C CG2 . VAL A 73  ? 0.0758 0.2638 0.1453 -0.0123 0.0660  0.0199  73  VAL A CG2 
484  N N   . THR A 74  ? 0.0667 0.2740 0.0695 -0.0031 0.0615  0.0073  74  THR A N   
485  C CA  . THR A 74  ? 0.0621 0.2649 0.0730 -0.0083 0.0609  -0.0013 74  THR A CA  
486  C C   . THR A 74  ? 0.0611 0.2696 0.0656 -0.0144 0.0570  -0.0156 74  THR A C   
487  O O   . THR A 74  ? 0.0502 0.2755 0.0614 0.0024  0.0477  -0.0269 74  THR A O   
488  C CB  . THR A 74  ? 0.0566 0.2707 0.0790 -0.0020 0.0604  0.0049  74  THR A CB  
489  O OG1 . THR A 74  ? 0.0827 0.2769 0.0921 -0.0111 0.0748  -0.0042 74  THR A OG1 
490  C CG2 . THR A 74  ? 0.0646 0.2710 0.0758 -0.0021 0.0635  0.0069  74  THR A CG2 
491  N N   . ASN A 75  ? 0.0621 0.2981 0.0721 -0.0119 0.0603  -0.0254 75  ASN A N   
492  C CA  . ASN A 75  ? 0.0423 0.2822 0.0961 -0.0092 0.0567  -0.0260 75  ASN A CA  
493  C C   . ASN A 75  ? 0.0445 0.2790 0.1026 -0.0045 0.0604  -0.0217 75  ASN A C   
494  O O   . ASN A 75  ? 0.0615 0.2870 0.0927 -0.0045 0.0676  -0.0369 75  ASN A O   
495  C CB  . ASN A 75  ? 0.0497 0.2855 0.0910 -0.0132 0.0515  -0.0170 75  ASN A CB  
496  C CG  . ASN A 75  ? 0.0490 0.2988 0.0942 -0.0065 0.0545  -0.0297 75  ASN A CG  
497  O OD1 . ASN A 75  ? 0.0515 0.3224 0.1107 -0.0001 0.0501  -0.0378 75  ASN A OD1 
498  N ND2 . ASN A 75  ? 0.0458 0.3139 0.0866 0.0060  0.0487  -0.0328 75  ASN A ND2 
499  N N   . PHE A 76  ? 0.0709 0.2721 0.1016 -0.0027 0.0746  -0.0071 76  PHE A N   
500  C CA  . PHE A 76  ? 0.0606 0.2669 0.1083 0.0035  0.0741  -0.0073 76  PHE A CA  
501  C C   . PHE A 76  ? 0.0912 0.2761 0.1405 -0.0014 0.0807  -0.0030 76  PHE A C   
502  O O   . PHE A 76  ? 0.1152 0.3098 0.1536 -0.0178 0.0945  -0.0305 76  PHE A O   
503  C CB  . PHE A 76  ? 0.0635 0.2649 0.1173 -0.0051 0.0795  0.0039  76  PHE A CB  
504  C CG  . PHE A 76  ? 0.0623 0.2744 0.1278 -0.0058 0.0819  0.0116  76  PHE A CG  
505  C CD1 . PHE A 76  ? 0.0711 0.2940 0.1305 0.0042  0.0895  0.0169  76  PHE A CD1 
506  C CD2 . PHE A 76  ? 0.0838 0.2887 0.1266 0.0137  0.0964  0.0115  76  PHE A CD2 
507  C CE1 . PHE A 76  ? 0.0673 0.2904 0.1429 0.0112  0.0911  0.0070  76  PHE A CE1 
508  C CE2 . PHE A 76  ? 0.0873 0.3061 0.1284 0.0094  0.0993  0.0181  76  PHE A CE2 
509  C CZ  . PHE A 76  ? 0.0989 0.2962 0.1148 -0.0017 0.0868  0.0351  76  PHE A CZ  
510  N N   . PRO A 77  ? 0.0937 0.2785 0.1442 -0.0126 0.0799  0.0062  77  PRO A N   
511  C CA  . PRO A 77  ? 0.0823 0.2811 0.1461 -0.0210 0.0797  0.0146  77  PRO A CA  
512  C C   . PRO A 77  ? 0.0809 0.2889 0.1200 -0.0274 0.0746  -0.0088 77  PRO A C   
513  O O   . PRO A 77  ? 0.0901 0.3218 0.1067 -0.0381 0.0811  -0.0021 77  PRO A O   
514  C CB  . PRO A 77  ? 0.0993 0.3090 0.1841 -0.0161 0.0751  0.0169  77  PRO A CB  
515  C CG  . PRO A 77  ? 0.1158 0.2857 0.1792 -0.0155 0.0919  0.0236  77  PRO A CG  
516  C CD  . PRO A 77  ? 0.1088 0.2819 0.1696 -0.0375 0.0950  0.0133  77  PRO A CD  
517  N N   . HIS A 78  ? 0.0749 0.2987 0.1048 -0.0212 0.0818  -0.0099 78  HIS A N   
518  C CA  . HIS A 78  ? 0.0678 0.2959 0.1018 -0.0261 0.0745  0.0061  78  HIS A CA  
519  C C   . HIS A 78  ? 0.0743 0.3022 0.0901 -0.0205 0.0749  -0.0033 78  HIS A C   
520  O O   . HIS A 78  ? 0.0781 0.3307 0.1069 -0.0297 0.0840  -0.0076 78  HIS A O   
521  C CB  . HIS A 78  ? 0.0983 0.2983 0.1258 -0.0250 0.0612  -0.0122 78  HIS A CB  
522  C CG  . HIS A 78  ? 0.1043 0.3095 0.1173 -0.0242 0.0651  -0.0149 78  HIS A CG  
523  N ND1 . HIS A 78  ? 0.1130 0.2980 0.0851 -0.0240 0.0696  -0.0169 78  HIS A ND1 
524  C CD2 . HIS A 78  ? 0.1390 0.2991 0.1437 -0.0009 0.0723  -0.0186 78  HIS A CD2 
525  C CE1 . HIS A 78  ? 0.1455 0.2962 0.0893 -0.0267 0.0766  -0.0090 78  HIS A CE1 
526  N NE2 . HIS A 78  ? 0.1484 0.2902 0.1494 -0.0135 0.0468  -0.0058 78  HIS A NE2 
527  N N   . GLY A 79  ? 0.0854 0.3102 0.0844 -0.0057 0.0786  -0.0069 79  GLY A N   
528  C CA  . GLY A 79  ? 0.0812 0.3023 0.0718 -0.0208 0.0696  -0.0050 79  GLY A CA  
529  C C   . GLY A 79  ? 0.0725 0.3053 0.0927 -0.0114 0.0753  -0.0255 79  GLY A C   
530  O O   . GLY A 79  ? 0.0725 0.3335 0.0884 -0.0028 0.0732  -0.0225 79  GLY A O   
531  N N   . ASN A 80  ? 0.0638 0.3242 0.0903 -0.0101 0.0692  -0.0253 80  ASN A N   
532  C CA  . ASN A 80  ? 0.0568 0.3346 0.1061 -0.0126 0.0590  -0.0414 80  ASN A CA  
533  C C   . ASN A 80  ? 0.0671 0.3352 0.0866 -0.0098 0.0516  -0.0354 80  ASN A C   
534  O O   . ASN A 80  ? 0.0809 0.3311 0.0965 0.0016  0.0805  -0.0308 80  ASN A O   
535  C CB  . ASN A 80  ? 0.0579 0.3369 0.1030 -0.0018 0.0673  -0.0448 80  ASN A CB  
536  C CG  . ASN A 80  ? 0.0860 0.3482 0.1400 -0.0116 0.0565  -0.0332 80  ASN A CG  
537  O OD1 . ASN A 80  ? 0.1417 0.3655 0.1698 -0.0198 0.0408  -0.0053 80  ASN A OD1 
538  N ND2 . ASN A 80  ? 0.1580 0.3540 0.1467 -0.0292 0.0565  -0.0369 80  ASN A ND2 
539  N N   . ASP A 81  ? 0.0608 0.3609 0.1310 0.0027  0.0559  -0.0272 81  ASP A N   
540  C CA  . ASP A 81  ? 0.0627 0.3719 0.1130 0.0156  0.0538  -0.0243 81  ASP A CA  
541  C C   . ASP A 81  ? 0.0680 0.3757 0.1085 0.0346  0.0626  -0.0342 81  ASP A C   
542  O O   . ASP A 81  ? 0.1035 0.4134 0.1237 0.0545  0.0738  -0.0254 81  ASP A O   
543  C CB  . ASP A 81  ? 0.0711 0.4240 0.1460 0.0305  0.0687  -0.0184 81  ASP A CB  
544  C CG  . ASP A 81  ? 0.0694 0.4622 0.2124 0.0111  0.0893  -0.0200 81  ASP A CG  
545  O OD1 . ASP A 81  ? 0.1013 0.5340 0.2740 -0.0311 0.0637  -0.0466 81  ASP A OD1 
546  O OD2 . ASP A 81  ? 0.1168 0.5505 0.2778 -0.0117 0.1550  -0.0028 81  ASP A OD2 
547  N N   . ASP A 82  ? 0.0709 0.3491 0.1104 0.0203  0.0655  -0.0378 82  ASP A N   
548  C CA  . ASP A 82  ? 0.0704 0.3493 0.1289 -0.0032 0.0525  -0.0172 82  ASP A CA  
549  C C   . ASP A 82  ? 0.0574 0.3357 0.0823 0.0147  0.0616  -0.0044 82  ASP A C   
550  O O   . ASP A 82  ? 0.0536 0.3406 0.0993 0.0186  0.0577  -0.0149 82  ASP A O   
551  C CB  . ASP A 82  ? 0.0508 0.3723 0.1420 -0.0090 0.0668  -0.0168 82  ASP A CB  
552  C CG  . ASP A 82  ? 0.0532 0.4162 0.1490 -0.0142 0.0647  -0.0296 82  ASP A CG  
553  O OD1 . ASP A 82  ? 0.0803 0.4407 0.1366 -0.0139 0.0881  -0.0243 82  ASP A OD1 
554  O OD2 . ASP A 82  ? 0.1454 0.4594 0.1904 -0.0508 0.0265  -0.0318 82  ASP A OD2 
555  N N   . ILE A 83  ? 0.0809 0.3333 0.1002 0.0139  0.0738  -0.0093 83  ILE A N   
556  C CA  . ILE A 83  ? 0.0823 0.3265 0.0828 0.0100  0.0654  -0.0055 83  ILE A CA  
557  C C   . ILE A 83  ? 0.0589 0.3465 0.0981 0.0194  0.0669  -0.0225 83  ILE A C   
558  O O   . ILE A 83  ? 0.0600 0.3727 0.1359 0.0134  0.0499  -0.0106 83  ILE A O   
559  C CB  . ILE A 83  ? 0.1193 0.3332 0.1088 0.0116  0.0614  -0.0070 83  ILE A CB  
560  C CG1 . ILE A 83  ? 0.1212 0.3650 0.1193 0.0174  0.0625  -0.0158 83  ILE A CG1 
561  C CG2 . ILE A 83  ? 0.1383 0.3378 0.1367 0.0155  0.0511  -0.0049 83  ILE A CG2 
562  C CD1 . ILE A 83  ? 0.1838 0.3717 0.1773 0.0196  0.0808  -0.0216 83  ILE A CD1 
563  N N   . GLU A 84  ? 0.0774 0.3828 0.0914 0.0265  0.0742  -0.0252 84  GLU A N   
564  C CA  . GLU A 84  ? 0.0868 0.4042 0.0934 0.0242  0.0817  -0.0154 84  GLU A CA  
565  C C   . GLU A 84  ? 0.0704 0.3707 0.1045 0.0196  0.0708  -0.0113 84  GLU A C   
566  O O   . GLU A 84  ? 0.0881 0.4034 0.1058 -0.0069 0.0810  -0.0141 84  GLU A O   
567  C CB  . GLU A 84  ? 0.1155 0.4707 0.0807 0.0288  0.0768  -0.0038 84  GLU A CB  
568  C CG  . GLU A 84  ? 0.2090 0.5320 0.1236 0.0597  0.0729  -0.0035 84  GLU A CG  
569  C CD  . GLU A 84  ? 0.3022 0.7027 0.2796 -0.0123 0.0669  0.0266  84  GLU A CD  
570  O OE1 . GLU A 84  ? 0.4726 0.8365 0.3543 -0.0528 0.1042  0.1055  84  GLU A OE1 
571  O OE2 . GLU A 84  ? 0.4736 0.8087 0.4733 -0.0942 0.1325  0.1020  84  GLU A OE2 
572  N N   . ILE A 85  ? 0.0622 0.3647 0.0797 0.0221  0.0615  -0.0203 85  ILE A N   
573  C CA  . ILE A 85  ? 0.0836 0.3407 0.0880 0.0086  0.0663  -0.0359 85  ILE A CA  
574  C C   . ILE A 85  ? 0.0822 0.3429 0.0818 -0.0026 0.0659  -0.0212 85  ILE A C   
575  O O   . ILE A 85  ? 0.0889 0.3460 0.0830 0.0056  0.0721  -0.0240 85  ILE A O   
576  C CB  . ILE A 85  ? 0.0835 0.3395 0.1251 -0.0142 0.0736  -0.0360 85  ILE A CB  
577  C CG1 . ILE A 85  ? 0.0733 0.3558 0.1402 -0.0157 0.0869  -0.0418 85  ILE A CG1 
578  C CG2 . ILE A 85  ? 0.0999 0.3346 0.1739 -0.0194 0.0706  -0.0500 85  ILE A CG2 
579  C CD1 . ILE A 85  ? 0.1238 0.3722 0.1766 -0.0264 0.0552  -0.0422 85  ILE A CD1 
580  N N   . ALA A 86  ? 0.0628 0.3271 0.0868 -0.0038 0.0669  -0.0244 86  ALA A N   
581  C CA  . ALA A 86  ? 0.0776 0.3199 0.0770 -0.0029 0.0597  -0.0154 86  ALA A CA  
582  C C   . ALA A 86  ? 0.0628 0.3061 0.0754 0.0133  0.0592  -0.0200 86  ALA A C   
583  O O   . ALA A 86  ? 0.0631 0.3316 0.0804 0.0073  0.0635  -0.0234 86  ALA A O   
584  C CB  . ALA A 86  ? 0.0779 0.3482 0.0812 0.0022  0.0731  -0.0063 86  ALA A CB  
585  N N   . LEU A 87  ? 0.0682 0.3076 0.0900 0.0058  0.0590  -0.0057 87  LEU A N   
586  C CA  . LEU A 87  ? 0.1018 0.3002 0.0740 0.0086  0.0626  -0.0093 87  LEU A CA  
587  C C   . LEU A 87  ? 0.0718 0.3022 0.0834 0.0040  0.0599  -0.0138 87  LEU A C   
588  O O   . LEU A 87  ? 0.0678 0.3093 0.0807 -0.0072 0.0491  -0.0061 87  LEU A O   
589  C CB  . LEU A 87  ? 0.1218 0.3231 0.0869 0.0222  0.0573  -0.0024 87  LEU A CB  
590  C CG  . LEU A 87  ? 0.1261 0.3364 0.0831 0.0291  0.0705  -0.0064 87  LEU A CG  
591  C CD1 . LEU A 87  ? 0.1446 0.3271 0.0920 0.0288  0.0669  -0.0104 87  LEU A CD1 
592  C CD2 . LEU A 87  ? 0.1590 0.3506 0.1279 0.0357  0.0475  0.0043  87  LEU A CD2 
593  N N   . ALA A 88  ? 0.0651 0.3092 0.0858 0.0108  0.0665  -0.0230 88  ALA A N   
594  C CA  . ALA A 88  ? 0.0937 0.3098 0.0539 0.0116  0.0625  -0.0211 88  ALA A CA  
595  C C   . ALA A 88  ? 0.0838 0.2987 0.0578 0.0068  0.0622  -0.0156 88  ALA A C   
596  O O   . ALA A 88  ? 0.0642 0.3157 0.0908 0.0061  0.0662  -0.0143 88  ALA A O   
597  C CB  . ALA A 88  ? 0.0905 0.3099 0.0837 0.0081  0.0538  -0.0279 88  ALA A CB  
598  N N   . GLU A 89  ? 0.0704 0.2994 0.0603 0.0048  0.0585  -0.0075 89  GLU A N   
599  C CA  . GLU A 89  ? 0.0694 0.2757 0.0672 0.0089  0.0611  -0.0132 89  GLU A CA  
600  C C   . GLU A 89  ? 0.0514 0.2742 0.0952 0.0078  0.0619  -0.0214 89  GLU A C   
601  O O   . GLU A 89  ? 0.0621 0.2964 0.0763 0.0057  0.0616  -0.0168 89  GLU A O   
602  C CB  . GLU A 89  ? 0.0814 0.2837 0.0725 -0.0037 0.0630  -0.0111 89  GLU A CB  
603  C CG  . GLU A 89  ? 0.0980 0.2941 0.0981 -0.0125 0.0785  -0.0164 89  GLU A CG  
604  C CD  . GLU A 89  ? 0.1398 0.3026 0.1123 -0.0303 0.0968  -0.0205 89  GLU A CD  
605  O OE1 . GLU A 89  ? 0.2248 0.3643 0.1120 -0.0680 0.0856  -0.0242 89  GLU A OE1 
606  O OE2 . GLU A 89  ? 0.1572 0.3329 0.1184 -0.0467 0.0903  -0.0301 89  GLU A OE2 
607  N N   . THR A 90  ? 0.0607 0.2595 0.0797 0.0071  0.0566  -0.0229 90  THR A N   
608  C CA  . THR A 90  ? 0.0867 0.2666 0.0626 0.0064  0.0548  -0.0245 90  THR A CA  
609  C C   . THR A 90  ? 0.0871 0.2750 0.0612 -0.0028 0.0491  -0.0191 90  THR A C   
610  O O   . THR A 90  ? 0.0858 0.2859 0.0590 -0.0069 0.0645  -0.0155 90  THR A O   
611  C CB  . THR A 90  ? 0.1065 0.2859 0.0531 0.0027  0.0668  -0.0233 90  THR A CB  
612  O OG1 . THR A 90  ? 0.1079 0.2971 0.0612 0.0055  0.0636  -0.0112 90  THR A OG1 
613  C CG2 . THR A 90  ? 0.1116 0.2794 0.0544 0.0080  0.0667  -0.0210 90  THR A CG2 
614  N N   . ARG A 91  ? 0.0635 0.2854 0.0698 -0.0015 0.0602  0.0032  91  ARG A N   
615  C CA  . ARG A 91  ? 0.0983 0.2902 0.0504 0.0037  0.0637  0.0051  91  ARG A CA  
616  C C   . ARG A 91  ? 0.0732 0.2695 0.0701 -0.0073 0.0551  -0.0052 91  ARG A C   
617  O O   . ARG A 91  ? 0.0796 0.2794 0.0735 -0.0016 0.0693  -0.0226 91  ARG A O   
618  C CB  . ARG A 91  ? 0.0959 0.3065 0.0640 0.0254  0.0613  -0.0005 91  ARG A CB  
619  C CG  . ARG A 91  ? 0.1302 0.3208 0.0926 0.0319  0.0660  0.0204  91  ARG A CG  
620  C CD  . ARG A 91  ? 0.1658 0.3689 0.1442 0.0449  0.0489  0.0205  91  ARG A CD  
621  N NE  . ARG A 91  ? 0.1907 0.4074 0.1617 0.0744  0.0548  0.0414  91  ARG A NE  
622  C CZ  . ARG A 91  ? 0.2405 0.4640 0.2032 0.0793  0.0257  0.0626  91  ARG A CZ  
623  N NH1 . ARG A 91  ? 0.2958 0.5125 0.3358 0.0744  -0.0105 0.0406  91  ARG A NH1 
624  N NH2 . ARG A 91  ? 0.2647 0.4947 0.2866 0.1115  0.0477  0.0706  91  ARG A NH2 
625  N N   . ALA A 92  ? 0.0687 0.2680 0.0625 -0.0075 0.0591  -0.0122 92  ALA A N   
626  C CA  . ALA A 92  ? 0.0826 0.2672 0.0598 -0.0025 0.0628  -0.0236 92  ALA A CA  
627  C C   . ALA A 92  ? 0.0662 0.2610 0.0619 -0.0155 0.0577  -0.0161 92  ALA A C   
628  O O   . ALA A 92  ? 0.0581 0.2969 0.0744 -0.0226 0.0578  0.0064  92  ALA A O   
629  C CB  . ALA A 92  ? 0.0711 0.2710 0.0876 0.0053  0.0704  -0.0292 92  ALA A CB  
630  N N   . ALA A 93  ? 0.0809 0.2691 0.0543 -0.0198 0.0598  -0.0220 93  ALA A N   
631  C CA  . ALA A 93  ? 0.0845 0.2654 0.0559 -0.0175 0.0622  -0.0186 93  ALA A CA  
632  C C   . ALA A 93  ? 0.0753 0.2688 0.0582 -0.0176 0.0596  -0.0058 93  ALA A C   
633  O O   . ALA A 93  ? 0.0670 0.2999 0.0733 -0.0140 0.0637  -0.0097 93  ALA A O   
634  C CB  . ALA A 93  ? 0.0787 0.2730 0.0568 -0.0105 0.0604  -0.0147 93  ALA A CB  
635  N N   . ILE A 94  ? 0.0728 0.2653 0.0597 -0.0168 0.0595  -0.0107 94  ILE A N   
636  C CA  . ILE A 94  ? 0.1070 0.2674 0.0563 -0.0285 0.0680  -0.0057 94  ILE A CA  
637  C C   . ILE A 94  ? 0.0762 0.2813 0.0566 -0.0312 0.0588  -0.0113 94  ILE A C   
638  O O   . ILE A 94  ? 0.0762 0.3205 0.0649 -0.0401 0.0562  -0.0073 94  ILE A O   
639  C CB  . ILE A 94  ? 0.1295 0.2751 0.0602 -0.0268 0.0708  -0.0070 94  ILE A CB  
640  C CG1 . ILE A 94  ? 0.1179 0.2778 0.0676 -0.0243 0.0733  -0.0136 94  ILE A CG1 
641  C CG2 . ILE A 94  ? 0.1425 0.2879 0.0726 -0.0296 0.0802  -0.0007 94  ILE A CG2 
642  C CD1 . ILE A 94  ? 0.1351 0.2860 0.1050 -0.0061 0.0814  -0.0150 94  ILE A CD1 
643  N N   . ALA A 95  ? 0.0825 0.2993 0.0509 -0.0336 0.0576  -0.0088 95  ALA A N   
644  C CA  . ALA A 95  ? 0.0903 0.3040 0.0618 -0.0325 0.0669  -0.0016 95  ALA A CA  
645  C C   . ALA A 95  ? 0.0836 0.3136 0.0789 -0.0293 0.0736  -0.0010 95  ALA A C   
646  O O   . ALA A 95  ? 0.1060 0.3376 0.0811 -0.0331 0.0859  -0.0138 95  ALA A O   
647  C CB  . ALA A 95  ? 0.0986 0.3121 0.0608 -0.0194 0.0707  -0.0054 95  ALA A CB  
648  N N   . TYR A 96  ? 0.0932 0.3080 0.0742 -0.0112 0.0767  -0.0157 96  TYR A N   
649  C CA  . TYR A 96  ? 0.0960 0.2910 0.0646 -0.0090 0.0720  -0.0181 96  TYR A CA  
650  C C   . TYR A 96  ? 0.0926 0.2997 0.0882 -0.0002 0.0605  -0.0336 96  TYR A C   
651  O O   . TYR A 96  ? 0.0848 0.3416 0.1325 -0.0001 0.0570  -0.0595 96  TYR A O   
652  C CB  . TYR A 96  ? 0.0804 0.2875 0.0648 -0.0059 0.0657  -0.0126 96  TYR A CB  
653  C CG  . TYR A 96  ? 0.0693 0.2804 0.0778 -0.0053 0.0669  -0.0173 96  TYR A CG  
654  C CD1 . TYR A 96  ? 0.0844 0.2804 0.0777 -0.0023 0.0744  -0.0145 96  TYR A CD1 
655  C CD2 . TYR A 96  ? 0.0766 0.2956 0.0709 0.0008  0.0672  -0.0076 96  TYR A CD2 
656  C CE1 . TYR A 96  ? 0.0907 0.2682 0.0846 -0.0005 0.0812  -0.0079 96  TYR A CE1 
657  C CE2 . TYR A 96  ? 0.0735 0.2730 0.0841 0.0113  0.0712  -0.0131 96  TYR A CE2 
658  C CZ  . TYR A 96  ? 0.0852 0.2723 0.0781 -0.0038 0.0752  -0.0106 96  TYR A CZ  
659  O OH  . TYR A 96  ? 0.1022 0.2961 0.0958 -0.0059 0.0773  -0.0074 96  TYR A OH  
660  N N   . GLY A 97  ? 0.0731 0.3060 0.0698 -0.0207 0.0644  -0.0396 97  GLY A N   
661  C CA  . GLY A 97  ? 0.0998 0.2943 0.0660 -0.0236 0.0596  -0.0289 97  GLY A CA  
662  C C   . GLY A 97  ? 0.0985 0.3013 0.0668 -0.0334 0.0680  -0.0210 97  GLY A C   
663  O O   . GLY A 97  ? 0.0742 0.3186 0.0898 -0.0316 0.0676  -0.0139 97  GLY A O   
664  N N   . ALA A 98  ? 0.0841 0.2883 0.0636 -0.0296 0.0536  -0.0120 98  ALA A N   
665  C CA  . ALA A 98  ? 0.0753 0.2686 0.0646 -0.0224 0.0633  -0.0135 98  ALA A CA  
666  C C   . ALA A 98  ? 0.0816 0.2650 0.0620 -0.0216 0.0643  -0.0061 98  ALA A C   
667  O O   . ALA A 98  ? 0.0942 0.2728 0.0828 -0.0118 0.0717  -0.0093 98  ALA A O   
668  C CB  . ALA A 98  ? 0.0672 0.2770 0.0846 -0.0325 0.0639  -0.0154 98  ALA A CB  
669  N N   . ASP A 99  ? 0.0762 0.2686 0.0698 -0.0069 0.0516  -0.0085 99  ASP A N   
670  C CA  . ASP A 99  ? 0.0747 0.2659 0.0752 -0.0179 0.0681  -0.0028 99  ASP A CA  
671  C C   . ASP A 99  ? 0.0833 0.2593 0.0582 -0.0200 0.0629  -0.0051 99  ASP A C   
672  O O   . ASP A 99  ? 0.0979 0.2749 0.0691 -0.0125 0.0755  0.0010  99  ASP A O   
673  C CB  . ASP A 99  ? 0.0754 0.2822 0.0803 -0.0221 0.0706  -0.0014 99  ASP A CB  
674  C CG  . ASP A 99  ? 0.0788 0.2886 0.1022 -0.0254 0.0812  0.0079  99  ASP A CG  
675  O OD1 . ASP A 99  ? 0.1210 0.3245 0.1233 -0.0018 0.0905  0.0216  99  ASP A OD1 
676  O OD2 . ASP A 99  ? 0.1083 0.3100 0.1000 -0.0272 0.0824  0.0052  99  ASP A OD2 
677  N N   . GLU A 100 ? 0.0718 0.2582 0.0717 -0.0194 0.0652  -0.0084 100 GLU A N   
678  C CA  . GLU A 100 ? 0.0780 0.2594 0.0662 -0.0175 0.0655  -0.0127 100 GLU A CA  
679  C C   . GLU A 100 ? 0.0827 0.2414 0.0570 -0.0127 0.0620  -0.0011 100 GLU A C   
680  O O   . GLU A 100 ? 0.0705 0.2333 0.0733 -0.0204 0.0652  -0.0095 100 GLU A O   
681  C CB  . GLU A 100 ? 0.0699 0.2840 0.0707 -0.0254 0.0618  -0.0144 100 GLU A CB  
682  C CG  . GLU A 100 ? 0.0956 0.3018 0.0778 -0.0341 0.0489  -0.0121 100 GLU A CG  
683  C CD  . GLU A 100 ? 0.1180 0.3237 0.0819 -0.0364 0.0458  -0.0110 100 GLU A CD  
684  O OE1 . GLU A 100 ? 0.0979 0.3391 0.0986 -0.0418 0.0399  0.0005  100 GLU A OE1 
685  O OE2 . GLU A 100 ? 0.1606 0.3757 0.0798 -0.0865 0.0484  0.0109  100 GLU A OE2 
686  N N   . VAL A 101 ? 0.0779 0.2342 0.0567 -0.0024 0.0598  -0.0106 101 VAL A N   
687  C CA  . VAL A 101 ? 0.0793 0.2442 0.0633 -0.0115 0.0645  -0.0074 101 VAL A CA  
688  C C   . VAL A 101 ? 0.0790 0.2455 0.0746 -0.0044 0.0704  -0.0106 101 VAL A C   
689  O O   . VAL A 101 ? 0.0919 0.2470 0.0754 -0.0099 0.0769  -0.0071 101 VAL A O   
690  C CB  . VAL A 101 ? 0.0849 0.2547 0.0670 -0.0116 0.0687  0.0012  101 VAL A CB  
691  C CG1 . VAL A 101 ? 0.0917 0.2845 0.1059 -0.0196 0.0547  0.0050  101 VAL A CG1 
692  C CG2 . VAL A 101 ? 0.0929 0.2500 0.0490 -0.0001 0.0607  0.0027  101 VAL A CG2 
693  N N   . ASP A 102 ? 0.0784 0.2477 0.0866 -0.0012 0.0756  -0.0149 102 ASP A N   
694  C CA  . ASP A 102 ? 0.0768 0.2604 0.0840 -0.0157 0.0739  -0.0083 102 ASP A CA  
695  C C   . ASP A 102 ? 0.0768 0.2559 0.0759 -0.0131 0.0700  -0.0098 102 ASP A C   
696  O O   . ASP A 102 ? 0.0558 0.2610 0.0992 -0.0242 0.0663  -0.0021 102 ASP A O   
697  C CB  . ASP A 102 ? 0.0698 0.2612 0.0923 -0.0142 0.0731  0.0037  102 ASP A CB  
698  C CG  . ASP A 102 ? 0.0761 0.2828 0.1070 -0.0090 0.0675  0.0060  102 ASP A CG  
699  O OD1 . ASP A 102 ? 0.1004 0.2851 0.1142 -0.0137 0.0693  0.0063  102 ASP A OD1 
700  O OD2 . ASP A 102 ? 0.0965 0.3191 0.1561 0.0133  0.0584  0.0273  102 ASP A OD2 
701  N N   . VAL A 103 ? 0.0643 0.2458 0.0873 -0.0104 0.0685  -0.0171 103 VAL A N   
702  C CA  . VAL A 103 ? 0.0740 0.2565 0.0736 -0.0153 0.0675  -0.0155 103 VAL A CA  
703  C C   . VAL A 103 ? 0.0668 0.2449 0.0595 -0.0034 0.0557  -0.0245 103 VAL A C   
704  O O   . VAL A 103 ? 0.0725 0.2686 0.0640 -0.0256 0.0617  -0.0291 103 VAL A O   
705  C CB  . VAL A 103 ? 0.0873 0.2633 0.0563 -0.0113 0.0636  -0.0105 103 VAL A CB  
706  C CG1 . VAL A 103 ? 0.1024 0.2606 0.0977 -0.0086 0.0629  0.0018  103 VAL A CG1 
707  C CG2 . VAL A 103 ? 0.0871 0.2921 0.0641 -0.0045 0.0681  -0.0150 103 VAL A CG2 
708  N N   . VAL A 104 ? 0.0749 0.2609 0.0602 -0.0041 0.0604  -0.0160 104 VAL A N   
709  C CA  . VAL A 104 ? 0.0684 0.2738 0.0646 -0.0017 0.0600  -0.0076 104 VAL A CA  
710  C C   . VAL A 104 ? 0.0565 0.2768 0.0550 -0.0011 0.0490  -0.0158 104 VAL A C   
711  O O   . VAL A 104 ? 0.0535 0.3027 0.0668 0.0058  0.0519  -0.0251 104 VAL A O   
712  C CB  . VAL A 104 ? 0.0528 0.2702 0.0830 -0.0029 0.0595  -0.0130 104 VAL A CB  
713  C CG1 . VAL A 104 ? 0.0621 0.2851 0.0850 -0.0006 0.0661  -0.0106 104 VAL A CG1 
714  C CG2 . VAL A 104 ? 0.0623 0.2511 0.0915 0.0046  0.0688  -0.0045 104 VAL A CG2 
715  N N   . PHE A 105 ? 0.0625 0.3028 0.0586 0.0011  0.0538  -0.0134 105 PHE A N   
716  C CA  . PHE A 105 ? 0.0626 0.2833 0.0737 0.0043  0.0610  -0.0144 105 PHE A CA  
717  C C   . PHE A 105 ? 0.0761 0.2836 0.0752 -0.0004 0.0595  -0.0267 105 PHE A C   
718  O O   . PHE A 105 ? 0.0725 0.2790 0.0947 -0.0085 0.0765  -0.0100 105 PHE A O   
719  C CB  . PHE A 105 ? 0.0660 0.2889 0.0851 0.0065  0.0677  -0.0171 105 PHE A CB  
720  C CG  . PHE A 105 ? 0.0698 0.2827 0.0919 0.0174  0.0687  -0.0234 105 PHE A CG  
721  C CD1 . PHE A 105 ? 0.0789 0.2927 0.1218 0.0184  0.0697  -0.0272 105 PHE A CD1 
722  C CD2 . PHE A 105 ? 0.0934 0.2971 0.1190 0.0059  0.0873  -0.0154 105 PHE A CD2 
723  C CE1 . PHE A 105 ? 0.0902 0.2887 0.1436 0.0209  0.0601  -0.0234 105 PHE A CE1 
724  C CE2 . PHE A 105 ? 0.0944 0.3116 0.1413 0.0239  0.0695  -0.0305 105 PHE A CE2 
725  C CZ  . PHE A 105 ? 0.0673 0.3091 0.1539 0.0381  0.0695  -0.0474 105 PHE A CZ  
726  N N   . PRO A 106 ? 0.0624 0.3001 0.0953 0.0014  0.0702  -0.0166 106 PRO A N   
727  C CA  . PRO A 106 ? 0.0781 0.3061 0.0920 -0.0049 0.0642  -0.0107 106 PRO A CA  
728  C C   . PRO A 106 ? 0.0652 0.3111 0.0872 0.0234  0.0578  -0.0143 106 PRO A C   
729  O O   . PRO A 106 ? 0.0658 0.3321 0.0897 0.0265  0.0689  -0.0024 106 PRO A O   
730  C CB  . PRO A 106 ? 0.0685 0.3241 0.0898 0.0029  0.0672  -0.0181 106 PRO A CB  
731  C CG  . PRO A 106 ? 0.0673 0.3222 0.0878 -0.0009 0.0665  -0.0007 106 PRO A CG  
732  C CD  . PRO A 106 ? 0.0617 0.3065 0.0880 -0.0041 0.0672  -0.0043 106 PRO A CD  
733  N N   . TYR A 107 ? 0.0669 0.3062 0.0964 0.0222  0.0657  -0.0060 107 TYR A N   
734  C CA  . TYR A 107 ? 0.0673 0.3100 0.0957 0.0025  0.0588  -0.0078 107 TYR A CA  
735  C C   . TYR A 107 ? 0.0677 0.3316 0.1070 0.0037  0.0780  -0.0169 107 TYR A C   
736  O O   . TYR A 107 ? 0.0680 0.3697 0.1183 0.0056  0.0826  -0.0137 107 TYR A O   
737  C CB  . TYR A 107 ? 0.0647 0.3140 0.0895 -0.0018 0.0633  0.0123  107 TYR A CB  
738  C CG  . TYR A 107 ? 0.0473 0.3130 0.0939 -0.0032 0.0594  0.0178  107 TYR A CG  
739  C CD1 . TYR A 107 ? 0.0699 0.3215 0.1148 -0.0070 0.0665  0.0291  107 TYR A CD1 
740  C CD2 . TYR A 107 ? 0.0423 0.3123 0.1016 -0.0007 0.0583  0.0150  107 TYR A CD2 
741  C CE1 . TYR A 107 ? 0.0731 0.3098 0.1253 -0.0167 0.0721  0.0280  107 TYR A CE1 
742  C CE2 . TYR A 107 ? 0.0687 0.3100 0.1105 -0.0074 0.0663  0.0233  107 TYR A CE2 
743  C CZ  . TYR A 107 ? 0.0717 0.3070 0.1180 -0.0080 0.0625  0.0222  107 TYR A CZ  
744  O OH  . TYR A 107 ? 0.1097 0.3077 0.1529 -0.0126 0.0649  0.0283  107 TYR A OH  
745  N N   . ARG A 108 ? 0.0536 0.3486 0.1236 -0.0043 0.0741  -0.0261 108 ARG A N   
746  C CA  . ARG A 108 ? 0.0611 0.3638 0.1150 -0.0242 0.0764  -0.0067 108 ARG A CA  
747  C C   . ARG A 108 ? 0.0665 0.3641 0.1246 -0.0064 0.0843  -0.0054 108 ARG A C   
748  O O   . ARG A 108 ? 0.0669 0.3848 0.1252 0.0042  0.0832  -0.0355 108 ARG A O   
749  C CB  . ARG A 108 ? 0.0693 0.3695 0.1538 -0.0488 0.0918  -0.0048 108 ARG A CB  
750  C CG  . ARG A 108 ? 0.1062 0.3667 0.1607 -0.0661 0.1074  0.0051  108 ARG A CG  
751  C CD  . ARG A 108 ? 0.1749 0.3743 0.2067 -0.0649 0.0972  0.0035  108 ARG A CD  
752  N NE  . ARG A 108 ? 0.2242 0.4239 0.2247 -0.0459 0.0513  -0.0151 108 ARG A NE  
753  C CZ  . ARG A 108 ? 0.2044 0.4389 0.2426 -0.0625 0.0384  0.0168  108 ARG A CZ  
754  N NH1 . ARG A 108 ? 0.2586 0.4703 0.2900 -0.0578 0.0117  0.0223  108 ARG A NH1 
755  N NH2 . ARG A 108 ? 0.1867 0.4432 0.2042 -0.0507 0.0296  -0.0167 108 ARG A NH2 
756  N N   . ALA A 109 ? 0.0505 0.3597 0.1134 0.0179  0.0676  -0.0091 109 ALA A N   
757  C CA  . ALA A 109 ? 0.0430 0.3682 0.1109 0.0123  0.0600  -0.0160 109 ALA A CA  
758  C C   . ALA A 109 ? 0.0546 0.3758 0.0911 0.0075  0.0631  -0.0199 109 ALA A C   
759  O O   . ALA A 109 ? 0.0508 0.3876 0.1330 0.0206  0.0526  -0.0204 109 ALA A O   
760  C CB  . ALA A 109 ? 0.0736 0.3811 0.1175 0.0181  0.0618  0.0007  109 ALA A CB  
761  N N   . LEU A 110 ? 0.0503 0.3788 0.0974 0.0029  0.0619  -0.0342 110 LEU A N   
762  C CA  . LEU A 110 ? 0.0669 0.3607 0.1070 0.0080  0.0562  -0.0227 110 LEU A CA  
763  C C   . LEU A 110 ? 0.0518 0.3818 0.1176 0.0134  0.0562  -0.0140 110 LEU A C   
764  O O   . LEU A 110 ? 0.0525 0.4130 0.1495 0.0181  0.0729  -0.0393 110 LEU A O   
765  C CB  . LEU A 110 ? 0.0523 0.3748 0.1307 0.0053  0.0693  -0.0316 110 LEU A CB  
766  C CG  . LEU A 110 ? 0.0801 0.3680 0.1452 0.0102  0.0541  -0.0342 110 LEU A CG  
767  C CD1 . LEU A 110 ? 0.0788 0.3954 0.1504 0.0119  0.0790  -0.0308 110 LEU A CD1 
768  C CD2 . LEU A 110 ? 0.0894 0.3830 0.1453 -0.0094 0.0467  -0.0314 110 LEU A CD2 
769  N N   . MET A 111 ? 0.0581 0.3895 0.1163 -0.0016 0.0754  0.0020  111 MET A N   
770  C CA  . MET A 111 ? 0.0806 0.4288 0.1102 -0.0196 0.0877  -0.0123 111 MET A CA  
771  C C   . MET A 111 ? 0.0697 0.4211 0.1179 -0.0069 0.0841  -0.0131 111 MET A C   
772  O O   . MET A 111 ? 0.0905 0.4988 0.1051 -0.0139 0.0912  -0.0114 111 MET A O   
773  C CB  . MET A 111 ? 0.0942 0.4503 0.1571 -0.0179 0.1142  0.0089  111 MET A CB  
774  C CG  . MET A 111 ? 0.0687 0.4659 0.2263 -0.0316 0.1132  0.0219  111 MET A CG  
775  S SD  . MET A 111 ? 0.1599 0.5048 0.4185 -0.0208 0.0292  0.0890  111 MET A SD  
776  C CE  . MET A 111 ? 0.1383 0.5826 0.3700 0.0086  0.0687  0.0215  111 MET A CE  
777  N N   . ALA A 112 ? 0.0547 0.4304 0.1194 -0.0082 0.0739  -0.0162 112 ALA A N   
778  C CA  . ALA A 112 ? 0.0551 0.4438 0.1144 -0.0111 0.0725  -0.0050 112 ALA A CA  
779  C C   . ALA A 112 ? 0.0608 0.4527 0.1373 -0.0070 0.0845  -0.0093 112 ALA A C   
780  O O   . ALA A 112 ? 0.0614 0.4537 0.2378 0.0080  0.0571  -0.0202 112 ALA A O   
781  C CB  . ALA A 112 ? 0.0469 0.4535 0.1454 -0.0123 0.0741  -0.0187 112 ALA A CB  
782  N N   . GLY A 113 ? 0.0567 0.4556 0.1524 0.0130  0.0843  -0.0248 113 GLY A N   
783  C CA  . GLY A 113 ? 0.0723 0.4573 0.1843 0.0281  0.0860  -0.0104 113 GLY A CA  
784  C C   . GLY A 113 ? 0.1017 0.4363 0.1853 0.0617  0.0845  -0.0213 113 GLY A C   
785  O O   . GLY A 113 ? 0.1840 0.4398 0.2156 0.0821  0.1318  0.0050  113 GLY A O   
786  N N   . ASN A 114 ? 0.0396 0.4023 0.1943 0.0399  0.0720  -0.0194 114 ASN A N   
787  C CA  . ASN A 114 ? 0.0576 0.4063 0.1715 0.0371  0.0564  -0.0122 114 ASN A CA  
788  C C   . ASN A 114 ? 0.0635 0.3848 0.1552 0.0408  0.0601  -0.0118 114 ASN A C   
789  O O   . ASN A 114 ? 0.0645 0.3627 0.2409 0.0305  0.0657  -0.0273 114 ASN A O   
790  C CB  . ASN A 114 ? 0.0531 0.4265 0.1853 0.0246  0.0473  -0.0128 114 ASN A CB  
791  C CG  . ASN A 114 ? 0.0578 0.4364 0.1888 0.0090  0.0488  -0.0153 114 ASN A CG  
792  O OD1 . ASN A 114 ? 0.0739 0.4355 0.1973 0.0292  0.0832  0.0022  114 ASN A OD1 
793  N ND2 . ASN A 114 ? 0.1520 0.4726 0.2201 -0.0322 0.0308  -0.0436 114 ASN A ND2 
794  N N   . GLU A 115 ? 0.0806 0.4021 0.1589 0.0490  0.0656  -0.0253 115 GLU A N   
795  C CA  . GLU A 115 ? 0.1028 0.4064 0.1399 0.0469  0.0549  -0.0201 115 GLU A CA  
796  C C   . GLU A 115 ? 0.0739 0.4099 0.1529 0.0481  0.0612  -0.0089 115 GLU A C   
797  O O   . GLU A 115 ? 0.0745 0.4090 0.1485 0.0233  0.0610  -0.0142 115 GLU A O   
798  C CB  . GLU A 115 ? 0.1503 0.4130 0.1679 0.0522  0.0459  -0.0231 115 GLU A CB  
799  C CG  . GLU A 115 ? 0.2062 0.4425 0.1610 0.0513  0.0740  -0.0335 115 GLU A CG  
800  C CD  . GLU A 115 ? 0.2561 0.4578 0.2169 0.0591  0.0964  -0.0456 115 GLU A CD  
801  O OE1 . GLU A 115 ? 0.3702 0.4712 0.2609 0.0358  0.0795  -0.0762 115 GLU A OE1 
802  O OE2 . GLU A 115 ? 0.3514 0.5279 0.2348 0.0404  0.1079  -0.0197 115 GLU A OE2 
803  N N   . GLN A 116 ? 0.0863 0.4047 0.1538 0.0414  0.0555  -0.0017 116 GLN A N   
804  C CA  . GLN A 116 ? 0.1084 0.3970 0.1713 0.0712  0.0543  -0.0054 116 GLN A CA  
805  C C   . GLN A 116 ? 0.0926 0.3641 0.1673 0.0556  0.0553  0.0030  116 GLN A C   
806  O O   . GLN A 116 ? 0.1033 0.3772 0.1801 0.0530  0.0701  0.0292  116 GLN A O   
807  C CB  . GLN A 116 ? 0.1111 0.4128 0.1900 0.0848  0.0667  0.0083  116 GLN A CB  
808  C CG  . GLN A 116 ? 0.1707 0.4339 0.2063 0.1095  0.0841  0.0219  116 GLN A CG  
809  C CD  . GLN A 116 ? 0.2517 0.4442 0.2525 0.1179  0.0954  0.0010  116 GLN A CD  
810  O OE1 . GLN A 116 ? 0.3713 0.4938 0.2664 0.1286  0.1532  -0.0120 116 GLN A OE1 
811  N NE2 . GLN A 116 ? 0.2724 0.4862 0.3248 0.1071  0.0951  -0.0100 116 GLN A NE2 
812  N N   . VAL A 117 ? 0.1072 0.3561 0.1448 0.0370  0.0488  -0.0055 117 VAL A N   
813  C CA  . VAL A 117 ? 0.1219 0.3486 0.1205 0.0300  0.0456  -0.0050 117 VAL A CA  
814  C C   . VAL A 117 ? 0.0961 0.3468 0.1122 0.0170  0.0739  -0.0013 117 VAL A C   
815  O O   . VAL A 117 ? 0.0883 0.3493 0.1249 0.0132  0.0775  -0.0132 117 VAL A O   
816  C CB  . VAL A 117 ? 0.1065 0.3526 0.1155 0.0258  0.0498  -0.0185 117 VAL A CB  
817  C CG1 . VAL A 117 ? 0.1096 0.3383 0.1438 0.0156  0.0549  -0.0127 117 VAL A CG1 
818  C CG2 . VAL A 117 ? 0.1283 0.3777 0.1099 0.0198  0.0600  -0.0165 117 VAL A CG2 
819  N N   . GLY A 118 ? 0.0872 0.3503 0.1148 0.0167  0.0613  -0.0086 118 GLY A N   
820  C CA  . GLY A 118 ? 0.0949 0.3320 0.1054 0.0400  0.0485  -0.0082 118 GLY A CA  
821  C C   . GLY A 118 ? 0.1006 0.3198 0.1036 0.0411  0.0396  -0.0026 118 GLY A C   
822  O O   . GLY A 118 ? 0.1095 0.3285 0.1184 0.0330  0.0540  -0.0048 118 GLY A O   
823  N N   . PHE A 119 ? 0.1057 0.3078 0.0843 0.0364  0.0445  0.0021  119 PHE A N   
824  C CA  . PHE A 119 ? 0.0884 0.3052 0.0931 0.0507  0.0510  -0.0100 119 PHE A CA  
825  C C   . PHE A 119 ? 0.0981 0.3280 0.0917 0.0528  0.0481  -0.0073 119 PHE A C   
826  O O   . PHE A 119 ? 0.0819 0.3286 0.1250 0.0554  0.0570  -0.0234 119 PHE A O   
827  C CB  . PHE A 119 ? 0.1233 0.3106 0.0930 0.0629  0.0523  -0.0222 119 PHE A CB  
828  C CG  . PHE A 119 ? 0.1373 0.3159 0.1433 0.0682  0.0278  -0.0071 119 PHE A CG  
829  C CD1 . PHE A 119 ? 0.1773 0.3302 0.1440 0.0583  0.0440  -0.0017 119 PHE A CD1 
830  C CD2 . PHE A 119 ? 0.1547 0.3197 0.1740 0.0658  0.0174  -0.0091 119 PHE A CD2 
831  C CE1 . PHE A 119 ? 0.2028 0.3203 0.1732 0.0456  0.0231  0.0073  119 PHE A CE1 
832  C CE2 . PHE A 119 ? 0.1837 0.3301 0.2086 0.0673  -0.0064 -0.0056 119 PHE A CE2 
833  C CZ  . PHE A 119 ? 0.2080 0.3328 0.1962 0.0505  0.0174  0.0085  119 PHE A CZ  
834  N N   . ASP A 120 ? 0.1115 0.3277 0.0909 0.0465  0.0633  -0.0057 120 ASP A N   
835  C CA  . ASP A 120 ? 0.1227 0.3313 0.0926 0.0568  0.0510  -0.0123 120 ASP A CA  
836  C C   . ASP A 120 ? 0.1191 0.3166 0.0911 0.0470  0.0525  -0.0101 120 ASP A C   
837  O O   . ASP A 120 ? 0.1261 0.3497 0.0864 0.0377  0.0510  0.0060  120 ASP A O   
838  C CB  . ASP A 120 ? 0.1432 0.3523 0.1273 0.0638  0.0372  -0.0197 120 ASP A CB  
839  C CG  . ASP A 120 ? 0.1640 0.3842 0.1898 0.0840  0.0349  -0.0135 120 ASP A CG  
840  O OD1 . ASP A 120 ? 0.2301 0.3729 0.2296 0.1172  0.0164  -0.0172 120 ASP A OD1 
841  O OD2 . ASP A 120 ? 0.1627 0.4865 0.2601 0.0730  0.0431  -0.0091 120 ASP A OD2 
842  N N   . LEU A 121 ? 0.0986 0.2975 0.0847 0.0490  0.0553  -0.0111 121 LEU A N   
843  C CA  . LEU A 121 ? 0.0949 0.2988 0.0896 0.0415  0.0509  -0.0142 121 LEU A CA  
844  C C   . LEU A 121 ? 0.0834 0.3133 0.0786 0.0313  0.0546  -0.0123 121 LEU A C   
845  O O   . LEU A 121 ? 0.0921 0.3181 0.0910 0.0290  0.0657  -0.0134 121 LEU A O   
846  C CB  . LEU A 121 ? 0.0959 0.3061 0.1038 0.0424  0.0506  -0.0215 121 LEU A CB  
847  C CG  . LEU A 121 ? 0.1114 0.3180 0.0925 0.0376  0.0596  -0.0267 121 LEU A CG  
848  C CD1 . LEU A 121 ? 0.1419 0.3260 0.0889 0.0345  0.0470  -0.0378 121 LEU A CD1 
849  C CD2 . LEU A 121 ? 0.0890 0.3347 0.1151 0.0319  0.0723  -0.0111 121 LEU A CD2 
850  N N   . VAL A 122 ? 0.0764 0.3115 0.0614 0.0243  0.0519  -0.0085 122 VAL A N   
851  C CA  . VAL A 122 ? 0.0699 0.3039 0.0738 0.0337  0.0526  -0.0049 122 VAL A CA  
852  C C   . VAL A 122 ? 0.0877 0.3029 0.0973 0.0277  0.0431  0.0020  122 VAL A C   
853  O O   . VAL A 122 ? 0.1002 0.3229 0.0710 0.0311  0.0641  0.0061  122 VAL A O   
854  C CB  . VAL A 122 ? 0.0875 0.3126 0.0882 0.0355  0.0275  0.0014  122 VAL A CB  
855  C CG1 . VAL A 122 ? 0.1031 0.3052 0.0803 0.0226  0.0332  0.0140  122 VAL A CG1 
856  C CG2 . VAL A 122 ? 0.0887 0.3189 0.0835 0.0313  0.0339  0.0145  122 VAL A CG2 
857  N N   . LYS A 123 ? 0.0965 0.3164 0.0825 0.0466  0.0680  0.0053  123 LYS A N   
858  C CA  . LYS A 123 ? 0.1401 0.3106 0.0910 0.0482  0.0494  0.0050  123 LYS A CA  
859  C C   . LYS A 123 ? 0.1289 0.3124 0.1000 0.0383  0.0610  -0.0032 123 LYS A C   
860  O O   . LYS A 123 ? 0.1395 0.3129 0.1196 0.0361  0.0715  0.0051  123 LYS A O   
861  C CB  . LYS A 123 ? 0.1724 0.3346 0.1037 0.0659  0.0710  0.0006  123 LYS A CB  
862  C CG  . LYS A 123 ? 0.2359 0.3652 0.1510 0.0636  0.0849  0.0344  123 LYS A CG  
863  C CD  . LYS A 123 ? 0.3170 0.4203 0.2480 0.0768  0.0809  0.0315  123 LYS A CD  
864  C CE  . LYS A 123 ? 0.4116 0.4685 0.3191 0.0596  0.0875  0.0495  123 LYS A CE  
865  N NZ  . LYS A 123 ? 0.4617 0.5478 0.4433 0.0426  0.0633  0.0341  123 LYS A NZ  
866  N N   . ALA A 124 ? 0.1317 0.3136 0.0727 0.0361  0.0603  0.0052  124 ALA A N   
867  C CA  . ALA A 124 ? 0.1352 0.3270 0.0695 0.0490  0.0422  0.0068  124 ALA A CA  
868  C C   . ALA A 124 ? 0.1176 0.3061 0.0636 0.0433  0.0691  0.0127  124 ALA A C   
869  O O   . ALA A 124 ? 0.1517 0.3320 0.0778 0.0299  0.0849  0.0181  124 ALA A O   
870  C CB  . ALA A 124 ? 0.1550 0.3483 0.1033 0.0424  0.0412  0.0061  124 ALA A CB  
871  N N   . CYS A 125 ? 0.1175 0.3096 0.0951 0.0396  0.0542  0.0188  125 CYS A N   
872  C CA  . CYS A 125 ? 0.1085 0.2985 0.0756 0.0223  0.0646  0.0130  125 CYS A CA  
873  C C   . CYS A 125 ? 0.1157 0.2951 0.0705 0.0094  0.0837  0.0013  125 CYS A C   
874  O O   . CYS A 125 ? 0.1072 0.3077 0.0849 0.0189  0.0844  0.0017  125 CYS A O   
875  C CB  . CYS A 125 ? 0.0971 0.2996 0.0827 0.0225  0.0747  0.0122  125 CYS A CB  
876  S SG  . CYS A 125 ? 0.1386 0.3410 0.1219 0.0130  0.0888  0.0152  125 CYS A SG  
877  N N   . LYS A 126 ? 0.1294 0.2826 0.0852 0.0076  0.0683  -0.0101 126 LYS A N   
878  C CA  . LYS A 126 ? 0.1317 0.2920 0.0768 0.0128  0.0871  -0.0160 126 LYS A CA  
879  C C   . LYS A 126 ? 0.1502 0.2981 0.1008 0.0096  0.0869  0.0064  126 LYS A C   
880  O O   . LYS A 126 ? 0.1511 0.3221 0.1016 0.0083  0.0855  0.0011  126 LYS A O   
881  C CB  . LYS A 126 ? 0.1436 0.3122 0.0812 0.0190  0.0910  -0.0243 126 LYS A CB  
882  C CG  . LYS A 126 ? 0.1870 0.3159 0.1088 0.0077  0.0946  -0.0238 126 LYS A CG  
883  C CD  . LYS A 126 ? 0.1919 0.3464 0.1148 -0.0120 0.1008  -0.0040 126 LYS A CD  
884  C CE  . LYS A 126 ? 0.2536 0.3539 0.1702 -0.0319 0.0862  0.0138  126 LYS A CE  
885  N NZ  . LYS A 126 ? 0.2899 0.3907 0.2255 -0.0699 0.0995  0.0208  126 LYS A NZ  
886  N N   . GLU A 127 ? 0.1660 0.3138 0.0965 0.0182  0.0930  0.0332  127 GLU A N   
887  C CA  . GLU A 127 ? 0.1817 0.3137 0.1191 0.0261  0.0862  0.0405  127 GLU A CA  
888  C C   . GLU A 127 ? 0.1443 0.2941 0.1048 0.0046  0.0747  0.0348  127 GLU A C   
889  O O   . GLU A 127 ? 0.1465 0.3376 0.1451 -0.0002 0.1016  0.0451  127 GLU A O   
890  C CB  . GLU A 127 ? 0.2079 0.3565 0.1659 0.0408  0.0858  0.0593  127 GLU A CB  
891  C CG  . GLU A 127 ? 0.2679 0.4094 0.2156 0.0682  0.0994  0.0503  127 GLU A CG  
892  C CD  . GLU A 127 ? 0.3080 0.5153 0.3190 0.0878  0.0848  0.0402  127 GLU A CD  
893  O OE1 . GLU A 127 ? 0.3105 0.6487 0.3783 0.1128  0.0280  0.0442  127 GLU A OE1 
894  O OE2 . GLU A 127 ? 0.4011 0.5258 0.3978 0.1379  0.1340  0.0734  127 GLU A OE2 
895  N N   . ALA A 128 ? 0.1330 0.2956 0.0938 0.0053  0.0820  0.0231  128 ALA A N   
896  C CA  . ALA A 128 ? 0.1489 0.2812 0.0623 0.0198  0.0545  0.0169  128 ALA A CA  
897  C C   . ALA A 128 ? 0.1305 0.2764 0.0633 0.0018  0.0667  0.0147  128 ALA A C   
898  O O   . ALA A 128 ? 0.1469 0.3088 0.0861 0.0079  0.0870  0.0136  128 ALA A O   
899  C CB  . ALA A 128 ? 0.1539 0.3116 0.0603 0.0154  0.0424  0.0026  128 ALA A CB  
900  N N   . CYS A 129 ? 0.1217 0.2890 0.0568 0.0044  0.0630  -0.0072 129 CYS A N   
901  C CA  . CYS A 129 ? 0.1029 0.2863 0.0675 0.0089  0.0703  0.0035  129 CYS A CA  
902  C C   . CYS A 129 ? 0.1411 0.2898 0.1005 -0.0037 0.0661  0.0011  129 CYS A C   
903  O O   . CYS A 129 ? 0.1280 0.2972 0.1048 -0.0065 0.0636  0.0289  129 CYS A O   
904  C CB  . CYS A 129 ? 0.0936 0.2986 0.0740 0.0082  0.0656  0.0061  129 CYS A CB  
905  S SG  . CYS A 129 ? 0.1204 0.3027 0.1029 0.0012  0.0701  0.0200  129 CYS A SG  
906  N N   . ALA A 130 ? 0.1608 0.2942 0.0863 -0.0198 0.0823  0.0039  130 ALA A N   
907  C CA  . ALA A 130 ? 0.2019 0.2940 0.1203 -0.0248 0.0820  -0.0112 130 ALA A CA  
908  C C   . ALA A 130 ? 0.1855 0.2749 0.1393 -0.0491 0.0884  0.0032  130 ALA A C   
909  O O   . ALA A 130 ? 0.1983 0.3102 0.1457 -0.0692 0.0844  -0.0021 130 ALA A O   
910  C CB  . ALA A 130 ? 0.1933 0.2827 0.1456 -0.0251 0.1166  -0.0201 130 ALA A CB  
911  N N   . ALA A 131 ? 0.1739 0.2860 0.1304 -0.0332 0.0919  0.0358  131 ALA A N   
912  C CA  . ALA A 131 ? 0.2285 0.3024 0.1219 -0.0187 0.0909  0.0359  131 ALA A CA  
913  C C   . ALA A 131 ? 0.2276 0.2954 0.1070 -0.0213 0.1006  0.0380  131 ALA A C   
914  O O   . ALA A 131 ? 0.2563 0.3481 0.1512 -0.0094 0.1371  0.0701  131 ALA A O   
