data_9KLC
# 
_entry.id   9KLC 
# 
_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   9KLC         pdb_00009klc 10.2210/pdb9klc/pdb 
WWPDB D_1300052656 ?            ?                   
# 
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 2025-05-21 ? 
2 'Structure model' 1 1 2025-06-04 ? 
# 
_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.country'                 
2  2 'Structure model' '_citation.journal_abbrev'          
3  2 'Structure model' '_citation.journal_id_ASTM'         
4  2 'Structure model' '_citation.journal_id_CSD'          
5  2 'Structure model' '_citation.journal_id_ISSN'         
6  2 'Structure model' '_citation.journal_volume'          
7  2 'Structure model' '_citation.page_first'              
8  2 'Structure model' '_citation.page_last'               
9  2 'Structure model' '_citation.pdbx_database_id_DOI'    
10 2 'Structure model' '_citation.pdbx_database_id_PubMed' 
11 2 'Structure model' '_citation.year'                    
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        9KLC 
_pdbx_database_status.recvd_initial_deposition_date   2024-11-14 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBJ 
_pdbx_database_status.process_site                    PDBJ 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              takashi.umehara@riken.jp 
_pdbx_contact_author.name_first         Takashi 
_pdbx_contact_author.name_last          Umehara 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-3464-2960 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Niwa, H.'      1 0000-0001-9544-9350 
'Shirai, F.'    2 0000-0003-0593-2467 
'Sato, S.'      3 ?                   
'Nishigaya, Y.' 4 0000-0001-5059-3244 
'Ihara, K.'     5 0000-0002-7637-2236 
'Shirouzu, M.'  6 0000-0002-7997-2149 
'Umehara, T.'   7 0000-0003-3464-2960 
# 
_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                   FR 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Eur.J.Med.Chem. 
_citation.journal_id_ASTM           EJMCA5 
_citation.journal_id_CSD            0493 
_citation.journal_id_ISSN           0223-5234 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            293 
_citation.language                  ? 
_citation.page_first                117721 
_citation.page_last                 117721 
_citation.title                     
'Discovery of potent substrate-type lysine methyltransferase G9a inhibitors for the treatment of sickle cell disease.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1016/j.ejmech.2025.117721 
_citation.pdbx_database_id_PubMed   40367677 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Nishigaya, Y.' 1  ? 
primary 'Takase, S.'    2  ? 
primary 'Sumiya, T.'    3  ? 
primary 'Kikuzato, K.'  4  ? 
primary 'Hiroyama, T.'  5  ? 
primary 'Maemoto, Y.'   6  ? 
primary 'Aoki, K.'      7  ? 
primary 'Sato, T.'      8  ? 
primary 'Niwa, H.'      9  ? 
primary 'Sato, S.'      10 ? 
primary 'Ihara, K.'     11 ? 
primary 'Nakata, A.'    12 ? 
primary 'Matsuoka, S.'  13 ? 
primary 'Hashimoto, N.' 14 ? 
primary 'Namie, R.'     15 ? 
primary 'Honma, T.'     16 ? 
primary 'Umehara, T.'   17 ? 
primary 'Shirouzu, M.'  18 ? 
primary 'Koyama, H.'    19 ? 
primary 'Nakamura, Y.'  20 ? 
primary 'Yoshida, M.'   21 ? 
primary 'Ito, A.'       22 ? 
primary 'Shirai, F.'    23 ? 
# 
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 'Histone-lysine N-methyltransferase EHMT2' 32604.924 2   2.1.1.- ? ? ? 
2 non-polymer syn 'ZINC ION' 65.409    8   ?       ? ? ? 
3 non-polymer syn SINEFUNGIN 381.387   2   ?       ? ? ? 
4 non-polymer syn 
'~{N}-[(2~{S})-1-[[6-(1-methylpiperidin-4-yl)oxypyridin-3-yl]amino]-1-oxidanylidene-hexan-2-yl]-3-(pyridin-4-ylamino)benzamide' 
516.635   2   ?       ? ? ? 
5 water       nat water 18.015    219 ?       ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        
;Euchromatic histone-lysine N-methyltransferase 2,HLA-B-associated transcript 8,Histone H3-K9 methyltransferase 3,H3-K9-HMTase 3,Lysine N-methyltransferase 1C,Protein G9a
;
# 
_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       
;GSNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQL
SIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGE
LISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEEL
GFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLD
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSNRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQL
SIRCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGE
LISDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEEL
GFDYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLD
;
_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 'ZINC ION'                                                                                                                      
ZN    
3 SINEFUNGIN                                                                                                                      
SFG   
4 '~{N}-[(2~{S})-1-[[6-(1-methylpiperidin-4-yl)oxypyridin-3-yl]amino]-1-oxidanylidene-hexan-2-yl]-3-(pyridin-4-ylamino)benzamide' 
A1L58 
5 water                                                                                                                           
HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   ASN n 
1 4   ARG n 
1 5   ALA n 
1 6   ILE n 
1 7   ARG n 
1 8   THR n 
1 9   GLU n 
1 10  LYS n 
1 11  ILE n 
1 12  ILE n 
1 13  CYS n 
1 14  ARG n 
1 15  ASP n 
1 16  VAL n 
1 17  ALA n 
1 18  ARG n 
1 19  GLY n 
1 20  TYR n 
1 21  GLU n 
1 22  ASN n 
1 23  VAL n 
1 24  PRO n 
1 25  ILE n 
1 26  PRO n 
1 27  CYS n 
1 28  VAL n 
1 29  ASN n 
1 30  GLY n 
1 31  VAL n 
1 32  ASP n 
1 33  GLY n 
1 34  GLU n 
1 35  PRO n 
1 36  CYS n 
1 37  PRO n 
1 38  GLU n 
1 39  ASP n 
1 40  TYR n 
1 41  LYS n 
1 42  TYR n 
1 43  ILE n 
1 44  SER n 
1 45  GLU n 
1 46  ASN n 
1 47  CYS n 
1 48  GLU n 
1 49  THR n 
1 50  SER n 
1 51  THR n 
1 52  MET n 
1 53  ASN n 
1 54  ILE n 
1 55  ASP n 
1 56  ARG n 
1 57  ASN n 
1 58  ILE n 
1 59  THR n 
1 60  HIS n 
1 61  LEU n 
1 62  GLN n 
1 63  HIS n 
1 64  CYS n 
1 65  THR n 
1 66  CYS n 
1 67  VAL n 
1 68  ASP n 
1 69  ASP n 
1 70  CYS n 
1 71  SER n 
1 72  SER n 
1 73  SER n 
1 74  ASN n 
1 75  CYS n 
1 76  LEU n 
1 77  CYS n 
1 78  GLY n 
1 79  GLN n 
1 80  LEU n 
1 81  SER n 
1 82  ILE n 
1 83  ARG n 
1 84  CYS n 
1 85  TRP n 
1 86  TYR n 
1 87  ASP n 
1 88  LYS n 
1 89  ASP n 
1 90  GLY n 
1 91  ARG n 
1 92  LEU n 
1 93  LEU n 
1 94  GLN n 
1 95  GLU n 
1 96  PHE n 
1 97  ASN n 
1 98  LYS n 
1 99  ILE n 
1 100 GLU n 
1 101 PRO n 
1 102 PRO n 
1 103 LEU n 
1 104 ILE n 
1 105 PHE n 
1 106 GLU n 
1 107 CYS n 
1 108 ASN n 
1 109 GLN n 
1 110 ALA n 
1 111 CYS n 
1 112 SER n 
1 113 CYS n 
1 114 TRP n 
1 115 ARG n 
1 116 ASN n 
1 117 CYS n 
1 118 LYS n 
1 119 ASN n 
1 120 ARG n 
1 121 VAL n 
1 122 VAL n 
1 123 GLN n 
1 124 SER n 
1 125 GLY n 
1 126 ILE n 
1 127 LYS n 
1 128 VAL n 
1 129 ARG n 
1 130 LEU n 
1 131 GLN n 
1 132 LEU n 
1 133 TYR n 
1 134 ARG n 
1 135 THR n 
1 136 ALA n 
1 137 LYS n 
1 138 MET n 
1 139 GLY n 
1 140 TRP n 
1 141 GLY n 
1 142 VAL n 
1 143 ARG n 
1 144 ALA n 
1 145 LEU n 
1 146 GLN n 
1 147 THR n 
1 148 ILE n 
1 149 PRO n 
1 150 GLN n 
1 151 GLY n 
1 152 THR n 
1 153 PHE n 
1 154 ILE n 
1 155 CYS n 
1 156 GLU n 
1 157 TYR n 
1 158 VAL n 
1 159 GLY n 
1 160 GLU n 
1 161 LEU n 
1 162 ILE n 
1 163 SER n 
1 164 ASP n 
1 165 ALA n 
1 166 GLU n 
1 167 ALA n 
1 168 ASP n 
1 169 VAL n 
1 170 ARG n 
1 171 GLU n 
1 172 ASP n 
1 173 ASP n 
1 174 SER n 
1 175 TYR n 
1 176 LEU n 
1 177 PHE n 
1 178 ASP n 
1 179 LEU n 
1 180 ASP n 
1 181 ASN n 
1 182 LYS n 
1 183 ASP n 
1 184 GLY n 
1 185 GLU n 
1 186 VAL n 
1 187 TYR n 
1 188 CYS n 
1 189 ILE n 
1 190 ASP n 
1 191 ALA n 
1 192 ARG n 
1 193 TYR n 
1 194 TYR n 
1 195 GLY n 
1 196 ASN n 
1 197 ILE n 
1 198 SER n 
1 199 ARG n 
1 200 PHE n 
1 201 ILE n 
1 202 ASN n 
1 203 HIS n 
1 204 LEU n 
1 205 CYS n 
1 206 ASP n 
1 207 PRO n 
1 208 ASN n 
1 209 ILE n 
1 210 ILE n 
1 211 PRO n 
1 212 VAL n 
1 213 ARG n 
1 214 VAL n 
1 215 PHE n 
1 216 MET n 
1 217 LEU n 
1 218 HIS n 
1 219 GLN n 
1 220 ASP n 
1 221 LEU n 
1 222 ARG n 
1 223 PHE n 
1 224 PRO n 
1 225 ARG n 
1 226 ILE n 
1 227 ALA n 
1 228 PHE n 
1 229 PHE n 
1 230 SER n 
1 231 SER n 
1 232 ARG n 
1 233 ASP n 
1 234 ILE n 
1 235 ARG n 
1 236 THR n 
1 237 GLY n 
1 238 GLU n 
1 239 GLU n 
1 240 LEU n 
1 241 GLY n 
1 242 PHE n 
1 243 ASP n 
1 244 TYR n 
1 245 GLY n 
1 246 ASP n 
1 247 ARG n 
1 248 PHE n 
1 249 TRP n 
1 250 ASP n 
1 251 ILE n 
1 252 LYS n 
1 253 SER n 
1 254 LYS n 
1 255 TYR n 
1 256 PHE n 
1 257 THR n 
1 258 CYS n 
1 259 GLN n 
1 260 CYS n 
1 261 GLY n 
1 262 SER n 
1 263 GLU n 
1 264 LYS n 
1 265 CYS n 
1 266 LYS n 
1 267 HIS n 
1 268 SER n 
1 269 ALA n 
1 270 GLU n 
1 271 ALA n 
1 272 ILE n 
1 273 ALA n 
1 274 LEU n 
1 275 GLU n 
1 276 GLN n 
1 277 SER n 
1 278 ARG n 
1 279 LEU n 
1 280 ALA n 
1 281 ARG n 
1 282 LEU n 
1 283 ASP 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                      ? 
_entity_src_gen.pdbx_beg_seq_num                   ? 
_entity_src_gen.pdbx_end_seq_num                   ? 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 ? 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_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 
A1L58 non-polymer         . 
'~{N}-[(2~{S})-1-[[6-(1-methylpiperidin-4-yl)oxypyridin-3-yl]amino]-1-oxidanylidene-hexan-2-yl]-3-(pyridin-4-ylamino)benzamide' ? 
'C29 H36 N6 O3'  516.635 
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  
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 
SFG   non-polymer         . SINEFUNGIN ADENOSYL-ORNITHINE 'C15 H23 N7 O5'  381.387 
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 
ZN    non-polymer         . 'ZINC ION' ?                  'Zn 2'           65.409  
# 
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   GLY 1   911  ?    ?   ?   A . n 
A 1 2   SER 2   912  ?    ?   ?   A . n 
A 1 3   ASN 3   913  ?    ?   ?   A . n 
A 1 4   ARG 4   914  ?    ?   ?   A . n 
A 1 5   ALA 5   915  ?    ?   ?   A . n 
A 1 6   ILE 6   916  ?    ?   ?   A . n 
A 1 7   ARG 7   917  ?    ?   ?   A . n 
A 1 8   THR 8   918  918  THR THR A . n 
A 1 9   GLU 9   919  919  GLU GLU A . n 
A 1 10  LYS 10  920  920  LYS LYS A . n 
A 1 11  ILE 11  921  921  ILE ILE A . n 
A 1 12  ILE 12  922  922  ILE ILE A . n 
A 1 13  CYS 13  923  923  CYS CYS A . n 
A 1 14  ARG 14  924  924  ARG ARG A . n 
A 1 15  ASP 15  925  925  ASP ASP A . n 
A 1 16  VAL 16  926  926  VAL VAL A . n 
A 1 17  ALA 17  927  927  ALA ALA A . n 
A 1 18  ARG 18  928  928  ARG ARG A . n 
A 1 19  GLY 19  929  929  GLY GLY A . n 
A 1 20  TYR 20  930  930  TYR TYR A . n 
A 1 21  GLU 21  931  931  GLU GLU A . n 
A 1 22  ASN 22  932  932  ASN ASN A . n 
A 1 23  VAL 23  933  933  VAL VAL A . n 
A 1 24  PRO 24  934  934  PRO PRO A . n 
A 1 25  ILE 25  935  935  ILE ILE A . n 
A 1 26  PRO 26  936  936  PRO PRO A . n 
A 1 27  CYS 27  937  937  CYS CYS A . n 
A 1 28  VAL 28  938  938  VAL VAL A . n 
A 1 29  ASN 29  939  939  ASN ASN A . n 
A 1 30  GLY 30  940  940  GLY GLY A . n 
A 1 31  VAL 31  941  941  VAL VAL A . n 
A 1 32  ASP 32  942  942  ASP ASP A . n 
A 1 33  GLY 33  943  943  GLY GLY A . n 
A 1 34  GLU 34  944  944  GLU GLU A . n 
A 1 35  PRO 35  945  945  PRO PRO A . n 
A 1 36  CYS 36  946  946  CYS CYS A . n 
A 1 37  PRO 37  947  947  PRO PRO A . n 
A 1 38  GLU 38  948  948  GLU GLU A . n 
A 1 39  ASP 39  949  949  ASP ASP A . n 
A 1 40  TYR 40  950  950  TYR TYR A . n 
A 1 41  LYS 41  951  951  LYS LYS A . n 
A 1 42  TYR 42  952  952  TYR TYR A . n 
A 1 43  ILE 43  953  953  ILE ILE A . n 
A 1 44  SER 44  954  954  SER SER A . n 
A 1 45  GLU 45  955  955  GLU GLU A . n 
A 1 46  ASN 46  956  956  ASN ASN A . n 
A 1 47  CYS 47  957  957  CYS CYS A . n 
A 1 48  GLU 48  958  958  GLU GLU A . n 
A 1 49  THR 49  959  959  THR THR A . n 
A 1 50  SER 50  960  960  SER SER A . n 
A 1 51  THR 51  961  961  THR THR A . n 
A 1 52  MET 52  962  962  MET MET A . n 
A 1 53  ASN 53  963  963  ASN ASN A . n 
A 1 54  ILE 54  964  964  ILE ILE A . n 
A 1 55  ASP 55  965  965  ASP ASP A . n 
A 1 56  ARG 56  966  966  ARG ARG A . n 
A 1 57  ASN 57  967  967  ASN ASN A . n 
A 1 58  ILE 58  968  968  ILE ILE A . n 
A 1 59  THR 59  969  969  THR THR A . n 
A 1 60  HIS 60  970  970  HIS HIS A . n 
A 1 61  LEU 61  971  971  LEU LEU A . n 
A 1 62  GLN 62  972  972  GLN GLN A . n 
A 1 63  HIS 63  973  973  HIS HIS A . n 
A 1 64  CYS 64  974  974  CYS CYS A . n 
A 1 65  THR 65  975  975  THR THR A . n 
A 1 66  CYS 66  976  976  CYS CYS A . n 
A 1 67  VAL 67  977  977  VAL VAL A . n 
A 1 68  ASP 68  978  978  ASP ASP A . n 
A 1 69  ASP 69  979  979  ASP ASP A . n 
A 1 70  CYS 70  980  980  CYS CYS A . n 
A 1 71  SER 71  981  981  SER SER A . n 
A 1 72  SER 72  982  982  SER SER A . n 
A 1 73  SER 73  983  983  SER SER A . n 
A 1 74  ASN 74  984  984  ASN ASN A . n 
A 1 75  CYS 75  985  985  CYS CYS A . n 
A 1 76  LEU 76  986  986  LEU LEU A . n 
A 1 77  CYS 77  987  987  CYS CYS A . n 
A 1 78  GLY 78  988  988  GLY GLY A . n 
A 1 79  GLN 79  989  989  GLN GLN A . n 
A 1 80  LEU 80  990  990  LEU LEU A . n 
A 1 81  SER 81  991  991  SER SER A . n 
A 1 82  ILE 82  992  992  ILE ILE A . n 
A 1 83  ARG 83  993  993  ARG ARG A . n 
A 1 84  CYS 84  994  994  CYS CYS A . n 
A 1 85  TRP 85  995  995  TRP TRP A . n 
A 1 86  TYR 86  996  996  TYR TYR A . n 
A 1 87  ASP 87  997  997  ASP ASP A . n 
A 1 88  LYS 88  998  998  LYS LYS A . n 
A 1 89  ASP 89  999  999  ASP ASP A . n 
A 1 90  GLY 90  1000 1000 GLY GLY A . n 
A 1 91  ARG 91  1001 1001 ARG ARG A . n 
A 1 92  LEU 92  1002 1002 LEU LEU A . n 
A 1 93  LEU 93  1003 1003 LEU LEU A . n 
A 1 94  GLN 94  1004 1004 GLN GLN A . n 
A 1 95  GLU 95  1005 1005 GLU GLU A . n 
A 1 96  PHE 96  1006 1006 PHE PHE A . n 
A 1 97  ASN 97  1007 1007 ASN ASN A . n 
A 1 98  LYS 98  1008 1008 LYS LYS A . n 
A 1 99  ILE 99  1009 1009 ILE ILE A . n 
A 1 100 GLU 100 1010 1010 GLU GLU A . n 
A 1 101 PRO 101 1011 1011 PRO PRO A . n 
A 1 102 PRO 102 1012 1012 PRO PRO A . n 
A 1 103 LEU 103 1013 1013 LEU LEU A . n 
A 1 104 ILE 104 1014 1014 ILE ILE A . n 
A 1 105 PHE 105 1015 1015 PHE PHE A . n 
A 1 106 GLU 106 1016 1016 GLU GLU A . n 
A 1 107 CYS 107 1017 1017 CYS CYS A . n 
A 1 108 ASN 108 1018 1018 ASN ASN A . n 
A 1 109 GLN 109 1019 1019 GLN GLN A . n 
A 1 110 ALA 110 1020 1020 ALA ALA A . n 
A 1 111 CYS 111 1021 1021 CYS CYS A . n 
A 1 112 SER 112 1022 1022 SER SER A . n 
A 1 113 CYS 113 1023 1023 CYS CYS A . n 
A 1 114 TRP 114 1024 1024 TRP TRP A . n 
A 1 115 ARG 115 1025 1025 ARG ARG A . n 
A 1 116 ASN 116 1026 1026 ASN ASN A . n 
A 1 117 CYS 117 1027 1027 CYS CYS A . n 
A 1 118 LYS 118 1028 1028 LYS LYS A . n 
A 1 119 ASN 119 1029 1029 ASN ASN A . n 
A 1 120 ARG 120 1030 1030 ARG ARG A . n 
A 1 121 VAL 121 1031 1031 VAL VAL A . n 
A 1 122 VAL 122 1032 1032 VAL VAL A . n 
A 1 123 GLN 123 1033 1033 GLN GLN A . n 
A 1 124 SER 124 1034 1034 SER SER A . n 
A 1 125 GLY 125 1035 1035 GLY GLY A . n 
A 1 126 ILE 126 1036 1036 ILE ILE A . n 
A 1 127 LYS 127 1037 1037 LYS LYS A . n 
A 1 128 VAL 128 1038 1038 VAL VAL A . n 
A 1 129 ARG 129 1039 1039 ARG ARG A . n 
A 1 130 LEU 130 1040 1040 LEU LEU A . n 
A 1 131 GLN 131 1041 1041 GLN GLN A . n 
A 1 132 LEU 132 1042 1042 LEU LEU A . n 
A 1 133 TYR 133 1043 1043 TYR TYR A . n 
A 1 134 ARG 134 1044 1044 ARG ARG A . n 
A 1 135 THR 135 1045 1045 THR THR A . n 
A 1 136 ALA 136 1046 1046 ALA ALA A . n 
A 1 137 LYS 137 1047 1047 LYS LYS A . n 
A 1 138 MET 138 1048 1048 MET MET A . n 
A 1 139 GLY 139 1049 1049 GLY GLY A . n 
A 1 140 TRP 140 1050 1050 TRP TRP A . n 
A 1 141 GLY 141 1051 1051 GLY GLY A . n 
A 1 142 VAL 142 1052 1052 VAL VAL A . n 
A 1 143 ARG 143 1053 1053 ARG ARG A . n 
A 1 144 ALA 144 1054 1054 ALA ALA A . n 
A 1 145 LEU 145 1055 1055 LEU LEU A . n 
A 1 146 GLN 146 1056 1056 GLN GLN A . n 
A 1 147 THR 147 1057 1057 THR THR A . n 
A 1 148 ILE 148 1058 1058 ILE ILE A . n 
A 1 149 PRO 149 1059 1059 PRO PRO A . n 
A 1 150 GLN 150 1060 1060 GLN GLN A . n 
A 1 151 GLY 151 1061 1061 GLY GLY A . n 
A 1 152 THR 152 1062 1062 THR THR A . n 
A 1 153 PHE 153 1063 1063 PHE PHE A . n 
A 1 154 ILE 154 1064 1064 ILE ILE A . n 
A 1 155 CYS 155 1065 1065 CYS CYS A . n 
A 1 156 GLU 156 1066 1066 GLU GLU A . n 
A 1 157 TYR 157 1067 1067 TYR TYR A . n 
A 1 158 VAL 158 1068 1068 VAL VAL A . n 
A 1 159 GLY 159 1069 1069 GLY GLY A . n 
A 1 160 GLU 160 1070 1070 GLU GLU A . n 
A 1 161 LEU 161 1071 1071 LEU LEU A . n 
A 1 162 ILE 162 1072 1072 ILE ILE A . n 
A 1 163 SER 163 1073 1073 SER SER A . n 
A 1 164 ASP 164 1074 1074 ASP ASP A . n 
A 1 165 ALA 165 1075 1075 ALA ALA A . n 
A 1 166 GLU 166 1076 1076 GLU GLU A . n 
A 1 167 ALA 167 1077 1077 ALA ALA A . n 
A 1 168 ASP 168 1078 1078 ASP ASP A . n 
A 1 169 VAL 169 1079 1079 VAL VAL A . n 
A 1 170 ARG 170 1080 1080 ARG ARG A . n 
A 1 171 GLU 171 1081 1081 GLU GLU A . n 
A 1 172 ASP 172 1082 1082 ASP ASP A . n 
A 1 173 ASP 173 1083 1083 ASP ASP A . n 
A 1 174 SER 174 1084 1084 SER SER A . n 
A 1 175 TYR 175 1085 1085 TYR TYR A . n 
A 1 176 LEU 176 1086 1086 LEU LEU A . n 
A 1 177 PHE 177 1087 1087 PHE PHE A . n 
A 1 178 ASP 178 1088 1088 ASP ASP A . n 
A 1 179 LEU 179 1089 1089 LEU LEU A . n 
A 1 180 ASP 180 1090 1090 ASP ASP A . n 
A 1 181 ASN 181 1091 1091 ASN ASN A . n 
A 1 182 LYS 182 1092 ?    ?   ?   A . n 
A 1 183 ASP 183 1093 ?    ?   ?   A . n 
A 1 184 GLY 184 1094 1094 GLY GLY A . n 
A 1 185 GLU 185 1095 1095 GLU GLU A . n 
A 1 186 VAL 186 1096 1096 VAL VAL A . n 
A 1 187 TYR 187 1097 1097 TYR TYR A . n 
A 1 188 CYS 188 1098 1098 CYS CYS A . n 
A 1 189 ILE 189 1099 1099 ILE ILE A . n 
A 1 190 ASP 190 1100 1100 ASP ASP A . n 
A 1 191 ALA 191 1101 1101 ALA ALA A . n 
A 1 192 ARG 192 1102 1102 ARG ARG A . n 
A 1 193 TYR 193 1103 1103 TYR TYR A . n 
A 1 194 TYR 194 1104 1104 TYR TYR A . n 
A 1 195 GLY 195 1105 1105 GLY GLY A . n 
A 1 196 ASN 196 1106 1106 ASN ASN A . n 
A 1 197 ILE 197 1107 1107 ILE ILE A . n 
A 1 198 SER 198 1108 1108 SER SER A . n 
A 1 199 ARG 199 1109 1109 ARG ARG A . n 
A 1 200 PHE 200 1110 1110 PHE PHE A . n 
A 1 201 ILE 201 1111 1111 ILE ILE A . n 
A 1 202 ASN 202 1112 1112 ASN ASN A . n 
A 1 203 HIS 203 1113 1113 HIS HIS A . n 
A 1 204 LEU 204 1114 1114 LEU LEU A . n 
A 1 205 CYS 205 1115 1115 CYS CYS A . n 
A 1 206 ASP 206 1116 1116 ASP ASP A . n 
A 1 207 PRO 207 1117 1117 PRO PRO A . n 
A 1 208 ASN 208 1118 1118 ASN ASN A . n 
A 1 209 ILE 209 1119 1119 ILE ILE A . n 
A 1 210 ILE 210 1120 1120 ILE ILE A . n 
A 1 211 PRO 211 1121 1121 PRO PRO A . n 
A 1 212 VAL 212 1122 1122 VAL VAL A . n 
A 1 213 ARG 213 1123 1123 ARG ARG A . n 
A 1 214 VAL 214 1124 1124 VAL VAL A . n 
A 1 215 PHE 215 1125 1125 PHE PHE A . n 
A 1 216 MET 216 1126 1126 MET MET A . n 
A 1 217 LEU 217 1127 1127 LEU LEU A . n 
A 1 218 HIS 218 1128 1128 HIS HIS A . n 
A 1 219 GLN 219 1129 1129 GLN GLN A . n 
A 1 220 ASP 220 1130 1130 ASP ASP A . n 
A 1 221 LEU 221 1131 1131 LEU LEU A . n 
A 1 222 ARG 222 1132 1132 ARG ARG A . n 
A 1 223 PHE 223 1133 1133 PHE PHE A . n 
A 1 224 PRO 224 1134 1134 PRO PRO A . n 
A 1 225 ARG 225 1135 1135 ARG ARG A . n 
A 1 226 ILE 226 1136 1136 ILE ILE A . n 
A 1 227 ALA 227 1137 1137 ALA ALA A . n 
A 1 228 PHE 228 1138 1138 PHE PHE A . n 
A 1 229 PHE 229 1139 1139 PHE PHE A . n 
A 1 230 SER 230 1140 1140 SER SER A . n 
A 1 231 SER 231 1141 1141 SER SER A . n 
A 1 232 ARG 232 1142 1142 ARG ARG A . n 
A 1 233 ASP 233 1143 1143 ASP ASP A . n 
A 1 234 ILE 234 1144 1144 ILE ILE A . n 
A 1 235 ARG 235 1145 1145 ARG ARG A . n 
A 1 236 THR 236 1146 1146 THR THR A . n 
A 1 237 GLY 237 1147 1147 GLY GLY A . n 
A 1 238 GLU 238 1148 1148 GLU GLU A . n 
A 1 239 GLU 239 1149 1149 GLU GLU A . n 
A 1 240 LEU 240 1150 1150 LEU LEU A . n 
A 1 241 GLY 241 1151 1151 GLY GLY A . n 
A 1 242 PHE 242 1152 1152 PHE PHE A . n 
A 1 243 ASP 243 1153 1153 ASP ASP A . n 
A 1 244 TYR 244 1154 1154 TYR TYR A . n 
A 1 245 GLY 245 1155 1155 GLY GLY A . n 
A 1 246 ASP 246 1156 1156 ASP ASP A . n 
A 1 247 ARG 247 1157 1157 ARG ARG A . n 
A 1 248 PHE 248 1158 1158 PHE PHE A . n 
A 1 249 TRP 249 1159 1159 TRP TRP A . n 
A 1 250 ASP 250 1160 1160 ASP ASP A . n 
A 1 251 ILE 251 1161 1161 ILE ILE A . n 
A 1 252 LYS 252 1162 1162 LYS LYS A . n 
A 1 253 SER 253 1163 1163 SER SER A . n 
A 1 254 LYS 254 1164 1164 LYS LYS A . n 
A 1 255 TYR 255 1165 1165 TYR TYR A . n 
A 1 256 PHE 256 1166 1166 PHE PHE A . n 
A 1 257 THR 257 1167 1167 THR THR A . n 
A 1 258 CYS 258 1168 1168 CYS CYS A . n 
A 1 259 GLN 259 1169 1169 GLN GLN A . n 
A 1 260 CYS 260 1170 1170 CYS CYS A . n 
A 1 261 GLY 261 1171 1171 GLY GLY A . n 
A 1 262 SER 262 1172 1172 SER SER A . n 
A 1 263 GLU 263 1173 1173 GLU GLU A . n 
A 1 264 LYS 264 1174 1174 LYS LYS A . n 
A 1 265 CYS 265 1175 1175 CYS CYS A . n 
A 1 266 LYS 266 1176 1176 LYS LYS A . n 
A 1 267 HIS 267 1177 1177 HIS HIS A . n 
A 1 268 SER 268 1178 1178 SER SER A . n 
A 1 269 ALA 269 1179 1179 ALA ALA A . n 
A 1 270 GLU 270 1180 1180 GLU GLU A . n 
A 1 271 ALA 271 1181 1181 ALA ALA A . n 
A 1 272 ILE 272 1182 1182 ILE ILE A . n 
A 1 273 ALA 273 1183 1183 ALA ALA A . n 
A 1 274 LEU 274 1184 1184 LEU LEU A . n 
A 1 275 GLU 275 1185 1185 GLU GLU A . n 
A 1 276 GLN 276 1186 1186 GLN GLN A . n 
A 1 277 SER 277 1187 1187 SER SER A . n 
A 1 278 ARG 278 1188 1188 ARG ARG A . n 
A 1 279 LEU 279 1189 1189 LEU LEU A . n 
A 1 280 ALA 280 1190 ?    ?   ?   A . n 
A 1 281 ARG 281 1191 ?    ?   ?   A . n 
A 1 282 LEU 282 1192 ?    ?   ?   A . n 
A 1 283 ASP 283 1193 ?    ?   ?   A . n 
B 1 1   GLY 1   911  ?    ?   ?   B . n 
B 1 2   SER 2   912  ?    ?   ?   B . n 
B 1 3   ASN 3   913  ?    ?   ?   B . n 
B 1 4   ARG 4   914  ?    ?   ?   B . n 
B 1 5   ALA 5   915  ?    ?   ?   B . n 
B 1 6   ILE 6   916  ?    ?   ?   B . n 
B 1 7   ARG 7   917  917  ARG ARG B . n 
B 1 8   THR 8   918  918  THR THR B . n 
B 1 9   GLU 9   919  919  GLU GLU B . n 
B 1 10  LYS 10  920  920  LYS LYS B . n 
B 1 11  ILE 11  921  921  ILE ILE B . n 
B 1 12  ILE 12  922  922  ILE ILE B . n 
B 1 13  CYS 13  923  923  CYS CYS B . n 
B 1 14  ARG 14  924  924  ARG ARG B . n 
B 1 15  ASP 15  925  925  ASP ASP B . n 
B 1 16  VAL 16  926  926  VAL VAL B . n 
B 1 17  ALA 17  927  927  ALA ALA B . n 
B 1 18  ARG 18  928  928  ARG ARG B . n 
B 1 19  GLY 19  929  929  GLY GLY B . n 
B 1 20  TYR 20  930  930  TYR TYR B . n 
B 1 21  GLU 21  931  931  GLU GLU B . n 
B 1 22  ASN 22  932  932  ASN ASN B . n 
B 1 23  VAL 23  933  933  VAL VAL B . n 
B 1 24  PRO 24  934  934  PRO PRO B . n 
B 1 25  ILE 25  935  935  ILE ILE B . n 
B 1 26  PRO 26  936  936  PRO PRO B . n 
B 1 27  CYS 27  937  937  CYS CYS B . n 
B 1 28  VAL 28  938  938  VAL VAL B . n 
B 1 29  ASN 29  939  939  ASN ASN B . n 
B 1 30  GLY 30  940  940  GLY GLY B . n 
B 1 31  VAL 31  941  941  VAL VAL B . n 
B 1 32  ASP 32  942  942  ASP ASP B . n 
B 1 33  GLY 33  943  943  GLY GLY B . n 
B 1 34  GLU 34  944  944  GLU GLU B . n 
B 1 35  PRO 35  945  945  PRO PRO B . n 
B 1 36  CYS 36  946  946  CYS CYS B . n 
B 1 37  PRO 37  947  947  PRO PRO B . n 
B 1 38  GLU 38  948  948  GLU GLU B . n 
B 1 39  ASP 39  949  949  ASP ASP B . n 
B 1 40  TYR 40  950  950  TYR TYR B . n 
B 1 41  LYS 41  951  951  LYS LYS B . n 
B 1 42  TYR 42  952  952  TYR TYR B . n 
B 1 43  ILE 43  953  953  ILE ILE B . n 
B 1 44  SER 44  954  954  SER SER B . n 
B 1 45  GLU 45  955  955  GLU GLU B . n 
B 1 46  ASN 46  956  956  ASN ASN B . n 
B 1 47  CYS 47  957  957  CYS CYS B . n 
B 1 48  GLU 48  958  958  GLU GLU B . n 
B 1 49  THR 49  959  959  THR THR B . n 
B 1 50  SER 50  960  960  SER SER B . n 
B 1 51  THR 51  961  961  THR THR B . n 
B 1 52  MET 52  962  962  MET MET B . n 
B 1 53  ASN 53  963  963  ASN ASN B . n 
B 1 54  ILE 54  964  964  ILE ILE B . n 
B 1 55  ASP 55  965  965  ASP ASP B . n 
B 1 56  ARG 56  966  966  ARG ARG B . n 
B 1 57  ASN 57  967  967  ASN ASN B . n 
B 1 58  ILE 58  968  968  ILE ILE B . n 
B 1 59  THR 59  969  969  THR THR B . n 
B 1 60  HIS 60  970  970  HIS HIS B . n 
B 1 61  LEU 61  971  971  LEU LEU B . n 
B 1 62  GLN 62  972  972  GLN GLN B . n 
B 1 63  HIS 63  973  973  HIS HIS B . n 
B 1 64  CYS 64  974  974  CYS CYS B . n 
B 1 65  THR 65  975  975  THR THR B . n 
B 1 66  CYS 66  976  976  CYS CYS B . n 
B 1 67  VAL 67  977  977  VAL VAL B . n 
B 1 68  ASP 68  978  978  ASP ASP B . n 
B 1 69  ASP 69  979  979  ASP ASP B . n 
B 1 70  CYS 70  980  980  CYS CYS B . n 
B 1 71  SER 71  981  981  SER SER B . n 
B 1 72  SER 72  982  982  SER SER B . n 
B 1 73  SER 73  983  983  SER SER B . n 
B 1 74  ASN 74  984  984  ASN ASN B . n 
B 1 75  CYS 75  985  985  CYS CYS B . n 
B 1 76  LEU 76  986  986  LEU LEU B . n 
B 1 77  CYS 77  987  987  CYS CYS B . n 
B 1 78  GLY 78  988  988  GLY GLY B . n 
B 1 79  GLN 79  989  989  GLN GLN B . n 
B 1 80  LEU 80  990  990  LEU LEU B . n 
B 1 81  SER 81  991  991  SER SER B . n 
B 1 82  ILE 82  992  992  ILE ILE B . n 
B 1 83  ARG 83  993  993  ARG ARG B . n 
B 1 84  CYS 84  994  994  CYS CYS B . n 
B 1 85  TRP 85  995  995  TRP TRP B . n 
B 1 86  TYR 86  996  996  TYR TYR B . n 
B 1 87  ASP 87  997  997  ASP ASP B . n 
B 1 88  LYS 88  998  998  LYS LYS B . n 
B 1 89  ASP 89  999  999  ASP ASP B . n 
B 1 90  GLY 90  1000 1000 GLY GLY B . n 
B 1 91  ARG 91  1001 1001 ARG ARG B . n 
B 1 92  LEU 92  1002 1002 LEU LEU B . n 
B 1 93  LEU 93  1003 1003 LEU LEU B . n 
B 1 94  GLN 94  1004 1004 GLN GLN B . n 
B 1 95  GLU 95  1005 1005 GLU GLU B . n 
B 1 96  PHE 96  1006 1006 PHE PHE B . n 
B 1 97  ASN 97  1007 1007 ASN ASN B . n 
B 1 98  LYS 98  1008 1008 LYS LYS B . n 
B 1 99  ILE 99  1009 1009 ILE ILE B . n 
B 1 100 GLU 100 1010 1010 GLU GLU B . n 
B 1 101 PRO 101 1011 1011 PRO PRO B . n 
B 1 102 PRO 102 1012 1012 PRO PRO B . n 
B 1 103 LEU 103 1013 1013 LEU LEU B . n 
B 1 104 ILE 104 1014 1014 ILE ILE B . n 
B 1 105 PHE 105 1015 1015 PHE PHE B . n 
B 1 106 GLU 106 1016 1016 GLU GLU B . n 
B 1 107 CYS 107 1017 1017 CYS CYS B . n 
B 1 108 ASN 108 1018 1018 ASN ASN B . n 
B 1 109 GLN 109 1019 1019 GLN GLN B . n 
B 1 110 ALA 110 1020 1020 ALA ALA B . n 
B 1 111 CYS 111 1021 1021 CYS CYS B . n 
B 1 112 SER 112 1022 1022 SER SER B . n 
B 1 113 CYS 113 1023 1023 CYS CYS B . n 
B 1 114 TRP 114 1024 1024 TRP TRP B . n 
B 1 115 ARG 115 1025 1025 ARG ARG B . n 
B 1 116 ASN 116 1026 1026 ASN ASN B . n 
B 1 117 CYS 117 1027 1027 CYS CYS B . n 
B 1 118 LYS 118 1028 1028 LYS LYS B . n 
B 1 119 ASN 119 1029 1029 ASN ASN B . n 
B 1 120 ARG 120 1030 1030 ARG ARG B . n 
B 1 121 VAL 121 1031 1031 VAL VAL B . n 
B 1 122 VAL 122 1032 1032 VAL VAL B . n 
B 1 123 GLN 123 1033 1033 GLN GLN B . n 
B 1 124 SER 124 1034 1034 SER SER B . n 
B 1 125 GLY 125 1035 1035 GLY GLY B . n 
B 1 126 ILE 126 1036 1036 ILE ILE B . n 
B 1 127 LYS 127 1037 1037 LYS LYS B . n 
B 1 128 VAL 128 1038 1038 VAL VAL B . n 
B 1 129 ARG 129 1039 1039 ARG ARG B . n 
B 1 130 LEU 130 1040 1040 LEU LEU B . n 
B 1 131 GLN 131 1041 1041 GLN GLN B . n 
B 1 132 LEU 132 1042 1042 LEU LEU B . n 
B 1 133 TYR 133 1043 1043 TYR TYR B . n 
B 1 134 ARG 134 1044 1044 ARG ARG B . n 
B 1 135 THR 135 1045 1045 THR THR B . n 
B 1 136 ALA 136 1046 1046 ALA ALA B . n 
B 1 137 LYS 137 1047 1047 LYS LYS B . n 
B 1 138 MET 138 1048 1048 MET MET B . n 
B 1 139 GLY 139 1049 1049 GLY GLY B . n 
B 1 140 TRP 140 1050 1050 TRP TRP B . n 
B 1 141 GLY 141 1051 1051 GLY GLY B . n 
B 1 142 VAL 142 1052 1052 VAL VAL B . n 
B 1 143 ARG 143 1053 1053 ARG ARG B . n 
B 1 144 ALA 144 1054 1054 ALA ALA B . n 
B 1 145 LEU 145 1055 1055 LEU LEU B . n 
B 1 146 GLN 146 1056 1056 GLN GLN B . n 
B 1 147 THR 147 1057 1057 THR THR B . n 
B 1 148 ILE 148 1058 1058 ILE ILE B . n 
B 1 149 PRO 149 1059 1059 PRO PRO B . n 
B 1 150 GLN 150 1060 1060 GLN GLN B . n 
B 1 151 GLY 151 1061 1061 GLY GLY B . n 
B 1 152 THR 152 1062 1062 THR THR B . n 
B 1 153 PHE 153 1063 1063 PHE PHE B . n 
B 1 154 ILE 154 1064 1064 ILE ILE B . n 
B 1 155 CYS 155 1065 1065 CYS CYS B . n 
B 1 156 GLU 156 1066 1066 GLU GLU B . n 
B 1 157 TYR 157 1067 1067 TYR TYR B . n 
B 1 158 VAL 158 1068 1068 VAL VAL B . n 
B 1 159 GLY 159 1069 1069 GLY GLY B . n 
B 1 160 GLU 160 1070 1070 GLU GLU B . n 
B 1 161 LEU 161 1071 1071 LEU LEU B . n 
B 1 162 ILE 162 1072 1072 ILE ILE B . n 
B 1 163 SER 163 1073 1073 SER SER B . n 
B 1 164 ASP 164 1074 1074 ASP ASP B . n 
B 1 165 ALA 165 1075 1075 ALA ALA B . n 
B 1 166 GLU 166 1076 1076 GLU GLU B . n 
B 1 167 ALA 167 1077 1077 ALA ALA B . n 
B 1 168 ASP 168 1078 1078 ASP ASP B . n 
B 1 169 VAL 169 1079 1079 VAL VAL B . n 
B 1 170 ARG 170 1080 1080 ARG ARG B . n 
B 1 171 GLU 171 1081 1081 GLU GLU B . n 
B 1 172 ASP 172 1082 1082 ASP ASP B . n 
B 1 173 ASP 173 1083 1083 ASP ASP B . n 
B 1 174 SER 174 1084 1084 SER SER B . n 
B 1 175 TYR 175 1085 1085 TYR TYR B . n 
B 1 176 LEU 176 1086 1086 LEU LEU B . n 
B 1 177 PHE 177 1087 1087 PHE PHE B . n 
B 1 178 ASP 178 1088 1088 ASP ASP B . n 
B 1 179 LEU 179 1089 1089 LEU LEU B . n 
B 1 180 ASP 180 1090 1090 ASP ASP B . n 
B 1 181 ASN 181 1091 1091 ASN ASN B . n 
B 1 182 LYS 182 1092 1092 LYS LYS B . n 
B 1 183 ASP 183 1093 1093 ASP ASP B . n 
B 1 184 GLY 184 1094 1094 GLY GLY B . n 
B 1 185 GLU 185 1095 1095 GLU GLU B . n 
B 1 186 VAL 186 1096 1096 VAL VAL B . n 
B 1 187 TYR 187 1097 1097 TYR TYR B . n 
B 1 188 CYS 188 1098 1098 CYS CYS B . n 
B 1 189 ILE 189 1099 1099 ILE ILE B . n 
B 1 190 ASP 190 1100 1100 ASP ASP B . n 
B 1 191 ALA 191 1101 1101 ALA ALA B . n 
B 1 192 ARG 192 1102 1102 ARG ARG B . n 
B 1 193 TYR 193 1103 1103 TYR TYR B . n 
B 1 194 TYR 194 1104 1104 TYR TYR B . n 
B 1 195 GLY 195 1105 1105 GLY GLY B . n 
B 1 196 ASN 196 1106 1106 ASN ASN B . n 
B 1 197 ILE 197 1107 1107 ILE ILE B . n 
B 1 198 SER 198 1108 1108 SER SER B . n 
B 1 199 ARG 199 1109 1109 ARG ARG B . n 
B 1 200 PHE 200 1110 1110 PHE PHE B . n 
B 1 201 ILE 201 1111 1111 ILE ILE B . n 
B 1 202 ASN 202 1112 1112 ASN ASN B . n 
B 1 203 HIS 203 1113 1113 HIS HIS B . n 
B 1 204 LEU 204 1114 1114 LEU LEU B . n 
B 1 205 CYS 205 1115 1115 CYS CYS B . n 
B 1 206 ASP 206 1116 1116 ASP ASP B . n 
B 1 207 PRO 207 1117 1117 PRO PRO B . n 
B 1 208 ASN 208 1118 1118 ASN ASN B . n 
B 1 209 ILE 209 1119 1119 ILE ILE B . n 
B 1 210 ILE 210 1120 1120 ILE ILE B . n 
B 1 211 PRO 211 1121 1121 PRO PRO B . n 
B 1 212 VAL 212 1122 1122 VAL VAL B . n 
B 1 213 ARG 213 1123 1123 ARG ARG B . n 
B 1 214 VAL 214 1124 1124 VAL VAL B . n 
B 1 215 PHE 215 1125 1125 PHE PHE B . n 
B 1 216 MET 216 1126 1126 MET MET B . n 
B 1 217 LEU 217 1127 1127 LEU LEU B . n 
B 1 218 HIS 218 1128 1128 HIS HIS B . n 
B 1 219 GLN 219 1129 1129 GLN GLN B . n 
B 1 220 ASP 220 1130 1130 ASP ASP B . n 
B 1 221 LEU 221 1131 1131 LEU LEU B . n 
B 1 222 ARG 222 1132 1132 ARG ARG B . n 
B 1 223 PHE 223 1133 1133 PHE PHE B . n 
B 1 224 PRO 224 1134 1134 PRO PRO B . n 
B 1 225 ARG 225 1135 1135 ARG ARG B . n 
B 1 226 ILE 226 1136 1136 ILE ILE B . n 
B 1 227 ALA 227 1137 1137 ALA ALA B . n 
B 1 228 PHE 228 1138 1138 PHE PHE B . n 
B 1 229 PHE 229 1139 1139 PHE PHE B . n 
B 1 230 SER 230 1140 1140 SER SER B . n 
B 1 231 SER 231 1141 1141 SER SER B . n 
B 1 232 ARG 232 1142 1142 ARG ARG B . n 
B 1 233 ASP 233 1143 1143 ASP ASP B . n 
B 1 234 ILE 234 1144 1144 ILE ILE B . n 
B 1 235 ARG 235 1145 1145 ARG ARG B . n 
B 1 236 THR 236 1146 1146 THR THR B . n 
B 1 237 GLY 237 1147 1147 GLY GLY B . n 
B 1 238 GLU 238 1148 1148 GLU GLU B . n 
B 1 239 GLU 239 1149 1149 GLU GLU B . n 
B 1 240 LEU 240 1150 1150 LEU LEU B . n 
B 1 241 GLY 241 1151 1151 GLY GLY B . n 
B 1 242 PHE 242 1152 1152 PHE PHE B . n 
B 1 243 ASP 243 1153 1153 ASP ASP B . n 
B 1 244 TYR 244 1154 1154 TYR TYR B . n 
B 1 245 GLY 245 1155 1155 GLY GLY B . n 
B 1 246 ASP 246 1156 1156 ASP ASP B . n 
B 1 247 ARG 247 1157 1157 ARG ARG B . n 
B 1 248 PHE 248 1158 1158 PHE PHE B . n 
B 1 249 TRP 249 1159 1159 TRP TRP B . n 
B 1 250 ASP 250 1160 1160 ASP ASP B . n 
B 1 251 ILE 251 1161 1161 ILE ILE B . n 
B 1 252 LYS 252 1162 1162 LYS LYS B . n 
B 1 253 SER 253 1163 1163 SER SER B . n 
B 1 254 LYS 254 1164 1164 LYS LYS B . n 
B 1 255 TYR 255 1165 1165 TYR TYR B . n 
B 1 256 PHE 256 1166 1166 PHE PHE B . n 
B 1 257 THR 257 1167 1167 THR THR B . n 
B 1 258 CYS 258 1168 1168 CYS CYS B . n 
B 1 259 GLN 259 1169 1169 GLN GLN B . n 
B 1 260 CYS 260 1170 1170 CYS CYS B . n 
B 1 261 GLY 261 1171 1171 GLY GLY B . n 
B 1 262 SER 262 1172 1172 SER SER B . n 
B 1 263 GLU 263 1173 1173 GLU GLU B . n 
B 1 264 LYS 264 1174 1174 LYS LYS B . n 
B 1 265 CYS 265 1175 1175 CYS CYS B . n 
B 1 266 LYS 266 1176 1176 LYS LYS B . n 
B 1 267 HIS 267 1177 1177 HIS HIS B . n 
B 1 268 SER 268 1178 1178 SER SER B . n 
B 1 269 ALA 269 1179 1179 ALA ALA B . n 
B 1 270 GLU 270 1180 1180 GLU GLU B . n 
B 1 271 ALA 271 1181 1181 ALA ALA B . n 
B 1 272 ILE 272 1182 1182 ILE ILE B . n 
B 1 273 ALA 273 1183 1183 ALA ALA B . n 
B 1 274 LEU 274 1184 1184 LEU LEU B . n 
B 1 275 GLU 275 1185 1185 GLU GLU B . n 
B 1 276 GLN 276 1186 1186 GLN GLN B . n 
B 1 277 SER 277 1187 1187 SER SER B . n 
B 1 278 ARG 278 1188 ?    ?   ?   B . n 
B 1 279 LEU 279 1189 ?    ?   ?   B . n 
B 1 280 ALA 280 1190 ?    ?   ?   B . n 
B 1 281 ARG 281 1191 ?    ?   ?   B . n 
B 1 282 LEU 282 1192 ?    ?   ?   B . n 
B 1 283 ASP 283 1193 ?    ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1L58 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1L58 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 ZN    1   1201 1394 ZN    ZN  A . 
D 2 ZN    1   1202 1395 ZN    ZN  A . 
E 2 ZN    1   1203 1396 ZN    ZN  A . 
F 2 ZN    1   1204 1397 ZN    ZN  A . 
G 3 SFG   1   1205 1501 SFG   SFG A . 
H 4 A1L58 1   1206 2001 A1L58 902 A . 
I 2 ZN    1   1201 1394 ZN    ZN  B . 
J 2 ZN    1   1202 1395 ZN    ZN  B . 
K 2 ZN    1   1203 1396 ZN    ZN  B . 
L 2 ZN    1   1204 1397 ZN    ZN  B . 
M 3 SFG   1   1205 1501 SFG   SFG B . 
N 4 A1L58 1   1206 2001 A1L58 902 B . 
O 5 HOH   1   1301 113  HOH   HOH A . 
O 5 HOH   2   1302 218  HOH   HOH A . 
O 5 HOH   3   1303 81   HOH   HOH A . 
O 5 HOH   4   1304 116  HOH   HOH A . 
O 5 HOH   5   1305 167  HOH   HOH A . 
O 5 HOH   6   1306 25   HOH   HOH A . 
O 5 HOH   7   1307 119  HOH   HOH A . 
O 5 HOH   8   1308 186  HOH   HOH A . 
O 5 HOH   9   1309 22   HOH   HOH A . 
O 5 HOH   10  1310 166  HOH   HOH A . 
O 5 HOH   11  1311 82   HOH   HOH A . 
O 5 HOH   12  1312 54   HOH   HOH A . 
O 5 HOH   13  1313 185  HOH   HOH A . 
O 5 HOH   14  1314 171  HOH   HOH A . 
O 5 HOH   15  1315 176  HOH   HOH A . 
O 5 HOH   16  1316 48   HOH   HOH A . 
O 5 HOH   17  1317 210  HOH   HOH A . 
O 5 HOH   18  1318 109  HOH   HOH A . 
O 5 HOH   19  1319 127  HOH   HOH A . 
O 5 HOH   20  1320 183  HOH   HOH A . 
O 5 HOH   21  1321 112  HOH   HOH A . 
O 5 HOH   22  1322 28   HOH   HOH A . 
O 5 HOH   23  1323 151  HOH   HOH A . 
O 5 HOH   24  1324 46   HOH   HOH A . 
O 5 HOH   25  1325 194  HOH   HOH A . 
O 5 HOH   26  1326 65   HOH   HOH A . 
O 5 HOH   27  1327 49   HOH   HOH A . 
O 5 HOH   28  1328 43   HOH   HOH A . 
O 5 HOH   29  1329 23   HOH   HOH A . 
O 5 HOH   30  1330 188  HOH   HOH A . 
O 5 HOH   31  1331 52   HOH   HOH A . 
O 5 HOH   32  1332 198  HOH   HOH A . 
O 5 HOH   33  1333 95   HOH   HOH A . 
O 5 HOH   34  1334 2    HOH   HOH A . 
O 5 HOH   35  1335 73   HOH   HOH A . 
O 5 HOH   36  1336 197  HOH   HOH A . 
O 5 HOH   37  1337 10   HOH   HOH A . 
O 5 HOH   38  1338 40   HOH   HOH A . 
O 5 HOH   39  1339 160  HOH   HOH A . 
O 5 HOH   40  1340 158  HOH   HOH A . 
O 5 HOH   41  1341 7    HOH   HOH A . 
O 5 HOH   42  1342 15   HOH   HOH A . 
O 5 HOH   43  1343 162  HOH   HOH A . 
O 5 HOH   44  1344 11   HOH   HOH A . 
O 5 HOH   45  1345 37   HOH   HOH A . 
O 5 HOH   46  1346 70   HOH   HOH A . 
O 5 HOH   47  1347 122  HOH   HOH A . 
O 5 HOH   48  1348 213  HOH   HOH A . 
O 5 HOH   49  1349 169  HOH   HOH A . 
O 5 HOH   50  1350 129  HOH   HOH A . 
O 5 HOH   51  1351 50   HOH   HOH A . 
O 5 HOH   52  1352 76   HOH   HOH A . 
O 5 HOH   53  1353 9    HOH   HOH A . 
O 5 HOH   54  1354 53   HOH   HOH A . 
O 5 HOH   55  1355 209  HOH   HOH A . 
O 5 HOH   56  1356 106  HOH   HOH A . 
O 5 HOH   57  1357 203  HOH   HOH A . 
O 5 HOH   58  1358 72   HOH   HOH A . 
O 5 HOH   59  1359 111  HOH   HOH A . 
O 5 HOH   60  1360 96   HOH   HOH A . 
O 5 HOH   61  1361 51   HOH   HOH A . 
O 5 HOH   62  1362 202  HOH   HOH A . 
O 5 HOH   63  1363 58   HOH   HOH A . 
O 5 HOH   64  1364 189  HOH   HOH A . 
O 5 HOH   65  1365 215  HOH   HOH A . 
O 5 HOH   66  1366 4    HOH   HOH A . 
O 5 HOH   67  1367 153  HOH   HOH A . 
O 5 HOH   68  1368 100  HOH   HOH A . 
O 5 HOH   69  1369 123  HOH   HOH A . 
O 5 HOH   70  1370 14   HOH   HOH A . 
O 5 HOH   71  1371 148  HOH   HOH A . 
O 5 HOH   72  1372 87   HOH   HOH A . 
O 5 HOH   73  1373 55   HOH   HOH A . 
O 5 HOH   74  1374 20   HOH   HOH A . 
O 5 HOH   75  1375 64   HOH   HOH A . 
O 5 HOH   76  1376 135  HOH   HOH A . 
O 5 HOH   77  1377 31   HOH   HOH A . 
O 5 HOH   78  1378 208  HOH   HOH A . 
O 5 HOH   79  1379 130  HOH   HOH A . 
O 5 HOH   80  1380 205  HOH   HOH A . 
O 5 HOH   81  1381 201  HOH   HOH A . 
O 5 HOH   82  1382 155  HOH   HOH A . 
O 5 HOH   83  1383 177  HOH   HOH A . 
O 5 HOH   84  1384 140  HOH   HOH A . 
O 5 HOH   85  1385 181  HOH   HOH A . 
O 5 HOH   86  1386 156  HOH   HOH A . 
O 5 HOH   87  1387 180  HOH   HOH A . 
O 5 HOH   88  1388 110  HOH   HOH A . 
O 5 HOH   89  1389 125  HOH   HOH A . 
O 5 HOH   90  1390 61   HOH   HOH A . 
O 5 HOH   91  1391 92   HOH   HOH A . 
O 5 HOH   92  1392 69   HOH   HOH A . 
O 5 HOH   93  1393 164  HOH   HOH A . 
O 5 HOH   94  1394 128  HOH   HOH A . 
O 5 HOH   95  1395 217  HOH   HOH A . 
O 5 HOH   96  1396 83   HOH   HOH A . 
O 5 HOH   97  1397 163  HOH   HOH A . 
O 5 HOH   98  1398 94   HOH   HOH A . 
O 5 HOH   99  1399 172  HOH   HOH A . 
O 5 HOH   100 1400 59   HOH   HOH A . 
O 5 HOH   101 1401 68   HOH   HOH A . 
O 5 HOH   102 1402 80   HOH   HOH A . 
O 5 HOH   103 1403 214  HOH   HOH A . 
O 5 HOH   104 1404 184  HOH   HOH A . 
O 5 HOH   105 1405 157  HOH   HOH A . 
O 5 HOH   106 1406 131  HOH   HOH A . 
O 5 HOH   107 1407 99   HOH   HOH A . 
O 5 HOH   108 1408 159  HOH   HOH A . 
O 5 HOH   109 1409 206  HOH   HOH A . 
O 5 HOH   110 1410 178  HOH   HOH A . 
O 5 HOH   111 1411 152  HOH   HOH A . 
O 5 HOH   112 1412 193  HOH   HOH A . 
O 5 HOH   113 1413 147  HOH   HOH A . 
O 5 HOH   114 1414 192  HOH   HOH A . 
O 5 HOH   115 1415 114  HOH   HOH A . 
P 5 HOH   1   1301 132  HOH   HOH B . 
P 5 HOH   2   1302 1    HOH   HOH B . 
P 5 HOH   3   1303 138  HOH   HOH B . 
P 5 HOH   4   1304 63   HOH   HOH B . 
P 5 HOH   5   1305 62   HOH   HOH B . 
P 5 HOH   6   1306 89   HOH   HOH B . 
P 5 HOH   7   1307 24   HOH   HOH B . 
P 5 HOH   8   1308 56   HOH   HOH B . 
P 5 HOH   9   1309 107  HOH   HOH B . 
P 5 HOH   10  1310 74   HOH   HOH B . 
P 5 HOH   11  1311 105  HOH   HOH B . 
P 5 HOH   12  1312 36   HOH   HOH B . 
P 5 HOH   13  1313 179  HOH   HOH B . 
P 5 HOH   14  1314 175  HOH   HOH B . 
P 5 HOH   15  1315 84   HOH   HOH B . 
P 5 HOH   16  1316 12   HOH   HOH B . 
P 5 HOH   17  1317 98   HOH   HOH B . 
P 5 HOH   18  1318 26   HOH   HOH B . 
P 5 HOH   19  1319 137  HOH   HOH B . 
P 5 HOH   20  1320 91   HOH   HOH B . 
P 5 HOH   21  1321 29   HOH   HOH B . 
P 5 HOH   22  1322 18   HOH   HOH B . 
P 5 HOH   23  1323 75   HOH   HOH B . 
P 5 HOH   24  1324 136  HOH   HOH B . 
P 5 HOH   25  1325 6    HOH   HOH B . 
P 5 HOH   26  1326 21   HOH   HOH B . 
P 5 HOH   27  1327 117  HOH   HOH B . 
P 5 HOH   28  1328 120  HOH   HOH B . 
P 5 HOH   29  1329 8    HOH   HOH B . 
P 5 HOH   30  1330 115  HOH   HOH B . 
P 5 HOH   31  1331 118  HOH   HOH B . 
P 5 HOH   32  1332 5    HOH   HOH B . 
P 5 HOH   33  1333 165  HOH   HOH B . 
P 5 HOH   34  1334 39   HOH   HOH B . 
P 5 HOH   35  1335 13   HOH   HOH B . 
P 5 HOH   36  1336 150  HOH   HOH B . 
P 5 HOH   37  1337 3    HOH   HOH B . 
P 5 HOH   38  1338 85   HOH   HOH B . 
P 5 HOH   39  1339 219  HOH   HOH B . 
P 5 HOH   40  1340 35   HOH   HOH B . 
P 5 HOH   41  1341 161  HOH   HOH B . 
P 5 HOH   42  1342 33   HOH   HOH B . 
P 5 HOH   43  1343 168  HOH   HOH B . 
P 5 HOH   44  1344 47   HOH   HOH B . 
P 5 HOH   45  1345 79   HOH   HOH B . 
P 5 HOH   46  1346 30   HOH   HOH B . 
P 5 HOH   47  1347 19   HOH   HOH B . 
P 5 HOH   48  1348 45   HOH   HOH B . 
P 5 HOH   49  1349 67   HOH   HOH B . 
P 5 HOH   50  1350 216  HOH   HOH B . 
P 5 HOH   51  1351 27   HOH   HOH B . 
P 5 HOH   52  1352 34   HOH   HOH B . 
P 5 HOH   53  1353 134  HOH   HOH B . 
P 5 HOH   54  1354 170  HOH   HOH B . 
P 5 HOH   55  1355 90   HOH   HOH B . 
P 5 HOH   56  1356 71   HOH   HOH B . 
P 5 HOH   57  1357 103  HOH   HOH B . 
P 5 HOH   58  1358 42   HOH   HOH B . 
P 5 HOH   59  1359 77   HOH   HOH B . 
P 5 HOH   60  1360 199  HOH   HOH B . 
P 5 HOH   61  1361 41   HOH   HOH B . 
P 5 HOH   62  1362 86   HOH   HOH B . 
P 5 HOH   63  1363 57   HOH   HOH B . 
P 5 HOH   64  1364 66   HOH   HOH B . 
P 5 HOH   65  1365 97   HOH   HOH B . 
P 5 HOH   66  1366 16   HOH   HOH B . 
P 5 HOH   67  1367 108  HOH   HOH B . 
P 5 HOH   68  1368 173  HOH   HOH B . 
P 5 HOH   69  1369 144  HOH   HOH B . 
P 5 HOH   70  1370 104  HOH   HOH B . 
P 5 HOH   71  1371 133  HOH   HOH B . 
P 5 HOH   72  1372 174  HOH   HOH B . 
P 5 HOH   73  1373 143  HOH   HOH B . 
P 5 HOH   74  1374 211  HOH   HOH B . 
P 5 HOH   75  1375 17   HOH   HOH B . 
P 5 HOH   76  1376 101  HOH   HOH B . 
P 5 HOH   77  1377 32   HOH   HOH B . 
P 5 HOH   78  1378 207  HOH   HOH B . 
P 5 HOH   79  1379 212  HOH   HOH B . 
P 5 HOH   80  1380 126  HOH   HOH B . 
P 5 HOH   81  1381 190  HOH   HOH B . 
P 5 HOH   82  1382 187  HOH   HOH B . 
P 5 HOH   83  1383 44   HOH   HOH B . 
P 5 HOH   84  1384 191  HOH   HOH B . 
P 5 HOH   85  1385 196  HOH   HOH B . 
P 5 HOH   86  1386 142  HOH   HOH B . 
P 5 HOH   87  1387 88   HOH   HOH B . 
P 5 HOH   88  1388 38   HOH   HOH B . 
P 5 HOH   89  1389 60   HOH   HOH B . 
P 5 HOH   90  1390 182  HOH   HOH B . 
P 5 HOH   91  1391 139  HOH   HOH B . 
P 5 HOH   92  1392 204  HOH   HOH B . 
P 5 HOH   93  1393 93   HOH   HOH B . 
P 5 HOH   94  1394 141  HOH   HOH B . 
P 5 HOH   95  1395 121  HOH   HOH B . 
P 5 HOH   96  1396 102  HOH   HOH B . 
P 5 HOH   97  1397 145  HOH   HOH B . 
P 5 HOH   98  1398 200  HOH   HOH B . 
P 5 HOH   99  1399 124  HOH   HOH B . 
P 5 HOH   100 1400 78   HOH   HOH B . 
P 5 HOH   101 1401 154  HOH   HOH B . 
P 5 HOH   102 1402 149  HOH   HOH B . 
P 5 HOH   103 1403 195  HOH   HOH B . 
P 5 HOH   104 1404 146  HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A ASP 1090 ? CG  ? A ASP 180 CG  
2  1 Y 1 A ASP 1090 ? OD1 ? A ASP 180 OD1 
3  1 Y 1 A ASP 1090 ? OD2 ? A ASP 180 OD2 
4  1 Y 1 A ASN 1091 ? CG  ? A ASN 181 CG  
5  1 Y 1 A ASN 1091 ? OD1 ? A ASN 181 OD1 
6  1 Y 1 A ASN 1091 ? ND2 ? A ASN 181 ND2 
7  1 Y 1 A LYS 1164 ? CG  ? A LYS 254 CG  
8  1 Y 1 A LYS 1164 ? CD  ? A LYS 254 CD  
9  1 Y 1 A LYS 1164 ? CE  ? A LYS 254 CE  
10 1 Y 1 A LYS 1164 ? NZ  ? A LYS 254 NZ  
11 1 Y 1 A GLU 1173 ? CG  ? A GLU 263 CG  
12 1 Y 1 A GLU 1173 ? CD  ? A GLU 263 CD  
13 1 Y 1 A GLU 1173 ? OE1 ? A GLU 263 OE1 
14 1 Y 1 A GLU 1173 ? OE2 ? A GLU 263 OE2 
15 1 Y 1 B GLU 1081 ? CG  ? B GLU 171 CG  
16 1 Y 1 B GLU 1081 ? CD  ? B GLU 171 CD  
17 1 Y 1 B GLU 1081 ? OE1 ? B GLU 171 OE1 
18 1 Y 1 B GLU 1081 ? OE2 ? B GLU 171 OE2 
19 1 Y 1 B LYS 1092 ? CB  ? B LYS 182 CB  
20 1 Y 1 B LYS 1092 ? CG  ? B LYS 182 CG  
21 1 Y 1 B LYS 1092 ? CD  ? B LYS 182 CD  
22 1 Y 1 B LYS 1092 ? CE  ? B LYS 182 CE  
23 1 Y 1 B LYS 1092 ? NZ  ? B LYS 182 NZ  
24 1 Y 1 B ASP 1093 ? CB  ? B ASP 183 CB  
25 1 Y 1 B ASP 1093 ? CG  ? B ASP 183 CG  
26 1 Y 1 B ASP 1093 ? OD1 ? B ASP 183 OD1 
27 1 Y 1 B ASP 1093 ? OD2 ? B ASP 183 OD2 
28 1 Y 1 B LYS 1164 ? CG  ? B LYS 254 CG  
29 1 Y 1 B LYS 1164 ? CD  ? B LYS 254 CD  
30 1 Y 1 B LYS 1164 ? CE  ? B LYS 254 CE  
31 1 Y 1 B LYS 1164 ? NZ  ? B LYS 254 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX   ? ? ? '(1.20.1_4487: ???)' 1 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    2 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? HKL-2000 ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   91.30 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9KLC 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     56.714 
_cell.length_a_esd                 ? 
_cell.length_b                     78.066 
_cell.length_b_esd                 ? 
_cell.length_c                     70.583 
_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                         9KLC 
_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                   9KLC 
_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             2.40 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          48.65 
_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, HANGING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
'0.1M Bis-Tris propane (pH~7.5), 0.2M Sodium Formate or Fluoride, 10% Ethylene Glycol, ~25% PEG3350' 
_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                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'MARMOSAIC 225 mm CCD' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2014-06-27 
_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   1.000 
_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                        'SPRING-8 BEAMLINE BL26B2' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.000 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   BL26B2 
_diffrn_source.pdbx_synchrotron_site       SPring-8 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9KLC 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              2.15 
_reflns.d_resolution_low                               50.00 
_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                                     31362 
_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                           93.6 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                3.5 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          7.5 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.145 
_reflns.pdbx_Rpim_I_all                                0.075 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   ? 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              0.124 
_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                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
2.15 2.19  ? ? ? ? ? ? 1077 ? ? ? ? ? ? ? ? ? ? ? 2.9 0.958 ? ? 0.510 0.283 ? 1  1 0.741 0.923 ? 63.8  ? 0.422 ? ? ? ? ? ? ? ? ? 
2.19 2.23  ? ? ? ? ? ? 1113 ? ? ? ? ? ? ? ? ? ? ? 2.9 0.941 ? ? 0.480 0.265 ? 2  1 0.796 0.941 ? 67.9  ? 0.398 ? ? ? ? ? ? ? ? ? 
2.23 2.27  ? ? ? ? ? ? 1253 ? ? ? ? ? ? ? ? ? ? ? 2.9 1.044 ? ? 0.389 0.213 ? 3  1 0.923 0.980 ? 75.5  ? 0.323 ? ? ? ? ? ? ? ? ? 
2.27 2.32  ? ? ? ? ? ? 1361 ? ? ? ? ? ? ? ? ? ? ? 3.0 0.975 ? ? 0.469 0.256 ? 4  1 0.832 0.953 ? 82.6  ? 0.391 ? ? ? ? ? ? ? ? ? 
2.32 2.37  ? ? ? ? ? ? 1506 ? ? ? ? ? ? ? ? ? ? ? 3.1 0.990 ? ? 0.411 0.222 ? 5  1 0.907 0.975 ? 89.1  ? 0.344 ? ? ? ? ? ? ? ? ? 
2.37 2.42  ? ? ? ? ? ? 1577 ? ? ? ? ? ? ? ? ? ? ? 3.2 1.006 ? ? 0.468 0.252 ? 6  1 0.872 0.965 ? 95.0  ? 0.393 ? ? ? ? ? ? ? ? ? 
2.42 2.48  ? ? ? ? ? ? 1648 ? ? ? ? ? ? ? ? ? ? ? 3.4 1.026 ? ? 0.431 0.229 ? 7  1 0.910 0.976 ? 98.8  ? 0.364 ? ? ? ? ? ? ? ? ? 
2.48 2.55  ? ? ? ? ? ? 1673 ? ? ? ? ? ? ? ? ? ? ? 3.5 1.076 ? ? 0.439 0.230 ? 8  1 0.897 0.972 ? 99.9  ? 0.373 ? ? ? ? ? ? ? ? ? 
2.55 2.62  ? ? ? ? ? ? 1655 ? ? ? ? ? ? ? ? ? ? ? 3.6 1.065 ? ? 0.354 0.183 ? 9  1 0.940 0.984 ? 99.9  ? 0.302 ? ? ? ? ? ? ? ? ? 
2.62 2.71  ? ? ? ? ? ? 1680 ? ? ? ? ? ? ? ? ? ? ? 3.7 1.143 ? ? 0.310 0.160 ? 10 1 0.950 0.987 ? 99.9  ? 0.265 ? ? ? ? ? ? ? ? ? 
2.71 2.81  ? ? ? ? ? ? 1653 ? ? ? ? ? ? ? ? ? ? ? 3.7 1.044 ? ? 0.273 0.141 ? 11 1 0.954 0.988 ? 99.9  ? 0.234 ? ? ? ? ? ? ? ? ? 
2.81 2.92  ? ? ? ? ? ? 1681 ? ? ? ? ? ? ? ? ? ? ? 3.7 1.107 ? ? 0.225 0.116 ? 12 1 0.966 0.991 ? 100.0 ? 0.193 ? ? ? ? ? ? ? ? ? 
2.92 3.05  ? ? ? ? ? ? 1665 ? ? ? ? ? ? ? ? ? ? ? 3.8 1.157 ? ? 0.204 0.105 ? 13 1 0.969 0.992 ? 100.0 ? 0.175 ? ? ? ? ? ? ? ? ? 
3.05 3.21  ? ? ? ? ? ? 1685 ? ? ? ? ? ? ? ? ? ? ? 3.8 1.051 ? ? 0.167 0.086 ? 14 1 0.976 0.994 ? 100.0 ? 0.143 ? ? ? ? ? ? ? ? ? 
3.21 3.41  ? ? ? ? ? ? 1662 ? ? ? ? ? ? ? ? ? ? ? 3.8 1.077 ? ? 0.148 0.076 ? 15 1 0.977 0.994 ? 100.0 ? 0.127 ? ? ? ? ? ? ? ? ? 
3.41 3.68  ? ? ? ? ? ? 1676 ? ? ? ? ? ? ? ? ? ? ? 3.8 1.105 ? ? 0.135 0.069 ? 16 1 0.980 0.995 ? 100.0 ? 0.116 ? ? ? ? ? ? ? ? ? 
3.68 4.05  ? ? ? ? ? ? 1689 ? ? ? ? ? ? ? ? ? ? ? 3.8 1.096 ? ? 0.130 0.066 ? 17 1 0.982 0.995 ? 100.0 ? 0.111 ? ? ? ? ? ? ? ? ? 
4.05 4.63  ? ? ? ? ? ? 1685 ? ? ? ? ? ? ? ? ? ? ? 3.8 1.111 ? ? 0.108 0.055 ? 18 1 0.983 0.996 ? 100.0 ? 0.093 ? ? ? ? ? ? ? ? ? 
4.63 5.83  ? ? ? ? ? ? 1691 ? ? ? ? ? ? ? ? ? ? ? 3.8 1.074 ? ? 0.078 0.040 ? 19 1 0.993 0.998 ? 100.0 ? 0.067 ? ? ? ? ? ? ? ? ? 
5.83 50.00 ? ? ? ? ? ? 1732 ? ? ? ? ? ? ? ? ? ? ? 3.7 1.201 ? ? 0.069 0.036 ? 20 1 0.995 0.999 ? 99.5  ? 0.059 ? ? ? ? ? ? ? ? ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9KLC 
_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                            2.15 
_refine.ls_d_res_low                             38.79 
_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                     31332 
_refine.ls_number_reflns_R_free                  1588 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    93.40 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2098 
_refine.ls_R_factor_R_free                       0.2534 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2074 
_refine.ls_R_Fsqd_factor_obs                     ? 
_refine.ls_R_I_factor_obs                        ? 
_refine.ls_redundancy_reflns_all                 ? 
_refine.ls_redundancy_reflns_obs                 ? 
_refine.ls_restrained_S_all                      ? 
_refine.ls_restrained_S_obs                      ? 
_refine.ls_shift_over_esd_max                    ? 
_refine.ls_shift_over_esd_mean                   ? 
_refine.ls_structure_factor_coef                 ? 
_refine.ls_weighting_details                     ? 
_refine.ls_weighting_scheme                      ? 
_refine.ls_wR_factor_all                         ? 
_refine.ls_wR_factor_obs                         ? 
_refine.ls_wR_factor_R_free                      ? 
_refine.ls_wR_factor_R_work                      ? 
_refine.occupancy_max                            ? 
_refine.occupancy_min                            ? 
_refine.solvent_model_details                    'FLAT BULK SOLVENT MODEL' 
_refine.solvent_model_param_bsol                 ? 
_refine.solvent_model_param_ksol                 ? 
_refine.pdbx_R_complete                          ? 
_refine.ls_R_factor_gt                           ? 
_refine.ls_goodness_of_fit_gt                    ? 
_refine.ls_goodness_of_fit_ref                   ? 
_refine.ls_shift_over_su_max                     ? 
_refine.ls_shift_over_su_max_lt                  ? 
_refine.ls_shift_over_su_mean                    ? 
_refine.ls_shift_over_su_mean_lt                 ? 
_refine.pdbx_ls_sigma_I                          ? 
_refine.pdbx_ls_sigma_F                          1.37 
_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               'FREE R-VALUE' 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            ? 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 29.26 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.31 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.pdbx_number_atoms_protein        4326 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         138 
_refine_hist.number_atoms_solvent             219 
_refine_hist.number_atoms_total               4683 
_refine_hist.d_res_high                       2.15 
_refine_hist.d_res_low                        38.79 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.008  ? ?    ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.917  ? ?    ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 17.625 ? 1700 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.053  ? 650  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 804  ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 2.15 2.22  . . 106 1833 65.00  . . . . 0.2649 . . . . . . . . . . . 0.3588 
'X-RAY DIFFRACTION' 2.22 2.30  . . 108 2209 76.00  . . . . 0.2644 . . . . . . . . . . . 0.2865 
'X-RAY DIFFRACTION' 2.30 2.39  . . 138 2538 89.00  . . . . 0.2593 . . . . . . . . . . . 0.3111 
'X-RAY DIFFRACTION' 2.39 2.50  . . 155 2817 98.00  . . . . 0.2595 . . . . . . . . . . . 0.3308 
'X-RAY DIFFRACTION' 2.50 2.63  . . 167 2869 100.00 . . . . 0.2417 . . . . . . . . . . . 0.2716 
'X-RAY DIFFRACTION' 2.63 2.80  . . 158 2898 100.00 . . . . 0.2314 . . . . . . . . . . . 0.2954 
'X-RAY DIFFRACTION' 2.80 3.01  . . 128 2927 100.00 . . . . 0.2307 . . . . . . . . . . . 0.2932 
'X-RAY DIFFRACTION' 3.01 3.32  . . 148 2890 100.00 . . . . 0.2228 . . . . . . . . . . . 0.2611 
'X-RAY DIFFRACTION' 3.32 3.80  . . 169 2876 100.00 . . . . 0.1861 . . . . . . . . . . . 0.2473 
'X-RAY DIFFRACTION' 3.80 4.78  . . 152 2932 100.00 . . . . 0.1656 . . . . . . . . . . . 0.2186 
'X-RAY DIFFRACTION' 4.78 38.79 . . 159 2955 100.00 . . . . 0.1828 . . . . . . . . . . . 0.2018 
# 
_struct.entry_id                     9KLC 
_struct.title                        'G9a in complex with the S-isomer of RK-131902 (racemic compound rac-10a)' 
_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        9KLC 
_struct_keywords.text            'histone lysine methyltransferase, inhibitor, protein-inhibitor complex, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
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 3 ? 
H N N 4 ? 
I N N 2 ? 
J N N 2 ? 
K N N 2 ? 
L N N 2 ? 
M N N 3 ? 
N N N 4 ? 
O N N 5 ? 
P N N 5 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    EHMT2_HUMAN 
_struct_ref.pdbx_db_accession          Q96KQ7 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;NRAIRTEKIICRDVARGYENVPIPCVNGVDGEPCPEDYKYISENCETSTMNIDRNITHLQHCTCVDDCSSSNCLCGQLSI
RCWYDKDGRLLQEFNKIEPPLIFECNQACSCWRNCKNRVVQSGIKVRLQLYRTAKMGWGVRALQTIPQGTFICEYVGELI
SDAEADVREDDSYLFDLDNKDGEVYCIDARYYGNISRFINHLCDPNIIPVRVFMLHQDLRFPRIAFFSSRDIRTGEELGF
DYGDRFWDIKSKYFTCQCGSEKCKHSAEAIALEQSRLARLD
;
_struct_ref.pdbx_align_begin           913 
# 
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 9KLC A 3 ? 283 ? Q96KQ7 913 ? 1193 ? 913 1193 
2 1 9KLC B 3 ? 283 ? Q96KQ7 913 ? 1193 ? 913 1193 
# 
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 9KLC GLY A 1 ? UNP Q96KQ7 ? ? 'expression tag' 911 1 
1 9KLC SER A 2 ? UNP Q96KQ7 ? ? 'expression tag' 912 2 
2 9KLC GLY B 1 ? UNP Q96KQ7 ? ? 'expression tag' 911 3 
2 9KLC SER B 2 ? UNP Q96KQ7 ? ? 'expression tag' 912 4 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_and_software_defined_assembly 
_pdbx_struct_assembly.method_details       PISA 
_pdbx_struct_assembly.oligomeric_details   dimeric 
_pdbx_struct_assembly.oligomeric_count     2 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 2240  ? 
1 MORE         -10   ? 
1 'SSA (A^2)'  25500 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I,J,K,L,M,N,O,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 ASN A 57  ? LEU A 61  ? ASN A 967  LEU A 971  5 ? 5  
HELX_P HELX_P2  AA2 CYS A 75  ? SER A 81  ? CYS A 985  SER A 991  1 ? 7  
HELX_P HELX_P3  AA3 VAL A 121 ? GLY A 125 ? VAL A 1031 GLY A 1035 5 ? 5  
HELX_P HELX_P4  AA4 ASP A 164 ? VAL A 169 ? ASP A 1074 VAL A 1079 1 ? 6  
HELX_P HELX_P5  AA5 ILE A 197 ? ILE A 201 ? ILE A 1107 ILE A 1111 5 ? 5  
HELX_P HELX_P6  AA6 GLY A 245 ? SER A 253 ? GLY A 1155 SER A 1163 1 ? 9  
HELX_P HELX_P7  AA7 SER A 268 ? LEU A 279 ? SER A 1178 LEU A 1189 1 ? 12 
HELX_P HELX_P8  AA8 ASN B 57  ? LEU B 61  ? ASN B 967  LEU B 971  5 ? 5  
HELX_P HELX_P9  AA9 CYS B 75  ? SER B 81  ? CYS B 985  SER B 991  1 ? 7  
HELX_P HELX_P10 AB1 VAL B 121 ? GLY B 125 ? VAL B 1031 GLY B 1035 5 ? 5  
HELX_P HELX_P11 AB2 ASP B 164 ? ARG B 170 ? ASP B 1074 ARG B 1080 1 ? 7  
HELX_P HELX_P12 AB3 ILE B 197 ? ILE B 201 ? ILE B 1107 ILE B 1111 5 ? 5  
HELX_P HELX_P13 AB4 GLY B 245 ? LYS B 252 ? GLY B 1155 LYS B 1162 1 ? 8  
HELX_P HELX_P14 AB5 SER B 268 ? GLN B 276 ? SER B 1178 GLN B 1186 1 ? 9  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A CYS 64  SG ? ? ? 1_555 C ZN . ZN ? ? A CYS 974  A ZN 1201 1_555 ? ? ? ? ? ? ? 2.430 ? ? 
metalc2  metalc ? ? A CYS 64  SG ? ? ? 1_555 E ZN . ZN ? ? A CYS 974  A ZN 1203 1_555 ? ? ? ? ? ? ? 2.273 ? ? 
metalc3  metalc ? ? A CYS 66  SG ? ? ? 1_555 E ZN . ZN ? ? A CYS 976  A ZN 1203 1_555 ? ? ? ? ? ? ? 2.386 ? ? 
metalc4  metalc ? ? A CYS 70  SG ? ? ? 1_555 D ZN . ZN ? ? A CYS 980  A ZN 1202 1_555 ? ? ? ? ? ? ? 2.383 ? ? 
metalc5  metalc ? ? A CYS 70  SG ? ? ? 1_555 E ZN . ZN ? ? A CYS 980  A ZN 1203 1_555 ? ? ? ? ? ? ? 2.288 ? ? 
metalc6  metalc ? ? A CYS 75  SG ? ? ? 1_555 E ZN . ZN ? ? A CYS 985  A ZN 1203 1_555 ? ? ? ? ? ? ? 2.259 ? ? 
metalc7  metalc ? ? A CYS 77  SG ? ? ? 1_555 C ZN . ZN ? ? A CYS 987  A ZN 1201 1_555 ? ? ? ? ? ? ? 2.297 ? ? 
metalc8  metalc ? ? A CYS 107 SG ? ? ? 1_555 C ZN . ZN ? ? A CYS 1017 A ZN 1201 1_555 ? ? ? ? ? ? ? 2.291 ? ? 
metalc9  metalc ? ? A CYS 107 SG ? ? ? 1_555 D ZN . ZN ? ? A CYS 1017 A ZN 1202 1_555 ? ? ? ? ? ? ? 2.350 ? ? 
metalc10 metalc ? ? A CYS 111 SG ? ? ? 1_555 C ZN . ZN ? ? A CYS 1021 A ZN 1201 1_555 ? ? ? ? ? ? ? 2.287 ? ? 
metalc11 metalc ? ? A CYS 113 SG ? ? ? 1_555 D ZN . ZN ? ? A CYS 1023 A ZN 1202 1_555 ? ? ? ? ? ? ? 2.331 ? ? 
metalc12 metalc ? ? A CYS 117 SG ? ? ? 1_555 D ZN . ZN ? ? A CYS 1027 A ZN 1202 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc13 metalc ? ? A CYS 205 SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 1115 A ZN 1204 1_555 ? ? ? ? ? ? ? 2.318 ? ? 
metalc14 metalc ? ? A CYS 258 SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 1168 A ZN 1204 1_555 ? ? ? ? ? ? ? 2.356 ? ? 
metalc15 metalc ? ? A CYS 260 SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 1170 A ZN 1204 1_555 ? ? ? ? ? ? ? 2.325 ? ? 
metalc16 metalc ? ? A CYS 265 SG ? ? ? 1_555 F ZN . ZN ? ? A CYS 1175 A ZN 1204 1_555 ? ? ? ? ? ? ? 2.349 ? ? 
metalc17 metalc ? ? B CYS 64  SG ? ? ? 1_555 I ZN . ZN ? ? B CYS 974  B ZN 1201 1_555 ? ? ? ? ? ? ? 2.404 ? ? 
metalc18 metalc ? ? B CYS 64  SG ? ? ? 1_555 K ZN . ZN ? ? B CYS 974  B ZN 1203 1_555 ? ? ? ? ? ? ? 2.296 ? ? 
metalc19 metalc ? ? B CYS 66  SG ? ? ? 1_555 K ZN . ZN ? ? B CYS 976  B ZN 1203 1_555 ? ? ? ? ? ? ? 2.348 ? ? 
metalc20 metalc ? ? B CYS 70  SG ? ? ? 1_555 J ZN . ZN ? ? B CYS 980  B ZN 1202 1_555 ? ? ? ? ? ? ? 2.352 ? ? 
metalc21 metalc ? ? B CYS 70  SG ? ? ? 1_555 K ZN . ZN ? ? B CYS 980  B ZN 1203 1_555 ? ? ? ? ? ? ? 2.391 ? ? 
metalc22 metalc ? ? B CYS 75  SG ? ? ? 1_555 K ZN . ZN ? ? B CYS 985  B ZN 1203 1_555 ? ? ? ? ? ? ? 2.225 ? ? 
metalc23 metalc ? ? B CYS 77  SG ? ? ? 1_555 I ZN . ZN ? ? B CYS 987  B ZN 1201 1_555 ? ? ? ? ? ? ? 2.183 ? ? 
metalc24 metalc ? ? B CYS 107 SG ? ? ? 1_555 I ZN . ZN ? ? B CYS 1017 B ZN 1201 1_555 ? ? ? ? ? ? ? 2.339 ? ? 
metalc25 metalc ? ? B CYS 107 SG ? ? ? 1_555 J ZN . ZN ? ? B CYS 1017 B ZN 1202 1_555 ? ? ? ? ? ? ? 2.336 ? ? 
metalc26 metalc ? ? B CYS 111 SG ? ? ? 1_555 I ZN . ZN ? ? B CYS 1021 B ZN 1201 1_555 ? ? ? ? ? ? ? 2.298 ? ? 
metalc27 metalc ? ? B CYS 113 SG ? ? ? 1_555 J ZN . ZN ? ? B CYS 1023 B ZN 1202 1_555 ? ? ? ? ? ? ? 2.280 ? ? 
metalc28 metalc ? ? B CYS 117 SG ? ? ? 1_555 J ZN . ZN ? ? B CYS 1027 B ZN 1202 1_555 ? ? ? ? ? ? ? 2.378 ? ? 
metalc29 metalc ? ? B CYS 205 SG ? ? ? 1_555 L ZN . ZN ? ? B CYS 1115 B ZN 1204 1_555 ? ? ? ? ? ? ? 2.367 ? ? 
metalc30 metalc ? ? B CYS 258 SG ? ? ? 1_555 L ZN . ZN ? ? B CYS 1168 B ZN 1204 1_555 ? ? ? ? ? ? ? 2.293 ? ? 
metalc31 metalc ? ? B CYS 260 SG ? ? ? 1_555 L ZN . ZN ? ? B CYS 1170 B ZN 1204 1_555 ? ? ? ? ? ? ? 2.313 ? ? 
metalc32 metalc ? ? B CYS 265 SG ? ? ? 1_555 L ZN . ZN ? ? B CYS 1175 B ZN 1204 1_555 ? ? ? ? ? ? ? 2.319 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG ? A CYS 64  ? A CYS 974  ? 1_555 ZN ? C ZN . ? A ZN 1201 ? 1_555 SG ? A CYS 77  ? A CYS 987  ? 1_555 106.8 ? 
2  SG ? A CYS 64  ? A CYS 974  ? 1_555 ZN ? C ZN . ? A ZN 1201 ? 1_555 SG ? A CYS 107 ? A CYS 1017 ? 1_555 105.0 ? 
3  SG ? A CYS 77  ? A CYS 987  ? 1_555 ZN ? C ZN . ? A ZN 1201 ? 1_555 SG ? A CYS 107 ? A CYS 1017 ? 1_555 113.1 ? 
4  SG ? A CYS 64  ? A CYS 974  ? 1_555 ZN ? C ZN . ? A ZN 1201 ? 1_555 SG ? A CYS 111 ? A CYS 1021 ? 1_555 103.9 ? 
5  SG ? A CYS 77  ? A CYS 987  ? 1_555 ZN ? C ZN . ? A ZN 1201 ? 1_555 SG ? A CYS 111 ? A CYS 1021 ? 1_555 105.8 ? 
6  SG ? A CYS 107 ? A CYS 1017 ? 1_555 ZN ? C ZN . ? A ZN 1201 ? 1_555 SG ? A CYS 111 ? A CYS 1021 ? 1_555 121.2 ? 
7  SG ? A CYS 64  ? A CYS 974  ? 1_555 ZN ? E ZN . ? A ZN 1203 ? 1_555 SG ? A CYS 66  ? A CYS 976  ? 1_555 102.4 ? 
8  SG ? A CYS 64  ? A CYS 974  ? 1_555 ZN ? E ZN . ? A ZN 1203 ? 1_555 SG ? A CYS 70  ? A CYS 980  ? 1_555 112.2 ? 
9  SG ? A CYS 66  ? A CYS 976  ? 1_555 ZN ? E ZN . ? A ZN 1203 ? 1_555 SG ? A CYS 70  ? A CYS 980  ? 1_555 103.7 ? 
10 SG ? A CYS 64  ? A CYS 974  ? 1_555 ZN ? E ZN . ? A ZN 1203 ? 1_555 SG ? A CYS 75  ? A CYS 985  ? 1_555 120.9 ? 
11 SG ? A CYS 66  ? A CYS 976  ? 1_555 ZN ? E ZN . ? A ZN 1203 ? 1_555 SG ? A CYS 75  ? A CYS 985  ? 1_555 97.9  ? 
12 SG ? A CYS 70  ? A CYS 980  ? 1_555 ZN ? E ZN . ? A ZN 1203 ? 1_555 SG ? A CYS 75  ? A CYS 985  ? 1_555 115.7 ? 
13 SG ? A CYS 70  ? A CYS 980  ? 1_555 ZN ? D ZN . ? A ZN 1202 ? 1_555 SG ? A CYS 107 ? A CYS 1017 ? 1_555 106.5 ? 
14 SG ? A CYS 70  ? A CYS 980  ? 1_555 ZN ? D ZN . ? A ZN 1202 ? 1_555 SG ? A CYS 113 ? A CYS 1023 ? 1_555 108.4 ? 
15 SG ? A CYS 107 ? A CYS 1017 ? 1_555 ZN ? D ZN . ? A ZN 1202 ? 1_555 SG ? A CYS 113 ? A CYS 1023 ? 1_555 108.7 ? 
16 SG ? A CYS 70  ? A CYS 980  ? 1_555 ZN ? D ZN . ? A ZN 1202 ? 1_555 SG ? A CYS 117 ? A CYS 1027 ? 1_555 115.5 ? 
17 SG ? A CYS 107 ? A CYS 1017 ? 1_555 ZN ? D ZN . ? A ZN 1202 ? 1_555 SG ? A CYS 117 ? A CYS 1027 ? 1_555 113.2 ? 
18 SG ? A CYS 113 ? A CYS 1023 ? 1_555 ZN ? D ZN . ? A ZN 1202 ? 1_555 SG ? A CYS 117 ? A CYS 1027 ? 1_555 104.3 ? 
19 SG ? A CYS 205 ? A CYS 1115 ? 1_555 ZN ? F ZN . ? A ZN 1204 ? 1_555 SG ? A CYS 258 ? A CYS 1168 ? 1_555 121.3 ? 
20 SG ? A CYS 205 ? A CYS 1115 ? 1_555 ZN ? F ZN . ? A ZN 1204 ? 1_555 SG ? A CYS 260 ? A CYS 1170 ? 1_555 112.4 ? 
21 SG ? A CYS 258 ? A CYS 1168 ? 1_555 ZN ? F ZN . ? A ZN 1204 ? 1_555 SG ? A CYS 260 ? A CYS 1170 ? 1_555 105.9 ? 
22 SG ? A CYS 205 ? A CYS 1115 ? 1_555 ZN ? F ZN . ? A ZN 1204 ? 1_555 SG ? A CYS 265 ? A CYS 1175 ? 1_555 99.4  ? 
23 SG ? A CYS 258 ? A CYS 1168 ? 1_555 ZN ? F ZN . ? A ZN 1204 ? 1_555 SG ? A CYS 265 ? A CYS 1175 ? 1_555 110.8 ? 
24 SG ? A CYS 260 ? A CYS 1170 ? 1_555 ZN ? F ZN . ? A ZN 1204 ? 1_555 SG ? A CYS 265 ? A CYS 1175 ? 1_555 106.2 ? 
25 SG ? B CYS 64  ? B CYS 974  ? 1_555 ZN ? I ZN . ? B ZN 1201 ? 1_555 SG ? B CYS 77  ? B CYS 987  ? 1_555 111.3 ? 
26 SG ? B CYS 64  ? B CYS 974  ? 1_555 ZN ? I ZN . ? B ZN 1201 ? 1_555 SG ? B CYS 107 ? B CYS 1017 ? 1_555 108.5 ? 
27 SG ? B CYS 77  ? B CYS 987  ? 1_555 ZN ? I ZN . ? B ZN 1201 ? 1_555 SG ? B CYS 107 ? B CYS 1017 ? 1_555 109.2 ? 
28 SG ? B CYS 64  ? B CYS 974  ? 1_555 ZN ? I ZN . ? B ZN 1201 ? 1_555 SG ? B CYS 111 ? B CYS 1021 ? 1_555 106.6 ? 
29 SG ? B CYS 77  ? B CYS 987  ? 1_555 ZN ? I ZN . ? B ZN 1201 ? 1_555 SG ? B CYS 111 ? B CYS 1021 ? 1_555 101.9 ? 
30 SG ? B CYS 107 ? B CYS 1017 ? 1_555 ZN ? I ZN . ? B ZN 1201 ? 1_555 SG ? B CYS 111 ? B CYS 1021 ? 1_555 119.2 ? 
31 SG ? B CYS 64  ? B CYS 974  ? 1_555 ZN ? K ZN . ? B ZN 1203 ? 1_555 SG ? B CYS 66  ? B CYS 976  ? 1_555 103.2 ? 
32 SG ? B CYS 64  ? B CYS 974  ? 1_555 ZN ? K ZN . ? B ZN 1203 ? 1_555 SG ? B CYS 70  ? B CYS 980  ? 1_555 109.8 ? 
33 SG ? B CYS 66  ? B CYS 976  ? 1_555 ZN ? K ZN . ? B ZN 1203 ? 1_555 SG ? B CYS 70  ? B CYS 980  ? 1_555 106.4 ? 
34 SG ? B CYS 64  ? B CYS 974  ? 1_555 ZN ? K ZN . ? B ZN 1203 ? 1_555 SG ? B CYS 75  ? B CYS 985  ? 1_555 113.9 ? 
35 SG ? B CYS 66  ? B CYS 976  ? 1_555 ZN ? K ZN . ? B ZN 1203 ? 1_555 SG ? B CYS 75  ? B CYS 985  ? 1_555 100.7 ? 
36 SG ? B CYS 70  ? B CYS 980  ? 1_555 ZN ? K ZN . ? B ZN 1203 ? 1_555 SG ? B CYS 75  ? B CYS 985  ? 1_555 120.6 ? 
37 SG ? B CYS 70  ? B CYS 980  ? 1_555 ZN ? J ZN . ? B ZN 1202 ? 1_555 SG ? B CYS 107 ? B CYS 1017 ? 1_555 116.2 ? 
38 SG ? B CYS 70  ? B CYS 980  ? 1_555 ZN ? J ZN . ? B ZN 1202 ? 1_555 SG ? B CYS 113 ? B CYS 1023 ? 1_555 107.4 ? 
39 SG ? B CYS 107 ? B CYS 1017 ? 1_555 ZN ? J ZN . ? B ZN 1202 ? 1_555 SG ? B CYS 113 ? B CYS 1023 ? 1_555 108.1 ? 
40 SG ? B CYS 70  ? B CYS 980  ? 1_555 ZN ? J ZN . ? B ZN 1202 ? 1_555 SG ? B CYS 117 ? B CYS 1027 ? 1_555 117.1 ? 
41 SG ? B CYS 107 ? B CYS 1017 ? 1_555 ZN ? J ZN . ? B ZN 1202 ? 1_555 SG ? B CYS 117 ? B CYS 1027 ? 1_555 100.6 ? 
42 SG ? B CYS 113 ? B CYS 1023 ? 1_555 ZN ? J ZN . ? B ZN 1202 ? 1_555 SG ? B CYS 117 ? B CYS 1027 ? 1_555 106.8 ? 
43 SG ? B CYS 205 ? B CYS 1115 ? 1_555 ZN ? L ZN . ? B ZN 1204 ? 1_555 SG ? B CYS 258 ? B CYS 1168 ? 1_555 116.7 ? 
44 SG ? B CYS 205 ? B CYS 1115 ? 1_555 ZN ? L ZN . ? B ZN 1204 ? 1_555 SG ? B CYS 260 ? B CYS 1170 ? 1_555 110.9 ? 
45 SG ? B CYS 258 ? B CYS 1168 ? 1_555 ZN ? L ZN . ? B ZN 1204 ? 1_555 SG ? B CYS 260 ? B CYS 1170 ? 1_555 104.0 ? 
46 SG ? B CYS 205 ? B CYS 1115 ? 1_555 ZN ? L ZN . ? B ZN 1204 ? 1_555 SG ? B CYS 265 ? B CYS 1175 ? 1_555 100.9 ? 
47 SG ? B CYS 258 ? B CYS 1168 ? 1_555 ZN ? L ZN . ? B ZN 1204 ? 1_555 SG ? B CYS 265 ? B CYS 1175 ? 1_555 114.2 ? 
48 SG ? B CYS 260 ? B CYS 1170 ? 1_555 ZN ? L ZN . ? B ZN 1204 ? 1_555 SG ? B CYS 265 ? B CYS 1175 ? 1_555 110.3 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 4 ? 
AA3 ? 3 ? 
AA4 ? 4 ? 
AA5 ? 2 ? 
AA6 ? 4 ? 
AA7 ? 4 ? 
AA8 ? 3 ? 
AA9 ? 4 ? 
AB1 ? 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 ? anti-parallel 
AA1 2 3 ? parallel      
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? parallel      
AA3 1 2 ? parallel      
AA3 2 3 ? anti-parallel 
AA4 1 2 ? parallel      
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? parallel      
AA6 1 2 ? anti-parallel 
AA6 2 3 ? parallel      
AA6 3 4 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? parallel      
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA9 1 2 ? parallel      
AA9 2 3 ? anti-parallel 
AA9 3 4 ? anti-parallel 
AB1 1 2 ? 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 LYS A 10  ? CYS A 13  ? LYS A 920  CYS A 923  
AA1 2 CYS A 27  ? ASN A 29  ? CYS A 937  ASN A 939  
AA1 3 LEU A 130 ? ARG A 134 ? LEU A 1040 ARG A 1044 
AA1 4 TRP A 140 ? ALA A 144 ? TRP A 1050 ALA A 1054 
AA2 1 LYS A 41  ? TYR A 42  ? LYS A 951  TYR A 952  
AA2 2 TYR A 187 ? GLY A 195 ? TYR A 1097 GLY A 1105 
AA2 3 GLY A 159 ? SER A 163 ? GLY A 1069 SER A 1073 
AA2 4 CYS A 47  ? GLU A 48  ? CYS A 957  GLU A 958  
AA3 1 LYS A 41  ? TYR A 42  ? LYS A 951  TYR A 952  
AA3 2 TYR A 187 ? GLY A 195 ? TYR A 1097 GLY A 1105 
AA3 3 LEU A 176 ? ASP A 178 ? LEU A 1086 ASP A 1088 
AA4 1 ILE A 104 ? PHE A 105 ? ILE A 1014 PHE A 1015 
AA4 2 ILE A 209 ? PHE A 215 ? ILE A 1119 PHE A 1125 
AA4 3 ARG A 225 ? SER A 230 ? ARG A 1135 SER A 1140 
AA4 4 PHE A 153 ? TYR A 157 ? PHE A 1063 TYR A 1067 
AA5 1 ASN A 202 ? HIS A 203 ? ASN A 1112 HIS A 1113 
AA5 2 GLY A 241 ? PHE A 242 ? GLY A 1151 PHE A 1152 
AA6 1 LYS B 10  ? CYS B 13  ? LYS B 920  CYS B 923  
AA6 2 CYS B 27  ? ASN B 29  ? CYS B 937  ASN B 939  
AA6 3 LEU B 130 ? ARG B 134 ? LEU B 1040 ARG B 1044 
AA6 4 TRP B 140 ? ALA B 144 ? TRP B 1050 ALA B 1054 
AA7 1 LYS B 41  ? TYR B 42  ? LYS B 951  TYR B 952  
AA7 2 TYR B 187 ? GLY B 195 ? TYR B 1097 GLY B 1105 
AA7 3 GLY B 159 ? SER B 163 ? GLY B 1069 SER B 1073 
AA7 4 CYS B 47  ? GLU B 48  ? CYS B 957  GLU B 958  
AA8 1 LYS B 41  ? TYR B 42  ? LYS B 951  TYR B 952  
AA8 2 TYR B 187 ? GLY B 195 ? TYR B 1097 GLY B 1105 
AA8 3 LEU B 176 ? ASP B 178 ? LEU B 1086 ASP B 1088 
AA9 1 ILE B 104 ? PHE B 105 ? ILE B 1014 PHE B 1015 
AA9 2 ILE B 209 ? PHE B 215 ? ILE B 1119 PHE B 1125 
AA9 3 ARG B 225 ? SER B 230 ? ARG B 1135 SER B 1140 
AA9 4 PHE B 153 ? GLU B 156 ? PHE B 1063 GLU B 1066 
AB1 1 ASN B 202 ? HIS B 203 ? ASN B 1112 HIS B 1113 
AB1 2 GLY B 241 ? PHE B 242 ? GLY B 1151 PHE B 1152 
# 
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 ILE A 12  ? N ILE A 922  O CYS A 27  ? O CYS A 937  
AA1 2 3 N VAL A 28  ? N VAL A 938  O LEU A 132 ? O LEU A 1042 
AA1 3 4 N TYR A 133 ? N TYR A 1043 O GLY A 141 ? O GLY A 1051 
AA2 1 2 N LYS A 41  ? N LYS A 951  O TYR A 193 ? O TYR A 1103 
AA2 2 3 O ASP A 190 ? O ASP A 1100 N GLU A 160 ? N GLU A 1070 
AA2 3 4 O LEU A 161 ? O LEU A 1071 N CYS A 47  ? N CYS A 957  
AA3 1 2 N LYS A 41  ? N LYS A 951  O TYR A 193 ? O TYR A 1103 
AA3 2 3 O ILE A 189 ? O ILE A 1099 N PHE A 177 ? N PHE A 1087 
AA4 1 2 N ILE A 104 ? N ILE A 1014 O PHE A 215 ? O PHE A 1125 
AA4 2 3 N ILE A 210 ? N ILE A 1120 O PHE A 229 ? O PHE A 1139 
AA4 3 4 O ILE A 226 ? O ILE A 1136 N TYR A 157 ? N TYR A 1067 
AA5 1 2 N ASN A 202 ? N ASN A 1112 O PHE A 242 ? O PHE A 1152 
AA6 1 2 N ILE B 12  ? N ILE B 922  O CYS B 27  ? O CYS B 937  
AA6 2 3 N VAL B 28  ? N VAL B 938  O LEU B 132 ? O LEU B 1042 
AA6 3 4 N TYR B 133 ? N TYR B 1043 O GLY B 141 ? O GLY B 1051 
AA7 1 2 N LYS B 41  ? N LYS B 951  O TYR B 193 ? O TYR B 1103 
AA7 2 3 O ASP B 190 ? O ASP B 1100 N GLU B 160 ? N GLU B 1070 
AA7 3 4 O LEU B 161 ? O LEU B 1071 N CYS B 47  ? N CYS B 957  
AA8 1 2 N LYS B 41  ? N LYS B 951  O TYR B 193 ? O TYR B 1103 
AA8 2 3 O ILE B 189 ? O ILE B 1099 N PHE B 177 ? N PHE B 1087 
AA9 1 2 N ILE B 104 ? N ILE B 1014 O PHE B 215 ? O PHE B 1125 
AA9 2 3 N VAL B 212 ? N VAL B 1122 O ALA B 227 ? O ALA B 1137 
AA9 3 4 O PHE B 228 ? O PHE B 1138 N ILE B 154 ? N ILE B 1064 
AB1 1 2 N ASN B 202 ? N ASN B 1112 O PHE B 242 ? O PHE B 1152 
# 
_pdbx_entry_details.entry_id                   9KLC 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O   A ASN 1026 ? ? O A HOH 1301 ? ? 2.14 
2 1 O   B HOH 1354 ? ? O B HOH 1403 ? ? 2.17 
3 1 OXT B SFG 1205 ? ? O B HOH 1301 ? ? 2.19 
# 
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 ASP A 949  ? ? -94.17  36.37   
2  1 ASP A 978  ? ? -72.35  -150.07 
3  1 ILE A 992  ? ? 73.67   -66.63  
4  1 ASN A 1029 ? ? -113.93 50.33   
5  1 ARG A 1030 ? ? -145.36 41.16   
6  1 ILE A 1064 ? ? -105.46 -68.54  
7  1 ASP A 1083 ? ? -92.26  46.88   
8  1 TYR A 1085 ? ? -142.49 22.17   
9  1 ASP A 1090 ? ? 78.07   132.07  
10 1 ASN A 1106 ? ? -104.07 -156.26 
11 1 ASP A 1116 ? ? -112.95 73.68   
12 1 MET A 1126 ? ? -135.04 -87.53  
13 1 LYS A 1174 ? ? -100.83 71.68   
14 1 ASP B 925  ? ? -166.20 102.53  
15 1 VAL B 941  ? ? -108.45 -61.15  
16 1 GLU B 948  ? ? -154.33 18.02   
17 1 ASP B 965  ? ? -62.89  97.59   
18 1 ASP B 978  ? ? -106.94 -155.32 
19 1 ILE B 992  ? ? 71.90   -51.63  
20 1 ASN B 1007 ? ? -60.33  79.97   
21 1 LYS B 1008 ? ? -77.96  20.24   
22 1 LYS B 1028 ? ? -66.43  3.43    
23 1 ARG B 1030 ? ? -152.25 36.28   
24 1 ILE B 1064 ? ? -101.59 -69.20  
25 1 ASP B 1090 ? ? 70.75   59.55   
26 1 ASN B 1106 ? ? -122.50 -166.15 
27 1 ASP B 1116 ? ? -116.21 73.38   
28 1 MET B 1126 ? ? -135.73 -87.60  
29 1 TYR B 1165 ? ? -112.37 -71.28  
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined -14.6413 -4.6532 106.6217 0.2115 ? 0.0172  ? 0.0154  ? 0.3122 ? 0.0724  ? 0.8698 ? 1.9692 ? 
0.7508  ? -0.3510 ? 0.3000 ? -0.2133 ? 1.2158 ? -0.0002 ? -0.2207 ? -0.2745 ? -0.0825 ? -0.0163 ? 0.4893  ? 0.1090  ? -0.1887 ? 
0.0410  ? 
2  'X-RAY DIFFRACTION' ? refined 12.9028  10.9849 105.8394 0.1751 ? 0.0257  ? -0.0000 ? 0.3592 ? -0.0637 ? 0.6236 ? 0.6405 ? 
0.6439  ? -0.1224 ? 0.8142 ? -0.8191 ? 2.7488 ? 0.2427  ? 0.1512  ? -0.0516 ? 0.1459  ? -0.1210 ? 0.0850  ? -0.1688 ? 0.4367  ? 
-0.0629 ? 
3  'X-RAY DIFFRACTION' ? refined 13.7661  3.5905  116.7952 0.2379 ? 0.0373  ? -0.0213 ? 0.4019 ? -0.0179 ? 0.4707 ? 2.1060 ? 
0.4027  ? -0.8620 ? 2.9552 ? -0.8355 ? 3.6918 ? 0.0591  ? -0.3910 ? -0.1387 ? 0.3502  ? -0.0554 ? -0.0860 ? 0.0519  ? 0.3092  ? 
0.0123  ? 
4  'X-RAY DIFFRACTION' ? refined -4.4109  -3.8779 113.6628 0.1681 ? 0.0314  ? -0.0247 ? 0.2495 ? 0.0230  ? 0.5821 ? 3.4776 ? 
1.9116  ? 0.2039  ? 2.0145 ? -0.8800 ? 1.5216 ? 0.1278  ? -0.2158 ? -0.3659 ? -0.0339 ? 0.1251  ? 0.3591  ? 0.0222  ? -0.1387 ? 
-0.1812 ? 
5  'X-RAY DIFFRACTION' ? refined -5.7779  10.3232 114.0799 0.2803 ? 0.0129  ? 0.0989  ? 0.2447 ? -0.0735 ? 0.7872 ? 1.3339 ? 
-1.3949 ? 0.9466  ? 1.8993 ? -1.5398 ? 1.8662 ? -0.0838 ? -0.4278 ? 0.1897  ? 0.7168  ? 0.4219  ? 0.4228  ? -0.4918 ? -0.1406 ? 
-0.2319 ? 
6  'X-RAY DIFFRACTION' ? refined -3.1428  8.9807  113.8556 0.2580 ? 0.0229  ? 0.0784  ? 0.2779 ? -0.0625 ? 0.6319 ? 1.5504 ? 