915  C CB  . ALA A 131 ? 0.2340 0.3363 0.1317 -0.0062 0.0934  0.0522  131 ALA A CB  
916  N N   . ALA A 132 ? 0.1876 0.2870 0.1111 -0.0206 0.0866  0.0269  132 ALA A N   
917  C CA  . ALA A 132 ? 0.1857 0.2884 0.1079 -0.0167 0.0941  0.0217  132 ALA A CA  
918  C C   . ALA A 132 ? 0.1756 0.2733 0.1390 -0.0320 0.0846  0.0363  132 ALA A C   
919  O O   . ALA A 132 ? 0.1775 0.3135 0.1532 -0.0211 0.0956  0.0310  132 ALA A O   
920  C CB  . ALA A 132 ? 0.2281 0.3098 0.1286 -0.0209 0.0785  0.0146  132 ALA A CB  
921  N N   . ASN A 133 ? 0.1660 0.2927 0.1430 -0.0448 0.0731  0.0285  133 ASN A N   
922  C CA  . ASN A 133 ? 0.1700 0.3246 0.1853 -0.0507 0.0564  0.0413  133 ASN A CA  
923  C C   . ASN A 133 ? 0.1463 0.3115 0.1372 -0.0576 0.0577  0.0332  133 ASN A C   
924  O O   . ASN A 133 ? 0.1457 0.3479 0.2095 -0.0646 0.0531  0.0415  133 ASN A O   
925  C CB  . ASN A 133 ? 0.2024 0.3811 0.2435 -0.0827 0.0763  0.0509  133 ASN A CB  
926  C CG  . ASN A 133 ? 0.3077 0.4867 0.3270 -0.0939 0.0735  0.0317  133 ASN A CG  
927  O OD1 . ASN A 133 ? 0.5029 0.5865 0.3456 -0.0736 0.0640  0.0200  133 ASN A OD1 
928  N ND2 . ASN A 133 ? 0.3573 0.6110 0.3941 -0.1151 0.1182  0.0349  133 ASN A ND2 
929  N N   . VAL A 134 ? 0.1228 0.2803 0.1115 -0.0298 0.0647  0.0131  134 VAL A N   
930  C CA  . VAL A 134 ? 0.1143 0.2714 0.0922 -0.0208 0.0811  0.0018  134 VAL A CA  
931  C C   . VAL A 134 ? 0.1176 0.2683 0.0801 -0.0062 0.0685  0.0003  134 VAL A C   
932  O O   . VAL A 134 ? 0.1166 0.2931 0.1143 0.0006  0.0659  0.0019  134 VAL A O   
933  C CB  . VAL A 134 ? 0.1004 0.2653 0.0894 -0.0078 0.0757  -0.0010 134 VAL A CB  
934  C CG1 . VAL A 134 ? 0.0942 0.2644 0.0996 -0.0088 0.0587  -0.0016 134 VAL A CG1 
935  C CG2 . VAL A 134 ? 0.1443 0.2876 0.0888 -0.0136 0.0922  -0.0006 134 VAL A CG2 
936  N N   . LEU A 135 ? 0.1104 0.2592 0.0987 -0.0129 0.0833  0.0047  135 LEU A N   
937  C CA  . LEU A 135 ? 0.1315 0.2617 0.0912 -0.0068 0.0768  -0.0136 135 LEU A CA  
938  C C   . LEU A 135 ? 0.1189 0.2487 0.0794 -0.0093 0.0642  -0.0143 135 LEU A C   
939  O O   . LEU A 135 ? 0.1207 0.2536 0.0950 -0.0273 0.0886  -0.0189 135 LEU A O   
940  C CB  . LEU A 135 ? 0.1775 0.3100 0.1462 -0.0229 0.0490  0.0082  135 LEU A CB  
941  C CG  . LEU A 135 ? 0.2629 0.3810 0.1973 -0.0271 0.0737  0.0135  135 LEU A CG  
942  C CD1 . LEU A 135 ? 0.3612 0.4258 0.2443 -0.0358 -0.0171 -0.0083 135 LEU A CD1 
943  C CD2 . LEU A 135 ? 0.3771 0.4148 0.2889 -0.0165 0.0380  0.0095  135 LEU A CD2 
944  N N   . LEU A 136 ? 0.1260 0.2600 0.0752 -0.0065 0.0720  -0.0095 136 LEU A N   
945  C CA  . LEU A 136 ? 0.1168 0.2540 0.0598 -0.0086 0.0519  -0.0006 136 LEU A CA  
946  C C   . LEU A 136 ? 0.0899 0.2490 0.0581 -0.0047 0.0616  -0.0113 136 LEU A C   
947  O O   . LEU A 136 ? 0.1248 0.2474 0.0795 -0.0044 0.0697  -0.0095 136 LEU A O   
948  C CB  . LEU A 136 ? 0.1140 0.2748 0.0673 -0.0074 0.0624  0.0137  136 LEU A CB  
949  C CG  . LEU A 136 ? 0.1039 0.2945 0.0896 -0.0034 0.0696  0.0224  136 LEU A CG  
950  C CD1 . LEU A 136 ? 0.1190 0.2963 0.1168 -0.0135 0.0606  0.0150  136 LEU A CD1 
951  C CD2 . LEU A 136 ? 0.1286 0.3096 0.1038 0.0101  0.0525  0.0260  136 LEU A CD2 
952  N N   . LYS A 137 ? 0.0951 0.2521 0.0549 -0.0041 0.0656  -0.0003 137 LYS A N   
953  C CA  . LYS A 137 ? 0.0868 0.2532 0.0591 -0.0086 0.0650  0.0011  137 LYS A CA  
954  C C   . LYS A 137 ? 0.0796 0.2652 0.0611 -0.0080 0.0632  -0.0142 137 LYS A C   
955  O O   . LYS A 137 ? 0.0812 0.2840 0.0724 -0.0134 0.0701  -0.0237 137 LYS A O   
956  C CB  . LYS A 137 ? 0.0744 0.2638 0.0777 -0.0169 0.0685  0.0074  137 LYS A CB  
957  C CG  . LYS A 137 ? 0.0659 0.2714 0.0960 -0.0064 0.0731  -0.0041 137 LYS A CG  
958  C CD  . LYS A 137 ? 0.0896 0.2875 0.0805 -0.0057 0.0786  -0.0059 137 LYS A CD  
959  C CE  . LYS A 137 ? 0.0954 0.3075 0.0805 -0.0153 0.0813  -0.0120 137 LYS A CE  
960  N NZ  . LYS A 137 ? 0.1012 0.3233 0.0858 -0.0089 0.0868  -0.0084 137 LYS A NZ  
961  N N   . VAL A 138 ? 0.0652 0.2409 0.0603 0.0049  0.0556  -0.0132 138 VAL A N   
962  C CA  . VAL A 138 ? 0.0675 0.2407 0.0776 0.0026  0.0425  -0.0097 138 VAL A CA  
963  C C   . VAL A 138 ? 0.0460 0.2493 0.0848 0.0046  0.0555  -0.0083 138 VAL A C   
964  O O   . VAL A 138 ? 0.0683 0.2687 0.0774 -0.0031 0.0663  -0.0077 138 VAL A O   
965  C CB  . VAL A 138 ? 0.0639 0.2462 0.0666 0.0029  0.0587  -0.0080 138 VAL A CB  
966  C CG1 . VAL A 138 ? 0.0616 0.2618 0.0883 -0.0007 0.0649  -0.0086 138 VAL A CG1 
967  C CG2 . VAL A 138 ? 0.0905 0.2499 0.0798 0.0108  0.0541  -0.0037 138 VAL A CG2 
968  N N   . ILE A 139 ? 0.0708 0.2570 0.0707 -0.0008 0.0643  -0.0080 139 ILE A N   
969  C CA  . ILE A 139 ? 0.0519 0.2589 0.0805 0.0033  0.0581  -0.0021 139 ILE A CA  
970  C C   . ILE A 139 ? 0.0530 0.2797 0.0773 0.0102  0.0565  -0.0147 139 ILE A C   
971  O O   . ILE A 139 ? 0.0644 0.3017 0.0651 0.0001  0.0580  -0.0160 139 ILE A O   
972  C CB  . ILE A 139 ? 0.0494 0.2566 0.0954 -0.0068 0.0598  0.0026  139 ILE A CB  
973  C CG1 . ILE A 139 ? 0.0543 0.2722 0.1029 -0.0024 0.0670  -0.0030 139 ILE A CG1 
974  C CG2 . ILE A 139 ? 0.0519 0.2572 0.1097 -0.0076 0.0582  0.0009  139 ILE A CG2 
975  C CD1 . ILE A 139 ? 0.0759 0.2898 0.1049 0.0013  0.0782  -0.0039 139 ILE A CD1 
976  N N   . ILE A 140 ? 0.0536 0.2905 0.0690 0.0118  0.0529  -0.0030 140 ILE A N   
977  C CA  . ILE A 140 ? 0.0539 0.2882 0.1009 0.0020  0.0612  -0.0039 140 ILE A CA  
978  C C   . ILE A 140 ? 0.0536 0.2942 0.0878 -0.0020 0.0587  0.0020  140 ILE A C   
979  O O   . ILE A 140 ? 0.0501 0.3057 0.1180 0.0004  0.0649  0.0077  140 ILE A O   
980  C CB  . ILE A 140 ? 0.0671 0.3149 0.0872 0.0085  0.0695  -0.0026 140 ILE A CB  
981  C CG1 . ILE A 140 ? 0.0915 0.3336 0.0723 0.0151  0.0737  -0.0137 140 ILE A CG1 
982  C CG2 . ILE A 140 ? 0.0991 0.3093 0.0929 0.0244  0.0598  -0.0018 140 ILE A CG2 
983  C CD1 . ILE A 140 ? 0.1009 0.3423 0.0858 0.0131  0.0841  -0.0181 140 ILE A CD1 
984  N N   . GLU A 141 ? 0.0734 0.2901 0.0893 0.0064  0.0746  0.0120  141 GLU A N   
985  C CA  . GLU A 141 ? 0.0712 0.2819 0.0866 0.0062  0.0653  0.0015  141 GLU A CA  
986  C C   . GLU A 141 ? 0.0781 0.2928 0.0805 -0.0160 0.0622  0.0092  141 GLU A C   
987  O O   . GLU A 141 ? 0.0705 0.3185 0.1090 -0.0115 0.0771  0.0106  141 GLU A O   
988  C CB  . GLU A 141 ? 0.0701 0.2942 0.1056 -0.0113 0.0793  0.0006  141 GLU A CB  
989  C CG  . GLU A 141 ? 0.0714 0.3086 0.1191 -0.0246 0.0770  -0.0082 141 GLU A CG  
990  C CD  . GLU A 141 ? 0.0750 0.3043 0.1142 -0.0257 0.0715  -0.0146 141 GLU A CD  
991  O OE1 . GLU A 141 ? 0.0874 0.2947 0.1005 -0.0429 0.0605  -0.0015 141 GLU A OE1 
992  O OE2 . GLU A 141 ? 0.1155 0.3088 0.1130 -0.0337 0.0881  -0.0052 141 GLU A OE2 
993  N N   . THR A 142 ? 0.0755 0.3057 0.0639 -0.0139 0.0620  0.0116  142 THR A N   
994  C CA  . THR A 142 ? 0.0994 0.3124 0.0631 -0.0189 0.0710  0.0132  142 THR A CA  
995  C C   . THR A 142 ? 0.0931 0.3357 0.0983 -0.0282 0.0854  0.0225  142 THR A C   
996  O O   . THR A 142 ? 0.0895 0.3755 0.1067 -0.0274 0.0892  0.0117  142 THR A O   
997  C CB  . THR A 142 ? 0.0956 0.3200 0.0602 -0.0084 0.0643  0.0007  142 THR A CB  
998  O OG1 . THR A 142 ? 0.0926 0.3236 0.0879 -0.0099 0.0546  0.0254  142 THR A OG1 
999  C CG2 . THR A 142 ? 0.1127 0.3205 0.0638 -0.0125 0.0651  -0.0036 142 THR A CG2 
1000 N N   . GLY A 143 ? 0.0853 0.3213 0.1041 -0.0322 0.0813  0.0320  143 GLY A N   
1001 C CA  . GLY A 143 ? 0.1045 0.3442 0.0918 -0.0329 0.0718  0.0433  143 GLY A CA  
1002 C C   . GLY A 143 ? 0.1189 0.3685 0.1358 -0.0583 0.0670  0.0497  143 GLY A C   
1003 O O   . GLY A 143 ? 0.2013 0.4127 0.2298 -0.0981 0.0381  0.1099  143 GLY A O   
1004 N N   . GLU A 144 ? 0.0816 0.3629 0.1200 -0.0502 0.0810  0.0387  144 GLU A N   
1005 C CA  . GLU A 144 ? 0.0812 0.3612 0.1311 -0.0480 0.0898  0.0166  144 GLU A CA  
1006 C C   . GLU A 144 ? 0.0788 0.3614 0.1555 -0.0459 0.0791  -0.0060 144 GLU A C   
1007 O O   . GLU A 144 ? 0.0861 0.3793 0.2000 -0.0428 0.0983  0.0104  144 GLU A O   
1008 C CB  . GLU A 144 ? 0.1242 0.3895 0.1423 -0.0358 0.0742  0.0236  144 GLU A CB  
1009 C CG  . GLU A 144 ? 0.1502 0.3943 0.1507 -0.0330 0.0796  0.0225  144 GLU A CG  
1010 C CD  . GLU A 144 ? 0.1477 0.4169 0.2327 -0.0430 0.0995  0.0265  144 GLU A CD  
1011 O OE1 . GLU A 144 ? 0.1531 0.4555 0.3043 -0.0871 0.1090  -0.0131 144 GLU A OE1 
1012 O OE2 . GLU A 144 ? 0.1940 0.4408 0.2806 -0.0191 0.0949  0.0310  144 GLU A OE2 
1013 N N   . LEU A 145 ? 0.0837 0.3638 0.1242 -0.0296 0.0925  -0.0088 145 LEU A N   
1014 C CA  . LEU A 145 ? 0.0863 0.3778 0.1200 -0.0203 0.0833  -0.0119 145 LEU A CA  
1015 C C   . LEU A 145 ? 0.1147 0.4194 0.1287 -0.0299 0.0799  0.0004  145 LEU A C   
1016 O O   . LEU A 145 ? 0.1263 0.4612 0.1601 0.0050  0.0971  0.0073  145 LEU A O   
1017 C CB  . LEU A 145 ? 0.1314 0.3783 0.0983 -0.0114 0.0795  -0.0167 145 LEU A CB  
1018 C CG  . LEU A 145 ? 0.1048 0.3888 0.0961 -0.0097 0.0937  -0.0239 145 LEU A CG  
1019 C CD1 . LEU A 145 ? 0.1573 0.3780 0.1405 -0.0159 0.0811  -0.0166 145 LEU A CD1 
1020 C CD2 . LEU A 145 ? 0.1316 0.3977 0.1217 -0.0014 0.0737  -0.0130 145 LEU A CD2 
1021 N N   . LYS A 146 ? 0.1250 0.4266 0.1228 -0.0462 0.0787  0.0203  146 LYS A N   
1022 C CA  . LYS A 146 ? 0.1702 0.4701 0.1328 -0.0387 0.0989  0.0180  146 LYS A CA  
1023 C C   . LYS A 146 ? 0.1901 0.4834 0.1270 -0.0127 0.1110  0.0166  146 LYS A C   
1024 O O   . LYS A 146 ? 0.3102 0.5546 0.1820 -0.0065 0.1055  -0.0170 146 LYS A O   
1025 C CB  . LYS A 146 ? 0.2610 0.4833 0.1652 -0.0523 0.1204  0.0428  146 LYS A CB  
1026 C CG  . LYS A 146 ? 0.4104 0.4939 0.2177 -0.0739 0.1020  0.0426  146 LYS A CG  
1027 C CD  . LYS A 146 ? 0.4969 0.5283 0.3296 -0.1032 0.1063  0.0440  146 LYS A CD  
1028 C CE  . LYS A 146 ? 0.5602 0.5977 0.3988 -0.0839 0.0965  0.0187  146 LYS A CE  
1029 N NZ  . LYS A 146 ? 0.6260 0.6760 0.4721 -0.0867 0.0452  0.0126  146 LYS A NZ  
1030 N N   . ASP A 147 ? 0.2708 0.4684 0.1215 -0.0058 0.1245  0.0328  147 ASP A N   
1031 C CA  . ASP A 147 ? 0.1954 0.4605 0.1096 0.0056  0.1240  0.0291  147 ASP A CA  
1032 C C   . ASP A 147 ? 0.1536 0.4256 0.1096 0.0128  0.1234  0.0114  147 ASP A C   
1033 O O   . ASP A 147 ? 0.1746 0.4178 0.1020 0.0130  0.1114  0.0145  147 ASP A O   
1034 C CB  . ASP A 147 ? 0.2073 0.5333 0.2146 -0.0295 0.0951  0.0425  147 ASP A CB  
1035 C CG  . ASP A 147 ? 0.2434 0.6011 0.3096 0.0109  0.1139  0.0368  147 ASP A CG  
1036 O OD1 . ASP A 147 ? 0.3468 0.7480 0.3162 0.0453  0.1003  0.1006  147 ASP A OD1 
1037 O OD2 . ASP A 147 ? 0.3354 0.7118 0.3693 0.0217  0.1146  0.0796  147 ASP A OD2 
1038 N N   . GLU A 148 ? 0.1354 0.4344 0.1249 0.0244  0.1231  -0.0004 148 GLU A N   
1039 C CA  . GLU A 148 ? 0.1505 0.4246 0.1001 0.0372  0.1150  0.0008  148 GLU A CA  
1040 C C   . GLU A 148 ? 0.1312 0.3960 0.1107 0.0401  0.1041  -0.0106 148 GLU A C   
1041 O O   . GLU A 148 ? 0.1308 0.4153 0.1073 0.0193  0.0816  0.0079  148 GLU A O   
1042 C CB  . GLU A 148 ? 0.1590 0.4447 0.1111 0.0643  0.0974  -0.0064 148 GLU A CB  
1043 C CG  . GLU A 148 ? 0.1988 0.4668 0.1581 0.0535  0.0943  -0.0173 148 GLU A CG  
1044 C CD  . GLU A 148 ? 0.3300 0.4898 0.1823 0.0393  0.0690  -0.0171 148 GLU A CD  
1045 O OE1 . GLU A 148 ? 0.4801 0.5129 0.1663 0.0589  0.0548  -0.0317 148 GLU A OE1 
1046 O OE2 . GLU A 148 ? 0.4502 0.5117 0.2539 0.0277  0.0305  -0.0444 148 GLU A OE2 
1047 N N   . ALA A 149 ? 0.1276 0.4180 0.1166 0.0429  0.1027  -0.0048 149 ALA A N   
1048 C CA  . ALA A 149 ? 0.1254 0.4151 0.1392 0.0344  0.0996  -0.0069 149 ALA A CA  
1049 C C   . ALA A 149 ? 0.1119 0.4022 0.1388 0.0323  0.0963  -0.0051 149 ALA A C   
1050 O O   . ALA A 149 ? 0.1194 0.3892 0.1514 0.0362  0.0988  -0.0130 149 ALA A O   
1051 C CB  . ALA A 149 ? 0.1255 0.4298 0.1389 0.0339  0.0988  -0.0069 149 ALA A CB  
1052 N N   . LEU A 150 ? 0.0858 0.4016 0.1136 0.0270  0.0914  0.0015  150 LEU A N   
1053 C CA  . LEU A 150 ? 0.0915 0.3879 0.1243 0.0257  0.0929  -0.0092 150 LEU A CA  
1054 C C   . LEU A 150 ? 0.0808 0.3556 0.1223 0.0130  0.0702  0.0069  150 LEU A C   
1055 O O   . LEU A 150 ? 0.0798 0.3600 0.1125 0.0037  0.0754  0.0002  150 LEU A O   
1056 C CB  . LEU A 150 ? 0.0798 0.3926 0.1388 0.0096  0.0913  0.0101  150 LEU A CB  
1057 C CG  . LEU A 150 ? 0.0861 0.4246 0.1860 0.0094  0.0779  0.0119  150 LEU A CG  
1058 C CD1 . LEU A 150 ? 0.1058 0.4436 0.1899 0.0198  0.0918  0.0098  150 LEU A CD1 
1059 C CD2 . LEU A 150 ? 0.1421 0.4381 0.2471 0.0022  0.0474  0.0437  150 LEU A CD2 
1060 N N   . ILE A 151 ? 0.0690 0.3488 0.1117 0.0016  0.0812  -0.0019 151 ILE A N   
1061 C CA  . ILE A 151 ? 0.0823 0.3438 0.0963 0.0072  0.0824  -0.0058 151 ILE A CA  
1062 C C   . ILE A 151 ? 0.0977 0.3377 0.0905 0.0122  0.0847  -0.0073 151 ILE A C   
1063 O O   . ILE A 151 ? 0.0817 0.3376 0.0903 0.0139  0.0791  -0.0025 151 ILE A O   
1064 C CB  . ILE A 151 ? 0.0926 0.3486 0.1043 0.0148  0.0913  -0.0062 151 ILE A CB  
1065 C CG1 . ILE A 151 ? 0.0983 0.3483 0.0891 0.0071  0.0872  0.0008  151 ILE A CG1 
1066 C CG2 . ILE A 151 ? 0.0869 0.3425 0.1076 0.0057  0.0903  -0.0009 151 ILE A CG2 
1067 C CD1 . ILE A 151 ? 0.1288 0.3538 0.0994 0.0113  0.0854  0.0150  151 ILE A CD1 
1068 N N   . ARG A 152 ? 0.0823 0.3476 0.0955 0.0126  0.0813  -0.0143 152 ARG A N   
1069 C CA  . ARG A 152 ? 0.0928 0.3452 0.0994 0.0266  0.0825  -0.0182 152 ARG A CA  
1070 C C   . ARG A 152 ? 0.0993 0.3409 0.0968 0.0241  0.0760  -0.0073 152 ARG A C   
1071 O O   . ARG A 152 ? 0.1130 0.3508 0.1022 0.0152  0.0716  -0.0061 152 ARG A O   
1072 C CB  . ARG A 152 ? 0.0962 0.3725 0.1149 0.0426  0.0782  -0.0326 152 ARG A CB  
1073 C CG  . ARG A 152 ? 0.1437 0.4100 0.1248 0.0416  0.0589  -0.0399 152 ARG A CG  
1074 C CD  . ARG A 152 ? 0.1816 0.4395 0.1501 0.0577  0.0655  -0.0585 152 ARG A CD  
1075 N NE  . ARG A 152 ? 0.2116 0.4869 0.1438 0.0359  0.0940  -0.0319 152 ARG A NE  
1076 C CZ  . ARG A 152 ? 0.2451 0.5080 0.1945 0.0500  0.0543  -0.0419 152 ARG A CZ  
1077 N NH1 . ARG A 152 ? 0.2752 0.5384 0.1903 0.0011  0.0636  -0.0515 152 ARG A NH1 
1078 N NH2 . ARG A 152 ? 0.2918 0.5456 0.2420 0.0811  0.0301  -0.0333 152 ARG A NH2 
1079 N N   . LYS A 153 ? 0.0995 0.3466 0.0858 0.0205  0.0840  -0.0167 153 LYS A N   
1080 C CA  . LYS A 153 ? 0.1111 0.3459 0.1018 0.0276  0.0816  -0.0250 153 LYS A CA  
1081 C C   . LYS A 153 ? 0.1115 0.3217 0.0896 0.0136  0.0804  -0.0110 153 LYS A C   
1082 O O   . LYS A 153 ? 0.0839 0.3348 0.1134 0.0229  0.0894  -0.0095 153 LYS A O   
1083 C CB  . LYS A 153 ? 0.1289 0.3605 0.1147 0.0227  0.0775  -0.0308 153 LYS A CB  
1084 C CG  . LYS A 153 ? 0.1598 0.3928 0.1698 0.0406  0.0721  -0.0326 153 LYS A CG  
1085 C CD  . LYS A 153 ? 0.2307 0.4224 0.2458 0.0492  0.0579  -0.0367 153 LYS A CD  
1086 C CE  . LYS A 153 ? 0.3091 0.4662 0.2522 0.0610  0.0559  -0.0386 153 LYS A CE  
1087 N NZ  . LYS A 153 ? 0.3527 0.4741 0.3479 0.0735  0.0407  -0.0357 153 LYS A NZ  
1088 N N   . ALA A 154 ? 0.0981 0.3238 0.0759 0.0100  0.0794  -0.0084 154 ALA A N   
1089 C CA  . ALA A 154 ? 0.0867 0.3094 0.0656 0.0089  0.0687  -0.0059 154 ALA A CA  
1090 C C   . ALA A 154 ? 0.0921 0.3016 0.0847 0.0031  0.0641  -0.0070 154 ALA A C   
1091 O O   . ALA A 154 ? 0.0917 0.3123 0.0685 0.0264  0.0643  -0.0174 154 ALA A O   
1092 C CB  . ALA A 154 ? 0.0848 0.3068 0.0902 0.0061  0.0588  -0.0045 154 ALA A CB  
1093 N N   . SER A 155 ? 0.0831 0.2985 0.0761 0.0073  0.0707  -0.0079 155 SER A N   
1094 C CA  . SER A 155 ? 0.0762 0.2865 0.0903 0.0271  0.0669  -0.0212 155 SER A CA  
1095 C C   . SER A 155 ? 0.0995 0.2951 0.0785 0.0278  0.0704  -0.0097 155 SER A C   
1096 O O   . SER A 155 ? 0.1166 0.3136 0.0826 0.0130  0.0726  -0.0034 155 SER A O   
1097 C CB  . SER A 155 ? 0.0792 0.2981 0.0969 0.0151  0.0644  -0.0158 155 SER A CB  
1098 O OG  . SER A 155 ? 0.0896 0.3067 0.1024 0.0223  0.0620  -0.0125 155 SER A OG  
1099 N N   . GLU A 156 ? 0.1013 0.3049 0.0949 0.0395  0.0713  -0.0124 156 GLU A N   
1100 C CA  . GLU A 156 ? 0.1200 0.3157 0.1159 0.0447  0.0664  -0.0193 156 GLU A CA  
1101 C C   . GLU A 156 ? 0.1164 0.2953 0.1123 0.0425  0.0629  -0.0259 156 GLU A C   
1102 O O   . GLU A 156 ? 0.1403 0.2990 0.1178 0.0234  0.0521  -0.0325 156 GLU A O   
1103 C CB  . GLU A 156 ? 0.1404 0.3585 0.1367 0.0720  0.0703  -0.0372 156 GLU A CB  
1104 C CG  . GLU A 156 ? 0.2386 0.4119 0.1997 0.0800  0.0783  -0.0251 156 GLU A CG  
1105 C CD  . GLU A 156 ? 0.2934 0.4788 0.3255 0.1100  0.1423  0.0023  156 GLU A CD  
1106 O OE1 . GLU A 156 ? 0.3646 0.4897 0.3506 0.1170  0.2567  -0.0352 156 GLU A OE1 
1107 O OE2 . GLU A 156 ? 0.3734 0.5606 0.4815 0.1555  0.1788  0.0521  156 GLU A OE2 
1108 N N   . ILE A 157 ? 0.1004 0.3104 0.0889 0.0343  0.0585  -0.0206 157 ILE A N   
1109 C CA  . ILE A 157 ? 0.1024 0.3045 0.0895 0.0365  0.0578  -0.0208 157 ILE A CA  
1110 C C   . ILE A 157 ? 0.0952 0.2804 0.0907 0.0359  0.0557  -0.0029 157 ILE A C   
1111 O O   . ILE A 157 ? 0.1256 0.3011 0.0972 0.0279  0.0455  0.0133  157 ILE A O   
1112 C CB  . ILE A 157 ? 0.1030 0.3180 0.0938 0.0289  0.0708  -0.0206 157 ILE A CB  
1113 C CG1 . ILE A 157 ? 0.0972 0.3399 0.1044 0.0255  0.0666  -0.0368 157 ILE A CG1 
1114 C CG2 . ILE A 157 ? 0.1055 0.3214 0.0996 0.0221  0.0536  -0.0058 157 ILE A CG2 
1115 C CD1 . ILE A 157 ? 0.1209 0.3569 0.1116 0.0125  0.0488  -0.0238 157 ILE A CD1 
1116 N N   . SER A 158 ? 0.1025 0.2699 0.0736 0.0344  0.0587  -0.0045 158 SER A N   
1117 C CA  . SER A 158 ? 0.1200 0.2620 0.0740 0.0352  0.0656  -0.0338 158 SER A CA  
1118 C C   . SER A 158 ? 0.1266 0.2640 0.0929 0.0376  0.0638  -0.0196 158 SER A C   
1119 O O   . SER A 158 ? 0.1258 0.2901 0.0925 0.0378  0.0495  -0.0025 158 SER A O   
1120 C CB  . SER A 158 ? 0.1231 0.2560 0.0783 0.0319  0.0740  -0.0352 158 SER A CB  
1121 O OG  . SER A 158 ? 0.1439 0.2660 0.1000 0.0200  0.0730  -0.0312 158 SER A OG  
1122 N N   . ILE A 159 ? 0.1179 0.2730 0.0978 0.0239  0.0550  -0.0153 159 ILE A N   
1123 C CA  . ILE A 159 ? 0.1360 0.2666 0.1020 0.0194  0.0502  -0.0105 159 ILE A CA  
1124 C C   . ILE A 159 ? 0.1388 0.2661 0.0994 0.0395  0.0519  -0.0136 159 ILE A C   
1125 O O   . ILE A 159 ? 0.1769 0.2748 0.0947 0.0310  0.0513  0.0130  159 ILE A O   
1126 C CB  . ILE A 159 ? 0.1459 0.2706 0.1030 0.0130  0.0541  -0.0113 159 ILE A CB  
1127 C CG1 . ILE A 159 ? 0.1401 0.2694 0.1109 0.0069  0.0511  -0.0101 159 ILE A CG1 
1128 C CG2 . ILE A 159 ? 0.1688 0.2758 0.1077 0.0169  0.0501  -0.0112 159 ILE A CG2 
1129 C CD1 . ILE A 159 ? 0.1532 0.2754 0.1278 0.0042  0.0412  -0.0112 159 ILE A CD1 
1130 N N   . LYS A 160 ? 0.1374 0.2889 0.1054 0.0301  0.0549  -0.0098 160 LYS A N   
1131 C CA  . LYS A 160 ? 0.1641 0.2828 0.1163 0.0525  0.0407  -0.0203 160 LYS A CA  
1132 C C   . LYS A 160 ? 0.1597 0.2870 0.1207 0.0528  0.0477  -0.0148 160 LYS A C   
1133 O O   . LYS A 160 ? 0.2277 0.2983 0.1487 0.0405  0.0397  0.0042  160 LYS A O   
1134 C CB  . LYS A 160 ? 0.1647 0.3133 0.1560 0.0673  0.0303  -0.0241 160 LYS A CB  
1135 C CG  . LYS A 160 ? 0.1955 0.3549 0.1788 0.0570  0.0578  -0.0315 160 LYS A CG  
1136 C CD  . LYS A 160 ? 0.2209 0.4267 0.2259 0.0592  0.0701  -0.0234 160 LYS A CD  
1137 C CE  . LYS A 160 ? 0.3372 0.5058 0.2809 0.0735  0.0705  -0.0633 160 LYS A CE  
1138 N NZ  . LYS A 160 ? 0.3421 0.5684 0.3728 0.0846  0.0636  -0.0299 160 LYS A NZ  
1139 N N   . ALA A 161 ? 0.1634 0.2880 0.0978 0.0348  0.0414  -0.0221 161 ALA A N   
1140 C CA  . ALA A 161 ? 0.1763 0.3096 0.0953 0.0431  0.0564  -0.0208 161 ALA A CA  
1141 C C   . ALA A 161 ? 0.1781 0.3208 0.1006 0.0376  0.0525  -0.0124 161 ALA A C   
1142 O O   . ALA A 161 ? 0.1989 0.3603 0.1004 0.0183  0.0583  0.0024  161 ALA A O   
1143 C CB  . ALA A 161 ? 0.1518 0.3337 0.1045 0.0281  0.0682  -0.0194 161 ALA A CB  
1144 N N   . GLY A 162 ? 0.1742 0.3137 0.0777 0.0283  0.0571  -0.0070 162 GLY A N   
1145 C CA  . GLY A 162 ? 0.1698 0.3217 0.0921 0.0328  0.0447  -0.0039 162 GLY A CA  
1146 C C   . GLY A 162 ? 0.1673 0.3146 0.0896 0.0348  0.0508  0.0017  162 GLY A C   
1147 O O   . GLY A 162 ? 0.1804 0.3461 0.0962 0.0355  0.0713  -0.0039 162 GLY A O   
1148 N N   . ALA A 163 ? 0.1391 0.2917 0.0865 0.0285  0.0636  -0.0004 163 ALA A N   
1149 C CA  . ALA A 163 ? 0.1200 0.2802 0.0839 0.0212  0.0701  -0.0070 163 ALA A CA  
1150 C C   . ALA A 163 ? 0.1261 0.2831 0.0833 0.0173  0.0756  -0.0103 163 ALA A C   
1151 O O   . ALA A 163 ? 0.1251 0.3050 0.0945 0.0210  0.0654  -0.0232 163 ALA A O   
1152 C CB  . ALA A 163 ? 0.1302 0.2916 0.1130 0.0158  0.0732  0.0029  163 ALA A CB  
1153 N N   . ASP A 164 ? 0.1032 0.2696 0.0703 -0.0023 0.0716  -0.0120 164 ASP A N   
1154 C CA  . ASP A 164 ? 0.1097 0.2601 0.0798 -0.0122 0.0713  -0.0040 164 ASP A CA  
1155 C C   . ASP A 164 ? 0.0971 0.2571 0.0717 -0.0167 0.0596  -0.0089 164 ASP A C   
1156 O O   . ASP A 164 ? 0.1062 0.2742 0.0934 -0.0406 0.0592  -0.0102 164 ASP A O   
1157 C CB  . ASP A 164 ? 0.1339 0.2702 0.0875 -0.0181 0.0874  -0.0039 164 ASP A CB  
1158 C CG  . ASP A 164 ? 0.1710 0.2529 0.1134 -0.0241 0.0785  -0.0041 164 ASP A CG  
1159 O OD1 . ASP A 164 ? 0.2136 0.2716 0.1104 -0.0015 0.0801  -0.0241 164 ASP A OD1 
1160 O OD2 . ASP A 164 ? 0.2026 0.2661 0.1270 -0.0264 0.0875  -0.0128 164 ASP A OD2 
1161 N N   . PHE A 165 ? 0.0951 0.2638 0.0757 -0.0135 0.0596  0.0028  165 PHE A N   
1162 C CA  . PHE A 165 ? 0.0729 0.2588 0.0755 -0.0091 0.0676  0.0008  165 PHE A CA  
1163 C C   . PHE A 165 ? 0.0675 0.2549 0.0713 -0.0079 0.0629  -0.0149 165 PHE A C   
1164 O O   . PHE A 165 ? 0.0648 0.2637 0.0736 -0.0163 0.0615  -0.0096 165 PHE A O   
1165 C CB  . PHE A 165 ? 0.0894 0.2692 0.0893 -0.0025 0.0705  -0.0038 165 PHE A CB  
1166 C CG  . PHE A 165 ? 0.0928 0.2722 0.1033 -0.0125 0.0753  -0.0117 165 PHE A CG  
1167 C CD1 . PHE A 165 ? 0.0867 0.2900 0.1578 -0.0135 0.0820  0.0045  165 PHE A CD1 
1168 C CD2 . PHE A 165 ? 0.0987 0.2848 0.1253 -0.0080 0.0697  -0.0200 165 PHE A CD2 
1169 C CE1 . PHE A 165 ? 0.0937 0.3070 0.2066 -0.0246 0.0595  -0.0100 165 PHE A CE1 
1170 C CE2 . PHE A 165 ? 0.1216 0.3076 0.1680 -0.0061 0.0495  -0.0278 165 PHE A CE2 
1171 C CZ  . PHE A 165 ? 0.1043 0.3057 0.1740 -0.0073 0.0785  -0.0330 165 PHE A CZ  
1172 N N   . ILE A 166 ? 0.0866 0.2647 0.0637 -0.0058 0.0519  -0.0156 166 ILE A N   
1173 C CA  . ILE A 166 ? 0.0770 0.2682 0.0655 -0.0059 0.0617  -0.0168 166 ILE A CA  
1174 C C   . ILE A 166 ? 0.0653 0.2595 0.0688 -0.0076 0.0606  -0.0118 166 ILE A C   
1175 O O   . ILE A 166 ? 0.0813 0.2711 0.0772 -0.0268 0.0491  -0.0040 166 ILE A O   
1176 C CB  . ILE A 166 ? 0.0926 0.2880 0.0740 0.0051  0.0647  -0.0262 166 ILE A CB  
1177 C CG1 . ILE A 166 ? 0.1087 0.2930 0.0943 0.0043  0.0647  -0.0387 166 ILE A CG1 
1178 C CG2 . ILE A 166 ? 0.0891 0.3148 0.0856 0.0104  0.0786  -0.0242 166 ILE A CG2 
1179 C CD1 . ILE A 166 ? 0.1288 0.2941 0.0922 0.0054  0.0728  -0.0427 166 ILE A CD1 
1180 N N   . LYS A 167 ? 0.0652 0.2491 0.0868 -0.0124 0.0550  0.0057  167 LYS A N   
1181 C CA  . LYS A 167 ? 0.0738 0.2538 0.0636 -0.0139 0.0612  0.0086  167 LYS A CA  
1182 C C   . LYS A 167 ? 0.0488 0.2545 0.0845 -0.0022 0.0572  0.0138  167 LYS A C   
1183 O O   . LYS A 167 ? 0.0531 0.2756 0.0733 -0.0042 0.0550  0.0200  167 LYS A O   
1184 C CB  . LYS A 167 ? 0.0878 0.2837 0.0686 -0.0037 0.0629  -0.0029 167 LYS A CB  
1185 C CG  . LYS A 167 ? 0.0878 0.3003 0.0746 0.0029  0.0744  -0.0070 167 LYS A CG  
1186 C CD  . LYS A 167 ? 0.0655 0.2994 0.0952 -0.0006 0.0725  -0.0088 167 LYS A CD  
1187 C CE  . LYS A 167 ? 0.0957 0.3111 0.1199 0.0094  0.0742  -0.0089 167 LYS A CE  
1188 N NZ  . LYS A 167 ? 0.1245 0.3394 0.1343 0.0122  0.0868  -0.0146 167 LYS A NZ  
1189 N N   . THR A 168 ? 0.0523 0.2609 0.0920 -0.0047 0.0613  0.0257  168 THR A N   
1190 C CA  . THR A 168 ? 0.0710 0.2584 0.0825 0.0087  0.0702  0.0120  168 THR A CA  
1191 C C   . THR A 168 ? 0.0680 0.2603 0.0856 0.0036  0.0698  0.0093  168 THR A C   
1192 O O   . THR A 168 ? 0.0624 0.2904 0.0925 -0.0022 0.0629  0.0128  168 THR A O   
1193 C CB  . THR A 168 ? 0.0713 0.2635 0.0915 0.0156  0.0708  0.0111  168 THR A CB  
1194 O OG1 . THR A 168 ? 0.0764 0.2719 0.0795 0.0219  0.0709  0.0078  168 THR A OG1 
1195 C CG2 . THR A 168 ? 0.0736 0.2788 0.0981 0.0174  0.0588  0.0036  168 THR A CG2 
1196 N N   . SER A 169 ? 0.0746 0.2532 0.0859 -0.0029 0.0734  0.0090  169 SER A N   
1197 C CA  . SER A 169 ? 0.0692 0.2641 0.0872 -0.0049 0.0709  0.0088  169 SER A CA  
1198 C C   . SER A 169 ? 0.0785 0.2538 0.0907 -0.0110 0.0778  -0.0017 169 SER A C   
1199 O O   . SER A 169 ? 0.0813 0.2697 0.0911 -0.0162 0.0781  0.0123  169 SER A O   
1200 C CB  . SER A 169 ? 0.0861 0.2731 0.0808 -0.0023 0.0597  0.0099  169 SER A CB  
1201 O OG  . SER A 169 ? 0.1232 0.2780 0.0716 -0.0186 0.0775  0.0188  169 SER A OG  
1202 N N   . THR A 170 ? 0.0946 0.2594 0.0817 -0.0156 0.0727  -0.0036 170 THR A N   
1203 C CA  . THR A 170 ? 0.1095 0.2588 0.0810 -0.0119 0.0707  -0.0075 170 THR A CA  
1204 C C   . THR A 170 ? 0.1201 0.2794 0.0962 0.0060  0.0809  0.0032  170 THR A C   
1205 O O   . THR A 170 ? 0.1179 0.3169 0.1164 0.0271  0.0820  -0.0063 170 THR A O   
1206 C CB  . THR A 170 ? 0.1137 0.2576 0.1009 -0.0286 0.0706  0.0050  170 THR A CB  
1207 O OG1 . THR A 170 ? 0.1215 0.2732 0.1038 -0.0269 0.0798  0.0140  170 THR A OG1 
1208 C CG2 . THR A 170 ? 0.0898 0.2643 0.0980 -0.0236 0.0766  0.0112  170 THR A CG2 
1209 N N   . GLY A 171 ? 0.1256 0.2810 0.1146 0.0026  0.0843  0.0231  171 GLY A N   
1210 C CA  . GLY A 171 ? 0.1375 0.2909 0.1375 0.0059  0.0822  0.0238  171 GLY A CA  
1211 C C   . GLY A 171 ? 0.1539 0.2805 0.1756 0.0092  0.0732  0.0312  171 GLY A C   
1212 O O   . GLY A 171 ? 0.2220 0.3111 0.3029 0.0352  0.0540  0.0293  171 GLY A O   
1213 N N   . ARG A 172 ? 0.1400 0.2797 0.1702 -0.0013 0.0770  0.0081  172 ARG A N   
1214 C CA  . ARG A 172 ? 0.1945 0.3084 0.1917 -0.0293 0.0710  0.0230  172 ARG A CA  
1215 C C   . ARG A 172 ? 0.1984 0.3027 0.2000 -0.0458 0.0751  0.0064  172 ARG A C   
1216 O O   . ARG A 172 ? 0.2657 0.3552 0.2237 -0.1026 0.1084  -0.0061 172 ARG A O   
1217 C CB  . ARG A 172 ? 0.1906 0.2998 0.1869 -0.0276 0.0754  0.0268  172 ARG A CB  
1218 C CG  . ARG A 172 ? 0.2077 0.3246 0.1923 -0.0019 0.0980  0.0132  172 ARG A CG  
1219 C CD  . ARG A 172 ? 0.2512 0.3750 0.2359 0.0272  0.1165  -0.0059 172 ARG A CD  
1220 N NE  . ARG A 172 ? 0.3201 0.4632 0.2605 -0.0066 0.1505  -0.0311 172 ARG A NE  
1221 C CZ  . ARG A 172 ? 0.3618 0.5552 0.3181 -0.0158 0.1878  -0.0425 172 ARG A CZ  
1222 N NH1 . ARG A 172 ? 0.3355 0.5635 0.4040 0.0298  0.1681  -0.0761 172 ARG A NH1 
1223 N NH2 . ARG A 172 ? 0.4127 0.6607 0.3784 0.0087  0.2317  -0.0479 172 ARG A NH2 
1224 N N   . VAL A 173 ? 0.1964 0.3108 0.1545 -0.0587 0.0728  0.0254  173 VAL A N   
1225 C CA  . VAL A 173 ? 0.1954 0.3067 0.1606 -0.0421 0.0837  0.0402  173 VAL A CA  
1226 C C   . VAL A 173 ? 0.2037 0.3313 0.1771 -0.0571 0.0718  0.0414  173 VAL A C   
1227 O O   . VAL A 173 ? 0.2161 0.3530 0.1881 -0.0436 0.0735  0.0390  173 VAL A O   
1228 C CB  . VAL A 173 ? 0.2090 0.3233 0.1479 -0.0308 0.0995  0.0364  173 VAL A CB  
1229 C CG1 . VAL A 173 ? 0.2230 0.3256 0.1386 -0.0237 0.1024  0.0014  173 VAL A CG1 
1230 C CG2 . VAL A 173 ? 0.2358 0.3289 0.1272 -0.0207 0.0962  0.0290  173 VAL A CG2 
1231 N N   . ALA A 174 ? 0.2254 0.3497 0.2121 -0.0616 0.0848  0.0545  174 ALA A N   
1232 C CA  . ALA A 174 ? 0.2582 0.3454 0.1967 -0.0633 0.0972  0.0682  174 ALA A CA  
1233 C C   . ALA A 174 ? 0.2315 0.3353 0.1709 -0.0454 0.0949  0.0752  174 ALA A C   
1234 O O   . ALA A 174 ? 0.2551 0.3884 0.2211 -0.0126 0.0548  0.0971  174 ALA A O   
1235 C CB  . ALA A 174 ? 0.3001 0.3539 0.1941 -0.0832 0.1153  0.0801  174 ALA A CB  
1236 N N   . VAL A 175 ? 0.1848 0.3367 0.1725 -0.0337 0.0845  0.0848  175 VAL A N   
1237 C CA  . VAL A 175 ? 0.1444 0.3203 0.1520 -0.0152 0.0919  0.0617  175 VAL A CA  
1238 C C   . VAL A 175 ? 0.1167 0.3082 0.1259 -0.0039 0.0794  0.0508  175 VAL A C   
1239 O O   . VAL A 175 ? 0.0949 0.3010 0.1398 -0.0046 0.0843  0.0596  175 VAL A O   
1240 C CB  . VAL A 175 ? 0.1556 0.3509 0.1498 -0.0489 0.1147  0.0637  175 VAL A CB  
1241 C CG1 . VAL A 175 ? 0.1890 0.3716 0.1494 -0.0388 0.0950  0.0545  175 VAL A CG1 
1242 C CG2 . VAL A 175 ? 0.1852 0.3843 0.1578 -0.0663 0.1377  0.0757  175 VAL A CG2 
1243 N N   . ASN A 176 ? 0.1244 0.3136 0.1194 -0.0276 0.0849  0.0333  176 ASN A N   
1244 C CA  . ASN A 176 ? 0.1035 0.3040 0.1115 -0.0252 0.0985  0.0135  176 ASN A CA  
1245 C C   . ASN A 176 ? 0.1069 0.3129 0.0940 -0.0138 0.0931  0.0089  176 ASN A C   
1246 O O   . ASN A 176 ? 0.1328 0.3586 0.0936 -0.0044 0.1050  -0.0074 176 ASN A O   
1247 C CB  . ASN A 176 ? 0.1471 0.2916 0.1218 -0.0200 0.1206  -0.0007 176 ASN A CB  
1248 C CG  . ASN A 176 ? 0.2035 0.2953 0.1468 -0.0235 0.1081  0.0077  176 ASN A CG  
1249 O OD1 . ASN A 176 ? 0.3680 0.3244 0.2318 -0.0208 0.1012  0.0114  176 ASN A OD1 
1250 N ND2 . ASN A 176 ? 0.2017 0.2631 0.1147 -0.0382 0.1065  0.0006  176 ASN A ND2 
1251 N N   . ALA A 177 ? 0.0903 0.3040 0.0808 -0.0052 0.0785  0.0123  177 ALA A N   
1252 C CA  . ALA A 177 ? 0.1018 0.2997 0.0770 -0.0013 0.0812  0.0202  177 ALA A CA  
1253 C C   . ALA A 177 ? 0.0853 0.2902 0.0774 0.0002  0.0739  0.0239  177 ALA A C   
1254 O O   . ALA A 177 ? 0.1272 0.3085 0.0725 0.0060  0.0844  0.0332  177 ALA A O   
1255 C CB  . ALA A 177 ? 0.1112 0.2917 0.0921 -0.0073 0.0934  0.0209  177 ALA A CB  
1256 N N   . THR A 178 ? 0.0939 0.3129 0.0690 0.0049  0.0740  0.0111  178 THR A N   
1257 C CA  . THR A 178 ? 0.0943 0.3126 0.0762 -0.0003 0.0776  0.0205  178 THR A CA  
1258 C C   . THR A 178 ? 0.0847 0.3054 0.0856 0.0016  0.0781  0.0221  178 THR A C   
1259 O O   . THR A 178 ? 0.0973 0.3073 0.0584 0.0085  0.0586  0.0199  178 THR A O   
1260 C CB  . THR A 178 ? 0.1025 0.3238 0.0973 -0.0053 0.0909  0.0351  178 THR A CB  
1261 O OG1 . THR A 178 ? 0.1196 0.3322 0.1052 0.0101  0.1049  0.0327  178 THR A OG1 
1262 C CG2 . THR A 178 ? 0.1214 0.3338 0.0829 -0.0071 0.0841  0.0298  178 THR A CG2 
1263 N N   . PRO A 179 ? 0.1019 0.3236 0.0768 -0.0026 0.0811  0.0208  179 PRO A N   
1264 C CA  . PRO A 179 ? 0.1062 0.3188 0.0669 -0.0112 0.0763  0.0176  179 PRO A CA  
1265 C C   . PRO A 179 ? 0.1153 0.3091 0.0711 -0.0064 0.0662  0.0118  179 PRO A C   
1266 O O   . PRO A 179 ? 0.1234 0.3320 0.0851 -0.0133 0.0940  0.0226  179 PRO A O   
1267 C CB  . PRO A 179 ? 0.1514 0.3342 0.0852 -0.0099 0.0572  0.0118  179 PRO A CB  
1268 C CG  . PRO A 179 ? 0.1494 0.3390 0.1199 -0.0046 0.0559  0.0074  179 PRO A CG  
1269 C CD  . PRO A 179 ? 0.1166 0.3315 0.1008 -0.0085 0.0745  0.0191  179 PRO A CD  
1270 N N   . GLU A 180 ? 0.1181 0.3252 0.0514 -0.0037 0.0605  0.0111  180 GLU A N   
1271 C CA  . GLU A 180 ? 0.1256 0.3373 0.0981 0.0006  0.0654  0.0206  180 GLU A CA  
1272 C C   . GLU A 180 ? 0.0832 0.3169 0.0951 -0.0114 0.0800  0.0157  180 GLU A C   
1273 O O   . GLU A 180 ? 0.1063 0.3138 0.0737 0.0014  0.0802  0.0048  180 GLU A O   
1274 C CB  . GLU A 180 ? 0.1544 0.3645 0.1147 -0.0040 0.0800  0.0279  180 GLU A CB  
1275 C CG  . GLU A 180 ? 0.2427 0.4096 0.1734 0.0069  0.0518  0.0250  180 GLU A CG  
1276 C CD  . GLU A 180 ? 0.3208 0.4418 0.2161 0.0161  0.0512  -0.0108 180 GLU A CD  
1277 O OE1 . GLU A 180 ? 0.3751 0.4265 0.2666 0.0457  0.1739  -0.0340 180 GLU A OE1 
1278 O OE2 . GLU A 180 ? 0.3810 0.5632 0.2872 -0.0004 -0.0166 -0.0209 180 GLU A OE2 
1279 N N   . SER A 181 ? 0.0806 0.3341 0.0858 -0.0118 0.0725  0.0107  181 SER A N   
1280 C CA  . SER A 181 ? 0.1057 0.3379 0.0867 0.0106  0.0631  0.0062  181 SER A CA  
1281 C C   . SER A 181 ? 0.1088 0.3115 0.0753 0.0145  0.0579  0.0009  181 SER A C   
1282 O O   . SER A 181 ? 0.1270 0.3095 0.0705 0.0061  0.0794  0.0034  181 SER A O   
1283 C CB  . SER A 181 ? 0.1660 0.3802 0.0667 0.0355  0.0570  -0.0100 181 SER A CB  
1284 O OG  . SER A 181 ? 0.1636 0.4053 0.1354 0.0163  0.0432  0.0056  181 SER A OG  
1285 N N   . ALA A 182 ? 0.1079 0.3060 0.0578 0.0248  0.0668  0.0015  182 ALA A N   
1286 C CA  . ALA A 182 ? 0.1174 0.3175 0.0780 0.0141  0.0702  0.0103  182 ALA A CA  
1287 C C   . ALA A 182 ? 0.1142 0.3118 0.0851 0.0135  0.0655  0.0191  182 ALA A C   
1288 O O   . ALA A 182 ? 0.1117 0.3250 0.1022 0.0159  0.0851  0.0097  182 ALA A O   
1289 C CB  . ALA A 182 ? 0.1483 0.3156 0.0795 0.0273  0.0692  0.0134  182 ALA A CB  
1290 N N   . ARG A 183 ? 0.1146 0.3146 0.0854 0.0076  0.0750  0.0102  183 ARG A N   
1291 C CA  . ARG A 183 ? 0.1469 0.3086 0.0982 0.0149  0.0591  -0.0056 183 ARG A CA  
1292 C C   . ARG A 183 ? 0.1568 0.3076 0.0613 0.0127  0.0587  -0.0121 183 ARG A C   
1293 O O   . ARG A 183 ? 0.1447 0.3139 0.0953 0.0160  0.0699  -0.0132 183 ARG A O   
1294 C CB  . ARG A 183 ? 0.1818 0.3420 0.1219 0.0096  0.0442  0.0091  183 ARG A CB  
1295 C CG  . ARG A 183 ? 0.2347 0.3742 0.1364 0.0090  0.0341  -0.0169 183 ARG A CG  
1296 C CD  . ARG A 183 ? 0.3360 0.4299 0.1507 0.0047  0.0564  -0.0166 183 ARG A CD  
1297 N NE  . ARG A 183 ? 0.4159 0.4589 0.2508 -0.0224 0.0805  -0.0012 183 ARG A NE  
1298 C CZ  . ARG A 183 ? 0.4069 0.5251 0.3381 -0.0226 0.0837  0.0285  183 ARG A CZ  
1299 N NH1 . ARG A 183 ? 0.4365 0.5494 0.4095 0.0075  0.0674  0.0392  183 ARG A NH1 
1300 N NH2 . ARG A 183 ? 0.4499 0.5831 0.3800 -0.0466 0.0905  0.0108  183 ARG A NH2 
1301 N N   . ILE A 184 ? 0.1398 0.3085 0.0597 0.0147  0.0665  0.0003  184 ILE A N   
1302 C CA  . ILE A 184 ? 0.1292 0.3086 0.0614 0.0298  0.0714  -0.0081 184 ILE A CA  
1303 C C   . ILE A 184 ? 0.1209 0.2948 0.0699 0.0250  0.0582  -0.0130 184 ILE A C   
1304 O O   . ILE A 184 ? 0.1295 0.3046 0.1097 0.0338  0.0768  -0.0250 184 ILE A O   
1305 C CB  . ILE A 184 ? 0.1548 0.3382 0.0880 0.0123  0.0631  0.0008  184 ILE A CB  
1306 C CG1 . ILE A 184 ? 0.1676 0.3550 0.1052 0.0178  0.0592  0.0303  184 ILE A CG1 
1307 C CG2 . ILE A 184 ? 0.1104 0.3625 0.0986 0.0088  0.0848  0.0051  184 ILE A CG2 
1308 C CD1 . ILE A 184 ? 0.1311 0.3691 0.1373 0.0293  0.0760  0.0491  184 ILE A CD1 
1309 N N   . MET A 185 ? 0.1149 0.2867 0.0759 0.0225  0.0559  -0.0129 185 MET A N   
1310 C CA  . MET A 185 ? 0.1152 0.2804 0.0742 0.0151  0.0501  -0.0127 185 MET A CA  
1311 C C   . MET A 185 ? 0.1339 0.2771 0.0641 0.0129  0.0557  -0.0171 185 MET A C   
1312 O O   . MET A 185 ? 0.1257 0.2914 0.0744 0.0065  0.0897  -0.0084 185 MET A O   
1313 C CB  . MET A 185 ? 0.0955 0.2785 0.0834 0.0091  0.0763  -0.0169 185 MET A CB  
1314 C CG  . MET A 185 ? 0.0993 0.2960 0.0911 0.0111  0.0721  -0.0198 185 MET A CG  
1315 S SD  . MET A 185 ? 0.0884 0.2969 0.1134 0.0040  0.0796  -0.0157 185 MET A SD  
1316 C CE  . MET A 185 ? 0.1429 0.3377 0.0893 -0.0039 0.1050  -0.0301 185 MET A CE  
1317 N N   . MET A 186 ? 0.1301 0.2812 0.0695 0.0063  0.0485  -0.0144 186 MET A N   
1318 C CA  . MET A 186 ? 0.1466 0.2818 0.0744 0.0044  0.0557  -0.0183 186 MET A CA  
1319 C C   . MET A 186 ? 0.1447 0.2780 0.0781 0.0001  0.0586  -0.0225 186 MET A C   
1320 O O   . MET A 186 ? 0.1318 0.2850 0.1227 0.0040  0.0527  -0.0150 186 MET A O   
1321 C CB  . MET A 186 ? 0.1371 0.2977 0.0808 0.0028  0.0469  -0.0289 186 MET A CB  
1322 C CG  . MET A 186 ? 0.1455 0.3152 0.1044 0.0175  0.0406  -0.0456 186 MET A CG  
1323 S SD  . MET A 186 ? 0.1228 0.3502 0.1797 0.0111  0.0587  -0.0456 186 MET A SD  
1324 C CE  . MET A 186 ? 0.1609 0.3748 0.1690 0.0076  0.0825  -0.0334 186 MET A CE  
1325 N N   . GLU A 187 ? 0.1475 0.2980 0.0876 0.0096  0.0650  -0.0174 187 GLU A N   
1326 C CA  . GLU A 187 ? 0.1503 0.3100 0.1013 0.0120  0.0543  -0.0299 187 GLU A CA  
1327 C C   . GLU A 187 ? 0.1528 0.3059 0.0942 0.0100  0.0669  -0.0266 187 GLU A C   
1328 O O   . GLU A 187 ? 0.2133 0.3066 0.1145 0.0021  0.0389  -0.0292 187 GLU A O   
1329 C CB  . GLU A 187 ? 0.1748 0.3329 0.1136 0.0163  0.0699  -0.0165 187 GLU A CB  
1330 C CG  . GLU A 187 ? 0.2026 0.3990 0.1039 0.0337  0.0865  -0.0175 187 GLU A CG  
1331 C CD  . GLU A 187 ? 0.2369 0.4738 0.1431 0.0310  0.1041  0.0228  187 GLU A CD  
1332 O OE1 . GLU A 187 ? 0.2558 0.5991 0.2696 0.0158  0.1069  0.0681  187 GLU A OE1 
1333 O OE2 . GLU A 187 ? 0.3245 0.5289 0.1539 0.0716  0.0882  0.0114  187 GLU A OE2 
1334 N N   . VAL A 188 ? 0.1376 0.3124 0.0916 0.0121  0.0653  -0.0269 188 VAL A N   
1335 C CA  . VAL A 188 ? 0.1417 0.3154 0.1083 0.0274  0.0718  -0.0209 188 VAL A CA  
1336 C C   . VAL A 188 ? 0.1625 0.2927 0.0942 0.0335  0.0533  -0.0158 188 VAL A C   
1337 O O   . VAL A 188 ? 0.1736 0.3088 0.1163 0.0470  0.0697  -0.0343 188 VAL A O   
1338 C CB  . VAL A 188 ? 0.1314 0.3205 0.1218 0.0270  0.0687  -0.0171 188 VAL A CB  
1339 C CG1 . VAL A 188 ? 0.1246 0.3192 0.1112 0.0312  0.0934  -0.0126 188 VAL A CG1 
1340 C CG2 . VAL A 188 ? 0.1574 0.3231 0.1092 0.0263  0.0790  -0.0076 188 VAL A CG2 
1341 N N   . ILE A 189 ? 0.1489 0.2655 0.1055 0.0280  0.0524  -0.0203 189 ILE A N   
1342 C CA  . ILE A 189 ? 0.1607 0.2596 0.1070 0.0193  0.0469  -0.0080 189 ILE A CA  
1343 C C   . ILE A 189 ? 0.1565 0.2675 0.1125 0.0182  0.0603  -0.0159 189 ILE A C   
1344 O O   . ILE A 189 ? 0.2033 0.2811 0.1169 0.0117  0.0681  -0.0195 189 ILE A O   
1345 C CB  . ILE A 189 ? 0.1402 0.2671 0.1047 0.0071  0.0477  -0.0072 189 ILE A CB  
1346 C CG1 . ILE A 189 ? 0.1444 0.2596 0.1260 0.0032  0.0374  -0.0073 189 ILE A CG1 