-0.5088 ? 0.5143  ? 1.1350 ? -0.2929 ? 0.4693 ? 0.0701  ? -0.2604 ? 0.1579  ? 0.2573  ? 0.1430  ? 0.3267  ? -0.1330 ? -0.0470 ? 
-0.2465 ? 
7  'X-RAY DIFFRACTION' ? refined -3.6338  -0.7621 121.6812 0.2531 ? 0.0222  ? 0.0482  ? 0.3057 ? 0.0576  ? 0.4709 ? 4.3952 ? 
0.5847  ? -0.5219 ? 2.0450 ? 0.6218  ? 2.4416 ? 0.4280  ? -0.3181 ? -0.4762 ? 0.3499  ? -0.1392 ? 0.3231  ? -0.1021 ? -0.0774 ? 
-0.2685 ? 
8  'X-RAY DIFFRACTION' ? refined -16.3183 10.7374 132.2613 0.6701 ? 0.0794  ? 0.3970  ? 0.9352 ? -0.1784 ? 1.1724 ? 2.0650 ? 
0.3966  ? 1.1282  ? 1.4081 ? 0.4890  ? 4.2955 ? -0.1333 ? -1.6750 ? 0.7022  ? 0.4944  ? -0.0360 ? 0.7294  ? -0.5899 ? -0.9471 ? 
0.1776  ? 
9  'X-RAY DIFFRACTION' ? refined 23.2753  -6.8393 92.9057  0.2482 ? 0.0915  ? -0.0656 ? 0.3384 ? -0.0210 ? 0.5648 ? 4.3351 ? 
1.3045  ? -0.6955 ? 1.4005 ? -1.2467 ? 3.7415 ? -0.4387 ? -0.2328 ? -0.8397 ? 0.1646  ? 0.0893  ? -0.6023 ? 0.1826  ? 0.8067  ? 
0.3798  ? 
10 'X-RAY DIFFRACTION' ? refined 6.5697   1.9684  85.4816  0.2041 ? 0.0218  ? -0.0054 ? 0.3017 ? -0.0019 ? 0.5109 ? 4.2915 ? 
0.2136  ? -0.5176 ? 0.6768 ? 0.1224  ? 0.5441 ? 0.0644  ? 0.4258  ? 0.0877  ? -0.0718 ? 0.0280  ? -0.0990 ? -0.0680 ? 0.0052  ? 
-0.0820 ? 
11 'X-RAY DIFFRACTION' ? refined 17.0970  10.5492 81.7105  0.1651 ? -0.0257 ? 0.0010  ? 0.4532 ? 0.0269  ? 0.6751 ? 1.8943 ? 
0.1850  ? -0.5130 ? 3.5086 ? 2.0029  ? 5.3613 ? 0.1125  ? 0.6171  ? 0.9633  ? -0.3732 ? -0.0390 ? 0.0988  ? -0.4553 ? 0.2155  ? 
-0.0888 ? 
12 'X-RAY DIFFRACTION' ? refined 16.4775  5.4924  73.5507  0.2423 ? -0.0259 ? 0.0501  ? 0.5236 ? -0.0263 ? 0.6559 ? 2.4582 ? 
-1.0100 ? -1.1087 ? 1.3458 ? 0.9548  ? 2.2618 ? 0.1800  ? 0.5772  ? 0.0902  ? -0.3143 ? 0.0001  ? -0.2780 ? -0.2465 ? 0.2860  ? 
-0.1866 ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 918:954 )
;
2  'X-RAY DIFFRACTION' 2  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 955:985 )
;
3  'X-RAY DIFFRACTION' 3  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 986:1025 )
;
4  'X-RAY DIFFRACTION' 4  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 1026:1054 )
;
5  'X-RAY DIFFRACTION' 5  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 1055:1096 )
;
6  'X-RAY DIFFRACTION' 6  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 1097:1134 )
;
7  'X-RAY DIFFRACTION' 7  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 1135:1155 )
;
8  'X-RAY DIFFRACTION' 8  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'A' and (resseq 1156:1189 )
;
9  'X-RAY DIFFRACTION' 9  ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 917:935 )
;
10 'X-RAY DIFFRACTION' 10 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 936:1079 )
;
11 'X-RAY DIFFRACTION' 11 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 1080:1118 )
;
12 'X-RAY DIFFRACTION' 12 ? ? ? ? ? ? ? ? ? ? ? 
;chain 'B' and (resseq 1119:1187 )
;
# 
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 GLY 911  ? A GLY 1   
2  1 Y 1 A SER 912  ? A SER 2   
3  1 Y 1 A ASN 913  ? A ASN 3   
4  1 Y 1 A ARG 914  ? A ARG 4   
5  1 Y 1 A ALA 915  ? A ALA 5   
6  1 Y 1 A ILE 916  ? A ILE 6   
7  1 Y 1 A ARG 917  ? A ARG 7   
8  1 Y 1 A LYS 1092 ? A LYS 182 
9  1 Y 1 A ASP 1093 ? A ASP 183 
10 1 Y 1 A ALA 1190 ? A ALA 280 
11 1 Y 1 A ARG 1191 ? A ARG 281 
12 1 Y 1 A LEU 1192 ? A LEU 282 
13 1 Y 1 A ASP 1193 ? A ASP 283 
14 1 Y 1 B GLY 911  ? B GLY 1   
15 1 Y 1 B SER 912  ? B SER 2   
16 1 Y 1 B ASN 913  ? B ASN 3   
17 1 Y 1 B ARG 914  ? B ARG 4   
18 1 Y 1 B ALA 915  ? B ALA 5   
19 1 Y 1 B ILE 916  ? B ILE 6   
20 1 Y 1 B ARG 1188 ? B ARG 278 
21 1 Y 1 B LEU 1189 ? B LEU 279 
22 1 Y 1 B ALA 1190 ? B ALA 280 
23 1 Y 1 B ARG 1191 ? B ARG 281 
24 1 Y 1 B LEU 1192 ? B LEU 282 
25 1 Y 1 B ASP 1193 ? B ASP 283 
# 
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 
A1L58 C11    C  N S 1   
A1L58 C12    C  N N 2   
A1L58 C13    C  N N 3   
A1L58 C14    C  N N 4   
A1L58 C21    C  Y N 5   
A1L58 C22    C  Y N 6   
A1L58 C29    C  N N 7   
A1L58 C30    C  N N 8   
A1L58 C33    C  Y N 9   
A1L58 C34    C  Y N 10  
A1L58 C01    C  Y N 11  
A1L58 C02    C  Y N 12  
A1L58 C03    C  Y N 13  
A1L58 C05    C  Y N 14  
A1L58 C06    C  Y N 15  
A1L58 C07    C  Y N 16  
A1L58 C08    C  N N 17  
A1L58 C15    C  N N 18  
A1L58 C16    C  N N 19  
A1L58 C19    C  Y N 20  
A1L58 C20    C  Y N 21  
A1L58 C24    C  N N 22  
A1L58 C25    C  N N 23  
A1L58 C26    C  N N 24  
A1L58 C28    C  N N 25  
A1L58 C32    C  Y N 26  
A1L58 C35    C  Y N 27  
A1L58 C36    C  Y N 28  
A1L58 C37    C  Y N 29  
A1L58 N04    N  N N 30  
A1L58 N10    N  N N 31  
A1L58 N18    N  N N 32  
A1L58 N27    N  N N 33  
A1L58 N31    N  Y N 34  
A1L58 N38    N  Y N 35  
A1L58 O09    O  N N 36  
A1L58 O17    O  N N 37  
A1L58 O23    O  N N 38  
A1L58 H1     H  N N 39  
A1L58 H2     H  N N 40  
A1L58 H3     H  N N 41  
A1L58 H4     H  N N 42  
A1L58 H5     H  N N 43  
A1L58 H6     H  N N 44  
A1L58 H7     H  N N 45  
A1L58 H8     H  N N 46  
A1L58 H9     H  N N 47  
A1L58 H10    H  N N 48  
A1L58 H11    H  N N 49  
A1L58 H12    H  N N 50  
A1L58 H13    H  N N 51  
A1L58 H14    H  N N 52  
A1L58 H15    H  N N 53  
A1L58 H16    H  N N 54  
A1L58 H17    H  N N 55  
A1L58 H18    H  N N 56  
A1L58 H19    H  N N 57  
A1L58 H20    H  N N 58  
A1L58 H21    H  N N 59  
A1L58 H22    H  N N 60  
A1L58 H23    H  N N 61  
A1L58 H24    H  N N 62  
A1L58 H25    H  N N 63  
A1L58 H26    H  N N 64  
A1L58 H27    H  N N 65  
A1L58 H28    H  N N 66  
A1L58 H29    H  N N 67  
A1L58 H30    H  N N 68  
A1L58 H31    H  N N 69  
A1L58 H32    H  N N 70  
A1L58 H33    H  N N 71  
A1L58 H34    H  N N 72  
A1L58 H35    H  N N 73  
A1L58 H36    H  N N 74  
ALA   N      N  N N 75  
ALA   CA     C  N S 76  
ALA   C      C  N N 77  
ALA   O      O  N N 78  
ALA   CB     C  N N 79  
ALA   OXT    O  N N 80  
ALA   H      H  N N 81  
ALA   H2     H  N N 82  
ALA   HA     H  N N 83  
ALA   HB1    H  N N 84  
ALA   HB2    H  N N 85  
ALA   HB3    H  N N 86  
ALA   HXT    H  N N 87  
ARG   N      N  N N 88  
ARG   CA     C  N S 89  
ARG   C      C  N N 90  
ARG   O      O  N N 91  
ARG   CB     C  N N 92  
ARG   CG     C  N N 93  
ARG   CD     C  N N 94  
ARG   NE     N  N N 95  
ARG   CZ     C  N N 96  
ARG   NH1    N  N N 97  
ARG   NH2    N  N N 98  
ARG   OXT    O  N N 99  
ARG   H      H  N N 100 
ARG   H2     H  N N 101 
ARG   HA     H  N N 102 
ARG   HB2    H  N N 103 
ARG   HB3    H  N N 104 
ARG   HG2    H  N N 105 
ARG   HG3    H  N N 106 
ARG   HD2    H  N N 107 
ARG   HD3    H  N N 108 
ARG   HE     H  N N 109 
ARG   HH11   H  N N 110 
ARG   HH12   H  N N 111 
ARG   HH21   H  N N 112 
ARG   HH22   H  N N 113 
ARG   HXT    H  N N 114 
ASN   N      N  N N 115 
ASN   CA     C  N S 116 
ASN   C      C  N N 117 
ASN   O      O  N N 118 
ASN   CB     C  N N 119 
ASN   CG     C  N N 120 
ASN   OD1    O  N N 121 
ASN   ND2    N  N N 122 
ASN   OXT    O  N N 123 
ASN   H      H  N N 124 
ASN   H2     H  N N 125 
ASN   HA     H  N N 126 
ASN   HB2    H  N N 127 
ASN   HB3    H  N N 128 
ASN   HD21   H  N N 129 
ASN   HD22   H  N N 130 
ASN   HXT    H  N N 131 
ASP   N      N  N N 132 
ASP   CA     C  N S 133 
ASP   C      C  N N 134 
ASP   O      O  N N 135 
ASP   CB     C  N N 136 
ASP   CG     C  N N 137 
ASP   OD1    O  N N 138 
ASP   OD2    O  N N 139 
ASP   OXT    O  N N 140 
ASP   H      H  N N 141 
ASP   H2     H  N N 142 
ASP   HA     H  N N 143 
ASP   HB2    H  N N 144 
ASP   HB3    H  N N 145 
ASP   HD2    H  N N 146 
ASP   HXT    H  N N 147 
CYS   N      N  N N 148 
CYS   CA     C  N R 149 
CYS   C      C  N N 150 
CYS   O      O  N N 151 
CYS   CB     C  N N 152 
CYS   SG     S  N N 153 
CYS   OXT    O  N N 154 
CYS   H      H  N N 155 
CYS   H2     H  N N 156 
CYS   HA     H  N N 157 
CYS   HB2    H  N N 158 
CYS   HB3    H  N N 159 
CYS   HG     H  N N 160 
CYS   HXT    H  N N 161 
GLN   N      N  N N 162 
GLN   CA     C  N S 163 
GLN   C      C  N N 164 
GLN   O      O  N N 165 
GLN   CB     C  N N 166 
GLN   CG     C  N N 167 
GLN   CD     C  N N 168 
GLN   OE1    O  N N 169 
GLN   NE2    N  N N 170 
GLN   OXT    O  N N 171 
GLN   H      H  N N 172 
GLN   H2     H  N N 173 
GLN   HA     H  N N 174 
GLN   HB2    H  N N 175 
GLN   HB3    H  N N 176 
GLN   HG2    H  N N 177 
GLN   HG3    H  N N 178 
GLN   HE21   H  N N 179 
GLN   HE22   H  N N 180 
GLN   HXT    H  N N 181 
GLU   N      N  N N 182 
GLU   CA     C  N S 183 
GLU   C      C  N N 184 
GLU   O      O  N N 185 
GLU   CB     C  N N 186 
GLU   CG     C  N N 187 
GLU   CD     C  N N 188 
GLU   OE1    O  N N 189 
GLU   OE2    O  N N 190 
GLU   OXT    O  N N 191 
GLU   H      H  N N 192 
GLU   H2     H  N N 193 
GLU   HA     H  N N 194 
GLU   HB2    H  N N 195 
GLU   HB3    H  N N 196 
GLU   HG2    H  N N 197 
GLU   HG3    H  N N 198 
GLU   HE2    H  N N 199 
GLU   HXT    H  N N 200 
GLY   N      N  N N 201 
GLY   CA     C  N N 202 
GLY   C      C  N N 203 
GLY   O      O  N N 204 
GLY   OXT    O  N N 205 
GLY   H      H  N N 206 
GLY   H2     H  N N 207 
GLY   HA2    H  N N 208 
GLY   HA3    H  N N 209 
GLY   HXT    H  N N 210 
HIS   N      N  N N 211 
HIS   CA     C  N S 212 
HIS   C      C  N N 213 
HIS   O      O  N N 214 
HIS   CB     C  N N 215 
HIS   CG     C  Y N 216 
HIS   ND1    N  Y N 217 
HIS   CD2    C  Y N 218 
HIS   CE1    C  Y N 219 
HIS   NE2    N  Y N 220 
HIS   OXT    O  N N 221 
HIS   H      H  N N 222 
HIS   H2     H  N N 223 
HIS   HA     H  N N 224 
HIS   HB2    H  N N 225 
HIS   HB3    H  N N 226 
HIS   HD1    H  N N 227 
HIS   HD2    H  N N 228 
HIS   HE1    H  N N 229 
HIS   HE2    H  N N 230 
HIS   HXT    H  N N 231 
HOH   O      O  N N 232 
HOH   H1     H  N N 233 
HOH   H2     H  N N 234 
ILE   N      N  N N 235 
ILE   CA     C  N S 236 
ILE   C      C  N N 237 
ILE   O      O  N N 238 
ILE   CB     C  N S 239 
ILE   CG1    C  N N 240 
ILE   CG2    C  N N 241 
ILE   CD1    C  N N 242 
ILE   OXT    O  N N 243 
ILE   H      H  N N 244 
ILE   H2     H  N N 245 
ILE   HA     H  N N 246 
ILE   HB     H  N N 247 
ILE   HG12   H  N N 248 
ILE   HG13   H  N N 249 
ILE   HG21   H  N N 250 
ILE   HG22   H  N N 251 
ILE   HG23   H  N N 252 
ILE   HD11   H  N N 253 
ILE   HD12   H  N N 254 
ILE   HD13   H  N N 255 
ILE   HXT    H  N N 256 
LEU   N      N  N N 257 
LEU   CA     C  N S 258 
LEU   C      C  N N 259 
LEU   O      O  N N 260 
LEU   CB     C  N N 261 
LEU   CG     C  N N 262 
LEU   CD1    C  N N 263 
LEU   CD2    C  N N 264 
LEU   OXT    O  N N 265 
LEU   H      H  N N 266 
LEU   H2     H  N N 267 
LEU   HA     H  N N 268 
LEU   HB2    H  N N 269 
LEU   HB3    H  N N 270 
LEU   HG     H  N N 271 
LEU   HD11   H  N N 272 
LEU   HD12   H  N N 273 
LEU   HD13   H  N N 274 
LEU   HD21   H  N N 275 
LEU   HD22   H  N N 276 
LEU   HD23   H  N N 277 
LEU   HXT    H  N N 278 
LYS   N      N  N N 279 
LYS   CA     C  N S 280 
LYS   C      C  N N 281 
LYS   O      O  N N 282 
LYS   CB     C  N N 283 
LYS   CG     C  N N 284 
LYS   CD     C  N N 285 
LYS   CE     C  N N 286 
LYS   NZ     N  N N 287 
LYS   OXT    O  N N 288 
LYS   H      H  N N 289 
LYS   H2     H  N N 290 
LYS   HA     H  N N 291 
LYS   HB2    H  N N 292 
LYS   HB3    H  N N 293 
LYS   HG2    H  N N 294 
LYS   HG3    H  N N 295 
LYS   HD2    H  N N 296 
LYS   HD3    H  N N 297 
LYS   HE2    H  N N 298 
LYS   HE3    H  N N 299 
LYS   HZ1    H  N N 300 
LYS   HZ2    H  N N 301 
LYS   HZ3    H  N N 302 
LYS   HXT    H  N N 303 
MET   N      N  N N 304 
MET   CA     C  N S 305 
MET   C      C  N N 306 
MET   O      O  N N 307 
MET   CB     C  N N 308 
MET   CG     C  N N 309 
MET   SD     S  N N 310 
MET   CE     C  N N 311 
MET   OXT    O  N N 312 
MET   H      H  N N 313 
MET   H2     H  N N 314 
MET   HA     H  N N 315 
MET   HB2    H  N N 316 
MET   HB3    H  N N 317 
MET   HG2    H  N N 318 
MET   HG3    H  N N 319 
MET   HE1    H  N N 320 
MET   HE2    H  N N 321 
MET   HE3    H  N N 322 
MET   HXT    H  N N 323 
PHE   N      N  N N 324 
PHE   CA     C  N S 325 
PHE   C      C  N N 326 
PHE   O      O  N N 327 
PHE   CB     C  N N 328 
PHE   CG     C  Y N 329 
PHE   CD1    C  Y N 330 
PHE   CD2    C  Y N 331 
PHE   CE1    C  Y N 332 
PHE   CE2    C  Y N 333 
PHE   CZ     C  Y N 334 
PHE   OXT    O  N N 335 
PHE   H      H  N N 336 
PHE   H2     H  N N 337 
PHE   HA     H  N N 338 
PHE   HB2    H  N N 339 
PHE   HB3    H  N N 340 
PHE   HD1    H  N N 341 
PHE   HD2    H  N N 342 
PHE   HE1    H  N N 343 
PHE   HE2    H  N N 344 
PHE   HZ     H  N N 345 
PHE   HXT    H  N N 346 
PRO   N      N  N N 347 
PRO   CA     C  N S 348 
PRO   C      C  N N 349 
PRO   O      O  N N 350 
PRO   CB     C  N N 351 
PRO   CG     C  N N 352 
PRO   CD     C  N N 353 
PRO   OXT    O  N N 354 
PRO   H      H  N N 355 
PRO   HA     H  N N 356 
PRO   HB2    H  N N 357 
PRO   HB3    H  N N 358 
PRO   HG2    H  N N 359 
PRO   HG3    H  N N 360 
PRO   HD2    H  N N 361 
PRO   HD3    H  N N 362 
PRO   HXT    H  N N 363 
SER   N      N  N N 364 
SER   CA     C  N S 365 
SER   C      C  N N 366 
SER   O      O  N N 367 
SER   CB     C  N N 368 
SER   OG     O  N N 369 
SER   OXT    O  N N 370 
SER   H      H  N N 371 
SER   H2     H  N N 372 
SER   HA     H  N N 373 
SER   HB2    H  N N 374 
SER   HB3    H  N N 375 
SER   HG     H  N N 376 
SER   HXT    H  N N 377 
SFG   N      N  N N 378 
SFG   CA     C  N S 379 
SFG   C      C  N N 380 
SFG   O      O  N N 381 
SFG   OXT    O  N N 382 
SFG   CB     C  N N 383 
SFG   CG     C  N N 384 
SFG   CD     C  N S 385 
SFG   NE     N  N N 386 
SFG   "C5'"  C  N N 387 
SFG   "C4'"  C  N R 388 
SFG   "O4'"  O  N N 389 
SFG   "C3'"  C  N S 390 
SFG   "O3'"  O  N N 391 
SFG   "C2'"  C  N R 392 
SFG   "O2'"  O  N N 393 
SFG   "C1'"  C  N R 394 
SFG   N9     N  Y N 395 
SFG   C8     C  Y N 396 
SFG   N7     N  Y N 397 
SFG   C5     C  Y N 398 
SFG   C6     C  Y N 399 
SFG   N6     N  N N 400 
SFG   N1     N  Y N 401 
SFG   C2     C  Y N 402 
SFG   N3     N  Y N 403 
SFG   C4     C  Y N 404 
SFG   HN1    H  N N 405 
SFG   HN2    H  N N 406 
SFG   HA     H  N N 407 
SFG   HXT    H  N N 408 
SFG   HB1    H  N N 409 
SFG   HB2    H  N N 410 
SFG   HG1    H  N N 411 
SFG   HG2    H  N N 412 
SFG   HD     H  N N 413 
SFG   HNE1   H  N N 414 
SFG   HNE2   H  N N 415 
SFG   "H5'1" H  N N 416 
SFG   "H5'2" H  N N 417 
SFG   "H4'"  H  N N 418 
SFG   "H3'"  H  N N 419 
SFG   "HO3'" H  N N 420 
SFG   "H2'"  H  N N 421 
SFG   "HO2'" H  N N 422 
SFG   "H1'"  H  N N 423 
SFG   H8     H  N N 424 
SFG   HN61   H  N N 425 
SFG   HN62   H  N N 426 
SFG   H2     H  N N 427 
THR   N      N  N N 428 
THR   CA     C  N S 429 
THR   C      C  N N 430 
THR   O      O  N N 431 
THR   CB     C  N R 432 
THR   OG1    O  N N 433 
THR   CG2    C  N N 434 
THR   OXT    O  N N 435 
THR   H      H  N N 436 
THR   H2     H  N N 437 
THR   HA     H  N N 438 
THR   HB     H  N N 439 
THR   HG1    H  N N 440 
THR   HG21   H  N N 441 
THR   HG22   H  N N 442 
THR   HG23   H  N N 443 
THR   HXT    H  N N 444 
TRP   N      N  N N 445 
TRP   CA     C  N S 446 
TRP   C      C  N N 447 
TRP   O      O  N N 448 
TRP   CB     C  N N 449 
TRP   CG     C  Y N 450 
TRP   CD1    C  Y N 451 
TRP   CD2    C  Y N 452 
TRP   NE1    N  Y N 453 
TRP   CE2    C  Y N 454 
TRP   CE3    C  Y N 455 
TRP   CZ2    C  Y N 456 
TRP   CZ3    C  Y N 457 
TRP   CH2    C  Y N 458 
TRP   OXT    O  N N 459 
TRP   H      H  N N 460 
TRP   H2     H  N N 461 
TRP   HA     H  N N 462 
TRP   HB2    H  N N 463 
TRP   HB3    H  N N 464 
TRP   HD1    H  N N 465 
TRP   HE1    H  N N 466 
TRP   HE3    H  N N 467 
TRP   HZ2    H  N N 468 
TRP   HZ3    H  N N 469 
TRP   HH2    H  N N 470 
TRP   HXT    H  N N 471 
TYR   N      N  N N 472 
TYR   CA     C  N S 473 
TYR   C      C  N N 474 
TYR   O      O  N N 475 
TYR   CB     C  N N 476 
TYR   CG     C  Y N 477 
TYR   CD1    C  Y N 478 
TYR   CD2    C  Y N 479 
TYR   CE1    C  Y N 480 
TYR   CE2    C  Y N 481 
TYR   CZ     C  Y N 482 
TYR   OH     O  N N 483 
TYR   OXT    O  N N 484 
TYR   H      H  N N 485 
TYR   H2     H  N N 486 
TYR   HA     H  N N 487 
TYR   HB2    H  N N 488 
TYR   HB3    H  N N 489 
TYR   HD1    H  N N 490 
TYR   HD2    H  N N 491 
TYR   HE1    H  N N 492 
TYR   HE2    H  N N 493 
TYR   HH     H  N N 494 
TYR   HXT    H  N N 495 
VAL   N      N  N N 496 
VAL   CA     C  N S 497 
VAL   C      C  N N 498 
VAL   O      O  N N 499 
VAL   CB     C  N N 500 
VAL   CG1    C  N N 501 
VAL   CG2    C  N N 502 
VAL   OXT    O  N N 503 
VAL   H      H  N N 504 
VAL   H2     H  N N 505 
VAL   HA     H  N N 506 
VAL   HB     H  N N 507 
VAL   HG11   H  N N 508 
VAL   HG12   H  N N 509 
VAL   HG13   H  N N 510 
VAL   HG21   H  N N 511 
VAL   HG22   H  N N 512 
VAL   HG23   H  N N 513 
VAL   HXT    H  N N 514 
ZN    ZN     ZN N N 515 
# 
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 
A1L58 C37   C36    doub Y N 1   
A1L58 C37   N38    sing Y N 2   
A1L58 C36   C03    sing Y N 3   
A1L58 N38   C01    doub Y N 4   
A1L58 C03   N04    sing N N 5   
A1L58 C03   C02    doub Y N 6   
A1L58 C01   C02    sing Y N 7   
A1L58 N04   C05    sing N N 8   
A1L58 C15   C14    sing N N 9   
A1L58 C35   C05    doub Y N 10  
A1L58 C35   C34    sing Y N 11  
A1L58 C05   C06    sing Y N 12  
A1L58 C14   C13    sing N N 13  
A1L58 C34   C33    doub Y N 14  
A1L58 C06   C07    doub Y N 15  
A1L58 C13   C12    sing N N 16  
A1L58 C33   C07    sing Y N 17  
A1L58 C12   C11    sing N N 18  
A1L58 C07   C08    sing N N 19  
A1L58 O17   C16    doub N N 20  
A1L58 N10   C08    sing N N 21  
A1L58 N10   C11    sing N N 22  
A1L58 C08   O09    doub N N 23  
A1L58 C11   C16    sing N N 24  
A1L58 C16   N18    sing N N 25  
A1L58 C32   N31    doub Y N 26  
A1L58 C32   C19    sing Y N 27  
A1L58 N31   C22    sing Y N 28  
A1L58 N18   C19    sing N N 29  
A1L58 C19   C20    doub Y N 30  
A1L58 C22   O23    sing N N 31  
A1L58 C22   C21    doub Y N 32  
A1L58 O23   C24    sing N N 33  
A1L58 C24   C30    sing N N 34  
A1L58 C24   C25    sing N N 35  
A1L58 C30   C29    sing N N 36  
A1L58 C20   C21    sing Y N 37  
A1L58 C25   C26    sing N N 38  
A1L58 C29   N27    sing N N 39  
A1L58 C26   N27    sing N N 40  
A1L58 N27   C28    sing N N 41  
A1L58 C11   H1     sing N N 42  
A1L58 C12   H2     sing N N 43  
A1L58 C12   H3     sing N N 44  
A1L58 C13   H4     sing N N 45  
A1L58 C13   H5     sing N N 46  
A1L58 C14   H6     sing N N 47  
A1L58 C14   H7     sing N N 48  
A1L58 C21   H8     sing N N 49  
A1L58 C29   H9     sing N N 50  
A1L58 C30   H10    sing N N 51  
A1L58 C33   H11    sing N N 52  
A1L58 C34   H12    sing N N 53  
A1L58 C01   H13    sing N N 54  
A1L58 C02   H14    sing N N 55  
A1L58 C06   H15    sing N N 56  
A1L58 C15   H16    sing N N 57  
A1L58 C15   H17    sing N N 58  
A1L58 C15   H18    sing N N 59  
A1L58 C20   H19    sing N N 60  
A1L58 C24   H20    sing N N 61  
A1L58 C25   H21    sing N N 62  
A1L58 C25   H22    sing N N 63  
A1L58 C26   H23    sing N N 64  
A1L58 C26   H24    sing N N 65  
A1L58 C28   H25    sing N N 66  
A1L58 C28   H26    sing N N 67  
A1L58 C28   H27    sing N N 68  
A1L58 C32   H28    sing N N 69  
A1L58 C35   H29    sing N N 70  
A1L58 C36   H30    sing N N 71  
A1L58 C37   H31    sing N N 72  
A1L58 N04   H32    sing N N 73  
A1L58 N10   H33    sing N N 74  
A1L58 N18   H34    sing N N 75  
A1L58 C29   H35    sing N N 76  
A1L58 C30   H36    sing N N 77  
ALA   N     CA     sing N N 78  
ALA   N     H      sing N N 79  
ALA   N     H2     sing N N 80  
ALA   CA    C      sing N N 81  
ALA   CA    CB     sing N N 82  
ALA   CA    HA     sing N N 83  
ALA   C     O      doub N N 84  
ALA   C     OXT    sing N N 85  
ALA   CB    HB1    sing N N 86  
ALA   CB    HB2    sing N N 87  
ALA   CB    HB3    sing N N 88  
ALA   OXT   HXT    sing N N 89  
ARG   N     CA     sing N N 90  
ARG   N     H      sing N N 91  
ARG   N     H2     sing N N 92  
ARG   CA    C      sing N N 93  
ARG   CA    CB     sing N N 94  
ARG   CA    HA     sing N N 95  
ARG   C     O      doub N N 96  
ARG   C     OXT    sing N N 97  
ARG   CB    CG     sing N N 98  
ARG   CB    HB2    sing N N 99  
ARG   CB    HB3    sing N N 100 
ARG   CG    CD     sing N N 101 
ARG   CG    HG2    sing N N 102 
ARG   CG    HG3    sing N N 103 
ARG   CD    NE     sing N N 104 
ARG   CD    HD2    sing N N 105 
ARG   CD    HD3    sing N N 106 
ARG   NE    CZ     sing N N 107 
ARG   NE    HE     sing N N 108 
ARG   CZ    NH1    sing N N 109 
ARG   CZ    NH2    doub N N 110 
ARG   NH1   HH11   sing N N 111 
ARG   NH1   HH12   sing N N 112 
ARG   NH2   HH21   sing N N 113 
ARG   NH2   HH22   sing N N 114 
ARG   OXT   HXT    sing N N 115 
ASN   N     CA     sing N N 116 
ASN   N     H      sing N N 117 
ASN   N     H2     sing N N 118 
ASN   CA    C      sing N N 119 
ASN   CA    CB     sing N N 120 
ASN   CA    HA     sing N N 121 
ASN   C     O      doub N N 122 
ASN   C     OXT    sing N N 123 
ASN   CB    CG     sing N N 124 
ASN   CB    HB2    sing N N 125 
ASN   CB    HB3    sing N N 126 
ASN   CG    OD1    doub N N 127 
ASN   CG    ND2    sing N N 128 
ASN   ND2   HD21   sing N N 129 
ASN   ND2   HD22   sing N N 130 
ASN   OXT   HXT    sing N N 131 
ASP   N     CA     sing N N 132 
ASP   N     H      sing N N 133 
ASP   N     H2     sing N N 134 
ASP   CA    C      sing N N 135 
ASP   CA    CB     sing N N 136 
ASP   CA    HA     sing N N 137 
ASP   C     O      doub N N 138 
ASP   C     OXT    sing N N 139 
ASP   CB    CG     sing N N 140 
ASP   CB    HB2    sing N N 141 
ASP   CB    HB3    sing N N 142 
ASP   CG    OD1    doub N N 143 
ASP   CG    OD2    sing N N 144 
ASP   OD2   HD2    sing N N 145 
ASP   OXT   HXT    sing N N 146 
CYS   N     CA     sing N N 147 
CYS   N     H      sing N N 148 
CYS   N     H2     sing N N 149 
CYS   CA    C      sing N N 150 
CYS   CA    CB     sing N N 151 
CYS   CA    HA     sing N N 152 
CYS   C     O      doub N N 153 
CYS   C     OXT    sing N N 154 
CYS   CB    SG     sing N N 155 
CYS   CB    HB2    sing N N 156 
CYS   CB    HB3    sing N N 157 
CYS   SG    HG     sing N N 158 
CYS   OXT   HXT    sing N N 159 
GLN   N     CA     sing N N 160 
GLN   N     H      sing N N 161 
GLN   N     H2     sing N N 162 
GLN   CA    C      sing N N 163 
GLN   CA    CB     sing N N 164 
GLN   CA    HA     sing N N 165 
GLN   C     O      doub N N 166 
GLN   C     OXT    sing N N 167 
GLN   CB    CG     sing N N 168 
GLN   CB    HB2    sing N N 169 
GLN   CB    HB3    sing N N 170 
GLN   CG    CD     sing N N 171 
GLN   CG    HG2    sing N N 172 
GLN   CG    HG3    sing N N 173 
GLN   CD    OE1    doub N N 174 
GLN   CD    NE2    sing N N 175 
GLN   NE2   HE21   sing N N 176 
GLN   NE2   HE22   sing N N 177 
GLN   OXT   HXT    sing N N 178 
GLU   N     CA     sing N N 179 
GLU   N     H      sing N N 180 
GLU   N     H2     sing N N 181 
GLU   CA    C      sing N N 182 
GLU   CA    CB     sing N N 183 
GLU   CA    HA     sing N N 184 
GLU   C     O      doub N N 185 
GLU   C     OXT    sing N N 186 
GLU   CB    CG     sing N N 187 
GLU   CB    HB2    sing N N 188 
GLU   CB    HB3    sing N N 189 
GLU   CG    CD     sing N N 190 
GLU   CG    HG2    sing N N 191 
GLU   CG    HG3    sing N N 192 
GLU   CD    OE1    doub N N 193 
GLU   CD    OE2    sing N N 194 
GLU   OE2   HE2    sing N N 195 
GLU   OXT   HXT    sing N N 196 
GLY   N     CA     sing N N 197 
GLY   N     H      sing N N 198 
GLY   N     H2     sing N N 199 
GLY   CA    C      sing N N 200 
GLY   CA    HA2    sing N N 201 
GLY   CA    HA3    sing N N 202 
GLY   C     O      doub N N 203 
GLY   C     OXT    sing N N 204 
GLY   OXT   HXT    sing N N 205 
HIS   N     CA     sing N N 206 
HIS   N     H      sing N N 207 
HIS   N     H2     sing N N 208 
HIS   CA    C      sing N N 209 
HIS   CA    CB     sing N N 210 
HIS   CA    HA     sing N N 211 
HIS   C     O      doub N N 212 
HIS   C     OXT    sing N N 213 
HIS   CB    CG     sing N N 214 
HIS   CB    HB2    sing N N 215 
HIS   CB    HB3    sing N N 216 
HIS   CG    ND1    sing Y N 217 
HIS   CG    CD2    doub Y N 218 
HIS   ND1   CE1    doub Y N 219 
HIS   ND1   HD1    sing N N 220 
HIS   CD2   NE2    sing Y N 221 
HIS   CD2   HD2    sing N N 222 
HIS   CE1   NE2    sing Y N 223 
HIS   CE1   HE1    sing N N 224 
HIS   NE2   HE2    sing N N 225 
HIS   OXT   HXT    sing N N 226 
HOH   O     H1     sing N N 227 
HOH   O     H2     sing N N 228 
ILE   N     CA     sing N N 229 
ILE   N     H      sing N N 230 
ILE   N     H2     sing N N 231 
ILE   CA    C      sing N N 232 
ILE   CA    CB     sing N N 233 
ILE   CA    HA     sing N N 234 
ILE   C     O      doub N N 235 
ILE   C     OXT    sing N N 236 
ILE   CB    CG1    sing N N 237 
ILE   CB    CG2    sing N N 238 
ILE   CB    HB     sing N N 239 
ILE   CG1   CD1    sing N N 240 
ILE   CG1   HG12   sing N N 241 
ILE   CG1   HG13   sing N N 242 
ILE   CG2   HG21   sing N N 243 
ILE   CG2   HG22   sing N N 244 
ILE   CG2   HG23   sing N N 245 
ILE   CD1   HD11   sing N N 246 
ILE   CD1   HD12   sing N N 247 
ILE   CD1   HD13   sing N N 248 
ILE   OXT   HXT    sing N N 249 
LEU   N     CA     sing N N 250 
LEU   N     H      sing N N 251 
LEU   N     H2     sing N N 252 
LEU   CA    C      sing N N 253 
LEU   CA    CB     sing N N 254 
LEU   CA    HA     sing N N 255 
LEU   C     O      doub N N 256 
LEU   C     OXT    sing N N 257 
LEU   CB    CG     sing N N 258 
LEU   CB    HB2    sing N N 259 
LEU   CB    HB3    sing N N 260 
LEU   CG    CD1    sing N N 261 
LEU   CG    CD2    sing N N 262 
LEU   CG    HG     sing N N 263 
LEU   CD1   HD11   sing N N 264 
LEU   CD1   HD12   sing N N 265 
LEU   CD1   HD13   sing N N 266 
LEU   CD2   HD21   sing N N 267 
LEU   CD2   HD22   sing N N 268 
LEU   CD2   HD23   sing N N 269 
LEU   OXT   HXT    sing N N 270 
LYS   N     CA     sing N N 271 
LYS   N     H      sing N N 272 
LYS   N     H2     sing N N 273 
LYS   CA    C      sing N N 274 
LYS   CA    CB     sing N N 275 
LYS   CA    HA     sing N N 276 
LYS   C     O      doub N N 277 
LYS   C     OXT    sing N N 278 
LYS   CB    CG     sing N N 279 
LYS   CB    HB2    sing N N 280 
LYS   CB    HB3    sing N N 281 
LYS   CG    CD     sing N N 282 
LYS   CG    HG2    sing N N 283 
LYS   CG    HG3    sing N N 284 
LYS   CD    CE     sing N N 285 
LYS   CD    HD2    sing N N 286 
LYS   CD    HD3    sing N N 287 
LYS   CE    NZ     sing N N 288 
LYS   CE    HE2    sing N N 289 
LYS   CE    HE3    sing N N 290 
LYS   NZ    HZ1    sing N N 291 
LYS   NZ    HZ2    sing N N 292 
LYS   NZ    HZ3    sing N N 293 
LYS   OXT   HXT    sing N N 294 
MET   N     CA     sing N N 295 
MET   N     H      sing N N 296 
MET   N     H2     sing N N 297 
MET   CA    C      sing N N 298 
MET   CA    CB     sing N N 299 
MET   CA    HA     sing N N 300 
MET   C     O      doub N N 301 
MET   C     OXT    sing N N 302 
MET   CB    CG     sing N N 303 
MET   CB    HB2    sing N N 304 
MET   CB    HB3    sing N N 305 
MET   CG    SD     sing N N 306 
MET   CG    HG2    sing N N 307 
MET   CG    HG3    sing N N 308 
MET   SD    CE     sing N N 309 
MET   CE    HE1    sing N N 310 
MET   CE    HE2    sing N N 311 
MET   CE    HE3    sing N N 312 
MET   OXT   HXT    sing N N 313 
PHE   N     CA     sing N N 314 
PHE   N     H      sing N N 315 
PHE   N     H2     sing N N 316 
PHE   CA    C      sing N N 317 
PHE   CA    CB     sing N N 318 
PHE   CA    HA     sing N N 319 
PHE   C     O      doub N N 320 
PHE   C     OXT    sing N N 321 
PHE   CB    CG     sing N N 322 
PHE   CB    HB2    sing N N 323 
PHE   CB    HB3    sing N N 324 
PHE   CG    CD1    doub Y N 325 
PHE   CG    CD2    sing Y N 326 
PHE   CD1   CE1    sing Y N 327 
PHE   CD1   HD1    sing N N 328 
PHE   CD2   CE2    doub Y N 329 
PHE   CD2   HD2    sing N N 330 
PHE   CE1   CZ     doub Y N 331 
PHE   CE1   HE1    sing N N 332 
PHE   CE2   CZ     sing Y N 333 
PHE   CE2   HE2    sing N N 334 
PHE   CZ    HZ     sing N N 335 
PHE   OXT   HXT    sing N N 336 
PRO   N     CA     sing N N 337 
PRO   N     CD     sing N N 338 
PRO   N     H      sing N N 339 
PRO   CA    C      sing N N 340 
PRO   CA    CB     sing N N 341 
PRO   CA    HA     sing N N 342 
PRO   C     O      doub N N 343 
PRO   C     OXT    sing N N 344 
PRO   CB    CG     sing N N 345 
PRO   CB    HB2    sing N N 346 
PRO   CB    HB3    sing N N 347 
PRO   CG    CD     sing N N 348 
PRO   CG    HG2    sing N N 349 
PRO   CG    HG3    sing N N 350 
PRO   CD    HD2    sing N N 351 
PRO   CD    HD3    sing N N 352 
PRO   OXT   HXT    sing N N 353 
SER   N     CA     sing N N 354 
SER   N     H      sing N N 355 
SER   N     H2     sing N N 356 
SER   CA    C      sing N N 357 
SER   CA    CB     sing N N 358 
SER   CA    HA     sing N N 359 
SER   C     O      doub N N 360 
SER   C     OXT    sing N N 361 
SER   CB    OG     sing N N 362 
SER   CB    HB2    sing N N 363 
SER   CB    HB3    sing N N 364 
SER   OG    HG     sing N N 365 
SER   OXT   HXT    sing N N 366 
SFG   N     CA     sing N N 367 
SFG   N     HN1    sing N N 368 
SFG   N     HN2    sing N N 369 
SFG   CA    C      sing N N 370 
SFG   CA    CB     sing N N 371 
SFG   CA    HA     sing N N 372 
SFG   C     O      doub N N 373 
SFG   C     OXT    sing N N 374 
SFG   OXT   HXT    sing N N 375 
SFG   CB    CG     sing N N 376 
SFG   CB    HB1    sing N N 377 
SFG   CB    HB2    sing N N 378 
SFG   CG    CD     sing N N 379 
SFG   CG    HG1    sing N N 380 
SFG   CG    HG2    sing N N 381 
SFG   CD    NE     sing N N 382 
SFG   CD    "C5'"  sing N N 383 
SFG   CD    HD     sing N N 384 
SFG   NE    HNE1   sing N N 385 
SFG   NE    HNE2   sing N N 386 
SFG   "C5'" "C4'"  sing N N 387 
SFG   "C5'" "H5'1" sing N N 388 
SFG   "C5'" "H5'2" sing N N 389 
SFG   "C4'" "O4'"  sing N N 390 
SFG   "C4'" "C3'"  sing N N 391 
SFG   "C4'" "H4'"  sing N N 392 
SFG   "O4'" "C1'"  sing N N 393 
SFG   "C3'" "O3'"  sing N N 394 
SFG   "C3'" "C2'"  sing N N 395 
SFG   "C3'" "H3'"  sing N N 396 
SFG   "O3'" "HO3'" sing N N 397 
SFG   "C2'" "O2'"  sing N N 398 
SFG   "C2'" "C1'"  sing N N 399 
SFG   "C2'" "H2'"  sing N N 400 
SFG   "O2'" "HO2'" sing N N 401 
SFG   "C1'" N9     sing N N 402 
SFG   "C1'" "H1'"  sing N N 403 
SFG   N9    C8     sing Y N 404 
SFG   N9    C4     sing Y N 405 
SFG   C8    N7     doub Y N 406 
SFG   C8    H8     sing N N 407 
SFG   N7    C5     sing Y N 408 
SFG   C5    C6     sing Y N 409 
SFG   C5    C4     doub Y N 410 
SFG   C6    N6     sing N N 411 
SFG   C6    N1     doub Y N 412 
SFG   N6    HN61   sing N N 413 
SFG   N6    HN62   sing N N 414 
SFG   N1    C2     sing Y N 415 
SFG   C2    N3     doub Y N 416 
SFG   C2    H2     sing N N 417 
SFG   N3    C4     sing Y N 418 
THR   N     CA     sing N N 419 
THR   N     H      sing N N 420 
THR   N     H2     sing N N 421 
THR   CA    C      sing N N 422 
THR   CA    CB     sing N N 423 
THR   CA    HA     sing N N 424 
THR   C     O      doub N N 425 
THR   C     OXT    sing N N 426 
THR   CB    OG1    sing N N 427 
THR   CB    CG2    sing N N 428 
THR   CB    HB     sing N N 429 
THR   OG1   HG1    sing N N 430 
THR   CG2   HG21   sing N N 431 
THR   CG2   HG22   sing N N 432 
THR   CG2   HG23   sing N N 433 
THR   OXT   HXT    sing N N 434 
TRP   N     CA     sing N N 435 
TRP   N     H      sing N N 436 
TRP   N     H2     sing N N 437 
TRP   CA    C      sing N N 438 
TRP   CA    CB     sing N N 439 
TRP   CA    HA     sing N N 440 
TRP   C     O      doub N N 441 
TRP   C     OXT    sing N N 442 
TRP   CB    CG     sing N N 443 
TRP   CB    HB2    sing N N 444 
TRP   CB    HB3    sing N N 445 
TRP   CG    CD1    doub Y N 446 
TRP   CG    CD2    sing Y N 447 
TRP   CD1   NE1    sing Y N 448 
TRP   CD1   HD1    sing N N 449 
TRP   CD2   CE2    doub Y N 450 
TRP   CD2   CE3    sing Y N 451 
TRP   NE1   CE2    sing Y N 452 
TRP   NE1   HE1    sing N N 453 
TRP   CE2   CZ2    sing Y N 454 
TRP   CE3   CZ3    doub Y N 455 
TRP   CE3   HE3    sing N N 456 
TRP   CZ2   CH2    doub Y N 457 
TRP   CZ2   HZ2    sing N N 458 
TRP   CZ3   CH2    sing Y N 459 
TRP   CZ3   HZ3    sing N N 460 
TRP   CH2   HH2    sing N N 461 
TRP   OXT   HXT    sing N N 462 
TYR   N     CA     sing N N 463 
TYR   N     H      sing N N 464 
TYR   N     H2     sing N N 465 
TYR   CA    C      sing N N 466 
TYR   CA    CB     sing N N 467 
TYR   CA    HA     sing N N 468 
TYR   C     O      doub N N 469 
TYR   C     OXT    sing N N 470 
TYR   CB    CG     sing N N 471 
TYR   CB    HB2    sing N N 472 
TYR   CB    HB3    sing N N 473 
TYR   CG    CD1    doub Y N 474 
TYR   CG    CD2    sing Y N 475 
TYR   CD1   CE1    sing Y N 476 
TYR   CD1   HD1    sing N N 477 
TYR   CD2   CE2    doub Y N 478 
TYR   CD2   HD2    sing N N 479 
TYR   CE1   CZ     doub Y N 480 
TYR   CE1   HE1    sing N N 481 
TYR   CE2   CZ     sing Y N 482 
TYR   CE2   HE2    sing N N 483 
TYR   CZ    OH     sing N N 484 
TYR   OH    HH     sing N N 485 
TYR   OXT   HXT    sing N N 486 
VAL   N     CA     sing N N 487 
VAL   N     H      sing N N 488 
VAL   N     H2     sing N N 489 
VAL   CA    C      sing N N 490 
VAL   CA    CB     sing N N 491 
VAL   CA    HA     sing N N 492 
VAL   C     O      doub N N 493 
VAL   C     OXT    sing N N 494 
VAL   CB    CG1    sing N N 495 
VAL   CB    CG2    sing N N 496 
VAL   CB    HB     sing N N 497 
VAL   CG1   HG11   sing N N 498 
VAL   CG1   HG12   sing N N 499 
VAL   CG1   HG13   sing N N 500 
VAL   CG2   HG21   sing N N 501 
VAL   CG2   HG22   sing N N 502 
VAL   CG2   HG23   sing N N 503 
VAL   OXT   HXT    sing N N 504 
# 
_pdbx_audit_support.funding_organization   'Japan Society for the Promotion of Science (JSPS)' 
_pdbx_audit_support.country                Japan 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   7XUA 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9KLC 
_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]   0.017632 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000400 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012810 
_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]   0.014171 
_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  
ZN 
# 
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     . THR   A 1 8   ? -25.517 -15.219 116.501 1.00 53.18  ? 918  THR   A N     1 
ATOM   2    C  CA    . THR   A 1 8   ? -24.834 -15.824 115.358 1.00 51.78  ? 918  THR   A CA    1 
ATOM   3    C  C     . THR   A 1 8   ? -23.894 -14.851 114.639 1.00 50.84  ? 918  THR   A C     1 
ATOM   4    O  O     . THR   A 1 8   ? -24.327 -13.814 114.137 1.00 49.56  ? 918  THR   A O     1 
ATOM   5    C  CB    . THR   A 1 8   ? -25.828 -16.350 114.321 1.00 55.25  ? 918  THR   A CB    1 
ATOM   6    O  OG1   . THR   A 1 8   ? -26.045 -15.340 113.322 1.00 60.59  ? 918  THR   A OG1   1 
ATOM   7    C  CG2   . THR   A 1 8   ? -27.155 -16.698 114.989 1.00 56.00  ? 918  THR   A CG2   1 
ATOM   8    N  N     . GLU   A 1 9   ? -22.613 -15.215 114.570 1.00 49.56  ? 919  GLU   A N     1 
ATOM   9    C  CA    . GLU   A 1 9   ? -21.612 -14.378 113.930 1.00 48.08  ? 919  GLU   A CA    1 
ATOM   10   C  C     . GLU   A 1 9   ? -21.619 -14.612 112.427 1.00 47.82  ? 919  GLU   A C     1 
ATOM   11   O  O     . GLU   A 1 9   ? -21.650 -15.755 111.964 1.00 48.62  ? 919  GLU   A O     1 
ATOM   12   C  CB    . GLU   A 1 9   ? -20.228 -14.671 114.500 1.00 47.64  ? 919  GLU   A CB    1 
ATOM   13   C  CG    . GLU   A 1 9   ? -19.305 -13.483 114.507 1.00 46.21  ? 919  GLU   A CG    1 
ATOM   14   C  CD    . GLU   A 1 9   ? -17.846 -13.899 114.578 1.00 45.72  ? 919  GLU   A CD    1 
ATOM   15   O  OE1   . GLU   A 1 9   ? -17.302 -14.344 113.550 1.00 45.41  ? 919  GLU   A OE1   1 
ATOM   16   O  OE2   . GLU   A 1 9   ? -17.262 -13.797 115.666 1.00 45.75  ? 919  GLU   A OE2   1 
ATOM   17   N  N     . LYS   A 1 10  ? -21.615 -13.526 111.668 1.00 46.83  ? 920  LYS   A N     1 
ATOM   18   C  CA    . LYS   A 1 10  ? -21.520 -13.575 110.220 1.00 46.49  ? 920  LYS   A CA    1 
ATOM   19   C  C     . LYS   A 1 10  ? -20.311 -12.758 109.794 1.00 45.05  ? 920  LYS   A C     1 
ATOM   20   O  O     . LYS   A 1 10  ? -19.869 -11.869 110.516 1.00 44.32  ? 920  LYS   A O     1 
ATOM   21   C  CB    . LYS   A 1 10  ? -22.797 -13.035 109.559 1.00 46.87  ? 920  LYS   A CB    1 
ATOM   22   C  CG    . LYS   A 1 10  ? -24.046 -13.893 109.856 1.00 50.10  ? 920  LYS   A CG    1 
ATOM   23   C  CD    . LYS   A 1 10  ? -25.304 -13.315 109.220 1.00 52.92  ? 920  LYS   A CD    1 
ATOM   24   C  CE    . LYS   A 1 10  ? -26.532 -14.140 109.573 1.00 54.22  ? 920  LYS   A CE    1 
ATOM   25   N  NZ    . LYS   A 1 10  ? -27.771 -13.530 109.001 1.00 59.98  ? 920  LYS   A NZ    1 
ATOM   26   N  N     . ILE   A 1 11  ? -19.788 -13.052 108.611 1.00 44.73  ? 921  ILE   A N     1 
ATOM   27   C  CA    . ILE   A 1 11  ? -18.703 -12.272 108.031 1.00 43.42  ? 921  ILE   A CA    1 