1347 C CG2 . ILE A 189 ? 0.1570 0.2907 0.0888 -0.0108 0.0476  -0.0123 189 ILE A CG2 
1348 C CD1 . ILE A 189 ? 0.1253 0.2689 0.1022 0.0021  0.0456  -0.0157 189 ILE A CD1 
1349 N N   . ARG A 190 ? 0.1966 0.2723 0.1206 0.0261  0.0453  -0.0238 190 ARG A N   
1350 C CA  . ARG A 190 ? 0.2118 0.2942 0.1416 0.0258  0.0301  -0.0362 190 ARG A CA  
1351 C C   . ARG A 190 ? 0.2279 0.2995 0.1607 0.0437  0.0299  -0.0417 190 ARG A C   
1352 O O   . ARG A 190 ? 0.2210 0.3050 0.2259 0.0347  0.0380  -0.0605 190 ARG A O   
1353 C CB  . ARG A 190 ? 0.2255 0.3202 0.1591 0.0295  0.0184  -0.0313 190 ARG A CB  
1354 C CG  . ARG A 190 ? 0.2630 0.3518 0.1702 0.0235  0.0308  -0.0592 190 ARG A CG  
1355 C CD  . ARG A 190 ? 0.3027 0.4089 0.1845 0.0325  0.0485  -0.0537 190 ARG A CD  
1356 N NE  . ARG A 190 ? 0.3355 0.4550 0.1732 0.0369  0.0699  -0.0575 190 ARG A NE  
1357 C CZ  . ARG A 190 ? 0.3831 0.5201 0.1915 0.0623  0.0841  -0.0243 190 ARG A CZ  
1358 N NH1 . ARG A 190 ? 0.3653 0.5553 0.1581 0.0640  0.0900  -0.0488 190 ARG A NH1 
1359 N NH2 . ARG A 190 ? 0.3808 0.5525 0.2330 0.0581  0.0931  -0.0053 190 ARG A NH2 
1360 N N   . ASP A 191 ? 0.2280 0.3248 0.1785 0.0636  0.0432  -0.0462 191 ASP A N   
1361 C CA  . ASP A 191 ? 0.2605 0.3459 0.1989 0.0839  0.0630  -0.0277 191 ASP A CA  
1362 C C   . ASP A 191 ? 0.2360 0.3225 0.1766 0.0722  0.0730  -0.0421 191 ASP A C   
1363 O O   . ASP A 191 ? 0.2751 0.3288 0.1995 0.0596  0.0963  -0.0321 191 ASP A O   
1364 C CB  . ASP A 191 ? 0.2711 0.3630 0.2142 0.0977  0.0789  -0.0197 191 ASP A CB  
1365 C CG  . ASP A 191 ? 0.2853 0.4255 0.2041 0.0855  0.1064  -0.0089 191 ASP A CG  
1366 O OD1 . ASP A 191 ? 0.3562 0.4817 0.1934 0.0548  0.1097  -0.0375 191 ASP A OD1 
1367 O OD2 . ASP A 191 ? 0.2762 0.4747 0.2521 0.0728  0.1348  0.0154  191 ASP A OD2 
1368 N N   . MET A 192 ? 0.2114 0.3136 0.1720 0.0685  0.0657  -0.0448 192 MET A N   
1369 C CA  . MET A 192 ? 0.2160 0.3230 0.1895 0.0750  0.0327  -0.0312 192 MET A CA  
1370 C C   . MET A 192 ? 0.2620 0.3169 0.1747 0.0808  0.0435  -0.0269 192 MET A C   
1371 O O   . MET A 192 ? 0.2714 0.3261 0.2151 0.0663  0.0410  0.0122  192 MET A O   
1372 C CB  . MET A 192 ? 0.2348 0.3405 0.1481 0.0705  0.0355  -0.0251 192 MET A CB  
1373 C CG  . MET A 192 ? 0.2490 0.3553 0.1539 0.0611  0.0299  -0.0168 192 MET A CG  
1374 S SD  . MET A 192 ? 0.2321 0.3682 0.1786 0.0591  0.0285  -0.0306 192 MET A SD  
1375 C CE  . MET A 192 ? 0.2874 0.3683 0.1710 0.0991  0.0401  -0.0662 192 MET A CE  
1376 N N   . GLY A 193 ? 0.2785 0.3189 0.1942 0.0485  0.0443  -0.0585 193 GLY A N   
1377 C CA  . GLY A 193 ? 0.2966 0.3031 0.1825 0.0329  0.0573  -0.0577 193 GLY A CA  
1378 C C   . GLY A 193 ? 0.2978 0.3064 0.1663 0.0258  0.0494  -0.0410 193 GLY A C   
1379 O O   . GLY A 193 ? 0.2958 0.3351 0.2154 0.0205  0.0459  -0.0293 193 GLY A O   
1380 N N   . VAL A 194 ? 0.2598 0.2793 0.1257 0.0177  0.0443  -0.0329 194 VAL A N   
1381 C CA  . VAL A 194 ? 0.2281 0.2738 0.1173 0.0160  0.0364  -0.0332 194 VAL A CA  
1382 C C   . VAL A 194 ? 0.2009 0.2623 0.1180 -0.0019 0.0472  -0.0285 194 VAL A C   
1383 O O   . VAL A 194 ? 0.2264 0.2703 0.1361 -0.0042 0.0348  -0.0401 194 VAL A O   
1384 C CB  . VAL A 194 ? 0.2097 0.2819 0.1112 0.0249  0.0502  -0.0347 194 VAL A CB  
1385 C CG1 . VAL A 194 ? 0.2264 0.2994 0.1378 0.0217  0.0503  -0.0191 194 VAL A CG1 
1386 C CG2 . VAL A 194 ? 0.2082 0.2893 0.0987 0.0200  0.0413  -0.0440 194 VAL A CG2 
1387 N N   . GLU A 195 ? 0.1987 0.2959 0.1339 -0.0059 0.0632  -0.0305 195 GLU A N   
1388 C CA  . GLU A 195 ? 0.1980 0.2966 0.1392 -0.0125 0.0583  -0.0155 195 GLU A CA  
1389 C C   . GLU A 195 ? 0.2068 0.2912 0.1491 -0.0124 0.0524  -0.0135 195 GLU A C   
1390 O O   . GLU A 195 ? 0.2111 0.3013 0.1849 0.0072  0.0467  0.0034  195 GLU A O   
1391 C CB  . GLU A 195 ? 0.2101 0.3686 0.1419 -0.0033 0.0769  -0.0295 195 GLU A CB  
1392 C CG  . GLU A 195 ? 0.2399 0.4152 0.1800 -0.0261 0.0658  -0.0521 195 GLU A CG  
1393 C CD  . GLU A 195 ? 0.3568 0.4414 0.2534 -0.0116 0.0518  -0.0835 195 GLU A CD  
1394 O OE1 . GLU A 195 ? 0.3574 0.4556 0.2889 0.0243  -0.0275 -0.1308 195 GLU A OE1 
1395 O OE2 . GLU A 195 ? 0.4310 0.5034 0.3970 -0.0446 0.0731  -0.1085 195 GLU A OE2 
1396 N N   . LYS A 196 ? 0.1970 0.2843 0.1857 -0.0171 0.0487  -0.0182 196 LYS A N   
1397 C CA  . LYS A 196 ? 0.2173 0.3020 0.2070 -0.0152 0.0788  -0.0190 196 LYS A CA  
1398 C C   . LYS A 196 ? 0.1961 0.2968 0.1973 -0.0247 0.0766  -0.0109 196 LYS A C   
1399 O O   . LYS A 196 ? 0.2185 0.3416 0.2085 0.0074  0.0761  -0.0273 196 LYS A O   
1400 C CB  . LYS A 196 ? 0.2669 0.3336 0.2567 -0.0266 0.0981  0.0039  196 LYS A CB  
1401 C CG  . LYS A 196 ? 0.3706 0.4150 0.3248 -0.0394 0.0694  -0.0117 196 LYS A CG  
1402 C CD  . LYS A 196 ? 0.5097 0.4463 0.4242 -0.0606 0.0443  -0.0156 196 LYS A CD  
1403 C CE  . LYS A 196 ? 0.5431 0.5415 0.4896 -0.0729 0.0309  -0.0351 196 LYS A CE  
1404 N NZ  . LYS A 196 ? 0.6075 0.5820 0.4904 -0.1022 0.0560  -0.0103 196 LYS A NZ  
1405 N N   . SER A 197 ? 0.1767 0.2701 0.1856 -0.0012 0.0791  -0.0259 197 SER A N   
1406 C CA  . SER A 197 ? 0.2166 0.2681 0.1769 -0.0208 0.0612  -0.0171 197 SER A CA  
1407 C C   . SER A 197 ? 0.2153 0.2622 0.1187 -0.0147 0.0579  -0.0062 197 SER A C   
1408 O O   . SER A 197 ? 0.2320 0.2720 0.1301 -0.0194 0.0652  -0.0184 197 SER A O   
1409 C CB  . SER A 197 ? 0.2701 0.3060 0.2037 -0.0105 0.0436  -0.0132 197 SER A CB  
1410 O OG  . SER A 197 ? 0.2888 0.3169 0.2058 -0.0021 0.0346  -0.0006 197 SER A OG  
1411 N N   . VAL A 198 ? 0.1729 0.2684 0.0993 0.0018  0.0597  -0.0102 198 VAL A N   
1412 C CA  . VAL A 198 ? 0.1563 0.2715 0.0863 0.0020  0.0659  -0.0148 198 VAL A CA  
1413 C C   . VAL A 198 ? 0.1434 0.2661 0.0998 -0.0060 0.0565  -0.0156 198 VAL A C   
1414 O O   . VAL A 198 ? 0.1632 0.2935 0.0906 0.0229  0.0386  -0.0117 198 VAL A O   
1415 C CB  . VAL A 198 ? 0.1547 0.2837 0.0993 0.0123  0.0631  -0.0156 198 VAL A CB  
1416 C CG1 . VAL A 198 ? 0.1397 0.3023 0.0979 0.0177  0.0748  -0.0253 198 VAL A CG1 
1417 C CG2 . VAL A 198 ? 0.1770 0.2825 0.1181 0.0073  0.0463  -0.0240 198 VAL A CG2 
1418 N N   . GLY A 199 ? 0.1187 0.2550 0.0918 -0.0176 0.0555  -0.0097 199 GLY A N   
1419 C CA  . GLY A 199 ? 0.0989 0.2448 0.0960 -0.0196 0.0590  -0.0029 199 GLY A CA  
1420 C C   . GLY A 199 ? 0.0755 0.2510 0.0745 -0.0100 0.0639  -0.0082 199 GLY A C   
1421 O O   . GLY A 199 ? 0.0703 0.2704 0.0638 -0.0144 0.0564  -0.0093 199 GLY A O   
1422 N N   . PHE A 200 ? 0.0727 0.2461 0.0888 -0.0008 0.0635  -0.0075 200 PHE A N   
1423 C CA  . PHE A 200 ? 0.0713 0.2580 0.0812 -0.0059 0.0637  0.0068  200 PHE A CA  
1424 C C   . PHE A 200 ? 0.0662 0.2639 0.0732 -0.0059 0.0631  0.0057  200 PHE A C   
1425 O O   . PHE A 200 ? 0.0544 0.2679 0.1121 -0.0036 0.0684  -0.0108 200 PHE A O   
1426 C CB  . PHE A 200 ? 0.0873 0.2748 0.0810 -0.0030 0.0635  0.0045  200 PHE A CB  
1427 C CG  . PHE A 200 ? 0.0912 0.2873 0.0602 -0.0116 0.0658  0.0050  200 PHE A CG  
1428 C CD1 . PHE A 200 ? 0.0928 0.3043 0.0831 -0.0012 0.0814  0.0027  200 PHE A CD1 
1429 C CD2 . PHE A 200 ? 0.1033 0.2982 0.0961 -0.0228 0.0542  0.0145  200 PHE A CD2 
1430 C CE1 . PHE A 200 ? 0.0930 0.3089 0.0975 -0.0032 0.0884  0.0143  200 PHE A CE1 
1431 C CE2 . PHE A 200 ? 0.1269 0.3125 0.1098 -0.0170 0.0461  0.0333  200 PHE A CE2 
1432 C CZ  . PHE A 200 ? 0.1093 0.3137 0.0895 -0.0183 0.0898  0.0222  200 PHE A CZ  
1433 N N   A LYS A 201 ? 0.0695 0.2774 0.0761 -0.0077 0.0662  0.0017  201 LYS A N   
1434 N N   B LYS A 201 ? 0.0633 0.2743 0.0790 -0.0055 0.0642  0.0032  201 LYS A N   
1435 C CA  A LYS A 201 ? 0.0745 0.2848 0.0733 -0.0107 0.0672  0.0025  201 LYS A CA  
1436 C CA  B LYS A 201 ? 0.0625 0.2797 0.0801 -0.0075 0.0641  0.0057  201 LYS A CA  
1437 C C   A LYS A 201 ? 0.0657 0.2933 0.0773 -0.0131 0.0645  0.0024  201 LYS A C   
1438 C C   B LYS A 201 ? 0.0606 0.2909 0.0806 -0.0119 0.0630  0.0037  201 LYS A C   
1439 O O   A LYS A 201 ? 0.0723 0.3204 0.0840 -0.0034 0.0716  0.0007  201 LYS A O   
1440 O O   B LYS A 201 ? 0.0684 0.3181 0.0862 -0.0024 0.0704  0.0022  201 LYS A O   
1441 C CB  A LYS A 201 ? 0.0805 0.3009 0.0746 -0.0109 0.0704  0.0101  201 LYS A CB  
1442 C CB  B LYS A 201 ? 0.0593 0.2894 0.0809 -0.0045 0.0623  0.0139  201 LYS A CB  
1443 C CG  A LYS A 201 ? 0.0828 0.3086 0.0876 -0.0064 0.0785  0.0076  201 LYS A CG  
1444 C CG  B LYS A 201 ? 0.0497 0.2925 0.1045 0.0024  0.0651  0.0142  201 LYS A CG  
1445 C CD  A LYS A 201 ? 0.0948 0.3119 0.0899 0.0009  0.0859  -0.0057 201 LYS A CD  
1446 C CD  B LYS A 201 ? 0.0578 0.2898 0.1113 0.0148  0.0624  0.0045  201 LYS A CD  
1447 C CE  A LYS A 201 ? 0.1069 0.3176 0.1107 0.0016  0.0865  -0.0074 201 LYS A CE  
1448 C CE  B LYS A 201 ? 0.0608 0.2922 0.1494 0.0217  0.0487  0.0070  201 LYS A CE  
1449 N NZ  A LYS A 201 ? 0.1082 0.3277 0.1158 0.0077  0.1000  -0.0129 201 LYS A NZ  
1450 N NZ  B LYS A 201 ? 0.0682 0.2775 0.1614 0.0248  0.0412  0.0103  201 LYS A NZ  
1451 N N   . VAL A 202 ? 0.0647 0.2967 0.0877 -0.0034 0.0684  0.0146  202 VAL A N   
1452 C CA  . VAL A 202 ? 0.0729 0.2892 0.1019 -0.0029 0.0681  0.0237  202 VAL A CA  
1453 C C   . VAL A 202 ? 0.0486 0.2829 0.1079 -0.0085 0.0643  0.0185  202 VAL A C   
1454 O O   . VAL A 202 ? 0.0584 0.2934 0.1505 -0.0105 0.0857  0.0118  202 VAL A O   
1455 C CB  . VAL A 202 ? 0.1617 0.3306 0.1024 -0.0185 0.0646  0.0442  202 VAL A CB  
1456 C CG1 . VAL A 202 ? 0.1913 0.3649 0.1761 -0.0051 0.0315  0.0432  202 VAL A CG1 
1457 C CG2 . VAL A 202 ? 0.2140 0.3390 0.1217 -0.0606 0.0422  0.0639  202 VAL A CG2 
1458 N N   . THR A 203 ? 0.0428 0.2963 0.1142 -0.0053 0.0622  0.0138  203 THR A N   
1459 C CA  . THR A 203 ? 0.0552 0.3069 0.1190 -0.0148 0.0723  0.0187  203 THR A CA  
1460 C C   . THR A 203 ? 0.0588 0.2975 0.1318 -0.0105 0.0792  0.0159  203 THR A C   
1461 O O   . THR A 203 ? 0.0901 0.3058 0.1106 -0.0243 0.0905  0.0168  203 THR A O   
1462 C CB  . THR A 203 ? 0.0687 0.3514 0.1237 -0.0176 0.0707  0.0114  203 THR A CB  
1463 O OG1 . THR A 203 ? 0.1370 0.3871 0.1499 -0.0300 0.0560  0.0473  203 THR A OG1 
1464 C CG2 . THR A 203 ? 0.0827 0.3586 0.1106 -0.0028 0.0859  0.0284  203 THR A CG2 
1465 N N   . GLY A 204 ? 0.0981 0.3076 0.1411 -0.0063 0.1088  0.0285  204 GLY A N   
1466 C CA  . GLY A 204 ? 0.1363 0.3072 0.2045 -0.0047 0.0958  0.0491  204 GLY A CA  
1467 C C   . GLY A 204 ? 0.1672 0.3345 0.2106 0.0146  0.1004  0.0393  204 GLY A C   
1468 O O   . GLY A 204 ? 0.1924 0.3526 0.1936 0.0183  0.0865  0.0178  204 GLY A O   
1469 N N   . GLY A 205 ? 0.2626 0.3880 0.1984 0.0111  0.1167  0.0489  205 GLY A N   
1470 C CA  . GLY A 205 ? 0.3010 0.4481 0.1563 0.0220  0.1488  0.0567  205 GLY A CA  
1471 C C   . GLY A 205 ? 0.3058 0.4841 0.1777 0.0104  0.1447  0.0685  205 GLY A C   
1472 O O   . GLY A 205 ? 0.4062 0.6092 0.2071 -0.0256 0.1460  0.0528  205 GLY A O   
1473 N N   . VAL A 206 ? 0.3328 0.5479 0.1917 -0.0235 0.1511  0.0708  206 VAL A N   
1474 C CA  . VAL A 206 ? 0.3133 0.5789 0.2263 0.0231  0.1130  0.0357  206 VAL A CA  
1475 C C   . VAL A 206 ? 0.2614 0.5913 0.2906 0.0385  0.1610  0.0407  206 VAL A C   
1476 O O   . VAL A 206 ? 0.3453 0.6572 0.2286 0.0495  0.1369  0.0256  206 VAL A O   
1477 C CB  . VAL A 206 ? 0.2950 0.5613 0.2602 -0.0024 0.0775  0.0524  206 VAL A CB  
1478 C CG1 . VAL A 206 ? 0.3216 0.5735 0.2497 0.0022  0.0753  0.0599  206 VAL A CG1 
1479 C CG2 . VAL A 206 ? 0.2590 0.5825 0.3377 -0.0152 0.0310  0.0786  206 VAL A CG2 
1480 N N   . SER A 207 ? 0.2737 0.5636 0.3274 0.0469  0.1534  0.0363  207 SER A N   
1481 C CA  . SER A 207 ? 0.3304 0.5530 0.3731 0.0371  0.1827  0.0321  207 SER A CA  
1482 C C   . SER A 207 ? 0.3096 0.4944 0.3815 0.0669  0.1573  -0.0018 207 SER A C   
1483 O O   . SER A 207 ? 0.3391 0.4937 0.4057 0.0525  0.2184  -0.0053 207 SER A O   
1484 C CB  . SER A 207 ? 0.3760 0.5314 0.4526 0.0073  0.1679  0.0635  207 SER A CB  
1485 O OG  . SER A 207 ? 0.4386 0.5680 0.5199 -0.0166 0.1658  0.0502  207 SER A OG  
1486 N N   . THR A 208 ? 0.2842 0.4637 0.2988 0.1022  0.1217  0.0374  208 THR A N   
1487 C CA  . THR A 208 ? 0.2707 0.4675 0.2986 0.0857  0.1312  0.0479  208 THR A CA  
1488 C C   . THR A 208 ? 0.2166 0.4837 0.2256 0.0920  0.1346  0.0532  208 THR A C   
1489 O O   . THR A 208 ? 0.1609 0.4891 0.1717 0.0667  0.1213  0.0531  208 THR A O   
1490 C CB  . THR A 208 ? 0.2661 0.4795 0.3087 0.0799  0.1353  0.0679  208 THR A CB  
1491 O OG1 . THR A 208 ? 0.2604 0.4889 0.2734 0.0665  0.1356  0.0667  208 THR A OG1 
1492 C CG2 . THR A 208 ? 0.2903 0.4647 0.3658 0.0596  0.1260  0.0928  208 THR A CG2 
1493 N N   . ALA A 209 ? 0.2004 0.4862 0.2306 0.0904  0.1200  0.0483  209 ALA A N   
1494 C CA  . ALA A 209 ? 0.2002 0.4999 0.2360 0.0937  0.1133  0.0489  209 ALA A CA  
1495 C C   . ALA A 209 ? 0.1493 0.5086 0.2043 0.0745  0.1329  0.0644  209 ALA A C   
1496 O O   . ALA A 209 ? 0.1770 0.5071 0.1931 0.0915  0.1388  0.0633  209 ALA A O   
1497 C CB  . ALA A 209 ? 0.1874 0.5060 0.2453 0.0842  0.1057  0.0777  209 ALA A CB  
1498 N N   . GLU A 210 ? 0.1742 0.5220 0.2264 0.0802  0.1166  0.0853  210 GLU A N   
1499 C CA  . GLU A 210 ? 0.1762 0.5121 0.1847 0.0810  0.0938  0.0959  210 GLU A CA  
1500 C C   . GLU A 210 ? 0.1820 0.4904 0.1489 0.0867  0.1002  0.0742  210 GLU A C   
1501 O O   . GLU A 210 ? 0.2140 0.4826 0.1608 0.0938  0.0938  0.0737  210 GLU A O   
1502 C CB  . GLU A 210 ? 0.2526 0.5468 0.1749 0.0867  0.0579  0.1090  210 GLU A CB  
1503 C CG  . GLU A 210 ? 0.2630 0.5921 0.2719 0.0884  0.0282  0.1060  210 GLU A CG  
1504 C CD  . GLU A 210 ? 0.2814 0.5994 0.3454 0.1218  -0.0012 0.1128  210 GLU A CD  
1505 O OE1 . GLU A 210 ? 0.3207 0.5794 0.3902 0.0823  0.0270  0.1306  210 GLU A OE1 
1506 O OE2 . GLU A 210 ? 0.3160 0.6988 0.4647 0.1595  -0.0022 0.1187  210 GLU A OE2 
1507 N N   . ASP A 211 ? 0.1575 0.4674 0.1310 0.0657  0.1218  0.0760  211 ASP A N   
1508 C CA  . ASP A 211 ? 0.1461 0.4641 0.1468 0.0580  0.1177  0.0607  211 ASP A CA  
1509 C C   . ASP A 211 ? 0.1598 0.4284 0.1326 0.0511  0.0980  0.0436  211 ASP A C   
1510 O O   . ASP A 211 ? 0.1411 0.4408 0.1294 0.0529  0.0889  0.0386  211 ASP A O   
1511 C CB  . ASP A 211 ? 0.1710 0.4672 0.1795 0.0576  0.1239  0.0560  211 ASP A CB  
1512 C CG  . ASP A 211 ? 0.2469 0.5005 0.2009 0.0396  0.1237  0.0696  211 ASP A CG  
1513 O OD1 . ASP A 211 ? 0.2997 0.5696 0.2039 -0.0080 0.1434  0.0900  211 ASP A OD1 
1514 O OD2 . ASP A 211 ? 0.3183 0.5035 0.2428 0.0067  0.1387  0.0721  211 ASP A OD2 
1515 N N   . ALA A 212 ? 0.1570 0.4131 0.1290 0.0469  0.0942  0.0533  212 ALA A N   
1516 C CA  . ALA A 212 ? 0.1706 0.4151 0.0942 0.0473  0.1117  0.0231  212 ALA A CA  
1517 C C   . ALA A 212 ? 0.1881 0.4238 0.0875 0.0630  0.1017  0.0159  212 ALA A C   
1518 O O   . ALA A 212 ? 0.2122 0.3914 0.0988 0.0529  0.0849  -0.0039 212 ALA A O   
1519 C CB  . ALA A 212 ? 0.1882 0.4317 0.0911 0.0405  0.1202  0.0241  212 ALA A CB  
1520 N N   . GLN A 213 ? 0.1836 0.4340 0.0972 0.0673  0.0851  0.0224  213 GLN A N   
1521 C CA  . GLN A 213 ? 0.1986 0.4518 0.1082 0.0622  0.0688  0.0189  213 GLN A CA  
1522 C C   . GLN A 213 ? 0.2101 0.4183 0.0922 0.0604  0.0703  0.0308  213 GLN A C   
1523 O O   . GLN A 213 ? 0.1917 0.4373 0.1285 0.0477  0.0646  0.0192  213 GLN A O   
1524 C CB  . GLN A 213 ? 0.2315 0.5058 0.1415 0.0666  0.0642  0.0337  213 GLN A CB  
1525 C CG  . GLN A 213 ? 0.2244 0.5741 0.1478 0.0557  0.0857  0.0280  213 GLN A CG  
1526 C CD  . GLN A 213 ? 0.2471 0.6565 0.2172 0.0662  0.0651  0.0854  213 GLN A CD  
1527 O OE1 . GLN A 213 ? 0.3575 0.7685 0.2521 0.0456  0.0332  0.1492  213 GLN A OE1 
1528 N NE2 . GLN A 213 ? 0.2894 0.7078 0.2724 0.0089  0.0114  0.1318  213 GLN A NE2 
1529 N N   . LYS A 214 ? 0.2192 0.4167 0.0978 0.0722  0.0898  0.0189  214 LYS A N   
1530 C CA  . LYS A 214 ? 0.2249 0.4007 0.1040 0.0662  0.0959  0.0072  214 LYS A CA  
1531 C C   . LYS A 214 ? 0.1951 0.4056 0.0847 0.0475  0.0994  0.0065  214 LYS A C   
1532 O O   . LYS A 214 ? 0.2087 0.4131 0.1286 0.0561  0.0911  0.0007  214 LYS A O   
1533 C CB  . LYS A 214 ? 0.2689 0.4150 0.1588 0.0606  0.0964  0.0284  214 LYS A CB  
1534 C CG  . LYS A 214 ? 0.2686 0.4643 0.2638 0.0422  0.1019  0.0215  214 LYS A CG  
1535 C CD  . LYS A 214 ? 0.3300 0.4917 0.3362 0.0092  0.0854  0.0588  214 LYS A CD  
1536 C CE  . LYS A 214 ? 0.2933 0.5356 0.3949 -0.0288 0.0520  0.0608  214 LYS A CE  
1537 N NZ  . LYS A 214 ? 0.3038 0.5721 0.4647 -0.0712 0.0459  0.0901  214 LYS A NZ  
1538 N N   . TYR A 215 ? 0.1564 0.4036 0.0805 0.0361  0.0947  0.0106  215 TYR A N   
1539 C CA  . TYR A 215 ? 0.1371 0.3675 0.0801 0.0133  0.0731  0.0077  215 TYR A CA  
1540 C C   . TYR A 215 ? 0.1482 0.3577 0.0840 0.0184  0.0787  -0.0068 215 TYR A C   
1541 O O   . TYR A 215 ? 0.1304 0.3605 0.1177 0.0122  0.0705  -0.0086 215 TYR A O   
1542 C CB  . TYR A 215 ? 0.1281 0.3588 0.0828 -0.0071 0.0871  0.0101  215 TYR A CB  
1543 C CG  . TYR A 215 ? 0.1095 0.3552 0.1024 -0.0055 0.0671  0.0311  215 TYR A CG  
1544 C CD1 . TYR A 215 ? 0.1209 0.3358 0.1071 0.0060  0.0527  0.0297  215 TYR A CD1 
1545 C CD2 . TYR A 215 ? 0.0932 0.3715 0.2450 -0.0113 0.0417  0.0550  215 TYR A CD2 
1546 C CE1 . TYR A 215 ? 0.1023 0.3488 0.1127 0.0062  0.0580  0.0421  215 TYR A CE1 
1547 C CE2 . TYR A 215 ? 0.1100 0.3505 0.2613 -0.0017 0.0406  0.0659  215 TYR A CE2 
1548 C CZ  . TYR A 215 ? 0.1081 0.3505 0.1688 0.0046  0.0594  0.0334  215 TYR A CZ  
1549 O OH  . TYR A 215 ? 0.1242 0.3721 0.1422 -0.0011 0.0715  0.0425  215 TYR A OH  
1550 N N   . LEU A 216 ? 0.1446 0.3628 0.0870 0.0162  0.0669  -0.0103 216 LEU A N   
1551 C CA  . LEU A 216 ? 0.1411 0.3712 0.1198 0.0081  0.0887  -0.0030 216 LEU A CA  
1552 C C   . LEU A 216 ? 0.1214 0.3556 0.1381 -0.0056 0.0629  -0.0007 216 LEU A C   
1553 O O   . LEU A 216 ? 0.1301 0.3467 0.1578 0.0007  0.0854  0.0011  216 LEU A O   
1554 C CB  . LEU A 216 ? 0.1476 0.3954 0.1480 0.0173  0.0823  -0.0069 216 LEU A CB  
1555 C CG  . LEU A 216 ? 0.2004 0.4322 0.1573 0.0112  0.0780  -0.0166 216 LEU A CG  
1556 C CD1 . LEU A 216 ? 0.2052 0.4577 0.1593 0.0069  0.0899  -0.0213 216 LEU A CD1 
1557 C CD2 . LEU A 216 ? 0.1900 0.4345 0.1533 0.0157  0.0992  -0.0262 216 LEU A CD2 
1558 N N   . ALA A 217 ? 0.1301 0.3838 0.1240 0.0126  0.0610  -0.0109 217 ALA A N   
1559 C CA  . ALA A 217 ? 0.1649 0.3859 0.1240 0.0127  0.0452  -0.0266 217 ALA A CA  
1560 C C   . ALA A 217 ? 0.1773 0.3717 0.1238 -0.0001 0.0584  -0.0278 217 ALA A C   
1561 O O   . ALA A 217 ? 0.1492 0.3868 0.1423 -0.0029 0.0692  -0.0438 217 ALA A O   
1562 C CB  . ALA A 217 ? 0.1956 0.3963 0.1611 0.0193  0.0348  -0.0125 217 ALA A CB  
1563 N N   . ILE A 218 ? 0.1448 0.3571 0.1136 -0.0018 0.0766  -0.0287 218 ILE A N   
1564 C CA  . ILE A 218 ? 0.1427 0.3566 0.1129 -0.0071 0.0580  -0.0418 218 ILE A CA  
1565 C C   . ILE A 218 ? 0.1281 0.3368 0.1033 -0.0157 0.0687  -0.0516 218 ILE A C   
1566 O O   . ILE A 218 ? 0.1483 0.3456 0.1134 -0.0086 0.0785  -0.0499 218 ILE A O   
1567 C CB  . ILE A 218 ? 0.1200 0.3705 0.1566 -0.0150 0.0795  -0.0328 218 ILE A CB  
1568 C CG1 . ILE A 218 ? 0.1407 0.3835 0.2073 -0.0015 0.0764  -0.0213 218 ILE A CG1 
1569 C CG2 . ILE A 218 ? 0.1232 0.3831 0.1694 -0.0078 0.0705  -0.0469 218 ILE A CG2 
1570 C CD1 . ILE A 218 ? 0.1472 0.3930 0.2205 -0.0214 0.0682  -0.0173 218 ILE A CD1 
1571 N N   . ALA A 219 ? 0.1451 0.3616 0.0991 -0.0151 0.0721  -0.0406 219 ALA A N   
1572 C CA  . ALA A 219 ? 0.1632 0.3563 0.0929 -0.0216 0.0608  -0.0341 219 ALA A CA  
1573 C C   . ALA A 219 ? 0.1711 0.3481 0.0953 -0.0112 0.0468  -0.0350 219 ALA A C   
1574 O O   . ALA A 219 ? 0.1799 0.3445 0.0964 -0.0083 0.0529  -0.0320 219 ALA A O   
1575 C CB  . ALA A 219 ? 0.1662 0.3750 0.0877 -0.0292 0.0620  -0.0356 219 ALA A CB  
1576 N N   . ASP A 220 ? 0.1638 0.3733 0.1233 0.0011  0.0471  -0.0527 220 ASP A N   
1577 C CA  . ASP A 220 ? 0.1806 0.3783 0.1389 -0.0073 0.0364  -0.0691 220 ASP A CA  
1578 C C   . ASP A 220 ? 0.1784 0.3718 0.1409 -0.0083 0.0141  -0.0799 220 ASP A C   
1579 O O   . ASP A 220 ? 0.2110 0.3860 0.1711 -0.0083 0.0161  -0.0969 220 ASP A O   
1580 C CB  . ASP A 220 ? 0.1992 0.4082 0.1516 -0.0033 0.0068  -0.0560 220 ASP A CB  
1581 C CG  . ASP A 220 ? 0.1998 0.4354 0.1630 -0.0068 0.0093  -0.0376 220 ASP A CG  
1582 O OD1 . ASP A 220 ? 0.1797 0.5061 0.1780 -0.0254 0.0285  -0.0197 220 ASP A OD1 
1583 O OD2 . ASP A 220 ? 0.2466 0.5080 0.1691 0.0428  0.0161  -0.0222 220 ASP A OD2 
1584 N N   . GLU A 221 ? 0.1752 0.3703 0.1654 -0.0018 0.0304  -0.0727 221 GLU A N   
1585 C CA  . GLU A 221 ? 0.2227 0.3898 0.1729 0.0215  0.0460  -0.0716 221 GLU A CA  
1586 C C   . GLU A 221 ? 0.2131 0.3646 0.1448 -0.0022 0.0564  -0.0636 221 GLU A C   
1587 O O   . GLU A 221 ? 0.2325 0.3746 0.1526 0.0125  0.0579  -0.0639 221 GLU A O   
1588 C CB  . GLU A 221 ? 0.2769 0.4033 0.2242 0.0371  0.0787  -0.0601 221 GLU A CB  
1589 C CG  . GLU A 221 ? 0.3970 0.5055 0.3419 0.0547  0.0629  -0.0184 221 GLU A CG  
1590 C CD  . GLU A 221 ? 0.5107 0.6219 0.4910 0.0355  0.0519  0.0665  221 GLU A CD  
1591 O OE1 . GLU A 221 ? 0.5267 0.8072 0.5470 0.0029  0.0936  0.0946  221 GLU A OE1 
1592 O OE2 . GLU A 221 ? 0.6862 0.7511 0.5882 0.1162  -0.0310 0.1518  221 GLU A OE2 
1593 N N   . LEU A 222 ? 0.1823 0.3472 0.1089 -0.0091 0.0733  -0.0575 222 LEU A N   
1594 C CA  . LEU A 222 ? 0.1500 0.3630 0.1264 -0.0079 0.0902  -0.0571 222 LEU A CA  
1595 C C   . LEU A 222 ? 0.1682 0.3540 0.1299 0.0038  0.0680  -0.0627 222 LEU A C   
1596 O O   . LEU A 222 ? 0.1640 0.3752 0.1777 0.0156  0.0646  -0.0445 222 LEU A O   
1597 C CB  . LEU A 222 ? 0.1714 0.3700 0.1423 -0.0210 0.0946  -0.0731 222 LEU A CB  
1598 C CG  . LEU A 222 ? 0.1762 0.3881 0.1933 -0.0328 0.0794  -0.0715 222 LEU A CG  
1599 C CD1 . LEU A 222 ? 0.1715 0.3877 0.1851 -0.0280 0.0809  -0.0676 222 LEU A CD1 
1600 C CD2 . LEU A 222 ? 0.2089 0.3971 0.2287 -0.0238 0.0840  -0.0849 222 LEU A CD2 
1601 N N   . PHE A 223 ? 0.1514 0.3352 0.1538 -0.0197 0.0786  -0.0478 223 PHE A N   
1602 C CA  . PHE A 223 ? 0.1554 0.3197 0.1411 -0.0256 0.0552  -0.0459 223 PHE A CA  
1603 C C   . PHE A 223 ? 0.1652 0.3442 0.1559 -0.0292 0.0464  -0.0530 223 PHE A C   
1604 O O   . PHE A 223 ? 0.2295 0.3403 0.2205 -0.0488 0.0315  -0.0406 223 PHE A O   
1605 C CB  . PHE A 223 ? 0.1499 0.3230 0.1271 -0.0328 0.0501  -0.0297 223 PHE A CB  
1606 C CG  . PHE A 223 ? 0.1502 0.3401 0.1264 -0.0228 0.0456  -0.0192 223 PHE A CG  
1607 C CD1 . PHE A 223 ? 0.1736 0.3461 0.1623 -0.0280 0.0305  -0.0157 223 PHE A CD1 
1608 C CD2 . PHE A 223 ? 0.1377 0.3295 0.1315 -0.0244 0.0471  -0.0251 223 PHE A CD2 
1609 C CE1 . PHE A 223 ? 0.1531 0.3536 0.1618 -0.0237 0.0320  0.0045  223 PHE A CE1 
1610 C CE2 . PHE A 223 ? 0.1444 0.3479 0.1250 -0.0279 0.0362  -0.0099 223 PHE A CE2 
1611 C CZ  . PHE A 223 ? 0.1730 0.3543 0.1648 -0.0192 0.0446  -0.0014 223 PHE A CZ  
1612 N N   . GLY A 224 ? 0.1666 0.3499 0.1625 -0.0269 0.0550  -0.0528 224 GLY A N   
1613 C CA  . GLY A 224 ? 0.1713 0.3732 0.1835 -0.0265 0.0180  -0.0663 224 GLY A CA  
1614 C C   . GLY A 224 ? 0.1631 0.3964 0.1864 -0.0289 0.0341  -0.0654 224 GLY A C   
1615 O O   . GLY A 224 ? 0.1446 0.4134 0.1889 -0.0471 0.0658  -0.0720 224 GLY A O   
1616 N N   . ALA A 225 ? 0.1820 0.4322 0.1659 -0.0277 0.0096  -0.0662 225 ALA A N   
1617 C CA  . ALA A 225 ? 0.2112 0.4489 0.2238 -0.0082 0.0239  -0.0698 225 ALA A CA  
1618 C C   . ALA A 225 ? 0.1749 0.4333 0.2307 -0.0304 0.0497  -0.0857 225 ALA A C   
1619 O O   . ALA A 225 ? 0.2211 0.4473 0.2630 -0.0170 0.1124  -0.0637 225 ALA A O   
1620 C CB  . ALA A 225 ? 0.2483 0.5082 0.2552 0.0102  0.0089  -0.0639 225 ALA A CB  
1621 N N   . ASP A 226 ? 0.1385 0.4393 0.1889 -0.0566 0.0831  -0.0812 226 ASP A N   
1622 C CA  . ASP A 226 ? 0.2145 0.4419 0.1890 -0.0711 0.0712  -0.0665 226 ASP A CA  
1623 C C   . ASP A 226 ? 0.1860 0.4145 0.1659 -0.0576 0.0863  -0.0598 226 ASP A C   
1624 O O   . ASP A 226 ? 0.1903 0.4421 0.1772 -0.0693 0.0982  -0.0704 226 ASP A O   
1625 C CB  . ASP A 226 ? 0.3007 0.4808 0.2860 -0.0874 0.0617  -0.0678 226 ASP A CB  
1626 C CG  . ASP A 226 ? 0.3556 0.5338 0.3862 -0.1133 0.0472  -0.0903 226 ASP A CG  
1627 O OD1 . ASP A 226 ? 0.3833 0.6192 0.5409 -0.1383 -0.0059 -0.0501 226 ASP A OD1 
1628 O OD2 . ASP A 226 ? 0.5093 0.5862 0.5164 -0.1741 0.0455  -0.0974 226 ASP A OD2 
1629 N N   . TRP A 227 ? 0.1763 0.3757 0.1561 -0.0458 0.0701  -0.0444 227 TRP A N   
1630 C CA  . TRP A 227 ? 0.1639 0.3391 0.1331 -0.0310 0.0886  -0.0560 227 TRP A CA  
1631 C C   . TRP A 227 ? 0.1406 0.3294 0.1403 -0.0244 0.0661  -0.0531 227 TRP A C   
1632 O O   . TRP A 227 ? 0.1658 0.3422 0.1404 -0.0340 0.0735  -0.0572 227 TRP A O   
1633 C CB  . TRP A 227 ? 0.1594 0.3198 0.1246 -0.0210 0.0795  -0.0569 227 TRP A CB  
1634 C CG  . TRP A 227 ? 0.1644 0.3309 0.1267 -0.0050 0.0721  -0.0301 227 TRP A CG  
1635 C CD1 . TRP A 227 ? 0.1965 0.3208 0.1652 -0.0107 0.0775  -0.0249 227 TRP A CD1 
1636 C CD2 . TRP A 227 ? 0.1805 0.3218 0.0880 -0.0046 0.0656  -0.0242 227 TRP A CD2 
1637 N NE1 . TRP A 227 ? 0.2173 0.3259 0.1592 0.0004  0.0480  -0.0220 227 TRP A NE1 
1638 C CE2 . TRP A 227 ? 0.1689 0.3189 0.1160 0.0013  0.0632  -0.0351 227 TRP A CE2 
1639 C CE3 . TRP A 227 ? 0.1709 0.3162 0.0932 0.0090  0.0510  -0.0308 227 TRP A CE3 
1640 C CZ2 . TRP A 227 ? 0.1529 0.3115 0.1075 0.0143  0.0709  -0.0388 227 TRP A CZ2 
1641 C CZ3 . TRP A 227 ? 0.1850 0.3139 0.1064 0.0080  0.0482  -0.0244 227 TRP A CZ3 
1642 C CH2 . TRP A 227 ? 0.1572 0.3151 0.1011 0.0070  0.0510  -0.0394 227 TRP A CH2 
1643 N N   . ALA A 228 ? 0.1195 0.3384 0.1215 -0.0239 0.0568  -0.0373 228 ALA A N   
1644 C CA  . ALA A 228 ? 0.1409 0.3446 0.1336 -0.0197 0.0677  -0.0479 228 ALA A CA  
1645 C C   . ALA A 228 ? 0.1349 0.3490 0.1292 -0.0187 0.0624  -0.0455 228 ALA A C   
1646 O O   . ALA A 228 ? 0.1704 0.3645 0.1648 0.0020  0.0766  -0.0241 228 ALA A O   
1647 C CB  . ALA A 228 ? 0.1373 0.3443 0.1618 -0.0106 0.0387  -0.0475 228 ALA A CB  
1648 N N   . ASP A 229 ? 0.1356 0.3446 0.1076 -0.0181 0.0708  -0.0474 229 ASP A N   
1649 C CA  . ASP A 229 ? 0.1169 0.3439 0.1161 -0.0240 0.0696  -0.0440 229 ASP A CA  
1650 C C   . ASP A 229 ? 0.0804 0.3420 0.1154 -0.0296 0.0698  -0.0263 229 ASP A C   
1651 O O   . ASP A 229 ? 0.0831 0.3341 0.1073 -0.0337 0.0758  -0.0238 229 ASP A O   
1652 C CB  . ASP A 229 ? 0.1435 0.3503 0.1370 -0.0481 0.0658  -0.0368 229 ASP A CB  
1653 C CG  . ASP A 229 ? 0.1771 0.3470 0.1817 -0.0615 0.0622  -0.0197 229 ASP A CG  
1654 O OD1 . ASP A 229 ? 0.1502 0.3147 0.1408 -0.0412 0.0646  -0.0149 229 ASP A OD1 
1655 O OD2 . ASP A 229 ? 0.2410 0.3741 0.3366 -0.0859 0.0385  0.0052  229 ASP A OD2 
1656 N N   . ALA A 230 ? 0.1013 0.3396 0.1071 -0.0244 0.0623  -0.0345 230 ALA A N   
1657 C CA  . ALA A 230 ? 0.1135 0.3434 0.1229 -0.0254 0.0727  -0.0347 230 ALA A CA  
1658 C C   . ALA A 230 ? 0.1004 0.3163 0.0825 -0.0383 0.0836  -0.0308 230 ALA A C   
1659 O O   . ALA A 230 ? 0.1197 0.3214 0.1261 -0.0475 0.0624  -0.0242 230 ALA A O   
1660 C CB  . ALA A 230 ? 0.1103 0.3699 0.1568 -0.0166 0.0785  -0.0472 230 ALA A CB  
1661 N N   . ARG A 231 ? 0.1139 0.3170 0.0895 -0.0307 0.0713  -0.0284 231 ARG A N   
1662 C CA  . ARG A 231 ? 0.1316 0.3006 0.0873 -0.0312 0.0757  -0.0156 231 ARG A CA  
1663 C C   . ARG A 231 ? 0.0997 0.2985 0.1006 -0.0394 0.0608  -0.0079 231 ARG A C   
1664 O O   . ARG A 231 ? 0.1003 0.3287 0.1225 -0.0408 0.0547  -0.0049 231 ARG A O   
1665 C CB  . ARG A 231 ? 0.1517 0.2990 0.1171 -0.0451 0.0717  -0.0084 231 ARG A CB  
1666 C CG  . ARG A 231 ? 0.1675 0.3047 0.1283 -0.0515 0.0761  0.0099  231 ARG A CG  
1667 C CD  . ARG A 231 ? 0.1556 0.3172 0.1080 -0.0456 0.0768  0.0244  231 ARG A CD  
1668 N NE  . ARG A 231 ? 0.1522 0.3397 0.1085 -0.0361 0.0736  0.0250  231 ARG A NE  
1669 C CZ  . ARG A 231 ? 0.1467 0.3305 0.0937 -0.0488 0.0588  0.0203  231 ARG A CZ  
1670 N NH1 . ARG A 231 ? 0.1339 0.3474 0.1090 -0.0549 0.0529  0.0292  231 ARG A NH1 
1671 N NH2 . ARG A 231 ? 0.1783 0.3422 0.1366 -0.0388 0.0431  0.0366  231 ARG A NH2 
1672 N N   . HIS A 232 ? 0.0856 0.2845 0.1129 -0.0335 0.0540  -0.0001 232 HIS A N   
1673 C CA  . HIS A 232 ? 0.0849 0.2846 0.1361 -0.0295 0.0653  -0.0102 232 HIS A CA  
1674 C C   . HIS A 232 ? 0.0674 0.2836 0.0977 -0.0154 0.0690  -0.0109 232 HIS A C   
1675 O O   . HIS A 232 ? 0.0682 0.2920 0.0956 -0.0196 0.0697  -0.0164 232 HIS A O   
1676 C CB  . HIS A 232 ? 0.1141 0.2892 0.1344 -0.0232 0.0630  -0.0182 232 HIS A CB  
1677 C CG  . HIS A 232 ? 0.1509 0.2980 0.1580 -0.0204 0.0643  -0.0095 232 HIS A CG  
1678 N ND1 . HIS A 232 ? 0.1937 0.3123 0.1614 -0.0448 0.0616  -0.0107 232 HIS A ND1 
1679 C CD2 . HIS A 232 ? 0.1653 0.3127 0.1797 -0.0241 0.0601  -0.0090 232 HIS A CD2 
1680 C CE1 . HIS A 232 ? 0.1977 0.3290 0.1746 -0.0292 0.0755  -0.0010 232 HIS A CE1 
1681 N NE2 . HIS A 232 ? 0.1863 0.3157 0.1823 -0.0396 0.0620  -0.0038 232 HIS A NE2 
1682 N N   . TYR A 233 ? 0.0912 0.2797 0.0870 -0.0093 0.0679  -0.0156 233 TYR A N   
1683 C CA  . TYR A 233 ? 0.0484 0.2782 0.1098 -0.0197 0.0515  -0.0142 233 TYR A CA  
1684 C C   . TYR A 233 ? 0.0486 0.2738 0.1057 -0.0219 0.0628  -0.0168 233 TYR A C   
1685 O O   . TYR A 233 ? 0.0569 0.2955 0.1390 -0.0295 0.0782  -0.0103 233 TYR A O   
1686 C CB  . TYR A 233 ? 0.0668 0.2948 0.1113 -0.0353 0.0470  -0.0106 233 TYR A CB  
1687 C CG  . TYR A 233 ? 0.0795 0.2883 0.1199 -0.0314 0.0470  -0.0049 233 TYR A CG  
1688 C CD1 . TYR A 233 ? 0.1247 0.3121 0.1067 -0.0158 0.0475  -0.0046 233 TYR A CD1 
1689 C CD2 . TYR A 233 ? 0.1493 0.2957 0.1087 -0.0322 0.0554  -0.0145 233 TYR A CD2 
1690 C CE1 . TYR A 233 ? 0.1709 0.3108 0.1182 -0.0125 0.0393  0.0030  233 TYR A CE1 
1691 C CE2 . TYR A 233 ? 0.1502 0.3131 0.1169 -0.0415 0.0659  -0.0021 233 TYR A CE2 
1692 C CZ  . TYR A 233 ? 0.1533 0.3222 0.1233 -0.0359 0.0588  0.0113  233 TYR A CZ  
1693 O OH  . TYR A 233 ? 0.1930 0.3782 0.1276 -0.0448 0.0701  0.0312  233 TYR A OH  
1694 N N   . ARG A 234 ? 0.0581 0.2628 0.0806 -0.0153 0.0620  -0.0140 234 ARG A N   
1695 C CA  . ARG A 234 ? 0.0496 0.2572 0.0875 -0.0100 0.0591  -0.0050 234 ARG A CA  
1696 C C   . ARG A 234 ? 0.0540 0.2712 0.0971 -0.0109 0.0655  -0.0001 234 ARG A C   
1697 O O   . ARG A 234 ? 0.0668 0.2781 0.0835 -0.0046 0.0683  -0.0039 234 ARG A O   
1698 C CB  . ARG A 234 ? 0.0636 0.2757 0.0879 -0.0045 0.0617  -0.0099 234 ARG A CB  
1699 C CG  . ARG A 234 ? 0.0521 0.2846 0.0853 0.0012  0.0555  -0.0099 234 ARG A CG  
1700 C CD  . ARG A 234 ? 0.0536 0.2879 0.0767 -0.0010 0.0576  0.0017  234 ARG A CD  
1701 N NE  . ARG A 234 ? 0.0706 0.3013 0.0657 -0.0040 0.0617  0.0025  234 ARG A NE  
1702 C CZ  . ARG A 234 ? 0.0986 0.2911 0.0657 -0.0090 0.0650  0.0011  234 ARG A CZ  
1703 N NH1 . ARG A 234 ? 0.1156 0.3032 0.0667 -0.0058 0.0802  0.0025  234 ARG A NH1 
1704 N NH2 . ARG A 234 ? 0.1296 0.3070 0.0783 -0.0118 0.0510  0.0032  234 ARG A NH2 
1705 N N   . PHE A 235 ? 0.0539 0.2795 0.1198 0.0102  0.0731  -0.0005 235 PHE A N   
1706 C CA  . PHE A 235 ? 0.0587 0.2863 0.1035 0.0091  0.0713  0.0065  235 PHE A CA  
1707 C C   . PHE A 235 ? 0.0618 0.2929 0.1238 -0.0097 0.0805  -0.0022 235 PHE A C   
1708 O O   . PHE A 235 ? 0.0883 0.2923 0.1201 -0.0052 0.0961  0.0110  235 PHE A O   
1709 C CB  . PHE A 235 ? 0.0765 0.3052 0.1103 0.0046  0.0714  0.0078  235 PHE A CB  
1710 C CG  . PHE A 235 ? 0.1239 0.3210 0.1278 0.0092  0.0457  -0.0088 235 PHE A CG  
1711 C CD1 . PHE A 235 ? 0.1656 0.3383 0.1212 -0.0080 0.0408  -0.0016 235 PHE A CD1 
1712 C CD2 . PHE A 235 ? 0.1307 0.3581 0.1263 -0.0167 0.0677  -0.0159 235 PHE A CD2 
1713 C CE1 . PHE A 235 ? 0.1940 0.3740 0.1284 -0.0037 0.0521  -0.0231 235 PHE A CE1 
1714 C CE2 . PHE A 235 ? 0.1497 0.3587 0.1554 -0.0136 0.0324  -0.0354 235 PHE A CE2 
1715 C CZ  . PHE A 235 ? 0.1761 0.3722 0.1398 -0.0064 0.0325  -0.0342 235 PHE A CZ  
1716 N N   . SER A 236 ? 0.0742 0.3084 0.1362 -0.0114 0.0935  0.0008  236 SER A N   
1717 C CA  A SER A 236 ? 0.0769 0.3044 0.1332 -0.0008 0.0823  0.0043  236 SER A CA  
1718 C CA  B SER A 236 ? 0.0671 0.3099 0.1536 -0.0064 0.0943  0.0061  236 SER A CA  
1719 C CA  C SER A 236 ? 0.0918 0.3157 0.1682 -0.0060 0.0894  0.0069  236 SER A CA  
1720 C C   . SER A 236 ? 0.0668 0.3028 0.1687 0.0034  0.0779  0.0161  236 SER A C   
1721 O O   . SER A 236 ? 0.0791 0.3240 0.1845 0.0188  0.0947  0.0307  236 SER A O   
1722 C CB  A SER A 236 ? 0.0861 0.3031 0.1135 0.0028  0.0836  0.0007  236 SER A CB  
1723 C CB  B SER A 236 ? 0.0682 0.3198 0.1543 -0.0088 0.0952  0.0084  236 SER A CB  
1724 C CB  C SER A 236 ? 0.1343 0.3589 0.1854 0.0016  0.0770  0.0029  236 SER A CB  
1725 O OG  A SER A 236 ? 0.0899 0.2986 0.0634 0.0060  0.0688  -0.0054 236 SER A OG  
1726 O OG  B SER A 236 ? 0.0773 0.3213 0.1505 -0.0197 0.0998  0.0067  236 SER A OG  
1727 O OG  C SER A 236 ? 0.2108 0.3964 0.2248 -0.0161 0.0684  0.0238  236 SER A OG  
1728 N N   . ALA A 237 ? 0.1198 0.3135 0.2173 0.0078  0.0720  0.0191  237 ALA A N   
1729 C CA  . ALA A 237 ? 0.1036 0.3242 0.2720 0.0140  0.0644  0.0389  237 ALA A CA  
1730 C C   . ALA A 237 ? 0.1209 0.3328 0.3877 0.0407  0.0553  0.0320  237 ALA A C   
1731 O O   . ALA A 237 ? 0.1200 0.3484 0.3791 0.0434  0.0964  0.0291  237 ALA A O   
1732 C CB  . ALA A 237 ? 0.1575 0.3596 0.2854 0.0111  0.0342  0.0357  237 ALA A CB  
1733 N N   . SER A 238 ? 0.1741 0.3366 0.4772 0.0285  0.0341  0.0289  238 SER A N   
1734 C CA  . SER A 238 ? 0.2069 0.3656 0.5542 0.0257  0.0357  0.0338  238 SER A CA  
1735 C C   . SER A 238 ? 0.2164 0.3899 0.5545 0.0368  0.0564  0.0490  238 SER A C   
1736 O O   . SER A 238 ? 0.2241 0.4633 0.5489 0.0310  0.0742  0.1400  238 SER A O   
1737 C CB  . SER A 238 ? 0.2832 0.4183 0.6081 -0.0186 -0.0065 0.0251  238 SER A CB  
1738 O OG  . SER A 238 ? 0.4454 0.5114 0.6647 -0.0222 -0.0639 -0.0131 238 SER A OG  
1739 N N   . GLY A 239 ? 0.2066 0.3600 0.5417 0.0427  0.0486  0.0517  239 GLY A N   
1740 C CA  . GLY A 239 ? 0.1729 0.3802 0.5191 0.0300  0.0619  0.0678  239 GLY A CA  
1741 C C   . GLY A 239 ? 0.1619 0.3683 0.4569 0.0505  0.0878  0.0658  239 GLY A C   
1742 O O   . GLY A 239 ? 0.1725 0.4172 0.4904 0.0595  0.0790  0.1096  239 GLY A O   
1743 N N   . LEU A 240 ? 0.1502 0.3931 0.3661 0.0529  0.1046  0.0819  240 LEU A N   
1744 C CA  . LEU A 240 ? 0.1388 0.3775 0.2447 0.0560  0.1186  0.0698  240 LEU A CA  
1745 C C   . LEU A 240 ? 0.1493 0.3707 0.2311 0.0366  0.1018  0.0840  240 LEU A C   
1746 O O   . LEU A 240 ? 0.1617 0.3702 0.2701 0.0335  0.0784  0.0529  240 LEU A O   
1747 C CB  . LEU A 240 ? 0.1346 0.3837 0.2019 0.0544  0.1281  0.0738  240 LEU A CB  
1748 C CG  . LEU A 240 ? 0.1323 0.4098 0.1874 0.0459  0.1070  0.0706  240 LEU A CG  
1749 C CD1 . LEU A 240 ? 0.1639 0.4396 0.1896 0.0399  0.0826  0.0564  240 LEU A CD1 
1750 C CD2 . LEU A 240 ? 0.1644 0.4038 0.2030 0.0481  0.0906  0.0676  240 LEU A CD2 
1751 N N   . LEU A 241 ? 0.1365 0.3740 0.2303 0.0568  0.0928  0.0606  241 LEU A N   
1752 C CA  . LEU A 241 ? 0.1362 0.3804 0.2349 0.0568  0.0911  0.0469  241 LEU A CA  
1753 C C   . LEU A 241 ? 0.1794 0.3986 0.2243 0.0731  0.0944  0.0586  241 LEU A C   
1754 O O   . LEU A 241 ? 0.1582 0.4343 0.2129 0.0930  0.1091  0.0564  241 LEU A O   
1755 C CB  . LEU A 241 ? 0.1425 0.3733 0.2298 0.0392  0.0730  0.0352  241 LEU A CB  
1756 C CG  . LEU A 241 ? 0.1556 0.4034 0.2129 0.0167  0.0626  0.0549  241 LEU A CG  
1757 C CD1 . LEU A 241 ? 0.1547 0.4336 0.2672 0.0122  0.0623  0.0422  241 LEU A CD1 
1758 C CD2 . LEU A 241 ? 0.1910 0.4314 0.2168 0.0268  0.0727  0.0347  241 LEU A CD2 
1759 N N   . ALA A 242 ? 0.1933 0.3934 0.2828 0.0976  0.0892  0.0710  242 ALA A N   
1760 C CA  . ALA A 242 ? 0.2050 0.4251 0.3210 0.0983  0.0717  0.0856  242 ALA A CA  
1761 C C   . ALA A 242 ? 0.2034 0.4502 0.3194 0.1146  0.0851  0.0930  242 ALA A C   
1762 O O   . ALA A 242 ? 0.2179 0.4778 0.3215 0.1162  0.0607  0.1345  242 ALA A O   
1763 C CB  . ALA A 242 ? 0.2568 0.4146 0.3338 0.1040  0.0668  0.0850  242 ALA A CB  
1764 N N   . SER A 243 ? 0.2264 0.4940 0.2572 0.1089  0.1044  0.1139  243 SER A N   
1765 C CA  . SER A 243 ? 0.2312 0.5023 0.2555 0.1105  0.1203  0.1190  243 SER A CA  
1766 C C   . SER A 243 ? 0.1946 0.5176 0.2084 0.0918  0.1024  0.1177  243 SER A C   
1767 O O   . SER A 243 ? 0.2076 0.5644 0.2079 0.1308  0.0881  0.1431  243 SER A O   
1768 C CB  . SER A 243 ? 0.2653 0.5138 0.2337 0.1206  0.1646  0.1343  243 SER A CB  
1769 O OG  . SER A 243 ? 0.2790 0.5473 0.2687 0.1349  0.1638  0.1205  243 SER A OG  
1770 N N   . LEU A 244 ? 0.1887 0.4855 0.1784 0.0792  0.0833  0.0902  244 LEU A N   
1771 C CA  . LEU A 244 ? 0.1620 0.4968 0.1740 0.0860  0.0802  0.0566  244 LEU A CA  
1772 C C   . LEU A 244 ? 0.1510 0.5142 0.1746 0.0874  0.0603  0.0571  244 LEU A C   
1773 O O   . LEU A 244 ? 0.1448 0.5365 0.1898 0.0619  0.0695  0.0890  244 LEU A O   
1774 C CB  . LEU A 244 ? 0.1434 0.4898 0.1030 0.0832  0.0689  0.0443  244 LEU A CB  
1775 C CG  . LEU A 244 ? 0.1476 0.4748 0.1073 0.0753  0.0627  0.0427  244 LEU A CG  
1776 C CD1 . LEU A 244 ? 0.1795 0.4822 0.1041 0.0731  0.0356  0.0361  244 LEU A CD1 
1777 C CD2 . LEU A 244 ? 0.2184 0.4749 0.1200 0.0617  0.0644  0.0423  244 LEU A CD2 
1778 N N   . LEU A 245 ? 0.1567 0.4897 0.2007 0.1064  0.0456  0.0528  245 LEU A N   
1779 C CA  . LEU A 245 ? 0.1549 0.5345 0.2210 0.1110  0.0345  0.0521  245 LEU A CA  
1780 C C   . LEU A 245 ? 0.2080 0.5528 0.2339 0.1317  0.0100  0.0492  245 LEU A C   
1781 O O   . LEU A 245 ? 0.1812 0.6088 0.2631 0.1238  0.0036  0.0834  245 LEU A O   
1782 C CB  . LEU A 245 ? 0.1399 0.5312 0.2262 0.1061  0.0115  0.0336  245 LEU A CB  
1783 C CG  . LEU A 245 ? 0.1447 0.5466 0.2376 0.1111  0.0470  0.0299  245 LEU A CG  
1784 C CD1 . LEU A 245 ? 0.1910 0.5690 0.2540 0.1156  0.0603  0.0102  245 LEU A CD1 
1785 C CD2 . LEU A 245 ? 0.1575 0.5480 0.2104 0.0952  0.0533  0.0307  245 LEU A CD2 
1786 N N   . LYS A 246 ? 0.2268 0.5554 0.2691 0.1768  0.0203  0.0555  246 LYS A N   
1787 C CA  . LYS A 246 ? 0.2519 0.6075 0.2822 0.1845  0.0307  0.0933  246 LYS A CA  
1788 C C   . LYS A 246 ? 0.2207 0.5951 0.2742 0.1660  0.0144  0.1251  246 LYS A C   
1789 O O   . LYS A 246 ? 0.3068 0.6459 0.2967 0.1650  -0.0494 0.0890  246 LYS A O   
1790 C CB  . LYS A 246 ? 0.3359 0.6328 0.3795 0.1866  0.0142  0.1200  246 LYS A CB  
1791 C CG  . LYS A 246 ? 0.4144 0.6997 0.4258 0.1808  0.0247  0.1456  246 LYS A CG  
1792 C CD  . LYS A 246 ? 0.4554 0.7549 0.5396 0.1635  -0.0078 0.1452  246 LYS A CD  
1793 C CE  . LYS A 246 ? 0.5839 0.8209 0.5679 0.1331  -0.0373 0.1465  246 LYS A CE  
1794 N NZ  . LYS A 246 ? 0.6069 0.9010 0.5582 0.1148  -0.0276 0.1457  246 LYS A NZ  
1795 N N   . ALA A 247 ? 0.2383 0.6247 0.2248 0.1454  0.0521  0.1106  247 ALA A N   
1796 C CA  . ALA A 247 ? 0.2501 0.6856 0.2089 0.1106  0.0311  0.1141  247 ALA A CA  
1797 C C   . ALA A 247 ? 0.2430 0.7492 0.2091 0.0991  0.0227  0.1014  247 ALA A C   
1798 O O   . ALA A 247 ? 0.2807 0.7857 0.2286 0.0874  0.0134  0.0578  247 ALA A O   
1799 C CB  . ALA A 247 ? 0.2433 0.7126 0.1656 0.0950  0.0921  0.1001  247 ALA A CB  
1800 N N   . LEU A 248 ? 0.1393 0.7361 0.2111 0.0998  0.0465  0.0824  248 LEU A N   
1801 C CA  . LEU A 248 ? 0.1709 0.7311 0.2423 0.0923  0.0482  0.0780  248 LEU A CA  
1802 C C   . LEU A 248 ? 0.2016 0.7248 0.3119 0.1142  0.0499  0.0832  248 LEU A C   
1803 O O   . LEU A 248 ? 0.2149 0.7614 0.3851 0.0993  0.0612  0.0621  248 LEU A O   
1804 C CB  . LEU A 248 ? 0.1759 0.7167 0.1930 0.0885  0.0807  0.0560  248 LEU A CB  
1805 C CG  . LEU A 248 ? 0.1610 0.6883 0.1688 0.0705  0.0980  0.0264  248 LEU A CG  
1806 C CD1 . LEU A 248 ? 0.1698 0.6703 0.1428 0.0655  0.1077  0.0227  248 LEU A CD1 
1807 C CD2 . LEU A 248 ? 0.2027 0.6920 0.1908 0.0794  0.0866  0.0194  248 LEU A CD2 
1808 N N   . GLY A 249 ? 0.1986 0.7437 0.3001 0.1345  0.0116  0.1161  249 GLY A N   
1809 C CA  . GLY A 249 ? 0.2327 0.7498 0.2891 0.1626  0.0390  0.1116  249 GLY A CA  
1810 C C   . GLY A 249 ? 0.2300 0.7603 0.3561 0.1686  0.1052  0.1056  249 GLY A C   
1811 O O   . GLY A 249 ? 0.2587 0.8214 0.4643 0.2065  0.1117  0.1061  249 GLY A O   
1812 N N   . HIS A 250 ? 0.2639 0.7358 0.3584 0.2017  0.1056  0.0984  250 HIS A N   
1813 C CA  . HIS A 250 ? 0.2173 0.7218 0.3724 0.1565  0.1347  0.1182  250 HIS A CA  
1814 C C   . HIS A 250 ? 0.3126 0.7534 0.5594 0.1297  0.0879  0.0648  250 HIS A C   
1815 O O   . HIS A 250 ? 0.3981 0.7525 0.6368 0.1151  -0.0035 -0.0041 250 HIS A O   
1816 C CB  . HIS A 250 ? 0.2646 0.7216 0.3178 0.1579  0.1325  0.1047  250 HIS A CB  
1817 C CG  . HIS A 250 ? 0.2981 0.7104 0.4541 0.1280  0.0505  0.1383  250 HIS A CG  
1818 N ND1 . HIS A 250 ? 0.3035 0.7276 0.4873 0.1027  0.0318  0.1471  250 HIS A ND1 
1819 C CD2 . HIS A 250 ? 0.2810 0.6990 0.4653 0.1207  0.0257  0.1435  250 HIS A CD2 
1820 C CE1 . HIS A 250 ? 0.3318 0.7059 0.4499 0.0997  0.0215  0.1593  250 HIS A CE1 
1821 N NE2 . HIS A 250 ? 0.2491 0.7263 0.4726 0.0848  0.0518  0.1738  250 HIS A NE2 
1822 N N   . ASP B 3   ? 0.4396 0.7468 0.2926 -0.0463 0.0215  -0.0881 3   ASP B N   
1823 C CA  . ASP B 3   ? 0.3778 0.6726 0.3028 -0.0068 -0.0029 -0.1473 3   ASP B CA  
1824 C C   . ASP B 3   ? 0.2973 0.5891 0.2946 -0.0470 0.0142  -0.1400 3   ASP B C   
1825 O O   . ASP B 3   ? 0.2674 0.5571 0.2417 -0.0136 0.0503  -0.1447 3   ASP B O   
1826 C CB  . ASP B 3   ? 0.4283 0.7294 0.3754 0.0236  -0.0264 -0.1254 3   ASP B CB  
1827 C CG  . ASP B 3   ? 0.4025 0.8041 0.4593 0.0316  -0.0171 -0.0726 3   ASP B CG  
1828 O OD1 . ASP B 3   ? 0.3885 0.8472 0.4058 0.0325  0.0232  -0.1302 3   ASP B OD1 
1829 O OD2 . ASP B 3   ? 0.4970 0.8239 0.6210 0.0888  -0.0290 -0.0701 3   ASP B OD2 
1830 N N   . LEU B 4   ? 0.2025 0.5599 0.2868 -0.0367 0.0284  -0.1566 4   LEU B N   
1831 C CA  . LEU B 4   ? 0.1743 0.5382 0.3082 -0.0381 0.0260  -0.1531 4   LEU B CA  
1832 C C   . LEU B 4   ? 0.1663 0.5201 0.2934 -0.0442 0.0360  -0.1403 4   LEU B C   
1833 O O   . LEU B 4   ? 0.1965 0.5233 0.2518 -0.0534 0.0466  -0.1298 4   LEU B O   
1834 C CB  . LEU B 4   ? 0.2192 0.5281 0.3646 -0.0313 0.0477  -0.1581 4   LEU B CB  
1835 C CG  . LEU B 4   ? 0.2104 0.5113 0.4055 -0.0214 0.0604  -0.1568 4   LEU B CG  
1836 C CD1 . LEU B 4   ? 0.2060 0.5274 0.4100 -0.0215 0.0389  -0.1356 4   LEU B CD1 
1837 C CD2 . LEU B 4   ? 0.2865 0.5381 0.4783 0.0027  0.0592  -0.1416 4   LEU B CD2 
1838 N N   . LYS B 5   ? 0.1703 0.5097 0.2927 -0.0500 0.0416  -0.1441 5   LYS B N   
1839 C CA  . LYS B 5   ? 0.1964 0.5213 0.2991 -0.0519 0.0419  -0.1504 5   LYS B CA  
1840 C C   . LYS B 5   ? 0.1605 0.4938 0.2440 -0.0415 0.0363  -0.1273 5   LYS B C   
1841 O O   . LYS B 5   ? 0.1580 0.5100 0.2376 -0.0618 0.0724  -0.1418 5   LYS B O   
1842 C CB  . LYS B 5   ? 0.2069 0.5719 0.3964 -0.0785 0.0312  -0.1413 5   LYS B CB  
1843 C CG  . LYS B 5   ? 0.2393 0.6152 0.4715 -0.0988 0.0521  -0.1434 5   LYS B CG  
1844 C CD  . LYS B 5   ? 0.2336 0.6963 0.5893 -0.1276 0.0308  -0.1402 5   LYS B CD  
1845 C CE  . LYS B 5   ? 0.4317 0.7391 0.6629 -0.1260 -0.0148 -0.1353 5   LYS B CE  
1846 N NZ  . LYS B 5   ? 0.5681 0.7927 0.6898 -0.1147 -0.0639 -0.1542 5   LYS B NZ  
1847 N N   . ALA B 6   ? 0.1847 0.4853 0.2428 -0.0385 0.0380  -0.1038 6   ALA B N   
1848 C CA  . ALA B 6   ? 0.1847 0.4638 0.2278 -0.0182 0.0252  -0.0934 6   ALA B CA  
1849 C C   . ALA B 6   ? 0.1565 0.4319 0.1819 -0.0008 0.0342  -0.0840 6   ALA B C   
1850 O O   . ALA B 6   ? 0.1512 0.4315 0.1957 0.0156  0.0690  -0.0776 6   ALA B O   
1851 C CB  . ALA B 6   ? 0.2189 0.4973 0.2352 -0.0072 0.0264  -0.0725 6   ALA B CB  
1852 N N   . SER B 7   ? 0.1468 0.4288 0.1902 -0.0173 0.0461  -0.0977 7   SER B N   
1853 C CA  . SER B 7   ? 0.1177 0.4171 0.1935 -0.0079 0.0723  -0.0891 7   SER B CA  
1854 C C   . SER B 7   ? 0.1268 0.3722 0.1828 -0.0124 0.0635  -0.0801 7   SER B C   
1855 O O   . SER B 7   ? 0.1203 0.3478 0.1683 -0.0002 0.0904  -0.0774 7   SER B O   
1856 C CB  . SER B 7   ? 0.1962 0.4437 0.2305 0.0217  0.1047  -0.0919 7   SER B CB  
1857 O OG  . SER B 7   ? 0.2278 0.5246 0.3386 -0.0295 0.0638  -0.1018 7   SER B OG  
1858 N N   . SER B 8   ? 0.1112 0.3532 0.1744 -0.0185 0.0552  -0.0800 8   SER B N   
1859 C CA  . SER B 8   ? 0.1082 0.3304 0.1801 -0.0100 0.0602  -0.0652 8   SER B CA  
1860 C C   . SER B 8   ? 0.1047 0.3280 0.1661 -0.0214 0.0652  -0.0537 8   SER B C   
1861 O O   . SER B 8   ? 0.1082 0.3365 0.1502 -0.0374 0.0745  -0.0475 8   SER B O   
1862 C CB  . SER B 8   ? 0.1218 0.3278 0.2141 -0.0180 0.0474  -0.0709 8   SER B CB  
1863 O OG  . SER B 8   ? 0.1490 0.3371 0.2516 -0.0094 0.0664  -0.0719 8   SER B OG  
1864 N N   . LEU B 9   ? 0.0981 0.3533 0.1597 -0.0120 0.0762  -0.0564 9   LEU B N   
1865 C CA  . LEU B 9   ? 0.0924 0.3528 0.1775 -0.0069 0.0779  -0.0563 9   LEU B CA  
1866 C C   . LEU B 9   ? 0.1201 0.3323 0.1540 0.0030  0.0828  -0.0493 9   LEU B C   
1867 O O   . LEU B 9   ? 0.1034 0.3435 0.1662 -0.0007 0.0825  -0.0584 9   LEU B O   
1868 C CB  . LEU B 9   ? 0.1053 0.4149 0.1993 -0.0122 0.0658  -0.0556 9   LEU B CB  
1869 C CG  . LEU B 9   ? 0.1406 0.4520 0.2435 0.0095  0.0531  -0.0731 9   LEU B CG  
1870 C CD1 . LEU B 9   ? 0.2022 0.4801 0.2562 0.0376  0.0859  -0.0707 9   LEU B CD1 
1871 C CD2 . LEU B 9   ? 0.1717 0.5122 0.2893 0.0080  0.0194  -0.0618 9   LEU B CD2 
1872 N N   . ARG B 10  ? 0.1440 0.3346 0.1337 -0.0040 0.0709  -0.0392 10  ARG B N   
1873 C CA  . ARG B 10  ? 0.1493 0.3218 0.1356 0.0039  0.0829  -0.0286 10  ARG B CA  
1874 C C   . ARG B 10  ? 0.1118 0.2916 0.1189 -0.0063 0.0946  -0.0246 10  ARG B C   
1875 O O   . ARG B 10  ? 0.1097 0.2950 0.1280 0.0009  0.0906  -0.0280 10  ARG B O   
1876 C CB  . ARG B 10  ? 0.1835 0.3659 0.1550 0.0293  0.0982  -0.0374 10  ARG B CB  
1877 C CG  . ARG B 10  ? 0.2072 0.4183 0.1956 0.0290  0.1158  -0.0165 10  ARG B CG  
1878 C CD  . ARG B 10  ? 0.2341 0.4689 0.1779 0.0376  0.1224  0.0226  10  ARG B CD  
1879 N NE  . ARG B 10  ? 0.1990 0.5382 0.1522 0.0049  0.1077  0.0483  10  ARG B NE  
1880 C CZ  . ARG B 10  ? 0.2530 0.5726 0.1107 0.0090  0.0826  -0.0006 10  ARG B CZ  
1881 N NH1 . ARG B 10  ? 0.2605 0.6005 0.1539 0.0385  0.1034  0.0350  10  ARG B NH1 
1882 N NH2 . ARG B 10  ? 0.2280 0.6293 0.1540 -0.0311 0.0579  0.0411  10  ARG B NH2 
1883 N N   . ALA B 11  ? 0.1067 0.2939 0.1178 -0.0143 0.0836  -0.0344 11  ALA B N   
1884 C CA  . ALA B 11  ? 0.0908 0.2794 0.1232 -0.0111 0.0828  -0.0226 11  ALA B CA  
1885 C C   . ALA B 11  ? 0.0747 0.2852 0.1212 -0.0124 0.0660  -0.0264 11  ALA B C   
1886 O O   . ALA B 11  ? 0.0699 0.2856 0.1195 0.0015  0.0741  -0.0362 11  ALA B O   
1887 C CB  . ALA B 11  ? 0.0913 0.2866 0.1318 -0.0076 0.0791  -0.0217 11  ALA B CB  
1888 N N   . LEU B 12  ? 0.0699 0.2866 0.1038 -0.0021 0.0706  -0.0330 12  LEU B N   
1889 C CA  . LEU B 12  ? 0.0572 0.2915 0.1075 -0.0034 0.0709  -0.0298 12  LEU B CA  
1890 C C   . LEU B 12  ? 0.0482 0.2923 0.1094 -0.0025 0.0655  -0.0173 12  LEU B C   
1891 O O   . LEU B 12  ? 0.0573 0.2979 0.0966 -0.0007 0.0676  -0.0145 12  LEU B O   
1892 C CB  . LEU B 12  ? 0.0632 0.3077 0.1303 -0.0048 0.0783  -0.0411 12  LEU B CB  
1893 C CG  . LEU B 12  ? 0.0793 0.3238 0.1270 -0.0160 0.0815  -0.0350 12  LEU B CG  
1894 C CD1 . LEU B 12  ? 0.0671 0.3553 0.1570 -0.0186 0.0956  -0.0202 12  LEU B CD1 
1895 C CD2 . LEU B 12  ? 0.0715 0.3373 0.1561 -0.0192 0.0722  -0.0231 12  LEU B CD2 
1896 N N   . LYS B 13  ? 0.0676 0.2970 0.0910 -0.0039 0.0719  -0.0131 13  LYS B N   
1897 C CA  . LYS B 13  ? 0.0695 0.2902 0.0981 0.0002  0.0679  -0.0132 13  LYS B CA  
1898 C C   . LYS B 13  ? 0.0593 0.2725 0.0847 0.0130  0.0603  -0.0204 13  LYS B C   
1899 O O   . LYS B 13  ? 0.0606 0.2863 0.1389 0.0039  0.0652  -0.0246 13  LYS B O   
1900 C CB  . LYS B 13  ? 0.0729 0.2961 0.1291 0.0211  0.0665  -0.0148 13  LYS B CB  
1901 C CG  . LYS B 13  ? 0.0751 0.3242 0.1699 0.0173  0.0651  -0.0165 13  LYS B CG  
1902 C CD  . LYS B 13  ? 0.0942 0.3641 0.2179 0.0185  0.0490  -0.0013 13  LYS B CD  
1903 C CE  . LYS B 13  ? 0.1008 0.4197 0.2815 0.0007  0.0472  -0.0127 13  LYS B CE  
1904 N NZ  . LYS B 13  ? 0.1663 0.4781 0.3086 0.0034  0.0295  -0.0024 13  LYS B NZ  
1905 N N   . LEU B 14  ? 0.0391 0.2755 0.0934 0.0085  0.0516  -0.0268 14  LEU B N   
1906 C CA  . LEU B 14  ? 0.0469 0.2825 0.0895 -0.0105 0.0525  -0.0104 14  LEU B CA  
1907 C C   . LEU B 14  ? 0.0480 0.2728 0.0859 -0.0110 0.0572  0.0027  14  LEU B C   
1908 O O   . LEU B 14  ? 0.0494 0.2916 0.0932 -0.0074 0.0611  -0.0126 14  LEU B O   
1909 C CB  . LEU B 14  ? 0.0558 0.2896 0.0984 -0.0011 0.0577  -0.0116 14  LEU B CB  
1910 C CG  . LEU B 14  ? 0.0687 0.3008 0.0864 -0.0101 0.0634  -0.0108 14  LEU B CG  
1911 C CD1 . LEU B 14  ? 0.0856 0.3026 0.0938 -0.0061 0.0682  -0.0110 14  LEU B CD1 
1912 C CD2 . LEU B 14  ? 0.0647 0.3049 0.0928 -0.0066 0.0555  -0.0188 14  LEU B CD2 
1913 N N   . MET B 15  ? 0.0671 0.2785 0.0868 -0.0061 0.0700  -0.0061 15  MET B N   
1914 C CA  . MET B 15  ? 0.0592 0.2636 0.0992 -0.0085 0.0700  -0.0080 15  MET B CA  
1915 C C   . MET B 15  ? 0.0587 0.2609 0.0937 -0.0011 0.0676  -0.0056 15  MET B C   
1916 O O   . MET B 15  ? 0.0618 0.2666 0.0997 0.0054  0.0698  -0.0144 15  MET B O   
1917 C CB  . MET B 15  ? 0.0675 0.2864 0.1473 -0.0301 0.0916  -0.0138 15  MET B CB  
1918 C CG  . MET B 15  ? 0.0874 0.3280 0.1832 -0.0553 0.0917  -0.0039 15  MET B CG  
1919 S SD  . MET B 15  ? 0.1425 0.3322 0.2719 -0.0327 0.1006  0.0337  15  MET B SD  
1920 C CE  . MET B 15  ? 0.1863 0.3234 0.2881 -0.0219 0.0657  0.0414  15  MET B CE  
1921 N N   . ASP B 16  ? 0.0611 0.2756 0.0855 0.0065  0.0653  -0.0114 16  ASP B N   
1922 C CA  . ASP B 16  ? 0.0563 0.2645 0.0978 0.0064  0.0673  -0.0054 16  ASP B CA  
1923 C C   . ASP B 16  ? 0.0653 0.2768 0.0929 0.0159  0.0711  0.0042  16  ASP B C   
1924 O O   . ASP B 16  ? 0.0885 0.3031 0.1075 0.0266  0.0742  0.0137  16  ASP B O   
1925 C CB  . ASP B 16  ? 0.0485 0.2689 0.1201 0.0028  0.0669  0.0057  16  ASP B CB  
1926 C CG  . ASP B 16  ? 0.0539 0.2827 0.1138 0.0009  0.0713  0.0143  16  ASP B CG  
1927 O OD1 . ASP B 16  ? 0.1117 0.2972 0.0885 0.0025  0.0582  0.0116  16  ASP B OD1 
1928 O OD2 . ASP B 16  ? 0.0790 0.3064 0.1955 -0.0261 0.1016  0.0155  16  ASP B OD2 
1929 N N   . LEU B 17  ? 0.0565 0.2726 0.1047 0.0175  0.0686  -0.0110 17  LEU B N   
1930 C CA  . LEU B 17  ? 0.0676 0.2666 0.1210 0.0069  0.0782  -0.0093 17  LEU B CA  
1931 C C   . LEU B 17  ? 0.0706 0.2624 0.1135 -0.0049 0.0828  0.0040  17  LEU B C   
1932 O O   . LEU B 17  ? 0.0886 0.2666 0.1302 -0.0132 0.0618  0.0171  17  LEU B O   
1933 C CB  . LEU B 17  ? 0.0826 0.2787 0.1124 0.0004  0.0894  -0.0169 17  LEU B CB  
1934 C CG  . LEU B 17  ? 0.0847 0.2921 0.1427 -0.0191 0.1010  -0.0100 17  LEU B CG  
1935 C CD1 . LEU B 17  ? 0.1198 0.2978 0.1757 -0.0230 0.0845  -0.0140 17  LEU B CD1 
1936 C CD2 . LEU B 17  ? 0.0841 0.3111 0.1561 -0.0313 0.1061  -0.0042 17  LEU B CD2 
1937 N N   . SER B 18  ? 0.1191 0.2773 0.1476 0.0138  0.0851  -0.0074 18  SER B N   
1938 C CA  . SER B 18  ? 0.1977 0.3268 0.2160 0.0129  0.0506  -0.0123 18  SER B CA  
1939 C C   . SER B 18  ? 0.3084 0.3256 0.2906 -0.0168 0.0208  -0.0026 18  SER B C   
1940 O O   . SER B 18  ? 0.3717 0.3118 0.3146 -0.0382 0.0040  0.0262  18  SER B O   
1941 C CB  . SER B 18  ? 0.2218 0.3862 0.3182 -0.0057 0.0383  -0.0199 18  SER B CB  
1942 O OG  . SER B 18  ? 0.2355 0.4990 0.4002 0.0264  0.0624  -0.0420 18  SER B OG  
1943 N N   . THR B 19  ? 0.3846 0.3787 0.3458 -0.0261 0.0098  0.0284  19  THR B N   
1944 C CA  . THR B 19  ? 0.4291 0.4483 0.3607 -0.0145 0.0812  0.0559  19  THR B CA  
1945 C C   . THR B 19  ? 0.3952 0.4491 0.4514 -0.0132 0.1006  0.0556  19  THR B C   
1946 O O   . THR B 19  ? 0.4955 0.5504 0.4240 0.0603  0.1083  0.0890  19  THR B O   
1947 C CB  . THR B 19  ? 0.3424 0.5115 0.4099 -0.0129 0.1326  0.0572  19  THR B CB  
1948 O OG1 . THR B 19  ? 0.3336 0.5850 0.4189 -0.0052 0.1132  0.1056  19  THR B OG1 
1949 C CG2 . THR B 19  ? 0.2252 0.5366 0.3745 -0.0489 0.1873  0.0641  19  THR B CG2 
1950 N N   . GLY B 22  ? 0.5282 0.5163 0.6007 0.0408  -0.0326 -0.0018 22  GLY B N   
1951 C CA  . GLY B 22  ? 0.4057 0.4598 0.5079 0.0372  -0.0435 -0.0015 22  GLY B CA  
1952 C C   . GLY B 22  ? 0.4202 0.4793 0.5538 0.0157  -0.0291 0.0382  22  GLY B C   
1953 O O   . GLY B 22  ? 0.4965 0.4733 0.6689 -0.0175 -0.1104 0.1475  22  GLY B O   
1954 N N   . ASP B 23  ? 0.3338 0.4556 0.4818 0.0593  0.0310  0.0183  23  ASP B N   
1955 C CA  . ASP B 23  ? 0.3676 0.4557 0.3485 0.0221  0.0509  0.0217  23  ASP B CA  
1956 C C   . ASP B 23  ? 0.3897 0.4713 0.3469 -0.0182 0.0488  0.0486  23  ASP B C   
1957 O O   . ASP B 23  ? 0.4042 0.5474 0.4726 -0.0713 0.0331  0.0331  23  ASP B O   
1958 C CB  . ASP B 23  ? 0.3272 0.4461 0.3392 0.0102  0.0938  0.0146  23  ASP B CB  
1959 C CG  . ASP B 23  ? 0.3237 0.4084 0.3418 0.0018  0.0901  0.0081  23  ASP B CG  
1960 O OD1 . ASP B 23  ? 0.3363 0.4799 0.4902 0.0165  0.1492  -0.0280 23  ASP B OD1 
1961 O OD2 . ASP B 23  ? 0.2076 0.3578 0.2234 0.0047  0.0867  0.0256  23  ASP B OD2 
1962 N N   . TYR B 24  ? 0.3137 0.4564 0.3157 -0.0033 0.0464  0.0724  24  TYR B N   
1963 C CA  . TYR B 24  ? 0.3046 0.4868 0.3155 0.0049  0.0496  0.0674  24  TYR B CA  
1964 C C   . TYR B 24  ? 0.2515 0.4887 0.3090 0.0271  0.0078  0.0241  24  TYR B C   
1965 O O   . TYR B 24  ? 0.3103 0.5576 0.3144 0.0027  0.0014  0.0072  24  TYR B O   
1966 C CB  . TYR B 24  ? 0.3047 0.4870 0.2979 0.0000  0.0714  0.0920  24  TYR B CB  
1967 C CG  . TYR B 24  ? 0.3275 0.4729 0.2892 -0.0149 0.0914  0.0718  24  TYR B CG  
1968 C CD1 . TYR B 24  ? 0.3549 0.4682 0.2855 -0.0214 0.0675  0.0598  24  TYR B CD1 
1969 C CD2 . TYR B 24  ? 0.3339 0.5090 0.3201 -0.0262 0.0929  0.0358  24  TYR B CD2 
1970 C CE1 . TYR B 24  ? 0.3392 0.5107 0.3482 -0.0063 0.0896  0.0579  24  TYR B CE1 
1971 C CE2 . TYR B 24  ? 0.3246 0.5679 0.3712 -0.0191 0.0956  0.0378  24  TYR B CE2 
1972 C CZ  . TYR B 24  ? 0.3333 0.5586 0.3804 0.0153  0.1056  0.0146  24  TYR B CZ  
1973 O OH  . TYR B 24  ? 0.3379 0.6263 0.4556 -0.0128 0.1534  0.0426  24  TYR B OH  
1974 N N   . THR B 25  ? 0.2040 0.4412 0.2735 0.0294  0.0203  0.0524  25  THR B N   
1975 C CA  . THR B 25  ? 0.2299 0.3939 0.2377 0.0140  0.0124  0.0414  25  THR B CA  
1976 C C   . THR B 25  ? 0.2289 0.3579 0.1824 0.0164  0.0281  0.0440  25  THR B C   
1977 O O   . THR B 25  ? 0.2347 0.3715 0.1663 -0.0127 0.0502  0.0471  25  THR B O   
1978 C CB  . THR B 25  ? 0.2588 0.3900 0.1957 0.0089  0.0136  0.0583  25  THR B CB  
1979 O OG1 . THR B 25  ? 0.2498 0.3734 0.1768 0.0079  0.0522  0.0450  25  THR B OG1 
1980 C CG2 . THR B 25  ? 0.2683 0.3864 0.2102 0.0127  0.0269  0.0642  25  THR B CG2 
1981 N N   . ASP B 26  ? 0.2678 0.3790 0.1818 0.0234  0.0256  0.0350  26  ASP B N   
1982 C CA  . ASP B 26  ? 0.2637 0.3507 0.1548 0.0379  0.0459  0.0255  26  ASP B CA  
1983 C C   . ASP B 26  ? 0.2349 0.3332 0.1305 0.0360  0.0622  0.0417  26  ASP B C   
1984 O O   . ASP B 26  ? 0.1994 0.3479 0.1050 0.0320  0.0567  0.0181  26  ASP B O   
1985 C CB  . ASP B 26  ? 0.3656 0.3737 0.1830 0.0297  0.0397  -0.0157 26  ASP B CB  
1986 C CG  . ASP B 26  ? 0.4233 0.4050 0.2430 0.0147  0.0304  -0.0411 26  ASP B CG  
1987 O OD1 . ASP B 26  ? 0.3733 0.4174 0.2655 -0.0042 -0.0095 -0.0286 26  ASP B OD1 
1988 O OD2 . ASP B 26  ? 0.5933 0.4834 0.2557 0.0052  0.0521  -0.0786 26  ASP B OD2 
1989 N N   . GLU B 27  ? 0.2366 0.3322 0.1352 0.0172  0.0560  0.0465  27  GLU B N   
1990 C CA  . GLU B 27  ? 0.2308 0.3470 0.1405 0.0087  0.0727  0.0473  27  GLU B CA  
1991 C C   . GLU B 27  ? 0.2036 0.3312 0.1220 -0.0064 0.0628  0.0508  27  GLU B C   
1992 O O   . GLU B 27  ? 0.2114 0.3598 0.1332 -0.0258 0.0628  0.0461  27  GLU B O   
1993 C CB  . GLU B 27  ? 0.2666 0.3882 0.1840 -0.0057 0.0783  0.0755  27  GLU B CB  
1994 C CG  . GLU B 27  ? 0.3173 0.4358 0.2545 0.0026  0.0895  0.0632  27  GLU B CG  
1995 C CD  . GLU B 27  ? 0.3122 0.5186 0.2843 -0.0386 0.1650  0.0760  27  GLU B CD  
1996 O OE1 . GLU B 27  ? 0.3777 0.6355 0.3568 -0.0195 0.1602  0.0618  27  GLU B OE1 
1997 O OE2 . GLU B 27  ? 0.4477 0.6153 0.4090 -0.1076 0.1014  0.0536  27  GLU B OE2 
1998 N N   . LYS B 28  ? 0.1961 0.3012 0.1017 -0.0119 0.0535  0.0391  28  LYS B N   
1999 C CA  . LYS B 28  ? 0.2238 0.3143 0.1051 -0.0075 0.0606  0.0405  28  LYS B CA  
2000 C C   . LYS B 28  ? 0.1463 0.2865 0.1037 -0.0046 0.0687  0.0296  28  LYS B C   
2001 O O   . LYS B 28  ? 0.1640 0.3201 0.1099 -0.0099 0.0657  0.0190  28  LYS B O   
2002 C CB  . LYS B 28  ? 0.2267 0.3617 0.1255 -0.0071 0.0679  0.0453  28  LYS B CB  
2003 C CG  . LYS B 28  ? 0.3300 0.3988 0.1876 -0.0049 0.0790  0.0522  28  LYS B CG  
2004 C CD  . LYS B 28  ? 0.3922 0.4304 0.1483 -0.0075 0.0742  0.0608  28  LYS B CD  
2005 C CE  . LYS B 28  ? 0.4038 0.4219 0.1671 -0.0112 0.0993  0.0554  28  LYS B CE  
2006 N NZ  . LYS B 28  ? 0.4093 0.4624 0.2831 0.0057  0.0381  0.0540  28  LYS B NZ  
2007 N N   . VAL B 29  ? 0.1430 0.2908 0.0982 -0.0088 0.0583  0.0240  29  VAL B N   
2008 C CA  . VAL B 29  ? 0.1217 0.2905 0.1076 -0.0121 0.0667  0.0225  29  VAL B CA  
2009 C C   . VAL B 29  ? 0.1129 0.2965 0.0651 -0.0098 0.0698  0.0239  29  VAL B C   
2010 O O   . VAL B 29  ? 0.1046 0.3259 0.0598 -0.0114 0.0696  0.0287  29  VAL B O   
2011 C CB  . VAL B 29  ? 0.1311 0.3019 0.1263 -0.0177 0.0630  0.0203  29  VAL B CB  
2012 C CG1 . VAL B 29  ? 0.1284 0.3039 0.1055 -0.0168 0.0733  0.0220  29  VAL B CG1 
2013 C CG2 . VAL B 29  ? 0.1467 0.3108 0.1709 -0.0255 0.0327  0.0345  29  VAL B CG2 
2014 N N   . ILE B 30  ? 0.1050 0.3339 0.0735 -0.0132 0.0720  0.0231  30  ILE B N   
2015 C CA  . ILE B 30  ? 0.1419 0.3425 0.0795 -0.0071 0.0670  0.0318  30  ILE B CA  
2016 C C   . ILE B 30  ? 0.1261 0.3376 0.0778 -0.0075 0.0806  0.0269  30  ILE B C   
2017 O O   . ILE B 30  ? 0.1247 0.3758 0.0965 -0.0153 0.0766  0.0253  30  ILE B O   
2018 C CB  . ILE B 30  ? 0.1776 0.3681 0.0913 0.0002  0.0856  0.0158  30  ILE B CB  
2019 C CG1 . ILE B 30  ? 0.2026 0.3701 0.1038 0.0119  0.0983  0.0035  30  ILE B CG1 
2020 C CG2 . ILE B 30  ? 0.1791 0.3864 0.1227 -0.0064 0.0788  0.0265  30  ILE B CG2 
2021 C CD1 . ILE B 30  ? 0.2446 0.3971 0.1062 0.0103  0.1068  0.0030  30  ILE B CD1 
2022 N N   . ALA B 31  ? 0.1159 0.3584 0.0901 -0.0148 0.0721  0.0353  31  ALA B N   
2023 C CA  . ALA B 31  ? 0.1281 0.3443 0.1163 -0.0276 0.0608  0.0283  31  ALA B CA  
2024 C C   . ALA B 31  ? 0.1228 0.3435 0.1025 -0.0405 0.0400  0.0240  31  ALA B C   
2025 O O   . ALA B 31  ? 0.1241 0.3546 0.0968 -0.0404 0.0429  0.0148  31  ALA B O   
2026 C CB  . ALA B 31  ? 0.1569 0.3465 0.1435 -0.0384 0.0560  0.0496  31  ALA B CB  
2027 N N   . LEU B 32  ? 0.1138 0.3148 0.0805 -0.0238 0.0638  0.0087  32  LEU B N   
2028 C CA  . LEU B 32  ? 0.1053 0.3025 0.0823 -0.0170 0.0726  -0.0009 32  LEU B CA  
2029 C C   . LEU B 32  ? 0.0901 0.3075 0.0820 -0.0108 0.0668  -0.0011 32  LEU B C   
2030 O O   . LEU B 32  ? 0.0728 0.3270 0.0903 -0.0227 0.0699  0.0083  32  LEU B O   
2031 C CB  . LEU B 32  ? 0.1151 0.3008 0.0801 -0.0273 0.0655  0.0092  32  LEU B CB  
2032 C CG  . LEU B 32  ? 0.1264 0.3156 0.0872 -0.0352 0.0666  0.0233  32  LEU B CG  
2033 C CD1 . LEU B 32  ? 0.1330 0.3507 0.1334 -0.0447 0.0654  0.0128  32  LEU B CD1 
2034 C CD2 . LEU B 32  ? 0.1055 0.3130 0.0999 -0.0187 0.0635  0.0286  32  LEU B CD2 
2035 N N   . CYS B 33  ? 0.1027 0.2987 0.0718 -0.0103 0.0641  0.0016  33  CYS B N   
2036 C CA  . CYS B 33  ? 0.0906 0.3077 0.0864 0.0001  0.0656  -0.0030 33  CYS B CA  
2037 C C   . CYS B 33  ? 0.0892 0.3190 0.0909 -0.0124 0.0666  0.0116  33  CYS B C   
2038 O O   . CYS B 33  ? 0.0880 0.3407 0.0838 0.0090  0.0795  0.0101  33  CYS B O   
2039 C CB  . CYS B 33  ? 0.1289 0.3278 0.0750 0.0136  0.0573  -0.0144 33  CYS B CB  
2040 S SG  . CYS B 33  ? 0.1868 0.3208 0.1430 -0.0033 0.0441  -0.0046 33  CYS B SG  
2041 N N   . HIS B 34  ? 0.0956 0.3279 0.0933 -0.0156 0.0685  0.0115  34  HIS B N   
2042 C CA  . HIS B 34  ? 0.0827 0.3718 0.1120 -0.0214 0.0896  -0.0103 34  HIS B CA  
2043 C C   . HIS B 34  ? 0.0944 0.3632 0.1026 -0.0257 0.0668  -0.0032 34  HIS B C   
2044 O O   . HIS B 34  ? 0.0912 0.3946 0.1217 -0.0296 0.0559  -0.0113 34  HIS B O   
2045 C CB  . HIS B 34  ? 0.1064 0.4064 0.1371 -0.0286 0.1073  0.0017  34  HIS B CB  
2046 C CG  . HIS B 34  ? 0.0952 0.4529 0.1501 -0.0162 0.1130  -0.0106 34  HIS B CG  
2047 N ND1 . HIS B 34  ? 0.1700 0.5028 0.1825 -0.0122 0.1177  0.0221  34  HIS B ND1 
2048 C CD2 . HIS B 34  ? 0.1281 0.4794 0.1720 -0.0223 0.1409  0.0089  34  HIS B CD2 
2049 C CE1 . HIS B 34  ? 0.1871 0.5213 0.1441 -0.0069 0.1572  0.0172  34  HIS B CE1 
2050 N NE2 . HIS B 34  ? 0.1679 0.5141 0.1616 -0.0218 0.1413  -0.0318 34  HIS B NE2 
2051 N N   A GLN B 35  ? 0.0789 0.3598 0.1009 -0.0351 0.0656  0.0016  35  GLN B N   
2052 N N   B GLN B 35  ? 0.0720 0.3596 0.1223 -0.0364 0.0646  -0.0136 35  GLN B N   
2053 C CA  A GLN B 35  ? 0.0980 0.3455 0.1030 -0.0355 0.0669  0.0031  35  GLN B CA  
2054 C CA  B GLN B 35  ? 0.0876 0.3420 0.1364 -0.0347 0.0651  -0.0201 35  GLN B CA  
2055 C C   A GLN B 35  ? 0.0994 0.3321 0.1053 -0.0296 0.0646  0.0008  35  GLN B C   
2056 C C   B GLN B 35  ? 0.0942 0.3318 0.1282 -0.0292 0.0632  -0.0186 35  GLN B C   
2057 O O   A GLN B 35  ? 0.1222 0.3420 0.1062 -0.0202 0.0668  0.0002  35  GLN B O   
2058 O O   B GLN B 35  ? 0.1177 0.3397 0.1303 -0.0184 0.0712  -0.0282 35  GLN B O   
2059 C CB  A GLN B 35  ? 0.1183 0.3510 0.1048 -0.0335 0.0700  0.0186  35  GLN B CB  
2060 C CB  B GLN B 35  ? 0.1017 0.3485 0.1779 -0.0298 0.0656  -0.0257 35  GLN B CB  
2061 C CG  A GLN B 35  ? 0.1690 0.3731 0.1128 -0.0320 0.0730  0.0394  35  GLN B CG  
2062 C CG  B GLN B 35  ? 0.1517 0.3557 0.2142 -0.0220 0.0664  -0.0315 35  GLN B CG  
2063 C CD  A GLN B 35  ? 0.2305 0.4032 0.1687 -0.0113 0.0590  0.0571  35  GLN B CD  
2064 C CD  B GLN B 35  ? 0.1863 0.3900 0.2828 -0.0059 0.0471  -0.0309 35  GLN B CD  
2065 O OE1 A GLN B 35  ? 0.2437 0.4730 0.2241 0.0012  0.0415  0.0698  35  GLN B OE1 
2066 O OE1 B GLN B 35  ? 0.2482 0.4287 0.3035 -0.0241 0.0497  -0.0310 35  GLN B OE1 
2067 N NE2 A GLN B 35  ? 0.2854 0.4208 0.1994 -0.0144 0.0365  0.0873  35  GLN B NE2 
2068 N NE2 B GLN B 35  ? 0.2554 0.3983 0.3576 0.0001  0.0190  -0.0186 35  GLN B NE2 
2069 N N   . ALA B 36  ? 0.0749 0.3203 0.0807 -0.0257 0.0659  -0.0098 36  ALA B N   
2070 C CA  . ALA B 36  ? 0.0821 0.3154 0.0897 -0.0187 0.0627  -0.0074 36  ALA B CA  
2071 C C   . ALA B 36  ? 0.0526 0.3138 0.1017 -0.0162 0.0660  -0.0038 36  ALA B C   
2072 O O   . ALA B 36  ? 0.0371 0.3364 0.1063 0.0048  0.0553  -0.0073 36  ALA B O   
2073 C CB  . ALA B 36  ? 0.0790 0.3117 0.0848 -0.0218 0.0725  -0.0148 36  ALA B CB  
2074 N N   . LYS B 37  ? 0.0586 0.3437 0.0864 -0.0137 0.0647  -0.0156 37  LYS B N   
2075 C CA  . LYS B 37  ? 0.0613 0.3364 0.0994 -0.0138 0.0715  -0.0142 37  LYS B CA  
2076 C C   . LYS B 37  ? 0.0728 0.3214 0.1081 -0.0119 0.0796  -0.0194 37  LYS B C   
2077 O O   . LYS B 37  ? 0.0898 0.3703 0.1266 -0.0318 0.0997  -0.0174 37  LYS B O   
2078 C CB  . LYS B 37  ? 0.0792 0.3418 0.1081 -0.0061 0.0773  -0.0263 37  LYS B CB  
2079 C CG  . LYS B 37  ? 0.0699 0.3445 0.1016 -0.0232 0.0766  -0.0225 37  LYS B CG  
2080 C CD  . LYS B 37  ? 0.0829 0.3715 0.1389 0.0030  0.0895  -0.0400 37  LYS B CD  
2081 C CE  . LYS B 37  ? 0.1245 0.4137 0.1730 0.0187  0.0786  -0.0397 37  LYS B CE  
2082 N NZ  . LYS B 37  ? 0.1468 0.4470 0.2020 0.0139  0.0853  -0.0629 37  LYS B NZ  
2083 N N   . THR B 38  ? 0.0645 0.3123 0.1277 0.0220  0.0793  -0.0330 38  THR B N   
2084 C CA  . THR B 38  ? 0.0662 0.3132 0.1205 0.0089  0.0808  -0.0268 38  THR B CA  
2085 C C   . THR B 38  ? 0.0788 0.3030 0.1166 0.0202  0.0823  -0.0378 38  THR B C   
2086 O O   . THR B 38  ? 0.0612 0.3067 0.1383 0.0205  0.0806  -0.0332 38  THR B O   
2087 C CB  . THR B 38  ? 0.0802 0.3238 0.1342 0.0500  0.0583  -0.0378 38  THR B CB  
2088 O OG1 . THR B 38  ? 0.0663 0.3383 0.1259 0.0315  0.0437  -0.0383 38  THR B OG1 
2089 C CG2 . THR B 38  ? 0.0799 0.3447 0.1619 0.0702  0.0396  -0.0421 38  THR B CG2 
2090 N N   . PRO B 39  ? 0.0981 0.3185 0.1565 0.0131  0.0807  -0.0281 39  PRO B N   
2091 C CA  . PRO B 39  ? 0.0762 0.3138 0.1799 0.0000  0.0673  -0.0231 39  PRO B CA  
2092 C C   . PRO B 39  ? 0.0486 0.3052 0.1730 -0.0032 0.0652  -0.0303 39  PRO B C   
2093 O O   . PRO B 39  ? 0.0868 0.3029 0.1809 0.0185  0.0467  -0.0239 39  PRO B O   
2094 C CB  . PRO B 39  ? 0.1281 0.3213 0.2288 0.0034  0.0555  -0.0171 39  PRO B CB  
2095 C CG  . PRO B 39  ? 0.1691 0.3349 0.2509 0.0075  0.0450  -0.0066 39  PRO B CG  
2096 C CD  . PRO B 39  ? 0.1449 0.3394 0.1984 0.0102  0.0808  -0.0042 39  PRO B CD  
2097 N N   . VAL B 40  ? 0.0470 0.3202 0.1587 0.0007  0.0603  -0.0287 40  VAL B N   
2098 C CA  . VAL B 40  ? 0.0779 0.3112 0.1351 0.0168  0.0404  -0.0519 40  VAL B CA  
2099 C C   . VAL B 40  ? 0.0482 0.3215 0.1278 0.0088  0.0604  -0.0349 40  VAL B C   
2100 O O   . VAL B 40  ? 0.0881 0.3229 0.1202 0.0063  0.0580  -0.0360 40  VAL B O   
2101 C CB  . VAL B 40  ? 0.1160 0.3314 0.1734 0.0252  0.0452  -0.0607 40  VAL B CB  
2102 C CG1 . VAL B 40  ? 0.1472 0.3360 0.2159 0.0161  0.0378  -0.0616 40  VAL B CG1 
2103 C CG2 . VAL B 40  ? 0.1275 0.3567 0.1815 0.0451  0.0377  -0.0588 40  VAL B CG2 
2104 N N   . GLY B 41  ? 0.0409 0.3290 0.1328 -0.0042 0.0656  -0.0327 41  GLY B N   
2105 C CA  . GLY B 41  ? 0.0601 0.3248 0.1222 0.0063  0.0604  -0.0389 41  GLY B CA  
2106 C C   . GLY B 41  ? 0.0480 0.3069 0.1127 0.0155  0.0638  -0.0270 41  GLY B C   
2107 O O   . GLY B 41  ? 0.0756 0.3082 0.1300 0.0186  0.0643  -0.0264 41  GLY B O   
2108 N N   . ASN B 42  ? 0.0615 0.3215 0.0968 -0.0006 0.0653  -0.0152 42  ASN B N   
2109 C CA  . ASN B 42  ? 0.0479 0.3219 0.1029 -0.0085 0.0602  -0.0061 42  ASN B CA  
2110 C C   . ASN B 42  ? 0.0596 0.3049 0.1017 -0.0016 0.0659  -0.0112 42  ASN B C   
2111 O O   . ASN B 42  ? 0.0751 0.3176 0.0969 0.0043  0.0519  -0.0150 42  ASN B O   
2112 C CB  . ASN B 42  ? 0.0515 0.3295 0.1116 -0.0048 0.0688  -0.0129 42  ASN B CB  
2113 C CG  . ASN B 42  ? 0.0610 0.3504 0.1185 0.0074  0.0690  -0.0300 42  ASN B CG  
2114 O OD1 . ASN B 42  ? 0.0536 0.4042 0.1435 0.0046  0.0726  -0.0297 42  ASN B OD1 
2115 N ND2 . ASN B 42  ? 0.1165 0.3653 0.1546 0.0325  0.0561  -0.0289 42  ASN B ND2 
2116 N N   . THR B 43  ? 0.0451 0.2909 0.1193 -0.0165 0.0656  -0.0047 43  THR B N   
2117 C CA  . THR B 43  ? 0.0532 0.2866 0.1018 -0.0066 0.0669  -0.0112 43  THR B CA  
2118 C C   . THR B 43  ? 0.0668 0.2710 0.0891 0.0094  0.0698  -0.0128 43  THR B C   
2119 O O   . THR B 43  ? 0.0704 0.2849 0.0933 0.0029  0.0721  -0.0149 43  THR B O   
2120 C CB  . THR B 43  ? 0.0639 0.2856 0.0979 0.0012  0.0724  -0.0109 43  THR B CB  
2121 O OG1 . THR B 43  ? 0.0837 0.3117 0.0895 -0.0074 0.0803  -0.0073 43  THR B OG1 
2122 C CG2 . THR B 43  ? 0.0565 0.2894 0.1114 0.0048  0.0716  -0.0102 43  THR B CG2 
2123 N N   . ALA B 44  ? 0.0724 0.2834 0.0800 0.0028  0.0686  -0.0232 44  ALA B N   
2124 C CA  . ALA B 44  ? 0.0567 0.2769 0.0801 0.0026  0.0606  -0.0129 44  ALA B CA  
2125 C C   . ALA B 44  ? 0.0614 0.2470 0.0893 -0.0068 0.0676  -0.0085 44  ALA B C   
2126 O O   . ALA B 44  ? 0.0623 0.2575 0.0854 -0.0003 0.0571  -0.0132 44  ALA B O   
2127 C CB  . ALA B 44  ? 0.0762 0.2919 0.0795 -0.0066 0.0715  -0.0045 44  ALA B CB  
2128 N N   . ALA B 45  ? 0.0565 0.2422 0.0951 0.0000  0.0663  -0.0161 45  ALA B N   
2129 C CA  . ALA B 45  ? 0.0541 0.2397 0.0980 -0.0007 0.0659  -0.0124 45  ALA B CA  
2130 C C   . ALA B 45  ? 0.0513 0.2513 0.1018 0.0053  0.0651  -0.0101 45  ALA B C   
2131 O O   . ALA B 45  ? 0.0656 0.2602 0.0946 0.0057  0.0720  -0.0064 45  ALA B O   
2132 C CB  . ALA B 45  ? 0.0508 0.2488 0.1143 -0.0013 0.0689  -0.0203 45  ALA B CB  
2133 N N   . ILE B 46  ? 0.0605 0.2426 0.0934 0.0087  0.0641  -0.0154 46  ILE B N   
2134 C CA  . ILE B 46  ? 0.0689 0.2541 0.0919 0.0014  0.0627  0.0038  46  ILE B CA  
2135 C C   . ILE B 46  ? 0.0725 0.2517 0.0878 -0.0032 0.0493  0.0049  46  ILE B C   
2136 O O   . ILE B 46  ? 0.0648 0.2687 0.1490 -0.0084 0.0384  0.0215  46  ILE B O   
2137 C CB  . ILE B 46  ? 0.1012 0.2850 0.0757 -0.0027 0.0575  0.0155  46  ILE B CB  
2138 C CG1 . ILE B 46  ? 0.1488 0.2995 0.1222 0.0123  0.0718  -0.0024 46  ILE B CG1 
2139 C CG2 . ILE B 46  ? 0.0843 0.3029 0.0957 0.0097  0.0566  0.0188  46  ILE B CG2 
2140 C CD1 . ILE B 46  ? 0.2473 0.3511 0.1259 0.0176  0.0737  -0.0024 46  ILE B CD1 
2141 N N   . SER B 47  ? 0.0615 0.2507 0.0827 -0.0199 0.0629  0.0107  47  SER B N   
2142 C CA  . SER B 47  ? 0.0682 0.2707 0.0921 -0.0108 0.0400  -0.0006 47  SER B CA  
2143 C C   . SER B 47  ? 0.0684 0.2621 0.0929 -0.0039 0.0497  0.0044  47  SER B C   
2144 O O   . SER B 47  ? 0.1085 0.2798 0.1155 -0.0102 0.0210  0.0009  47  SER B O   
2145 C CB  . SER B 47  ? 0.0900 0.3126 0.1267 -0.0057 0.0533  -0.0176 47  SER B CB  
2146 O OG  . SER B 47  ? 0.1008 0.3889 0.2441 -0.0246 0.0820  -0.0403 47  SER B OG  
2147 N N   . VAL B 48  ? 0.0808 0.2559 0.0846 -0.0080 0.0577  0.0073  48  VAL B N   
2148 C CA  . VAL B 48  ? 0.0930 0.2474 0.0827 -0.0007 0.0482  -0.0044 48  VAL B CA  
2149 C C   . VAL B 48  ? 0.0877 0.2616 0.0873 -0.0059 0.0457  0.0057  48  VAL B C   
2150 O O   . VAL B 48  ? 0.1054 0.2947 0.0922 -0.0387 0.0431  0.0156  48  VAL B O   
2151 C CB  . VAL B 48  ? 0.1041 0.2735 0.1070 0.0039  0.0589  -0.0147 48  VAL B CB  
2152 C CG1 . VAL B 48  ? 0.1154 0.2779 0.1243 -0.0064 0.0683  -0.0167 48  VAL B CG1 
2153 C CG2 . VAL B 48  ? 0.0926 0.2789 0.1123 0.0159  0.0590  -0.0197 48  VAL B CG2 
2154 N N   . TYR B 49  ? 0.1033 0.2573 0.0713 -0.0078 0.0491  -0.0055 49  TYR B N   
2155 C CA  . TYR B 49  ? 0.1007 0.2594 0.0888 -0.0018 0.0481  0.0003  49  TYR B CA  
2156 C C   . TYR B 49  ? 0.0879 0.2698 0.0792 0.0001  0.0481  -0.0103 49  TYR B C   
2157 O O   . TYR B 49  ? 0.0759 0.2809 0.0852 -0.0071 0.0542  -0.0128 49  TYR B O   
2158 C CB  . TYR B 49  ? 0.1395 0.2798 0.0993 0.0027  0.0513  0.0100  49  TYR B CB  
2159 C CG  . TYR B 49  ? 0.1863 0.2846 0.1357 0.0270  0.0275  0.0185  49  TYR B CG  
2160 C CD1 . TYR B 49  ? 0.2193 0.3087 0.1868 0.0346  0.0508  0.0218  49  TYR B CD1 
2161 C CD2 . TYR B 49  ? 0.2135 0.3116 0.1809 0.0253  0.0826  0.0115  49  TYR B CD2 
2162 C CE1 . TYR B 49  ? 0.2167 0.3291 0.2089 0.0517  0.0582  0.0114  49  TYR B CE1 
2163 C CE2 . TYR B 49  ? 0.2618 0.3167 0.2463 0.0455  0.0648  0.0285  49  TYR B CE2 
2164 C CZ  . TYR B 49  ? 0.2322 0.3299 0.2646 0.0675  0.0548  0.0094  49  TYR B CZ  
2165 O OH  . TYR B 49  ? 0.3277 0.3793 0.3298 0.1080  0.0812  -0.0201 49  TYR B OH  
2166 N N   . PRO B 50  ? 0.0611 0.2767 0.0929 0.0102  0.0609  -0.0184 50  PRO B N   
2167 C CA  . PRO B 50  ? 0.0755 0.2799 0.0858 0.0074  0.0602  -0.0279 50  PRO B CA  
2168 C C   . PRO B 50  ? 0.0821 0.2765 0.0779 0.0000  0.0633  -0.0130 50  PRO B C   
2169 O O   . PRO B 50  ? 0.0641 0.2793 0.0957 -0.0026 0.0706  -0.0171 50  PRO B O   
2170 C CB  . PRO B 50  ? 0.0885 0.2874 0.1064 -0.0002 0.0609  -0.0231 50  PRO B CB  
2171 C CG  . PRO B 50  ? 0.0625 0.2925 0.1234 0.0056  0.0609  -0.0285 50  PRO B CG  
2172 C CD  . PRO B 50  ? 0.0635 0.2843 0.0961 0.0140  0.0656  -0.0237 50  PRO B CD  
2173 N N   . ARG B 51  ? 0.0778 0.2879 0.0733 0.0001  0.0624  -0.0126 51  ARG B N   
2174 C CA  . ARG B 51  ? 0.0893 0.3132 0.0782 -0.0069 0.0658  -0.0255 51  ARG B CA  
2175 C C   . ARG B 51  ? 0.0929 0.3213 0.0692 -0.0029 0.0728  -0.0256 51  ARG B C   
2176 O O   . ARG B 51  ? 0.1021 0.3515 0.0630 -0.0031 0.0727  -0.0253 51  ARG B O   
2177 C CB  . ARG B 51  ? 0.1163 0.3260 0.0862 -0.0138 0.0649  -0.0077 51  ARG B CB  
2178 C CG  . ARG B 51  ? 0.1660 0.3544 0.1436 -0.0195 0.0516  0.0314  51  ARG B CG  
2179 C CD  . ARG B 51  ? 0.2716 0.4076 0.2389 0.0102  0.0124  0.0539  51  ARG B CD  
2180 N NE  . ARG B 51  ? 0.4136 0.4343 0.3434 0.0102  0.0246  0.0950  51  ARG B NE  
2181 C CZ  . ARG B 51  ? 0.5396 0.4860 0.3700 0.0432  0.0859  0.0927  51  ARG B CZ  
2182 N NH1 . ARG B 51  ? 0.5875 0.5155 0.4247 0.0445  0.0582  0.1134  51  ARG B NH1 
2183 N NH2 . ARG B 51  ? 0.6391 0.5088 0.4075 0.0452  0.1410  0.1093  51  ARG B NH2 
2184 N N   . SER B 52  ? 0.0837 0.2991 0.0691 -0.0153 0.0641  -0.0193 52  SER B N   
2185 C CA  . SER B 52  ? 0.0686 0.2851 0.0917 -0.0094 0.0716  -0.0005 52  SER B CA  
2186 C C   . SER B 52  ? 0.0648 0.2642 0.0856 -0.0141 0.0679  -0.0077 52  SER B C   
2187 O O   . SER B 52  ? 0.0653 0.2853 0.0879 -0.0182 0.0692  -0.0101 52  SER B O   
2188 C CB  . SER B 52  ? 0.0618 0.2898 0.1519 -0.0051 0.0768  0.0164  52  SER B CB  
2189 O OG  . SER B 52  ? 0.1201 0.2983 0.2132 0.0094  0.0388  0.0360  52  SER B OG  
2190 N N   . ILE B 53  ? 0.0664 0.2582 0.0908 -0.0168 0.0629  -0.0153 53  ILE B N   
2191 C CA  . ILE B 53  ? 0.0813 0.2517 0.0887 -0.0003 0.0681  -0.0169 53  ILE B CA  
2192 C C   . ILE B 53  ? 0.0822 0.2722 0.0815 0.0045  0.0573  -0.0330 53  ILE B C   
2193 O O   . ILE B 53  ? 0.0795 0.2894 0.0796 0.0126  0.0585  -0.0148 53  ILE B O   
2194 C CB  . ILE B 53  ? 0.0941 0.2456 0.1063 -0.0004 0.0693  -0.0244 53  ILE B CB  
2195 C CG1 . ILE B 53  ? 0.0909 0.2645 0.0983 0.0063  0.0747  -0.0192 53  ILE B CG1 
2196 C CG2 . ILE B 53  ? 0.1208 0.2354 0.1145 -0.0027 0.0693  -0.0159 53  ILE B CG2 
2197 C CD1 . ILE B 53  ? 0.1039 0.2803 0.1312 0.0126  0.0894  -0.0016 53  ILE B CD1 
2198 N N   . PRO B 54  ? 0.0849 0.3155 0.0789 -0.0053 0.0742  -0.0326 54  PRO B N   
2199 C CA  . PRO B 54  ? 0.0740 0.2990 0.1094 0.0020  0.0777  -0.0400 54  PRO B CA  
2200 C C   . PRO B 54  ? 0.0868 0.2887 0.0965 -0.0003 0.0761  -0.0265 54  PRO B C   
2201 O O   . PRO B 54  ? 0.0903 0.3197 0.0976 0.0125  0.0749  -0.0161 54  PRO B O   
2202 C CB  . PRO B 54  ? 0.0889 0.3274 0.0897 -0.0090 0.0817  -0.0373 54  PRO B CB  
2203 C CG  . PRO B 54  ? 0.0698 0.3278 0.1046 -0.0113 0.0755  -0.0376 54  PRO B CG  
2204 C CD  . PRO B 54  ? 0.0898 0.3235 0.0771 -0.0126 0.0753  -0.0417 54  PRO B CD  
2205 N N   . ILE B 55  ? 0.0858 0.2965 0.0850 -0.0040 0.0612  -0.0172 55  ILE B N   
2206 C CA  . ILE B 55  ? 0.0810 0.3071 0.1086 -0.0089 0.0634  -0.0080 55  ILE B CA  
2207 C C   . ILE B 55  ? 0.0647 0.2944 0.0970 -0.0113 0.0727  -0.0188 55  ILE B C   
2208 O O   . ILE B 55  ? 0.0692 0.3302 0.0863 -0.0115 0.0619  -0.0244 55  ILE B O   
2209 C CB  . ILE B 55  ? 0.1148 0.3319 0.1462 -0.0138 0.0539  0.0162  55  ILE B CB  
2210 C CG1 . ILE B 55  ? 0.1429 0.3763 0.2019 -0.0326 0.0681  0.0320  55  ILE B CG1 