ATOM   28   C  C     . ILE   A 1 11  ? -19.278 -11.439 106.900 1.00 43.11  ? 921  ILE   A C     1 
ATOM   29   O  O     . ILE   A 1 11  ? -19.856 -11.975 105.948 1.00 43.78  ? 921  ILE   A O     1 
ATOM   30   C  CB    . ILE   A 1 11  ? -17.547 -13.159 107.546 1.00 43.30  ? 921  ILE   A CB    1 
ATOM   31   C  CG1   . ILE   A 1 11  ? -16.962 -13.940 108.726 1.00 43.73  ? 921  ILE   A CG1   1 
ATOM   32   C  CG2   . ILE   A 1 11  ? -16.486 -12.306 106.865 1.00 41.98  ? 921  ILE   A CG2   1 
ATOM   33   C  CD1   . ILE   A 1 11  ? -15.815 -14.892 108.359 1.00 43.84  ? 921  ILE   A CD1   1 
ATOM   34   N  N     . ILE   A 1 12  ? -19.095 -10.125 106.993 1.00 42.20  ? 922  ILE   A N     1 
ATOM   35   C  CA    . ILE   A 1 12  ? -19.744 -9.192  106.085 1.00 46.41  ? 922  ILE   A CA    1 
ATOM   36   C  C     . ILE   A 1 12  ? -18.757 -8.489  105.190 1.00 40.96  ? 922  ILE   A C     1 
ATOM   37   O  O     . ILE   A 1 12  ? -19.160 -7.687  104.336 1.00 40.84  ? 922  ILE   A O     1 
ATOM   38   C  CB    . ILE   A 1 12  ? -20.602 -8.172  106.857 1.00 43.80  ? 922  ILE   A CB    1 
ATOM   39   C  CG1   . ILE   A 1 12  ? -19.728 -7.394  107.841 1.00 41.41  ? 922  ILE   A CG1   1 
ATOM   40   C  CG2   . ILE   A 1 12  ? -21.736 -8.886  107.578 1.00 43.45  ? 922  ILE   A CG2   1 
ATOM   41   C  CD1   . ILE   A 1 12  ? -20.514 -6.524  108.810 1.00 45.44  ? 922  ILE   A CD1   1 
ATOM   42   N  N     . CYS   A 1 13  ? -17.471 -8.756  105.359 1.00 45.79  ? 923  CYS   A N     1 
ATOM   43   C  CA    . CYS   A 1 13  ? -16.466 -8.269  104.433 1.00 39.67  ? 923  CYS   A CA    1 
ATOM   44   C  C     . CYS   A 1 13  ? -15.231 -9.125  104.634 1.00 39.03  ? 923  CYS   A C     1 
ATOM   45   O  O     . CYS   A 1 13  ? -14.866 -9.420  105.774 1.00 39.06  ? 923  CYS   A O     1 
ATOM   46   C  CB    . CYS   A 1 13  ? -16.165 -6.786  104.662 1.00 38.41  ? 923  CYS   A CB    1 
ATOM   47   S  SG    . CYS   A 1 13  ? -14.953 -6.095  103.499 1.00 39.37  ? 923  CYS   A SG    1 
ATOM   48   N  N     . ARG   A 1 14  ? -14.611 -9.543  103.533 1.00 39.72  ? 924  ARG   A N     1 
ATOM   49   C  CA    . ARG   A 1 14  ? -13.400 -10.339 103.662 1.00 38.73  ? 924  ARG   A CA    1 
ATOM   50   C  C     . ARG   A 1 14  ? -12.186 -9.462  103.978 1.00 37.52  ? 924  ARG   A C     1 
ATOM   51   O  O     . ARG   A 1 14  ? -11.316 -9.880  104.742 1.00 37.38  ? 924  ARG   A O     1 
ATOM   52   C  CB    . ARG   A 1 14  ? -13.141 -11.151 102.393 1.00 41.00  ? 924  ARG   A CB    1 
ATOM   53   C  CG    . ARG   A 1 14  ? -14.348 -11.724 101.719 1.00 47.42  ? 924  ARG   A CG    1 
ATOM   54   C  CD    . ARG   A 1 14  ? -13.937 -12.737 100.654 1.00 51.76  ? 924  ARG   A CD    1 
ATOM   55   N  NE    . ARG   A 1 14  ? -12.698 -12.345 99.994  1.00 52.01  ? 924  ARG   A NE    1 
ATOM   56   C  CZ    . ARG   A 1 14  ? -12.614 -11.407 99.060  1.00 53.20  ? 924  ARG   A CZ    1 
ATOM   57   N  NH1   . ARG   A 1 14  ? -13.686 -10.735 98.657  1.00 48.82  ? 924  ARG   A NH1   1 
ATOM   58   N  NH2   . ARG   A 1 14  ? -11.425 -11.132 98.521  1.00 49.65  ? 924  ARG   A NH2   1 
ATOM   59   N  N     . ASP   A 1 15  ? -12.115 -8.249  103.414 1.00 36.73  ? 925  ASP   A N     1 
ATOM   60   C  CA    . ASP   A 1 15  ? -10.990 -7.343  103.672 1.00 35.64  ? 925  ASP   A CA    1 
ATOM   61   C  C     . ASP   A 1 15  ? -11.465 -5.898  103.522 1.00 35.16  ? 925  ASP   A C     1 
ATOM   62   O  O     . ASP   A 1 15  ? -11.562 -5.395  102.402 1.00 34.97  ? 925  ASP   A O     1 
ATOM   63   C  CB    . ASP   A 1 15  ? -9.831  -7.638  102.727 1.00 35.20  ? 925  ASP   A CB    1 
ATOM   64   C  CG    . ASP   A 1 15  ? -8.598  -6.792  103.025 1.00 34.14  ? 925  ASP   A CG    1 
ATOM   65   O  OD1   . ASP   A 1 15  ? -8.501  -6.240  104.145 1.00 33.85  ? 925  ASP   A OD1   1 
ATOM   66   O  OD2   . ASP   A 1 15  ? -7.734  -6.678  102.133 1.00 33.67  ? 925  ASP   A OD2   1 
ATOM   67   N  N     . VAL   A 1 16  ? -11.701 -5.218  104.646 1.00 35.04  ? 926  VAL   A N     1 
ATOM   68   C  CA    . VAL   A 1 16  ? -12.143 -3.831  104.561 1.00 34.75  ? 926  VAL   A CA    1 
ATOM   69   C  C     . VAL   A 1 16  ? -11.131 -2.948  103.853 1.00 33.83  ? 926  VAL   A C     1 
ATOM   70   O  O     . VAL   A 1 16  ? -11.493 -1.886  103.341 1.00 33.71  ? 926  VAL   A O     1 
ATOM   71   C  CB    . VAL   A 1 16  ? -12.461 -3.249  105.954 1.00 36.94  ? 926  VAL   A CB    1 
ATOM   72   C  CG1   . VAL   A 1 16  ? -13.717 -3.907  106.542 1.00 35.92  ? 926  VAL   A CG1   1 
ATOM   73   C  CG2   . VAL   A 1 16  ? -11.264 -3.386  106.889 1.00 34.37  ? 926  VAL   A CG2   1 
ATOM   74   N  N     . ALA   A 1 17  ? -9.866  -3.363  103.803 1.00 34.33  ? 927  ALA   A N     1 
ATOM   75   C  CA    . ALA   A 1 17  ? -8.811  -2.596  103.164 1.00 32.41  ? 927  ALA   A CA    1 
ATOM   76   C  C     . ALA   A 1 17  ? -8.667  -2.908  101.683 1.00 32.42  ? 927  ALA   A C     1 
ATOM   77   O  O     . ALA   A 1 17  ? -7.957  -2.190  100.982 1.00 31.82  ? 927  ALA   A O     1 
ATOM   78   C  CB    . ALA   A 1 17  ? -7.491  -2.830  103.894 1.00 31.86  ? 927  ALA   A CB    1 
ATOM   79   N  N     . ARG   A 1 18  ? -9.322  -3.953  101.191 1.00 33.17  ? 928  ARG   A N     1 
ATOM   80   C  CA    . ARG   A 1 18  ? -9.392  -4.243  99.755  1.00 35.18  ? 928  ARG   A CA    1 
ATOM   81   C  C     . ARG   A 1 18  ? -8.013  -4.583  99.195  1.00 32.93  ? 928  ARG   A C     1 
ATOM   82   O  O     . ARG   A 1 18  ? -7.636  -4.142  98.107  1.00 34.88  ? 928  ARG   A O     1 
ATOM   83   C  CB    . ARG   A 1 18  ? -10.032 -3.090  98.968  1.00 33.41  ? 928  ARG   A CB    1 
ATOM   84   C  CG    . ARG   A 1 18  ? -11.400 -2.621  99.499  1.00 34.01  ? 928  ARG   A CG    1 
ATOM   85   C  CD    . ARG   A 1 18  ? -12.022 -1.543  98.600  1.00 34.20  ? 928  ARG   A CD    1 
ATOM   86   N  NE    . ARG   A 1 18  ? -10.996 -0.721  97.963  1.00 33.93  ? 928  ARG   A NE    1 
ATOM   87   C  CZ    . ARG   A 1 18  ? -10.559 0.451   98.415  1.00 36.41  ? 928  ARG   A CZ    1 
ATOM   88   N  NH1   . ARG   A 1 18  ? -11.110 1.043   99.466  1.00 35.71  ? 928  ARG   A NH1   1 
ATOM   89   N  NH2   . ARG   A 1 18  ? -9.542  1.045   97.798  1.00 32.23  ? 928  ARG   A NH2   1 
ATOM   90   N  N     . GLY   A 1 19  ? -7.258  -5.387  99.938  1.00 34.82  ? 929  GLY   A N     1 
ATOM   91   C  CA    . GLY   A 1 19  ? -5.920  -5.749  99.544  1.00 33.39  ? 929  GLY   A CA    1 
ATOM   92   C  C     . GLY   A 1 19  ? -4.854  -4.685  99.726  1.00 36.04  ? 929  GLY   A C     1 
ATOM   93   O  O     . GLY   A 1 19  ? -3.699  -4.945  99.369  1.00 31.13  ? 929  GLY   A O     1 
ATOM   94   N  N     . TYR   A 1 20  ? -5.191  -3.493  100.268 1.00 34.34  ? 930  TYR   A N     1 
ATOM   95   C  CA    . TYR   A 1 20  ? -4.195  -2.428  100.411 1.00 30.13  ? 930  TYR   A CA    1 
ATOM   96   C  C     . TYR   A 1 20  ? -3.222  -2.626  101.572 1.00 31.25  ? 930  TYR   A C     1 
ATOM   97   O  O     . TYR   A 1 20  ? -2.206  -1.920  101.629 1.00 29.47  ? 930  TYR   A O     1 
ATOM   98   C  CB    . TYR   A 1 20  ? -4.877  -1.063  100.582 1.00 29.96  ? 930  TYR   A CB    1 
ATOM   99   C  CG    . TYR   A 1 20  ? -5.116  -0.344  99.279  1.00 29.93  ? 930  TYR   A CG    1 
ATOM   100  C  CD1   . TYR   A 1 20  ? -4.128  0.439   98.683  1.00 29.30  ? 930  TYR   A CD1   1 
ATOM   101  C  CD2   . TYR   A 1 20  ? -6.343  -0.454  98.631  1.00 31.84  ? 930  TYR   A CD2   1 
ATOM   102  C  CE1   . TYR   A 1 20  ? -4.367  1.094   97.471  1.00 29.39  ? 930  TYR   A CE1   1 
ATOM   103  C  CE2   . TYR   A 1 20  ? -6.594  0.194   97.444  1.00 30.74  ? 930  TYR   A CE2   1 
ATOM   104  C  CZ    . TYR   A 1 20  ? -5.621  0.964   96.863  1.00 32.41  ? 930  TYR   A CZ    1 
ATOM   105  O  OH    . TYR   A 1 20  ? -5.929  1.583   95.670  1.00 31.09  ? 930  TYR   A OH    1 
ATOM   106  N  N     . GLU   A 1 21  ? -3.504  -3.523  102.513 1.00 31.20  ? 931  GLU   A N     1 
ATOM   107  C  CA    . GLU   A 1 21  ? -2.568  -3.790  103.597 1.00 34.78  ? 931  GLU   A CA    1 
ATOM   108  C  C     . GLU   A 1 21  ? -1.827  -5.098  103.323 1.00 31.02  ? 931  GLU   A C     1 
ATOM   109  O  O     . GLU   A 1 21  ? -2.171  -5.846  102.406 1.00 32.66  ? 931  GLU   A O     1 
ATOM   110  C  CB    . GLU   A 1 21  ? -3.293  -3.836  104.951 1.00 30.59  ? 931  GLU   A CB    1 
ATOM   111  C  CG    . GLU   A 1 21  ? -4.196  -2.642  105.261 1.00 30.48  ? 931  GLU   A CG    1 
ATOM   112  C  CD    . GLU   A 1 21  ? -3.432  -1.359  105.598 1.00 30.20  ? 931  GLU   A CD    1 
ATOM   113  O  OE1   . GLU   A 1 21  ? -2.179  -1.354  105.533 1.00 31.70  ? 931  GLU   A OE1   1 
ATOM   114  O  OE2   . GLU   A 1 21  ? -4.082  -0.354  105.940 1.00 29.81  ? 931  GLU   A OE2   1 
ATOM   115  N  N     . ASN   A 1 22  ? -0.774  -5.362  104.115 1.00 32.18  ? 932  ASN   A N     1 
ATOM   116  C  CA    . ASN   A 1 22  ? -0.042  -6.625  103.987 1.00 30.98  ? 932  ASN   A CA    1 
ATOM   117  C  C     . ASN   A 1 22  ? -0.892  -7.844  104.314 1.00 33.00  ? 932  ASN   A C     1 
ATOM   118  O  O     . ASN   A 1 22  ? -0.505  -8.966  103.962 1.00 32.72  ? 932  ASN   A O     1 
ATOM   119  C  CB    . ASN   A 1 22  ? 1.169   -6.679  104.922 1.00 36.37  ? 932  ASN   A CB    1 
ATOM   120  C  CG    . ASN   A 1 22  ? 2.177   -5.611  104.648 1.00 30.03  ? 932  ASN   A CG    1 
ATOM   121  O  OD1   . ASN   A 1 22  ? 2.688   -5.002  105.576 1.00 35.97  ? 932  ASN   A OD1   1 
ATOM   122  N  ND2   . ASN   A 1 22  ? 2.480   -5.378  103.380 1.00 32.23  ? 932  ASN   A ND2   1 
ATOM   123  N  N     . VAL   A 1 23  ? -2.007  -7.654  105.017 1.00 34.60  ? 933  VAL   A N     1 
ATOM   124  C  CA    . VAL   A 1 23  ? -2.874  -8.750  105.447 1.00 33.51  ? 933  VAL   A CA    1 
ATOM   125  C  C     . VAL   A 1 23  ? -4.317  -8.306  105.360 1.00 33.51  ? 933  VAL   A C     1 
ATOM   126  O  O     . VAL   A 1 23  ? -4.641  -7.106  105.466 1.00 32.87  ? 933  VAL   A O     1 
ATOM   127  C  CB    . VAL   A 1 23  ? -2.560  -9.186  106.892 1.00 35.76  ? 933  VAL   A CB    1 
ATOM   128  C  CG1   . VAL   A 1 23  ? -1.257  -9.966  106.970 1.00 34.40  ? 933  VAL   A CG1   1 
ATOM   129  C  CG2   . VAL   A 1 23  ? -2.509  -7.959  107.803 1.00 37.00  ? 933  VAL   A CG2   1 
ATOM   130  N  N     . PRO   A 1 24  ? -5.235  -9.244  105.159 1.00 34.44  ? 934  PRO   A N     1 
ATOM   131  C  CA    . PRO   A 1 24  ? -6.657  -8.896  105.150 1.00 35.81  ? 934  PRO   A CA    1 
ATOM   132  C  C     . PRO   A 1 24  ? -7.155  -8.519  106.534 1.00 35.02  ? 934  PRO   A C     1 
ATOM   133  O  O     . PRO   A 1 24  ? -6.714  -9.067  107.551 1.00 35.21  ? 934  PRO   A O     1 
ATOM   134  C  CB    . PRO   A 1 24  ? -7.331  -10.173 104.660 1.00 36.42  ? 934  PRO   A CB    1 
ATOM   135  C  CG    . PRO   A 1 24  ? -6.370  -11.240 105.023 1.00 36.39  ? 934  PRO   A CG    1 
ATOM   136  C  CD    . PRO   A 1 24  ? -5.024  -10.657 104.807 1.00 35.38  ? 934  PRO   A CD    1 
ATOM   137  N  N     . ILE   A 1 25  ? -8.094  -7.574  106.551 1.00 34.66  ? 935  ILE   A N     1 
ATOM   138  C  CA    . ILE   A 1 25  ? -8.766  -7.124  107.768 1.00 34.91  ? 935  ILE   A CA    1 
ATOM   139  C  C     . ILE   A 1 25  ? -10.268 -7.369  107.618 1.00 35.71  ? 935  ILE   A C     1 
ATOM   140  O  O     . ILE   A 1 25  ? -11.000 -6.502  107.116 1.00 35.54  ? 935  ILE   A O     1 
ATOM   141  C  CB    . ILE   A 1 25  ? -8.436  -5.651  108.058 1.00 34.07  ? 935  ILE   A CB    1 
ATOM   142  C  CG1   . ILE   A 1 25  ? -6.903  -5.485  108.200 1.00 33.35  ? 935  ILE   A CG1   1 
ATOM   143  C  CG2   . ILE   A 1 25  ? -9.099  -5.205  109.334 1.00 34.47  ? 935  ILE   A CG2   1 
ATOM   144  C  CD1   . ILE   A 1 25  ? -6.468  -4.071  108.483 1.00 32.60  ? 935  ILE   A CD1   1 
ATOM   145  N  N     . PRO   A 1 26  ? -10.766 -8.535  108.013 1.00 36.68  ? 936  PRO   A N     1 
ATOM   146  C  CA    . PRO   A 1 26  ? -12.172 -8.860  107.780 1.00 37.52  ? 936  PRO   A CA    1 
ATOM   147  C  C     . PRO   A 1 26  ? -13.067 -8.166  108.795 1.00 37.77  ? 936  PRO   A C     1 
ATOM   148  O  O     . PRO   A 1 26  ? -12.621 -7.656  109.822 1.00 38.72  ? 936  PRO   A O     1 
ATOM   149  C  CB    . PRO   A 1 26  ? -12.215 -10.382 107.953 1.00 40.21  ? 936  PRO   A CB    1 
ATOM   150  C  CG    . PRO   A 1 26  ? -11.138 -10.667 108.960 1.00 38.41  ? 936  PRO   A CG    1 
ATOM   151  C  CD    . PRO   A 1 26  ? -10.043 -9.642  108.674 1.00 38.25  ? 936  PRO   A CD    1 
ATOM   152  N  N     . CYS   A 1 27  ? -14.359 -8.164  108.486 1.00 42.23  ? 937  CYS   A N     1 
ATOM   153  C  CA    . CYS   A 1 27  ? -15.376 -7.596  109.360 1.00 38.89  ? 937  CYS   A CA    1 
ATOM   154  C  C     . CYS   A 1 27  ? -16.437 -8.646  109.660 1.00 40.12  ? 937  CYS   A C     1 
ATOM   155  O  O     . CYS   A 1 27  ? -17.012 -9.224  108.733 1.00 42.38  ? 937  CYS   A O     1 
ATOM   156  C  CB    . CYS   A 1 27  ? -16.016 -6.372  108.712 1.00 38.60  ? 937  CYS   A CB    1 
ATOM   157  S  SG    . CYS   A 1 27  ? -17.229 -5.578  109.777 1.00 41.84  ? 937  CYS   A SG    1 
ATOM   158  N  N     . VAL   A 1 28  ? -16.717 -8.869  110.949 1.00 40.71  ? 938  VAL   A N     1 
ATOM   159  C  CA    . VAL   A 1 28  ? -17.804 -9.746  111.372 1.00 41.95  ? 938  VAL   A CA    1 
ATOM   160  C  C     . VAL   A 1 28  ? -18.783 -8.980  112.258 1.00 42.40  ? 938  VAL   A C     1 
ATOM   161  O  O     . VAL   A 1 28  ? -18.436 -7.974  112.879 1.00 41.89  ? 938  VAL   A O     1 
ATOM   162  C  CB    . VAL   A 1 28  ? -17.302 -10.995 112.123 1.00 42.60  ? 938  VAL   A CB    1 
ATOM   163  C  CG1   . VAL   A 1 28  ? -16.016 -11.569 111.496 1.00 42.07  ? 938  VAL   A CG1   1 
ATOM   164  C  CG2   . VAL   A 1 28  ? -17.099 -10.668 113.586 1.00 44.93  ? 938  VAL   A CG2   1 
ATOM   165  N  N     . ASN   A 1 29  ? -20.020 -9.505  112.338 1.00 43.50  ? 939  ASN   A N     1 
ATOM   166  C  CA    . ASN   A 1 29  ? -21.040 -9.013  113.264 1.00 44.23  ? 939  ASN   A CA    1 
ATOM   167  C  C     . ASN   A 1 29  ? -21.873 -10.186 113.768 1.00 45.55  ? 939  ASN   A C     1 
ATOM   168  O  O     . ASN   A 1 29  ? -22.547 -10.862 112.979 1.00 46.14  ? 939  ASN   A O     1 
ATOM   169  C  CB    . ASN   A 1 29  ? -21.942 -7.967  112.590 1.00 44.19  ? 939  ASN   A CB    1 
ATOM   170  C  CG    . ASN   A 1 29  ? -22.954 -7.309  113.557 1.00 45.82  ? 939  ASN   A CG    1 
ATOM   171  O  OD1   . ASN   A 1 29  ? -23.320 -7.875  114.591 1.00 45.82  ? 939  ASN   A OD1   1 
ATOM   172  N  ND2   . ASN   A 1 29  ? -23.401 -6.102  113.207 1.00 44.82  ? 939  ASN   A ND2   1 
ATOM   173  N  N     . GLY   A 1 30  ? -21.830 -10.420 115.080 1.00 46.10  ? 940  GLY   A N     1 
ATOM   174  C  CA    . GLY   A 1 30  ? -22.753 -11.329 115.737 1.00 47.49  ? 940  GLY   A CA    1 
ATOM   175  C  C     . GLY   A 1 30  ? -23.546 -10.658 116.847 1.00 48.13  ? 940  GLY   A C     1 
ATOM   176  O  O     . GLY   A 1 30  ? -23.886 -11.306 117.844 1.00 49.16  ? 940  GLY   A O     1 
ATOM   177  N  N     . VAL   A 1 31  ? -23.849 -9.362  116.685 1.00 47.65  ? 941  VAL   A N     1 
ATOM   178  C  CA    . VAL   A 1 31  ? -24.471 -8.547  117.727 1.00 48.24  ? 941  VAL   A CA    1 
ATOM   179  C  C     . VAL   A 1 31  ? -25.858 -8.058  117.310 1.00 48.94  ? 941  VAL   A C     1 
ATOM   180  O  O     . VAL   A 1 31  ? -26.818 -8.186  118.068 1.00 51.05  ? 941  VAL   A O     1 
ATOM   181  C  CB    . VAL   A 1 31  ? -23.562 -7.360  118.123 1.00 47.31  ? 941  VAL   A CB    1 
ATOM   182  C  CG1   . VAL   A 1 31  ? -24.386 -6.252  118.797 1.00 52.92  ? 941  VAL   A CG1   1 
ATOM   183  C  CG2   . VAL   A 1 31  ? -22.479 -7.827  119.064 1.00 47.17  ? 941  VAL   A CG2   1 
ATOM   184  N  N     . ASP   A 1 32  ? -25.972 -7.480  116.118 1.00 48.33  ? 942  ASP   A N     1 
ATOM   185  C  CA    . ASP   A 1 32  ? -27.237 -6.942  115.600 1.00 51.47  ? 942  ASP   A CA    1 
ATOM   186  C  C     . ASP   A 1 32  ? -27.175 -6.978  114.071 1.00 51.03  ? 942  ASP   A C     1 
ATOM   187  O  O     . ASP   A 1 32  ? -26.326 -7.660  113.489 1.00 47.76  ? 942  ASP   A O     1 
ATOM   188  C  CB    . ASP   A 1 32  ? -27.497 -5.528  116.166 1.00 49.11  ? 942  ASP   A CB    1 
ATOM   189  C  CG    . ASP   A 1 32  ? -26.292 -4.593  116.006 1.00 52.97  ? 942  ASP   A CG    1 
ATOM   190  O  OD1   . ASP   A 1 32  ? -25.626 -4.647  114.947 1.00 46.86  ? 942  ASP   A OD1   1 
ATOM   191  O  OD2   . ASP   A 1 32  ? -26.037 -3.782  116.928 1.00 54.81  ? 942  ASP   A OD2   1 
ATOM   192  N  N     . GLY   A 1 33  ? -28.056 -6.221  113.415 1.00 49.35  ? 943  GLY   A N     1 
ATOM   193  C  CA    . GLY   A 1 33  ? -28.175 -6.223  111.969 1.00 49.39  ? 943  GLY   A CA    1 
ATOM   194  C  C     . GLY   A 1 33  ? -27.405 -5.144  111.232 1.00 47.42  ? 943  GLY   A C     1 
ATOM   195  O  O     . GLY   A 1 33  ? -27.634 -4.925  110.037 1.00 47.34  ? 943  GLY   A O     1 
ATOM   196  N  N     . GLU   A 1 34  ? -26.506 -4.457  111.892 1.00 46.64  ? 944  GLU   A N     1 
ATOM   197  C  CA    . GLU   A 1 34  ? -25.737 -3.421  111.205 1.00 45.62  ? 944  GLU   A CA    1 
ATOM   198  C  C     . GLU   A 1 34  ? -24.839 -4.051  110.144 1.00 45.58  ? 944  GLU   A C     1 
ATOM   199  O  O     . GLU   A 1 34  ? -24.020 -4.916  110.479 1.00 44.28  ? 944  GLU   A O     1 
ATOM   200  C  CB    . GLU   A 1 34  ? -24.919 -2.642  112.217 1.00 47.57  ? 944  GLU   A CB    1 
ATOM   201  C  CG    . GLU   A 1 34  ? -24.398 -1.327  111.697 1.00 50.04  ? 944  GLU   A CG    1 
ATOM   202  C  CD    . GLU   A 1 34  ? -25.509 -0.366  111.357 1.00 45.41  ? 944  GLU   A CD    1 
ATOM   203  O  OE1   . GLU   A 1 34  ? -26.604 -0.496  111.954 1.00 49.88  ? 944  GLU   A OE1   1 
ATOM   204  O  OE2   . GLU   A 1 34  ? -25.276 0.523   110.503 1.00 44.87  ? 944  GLU   A OE2   1 
ATOM   205  N  N     . PRO   A 1 35  ? -24.982 -3.693  108.872 1.00 48.59  ? 945  PRO   A N     1 
ATOM   206  C  CA    . PRO   A 1 35  ? -24.118 -4.247  107.825 1.00 43.77  ? 945  PRO   A CA    1 
ATOM   207  C  C     . PRO   A 1 35  ? -22.747 -3.599  107.894 1.00 42.49  ? 945  PRO   A C     1 
ATOM   208  O  O     . PRO   A 1 35  ? -22.506 -2.719  108.722 1.00 45.23  ? 945  PRO   A O     1 
ATOM   209  C  CB    . PRO   A 1 35  ? -24.838 -3.874  106.527 1.00 44.61  ? 945  PRO   A CB    1 
ATOM   210  C  CG    . PRO   A 1 35  ? -25.642 -2.669  106.880 1.00 46.36  ? 945  PRO   A CG    1 
ATOM   211  C  CD    . PRO   A 1 35  ? -26.019 -2.797  108.330 1.00 45.51  ? 945  PRO   A CD    1 
ATOM   212  N  N     . CYS   A 1 36  ? -21.874 -4.022  106.987 1.00 42.21  ? 946  CYS   A N     1 
ATOM   213  C  CA    . CYS   A 1 36  ? -20.513 -3.502  106.950 1.00 40.57  ? 946  CYS   A CA    1 
ATOM   214  C  C     . CYS   A 1 36  ? -20.534 -1.991  106.761 1.00 41.72  ? 946  CYS   A C     1 
ATOM   215  O  O     . CYS   A 1 36  ? -21.215 -1.485  105.851 1.00 40.69  ? 946  CYS   A O     1 
ATOM   216  C  CB    . CYS   A 1 36  ? -19.704 -4.155  105.841 1.00 40.17  ? 946  CYS   A CB    1 
ATOM   217  S  SG    . CYS   A 1 36  ? -17.926 -3.822  105.992 1.00 41.44  ? 946  CYS   A SG    1 
ATOM   218  N  N     . PRO   A 1 37  ? -19.846 -1.237  107.611 1.00 39.75  ? 947  PRO   A N     1 
ATOM   219  C  CA    . PRO   A 1 37  ? -19.859 0.224   107.473 1.00 41.06  ? 947  PRO   A CA    1 
ATOM   220  C  C     . PRO   A 1 37  ? -19.150 0.625   106.189 1.00 41.83  ? 947  PRO   A C     1 
ATOM   221  O  O     . PRO   A 1 37  ? -18.069 0.120   105.885 1.00 38.04  ? 947  PRO   A O     1 
ATOM   222  C  CB    . PRO   A 1 37  ? -19.110 0.712   108.722 1.00 39.24  ? 947  PRO   A CB    1 
ATOM   223  C  CG    . PRO   A 1 37  ? -18.306 -0.449  109.165 1.00 38.78  ? 947  PRO   A CG    1 
ATOM   224  C  CD    . PRO   A 1 37  ? -19.035 -1.688  108.750 1.00 39.38  ? 947  PRO   A CD    1 
ATOM   225  N  N     . GLU   A 1 38  ? -19.798 1.484   105.404 1.00 39.35  ? 948  GLU   A N     1 
ATOM   226  C  CA    . GLU   A 1 38  ? -19.237 1.932   104.138 1.00 38.82  ? 948  GLU   A CA    1 
ATOM   227  C  C     . GLU   A 1 38  ? -19.501 3.416   103.929 1.00 39.14  ? 948  GLU   A C     1 
ATOM   228  O  O     . GLU   A 1 38  ? -19.590 3.883   102.789 1.00 39.90  ? 948  GLU   A O     1 
ATOM   229  C  CB    . GLU   A 1 38  ? -19.770 1.101   102.962 1.00 41.22  ? 948  GLU   A CB    1 
ATOM   230  C  CG    . GLU   A 1 38  ? -19.366 -0.422  103.009 1.00 45.09  ? 948  GLU   A CG    1 
ATOM   231  C  CD    . GLU   A 1 38  ? -20.128 -1.320  102.011 1.00 50.83  ? 948  GLU   A CD    1 
ATOM   232  O  OE1   . GLU   A 1 38  ? -20.348 -0.900  100.852 1.00 50.75  ? 948  GLU   A OE1   1 
ATOM   233  O  OE2   . GLU   A 1 38  ? -20.506 -2.456  102.390 1.00 57.52  ? 948  GLU   A OE2   1 
ATOM   234  N  N     . ASP   A 1 39  ? -19.612 4.168   105.024 1.00 39.39  ? 949  ASP   A N     1 
ATOM   235  C  CA    . ASP   A 1 39  ? -19.799 5.617   105.002 1.00 40.45  ? 949  ASP   A CA    1 
ATOM   236  C  C     . ASP   A 1 39  ? -18.473 6.368   105.114 1.00 38.91  ? 949  ASP   A C     1 
ATOM   237  O  O     . ASP   A 1 39  ? -18.408 7.418   105.751 1.00 40.72  ? 949  ASP   A O     1 
ATOM   238  C  CB    . ASP   A 1 39  ? -20.752 6.017   106.126 1.00 43.29  ? 949  ASP   A CB    1 
ATOM   239  C  CG    . ASP   A 1 39  ? -21.277 7.433   105.983 1.00 44.42  ? 949  ASP   A CG    1 
ATOM   240  O  OD1   . ASP   A 1 39  ? -21.161 8.014   104.881 1.00 41.78  ? 949  ASP   A OD1   1 
ATOM   241  O  OD2   . ASP   A 1 39  ? -21.796 7.969   106.990 1.00 48.63  ? 949  ASP   A OD2   1 
ATOM   242  N  N     . TYR   A 1 40  ? -17.413 5.841   104.506 1.00 37.80  ? 950  TYR   A N     1 
ATOM   243  C  CA    . TYR   A 1 40  ? -16.053 6.381   104.543 1.00 36.81  ? 950  TYR   A CA    1 
ATOM   244  C  C     . TYR   A 1 40  ? -15.246 5.656   103.475 1.00 35.97  ? 950  TYR   A C     1 
ATOM   245  O  O     . TYR   A 1 40  ? -15.493 4.480   103.196 1.00 35.98  ? 950  TYR   A O     1 
ATOM   246  C  CB    . TYR   A 1 40  ? -15.383 6.179   105.916 1.00 36.39  ? 950  TYR   A CB    1 
ATOM   247  C  CG    . TYR   A 1 40  ? -14.837 4.765   106.099 1.00 35.76  ? 950  TYR   A CG    1 
ATOM   248  C  CD1   . TYR   A 1 40  ? -15.699 3.676   106.257 1.00 36.31  ? 950  TYR   A CD1   1 
ATOM   249  C  CD2   . TYR   A 1 40  ? -13.453 4.515   106.088 1.00 36.50  ? 950  TYR   A CD2   1 
ATOM   250  C  CE1   . TYR   A 1 40  ? -15.216 2.383   106.407 1.00 35.91  ? 950  TYR   A CE1   1 
ATOM   251  C  CE2   . TYR   A 1 40  ? -12.958 3.221   106.243 1.00 34.32  ? 950  TYR   A CE2   1 
ATOM   252  C  CZ    . TYR   A 1 40  ? -13.835 2.163   106.402 1.00 37.74  ? 950  TYR   A CZ    1 
ATOM   253  O  OH    . TYR   A 1 40  ? -13.334 0.883   106.555 1.00 41.99  ? 950  TYR   A OH    1 
ATOM   254  N  N     . LYS   A 1 41  ? -14.287 6.345   102.885 1.00 35.33  ? 951  LYS   A N     1 
ATOM   255  C  CA    . LYS   A 1 41  ? -13.334 5.664   102.013 1.00 38.45  ? 951  LYS   A CA    1 
ATOM   256  C  C     . LYS   A 1 41  ? -12.205 5.099   102.863 1.00 33.61  ? 951  LYS   A C     1 
ATOM   257  O  O     . LYS   A 1 41  ? -11.576 5.847   103.617 1.00 33.30  ? 951  LYS   A O     1 
ATOM   258  C  CB    . LYS   A 1 41  ? -12.779 6.617   100.959 1.00 34.24  ? 951  LYS   A CB    1 
ATOM   259  C  CG    . LYS   A 1 41  ? -11.905 5.949   99.908  1.00 33.54  ? 951  LYS   A CG    1 
ATOM   260  C  CD    . LYS   A 1 41  ? -12.671 4.914   99.073  1.00 34.06  ? 951  LYS   A CD    1 
ATOM   261  C  CE    . LYS   A 1 41  ? -11.790 4.420   97.921  1.00 34.59  ? 951  LYS   A CE    1 
ATOM   262  N  NZ    . LYS   A 1 41  ? -12.290 3.228   97.191  1.00 33.98  ? 951  LYS   A NZ    1 
ATOM   263  N  N     . TYR   A 1 42  ? -11.975 3.780   102.771 1.00 33.36  ? 952  TYR   A N     1 
ATOM   264  C  CA    . TYR   A 1 42  ? -10.763 3.194   103.351 1.00 32.58  ? 952  TYR   A CA    1 
ATOM   265  C  C     . TYR   A 1 42  ? -9.531  3.637   102.563 1.00 31.76  ? 952  TYR   A C     1 
ATOM   266  O  O     . TYR   A 1 42  ? -9.496  3.514   101.336 1.00 31.78  ? 952  TYR   A O     1 
ATOM   267  C  CB    . TYR   A 1 42  ? -10.825 1.657   103.379 1.00 32.69  ? 952  TYR   A CB    1 
ATOM   268  C  CG    . TYR   A 1 42  ? -9.748  1.072   104.274 1.00 38.83  ? 952  TYR   A CG    1 
ATOM   269  C  CD1   . TYR   A 1 42  ? -8.401  0.992   103.842 1.00 31.37  ? 952  TYR   A CD1   1 
ATOM   270  C  CD2   . TYR   A 1 42  ? -10.043 0.638   105.560 1.00 33.92  ? 952  TYR   A CD2   1 
ATOM   271  C  CE1   . TYR   A 1 42  ? -7.416  0.515   104.654 1.00 31.00  ? 952  TYR   A CE1   1 
ATOM   272  C  CE2   . TYR   A 1 42  ? -9.028  0.140   106.379 1.00 33.85  ? 952  TYR   A CE2   1 
ATOM   273  C  CZ    . TYR   A 1 42  ? -7.719  0.092   105.915 1.00 31.41  ? 952  TYR   A CZ    1 
ATOM   274  O  OH    . TYR   A 1 42  ? -6.715  -0.402  106.712 1.00 31.15  ? 952  TYR   A OH    1 
ATOM   275  N  N     . ILE   A 1 43  ? -8.503  4.125   103.266 1.00 31.17  ? 953  ILE   A N     1 
ATOM   276  C  CA    . ILE   A 1 43  ? -7.206  4.438   102.658 1.00 30.38  ? 953  ILE   A CA    1 
ATOM   277  C  C     . ILE   A 1 43  ? -6.083  3.850   103.514 1.00 29.82  ? 953  ILE   A C     1 
ATOM   278  O  O     . ILE   A 1 43  ? -6.093  3.987   104.742 1.00 29.96  ? 953  ILE   A O     1 
ATOM   279  C  CB    . ILE   A 1 43  ? -6.987  5.957   102.470 1.00 30.31  ? 953  ILE   A CB    1 
ATOM   280  C  CG1   . ILE   A 1 43  ? -7.364  6.741   103.732 1.00 30.72  ? 953  ILE   A CG1   1 
ATOM   281  C  CG2   . ILE   A 1 43  ? -7.693  6.469   101.223 1.00 30.74  ? 953  ILE   A CG2   1 
ATOM   282  C  CD1   . ILE   A 1 43  ? -6.942  8.173   103.678 1.00 30.71  ? 953  ILE   A CD1   1 
ATOM   283  N  N     . SER   A 1 44  ? -5.102  3.211   102.864 1.00 29.29  ? 954  SER   A N     1 
ATOM   284  C  CA    . SER   A 1 44  ? -3.972  2.666   103.623 1.00 32.07  ? 954  SER   A CA    1 
ATOM   285  C  C     . SER   A 1 44  ? -3.011  3.753   104.100 1.00 33.69  ? 954  SER   A C     1 
ATOM   286  O  O     . SER   A 1 44  ? -2.359  3.569   105.132 1.00 36.89  ? 954  SER   A O     1 
ATOM   287  C  CB    . SER   A 1 44  ? -3.197  1.620   102.808 1.00 28.98  ? 954  SER   A CB    1 
ATOM   288  O  OG    . SER   A 1 44  ? -3.002  2.039   101.473 1.00 29.54  ? 954  SER   A OG    1 
ATOM   289  N  N     . GLU   A 1 45  ? -2.905  4.871   103.377 1.00 32.29  ? 955  GLU   A N     1 
ATOM   290  C  CA    . GLU   A 1 45  ? -1.978  5.949   103.699 1.00 31.71  ? 955  GLU   A CA    1 
ATOM   291  C  C     . GLU   A 1 45  ? -2.713  7.277   103.740 1.00 32.07  ? 955  GLU   A C     1 
ATOM   292  O  O     . GLU   A 1 45  ? -3.695  7.476   103.019 1.00 32.74  ? 955  GLU   A O     1 
ATOM   293  C  CB    . GLU   A 1 45  ? -0.832  6.049   102.667 1.00 31.35  ? 955  GLU   A CB    1 
ATOM   294  C  CG    . GLU   A 1 45  ? 0.138   4.906   102.734 1.00 39.12  ? 955  GLU   A CG    1 
ATOM   295  C  CD    . GLU   A 1 45  ? 0.958   4.739   101.463 1.00 39.77  ? 955  GLU   A CD    1 
ATOM   296  O  OE1   . GLU   A 1 45  ? 0.680   5.426   100.454 1.00 40.76  ? 955  GLU   A OE1   1 
ATOM   297  O  OE2   . GLU   A 1 45  ? 1.870   3.901   101.480 1.00 37.81  ? 955  GLU   A OE2   1 
ATOM   298  N  N     . ASN   A 1 46  ? -2.222  8.182   104.586 1.00 31.78  ? 956  ASN   A N     1 
ATOM   299  C  CA    . ASN   A 1 46  ? -2.809  9.512   104.706 1.00 32.26  ? 956  ASN   A CA    1 
ATOM   300  C  C     . ASN   A 1 46  ? -2.960  10.185  103.345 1.00 32.60  ? 956  ASN   A C     1 
ATOM   301  O  O     . ASN   A 1 46  ? -2.129  10.018  102.444 1.00 32.21  ? 956  ASN   A O     1 
ATOM   302  C  CB    . ASN   A 1 46  ? -1.962  10.401  105.613 1.00 31.92  ? 956  ASN   A CB    1 
ATOM   303  C  CG    . ASN   A 1 46  ? -1.816  9.844   107.009 1.00 35.13  ? 956  ASN   A CG    1 
ATOM   304  O  OD1   . ASN   A 1 46  ? -2.685  9.134   107.510 1.00 31.98  ? 956  ASN   A OD1   1 
ATOM   305  N  ND2   . ASN   A 1 46  ? -0.682  10.150  107.645 1.00 34.20  ? 956  ASN   A ND2   1 
ATOM   306  N  N     . CYS   A 1 47  ? -4.027  10.990  103.226 1.00 33.45  ? 957  CYS   A N     1 
ATOM   307  C  CA    . CYS   A 1 47  ? -4.401  11.692  102.011 1.00 34.01  ? 957  CYS   A CA    1 
ATOM   308  C  C     . CYS   A 1 47  ? -4.474  13.186  102.301 1.00 34.50  ? 957  CYS   A C     1 
ATOM   309  O  O     . CYS   A 1 47  ? -4.522  13.606  103.457 1.00 39.44  ? 957  CYS   A O     1 
ATOM   310  C  CB    . CYS   A 1 47  ? -5.754  11.184  101.485 1.00 34.91  ? 957  CYS   A CB    1 
ATOM   311  S  SG    . CYS   A 1 47  ? -7.210  11.756  102.436 1.00 36.12  ? 957  CYS   A SG    1 
ATOM   312  N  N     . GLU   A 1 48  ? -4.521  14.000  101.242 1.00 34.95  ? 958  GLU   A N     1 
ATOM   313  C  CA    . GLU   A 1 48  ? -4.624  15.455  101.369 1.00 37.33  ? 958  GLU   A CA    1 
ATOM   314  C  C     . GLU   A 1 48  ? -5.796  15.964  100.542 1.00 36.87  ? 958  GLU   A C     1 
ATOM   315  O  O     . GLU   A 1 48  ? -5.948  15.580  99.380  1.00 36.94  ? 958  GLU   A O     1 
ATOM   316  C  CB    . GLU   A 1 48  ? -3.334  16.175  100.915 1.00 35.12  ? 958  GLU   A CB    1 
ATOM   317  C  CG    . GLU   A 1 48  ? -2.051  15.611  101.490 1.00 34.00  ? 958  GLU   A CG    1 
ATOM   318  C  CD    . GLU   A 1 48  ? -0.791  16.250  100.886 1.00 38.79  ? 958  GLU   A CD    1 
ATOM   319  O  OE1   . GLU   A 1 48  ? -0.839  17.449  100.529 1.00 38.59  ? 958  GLU   A OE1   1 
ATOM   320  O  OE2   . GLU   A 1 48  ? 0.248   15.550  100.770 1.00 43.21  ? 958  GLU   A OE2   1 
ATOM   321  N  N     . THR   A 1 49  ? -6.611  16.840  101.125 1.00 37.96  ? 959  THR   A N     1 
ATOM   322  C  CA    . THR   A 1 49  ? -7.704  17.464  100.385 1.00 39.37  ? 959  THR   A CA    1 
ATOM   323  C  C     . THR   A 1 49  ? -7.462  18.935  100.083 1.00 40.10  ? 959  THR   A C     1 
ATOM   324  O  O     . THR   A 1 49  ? -8.360  19.596  99.556  1.00 41.47  ? 959  THR   A O     1 
ATOM   325  C  CB    . THR   A 1 49  ? -9.041  17.303  101.126 1.00 40.50  ? 959  THR   A CB    1 
ATOM   326  O  OG1   . THR   A 1 49  ? -8.873  17.606  102.512 1.00 40.45  ? 959  THR   A OG1   1 
ATOM   327  C  CG2   . THR   A 1 49  ? -9.583  15.887  100.975 1.00 40.25  ? 959  THR   A CG2   1 
ATOM   328  N  N     . SER   A 1 50  ? -6.282  19.458  100.398 1.00 39.38  ? 960  SER   A N     1 
ATOM   329  C  CA    . SER   A 1 50  ? -5.864  20.790  99.977  1.00 40.00  ? 960  SER   A CA    1 
ATOM   330  C  C     . SER   A 1 50  ? -4.340  20.805  100.034 1.00 39.78  ? 960  SER   A C     1 
ATOM   331  O  O     . SER   A 1 50  ? -3.711  19.812  100.407 1.00 44.20  ? 960  SER   A O     1 
ATOM   332  C  CB    . SER   A 1 50  ? -6.508  21.894  100.832 1.00 41.42  ? 960  SER   A CB    1 
ATOM   333  O  OG    . SER   A 1 50  ? -6.488  21.602  102.224 1.00 41.16  ? 960  SER   A OG    1 
ATOM   334  N  N     . THR   A 1 51  ? -3.743  21.925  99.646  1.00 39.18  ? 961  THR   A N     1 
ATOM   335  C  CA    . THR   A 1 51  ? -2.281  22.000  99.540  1.00 40.60  ? 961  THR   A CA    1 
ATOM   336  C  C     . THR   A 1 51  ? -1.644  22.085  100.930 1.00 37.83  ? 961  THR   A C     1 
ATOM   337  O  O     . THR   A 1 51  ? -1.843  23.074  101.640 1.00 42.06  ? 961  THR   A O     1 
ATOM   338  C  CB    . THR   A 1 51  ? -1.898  23.217  98.697  1.00 38.96  ? 961  THR   A CB    1 
ATOM   339  O  OG1   . THR   A 1 51  ? -2.624  23.192  97.461  1.00 42.81  ? 961  THR   A OG1   1 
ATOM   340  C  CG2   . THR   A 1 51  ? -0.408  23.241  98.384  1.00 40.55  ? 961  THR   A CG2   1 
ATOM   341  N  N     . MET   A 1 52  ? -0.880  21.060  101.324 1.00 40.07  ? 962  MET   A N     1 
ATOM   342  C  CA    . MET   A 1 52  ? -0.197  21.063  102.618 1.00 36.22  ? 962  MET   A CA    1 
ATOM   343  C  C     . MET   A 1 52  ? 1.281   21.468  102.543 1.00 37.70  ? 962  MET   A C     1 
ATOM   344  O  O     . MET   A 1 52  ? 1.878   21.763  103.585 1.00 37.36  ? 962  MET   A O     1 
ATOM   345  C  CB    . MET   A 1 52  ? -0.287  19.685  103.291 1.00 35.30  ? 962  MET   A CB    1 
ATOM   346  C  CG    . MET   A 1 52  ? -1.674  19.061  103.398 1.00 38.96  ? 962  MET   A CG    1 
ATOM   347  S  SD    . MET   A 1 52  ? -2.780  19.893  104.552 1.00 44.24  ? 962  MET   A SD    1 
ATOM   348  C  CE    . MET   A 1 52  ? -3.723  20.872  103.416 1.00 40.56  ? 962  MET   A CE    1 
ATOM   349  N  N     . ASN   A 1 53  ? 1.891   21.466  101.363 1.00 35.51  ? 963  ASN   A N     1 
ATOM   350  C  CA    . ASN   A 1 53  ? 3.291   21.877  101.203 1.00 36.24  ? 963  ASN   A CA    1 
ATOM   351  C  C     . ASN   A 1 53  ? 4.216   21.134  102.170 1.00 37.97  ? 963  ASN   A C     1 
ATOM   352  O  O     . ASN   A 1 53  ? 5.045   21.730  102.865 1.00 37.09  ? 963  ASN   A O     1 
ATOM   353  C  CB    . ASN   A 1 53  ? 3.441   23.393  101.373 1.00 36.39  ? 963  ASN   A CB    1 
ATOM   354  C  CG    . ASN   A 1 53  ? 4.699   23.925  100.726 1.00 39.35  ? 963  ASN   A CG    1 
ATOM   355  O  OD1   . ASN   A 1 53  ? 5.142   23.409  99.689  1.00 35.85  ? 963  ASN   A OD1   1 
ATOM   356  N  ND2   . ASN   A 1 53  ? 5.288   24.964  101.329 1.00 37.16  ? 963  ASN   A ND2   1 
ATOM   357  N  N     . ILE   A 1 54  ? 4.063   19.811  102.215 1.00 35.44  ? 964  ILE   A N     1 
ATOM   358  C  CA    . ILE   A 1 54  ? 4.957   18.985  103.016 1.00 33.50  ? 964  ILE   A CA    1 
ATOM   359  C  C     . ILE   A 1 54  ? 6.351   19.018  102.395 1.00 32.65  ? 964  ILE   A C     1 
ATOM   360  O  O     . ILE   A 1 54  ? 6.521   18.738  101.202 1.00 32.49  ? 964  ILE   A O     1 
ATOM   361  C  CB    . ILE   A 1 54  ? 4.414   17.551  103.114 1.00 34.25  ? 964  ILE   A CB    1 
ATOM   362  C  CG1   . ILE   A 1 54  ? 3.004   17.545  103.728 1.00 34.28  ? 964  ILE   A CG1   1 
ATOM   363  C  CG2   . ILE   A 1 54  ? 5.395   16.666  103.901 1.00 34.26  ? 964  ILE   A CG2   1 
ATOM   364  C  CD1   . ILE   A 1 54  ? 2.358   16.138  103.881 1.00 33.26  ? 964  ILE   A CD1   1 
ATOM   365  N  N     . ASP   A 1 55  ? 7.351   19.404  103.190 1.00 35.67  ? 965  ASP   A N     1 
ATOM   366  C  CA    . ASP   A 1 55  ? 8.748   19.405  102.744 1.00 32.70  ? 965  ASP   A CA    1 
ATOM   367  C  C     . ASP   A 1 55  ? 9.178   17.968  102.446 1.00 33.75  ? 965  ASP   A C     1 
ATOM   368  O  O     . ASP   A 1 55  ? 9.444   17.182  103.361 1.00 31.60  ? 965  ASP   A O     1 
ATOM   369  C  CB    . ASP   A 1 55  ? 9.645   20.045  103.803 1.00 33.14  ? 965  ASP   A CB    1 
ATOM   370  C  CG    . ASP   A 1 55  ? 11.155  20.059  103.404 1.00 39.08  ? 965  ASP   A CG    1 
ATOM   371  O  OD1   . ASP   A 1 55  ? 11.484  19.939  102.202 1.00 37.40  ? 965  ASP   A OD1   1 
ATOM   372  O  OD2   . ASP   A 1 55  ? 12.002  20.204  104.316 1.00 33.52  ? 965  ASP   A OD2   1 
ATOM   373  N  N     . ARG   A 1 56  ? 9.228   17.612  101.161 1.00 31.81  ? 966  ARG   A N     1 
ATOM   374  C  CA    . ARG   A 1 56  ? 9.702   16.304  100.733 1.00 31.33  ? 966  ARG   A CA    1 
ATOM   375  C  C     . ARG   A 1 56  ? 11.058  16.380  100.038 1.00 35.17  ? 966  ARG   A C     1 
ATOM   376  O  O     . ARG   A 1 56  ? 11.440  15.429  99.344  1.00 31.54  ? 966  ARG   A O     1 
ATOM   377  C  CB    . ARG   A 1 56  ? 8.687   15.636  99.810  1.00 32.74  ? 966  ARG   A CB    1 
ATOM   378  C  CG    . ARG   A 1 56  ? 7.311   15.470  100.441 1.00 37.95  ? 966  ARG   A CG    1 
ATOM   379  C  CD    . ARG   A 1 56  ? 6.260   15.213  99.387  1.00 42.12  ? 966  ARG   A CD    1 
ATOM   380  N  NE    . ARG   A 1 56  ? 4.931   15.054  99.962  1.00 45.43  ? 966  ARG   A NE    1 
ATOM   381  C  CZ    . ARG   A 1 56  ? 4.545   13.980  100.633 1.00 47.14  ? 966  ARG   A CZ    1 
ATOM   382  N  NH1   . ARG   A 1 56  ? 5.387   12.984  100.886 1.00 42.97  ? 966  ARG   A NH1   1 
ATOM   383  N  NH2   . ARG   A 1 56  ? 3.284   13.897  101.056 1.00 45.55  ? 966  ARG   A NH2   1 
ATOM   384  N  N     . ASN   A 1 57  ? 11.779  17.496  100.191 1.00 32.08  ? 967  ASN   A N     1 
ATOM   385  C  CA    . ASN   A 1 57  ? 13.113  17.633  99.605  1.00 35.65  ? 967  ASN   A CA    1 
ATOM   386  C  C     . ASN   A 1 57  ? 14.050  16.555  100.144 1.00 32.31  ? 967  ASN   A C     1 
ATOM   387  O  O     . ASN   A 1 57  ? 14.396  16.561  101.326 1.00 32.37  ? 967  ASN   A O     1 
ATOM   388  C  CB    . ASN   A 1 57  ? 13.681  19.034  99.884  1.00 33.18  ? 967  ASN   A CB    1 
ATOM   389  C  CG    . ASN   A 1 57  ? 14.934  19.342  99.070  1.00 33.74  ? 967  ASN   A CG    1 
ATOM   390  O  OD1   . ASN   A 1 57  ? 15.704  18.450  98.742  1.00 33.77  ? 967  ASN   A OD1   1 
ATOM   391  N  ND2   . ASN   A 1 57  ? 15.133  20.614  98.739  1.00 36.10  ? 967  ASN   A ND2   1 
ATOM   392  N  N     . ILE   A 1 58  ? 14.437  15.609  99.290  1.00 32.94  ? 968  ILE   A N     1 
ATOM   393  C  CA    . ILE   A 1 58  ? 15.345  14.552  99.732  1.00 32.62  ? 968  ILE   A CA    1 
ATOM   394  C  C     . ILE   A 1 58  ? 16.607  15.130  100.373 1.00 34.56  ? 968  ILE   A C     1 
ATOM   395  O  O     . ILE   A 1 58  ? 17.112  14.568  101.349 1.00 33.35  ? 968  ILE   A O     1 
ATOM   396  C  CB    . ILE   A 1 58  ? 15.682  13.599  98.571  1.00 33.50  ? 968  ILE   A CB    1 