2211 C CG2 . ILE B 55  ? 0.1658 0.3386 0.1300 0.0008  0.0417  0.0094  55  ILE B CG2 
2212 C CD1 . ILE B 55  ? 0.2175 0.4224 0.2757 0.0052  0.0835  0.0261  55  ILE B CD1 
2213 N N   . ALA B 56  ? 0.0666 0.2909 0.0793 -0.0015 0.0662  -0.0086 56  ALA B N   
2214 C CA  . ALA B 56  ? 0.0773 0.2774 0.0808 -0.0022 0.0702  -0.0122 56  ALA B CA  
2215 C C   . ALA B 56  ? 0.0717 0.2863 0.0744 0.0000  0.0658  -0.0229 56  ALA B C   
2216 O O   . ALA B 56  ? 0.0628 0.3007 0.0877 -0.0047 0.0675  -0.0185 56  ALA B O   
2217 C CB  . ALA B 56  ? 0.0704 0.2787 0.0883 0.0018  0.0677  -0.0108 56  ALA B CB  
2218 N N   . ARG B 57  ? 0.0830 0.2909 0.0767 0.0141  0.0711  -0.0221 57  ARG B N   
2219 C CA  . ARG B 57  ? 0.0897 0.2966 0.0866 0.0264  0.0780  -0.0211 57  ARG B CA  
2220 C C   . ARG B 57  ? 0.0751 0.3112 0.0872 0.0205  0.0702  -0.0313 57  ARG B C   
2221 O O   . ARG B 57  ? 0.0788 0.3515 0.0854 0.0244  0.0713  -0.0188 57  ARG B O   
2222 C CB  . ARG B 57  ? 0.0979 0.3039 0.1110 0.0185  0.0956  -0.0101 57  ARG B CB  
2223 C CG  . ARG B 57  ? 0.0860 0.3162 0.1640 0.0310  0.0877  -0.0166 57  ARG B CG  
2224 C CD  . ARG B 57  ? 0.1194 0.3491 0.1824 0.0096  0.0612  0.0103  57  ARG B CD  
2225 N NE  . ARG B 57  ? 0.1094 0.3567 0.1431 0.0264  0.0669  -0.0005 57  ARG B NE  
2226 C CZ  . ARG B 57  ? 0.1181 0.3594 0.1292 0.0097  0.0532  0.0008  57  ARG B CZ  
2227 N NH1 . ARG B 57  ? 0.1548 0.3798 0.1713 0.0103  0.0197  0.0017  57  ARG B NH1 
2228 N NH2 . ARG B 57  ? 0.1189 0.3910 0.1221 -0.0003 0.0631  -0.0156 57  ARG B NH2 
2229 N N   . LYS B 58  ? 0.0714 0.3216 0.0865 0.0075  0.0708  -0.0235 58  LYS B N   
2230 C CA  . LYS B 58  ? 0.0893 0.3327 0.1021 0.0004  0.0882  -0.0243 58  LYS B CA  
2231 C C   . LYS B 58  ? 0.0747 0.3350 0.1041 0.0057  0.0813  -0.0132 58  LYS B C   
2232 O O   . LYS B 58  ? 0.0662 0.3687 0.1385 0.0032  0.0781  -0.0321 58  LYS B O   
2233 C CB  . LYS B 58  ? 0.0825 0.3518 0.1034 -0.0089 0.0853  -0.0332 58  LYS B CB  
2234 C CG  . LYS B 58  ? 0.0886 0.3935 0.1311 0.0034  0.0991  -0.0419 58  LYS B CG  
2235 C CD  . LYS B 58  ? 0.1318 0.4342 0.1278 0.0055  0.1019  -0.0518 58  LYS B CD  
2236 C CE  . LYS B 58  ? 0.1611 0.4671 0.1390 0.0087  0.1169  -0.0661 58  LYS B CE  
2237 N NZ  . LYS B 58  ? 0.2353 0.5187 0.1629 -0.0124 0.0960  -0.0527 58  LYS B NZ  
2238 N N   . THR B 59  ? 0.0822 0.3130 0.0945 0.0067  0.0811  -0.0140 59  THR B N   
2239 C CA  . THR B 59  ? 0.0774 0.3228 0.1031 -0.0051 0.0828  -0.0121 59  THR B CA  
2240 C C   . THR B 59  ? 0.0650 0.3329 0.1057 0.0014  0.0759  -0.0173 59  THR B C   
2241 O O   . THR B 59  ? 0.0566 0.3558 0.1393 0.0076  0.0770  -0.0341 59  THR B O   
2242 C CB  . THR B 59  ? 0.0902 0.3367 0.0931 -0.0109 0.0715  0.0017  59  THR B CB  
2243 O OG1 . THR B 59  ? 0.1269 0.3353 0.1013 -0.0132 0.0521  0.0175  59  THR B OG1 
2244 C CG2 . THR B 59  ? 0.1068 0.3377 0.1165 -0.0071 0.0704  -0.0180 59  THR B CG2 
2245 N N   . LEU B 60  ? 0.0711 0.3221 0.0910 0.0003  0.0738  -0.0138 60  LEU B N   
2246 C CA  . LEU B 60  ? 0.0708 0.3095 0.1093 0.0090  0.0686  -0.0177 60  LEU B CA  
2247 C C   . LEU B 60  ? 0.0739 0.3346 0.1175 0.0266  0.0615  -0.0262 60  LEU B C   
2248 O O   . LEU B 60  ? 0.0642 0.3796 0.1339 0.0223  0.0580  -0.0249 60  LEU B O   
2249 C CB  . LEU B 60  ? 0.0731 0.2963 0.1013 0.0078  0.0697  -0.0248 60  LEU B CB  
2250 C CG  . LEU B 60  ? 0.0662 0.3065 0.1086 0.0085  0.0706  -0.0105 60  LEU B CG  
2251 C CD1 . LEU B 60  ? 0.0760 0.3342 0.1279 -0.0008 0.0875  -0.0250 60  LEU B CD1 
2252 C CD2 . LEU B 60  ? 0.0719 0.3091 0.1030 0.0159  0.0779  -0.0158 60  LEU B CD2 
2253 N N   . LYS B 61  ? 0.0793 0.3335 0.1346 0.0427  0.0486  -0.0391 61  LYS B N   
2254 C CA  . LYS B 61  ? 0.0833 0.3528 0.1302 0.0453  0.0706  -0.0373 61  LYS B CA  
2255 C C   . LYS B 61  ? 0.0757 0.3927 0.1519 0.0409  0.0677  -0.0367 61  LYS B C   
2256 O O   . LYS B 61  ? 0.1022 0.4311 0.1651 0.0670  0.0540  -0.0212 61  LYS B O   
2257 C CB  . LYS B 61  ? 0.1286 0.3618 0.1877 0.0499  0.0792  -0.0379 61  LYS B CB  
2258 C CG  . LYS B 61  ? 0.1927 0.4003 0.2627 0.0373  0.0778  -0.0177 61  LYS B CG  
2259 C CD  . LYS B 61  ? 0.2905 0.4606 0.3115 0.0233  0.0643  -0.0366 61  LYS B CD  
2260 C CE  . LYS B 61  ? 0.3464 0.5048 0.4177 0.0245  0.0484  -0.0335 61  LYS B CE  
2261 N NZ  . LYS B 61  ? 0.4296 0.5444 0.4494 0.0245  0.0235  -0.0480 61  LYS B NZ  
2262 N N   . GLU B 62  ? 0.0592 0.4075 0.1650 0.0339  0.0730  -0.0480 62  GLU B N   
2263 C CA  . GLU B 62  ? 0.0692 0.4369 0.1745 0.0305  0.0897  -0.0686 62  GLU B CA  
2264 C C   . GLU B 62  ? 0.0677 0.4249 0.1470 0.0185  0.0852  -0.0706 62  GLU B C   
2265 O O   . GLU B 62  ? 0.0654 0.5072 0.1824 0.0329  0.0856  -0.0756 62  GLU B O   
2266 C CB  . GLU B 62  ? 0.1184 0.4903 0.1875 0.0035  0.1161  -0.0504 62  GLU B CB  
2267 C CG  . GLU B 62  ? 0.2145 0.5238 0.2443 -0.0085 0.1117  -0.0613 62  GLU B CG  
2268 C CD  . GLU B 62  ? 0.3428 0.5799 0.2740 -0.0166 0.0864  -0.0510 62  GLU B CD  
2269 O OE1 . GLU B 62  ? 0.4989 0.6128 0.3562 0.0303  0.1151  0.0004  62  GLU B OE1 
2270 O OE2 . GLU B 62  ? 0.3582 0.6494 0.3152 0.0020  0.0826  -0.1128 62  GLU B OE2 
2271 N N   . GLN B 63  ? 0.0699 0.4006 0.1428 0.0086  0.0892  -0.0544 63  GLN B N   
2272 C CA  . GLN B 63  ? 0.0626 0.4034 0.1556 -0.0074 0.0913  -0.0337 63  GLN B CA  
2273 C C   . GLN B 63  ? 0.0548 0.4119 0.1596 0.0015  0.0844  -0.0488 63  GLN B C   
2274 O O   . GLN B 63  ? 0.0817 0.4567 0.1976 -0.0119 0.0308  -0.0543 63  GLN B O   
2275 C CB  . GLN B 63  ? 0.0772 0.3873 0.1642 -0.0223 0.0837  -0.0189 63  GLN B CB  
2276 C CG  . GLN B 63  ? 0.0811 0.3731 0.1586 -0.0157 0.0841  -0.0039 63  GLN B CG  
2277 C CD  . GLN B 63  ? 0.0978 0.3637 0.1431 -0.0056 0.1114  0.0138  63  GLN B CD  
2278 O OE1 . GLN B 63  ? 0.1981 0.3953 0.1559 0.0255  0.1346  0.0160  63  GLN B OE1 
2279 N NE2 . GLN B 63  ? 0.0804 0.3305 0.1253 0.0044  0.0938  -0.0026 63  GLN B NE2 
2280 N N   . GLY B 64  ? 0.0716 0.4128 0.1649 0.0223  0.0618  -0.0499 64  GLY B N   
2281 C CA  . GLY B 64  ? 0.0748 0.4229 0.1516 0.0339  0.0528  -0.0467 64  GLY B CA  
2282 C C   . GLY B 64  ? 0.0667 0.4233 0.1411 0.0176  0.0514  -0.0296 64  GLY B C   
2283 O O   . GLY B 64  ? 0.0655 0.4937 0.1478 0.0240  0.0449  -0.0277 64  GLY B O   
2284 N N   . THR B 65  ? 0.0701 0.3883 0.1278 0.0143  0.0549  -0.0202 65  THR B N   
2285 C CA  . THR B 65  ? 0.0893 0.3421 0.1292 0.0206  0.0625  -0.0168 65  THR B CA  
2286 C C   . THR B 65  ? 0.0944 0.3318 0.1344 0.0329  0.0507  -0.0049 65  THR B C   
2287 O O   . THR B 65  ? 0.0988 0.3098 0.1434 0.0349  0.0404  -0.0062 65  THR B O   
2288 C CB  . THR B 65  ? 0.0904 0.3441 0.1274 0.0083  0.0689  -0.0213 65  THR B CB  
2289 O OG1 . THR B 65  ? 0.1091 0.3365 0.1238 0.0034  0.0661  -0.0028 65  THR B OG1 
2290 C CG2 . THR B 65  ? 0.1004 0.3619 0.1423 -0.0031 0.0773  -0.0465 65  THR B CG2 
2291 N N   . PRO B 66  ? 0.0866 0.3294 0.2117 0.0335  0.0402  -0.0116 66  PRO B N   
2292 C CA  . PRO B 66  ? 0.0972 0.3455 0.2220 0.0299  0.0403  -0.0113 66  PRO B CA  
2293 C C   . PRO B 66  ? 0.1139 0.3476 0.2391 0.0208  0.0468  -0.0054 66  PRO B C   
2294 O O   . PRO B 66  ? 0.1242 0.3857 0.2871 -0.0108 0.0106  -0.0105 66  PRO B O   
2295 C CB  . PRO B 66  ? 0.1669 0.3537 0.2883 0.0332  0.0421  -0.0236 66  PRO B CB  
2296 C CG  . PRO B 66  ? 0.1389 0.3426 0.2669 0.0549  0.0533  -0.0230 66  PRO B CG  
2297 C CD  . PRO B 66  ? 0.1173 0.3533 0.2518 0.0676  0.0624  -0.0136 66  PRO B CD  
2298 N N   . GLU B 67  ? 0.1284 0.3594 0.2128 0.0174  0.0472  0.0236  67  GLU B N   
2299 C CA  . GLU B 67  ? 0.1306 0.3865 0.2267 0.0130  0.0693  0.0396  67  GLU B CA  
2300 C C   . GLU B 67  ? 0.0889 0.3521 0.1540 -0.0019 0.0717  0.0524  67  GLU B C   
2301 O O   . GLU B 67  ? 0.1124 0.4011 0.1628 0.0099  0.0899  0.0609  67  GLU B O   
2302 C CB  . GLU B 67  ? 0.2025 0.4794 0.2369 -0.0042 0.0473  0.0474  67  GLU B CB  
2303 C CG  . GLU B 67  ? 0.2811 0.5705 0.2723 -0.0190 0.0005  0.0361  67  GLU B CG  
2304 C CD  . GLU B 67  ? 0.3559 0.6477 0.2909 -0.0199 0.0102  0.0316  67  GLU B CD  
2305 O OE1 . GLU B 67  ? 0.2675 0.6479 0.1991 -0.1276 0.0584  0.0416  67  GLU B OE1 
2306 O OE2 . GLU B 67  ? 0.3798 0.7830 0.5306 -0.0196 -0.0389 -0.0260 67  GLU B OE2 
2307 N N   . ILE B 68  ? 0.0687 0.3152 0.1144 0.0053  0.0408  0.0261  68  ILE B N   
2308 C CA  . ILE B 68  ? 0.0695 0.2951 0.1016 0.0010  0.0468  0.0018  68  ILE B CA  
2309 C C   . ILE B 68  ? 0.0647 0.3072 0.1002 0.0036  0.0518  -0.0103 68  ILE B C   
2310 O O   . ILE B 68  ? 0.0721 0.3404 0.0984 -0.0182 0.0469  -0.0174 68  ILE B O   
2311 C CB  . ILE B 68  ? 0.0695 0.2842 0.1141 0.0031  0.0372  -0.0132 68  ILE B CB  
2312 C CG1 . ILE B 68  ? 0.0450 0.3039 0.1069 -0.0017 0.0592  -0.0162 68  ILE B CG1 
2313 C CG2 . ILE B 68  ? 0.0693 0.2959 0.1191 0.0131  0.0463  -0.0047 68  ILE B CG2 
2314 C CD1 . ILE B 68  ? 0.0641 0.3041 0.1279 -0.0120 0.0505  -0.0161 68  ILE B CD1 
2315 N N   . ARG B 69  ? 0.0706 0.2817 0.0810 0.0093  0.0476  -0.0199 69  ARG B N   
2316 C CA  . ARG B 69  ? 0.0831 0.2721 0.0795 0.0138  0.0491  -0.0158 69  ARG B CA  
2317 C C   . ARG B 69  ? 0.0621 0.2512 0.0844 0.0091  0.0630  -0.0167 69  ARG B C   
2318 O O   . ARG B 69  ? 0.0887 0.2429 0.0979 0.0079  0.0377  -0.0131 69  ARG B O   
2319 C CB  . ARG B 69  ? 0.0983 0.3013 0.0905 -0.0026 0.0607  -0.0050 69  ARG B CB  
2320 C CG  . ARG B 69  ? 0.1109 0.3547 0.1257 -0.0077 0.0518  0.0245  69  ARG B CG  
2321 C CD  . ARG B 69  ? 0.1787 0.4353 0.1647 0.0117  0.0521  0.0014  69  ARG B CD  
2322 N NE  . ARG B 69  ? 0.2895 0.4796 0.1770 0.0050  0.0498  0.0207  69  ARG B NE  
2323 C CZ  . ARG B 69  ? 0.3312 0.4904 0.2135 0.0123  -0.0108 0.0216  69  ARG B CZ  
2324 N NH1 . ARG B 69  ? 0.3908 0.4656 0.2551 -0.0202 -0.0488 0.0262  69  ARG B NH1 
2325 N NH2 . ARG B 69  ? 0.4321 0.5012 0.2269 0.0335  -0.0162 0.0409  69  ARG B NH2 
2326 N N   . ILE B 70  ? 0.0451 0.2362 0.1101 0.0056  0.0534  -0.0184 70  ILE B N   
2327 C CA  . ILE B 70  ? 0.0452 0.2465 0.0905 0.0004  0.0568  -0.0168 70  ILE B CA  
2328 C C   . ILE B 70  ? 0.0405 0.2422 0.0930 -0.0056 0.0518  -0.0071 70  ILE B C   
2329 O O   . ILE B 70  ? 0.0652 0.2437 0.1011 0.0004  0.0521  -0.0157 70  ILE B O   
2330 C CB  . ILE B 70  ? 0.0616 0.2679 0.0968 0.0059  0.0587  -0.0224 70  ILE B CB  
2331 C CG1 . ILE B 70  ? 0.0728 0.2931 0.0884 0.0022  0.0732  -0.0177 70  ILE B CG1 
2332 C CG2 . ILE B 70  ? 0.0835 0.2867 0.0944 0.0102  0.0502  -0.0206 70  ILE B CG2 
2333 C CD1 . ILE B 70  ? 0.0970 0.3235 0.0870 0.0151  0.0667  -0.0270 70  ILE B CD1 
2334 N N   . ALA B 71  ? 0.0467 0.2443 0.0779 -0.0101 0.0536  -0.0025 71  ALA B N   
2335 C CA  . ALA B 71  ? 0.0496 0.2466 0.0908 -0.0059 0.0603  0.0023  71  ALA B CA  
2336 C C   . ALA B 71  ? 0.0512 0.2449 0.1070 -0.0111 0.0631  0.0089  71  ALA B C   
2337 O O   . ALA B 71  ? 0.0633 0.2595 0.0994 -0.0116 0.0608  0.0262  71  ALA B O   
2338 C CB  . ALA B 71  ? 0.0613 0.2534 0.1036 0.0005  0.0608  0.0002  71  ALA B CB  
2339 N N   . THR B 72  ? 0.0564 0.2694 0.1073 -0.0027 0.0704  0.0188  72  THR B N   
2340 C CA  . THR B 72  ? 0.0616 0.2620 0.0982 0.0016  0.0712  0.0073  72  THR B CA  
2341 C C   . THR B 72  ? 0.0630 0.2782 0.0846 0.0146  0.0665  0.0114  72  THR B C   
2342 O O   . THR B 72  ? 0.0718 0.3160 0.0842 0.0188  0.0714  0.0219  72  THR B O   
2343 C CB  . THR B 72  ? 0.0545 0.2721 0.1132 0.0165  0.0712  0.0031  72  THR B CB  
2344 O OG1 . THR B 72  ? 0.0629 0.2875 0.0945 0.0006  0.0706  0.0035  72  THR B OG1 
2345 C CG2 . THR B 72  ? 0.0767 0.2702 0.1129 0.0153  0.0860  -0.0010 72  THR B CG2 
2346 N N   . VAL B 73  ? 0.0532 0.2717 0.0874 0.0063  0.0616  0.0127  73  VAL B N   
2347 C CA  . VAL B 73  ? 0.0528 0.2683 0.0780 0.0051  0.0577  0.0098  73  VAL B CA  
2348 C C   . VAL B 73  ? 0.0628 0.2668 0.0671 0.0035  0.0586  0.0013  73  VAL B C   
2349 O O   . VAL B 73  ? 0.0654 0.2992 0.0840 0.0070  0.0672  -0.0106 73  VAL B O   
2350 C CB  . VAL B 73  ? 0.0597 0.2730 0.0969 0.0014  0.0693  0.0147  73  VAL B CB  
2351 C CG1 . VAL B 73  ? 0.0624 0.2804 0.1241 -0.0111 0.0721  0.0200  73  VAL B CG1 
2352 C CG2 . VAL B 73  ? 0.0547 0.2671 0.1107 -0.0080 0.0638  0.0322  73  VAL B CG2 
2353 N N   . THR B 74  ? 0.0738 0.2518 0.0561 -0.0049 0.0579  0.0001  74  THR B N   
2354 C CA  . THR B 74  ? 0.0721 0.2526 0.0544 0.0067  0.0558  -0.0083 74  THR B CA  
2355 C C   . THR B 74  ? 0.0620 0.2439 0.0782 0.0014  0.0508  -0.0174 74  THR B C   
2356 O O   . THR B 74  ? 0.0624 0.2706 0.0704 -0.0139 0.0598  -0.0215 74  THR B O   
2357 C CB  . THR B 74  ? 0.0801 0.2632 0.0698 0.0127  0.0584  -0.0116 74  THR B CB  
2358 O OG1 . THR B 74  ? 0.0700 0.2650 0.0834 0.0019  0.0663  0.0086  74  THR B OG1 
2359 C CG2 . THR B 74  ? 0.0860 0.2587 0.0889 0.0147  0.0681  -0.0155 74  THR B CG2 
2360 N N   . ASN B 75  ? 0.0622 0.2424 0.0616 0.0023  0.0546  -0.0188 75  ASN B N   
2361 C CA  . ASN B 75  ? 0.0588 0.2460 0.0656 0.0027  0.0556  -0.0056 75  ASN B CA  
2362 C C   . ASN B 75  ? 0.0671 0.2449 0.0687 0.0079  0.0601  -0.0103 75  ASN B C   
2363 O O   . ASN B 75  ? 0.0582 0.2634 0.0881 0.0049  0.0645  -0.0144 75  ASN B O   
2364 C CB  . ASN B 75  ? 0.0564 0.2593 0.0644 -0.0043 0.0510  -0.0019 75  ASN B CB  
2365 C CG  . ASN B 75  ? 0.0572 0.2636 0.0624 0.0040  0.0532  -0.0052 75  ASN B CG  
2366 O OD1 . ASN B 75  ? 0.0478 0.2916 0.0835 -0.0040 0.0566  -0.0112 75  ASN B OD1 
2367 N ND2 . ASN B 75  ? 0.0568 0.2680 0.0608 0.0080  0.0519  -0.0087 75  ASN B ND2 
2368 N N   . PHE B 76  ? 0.0723 0.2376 0.0878 0.0024  0.0652  0.0056  76  PHE B N   
2369 C CA  . PHE B 76  ? 0.0761 0.2517 0.0840 0.0088  0.0648  0.0084  76  PHE B CA  
2370 C C   . PHE B 76  ? 0.0878 0.2647 0.0864 -0.0013 0.0744  0.0223  76  PHE B C   
2371 O O   . PHE B 76  ? 0.1114 0.3077 0.0852 0.0119  0.0728  0.0181  76  PHE B O   
2372 C CB  . PHE B 76  ? 0.0742 0.2542 0.0989 0.0106  0.0661  -0.0039 76  PHE B CB  
2373 C CG  . PHE B 76  ? 0.0692 0.2674 0.1189 -0.0030 0.0841  -0.0072 76  PHE B CG  
2374 C CD1 . PHE B 76  ? 0.0742 0.2642 0.1449 -0.0034 0.0870  0.0043  76  PHE B CD1 
2375 C CD2 . PHE B 76  ? 0.0656 0.2711 0.1313 -0.0002 0.0852  -0.0254 76  PHE B CD2 
2376 C CE1 . PHE B 76  ? 0.0753 0.2556 0.1567 -0.0142 0.0999  0.0169  76  PHE B CE1 
2377 C CE2 . PHE B 76  ? 0.0977 0.2705 0.1575 0.0041  0.0920  -0.0302 76  PHE B CE2 
2378 C CZ  . PHE B 76  ? 0.0712 0.2611 0.1918 -0.0171 0.0810  -0.0120 76  PHE B CZ  
2379 N N   . PRO B 77  ? 0.0916 0.2673 0.1067 0.0006  0.0799  0.0244  77  PRO B N   
2380 C CA  . PRO B 77  ? 0.0911 0.2737 0.1193 0.0086  0.0741  0.0119  77  PRO B CA  
2381 C C   . PRO B 77  ? 0.0774 0.2645 0.1099 0.0133  0.0564  -0.0001 77  PRO B C   
2382 O O   . PRO B 77  ? 0.1019 0.2782 0.1267 0.0216  0.0297  -0.0214 77  PRO B O   
2383 C CB  . PRO B 77  ? 0.0902 0.2866 0.1670 0.0043  0.0682  0.0139  77  PRO B CB  
2384 C CG  . PRO B 77  ? 0.1136 0.2882 0.1572 -0.0100 0.0899  0.0387  77  PRO B CG  
2385 C CD  . PRO B 77  ? 0.1168 0.2870 0.1419 -0.0085 0.0761  0.0415  77  PRO B CD  
2386 N N   . HIS B 78  C 0.0730 0.2681 0.0878 0.0215  0.0719  -0.0089 78  HIS B N   
2387 C CA  . HIS B 78  C 0.0712 0.2763 0.1095 0.0253  0.0606  0.0000  78  HIS B CA  
2388 C C   . HIS B 78  C 0.0737 0.2678 0.1053 0.0221  0.0517  -0.0079 78  HIS B C   
2389 O O   . HIS B 78  C 0.0687 0.2994 0.1172 0.0285  0.0546  -0.0097 78  HIS B O   
2390 C CB  . HIS B 78  C 0.1036 0.3020 0.0911 0.0102  0.0560  0.0151  78  HIS B CB  
2391 C CG  . HIS B 78  C 0.0948 0.3149 0.1027 0.0188  0.0741  0.0051  78  HIS B CG  
2392 N ND1 . HIS B 78  C 0.0966 0.3122 0.0918 0.0151  0.0595  0.0082  78  HIS B ND1 
2393 C CD2 . HIS B 78  C 0.1266 0.3263 0.1030 0.0252  0.0911  0.0227  78  HIS B CD2 
2394 C CE1 . HIS B 78  C 0.1320 0.2959 0.1352 0.0065  0.0590  0.0045  78  HIS B CE1 
2395 N NE2 . HIS B 78  C 0.1375 0.3229 0.1300 0.0165  0.0672  0.0231  78  HIS B NE2 
2396 N N   . GLY B 79  ? 0.0577 0.2718 0.0724 0.0100  0.0578  -0.0055 79  GLY B N   
2397 C CA  . GLY B 79  ? 0.0545 0.2788 0.0710 -0.0019 0.0558  -0.0064 79  GLY B CA  
2398 C C   . GLY B 79  ? 0.0511 0.2809 0.0662 -0.0088 0.0516  -0.0182 79  GLY B C   
2399 O O   . GLY B 79  ? 0.0535 0.2881 0.0882 0.0015  0.0620  -0.0081 79  GLY B O   
2400 N N   . ASN B 80  ? 0.0467 0.2709 0.0754 -0.0077 0.0522  -0.0306 80  ASN B N   
2401 C CA  . ASN B 80  ? 0.0464 0.2807 0.0894 -0.0047 0.0520  -0.0340 80  ASN B CA  
2402 C C   . ASN B 80  ? 0.0642 0.2905 0.0786 -0.0032 0.0636  -0.0289 80  ASN B C   
2403 O O   . ASN B 80  ? 0.0625 0.3069 0.1059 0.0044  0.0744  -0.0129 80  ASN B O   
2404 C CB  . ASN B 80  ? 0.0768 0.2910 0.0970 0.0018  0.0298  -0.0280 80  ASN B CB  
2405 C CG  . ASN B 80  ? 0.1041 0.3037 0.1153 0.0087  0.0353  -0.0187 80  ASN B CG  
2406 O OD1 . ASN B 80  ? 0.1319 0.3066 0.1536 0.0166  0.0419  -0.0131 80  ASN B OD1 
2407 N ND2 . ASN B 80  ? 0.1708 0.3277 0.1099 0.0192  0.0352  -0.0092 80  ASN B ND2 
2408 N N   . ASP B 81  ? 0.0584 0.3158 0.1051 -0.0085 0.0541  -0.0233 81  ASP B N   
2409 C CA  . ASP B 81  ? 0.0524 0.3246 0.1154 -0.0112 0.0708  -0.0246 81  ASP B CA  
2410 C C   . ASP B 81  ? 0.0861 0.3375 0.1047 -0.0103 0.0744  -0.0319 81  ASP B C   
2411 O O   . ASP B 81  ? 0.1298 0.3390 0.1449 -0.0194 0.0822  -0.0296 81  ASP B O   
2412 C CB  . ASP B 81  ? 0.0769 0.3661 0.1198 -0.0143 0.0893  -0.0295 81  ASP B CB  
2413 C CG  . ASP B 81  ? 0.0851 0.4205 0.1655 -0.0125 0.0929  -0.0216 81  ASP B CG  
2414 O OD1 . ASP B 81  ? 0.1250 0.5057 0.1880 0.0058  0.0482  0.0015  81  ASP B OD1 
2415 O OD2 . ASP B 81  ? 0.1128 0.5276 0.2899 0.0234  0.1312  -0.0504 81  ASP B OD2 
2416 N N   . ASP B 82  ? 0.0479 0.3100 0.1168 -0.0173 0.0677  -0.0230 82  ASP B N   
2417 C CA  . ASP B 82  ? 0.0665 0.3124 0.1143 -0.0193 0.0574  -0.0136 82  ASP B CA  
2418 C C   . ASP B 82  ? 0.0492 0.3021 0.0986 -0.0199 0.0627  -0.0158 82  ASP B C   
2419 O O   . ASP B 82  ? 0.0483 0.3053 0.1200 -0.0120 0.0690  -0.0097 82  ASP B O   
2420 C CB  . ASP B 82  ? 0.0695 0.3241 0.1098 -0.0094 0.0527  -0.0142 82  ASP B CB  
2421 C CG  . ASP B 82  ? 0.0813 0.3426 0.1377 -0.0137 0.0469  -0.0151 82  ASP B CG  
2422 O OD1 . ASP B 82  ? 0.1163 0.3486 0.1343 -0.0147 0.0554  -0.0288 82  ASP B OD1 
2423 O OD2 . ASP B 82  ? 0.1782 0.4224 0.1757 0.0160  -0.0088 -0.0289 82  ASP B OD2 
2424 N N   . ILE B 83  ? 0.0620 0.2878 0.1118 -0.0150 0.0716  -0.0176 83  ILE B N   
2425 C CA  . ILE B 83  ? 0.0773 0.2897 0.1094 -0.0268 0.0631  -0.0089 83  ILE B CA  
2426 C C   . ILE B 83  ? 0.0530 0.2939 0.1110 -0.0264 0.0671  -0.0113 83  ILE B C   
2427 O O   . ILE B 83  ? 0.0568 0.3195 0.1275 -0.0099 0.0647  -0.0061 83  ILE B O   
2428 C CB  . ILE B 83  ? 0.0964 0.3000 0.1174 -0.0194 0.0748  0.0022  83  ILE B CB  
2429 C CG1 . ILE B 83  ? 0.1304 0.3152 0.1386 -0.0115 0.0716  -0.0140 83  ILE B CG1 
2430 C CG2 . ILE B 83  ? 0.1294 0.3036 0.1307 -0.0213 0.0795  0.0227  83  ILE B CG2 
2431 C CD1 . ILE B 83  ? 0.1780 0.3429 0.1573 -0.0032 0.1007  0.0117  83  ILE B CD1 
2432 N N   . GLU B 84  ? 0.0707 0.3063 0.1140 -0.0194 0.0781  -0.0253 84  GLU B N   
2433 C CA  . GLU B 84  ? 0.1150 0.3158 0.1199 -0.0204 0.0807  -0.0363 84  GLU B CA  
2434 C C   . GLU B 84  ? 0.0718 0.3138 0.1128 -0.0092 0.0749  -0.0370 84  GLU B C   
2435 O O   . GLU B 84  ? 0.0862 0.3240 0.1430 0.0034  0.0828  -0.0431 84  GLU B O   
2436 C CB  . GLU B 84  ? 0.1344 0.3594 0.1392 -0.0439 0.0910  -0.0656 84  GLU B CB  
2437 C CG  . GLU B 84  ? 0.2063 0.4001 0.2437 -0.0818 0.0899  -0.0638 84  GLU B CG  
2438 C CD  . GLU B 84  ? 0.2915 0.4730 0.3851 -0.0606 0.1312  -0.0406 84  GLU B CD  
2439 O OE1 . GLU B 84  ? 0.3068 0.5981 0.5418 -0.0576 0.1219  -0.1014 84  GLU B OE1 
2440 O OE2 . GLU B 84  ? 0.4703 0.5794 0.5171 -0.1170 0.1360  0.0314  84  GLU B OE2 
2441 N N   . ILE B 85  ? 0.0703 0.3137 0.0928 -0.0088 0.0739  -0.0277 85  ILE B N   
2442 C CA  . ILE B 85  ? 0.0674 0.3015 0.0863 -0.0124 0.0600  -0.0130 85  ILE B CA  
2443 C C   . ILE B 85  ? 0.0578 0.2935 0.0774 0.0018  0.0602  -0.0102 85  ILE B C   
2444 O O   . ILE B 85  ? 0.0560 0.2910 0.0941 0.0014  0.0634  -0.0076 85  ILE B O   
2445 C CB  . ILE B 85  ? 0.0883 0.3227 0.0945 0.0021  0.0615  -0.0038 85  ILE B CB  
2446 C CG1 . ILE B 85  ? 0.0690 0.3500 0.1005 0.0085  0.0726  -0.0071 85  ILE B CG1 
2447 C CG2 . ILE B 85  ? 0.0931 0.3225 0.1168 0.0058  0.0487  0.0069  85  ILE B CG2 
2448 C CD1 . ILE B 85  ? 0.0999 0.3721 0.0932 0.0073  0.0731  0.0040  85  ILE B CD1 
2449 N N   . ALA B 86  ? 0.0581 0.2797 0.0854 0.0057  0.0633  -0.0146 86  ALA B N   
2450 C CA  . ALA B 86  ? 0.0752 0.2673 0.0765 -0.0079 0.0647  -0.0115 86  ALA B CA  
2451 C C   . ALA B 86  ? 0.0601 0.2620 0.0748 -0.0176 0.0606  -0.0169 86  ALA B C   
2452 O O   . ALA B 86  ? 0.0509 0.2817 0.0896 -0.0205 0.0604  -0.0083 86  ALA B O   
2453 C CB  . ALA B 86  ? 0.0840 0.2847 0.0803 0.0058  0.0724  -0.0102 86  ALA B CB  
2454 N N   . LEU B 87  ? 0.0863 0.2583 0.0704 -0.0149 0.0658  -0.0070 87  LEU B N   
2455 C CA  . LEU B 87  ? 0.1033 0.2496 0.0626 -0.0171 0.0739  -0.0129 87  LEU B CA  
2456 C C   . LEU B 87  ? 0.0847 0.2657 0.0654 -0.0020 0.0678  -0.0112 87  LEU B C   
2457 O O   . LEU B 87  ? 0.0707 0.2799 0.0741 -0.0048 0.0636  -0.0076 87  LEU B O   
2458 C CB  . LEU B 87  ? 0.0962 0.2654 0.0734 -0.0238 0.0776  -0.0151 87  LEU B CB  
2459 C CG  . LEU B 87  ? 0.1066 0.2869 0.0894 -0.0231 0.0766  -0.0106 87  LEU B CG  
2460 C CD1 . LEU B 87  ? 0.1151 0.2964 0.1069 -0.0080 0.0663  -0.0038 87  LEU B CD1 
2461 C CD2 . LEU B 87  ? 0.1165 0.2953 0.1387 -0.0366 0.0768  0.0001  87  LEU B CD2 
2462 N N   . ALA B 88  ? 0.0721 0.2797 0.0756 0.0140  0.0631  -0.0257 88  ALA B N   
2463 C CA  . ALA B 88  ? 0.0709 0.2679 0.0711 0.0023  0.0614  -0.0233 88  ALA B CA  
2464 C C   . ALA B 88  ? 0.0634 0.2616 0.0699 0.0064  0.0572  -0.0172 88  ALA B C   
2465 O O   . ALA B 88  ? 0.0655 0.2845 0.0892 0.0030  0.0699  -0.0069 88  ALA B O   
2466 C CB  . ALA B 88  ? 0.0725 0.2802 0.0812 -0.0109 0.0546  -0.0184 88  ALA B CB  
2467 N N   . GLU B 89  ? 0.0553 0.2581 0.0804 -0.0006 0.0599  -0.0133 89  GLU B N   
2468 C CA  . GLU B 89  ? 0.0704 0.2562 0.0701 -0.0106 0.0582  -0.0097 89  GLU B CA  
2469 C C   . GLU B 89  ? 0.0597 0.2597 0.0665 -0.0097 0.0567  -0.0071 89  GLU B C   
2470 O O   . GLU B 89  ? 0.0640 0.2739 0.0742 -0.0060 0.0626  -0.0076 89  GLU B O   
2471 C CB  . GLU B 89  ? 0.0775 0.2682 0.0872 -0.0089 0.0633  -0.0043 89  GLU B CB  
2472 C CG  . GLU B 89  ? 0.1154 0.2807 0.0731 -0.0089 0.0557  -0.0030 89  GLU B CG  
2473 C CD  . GLU B 89  ? 0.1049 0.3035 0.0828 0.0098  0.0562  -0.0161 89  GLU B CD  
2474 O OE1 . GLU B 89  ? 0.2472 0.3394 0.1111 0.0310  0.0194  -0.0515 89  GLU B OE1 
2475 O OE2 . GLU B 89  ? 0.1404 0.3526 0.1105 0.0420  0.0456  -0.0118 89  GLU B OE2 
2476 N N   . THR B 90  ? 0.0669 0.2479 0.0650 -0.0025 0.0594  -0.0120 90  THR B N   
2477 C CA  . THR B 90  ? 0.0673 0.2405 0.0742 -0.0038 0.0644  -0.0037 90  THR B CA  
2478 C C   . THR B 90  ? 0.0751 0.2403 0.0554 -0.0092 0.0581  -0.0072 90  THR B C   
2479 O O   . THR B 90  ? 0.0741 0.2681 0.0646 -0.0117 0.0628  -0.0116 90  THR B O   
2480 C CB  . THR B 90  ? 0.0793 0.2547 0.0780 -0.0143 0.0711  -0.0060 90  THR B CB  
2481 O OG1 . THR B 90  ? 0.0735 0.2650 0.0918 -0.0054 0.0757  -0.0059 90  THR B OG1 
2482 C CG2 . THR B 90  ? 0.0820 0.2738 0.0846 -0.0103 0.0714  -0.0130 90  THR B CG2 
2483 N N   . ARG B 91  ? 0.0720 0.2464 0.0881 -0.0108 0.0733  -0.0129 91  ARG B N   
2484 C CA  . ARG B 91  ? 0.0863 0.2456 0.0835 -0.0079 0.0746  -0.0041 91  ARG B CA  
2485 C C   . ARG B 91  ? 0.0575 0.2565 0.0860 0.0015  0.0638  -0.0023 91  ARG B C   
2486 O O   . ARG B 91  ? 0.0827 0.2768 0.0669 0.0142  0.0667  -0.0130 91  ARG B O   
2487 C CB  . ARG B 91  ? 0.0885 0.2691 0.0982 -0.0076 0.0865  -0.0231 91  ARG B CB  
2488 C CG  . ARG B 91  ? 0.1097 0.2753 0.1176 -0.0229 0.0971  -0.0090 91  ARG B CG  
2489 C CD  . ARG B 91  ? 0.1326 0.3026 0.1815 -0.0347 0.0912  -0.0113 91  ARG B CD  
2490 N NE  . ARG B 91  ? 0.1425 0.3220 0.2242 -0.0642 0.0949  -0.0116 91  ARG B NE  
2491 C CZ  . ARG B 91  ? 0.1696 0.3599 0.2613 -0.0723 0.0836  -0.0100 91  ARG B CZ  
2492 N NH1 . ARG B 91  ? 0.2057 0.4497 0.3201 -0.0797 0.0394  -0.0081 91  ARG B NH1 
2493 N NH2 . ARG B 91  ? 0.2435 0.3832 0.2869 -0.0726 0.1378  0.0096  91  ARG B NH2 
2494 N N   . ALA B 92  ? 0.0539 0.2602 0.0832 0.0081  0.0597  -0.0114 92  ALA B N   
2495 C CA  . ALA B 92  ? 0.0573 0.2628 0.0748 0.0005  0.0587  -0.0137 92  ALA B CA  
2496 C C   . ALA B 92  ? 0.0517 0.2462 0.0853 0.0105  0.0577  -0.0229 92  ALA B C   
2497 O O   . ALA B 92  ? 0.0613 0.2755 0.0711 -0.0007 0.0593  -0.0154 92  ALA B O   
2498 C CB  . ALA B 92  ? 0.0694 0.2718 0.0731 -0.0020 0.0609  -0.0105 92  ALA B CB  
2499 N N   . ALA B 93  ? 0.0612 0.2510 0.0640 -0.0042 0.0560  -0.0145 93  ALA B N   
2500 C CA  . ALA B 93  ? 0.0733 0.2311 0.0604 -0.0091 0.0506  -0.0135 93  ALA B CA  
2501 C C   . ALA B 93  ? 0.0616 0.2349 0.0654 -0.0081 0.0539  -0.0074 93  ALA B C   
2502 O O   . ALA B 93  ? 0.0534 0.2754 0.0634 -0.0081 0.0498  -0.0034 93  ALA B O   
2503 C CB  . ALA B 93  ? 0.0792 0.2443 0.0794 0.0002  0.0566  -0.0280 93  ALA B CB  
2504 N N   . ILE B 94  ? 0.0626 0.2369 0.0670 -0.0017 0.0583  0.0060  94  ILE B N   
2505 C CA  . ILE B 94  ? 0.0901 0.2432 0.0531 0.0084  0.0623  -0.0040 94  ILE B CA  
2506 C C   . ILE B 94  ? 0.0662 0.2589 0.0682 0.0138  0.0591  -0.0161 94  ILE B C   
2507 O O   . ILE B 94  ? 0.0693 0.3116 0.0741 0.0225  0.0628  -0.0166 94  ILE B O   
2508 C CB  . ILE B 94  ? 0.0982 0.2592 0.0572 0.0034  0.0637  0.0013  94  ILE B CB  
2509 C CG1 . ILE B 94  ? 0.0982 0.2690 0.0620 0.0091  0.0616  -0.0033 94  ILE B CG1 
2510 C CG2 . ILE B 94  ? 0.1287 0.2650 0.0658 0.0068  0.0739  0.0022  94  ILE B CG2 
2511 C CD1 . ILE B 94  ? 0.1109 0.2823 0.0912 -0.0039 0.0630  -0.0023 94  ILE B CD1 
2512 N N   . ALA B 95  ? 0.0641 0.2735 0.0669 0.0146  0.0576  -0.0145 95  ALA B N   
2513 C CA  . ALA B 95  ? 0.0683 0.2726 0.0814 0.0153  0.0664  -0.0154 95  ALA B CA  
2514 C C   . ALA B 95  ? 0.0686 0.2710 0.0707 0.0095  0.0618  -0.0183 95  ALA B C   
2515 O O   . ALA B 95  ? 0.0861 0.3040 0.0919 0.0278  0.0751  -0.0392 95  ALA B O   
2516 C CB  . ALA B 95  ? 0.0859 0.2823 0.0694 0.0172  0.0684  -0.0195 95  ALA B CB  
2517 N N   . TYR B 96  ? 0.0656 0.2768 0.0735 0.0057  0.0625  -0.0131 96  TYR B N   
2518 C CA  . TYR B 96  ? 0.0661 0.2952 0.0593 -0.0100 0.0562  -0.0131 96  TYR B CA  
2519 C C   . TYR B 96  ? 0.0633 0.3181 0.0684 0.0082  0.0588  -0.0122 96  TYR B C   
2520 O O   . TYR B 96  ? 0.0690 0.3899 0.0756 -0.0062 0.0659  -0.0081 96  TYR B O   
2521 C CB  . TYR B 96  ? 0.0652 0.3019 0.0602 -0.0063 0.0563  -0.0106 96  TYR B CB  
2522 C CG  . TYR B 96  ? 0.0612 0.2908 0.0630 -0.0002 0.0556  -0.0102 96  TYR B CG  
2523 C CD1 . TYR B 96  ? 0.0556 0.2997 0.0756 -0.0054 0.0583  0.0028  96  TYR B CD1 
2524 C CD2 . TYR B 96  ? 0.0676 0.3052 0.0791 -0.0052 0.0667  -0.0117 96  TYR B CD2 
2525 C CE1 . TYR B 96  ? 0.0649 0.2923 0.0755 0.0138  0.0629  -0.0067 96  TYR B CE1 
2526 C CE2 . TYR B 96  ? 0.0646 0.3034 0.0870 -0.0051 0.0685  -0.0082 96  TYR B CE2 
2527 C CZ  . TYR B 96  ? 0.0653 0.2935 0.0679 0.0118  0.0595  -0.0094 96  TYR B CZ  
2528 O OH  . TYR B 96  ? 0.1007 0.3153 0.0785 0.0095  0.0572  -0.0023 96  TYR B OH  
2529 N N   . GLY B 97  ? 0.0759 0.3154 0.0558 0.0254  0.0522  -0.0184 97  GLY B N   
2530 C CA  . GLY B 97  ? 0.0811 0.3057 0.0595 0.0302  0.0570  -0.0270 97  GLY B CA  
2531 C C   . GLY B 97  ? 0.0919 0.2955 0.0605 0.0239  0.0580  -0.0172 97  GLY B C   
2532 O O   . GLY B 97  ? 0.0807 0.3077 0.0777 0.0078  0.0605  -0.0211 97  GLY B O   
2533 N N   . ALA B 98  ? 0.0723 0.2649 0.0768 0.0076  0.0540  -0.0062 98  ALA B N   
2534 C CA  . ALA B 98  ? 0.0644 0.2619 0.0753 0.0048  0.0629  -0.0099 98  ALA B CA  
2535 C C   . ALA B 98  ? 0.0836 0.2508 0.0695 0.0032  0.0695  -0.0090 98  ALA B C   
2536 O O   . ALA B 98  ? 0.0987 0.2365 0.0600 0.0166  0.0689  -0.0044 98  ALA B O   
2537 C CB  . ALA B 98  ? 0.0729 0.2823 0.0782 -0.0052 0.0691  -0.0123 98  ALA B CB  
2538 N N   . ASP B 99  ? 0.0631 0.2409 0.0700 0.0011  0.0600  -0.0051 99  ASP B N   
2539 C CA  . ASP B 99  ? 0.0655 0.2422 0.0705 0.0134  0.0611  -0.0024 99  ASP B CA  
2540 C C   . ASP B 99  ? 0.0643 0.2323 0.0657 0.0177  0.0582  0.0029  99  ASP B C   
2541 O O   . ASP B 99  ? 0.0623 0.2367 0.0869 0.0095  0.0672  0.0120  99  ASP B O   
2542 C CB  . ASP B 99  ? 0.0743 0.2425 0.0737 0.0053  0.0640  -0.0021 99  ASP B CB  
2543 C CG  . ASP B 99  ? 0.0746 0.2381 0.1183 0.0134  0.0690  -0.0070 99  ASP B CG  
2544 O OD1 . ASP B 99  ? 0.0979 0.2450 0.1817 0.0096  0.1075  -0.0050 99  ASP B OD1 
2545 O OD2 . ASP B 99  ? 0.0860 0.2464 0.1480 0.0140  0.0548  0.0018  99  ASP B OD2 
2546 N N   . GLU B 100 ? 0.0648 0.2372 0.0724 0.0237  0.0608  -0.0002 100 GLU B N   
2547 C CA  . GLU B 100 ? 0.0615 0.2279 0.0773 0.0166  0.0616  -0.0028 100 GLU B CA  
2548 C C   . GLU B 100 ? 0.0654 0.2248 0.0703 0.0160  0.0612  0.0053  100 GLU B C   
2549 O O   . GLU B 100 ? 0.0635 0.2483 0.0726 0.0061  0.0611  0.0216  100 GLU B O   
2550 C CB  . GLU B 100 ? 0.0588 0.2455 0.0936 0.0087  0.0672  -0.0051 100 GLU B CB  
2551 C CG  . GLU B 100 ? 0.0786 0.2538 0.1123 0.0096  0.0488  -0.0138 100 GLU B CG  
2552 C CD  . GLU B 100 ? 0.1033 0.2730 0.1117 0.0201  0.0382  -0.0194 100 GLU B CD  
2553 O OE1 . GLU B 100 ? 0.0877 0.2905 0.1387 0.0138  0.0298  -0.0280 100 GLU B OE1 
2554 O OE2 . GLU B 100 ? 0.1636 0.3121 0.1145 0.0336  0.0015  -0.0376 100 GLU B OE2 
2555 N N   . VAL B 101 ? 0.0766 0.2339 0.0603 0.0091  0.0615  0.0031  101 VAL B N   
2556 C CA  . VAL B 101 ? 0.0841 0.2218 0.0572 0.0183  0.0613  -0.0090 101 VAL B CA  
2557 C C   . VAL B 101 ? 0.0715 0.2332 0.0628 0.0049  0.0606  -0.0016 101 VAL B C   
2558 O O   . VAL B 101 ? 0.1017 0.2588 0.0639 0.0188  0.0741  0.0138  101 VAL B O   
2559 C CB  . VAL B 101 ? 0.0913 0.2231 0.0593 0.0149  0.0583  -0.0111 101 VAL B CB  
2560 C CG1 . VAL B 101 ? 0.1003 0.2452 0.1058 0.0086  0.0449  -0.0117 101 VAL B CG1 
2561 C CG2 . VAL B 101 ? 0.0932 0.2315 0.0582 0.0039  0.0604  -0.0201 101 VAL B CG2 
2562 N N   . ASP B 102 ? 0.0708 0.2408 0.0641 0.0185  0.0592  -0.0107 102 ASP B N   
2563 C CA  . ASP B 102 ? 0.0829 0.2360 0.0638 0.0184  0.0647  -0.0100 102 ASP B CA  
2564 C C   . ASP B 102 ? 0.0681 0.2436 0.0676 0.0035  0.0615  0.0026  102 ASP B C   
2565 O O   . ASP B 102 ? 0.0604 0.2786 0.0704 -0.0017 0.0582  0.0179  102 ASP B O   
2566 C CB  . ASP B 102 ? 0.0803 0.2400 0.0726 0.0158  0.0678  -0.0161 102 ASP B CB  
2567 C CG  . ASP B 102 ? 0.0821 0.2639 0.0916 0.0024  0.0803  -0.0034 102 ASP B CG  
2568 O OD1 . ASP B 102 ? 0.0964 0.3014 0.0794 -0.0046 0.0808  0.0090  102 ASP B OD1 
2569 O OD2 . ASP B 102 ? 0.1109 0.3082 0.1507 -0.0181 0.0551  -0.0073 102 ASP B OD2 
2570 N N   . VAL B 103 ? 0.0656 0.2503 0.0660 0.0052  0.0593  -0.0044 103 VAL B N   
2571 C CA  . VAL B 103 ? 0.0742 0.2439 0.0617 0.0140  0.0597  -0.0136 103 VAL B CA  
2572 C C   . VAL B 103 ? 0.0544 0.2332 0.0680 -0.0008 0.0543  -0.0104 103 VAL B C   
2573 O O   . VAL B 103 ? 0.0515 0.2587 0.0599 0.0041  0.0487  -0.0119 103 VAL B O   
2574 C CB  . VAL B 103 ? 0.0773 0.2370 0.0778 0.0094  0.0699  -0.0154 103 VAL B CB  
2575 C CG1 . VAL B 103 ? 0.0870 0.2526 0.0893 0.0027  0.0814  -0.0112 103 VAL B CG1 
2576 C CG2 . VAL B 103 ? 0.0704 0.2444 0.1112 0.0045  0.0722  -0.0129 103 VAL B CG2 
2577 N N   . VAL B 104 ? 0.0602 0.2403 0.0719 0.0142  0.0590  0.0014  104 VAL B N   
2578 C CA  . VAL B 104 ? 0.0403 0.2245 0.0905 0.0113  0.0528  -0.0047 104 VAL B CA  
2579 C C   . VAL B 104 ? 0.0520 0.2301 0.0655 -0.0077 0.0512  -0.0029 104 VAL B C   
2580 O O   . VAL B 104 ? 0.0576 0.2587 0.0770 -0.0134 0.0600  -0.0040 104 VAL B O   
2581 C CB  . VAL B 104 ? 0.0376 0.2268 0.0911 0.0072  0.0494  -0.0008 104 VAL B CB  
2582 C CG1 . VAL B 104 ? 0.0540 0.2292 0.0937 0.0050  0.0466  -0.0081 104 VAL B CG1 
2583 C CG2 . VAL B 104 ? 0.0573 0.2234 0.0790 -0.0015 0.0495  0.0140  104 VAL B CG2 
2584 N N   . PHE B 105 ? 0.0368 0.2490 0.0771 -0.0040 0.0464  -0.0141 105 PHE B N   
2585 C CA  . PHE B 105 ? 0.0344 0.2410 0.0903 -0.0031 0.0485  -0.0108 105 PHE B CA  
2586 C C   . PHE B 105 ? 0.0555 0.2346 0.0633 0.0008  0.0473  -0.0208 105 PHE B C   
2587 O O   . PHE B 105 ? 0.0562 0.2482 0.0943 0.0011  0.0662  -0.0029 105 PHE B O   
2588 C CB  . PHE B 105 ? 0.0408 0.2400 0.0836 -0.0053 0.0516  -0.0071 105 PHE B CB  
2589 C CG  . PHE B 105 ? 0.0455 0.2481 0.0880 0.0012  0.0565  0.0081  105 PHE B CG  
2590 C CD1 . PHE B 105 ? 0.0692 0.2464 0.0880 0.0076  0.0694  0.0080  105 PHE B CD1 
2591 C CD2 . PHE B 105 ? 0.0737 0.2628 0.0737 0.0229  0.0585  0.0135  105 PHE B CD2 
2592 C CE1 . PHE B 105 ? 0.0895 0.2521 0.1074 -0.0003 0.0734  0.0303  105 PHE B CE1 
2593 C CE2 . PHE B 105 ? 0.0858 0.2802 0.1052 0.0107  0.0676  0.0159  105 PHE B CE2 
2594 C CZ  . PHE B 105 ? 0.0929 0.2685 0.0750 0.0049  0.0745  0.0208  105 PHE B CZ  
2595 N N   . PRO B 106 ? 0.0584 0.2530 0.0787 0.0028  0.0599  -0.0263 106 PRO B N   
2596 C CA  . PRO B 106 ? 0.0654 0.2620 0.0816 0.0060  0.0659  -0.0150 106 PRO B CA  
2597 C C   . PRO B 106 ? 0.0491 0.2645 0.0955 0.0036  0.0604  -0.0255 106 PRO B C   
2598 O O   . PRO B 106 ? 0.0390 0.2767 0.1371 -0.0183 0.0558  -0.0064 106 PRO B O   
2599 C CB  . PRO B 106 ? 0.0525 0.2730 0.1034 0.0060  0.0657  -0.0232 106 PRO B CB  
2600 C CG  . PRO B 106 ? 0.0500 0.2646 0.1123 -0.0021 0.0626  -0.0253 106 PRO B CG  
2601 C CD  . PRO B 106 ? 0.0545 0.2593 0.0901 -0.0019 0.0626  -0.0270 106 PRO B CD  
2602 N N   . TYR B 107 ? 0.0511 0.2528 0.0867 0.0147  0.0571  -0.0238 107 TYR B N   
2603 C CA  . TYR B 107 ? 0.0550 0.2613 0.0909 0.0023  0.0613  -0.0220 107 TYR B CA  
2604 C C   . TYR B 107 ? 0.0697 0.2600 0.0894 0.0190  0.0483  -0.0309 107 TYR B C   
2605 O O   . TYR B 107 ? 0.0592 0.2686 0.0969 0.0104  0.0590  -0.0258 107 TYR B O   
2606 C CB  . TYR B 107 ? 0.0639 0.2642 0.1093 0.0066  0.0394  -0.0119 107 TYR B CB  
2607 C CG  . TYR B 107 ? 0.0632 0.2504 0.1164 0.0078  0.0477  -0.0064 107 TYR B CG  
2608 C CD1 . TYR B 107 ? 0.0798 0.2596 0.1390 0.0147  0.0538  -0.0022 107 TYR B CD1 
2609 C CD2 . TYR B 107 ? 0.0568 0.2540 0.1219 0.0147  0.0423  -0.0069 107 TYR B CD2 
2610 C CE1 . TYR B 107 ? 0.0734 0.2546 0.1378 0.0266  0.0530  -0.0049 107 TYR B CE1 
2611 C CE2 . TYR B 107 ? 0.0676 0.2530 0.1105 0.0110  0.0421  0.0017  107 TYR B CE2 
2612 C CZ  . TYR B 107 ? 0.0792 0.2582 0.1152 0.0175  0.0558  0.0060  107 TYR B CZ  
2613 O OH  . TYR B 107 ? 0.1153 0.2739 0.1576 -0.0004 0.0324  0.0165  107 TYR B OH  
2614 N N   . ARG B 108 ? 0.0529 0.2748 0.1071 0.0244  0.0439  -0.0155 108 ARG B N   
2615 C CA  . ARG B 108 ? 0.0483 0.2794 0.0973 0.0180  0.0587  -0.0229 108 ARG B CA  
2616 C C   . ARG B 108 ? 0.0664 0.2722 0.1061 0.0181  0.0539  -0.0164 108 ARG B C   
2617 O O   . ARG B 108 ? 0.0737 0.2980 0.1218 0.0303  0.0581  -0.0335 108 ARG B O   
2618 C CB  . ARG B 108 ? 0.0565 0.2900 0.1111 0.0341  0.0441  -0.0201 108 ARG B CB  
2619 C CG  . ARG B 108 ? 0.0987 0.3052 0.1222 0.0379  0.0627  -0.0128 108 ARG B CG  
2620 C CD  . ARG B 108 ? 0.1637 0.3324 0.1479 0.0297  0.0477  -0.0020 108 ARG B CD  
2621 N NE  . ARG B 108 ? 0.2301 0.3638 0.1768 0.0258  0.0385  -0.0045 108 ARG B NE  
2622 C CZ  . ARG B 108 ? 0.1995 0.3463 0.1934 0.0297  0.0181  -0.0300 108 ARG B CZ  
2623 N NH1 . ARG B 108 ? 0.2852 0.3675 0.2295 0.0206  0.0133  -0.0497 108 ARG B NH1 
2624 N NH2 . ARG B 108 ? 0.1825 0.3583 0.1431 0.0280  0.0234  -0.0521 108 ARG B NH2 
2625 N N   . ALA B 109 ? 0.0675 0.2725 0.0933 0.0086  0.0610  -0.0168 109 ALA B N   
2626 C CA  . ALA B 109 ? 0.0456 0.2729 0.0972 0.0003  0.0468  -0.0223 109 ALA B CA  
2627 C C   . ALA B 109 ? 0.0417 0.2788 0.0940 0.0041  0.0551  -0.0148 109 ALA B C   
2628 O O   . ALA B 109 ? 0.0383 0.2907 0.1315 -0.0026 0.0632  -0.0100 109 ALA B O   
2629 C CB  . ALA B 109 ? 0.0707 0.2681 0.1189 -0.0051 0.0556  -0.0115 109 ALA B CB  
2630 N N   . LEU B 110 ? 0.0533 0.2969 0.0887 0.0176  0.0551  -0.0200 110 LEU B N   
2631 C CA  . LEU B 110 ? 0.0489 0.2925 0.0898 0.0077  0.0594  -0.0015 110 LEU B CA  
2632 C C   . LEU B 110 ? 0.0448 0.2858 0.1112 0.0147  0.0619  -0.0141 110 LEU B C   
2633 O O   . LEU B 110 ? 0.0461 0.3430 0.1347 0.0111  0.0704  -0.0154 110 LEU B O   
2634 C CB  . LEU B 110 ? 0.0518 0.2935 0.0832 0.0153  0.0537  0.0010  110 LEU B CB  
2635 C CG  . LEU B 110 ? 0.0603 0.3136 0.0823 0.0038  0.0640  0.0022  110 LEU B CG  
2636 C CD1 . LEU B 110 ? 0.0687 0.3355 0.0992 0.0014  0.0619  0.0054  110 LEU B CD1 
2637 C CD2 . LEU B 110 ? 0.0637 0.3237 0.0999 0.0064  0.0648  0.0072  110 LEU B CD2 
2638 N N   . MET B 111 ? 0.0467 0.2884 0.1131 0.0203  0.0615  -0.0288 111 MET B N   
2639 C CA  . MET B 111 ? 0.0603 0.2831 0.1411 0.0278  0.0564  -0.0232 111 MET B CA  
2640 C C   . MET B 111 ? 0.0609 0.2835 0.1467 0.0265  0.0539  -0.0253 111 MET B C   
2641 O O   . MET B 111 ? 0.0735 0.3312 0.1651 0.0339  0.0640  -0.0558 111 MET B O   