ATOM   397  C  CG1   . ILE   A 1 58  ? 16.259  12.289  99.115  1.00 32.50  ? 968  ILE   A CG1   1 
ATOM   398  C  CG2   . ILE   A 1 58  ? 16.636  14.238  97.570  1.00 33.09  ? 968  ILE   A CG2   1 
ATOM   399  C  CD1   . ILE   A 1 58  ? 16.195  11.152  98.114  1.00 32.60  ? 968  ILE   A CD1   1 
ATOM   400  N  N     . THR   A 1 59  ? 17.091  16.287  99.902  1.00 33.49  ? 969  THR   A N     1 
ATOM   401  C  CA    . THR   A 1 59  ? 18.317  16.810  100.496 1.00 34.25  ? 969  THR   A CA    1 
ATOM   402  C  C     . THR   A 1 59  ? 18.105  17.343  101.902 1.00 35.23  ? 969  THR   A C     1 
ATOM   403  O  O     . THR   A 1 59  ? 19.096  17.669  102.569 1.00 34.96  ? 969  THR   A O     1 
ATOM   404  C  CB    . THR   A 1 59  ? 18.963  17.922  99.649  1.00 36.45  ? 969  THR   A CB    1 
ATOM   405  O  OG1   . THR   A 1 59  ? 18.137  19.096  99.644  1.00 35.00  ? 969  THR   A OG1   1 
ATOM   406  C  CG2   . THR   A 1 59  ? 19.221  17.462  98.220  1.00 35.12  ? 969  THR   A CG2   1 
ATOM   407  N  N     . HIS   A 1 60  ? 16.859  17.449  102.375 1.00 33.68  ? 970  HIS   A N     1 
ATOM   408  C  CA    . HIS   A 1 60  ? 16.647  17.877  103.749 1.00 33.78  ? 970  HIS   A CA    1 
ATOM   409  C  C     . HIS   A 1 60  ? 16.530  16.705  104.704 1.00 35.74  ? 970  HIS   A C     1 
ATOM   410  O  O     . HIS   A 1 60  ? 16.476  16.920  105.922 1.00 35.80  ? 970  HIS   A O     1 
ATOM   411  C  CB    . HIS   A 1 60  ? 15.402  18.768  103.865 1.00 36.58  ? 970  HIS   A CB    1 
ATOM   412  C  CG    . HIS   A 1 60  ? 15.464  20.005  103.024 1.00 34.26  ? 970  HIS   A CG    1 
ATOM   413  N  ND1   . HIS   A 1 60  ? 14.392  20.860  102.881 1.00 36.70  ? 970  HIS   A ND1   1 
ATOM   414  C  CD2   . HIS   A 1 60  ? 16.462  20.524  102.271 1.00 34.90  ? 970  HIS   A CD2   1 
ATOM   415  C  CE1   . HIS   A 1 60  ? 14.729  21.858  102.079 1.00 35.93  ? 970  HIS   A CE1   1 
ATOM   416  N  NE2   . HIS   A 1 60  ? 15.977  21.671  101.688 1.00 38.90  ? 970  HIS   A NE2   1 
ATOM   417  N  N     . LEU   A 1 61  ? 16.511  15.475  104.184 1.00 36.89  ? 971  LEU   A N     1 
ATOM   418  C  CA    . LEU   A 1 61  ? 16.493  14.301  105.046 1.00 35.01  ? 971  LEU   A CA    1 
ATOM   419  C  C     . LEU   A 1 61  ? 17.778  14.213  105.852 1.00 34.86  ? 971  LEU   A C     1 
ATOM   420  O  O     . LEU   A 1 61  ? 18.879  14.249  105.291 1.00 35.48  ? 971  LEU   A O     1 
ATOM   421  C  CB    . LEU   A 1 61  ? 16.310  13.021  104.224 1.00 32.22  ? 971  LEU   A CB    1 
ATOM   422  C  CG    . LEU   A 1 61  ? 14.930  12.814  103.601 1.00 31.58  ? 971  LEU   A CG    1 
ATOM   423  C  CD1   . LEU   A 1 61  ? 14.800  11.395  103.042 1.00 32.57  ? 971  LEU   A CD1   1 
ATOM   424  C  CD2   . LEU   A 1 61  ? 13.839  13.122  104.621 1.00 31.20  ? 971  LEU   A CD2   1 
ATOM   425  N  N     . GLN   A 1 62  ? 17.637  14.101  107.171 1.00 35.54  ? 972  GLN   A N     1 
ATOM   426  C  CA    . GLN   A 1 62  ? 18.737  13.636  108.007 1.00 36.23  ? 972  GLN   A CA    1 
ATOM   427  C  C     . GLN   A 1 62  ? 18.805  12.114  107.891 1.00 36.07  ? 972  GLN   A C     1 
ATOM   428  O  O     . GLN   A 1 62  ? 17.821  11.424  108.173 1.00 35.54  ? 972  GLN   A O     1 
ATOM   429  C  CB    . GLN   A 1 62  ? 18.543  14.080  109.460 1.00 34.71  ? 972  GLN   A CB    1 
ATOM   430  C  CG    . GLN   A 1 62  ? 18.916  15.557  109.709 1.00 36.18  ? 972  GLN   A CG    1 
ATOM   431  C  CD    . GLN   A 1 62  ? 19.025  15.919  111.188 1.00 38.28  ? 972  GLN   A CD    1 
ATOM   432  O  OE1   . GLN   A 1 62  ? 20.109  15.867  111.778 1.00 45.12  ? 972  GLN   A OE1   1 
ATOM   433  N  NE2   . GLN   A 1 62  ? 17.907  16.314  111.783 1.00 40.00  ? 972  GLN   A NE2   1 
ATOM   434  N  N     . HIS   A 1 63  ? 19.951  11.587  107.467 1.00 34.35  ? 973  HIS   A N     1 
ATOM   435  C  CA    . HIS   A 1 63  ? 20.107  10.171  107.155 1.00 36.25  ? 973  HIS   A CA    1 
ATOM   436  C  C     . HIS   A 1 63  ? 21.365  9.617   107.828 1.00 40.80  ? 973  HIS   A C     1 
ATOM   437  O  O     . HIS   A 1 63  ? 22.212  10.364  108.328 1.00 46.25  ? 973  HIS   A O     1 
ATOM   438  C  CB    . HIS   A 1 63  ? 20.171  9.962   105.637 1.00 34.40  ? 973  HIS   A CB    1 
ATOM   439  C  CG    . HIS   A 1 63  ? 21.344  10.636  104.991 1.00 40.39  ? 973  HIS   A CG    1 
ATOM   440  N  ND1   . HIS   A 1 63  ? 21.239  11.840  104.328 1.00 42.39  ? 973  HIS   A ND1   1 
ATOM   441  C  CD2   . HIS   A 1 63  ? 22.652  10.284  104.924 1.00 38.70  ? 973  HIS   A CD2   1 
ATOM   442  C  CE1   . HIS   A 1 63  ? 22.427  12.193  103.868 1.00 39.68  ? 973  HIS   A CE1   1 
ATOM   443  N  NE2   . HIS   A 1 63  ? 23.301  11.267  104.218 1.00 40.14  ? 973  HIS   A NE2   1 
ATOM   444  N  N     . CYS   A 1 64  ? 21.495  8.290   107.830 1.00 42.45  ? 974  CYS   A N     1 
ATOM   445  C  CA    . CYS   A 1 64  ? 22.599  7.613   108.500 1.00 40.11  ? 974  CYS   A CA    1 
ATOM   446  C  C     . CYS   A 1 64  ? 23.537  6.960   107.491 1.00 37.63  ? 974  CYS   A C     1 
ATOM   447  O  O     . CYS   A 1 64  ? 23.193  6.735   106.325 1.00 37.36  ? 974  CYS   A O     1 
ATOM   448  C  CB    . CYS   A 1 64  ? 22.093  6.551   109.488 1.00 36.40  ? 974  CYS   A CB    1 
ATOM   449  S  SG    . CYS   A 1 64  ? 21.512  5.034   108.735 1.00 36.20  ? 974  CYS   A SG    1 
ATOM   450  N  N     . THR   A 1 65  ? 24.742  6.645   107.968 1.00 41.33  ? 975  THR   A N     1 
ATOM   451  C  CA    . THR   A 1 65  ? 25.797  6.102   107.121 1.00 40.20  ? 975  THR   A CA    1 
ATOM   452  C  C     . THR   A 1 65  ? 26.140  4.657   107.457 1.00 41.03  ? 975  THR   A C     1 
ATOM   453  O  O     . THR   A 1 65  ? 27.163  4.148   106.987 1.00 49.66  ? 975  THR   A O     1 
ATOM   454  C  CB    . THR   A 1 65  ? 27.044  6.976   107.218 1.00 41.40  ? 975  THR   A CB    1 
ATOM   455  O  OG1   . THR   A 1 65  ? 27.705  6.731   108.462 1.00 42.27  ? 975  THR   A OG1   1 
ATOM   456  C  CG2   . THR   A 1 65  ? 26.647  8.442   107.145 1.00 40.65  ? 975  THR   A CG2   1 
ATOM   457  N  N     . CYS   A 1 66  ? 25.309  3.986   108.246 1.00 45.44  ? 976  CYS   A N     1 
ATOM   458  C  CA    . CYS   A 1 66  ? 25.564  2.605   108.621 1.00 43.74  ? 976  CYS   A CA    1 
ATOM   459  C  C     . CYS   A 1 66  ? 25.545  1.702   107.401 1.00 48.82  ? 976  CYS   A C     1 
ATOM   460  O  O     . CYS   A 1 66  ? 24.884  1.991   106.396 1.00 42.07  ? 976  CYS   A O     1 
ATOM   461  C  CB    . CYS   A 1 66  ? 24.507  2.118   109.609 1.00 48.50  ? 976  CYS   A CB    1 
ATOM   462  S  SG    . CYS   A 1 66  ? 24.008  3.351   110.768 1.00 39.17  ? 976  CYS   A SG    1 
ATOM   463  N  N     . VAL   A 1 67  ? 26.274  0.587   107.514 1.00 64.47  ? 977  VAL   A N     1 
ATOM   464  C  CA    . VAL   A 1 67  ? 26.311  -0.462  106.502 1.00 66.60  ? 977  VAL   A CA    1 
ATOM   465  C  C     . VAL   A 1 67  ? 25.817  -1.764  107.119 1.00 67.98  ? 977  VAL   A C     1 
ATOM   466  O  O     . VAL   A 1 67  ? 25.264  -2.621  106.417 1.00 71.24  ? 977  VAL   A O     1 
ATOM   467  C  CB    . VAL   A 1 67  ? 27.722  -0.612  105.905 1.00 64.48  ? 977  VAL   A CB    1 
ATOM   468  C  CG1   . VAL   A 1 67  ? 27.804  -1.821  104.979 1.00 62.92  ? 977  VAL   A CG1   1 
ATOM   469  C  CG2   . VAL   A 1 67  ? 28.095  0.648   105.152 1.00 64.78  ? 977  VAL   A CG2   1 
ATOM   470  N  N     . ASP   A 1 68  ? 25.968  -1.914  108.440 1.00 59.21  ? 978  ASP   A N     1 
ATOM   471  C  CA    . ASP   A 1 68  ? 25.394  -3.080  109.108 1.00 58.50  ? 978  ASP   A CA    1 
ATOM   472  C  C     . ASP   A 1 68  ? 23.876  -2.923  109.164 1.00 53.19  ? 978  ASP   A C     1 
ATOM   473  O  O     . ASP   A 1 68  ? 23.290  -2.306  108.270 1.00 54.14  ? 978  ASP   A O     1 
ATOM   474  C  CB    . ASP   A 1 68  ? 25.987  -3.288  110.509 1.00 54.30  ? 978  ASP   A CB    1 
ATOM   475  C  CG    . ASP   A 1 68  ? 25.749  -2.103  111.441 1.00 57.77  ? 978  ASP   A CG    1 
ATOM   476  O  OD1   . ASP   A 1 68  ? 25.262  -1.048  110.975 1.00 57.18  ? 978  ASP   A OD1   1 
ATOM   477  O  OD2   . ASP   A 1 68  ? 26.053  -2.228  112.650 1.00 56.74  ? 978  ASP   A OD2   1 
ATOM   478  N  N     . ASP   A 1 69  ? 23.223  -3.482  110.185 1.00 50.95  ? 979  ASP   A N     1 
ATOM   479  C  CA    . ASP   A 1 69  ? 21.770  -3.424  110.284 1.00 48.19  ? 979  ASP   A CA    1 
ATOM   480  C  C     . ASP   A 1 69  ? 21.286  -2.241  111.119 1.00 45.46  ? 979  ASP   A C     1 
ATOM   481  O  O     . ASP   A 1 69  ? 20.145  -2.253  111.592 1.00 44.32  ? 979  ASP   A O     1 
ATOM   482  C  CB    . ASP   A 1 69  ? 21.223  -4.738  110.847 1.00 47.38  ? 979  ASP   A CB    1 
ATOM   483  C  CG    . ASP   A 1 69  ? 21.739  -5.044  112.230 1.00 47.67  ? 979  ASP   A CG    1 
ATOM   484  O  OD1   . ASP   A 1 69  ? 22.901  -4.703  112.510 1.00 52.38  ? 979  ASP   A OD1   1 
ATOM   485  O  OD2   . ASP   A 1 69  ? 20.990  -5.622  113.049 1.00 49.74  ? 979  ASP   A OD2   1 
ATOM   486  N  N     . CYS   A 1 70  ? 22.129  -1.224  111.297 1.00 47.41  ? 980  CYS   A N     1 
ATOM   487  C  CA    . CYS   A 1 70  ? 21.827  -0.064  112.122 1.00 42.31  ? 980  CYS   A CA    1 
ATOM   488  C  C     . CYS   A 1 70  ? 21.430  -0.467  113.543 1.00 43.53  ? 980  CYS   A C     1 
ATOM   489  O  O     . CYS   A 1 70  ? 20.439  0.014   114.090 1.00 47.50  ? 980  CYS   A O     1 
ATOM   490  C  CB    . CYS   A 1 70  ? 20.730  0.803   111.483 1.00 45.30  ? 980  CYS   A CB    1 
ATOM   491  S  SG    . CYS   A 1 70  ? 21.025  1.434   109.799 1.00 37.04  ? 980  CYS   A SG    1 
ATOM   492  N  N     . SER   A 1 71  ? 22.218  -1.348  114.162 1.00 46.74  ? 981  SER   A N     1 
ATOM   493  C  CA    . SER   A 1 71  ? 22.007  -1.700  115.564 1.00 44.89  ? 981  SER   A CA    1 
ATOM   494  C  C     . SER   A 1 71  ? 23.026  -1.077  116.504 1.00 45.11  ? 981  SER   A C     1 
ATOM   495  O  O     . SER   A 1 71  ? 22.949  -1.309  117.716 1.00 46.95  ? 981  SER   A O     1 
ATOM   496  C  CB    . SER   A 1 71  ? 22.007  -3.223  115.766 1.00 43.98  ? 981  SER   A CB    1 
ATOM   497  O  OG    . SER   A 1 71  ? 22.700  -3.894  114.738 1.00 46.98  ? 981  SER   A OG    1 
ATOM   498  N  N     . SER   A 1 72  ? 23.970  -0.293  115.988 1.00 48.25  ? 982  SER   A N     1 
ATOM   499  C  CA    . SER   A 1 72  ? 24.982  0.336   116.820 1.00 43.95  ? 982  SER   A CA    1 
ATOM   500  C  C     . SER   A 1 72  ? 24.514  1.718   117.261 1.00 48.58  ? 982  SER   A C     1 
ATOM   501  O  O     . SER   A 1 72  ? 23.456  2.209   116.854 1.00 43.45  ? 982  SER   A O     1 
ATOM   502  C  CB    . SER   A 1 72  ? 26.300  0.463   116.067 1.00 43.36  ? 982  SER   A CB    1 
ATOM   503  O  OG    . SER   A 1 72  ? 26.331  1.709   115.393 1.00 42.77  ? 982  SER   A OG    1 
ATOM   504  N  N     . SER   A 1 73  ? 25.337  2.376   118.072 1.00 49.59  ? 983  SER   A N     1 
ATOM   505  C  CA    . SER   A 1 73  ? 25.003  3.700   118.573 1.00 50.69  ? 983  SER   A CA    1 
ATOM   506  C  C     . SER   A 1 73  ? 25.461  4.826   117.654 1.00 49.15  ? 983  SER   A C     1 
ATOM   507  O  O     . SER   A 1 73  ? 25.143  5.987   117.926 1.00 52.27  ? 983  SER   A O     1 
ATOM   508  C  CB    . SER   A 1 73  ? 25.597  3.897   119.968 1.00 53.38  ? 983  SER   A CB    1 
ATOM   509  O  OG    . SER   A 1 73  ? 27.003  3.749   119.945 1.00 55.96  ? 983  SER   A OG    1 
ATOM   510  N  N     . ASN   A 1 74  ? 26.187  4.527   116.577 1.00 43.38  ? 984  ASN   A N     1 
ATOM   511  C  CA    . ASN   A 1 74  ? 26.559  5.552   115.612 1.00 44.85  ? 984  ASN   A CA    1 
ATOM   512  C  C     . ASN   A 1 74  ? 25.536  5.705   114.508 1.00 44.66  ? 984  ASN   A C     1 
ATOM   513  O  O     . ASN   A 1 74  ? 25.799  6.394   113.517 1.00 43.46  ? 984  ASN   A O     1 
ATOM   514  C  CB    . ASN   A 1 74  ? 27.937  5.258   115.027 1.00 44.94  ? 984  ASN   A CB    1 
ATOM   515  C  CG    . ASN   A 1 74  ? 29.008  5.392   116.053 1.00 46.01  ? 984  ASN   A CG    1 
ATOM   516  O  OD1   . ASN   A 1 74  ? 28.714  5.626   117.223 1.00 48.30  ? 984  ASN   A OD1   1 
ATOM   517  N  ND2   . ASN   A 1 74  ? 30.253  5.257   115.641 1.00 51.06  ? 984  ASN   A ND2   1 
ATOM   518  N  N     . CYS   A 1 75  ? 24.374  5.092   114.663 1.00 43.39  ? 985  CYS   A N     1 
ATOM   519  C  CA    . CYS   A 1 75  ? 23.279  5.297   113.733 1.00 41.89  ? 985  CYS   A CA    1 
ATOM   520  C  C     . CYS   A 1 75  ? 22.679  6.663   114.019 1.00 41.01  ? 985  CYS   A C     1 
ATOM   521  O  O     . CYS   A 1 75  ? 22.057  6.869   115.069 1.00 40.50  ? 985  CYS   A O     1 
ATOM   522  C  CB    . CYS   A 1 75  ? 22.241  4.192   113.889 1.00 41.43  ? 985  CYS   A CB    1 
ATOM   523  S  SG    . CYS   A 1 75  ? 21.094  4.129   112.549 1.00 36.97  ? 985  CYS   A SG    1 
ATOM   524  N  N     . LEU   A 1 76  ? 22.867  7.608   113.103 1.00 40.10  ? 986  LEU   A N     1 
ATOM   525  C  CA    . LEU   A 1 76  ? 22.382  8.949   113.402 1.00 45.09  ? 986  LEU   A CA    1 
ATOM   526  C  C     . LEU   A 1 76  ? 20.873  8.964   113.548 1.00 39.28  ? 986  LEU   A C     1 
ATOM   527  O  O     . LEU   A 1 76  ? 20.344  9.743   114.349 1.00 41.03  ? 986  LEU   A O     1 
ATOM   528  C  CB    . LEU   A 1 76  ? 22.827  9.955   112.340 1.00 45.23  ? 986  LEU   A CB    1 
ATOM   529  C  CG    . LEU   A 1 76  ? 22.278  11.362  112.618 1.00 42.77  ? 986  LEU   A CG    1 
ATOM   530  C  CD1   . LEU   A 1 76  ? 23.381  12.396  112.878 1.00 43.80  ? 986  LEU   A CD1   1 
ATOM   531  C  CD2   . LEU   A 1 76  ? 21.352  11.788  111.490 1.00 39.98  ? 986  LEU   A CD2   1 
ATOM   532  N  N     . CYS   A 1 77  ? 20.168  8.080   112.825 1.00 37.89  ? 987  CYS   A N     1 
ATOM   533  C  CA    . CYS   A 1 77  ? 18.708  8.044   112.908 1.00 40.33  ? 987  CYS   A CA    1 
ATOM   534  C  C     . CYS   A 1 77  ? 18.237  7.501   114.247 1.00 37.53  ? 987  CYS   A C     1 
ATOM   535  O  O     . CYS   A 1 77  ? 17.126  7.822   114.693 1.00 41.38  ? 987  CYS   A O     1 
ATOM   536  C  CB    . CYS   A 1 77  ? 18.135  7.213   111.766 1.00 38.32  ? 987  CYS   A CB    1 
ATOM   537  S  SG    . CYS   A 1 77  ? 19.020  7.482   110.221 1.00 41.77  ? 987  CYS   A SG    1 
ATOM   538  N  N     . GLY   A 1 78  ? 19.062  6.688   114.901 1.00 39.14  ? 988  GLY   A N     1 
ATOM   539  C  CA    . GLY   A 1 78  ? 18.777  6.335   116.279 1.00 42.56  ? 988  GLY   A CA    1 
ATOM   540  C  C     . GLY   A 1 78  ? 19.046  7.483   117.231 1.00 43.95  ? 988  GLY   A C     1 
ATOM   541  O  O     . GLY   A 1 78  ? 18.327  7.663   118.216 1.00 44.36  ? 988  GLY   A O     1 
ATOM   542  N  N     . GLN   A 1 79  ? 20.092  8.270   116.957 1.00 42.75  ? 989  GLN   A N     1 
ATOM   543  C  CA    . GLN   A 1 79  ? 20.400  9.409   117.812 1.00 40.75  ? 989  GLN   A CA    1 
ATOM   544  C  C     . GLN   A 1 79  ? 19.296  10.446  117.757 1.00 39.59  ? 989  GLN   A C     1 
ATOM   545  O  O     . GLN   A 1 79  ? 18.939  11.034  118.782 1.00 41.13  ? 989  GLN   A O     1 
ATOM   546  C  CB    . GLN   A 1 79  ? 21.721  10.031  117.398 1.00 38.02  ? 989  GLN   A CB    1 
ATOM   547  C  CG    . GLN   A 1 79  ? 22.872  9.056   117.495 1.00 45.88  ? 989  GLN   A CG    1 
ATOM   548  C  CD    . GLN   A 1 79  ? 24.170  9.725   117.230 1.00 42.72  ? 989  GLN   A CD    1 
ATOM   549  O  OE1   . GLN   A 1 79  ? 24.418  10.828  117.718 1.00 48.70  ? 989  GLN   A OE1   1 
ATOM   550  N  NE2   . GLN   A 1 79  ? 25.017  9.080   116.443 1.00 52.12  ? 989  GLN   A NE2   1 
ATOM   551  N  N     . LEU   A 1 80  ? 18.750  10.688  116.564 1.00 40.16  ? 990  LEU   A N     1 
ATOM   552  C  CA    . LEU   A 1 80  ? 17.632  11.608  116.433 1.00 38.43  ? 990  LEU   A CA    1 
ATOM   553  C  C     . LEU   A 1 80  ? 16.474  11.188  117.317 1.00 42.27  ? 990  LEU   A C     1 
ATOM   554  O  O     . LEU   A 1 80  ? 15.705  12.038  117.780 1.00 40.37  ? 990  LEU   A O     1 
ATOM   555  C  CB    . LEU   A 1 80  ? 17.190  11.674  114.974 1.00 37.71  ? 990  LEU   A CB    1 
ATOM   556  C  CG    . LEU   A 1 80  ? 18.307  12.106  114.029 1.00 40.15  ? 990  LEU   A CG    1 
ATOM   557  C  CD1   . LEU   A 1 80  ? 17.980  11.701  112.588 1.00 36.64  ? 990  LEU   A CD1   1 
ATOM   558  C  CD2   . LEU   A 1 80  ? 18.553  13.604  114.152 1.00 32.81  ? 990  LEU   A CD2   1 
ATOM   559  N  N     . SER   A 1 81  ? 16.340  9.885   117.563 1.00 40.72  ? 991  SER   A N     1 
ATOM   560  C  CA    . SER   A 1 81  ? 15.263  9.328   118.367 1.00 41.64  ? 991  SER   A CA    1 
ATOM   561  C  C     . SER   A 1 81  ? 15.700  9.064   119.801 1.00 45.78  ? 991  SER   A C     1 
ATOM   562  O  O     . SER   A 1 81  ? 15.047  8.280   120.495 1.00 45.15  ? 991  SER   A O     1 
ATOM   563  C  CB    . SER   A 1 81  ? 14.754  8.026   117.737 1.00 42.12  ? 991  SER   A CB    1 
ATOM   564  O  OG    . SER   A 1 81  ? 14.758  8.067   116.313 1.00 39.23  ? 991  SER   A OG    1 
ATOM   565  N  N     . ILE   A 1 82  ? 16.792  9.703   120.250 1.00 46.19  ? 992  ILE   A N     1 
ATOM   566  C  CA    . ILE   A 1 82  ? 17.524  9.379   121.481 1.00 47.01  ? 992  ILE   A CA    1 
ATOM   567  C  C     . ILE   A 1 82  ? 18.312  8.092   121.258 1.00 47.77  ? 992  ILE   A C     1 
ATOM   568  O  O     . ILE   A 1 82  ? 19.548  8.091   121.262 1.00 45.22  ? 992  ILE   A O     1 
ATOM   569  C  CB    . ILE   A 1 82  ? 16.613  9.244   122.723 1.00 51.09  ? 992  ILE   A CB    1 
ATOM   570  C  CG1   . ILE   A 1 82  ? 15.993  10.587  123.118 1.00 48.59  ? 992  ILE   A CG1   1 
ATOM   571  C  CG2   . ILE   A 1 82  ? 17.401  8.657   123.905 1.00 42.58  ? 992  ILE   A CG2   1 
ATOM   572  C  CD1   . ILE   A 1 82  ? 14.790  10.981  122.309 1.00 49.05  ? 992  ILE   A CD1   1 
ATOM   573  N  N     . ARG   A 1 83  ? 17.598  6.985   121.084 1.00 49.78  ? 993  ARG   A N     1 
ATOM   574  C  CA    . ARG   A 1 83  ? 18.191  5.745   120.614 1.00 50.66  ? 993  ARG   A CA    1 
ATOM   575  C  C     . ARG   A 1 83  ? 17.151  5.060   119.750 1.00 51.08  ? 993  ARG   A C     1 
ATOM   576  O  O     . ARG   A 1 83  ? 15.969  5.398   119.796 1.00 55.47  ? 993  ARG   A O     1 
ATOM   577  C  CB    . ARG   A 1 83  ? 18.626  4.827   121.769 1.00 53.30  ? 993  ARG   A CB    1 
ATOM   578  C  CG    . ARG   A 1 83  ? 17.453  4.188   122.518 1.00 58.77  ? 993  ARG   A CG    1 
ATOM   579  C  CD    . ARG   A 1 83  ? 17.894  3.244   123.643 1.00 59.04  ? 993  ARG   A CD    1 
ATOM   580  N  NE    . ARG   A 1 83  ? 18.426  1.981   123.142 1.00 62.31  ? 993  ARG   A NE    1 
ATOM   581  C  CZ    . ARG   A 1 83  ? 18.781  0.958   123.911 1.00 67.75  ? 993  ARG   A CZ    1 
ATOM   582  N  NH1   . ARG   A 1 83  ? 18.641  1.001   125.227 1.00 71.57  ? 993  ARG   A NH1   1 
ATOM   583  N  NH2   . ARG   A 1 83  ? 19.283  -0.138  123.345 1.00 67.65  ? 993  ARG   A NH2   1 
ATOM   584  N  N     . CYS   A 1 84  ? 17.598  4.109   118.947 1.00 46.75  ? 994  CYS   A N     1 
ATOM   585  C  CA    . CYS   A 1 84  ? 16.660  3.187   118.333 1.00 44.38  ? 994  CYS   A CA    1 
ATOM   586  C  C     . CYS   A 1 84  ? 15.981  2.368   119.427 1.00 45.78  ? 994  CYS   A C     1 
ATOM   587  O  O     . CYS   A 1 84  ? 16.645  1.629   120.165 1.00 45.53  ? 994  CYS   A O     1 
ATOM   588  C  CB    . CYS   A 1 84  ? 17.382  2.278   117.343 1.00 44.74  ? 994  CYS   A CB    1 
ATOM   589  S  SG    . CYS   A 1 84  ? 16.275  1.119   116.494 1.00 42.57  ? 994  CYS   A SG    1 
ATOM   590  N  N     . TRP   A 1 85  ? 14.658  2.511   119.539 1.00 45.25  ? 995  TRP   A N     1 
ATOM   591  C  CA    . TRP   A 1 85  ? 13.882  1.837   120.576 1.00 43.62  ? 995  TRP   A CA    1 
ATOM   592  C  C     . TRP   A 1 85  ? 13.376  0.463   120.152 1.00 41.53  ? 995  TRP   A C     1 
ATOM   593  O  O     . TRP   A 1 85  ? 12.707  -0.212  120.944 1.00 43.74  ? 995  TRP   A O     1 
ATOM   594  C  CB    . TRP   A 1 85  ? 12.712  2.724   121.007 1.00 39.53  ? 995  TRP   A CB    1 
ATOM   595  C  CG    . TRP   A 1 85  ? 13.190  4.009   121.624 1.00 43.74  ? 995  TRP   A CG    1 
ATOM   596  C  CD1   . TRP   A 1 85  ? 13.331  5.214   121.004 1.00 45.02  ? 995  TRP   A CD1   1 
ATOM   597  C  CD2   . TRP   A 1 85  ? 13.626  4.201   122.975 1.00 44.84  ? 995  TRP   A CD2   1 
ATOM   598  N  NE1   . TRP   A 1 85  ? 13.812  6.148   121.888 1.00 43.98  ? 995  TRP   A NE1   1 
ATOM   599  C  CE2   . TRP   A 1 85  ? 13.998  5.551   123.106 1.00 45.37  ? 995  TRP   A CE2   1 
ATOM   600  C  CE3   . TRP   A 1 85  ? 13.728  3.363   124.090 1.00 46.43  ? 995  TRP   A CE3   1 
ATOM   601  C  CZ2   . TRP   A 1 85  ? 14.468  6.081   124.306 1.00 48.48  ? 995  TRP   A CZ2   1 
ATOM   602  C  CZ3   . TRP   A 1 85  ? 14.188  3.891   125.279 1.00 46.19  ? 995  TRP   A CZ3   1 
ATOM   603  C  CH2   . TRP   A 1 85  ? 14.555  5.236   125.379 1.00 45.64  ? 995  TRP   A CH2   1 
ATOM   604  N  N     . TYR   A 1 86  ? 13.703  0.026   118.943 1.00 35.28  ? 996  TYR   A N     1 
ATOM   605  C  CA    . TYR   A 1 86  ? 13.278  -1.268  118.444 1.00 37.91  ? 996  TYR   A CA    1 
ATOM   606  C  C     . TYR   A 1 86  ? 14.261  -2.337  118.890 1.00 41.21  ? 996  TYR   A C     1 
ATOM   607  O  O     . TYR   A 1 86  ? 15.478  -2.152  118.771 1.00 46.60  ? 996  TYR   A O     1 
ATOM   608  C  CB    . TYR   A 1 86  ? 13.189  -1.246  116.919 1.00 36.91  ? 996  TYR   A CB    1 
ATOM   609  C  CG    . TYR   A 1 86  ? 12.220  -0.232  116.373 1.00 32.99  ? 996  TYR   A CG    1 
ATOM   610  C  CD1   . TYR   A 1 86  ? 11.050  0.084   117.057 1.00 38.15  ? 996  TYR   A CD1   1 
ATOM   611  C  CD2   . TYR   A 1 86  ? 12.470  0.427   115.176 1.00 33.21  ? 996  TYR   A CD2   1 
ATOM   612  C  CE1   . TYR   A 1 86  ? 10.164  1.014   116.564 1.00 29.25  ? 996  TYR   A CE1   1 
ATOM   613  C  CE2   . TYR   A 1 86  ? 11.574  1.372   114.672 1.00 32.96  ? 996  TYR   A CE2   1 
ATOM   614  C  CZ    . TYR   A 1 86  ? 10.423  1.655   115.374 1.00 31.93  ? 996  TYR   A CZ    1 
ATOM   615  O  OH    . TYR   A 1 86  ? 9.524   2.589   114.879 1.00 32.81  ? 996  TYR   A OH    1 
ATOM   616  N  N     . ASP   A 1 87  ? 13.739  -3.449  119.402 1.00 40.13  ? 997  ASP   A N     1 
ATOM   617  C  CA    . ASP   A 1 87  ? 14.594  -4.594  119.662 1.00 39.32  ? 997  ASP   A CA    1 
ATOM   618  C  C     . ASP   A 1 87  ? 14.689  -5.443  118.393 1.00 42.26  ? 997  ASP   A C     1 
ATOM   619  O  O     . ASP   A 1 87  ? 14.037  -5.161  117.384 1.00 42.16  ? 997  ASP   A O     1 
ATOM   620  C  CB    . ASP   A 1 87  ? 14.097  -5.386  120.876 1.00 40.02  ? 997  ASP   A CB    1 
ATOM   621  C  CG    . ASP   A 1 87  ? 12.743  -6.041  120.667 1.00 39.80  ? 997  ASP   A CG    1 
ATOM   622  O  OD1   . ASP   A 1 87  ? 12.302  -6.219  119.516 1.00 41.25  ? 997  ASP   A OD1   1 
ATOM   623  O  OD2   . ASP   A 1 87  ? 12.109  -6.384  121.686 1.00 41.35  ? 997  ASP   A OD2   1 
ATOM   624  N  N     . LYS   A 1 88  ? 15.507  -6.503  118.443 1.00 46.65  ? 998  LYS   A N     1 
ATOM   625  C  CA    . LYS   A 1 88  ? 15.802  -7.293  117.248 1.00 47.59  ? 998  LYS   A CA    1 
ATOM   626  C  C     . LYS   A 1 88  ? 14.547  -7.830  116.563 1.00 45.35  ? 998  LYS   A C     1 
ATOM   627  O  O     . LYS   A 1 88  ? 14.597  -8.151  115.370 1.00 44.65  ? 998  LYS   A O     1 
ATOM   628  C  CB    . LYS   A 1 88  ? 16.734  -8.454  117.600 1.00 46.54  ? 998  LYS   A CB    1 
ATOM   629  C  CG    . LYS   A 1 88  ? 16.234  -9.292  118.757 1.00 46.67  ? 998  LYS   A CG    1 
ATOM   630  C  CD    . LYS   A 1 88  ? 17.299  -10.223 119.271 1.00 54.30  ? 998  LYS   A CD    1 
ATOM   631  C  CE    . LYS   A 1 88  ? 18.591  -9.483  119.610 1.00 54.27  ? 998  LYS   A CE    1 
ATOM   632  N  NZ    . LYS   A 1 88  ? 19.545  -10.376 120.347 1.00 47.76  ? 998  LYS   A NZ    1 
ATOM   633  N  N     . ASP   A 1 89  ? 13.428  -7.932  117.278 1.00 42.36  ? 999  ASP   A N     1 
ATOM   634  C  CA    . ASP   A 1 89  ? 12.177  -8.422  116.711 1.00 43.34  ? 999  ASP   A CA    1 
ATOM   635  C  C     . ASP   A 1 89  ? 11.187  -7.304  116.384 1.00 40.66  ? 999  ASP   A C     1 
ATOM   636  O  O     . ASP   A 1 89  ? 9.970   -7.529  116.403 1.00 41.22  ? 999  ASP   A O     1 
ATOM   637  C  CB    . ASP   A 1 89  ? 11.532  -9.422  117.663 1.00 46.28  ? 999  ASP   A CB    1 
ATOM   638  C  CG    . ASP   A 1 89  ? 12.278  -10.726 117.716 1.00 49.79  ? 999  ASP   A CG    1 
ATOM   639  O  OD1   . ASP   A 1 89  ? 13.468  -10.737 117.344 1.00 57.66  ? 999  ASP   A OD1   1 
ATOM   640  O  OD2   . ASP   A 1 89  ? 11.677  -11.743 118.120 1.00 53.41  ? 999  ASP   A OD2   1 
ATOM   641  N  N     . GLY   A 1 90  ? 11.671  -6.101  116.090 1.00 37.76  ? 1000 GLY   A N     1 
ATOM   642  C  CA    . GLY   A 1 90  ? 10.790  -4.997  115.745 1.00 40.94  ? 1000 GLY   A CA    1 
ATOM   643  C  C     . GLY   A 1 90  ? 9.995   -4.392  116.886 1.00 38.54  ? 1000 GLY   A C     1 
ATOM   644  O  O     . GLY   A 1 90  ? 9.347   -3.358  116.683 1.00 35.78  ? 1000 GLY   A O     1 
ATOM   645  N  N     . ARG   A 1 91  ? 10.048  -4.970  118.081 1.00 39.12  ? 1001 ARG   A N     1 
ATOM   646  C  CA    . ARG   A 1 91  ? 9.265   -4.512  119.217 1.00 37.41  ? 1001 ARG   A CA    1 
ATOM   647  C  C     . ARG   A 1 91  ? 9.988   -3.433  120.006 1.00 40.13  ? 1001 ARG   A C     1 
ATOM   648  O  O     . ARG   A 1 91  ? 11.216  -3.446  120.140 1.00 40.97  ? 1001 ARG   A O     1 
ATOM   649  C  CB    . ARG   A 1 91  ? 8.952   -5.689  120.134 1.00 39.96  ? 1001 ARG   A CB    1 
ATOM   650  C  CG    . ARG   A 1 91  ? 8.511   -6.895  119.353 1.00 39.74  ? 1001 ARG   A CG    1 
ATOM   651  C  CD    . ARG   A 1 91  ? 7.587   -7.773  120.152 1.00 40.03  ? 1001 ARG   A CD    1 
ATOM   652  N  NE    . ARG   A 1 91  ? 6.828   -8.654  119.274 1.00 40.72  ? 1001 ARG   A NE    1 
ATOM   653  C  CZ    . ARG   A 1 91  ? 7.284   -9.800  118.786 1.00 44.94  ? 1001 ARG   A CZ    1 
ATOM   654  N  NH1   . ARG   A 1 91  ? 8.510   -10.233 119.060 1.00 43.99  ? 1001 ARG   A NH1   1 
ATOM   655  N  NH2   . ARG   A 1 91  ? 6.495   -10.525 117.998 1.00 41.08  ? 1001 ARG   A NH2   1 
ATOM   656  N  N     . LEU   A 1 92  ? 9.205   -2.502  120.548 1.00 41.43  ? 1002 LEU   A N     1 
ATOM   657  C  CA    . LEU   A 1 92  ? 9.762   -1.484  121.427 1.00 41.92  ? 1002 LEU   A CA    1 
ATOM   658  C  C     . LEU   A 1 92  ? 10.368  -2.121  122.673 1.00 46.69  ? 1002 LEU   A C     1 
ATOM   659  O  O     . LEU   A 1 92  ? 9.900   -3.153  123.168 1.00 44.39  ? 1002 LEU   A O     1 
ATOM   660  C  CB    . LEU   A 1 92  ? 8.692   -0.481  121.833 1.00 42.36  ? 1002 LEU   A CB    1 
ATOM   661  C  CG    . LEU   A 1 92  ? 8.090   0.376   120.717 1.00 42.09  ? 1002 LEU   A CG    1 
ATOM   662  C  CD1   . LEU   A 1 92  ? 6.954   1.213   121.280 1.00 36.82  ? 1002 LEU   A CD1   1 
ATOM   663  C  CD2   . LEU   A 1 92  ? 9.165   1.251   120.116 1.00 39.64  ? 1002 LEU   A CD2   1 
ATOM   664  N  N     . LEU   A 1 93  ? 11.428  -1.494  123.177 1.00 45.36  ? 1003 LEU   A N     1 
ATOM   665  C  CA    . LEU   A 1 93  ? 12.040  -1.952  124.412 1.00 52.15  ? 1003 LEU   A CA    1 
ATOM   666  C  C     . LEU   A 1 93  ? 11.084  -1.760  125.579 1.00 55.81  ? 1003 LEU   A C     1 
ATOM   667  O  O     . LEU   A 1 93  ? 10.220  -0.880  125.566 1.00 57.55  ? 1003 LEU   A O     1 
ATOM   668  C  CB    . LEU   A 1 93  ? 13.343  -1.201  124.684 1.00 53.45  ? 1003 LEU   A CB    1 
ATOM   669  C  CG    . LEU   A 1 93  ? 14.469  -1.360  123.667 1.00 47.65  ? 1003 LEU   A CG    1 
ATOM   670  C  CD1   . LEU   A 1 93  ? 15.755  -0.780  124.240 1.00 56.81  ? 1003 LEU   A CD1   1 
ATOM   671  C  CD2   . LEU   A 1 93  ? 14.653  -2.824  123.310 1.00 45.08  ? 1003 LEU   A CD2   1 
ATOM   672  N  N     . GLN   A 1 94  ? 11.252  -2.604  126.595 1.00 58.60  ? 1004 GLN   A N     1 
ATOM   673  C  CA    . GLN   A 1 94  ? 10.412  -2.524  127.784 1.00 63.06  ? 1004 GLN   A CA    1 
ATOM   674  C  C     . GLN   A 1 94  ? 10.527  -1.159  128.449 1.00 62.63  ? 1004 GLN   A C     1 
ATOM   675  O  O     . GLN   A 1 94  ? 9.541   -0.631  128.978 1.00 64.38  ? 1004 GLN   A O     1 
ATOM   676  C  CB    . GLN   A 1 94  ? 10.809  -3.635  128.753 1.00 67.18  ? 1004 GLN   A CB    1 
ATOM   677  C  CG    . GLN   A 1 94  ? 9.838   -3.935  129.872 1.00 71.89  ? 1004 GLN   A CG    1 
ATOM   678  C  CD    . GLN   A 1 94  ? 10.190  -5.242  130.570 1.00 78.87  ? 1004 GLN   A CD    1 
ATOM   679  O  OE1   . GLN   A 1 94  ? 11.197  -5.870  130.246 1.00 86.17  ? 1004 GLN   A OE1   1 
ATOM   680  N  NE2   . GLN   A 1 94  ? 9.365   -5.658  131.524 1.00 77.73  ? 1004 GLN   A NE2   1 
ATOM   681  N  N     . GLU   A 1 95  ? 11.718  -0.562  128.411 1.00 59.29  ? 1005 GLU   A N     1 
ATOM   682  C  CA    . GLU   A 1 95  ? 11.988  0.705   129.077 1.00 59.05  ? 1005 GLU   A CA    1 
ATOM   683  C  C     . GLU   A 1 95  ? 11.463  1.917   128.306 1.00 57.52  ? 1005 GLU   A C     1 
ATOM   684  O  O     . GLU   A 1 95  ? 11.679  3.051   128.749 1.00 56.30  ? 1005 GLU   A O     1 
ATOM   685  C  CB    . GLU   A 1 95  ? 13.502  0.846   129.317 1.00 62.03  ? 1005 GLU   A CB    1 
ATOM   686  C  CG    . GLU   A 1 95  ? 14.302  1.236   128.080 1.00 58.20  ? 1005 GLU   A CG    1 
ATOM   687  C  CD    . GLU   A 1 95  ? 15.778  0.875   128.179 1.00 67.72  ? 1005 GLU   A CD    1 
ATOM   688  O  OE1   . GLU   A 1 95  ? 16.087  -0.308  128.445 1.00 67.12  ? 1005 GLU   A OE1   1 
ATOM   689  O  OE2   . GLU   A 1 95  ? 16.633  1.773   127.982 1.00 68.93  ? 1005 GLU   A OE2   1 
ATOM   690  N  N     . PHE   A 1 96  ? 10.781  1.708   127.178 1.00 57.88  ? 1006 PHE   A N     1 
ATOM   691  C  CA    . PHE   A 1 96  ? 10.310  2.815   126.352 1.00 54.75  ? 1006 PHE   A CA    1 
ATOM   692  C  C     . PHE   A 1 96  ? 9.309   3.673   127.119 1.00 55.91  ? 1006 PHE   A C     1 
ATOM   693  O  O     . PHE   A 1 96  ? 8.326   3.166   127.665 1.00 57.32  ? 1006 PHE   A O     1 
ATOM   694  C  CB    . PHE   A 1 96  ? 9.683   2.278   125.059 1.00 48.35  ? 1006 PHE   A CB    1 
ATOM   695  C  CG    . PHE   A 1 96  ? 9.130   3.350   124.153 1.00 47.73  ? 1006 PHE   A CG    1 
ATOM   696  C  CD1   . PHE   A 1 96  ? 9.953   4.016   123.257 1.00 48.54  ? 1006 PHE   A CD1   1 
ATOM   697  C  CD2   . PHE   A 1 96  ? 7.779   3.684   124.188 1.00 51.14  ? 1006 PHE   A CD2   1 
ATOM   698  C  CE1   . PHE   A 1 96  ? 9.446   5.002   122.416 1.00 48.32  ? 1006 PHE   A CE1   1 
ATOM   699  C  CE2   . PHE   A 1 96  ? 7.268   4.663   123.355 1.00 48.39  ? 1006 PHE   A CE2   1 
ATOM   700  C  CZ    . PHE   A 1 96  ? 8.100   5.324   122.470 1.00 48.36  ? 1006 PHE   A CZ    1 
ATOM   701  N  N     . ASN   A 1 97  ? 9.573   4.980   127.161 1.00 56.30  ? 1007 ASN   A N     1 
ATOM   702  C  CA    . ASN   A 1 97  ? 8.712   5.937   127.845 1.00 56.38  ? 1007 ASN   A CA    1 
ATOM   703  C  C     . ASN   A 1 97  ? 7.324   5.917   127.228 1.00 56.74  ? 1007 ASN   A C     1 
ATOM   704  O  O     . ASN   A 1 97  ? 7.114   6.486   126.154 1.00 55.65  ? 1007 ASN   A O     1 
ATOM   705  C  CB    . ASN   A 1 97  ? 9.307   7.341   127.762 1.00 58.26  ? 1007 ASN   A CB    1 
ATOM   706  C  CG    . ASN   A 1 97  ? 8.628   8.321   128.690 1.00 59.40  ? 1007 ASN   A CG    1 
ATOM   707  O  OD1   . ASN   A 1 97  ? 7.403   8.425   128.728 1.00 60.00  ? 1007 ASN   A OD1   1 
ATOM   708  N  ND2   . ASN   A 1 97  ? 9.430   9.046   129.455 1.00 59.22  ? 1007 ASN   A ND2   1 
ATOM   709  N  N     . LYS   A 1 98  ? 6.368   5.280   127.901 1.00 60.03  ? 1008 LYS   A N     1 
ATOM   710  C  CA    . LYS   A 1 98  ? 5.054   5.072   127.298 1.00 62.55  ? 1008 LYS   A CA    1 
ATOM   711  C  C     . LYS   A 1 98  ? 4.120   6.255   127.525 1.00 61.47  ? 1008 LYS   A C     1 
ATOM   712  O  O     . LYS   A 1 98  ? 3.293   6.565   126.658 1.00 58.25  ? 1008 LYS   A O     1 
ATOM   713  C  CB    . LYS   A 1 98  ? 4.432   3.778   127.831 1.00 61.63  ? 1008 LYS   A CB    1 
ATOM   714  C  CG    . LYS   A 1 98  ? 5.128   2.525   127.321 1.00 61.52  ? 1008 LYS   A CG    1 
ATOM   715  C  CD    . LYS   A 1 98  ? 5.354   1.515   128.442 1.00 64.68  ? 1008 LYS   A CD    1 
ATOM   716  C  CE    . LYS   A 1 98  ? 6.005   0.238   127.919 1.00 63.83  ? 1008 LYS   A CE    1 
ATOM   717  N  NZ    . LYS   A 1 98  ? 6.228   -0.757  129.008 1.00 62.42  ? 1008 LYS   A NZ    1 
ATOM   718  N  N     . ILE   A 1 99  ? 4.222   6.913   128.681 1.00 63.11  ? 1009 ILE   A N     1 
ATOM   719  C  CA    . ILE   A 1 99  ? 3.422   8.110   128.930 1.00 63.67  ? 1009 ILE   A CA    1 
ATOM   720  C  C     . ILE   A 1 99  ? 3.745   9.176   127.893 1.00 64.97  ? 1009 ILE   A C     1 
ATOM   721  O  O     . ILE   A 1 99  ? 2.873   9.632   127.146 1.00 64.51  ? 1009 ILE   A O     1 
ATOM   722  C  CB    . ILE   A 1 99  ? 3.664   8.638   130.354 1.00 65.69  ? 1009 ILE   A CB    1 
ATOM   723  C  CG1   . ILE   A 1 99  ? 3.195   7.640   131.406 1.00 64.99  ? 1009 ILE   A CG1   1 
ATOM   724  C  CG2   . ILE   A 1 99  ? 2.966   9.971   130.538 1.00 68.40  ? 1009 ILE   A CG2   1 
ATOM   725  C  CD1   . ILE   A 1 99  ? 3.626   8.011   132.813 1.00 65.15  ? 1009 ILE   A CD1   1 
ATOM   726  N  N     . GLU   A 1 100 ? 5.012   9.593   127.840 1.00 62.03  ? 1010 GLU   A N     1 
ATOM   727  C  CA    . GLU   A 1 100 ? 5.471   10.633  126.923 1.00 65.58  ? 1010 GLU   A CA    1 
ATOM   728  C  C     . GLU   A 1 100 ? 6.534   10.032  126.005 1.00 61.06  ? 1010 GLU   A C     1 
ATOM   729  O  O     . GLU   A 1 100 ? 7.734   10.085  126.302 1.00 57.70  ? 1010 GLU   A O     1 
ATOM   730  C  CB    . GLU   A 1 100 ? 6.007   11.844  127.686 1.00 68.52  ? 1010 GLU   A CB    1 
ATOM   731  C  CG    . GLU   A 1 100 ? 5.791   13.151  126.946 1.00 72.88  ? 1010 GLU   A CG    1 
ATOM   732  C  CD    . GLU   A 1 100 ? 4.372   13.270  126.405 1.00 74.26  ? 1010 GLU   A CD    1 
ATOM   733  O  OE1   . GLU   A 1 100 ? 3.416   13.209  127.210 1.00 74.29  ? 1010 GLU   A OE1   1 
ATOM   734  O  OE2   . GLU   A 1 100 ? 4.214   13.401  125.171 1.00 74.09  ? 1010 GLU   A OE2   1 
ATOM   735  N  N     . PRO   A 1 101 ? 6.115   9.434   124.885 1.00 59.50  ? 1011 PRO   A N     1 
ATOM   736  C  CA    . PRO   A 1 101 ? 7.107   8.844   123.983 1.00 50.95  ? 1011 PRO   A CA    1 
ATOM   737  C  C     . PRO   A 1 101 ? 7.990   9.902   123.376 1.00 50.87  ? 1011 PRO   A C     1 
ATOM   738  O  O     . PRO   A 1 101 ? 7.583   11.065  123.215 1.00 49.88  ? 1011 PRO   A O     1 
ATOM   739  C  CB    . PRO   A 1 101 ? 6.219   8.167   122.909 1.00 49.38  ? 1011 PRO   A CB    1 
ATOM   740  C  CG    . PRO   A 1 101 ? 4.864   8.839   123.033 1.00 48.73  ? 1011 PRO   A CG    1 
ATOM   741  C  CD    . PRO   A 1 101 ? 4.729   9.184   124.476 1.00 53.73  ? 1011 PRO   A CD    1 
ATOM   742  N  N     . PRO   A 1 102 ? 9.231   9.558   123.024 1.00 48.37  ? 1012 PRO   A N     1 
ATOM   743  C  CA    . PRO   A 1 102 ? 10.060  10.462  122.225 1.00 45.93  ? 1012 PRO   A CA    1 
ATOM   744  C  C     . PRO   A 1 102 ? 9.797   10.249  120.743 1.00 43.81  ? 1012 PRO   A C     1 
ATOM   745  O  O     . PRO   A 1 102 ? 9.408   9.163   120.311 1.00 45.66  ? 1012 PRO   A O     1 
ATOM   746  C  CB    . PRO   A 1 102 ? 11.483  10.027  122.598 1.00 50.98  ? 1012 PRO   A CB    1 
ATOM   747  C  CG    . PRO   A 1 102 ? 11.345  8.534   122.787 1.00 48.93  ? 1012 PRO   A CG    1 
ATOM   748  C  CD    . PRO   A 1 102 ? 9.951   8.321   123.379 1.00 47.50  ? 1012 PRO   A CD    1 
ATOM   749  N  N     . LEU   A 1 103 ? 9.999   11.309  119.957 1.00 39.85  ? 1013 LEU   A N     1 
ATOM   750  C  CA    . LEU   A 1 103 ? 9.825   11.172  118.516 1.00 35.33  ? 1013 LEU   A CA    1 
ATOM   751  C  C     . LEU   A 1 103 ? 10.720  10.056  117.983 1.00 37.73  ? 1013 LEU   A C     1 
ATOM   752  O  O     . LEU   A 1 103 ? 11.822  9.824   118.484 1.00 39.69  ? 1013 LEU   A O     1 
ATOM   753  C  CB    . LEU   A 1 103 ? 10.140  12.482  117.798 1.00 31.80  ? 1013 LEU   A CB    1 
ATOM   754  C  CG    . LEU   A 1 103 ? 9.353   13.755  118.125 1.00 39.66  ? 1013 LEU   A CG    1 
ATOM   755  C  CD1   . LEU   A 1 103 ? 9.945   14.930  117.355 1.00 33.41  ? 1013 LEU   A CD1   1 
ATOM   756  C  CD2   . LEU   A 1 103 ? 7.859   13.619  117.840 1.00 33.13  ? 1013 LEU   A CD2   1 
ATOM   757  N  N     . ILE   A 1 104 ? 10.228  9.339   116.975 1.00 35.37  ? 1014 ILE   A N     1 
ATOM   758  C  CA    . ILE   A 1 104 ? 10.955  8.220   116.385 1.00 35.94  ? 1014 ILE   A CA    1 
ATOM   759  C  C     . ILE   A 1 104 ? 11.311  8.562   114.947 1.00 34.86  ? 1014 ILE   A C     1 
ATOM   760  O  O     . ILE   A 1 104 ? 10.420  8.801   114.120 1.00 31.53  ? 1014 ILE   A O     1 
ATOM   761  C  CB    . ILE   A 1 104 ? 10.148  6.918   116.427 1.00 35.38  ? 1014 ILE   A CB    1 
ATOM   762  C  CG1   . ILE   A 1 104 ? 10.030  6.388   117.853 1.00 34.81  ? 1014 ILE   A CG1   1 
ATOM   763  C  CG2   . ILE   A 1 104 ? 10.803  5.904   115.505 1.00 35.02  ? 1014 ILE   A CG2   1 
ATOM   764  C  CD1   . ILE   A 1 104 ? 9.476   4.965   117.914 1.00 38.07  ? 1014 ILE   A CD1   1 
ATOM   765  N  N     . PHE   A 1 105 ? 12.614  8.548   114.640 1.00 36.24  ? 1015 PHE   A N     1 
ATOM   766  C  CA    . PHE   A 1 105 ? 13.125  8.779   113.290 1.00 32.73  ? 1015 PHE   A CA    1 