2642 C CB  . MET B 111 ? 0.0801 0.2904 0.1845 0.0427  0.0535  -0.0120 111 MET B CB  
2643 C CG  . MET B 111 ? 0.1121 0.3515 0.2219 0.0135  0.0409  -0.0121 111 MET B CG  
2644 S SD  . MET B 111 ? 0.1474 0.4025 0.3824 -0.0188 0.0307  0.0144  111 MET B SD  
2645 C CE  . MET B 111 ? 0.1134 0.4647 0.3267 -0.0398 0.0715  -0.0458 111 MET B CE  
2646 N N   . ALA B 112 ? 0.0467 0.3027 0.1438 0.0121  0.0722  -0.0275 112 ALA B N   
2647 C CA  . ALA B 112 ? 0.0414 0.3160 0.1451 0.0195  0.0654  -0.0158 112 ALA B CA  
2648 C C   . ALA B 112 ? 0.0502 0.3404 0.1568 0.0039  0.0810  -0.0100 112 ALA B C   
2649 O O   . ALA B 112 ? 0.0645 0.3630 0.1936 -0.0116 0.0506  -0.0072 112 ALA B O   
2650 C CB  . ALA B 112 ? 0.0468 0.3297 0.1535 0.0310  0.0522  -0.0251 112 ALA B CB  
2651 N N   . GLY B 113 ? 0.0614 0.3445 0.1510 0.0129  0.0885  -0.0085 113 GLY B N   
2652 C CA  . GLY B 113 ? 0.0637 0.3541 0.1507 -0.0083 0.0909  -0.0005 113 GLY B CA  
2653 C C   . GLY B 113 ? 0.0721 0.3636 0.1551 -0.0119 0.0987  -0.0025 113 GLY B C   
2654 O O   . GLY B 113 ? 0.1694 0.3617 0.1972 -0.0055 0.1133  0.0290  113 GLY B O   
2655 N N   . ASN B 114 ? 0.0590 0.3453 0.1424 -0.0070 0.0846  -0.0072 114 ASN B N   
2656 C CA  . ASN B 114 ? 0.0571 0.3374 0.1748 -0.0067 0.0714  -0.0074 114 ASN B CA  
2657 C C   . ASN B 114 ? 0.0658 0.3177 0.1620 0.0049  0.0813  -0.0027 114 ASN B C   
2658 O O   . ASN B 114 ? 0.0598 0.3733 0.1642 0.0099  0.0857  0.0004  114 ASN B O   
2659 C CB  . ASN B 114 ? 0.0506 0.3482 0.1807 0.0009  0.0661  -0.0110 114 ASN B CB  
2660 C CG  . ASN B 114 ? 0.0658 0.3520 0.1934 0.0113  0.0615  -0.0196 114 ASN B CG  
2661 O OD1 . ASN B 114 ? 0.0620 0.3427 0.1936 -0.0102 0.0877  -0.0203 114 ASN B OD1 
2662 N ND2 . ASN B 114 ? 0.1242 0.3983 0.2329 0.0280  0.0311  -0.0489 114 ASN B ND2 
2663 N N   . GLU B 115 ? 0.0699 0.3283 0.1517 0.0005  0.0734  -0.0080 115 GLU B N   
2664 C CA  . GLU B 115 ? 0.0740 0.3202 0.1542 -0.0081 0.0721  -0.0074 115 GLU B CA  
2665 C C   . GLU B 115 ? 0.0760 0.3150 0.1502 -0.0115 0.0718  -0.0082 115 GLU B C   
2666 O O   . GLU B 115 ? 0.0589 0.3362 0.1805 -0.0155 0.0562  -0.0109 115 GLU B O   
2667 C CB  . GLU B 115 ? 0.1058 0.3440 0.1598 -0.0214 0.0749  -0.0086 115 GLU B CB  
2668 C CG  . GLU B 115 ? 0.1122 0.3495 0.1586 -0.0265 0.0736  -0.0041 115 GLU B CG  
2669 C CD  . GLU B 115 ? 0.1988 0.3684 0.1661 -0.0014 0.0835  0.0027  115 GLU B CD  
2670 O OE1 . GLU B 115 ? 0.3133 0.4118 0.1878 0.0094  0.0676  0.0021  115 GLU B OE1 
2671 O OE2 . GLU B 115 ? 0.2312 0.4291 0.2089 -0.0022 0.0991  -0.0423 115 GLU B OE2 
2672 N N   . GLN B 116 ? 0.0732 0.3117 0.1380 -0.0168 0.0748  -0.0110 116 GLN B N   
2673 C CA  . GLN B 116 ? 0.0836 0.3148 0.1591 -0.0189 0.0858  -0.0136 116 GLN B CA  
2674 C C   . GLN B 116 ? 0.0749 0.2919 0.1513 -0.0056 0.0783  -0.0146 116 GLN B C   
2675 O O   . GLN B 116 ? 0.0538 0.2986 0.1745 -0.0107 0.0888  0.0006  116 GLN B O   
2676 C CB  . GLN B 116 ? 0.0956 0.3492 0.1877 -0.0392 0.1124  -0.0057 116 GLN B CB  
2677 C CG  . GLN B 116 ? 0.1467 0.3831 0.2230 -0.0358 0.1171  -0.0048 116 GLN B CG  
2678 C CD  . GLN B 116 ? 0.2186 0.4396 0.2424 -0.0108 0.1416  0.0203  116 GLN B CD  
2679 O OE1 . GLN B 116 ? 0.3126 0.5333 0.2610 -0.0190 0.1917  0.0144  116 GLN B OE1 
2680 N NE2 . GLN B 116 ? 0.2390 0.4716 0.2920 0.0151  0.1488  0.0469  116 GLN B NE2 
2681 N N   . VAL B 117 ? 0.0563 0.2904 0.1470 -0.0116 0.0838  -0.0233 117 VAL B N   
2682 C CA  . VAL B 117 ? 0.0665 0.2818 0.1283 -0.0084 0.0709  -0.0242 117 VAL B CA  
2683 C C   . VAL B 117 ? 0.0745 0.2771 0.1500 0.0017  0.0622  -0.0187 117 VAL B C   
2684 O O   . VAL B 117 ? 0.0801 0.2910 0.1178 0.0038  0.0717  -0.0151 117 VAL B O   
2685 C CB  . VAL B 117 ? 0.0619 0.2990 0.1278 -0.0049 0.0625  -0.0278 117 VAL B CB  
2686 C CG1 . VAL B 117 ? 0.0753 0.3074 0.1446 -0.0029 0.0471  -0.0172 117 VAL B CG1 
2687 C CG2 . VAL B 117 ? 0.1153 0.3077 0.1152 0.0124  0.0534  -0.0396 117 VAL B CG2 
2688 N N   . GLY B 118 ? 0.0473 0.2707 0.1401 -0.0023 0.0646  -0.0070 118 GLY B N   
2689 C CA  . GLY B 118 ? 0.0581 0.2653 0.1283 -0.0213 0.0652  0.0117  118 GLY B CA  
2690 C C   . GLY B 118 ? 0.0505 0.2722 0.1177 -0.0191 0.0668  0.0093  118 GLY B C   
2691 O O   . GLY B 118 ? 0.0565 0.2970 0.1067 -0.0186 0.0706  -0.0101 118 GLY B O   
2692 N N   . PHE B 119 ? 0.0658 0.2703 0.0987 -0.0174 0.0738  -0.0082 119 PHE B N   
2693 C CA  . PHE B 119 ? 0.0746 0.2706 0.1002 -0.0189 0.0799  -0.0129 119 PHE B CA  
2694 C C   . PHE B 119 ? 0.0837 0.2572 0.0977 -0.0186 0.0647  -0.0104 119 PHE B C   
2695 O O   . PHE B 119 ? 0.0940 0.2872 0.0870 -0.0022 0.0841  0.0040  119 PHE B O   
2696 C CB  . PHE B 119 ? 0.0731 0.2904 0.1147 -0.0254 0.0840  -0.0047 119 PHE B CB  
2697 C CG  . PHE B 119 ? 0.0903 0.2894 0.1203 -0.0331 0.0829  0.0048  119 PHE B CG  
2698 C CD1 . PHE B 119 ? 0.1167 0.2940 0.1219 -0.0279 0.0737  0.0137  119 PHE B CD1 
2699 C CD2 . PHE B 119 ? 0.1172 0.2930 0.1267 -0.0357 0.0669  0.0090  119 PHE B CD2 
2700 C CE1 . PHE B 119 ? 0.1140 0.3064 0.1538 -0.0343 0.0704  0.0126  119 PHE B CE1 
2701 C CE2 . PHE B 119 ? 0.1431 0.3016 0.1530 -0.0326 0.0536  0.0031  119 PHE B CE2 
2702 C CZ  . PHE B 119 ? 0.1166 0.3063 0.1652 -0.0350 0.0635  0.0230  119 PHE B CZ  
2703 N N   . ASP B 120 ? 0.0793 0.2669 0.1012 -0.0195 0.0556  -0.0122 120 ASP B N   
2704 C CA  . ASP B 120 ? 0.0764 0.2659 0.0977 -0.0304 0.0740  -0.0140 120 ASP B CA  
2705 C C   . ASP B 120 ? 0.0787 0.2605 0.0961 -0.0221 0.0771  -0.0131 120 ASP B C   
2706 O O   . ASP B 120 ? 0.0949 0.2885 0.1081 -0.0175 0.0915  -0.0177 120 ASP B O   
2707 C CB  . ASP B 120 ? 0.0808 0.2973 0.1228 -0.0408 0.0750  -0.0196 120 ASP B CB  
2708 C CG  . ASP B 120 ? 0.1132 0.3288 0.1685 -0.0624 0.0760  0.0103  120 ASP B CG  
2709 O OD1 . ASP B 120 ? 0.1735 0.3870 0.1786 -0.0627 0.0570  0.0344  120 ASP B OD1 
2710 O OD2 . ASP B 120 ? 0.1180 0.4201 0.2234 -0.0240 0.0876  -0.0296 120 ASP B OD2 
2711 N N   . LEU B 121 ? 0.0896 0.2622 0.0991 -0.0155 0.0877  -0.0070 121 LEU B N   
2712 C CA  . LEU B 121 ? 0.0821 0.2663 0.0938 -0.0179 0.0807  0.0010  121 LEU B CA  
2713 C C   . LEU B 121 ? 0.0750 0.2698 0.0917 -0.0194 0.0765  -0.0157 121 LEU B C   
2714 O O   . LEU B 121 ? 0.0808 0.3083 0.0852 -0.0109 0.0766  -0.0072 121 LEU B O   
2715 C CB  . LEU B 121 ? 0.1077 0.2657 0.0942 -0.0264 0.0806  -0.0028 121 LEU B CB  
2716 C CG  . LEU B 121 ? 0.1026 0.2644 0.1007 -0.0219 0.0824  -0.0004 121 LEU B CG  
2717 C CD1 . LEU B 121 ? 0.1138 0.2786 0.1218 -0.0278 0.0759  0.0095  121 LEU B CD1 
2718 C CD2 . LEU B 121 ? 0.1026 0.2712 0.1104 -0.0137 0.0773  -0.0086 121 LEU B CD2 
2719 N N   . VAL B 122 ? 0.0720 0.2602 0.0868 -0.0101 0.0726  -0.0202 122 VAL B N   
2720 C CA  . VAL B 122 ? 0.0822 0.2577 0.0833 -0.0158 0.0764  -0.0127 122 VAL B CA  
2721 C C   . VAL B 122 ? 0.0833 0.2535 0.0802 -0.0091 0.0753  -0.0040 122 VAL B C   
2722 O O   . VAL B 122 ? 0.0690 0.2572 0.1022 -0.0047 0.0771  -0.0222 122 VAL B O   
2723 C CB  . VAL B 122 ? 0.0616 0.2452 0.0894 -0.0199 0.0675  -0.0190 122 VAL B CB  
2724 C CG1 . VAL B 122 ? 0.0634 0.2473 0.0992 -0.0220 0.0696  -0.0061 122 VAL B CG1 
2725 C CG2 . VAL B 122 ? 0.0539 0.2568 0.1058 -0.0233 0.0665  -0.0245 122 VAL B CG2 
2726 N N   . LYS B 123 ? 0.0947 0.2270 0.0940 -0.0237 0.0743  -0.0073 123 LYS B N   
2727 C CA  . LYS B 123 ? 0.1121 0.2425 0.1013 -0.0216 0.0769  -0.0053 123 LYS B CA  
2728 C C   . LYS B 123 ? 0.1162 0.2293 0.1120 -0.0139 0.0728  -0.0112 123 LYS B C   
2729 O O   . LYS B 123 ? 0.1248 0.2504 0.1036 0.0021  0.0663  -0.0021 123 LYS B O   
2730 C CB  . LYS B 123 ? 0.1506 0.2550 0.1244 -0.0383 0.0914  -0.0003 123 LYS B CB  
2731 C CG  . LYS B 123 ? 0.2034 0.2842 0.1546 -0.0236 0.1082  0.0033  123 LYS B CG  
2732 C CD  . LYS B 123 ? 0.2312 0.3202 0.2286 -0.0228 0.1357  0.0322  123 LYS B CD  
2733 C CE  . LYS B 123 ? 0.3355 0.3686 0.3591 -0.0160 0.1049  0.0093  123 LYS B CE  
2734 N NZ  . LYS B 123 ? 0.4273 0.4398 0.3939 -0.0195 0.1080  -0.0139 123 LYS B NZ  
2735 N N   . ALA B 124 ? 0.0841 0.2457 0.1137 -0.0129 0.0763  -0.0295 124 ALA B N   
2736 C CA  . ALA B 124 ? 0.0950 0.2516 0.1174 -0.0061 0.0733  -0.0292 124 ALA B CA  
2737 C C   . ALA B 124 ? 0.0885 0.2325 0.1194 -0.0019 0.0658  -0.0237 124 ALA B C   
2738 O O   . ALA B 124 ? 0.0982 0.2472 0.1038 -0.0024 0.0796  -0.0183 124 ALA B O   
2739 C CB  . ALA B 124 ? 0.0950 0.2826 0.1429 -0.0087 0.0679  -0.0328 124 ALA B CB  
2740 N N   . CYS B 125 ? 0.0669 0.2298 0.1003 -0.0086 0.0755  -0.0127 125 CYS B N   
2741 C CA  . CYS B 125 ? 0.0673 0.2404 0.0931 -0.0091 0.0727  -0.0101 125 CYS B CA  
2742 C C   . CYS B 125 ? 0.0768 0.2360 0.0894 0.0059  0.0761  -0.0073 125 CYS B C   
2743 O O   . CYS B 125 ? 0.0712 0.2526 0.1033 0.0013  0.0793  -0.0054 125 CYS B O   
2744 C CB  . CYS B 125 ? 0.0737 0.2543 0.1033 -0.0164 0.0803  -0.0032 125 CYS B CB  
2745 S SG  . CYS B 125 ? 0.1085 0.2925 0.1292 -0.0003 0.0847  0.0008  125 CYS B SG  
2746 N N   . LYS B 126 ? 0.0834 0.2398 0.0799 0.0004  0.0752  0.0080  126 LYS B N   
2747 C CA  . LYS B 126 ? 0.0931 0.2560 0.0804 0.0117  0.0799  -0.0005 126 LYS B CA  
2748 C C   . LYS B 126 ? 0.1120 0.2475 0.0879 0.0161  0.0655  -0.0002 126 LYS B C   
2749 O O   . LYS B 126 ? 0.1091 0.2890 0.0890 0.0307  0.0790  -0.0152 126 LYS B O   
2750 C CB  . LYS B 126 ? 0.1242 0.2658 0.0801 0.0055  0.0870  -0.0015 126 LYS B CB  
2751 C CG  . LYS B 126 ? 0.1439 0.2697 0.0957 0.0101  0.0813  -0.0054 126 LYS B CG  
2752 C CD  . LYS B 126 ? 0.1540 0.2887 0.1257 0.0151  0.0740  -0.0094 126 LYS B CD  
2753 C CE  . LYS B 126 ? 0.1962 0.2972 0.1701 0.0344  0.0749  0.0063  126 LYS B CE  
2754 N NZ  . LYS B 126 ? 0.2620 0.3612 0.2235 0.0572  0.0358  -0.0066 126 LYS B NZ  
2755 N N   . GLU B 127 ? 0.1173 0.2475 0.1070 0.0188  0.0752  -0.0093 127 GLU B N   
2756 C CA  . GLU B 127 ? 0.1572 0.2568 0.1262 0.0152  0.0743  -0.0044 127 GLU B CA  
2757 C C   . GLU B 127 ? 0.1389 0.2421 0.1228 0.0107  0.0670  -0.0058 127 GLU B C   
2758 O O   . GLU B 127 ? 0.1586 0.2707 0.1394 0.0258  0.0809  0.0020  127 GLU B O   
2759 C CB  . GLU B 127 ? 0.1851 0.2827 0.1797 -0.0072 0.0646  -0.0110 127 GLU B CB  
2760 C CG  . GLU B 127 ? 0.2469 0.3369 0.2153 0.0083  0.1020  -0.0137 127 GLU B CG  
2761 C CD  . GLU B 127 ? 0.3243 0.4496 0.2405 -0.0291 0.0925  0.0139  127 GLU B CD  
2762 O OE1 . GLU B 127 ? 0.4635 0.6197 0.3526 -0.0533 -0.0023 -0.0049 127 GLU B OE1 
2763 O OE2 . GLU B 127 ? 0.3733 0.5494 0.3014 -0.0699 0.1835  0.0282  127 GLU B OE2 
2764 N N   . ALA B 128 ? 0.1152 0.2432 0.1118 0.0051  0.0707  -0.0203 128 ALA B N   
2765 C CA  . ALA B 128 ? 0.1005 0.2447 0.1205 -0.0065 0.0719  -0.0222 128 ALA B CA  
2766 C C   . ALA B 128 ? 0.1005 0.2317 0.1102 0.0051  0.0660  -0.0150 128 ALA B C   
2767 O O   . ALA B 128 ? 0.1233 0.2419 0.1320 0.0120  0.0804  -0.0255 128 ALA B O   
2768 C CB  . ALA B 128 ? 0.0835 0.2631 0.1344 -0.0113 0.0668  -0.0137 128 ALA B CB  
2769 N N   . CYS B 129 ? 0.0907 0.2323 0.1005 0.0112  0.0776  -0.0213 129 CYS B N   
2770 C CA  . CYS B 129 ? 0.0748 0.2263 0.1001 0.0069  0.0801  0.0019  129 CYS B CA  
2771 C C   . CYS B 129 ? 0.0952 0.2379 0.1050 0.0146  0.0786  0.0023  129 CYS B C   
2772 O O   . CYS B 129 ? 0.0985 0.2525 0.1368 0.0262  0.0733  -0.0084 129 CYS B O   
2773 C CB  . CYS B 129 ? 0.0620 0.2431 0.1192 0.0052  0.0754  -0.0054 129 CYS B CB  
2774 S SG  . CYS B 129 ? 0.0845 0.2579 0.1246 0.0111  0.0702  -0.0007 129 CYS B SG  
2775 N N   . ALA B 130 ? 0.1097 0.2499 0.1032 0.0269  0.0907  0.0051  130 ALA B N   
2776 C CA  . ALA B 130 ? 0.1347 0.2535 0.1125 0.0301  0.0691  0.0068  130 ALA B CA  
2777 C C   . ALA B 130 ? 0.1669 0.2490 0.1290 0.0352  0.0635  0.0172  130 ALA B C   
2778 O O   . ALA B 130 ? 0.1662 0.2743 0.1415 0.0479  0.0699  0.0190  130 ALA B O   
2779 C CB  . ALA B 130 ? 0.1659 0.2784 0.1106 0.0396  0.0800  0.0197  130 ALA B CB  
2780 N N   . ALA B 131 ? 0.1748 0.2321 0.1660 0.0232  0.0540  -0.0070 131 ALA B N   
2781 C CA  . ALA B 131 ? 0.1935 0.2431 0.1704 0.0237  0.0781  0.0038  131 ALA B CA  
2782 C C   . ALA B 131 ? 0.1960 0.2487 0.1488 0.0304  0.0765  0.0017  131 ALA B C   
2783 O O   . ALA B 131 ? 0.2809 0.2497 0.1914 0.0488  0.0943  0.0233  131 ALA B O   
2784 C CB  . ALA B 131 ? 0.2383 0.2655 0.2154 0.0224  0.0508  -0.0220 131 ALA B CB  
2785 N N   . ALA B 132 ? 0.1413 0.2410 0.1154 0.0225  0.0686  -0.0063 132 ALA B N   
2786 C CA  . ALA B 132 ? 0.1679 0.2720 0.1116 0.0276  0.0922  0.0069  132 ALA B CA  
2787 C C   . ALA B 132 ? 0.1360 0.2692 0.1369 0.0417  0.0833  0.0078  132 ALA B C   
2788 O O   . ALA B 132 ? 0.1492 0.2838 0.1820 0.0254  0.0988  0.0122  132 ALA B O   
2789 C CB  . ALA B 132 ? 0.1961 0.2874 0.1292 0.0195  0.0713  0.0202  132 ALA B CB  
2790 N N   . ASN B 133 ? 0.1394 0.2609 0.1437 0.0148  0.0714  0.0142  133 ASN B N   
2791 C CA  . ASN B 133 ? 0.1291 0.2452 0.1723 0.0137  0.0567  0.0152  133 ASN B CA  
2792 C C   . ASN B 133 ? 0.1164 0.2498 0.1573 0.0088  0.0448  0.0091  133 ASN B C   
2793 O O   . ASN B 133 ? 0.1152 0.2705 0.2450 0.0052  0.0354  0.0211  133 ASN B O   
2794 C CB  . ASN B 133 ? 0.1612 0.2742 0.2450 0.0323  0.0662  0.0060  133 ASN B CB  
2795 C CG  . ASN B 133 ? 0.2723 0.3283 0.3250 0.0095  0.0525  0.0054  133 ASN B CG  
2796 O OD1 . ASN B 133 ? 0.3667 0.4136 0.4452 0.0287  0.0852  -0.0546 133 ASN B OD1 
2797 N ND2 . ASN B 133 ? 0.3283 0.3630 0.3236 -0.0241 0.0439  0.0231  133 ASN B ND2 
2798 N N   . VAL B 134 ? 0.0794 0.2507 0.1031 0.0032  0.0722  0.0174  134 VAL B N   
2799 C CA  . VAL B 134 ? 0.0643 0.2428 0.0996 0.0036  0.0649  -0.0036 134 VAL B CA  
2800 C C   . VAL B 134 ? 0.0887 0.2340 0.0968 -0.0024 0.0604  -0.0076 134 VAL B C   
2801 O O   . VAL B 134 ? 0.0919 0.2655 0.0936 -0.0125 0.0683  0.0102  134 VAL B O   
2802 C CB  . VAL B 134 ? 0.0707 0.2465 0.0942 0.0020  0.0746  -0.0027 134 VAL B CB  
2803 C CG1 . VAL B 134 ? 0.0684 0.2534 0.1015 -0.0094 0.0574  0.0093  134 VAL B CG1 
2804 C CG2 . VAL B 134 ? 0.1161 0.2433 0.0991 0.0159  0.0806  -0.0172 134 VAL B CG2 
2805 N N   . LEU B 135 ? 0.0860 0.2345 0.0865 0.0043  0.0558  -0.0112 135 LEU B N   
2806 C CA  . LEU B 135 ? 0.0950 0.2535 0.1023 0.0165  0.0668  -0.0108 135 LEU B CA  
2807 C C   . LEU B 135 ? 0.0872 0.2556 0.0743 0.0137  0.0717  0.0116  135 LEU B C   
2808 O O   . LEU B 135 ? 0.0938 0.2700 0.0850 0.0260  0.0829  0.0231  135 LEU B O   
2809 C CB  . LEU B 135 ? 0.1458 0.2943 0.1644 0.0033  0.0316  -0.0093 135 LEU B CB  
2810 C CG  . LEU B 135 ? 0.1868 0.3522 0.2203 0.0135  0.0233  -0.0103 135 LEU B CG  
2811 C CD1 . LEU B 135 ? 0.2528 0.4147 0.2350 -0.0247 -0.0034 -0.0252 135 LEU B CD1 
2812 C CD2 . LEU B 135 ? 0.2211 0.4041 0.2344 0.0015  0.0001  0.0195  135 LEU B CD2 
2813 N N   . LEU B 136 ? 0.0868 0.2433 0.0948 0.0144  0.0780  0.0054  136 LEU B N   
2814 C CA  . LEU B 136 ? 0.0950 0.2244 0.0892 0.0034  0.0715  0.0047  136 LEU B CA  
2815 C C   . LEU B 136 ? 0.0718 0.2213 0.0746 0.0182  0.0657  -0.0036 136 LEU B C   
2816 O O   . LEU B 136 ? 0.0876 0.2515 0.0695 0.0106  0.0716  0.0055  136 LEU B O   
2817 C CB  . LEU B 136 ? 0.0840 0.2490 0.0900 0.0016  0.0680  -0.0051 136 LEU B CB  
2818 C CG  . LEU B 136 ? 0.0796 0.2596 0.1020 0.0029  0.0835  -0.0072 136 LEU B CG  
2819 C CD1 . LEU B 136 ? 0.0799 0.2719 0.1110 -0.0006 0.0609  0.0003  136 LEU B CD1 
2820 C CD2 . LEU B 136 ? 0.0944 0.2705 0.1358 -0.0147 0.0867  -0.0027 136 LEU B CD2 
2821 N N   . LYS B 137 ? 0.0648 0.2190 0.0752 0.0092  0.0628  -0.0068 137 LYS B N   
2822 C CA  . LYS B 137 ? 0.0642 0.2183 0.0691 0.0051  0.0602  -0.0002 137 LYS B CA  
2823 C C   . LYS B 137 ? 0.0550 0.2439 0.0782 0.0053  0.0586  -0.0104 137 LYS B C   
2824 O O   . LYS B 137 ? 0.0465 0.2895 0.0854 0.0196  0.0544  -0.0115 137 LYS B O   
2825 C CB  . LYS B 137 ? 0.0596 0.2274 0.0762 0.0032  0.0605  -0.0126 137 LYS B CB  
2826 C CG  . LYS B 137 ? 0.0695 0.2381 0.0683 0.0068  0.0614  -0.0164 137 LYS B CG  
2827 C CD  . LYS B 137 ? 0.0760 0.2519 0.0775 -0.0024 0.0702  -0.0137 137 LYS B CD  
2828 C CE  . LYS B 137 ? 0.0726 0.2702 0.0979 -0.0079 0.0672  0.0020  137 LYS B CE  
2829 N NZ  . LYS B 137 ? 0.0834 0.2586 0.1014 -0.0053 0.0814  0.0064  137 LYS B NZ  
2830 N N   . VAL B 138 ? 0.0533 0.2358 0.0589 0.0083  0.0490  -0.0091 138 VAL B N   
2831 C CA  . VAL B 138 ? 0.0560 0.2305 0.0558 -0.0065 0.0491  0.0078  138 VAL B CA  
2832 C C   . VAL B 138 ? 0.0383 0.2300 0.0749 -0.0012 0.0468  -0.0033 138 VAL B C   
2833 O O   . VAL B 138 ? 0.0580 0.2430 0.0635 -0.0082 0.0507  -0.0036 138 VAL B O   
2834 C CB  . VAL B 138 ? 0.0652 0.2460 0.0692 -0.0072 0.0606  0.0050  138 VAL B CB  
2835 C CG1 . VAL B 138 ? 0.0704 0.2632 0.0722 0.0008  0.0649  -0.0051 138 VAL B CG1 
2836 C CG2 . VAL B 138 ? 0.0690 0.2501 0.0758 -0.0067 0.0656  0.0077  138 VAL B CG2 
2837 N N   . ILE B 139 ? 0.0527 0.2331 0.0749 0.0013  0.0563  -0.0025 139 ILE B N   
2838 C CA  . ILE B 139 ? 0.0496 0.2328 0.0646 -0.0003 0.0500  0.0111  139 ILE B CA  
2839 C C   . ILE B 139 ? 0.0489 0.2325 0.0671 -0.0062 0.0508  -0.0053 139 ILE B C   
2840 O O   . ILE B 139 ? 0.0545 0.2594 0.0776 0.0028  0.0584  -0.0084 139 ILE B O   
2841 C CB  . ILE B 139 ? 0.0487 0.2449 0.0612 0.0020  0.0480  0.0126  139 ILE B CB  
2842 C CG1 . ILE B 139 ? 0.0497 0.2580 0.0827 0.0155  0.0502  0.0141  139 ILE B CG1 
2843 C CG2 . ILE B 139 ? 0.0770 0.2519 0.0683 -0.0098 0.0642  0.0206  139 ILE B CG2 
2844 C CD1 . ILE B 139 ? 0.0609 0.2540 0.0800 0.0061  0.0433  0.0044  139 ILE B CD1 
2845 N N   . ILE B 140 ? 0.0580 0.2427 0.0753 -0.0050 0.0597  -0.0092 140 ILE B N   
2846 C CA  . ILE B 140 ? 0.0523 0.2468 0.0851 -0.0032 0.0602  -0.0035 140 ILE B CA  
2847 C C   . ILE B 140 ? 0.0608 0.2481 0.0687 0.0018  0.0523  -0.0044 140 ILE B C   
2848 O O   . ILE B 140 ? 0.0660 0.2672 0.0989 0.0149  0.0638  0.0020  140 ILE B O   
2849 C CB  . ILE B 140 ? 0.0756 0.2549 0.0800 0.0048  0.0669  -0.0090 140 ILE B CB  
2850 C CG1 . ILE B 140 ? 0.0821 0.2629 0.0867 0.0036  0.0777  -0.0101 140 ILE B CG1 
2851 C CG2 . ILE B 140 ? 0.0946 0.2610 0.0918 -0.0037 0.0726  -0.0063 140 ILE B CG2 
2852 C CD1 . ILE B 140 ? 0.0975 0.2806 0.0970 0.0051  0.0897  -0.0209 140 ILE B CD1 
2853 N N   . GLU B 141 ? 0.0575 0.2453 0.0882 0.0028  0.0642  -0.0142 141 GLU B N   
2854 C CA  . GLU B 141 ? 0.0600 0.2481 0.0864 -0.0012 0.0653  -0.0132 141 GLU B CA  
2855 C C   . GLU B 141 ? 0.0576 0.2385 0.0871 0.0094  0.0629  -0.0176 141 GLU B C   
2856 O O   . GLU B 141 ? 0.0557 0.2433 0.0955 0.0044  0.0660  -0.0076 141 GLU B O   
2857 C CB  . GLU B 141 ? 0.0602 0.2549 0.0979 0.0069  0.0629  -0.0023 141 GLU B CB  
2858 C CG  . GLU B 141 ? 0.0484 0.2567 0.1243 0.0089  0.0634  -0.0044 141 GLU B CG  
2859 C CD  . GLU B 141 ? 0.0600 0.2623 0.0848 -0.0013 0.0626  -0.0100 141 GLU B CD  
2860 O OE1 . GLU B 141 ? 0.0944 0.2701 0.0883 0.0009  0.0604  -0.0125 141 GLU B OE1 
2861 O OE2 . GLU B 141 ? 0.0660 0.2697 0.0906 0.0013  0.0608  -0.0158 141 GLU B OE2 
2862 N N   . THR B 142 ? 0.0578 0.2346 0.0895 0.0072  0.0634  -0.0251 142 THR B N   
2863 C CA  . THR B 142 ? 0.0626 0.2386 0.1016 0.0202  0.0624  -0.0394 142 THR B CA  
2864 C C   . THR B 142 ? 0.0678 0.2300 0.1209 0.0150  0.0547  -0.0312 142 THR B C   
2865 O O   . THR B 142 ? 0.0731 0.2530 0.1263 0.0244  0.0652  -0.0264 142 THR B O   
2866 C CB  . THR B 142 ? 0.0712 0.2611 0.1200 0.0100  0.0561  -0.0271 142 THR B CB  
2867 O OG1 . THR B 142 ? 0.0706 0.2637 0.1298 0.0009  0.0373  -0.0113 142 THR B OG1 
2868 C CG2 . THR B 142 ? 0.0678 0.2694 0.1058 0.0081  0.0674  -0.0227 142 THR B CG2 
2869 N N   . GLY B 143 ? 0.0794 0.2311 0.1302 0.0063  0.0418  -0.0200 143 GLY B N   
2870 C CA  . GLY B 143 ? 0.0831 0.2321 0.1432 0.0008  0.0446  -0.0181 143 GLY B CA  
2871 C C   . GLY B 143 ? 0.0865 0.2405 0.1517 0.0222  0.0512  -0.0118 143 GLY B C   
2872 O O   . GLY B 143 ? 0.1276 0.2500 0.2394 0.0122  0.0137  -0.0071 143 GLY B O   
2873 N N   . GLU B 144 ? 0.0739 0.2485 0.1051 0.0180  0.0551  -0.0102 144 GLU B N   
2874 C CA  . GLU B 144 ? 0.0901 0.2524 0.1390 0.0173  0.0402  -0.0025 144 GLU B CA  
2875 C C   . GLU B 144 ? 0.0986 0.2593 0.1313 0.0262  0.0449  -0.0069 144 GLU B C   
2876 O O   . GLU B 144 ? 0.0810 0.2887 0.1823 0.0286  0.0466  0.0053  144 GLU B O   
2877 C CB  . GLU B 144 ? 0.0900 0.2676 0.1341 0.0094  0.0534  0.0028  144 GLU B CB  
2878 C CG  . GLU B 144 ? 0.1040 0.2830 0.1332 0.0040  0.0582  0.0092  144 GLU B CG  
2879 C CD  . GLU B 144 ? 0.1315 0.3123 0.1905 0.0115  0.0426  0.0145  144 GLU B CD  
2880 O OE1 . GLU B 144 ? 0.1326 0.3727 0.2616 0.0393  0.0466  0.0353  144 GLU B OE1 
2881 O OE2 . GLU B 144 ? 0.1995 0.3181 0.2225 0.0084  0.0357  0.0277  144 GLU B OE2 
2882 N N   . LEU B 145 ? 0.0714 0.2670 0.1035 0.0260  0.0636  -0.0055 145 LEU B N   
2883 C CA  . LEU B 145 ? 0.0748 0.2694 0.1168 0.0080  0.0770  -0.0128 145 LEU B CA  
2884 C C   . LEU B 145 ? 0.0689 0.2782 0.1299 0.0189  0.0852  -0.0189 145 LEU B C   
2885 O O   . LEU B 145 ? 0.0708 0.3181 0.1607 0.0257  0.0957  -0.0223 145 LEU B O   
2886 C CB  . LEU B 145 ? 0.0935 0.2727 0.0976 0.0033  0.0892  0.0008  145 LEU B CB  
2887 C CG  . LEU B 145 ? 0.1098 0.2778 0.0983 -0.0085 0.0961  -0.0066 145 LEU B CG  
2888 C CD1 . LEU B 145 ? 0.1476 0.2868 0.0893 0.0030  0.0987  -0.0052 145 LEU B CD1 
2889 C CD2 . LEU B 145 ? 0.1268 0.2889 0.1024 -0.0195 0.0930  -0.0246 145 LEU B CD2 
2890 N N   . LYS B 146 ? 0.1025 0.2838 0.1612 0.0148  0.0891  -0.0299 146 LYS B N   
2891 C CA  . LYS B 146 ? 0.1369 0.3038 0.1728 0.0072  0.0798  -0.0414 146 LYS B CA  
2892 C C   . LYS B 146 ? 0.1593 0.3325 0.1642 0.0114  0.0824  -0.0620 146 LYS B C   
2893 O O   . LYS B 146 ? 0.1753 0.3632 0.1682 0.0177  0.0732  -0.0520 146 LYS B O   
2894 C CB  . LYS B 146 ? 0.1914 0.3182 0.2082 0.0579  0.0916  -0.0249 146 LYS B CB  
2895 C CG  . LYS B 146 ? 0.2783 0.3678 0.2335 0.0564  0.0895  -0.0045 146 LYS B CG  
2896 C CD  . LYS B 146 ? 0.3714 0.3964 0.3296 0.0688  0.0807  0.0261  146 LYS B CD  
2897 C CE  . LYS B 146 ? 0.3704 0.4389 0.3618 0.0566  0.1079  0.0340  146 LYS B CE  
2898 N NZ  . LYS B 146 ? 0.4348 0.4244 0.4803 0.0290  0.0671  0.0466  146 LYS B NZ  
2899 N N   . ASP B 147 ? 0.1563 0.3308 0.1519 0.0298  0.0876  -0.0521 147 ASP B N   
2900 C CA  A ASP B 147 ? 0.1397 0.3286 0.1647 0.0298  0.1005  -0.0455 147 ASP B CA  
2901 C CA  B ASP B 147 ? 0.1427 0.3280 0.1613 0.0328  0.0928  -0.0470 147 ASP B CA  
2902 C C   . ASP B 147 ? 0.1391 0.3224 0.1390 0.0205  0.0903  -0.0466 147 ASP B C   
2903 O O   . ASP B 147 ? 0.1160 0.3269 0.1444 0.0149  0.0934  -0.0435 147 ASP B O   
2904 C CB  A ASP B 147 ? 0.1508 0.3524 0.2175 0.0378  0.0894  -0.0462 147 ASP B CB  
2905 C CB  B ASP B 147 ? 0.1479 0.3523 0.2197 0.0439  0.0732  -0.0454 147 ASP B CB  
2906 C CG  A ASP B 147 ? 0.1817 0.3811 0.2419 0.0336  0.1028  -0.0344 147 ASP B CG  
2907 C CG  B ASP B 147 ? 0.1819 0.3705 0.2653 0.0583  0.0614  -0.0441 147 ASP B CG  
2908 O OD1 A ASP B 147 ? 0.2143 0.4519 0.3070 0.0497  0.1538  -0.0774 147 ASP B OD1 
2909 O OD1 B ASP B 147 ? 0.2655 0.4043 0.2960 0.0601  0.0538  -0.0237 147 ASP B OD1 
2910 O OD2 A ASP B 147 ? 0.2196 0.4103 0.3359 0.0083  0.0561  -0.0181 147 ASP B OD2 
2911 O OD2 B ASP B 147 ? 0.1995 0.4485 0.3628 0.0576  0.0393  -0.0431 147 ASP B OD2 
2912 N N   . GLU B 148 ? 0.1502 0.3257 0.1311 0.0184  0.1090  -0.0510 148 GLU B N   
2913 C CA  . GLU B 148 ? 0.1445 0.3220 0.1292 0.0211  0.1116  -0.0483 148 GLU B CA  
2914 C C   . GLU B 148 ? 0.1218 0.3124 0.1116 0.0194  0.0980  -0.0553 148 GLU B C   
2915 O O   . GLU B 148 ? 0.1297 0.3226 0.1171 0.0353  0.1072  -0.0429 148 GLU B O   
2916 C CB  . GLU B 148 ? 0.1971 0.3295 0.1439 0.0122  0.0919  -0.0561 148 GLU B CB  
2917 C CG  . GLU B 148 ? 0.2323 0.3614 0.1453 0.0188  0.1078  -0.0625 148 GLU B CG  
2918 C CD  . GLU B 148 ? 0.3141 0.4041 0.1853 0.0163  0.0696  -0.0695 148 GLU B CD  
2919 O OE1 . GLU B 148 ? 0.3833 0.4282 0.2729 0.0446  0.0375  -0.1267 148 GLU B OE1 
2920 O OE2 . GLU B 148 ? 0.4350 0.4983 0.1981 0.0075  0.0600  -0.0100 148 GLU B OE2 
2921 N N   . ALA B 149 ? 0.1202 0.3276 0.1461 0.0116  0.1079  -0.0533 149 ALA B N   
2922 C CA  . ALA B 149 ? 0.1210 0.3221 0.1419 0.0067  0.1219  -0.0366 149 ALA B CA  
2923 C C   . ALA B 149 ? 0.0943 0.3033 0.1295 0.0124  0.1024  -0.0201 149 ALA B C   
2924 O O   . ALA B 149 ? 0.1036 0.3205 0.1269 0.0019  0.1079  -0.0122 149 ALA B O   
2925 C CB  . ALA B 149 ? 0.1203 0.3366 0.1637 0.0136  0.1280  -0.0519 149 ALA B CB  
2926 N N   . LEU B 150 ? 0.0886 0.2918 0.1267 0.0073  0.0954  -0.0253 150 LEU B N   
2927 C CA  . LEU B 150 ? 0.0770 0.2837 0.1253 0.0202  0.0851  -0.0272 150 LEU B CA  
2928 C C   . LEU B 150 ? 0.0685 0.2600 0.1040 0.0065  0.0712  -0.0187 150 LEU B C   
2929 O O   . LEU B 150 ? 0.0681 0.2745 0.1070 0.0075  0.0677  -0.0249 150 LEU B O   
2930 C CB  . LEU B 150 ? 0.0839 0.2960 0.1649 0.0444  0.0760  -0.0174 150 LEU B CB  
2931 C CG  . LEU B 150 ? 0.0835 0.3250 0.1970 0.0356  0.0782  -0.0126 150 LEU B CG  
2932 C CD1 . LEU B 150 ? 0.1045 0.3406 0.2122 0.0473  0.0500  -0.0046 150 LEU B CD1 
2933 C CD2 . LEU B 150 ? 0.1208 0.3575 0.2814 0.0221  0.0352  -0.0221 150 LEU B CD2 
2934 N N   . ILE B 151 ? 0.0730 0.2661 0.0969 0.0099  0.0704  -0.0247 151 ILE B N   
2935 C CA  . ILE B 151 ? 0.0787 0.2596 0.0946 0.0178  0.0741  -0.0214 151 ILE B CA  
2936 C C   . ILE B 151 ? 0.0805 0.2710 0.0742 0.0126  0.0683  -0.0245 151 ILE B C   
2937 O O   . ILE B 151 ? 0.0770 0.2755 0.0976 0.0060  0.0799  -0.0096 151 ILE B O   
2938 C CB  . ILE B 151 ? 0.0777 0.2645 0.1019 0.0165  0.0789  -0.0190 151 ILE B CB  
2939 C CG1 . ILE B 151 ? 0.0730 0.2677 0.1246 0.0192  0.0831  -0.0128 151 ILE B CG1 
2940 C CG2 . ILE B 151 ? 0.0833 0.2671 0.0935 0.0115  0.0700  -0.0219 151 ILE B CG2 
2941 C CD1 . ILE B 151 ? 0.1160 0.2727 0.1446 0.0062  0.0855  -0.0041 151 ILE B CD1 
2942 N N   . ARG B 152 ? 0.0870 0.2830 0.0842 0.0166  0.0749  -0.0324 152 ARG B N   
2943 C CA  . ARG B 152 ? 0.0852 0.2864 0.0814 0.0100  0.0750  -0.0233 152 ARG B CA  
2944 C C   . ARG B 152 ? 0.0945 0.2910 0.0736 0.0035  0.0769  -0.0045 152 ARG B C   
2945 O O   . ARG B 152 ? 0.1056 0.3162 0.1057 0.0130  0.0989  -0.0038 152 ARG B O   
2946 C CB  . ARG B 152 ? 0.1017 0.3122 0.0705 0.0027  0.0757  -0.0316 152 ARG B CB  
2947 C CG  . ARG B 152 ? 0.1251 0.3462 0.0816 0.0005  0.0660  -0.0430 152 ARG B CG  
2948 C CD  . ARG B 152 ? 0.1792 0.3933 0.0797 -0.0012 0.0670  -0.0586 152 ARG B CD  
2949 N NE  . ARG B 152 ? 0.2465 0.4610 0.1150 -0.0057 0.0691  -0.0635 152 ARG B NE  
2950 C CZ  . ARG B 152 ? 0.2655 0.4966 0.1097 -0.0110 0.0582  -0.0557 152 ARG B CZ  
2951 N NH1 . ARG B 152 ? 0.2702 0.5843 0.2491 0.0249  0.0170  -0.0809 152 ARG B NH1 
2952 N NH2 . ARG B 152 ? 0.2768 0.5220 0.1885 -0.0638 0.0463  -0.0243 152 ARG B NH2 
2953 N N   . LYS B 153 ? 0.0861 0.2793 0.0973 0.0112  0.0850  0.0008  153 LYS B N   
2954 C CA  . LYS B 153 ? 0.0939 0.2749 0.0941 0.0054  0.0875  -0.0028 153 LYS B CA  
2955 C C   . LYS B 153 ? 0.0656 0.2614 0.0968 -0.0040 0.0732  -0.0005 153 LYS B C   
2956 O O   . LYS B 153 ? 0.0598 0.2883 0.1179 -0.0022 0.0772  0.0011  153 LYS B O   
2957 C CB  . LYS B 153 ? 0.1064 0.2955 0.1153 0.0103  0.1034  -0.0140 153 LYS B CB  
2958 C CG  . LYS B 153 ? 0.1028 0.3421 0.1587 0.0153  0.1112  -0.0151 153 LYS B CG  
2959 C CD  . LYS B 153 ? 0.1346 0.3592 0.2122 -0.0044 0.1058  -0.0062 153 LYS B CD  
2960 C CE  . LYS B 153 ? 0.1992 0.4025 0.1994 -0.0159 0.1136  0.0125  153 LYS B CE  
2961 N NZ  . LYS B 153 ? 0.2596 0.4475 0.2359 -0.0295 0.1266  0.0229  153 LYS B NZ  
2962 N N   . ALA B 154 ? 0.0619 0.2487 0.1003 -0.0001 0.0722  -0.0094 154 ALA B N   
2963 C CA  . ALA B 154 ? 0.0630 0.2486 0.1017 0.0045  0.0724  -0.0214 154 ALA B CA  
2964 C C   . ALA B 154 ? 0.0563 0.2414 0.1038 -0.0104 0.0695  -0.0001 154 ALA B C   
2965 O O   . ALA B 154 ? 0.0739 0.2577 0.0917 -0.0124 0.0759  -0.0139 154 ALA B O   
2966 C CB  . ALA B 154 ? 0.0521 0.2514 0.1118 0.0005  0.0624  -0.0193 154 ALA B CB  
2967 N N   . SER B 155 ? 0.0685 0.2547 0.0877 -0.0036 0.0709  -0.0165 155 SER B N   
2968 C CA  . SER B 155 ? 0.0652 0.2538 0.0911 0.0027  0.0699  -0.0176 155 SER B CA  
2969 C C   . SER B 155 ? 0.0751 0.2554 0.0829 0.0017  0.0719  -0.0162 155 SER B C   
2970 O O   . SER B 155 ? 0.0834 0.2618 0.0822 0.0013  0.0764  -0.0023 155 SER B O   
2971 C CB  . SER B 155 ? 0.0596 0.2614 0.0943 0.0004  0.0680  -0.0157 155 SER B CB  
2972 O OG  . SER B 155 ? 0.0801 0.2631 0.0781 -0.0092 0.0727  -0.0145 155 SER B OG  
2973 N N   . GLU B 156 ? 0.0750 0.2655 0.0933 0.0047  0.0772  -0.0021 156 GLU B N   
2974 C CA  . GLU B 156 ? 0.0969 0.2735 0.0955 -0.0073 0.0847  0.0052  156 GLU B CA  
2975 C C   . GLU B 156 ? 0.0946 0.2689 0.0819 -0.0151 0.0801  0.0134  156 GLU B C   
2976 O O   . GLU B 156 ? 0.0960 0.2795 0.0733 -0.0111 0.0770  0.0054  156 GLU B O   
2977 C CB  . GLU B 156 ? 0.1256 0.3157 0.1170 0.0027  0.1062  -0.0077 156 GLU B CB  
2978 C CG  . GLU B 156 ? 0.1740 0.3702 0.1620 -0.0150 0.1256  -0.0016 156 GLU B CG  
2979 C CD  . GLU B 156 ? 0.2265 0.4361 0.2278 -0.0024 0.1919  0.0350  156 GLU B CD  
2980 O OE1 . GLU B 156 ? 0.2933 0.5383 0.3371 0.0219  0.2101  0.0608  156 GLU B OE1 
2981 O OE2 . GLU B 156 ? 0.3935 0.5891 0.3219 -0.0428 0.2211  0.1392  156 GLU B OE2 
2982 N N   . ILE B 157 ? 0.0882 0.2578 0.0855 -0.0071 0.0801  0.0068  157 ILE B N   
2983 C CA  . ILE B 157 ? 0.0822 0.2576 0.0870 -0.0080 0.0781  -0.0006 157 ILE B CA  
2984 C C   . ILE B 157 ? 0.0727 0.2553 0.0913 -0.0147 0.0748  -0.0038 157 ILE B C   
2985 O O   . ILE B 157 ? 0.0973 0.2582 0.0904 -0.0214 0.0842  0.0071  157 ILE B O   
2986 C CB  . ILE B 157 ? 0.0672 0.2828 0.1023 -0.0108 0.0764  -0.0074 157 ILE B CB  
2987 C CG1 . ILE B 157 ? 0.0736 0.2970 0.1033 -0.0063 0.0806  -0.0187 157 ILE B CG1 
2988 C CG2 . ILE B 157 ? 0.0740 0.2942 0.0998 -0.0119 0.0790  0.0047  157 ILE B CG2 
2989 C CD1 . ILE B 157 ? 0.0746 0.3011 0.1259 -0.0092 0.0696  -0.0229 157 ILE B CD1 
2990 N N   . SER B 158 ? 0.0764 0.2518 0.0912 -0.0045 0.0771  -0.0069 158 SER B N   
2991 C CA  . SER B 158 ? 0.0759 0.2541 0.0840 0.0022  0.0735  -0.0004 158 SER B CA  
2992 C C   . SER B 158 ? 0.0769 0.2478 0.0897 -0.0133 0.0763  -0.0003 158 SER B C   
2993 O O   . SER B 158 ? 0.0875 0.2509 0.0930 -0.0045 0.0635  0.0017  158 SER B O   
2994 C CB  . SER B 158 ? 0.0890 0.2502 0.0766 -0.0004 0.0759  0.0108  158 SER B CB  
2995 O OG  . SER B 158 ? 0.0955 0.2752 0.0696 0.0160  0.0751  0.0140  158 SER B OG  
2996 N N   . ILE B 159 ? 0.0739 0.2600 0.0837 -0.0016 0.0723  0.0007  159 ILE B N   
2997 C CA  . ILE B 159 ? 0.0650 0.2387 0.1019 -0.0036 0.0684  -0.0005 159 ILE B CA  
2998 C C   . ILE B 159 ? 0.0907 0.2374 0.0871 -0.0034 0.0708  0.0137  159 ILE B C   
2999 O O   . ILE B 159 ? 0.1128 0.2397 0.0973 -0.0031 0.0723  0.0081  159 ILE B O   
3000 C CB  . ILE B 159 ? 0.0819 0.2479 0.1113 -0.0040 0.0620  0.0001  159 ILE B CB  
3001 C CG1 . ILE B 159 ? 0.0990 0.2464 0.1353 -0.0025 0.0477  -0.0045 159 ILE B CG1 
3002 C CG2 . ILE B 159 ? 0.0925 0.2492 0.1133 -0.0140 0.0587  0.0119  159 ILE B CG2 
3003 C CD1 . ILE B 159 ? 0.1212 0.2581 0.1546 -0.0038 0.0322  -0.0085 159 ILE B CD1 
3004 N N   . LYS B 160 ? 0.0910 0.2584 0.0828 -0.0124 0.0765  0.0016  160 LYS B N   
3005 C CA  . LYS B 160 ? 0.1239 0.2642 0.1071 -0.0191 0.0765  0.0108  160 LYS B CA  
3006 C C   . LYS B 160 ? 0.0943 0.2421 0.1064 -0.0284 0.0785  0.0110  160 LYS B C   
3007 O O   . LYS B 160 ? 0.1531 0.2616 0.1220 -0.0234 0.0896  0.0104  160 LYS B O   
3008 C CB  . LYS B 160 ? 0.1165 0.2982 0.1274 -0.0289 0.0772  0.0169  160 LYS B CB  
3009 C CG  . LYS B 160 ? 0.1587 0.3525 0.1578 -0.0166 0.0938  -0.0005 160 LYS B CG  
3010 C CD  . LYS B 160 ? 0.1900 0.4121 0.2319 -0.0273 0.1291  0.0132  160 LYS B CD  
3011 C CE  . LYS B 160 ? 0.2948 0.4673 0.2804 -0.0135 0.1212  0.0036  160 LYS B CE  
3012 N NZ  . LYS B 160 ? 0.3261 0.4965 0.3883 0.0176  0.1354  0.0063  160 LYS B NZ  
3013 N N   . ALA B 161 ? 0.1077 0.2507 0.0969 -0.0283 0.0822  0.0069  161 ALA B N   
3014 C CA  . ALA B 161 ? 0.1045 0.2531 0.1197 -0.0144 0.0686  -0.0188 161 ALA B CA  
3015 C C   . ALA B 161 ? 0.1212 0.2569 0.1113 -0.0078 0.0775  -0.0217 161 ALA B C   
3016 O O   . ALA B 161 ? 0.1368 0.2994 0.1330 -0.0047 0.0773  -0.0453 161 ALA B O   
3017 C CB  . ALA B 161 ? 0.1211 0.2672 0.1319 -0.0124 0.0745  -0.0239 161 ALA B CB  
3018 N N   . GLY B 162 ? 0.1112 0.2554 0.1028 0.0006  0.0835  -0.0242 162 GLY B N   
3019 C CA  . GLY B 162 ? 0.1205 0.2476 0.1180 0.0019  0.0805  -0.0216 162 GLY B CA  
3020 C C   . GLY B 162 ? 0.1165 0.2517 0.1034 -0.0006 0.0635  -0.0152 162 GLY B C   
3021 O O   . GLY B 162 ? 0.1261 0.2780 0.1363 0.0020  0.0882  -0.0186 162 GLY B O   
3022 N N   . ALA B 163 ? 0.0649 0.2525 0.0852 -0.0042 0.0586  0.0028  163 ALA B N   
3023 C CA  . ALA B 163 ? 0.0862 0.2489 0.0772 -0.0064 0.0518  0.0025  163 ALA B CA  
3024 C C   . ALA B 163 ? 0.0720 0.2455 0.0660 0.0064  0.0625  -0.0016 163 ALA B C   
3025 O O   . ALA B 163 ? 0.0855 0.2660 0.0652 0.0095  0.0681  0.0062  163 ALA B O   
3026 C CB  . ALA B 163 ? 0.0861 0.2557 0.1029 -0.0018 0.0535  0.0127  163 ALA B CB  
3027 N N   . ASP B 164 ? 0.0809 0.2510 0.0611 0.0075  0.0636  -0.0056 164 ASP B N   
3028 C CA  . ASP B 164 ? 0.0908 0.2473 0.0603 0.0079  0.0674  -0.0011 164 ASP B CA  
3029 C C   . ASP B 164 ? 0.0840 0.2442 0.0646 0.0085  0.0672  0.0018  164 ASP B C   
3030 O O   . ASP B 164 ? 0.0781 0.2578 0.0824 0.0128  0.0531  0.0067  164 ASP B O   
3031 C CB  . ASP B 164 ? 0.0937 0.2430 0.0623 0.0147  0.0689  0.0017  164 ASP B CB  
3032 C CG  . ASP B 164 ? 0.1206 0.2552 0.0957 0.0069  0.0657  0.0110  164 ASP B CG  
3033 O OD1 . ASP B 164 ? 0.1762 0.2769 0.1110 0.0000  0.0839  0.0245  164 ASP B OD1 
3034 O OD2 . ASP B 164 ? 0.1473 0.2774 0.1021 0.0174  0.0877  0.0096  164 ASP B OD2 
3035 N N   . PHE B 165 ? 0.0677 0.2494 0.0734 0.0184  0.0603  -0.0051 165 PHE B N   
3036 C CA  . PHE B 165 ? 0.0587 0.2444 0.0681 0.0121  0.0567  0.0047  165 PHE B CA  
3037 C C   . PHE B 165 ? 0.0668 0.2410 0.0580 0.0175  0.0546  -0.0072 165 PHE B C   
3038 O O   . PHE B 165 ? 0.0625 0.2518 0.0731 0.0177  0.0583  -0.0208 165 PHE B O   
3039 C CB  . PHE B 165 ? 0.0729 0.2542 0.0774 0.0066  0.0688  0.0070  165 PHE B CB  
3040 C CG  . PHE B 165 ? 0.0783 0.2719 0.0823 -0.0029 0.0732  0.0165  165 PHE B CG  
3041 C CD1 . PHE B 165 ? 0.0668 0.2783 0.1596 -0.0044 0.0780  0.0170  165 PHE B CD1 
3042 C CD2 . PHE B 165 ? 0.0853 0.2952 0.0814 -0.0102 0.0760  0.0134  165 PHE B CD2 
3043 C CE1 . PHE B 165 ? 0.0721 0.3049 0.1851 0.0168  0.0520  0.0258  165 PHE B CE1 
3044 C CE2 . PHE B 165 ? 0.0878 0.3115 0.0979 -0.0079 0.0612  0.0223  165 PHE B CE2 
3045 C CZ  . PHE B 165 ? 0.0564 0.3127 0.1553 0.0089  0.0551  0.0313  165 PHE B CZ  
3046 N N   . ILE B 166 ? 0.0740 0.2209 0.0577 0.0091  0.0531  -0.0076 166 ILE B N   
3047 C CA  . ILE B 166 ? 0.0688 0.2274 0.0535 0.0107  0.0533  -0.0108 166 ILE B CA  
3048 C C   . ILE B 166 ? 0.0640 0.2288 0.0540 0.0038  0.0516  -0.0151 166 ILE B C   
3049 O O   . ILE B 166 ? 0.0594 0.2501 0.0778 -0.0149 0.0541  -0.0041 166 ILE B O   
3050 C CB  . ILE B 166 ? 0.0810 0.2442 0.0700 0.0132  0.0672  -0.0151 166 ILE B CB  
3051 C CG1 . ILE B 166 ? 0.0884 0.2430 0.0628 0.0062  0.0676  -0.0093 166 ILE B CG1 
3052 C CG2 . ILE B 166 ? 0.1082 0.2490 0.0791 0.0112  0.0563  -0.0078 166 ILE B CG2 
3053 C CD1 . ILE B 166 ? 0.1158 0.2607 0.0596 0.0077  0.0754  -0.0135 166 ILE B CD1 
3054 N N   . LYS B 167 ? 0.0584 0.2275 0.0811 -0.0029 0.0404  -0.0049 167 LYS B N   
3055 C CA  . LYS B 167 ? 0.0661 0.2254 0.0787 -0.0015 0.0382  -0.0024 167 LYS B CA  
3056 C C   . LYS B 167 ? 0.0570 0.2223 0.0683 -0.0050 0.0487  -0.0007 167 LYS B C   
3057 O O   . LYS B 167 ? 0.0601 0.2360 0.0733 -0.0105 0.0404  -0.0087 167 LYS B O   
3058 C CB  . LYS B 167 ? 0.0451 0.2515 0.0897 0.0061  0.0493  -0.0050 167 LYS B CB  
3059 C CG  . LYS B 167 ? 0.0539 0.2673 0.1044 0.0006  0.0608  -0.0076 167 LYS B CG  
3060 C CD  . LYS B 167 ? 0.0654 0.2832 0.1113 0.0064  0.0696  -0.0113 167 LYS B CD  
3061 C CE  . LYS B 167 ? 0.0983 0.3106 0.1439 -0.0249 0.0886  -0.0122 167 LYS B CE  
3062 N NZ  . LYS B 167 ? 0.1467 0.3417 0.1759 -0.0210 0.1111  -0.0267 167 LYS B NZ  
3063 N N   . THR B 168 ? 0.0475 0.2205 0.0833 -0.0079 0.0562  -0.0051 168 THR B N   
3064 C CA  . THR B 168 ? 0.0617 0.2233 0.0914 -0.0043 0.0581  -0.0017 168 THR B CA  
3065 C C   . THR B 168 ? 0.0553 0.2256 0.0817 0.0076  0.0574  -0.0174 168 THR B C   
3066 O O   . THR B 168 ? 0.0554 0.2672 0.0999 0.0035  0.0540  -0.0048 168 THR B O   
3067 C CB  . THR B 168 ? 0.0652 0.2373 0.0797 -0.0178 0.0655  -0.0092 168 THR B CB  
3068 O OG1 . THR B 168 ? 0.0566 0.2413 0.1013 -0.0174 0.0691  -0.0172 168 THR B OG1 
3069 C CG2 . THR B 168 ? 0.0683 0.2460 0.0898 -0.0287 0.0554  0.0069  168 THR B CG2 
3070 N N   . SER B 169 ? 0.0458 0.2270 0.0882 0.0131  0.0556  -0.0092 169 SER B N   
3071 C CA  . SER B 169 ? 0.0573 0.2277 0.0880 0.0121  0.0570  -0.0054 169 SER B CA  
3072 C C   . SER B 169 ? 0.0586 0.2341 0.0892 0.0196  0.0561  -0.0045 169 SER B C   
3073 O O   . SER B 169 ? 0.0513 0.2375 0.1172 0.0151  0.0607  0.0068  169 SER B O   