ATOM   767  C  C     . PHE   A 1 105 ? 13.619  7.457   112.726 1.00 33.51  ? 1015 PHE   A C     1 
ATOM   768  O  O     . PHE   A 1 105 ? 14.712  6.997   113.072 1.00 36.88  ? 1015 PHE   A O     1 
ATOM   769  C  CB    . PHE   A 1 105 ? 14.224  9.832   113.302 1.00 36.05  ? 1015 PHE   A CB    1 
ATOM   770  C  CG    . PHE   A 1 105 ? 13.710  11.198  113.593 1.00 31.67  ? 1015 PHE   A CG    1 
ATOM   771  C  CD1   . PHE   A 1 105 ? 13.424  11.571  114.888 1.00 33.18  ? 1015 PHE   A CD1   1 
ATOM   772  C  CD2   . PHE   A 1 105 ? 13.450  12.079  112.565 1.00 28.45  ? 1015 PHE   A CD2   1 
ATOM   773  C  CE1   . PHE   A 1 105 ? 12.917  12.805  115.155 1.00 31.33  ? 1015 PHE   A CE1   1 
ATOM   774  C  CE2   . PHE   A 1 105 ? 12.939  13.308  112.817 1.00 29.24  ? 1015 PHE   A CE2   1 
ATOM   775  C  CZ    . PHE   A 1 105 ? 12.674  13.680  114.117 1.00 32.25  ? 1015 PHE   A CZ    1 
ATOM   776  N  N     . GLU   A 1 106 ? 12.804  6.856   111.862 1.00 27.94  ? 1016 GLU   A N     1 
ATOM   777  C  CA    . GLU   A 1 106 ? 13.144  5.635   111.158 1.00 30.72  ? 1016 GLU   A CA    1 
ATOM   778  C  C     . GLU   A 1 106 ? 14.030  5.965   109.963 1.00 34.26  ? 1016 GLU   A C     1 
ATOM   779  O  O     . GLU   A 1 106 ? 13.990  7.079   109.425 1.00 33.74  ? 1016 GLU   A O     1 
ATOM   780  C  CB    . GLU   A 1 106 ? 11.874  4.887   110.699 1.00 31.72  ? 1016 GLU   A CB    1 
ATOM   781  C  CG    . GLU   A 1 106 ? 11.195  4.061   111.811 1.00 30.19  ? 1016 GLU   A CG    1 
ATOM   782  C  CD    . GLU   A 1 106 ? 10.128  3.060   111.314 1.00 32.53  ? 1016 GLU   A CD    1 
ATOM   783  O  OE1   . GLU   A 1 106 ? 10.005  2.815   110.089 1.00 31.24  ? 1016 GLU   A OE1   1 
ATOM   784  O  OE2   . GLU   A 1 106 ? 9.396   2.524   112.177 1.00 32.85  ? 1016 GLU   A OE2   1 
ATOM   785  N  N     . CYS   A 1 107 ? 14.840  4.986   109.560 1.00 31.13  ? 1017 CYS   A N     1 
ATOM   786  C  CA    . CYS   A 1 107 ? 15.775  5.167   108.452 1.00 31.92  ? 1017 CYS   A CA    1 
ATOM   787  C  C     . CYS   A 1 107 ? 14.987  5.323   107.153 1.00 33.35  ? 1017 CYS   A C     1 
ATOM   788  O  O     . CYS   A 1 107 ? 13.870  4.808   107.026 1.00 33.59  ? 1017 CYS   A O     1 
ATOM   789  C  CB    . CYS   A 1 107 ? 16.731  3.966   108.357 1.00 28.40  ? 1017 CYS   A CB    1 
ATOM   790  S  SG    . CYS   A 1 107 ? 18.081  3.820   109.619 1.00 40.10  ? 1017 CYS   A SG    1 
ATOM   791  N  N     . ASN   A 1 108 ? 15.573  6.021   106.173 1.00 29.52  ? 1018 ASN   A N     1 
ATOM   792  C  CA    . ASN   A 1 108 ? 14.811  6.470   105.002 1.00 30.80  ? 1018 ASN   A CA    1 
ATOM   793  C  C     . ASN   A 1 108 ? 15.594  6.199   103.712 1.00 30.73  ? 1018 ASN   A C     1 
ATOM   794  O  O     . ASN   A 1 108 ? 16.666  5.586   103.715 1.00 32.61  ? 1018 ASN   A O     1 
ATOM   795  C  CB    . ASN   A 1 108 ? 14.472  7.959   105.138 1.00 32.45  ? 1018 ASN   A CB    1 
ATOM   796  C  CG    . ASN   A 1 108 ? 15.699  8.788   105.403 1.00 32.12  ? 1018 ASN   A CG    1 
ATOM   797  O  OD1   . ASN   A 1 108 ? 16.569  8.922   104.530 1.00 32.09  ? 1018 ASN   A OD1   1 
ATOM   798  N  ND2   . ASN   A 1 108 ? 15.808  9.314   106.620 1.00 29.54  ? 1018 ASN   A ND2   1 
ATOM   799  N  N     . GLN   A 1 109 ? 15.053  6.688   102.590 1.00 30.90  ? 1019 GLN   A N     1 
ATOM   800  C  CA    . GLN   A 1 109 ? 15.670  6.481   101.284 1.00 30.12  ? 1019 GLN   A CA    1 
ATOM   801  C  C     . GLN   A 1 109 ? 16.938  7.292   101.070 1.00 28.76  ? 1019 GLN   A C     1 
ATOM   802  O  O     . GLN   A 1 109 ? 17.540  7.150   100.005 1.00 32.18  ? 1019 GLN   A O     1 
ATOM   803  C  CB    . GLN   A 1 109 ? 14.688  6.803   100.161 1.00 28.55  ? 1019 GLN   A CB    1 
ATOM   804  C  CG    . GLN   A 1 109 ? 14.245  8.269   100.077 1.00 28.47  ? 1019 GLN   A CG    1 
ATOM   805  C  CD    . GLN   A 1 109 ? 13.145  8.631   101.063 1.00 30.73  ? 1019 GLN   A CD    1 
ATOM   806  O  OE1   . GLN   A 1 109 ? 12.790  7.841   101.946 1.00 32.20  ? 1019 GLN   A OE1   1 
ATOM   807  N  NE2   . GLN   A 1 109 ? 12.594  9.837   100.914 1.00 28.91  ? 1019 GLN   A NE2   1 
ATOM   808  N  N     . ALA   A 1 110 ? 17.349  8.149   102.001 1.00 28.52  ? 1020 ALA   A N     1 
ATOM   809  C  CA    . ALA   A 1 110 ? 18.673  8.758   101.893 1.00 34.48  ? 1020 ALA   A CA    1 
ATOM   810  C  C     . ALA   A 1 110 ? 19.721  8.039   102.728 1.00 34.10  ? 1020 ALA   A C     1 
ATOM   811  O  O     . ALA   A 1 110 ? 20.913  8.309   102.558 1.00 39.04  ? 1020 ALA   A O     1 
ATOM   812  C  CB    . ALA   A 1 110 ? 18.640  10.242  102.290 1.00 29.78  ? 1020 ALA   A CB    1 
ATOM   813  N  N     . CYS   A 1 111 ? 19.305  7.157   103.636 1.00 30.97  ? 1021 CYS   A N     1 
ATOM   814  C  CA    . CYS   A 1 111 ? 20.246  6.358   104.393 1.00 30.58  ? 1021 CYS   A CA    1 
ATOM   815  C  C     . CYS   A 1 111 ? 21.027  5.450   103.458 1.00 35.12  ? 1021 CYS   A C     1 
ATOM   816  O  O     . CYS   A 1 111 ? 20.514  4.982   102.438 1.00 36.27  ? 1021 CYS   A O     1 
ATOM   817  C  CB    . CYS   A 1 111 ? 19.526  5.517   105.436 1.00 34.27  ? 1021 CYS   A CB    1 
ATOM   818  S  SG    . CYS   A 1 111 ? 18.745  6.474   106.718 1.00 29.34  ? 1021 CYS   A SG    1 
ATOM   819  N  N     . SER   A 1 112 ? 22.292  5.224   103.801 1.00 32.21  ? 1022 SER   A N     1 
ATOM   820  C  CA    . SER   A 1 112 ? 23.081  4.253   103.059 1.00 38.76  ? 1022 SER   A CA    1 
ATOM   821  C  C     . SER   A 1 112 ? 22.730  2.819   103.437 1.00 35.59  ? 1022 SER   A C     1 
ATOM   822  O  O     . SER   A 1 112 ? 23.065  1.897   102.683 1.00 37.59  ? 1022 SER   A O     1 
ATOM   823  C  CB    . SER   A 1 112 ? 24.579  4.515   103.267 1.00 35.29  ? 1022 SER   A CB    1 
ATOM   824  O  OG    . SER   A 1 112 ? 24.939  4.372   104.629 1.00 35.56  ? 1022 SER   A OG    1 
ATOM   825  N  N     . CYS   A 1 113 ? 22.048  2.619   104.565 1.00 32.73  ? 1023 CYS   A N     1 
ATOM   826  C  CA    . CYS   A 1 113 ? 21.668  1.292   105.029 1.00 34.01  ? 1023 CYS   A CA    1 
ATOM   827  C  C     . CYS   A 1 113 ? 20.714  0.620   104.053 1.00 36.59  ? 1023 CYS   A C     1 
ATOM   828  O  O     . CYS   A 1 113 ? 20.312  1.214   103.050 1.00 36.14  ? 1023 CYS   A O     1 
ATOM   829  C  CB    . CYS   A 1 113 ? 21.026  1.376   106.410 1.00 32.04  ? 1023 CYS   A CB    1 
ATOM   830  S  SG    . CYS   A 1 113 ? 19.361  2.173   106.438 1.00 30.09  ? 1023 CYS   A SG    1 
ATOM   831  N  N     . TRP   A 1 114 ? 20.365  -0.630  104.315 1.00 36.27  ? 1024 TRP   A N     1 
ATOM   832  C  CA    . TRP   A 1 114 ? 19.422  -1.324  103.450 1.00 35.97  ? 1024 TRP   A CA    1 
ATOM   833  C  C     . TRP   A 1 114 ? 17.990  -1.128  103.951 1.00 36.38  ? 1024 TRP   A C     1 
ATOM   834  O  O     . TRP   A 1 114 ? 17.753  -0.744  105.101 1.00 35.44  ? 1024 TRP   A O     1 
ATOM   835  C  CB    . TRP   A 1 114 ? 19.753  -2.816  103.376 1.00 36.80  ? 1024 TRP   A CB    1 
ATOM   836  C  CG    . TRP   A 1 114 ? 20.859  -3.144  102.431 1.00 41.97  ? 1024 TRP   A CG    1 
ATOM   837  C  CD1   . TRP   A 1 114 ? 22.014  -2.439  102.235 1.00 40.79  ? 1024 TRP   A CD1   1 
ATOM   838  C  CD2   . TRP   A 1 114 ? 20.913  -4.262  101.541 1.00 38.37  ? 1024 TRP   A CD2   1 
ATOM   839  N  NE1   . TRP   A 1 114 ? 22.786  -3.062  101.278 1.00 44.89  ? 1024 TRP   A NE1   1 
ATOM   840  C  CE2   . TRP   A 1 114 ? 22.127  -4.179  100.836 1.00 41.16  ? 1024 TRP   A CE2   1 
ATOM   841  C  CE3   . TRP   A 1 114 ? 20.047  -5.324  101.273 1.00 39.90  ? 1024 TRP   A CE3   1 
ATOM   842  C  CZ2   . TRP   A 1 114 ? 22.504  -5.123  99.885  1.00 42.11  ? 1024 TRP   A CZ2   1 
ATOM   843  C  CZ3   . TRP   A 1 114 ? 20.413  -6.250  100.330 1.00 41.16  ? 1024 TRP   A CZ3   1 
ATOM   844  C  CH2   . TRP   A 1 114 ? 21.640  -6.149  99.647  1.00 42.70  ? 1024 TRP   A CH2   1 
ATOM   845  N  N     . ARG   A 1 115 ? 17.034  -1.400  103.060 1.00 33.43  ? 1025 ARG   A N     1 
ATOM   846  C  CA    . ARG   A 1 115 ? 15.611  -1.291  103.375 1.00 36.87  ? 1025 ARG   A CA    1 
ATOM   847  C  C     . ARG   A 1 115 ? 15.149  -2.279  104.446 1.00 40.72  ? 1025 ARG   A C     1 
ATOM   848  O  O     . ARG   A 1 115 ? 14.016  -2.155  104.918 1.00 38.89  ? 1025 ARG   A O     1 
ATOM   849  C  CB    . ARG   A 1 115 ? 14.802  -1.487  102.086 1.00 36.62  ? 1025 ARG   A CB    1 
ATOM   850  C  CG    . ARG   A 1 115 ? 13.275  -1.343  102.185 1.00 34.26  ? 1025 ARG   A CG    1 
ATOM   851  C  CD    . ARG   A 1 115 ? 12.868  -0.057  102.859 1.00 37.28  ? 1025 ARG   A CD    1 
ATOM   852  N  NE    . ARG   A 1 115 ? 11.435  0.198   102.757 1.00 37.19  ? 1025 ARG   A NE    1 
ATOM   853  C  CZ    . ARG   A 1 115 ? 10.516  -0.422  103.485 1.00 36.35  ? 1025 ARG   A CZ    1 
ATOM   854  N  NH1   . ARG   A 1 115 ? 10.844  -1.358  104.359 1.00 33.91  ? 1025 ARG   A NH1   1 
ATOM   855  N  NH2   . ARG   A 1 115 ? 9.237   -0.086  103.339 1.00 39.26  ? 1025 ARG   A NH2   1 
ATOM   856  N  N     . ASN   A 1 116 ? 15.970  -3.263  104.843 1.00 43.15  ? 1026 ASN   A N     1 
ATOM   857  C  CA    . ASN   A 1 116 ? 15.549  -4.261  105.826 1.00 44.17  ? 1026 ASN   A CA    1 
ATOM   858  C  C     . ASN   A 1 116 ? 16.313  -4.153  107.147 1.00 39.90  ? 1026 ASN   A C     1 
ATOM   859  O  O     . ASN   A 1 116 ? 16.496  -5.152  107.844 1.00 40.83  ? 1026 ASN   A O     1 
ATOM   860  C  CB    . ASN   A 1 116 ? 15.672  -5.677  105.257 1.00 45.84  ? 1026 ASN   A CB    1 
ATOM   861  C  CG    . ASN   A 1 116 ? 17.116  -6.103  105.060 1.00 51.25  ? 1026 ASN   A CG    1 
ATOM   862  O  OD1   . ASN   A 1 116 ? 18.002  -5.266  104.910 1.00 46.86  ? 1026 ASN   A OD1   1 
ATOM   863  N  ND2   . ASN   A 1 116 ? 17.358  -7.416  105.056 1.00 57.23  ? 1026 ASN   A ND2   1 
ATOM   864  N  N     . CYS   A 1 117 ? 16.716  -2.946  107.528 1.00 40.26  ? 1027 CYS   A N     1 
ATOM   865  C  CA    . CYS   A 1 117 ? 17.486  -2.741  108.743 1.00 37.89  ? 1027 CYS   A CA    1 
ATOM   866  C  C     . CYS   A 1 117 ? 16.564  -2.656  109.958 1.00 37.66  ? 1027 CYS   A C     1 
ATOM   867  O  O     . CYS   A 1 117 ? 15.333  -2.641  109.845 1.00 41.24  ? 1027 CYS   A O     1 
ATOM   868  C  CB    . CYS   A 1 117 ? 18.347  -1.485  108.617 1.00 37.93  ? 1027 CYS   A CB    1 
ATOM   869  S  SG    . CYS   A 1 117 ? 17.437  0.074   108.755 1.00 39.99  ? 1027 CYS   A SG    1 
ATOM   870  N  N     . LYS   A 1 118 ? 17.174  -2.590  111.145 1.00 35.71  ? 1028 LYS   A N     1 
ATOM   871  C  CA    . LYS   A 1 118 ? 16.401  -2.688  112.383 1.00 36.35  ? 1028 LYS   A CA    1 
ATOM   872  C  C     . LYS   A 1 118 ? 15.528  -1.465  112.668 1.00 38.04  ? 1028 LYS   A C     1 
ATOM   873  O  O     . LYS   A 1 118 ? 14.759  -1.497  113.636 1.00 38.03  ? 1028 LYS   A O     1 
ATOM   874  C  CB    . LYS   A 1 118 ? 17.337  -2.915  113.570 1.00 37.91  ? 1028 LYS   A CB    1 
ATOM   875  C  CG    . LYS   A 1 118 ? 17.994  -4.284  113.583 1.00 46.66  ? 1028 LYS   A CG    1 
ATOM   876  C  CD    . LYS   A 1 118 ? 16.963  -5.414  113.628 1.00 49.31  ? 1028 LYS   A CD    1 
ATOM   877  C  CE    . LYS   A 1 118 ? 17.670  -6.759  113.871 1.00 56.39  ? 1028 LYS   A CE    1 
ATOM   878  N  NZ    . LYS   A 1 118 ? 16.712  -7.897  113.988 1.00 58.57  ? 1028 LYS   A NZ    1 
ATOM   879  N  N     . ASN   A 1 119 ? 15.627  -0.401  111.869 1.00 33.74  ? 1029 ASN   A N     1 
ATOM   880  C  CA    . ASN   A 1 119 ? 14.934  0.844   112.159 1.00 34.65  ? 1029 ASN   A CA    1 
ATOM   881  C  C     . ASN   A 1 119 ? 13.874  1.102   111.092 1.00 33.72  ? 1029 ASN   A C     1 
ATOM   882  O  O     . ASN   A 1 119 ? 13.835  2.190   110.510 1.00 33.81  ? 1029 ASN   A O     1 
ATOM   883  C  CB    . ASN   A 1 119 ? 15.944  1.992   112.223 1.00 32.97  ? 1029 ASN   A CB    1 
ATOM   884  C  CG    . ASN   A 1 119 ? 15.459  3.187   113.031 1.00 36.18  ? 1029 ASN   A CG    1 
ATOM   885  O  OD1   . ASN   A 1 119 ? 14.759  3.057   114.038 1.00 34.93  ? 1029 ASN   A OD1   1 
ATOM   886  N  ND2   . ASN   A 1 119 ? 15.869  4.374   112.598 1.00 33.96  ? 1029 ASN   A ND2   1 
ATOM   887  N  N     . ARG   A 1 120 ? 13.027  0.104   110.810 1.00 31.47  ? 1030 ARG   A N     1 
ATOM   888  C  CA    . ARG   A 1 120 ? 12.056  0.222   109.725 1.00 31.88  ? 1030 ARG   A CA    1 
ATOM   889  C  C     . ARG   A 1 120 ? 10.751  -0.500  110.069 1.00 32.17  ? 1030 ARG   A C     1 
ATOM   890  O  O     . ARG   A 1 120 ? 10.128  -1.143  109.212 1.00 28.95  ? 1030 ARG   A O     1 
ATOM   891  C  CB    . ARG   A 1 120 ? 12.650  -0.280  108.408 1.00 29.51  ? 1030 ARG   A CB    1 
ATOM   892  C  CG    . ARG   A 1 120 ? 13.690  0.700   107.870 1.00 33.22  ? 1030 ARG   A CG    1 
ATOM   893  C  CD    . ARG   A 1 120 ? 14.222  0.339   106.506 1.00 37.31  ? 1030 ARG   A CD    1 
ATOM   894  N  NE    . ARG   A 1 120 ? 15.445  1.067   106.185 1.00 31.95  ? 1030 ARG   A NE    1 
ATOM   895  C  CZ    . ARG   A 1 120 ? 15.505  2.120   105.383 1.00 33.49  ? 1030 ARG   A CZ    1 
ATOM   896  N  NH1   . ARG   A 1 120 ? 14.420  2.619   104.804 1.00 32.98  ? 1030 ARG   A NH1   1 
ATOM   897  N  NH2   . ARG   A 1 120 ? 16.683  2.694   105.158 1.00 33.63  ? 1030 ARG   A NH2   1 
ATOM   898  N  N     . VAL   A 1 121 ? 10.302  -0.367  111.319 1.00 29.73  ? 1031 VAL   A N     1 
ATOM   899  C  CA    . VAL   A 1 121 ? 9.125   -1.107  111.761 1.00 31.77  ? 1031 VAL   A CA    1 
ATOM   900  C  C     . VAL   A 1 121 ? 7.861   -0.518  111.150 1.00 29.23  ? 1031 VAL   A C     1 
ATOM   901  O  O     . VAL   A 1 121 ? 7.162   -1.169  110.362 1.00 26.03  ? 1031 VAL   A O     1 
ATOM   902  C  CB    . VAL   A 1 121 ? 9.035   -1.126  113.294 1.00 32.24  ? 1031 VAL   A CB    1 
ATOM   903  C  CG1   . VAL   A 1 121 ? 7.672   -1.685  113.716 1.00 24.72  ? 1031 VAL   A CG1   1 
ATOM   904  C  CG2   . VAL   A 1 121 ? 10.175  -1.944  113.874 1.00 31.27  ? 1031 VAL   A CG2   1 
ATOM   905  N  N     . VAL   A 1 122 ? 7.553   0.729   111.501 1.00 28.03  ? 1032 VAL   A N     1 
ATOM   906  C  CA    . VAL   A 1 122 ? 6.250   1.270   111.148 1.00 28.62  ? 1032 VAL   A CA    1 
ATOM   907  C  C     . VAL   A 1 122 ? 6.095   1.338   109.638 1.00 28.78  ? 1032 VAL   A C     1 
ATOM   908  O  O     . VAL   A 1 122 ? 5.056   0.938   109.089 1.00 30.39  ? 1032 VAL   A O     1 
ATOM   909  C  CB    . VAL   A 1 122 ? 6.044   2.631   111.827 1.00 29.10  ? 1032 VAL   A CB    1 
ATOM   910  C  CG1   . VAL   A 1 122 ? 4.679   3.231   111.442 1.00 24.33  ? 1032 VAL   A CG1   1 
ATOM   911  C  CG2   . VAL   A 1 122 ? 6.153   2.442   113.327 1.00 28.53  ? 1032 VAL   A CG2   1 
ATOM   912  N  N     . GLN   A 1 123 ? 7.140   1.782   108.939 1.00 26.57  ? 1033 GLN   A N     1 
ATOM   913  C  CA    . GLN   A 1 123 ? 7.096   1.845   107.481 1.00 28.86  ? 1033 GLN   A CA    1 
ATOM   914  C  C     . GLN   A 1 123 ? 6.898   0.483   106.829 1.00 32.33  ? 1033 GLN   A C     1 
ATOM   915  O  O     . GLN   A 1 123 ? 6.583   0.434   105.632 1.00 34.55  ? 1033 GLN   A O     1 
ATOM   916  C  CB    . GLN   A 1 123 ? 8.373   2.500   106.929 1.00 28.88  ? 1033 GLN   A CB    1 
ATOM   917  C  CG    . GLN   A 1 123 ? 9.646   1.659   107.024 1.00 31.05  ? 1033 GLN   A CG    1 
ATOM   918  C  CD    . GLN   A 1 123 ? 10.910  2.494   106.797 1.00 29.06  ? 1033 GLN   A CD    1 
ATOM   919  O  OE1   . GLN   A 1 123 ? 11.413  2.603   105.680 1.00 23.63  ? 1033 GLN   A OE1   1 
ATOM   920  N  NE2   . GLN   A 1 123 ? 11.405  3.099   107.858 1.00 29.81  ? 1033 GLN   A NE2   1 
ATOM   921  N  N     . SER   A 1 124 ? 7.048   -0.617  107.573 1.00 26.89  ? 1034 SER   A N     1 
ATOM   922  C  CA    . SER   A 1 124 ? 6.849   -1.930  106.988 1.00 28.73  ? 1034 SER   A CA    1 
ATOM   923  C  C     . SER   A 1 124 ? 5.402   -2.411  107.033 1.00 31.73  ? 1034 SER   A C     1 
ATOM   924  O  O     . SER   A 1 124 ? 5.102   -3.444  106.433 1.00 35.77  ? 1034 SER   A O     1 
ATOM   925  C  CB    . SER   A 1 124 ? 7.752   -2.956  107.678 1.00 30.49  ? 1034 SER   A CB    1 
ATOM   926  O  OG    . SER   A 1 124 ? 9.118   -2.691  107.385 1.00 31.04  ? 1034 SER   A OG    1 
ATOM   927  N  N     . GLY   A 1 125 ? 4.501   -1.712  107.726 1.00 30.31  ? 1035 GLY   A N     1 
ATOM   928  C  CA    . GLY   A 1 125 ? 3.082   -2.014  107.640 1.00 30.33  ? 1035 GLY   A CA    1 
ATOM   929  C  C     . GLY   A 1 125 ? 2.572   -3.009  108.676 1.00 32.72  ? 1035 GLY   A C     1 
ATOM   930  O  O     . GLY   A 1 125 ? 3.304   -3.542  109.520 1.00 29.99  ? 1035 GLY   A O     1 
ATOM   931  N  N     . ILE   A 1 126 ? 1.256   -3.252  108.584 1.00 31.24  ? 1036 ILE   A N     1 
ATOM   932  C  CA    . ILE   A 1 126 ? 0.557   -4.092  109.550 1.00 31.82  ? 1036 ILE   A CA    1 
ATOM   933  C  C     . ILE   A 1 126 ? 1.034   -5.528  109.408 1.00 31.45  ? 1036 ILE   A C     1 
ATOM   934  O  O     . ILE   A 1 126 ? 1.103   -6.073  108.298 1.00 32.95  ? 1036 ILE   A O     1 
ATOM   935  C  CB    . ILE   A 1 126 ? -0.968  -3.992  109.348 1.00 32.93  ? 1036 ILE   A CB    1 
ATOM   936  C  CG1   . ILE   A 1 126 ? -1.461  -2.592  109.723 1.00 30.15  ? 1036 ILE   A CG1   1 
ATOM   937  C  CG2   . ILE   A 1 126 ? -1.706  -5.068  110.152 1.00 29.86  ? 1036 ILE   A CG2   1 
ATOM   938  C  CD1   . ILE   A 1 126 ? -2.712  -2.199  109.003 1.00 32.68  ? 1036 ILE   A CD1   1 
ATOM   939  N  N     . LYS   A 1 127 ? 1.360   -6.151  110.529 1.00 31.49  ? 1037 LYS   A N     1 
ATOM   940  C  CA    . LYS   A 1 127 ? 1.773   -7.543  110.537 1.00 30.99  ? 1037 LYS   A CA    1 
ATOM   941  C  C     . LYS   A 1 127 ? 0.898   -8.434  111.404 1.00 32.51  ? 1037 LYS   A C     1 
ATOM   942  O  O     . LYS   A 1 127 ? 0.709   -9.607  111.068 1.00 39.50  ? 1037 LYS   A O     1 
ATOM   943  C  CB    . LYS   A 1 127 ? 3.229   -7.672  111.016 1.00 33.35  ? 1037 LYS   A CB    1 
ATOM   944  C  CG    . LYS   A 1 127 ? 4.257   -7.141  110.029 1.00 35.10  ? 1037 LYS   A CG    1 
ATOM   945  C  CD    . LYS   A 1 127 ? 4.201   -7.906  108.716 1.00 40.73  ? 1037 LYS   A CD    1 
ATOM   946  C  CE    . LYS   A 1 127 ? 5.096   -7.263  107.653 1.00 43.63  ? 1037 LYS   A CE    1 
ATOM   947  N  NZ    . LYS   A 1 127 ? 6.457   -6.880  108.133 1.00 43.67  ? 1037 LYS   A NZ    1 
ATOM   948  N  N     . VAL   A 1 128 ? 0.367   -7.928  112.514 1.00 36.04  ? 1038 VAL   A N     1 
ATOM   949  C  CA    . VAL   A 1 128 ? -0.517  -8.740  113.340 1.00 35.35  ? 1038 VAL   A CA    1 
ATOM   950  C  C     . VAL   A 1 128 ? -1.866  -8.893  112.645 1.00 33.81  ? 1038 VAL   A C     1 
ATOM   951  O  O     . VAL   A 1 128 ? -2.270  -8.074  111.809 1.00 33.07  ? 1038 VAL   A O     1 
ATOM   952  C  CB    . VAL   A 1 128 ? -0.685  -8.113  114.737 1.00 36.57  ? 1038 VAL   A CB    1 
ATOM   953  C  CG1   . VAL   A 1 128 ? 0.666   -7.954  115.419 1.00 34.33  ? 1038 VAL   A CG1   1 
ATOM   954  C  CG2   . VAL   A 1 128 ? -1.409  -6.784  114.624 1.00 32.32  ? 1038 VAL   A CG2   1 
ATOM   955  N  N     . ARG   A 1 129 ? -2.577  -9.944  113.005 1.00 38.82  ? 1039 ARG   A N     1 
ATOM   956  C  CA    . ARG   A 1 129 ? -3.889  -10.208 112.434 1.00 32.29  ? 1039 ARG   A CA    1 
ATOM   957  C  C     . ARG   A 1 129 ? -4.944  -9.491  113.265 1.00 33.10  ? 1039 ARG   A C     1 
ATOM   958  O  O     . ARG   A 1 129 ? -5.026  -9.696  114.480 1.00 32.29  ? 1039 ARG   A O     1 
ATOM   959  C  CB    . ARG   A 1 129 ? -4.152  -11.711 112.375 1.00 33.78  ? 1039 ARG   A CB    1 
ATOM   960  C  CG    . ARG   A 1 129 ? -3.170  -12.466 111.474 1.00 36.23  ? 1039 ARG   A CG    1 
ATOM   961  C  CD    . ARG   A 1 129 ? -3.146  -11.893 110.059 1.00 34.41  ? 1039 ARG   A CD    1 
ATOM   962  N  NE    . ARG   A 1 129 ? -4.353  -12.234 109.315 1.00 37.86  ? 1039 ARG   A NE    1 
ATOM   963  C  CZ    . ARG   A 1 129 ? -4.424  -13.224 108.436 1.00 37.94  ? 1039 ARG   A CZ    1 
ATOM   964  N  NH1   . ARG   A 1 129 ? -3.365  -13.955 108.132 1.00 40.29  ? 1039 ARG   A NH1   1 
ATOM   965  N  NH2   . ARG   A 1 129 ? -5.584  -13.486 107.843 1.00 39.27  ? 1039 ARG   A NH2   1 
ATOM   966  N  N     . LEU   A 1 130 ? -5.739  -8.648  112.606 1.00 32.06  ? 1040 LEU   A N     1 
ATOM   967  C  CA    . LEU   A 1 130 ? -6.738  -7.806  113.247 1.00 33.27  ? 1040 LEU   A CA    1 
ATOM   968  C  C     . LEU   A 1 130 ? -8.106  -8.061  112.625 1.00 30.10  ? 1040 LEU   A C     1 
ATOM   969  O  O     . LEU   A 1 130 ? -8.216  -8.460  111.464 1.00 30.44  ? 1040 LEU   A O     1 
ATOM   970  C  CB    . LEU   A 1 130 ? -6.394  -6.315  113.104 1.00 28.30  ? 1040 LEU   A CB    1 
ATOM   971  C  CG    . LEU   A 1 130 ? -5.119  -5.724  113.702 1.00 28.64  ? 1040 LEU   A CG    1 
ATOM   972  C  CD1   . LEU   A 1 130 ? -5.252  -4.187  113.775 1.00 27.90  ? 1040 LEU   A CD1   1 
ATOM   973  C  CD2   . LEU   A 1 130 ? -4.836  -6.310  115.072 1.00 30.36  ? 1040 LEU   A CD2   1 
ATOM   974  N  N     . GLN   A 1 131 ? -9.156  -7.796  113.393 1.00 30.60  ? 1041 GLN   A N     1 
ATOM   975  C  CA    . GLN   A 1 131 ? -10.513 -8.001  112.887 1.00 34.87  ? 1041 GLN   A CA    1 
ATOM   976  C  C     . GLN   A 1 131 ? -11.427 -6.842  113.268 1.00 31.71  ? 1041 GLN   A C     1 
ATOM   977  O  O     . GLN   A 1 131 ? -11.486 -6.453  114.437 1.00 33.53  ? 1041 GLN   A O     1 
ATOM   978  C  CB    . GLN   A 1 131 ? -11.087 -9.310  113.426 1.00 37.84  ? 1041 GLN   A CB    1 
ATOM   979  C  CG    . GLN   A 1 131 ? -12.465 -9.663  112.904 1.00 34.65  ? 1041 GLN   A CG    1 
ATOM   980  C  CD    . GLN   A 1 131 ? -13.010 -10.854 113.605 1.00 36.68  ? 1041 GLN   A CD    1 
ATOM   981  O  OE1   . GLN   A 1 131 ? -13.319 -10.786 114.795 1.00 41.54  ? 1041 GLN   A OE1   1 
ATOM   982  N  NE2   . GLN   A 1 131 ? -13.112 -11.974 112.892 1.00 35.83  ? 1041 GLN   A NE2   1 
ATOM   983  N  N     . LEU   A 1 132 ? -12.138 -6.298  112.288 1.00 32.00  ? 1042 LEU   A N     1 
ATOM   984  C  CA    . LEU   A 1 132 ? -13.255 -5.404  112.582 1.00 37.87  ? 1042 LEU   A CA    1 
ATOM   985  C  C     . LEU   A 1 132 ? -14.449 -6.218  113.062 1.00 34.08  ? 1042 LEU   A C     1 
ATOM   986  O  O     . LEU   A 1 132 ? -14.920 -7.110  112.353 1.00 36.83  ? 1042 LEU   A O     1 
ATOM   987  C  CB    . LEU   A 1 132 ? -13.640 -4.598  111.342 1.00 37.61  ? 1042 LEU   A CB    1 
ATOM   988  C  CG    . LEU   A 1 132 ? -14.663 -3.472  111.503 1.00 33.80  ? 1042 LEU   A CG    1 
ATOM   989  C  CD1   . LEU   A 1 132 ? -14.202 -2.453  112.538 1.00 33.39  ? 1042 LEU   A CD1   1 
ATOM   990  C  CD2   . LEU   A 1 132 ? -14.939 -2.799  110.161 1.00 34.13  ? 1042 LEU   A CD2   1 
ATOM   991  N  N     . TYR   A 1 133 ? -14.946 -5.924  114.260 1.00 35.81  ? 1043 TYR   A N     1 
ATOM   992  C  CA    . TYR   A 1 133 ? -16.149 -6.593  114.739 1.00 38.46  ? 1043 TYR   A CA    1 
ATOM   993  C  C     . TYR   A 1 133 ? -17.110 -5.600  115.396 1.00 38.55  ? 1043 TYR   A C     1 
ATOM   994  O  O     . TYR   A 1 133 ? -16.758 -4.467  115.737 1.00 36.96  ? 1043 TYR   A O     1 
ATOM   995  C  CB    . TYR   A 1 133 ? -15.806 -7.710  115.716 1.00 36.39  ? 1043 TYR   A CB    1 
ATOM   996  C  CG    . TYR   A 1 133 ? -15.454 -7.209  117.094 1.00 41.23  ? 1043 TYR   A CG    1 
ATOM   997  C  CD1   . TYR   A 1 133 ? -14.347 -6.387  117.295 1.00 37.74  ? 1043 TYR   A CD1   1 
ATOM   998  C  CD2   . TYR   A 1 133 ? -16.228 -7.560  118.202 1.00 38.67  ? 1043 TYR   A CD2   1 
ATOM   999  C  CE1   . TYR   A 1 133 ? -14.020 -5.929  118.562 1.00 35.58  ? 1043 TYR   A CE1   1 
ATOM   1000 C  CE2   . TYR   A 1 133 ? -15.903 -7.109  119.471 1.00 38.71  ? 1043 TYR   A CE2   1 
ATOM   1001 C  CZ    . TYR   A 1 133 ? -14.787 -6.295  119.644 1.00 37.08  ? 1043 TYR   A CZ    1 
ATOM   1002 O  OH    . TYR   A 1 133 ? -14.471 -5.845  120.902 1.00 37.66  ? 1043 TYR   A OH    1 
ATOM   1003 N  N     . ARG   A 1 134 ? -18.347 -6.061  115.584 1.00 39.85  ? 1044 ARG   A N     1 
ATOM   1004 C  CA    . ARG   A 1 134 ? -19.407 -5.275  116.208 1.00 40.34  ? 1044 ARG   A CA    1 
ATOM   1005 C  C     . ARG   A 1 134 ? -19.395 -5.509  117.715 1.00 41.05  ? 1044 ARG   A C     1 
ATOM   1006 O  O     . ARG   A 1 134 ? -19.633 -6.631  118.170 1.00 41.61  ? 1044 ARG   A O     1 
ATOM   1007 C  CB    . ARG   A 1 134 ? -20.751 -5.672  115.617 1.00 41.85  ? 1044 ARG   A CB    1 
ATOM   1008 C  CG    . ARG   A 1 134 ? -21.924 -4.798  116.022 1.00 43.70  ? 1044 ARG   A CG    1 
ATOM   1009 C  CD    . ARG   A 1 134 ? -21.846 -3.470  115.315 1.00 43.55  ? 1044 ARG   A CD    1 
ATOM   1010 N  NE    . ARG   A 1 134 ? -23.051 -2.669  115.495 1.00 47.35  ? 1044 ARG   A NE    1 
ATOM   1011 C  CZ    . ARG   A 1 134 ? -23.134 -1.384  115.178 1.00 48.01  ? 1044 ARG   A CZ    1 
ATOM   1012 N  NH1   . ARG   A 1 134 ? -22.088 -0.721  114.699 1.00 44.64  ? 1044 ARG   A NH1   1 
ATOM   1013 N  NH2   . ARG   A 1 134 ? -24.290 -0.747  115.346 1.00 48.45  ? 1044 ARG   A NH2   1 
ATOM   1014 N  N     . THR   A 1 135 ? -19.123 -4.461  118.490 1.00 41.23  ? 1045 THR   A N     1 
ATOM   1015 C  CA    . THR   A 1 135 ? -19.098 -4.613  119.938 1.00 42.19  ? 1045 THR   A CA    1 
ATOM   1016 C  C     . THR   A 1 135 ? -20.512 -4.545  120.523 1.00 44.54  ? 1045 THR   A C     1 
ATOM   1017 O  O     . THR   A 1 135 ? -21.480 -4.176  119.852 1.00 45.44  ? 1045 THR   A O     1 
ATOM   1018 C  CB    . THR   A 1 135 ? -18.220 -3.549  120.596 1.00 41.75  ? 1045 THR   A CB    1 
ATOM   1019 O  OG1   . THR   A 1 135 ? -18.950 -2.328  120.721 1.00 43.12  ? 1045 THR   A OG1   1 
ATOM   1020 C  CG2   . THR   A 1 135 ? -16.975 -3.286  119.769 1.00 39.60  ? 1045 THR   A CG2   1 
ATOM   1021 N  N     . ALA   A 1 136 ? -20.612 -4.891  121.811 1.00 45.73  ? 1046 ALA   A N     1 
ATOM   1022 C  CA    . ALA   A 1 136 ? -21.906 -4.902  122.484 1.00 51.63  ? 1046 ALA   A CA    1 
ATOM   1023 C  C     . ALA   A 1 136 ? -22.471 -3.496  122.660 1.00 51.99  ? 1046 ALA   A C     1 
ATOM   1024 O  O     . ALA   A 1 136 ? -23.695 -3.309  122.612 1.00 51.55  ? 1046 ALA   A O     1 
ATOM   1025 C  CB    . ALA   A 1 136 ? -21.781 -5.599  123.842 1.00 49.29  ? 1046 ALA   A CB    1 
ATOM   1026 N  N     . LYS   A 1 137 ? -21.605 -2.500  122.850 1.00 48.89  ? 1047 LYS   A N     1 
ATOM   1027 C  CA    . LYS   A 1 137 ? -22.057 -1.168  123.244 1.00 50.64  ? 1047 LYS   A CA    1 
ATOM   1028 C  C     . LYS   A 1 137 ? -21.402 -0.025  122.488 1.00 52.81  ? 1047 LYS   A C     1 
ATOM   1029 O  O     . LYS   A 1 137 ? -21.960 1.077   122.496 1.00 56.13  ? 1047 LYS   A O     1 
ATOM   1030 C  CB    . LYS   A 1 137 ? -21.826 -0.945  124.744 1.00 52.16  ? 1047 LYS   A CB    1 
ATOM   1031 C  CG    . LYS   A 1 137 ? -22.377 -2.046  125.626 1.00 61.11  ? 1047 LYS   A CG    1 
ATOM   1032 C  CD    . LYS   A 1 137 ? -22.268 -1.700  127.103 1.00 64.70  ? 1047 LYS   A CD    1 
ATOM   1033 C  CE    . LYS   A 1 137 ? -23.170 -2.606  127.933 1.00 65.51  ? 1047 LYS   A CE    1 
ATOM   1034 N  NZ    . LYS   A 1 137 ? -23.197 -2.227  129.376 1.00 69.15  ? 1047 LYS   A NZ    1 
ATOM   1035 N  N     . MET   A 1 138 ? -20.266 -0.229  121.824 1.00 48.24  ? 1048 MET   A N     1 
ATOM   1036 C  CA    . MET   A 1 138 ? -19.474 0.856   121.255 1.00 48.79  ? 1048 MET   A CA    1 
ATOM   1037 C  C     . MET   A 1 138 ? -19.506 0.879   119.731 1.00 45.84  ? 1048 MET   A C     1 
ATOM   1038 O  O     . MET   A 1 138 ? -18.512 1.259   119.099 1.00 46.81  ? 1048 MET   A O     1 
ATOM   1039 C  CB    . MET   A 1 138 ? -18.019 0.749   121.714 1.00 46.83  ? 1048 MET   A CB    1 
ATOM   1040 C  CG    . MET   A 1 138 ? -17.786 1.037   123.181 1.00 49.72  ? 1048 MET   A CG    1 
ATOM   1041 S  SD    . MET   A 1 138 ? -16.031 0.930   123.565 1.00 52.33  ? 1048 MET   A SD    1 
ATOM   1042 C  CE    . MET   A 1 138 ? -15.803 -0.860  123.525 1.00 48.69  ? 1048 MET   A CE    1 
ATOM   1043 N  N     . GLY   A 1 139 ? -20.604 0.445   119.123 1.00 45.42  ? 1049 GLY   A N     1 
ATOM   1044 C  CA    . GLY   A 1 139 ? -20.572 0.308   117.678 1.00 44.29  ? 1049 GLY   A CA    1 
ATOM   1045 C  C     . GLY   A 1 139 ? -19.503 -0.684  117.255 1.00 42.00  ? 1049 GLY   A C     1 
ATOM   1046 O  O     . GLY   A 1 139 ? -19.357 -1.762  117.843 1.00 41.74  ? 1049 GLY   A O     1 
ATOM   1047 N  N     . TRP   A 1 140 ? -18.735 -0.319  116.230 1.00 40.88  ? 1050 TRP   A N     1 
ATOM   1048 C  CA    . TRP   A 1 140 ? -17.660 -1.181  115.743 1.00 39.24  ? 1050 TRP   A CA    1 
ATOM   1049 C  C     . TRP   A 1 140 ? -16.383 -0.993  116.549 1.00 37.37  ? 1050 TRP   A C     1 
ATOM   1050 O  O     . TRP   A 1 140 ? -16.101 0.084   117.076 1.00 37.64  ? 1050 TRP   A O     1 
ATOM   1051 C  CB    . TRP   A 1 140 ? -17.354 -0.912  114.268 1.00 40.16  ? 1050 TRP   A CB    1 
ATOM   1052 C  CG    . TRP   A 1 140 ? -18.539 -1.108  113.343 1.00 40.98  ? 1050 TRP   A CG    1 
ATOM   1053 C  CD1   . TRP   A 1 140 ? -19.283 -0.132  112.761 1.00 40.18  ? 1050 TRP   A CD1   1 
ATOM   1054 C  CD2   . TRP   A 1 140 ? -19.086 -2.357  112.888 1.00 39.28  ? 1050 TRP   A CD2   1 
ATOM   1055 N  NE1   . TRP   A 1 140 ? -20.264 -0.689  111.977 1.00 41.26  ? 1050 TRP   A NE1   1 
ATOM   1056 C  CE2   . TRP   A 1 140 ? -20.161 -2.053  112.033 1.00 43.53  ? 1050 TRP   A CE2   1 
ATOM   1057 C  CE3   . TRP   A 1 140 ? -18.763 -3.701  113.113 1.00 40.70  ? 1050 TRP   A CE3   1 
ATOM   1058 C  CZ2   . TRP   A 1 140 ? -20.940 -3.046  111.419 1.00 44.10  ? 1050 TRP   A CZ2   1 
ATOM   1059 C  CZ3   . TRP   A 1 140 ? -19.531 -4.691  112.492 1.00 39.54  ? 1050 TRP   A CZ3   1 
ATOM   1060 C  CH2   . TRP   A 1 140 ? -20.605 -4.353  111.659 1.00 40.92  ? 1050 TRP   A CH2   1 
ATOM   1061 N  N     . GLY   A 1 141 ? -15.613 -2.068  116.638 1.00 36.24  ? 1051 GLY   A N     1 
ATOM   1062 C  CA    . GLY   A 1 141 ? -14.289 -2.036  117.225 1.00 40.18  ? 1051 GLY   A CA    1 
ATOM   1063 C  C     . GLY   A 1 141 ? -13.326 -2.899  116.433 1.00 33.59  ? 1051 GLY   A C     1 
ATOM   1064 O  O     . GLY   A 1 141 ? -13.705 -3.562  115.467 1.00 34.26  ? 1051 GLY   A O     1 
ATOM   1065 N  N     . VAL   A 1 142 ? -12.074 -2.889  116.868 1.00 40.18  ? 1052 VAL   A N     1 
ATOM   1066 C  CA    . VAL   A 1 142 ? -11.009 -3.689  116.259 1.00 33.88  ? 1052 VAL   A CA    1 
ATOM   1067 C  C     . VAL   A 1 142 ? -10.479 -4.632  117.323 1.00 37.74  ? 1052 VAL   A C     1 
ATOM   1068 O  O     . VAL   A 1 142 ? -9.999  -4.182  118.373 1.00 38.22  ? 1052 VAL   A O     1 
ATOM   1069 C  CB    . VAL   A 1 142 ? -9.877  -2.814  115.704 1.00 30.57  ? 1052 VAL   A CB    1 
ATOM   1070 C  CG1   . VAL   A 1 142 ? -8.711  -3.695  115.229 1.00 33.45  ? 1052 VAL   A CG1   1 
ATOM   1071 C  CG2   . VAL   A 1 142 ? -10.380 -1.937  114.573 1.00 30.17  ? 1052 VAL   A CG2   1 
ATOM   1072 N  N     . ARG   A 1 143 ? -10.557 -5.936  117.059 1.00 33.39  ? 1053 ARG   A N     1 
ATOM   1073 C  CA    . ARG   A 1 143 ? -10.077 -6.914  118.016 1.00 36.54  ? 1053 ARG   A CA    1 
ATOM   1074 C  C     . ARG   A 1 143 ? -8.881  -7.667  117.442 1.00 37.04  ? 1053 ARG   A C     1 
ATOM   1075 O  O     . ARG   A 1 143 ? -8.746  -7.825  116.223 1.00 38.46  ? 1053 ARG   A O     1 
ATOM   1076 C  CB    . ARG   A 1 143 ? -11.217 -7.892  118.456 1.00 39.52  ? 1053 ARG   A CB    1 
ATOM   1077 C  CG    . ARG   A 1 143 ? -11.679 -8.960  117.462 1.00 39.93  ? 1053 ARG   A CG    1 
ATOM   1078 C  CD    . ARG   A 1 143 ? -12.626 -9.942  118.160 1.00 37.82  ? 1053 ARG   A CD    1 
ATOM   1079 N  NE    . ARG   A 1 143 ? -13.675 -10.464 117.288 1.00 40.17  ? 1053 ARG   A NE    1 
ATOM   1080 C  CZ    . ARG   A 1 143 ? -14.832 -10.948 117.727 1.00 40.56  ? 1053 ARG   A CZ    1 
ATOM   1081 N  NH1   . ARG   A 1 143 ? -15.140 -10.947 119.015 1.00 38.56  ? 1053 ARG   A NH1   1 
ATOM   1082 N  NH2   . ARG   A 1 143 ? -15.696 -11.457 116.856 1.00 41.42  ? 1053 ARG   A NH2   1 
ATOM   1083 N  N     . ALA   A 1 144 ? -8.000  -8.108  118.336 1.00 31.67  ? 1054 ALA   A N     1 
ATOM   1084 C  CA    . ALA   A 1 144 ? -6.875  -8.938  117.938 1.00 37.24  ? 1054 ALA   A CA    1 
ATOM   1085 C  C     . ALA   A 1 144 ? -7.313  -10.373 117.655 1.00 41.96  ? 1054 ALA   A C     1 
ATOM   1086 O  O     . ALA   A 1 144 ? -8.173  -10.936 118.341 1.00 40.16  ? 1054 ALA   A O     1 
ATOM   1087 C  CB    . ALA   A 1 144 ? -5.792  -8.936  119.019 1.00 42.48  ? 1054 ALA   A CB    1 
ATOM   1088 N  N     . LEU   A 1 145 ? -6.697  -10.962 116.636 1.00 39.70  ? 1055 LEU   A N     1 
ATOM   1089 C  CA    . LEU   A 1 145 ? -6.935  -12.337 116.245 1.00 37.07  ? 1055 LEU   A CA    1 
ATOM   1090 C  C     . LEU   A 1 145 ? -5.848  -13.271 116.737 1.00 37.00  ? 1055 LEU   A C     1 
ATOM   1091 O  O     . LEU   A 1 145 ? -5.842  -14.447 116.364 1.00 37.96  ? 1055 LEU   A O     1 
ATOM   1092 C  CB    . LEU   A 1 145 ? -7.054  -12.428 114.723 1.00 38.14  ? 1055 LEU   A CB    1 
ATOM   1093 C  CG    . LEU   A 1 145 ? -8.330  -11.813 114.139 1.00 37.01  ? 1055 LEU   A CG    1 
ATOM   1094 C  CD1   . LEU   A 1 145 ? -8.447  -12.116 112.657 1.00 35.70  ? 1055 LEU   A CD1   1 
ATOM   1095 C  CD2   . LEU   A 1 145 ? -9.544  -12.330 114.884 1.00 38.34  ? 1055 LEU   A CD2   1 
ATOM   1096 N  N     . GLN   A 1 146 ? -4.932  -12.776 117.566 1.00 39.75  ? 1056 GLN   A N     1 
ATOM   1097 C  CA    . GLN   A 1 146 ? -3.716  -13.502 117.922 1.00 42.79  ? 1056 GLN   A CA    1 
ATOM   1098 C  C     . GLN   A 1 146 ? -3.113  -12.886 119.178 1.00 39.00  ? 1056 GLN   A C     1 
ATOM   1099 O  O     . GLN   A 1 146 ? -3.410  -11.744 119.544 1.00 37.05  ? 1056 GLN   A O     1 
ATOM   1100 C  CB    . GLN   A 1 146 ? -2.684  -13.482 116.779 1.00 39.37  ? 1056 GLN   A CB    1 
ATOM   1101 C  CG    . GLN   A 1 146 ? -2.041  -12.112 116.520 1.00 39.17  ? 1056 GLN   A CG    1 
ATOM   1102 C  CD    . GLN   A 1 146 ? -0.960  -12.149 115.440 1.00 40.71  ? 1056 GLN   A CD    1 
ATOM   1103 O  OE1   . GLN   A 1 146 ? -1.248  -12.407 114.270 1.00 42.36  ? 1056 GLN   A OE1   1 
ATOM   1104 N  NE2   . GLN   A 1 146 ? 0.297   -11.897 115.836 1.00 42.59  ? 1056 GLN   A NE2   1 
ATOM   1105 N  N     . THR   A 1 147 ? -2.273  -13.669 119.843 1.00 34.79  ? 1057 THR   A N     1 
ATOM   1106 C  CA    . THR   A 1 147 ? -1.439  -13.115 120.900 1.00 45.07  ? 1057 THR   A CA    1 
ATOM   1107 C  C     . THR   A 1 147 ? -0.488  -12.069 120.321 1.00 37.05  ? 1057 THR   A C     1 
ATOM   1108 O  O     . THR   A 1 147 ? 0.042   -12.237 119.224 1.00 35.10  ? 1057 THR   A O     1 
ATOM   1109 C  CB    . THR   A 1 147 ? -0.680  -14.233 121.614 1.00 42.16  ? 1057 THR   A CB    1 
ATOM   1110 O  OG1   . THR   A 1 147 ? -1.483  -14.697 122.706 1.00 45.04  ? 1057 THR   A OG1   1 
ATOM   1111 C  CG2   . THR   A 1 147 ? 0.643   -13.756 122.143 1.00 45.70  ? 1057 THR   A CG2   1 
ATOM   1112 N  N     . ILE   A 1 148 ? -0.355  -10.953 121.027 1.00 38.73  ? 1058 ILE   A N     1 
ATOM   1113 C  CA    . ILE   A 1 148 ? 0.439   -9.807  120.593 1.00 38.58  ? 1058 ILE   A CA    1 
ATOM   1114 C  C     . ILE   A 1 148 ? 1.287   -9.367  121.774 1.00 41.57  ? 1058 ILE   A C     1 
ATOM   1115 O  O     . ILE   A 1 148 ? 0.753   -8.794  122.737 1.00 41.04  ? 1058 ILE   A O     1 
ATOM   1116 C  CB    . ILE   A 1 148 ? -0.419  -8.625  120.111 1.00 37.16  ? 1058 ILE   A CB    1 
ATOM   1117 C  CG1   . ILE   A 1 148 ? -1.277  -8.972  118.892 1.00 37.75  ? 1058 ILE   A CG1   1 
ATOM   1118 C  CG2   . ILE   A 1 148 ? 0.483   -7.453  119.772 1.00 36.12  ? 1058 ILE   A CG2   1 
ATOM   1119 C  CD1   . ILE   A 1 148 ? -1.935  -7.739  118.262 1.00 31.32  ? 1058 ILE   A CD1   1 
ATOM   1120 N  N     . PRO   A 1 149 ? 2.593   -9.616  121.742 1.00 35.50  ? 1059 PRO   A N     1 
ATOM   1121 C  CA    . PRO   A 1 149 ? 3.451   -9.190  122.842 1.00 38.05  ? 1059 PRO   A CA    1 
ATOM   1122 C  C     . PRO   A 1 149 ? 3.598   -7.679  122.864 1.00 40.24  ? 1059 PRO   A C     1 
ATOM   1123 O  O     . PRO   A 1 149 ? 3.451   -6.991  121.851 1.00 39.95  ? 1059 PRO   A O     1 
ATOM   1124 C  CB    . PRO   A 1 149 ? 4.796   -9.869  122.539 1.00 40.98  ? 1059 PRO   A CB    1 
ATOM   1125 C  CG    . PRO   A 1 149 ? 4.522   -10.855 121.431 1.00 38.30  ? 1059 PRO   A CG    1 
ATOM   1126 C  CD    . PRO   A 1 149 ? 3.334   -10.321 120.692 1.00 37.17  ? 1059 PRO   A CD    1 
ATOM   1127 N  N     . GLN   A 1 150 ? 3.901   -7.176  124.060 1.00 42.85  ? 1060 GLN   A N     1 
ATOM   1128 C  CA    . GLN   A 1 150 ? 4.122   -5.754  124.278 1.00 39.16  ? 1060 GLN   A CA    1 
ATOM   1129 C  C     . GLN   A 1 150 ? 5.232   -5.237  123.370 1.00 40.79  ? 1060 GLN   A C     1 
ATOM   1130 O  O     . GLN   A 1 150 ? 6.253   -5.897  123.167 1.00 36.91  ? 1060 GLN   A O     1 
ATOM   1131 C  CB    . GLN   A 1 150 ? 4.482   -5.526  125.743 1.00 40.40  ? 1060 GLN   A CB    1 
ATOM   1132 C  CG    . GLN   A 1 150 ? 4.617   -4.089  126.149 1.00 46.32  ? 1060 GLN   A CG    1 
ATOM   1133 C  CD    . GLN   A 1 150 ? 5.506   -3.922  127.360 1.00 52.51  ? 1060 GLN   A CD    1 
ATOM   1134 O  OE1   . GLN   A 1 150 ? 5.172   -3.199  128.298 1.00 56.94  ? 1060 GLN   A OE1   1 
ATOM   1135 N  NE2   . GLN   A 1 150 ? 6.664   -4.579  127.336 1.00 58.99  ? 1060 GLN   A NE2   1 
ATOM   1136 N  N     . GLY   A 1 151 ? 5.026   -4.047  122.815 1.00 40.16  ? 1061 GLY   A N     1 