3074 C CB  . SER B 169 ? 0.0732 0.2333 0.1030 0.0117  0.0456  -0.0152 169 SER B CB  
3075 O OG  . SER B 169 ? 0.0915 0.2474 0.1105 0.0056  0.0525  -0.0144 169 SER B OG  
3076 N N   . THR B 170 ? 0.0594 0.2394 0.0831 0.0099  0.0637  0.0020  170 THR B N   
3077 C CA  . THR B 170 ? 0.0883 0.2337 0.0790 0.0061  0.0771  -0.0006 170 THR B CA  
3078 C C   . THR B 170 ? 0.0912 0.2485 0.1202 -0.0009 0.0779  0.0045  170 THR B C   
3079 O O   . THR B 170 ? 0.1001 0.3034 0.1447 -0.0159 0.1042  -0.0062 170 THR B O   
3080 C CB  . THR B 170 ? 0.1025 0.2331 0.0707 -0.0005 0.0716  0.0145  170 THR B CB  
3081 O OG1 . THR B 170 ? 0.1092 0.2329 0.0908 0.0088  0.0477  0.0234  170 THR B OG1 
3082 C CG2 . THR B 170 ? 0.0987 0.2318 0.0899 0.0055  0.0732  0.0159  170 THR B CG2 
3083 N N   . GLY B 171 ? 0.0959 0.2533 0.1105 -0.0111 0.0869  -0.0007 171 GLY B N   
3084 C CA  . GLY B 171 ? 0.1078 0.2661 0.1430 -0.0175 0.0810  0.0041  171 GLY B CA  
3085 C C   . GLY B 171 ? 0.1184 0.2816 0.1495 -0.0291 0.0841  0.0257  171 GLY B C   
3086 O O   . GLY B 171 ? 0.1948 0.3111 0.2233 -0.0639 0.0584  0.0590  171 GLY B O   
3087 N N   . ARG B 172 ? 0.1245 0.2666 0.1298 -0.0179 0.0817  0.0162  172 ARG B N   
3088 C CA  . ARG B 172 ? 0.1716 0.2798 0.1405 -0.0020 0.0722  0.0319  172 ARG B CA  
3089 C C   . ARG B 172 ? 0.2005 0.2951 0.1236 0.0178  0.0586  0.0347  172 ARG B C   
3090 O O   . ARG B 172 ? 0.2465 0.4093 0.1337 0.0459  0.0498  0.0461  172 ARG B O   
3091 C CB  . ARG B 172 ? 0.2107 0.2939 0.1401 0.0035  0.0545  0.0328  172 ARG B CB  
3092 C CG  . ARG B 172 ? 0.2456 0.3031 0.1555 0.0037  0.0740  0.0157  172 ARG B CG  
3093 C CD  . ARG B 172 ? 0.3210 0.3434 0.1812 -0.0183 0.0725  0.0306  172 ARG B CD  
3094 N NE  . ARG B 172 ? 0.4022 0.4362 0.2959 -0.0220 0.0555  0.0374  172 ARG B NE  
3095 C CZ  . ARG B 172 ? 0.4405 0.4861 0.2812 -0.0154 0.0571  0.0209  172 ARG B CZ  
3096 N NH1 . ARG B 172 ? 0.4918 0.4502 0.3203 0.0189  0.0456  0.0556  172 ARG B NH1 
3097 N NH2 . ARG B 172 ? 0.4296 0.5560 0.3250 -0.0363 0.0570  0.0259  172 ARG B NH2 
3098 N N   . VAL B 173 ? 0.1703 0.2730 0.1194 0.0272  0.0665  0.0203  173 VAL B N   
3099 C CA  . VAL B 173 ? 0.1750 0.2747 0.1477 0.0234  0.0537  0.0215  173 VAL B CA  
3100 C C   . VAL B 173 ? 0.1740 0.2509 0.1369 0.0247  0.0472  0.0327  173 VAL B C   
3101 O O   . VAL B 173 ? 0.1616 0.2827 0.1690 0.0141  0.0478  0.0158  173 VAL B O   
3102 C CB  . VAL B 173 ? 0.1637 0.2806 0.1615 0.0165  0.0591  0.0077  173 VAL B CB  
3103 C CG1 . VAL B 173 ? 0.1625 0.2981 0.1864 0.0185  0.0394  0.0115  173 VAL B CG1 
3104 C CG2 . VAL B 173 ? 0.2031 0.2744 0.1524 0.0036  0.0755  0.0149  173 VAL B CG2 
3105 N N   . ALA B 174 ? 0.2004 0.2647 0.1727 0.0349  0.0493  0.0179  174 ALA B N   
3106 C CA  . ALA B 174 ? 0.2336 0.2670 0.1804 0.0290  0.0256  0.0057  174 ALA B CA  
3107 C C   . ALA B 174 ? 0.1965 0.2435 0.1654 0.0089  0.0377  0.0092  174 ALA B C   
3108 O O   . ALA B 174 ? 0.2090 0.2819 0.1608 -0.0228 0.0662  -0.0104 174 ALA B O   
3109 C CB  . ALA B 174 ? 0.2638 0.2667 0.2270 0.0489  0.0183  -0.0191 174 ALA B CB  
3110 N N   . VAL B 175 ? 0.1551 0.2286 0.1540 0.0202  0.0297  0.0070  175 VAL B N   
3111 C CA  . VAL B 175 ? 0.1045 0.2281 0.1507 0.0015  0.0465  -0.0069 175 VAL B CA  
3112 C C   . VAL B 175 ? 0.1026 0.2331 0.1183 0.0131  0.0578  -0.0084 175 VAL B C   
3113 O O   . VAL B 175 ? 0.1349 0.2413 0.1212 0.0034  0.0506  -0.0059 175 VAL B O   
3114 C CB  . VAL B 175 ? 0.0955 0.2418 0.1541 0.0068  0.0468  -0.0132 175 VAL B CB  
3115 C CG1 . VAL B 175 ? 0.0823 0.2636 0.1370 0.0113  0.0643  -0.0215 175 VAL B CG1 
3116 C CG2 . VAL B 175 ? 0.0858 0.2581 0.1904 0.0189  0.0445  -0.0190 175 VAL B CG2 
3117 N N   . ASN B 176 ? 0.0966 0.2506 0.1245 0.0080  0.0471  0.0009  176 ASN B N   
3118 C CA  . ASN B 176 ? 0.1110 0.2541 0.1115 0.0164  0.0640  0.0066  176 ASN B CA  
3119 C C   . ASN B 176 ? 0.1208 0.2537 0.1058 0.0253  0.0577  -0.0061 176 ASN B C   
3120 O O   . ASN B 176 ? 0.1176 0.2850 0.1312 0.0238  0.0669  -0.0171 176 ASN B O   
3121 C CB  . ASN B 176 ? 0.1308 0.2705 0.1159 0.0255  0.0782  0.0252  176 ASN B CB  
3122 C CG  . ASN B 176 ? 0.1681 0.2851 0.1247 0.0045  0.0735  0.0427  176 ASN B CG  
3123 O OD1 . ASN B 176 ? 0.2841 0.3538 0.2125 -0.0071 0.0913  0.0716  176 ASN B OD1 
3124 N ND2 . ASN B 176 ? 0.1625 0.2848 0.0967 0.0292  0.0866  0.0408  176 ASN B ND2 
3125 N N   . ALA B 177 ? 0.1040 0.2523 0.0874 0.0064  0.0650  -0.0043 177 ALA B N   
3126 C CA  . ALA B 177 ? 0.0862 0.2565 0.0991 -0.0012 0.0549  0.0023  177 ALA B CA  
3127 C C   . ALA B 177 ? 0.0849 0.2482 0.1139 -0.0059 0.0640  0.0064  177 ALA B C   
3128 O O   . ALA B 177 ? 0.1215 0.2573 0.1215 -0.0165 0.0744  0.0048  177 ALA B O   
3129 C CB  . ALA B 177 ? 0.0986 0.2540 0.1131 0.0039  0.0476  -0.0040 177 ALA B CB  
3130 N N   . THR B 178 ? 0.0986 0.2382 0.1091 -0.0075 0.0698  -0.0010 178 THR B N   
3131 C CA  . THR B 178 ? 0.1099 0.2386 0.1150 -0.0016 0.0697  -0.0002 178 THR B CA  
3132 C C   . THR B 178 ? 0.1250 0.2360 0.1193 0.0071  0.0609  -0.0153 178 THR B C   
3133 O O   . THR B 178 ? 0.1005 0.2481 0.0781 0.0059  0.0564  -0.0218 178 THR B O   
3134 C CB  . THR B 178 ? 0.1394 0.2345 0.1589 0.0233  0.0673  0.0097  178 THR B CB  
3135 O OG1 . THR B 178 ? 0.1856 0.2883 0.1359 0.0196  0.0965  0.0293  178 THR B OG1 
3136 C CG2 . THR B 178 ? 0.1574 0.2500 0.1793 0.0340  0.0614  0.0111  178 THR B CG2 
3137 N N   . PRO B 179 ? 0.1473 0.2723 0.1271 -0.0178 0.0545  -0.0128 179 PRO B N   
3138 C CA  . PRO B 179 ? 0.1266 0.2750 0.1111 -0.0171 0.0592  -0.0224 179 PRO B CA  
3139 C C   . PRO B 179 ? 0.1276 0.2734 0.0995 -0.0180 0.0471  -0.0227 179 PRO B C   
3140 O O   . PRO B 179 ? 0.1218 0.2899 0.1123 0.0008  0.0566  -0.0201 179 PRO B O   
3141 C CB  . PRO B 179 ? 0.1473 0.3053 0.1240 -0.0293 0.0594  -0.0240 179 PRO B CB  
3142 C CG  . PRO B 179 ? 0.1950 0.2990 0.1413 -0.0285 0.0459  -0.0175 179 PRO B CG  
3143 C CD  . PRO B 179 ? 0.1767 0.2762 0.1296 -0.0106 0.0519  -0.0217 179 PRO B CD  
3144 N N   . GLU B 180 ? 0.1371 0.2721 0.1209 -0.0102 0.0457  -0.0201 180 GLU B N   
3145 C CA  . GLU B 180 ? 0.1409 0.2932 0.1361 -0.0058 0.0565  -0.0049 180 GLU B CA  
3146 C C   . GLU B 180 ? 0.1006 0.2801 0.1140 0.0017  0.0619  -0.0032 180 GLU B C   
3147 O O   . GLU B 180 ? 0.1133 0.2794 0.1194 0.0072  0.0779  -0.0052 180 GLU B O   
3148 C CB  . GLU B 180 ? 0.1970 0.3218 0.1941 0.0173  0.0422  0.0078  180 GLU B CB  
3149 C CG  . GLU B 180 ? 0.2762 0.4109 0.2659 -0.0002 0.0661  0.0322  180 GLU B CG  
3150 C CD  . GLU B 180 ? 0.3738 0.4794 0.3597 0.0301  0.1534  0.0416  180 GLU B CD  
3151 O OE1 . GLU B 180 ? 0.5663 0.5352 0.4875 0.0195  0.1603  0.0670  180 GLU B OE1 
3152 O OE2 . GLU B 180 ? 0.4298 0.6304 0.3809 0.0033  0.2266  0.0229  180 GLU B OE2 
3153 N N   . SER B 181 ? 0.1103 0.2841 0.1061 -0.0128 0.0637  -0.0013 181 SER B N   
3154 C CA  A SER B 181 ? 0.1137 0.2800 0.0823 -0.0209 0.0655  -0.0052 181 SER B CA  
3155 C CA  B SER B 181 ? 0.1351 0.2928 0.1079 -0.0088 0.0587  -0.0088 181 SER B CA  
3156 C C   . SER B 181 ? 0.1078 0.2710 0.0773 -0.0221 0.0629  -0.0203 181 SER B C   
3157 O O   . SER B 181 ? 0.1117 0.2838 0.0760 -0.0239 0.0713  -0.0182 181 SER B O   
3158 C CB  A SER B 181 ? 0.0980 0.2773 0.0861 -0.0327 0.0637  0.0021  181 SER B CB  
3159 C CB  B SER B 181 ? 0.1603 0.3160 0.1228 -0.0014 0.0452  0.0063  181 SER B CB  
3160 O OG  A SER B 181 ? 0.0867 0.2828 0.0796 -0.0400 0.0643  -0.0182 181 SER B OG  
3161 O OG  B SER B 181 ? 0.1523 0.3585 0.1723 0.0177  0.0463  0.0016  181 SER B OG  
3162 N N   . ALA B 182 ? 0.1103 0.2638 0.0941 -0.0225 0.0616  -0.0149 182 ALA B N   
3163 C CA  . ALA B 182 ? 0.1171 0.2544 0.1110 -0.0104 0.0641  -0.0179 182 ALA B CA  
3164 C C   . ALA B 182 ? 0.0964 0.2530 0.1192 0.0030  0.0522  -0.0222 182 ALA B C   
3165 O O   . ALA B 182 ? 0.1043 0.2484 0.1078 -0.0007 0.0826  -0.0219 182 ALA B O   
3166 C CB  . ALA B 182 ? 0.1160 0.2577 0.1102 -0.0083 0.0702  -0.0265 182 ALA B CB  
3167 N N   . ARG B 183 ? 0.0800 0.2607 0.1006 0.0036  0.0594  -0.0202 183 ARG B N   
3168 C CA  . ARG B 183 ? 0.1148 0.2751 0.1009 -0.0072 0.0485  -0.0174 183 ARG B CA  
3169 C C   . ARG B 183 ? 0.0956 0.2556 0.0852 0.0034  0.0654  -0.0265 183 ARG B C   
3170 O O   . ARG B 183 ? 0.1086 0.2755 0.0744 0.0077  0.0681  -0.0095 183 ARG B O   
3171 C CB  . ARG B 183 ? 0.1349 0.2970 0.1065 -0.0136 0.0483  -0.0326 183 ARG B CB  
3172 C CG  . ARG B 183 ? 0.1880 0.3311 0.1128 -0.0118 0.0562  -0.0195 183 ARG B CG  
3173 C CD  . ARG B 183 ? 0.2871 0.3721 0.1289 0.0152  0.0703  -0.0399 183 ARG B CD  
3174 N NE  . ARG B 183 ? 0.3351 0.4446 0.1719 0.0401  0.0755  -0.0836 183 ARG B NE  
3175 C CZ  . ARG B 183 ? 0.4008 0.4654 0.1672 0.0190  0.0534  -0.1220 183 ARG B CZ  
3176 N NH1 . ARG B 183 ? 0.3786 0.4945 0.2794 -0.0364 0.1054  -0.1019 183 ARG B NH1 
3177 N NH2 . ARG B 183 ? 0.4785 0.5256 0.2703 0.0709  0.0469  -0.1280 183 ARG B NH2 
3178 N N   . ILE B 184 ? 0.1003 0.2539 0.0743 -0.0050 0.0661  -0.0268 184 ILE B N   
3179 C CA  . ILE B 184 ? 0.1091 0.2583 0.0670 -0.0108 0.0788  -0.0163 184 ILE B CA  
3180 C C   . ILE B 184 ? 0.0994 0.2584 0.0688 -0.0120 0.0762  -0.0036 184 ILE B C   
3181 O O   . ILE B 184 ? 0.1018 0.2777 0.0846 -0.0111 0.0864  -0.0041 184 ILE B O   
3182 C CB  . ILE B 184 ? 0.0974 0.2748 0.0931 -0.0002 0.0873  -0.0183 184 ILE B CB  
3183 C CG1 . ILE B 184 ? 0.1163 0.2872 0.1180 0.0023  0.0863  -0.0207 184 ILE B CG1 
3184 C CG2 . ILE B 184 ? 0.1054 0.2864 0.0846 -0.0055 0.0861  -0.0152 184 ILE B CG2 
3185 C CD1 . ILE B 184 ? 0.1082 0.2993 0.1465 0.0192  0.0913  -0.0219 184 ILE B CD1 
3186 N N   . MET B 185 ? 0.0816 0.2432 0.0695 -0.0091 0.0689  -0.0048 185 MET B N   
3187 C CA  . MET B 185 ? 0.0845 0.2479 0.0659 -0.0060 0.0682  -0.0065 185 MET B CA  
3188 C C   . MET B 185 ? 0.1056 0.2476 0.0574 0.0018  0.0704  -0.0156 185 MET B C   
3189 O O   . MET B 185 ? 0.1139 0.2482 0.0592 0.0064  0.0668  -0.0075 185 MET B O   
3190 C CB  . MET B 185 ? 0.0863 0.2522 0.0647 0.0018  0.0683  0.0040  185 MET B CB  
3191 C CG  . MET B 185 ? 0.0771 0.2491 0.0656 0.0003  0.0648  -0.0003 185 MET B CG  
3192 S SD  . MET B 185 ? 0.0866 0.2768 0.0754 0.0128  0.0736  0.0088  185 MET B SD  
3193 C CE  . MET B 185 ? 0.0717 0.3045 0.0971 0.0274  0.0715  0.0004  185 MET B CE  
3194 N N   . MET B 186 ? 0.0986 0.2699 0.0653 -0.0020 0.0738  -0.0045 186 MET B N   
3195 C CA  . MET B 186 ? 0.1045 0.2707 0.0652 0.0046  0.0584  -0.0047 186 MET B CA  
3196 C C   . MET B 186 ? 0.1066 0.2617 0.0674 -0.0001 0.0572  -0.0036 186 MET B C   
3197 O O   . MET B 186 ? 0.0819 0.2757 0.0815 -0.0030 0.0747  0.0086  186 MET B O   
3198 C CB  . MET B 186 ? 0.1084 0.3036 0.0614 -0.0089 0.0636  -0.0066 186 MET B CB  
3199 C CG  . MET B 186 ? 0.0977 0.3515 0.0739 -0.0121 0.0677  -0.0097 186 MET B CG  
3200 S SD  . MET B 186 ? 0.0970 0.4025 0.1235 -0.0154 0.0715  0.0197  186 MET B SD  
3201 C CE  . MET B 186 ? 0.1524 0.3820 0.1385 -0.0126 0.0605  0.0003  186 MET B CE  
3202 N N   . GLU B 187 ? 0.1154 0.2633 0.0682 -0.0035 0.0816  0.0114  187 GLU B N   
3203 C CA  . GLU B 187 ? 0.1292 0.2766 0.0670 -0.0118 0.0861  0.0007  187 GLU B CA  
3204 C C   . GLU B 187 ? 0.1185 0.2756 0.0653 -0.0032 0.0812  0.0037  187 GLU B C   
3205 O O   . GLU B 187 ? 0.1277 0.2838 0.0606 -0.0169 0.0712  0.0160  187 GLU B O   
3206 C CB  . GLU B 187 ? 0.1266 0.2966 0.0941 -0.0043 0.0916  -0.0118 187 GLU B CB  
3207 C CG  . GLU B 187 ? 0.1619 0.3111 0.1050 -0.0162 0.1220  -0.0224 187 GLU B CG  
3208 C CD  . GLU B 187 ? 0.2141 0.3423 0.1754 -0.0056 0.1212  -0.0494 187 GLU B CD  
3209 O OE1 . GLU B 187 ? 0.2622 0.4216 0.3217 0.0304  0.1007  -0.1016 187 GLU B OE1 
3210 O OE2 . GLU B 187 ? 0.3076 0.4011 0.1730 -0.0138 0.1075  -0.0691 187 GLU B OE2 
3211 N N   . VAL B 188 ? 0.1241 0.2809 0.0591 -0.0086 0.0788  -0.0055 188 VAL B N   
3212 C CA  . VAL B 188 ? 0.1101 0.2689 0.0616 -0.0055 0.0757  -0.0009 188 VAL B CA  
3213 C C   . VAL B 188 ? 0.0965 0.2592 0.0689 -0.0136 0.0664  0.0071  188 VAL B C   
3214 O O   . VAL B 188 ? 0.1155 0.2634 0.0773 -0.0023 0.0712  0.0132  188 VAL B O   
3215 C CB  . VAL B 188 ? 0.1072 0.2770 0.0727 -0.0005 0.0711  0.0080  188 VAL B CB  
3216 C CG1 . VAL B 188 ? 0.1286 0.2805 0.0578 -0.0003 0.0639  -0.0046 188 VAL B CG1 
3217 C CG2 . VAL B 188 ? 0.1192 0.2809 0.0651 0.0015  0.0761  0.0115  188 VAL B CG2 
3218 N N   . ILE B 189 ? 0.0985 0.2573 0.0599 -0.0110 0.0673  0.0127  189 ILE B N   
3219 C CA  . ILE B 189 ? 0.0991 0.2711 0.0621 -0.0009 0.0717  0.0095  189 ILE B CA  
3220 C C   . ILE B 189 ? 0.0938 0.2749 0.0668 0.0013  0.0725  0.0117  189 ILE B C   
3221 O O   . ILE B 189 ? 0.1189 0.2874 0.0743 0.0079  0.0615  0.0087  189 ILE B O   
3222 C CB  . ILE B 189 ? 0.0960 0.2761 0.0599 0.0082  0.0693  0.0113  189 ILE B CB  
3223 C CG1 . ILE B 189 ? 0.1109 0.2710 0.0568 0.0025  0.0725  0.0091  189 ILE B CG1 
3224 C CG2 . ILE B 189 ? 0.1133 0.2918 0.0577 0.0163  0.0706  0.0179  189 ILE B CG2 
3225 C CD1 . ILE B 189 ? 0.1067 0.2755 0.0673 -0.0048 0.0680  0.0130  189 ILE B CD1 
3226 N N   . ARG B 190 ? 0.1089 0.2831 0.0623 -0.0098 0.0749  0.0123  190 ARG B N   
3227 C CA  . ARG B 190 ? 0.1258 0.3121 0.0613 -0.0073 0.0803  0.0121  190 ARG B CA  
3228 C C   . ARG B 190 ? 0.1309 0.3024 0.0604 -0.0052 0.0812  0.0154  190 ARG B C   
3229 O O   . ARG B 190 ? 0.1410 0.3185 0.0786 -0.0026 0.0711  0.0292  190 ARG B O   
3230 C CB  . ARG B 190 ? 0.1830 0.3449 0.0905 -0.0172 0.0775  0.0188  190 ARG B CB  
3231 C CG  . ARG B 190 ? 0.2729 0.4317 0.1169 -0.0074 0.0519  0.0156  190 ARG B CG  
3232 C CD  . ARG B 190 ? 0.3526 0.5240 0.1734 0.0183  0.0827  0.0069  190 ARG B CD  
3233 N NE  . ARG B 190 ? 0.3566 0.5706 0.1769 -0.0288 0.1634  -0.0101 190 ARG B NE  
3234 C CZ  . ARG B 190 ? 0.4277 0.5885 0.2881 -0.0657 0.1746  -0.0389 190 ARG B CZ  
3235 N NH1 . ARG B 190 ? 0.4589 0.6285 0.3835 -0.1286 0.1674  -0.0697 190 ARG B NH1 
3236 N NH2 . ARG B 190 ? 0.4307 0.6196 0.2937 -0.0793 0.1672  -0.0380 190 ARG B NH2 
3237 N N   . ASP B 191 ? 0.1340 0.2947 0.0520 -0.0042 0.0754  0.0154  191 ASP B N   
3238 C CA  . ASP B 191 ? 0.1488 0.3082 0.0653 -0.0044 0.0905  0.0186  191 ASP B CA  
3239 C C   . ASP B 191 ? 0.1243 0.3052 0.0611 -0.0156 0.0770  0.0263  191 ASP B C   
3240 O O   . ASP B 191 ? 0.1186 0.3242 0.0917 -0.0346 0.0909  0.0320  191 ASP B O   
3241 C CB  . ASP B 191 ? 0.1449 0.3285 0.0766 0.0003  0.0980  0.0174  191 ASP B CB  
3242 C CG  . ASP B 191 ? 0.1976 0.3533 0.0964 0.0145  0.1041  0.0198  191 ASP B CG  
3243 O OD1 . ASP B 191 ? 0.2555 0.4026 0.1100 -0.0030 0.0922  -0.0134 191 ASP B OD1 
3244 O OD2 . ASP B 191 ? 0.2482 0.3816 0.1750 0.0424  0.1260  0.0188  191 ASP B OD2 
3245 N N   . MET B 192 ? 0.1128 0.3008 0.0687 -0.0001 0.0805  0.0211  192 MET B N   
3246 C CA  . MET B 192 ? 0.1149 0.2866 0.0822 -0.0083 0.0893  0.0185  192 MET B CA  
3247 C C   . MET B 192 ? 0.1275 0.2691 0.0639 -0.0127 0.0766  0.0197  192 MET B C   
3248 O O   . MET B 192 ? 0.1291 0.2845 0.1179 -0.0062 0.0689  0.0308  192 MET B O   
3249 C CB  . MET B 192 ? 0.1373 0.2816 0.0668 -0.0109 0.0888  0.0013  192 MET B CB  
3250 C CG  . MET B 192 ? 0.1442 0.2906 0.0800 -0.0140 0.0950  0.0040  192 MET B CG  
3251 S SD  . MET B 192 ? 0.1969 0.3654 0.1090 -0.0208 0.0688  0.0161  192 MET B SD  
3252 C CE  . MET B 192 ? 0.2299 0.3516 0.0514 -0.0166 0.0697  -0.0066 192 MET B CE  
3253 N N   . GLY B 193 ? 0.1102 0.2806 0.0638 -0.0090 0.0696  0.0169  193 GLY B N   
3254 C CA  . GLY B 193 ? 0.1121 0.2918 0.0902 -0.0072 0.0643  0.0324  193 GLY B CA  
3255 C C   . GLY B 193 ? 0.1214 0.2884 0.0947 -0.0065 0.0682  0.0433  193 GLY B C   
3256 O O   . GLY B 193 ? 0.1304 0.3132 0.0957 0.0096  0.1013  0.0528  193 GLY B O   
3257 N N   . VAL B 194 ? 0.1160 0.2932 0.0676 0.0023  0.0692  0.0248  194 VAL B N   
3258 C CA  . VAL B 194 ? 0.1366 0.2982 0.0780 0.0061  0.0621  0.0143  194 VAL B CA  
3259 C C   . VAL B 194 ? 0.1269 0.3047 0.0684 0.0183  0.0815  0.0234  194 VAL B C   
3260 O O   . VAL B 194 ? 0.1091 0.3175 0.0715 0.0152  0.0812  0.0300  194 VAL B O   
3261 C CB  . VAL B 194 ? 0.1331 0.2985 0.0538 0.0008  0.0758  0.0076  194 VAL B CB  
3262 C CG1 . VAL B 194 ? 0.1533 0.2970 0.0775 -0.0093 0.0659  0.0075  194 VAL B CG1 
3263 C CG2 . VAL B 194 ? 0.1276 0.2885 0.0598 -0.0097 0.0794  0.0137  194 VAL B CG2 
3264 N N   . GLU B 195 ? 0.1173 0.3222 0.0790 -0.0101 0.0879  0.0230  195 GLU B N   
3265 C CA  . GLU B 195 ? 0.0996 0.3020 0.1154 -0.0055 0.0871  0.0166  195 GLU B CA  
3266 C C   . GLU B 195 ? 0.1026 0.3033 0.1326 0.0081  0.0788  0.0149  195 GLU B C   
3267 O O   . GLU B 195 ? 0.0979 0.3282 0.1541 0.0041  0.0884  0.0143  195 GLU B O   
3268 C CB  . GLU B 195 ? 0.1338 0.3559 0.1742 -0.0253 0.0566  -0.0012 195 GLU B CB  
3269 C CG  . GLU B 195 ? 0.1609 0.3928 0.1800 -0.0168 0.0398  -0.0110 195 GLU B CG  
3270 C CD  . GLU B 195 ? 0.2235 0.4797 0.1717 -0.0400 0.0371  0.0162  195 GLU B CD  
3271 O OE1 . GLU B 195 ? 0.2024 0.5028 0.1377 -0.0315 0.0654  -0.0061 195 GLU B OE1 
3272 O OE2 . GLU B 195 ? 0.3475 0.6013 0.2380 -0.0457 0.0259  0.0592  195 GLU B OE2 
3273 N N   . LYS B 196 ? 0.1040 0.3103 0.1100 0.0262  0.0822  0.0123  196 LYS B N   
3274 C CA  . LYS B 196 ? 0.1280 0.3320 0.1552 0.0353  0.0964  0.0078  196 LYS B CA  
3275 C C   . LYS B 196 ? 0.1700 0.3240 0.1444 0.0241  0.0953  0.0154  196 LYS B C   
3276 O O   . LYS B 196 ? 0.1629 0.3469 0.1782 0.0191  0.1086  0.0320  196 LYS B O   
3277 C CB  . LYS B 196 ? 0.2161 0.3674 0.1740 0.0482  0.0979  0.0383  196 LYS B CB  
3278 C CG  . LYS B 196 ? 0.3155 0.4081 0.2564 0.0645  0.0841  0.0353  196 LYS B CG  
3279 C CD  . LYS B 196 ? 0.4349 0.4618 0.3195 0.0497  0.0805  0.0777  196 LYS B CD  
3280 C CE  . LYS B 196 ? 0.5507 0.5383 0.3348 0.0135  0.0864  0.0909  196 LYS B CE  
3281 N NZ  . LYS B 196 ? 0.6583 0.5387 0.3070 0.0096  0.0414  0.0839  196 LYS B NZ  
3282 N N   . SER B 197 ? 0.1506 0.2788 0.0895 0.0268  0.0888  0.0197  197 SER B N   
3283 C CA  . SER B 197 ? 0.1908 0.2771 0.0917 0.0236  0.0841  0.0123  197 SER B CA  
3284 C C   . SER B 197 ? 0.1573 0.2648 0.0942 0.0104  0.0673  0.0047  197 SER B C   
3285 O O   . SER B 197 ? 0.1962 0.2880 0.0877 0.0273  0.0795  0.0162  197 SER B O   
3286 C CB  . SER B 197 ? 0.2083 0.2948 0.1318 0.0140  0.0591  0.0108  197 SER B CB  
3287 O OG  . SER B 197 ? 0.2324 0.3245 0.1793 -0.0001 0.0659  0.0263  197 SER B OG  
3288 N N   . VAL B 198 ? 0.1310 0.2563 0.0552 0.0008  0.0746  0.0099  198 VAL B N   
3289 C CA  . VAL B 198 ? 0.0959 0.2513 0.0714 -0.0004 0.0764  -0.0002 198 VAL B CA  
3290 C C   . VAL B 198 ? 0.1005 0.2542 0.0658 -0.0050 0.0663  0.0058  198 VAL B C   
3291 O O   . VAL B 198 ? 0.1150 0.2772 0.0846 -0.0191 0.0600  -0.0048 198 VAL B O   
3292 C CB  . VAL B 198 ? 0.0979 0.2736 0.0796 -0.0083 0.0814  0.0078  198 VAL B CB  
3293 C CG1 . VAL B 198 ? 0.0790 0.2828 0.0957 -0.0122 0.0763  0.0092  198 VAL B CG1 
3294 C CG2 . VAL B 198 ? 0.1109 0.2799 0.0947 -0.0106 0.0842  0.0086  198 VAL B CG2 
3295 N N   . GLY B 199 ? 0.0894 0.2394 0.0625 0.0010  0.0631  0.0030  199 GLY B N   
3296 C CA  . GLY B 199 ? 0.0896 0.2365 0.0686 -0.0017 0.0583  -0.0008 199 GLY B CA  
3297 C C   . GLY B 199 ? 0.0752 0.2317 0.0569 -0.0082 0.0468  0.0008  199 GLY B C   
3298 O O   . GLY B 199 ? 0.0605 0.2381 0.0585 -0.0105 0.0525  0.0072  199 GLY B O   
3299 N N   . PHE B 200 ? 0.0434 0.2384 0.0799 -0.0152 0.0510  0.0063  200 PHE B N   
3300 C CA  . PHE B 200 ? 0.0600 0.2425 0.0632 -0.0108 0.0545  0.0085  200 PHE B CA  
3301 C C   . PHE B 200 ? 0.0476 0.2500 0.0761 -0.0042 0.0530  0.0159  200 PHE B C   
3302 O O   . PHE B 200 ? 0.0433 0.2623 0.0885 0.0012  0.0474  0.0170  200 PHE B O   
3303 C CB  . PHE B 200 ? 0.0779 0.2601 0.0564 -0.0095 0.0532  -0.0004 200 PHE B CB  
3304 C CG  . PHE B 200 ? 0.0855 0.2606 0.0604 0.0022  0.0653  -0.0060 200 PHE B CG  
3305 C CD1 . PHE B 200 ? 0.0951 0.2877 0.0691 0.0000  0.0745  0.0090  200 PHE B CD1 
3306 C CD2 . PHE B 200 ? 0.0929 0.2658 0.1007 0.0192  0.0671  -0.0137 200 PHE B CD2 
3307 C CE1 . PHE B 200 ? 0.0891 0.2806 0.0858 0.0125  0.0809  0.0017  200 PHE B CE1 
3308 C CE2 . PHE B 200 ? 0.1176 0.2652 0.1023 0.0094  0.0666  -0.0084 200 PHE B CE2 
3309 C CZ  . PHE B 200 ? 0.1134 0.2789 0.0963 0.0156  0.0681  -0.0061 200 PHE B CZ  
3310 N N   . LYS B 201 ? 0.0439 0.2606 0.0726 0.0003  0.0496  0.0131  201 LYS B N   
3311 C CA  A LYS B 201 ? 0.0525 0.2619 0.0771 -0.0020 0.0568  0.0139  201 LYS B CA  
3312 C CA  B LYS B 201 ? 0.0533 0.2627 0.0765 -0.0044 0.0567  0.0148  201 LYS B CA  
3313 C C   . LYS B 201 ? 0.0508 0.2595 0.0787 -0.0037 0.0567  0.0015  201 LYS B C   
3314 O O   . LYS B 201 ? 0.0499 0.2649 0.0904 -0.0032 0.0589  0.0054  201 LYS B O   
3315 C CB  A LYS B 201 ? 0.0460 0.2772 0.0846 0.0065  0.0557  0.0058  201 LYS B CB  
3316 C CB  B LYS B 201 ? 0.0472 0.2799 0.0822 0.0006  0.0556  0.0071  201 LYS B CB  
3317 C CG  A LYS B 201 ? 0.0602 0.2825 0.0879 0.0125  0.0662  0.0087  201 LYS B CG  
3318 C CG  B LYS B 201 ? 0.0714 0.2896 0.0890 0.0019  0.0617  0.0131  201 LYS B CG  
3319 C CD  A LYS B 201 ? 0.0615 0.2946 0.0999 0.0194  0.0713  0.0033  201 LYS B CD  
3320 C CD  B LYS B 201 ? 0.0787 0.3057 0.0979 0.0043  0.0677  0.0089  201 LYS B CD  
3321 C CE  A LYS B 201 ? 0.0767 0.3015 0.1107 0.0260  0.0743  0.0103  201 LYS B CE  
3322 C CE  B LYS B 201 ? 0.1020 0.3233 0.1082 -0.0013 0.0696  0.0196  201 LYS B CE  
3323 N NZ  A LYS B 201 ? 0.0834 0.3209 0.1261 0.0262  0.0724  0.0011  201 LYS B NZ  
3324 N NZ  B LYS B 201 ? 0.1253 0.3282 0.1304 -0.0014 0.0780  0.0221  201 LYS B NZ  
3325 N N   . VAL B 202 ? 0.0463 0.2583 0.1048 -0.0030 0.0623  0.0025  202 VAL B N   
3326 C CA  A VAL B 202 ? 0.0552 0.2720 0.1216 0.0055  0.0618  0.0067  202 VAL B CA  
3327 C CA  B VAL B 202 ? 0.0534 0.2670 0.1198 0.0010  0.0590  0.0051  202 VAL B CA  
3328 C C   . VAL B 202 ? 0.0424 0.2696 0.1266 0.0068  0.0630  0.0166  202 VAL B C   
3329 O O   . VAL B 202 ? 0.0531 0.3076 0.1589 0.0158  0.0841  0.0479  202 VAL B O   
3330 C CB  A VAL B 202 ? 0.0738 0.2755 0.1534 0.0092  0.0583  -0.0026 202 VAL B CB  
3331 C CB  B VAL B 202 ? 0.0584 0.2638 0.1513 0.0037  0.0510  -0.0024 202 VAL B CB  
3332 C CG1 A VAL B 202 ? 0.0829 0.2877 0.1650 0.0012  0.0689  0.0086  202 VAL B CG1 
3333 C CG1 B VAL B 202 ? 0.0562 0.2819 0.1623 -0.0036 0.0559  -0.0054 202 VAL B CG1 
3334 C CG2 A VAL B 202 ? 0.0675 0.2744 0.1592 0.0061  0.0577  0.0000  202 VAL B CG2 
3335 C CG2 B VAL B 202 ? 0.0763 0.2604 0.1644 0.0100  0.0422  -0.0011 202 VAL B CG2 
3336 N N   . THR B 203 ? 0.0329 0.2825 0.1218 0.0037  0.0547  0.0192  203 THR B N   
3337 C CA  . THR B 203 ? 0.0474 0.2919 0.1306 0.0054  0.0648  0.0135  203 THR B CA  
3338 C C   . THR B 203 ? 0.0451 0.2796 0.1468 -0.0007 0.0658  0.0211  203 THR B C   
3339 O O   . THR B 203 ? 0.0543 0.2908 0.1227 0.0229  0.0591  0.0088  203 THR B O   
3340 C CB  . THR B 203 ? 0.1152 0.3158 0.1597 0.0140  0.0385  -0.0069 203 THR B CB  
3341 O OG1 . THR B 203 ? 0.1815 0.3117 0.2461 0.0035  -0.0029 -0.0261 203 THR B OG1 
3342 C CG2 . THR B 203 ? 0.1222 0.3353 0.1432 -0.0034 0.0485  -0.0052 203 THR B CG2 
3343 N N   . GLY B 204 ? 0.0658 0.2820 0.1614 0.0121  0.0945  0.0227  204 GLY B N   
3344 C CA  . GLY B 204 ? 0.0952 0.2885 0.1886 0.0095  0.1057  0.0242  204 GLY B CA  
3345 C C   . GLY B 204 ? 0.1267 0.2829 0.2100 0.0033  0.1040  0.0174  204 GLY B C   
3346 O O   . GLY B 204 ? 0.1772 0.3062 0.1980 -0.0156 0.1008  0.0232  204 GLY B O   
3347 N N   . GLY B 205 ? 0.1772 0.2954 0.2584 0.0229  0.1069  0.0139  205 GLY B N   
3348 C CA  . GLY B 205 ? 0.1984 0.3242 0.2458 0.0298  0.1535  -0.0056 205 GLY B CA  
3349 C C   . GLY B 205 ? 0.2262 0.3357 0.2573 0.0652  0.1448  -0.0320 205 GLY B C   
3350 O O   . GLY B 205 ? 0.3488 0.4397 0.2660 0.0903  0.1163  -0.0352 205 GLY B O   
3351 N N   . VAL B 206 ? 0.2224 0.3101 0.2581 0.0517  0.1495  -0.0371 206 VAL B N   
3352 C CA  . VAL B 206 ? 0.1938 0.3406 0.2418 0.0215  0.1405  -0.0248 206 VAL B CA  
3353 C C   . VAL B 206 ? 0.1797 0.3293 0.2847 0.0351  0.1640  -0.0221 206 VAL B C   
3354 O O   . VAL B 206 ? 0.1822 0.3810 0.2271 0.0339  0.1225  -0.0585 206 VAL B O   
3355 C CB  . VAL B 206 ? 0.2409 0.3585 0.2285 0.0504  0.1081  -0.0392 206 VAL B CB  
3356 C CG1 . VAL B 206 ? 0.2702 0.3989 0.2694 0.0566  0.1014  -0.0323 206 VAL B CG1 
3357 C CG2 . VAL B 206 ? 0.2503 0.3626 0.2414 0.0536  0.1341  -0.0427 206 VAL B CG2 
3358 N N   . SER B 207 ? 0.2117 0.3341 0.3364 0.0381  0.1730  0.0179  207 SER B N   
3359 C CA  . SER B 207 ? 0.2510 0.3628 0.3894 0.0222  0.1861  0.0566  207 SER B CA  
3360 C C   . SER B 207 ? 0.2510 0.3394 0.3232 0.0046  0.2028  0.0812  207 SER B C   
3361 O O   . SER B 207 ? 0.3183 0.4285 0.3059 -0.0054 0.2311  0.0709  207 SER B O   
3362 C CB  . SER B 207 ? 0.2802 0.3947 0.4533 0.0163  0.1553  0.0930  207 SER B CB  
3363 O OG  . SER B 207 ? 0.4080 0.4789 0.5701 0.0261  0.1070  0.1093  207 SER B OG  
3364 N N   . THR B 208 ? 0.2302 0.3118 0.3153 0.0027  0.2210  0.0230  208 THR B N   
3365 C CA  . THR B 208 ? 0.2002 0.2991 0.3174 -0.0155 0.2148  0.0171  208 THR B CA  
3366 C C   . THR B 208 ? 0.1896 0.2765 0.3110 0.0001  0.1911  -0.0265 208 THR B C   
3367 O O   . THR B 208 ? 0.1515 0.3006 0.2874 -0.0081 0.1781  -0.0158 208 THR B O   
3368 C CB  . THR B 208 ? 0.2244 0.3079 0.3636 -0.0153 0.1847  0.0154  208 THR B CB  
3369 O OG1 . THR B 208 ? 0.2235 0.3337 0.3560 -0.0144 0.1907  -0.0375 208 THR B OG1 
3370 C CG2 . THR B 208 ? 0.2688 0.3262 0.4244 -0.0202 0.1558  0.0206  208 THR B CG2 
3371 N N   . ALA B 209 ? 0.1710 0.3246 0.3337 -0.0155 0.1916  -0.0350 209 ALA B N   
3372 C CA  . ALA B 209 ? 0.1544 0.3260 0.3431 -0.0015 0.1827  -0.0433 209 ALA B CA  
3373 C C   . ALA B 209 ? 0.1449 0.3117 0.3282 -0.0071 0.1546  -0.0560 209 ALA B C   
3374 O O   . ALA B 209 ? 0.1413 0.3291 0.3292 -0.0183 0.1596  -0.0544 209 ALA B O   
3375 C CB  . ALA B 209 ? 0.1681 0.3301 0.3651 -0.0154 0.1629  -0.0517 209 ALA B CB  
3376 N N   . GLU B 210 ? 0.1542 0.3082 0.3235 -0.0053 0.1614  -0.0555 210 GLU B N   
3377 C CA  . GLU B 210 ? 0.1499 0.3119 0.2939 -0.0214 0.1333  -0.0665 210 GLU B CA  
3378 C C   . GLU B 210 ? 0.1619 0.2953 0.2574 -0.0257 0.1153  -0.0613 210 GLU B C   
3379 O O   . GLU B 210 ? 0.1818 0.3268 0.2364 -0.0510 0.1339  -0.0730 210 GLU B O   
3380 C CB  . GLU B 210 ? 0.1633 0.3156 0.3670 -0.0280 0.1223  -0.0742 210 GLU B CB  
3381 C CG  . GLU B 210 ? 0.2000 0.3637 0.4383 -0.0489 0.0941  -0.0839 210 GLU B CG  
3382 C CD  . GLU B 210 ? 0.1971 0.4121 0.4891 -0.0661 0.1088  -0.0743 210 GLU B CD  
3383 O OE1 . GLU B 210 ? 0.2462 0.3915 0.5203 -0.0649 0.1366  -0.0811 210 GLU B OE1 
3384 O OE2 . GLU B 210 ? 0.2743 0.4518 0.6093 -0.1081 0.1164  -0.0576 210 GLU B OE2 
3385 N N   . ASP B 211 ? 0.1298 0.3014 0.2218 -0.0169 0.1222  -0.0531 211 ASP B N   
3386 C CA  . ASP B 211 ? 0.1052 0.3023 0.2118 -0.0093 0.1322  -0.0426 211 ASP B CA  
3387 C C   . ASP B 211 ? 0.1249 0.2996 0.1706 -0.0164 0.1280  -0.0432 211 ASP B C   
3388 O O   . ASP B 211 ? 0.1088 0.3113 0.1900 -0.0225 0.1184  -0.0264 211 ASP B O   
3389 C CB  . ASP B 211 ? 0.1237 0.3278 0.2117 -0.0147 0.1246  -0.0376 211 ASP B CB  
3390 C CG  . ASP B 211 ? 0.1533 0.3494 0.2302 0.0148  0.1169  -0.0400 211 ASP B CG  
3391 O OD1 . ASP B 211 ? 0.2454 0.3751 0.2652 0.0906  0.0952  -0.0532 211 ASP B OD1 
3392 O OD2 . ASP B 211 ? 0.2104 0.3681 0.2443 0.0381  0.1375  -0.0167 211 ASP B OD2 
3393 N N   . ALA B 212 ? 0.1479 0.2953 0.1595 -0.0070 0.1326  -0.0425 212 ALA B N   
3394 C CA  . ALA B 212 ? 0.1552 0.2788 0.1338 -0.0113 0.1292  -0.0466 212 ALA B CA  
3395 C C   . ALA B 212 ? 0.1569 0.2757 0.1476 -0.0177 0.1247  -0.0503 212 ALA B C   
3396 O O   . ALA B 212 ? 0.2004 0.2836 0.1250 -0.0277 0.1141  -0.0395 212 ALA B O   
3397 C CB  . ALA B 212 ? 0.1386 0.2818 0.1428 0.0070  0.1154  -0.0473 212 ALA B CB  
3398 N N   . GLN B 213 ? 0.1352 0.3180 0.1599 -0.0314 0.1158  -0.0400 213 GLN B N   
3399 C CA  . GLN B 213 ? 0.1510 0.3176 0.1898 -0.0250 0.0933  -0.0567 213 GLN B CA  
3400 C C   . GLN B 213 ? 0.1457 0.3193 0.1740 -0.0233 0.0871  -0.0351 213 GLN B C   
3401 O O   . GLN B 213 ? 0.1897 0.3628 0.1403 -0.0367 0.0648  -0.0370 213 GLN B O   
3402 C CB  . GLN B 213 ? 0.1725 0.3510 0.2256 -0.0174 0.0786  -0.0748 213 GLN B CB  
3403 C CG  . GLN B 213 ? 0.1947 0.3787 0.2401 -0.0168 0.0647  -0.1015 213 GLN B CG  
3404 C CD  . GLN B 213 ? 0.2396 0.4012 0.3495 -0.0443 0.0536  -0.0902 213 GLN B CD  
3405 O OE1 . GLN B 213 ? 0.3988 0.3976 0.4018 -0.0610 0.0568  -0.1089 213 GLN B OE1 
3406 N NE2 . GLN B 213 ? 0.2471 0.4896 0.4484 -0.0227 0.0647  -0.0808 213 GLN B NE2 
3407 N N   . LYS B 214 ? 0.1657 0.3061 0.1412 -0.0223 0.1126  -0.0501 214 LYS B N   
3408 C CA  . LYS B 214 ? 0.1784 0.3440 0.1345 0.0059  0.1170  -0.0594 214 LYS B CA  
3409 C C   . LYS B 214 ? 0.1827 0.3445 0.1392 0.0042  0.0845  -0.0483 214 LYS B C   
3410 O O   . LYS B 214 ? 0.1655 0.3629 0.1370 -0.0051 0.0807  -0.0349 214 LYS B O   
3411 C CB  . LYS B 214 ? 0.2075 0.3839 0.1652 0.0244  0.1203  -0.0571 214 LYS B CB  
3412 C CG  . LYS B 214 ? 0.2329 0.4411 0.2060 0.0507  0.1567  -0.0622 214 LYS B CG  
3413 C CD  . LYS B 214 ? 0.3361 0.4745 0.3079 0.0380  0.1431  -0.0436 214 LYS B CD  
3414 C CE  . LYS B 214 ? 0.4160 0.5201 0.3442 0.0692  0.1137  -0.0673 214 LYS B CE  
3415 N NZ  . LYS B 214 ? 0.4696 0.5625 0.4543 0.0982  0.0923  -0.0658 214 LYS B NZ  
3416 N N   . TYR B 215 ? 0.1216 0.3153 0.1192 0.0105  0.0906  -0.0366 215 TYR B N   
3417 C CA  . TYR B 215 ? 0.1028 0.3089 0.1037 -0.0006 0.0836  -0.0236 215 TYR B CA  
3418 C C   . TYR B 215 ? 0.0916 0.3043 0.0901 -0.0036 0.0811  -0.0235 215 TYR B C   
3419 O O   . TYR B 215 ? 0.1047 0.3156 0.1153 -0.0020 0.0907  0.0049  215 TYR B O   
3420 C CB  . TYR B 215 ? 0.1177 0.3133 0.1121 -0.0019 0.0686  -0.0160 215 TYR B CB  
3421 C CG  . TYR B 215 ? 0.1077 0.3184 0.1225 -0.0098 0.0672  0.0094  215 TYR B CG  
3422 C CD1 . TYR B 215 ? 0.1156 0.3090 0.1173 -0.0217 0.0574  0.0089  215 TYR B CD1 
3423 C CD2 . TYR B 215 ? 0.1266 0.3351 0.2436 -0.0156 0.0278  0.0481  215 TYR B CD2 
3424 C CE1 . TYR B 215 ? 0.1130 0.2924 0.1045 -0.0053 0.0853  -0.0026 215 TYR B CE1 
3425 C CE2 . TYR B 215 ? 0.1238 0.3314 0.2456 -0.0272 0.0285  0.0559  215 TYR B CE2 
3426 C CZ  . TYR B 215 ? 0.1180 0.3168 0.1736 -0.0145 0.0626  0.0155  215 TYR B CZ  
3427 O OH  . TYR B 215 ? 0.1245 0.3289 0.2276 -0.0040 0.0408  0.0318  215 TYR B OH  
3428 N N   . LEU B 216 ? 0.0884 0.3133 0.0885 0.0064  0.0731  -0.0263 216 LEU B N   
3429 C CA  . LEU B 216 ? 0.0939 0.3154 0.1050 0.0082  0.0669  -0.0225 216 LEU B CA  
3430 C C   . LEU B 216 ? 0.1002 0.3169 0.1135 0.0000  0.0709  -0.0113 216 LEU B C   
3431 O O   . LEU B 216 ? 0.1417 0.3321 0.1383 -0.0029 0.0919  0.0080  216 LEU B O   
3432 C CB  . LEU B 216 ? 0.0897 0.3378 0.1264 0.0059  0.0528  -0.0201 216 LEU B CB  
3433 C CG  . LEU B 216 ? 0.1336 0.3747 0.1355 0.0129  0.0640  -0.0200 216 LEU B CG  
3434 C CD1 . LEU B 216 ? 0.1240 0.3853 0.2215 0.0330  0.0758  -0.0203 216 LEU B CD1 
3435 C CD2 . LEU B 216 ? 0.1543 0.3651 0.1549 0.0375  0.0693  -0.0399 216 LEU B CD2 
3436 N N   . ALA B 217 ? 0.1166 0.3279 0.1003 -0.0050 0.0489  -0.0232 217 ALA B N   
3437 C CA  . ALA B 217 ? 0.1241 0.3457 0.1040 -0.0161 0.0689  -0.0203 217 ALA B CA  
3438 C C   . ALA B 217 ? 0.1250 0.3557 0.1200 -0.0304 0.0468  -0.0096 217 ALA B C   
3439 O O   . ALA B 217 ? 0.1371 0.3820 0.1072 -0.0050 0.0663  -0.0047 217 ALA B O   
3440 C CB  . ALA B 217 ? 0.1191 0.3583 0.1271 -0.0048 0.0778  -0.0364 217 ALA B CB  
3441 N N   . ILE B 218 ? 0.1121 0.3622 0.0875 -0.0135 0.0605  -0.0279 218 ILE B N   
3442 C CA  . ILE B 218 ? 0.1013 0.3872 0.0949 -0.0098 0.0764  -0.0372 218 ILE B CA  
3443 C C   . ILE B 218 ? 0.1060 0.3887 0.1071 -0.0181 0.0635  -0.0300 218 ILE B C   
3444 O O   . ILE B 218 ? 0.1260 0.4025 0.1020 -0.0346 0.0616  -0.0281 218 ILE B O   
3445 C CB  . ILE B 218 ? 0.0899 0.4115 0.1305 -0.0090 0.0663  -0.0320 218 ILE B CB  
3446 C CG1 . ILE B 218 ? 0.1209 0.4230 0.1616 -0.0085 0.0594  -0.0299 218 ILE B CG1 
3447 C CG2 . ILE B 218 ? 0.0889 0.4178 0.1626 -0.0063 0.0673  -0.0278 218 ILE B CG2 
3448 C CD1 . ILE B 218 ? 0.1205 0.4388 0.1891 0.0167  0.0651  -0.0227 218 ILE B CD1 
3449 N N   . ALA B 219 ? 0.1187 0.3581 0.0814 -0.0226 0.0539  -0.0316 219 ALA B N   
3450 C CA  . ALA B 219 ? 0.1092 0.3654 0.0918 -0.0125 0.0650  -0.0196 219 ALA B CA  
3451 C C   . ALA B 219 ? 0.1259 0.3749 0.1057 -0.0150 0.0632  -0.0055 219 ALA B C   
3452 O O   . ALA B 219 ? 0.1337 0.3870 0.0952 -0.0213 0.0737  0.0039  219 ALA B O   
3453 C CB  . ALA B 219 ? 0.1391 0.3730 0.0743 -0.0103 0.0677  -0.0103 219 ALA B CB  
3454 N N   . ASP B 220 ? 0.1016 0.3835 0.1069 -0.0245 0.0598  -0.0063 220 ASP B N   
3455 C CA  . ASP B 220 ? 0.1131 0.4008 0.1011 -0.0271 0.0547  -0.0020 220 ASP B CA  
3456 C C   . ASP B 220 ? 0.1472 0.4033 0.0935 -0.0320 0.0588  0.0012  220 ASP B C   
3457 O O   . ASP B 220 ? 0.2021 0.4149 0.1047 -0.0210 0.0536  0.0152  220 ASP B O   
3458 C CB  . ASP B 220 ? 0.1119 0.4165 0.1086 -0.0371 0.0354  -0.0095 220 ASP B CB  
3459 C CG  . ASP B 220 ? 0.1395 0.4152 0.1546 -0.0255 0.0682  -0.0224 220 ASP B CG  
3460 O OD1 . ASP B 220 ? 0.1414 0.4115 0.1949 -0.0216 0.0658  -0.0386 220 ASP B OD1 
3461 O OD2 . ASP B 220 ? 0.2048 0.4474 0.2222 -0.0480 0.0508  -0.0581 220 ASP B OD2 
3462 N N   . GLU B 221 ? 0.1275 0.4122 0.0881 -0.0292 0.0677  -0.0074 221 GLU B N   
3463 C CA  . GLU B 221 ? 0.1497 0.4373 0.0692 -0.0481 0.0648  0.0047  221 GLU B CA  
3464 C C   . GLU B 221 ? 0.1664 0.4169 0.0655 -0.0342 0.0663  -0.0035 221 GLU B C   
3465 O O   . GLU B 221 ? 0.2052 0.4952 0.0857 -0.0596 0.0638  0.0299  221 GLU B O   
3466 C CB  . GLU B 221 ? 0.1678 0.4511 0.1174 -0.0439 0.0864  -0.0133 221 GLU B CB  
3467 C CG  . GLU B 221 ? 0.2576 0.4962 0.2082 -0.0475 0.0531  -0.0267 221 GLU B CG  
3468 C CD  . GLU B 221 ? 0.3202 0.5670 0.3663 -0.0345 0.0034  -0.0012 221 GLU B CD  
3469 O OE1 . GLU B 221 ? 0.3154 0.6717 0.5489 -0.0012 0.0072  0.0075  221 GLU B OE1 
3470 O OE2 . GLU B 221 ? 0.4755 0.6039 0.4702 -0.1063 0.0051  0.0053  221 GLU B OE2 
3471 N N   . LEU B 222 ? 0.1458 0.3810 0.0729 -0.0280 0.0653  -0.0003 222 LEU B N   
3472 C CA  . LEU B 222 ? 0.1553 0.3852 0.0919 -0.0258 0.0677  -0.0037 222 LEU B CA  
3473 C C   . LEU B 222 ? 0.1609 0.3860 0.0859 -0.0244 0.0785  0.0094  222 LEU B C   
3474 O O   . LEU B 222 ? 0.2150 0.4053 0.1412 -0.0636 0.0726  0.0193  222 LEU B O   
3475 C CB  . LEU B 222 ? 0.1629 0.3808 0.0729 -0.0188 0.0780  -0.0150 222 LEU B CB  
3476 C CG  . LEU B 222 ? 0.1611 0.3903 0.1083 -0.0137 0.0740  -0.0115 222 LEU B CG  
3477 C CD1 . LEU B 222 ? 0.1774 0.4000 0.1086 -0.0120 0.0604  -0.0311 222 LEU B CD1 
3478 C CD2 . LEU B 222 ? 0.1889 0.4234 0.1225 -0.0059 0.0937  -0.0074 222 LEU B CD2 
3479 N N   . PHE B 223 ? 0.1286 0.3836 0.0825 -0.0153 0.0504  0.0129  223 PHE B N   
3480 C CA  . PHE B 223 ? 0.1582 0.3853 0.0910 -0.0013 0.0443  0.0302  223 PHE B CA  
3481 C C   . PHE B 223 ? 0.1956 0.4139 0.1216 0.0064  0.0082  0.0252  223 PHE B C   
3482 O O   . PHE B 223 ? 0.2088 0.4364 0.1970 0.0107  0.0175  0.0342  223 PHE B O   
3483 C CB  . PHE B 223 ? 0.1407 0.3545 0.1061 0.0069  0.0439  0.0125  223 PHE B CB  
3484 C CG  . PHE B 223 ? 0.1241 0.3296 0.1283 0.0001  0.0601  0.0068  223 PHE B CG  
3485 C CD1 . PHE B 223 ? 0.1230 0.3294 0.1655 0.0000  0.0484  0.0065  223 PHE B CD1 
3486 C CD2 . PHE B 223 ? 0.1318 0.3355 0.1298 0.0073  0.0454  -0.0069 223 PHE B CD2 
3487 C CE1 . PHE B 223 ? 0.1074 0.3435 0.1941 -0.0071 0.0499  -0.0072 223 PHE B CE1 
3488 C CE2 . PHE B 223 ? 0.1480 0.3355 0.1430 0.0074  0.0450  -0.0011 223 PHE B CE2 
3489 C CZ  . PHE B 223 ? 0.1149 0.3319 0.1885 0.0055  0.0390  -0.0095 223 PHE B CZ  
3490 N N   . GLY B 224 ? 0.1837 0.4374 0.1311 0.0088  0.0199  0.0193  224 GLY B N   
3491 C CA  . GLY B 224 ? 0.1897 0.4510 0.1420 0.0052  0.0103  -0.0030 224 GLY B CA  
3492 C C   . GLY B 224 ? 0.1771 0.4668 0.1428 -0.0046 -0.0018 0.0026  224 GLY B C   
3493 O O   . GLY B 224 ? 0.1905 0.4645 0.1288 0.0080  -0.0025 0.0147  224 GLY B O   
3494 N N   . ALA B 225 ? 0.1834 0.4942 0.1789 -0.0137 0.0180  -0.0109 225 ALA B N   
3495 C CA  . ALA B 225 ? 0.1819 0.5082 0.2003 -0.0088 0.0308  -0.0003 225 ALA B CA  
3496 C C   . ALA B 225 ? 0.1812 0.5069 0.1762 0.0020  0.0081  -0.0027 225 ALA B C   
3497 O O   . ALA B 225 ? 0.2521 0.5203 0.2181 0.0120  0.0795  0.0339  225 ALA B O   
3498 C CB  . ALA B 225 ? 0.2153 0.5332 0.2470 -0.0400 0.0154  -0.0208 225 ALA B CB  
3499 N N   . ASP B 226 ? 0.1451 0.4985 0.1920 0.0199  0.0063  0.0034  226 ASP B N   
3500 C CA  . ASP B 226 ? 0.2210 0.5119 0.1810 0.0314  0.0054  0.0022  226 ASP B CA  
3501 C C   . ASP B 226 ? 0.1772 0.4589 0.1494 0.0388  0.0344  -0.0106 226 ASP B C   
3502 O O   . ASP B 226 ? 0.2037 0.4662 0.1880 0.0375  0.0456  -0.0193 226 ASP B O   
3503 C CB  . ASP B 226 ? 0.2543 0.5522 0.2342 0.0523  -0.0369 0.0165  226 ASP B CB  
3504 C CG  . ASP B 226 ? 0.3316 0.6636 0.3501 0.0251  -0.0928 0.0366  226 ASP B CG  
3505 O OD1 . ASP B 226 ? 0.4217 0.7484 0.4492 0.0029  -0.0880 0.0559  226 ASP B OD1 
3506 O OD2 . ASP B 226 ? 0.5403 0.7532 0.4821 0.0373  -0.1156 0.1360  226 ASP B OD2 
3507 N N   . TRP B 227 ? 0.1678 0.4139 0.1102 0.0291  0.0264  0.0043  227 TRP B N   
3508 C CA  . TRP B 227 ? 0.1553 0.3632 0.1109 0.0260  0.0352  0.0101  227 TRP B CA  
3509 C C   . TRP B 227 ? 0.1151 0.3477 0.1027 0.0146  0.0393  0.0002  227 TRP B C   
3510 O O   . TRP B 227 ? 0.1284 0.3526 0.0972 0.0106  0.0391  0.0108  227 TRP B O   
3511 C CB  . TRP B 227 ? 0.1397 0.3497 0.1054 0.0073  0.0438  0.0307  227 TRP B CB  
3512 C CG  . TRP B 227 ? 0.1459 0.3446 0.0778 -0.0036 0.0604  0.0252  227 TRP B CG  
3513 C CD1 . TRP B 227 ? 0.1393 0.3332 0.0842 0.0012  0.0673  0.0187  227 TRP B CD1 
3514 C CD2 . TRP B 227 ? 0.1120 0.3466 0.0759 -0.0090 0.0732  0.0131  227 TRP B CD2 
3515 N NE1 . TRP B 227 ? 0.1261 0.3439 0.1041 -0.0061 0.0720  0.0109  227 TRP B NE1 
3516 C CE2 . TRP B 227 ? 0.1211 0.3406 0.0761 -0.0200 0.0801  0.0102  227 TRP B CE2 
3517 C CE3 . TRP B 227 ? 0.1275 0.3468 0.0761 -0.0202 0.0604  -0.0012 227 TRP B CE3 
3518 C CZ2 . TRP B 227 ? 0.1173 0.3412 0.0661 -0.0142 0.0814  -0.0101 227 TRP B CZ2 
3519 C CZ3 . TRP B 227 ? 0.1516 0.3448 0.0670 -0.0253 0.0622  0.0124  227 TRP B CZ3 
3520 C CH2 . TRP B 227 ? 0.1332 0.3586 0.0617 -0.0184 0.0546  -0.0011 227 TRP B CH2 
3521 N N   . ALA B 228 ? 0.1356 0.3457 0.0988 0.0145  0.0127  0.0073  228 ALA B N   
3522 C CA  . ALA B 228 ? 0.1290 0.3463 0.0821 0.0227  0.0182  -0.0081 228 ALA B CA  
3523 C C   . ALA B 228 ? 0.1040 0.3297 0.1216 -0.0022 0.0298  -0.0058 228 ALA B C   
3524 O O   . ALA B 228 ? 0.1379 0.3711 0.1631 -0.0221 0.0553  -0.0006 228 ALA B O   
3525 C CB  . ALA B 228 ? 0.1445 0.3448 0.1101 0.0234  -0.0015 -0.0178 228 ALA B CB  
3526 N N   . ASP B 229 ? 0.1127 0.3310 0.1108 0.0023  0.0538  -0.0029 229 ASP B N   
3527 C CA  . ASP B 229 ? 0.0810 0.3308 0.1174 0.0086  0.0532  0.0112  229 ASP B CA  
3528 C C   . ASP B 229 ? 0.0649 0.3037 0.1133 0.0096  0.0522  0.0124  229 ASP B C   
3529 O O   . ASP B 229 ? 0.0596 0.3100 0.1188 0.0131  0.0617  0.0151  229 ASP B O   
3530 C CB  . ASP B 229 ? 0.0852 0.3433 0.1040 0.0132  0.0611  0.0225  229 ASP B CB  
3531 C CG  . ASP B 229 ? 0.1237 0.3370 0.1416 0.0167  0.0209  0.0425  229 ASP B CG  
3532 O OD1 . ASP B 229 ? 0.1182 0.3548 0.1221 0.0143  0.0373  0.0266  229 ASP B OD1 
3533 O OD2 . ASP B 229 ? 0.1808 0.3730 0.2528 0.0245  -0.0154 0.0749  229 ASP B OD2 
3534 N N   . ALA B 230 ? 0.0981 0.3056 0.1024 0.0111  0.0526  0.0039  230 ALA B N   
3535 C CA  . ALA B 230 ? 0.0773 0.3009 0.0873 0.0007  0.0637  0.0237  230 ALA B CA  
3536 C C   . ALA B 230 ? 0.0704 0.3020 0.0726 0.0059  0.0545  0.0239  230 ALA B C   
3537 O O   . ALA B 230 ? 0.0803 0.3085 0.0713 -0.0052 0.0412  0.0156  230 ALA B O   
3538 C CB  . ALA B 230 ? 0.0632 0.3237 0.1113 -0.0039 0.0729  0.0265  230 ALA B CB  
3539 N N   . ARG B 231 ? 0.0889 0.2908 0.1011 0.0001  0.0387  0.0246  231 ARG B N   
3540 C CA  . ARG B 231 ? 0.0751 0.2800 0.0967 0.0086  0.0572  0.0088  231 ARG B CA  
3541 C C   . ARG B 231 ? 0.0686 0.2556 0.0971 0.0018  0.0569  0.0120  231 ARG B C   
3542 O O   . ARG B 231 ? 0.0713 0.2723 0.1261 0.0019  0.0571  -0.0008 231 ARG B O   
3543 C CB  . ARG B 231 ? 0.0876 0.2890 0.0952 0.0212  0.0571  0.0165  231 ARG B CB  
3544 C CG  . ARG B 231 ? 0.0869 0.2856 0.1252 0.0273  0.0536  0.0169  231 ARG B CG  
3545 C CD  . ARG B 231 ? 0.0943 0.2867 0.1129 0.0217  0.0719  0.0031  231 ARG B CD  
3546 N NE  . ARG B 231 ? 0.1192 0.2744 0.1434 0.0255  0.0534  -0.0017 231 ARG B NE  
3547 C CZ  . ARG B 231 ? 0.1115 0.2864 0.1423 0.0097  0.0492  -0.0028 231 ARG B CZ  
3548 N NH1 . ARG B 231 ? 0.0963 0.2804 0.1338 0.0122  0.0607  -0.0137 231 ARG B NH1 
3549 N NH2 . ARG B 231 ? 0.0912 0.2940 0.1474 0.0028  0.0650  0.0003  231 ARG B NH2 
3550 N N   . HIS B 232 ? 0.0560 0.2526 0.0940 0.0047  0.0657  0.0195  232 HIS B N   
3551 C CA  . HIS B 232 ? 0.0642 0.2614 0.0843 0.0126  0.0634  0.0091  232 HIS B CA  
3552 C C   . HIS B 232 ? 0.0609 0.2521 0.0840 0.0115  0.0516  0.0176  232 HIS B C   
3553 O O   . HIS B 232 ? 0.0661 0.2502 0.0949 0.0180  0.0588  0.0093  232 HIS B O   
3554 C CB  . HIS B 232 ? 0.0689 0.2792 0.0865 0.0298  0.0605  0.0143  232 HIS B CB  
3555 C CG  . HIS B 232 ? 0.1029 0.2952 0.0969 0.0273  0.0656  0.0336  232 HIS B CG  
3556 N ND1 . HIS B 232 ? 0.1329 0.3018 0.1236 0.0564  0.0663  0.0339  232 HIS B ND1 
3557 C CD2 . HIS B 232 ? 0.1181 0.3166 0.0926 0.0344  0.0982  0.0314  232 HIS B CD2 
3558 C CE1 . HIS B 232 ? 0.1320 0.3133 0.1401 0.0377  0.0806  0.0351  232 HIS B CE1 
3559 N NE2 . HIS B 232 ? 0.1448 0.3252 0.1294 0.0304  0.0940  0.0476  232 HIS B NE2 
3560 N N   . TYR B 233 ? 0.0546 0.2565 0.0669 0.0097  0.0541  0.0130  233 TYR B N   
3561 C CA  . TYR B 233 ? 0.0466 0.2644 0.0730 -0.0047 0.0511  0.0159  233 TYR B CA  
3562 C C   . TYR B 233 ? 0.0434 0.2623 0.0793 0.0020  0.0516  0.0201  233 TYR B C   
3563 O O   . TYR B 233 ? 0.0426 0.2855 0.0993 0.0059  0.0580  0.0151  233 TYR B O   
3564 C CB  . TYR B 233 ? 0.0589 0.2735 0.0949 -0.0141 0.0575  0.0133  233 TYR B CB  
3565 C CG  . TYR B 233 ? 0.0886 0.2651 0.0950 0.0007  0.0491  0.0044  233 TYR B CG  
3566 C CD1 . TYR B 233 ? 0.1165 0.2786 0.1158 -0.0007 0.0649  -0.0004 233 TYR B CD1 
3567 C CD2 . TYR B 233 ? 0.1267 0.2957 0.1011 0.0203  0.0596  0.0032  233 TYR B CD2 
3568 C CE1 . TYR B 233 ? 0.1510 0.2783 0.1461 -0.0074 0.0431  0.0027  233 TYR B CE1 
3569 C CE2 . TYR B 233 ? 0.1266 0.2990 0.1340 0.0266  0.0424  -0.0088 233 TYR B CE2 
3570 C CZ  . TYR B 233 ? 0.1563 0.3020 0.1524 0.0169  0.0348  -0.0258 233 TYR B CZ  
3571 O OH  . TYR B 233 ? 0.1677 0.3216 0.2145 0.0143  0.0333  -0.0403 233 TYR B OH  
3572 N N   . ARG B 234 ? 0.0413 0.2490 0.0688 0.0031  0.0463  0.0198  234 ARG B N   
3573 C CA  . ARG B 234 ? 0.0466 0.2464 0.0729 -0.0009 0.0516  0.0091  234 ARG B CA  
3574 C C   . ARG B 234 ? 0.0473 0.2466 0.0887 -0.0015 0.0580  0.0054  234 ARG B C   
3575 O O   . ARG B 234 ? 0.0487 0.2416 0.0910 0.0183  0.0586  -0.0038 234 ARG B O   
3576 C CB  . ARG B 234 ? 0.0549 0.2513 0.0853 -0.0073 0.0472  0.0014  234 ARG B CB  
3577 C CG  . ARG B 234 ? 0.0540 0.2446 0.0659 -0.0027 0.0532  -0.0022 234 ARG B CG  
3578 C CD  . ARG B 234 ? 0.0575 0.2476 0.0653 0.0054  0.0549  0.0006  234 ARG B CD  
3579 N NE  . ARG B 234 ? 0.0583 0.2530 0.0764 0.0042  0.0554  0.0063  234 ARG B NE  
3580 C CZ  . ARG B 234 ? 0.0750 0.2487 0.0665 0.0080  0.0545  -0.0032 234 ARG B CZ  
3581 N NH1 . ARG B 234 ? 0.0998 0.2518 0.0588 0.0006  0.0533  -0.0065 234 ARG B NH1 
3582 N NH2 . ARG B 234 ? 0.1142 0.2540 0.0694 0.0076  0.0400  -0.0157 234 ARG B NH2 
3583 N N   . PHE B 235 ? 0.0697 0.2484 0.0984 -0.0010 0.0764  -0.0023 235 PHE B N   
3584 C CA  . PHE B 235 ? 0.0664 0.2584 0.0973 0.0003  0.0738  -0.0083 235 PHE B CA  
3585 C C   . PHE B 235 ? 0.0629 0.2605 0.0942 0.0143  0.0701  0.0014  235 PHE B C   
3586 O O   . PHE B 235 ? 0.0641 0.2971 0.1027 0.0192  0.0734  -0.0049 235 PHE B O   
3587 C CB  . PHE B 235 ? 0.0853 0.2577 0.0956 -0.0044 0.0839  -0.0107 235 PHE B CB  
3588 C CG  . PHE B 235 ? 0.0807 0.2780 0.0902 -0.0061 0.0790  -0.0042 235 PHE B CG  
3589 C CD1 . PHE B 235 ? 0.1374 0.2925 0.1058 0.0181  0.0640  -0.0184 235 PHE B CD1 
3590 C CD2 . PHE B 235 ? 0.0832 0.3322 0.1138 0.0015  0.0822  -0.0050 235 PHE B CD2 
3591 C CE1 . PHE B 235 ? 0.1653 0.3107 0.1095 0.0107  0.0690  -0.0306 235 PHE B CE1 
3592 C CE2 . PHE B 235 ? 0.1400 0.3464 0.1331 0.0004  0.0568  -0.0181 235 PHE B CE2 
3593 C CZ  . PHE B 235 ? 0.1496 0.3261 0.1232 -0.0011 0.0529  -0.0228 235 PHE B CZ  
3594 N N   A SER B 236 ? 0.0623 0.2715 0.1069 0.0149  0.0748  0.0089  236 SER B N   
3595 N N   B SER B 236 ? 0.0647 0.2762 0.1181 0.0200  0.0802  0.0069  236 SER B N   
3596 C CA  A SER B 236 ? 0.0750 0.2854 0.1130 0.0126  0.0713  0.0223  236 SER B CA  
3597 C CA  B SER B 236 ? 0.0805 0.2934 0.1292 0.0191  0.0834  0.0201  236 SER B CA  
3598 C C   A SER B 236 ? 0.0599 0.2874 0.1307 0.0129  0.0816  0.0183  236 SER B C   
3599 C C   B SER B 236 ? 0.0663 0.2909 0.1468 0.0160  0.0911  0.0145  236 SER B C   
3600 O O   A SER B 236 ? 0.0693 0.3061 0.1245 0.0088  0.0857  0.0333  236 SER B O   
3601 O O   B SER B 236 ? 0.0563 0.3130 0.1876 0.0161  0.0950  0.0173  236 SER B O   
3602 C CB  A SER B 236 ? 0.0962 0.3057 0.1410 0.0020  0.0590  0.0222  236 SER B CB  
3603 C CB  B SER B 236 ? 0.1169 0.3199 0.1549 0.0078  0.0780  0.0194  236 SER B CB  
3604 O OG  A SER B 236 ? 0.1902 0.3271 0.1488 0.0053  0.0042  0.0263  236 SER B OG  
3605 O OG  B SER B 236 ? 0.1265 0.3656 0.2374 0.0259  0.0440  -0.0038 236 SER B OG  
3606 N N   . ALA B 237 ? 0.0795 0.2975 0.1902 0.0036  0.0810  0.0248  237 ALA B N   
3607 C CA  . ALA B 237 ? 0.1028 0.2937 0.2174 -0.0078 0.0886  0.0309  237 ALA B CA  
3608 C C   . ALA B 237 ? 0.1119 0.3073 0.2277 0.0043  0.0850  0.0525  237 ALA B C   
3609 O O   . ALA B 237 ? 0.0949 0.3206 0.2261 -0.0022 0.0737  0.0338  237 ALA B O   
3610 C CB  . ALA B 237 ? 0.1439 0.3082 0.2431 -0.0206 0.0809  0.0251  237 ALA B CB  
3611 N N   . SER B 238 ? 0.1724 0.3373 0.2499 -0.0089 0.0727  0.0822  238 SER B N   
3612 C CA  . SER B 238 ? 0.1636 0.3562 0.2601 -0.0134 0.0823  0.0792  238 SER B CA  
3613 C C   . SER B 238 ? 0.2169 0.3443 0.2941 -0.0201 0.0824  0.0613  238 SER B C   
3614 O O   . SER B 238 ? 0.1858 0.3539 0.3391 -0.0302 0.0925  0.0406  238 SER B O   
3615 C CB  . SER B 238 ? 0.2660 0.4016 0.2750 0.0222  0.0599  0.1031  238 SER B CB  
3616 O OG  . SER B 238 ? 0.4034 0.5145 0.3805 -0.0403 0.0252  0.1521  238 SER B OG  
3617 N N   . GLY B 239 ? 0.2129 0.3362 0.2959 -0.0181 0.0742  0.0656  239 GLY B N   
3618 C CA  . GLY B 239 ? 0.1719 0.3060 0.2825 -0.0286 0.1008  0.0747  239 GLY B CA  
3619 C C   . GLY B 239 ? 0.1450 0.2798 0.2859 -0.0217 0.0986  0.0584  239 GLY B C   
3620 O O   . GLY B 239 ? 0.1525 0.2915 0.2731 -0.0147 0.1096  0.0416  239 GLY B O   
3621 N N   . LEU B 240 ? 0.1034 0.2697 0.2345 -0.0125 0.1006  0.0385  240 LEU B N   
3622 C CA  . LEU B 240 ? 0.1296 0.2540 0.2137 -0.0018 0.1020  0.0170  240 LEU B CA  
3623 C C   . LEU B 240 ? 0.1232 0.2624 0.2280 -0.0118 0.0853  0.0035  240 LEU B C   
3624 O O   . LEU B 240 ? 0.1086 0.2929 0.2336 -0.0027 0.1024  -0.0105 240 LEU B O   
3625 C CB  . LEU B 240 ? 0.1273 0.2725 0.2068 -0.0011 0.1230  0.0095  240 LEU B CB  
3626 C CG  . LEU B 240 ? 0.1126 0.3066 0.1807 -0.0056 0.1359  0.0050  240 LEU B CG  
3627 C CD1 . LEU B 240 ? 0.1206 0.3218 0.1993 -0.0268 0.1280  0.0148  240 LEU B CD1 
3628 C CD2 . LEU B 240 ? 0.1190 0.3075 0.2073 -0.0119 0.1186  0.0144  240 LEU B CD2 
3629 N N   . LEU B 241 ? 0.1024 0.2675 0.2075 -0.0167 0.0795  -0.0083 241 LEU B N   
3630 C CA  . LEU B 241 ? 0.0975 0.2701 0.2035 -0.0160 0.0921  -0.0064 241 LEU B CA  
3631 C C   . LEU B 241 ? 0.1150 0.2879 0.2059 -0.0267 0.1020  -0.0063 241 LEU B C   
3632 O O   . LEU B 241 ? 0.1103 0.2925 0.1840 -0.0297 0.0986  -0.0212 241 LEU B O   
3633 C CB  . LEU B 241 ? 0.0873 0.2832 0.2104 0.0026  0.0771  -0.0120 241 LEU B CB  
3634 C CG  . LEU B 241 ? 0.0883 0.3133 0.2175 0.0060  0.0894  -0.0323 241 LEU B CG  
3635 C CD1 . LEU B 241 ? 0.1204 0.3323 0.2200 0.0185  0.0958  -0.0399 241 LEU B CD1 
3636 C CD2 . LEU B 241 ? 0.1295 0.3396 0.2338 -0.0030 0.0761  -0.0500 241 LEU B CD2 
3637 N N   . ALA B 242 ? 0.1139 0.2915 0.2397 -0.0328 0.1052  -0.0047 242 ALA B N   
3638 C CA  . ALA B 242 ? 0.1548 0.3022 0.2692 -0.0467 0.1066  -0.0008 242 ALA B CA  
3639 C C   . ALA B 242 ? 0.1427 0.2888 0.2752 -0.0464 0.1323  -0.0191 242 ALA B C   
3640 O O   . ALA B 242 ? 0.1641 0.3506 0.2809 -0.0669 0.1165  -0.0180 242 ALA B O   
3641 C CB  . ALA B 242 ? 0.1898 0.3211 0.2856 -0.0463 0.0954  0.0183  242 ALA B CB  
3642 N N   . SER B 243 ? 0.1202 0.2988 0.2830 -0.0387 0.1209  -0.0373 243 SER B N   
3643 C CA  . SER B 243 ? 0.1515 0.2983 0.3014 -0.0453 0.1317  -0.0531 243 SER B CA  
3644 C C   . SER B 243 ? 0.1229 0.2965 0.2735 -0.0307 0.1302  -0.0735 243 SER B C   
3645 O O   . SER B 243 ? 0.1626 0.3146 0.2830 -0.0392 0.1182  -0.0754 243 SER B O   
3646 C CB  . SER B 243 ? 0.1631 0.3101 0.3018 -0.0451 0.1598  -0.0531 243 SER B CB  
3647 O OG  . SER B 243 ? 0.1547 0.3488 0.3294 -0.0303 0.1662  -0.0483 243 SER B OG  
3648 N N   . LEU B 244 ? 0.1257 0.2963 0.2424 -0.0264 0.1127  -0.0511 244 LEU B N   
3649 C CA  . LEU B 244 ? 0.1089 0.3083 0.2091 -0.0305 0.0874  -0.0587 244 LEU B CA  
3650 C C   . LEU B 244 ? 0.1099 0.3288 0.2379 -0.0310 0.0803  -0.0638 244 LEU B C   
3651 O O   . LEU B 244 ? 0.1090 0.3476 0.2442 -0.0361 0.0802  -0.0658 244 LEU B O   
3652 C CB  . LEU B 244 ? 0.0848 0.3016 0.1861 -0.0276 0.0767  -0.0483 244 LEU B CB  
3653 C CG  . LEU B 244 ? 0.0798 0.3229 0.1808 -0.0299 0.0705  -0.0621 244 LEU B CG  
3654 C CD1 . LEU B 244 ? 0.1174 0.3278 0.1745 -0.0377 0.0713  -0.0572 244 LEU B CD1 
3655 C CD2 . LEU B 244 ? 0.0985 0.3409 0.1856 -0.0293 0.0800  -0.0679 244 LEU B CD2 
3656 N N   . LEU B 245 ? 0.0839 0.3248 0.2294 -0.0343 0.0930  -0.0467 245 LEU B N   
3657 C CA  . LEU B 245 ? 0.0862 0.3457 0.2600 -0.0386 0.1034  -0.0474 245 LEU B CA  
3658 C C   . LEU B 245 ? 0.1239 0.3519 0.2794 -0.0582 0.1211  -0.0480 245 LEU B C   
3659 O O   . LEU B 245 ? 0.1201 0.3845 0.3357 -0.0767 0.1066  -0.0765 245 LEU B O   
3660 C CB  . LEU B 245 ? 0.0617 0.3707 0.2540 -0.0371 0.1161  -0.0400 245 LEU B CB  
3661 C CG  . LEU B 245 ? 0.0868 0.3844 0.2529 -0.0404 0.1060  -0.0407 245 LEU B CG  
3662 C CD1 . LEU B 245 ? 0.1269 0.3976 0.2411 -0.0279 0.1200  -0.0420 245 LEU B CD1 
3663 C CD2 . LEU B 245 ? 0.1139 0.3754 0.2429 -0.0486 0.0859  -0.0349 245 LEU B CD2 
3664 N N   . LYS B 246 ? 0.1329 0.3475 0.3428 -0.0647 0.1164  -0.0683 246 LYS B N   
3665 C CA  . LYS B 246 ? 0.1519 0.3652 0.3843 -0.1070 0.1593  -0.0549 246 LYS B CA  
3666 C C   . LYS B 246 ? 0.1666 0.3679 0.3891 -0.1090 0.1349  -0.0804 246 LYS B C   
3667 O O   . LYS B 246 ? 0.1937 0.4010 0.4072 -0.0968 0.1139  -0.1013 246 LYS B O   
3668 C CB  . LYS B 246 ? 0.2270 0.3768 0.4654 -0.0805 0.1320  -0.0582 246 LYS B CB  
3669 C CG  . LYS B 246 ? 0.3353 0.4006 0.5551 -0.0653 0.1120  -0.0583 246 LYS B CG  
3670 C CD  . LYS B 246 ? 0.4152 0.4604 0.6353 -0.0335 0.1137  -0.0583 246 LYS B CD  
3671 C CE  . LYS B 246 ? 0.5469 0.4523 0.7052 -0.0066 0.0948  -0.0699 246 LYS B CE  
3672 N NZ  . LYS B 246 ? 0.5772 0.5196 0.7474 0.0186  0.0933  -0.0686 246 LYS B NZ  
3673 N N   . ALA B 247 ? 0.1650 0.3810 0.3284 -0.0967 0.1248  -0.0949 247 ALA B N   
3674 C CA  . ALA B 247 ? 0.2127 0.3843 0.3300 -0.0749 0.1120  -0.0851 247 ALA B CA  
3675 C C   . ALA B 247 ? 0.1866 0.4230 0.3440 -0.0861 0.0909  -0.1001 247 ALA B C   
3676 O O   . ALA B 247 ? 0.2552 0.4875 0.3486 -0.0517 0.0716  -0.1475 247 ALA B O   
3677 C CB  . ALA B 247 ? 0.2283 0.3856 0.2897 -0.0774 0.1104  -0.0841 247 ALA B CB  
3678 N N   . LEU B 248 ? 0.1766 0.4298 0.3290 -0.0685 0.0594  -0.1165 248 LEU B N   
3679 C CA  . LEU B 248 ? 0.1332 0.4586 0.3467 -0.0720 0.0776  -0.0882 248 LEU B CA  
3680 C C   . LEU B 248 ? 0.1561 0.4882 0.3908 -0.1080 0.0754  -0.0612 248 LEU B C   
3681 O O   . LEU B 248 ? 0.1912 0.5557 0.4713 -0.0676 0.0024  -0.0526 248 LEU B O   
3682 C CB  . LEU B 248 ? 0.1232 0.4520 0.3048 -0.0557 0.0857  -0.0788 248 LEU B CB  
3683 C CG  . LEU B 248 ? 0.1282 0.4640 0.3036 -0.0429 0.1050  -0.0833 248 LEU B CG  
3684 C CD1 . LEU B 248 ? 0.1478 0.4551 0.3151 -0.0249 0.0963  -0.0908 248 LEU B CD1 
3685 C CD2 . LEU B 248 ? 0.2177 0.4663 0.3211 -0.0540 0.0870  -0.0724 248 LEU B CD2 
3686 N N   . GLY B 249 ? 0.2074 0.5090 0.4556 -0.1048 0.0500  -0.0643 249 GLY B N   
3687 C CA  . GLY B 249 ? 0.1760 0.5511 0.4976 -0.1139 0.0882  -0.0640 249 GLY B CA  
3688 C C   . GLY B 249 ? 0.0785 0.5847 0.5506 -0.0828 0.1203  -0.0922 249 GLY B C   
3689 O O   . GLY B 249 ? 0.1516 0.6799 0.5996 -0.1573 0.1822  -0.0429 249 GLY B O   
3690 N N   . HIS B 250 ? 0.1878 0.5729 0.5108 -0.1447 0.1484  -0.0797 250 HIS B N   
3691 C CA  . HIS B 250 ? 0.1966 0.5384 0.4834 -0.1033 0.2018  -0.0447 250 HIS B CA  
3692 C C   . HIS B 250 ? 0.2432 0.6054 0.5057 -0.0718 0.1352  -0.0113 250 HIS B C   
3693 O O   . HIS B 250 ? 0.3349 0.6011 0.4644 -0.1449 0.0955  0.0782  250 HIS B O   
3694 C CB  . HIS B 250 ? 0.1957 0.5489 0.5203 -0.0980 0.2162  -0.0605 250 HIS B CB  
3695 C CG  . HIS B 250 ? 0.2158 0.5448 0.5774 -0.1119 0.1925  -0.0495 250 HIS B CG  
3696 N ND1 . HIS B 250 ? 0.2709 0.5606 0.6355 -0.1080 0.1441  -0.0205 250 HIS B ND1 
3697 C CD2 . HIS B 250 ? 0.2044 0.5276 0.5662 -0.0954 0.1830  -0.0555 250 HIS B CD2 
3698 C CE1 . HIS B 250 ? 0.2622 0.4944 0.5767 -0.0905 0.1398  -0.0740 250 HIS B CE1 
3699 N NE2 . HIS B 250 ? 0.2383 0.5280 0.5936 -0.0890 0.1305  -0.0724 250 HIS B NE2 
3700 C C1  . GOL C .   ? 0.3627 0.5266 0.4079 0.0066  -0.0592 -0.0957 301 GOL A C1  
3701 O O1  . GOL C .   ? 0.2907 0.5278 0.3364 0.0076  -0.0068 -0.0856 301 GOL A O1  
3702 C C2  . GOL C .   ? 0.4365 0.5498 0.4614 0.0185  -0.0658 -0.0732 301 GOL A C2  
3703 O O2  . GOL C .   ? 0.3112 0.5565 0.5233 0.0658  -0.0179 -0.0698 301 GOL A O2  
3704 C C3  . GOL C .   ? 0.4401 0.5451 0.4430 0.0318  -0.0438 -0.0426 301 GOL A C3  
3705 O O3  . GOL C .   ? 0.4871 0.4915 0.4956 0.0146  -0.0594 -0.0019 301 GOL A O3  
3706 C C1  . GOL D .   ? 0.3510 0.4457 0.4580 0.0070  0.1191  -0.0151 301 GOL B C1  
3707 O O1  . GOL D .   ? 0.4003 0.5629 0.4541 0.0401  0.1792  -0.0187 301 GOL B O1  
3708 C C2  . GOL D .   ? 0.3484 0.4143 0.2869 0.0030  0.0875  0.0049  301 GOL B C2  
3709 O O2  . GOL D .   ? 0.2742 0.3952 0.2919 0.0285  0.0966  -0.0082 301 GOL B O2  
3710 C C3  . GOL D .   ? 0.2725 0.4680 0.2805 -0.0428 0.0694  0.0161  301 GOL B C3  
3711 O O3  . GOL D .   ? 0.2879 0.4584 0.2509 -0.0729 0.0539  0.0598  301 GOL B O3  
3712 C C1  . GOL E .   ? 0.4334 0.6436 0.2651 -0.0127 0.1616  -0.0774 302 GOL B C1  
3713 O O1  . GOL E .   ? 0.4445 0.7047 0.2906 0.0041  0.1714  -0.0145 302 GOL B O1  
3714 C C2  . GOL E .   ? 0.3846 0.6612 0.2785 -0.0242 0.1887  -0.0836 302 GOL B C2  
3715 O O2  . GOL E .   ? 0.4347 0.6475 0.4348 -0.0759 0.1906  -0.0532 302 GOL B O2  
3716 C C3  . GOL E .   ? 0.4229 0.6371 0.3971 -0.0563 0.0967  -0.0298 302 GOL B C3  
3717 O O3  . GOL E .   ? 0.3132 0.6112 0.4099 0.0205  0.0183  -0.0334 302 GOL B O3  
3718 C C1  . GOL F .   ? 0.4509 0.7147 0.3780 -0.0407 0.0918  0.0679  303 GOL B C1  
3719 O O1  . GOL F .   ? 0.4681 0.7794 0.5346 -0.1014 0.0081  0.0848  303 GOL B O1  
3720 C C2  . GOL F .   ? 0.4039 0.6404 0.4357 -0.0206 0.0708  0.0599  303 GOL B C2  
3721 O O2  . GOL F .   ? 0.4304 0.5963 0.3967 -0.0478 0.0791  0.0162  303 GOL B O2  
3722 C C3  . GOL F .   ? 0.3824 0.6067 0.4167 0.0486  0.0706  0.1000  303 GOL B C3  
3723 O O3  . GOL F .   ? 0.3370 0.5819 0.5406 0.1051  0.0328  0.1939  303 GOL B O3  
3724 C C1  . GOL G .   ? 0.4638 0.5047 0.1867 0.0106  -0.0003 -0.0176 304 GOL B C1  
3725 O O1  . GOL G .   ? 0.5098 0.5056 0.2757 -0.0578 0.0083  -0.0097 304 GOL B O1  
3726 C C2  . GOL G .   ? 0.4245 0.5587 0.2983 -0.0204 0.0090  0.0092  304 GOL B C2  
3727 O O2  . GOL G .   ? 0.3848 0.6052 0.2975 -0.0050 -0.0183 0.0175  304 GOL B O2  
3728 C C3  . GOL G .   ? 0.4056 0.6426 0.3983 -0.0479 0.0415  0.0239  304 GOL B C3  
3729 O O3  . GOL G .   ? 0.4436 0.6802 0.4542 -0.0429 0.0307  0.0309  304 GOL B O3  
3730 O O   . HOH H .   ? 0.7127 0.6930 0.3228 0.1983  0.0210  0.0702  401 HOH A O   
3731 O O   A HOH H .   ? 0.1036 0.4145 0.2155 -0.0395 0.0644  -0.0035 402 HOH A O   
3732 O O   B HOH H .   ? 0.0988 0.3666 0.2001 0.0210  0.1335  0.0506  402 HOH A O   
3733 O O   . HOH H .   ? 0.4779 0.7361 0.3804 -0.0461 0.1573  0.0553  403 HOH A O   
3734 O O   . HOH H .   ? 0.2931 0.4654 0.3455 -0.0783 0.0580  0.0371  404 HOH A O   
3735 O O   . HOH H .   ? 0.2878 0.4149 0.2651 -0.0261 0.0791  0.0551  405 HOH A O   
3736 O O   . HOH H .   ? 0.2508 0.7058 0.6080 0.0352  0.1010  0.2449  406 HOH A O   
3737 O O   . HOH H .   ? 0.7242 0.6627 0.6029 -0.0298 0.1796  0.0708  407 HOH A O   
3738 O O   . HOH H .   ? 0.3275 0.5166 0.2431 0.0383  0.1513  0.1178  408 HOH A O   
3739 O O   . HOH H .   ? 0.2142 0.5259 0.2460 0.0029  0.1185  0.0186  409 HOH A O   
3740 O O   . HOH H .   ? 0.5444 0.8634 0.3288 -0.0888 0.1300  0.0318  410 HOH A O   
3741 O O   . HOH H .   ? 0.3134 0.3973 0.2522 0.0414  0.1017  -0.0346 411 HOH A O   
3742 O O   . HOH H .   ? 0.1111 0.3212 0.1293 -0.0107 0.0766  0.0158  412 HOH A O   
3743 O O   . HOH H .   ? 0.1977 0.3855 0.2373 0.0111  0.0623  -0.0528 413 HOH A O   
3744 O O   . HOH H .   ? 0.3134 1.0906 0.3528 0.1269  0.0827  0.1163  414 HOH A O   
3745 O O   . HOH H .   ? 0.4580 0.3252 0.1791 -0.0174 0.0106  -0.0250 415 HOH A O   
3746 O O   . HOH H .   ? 0.2738 0.4690 0.6150 -0.1434 0.0008  0.1325  416 HOH A O   
3747 O O   . HOH H .   ? 0.2570 0.6372 0.3392 -0.0954 0.0134  -0.0133 417 HOH A O   
3748 O O   . HOH H .   ? 0.3157 0.4304 0.9205 0.0359  0.3074  0.0697  418 HOH A O   
3749 O O   . HOH H .   ? 0.0797 0.4557 0.2451 -0.0195 0.1151  -0.0040 419 HOH A O   
3750 O O   . HOH H .   ? 0.2234 0.5346 0.6004 -0.0066 -0.0458 -0.0470 420 HOH A O   
3751 O O   . HOH H .   ? 0.7927 0.6011 0.2408 0.3181  -0.1413 -0.0930 421 HOH A O   
3752 O O   . HOH H .   ? 0.4102 0.3888 0.3574 -0.0717 -0.0935 0.0252  422 HOH A O   
3753 O O   . HOH H .   ? 0.4376 0.6146 0.9507 -0.0842 0.1096  0.0399  423 HOH A O   
3754 O O   . HOH H .   ? 0.4748 0.6756 0.5444 0.0849  0.1855  0.2557  424 HOH A O   
3755 O O   . HOH H .   ? 0.1807 0.4045 0.1439 -0.0064 0.0611  -0.0604 425 HOH A O   
3756 O O   . HOH H .   ? 0.5393 0.6348 0.5779 -0.2988 0.3359  -0.2235 426 HOH A O   
3757 O O   . HOH H .   ? 0.3120 0.3003 0.3042 -0.0024 0.1143  -0.0381 427 HOH A O   
3758 O O   . HOH H .   ? 0.1099 0.4521 0.4144 0.0110  0.0896  -0.0791 428 HOH A O   
3759 O O   . HOH H .   ? 0.2037 0.4798 0.4205 -0.0151 0.1368  0.1270  429 HOH A O   
3760 O O   . HOH H .   ? 0.2653 0.4028 0.1484 -0.0575 0.1036  -0.0118 430 HOH A O   
3761 O O   . HOH H .   ? 0.2758 0.5514 0.4704 -0.1096 0.1264  -0.0844 431 HOH A O   
3762 O O   . HOH H .   ? 0.3852 0.9479 0.4584 0.0664  0.0985  -0.0524 432 HOH A O   
3763 O O   . HOH H .   ? 0.0660 0.3495 0.1280 0.0015  0.0588  -0.0099 433 HOH A O   
3764 O O   . HOH H .   ? 0.4438 0.5955 0.4128 -0.0767 0.0870  -0.0830 434 HOH A O   
3765 O O   . HOH H .   ? 0.4065 1.0532 0.5729 -0.3469 -0.0132 0.0276  435 HOH A O   
3766 O O   . HOH H .   ? 0.1433 0.6248 0.2799 -0.0944 0.1209  -0.1751 436 HOH A O   
3767 O O   . HOH H .   ? 0.6739 0.7857 0.4953 -0.1625 -0.2445 -0.0689 437 HOH A O   
3768 O O   . HOH H .   ? 0.1401 0.3670 0.1013 0.0385  0.0594  -0.0040 438 HOH A O   
3769 O O   . HOH H .   ? 0.1123 0.4492 0.1170 -0.0305 0.0424  -0.0166 439 HOH A O   
3770 O O   . HOH H .   ? 0.3056 0.4872 0.2036 0.0468  0.0342  -0.0304 440 HOH A O   
3771 O O   . HOH H .   ? 0.2197 0.3970 0.1142 -0.0491 0.0769  -0.0408 441 HOH A O   
3772 O O   . HOH H .   ? 0.0827 0.3148 0.1303 -0.0209 0.0798  0.0119  442 HOH A O   
3773 O O   . HOH H .   ? 0.1992 0.4084 0.2252 -0.0565 0.1387  -0.0284 443 HOH A O   
3774 O O   . HOH H .   ? 0.2443 1.0077 0.3294 0.0527  0.0835  0.0368  444 HOH A O   
3775 O O   . HOH H .   ? 0.1473 0.3298 0.0908 -0.0425 0.0496  -0.0053 445 HOH A O   
3776 O O   . HOH H .   ? 0.3888 0.7180 0.3533 0.2278  0.1042  0.0825  446 HOH A O   
3777 O O   . HOH H .   ? 0.1782 0.4897 0.1963 -0.0527 0.1270  -0.0040 447 HOH A O   
3778 O O   . HOH H .   ? 0.3867 0.5159 0.7073 0.1090  0.0431  -0.1431 448 HOH A O   
3779 O O   . HOH H .   ? 0.4380 0.9207 0.3073 -0.0485 -0.0062 0.0362  449 HOH A O   
3780 O O   . HOH H .   ? 0.1997 0.6986 0.4418 0.1510  0.0564  -0.0470 450 HOH A O   
3781 O O   . HOH H .   ? 0.0827 0.3404 0.0963 -0.0228 0.0816  -0.0125 451 HOH A O   
3782 O O   . HOH H .   ? 0.1943 0.3195 0.1502 0.0285  0.0521  -0.0160 452 HOH A O   
3783 O O   . HOH H .   ? 0.5872 0.4981 0.4203 -0.0726 -0.0579 -0.0392 453 HOH A O   
3784 O O   . HOH H .   ? 0.4535 0.4497 0.1729 -0.0370 0.0281  -0.0181 454 HOH A O   
3785 O O   . HOH H .   ? 0.4226 0.4246 0.2932 -0.0714 0.1543  -0.0910 455 HOH A O   
3786 O O   . HOH H .   ? 0.4183 0.5703 0.1689 0.0979  0.1144  0.0454  456 HOH A O   
3787 O O   . HOH H .   ? 0.2391 0.8373 0.4499 0.0308  0.0112  0.0051  457 HOH A O   
3788 O O   . HOH H .   ? 0.3402 0.4630 0.4741 -0.0208 0.1511  0.0050  458 HOH A O   
3789 O O   . HOH H .   ? 0.2232 0.6255 0.3618 -0.0711 0.1017  0.0529  459 HOH A O   
3790 O O   . HOH H .   ? 0.0896 0.4746 0.1445 -0.0002 0.0786  -0.0205 460 HOH A O   
3791 O O   . HOH H .   ? 0.2919 0.6448 0.3517 -0.0898 0.1358  -0.0776 461 HOH A O   
3792 O O   . HOH H .   ? 0.2308 0.5487 0.3978 0.0563  -0.0112 -0.1964 462 HOH A O   
3793 O O   . HOH H .   ? 0.1837 0.3690 0.1257 -0.0152 0.0899  -0.0222 463 HOH A O   
3794 O O   . HOH H .   ? 0.1823 0.5204 0.3416 -0.0867 0.1270  -0.1185 464 HOH A O   
3795 O O   . HOH H .   ? 0.3331 0.9130 0.6906 0.1857  0.1414  0.3107  465 HOH A O   
3796 O O   . HOH H .   ? 0.4323 0.5506 0.2581 0.0518  -0.0032 -0.0951 466 HOH A O   
3797 O O   . HOH H .   ? 0.2639 0.7145 0.5910 0.0647  0.0428  -0.0781 467 HOH A O   
3798 O O   . HOH H .   ? 0.3081 0.4294 0.2838 -0.0295 0.0407  0.0573  468 HOH A O   
3799 O O   . HOH H .   ? 0.1190 0.4192 0.1305 0.0232  0.0381  -0.0391 469 HOH A O   
3800 O O   . HOH H .   ? 0.0996 0.3896 0.0964 0.0047  0.0883  -0.0106 470 HOH A O   
3801 O O   . HOH H .   ? 0.1813 0.5602 0.2034 0.0247  0.0654  -0.0684 471 HOH A O   
3802 O O   . HOH H .   ? 0.2844 0.5139 0.1753 0.0130  0.0646  -0.0083 472 HOH A O   
3803 O O   . HOH H .   ? 0.1645 0.5316 0.3048 0.0026  0.1034  0.0273  473 HOH A O   
3804 O O   . HOH H .   ? 0.4123 0.6328 0.2803 0.0974  0.0436  -0.0715 474 HOH A O   
3805 O O   . HOH H .   ? 0.6745 0.9182 0.6055 0.0775  0.1587  -0.0458 475 HOH A O   
3806 O O   . HOH H .   ? 0.3988 0.9492 0.2718 0.2238  0.0644  0.1760  476 HOH A O   
3807 O O   . HOH H .   ? 0.1915 0.4378 0.1289 0.0296  0.0545  -0.0597 477 HOH A O   
3808 O O   . HOH H .   ? 0.2535 0.3939 0.4119 0.0218  0.1159  0.0201  478 HOH A O   
3809 O O   . HOH H .   ? 0.4093 0.6528 0.8061 -0.0577 0.0624  -0.0362 479 HOH A O   
3810 O O   . HOH H .   ? 0.3020 0.6308 0.2134 -0.0876 0.0616  0.0685  480 HOH A O   
3811 O O   . HOH H .   ? 0.3305 0.8955 0.2291 -0.0601 0.0162  -0.2015 481 HOH A O   
3812 O O   . HOH H .   ? 0.2832 0.5626 0.5309 0.0488  0.0022  -0.1033 482 HOH A O   
3813 O O   . HOH H .   ? 0.4558 0.9543 0.3530 -0.0883 -0.0033 0.1574  483 HOH A O   
3814 O O   . HOH H .   ? 0.1686 0.4424 0.2736 -0.0051 0.0792  0.0080  484 HOH A O   
3815 O O   . HOH H .   ? 0.3271 0.9421 0.6302 0.0676  0.1285  -0.0081 485 HOH A O   
3816 O O   . HOH H .   ? 0.2538 0.7315 0.4720 0.1489  -0.1156 -0.3079 486 HOH A O   
3817 O O   . HOH H .   ? 0.7171 0.6095 0.4402 -0.2394 0.0287  -0.1122 487 HOH A O   
3818 O O   . HOH H .   ? 0.3594 0.9247 0.4209 0.0719  0.0957  -0.0185 488 HOH A O   
3819 O O   . HOH H .   ? 0.2639 1.0693 0.6008 -0.1067 -0.0425 -0.2063 489 HOH A O   
3820 O O   . HOH H .   ? 0.3702 0.4380 0.4408 -0.0313 0.0564  -0.0227 490 HOH A O   
3821 O O   . HOH H .   ? 0.7993 0.3968 1.0680 -0.0072 -0.1582 -0.0312 491 HOH A O   
3822 O O   . HOH H .   ? 0.5979 0.8337 0.4610 0.1922  -0.1802 -0.0351 492 HOH A O   
3823 O O   . HOH H .   ? 0.4930 0.8166 0.3256 0.0152  0.1924  -0.0927 493 HOH A O   
3824 O O   . HOH H .   ? 0.5508 1.0728 0.2970 -0.1004 -0.0938 0.1171  494 HOH A O   
3825 O O   . HOH H .   ? 0.3704 0.5025 0.3711 -0.0746 0.1148  0.1003  495 HOH A O   
3826 O O   . HOH H .   ? 0.2958 0.4148 0.1124 -0.0494 0.0870  -0.0380 496 HOH A O   
3827 O O   . HOH H .   ? 1.0427 0.6470 0.3111 0.2228  0.0376  0.0417  497 HOH A O   
3828 O O   . HOH H .   ? 0.3011 0.4475 0.4312 -0.0194 0.0788  0.0120  498 HOH A O   
3829 O O   . HOH H .   ? 0.6421 1.1967 0.8090 -0.0696 -0.2571 0.3093  499 HOH A O   
3830 O O   . HOH H .   ? 0.3255 0.7464 0.3820 0.0447  0.0536  -0.0099 500 HOH A O   
3831 O O   . HOH H .   ? 0.2132 0.7256 0.4266 -0.0664 0.1347  -0.1314 501 HOH A O   
3832 O O   . HOH H .   ? 0.2500 0.5635 0.5231 0.0313  0.0086  0.1134  502 HOH A O   
3833 O O   . HOH H .   ? 0.5850 0.4303 0.3728 -0.1035 0.0877  0.0232  503 HOH A O   
3834 O O   . HOH H .   ? 0.2693 1.0283 0.2286 0.0464  0.0653  -0.0207 504 HOH A O   
3835 O O   . HOH H .   ? 0.6140 0.9354 1.0729 0.1661  0.1717  -0.2107 505 HOH A O   
3836 O O   . HOH H .   ? 0.3538 0.9377 0.4829 0.0134  -0.0187 -0.1314 506 HOH A O   
3837 O O   . HOH H .   ? 0.5535 0.6096 0.5504 -0.1302 0.0494  -0.0872 507 HOH A O   
3838 O O   . HOH H .   ? 0.2583 0.5584 0.3870 0.0263  0.0830  -0.1552 508 HOH A O   
3839 O O   . HOH H .   ? 0.8289 0.9841 0.5037 0.0591  -0.1701 -0.0173 509 HOH A O   
3840 O O   . HOH H .   ? 0.2763 0.6400 0.4165 -0.1378 0.0732  0.0121  510 HOH A O   
3841 O O   . HOH H .   ? 0.8331 0.5187 0.7045 -0.1771 -0.0537 -0.0383 511 HOH A O   
3842 O O   . HOH H .   ? 0.6088 0.6759 0.6811 -0.2621 0.4129  -0.1426 512 HOH A O   
3843 O O   . HOH I .   ? 0.2304 0.4356 0.3330 0.0275  0.1990  0.0392  401 HOH B O   
3844 O O   . HOH I .   ? 0.3184 0.5405 0.3857 0.0291  0.1165  0.0515  402 HOH B O   
3845 O O   . HOH I .   ? 0.2673 0.5946 0.5993 -0.0307 0.1827  -0.2474 403 HOH B O   
3846 O O   . HOH I .   ? 0.8317 0.7725 0.3352 0.0906  0.2313  -0.1075 404 HOH B O   
3847 O O   . HOH I .   ? 0.2365 0.4643 0.3118 0.0708  0.1955  0.0315  405 HOH B O   
3848 O O   . HOH I .   ? 0.4010 0.3652 0.1637 0.0014  0.0266  0.0319  406 HOH B O   
3849 O O   . HOH I .   ? 0.6502 0.4983 0.8862 -0.1380 0.4058  -0.0793 407 HOH B O   
3850 O O   . HOH I .   ? 0.3368 0.5594 0.4670 -0.0572 0.2260  -0.0357 408 HOH B O   
3851 O O   . HOH I .   ? 0.1769 0.7212 0.4044 -0.1227 0.0127  0.1625  409 HOH B O   
3852 O O   . HOH I .   ? 0.0937 0.2924 0.1414 -0.0091 0.0690  -0.0166 410 HOH B O   
3853 O O   . HOH I .   ? 0.4758 0.4005 0.3253 0.0973  0.2416  0.0338  411 HOH B O   
3854 O O   . HOH I .   ? 0.3207 0.4041 0.2747 -0.0002 0.0079  0.0847  412 HOH B O   
3855 O O   . HOH I .   ? 0.2599 0.4106 0.2109 -0.0359 0.1578  0.0337  413 HOH B O   
3856 O O   . HOH I .   ? 0.1868 0.5791 0.1521 -0.0758 0.1074  -0.0218 414 HOH B O   
3857 O O   . HOH I .   ? 0.1475 0.2786 0.1361 -0.0209 0.0881  -0.0145 415 HOH B O   
3858 O O   . HOH I .   ? 0.2529 0.7599 0.4481 -0.1444 0.1518  -0.0959 416 HOH B O   
3859 O O   . HOH I .   ? 0.0977 0.3615 0.1743 0.0176  0.0941  0.0129  417 HOH B O   
3860 O O   . HOH I .   ? 0.1778 0.4450 0.1197 0.0280  0.0772  -0.0209 418 HOH B O   
3861 O O   . HOH I .   ? 0.1616 0.3755 0.1017 0.0193  0.1120  -0.0100 419 HOH B O   
3862 O O   . HOH I .   ? 0.5842 0.4057 0.5708 -0.1109 0.1203  -0.0105 420 HOH B O   
3863 O O   . HOH I .   ? 0.2034 0.3499 0.1077 0.0310  0.0992  0.0274  421 HOH B O   
3864 O O   . HOH I .   ? 0.5392 0.8729 0.3735 0.2501  0.1256  -0.1270 422 HOH B O   
3865 O O   . HOH I .   ? 0.2249 0.3709 0.3354 -0.0202 0.0243  0.0814  423 HOH B O   
3866 O O   . HOH I .   ? 0.9267 0.4709 0.3658 0.0974  -0.0618 0.0296  424 HOH B O   
3867 O O   . HOH I .   ? 0.4253 0.4180 0.2034 -0.0056 0.0995  -0.1256 425 HOH B O   
3868 O O   . HOH I .   ? 0.3374 0.4158 0.4924 0.0230  -0.1118 0.0342  426 HOH B O   
3869 O O   . HOH I .   ? 0.2795 0.4718 0.5146 -0.0067 0.0740  0.1811  427 HOH B O   
3870 O O   . HOH I .   ? 0.9809 0.5332 0.4042 -0.3781 0.2248  0.0061  428 HOH B O   
3871 O O   . HOH I .   ? 0.4563 0.4673 0.3547 0.0692  -0.0299 -0.0555 429 HOH B O   
3872 O O   . HOH I .   ? 0.1107 0.5237 0.3524 0.0258  0.1195  0.0106  430 HOH B O   
3873 O O   . HOH I .   ? 0.1724 0.4150 0.2471 0.0746  0.1600  0.1292  431 HOH B O   
3874 O O   . HOH I .   ? 0.2514 0.5427 0.7896 0.0860  0.0266  0.2770  432 HOH B O   
3875 O O   . HOH I .   ? 0.1201 0.3311 0.1581 0.0145  0.0287  -0.0426 433 HOH B O   
3876 O O   . HOH I .   ? 0.2007 0.3700 0.2480 0.0388  0.1241  -0.0233 434 HOH B O   
3877 O O   . HOH I .   ? 0.0721 0.2546 0.0972 0.0168  0.0636  -0.0123 435 HOH B O   
3878 O O   . HOH I .   ? 0.0766 0.2993 0.1043 0.0035  0.0447  -0.0088 436 HOH B O   
3879 O O   . HOH I .   ? 0.4148 0.3902 0.4904 0.0009  0.2115  0.0738  437 HOH B O   
3880 O O   . HOH I .   ? 0.1237 0.2969 0.0995 0.0320  0.0388  -0.0088 438 HOH B O   
3881 O O   . HOH I .   ? 0.3362 0.5091 0.1827 0.0818  0.1112  0.0626  439 HOH B O   
3882 O O   . HOH I .   ? 0.0860 0.3046 0.1564 -0.0059 0.0600  0.0021  440 HOH B O   
3883 O O   . HOH I .   ? 0.2010 0.4132 0.1029 -0.0095 0.0521  0.0022  441 HOH B O   
3884 O O   . HOH I .   ? 0.1599 0.3660 0.2187 0.0004  0.0473  -0.0276 442 HOH B O   
3885 O O   . HOH I .   ? 0.0924 0.2704 0.0966 0.0153  0.0584  -0.0017 443 HOH B O   
3886 O O   . HOH I .   ? 0.6398 0.5996 0.5347 0.0679  0.1226  0.1006  444 HOH B O   
3887 O O   . HOH I .   ? 0.3497 0.5454 0.5428 -0.1286 0.1823  -0.0472 445 HOH B O   
3888 O O   . HOH I .   ? 0.2232 0.5212 0.6244 -0.0009 0.0583  -0.0491 446 HOH B O   
3889 O O   . HOH I .   ? 0.5468 0.4434 0.1615 0.0668  0.1549  -0.0314 447 HOH B O   
3890 O O   . HOH I .   ? 0.5718 0.3567 0.2279 -0.0840 0.1156  -0.0431 448 HOH B O   
3891 O O   . HOH I .   ? 0.2258 0.6110 0.4262 -0.0452 0.0849  0.1829  449 HOH B O   
3892 O O   . HOH I .   ? 0.1075 0.3165 0.1261 -0.0026 0.0712  0.0296  450 HOH B O   
3893 O O   . HOH I .   ? 0.1958 0.3261 0.2671 -0.0296 0.0622  0.0454  451 HOH B O   
3894 O O   . HOH I .   ? 0.2883 0.4369 0.1776 -0.1085 0.0700  0.0165  452 HOH B O   
3895 O O   . HOH I .   ? 0.0714 0.3569 0.1814 0.0124  0.0582  -0.0321 453 HOH B O   
3896 O O   . HOH I .   ? 0.1369 0.8849 0.1495 0.1009  0.0346  -0.1324 454 HOH B O   
3897 O O   . HOH I .   ? 0.1474 0.5465 0.2140 -0.0368 0.0427  0.0480  455 HOH B O   
3898 O O   . HOH I .   ? 0.2240 0.3546 0.3327 -0.0774 0.1150  -0.0536 456 HOH B O   
3899 O O   . HOH I .   ? 0.1279 0.4032 0.1238 -0.0132 0.0724  -0.0460 457 HOH B O   
3900 O O   . HOH I .   ? 0.5070 0.5749 0.3589 -0.1524 -0.0610 0.0104  458 HOH B O   
3901 O O   . HOH I .   ? 0.2966 0.3312 0.4418 -0.0799 0.1423  -0.0355 459 HOH B O   
3902 O O   . HOH I .   ? 0.1233 0.3814 0.2692 0.0142  0.0486  -0.0140 460 HOH B O   
3903 O O   . HOH I .   ? 0.2966 0.5546 0.1913 -0.0444 0.0315  -0.0426 461 HOH B O   
3904 O O   . HOH I .   ? 0.4278 0.4623 0.2949 0.0538  0.0470  -0.1324 462 HOH B O   
3905 O O   . HOH I .   ? 0.1285 0.5006 0.4675 -0.0286 0.0997  0.1523  463 HOH B O   
3906 O O   . HOH I .   ? 0.6705 0.7809 0.4122 0.0055  0.0489  -0.2809 464 HOH B O   
3907 O O   . HOH I .   ? 0.2606 0.4081 0.3480 0.0003  0.1301  -0.0270 465 HOH B O   
3908 O O   . HOH I .   ? 0.5246 0.8502 0.7941 0.0769  0.1127  -0.0372 466 HOH B O   
3909 O O   . HOH I .   ? 0.6775 0.5660 0.3295 0.0262  -0.0374 0.1063  467 HOH B O   
3910 O O   . HOH I .   ? 0.2888 0.4971 0.2603 0.0129  0.0831  -0.0265 468 HOH B O   
3911 O O   . HOH I .   ? 0.0808 0.3100 0.1161 0.0057  0.0716  -0.0190 469 HOH B O   
3912 O O   . HOH I .   ? 0.1301 0.7409 0.1736 -0.0703 0.0868  -0.0149 470 HOH B O   
3913 O O   . HOH I .   ? 0.4466 0.5069 0.4050 0.0807  -0.0792 0.0057  471 HOH B O   
3914 O O   . HOH I .   ? 0.4239 0.7252 0.5333 -0.0138 0.1292  0.1856  472 HOH B O   
3915 O O   . HOH I .   ? 0.3080 0.4912 0.7406 -0.0695 0.2437  -0.2915 473 HOH B O   
3916 O O   . HOH I .   ? 0.3419 0.5633 0.4939 0.1637  -0.1340 -0.1065 474 HOH B O   
3917 O O   . HOH I .   ? 0.1840 0.3951 0.2906 -0.0139 0.0311  0.0032  475 HOH B O   
3918 O O   . HOH I .   ? 0.3129 0.4616 0.4904 0.0362  -0.1269 -0.0323 476 HOH B O   
3919 O O   . HOH I .   ? 0.4530 0.5671 0.2507 0.0547  0.0787  0.0875  477 HOH B O   
3920 O O   . HOH I .   ? 0.4679 0.6540 0.6585 -0.0694 0.0530  0.1346  478 HOH B O   
3921 O O   . HOH I .   ? 0.3625 0.3966 0.3535 0.0706  0.0750  0.0331  479 HOH B O   
3922 O O   . HOH I .   ? 0.1986 0.6476 0.4568 -0.0999 0.0856  -0.0743 480 HOH B O   
3923 O O   . HOH I .   ? 0.2383 0.3741 0.1191 0.0448  0.0378  -0.0365 481 HOH B O   
3924 O O   . HOH I .   ? 0.2503 0.4327 0.3484 -0.0066 0.0335  0.0199  482 HOH B O   
3925 O O   . HOH I .   ? 0.2385 0.7284 0.5354 0.0403  -0.0267 0.0344  483 HOH B O   
3926 O O   . HOH I .   ? 0.1373 0.3802 0.1403 -0.0066 0.0652  -0.0140 484 HOH B O   
3927 O O   . HOH I .   ? 0.3762 0.4864 0.6947 -0.0585 -0.0346 0.1019  485 HOH B O   
3928 O O   . HOH I .   ? 0.2414 0.5332 0.6407 -0.0109 0.0371  -0.3021 486 HOH B O   
3929 O O   . HOH I .   ? 0.3731 0.8948 0.5839 0.1087  0.2768  0.0317  487 HOH B O   
3930 O O   . HOH I .   ? 0.4433 0.5377 0.4391 0.1965  0.1759  0.2054  488 HOH B O   
3931 O O   . HOH I .   ? 0.2521 0.6559 0.5273 -0.0957 0.0257  -0.0071 489 HOH B O   
3932 O O   . HOH I .   ? 0.3493 0.4248 1.0726 -0.0406 -0.0492 -0.0208 490 HOH B O   
3933 O O   . HOH I .   ? 0.2894 1.2083 0.3592 -0.0868 -0.0165 -0.0748 491 HOH B O   
3934 O O   . HOH I .   ? 0.2801 0.6545 0.5383 -0.0167 0.0859  -0.0709 492 HOH B O   
3935 O O   . HOH I .   ? 0.2517 0.5208 0.4349 -0.0210 0.0923  -0.0032 493 HOH B O   
3936 O O   . HOH I .   ? 0.5567 0.4837 0.5120 -0.1333 -0.1027 0.0173  494 HOH B O   
3937 O O   . HOH I .   ? 0.8169 0.6548 0.2510 -0.1557 0.0935  -0.0216 495 HOH B O   
# 