ATOM   1137 C  CA    . GLY   A 1 151 ? 6.013   -3.413  121.971 1.00 39.89  ? 1061 GLY   A CA    1 
ATOM   1138 C  C     . GLY   A 1 151 ? 5.800   -3.620  120.487 1.00 35.16  ? 1061 GLY   A C     1 
ATOM   1139 O  O     . GLY   A 1 151 ? 6.378   -2.876  119.688 1.00 36.06  ? 1061 GLY   A O     1 
ATOM   1140 N  N     . THR   A 1 152 ? 4.986   -4.602  120.108 1.00 33.44  ? 1062 THR   A N     1 
ATOM   1141 C  CA    . THR   A 1 152 ? 4.641   -4.840  118.710 1.00 35.29  ? 1062 THR   A CA    1 
ATOM   1142 C  C     . THR   A 1 152 ? 3.893   -3.652  118.105 1.00 35.02  ? 1062 THR   A C     1 
ATOM   1143 O  O     . THR   A 1 152 ? 2.948   -3.120  118.705 1.00 34.00  ? 1062 THR   A O     1 
ATOM   1144 C  CB    . THR   A 1 152 ? 3.762   -6.096  118.603 1.00 34.41  ? 1062 THR   A CB    1 
ATOM   1145 O  OG1   . THR   A 1 152 ? 4.369   -7.171  119.325 1.00 35.77  ? 1062 THR   A OG1   1 
ATOM   1146 C  CG2   . THR   A 1 152 ? 3.572   -6.503  117.162 1.00 31.14  ? 1062 THR   A CG2   1 
ATOM   1147 N  N     . PHE   A 1 153 ? 4.299   -3.259  116.897 1.00 31.81  ? 1063 PHE   A N     1 
ATOM   1148 C  CA    . PHE   A 1 153 ? 3.532   -2.291  116.120 1.00 32.24  ? 1063 PHE   A CA    1 
ATOM   1149 C  C     . PHE   A 1 153 ? 2.216   -2.903  115.661 1.00 30.71  ? 1063 PHE   A C     1 
ATOM   1150 O  O     . PHE   A 1 153 ? 2.180   -4.047  115.207 1.00 35.82  ? 1063 PHE   A O     1 
ATOM   1151 C  CB    . PHE   A 1 153 ? 4.329   -1.834  114.901 1.00 29.00  ? 1063 PHE   A CB    1 
ATOM   1152 C  CG    . PHE   A 1 153 ? 3.527   -1.031  113.918 1.00 29.40  ? 1063 PHE   A CG    1 
ATOM   1153 C  CD1   . PHE   A 1 153 ? 3.166   0.272   114.202 1.00 32.56  ? 1063 PHE   A CD1   1 
ATOM   1154 C  CD2   . PHE   A 1 153 ? 3.141   -1.574  112.711 1.00 28.81  ? 1063 PHE   A CD2   1 
ATOM   1155 C  CE1   . PHE   A 1 153 ? 2.437   1.029   113.292 1.00 30.31  ? 1063 PHE   A CE1   1 
ATOM   1156 C  CE2   . PHE   A 1 153 ? 2.403   -0.826  111.801 1.00 28.59  ? 1063 PHE   A CE2   1 
ATOM   1157 C  CZ    . PHE   A 1 153 ? 2.063   0.478   112.089 1.00 27.86  ? 1063 PHE   A CZ    1 
ATOM   1158 N  N     . ILE   A 1 154 ? 1.134   -2.120  115.744 1.00 31.52  ? 1064 ILE   A N     1 
ATOM   1159 C  CA    . ILE   A 1 154 ? -0.209  -2.594  115.396 1.00 29.53  ? 1064 ILE   A CA    1 
ATOM   1160 C  C     . ILE   A 1 154 ? -0.662  -2.029  114.059 1.00 27.50  ? 1064 ILE   A C     1 
ATOM   1161 O  O     . ILE   A 1 154 ? -0.828  -2.762  113.082 1.00 28.54  ? 1064 ILE   A O     1 
ATOM   1162 C  CB    . ILE   A 1 154 ? -1.226  -2.223  116.489 1.00 29.56  ? 1064 ILE   A CB    1 
ATOM   1163 C  CG1   . ILE   A 1 154 ? -0.680  -2.619  117.862 1.00 32.84  ? 1064 ILE   A CG1   1 
ATOM   1164 C  CG2   . ILE   A 1 154 ? -2.556  -2.893  116.224 1.00 30.08  ? 1064 ILE   A CG2   1 
ATOM   1165 C  CD1   . ILE   A 1 154 ? -0.275  -4.071  117.959 1.00 31.95  ? 1064 ILE   A CD1   1 
ATOM   1166 N  N     . CYS   A 1 155 ? -0.903  -0.726  114.019 1.00 28.99  ? 1065 CYS   A N     1 
ATOM   1167 C  CA    . CYS   A 1 155 ? -1.363  -0.061  112.809 1.00 31.00  ? 1065 CYS   A CA    1 
ATOM   1168 C  C     . CYS   A 1 155 ? -1.053  1.425   112.936 1.00 29.93  ? 1065 CYS   A C     1 
ATOM   1169 O  O     . CYS   A 1 155 ? -0.720  1.922   114.015 1.00 28.57  ? 1065 CYS   A O     1 
ATOM   1170 C  CB    . CYS   A 1 155 ? -2.863  -0.306  112.586 1.00 31.43  ? 1065 CYS   A CB    1 
ATOM   1171 S  SG    . CYS   A 1 155 ? -3.839  -0.002  114.084 1.00 30.55  ? 1065 CYS   A SG    1 
ATOM   1172 N  N     . GLU   A 1 156 ? -1.171  2.127   111.818 1.00 26.98  ? 1066 GLU   A N     1 
ATOM   1173 C  CA    . GLU   A 1 156 ? -1.024  3.574   111.786 1.00 28.53  ? 1066 GLU   A CA    1 
ATOM   1174 C  C     . GLU   A 1 156 ? -2.407  4.229   111.825 1.00 29.17  ? 1066 GLU   A C     1 
ATOM   1175 O  O     . GLU   A 1 156 ? -3.353  3.718   111.229 1.00 30.05  ? 1066 GLU   A O     1 
ATOM   1176 C  CB    . GLU   A 1 156 ? -0.259  3.992   110.528 1.00 27.58  ? 1066 GLU   A CB    1 
ATOM   1177 C  CG    . GLU   A 1 156 ? -0.001  5.478   110.363 1.00 27.96  ? 1066 GLU   A CG    1 
ATOM   1178 C  CD    . GLU   A 1 156 ? 0.817   5.815   109.105 1.00 29.38  ? 1066 GLU   A CD    1 
ATOM   1179 O  OE1   . GLU   A 1 156 ? 1.262   4.906   108.374 1.00 25.86  ? 1066 GLU   A OE1   1 
ATOM   1180 O  OE2   . GLU   A 1 156 ? 1.020   7.015   108.840 1.00 32.75  ? 1066 GLU   A OE2   1 
ATOM   1181 N  N     . TYR   A 1 157 ? -2.528  5.348   112.543 1.00 30.93  ? 1067 TYR   A N     1 
ATOM   1182 C  CA    . TYR   A 1 157 ? -3.734  6.175   112.461 1.00 30.16  ? 1067 TYR   A CA    1 
ATOM   1183 C  C     . TYR   A 1 157 ? -3.727  6.926   111.139 1.00 30.71  ? 1067 TYR   A C     1 
ATOM   1184 O  O     . TYR   A 1 157 ? -3.053  7.948   111.004 1.00 29.25  ? 1067 TYR   A O     1 
ATOM   1185 C  CB    . TYR   A 1 157 ? -3.831  7.170   113.618 1.00 33.84  ? 1067 TYR   A CB    1 
ATOM   1186 C  CG    . TYR   A 1 157 ? -5.251  7.746   113.747 1.00 33.65  ? 1067 TYR   A CG    1 
ATOM   1187 C  CD1   . TYR   A 1 157 ? -5.697  8.761   112.910 1.00 32.50  ? 1067 TYR   A CD1   1 
ATOM   1188 C  CD2   . TYR   A 1 157 ? -6.150  7.237   114.683 1.00 33.74  ? 1067 TYR   A CD2   1 
ATOM   1189 C  CE1   . TYR   A 1 157 ? -7.001  9.277   113.014 1.00 33.61  ? 1067 TYR   A CE1   1 
ATOM   1190 C  CE2   . TYR   A 1 157 ? -7.463  7.739   114.790 1.00 34.95  ? 1067 TYR   A CE2   1 
ATOM   1191 C  CZ    . TYR   A 1 157 ? -7.878  8.755   113.953 1.00 35.82  ? 1067 TYR   A CZ    1 
ATOM   1192 O  OH    . TYR   A 1 157 ? -9.173  9.257   114.054 1.00 37.34  ? 1067 TYR   A OH    1 
ATOM   1193 N  N     . VAL   A 1 158 ? -4.509  6.455   110.169 1.00 29.55  ? 1068 VAL   A N     1 
ATOM   1194 C  CA    . VAL   A 1 158 ? -4.506  7.025   108.831 1.00 29.05  ? 1068 VAL   A CA    1 
ATOM   1195 C  C     . VAL   A 1 158 ? -5.815  7.759   108.587 1.00 28.54  ? 1068 VAL   A C     1 
ATOM   1196 O  O     . VAL   A 1 158 ? -6.898  7.265   108.922 1.00 29.20  ? 1068 VAL   A O     1 
ATOM   1197 C  CB    . VAL   A 1 158 ? -4.285  5.945   107.761 1.00 30.53  ? 1068 VAL   A CB    1 
ATOM   1198 C  CG1   . VAL   A 1 158 ? -4.615  6.475   106.373 1.00 27.56  ? 1068 VAL   A CG1   1 
ATOM   1199 C  CG2   . VAL   A 1 158 ? -2.851  5.403   107.833 1.00 32.75  ? 1068 VAL   A CG2   1 
ATOM   1200 N  N     . GLY   A 1 159 ? -5.713  8.931   107.978 1.00 29.19  ? 1069 GLY   A N     1 
ATOM   1201 C  CA    . GLY   A 1 159 ? -6.908  9.637   107.570 1.00 29.08  ? 1069 GLY   A CA    1 
ATOM   1202 C  C     . GLY   A 1 159 ? -6.568  10.858  106.750 1.00 31.48  ? 1069 GLY   A C     1 
ATOM   1203 O  O     . GLY   A 1 159 ? -5.553  10.900  106.049 1.00 33.33  ? 1069 GLY   A O     1 
ATOM   1204 N  N     . GLU   A 1 160 ? -7.392  11.879  106.869 1.00 32.29  ? 1070 GLU   A N     1 
ATOM   1205 C  CA    . GLU   A 1 160 ? -7.278  13.078  106.061 1.00 30.47  ? 1070 GLU   A CA    1 
ATOM   1206 C  C     . GLU   A 1 160 ? -6.515  14.133  106.846 1.00 30.69  ? 1070 GLU   A C     1 
ATOM   1207 O  O     . GLU   A 1 160 ? -6.875  14.453  107.982 1.00 31.96  ? 1070 GLU   A O     1 
ATOM   1208 C  CB    . GLU   A 1 160 ? -8.666  13.590  105.665 1.00 33.59  ? 1070 GLU   A CB    1 
ATOM   1209 C  CG    . GLU   A 1 160 ? -8.657  15.001  105.133 1.00 32.15  ? 1070 GLU   A CG    1 
ATOM   1210 C  CD    . GLU   A 1 160 ? -10.053 15.572  104.929 1.00 35.95  ? 1070 GLU   A CD    1 
ATOM   1211 O  OE1   . GLU   A 1 160 ? -11.016 15.141  105.609 1.00 39.11  ? 1070 GLU   A OE1   1 
ATOM   1212 O  OE2   . GLU   A 1 160 ? -10.174 16.458  104.071 1.00 35.02  ? 1070 GLU   A OE2   1 
ATOM   1213 N  N     . LEU   A 1 161 ? -5.439  14.634  106.259 1.00 31.60  ? 1071 LEU   A N     1 
ATOM   1214 C  CA    . LEU   A 1 161 ? -4.693  15.718  106.874 1.00 31.27  ? 1071 LEU   A CA    1 
ATOM   1215 C  C     . LEU   A 1 161 ? -5.465  17.018  106.656 1.00 32.27  ? 1071 LEU   A C     1 
ATOM   1216 O  O     . LEU   A 1 161 ? -5.820  17.368  105.523 1.00 31.71  ? 1071 LEU   A O     1 
ATOM   1217 C  CB    . LEU   A 1 161 ? -3.273  15.789  106.299 1.00 33.13  ? 1071 LEU   A CB    1 
ATOM   1218 C  CG    . LEU   A 1 161 ? -2.346  14.558  106.504 1.00 35.04  ? 1071 LEU   A CG    1 
ATOM   1219 C  CD1   . LEU   A 1 161 ? -1.154  14.578  105.553 1.00 36.47  ? 1071 LEU   A CD1   1 
ATOM   1220 C  CD2   . LEU   A 1 161 ? -1.849  14.408  107.943 1.00 31.23  ? 1071 LEU   A CD2   1 
ATOM   1221 N  N     . ILE   A 1 162 ? -5.757  17.712  107.749 1.00 33.86  ? 1072 ILE   A N     1 
ATOM   1222 C  CA    . ILE   A 1 162 ? -6.461  18.983  107.700 1.00 37.07  ? 1072 ILE   A CA    1 
ATOM   1223 C  C     . ILE   A 1 162 ? -5.735  19.947  108.622 1.00 41.87  ? 1072 ILE   A C     1 
ATOM   1224 O  O     . ILE   A 1 162 ? -4.906  19.549  109.448 1.00 37.01  ? 1072 ILE   A O     1 
ATOM   1225 C  CB    . ILE   A 1 162 ? -7.947  18.858  108.102 1.00 35.86  ? 1072 ILE   A CB    1 
ATOM   1226 C  CG1   . ILE   A 1 162 ? -8.079  18.309  109.521 1.00 36.87  ? 1072 ILE   A CG1   1 
ATOM   1227 C  CG2   . ILE   A 1 162 ? -8.683  17.976  107.122 1.00 34.48  ? 1072 ILE   A CG2   1 
ATOM   1228 C  CD1   . ILE   A 1 162 ? -9.513  18.178  109.974 1.00 37.90  ? 1072 ILE   A CD1   1 
ATOM   1229 N  N     . SER   A 1 163 ? -6.034  21.232  108.448 1.00 37.92  ? 1073 SER   A N     1 
ATOM   1230 C  CA    . SER   A 1 163 ? -5.415  22.239  109.286 1.00 39.80  ? 1073 SER   A CA    1 
ATOM   1231 C  C     . SER   A 1 163 ? -6.176  22.347  110.602 1.00 42.66  ? 1073 SER   A C     1 
ATOM   1232 O  O     . SER   A 1 163 ? -7.196  21.690  110.824 1.00 44.47  ? 1073 SER   A O     1 
ATOM   1233 C  CB    . SER   A 1 163 ? -5.355  23.586  108.564 1.00 40.55  ? 1073 SER   A CB    1 
ATOM   1234 O  OG    . SER   A 1 163 ? -6.602  24.260  108.577 1.00 42.20  ? 1073 SER   A OG    1 
ATOM   1235 N  N     . ASP   A 1 164 ? -5.668  23.197  111.488 1.00 44.55  ? 1074 ASP   A N     1 
ATOM   1236 C  CA    . ASP   A 1 164 ? -6.337  23.435  112.756 1.00 45.58  ? 1074 ASP   A CA    1 
ATOM   1237 C  C     . ASP   A 1 164 ? -7.631  24.212  112.549 1.00 50.63  ? 1074 ASP   A C     1 
ATOM   1238 O  O     . ASP   A 1 164 ? -8.639  23.949  113.221 1.00 51.33  ? 1074 ASP   A O     1 
ATOM   1239 C  CB    . ASP   A 1 164 ? -5.393  24.187  113.686 1.00 49.78  ? 1074 ASP   A CB    1 
ATOM   1240 C  CG    . ASP   A 1 164 ? -5.851  24.171  115.121 1.00 52.28  ? 1074 ASP   A CG    1 
ATOM   1241 O  OD1   . ASP   A 1 164 ? -6.330  23.110  115.582 1.00 49.07  ? 1074 ASP   A OD1   1 
ATOM   1242 O  OD2   . ASP   A 1 164 ? -5.690  25.221  115.791 1.00 52.73  ? 1074 ASP   A OD2   1 
ATOM   1243 N  N     . ALA   A 1 165 ? -7.626  25.167  111.617 1.00 49.78  ? 1075 ALA   A N     1 
ATOM   1244 C  CA    . ALA   A 1 165 ? -8.844  25.915  111.333 1.00 49.96  ? 1075 ALA   A CA    1 
ATOM   1245 C  C     . ALA   A 1 165 ? -9.904  25.019  110.703 1.00 49.59  ? 1075 ALA   A C     1 
ATOM   1246 O  O     . ALA   A 1 165 ? -11.093 25.135  111.028 1.00 51.23  ? 1075 ALA   A O     1 
ATOM   1247 C  CB    . ALA   A 1 165 ? -8.531  27.107  110.430 1.00 47.81  ? 1075 ALA   A CB    1 
ATOM   1248 N  N     . GLU   A 1 166 ? -9.495  24.110  109.812 1.00 45.53  ? 1076 GLU   A N     1 
ATOM   1249 C  CA    . GLU   A 1 166 ? -10.456 23.190  109.207 1.00 48.63  ? 1076 GLU   A CA    1 
ATOM   1250 C  C     . GLU   A 1 166 ? -11.110 22.307  110.265 1.00 49.03  ? 1076 GLU   A C     1 
ATOM   1251 O  O     . GLU   A 1 166 ? -12.334 22.135  110.274 1.00 47.31  ? 1076 GLU   A O     1 
ATOM   1252 C  CB    . GLU   A 1 166 ? -9.780  22.332  108.140 1.00 47.00  ? 1076 GLU   A CB    1 
ATOM   1253 C  CG    . GLU   A 1 166 ? -10.722 21.290  107.520 1.00 45.60  ? 1076 GLU   A CG    1 
ATOM   1254 C  CD    . GLU   A 1 166 ? -11.838 21.948  106.744 1.00 47.00  ? 1076 GLU   A CD    1 
ATOM   1255 O  OE1   . GLU   A 1 166 ? -11.577 23.032  106.188 1.00 46.97  ? 1076 GLU   A OE1   1 
ATOM   1256 O  OE2   . GLU   A 1 166 ? -12.971 21.401  106.701 1.00 47.18  ? 1076 GLU   A OE2   1 
ATOM   1257 N  N     . ALA   A 1 167 ? -10.306 21.738  111.171 1.00 49.68  ? 1077 ALA   A N     1 
ATOM   1258 C  CA    . ALA   A 1 167 ? -10.859 20.923  112.247 1.00 51.18  ? 1077 ALA   A CA    1 
ATOM   1259 C  C     . ALA   A 1 167 ? -11.889 21.674  113.091 1.00 51.05  ? 1077 ALA   A C     1 
ATOM   1260 O  O     . ALA   A 1 167 ? -12.704 21.026  113.757 1.00 54.73  ? 1077 ALA   A O     1 
ATOM   1261 C  CB    . ALA   A 1 167 ? -9.733  20.404  113.141 1.00 43.90  ? 1077 ALA   A CB    1 
ATOM   1262 N  N     . ASP   A 1 168 ? -11.866 23.014  113.085 1.00 47.80  ? 1078 ASP   A N     1 
ATOM   1263 C  CA    . ASP   A 1 168 ? -12.870 23.795  113.813 1.00 55.74  ? 1078 ASP   A CA    1 
ATOM   1264 C  C     . ASP   A 1 168 ? -14.256 23.634  113.198 1.00 51.56  ? 1078 ASP   A C     1 
ATOM   1265 O  O     . ASP   A 1 168 ? -15.251 23.464  113.912 1.00 51.84  ? 1078 ASP   A O     1 
ATOM   1266 C  CB    . ASP   A 1 168 ? -12.502 25.284  113.822 1.00 54.47  ? 1078 ASP   A CB    1 
ATOM   1267 C  CG    . ASP   A 1 168 ? -11.236 25.586  114.595 1.00 52.79  ? 1078 ASP   A CG    1 
ATOM   1268 O  OD1   . ASP   A 1 168 ? -10.575 24.639  115.029 1.00 52.25  ? 1078 ASP   A OD1   1 
ATOM   1269 O  OD2   . ASP   A 1 168 ? -10.900 26.785  114.770 1.00 55.38  ? 1078 ASP   A OD2   1 
ATOM   1270 N  N     . VAL   A 1 169 ? -14.337 23.713  111.870 1.00 49.83  ? 1079 VAL   A N     1 
ATOM   1271 C  CA    . VAL   A 1 169 ? -15.599 23.724  111.144 1.00 51.29  ? 1079 VAL   A CA    1 
ATOM   1272 C  C     . VAL   A 1 169 ? -16.015 22.311  110.772 1.00 51.20  ? 1079 VAL   A C     1 
ATOM   1273 O  O     . VAL   A 1 169 ? -16.922 22.122  109.955 1.00 51.62  ? 1079 VAL   A O     1 
ATOM   1274 C  CB    . VAL   A 1 169 ? -15.495 24.595  109.881 1.00 52.66  ? 1079 VAL   A CB    1 
ATOM   1275 C  CG1   . VAL   A 1 169 ? -15.098 26.012  110.247 1.00 49.25  ? 1079 VAL   A CG1   1 
ATOM   1276 C  CG2   . VAL   A 1 169 ? -14.504 23.987  108.914 1.00 45.00  ? 1079 VAL   A CG2   1 
ATOM   1277 N  N     . ARG   A 1 170 ? -15.344 21.312  111.339 1.00 50.30  ? 1080 ARG   A N     1 
ATOM   1278 C  CA    . ARG   A 1 170 ? -15.694 19.916  111.106 1.00 49.21  ? 1080 ARG   A CA    1 
ATOM   1279 C  C     . ARG   A 1 170 ? -16.749 19.536  112.140 1.00 52.70  ? 1080 ARG   A C     1 
ATOM   1280 O  O     . ARG   A 1 170 ? -16.471 19.523  113.344 1.00 54.27  ? 1080 ARG   A O     1 
ATOM   1281 C  CB    . ARG   A 1 170 ? -14.454 19.021  111.196 1.00 47.84  ? 1080 ARG   A CB    1 
ATOM   1282 C  CG    . ARG   A 1 170 ? -13.466 19.139  110.005 1.00 45.06  ? 1080 ARG   A CG    1 
ATOM   1283 C  CD    . ARG   A 1 170 ? -13.943 18.346  108.789 1.00 39.51  ? 1080 ARG   A CD    1 
ATOM   1284 N  NE    . ARG   A 1 170 ? -13.259 18.690  107.546 1.00 37.95  ? 1080 ARG   A NE    1 
ATOM   1285 C  CZ    . ARG   A 1 170 ? -12.537 17.846  106.813 1.00 38.76  ? 1080 ARG   A CZ    1 
ATOM   1286 N  NH1   . ARG   A 1 170 ? -12.348 16.588  107.180 1.00 35.54  ? 1080 ARG   A NH1   1 
ATOM   1287 N  NH2   . ARG   A 1 170 ? -12.001 18.271  105.673 1.00 35.04  ? 1080 ARG   A NH2   1 
ATOM   1288 N  N     . GLU   A 1 171 ? -17.969 19.251  111.675 1.00 51.97  ? 1081 GLU   A N     1 
ATOM   1289 C  CA    . GLU   A 1 171 ? -19.066 19.009  112.607 1.00 54.25  ? 1081 GLU   A CA    1 
ATOM   1290 C  C     . GLU   A 1 171 ? -18.906 17.672  113.319 1.00 58.31  ? 1081 GLU   A C     1 
ATOM   1291 O  O     . GLU   A 1 171 ? -19.081 17.584  114.542 1.00 58.56  ? 1081 GLU   A O     1 
ATOM   1292 C  CB    . GLU   A 1 171 ? -20.415 19.058  111.887 1.00 55.13  ? 1081 GLU   A CB    1 
ATOM   1293 C  CG    . GLU   A 1 171 ? -21.525 18.408  112.716 1.00 56.97  ? 1081 GLU   A CG    1 
ATOM   1294 C  CD    . GLU   A 1 171 ? -22.898 18.493  112.076 1.00 60.24  ? 1081 GLU   A CD    1 
ATOM   1295 O  OE1   . GLU   A 1 171 ? -23.003 19.077  110.975 1.00 60.76  ? 1081 GLU   A OE1   1 
ATOM   1296 O  OE2   . GLU   A 1 171 ? -23.870 17.978  112.681 1.00 54.98  ? 1081 GLU   A OE2   1 
ATOM   1297 N  N     . ASP   A 1 172 ? -18.591 16.614  112.568 1.00 57.17  ? 1082 ASP   A N     1 
ATOM   1298 C  CA    . ASP   A 1 172 ? -18.527 15.259  113.119 1.00 58.81  ? 1082 ASP   A CA    1 
ATOM   1299 C  C     . ASP   A 1 172 ? -17.085 14.974  113.505 1.00 57.29  ? 1082 ASP   A C     1 
ATOM   1300 O  O     . ASP   A 1 172 ? -16.325 14.373  112.749 1.00 53.54  ? 1082 ASP   A O     1 
ATOM   1301 C  CB    . ASP   A 1 172 ? -19.055 14.232  112.122 1.00 56.86  ? 1082 ASP   A CB    1 
ATOM   1302 C  CG    . ASP   A 1 172 ? -18.958 12.803  112.650 1.00 57.42  ? 1082 ASP   A CG    1 
ATOM   1303 O  OD1   . ASP   A 1 172 ? -18.666 12.622  113.855 1.00 57.12  ? 1082 ASP   A OD1   1 
ATOM   1304 O  OD2   . ASP   A 1 172 ? -19.164 11.852  111.864 1.00 56.48  ? 1082 ASP   A OD2   1 
ATOM   1305 N  N     . ASP   A 1 173 ? -16.711 15.398  114.709 1.00 60.83  ? 1083 ASP   A N     1 
ATOM   1306 C  CA    . ASP   A 1 173 ? -15.351 15.223  115.211 1.00 61.06  ? 1083 ASP   A CA    1 
ATOM   1307 C  C     . ASP   A 1 173 ? -15.182 13.936  116.010 1.00 60.39  ? 1083 ASP   A C     1 
ATOM   1308 O  O     . ASP   A 1 173 ? -14.575 13.936  117.087 1.00 61.47  ? 1083 ASP   A O     1 
ATOM   1309 C  CB    . ASP   A 1 173 ? -14.932 16.437  116.038 1.00 62.17  ? 1083 ASP   A CB    1 
ATOM   1310 C  CG    . ASP   A 1 173 ? -15.982 16.869  117.047 1.00 67.80  ? 1083 ASP   A CG    1 
ATOM   1311 O  OD1   . ASP   A 1 173 ? -17.199 16.710  116.785 1.00 70.42  ? 1083 ASP   A OD1   1 
ATOM   1312 O  OD2   . ASP   A 1 173 ? -15.584 17.388  118.110 1.00 68.75  ? 1083 ASP   A OD2   1 
ATOM   1313 N  N     . SER   A 1 174 ? -15.675 12.812  115.495 1.00 53.74  ? 1084 SER   A N     1 
ATOM   1314 C  CA    . SER   A 1 174 ? -15.567 11.528  116.177 1.00 49.88  ? 1084 SER   A CA    1 
ATOM   1315 C  C     . SER   A 1 174 ? -14.452 10.654  115.612 1.00 48.41  ? 1084 SER   A C     1 
ATOM   1316 O  O     . SER   A 1 174 ? -14.349 9.479   115.981 1.00 48.32  ? 1084 SER   A O     1 
ATOM   1317 C  CB    . SER   A 1 174 ? -16.904 10.785  116.107 1.00 52.61  ? 1084 SER   A CB    1 
ATOM   1318 O  OG    . SER   A 1 174 ? -17.978 11.632  116.491 1.00 50.97  ? 1084 SER   A OG    1 
ATOM   1319 N  N     . TYR   A 1 175 ? -13.609 11.205  114.737 1.00 46.44  ? 1085 TYR   A N     1 
ATOM   1320 C  CA    . TYR   A 1 175 ? -12.513 10.488  114.100 1.00 39.57  ? 1085 TYR   A CA    1 
ATOM   1321 C  C     . TYR   A 1 175 ? -11.302 11.413  113.966 1.00 43.84  ? 1085 TYR   A C     1 
ATOM   1322 O  O     . TYR   A 1 175 ? -10.390 11.169  113.161 1.00 40.58  ? 1085 TYR   A O     1 
ATOM   1323 C  CB    . TYR   A 1 175 ? -12.968 9.924   112.748 1.00 38.22  ? 1085 TYR   A CB    1 
ATOM   1324 C  CG    . TYR   A 1 175 ? -14.213 9.010   112.851 1.00 39.22  ? 1085 TYR   A CG    1 
ATOM   1325 C  CD1   . TYR   A 1 175 ? -14.078 7.656   113.149 1.00 38.98  ? 1085 TYR   A CD1   1 
ATOM   1326 C  CD2   . TYR   A 1 175 ? -15.497 9.506   112.661 1.00 40.55  ? 1085 TYR   A CD2   1 
ATOM   1327 C  CE1   . TYR   A 1 175 ? -15.137 6.830   113.240 1.00 40.04  ? 1085 TYR   A CE1   1 
ATOM   1328 C  CE2   . TYR   A 1 175 ? -16.621 8.659   112.761 1.00 42.98  ? 1085 TYR   A CE2   1 
ATOM   1329 C  CZ    . TYR   A 1 175 ? -16.422 7.318   113.058 1.00 41.47  ? 1085 TYR   A CZ    1 
ATOM   1330 O  OH    . TYR   A 1 175 ? -17.466 6.438   113.166 1.00 42.74  ? 1085 TYR   A OH    1 
ATOM   1331 N  N     . LEU   A 1 176 ? -11.267 12.447  114.799 1.00 42.32  ? 1086 LEU   A N     1 
ATOM   1332 C  CA    . LEU   A 1 176 ? -10.332 13.557  114.700 1.00 42.32  ? 1086 LEU   A CA    1 
ATOM   1333 C  C     . LEU   A 1 176 ? -9.209  13.359  115.714 1.00 42.85  ? 1086 LEU   A C     1 
ATOM   1334 O  O     . LEU   A 1 176 ? -9.463  13.343  116.925 1.00 42.37  ? 1086 LEU   A O     1 
ATOM   1335 C  CB    . LEU   A 1 176 ? -11.080 14.864  114.962 1.00 44.97  ? 1086 LEU   A CB    1 
ATOM   1336 C  CG    . LEU   A 1 176 ? -10.530 16.195  114.487 1.00 48.23  ? 1086 LEU   A CG    1 
ATOM   1337 C  CD1   . LEU   A 1 176 ? -10.362 16.168  112.985 1.00 44.38  ? 1086 LEU   A CD1   1 
ATOM   1338 C  CD2   . LEU   A 1 176 ? -11.488 17.301  114.899 1.00 51.14  ? 1086 LEU   A CD2   1 
ATOM   1339 N  N     . PHE   A 1 177 ? -7.978  13.201  115.220 1.00 40.08  ? 1087 PHE   A N     1 
ATOM   1340 C  CA    . PHE   A 1 177 ? -6.794  12.971  116.044 1.00 39.27  ? 1087 PHE   A CA    1 
ATOM   1341 C  C     . PHE   A 1 177 ? -5.864  14.187  115.999 1.00 39.75  ? 1087 PHE   A C     1 
ATOM   1342 O  O     . PHE   A 1 177 ? -5.613  14.743  114.928 1.00 38.81  ? 1087 PHE   A O     1 
ATOM   1343 C  CB    . PHE   A 1 177 ? -6.047  11.715  115.566 1.00 39.67  ? 1087 PHE   A CB    1 
ATOM   1344 C  CG    . PHE   A 1 177 ? -4.940  11.271  116.493 1.00 41.60  ? 1087 PHE   A CG    1 
ATOM   1345 C  CD1   . PHE   A 1 177 ? -3.742  11.972  116.562 1.00 38.82  ? 1087 PHE   A CD1   1 
ATOM   1346 C  CD2   . PHE   A 1 177 ? -5.097  10.156  117.293 1.00 40.38  ? 1087 PHE   A CD2   1 
ATOM   1347 C  CE1   . PHE   A 1 177 ? -2.744  11.584  117.415 1.00 38.05  ? 1087 PHE   A CE1   1 
ATOM   1348 C  CE2   . PHE   A 1 177 ? -4.079  9.752   118.137 1.00 37.98  ? 1087 PHE   A CE2   1 
ATOM   1349 C  CZ    . PHE   A 1 177 ? -2.905  10.472  118.197 1.00 38.08  ? 1087 PHE   A CZ    1 
ATOM   1350 N  N     . ASP   A 1 178 ? -5.333  14.571  117.167 1.00 41.35  ? 1088 ASP   A N     1 
ATOM   1351 C  CA    . ASP   A 1 178 ? -4.459  15.735  117.323 1.00 42.33  ? 1088 ASP   A CA    1 
ATOM   1352 C  C     . ASP   A 1 178 ? -2.982  15.342  117.227 1.00 44.45  ? 1088 ASP   A C     1 
ATOM   1353 O  O     . ASP   A 1 178 ? -2.478  14.608  118.082 1.00 43.67  ? 1088 ASP   A O     1 
ATOM   1354 C  CB    . ASP   A 1 178 ? -4.696  16.403  118.678 1.00 44.98  ? 1088 ASP   A CB    1 
ATOM   1355 C  CG    . ASP   A 1 178 ? -5.816  17.418  118.657 1.00 50.12  ? 1088 ASP   A CG    1 
ATOM   1356 O  OD1   . ASP   A 1 178 ? -6.299  17.776  117.556 1.00 47.45  ? 1088 ASP   A OD1   1 
ATOM   1357 O  OD2   . ASP   A 1 178 ? -6.200  17.856  119.761 1.00 49.30  ? 1088 ASP   A OD2   1 
ATOM   1358 N  N     . LEU   A 1 179 ? -2.270  15.876  116.232 1.00 44.86  ? 1089 LEU   A N     1 
ATOM   1359 C  CA    . LEU   A 1 179 ? -0.813  15.715  116.225 1.00 50.89  ? 1089 LEU   A CA    1 
ATOM   1360 C  C     . LEU   A 1 179 ? -0.146  16.622  117.265 1.00 54.03  ? 1089 LEU   A C     1 
ATOM   1361 O  O     . LEU   A 1 179 ? 0.740   16.177  118.004 1.00 57.72  ? 1089 LEU   A O     1 
ATOM   1362 C  CB    . LEU   A 1 179 ? -0.252  15.983  114.825 1.00 42.72  ? 1089 LEU   A CB    1 
ATOM   1363 C  CG    . LEU   A 1 179 ? -0.881  15.217  113.647 1.00 39.35  ? 1089 LEU   A CG    1 
ATOM   1364 C  CD1   . LEU   A 1 179 ? -0.424  15.796  112.318 1.00 39.13  ? 1089 LEU   A CD1   1 
ATOM   1365 C  CD2   . LEU   A 1 179 ? -0.588  13.731  113.683 1.00 36.47  ? 1089 LEU   A CD2   1 
ATOM   1366 N  N     . ASP   A 1 180 ? -0.546  17.901  117.310 1.00 58.52  ? 1090 ASP   A N     1 
ATOM   1367 C  CA    . ASP   A 1 180 ? -0.196  18.904  118.323 1.00 58.63  ? 1090 ASP   A CA    1 
ATOM   1368 C  C     . ASP   A 1 180 ? 1.197   19.487  118.139 1.00 74.44  ? 1090 ASP   A C     1 
ATOM   1369 O  O     . ASP   A 1 180 ? 2.176   18.750  117.973 1.00 71.87  ? 1090 ASP   A O     1 
ATOM   1370 C  CB    . ASP   A 1 180 ? -0.316  18.338  119.741 1.00 58.98  ? 1090 ASP   A CB    1 
ATOM   1371 N  N     . ASN   A 1 181 ? 1.287   20.816  118.196 1.00 80.97  ? 1091 ASN   A N     1 
ATOM   1372 C  CA    . ASN   A 1 181 ? 2.556   21.536  118.098 1.00 84.83  ? 1091 ASN   A CA    1 
ATOM   1373 C  C     . ASN   A 1 181 ? 2.446   22.941  118.688 1.00 87.70  ? 1091 ASN   A C     1 
ATOM   1374 O  O     . ASN   A 1 181 ? 2.274   23.117  119.896 1.00 86.17  ? 1091 ASN   A O     1 
ATOM   1375 C  CB    . ASN   A 1 181 ? 3.014   21.621  116.643 1.00 86.08  ? 1091 ASN   A CB    1 
ATOM   1376 N  N     . GLY   A 1 184 ? 4.640   24.860  116.820 1.00 98.61  ? 1094 GLY   A N     1 
ATOM   1377 C  CA    . GLY   A 1 184 ? 4.137   26.093  116.238 1.00 100.25 ? 1094 GLY   A CA    1 
ATOM   1378 C  C     . GLY   A 1 184 ? 2.865   25.934  115.417 1.00 99.84  ? 1094 GLY   A C     1 
ATOM   1379 O  O     . GLY   A 1 184 ? 1.796   26.404  115.813 1.00 102.86 ? 1094 GLY   A O     1 
ATOM   1380 N  N     . GLU   A 1 185 ? 2.983   25.272  114.266 1.00 83.02  ? 1095 GLU   A N     1 
ATOM   1381 C  CA    . GLU   A 1 185 ? 1.853   25.044  113.379 1.00 68.38  ? 1095 GLU   A CA    1 
ATOM   1382 C  C     . GLU   A 1 185 ? 1.181   23.729  113.726 1.00 62.85  ? 1095 GLU   A C     1 
ATOM   1383 O  O     . GLU   A 1 185 ? 1.848   22.711  113.928 1.00 64.52  ? 1095 GLU   A O     1 
ATOM   1384 C  CB    . GLU   A 1 185 ? 2.301   25.019  111.921 1.00 61.94  ? 1095 GLU   A CB    1 
ATOM   1385 C  CG    . GLU   A 1 185 ? 1.441   25.841  110.983 1.00 56.41  ? 1095 GLU   A CG    1 
ATOM   1386 C  CD    . GLU   A 1 185 ? 2.136   26.055  109.666 1.00 49.60  ? 1095 GLU   A CD    1 
ATOM   1387 O  OE1   . GLU   A 1 185 ? 2.115   25.140  108.813 1.00 43.81  ? 1095 GLU   A OE1   1 
ATOM   1388 O  OE2   . GLU   A 1 185 ? 2.753   27.127  109.515 1.00 50.55  ? 1095 GLU   A OE2   1 
ATOM   1389 N  N     . VAL   A 1 186 ? -0.146  23.752  113.756 1.00 57.24  ? 1096 VAL   A N     1 
ATOM   1390 C  CA    . VAL   A 1 186 ? -0.947  22.682  114.330 1.00 51.18  ? 1096 VAL   A CA    1 
ATOM   1391 C  C     . VAL   A 1 186 ? -1.780  22.042  113.228 1.00 48.93  ? 1096 VAL   A C     1 
ATOM   1392 O  O     . VAL   A 1 186 ? -2.522  22.741  112.523 1.00 47.13  ? 1096 VAL   A O     1 
ATOM   1393 C  CB    . VAL   A 1 186 ? -1.842  23.225  115.458 1.00 54.96  ? 1096 VAL   A CB    1 
ATOM   1394 C  CG1   . VAL   A 1 186 ? -3.003  22.284  115.724 1.00 49.51  ? 1096 VAL   A CG1   1 
ATOM   1395 C  CG2   . VAL   A 1 186 ? -1.016  23.469  116.719 1.00 62.84  ? 1096 VAL   A CG2   1 
ATOM   1396 N  N     . TYR   A 1 187 ? -1.663  20.716  113.081 1.00 41.86  ? 1097 TYR   A N     1 
ATOM   1397 C  CA    . TYR   A 1 187 ? -2.415  19.988  112.067 1.00 43.04  ? 1097 TYR   A CA    1 
ATOM   1398 C  C     . TYR   A 1 187 ? -3.167  18.811  112.692 1.00 42.29  ? 1097 TYR   A C     1 
ATOM   1399 O  O     . TYR   A 1 187 ? -2.928  18.427  113.843 1.00 44.08  ? 1097 TYR   A O     1 
ATOM   1400 C  CB    . TYR   A 1 187 ? -1.503  19.518  110.932 1.00 35.10  ? 1097 TYR   A CB    1 
ATOM   1401 C  CG    . TYR   A 1 187 ? -1.056  20.655  110.064 1.00 37.51  ? 1097 TYR   A CG    1 
ATOM   1402 C  CD1   . TYR   A 1 187 ? -1.911  21.206  109.118 1.00 39.47  ? 1097 TYR   A CD1   1 
ATOM   1403 C  CD2   . TYR   A 1 187 ? 0.212   21.209  110.217 1.00 38.88  ? 1097 TYR   A CD2   1 
ATOM   1404 C  CE1   . TYR   A 1 187 ? -1.519  22.263  108.333 1.00 39.16  ? 1097 TYR   A CE1   1 
ATOM   1405 C  CE2   . TYR   A 1 187 ? 0.623   22.264  109.436 1.00 42.19  ? 1097 TYR   A CE2   1 
ATOM   1406 C  CZ    . TYR   A 1 187 ? -0.237  22.790  108.494 1.00 40.66  ? 1097 TYR   A CZ    1 
ATOM   1407 O  OH    . TYR   A 1 187 ? 0.177   23.843  107.717 1.00 35.39  ? 1097 TYR   A OH    1 
ATOM   1408 N  N     . CYS   A 1 188 ? -4.091  18.241  111.914 1.00 34.00  ? 1098 CYS   A N     1 
ATOM   1409 C  CA    . CYS   A 1 188 ? -4.956  17.166  112.391 1.00 37.87  ? 1098 CYS   A CA    1 
ATOM   1410 C  C     . CYS   A 1 188 ? -5.065  16.046  111.360 1.00 35.77  ? 1098 CYS   A C     1 
ATOM   1411 O  O     . CYS   A 1 188 ? -4.832  16.240  110.164 1.00 36.90  ? 1098 CYS   A O     1 
ATOM   1412 C  CB    . CYS   A 1 188 ? -6.353  17.695  112.722 1.00 34.79  ? 1098 CYS   A CB    1 
ATOM   1413 S  SG    . CYS   A 1 188 ? -6.353  18.780  114.148 1.00 39.98  ? 1098 CYS   A SG    1 
ATOM   1414 N  N     . ILE   A 1 189 ? -5.438  14.859  111.837 1.00 34.46  ? 1099 ILE   A N     1 
ATOM   1415 C  CA    . ILE   A 1 189 ? -5.803  13.749  110.966 1.00 32.03  ? 1099 ILE   A CA    1 
ATOM   1416 C  C     . ILE   A 1 189 ? -7.287  13.513  111.168 1.00 37.08  ? 1099 ILE   A C     1 
ATOM   1417 O  O     . ILE   A 1 189 ? -7.709  13.063  112.240 1.00 40.85  ? 1099 ILE   A O     1 
ATOM   1418 C  CB    . ILE   A 1 189 ? -5.018  12.463  111.266 1.00 31.40  ? 1099 ILE   A CB    1 
ATOM   1419 C  CG1   . ILE   A 1 189 ? -3.519  12.634  111.029 1.00 35.80  ? 1099 ILE   A CG1   1 
ATOM   1420 C  CG2   . ILE   A 1 189 ? -5.537  11.320  110.402 1.00 30.88  ? 1099 ILE   A CG2   1 
ATOM   1421 C  CD1   . ILE   A 1 189 ? -2.770  11.302  111.138 1.00 30.24  ? 1099 ILE   A CD1   1 
ATOM   1422 N  N     . ASP   A 1 190 ? -8.089  13.803  110.159 1.00 33.81  ? 1100 ASP   A N     1 
ATOM   1423 C  CA    . ASP   A 1 190 ? -9.511  13.518  110.235 1.00 35.04  ? 1100 ASP   A CA    1 
ATOM   1424 C  C     . ASP   A 1 190 ? -9.776  12.229  109.469 1.00 32.54  ? 1100 ASP   A C     1 
ATOM   1425 O  O     . ASP   A 1 190 ? -9.745  12.209  108.234 1.00 32.11  ? 1100 ASP   A O     1 
ATOM   1426 C  CB    . ASP   A 1 190 ? -10.351 14.676  109.698 1.00 36.71  ? 1100 ASP   A CB    1 
ATOM   1427 C  CG    . ASP   A 1 190 ? -11.821 14.530  110.048 1.00 34.50  ? 1100 ASP   A CG    1 
ATOM   1428 O  OD1   . ASP   A 1 190 ? -12.188 13.500  110.662 1.00 35.13  ? 1100 ASP   A OD1   1 
ATOM   1429 O  OD2   . ASP   A 1 190 ? -12.608 15.432  109.702 1.00 36.55  ? 1100 ASP   A OD2   1 
ATOM   1430 N  N     . ALA   A 1 191 ? -10.036 11.160  110.209 1.00 32.63  ? 1101 ALA   A N     1 
ATOM   1431 C  CA    . ALA   A 1 191 ? -10.358 9.858   109.644 1.00 32.26  ? 1101 ALA   A CA    1 
ATOM   1432 C  C     . ALA   A 1 191 ? -11.855 9.670   109.369 1.00 32.88  ? 1101 ALA   A C     1 
ATOM   1433 O  O     . ALA   A 1 191 ? -12.281 8.546   109.068 1.00 32.81  ? 1101 ALA   A O     1 
ATOM   1434 C  CB    . ALA   A 1 191 ? -9.855  8.750   110.572 1.00 32.14  ? 1101 ALA   A CB    1 
ATOM   1435 N  N     . ARG   A 1 192 ? -12.655 10.733  109.468 1.00 33.57  ? 1102 ARG   A N     1 
ATOM   1436 C  CA    . ARG   A 1 192 ? -14.106 10.610  109.288 1.00 34.28  ? 1102 ARG   A CA    1 
ATOM   1437 C  C     . ARG   A 1 192 ? -14.472 10.240  107.855 1.00 33.92  ? 1102 ARG   A C     1 
ATOM   1438 O  O     . ARG   A 1 192 ? -15.238 9.297   107.620 1.00 34.14  ? 1102 ARG   A O     1 
ATOM   1439 C  CB    . ARG   A 1 192 ? -14.790 11.917  109.679 1.00 35.13  ? 1102 ARG   A CB    1 
ATOM   1440 C  CG    . ARG   A 1 192 ? -16.148 12.153  108.983 1.00 38.48  ? 1102 ARG   A CG    1 
ATOM   1441 C  CD    . ARG   A 1 192 ? -17.214 11.236  109.521 1.00 41.54  ? 1102 ARG   A CD    1 
ATOM   1442 N  NE    . ARG   A 1 192 ? -18.487 11.390  108.825 1.00 44.27  ? 1102 ARG   A NE    1 
ATOM   1443 C  CZ    . ARG   A 1 192 ? -18.920 10.573  107.872 1.00 45.14  ? 1102 ARG   A CZ    1 
ATOM   1444 N  NH1   . ARG   A 1 192 ? -18.179 9.559   107.435 1.00 35.99  ? 1102 ARG   A NH1   1 
ATOM   1445 N  NH2   . ARG   A 1 192 ? -20.126 10.776  107.345 1.00 43.27  ? 1102 ARG   A NH2   1 
ATOM   1446 N  N     . TYR   A 1 193 ? -13.991 11.008  106.893 1.00 33.52  ? 1103 TYR   A N     1 
ATOM   1447 C  CA    . TYR   A 1 193 ? -14.270 10.751  105.489 1.00 33.28  ? 1103 TYR   A CA    1 
ATOM   1448 C  C     . TYR   A 1 193 ? -13.250 9.838   104.839 1.00 32.44  ? 1103 TYR   A C     1 
ATOM   1449 O  O     . TYR   A 1 193 ? -13.593 9.122   103.896 1.00 32.36  ? 1103 TYR   A O     1 
ATOM   1450 C  CB    . TYR   A 1 193 ? -14.331 12.079  104.727 1.00 33.44  ? 1103 TYR   A CB    1 
ATOM   1451 C  CG    . TYR   A 1 193 ? -15.393 12.974  105.296 1.00 34.35  ? 1103 TYR   A CG    1 
ATOM   1452 C  CD1   . TYR   A 1 193 ? -16.743 12.678  105.103 1.00 35.01  ? 1103 TYR   A CD1   1 
ATOM   1453 C  CD2   . TYR   A 1 193 ? -15.060 14.087  106.056 1.00 34.96  ? 1103 TYR   A CD2   1 
ATOM   1454 C  CE1   . TYR   A 1 193 ? -17.735 13.488  105.634 1.00 37.47  ? 1103 TYR   A CE1   1 
ATOM   1455 C  CE2   . TYR   A 1 193 ? -16.031 14.892  106.592 1.00 35.84  ? 1103 TYR   A CE2   1 
ATOM   1456 C  CZ    . TYR   A 1 193 ? -17.373 14.584  106.379 1.00 40.53  ? 1103 TYR   A CZ    1 
ATOM   1457 O  OH    . TYR   A 1 193 ? -18.351 15.374  106.909 1.00 45.02  ? 1103 TYR   A OH    1 
ATOM   1458 N  N     . TYR   A 1 194 ? -12.000 9.868   105.313 1.00 31.89  ? 1104 TYR   A N     1 
ATOM   1459 C  CA    . TYR   A 1 194 ? -10.916 9.055   104.778 1.00 31.14  ? 1104 TYR   A CA    1 
ATOM   1460 C  C     . TYR   A 1 194 ? -10.193 8.452   105.965 1.00 30.91  ? 1104 TYR   A C     1 
ATOM   1461 O  O     . TYR   A 1 194 ? -9.756  9.184   106.850 1.00 31.02  ? 1104 TYR   A O     1 
ATOM   1462 C  CB    . TYR   A 1 194 ? -9.950  9.887   103.937 1.00 30.75  ? 1104 TYR   A CB    1 
ATOM   1463 C  CG    . TYR   A 1 194 ? -10.558 10.519  102.710 1.00 31.22  ? 1104 TYR   A CG    1 
ATOM   1464 C  CD1   . TYR   A 1 194 ? -10.644 9.817   101.515 1.00 34.68  ? 1104 TYR   A CD1   1 
ATOM   1465 C  CD2   . TYR   A 1 194 ? -11.019 11.832  102.737 1.00 31.52  ? 1104 TYR   A CD2   1 
ATOM   1466 C  CE1   . TYR   A 1 194 ? -11.180 10.402  100.378 1.00 31.24  ? 1104 TYR   A CE1   1 
ATOM   1467 C  CE2   . TYR   A 1 194 ? -11.569 12.416  101.610 1.00 31.84  ? 1104 TYR   A CE2   1 
ATOM   1468 C  CZ    . TYR   A 1 194 ? -11.644 11.688  100.431 1.00 31.70  ? 1104 TYR   A CZ    1 
ATOM   1469 O  OH    . TYR   A 1 194 ? -12.186 12.246  99.294  1.00 38.75  ? 1104 TYR   A OH    1 
ATOM   1470 N  N     . GLY   A 1 195 ? -10.093 7.132   106.007 1.00 30.69  ? 1105 GLY   A N     1 
ATOM   1471 C  CA    . GLY   A 1 195 ? -9.501  6.504   107.173 1.00 30.59  ? 1105 GLY   A CA    1 
ATOM   1472 C  C     . GLY   A 1 195 ? -9.061  5.094   106.875 1.00 30.20  ? 1105 GLY   A C     1 
ATOM   1473 O  O     . GLY   A 1 195 ? -9.462  4.498   105.872 1.00 30.18  ? 1105 GLY   A O     1 
ATOM   1474 N  N     . ASN   A 1 196 ? -8.198  4.577   107.745 1.00 31.11  ? 1106 ASN   A N     1 
ATOM   1475 C  CA    . ASN   A 1 196 ? -7.840  3.174   107.707 1.00 30.02  ? 1106 ASN   A CA    1 
ATOM   1476 C  C     . ASN   A 1 196 ? -8.561  2.443   108.845 1.00 32.86  ? 1106 ASN   A C     1 
ATOM   1477 O  O     . ASN   A 1 196 ? -9.602  2.907   109.335 1.00 34.41  ? 1106 ASN   A O     1 
ATOM   1478 C  CB    . ASN   A 1 196 ? -6.317  3.020   107.751 1.00 29.08  ? 1106 ASN   A CB    1 
ATOM   1479 C  CG    . ASN   A 1 196 ? -5.746  3.196   109.137 1.00 30.33  ? 1106 ASN   A CG    1 
ATOM   1480 O  OD1   . ASN   A 1 196 ? -6.363  3.814   110.005 1.00 29.71  ? 1106 ASN   A OD1   1 
ATOM   1481 N  ND2   . ASN   A 1 196 ? -4.543  2.634   109.356 1.00 28.72  ? 1106 ASN   A ND2   1 
ATOM   1482 N  N     . ILE   A 1 197 ? -8.013  1.305   109.275 1.00 32.22  ? 1107 ILE   A N     1 
ATOM   1483 C  CA    . ILE   A 1 197 ? -8.686  0.489   110.281 1.00 32.29  ? 1107 ILE   A CA    1 
ATOM   1484 C  C     . ILE   A 1 197 ? -8.655  1.176   111.641 1.00 32.66  ? 1107 ILE   A C     1 
ATOM   1485 O  O     . ILE   A 1 197 ? -9.544  0.950   112.479 1.00 32.22  ? 1107 ILE   A O     1 
ATOM   1486 C  CB    . ILE   A 1 197 ? -8.036  -0.910  110.314 1.00 30.74  ? 1107 ILE   A CB    1 
ATOM   1487 C  CG1   . ILE   A 1 197 ? -8.741  -1.825  111.320 1.00 31.57  ? 1107 ILE   A CG1   1 
ATOM   1488 C  CG2   . ILE   A 1 197 ? -6.522  -0.790  110.601 1.00 30.06  ? 1107 ILE   A CG2   1 
ATOM   1489 C  CD1   . ILE   A 1 197 ? -10.117 -2.184  110.933 1.00 33.45  ? 1107 ILE   A CD1   1 
ATOM   1490 N  N     . SER   A 1 198 ? -7.646  2.036   111.867 1.00 30.93  ? 1108 SER   A N     1 
ATOM   1491 C  CA    . SER   A 1 198 ? -7.498  2.777   113.125 1.00 32.29  ? 1108 SER   A CA    1 
ATOM   1492 C  C     . SER   A 1 198 ? -8.739  3.569   113.532 1.00 32.25  ? 1108 SER   A C     1 
ATOM   1493 O  O     . SER   A 1 198 ? -8.980  3.768   114.725 1.00 33.00  ? 1108 SER   A O     1 
ATOM   1494 C  CB    . SER   A 1 198 ? -6.334  3.753   113.023 1.00 30.83  ? 1108 SER   A CB    1 
ATOM   1495 O  OG    . SER   A 1 198 ? -5.139  3.089   112.663 1.00 32.08  ? 1108 SER   A OG    1 
ATOM   1496 N  N     . ARG   A 1 199 ? -9.502  4.082   112.573 1.00 32.23  ? 1109 ARG   A N     1 
ATOM   1497 C  CA    . ARG   A 1 199 ? -10.624 4.933   112.948 1.00 33.08  ? 1109 ARG   A CA    1 
ATOM   1498 C  C     . ARG   A 1 199 ? -11.661 4.184   113.782 1.00 34.05  ? 1109 ARG   A C     1 
ATOM   1499 O  O     . ARG   A 1 199 ? -12.484 4.827   114.441 1.00 34.94  ? 1109 ARG   A O     1 
ATOM   1500 C  CB    . ARG   A 1 199 ? -11.272 5.525   111.698 1.00 32.91  ? 1109 ARG   A CB    1 
ATOM   1501 C  CG    . ARG   A 1 199 ? -12.203 4.566   111.012 1.00 35.48  ? 1109 ARG   A CG    1 
ATOM   1502 C  CD    . ARG   A 1 199 ? -12.512 4.983   109.585 1.00 34.22  ? 1109 ARG   A CD    1 
ATOM   1503 N  NE    . ARG   A 1 199 ? -13.458 6.088   109.520 1.00 37.99  ? 1109 ARG   A NE    1 
ATOM   1504 C  CZ    . ARG   A 1 199 ? -14.780 5.969   109.559 1.00 34.18  ? 1109 ARG   A CZ    1 
ATOM   1505 N  NH1   . ARG   A 1 199 ? -15.372 4.788   109.691 1.00 34.57  ? 1109 ARG   A NH1   1 
ATOM   1506 N  NH2   . ARG   A 1 199 ? -15.526 7.061   109.456 1.00 34.69  ? 1109 ARG   A NH2   1 
ATOM   1507 N  N     . PHE   A 1 200 ? -11.610 2.849   113.804 1.00 34.01  ? 1110 PHE   A N     1 
ATOM   1508 C  CA    . PHE   A 1 200 ? -12.553 2.022   114.548 1.00 35.01  ? 1110 PHE   A CA    1 
ATOM   1509 C  C     . PHE   A 1 200 ? -12.068 1.633   115.932 1.00 35.78  ? 1110 PHE   A C     1 
ATOM   1510 O  O     . PHE   A 1 200 ? -12.835 1.017   116.685 1.00 36.51  ? 1110 PHE   A O     1 
ATOM   1511 C  CB    . PHE   A 1 200 ? -12.860 0.745   113.771 1.00 34.87  ? 1110 PHE   A CB    1 
ATOM   1512 C  CG    . PHE   A 1 200 ? -13.550 0.996   112.484 1.00 34.67  ? 1110 PHE   A CG    1 
ATOM   1513 C  CD1   . PHE   A 1 200 ? -14.889 1.338   112.467 1.00 35.55  ? 1110 PHE   A CD1   1 
ATOM   1514 C  CD2   . PHE   A 1 200 ? -12.874 0.899   111.294 1.00 33.72  ? 1110 PHE   A CD2   1 
ATOM   1515 C  CE1   . PHE   A 1 200 ? -15.541 1.571   111.277 1.00 37.28  ? 1110 PHE   A CE1   1 
ATOM   1516 C  CE2   . PHE   A 1 200 ? -13.518 1.131   110.101 1.00 33.66  ? 1110 PHE   A CE2   1 
ATOM   1517 C  CZ    . PHE   A 1 200 ? -14.851 1.463   110.091 1.00 35.15  ? 1110 PHE   A CZ    1 
ATOM   1518 N  N     . ILE   A 1 201 ? -10.816 1.941   116.263 1.00 34.91  ? 1111 ILE   A N     1 
ATOM   1519 C  CA    . ILE   A 1 201 ? -10.279 1.640   117.583 1.00 35.42  ? 1111 ILE   A CA    1 
ATOM   1520 C  C     . ILE   A 1 201 ? -10.955 2.535   118.611 1.00 36.55  ? 1111 ILE   A C     1 
ATOM   1521 O  O     . ILE   A 1 201 ? -10.828 3.764   118.565 1.00 36.48  ? 1111 ILE   A O     1 
ATOM   1522 C  CB    . ILE   A 1 201 ? -8.760  1.836   117.614 1.00 34.73  ? 1111 ILE   A CB    1 
ATOM   1523 C  CG1   . ILE   A 1 201 ? -8.067  0.822   116.702 1.00 34.85  ? 1111 ILE   A CG1   1 
ATOM   1524 C  CG2   . ILE   A 1 201 ? -8.264  1.758   119.053 1.00 36.36  ? 1111 ILE   A CG2   1 
ATOM   1525 C  CD1   . ILE   A 1 201 ? -6.547  1.070   116.535 1.00 32.65  ? 1111 ILE   A CD1   1 
ATOM   1526 N  N     . ASN   A 1 202 ? -11.660 1.920   119.553 1.00 38.30  ? 1112 ASN   A N     1 
ATOM   1527 C  CA    . ASN   A 1 202 ? -12.393 2.662   120.562 1.00 38.99  ? 1112 ASN   A CA    1 
ATOM   1528 C  C     . ASN   A 1 202 ? -11.458 3.156   121.657 1.00 39.28  ? 1112 ASN   A C     1 
ATOM   1529 O  O     . ASN   A 1 202 ? -10.268 2.832   121.702 1.00 39.83  ? 1112 ASN   A O     1 
ATOM   1530 C  CB    . ASN   A 1 202 ? -13.491 1.790   121.161 1.00 40.26  ? 1112 ASN   A CB    1 
ATOM   1531 C  CG    . ASN   A 1 202 ? -14.617 1.518   120.179 1.00 40.87  ? 1112 ASN   A CG    1 
ATOM   1532 O  OD1   . ASN   A 1 202 ? -15.108 2.442   119.525 1.00 40.91  ? 1112 ASN   A OD1   1 
ATOM   1533 N  ND2   . ASN   A 1 202 ? -15.030 0.250   120.065 1.00 40.59  ? 1112 ASN   A ND2   1 
ATOM   1534 N  N     . HIS   A 1 203 ? -12.022 3.948   122.552 1.00 40.50  ? 1113 HIS   A N     1 
ATOM   1535 C  CA    . HIS   A 1 203 ? -11.304 4.490   123.693 1.00 43.74  ? 1113 HIS   A CA    1 
ATOM   1536 C  C     . HIS   A 1 203 ? -11.458 3.542   124.868 1.00 45.28  ? 1113 HIS   A C     1 
ATOM   1537 O  O     . HIS   A 1 203 ? -12.576 3.119   125.178 1.00 44.66  ? 1113 HIS   A O     1 
ATOM   1538 C  CB    . HIS   A 1 203 ? -11.857 5.868   124.070 1.00 48.24  ? 1113 HIS   A CB    1 
ATOM   1539 C  CG    . HIS   A 1 203 ? -11.463 6.329   125.442 1.00 49.52  ? 1113 HIS   A CG    1 
ATOM   1540 N  ND1   . HIS   A 1 203 ? -10.500 7.290   125.652 1.00 49.26  ? 1113 HIS   A ND1   1 
ATOM   1541 C  CD2   . HIS   A 1 203 ? -11.911 5.974   126.671 1.00 53.07  ? 1113 HIS   A CD2   1 
ATOM   1542 C  CE1   . HIS   A 1 203 ? -10.362 7.501   126.949 1.00 51.42  ? 1113 HIS   A CE1   1 
ATOM   1543 N  NE2   . HIS   A 1 203 ? -11.201 6.710   127.590 1.00 52.80  ? 1113 HIS   A NE2   1 
ATOM   1544 N  N     . LEU   A 1 204 ? -10.349 3.240   125.539 1.00 45.92  ? 1114 LEU   A N     1 
ATOM   1545 C  CA    . LEU   A 1 204 ? -10.377 2.454   126.765 1.00 48.98  ? 1114 LEU   A CA    1 
ATOM   1546 C  C     . LEU   A 1 204 ? -9.690  3.224   127.880 1.00 51.63  ? 1114 LEU   A C     1 
ATOM   1547 O  O     . LEU   A 1 204 ? -8.557  3.693   127.714 1.00 53.06  ? 1114 LEU   A O     1 
ATOM   1548 C  CB    . LEU   A 1 204 ? -9.707  1.091   126.576 1.00 47.46  ? 1114 LEU   A CB    1 
ATOM   1549 C  CG    . LEU   A 1 204 ? -10.347 0.170   125.543 1.00 42.08  ? 1114 LEU   A CG    1 
ATOM   1550 C  CD1   . LEU   A 1 204 ? -9.745  -1.199  125.647 1.00 43.32  ? 1114 LEU   A CD1   1 
ATOM   1551 C  CD2   . LEU   A 1 204 ? -11.845 0.101   125.745 1.00 51.77  ? 1114 LEU   A CD2   1 
ATOM   1552 N  N     . CYS   A 1 205 ? -10.369 3.337   129.022 1.00 54.51  ? 1115 CYS   A N     1 
ATOM   1553 C  CA    . CYS   A 1 205 ? -9.756  3.998   130.167 1.00 59.19  ? 1115 CYS   A CA    1 
ATOM   1554 C  C     . CYS   A 1 205 ? -8.510  3.261   130.645 1.00 58.70  ? 1115 CYS   A C     1 
ATOM   1555 O  O     . CYS   A 1 205 ? -7.612  3.876   131.233 1.00 61.43  ? 1115 CYS   A O     1 
ATOM   1556 C  CB    . CYS   A 1 205 ? -10.775 4.135   131.294 1.00 65.66  ? 1115 CYS   A CB    1 
ATOM   1557 S  SG    . CYS   A 1 205 ? -11.950 5.475   131.013 1.00 71.16  ? 1115 CYS   A SG    1 
ATOM   1558 N  N     . ASP   A 1 206 ? -8.431  1.957   130.392 1.00 55.40  ? 1116 ASP   A N     1 
ATOM   1559 C  CA    . ASP   A 1 206 ? -7.247  1.157   130.672 1.00 52.89  ? 1116 ASP   A CA    1 
ATOM   1560 C  C     . ASP   A 1 206 ? -6.645  0.696   129.349 1.00 50.54  ? 1116 ASP   A C     1 
ATOM   1561 O  O     . ASP   A 1 206 ? -6.762  -0.484  128.992 1.00 49.47  ? 1116 ASP   A O     1 
ATOM   1562 C  CB    . ASP   A 1 206 ? -7.596  -0.040  131.560 1.00 58.35  ? 1116 ASP   A CB    1 
ATOM   1563 C  CG    . ASP   A 1 206 ? -6.367  -0.729  132.115 1.00 54.86  ? 1116 ASP   A CG    1 
ATOM   1564 O  OD1   . ASP   A 1 206 ? -5.250  -0.272  131.819 1.00 49.20  ? 1116 ASP   A OD1   1 
ATOM   1565 O  OD2   . ASP   A 1 206 ? -6.522  -1.719  132.855 1.00 63.02  ? 1116 ASP   A OD2   1 
ATOM   1566 N  N     . PRO   A 1 207 ? -5.999  1.591   128.603 1.00 48.22  ? 1117 PRO   A N     1 
ATOM   1567 C  CA    . PRO   A 1 207 ? -5.595  1.264   127.232 1.00 46.06  ? 1117 PRO   A CA    1 
ATOM   1568 C  C     . PRO   A 1 207 ? -4.557  0.153   127.170 1.00 42.52  ? 1117 PRO   A C     1 
ATOM   1569 O  O     . PRO   A 1 207 ? -3.810  -0.111  128.114 1.00 44.94  ? 1117 PRO   A O     1 
ATOM   1570 C  CB    . PRO   A 1 207 ? -5.016  2.584   126.710 1.00 40.79  ? 1117 PRO   A CB    1 
ATOM   1571 C  CG    . PRO   A 1 207 ? -4.610  3.319   127.918 1.00 43.65  ? 1117 PRO   A CG    1 
ATOM   1572 C  CD    . PRO   A 1 207 ? -5.616  2.962   128.972 1.00 47.57  ? 1117 PRO   A CD    1 
ATOM   1573 N  N     . ASN   A 1 208 ? -4.522  -0.506  126.017 1.00 38.90  ? 1118 ASN   A N     1 
ATOM   1574 C  CA    . ASN   A 1 208 ? -3.499  -1.497  125.735 1.00 41.91  ? 1118 ASN   A CA    1 
ATOM   1575 C  C     . ASN   A 1 208 ? -2.698  -1.170  124.483 1.00 37.86  ? 1118 ASN   A C     1 
ATOM   1576 O  O     . ASN   A 1 208 ? -1.943  -2.030  124.010 1.00 40.68  ? 1118 ASN   A O     1 
ATOM   1577 C  CB    . ASN   A 1 208 ? -4.122  -2.893  125.621 1.00 39.90  ? 1118 ASN   A CB    1 
ATOM   1578 C  CG    . ASN   A 1 208 ? -5.180  -2.990  124.541 1.00 39.14  ? 1118 ASN   A CG    1 
ATOM   1579 O  OD1   . ASN   A 1 208 ? -5.169  -2.242  123.566 1.00 38.89  ? 1118 ASN   A OD1   1 
ATOM   1580 N  ND2   . ASN   A 1 208 ? -6.102  -3.937  124.707 1.00 40.90  ? 1118 ASN   A ND2   1 
ATOM   1581 N  N     . ILE   A 1 209 ? -2.875  0.026   123.913 1.00 36.12  ? 1119 ILE   A N     1 
ATOM   1582 C  CA    . ILE   A 1 209 ? -2.034  0.529   122.833 1.00 34.83  ? 1119 ILE   A CA    1 
ATOM   1583 C  C     . ILE   A 1 209 ? -1.770  2.008   123.083 1.00 37.25  ? 1119 ILE   A C     1 
ATOM   1584 O  O     . ILE   A 1 209 ? -2.566  2.706   123.721 1.00 39.58  ? 1119 ILE   A O     1 
ATOM   1585 C  CB    . ILE   A 1 209 ? -2.629  0.334   121.414 1.00 33.99  ? 1119 ILE   A CB    1 
ATOM   1586 C  CG1   . ILE   A 1 209 ? -3.820  1.273   121.156 1.00 36.06  ? 1119 ILE   A CG1   1 
ATOM   1587 C  CG2   . ILE   A 1 209 ? -3.041  -1.092  121.177 1.00 38.00  ? 1119 ILE   A CG2   1 
ATOM   1588 C  CD1   . ILE   A 1 209 ? -4.343  1.189   119.729 1.00 33.60  ? 1119 ILE   A CD1   1 
ATOM   1589 N  N     . ILE   A 1 210 ? -0.632  2.484   122.586 1.00 34.47  ? 1120 ILE   A N     1 
ATOM   1590 C  CA    . ILE   A 1 210 ? -0.301  3.899   122.725 1.00 34.37  ? 1120 ILE   A CA    1 
ATOM   1591 C  C     . ILE   A 1 210 ? 0.108   4.458   121.370 1.00 33.26  ? 1120 ILE   A C     1 
ATOM   1592 O  O     . ILE   A 1 210 ? 0.645   3.726   120.527 1.00 34.07  ? 1120 ILE   A O     1 
ATOM   1593 C  CB    . ILE   A 1 210 ? 0.797   4.124   123.774 1.00 37.17  ? 1120 ILE   A CB    1 
ATOM   1594 C  CG1   . ILE   A 1 210 ? 2.013   3.237   123.481 1.00 35.17  ? 1120 ILE   A CG1   1 
ATOM   1595 C  CG2   . ILE   A 1 210 ? 0.251   3.897   125.173 1.00 36.26  ? 1120 ILE   A CG2   1 
ATOM   1596 C  CD1   . ILE   A 1 210 ? 3.147   3.482   124.424 1.00 43.50  ? 1120 ILE   A CD1   1 
ATOM   1597 N  N     . PRO   A 1 211 ? -0.146  5.737   121.109 1.00 33.41  ? 1121 PRO   A N     1 
ATOM   1598 C  CA    . PRO   A 1 211 ? 0.311   6.338   119.858 1.00 33.63  ? 1121 PRO   A CA    1 
ATOM   1599 C  C     . PRO   A 1 211 ? 1.715   6.909   120.009 1.00 34.70  ? 1121 PRO   A C     1 
ATOM   1600 O  O     . PRO   A 1 211 ? 2.086   7.462   121.047 1.00 35.01  ? 1121 PRO   A O     1 
ATOM   1601 C  CB    . PRO   A 1 211 ? -0.729  7.443   119.622 1.00 34.70  ? 1121 PRO   A CB    1 
ATOM   1602 C  CG    . PRO   A 1 211 ? -1.092  7.889   121.007 1.00 34.21  ? 1121 PRO   A CG    1 
ATOM   1603 C  CD    . PRO   A 1 211 ? -0.960  6.673   121.906 1.00 34.54  ? 1121 PRO   A CD    1 
ATOM   1604 N  N     . VAL   A 1 212 ? 2.507   6.749   118.951 1.00 35.36  ? 1122 VAL   A N     1 
ATOM   1605 C  CA    . VAL   A 1 212 ? 3.864   7.275   118.866 1.00 32.31  ? 1122 VAL   A CA    1 
ATOM   1606 C  C     . VAL   A 1 212 ? 3.960   8.103   117.592 1.00 30.59  ? 1122 VAL   A C     1 
ATOM   1607 O  O     . VAL   A 1 212 ? 3.415   7.717   116.550 1.00 31.17  ? 1122 VAL   A O     1 
ATOM   1608 C  CB    . VAL   A 1 212 ? 4.916   6.134   118.857 1.00 33.55  ? 1122 VAL   A CB    1 
ATOM   1609 C  CG1   . VAL   A 1 212 ? 6.347   6.693   118.807 1.00 31.51  ? 1122 VAL   A CG1   1 
ATOM   1610 C  CG2   . VAL   A 1 212 ? 4.743   5.217   120.057 1.00 32.53  ? 1122 VAL   A CG2   1 
ATOM   1611 N  N     . ARG   A 1 213 ? 4.654   9.237   117.670 1.00 30.89  ? 1123 ARG   A N     1 
ATOM   1612 C  CA    . ARG   A 1 213 ? 4.867   10.083  116.503 1.00 30.52  ? 1123 ARG   A CA    1 
ATOM   1613 C  C     . ARG   A 1 213 ? 6.131   9.608   115.798 1.00 31.66  ? 1123 ARG   A C     1 
ATOM   1614 O  O     . ARG   A 1 213 ? 7.203   9.540   116.414 1.00 31.71  ? 1123 ARG   A O     1 
ATOM   1615 C  CB    . ARG   A 1 213 ? 4.994   11.561  116.882 1.00 32.13  ? 1123 ARG   A CB    1 
ATOM   1616 C  CG    . ARG   A 1 213 ? 4.169   12.029  118.066 1.00 38.24  ? 1123 ARG   A CG    1 
ATOM   1617 C  CD    . ARG   A 1 213 ? 2.711   11.741  117.871 1.00 37.01  ? 1123 ARG   A CD    1 
ATOM   1618 N  NE    . ARG   A 1 213 ? 1.874   12.838  118.334 1.00 43.37  ? 1123 ARG   A NE    1 
ATOM   1619 C  CZ    . ARG   A 1 213 ? 0.886   12.722  119.211 1.00 47.98  ? 1123 ARG   A CZ    1 
ATOM   1620 N  NH1   . ARG   A 1 213 ? 0.581   11.557  119.765 1.00 46.95  ? 1123 ARG   A NH1   1 
ATOM   1621 N  NH2   . ARG   A 1 213 ? 0.182   13.800  119.537 1.00 48.71  ? 1123 ARG   A NH2   1 
ATOM   1622 N  N     . VAL   A 1 214 ? 6.011   9.291   114.512 1.00 30.73  ? 1124 VAL   A N     1 
ATOM   1623 C  CA    . VAL   A 1 214 ? 7.100   8.701   113.750 1.00 32.35  ? 1124 VAL   A CA    1 
ATOM   1624 C  C     . VAL   A 1 214 ? 7.347   9.517   112.488 1.00 32.97  ? 1124 VAL   A C     1 
ATOM   1625 O  O     . VAL   A 1 214 ? 6.447   10.186  111.964 1.00 28.46  ? 1124 VAL   A O     1 
ATOM   1626 C  CB    . VAL   A 1 214 ? 6.803   7.230   113.385 1.00 29.78  ? 1124 VAL   A CB    1 
ATOM   1627 C  CG1   . VAL   A 1 214 ? 8.082   6.541   112.922 1.00 32.56  ? 1124 VAL   A CG1   1 
ATOM   1628 C  CG2   . VAL   A 1 214 ? 6.223   6.516   114.565 1.00 28.43  ? 1124 VAL   A CG2   1 
ATOM   1629 N  N     . PHE   A 1 215 ? 8.590   9.439   111.989 1.00 29.49  ? 1125 PHE   A N     1 
ATOM   1630 C  CA    . PHE   A 1 215 ? 8.993   10.064  110.740 1.00 27.98  ? 1125 PHE   A CA    1 
ATOM   1631 C  C     . PHE   A 1 215 ? 9.670   9.021   109.872 1.00 29.93  ? 1125 PHE   A C     1 
ATOM   1632 O  O     . PHE   A 1 215 ? 10.481  8.227   110.353 1.00 31.13  ? 1125 PHE   A O     1 
ATOM   1633 C  CB    . PHE   A 1 215 ? 9.927   11.260  110.989 1.00 31.48  ? 1125 PHE   A CB    1 
ATOM   1634 C  CG    . PHE   A 1 215 ? 9.263   12.367  111.734 1.00 32.57  ? 1125 PHE   A CG    1 
ATOM   1635 C  CD1   . PHE   A 1 215 ? 8.357   13.200  111.087 1.00 29.43  ? 1125 PHE   A CD1   1 
ATOM   1636 C  CD2   . PHE   A 1 215 ? 9.495   12.542  113.090 1.00 30.27  ? 1125 PHE   A CD2   1 
ATOM   1637 C  CE1   . PHE   A 1 215 ? 7.710   14.192  111.766 1.00 30.13  ? 1125 PHE   A CE1   1 
ATOM   1638 C  CE2   . PHE   A 1 215 ? 8.850   13.538  113.778 1.00 31.93  ? 1125 PHE   A CE2   1 
ATOM   1639 C  CZ    . PHE   A 1 215 ? 7.948   14.366  113.115 1.00 34.11  ? 1125 PHE   A CZ    1 
ATOM   1640 N  N     . MET   A 1 216 ? 9.320   9.017   108.593 1.00 27.17  ? 1126 MET   A N     1 
ATOM   1641 C  CA    . MET   A 1 216 ? 9.785   7.973   107.706 1.00 29.44  ? 1126 MET   A CA    1 
ATOM   1642 C  C     . MET   A 1 216 ? 10.272  8.556   106.383 1.00 30.84  ? 1126 MET   A C     1 
ATOM   1643 O  O     . MET   A 1 216 ? 11.468  8.837   106.243 1.00 29.99  ? 1126 MET   A O     1 
ATOM   1644 C  CB    . MET   A 1 216 ? 8.681   6.927   107.508 1.00 26.40  ? 1126 MET   A CB    1 
ATOM   1645 C  CG    . MET   A 1 216 ? 8.601   5.911   108.650 1.00 28.17  ? 1126 MET   A CG    1 
ATOM   1646 S  SD    . MET   A 1 216 ? 6.966   5.103   108.889 1.00 31.43  ? 1126 MET   A SD    1 
ATOM   1647 C  CE    . MET   A 1 216 ? 6.039   6.542   109.407 1.00 26.70  ? 1126 MET   A CE    1 
ATOM   1648 N  N     . LEU   A 1 217 ? 9.384   8.741   105.405 1.00 26.84  ? 1127 LEU   A N     1 
ATOM   1649 C  CA    . LEU   A 1 217 ? 9.868   9.193   104.106 1.00 30.05  ? 1127 LEU   A CA    1 
ATOM   1650 C  C     . LEU   A 1 217 ? 10.163  10.689  104.066 1.00 31.89  ? 1127 LEU   A C     1 
ATOM   1651 O  O     . LEU   A 1 217 ? 10.873  11.135  103.156 1.00 30.53  ? 1127 LEU   A O     1 
ATOM   1652 C  CB    . LEU   A 1 217 ? 8.869   8.858   103.002 1.00 32.28  ? 1127 LEU   A CB    1 
ATOM   1653 C  CG    . LEU   A 1 217 ? 8.414   7.425   102.712 1.00 35.12  ? 1127 LEU   A CG    1 
ATOM   1654 C  CD1   . LEU   A 1 217 ? 7.327   7.478   101.629 1.00 36.03  ? 1127 LEU   A CD1   1 
ATOM   1655 C  CD2   . LEU   A 1 217 ? 9.553   6.528   102.278 1.00 29.21  ? 1127 LEU   A CD2   1 
ATOM   1656 N  N     . HIS   A 1 218 ? 9.607   11.471  104.999 1.00 27.85  ? 1128 HIS   A N     1 
ATOM   1657 C  CA    . HIS   A 1 218 ? 9.906   12.887  105.127 1.00 31.45  ? 1128 HIS   A CA    1 
ATOM   1658 C  C     . HIS   A 1 218 ? 10.130  13.206  106.595 1.00 28.81  ? 1128 HIS   A C     1 
ATOM   1659 O  O     . HIS   A 1 218 ? 9.737   12.453  107.484 1.00 29.70  ? 1128 HIS   A O     1 
ATOM   1660 C  CB    . HIS   A 1 218 ? 8.773   13.767  104.578 1.00 31.09  ? 1128 HIS   A CB    1 
ATOM   1661 C  CG    . HIS   A 1 218 ? 7.525   13.700  105.397 1.00 28.91  ? 1128 HIS   A CG    1 
ATOM   1662 N  ND1   . HIS   A 1 218 ? 7.402   14.336  106.611 1.00 29.11  ? 1128 HIS   A ND1   1 
ATOM   1663 C  CD2   . HIS   A 1 218 ? 6.362   13.034  105.200 1.00 28.38  ? 1128 HIS   A CD2   1 
ATOM   1664 C  CE1   . HIS   A 1 218 ? 6.211   14.084  107.120 1.00 29.03  ? 1128 HIS   A CE1   1 
ATOM   1665 N  NE2   . HIS   A 1 218 ? 5.562   13.291  106.286 1.00 31.67  ? 1128 HIS   A NE2   1 
ATOM   1666 N  N     . GLN   A 1 219 ? 10.759  14.332  106.858 1.00 30.15  ? 1129 GLN   A N     1 
ATOM   1667 C  CA    . GLN   A 1 219 ? 10.950  14.719  108.246 1.00 30.86  ? 1129 GLN   A CA    1 
ATOM   1668 C  C     . GLN   A 1 219 ? 10.381  16.105  108.488 1.00 31.24  ? 1129 GLN   A C     1 
ATOM   1669 O  O     . GLN   A 1 219 ? 10.967  16.924  109.201 1.00 37.95  ? 1129 GLN   A O     1 
ATOM   1670 C  CB    . GLN   A 1 219 ? 12.424  14.617  108.636 1.00 29.95  ? 1129 GLN   A CB    1 
ATOM   1671 C  CG    . GLN   A 1 219 ? 12.976  13.185  108.487 1.00 29.25  ? 1129 GLN   A CG    1 
ATOM   1672 C  CD    . GLN   A 1 219 ? 14.514  13.094  108.517 1.00 32.89  ? 1129 GLN   A CD    1 
ATOM   1673 O  OE1   . GLN   A 1 219 ? 15.212  14.106  108.578 1.00 30.22  ? 1129 GLN   A OE1   1 
ATOM   1674 N  NE2   . GLN   A 1 219 ? 15.038  11.860  108.465 1.00 28.95  ? 1129 GLN   A NE2   1 
ATOM   1675 N  N     . ASP   A 1 220 ? 9.222   16.391  107.890 1.00 33.05  ? 1130 ASP   A N     1 
ATOM   1676 C  CA    . ASP   A 1 220 ? 8.535   17.668  108.101 1.00 33.67  ? 1130 ASP   A CA    1 
ATOM   1677 C  C     . ASP   A 1 220 ? 7.846   17.599  109.451 1.00 31.76  ? 1130 ASP   A C     1 
ATOM   1678 O  O     . ASP   A 1 220 ? 6.870   16.858  109.621 1.00 33.38  ? 1130 ASP   A O     1 
ATOM   1679 C  CB    . ASP   A 1 220 ? 7.533   17.948  106.982 1.00 31.15  ? 1130 ASP   A CB    1 
ATOM   1680 C  CG    . ASP   A 1 220 ? 6.956   19.367  107.039 1.00 33.24  ? 1130 ASP   A CG    1 
ATOM   1681 O  OD1   . ASP   A 1 220 ? 6.556   19.802  108.134 1.00 34.26  ? 1130 ASP   A OD1   1 
ATOM   1682 O  OD2   . ASP   A 1 220 ? 6.915   20.053  105.988 1.00 32.34  ? 1130 ASP   A OD2   1 
ATOM   1683 N  N     . LEU   A 1 221 ? 8.364   18.358  110.415 1.00 32.16  ? 1131 LEU   A N     1 
ATOM   1684 C  CA    . LEU   A 1 221 ? 7.965   18.177  111.805 1.00 35.53  ? 1131 LEU   A CA    1 
ATOM   1685 C  C     . LEU   A 1 221 ? 6.508   18.521  112.074 1.00 32.75  ? 1131 LEU   A C     1 
ATOM   1686 O  O     . LEU   A 1 221 ? 6.037   18.269  113.186 1.00 35.39  ? 1131 LEU   A O     1 
ATOM   1687 C  CB    . LEU   A 1 221 ? 8.861   19.011  112.715 1.00 33.38  ? 1131 LEU   A CB    1 
ATOM   1688 C  CG    . LEU   A 1 221 ? 10.278  18.462  112.769 1.00 33.13  ? 1131 LEU   A CG    1 
ATOM   1689 C  CD1   . LEU   A 1 221 ? 11.270  19.582  113.089 1.00 34.13  ? 1131 LEU   A CD1   1 
ATOM   1690 C  CD2   . LEU   A 1 221 ? 10.363  17.341  113.786 1.00 32.78  ? 1131 LEU   A CD2   1 
ATOM   1691 N  N     . ARG   A 1 222 ? 5.805   19.123  111.115 1.00 34.03  ? 1132 ARG   A N     1 
ATOM   1692 C  CA    . ARG   A 1 222 ? 4.391   19.427  111.279 1.00 36.07  ? 1132 ARG   A CA    1 
ATOM   1693 C  C     . ARG   A 1 222 ? 3.502   18.234  110.959 1.00 37.93  ? 1132 ARG   A C     1 
ATOM   1694 O  O     . ARG   A 1 222 ? 2.287   18.316  111.169 1.00 38.31  ? 1132 ARG   A O     1 
ATOM   1695 C  CB    . ARG   A 1 222 ? 4.006   20.610  110.391 1.00 35.68  ? 1132 ARG   A CB    1 
ATOM   1696 C  CG    . ARG   A 1 222 ? 4.895   21.823  110.568 1.00 38.92  ? 1132 ARG   A CG    1 
ATOM   1697 C  CD    . ARG   A 1 222 ? 4.610   22.834  109.479 1.00 42.36  ? 1132 ARG   A CD    1 
ATOM   1698 N  NE    . ARG   A 1 222 ? 5.076   22.383  108.172 1.00 36.93  ? 1132 ARG   A NE    1 
ATOM   1699 C  CZ    . ARG   A 1 222 ? 4.562   22.779  107.015 1.00 39.77  ? 1132 ARG   A CZ    1 
ATOM   1700 N  NH1   . ARG   A 1 222 ? 3.525   23.619  106.963 1.00 34.92  ? 1132 ARG   A NH1   1 
ATOM   1701 N  NH2   . ARG   A 1 222 ? 5.078   22.303  105.884 1.00 33.80  ? 1132 ARG   A NH2   1 
ATOM   1702 N  N     . PHE   A 1 223 ? 4.074   17.135  110.461 1.00 34.64  ? 1133 PHE   A N     1 
ATOM   1703 C  CA    . PHE   A 1 223 ? 3.299   15.993  109.984 1.00 30.73  ? 1133 PHE   A CA    1 
ATOM   1704 C  C     . PHE   A 1 223 ? 3.925   14.684  110.453 1.00 31.65  ? 1133 PHE   A C     1 
ATOM   1705 O  O     . PHE   A 1 223 ? 4.299   13.831  109.644 1.00 29.48  ? 1133 PHE   A O     1 
ATOM   1706 C  CB    . PHE   A 1 223 ? 3.185   16.030  108.461 1.00 30.37  ? 1133 PHE   A CB    1 
ATOM   1707 C  CG    . PHE   A 1 223 ? 2.493   17.246  107.944 1.00 36.34  ? 1133 PHE   A CG    1 
ATOM   1708 C  CD1   . PHE   A 1 223 ? 1.108   17.299  107.890 1.00 35.09  ? 1133 PHE   A CD1   1 
ATOM   1709 C  CD2   . PHE   A 1 223 ? 3.219   18.348  107.521 1.00 33.63  ? 1133 PHE   A CD2   1 
ATOM   1710 C  CE1   . PHE   A 1 223 ? 0.469   18.427  107.412 1.00 35.39  ? 1133 PHE   A CE1   1 
ATOM   1711 C  CE2   . PHE   A 1 223 ? 2.585   19.469  107.037 1.00 32.08  ? 1133 PHE   A CE2   1 
ATOM   1712 C  CZ    . PHE   A 1 223 ? 1.206   19.512  106.985 1.00 38.38  ? 1133 PHE   A CZ    1 
ATOM   1713 N  N     . PRO   A 1 224 ? 4.019   14.469  111.764 1.00 33.14  ? 1134 PRO   A N     1 
ATOM   1714 C  CA    . PRO   A 1 224 ? 4.302   13.118  112.240 1.00 29.96  ? 1134 PRO   A CA    1 
ATOM   1715 C  C     . PRO   A 1 224 ? 3.181   12.175  111.835 1.00 32.09  ? 1134 PRO   A C     1 
ATOM   1716 O  O     . PRO   A 1 224 ? 2.027   12.578  111.657 1.00 32.38  ? 1134 PRO   A O     1 
ATOM   1717 C  CB    . PRO   A 1 224 ? 4.377   13.277  113.761 1.00 30.62  ? 1134 PRO   A CB    1 
ATOM   1718 C  CG    . PRO   A 1 224 ? 3.548   14.479  114.049 1.00 35.31  ? 1134 PRO   A CG    1 
ATOM   1719 C  CD    . PRO   A 1 224 ? 3.787   15.399  112.887 1.00 37.00  ? 1134 PRO   A CD    1 
ATOM   1720 N  N     . ARG   A 1 225 ? 3.553   10.921  111.646 1.00 31.84  ? 1135 ARG   A N     1 
ATOM   1721 C  CA    . ARG   A 1 225 ? 2.628   9.838   111.374 1.00 33.56  ? 1135 ARG   A CA    1 
ATOM   1722 C  C     . ARG   A 1 225 ? 2.391   9.092   112.681 1.00 33.29  ? 1135 ARG   A C     1 
ATOM   1723 O  O     . ARG   A 1 225 ? 3.321   8.907   113.474 1.00 35.80  ? 1135 ARG   A O     1 
ATOM   1724 C  CB    . ARG   A 1 225 ? 3.198   8.926   110.279 1.00 27.74  ? 1135 ARG   A CB    1 
ATOM   1725 C  CG    . ARG   A 1 225 ? 3.157   9.596   108.902 1.00 29.18  ? 1135 ARG   A CG    1 
ATOM   1726 C  CD    . ARG   A 1 225 ? 3.871   8.813   107.803 1.00 30.61  ? 1135 ARG   A CD    1 
ATOM   1727 N  NE    . ARG   A 1 225 ? 3.321   7.479   107.582 1.00 28.66  ? 1135 ARG   A NE    1 
ATOM   1728 C  CZ    . ARG   A 1 225 ? 3.821   6.602   106.718 1.00 29.29  ? 1135 ARG   A CZ    1 
ATOM   1729 N  NH1   . ARG   A 1 225 ? 4.868   6.898   105.956 1.00 31.66  ? 1135 ARG   A NH1   1 
ATOM   1730 N  NH2   . ARG   A 1 225 ? 3.277   5.390   106.630 1.00 28.42  ? 1135 ARG   A NH2   1 
ATOM   1731 N  N     . ILE   A 1 226 ? 1.147   8.703   112.924 1.00 29.57  ? 1136 ILE   A N     1 
ATOM   1732 C  CA    . ILE   A 1 226 ? 0.743   8.179   114.224 1.00 33.76  ? 1136 ILE   A CA    1 
ATOM   1733 C  C     . ILE   A 1 226 ? 0.783   6.652   114.177 1.00 33.15  ? 1136 ILE   A C     1 
ATOM   1734 O  O     . ILE   A 1 226 ? -0.000  6.015   113.462 1.00 31.41  ? 1136 ILE   A O     1 
ATOM   1735 C  CB    . ILE   A 1 226 ? -0.639  8.701   114.628 1.00 30.85  ? 1136 ILE   A CB    1 
ATOM   1736 C  CG1   . ILE   A 1 226 ? -0.639  10.215  114.522 1.00 33.43  ? 1136 ILE   A CG1   1 
ATOM   1737 C  CG2   . ILE   A 1 226 ? -0.940  8.346   116.068 1.00 31.17  ? 1136 ILE   A CG2   1 
ATOM   1738 C  CD1   . ILE   A 1 226 ? 0.148   10.884  115.621 1.00 35.86  ? 1136 ILE   A CD1   1 
ATOM   1739 N  N     . ALA   A 1 227 ? 1.696   6.066   114.946 1.00 31.88  ? 1137 ALA   A N     1 
ATOM   1740 C  CA    . ALA   A 1 227 ? 1.884   4.624   115.007 1.00 30.15  ? 1137 ALA   A CA    1 
ATOM   1741 C  C     . ALA   A 1 227 ? 1.422   4.114   116.361 1.00 30.70  ? 1137 ALA   A C     1 
ATOM   1742 O  O     . ALA   A 1 227 ? 1.769   4.684   117.402 1.00 34.02  ? 1137 ALA   A O     1 
ATOM   1743 C  CB    . ALA   A 1 227 ? 3.353   4.247   114.783 1.00 33.12  ? 1137 ALA   A CB    1 
ATOM   1744 N  N     . PHE   A 1 228 ? 0.650   3.046   116.347 1.00 32.14  ? 1138 PHE   A N     1 
ATOM   1745 C  CA    . PHE   A 1 228 ? 0.167   2.432   117.571 1.00 33.01  ? 1138 PHE   A CA    1 
ATOM   1746 C  C     . PHE   A 1 228 ? 1.053   1.249   117.923 1.00 31.27  ? 1138 PHE   A C     1 
ATOM   1747 O  O     . PHE   A 1 228 ? 1.416   0.458   117.051 1.00 30.53  ? 1138 PHE   A O     1 
ATOM   1748 C  CB    . PHE   A 1 228 ? -1.286  1.983   117.423 1.00 28.52  ? 1138 PHE   A CB    1 
ATOM   1749 C  CG    . PHE   A 1 228 ? -2.272  3.108   117.491 1.00 31.12  ? 1138 PHE   A CG    1 
ATOM   1750 C  CD1   . PHE   A 1 228 ? -2.448  3.819   118.665 1.00 32.25  ? 1138 PHE   A CD1   1 
ATOM   1751 C  CD2   . PHE   A 1 228 ? -3.033  3.449   116.389 1.00 31.22  ? 1138 PHE   A CD2   1 
ATOM   1752 C  CE1   . PHE   A 1 228 ? -3.358  4.850   118.732 1.00 33.42  ? 1138 PHE   A CE1   1 
ATOM   1753 C  CE2   . PHE   A 1 228 ? -3.937  4.477   116.451 1.00 30.10  ? 1138 PHE   A CE2   1 
ATOM   1754 C  CZ    . PHE   A 1 228 ? -4.106  5.179   117.624 1.00 31.51  ? 1138 PHE   A CZ    1 
ATOM   1755 N  N     . PHE   A 1 229 ? 1.398   1.147   119.198 1.00 31.26  ? 1139 PHE   A N     1 
ATOM   1756 C  CA    . PHE   A 1 229 ? 2.137   0.027   119.739 1.00 35.45  ? 1139 PHE   A CA    1 
ATOM   1757 C  C     . PHE   A 1 229 ? 1.420   -0.441  120.993 1.00 35.32  ? 1139 PHE   A C     1 
ATOM   1758 O  O     . PHE   A 1 229 ? 0.856   0.369   121.730 1.00 32.64  ? 1139 PHE   A O     1 
ATOM   1759 C  CB    . PHE   A 1 229 ? 3.600   0.402   120.084 1.00 31.02  ? 1139 PHE   A CB    1 
ATOM   1760 C  CG    . PHE   A 1 229 ? 4.412   0.858   118.902 1.00 33.57  ? 1139 PHE   A CG    1 
ATOM   1761 C  CD1   . PHE   A 1 229 ? 4.345   2.168   118.457 1.00 33.20  ? 1139 PHE   A CD1   1 
ATOM   1762 C  CD2   . PHE   A 1 229 ? 5.264   -0.017  118.249 1.00 34.19  ? 1139 PHE   A CD2   1 
ATOM   1763 C  CE1   . PHE   A 1 229 ? 5.092   2.587   117.378 1.00 30.67  ? 1139 PHE   A CE1   1 
ATOM   1764 C  CE2   . PHE   A 1 229 ? 6.014   0.399   117.167 1.00 32.61  ? 1139 PHE   A CE2   1 
ATOM   1765 C  CZ    . PHE   A 1 229 ? 5.927   1.701   116.733 1.00 33.26  ? 1139 PHE   A CZ    1 
ATOM   1766 N  N     . SER   A 1 230 ? 1.464   -1.751  121.238 1.00 37.15  ? 1140 SER   A N     1 
ATOM   1767 C  CA    . SER   A 1 230 ? 0.885   -2.308  122.452 1.00 39.46  ? 1140 SER   A CA    1 
ATOM   1768 C  C     . SER   A 1 230 ? 1.669   -1.851  123.676 1.00 41.84  ? 1140 SER   A C     1 
ATOM   1769 O  O     . SER   A 1 230 ? 2.891   -2.000  123.733 1.00 40.74  ? 1140 SER   A O     1 
ATOM   1770 C  CB    . SER   A 1 230 ? 0.862   -3.835  122.376 1.00 39.52  ? 1140 SER   A CB    1 
ATOM   1771 O  OG    . SER   A 1 230 ? 2.096   -4.361  121.923 1.00 34.60  ? 1140 SER   A OG    1 
ATOM   1772 N  N     . SER   A 1 231 ? 0.967   -1.279  124.655 1.00 46.03  ? 1141 SER   A N     1 
ATOM   1773 C  CA    . SER   A 1 231 ? 1.616   -0.889  125.902 1.00 47.76  ? 1141 SER   A CA    1 
ATOM   1774 C  C     . SER   A 1 231 ? 1.756   -2.053  126.869 1.00 46.98  ? 1141 SER   A C     1 
ATOM   1775 O  O     . SER   A 1 231 ? 2.339   -1.881  127.948 1.00 50.27  ? 1141 SER   A O     1 
ATOM   1776 C  CB    . SER   A 1 231 ? 0.845   0.250   126.565 1.00 48.05  ? 1141 SER   A CB    1 
ATOM   1777 O  OG    . SER   A 1 231 ? -0.510  -0.114  126.740 1.00 52.62  ? 1141 SER   A OG    1 
ATOM   1778 N  N     . ARG   A 1 232 ? 1.254   -3.225  126.488 1.00 43.31  ? 1142 ARG   A N     1 
ATOM   1779 C  CA    . ARG   A 1 232 ? 1.285   -4.430  127.304 1.00 44.59  ? 1142 ARG   A CA    1 
ATOM   1780 C  C     . ARG   A 1 232 ? 1.067   -5.620  126.382 1.00 43.21  ? 1142 ARG   A C     1 
ATOM   1781 O  O     . ARG   A 1 232 ? 0.834   -5.457  125.184 1.00 40.55  ? 1142 ARG   A O     1 
ATOM   1782 C  CB    . ARG   A 1 232 ? 0.221   -4.390  128.407 1.00 47.78  ? 1142 ARG   A CB    1 
ATOM   1783 C  CG    . ARG   A 1 232 ? -1.210  -4.149  127.902 1.00 48.09  ? 1142 ARG   A CG    1 
ATOM   1784 C  CD    . ARG   A 1 232 ? -2.246  -4.565  128.938 1.00 44.74  ? 1142 ARG   A CD    1 
ATOM   1785 N  NE    . ARG   A 1 232 ? -3.622  -4.325  128.514 1.00 47.94  ? 1142 ARG   A NE    1 
ATOM   1786 C  CZ    . ARG   A 1 232 ? -4.468  -5.264  128.097 1.00 49.97  ? 1142 ARG   A CZ    1 
ATOM   1787 N  NH1   . ARG   A 1 232 ? -4.099  -6.533  127.975 1.00 47.44  ? 1142 ARG   A NH1   1 
ATOM   1788 N  NH2   . ARG   A 1 232 ? -5.723  -4.925  127.803 1.00 51.68  ? 1142 ARG   A NH2   1 
ATOM   1789 N  N     . ASP   A 1 233 ? 1.161   -6.821  126.955 1.00 43.33  ? 1143 ASP   A N     1 
ATOM   1790 C  CA    . ASP   A 1 233 ? 0.779   -8.036  126.238 1.00 46.60  ? 1143 ASP   A CA    1 
ATOM   1791 C  C     . ASP   A 1 233 ? -0.719  -8.055  125.950 1.00 47.85  ? 1143 ASP   A C     1 
ATOM   1792 O  O     . ASP   A 1 233 ? -1.542  -7.770  126.828 1.00 50.20  ? 1143 ASP   A O     1 
ATOM   1793 C  CB    . ASP   A 1 233 ? 1.140   -9.282  127.051 1.00 48.93  ? 1143 ASP   A CB    1 
ATOM   1794 C  CG    . ASP   A 1 233 ? 2.639   -9.475  127.205 1.00 47.60  ? 1143 ASP   A CG    1 
ATOM   1795 O  OD1   . ASP   A 1 233 ? 3.409   -8.986  126.354 1.00 44.73  ? 1143 ASP   A OD1   1 
ATOM   1796 O  OD2   . ASP   A 1 233 ? 3.043   -10.134 128.182 1.00 53.96  ? 1143 ASP   A OD2   1 
ATOM   1797 N  N     . ILE   A 1 234 ? -1.082  -8.416  124.719 1.00 48.08  ? 1144 ILE   A N     1 
ATOM   1798 C  CA    . ILE   A 1 234 ? -2.484  -8.442  124.299 1.00 40.97  ? 1144 ILE   A CA    1 
ATOM   1799 C  C     . ILE   A 1 234 ? -2.894  -9.884  124.043 1.00 45.14  ? 1144 ILE   A C     1 
ATOM   1800 O  O     . ILE   A 1 234 ? -2.314  -10.563 123.186 1.00 41.94  ? 1144 ILE   A O     1 
ATOM   1801 C  CB    . ILE   A 1 234 ? -2.725  -7.578  123.056 1.00 40.07  ? 1144 ILE   A CB    1 
ATOM   1802 C  CG1   . ILE   A 1 234 ? -2.417  -6.118  123.372 1.00 39.30  ? 1144 ILE   A CG1   1 
ATOM   1803 C  CG2   . ILE   A 1 234 ? -4.174  -7.724  122.589 1.00 45.25  ? 1144 ILE   A CG2   1 
ATOM   1804 C  CD1   . ILE   A 1 234 ? -2.595  -5.201  122.204 1.00 36.74  ? 1144 ILE   A CD1   1 
ATOM   1805 N  N     . ARG   A 1 235 ? -3.917  -10.335 124.765 1.00 46.97  ? 1145 ARG   A N     1 
ATOM   1806 C  CA    . ARG   A 1 235 ? -4.419  -11.691 124.663 1.00 44.94  ? 1145 ARG   A CA    1 
ATOM   1807 C  C     . ARG   A 1 235 ? -5.258  -11.862 123.395 1.00 45.60  ? 1145 ARG   A C     1 
ATOM   1808 O  O     . ARG   A 1 235 ? -5.707  -10.895 122.775 1.00 45.60  ? 1145 ARG   A O     1 
ATOM   1809 C  CB    . ARG   A 1 235 ? -5.215  -12.039 125.925 1.00 44.68  ? 1145 ARG   A CB    1 
ATOM   1810 C  CG    . ARG   A 1 235 ? -4.334  -12.096 127.177 1.00 49.98  ? 1145 ARG   A CG    1 
ATOM   1811 C  CD    . ARG   A 1 235 ? -5.071  -11.734 128.456 1.00 52.88  ? 1145 ARG   A CD    1 
ATOM   1812 N  NE    . ARG   A 1 235 ? -6.208  -12.608 128.700 1.00 58.18  ? 1145 ARG   A NE    1 
ATOM   1813 C  CZ    . ARG   A 1 235 ? -7.471  -12.270 128.486 1.00 66.27  ? 1145 ARG   A CZ    1 
ATOM   1814 N  NH1   . ARG   A 1 235 ? -7.799  -11.065 128.051 1.00 68.54  ? 1145 ARG   A NH1   1 
ATOM   1815 N  NH2   . ARG   A 1 235 ? -8.429  -13.162 128.716 1.00 74.91  ? 1145 ARG   A NH2   1 
ATOM   1816 N  N     . THR   A 1 236 ? -5.435  -13.118 122.989 1.00 47.06  ? 1146 THR   A N     1 
ATOM   1817 C  CA    . THR   A 1 236 ? -6.189  -13.424 121.779 1.00 44.18  ? 1146 THR   A CA    1 
ATOM   1818 C  C     . THR   A 1 236 ? -7.646  -13.044 121.969 1.00 44.20  ? 1146 THR   A C     1 
ATOM   1819 O  O     . THR   A 1 236 ? -8.310  -13.551 122.880 1.00 46.55  ? 1146 THR   A O     1 
ATOM   1820 C  CB    . THR   A 1 236 ? -6.084  -14.909 121.446 1.00 44.42  ? 1146 THR   A CB    1 
ATOM   1821 O  OG1   . THR   A 1 236 ? -4.749  -15.211 121.022 1.00 43.42  ? 1146 THR   A OG1   1 
ATOM   1822 C  CG2   . THR   A 1 236 ? -7.071  -15.270 120.343 1.00 44.04  ? 1146 THR   A CG2   1 
ATOM   1823 N  N     . GLY   A 1 237 ? -8.154  -12.182 121.088 1.00 44.55  ? 1147 GLY   A N     1 
ATOM   1824 C  CA    . GLY   A 1 237 ? -9.527  -11.738 121.140 1.00 41.43  ? 1147 GLY   A CA    1 
ATOM   1825 C  C     . GLY   A 1 237 ? -9.724  -10.394 121.807 1.00 42.70  ? 1147 GLY   A C     1 
ATOM   1826 O  O     . GLY   A 1 237 ? -10.831 -9.841  121.736 1.00 38.75  ? 1147 GLY   A O     1 
ATOM   1827 N  N     . GLU   A 1 238 ? -8.687  -9.857  122.447 1.00 41.76  ? 1148 GLU   A N     1 
ATOM   1828 C  CA    . GLU   A 1 238 ? -8.807  -8.590  123.154 1.00 40.27  ? 1148 GLU   A CA    1 
ATOM   1829 C  C     . GLU   A 1 238 ? -9.113  -7.455  122.188 1.00 40.13  ? 1148 GLU   A C     1 
ATOM   1830 O  O     . GLU   A 1 238 ? -8.600  -7.419  121.064 1.00 40.21  ? 1148 GLU   A O     1 
ATOM   1831 C  CB    . GLU   A 1 238 ? -7.512  -8.285  123.905 1.00 43.46  ? 1148 GLU   A CB    1 
ATOM   1832 C  CG    . GLU   A 1 238 ? -7.435  -8.833  125.306 1.00 48.24  ? 1148 GLU   A CG    1 
ATOM   1833 C  CD    . GLU   A 1 238 ? -6.369  -8.126  126.097 1.00 47.38  ? 1148 GLU   A CD    1 
ATOM   1834 O  OE1   . GLU   A 1 238 ? -5.528  -7.471  125.458 1.00 47.67  ? 1148 GLU   A OE1   1 
ATOM   1835 O  OE2   . GLU   A 1 238 ? -6.369  -8.212  127.341 1.00 52.67  ? 1148 GLU   A OE2   1 
ATOM   1836 N  N     . GLU   A 1 239 ? -9.947  -6.513  122.634 1.00 40.98  ? 1149 GLU   A N     1 
ATOM   1837 C  CA    . GLU   A 1 239 ? -10.215 -5.315  121.846 1.00 42.70  ? 1149 GLU   A CA    1 
ATOM   1838 C  C     . GLU   A 1 239 ? -9.071  -4.325  122.018 1.00 40.24  ? 1149 GLU   A C     1 
ATOM   1839 O  O     . GLU   A 1 239 ? -8.560  -4.128  123.125 1.00 39.85  ? 1149 GLU   A O     1 
ATOM   1840 C  CB    . GLU   A 1 239 ? -11.555 -4.660  122.236 1.00 36.22  ? 1149 GLU   A CB    1 
ATOM   1841 C  CG    . GLU   A 1 239 ? -12.028 -3.613  121.215 1.00 35.61  ? 1149 GLU   A CG    1 
ATOM   1842 C  CD    . GLU   A 1 239 ? -13.319 -2.863  121.606 1.00 41.97  ? 1149 GLU   A CD    1 
ATOM   1843 O  OE1   . GLU   A 1 239 ? -13.957 -3.216  122.621 1.00 42.66  ? 1149 GLU   A OE1   1 
ATOM   1844 O  OE2   . GLU   A 1 239 ? -13.704 -1.915  120.882 1.00 40.52  ? 1149 GLU   A OE2   1 
ATOM   1845 N  N     . LEU   A 1 240 ? -8.659  -3.722  120.906 1.00 40.45  ? 1150 LEU   A N     1 
ATOM   1846 C  CA    . LEU   A 1 240 ? -7.633  -2.690  120.916 1.00 36.65  ? 1150 LEU   A CA    1 
ATOM   1847 C  C     . LEU   A 1 240 ? -8.228  -1.348  121.323 1.00 39.50  ? 1150 LEU   A C     1 
ATOM   1848 O  O     . LEU   A 1 240 ? -9.266  -0.929  120.800 1.00 38.61  ? 1150 LEU   A O     1 
ATOM   1849 C  CB    . LEU   A 1 240 ? -7.000  -2.563  119.535 1.00 38.83  ? 1150 LEU   A CB    1 
ATOM   1850 C  CG    . LEU   A 1 240 ? -6.383  -3.795  118.891 1.00 43.17  ? 1150 LEU   A CG    1 
ATOM   1851 C  CD1   . LEU   A 1 240 ? -5.986  -3.451  117.455 1.00 42.99  ? 1150 LEU   A CD1   1 
ATOM   1852 C  CD2   . LEU   A 1 240 ? -5.162  -4.294  119.689 1.00 42.94  ? 1150 LEU   A CD2   1 
ATOM   1853 N  N     . GLY   A 1 241 ? -7.565  -0.662  122.240 1.00 40.29  ? 1151 GLY   A N     1 
ATOM   1854 C  CA    . GLY   A 1 241 ? -7.992  0.674   122.619 1.00 38.20  ? 1151 GLY   A CA    1 
ATOM   1855 C  C     . GLY   A 1 241 ? -6.815  1.525   123.034 1.00 37.38  ? 1151 GLY   A C     1 
ATOM   1856 O  O     . GLY   A 1 241 ? -5.795  1.019   123.515 1.00 37.98  ? 1151 GLY   A O     1 
ATOM   1857 N  N     . PHE   A 1 242 ? -6.955  2.828   122.841 1.00 38.51  ? 1152 PHE   A N     1 
ATOM   1858 C  CA    . PHE   A 1 242 ? -6.029  3.779   123.425 1.00 40.80  ? 1152 PHE   A CA    1 
ATOM   1859 C  C     . PHE   A 1 242 ? -6.805  4.849   124.174 1.00 43.65  ? 1152 PHE   A C     1 
ATOM   1860 O  O     . PHE   A 1 242 ? -8.036  4.927   124.104 1.00 39.81  ? 1152 PHE   A O     1 
ATOM   1861 C  CB    . PHE   A 1 242 ? -5.130  4.415   122.374 1.00 37.99  ? 1152 PHE   A CB    1 
ATOM   1862 C  CG    . PHE   A 1 242 ? -5.842  5.299   121.401 1.00 36.11  ? 1152 PHE   A CG    1 
ATOM   1863 C  CD1   . PHE   A 1 242 ? -6.509  4.761   120.316 1.00 33.69  ? 1152 PHE   A CD1   1 
ATOM   1864 C  CD2   . PHE   A 1 242 ? -5.778  6.674   121.530 1.00 36.74  ? 1152 PHE   A CD2   1 
ATOM   1865 C  CE1   . PHE   A 1 242 ? -7.127  5.576   119.391 1.00 33.75  ? 1152 PHE   A CE1   1 
ATOM   1866 C  CE2   . PHE   A 1 242 ? -6.402  7.503   120.614 1.00 39.98  ? 1152 PHE   A CE2   1 
ATOM   1867 C  CZ    . PHE   A 1 242 ? -7.074  6.950   119.539 1.00 37.69  ? 1152 PHE   A CZ    1 
ATOM   1868 N  N     . ASP   A 1 243 ? -6.061  5.677   124.904 1.00 40.10  ? 1153 ASP   A N     1 
ATOM   1869 C  CA    . ASP   A 1 243 ? -6.662  6.747   125.689 1.00 42.30  ? 1153 ASP   A CA    1 
ATOM   1870 C  C     . ASP   A 1 243 ? -6.809  7.964   124.789 1.00 43.06  ? 1153 ASP   A C     1 
ATOM   1871 O  O     . ASP   A 1 243 ? -5.829  8.654   124.491 1.00 39.70  ? 1153 ASP   A O     1 
ATOM   1872 C  CB    . ASP   A 1 243 ? -5.838  7.065   126.931 1.00 42.23  ? 1153 ASP   A CB    1 
ATOM   1873 C  CG    . ASP   A 1 243 ? -6.620  7.892   127.928 1.00 45.30  ? 1153 ASP   A CG    1 
ATOM   1874 O  OD1   . ASP   A 1 243 ? -7.370  8.779   127.483 1.00 47.11  ? 1153 ASP   A OD1   1 
ATOM   1875 O  OD2   . ASP   A 1 243 ? -6.520  7.641   129.146 1.00 46.66  ? 1153 ASP   A OD2   1 
ATOM   1876 N  N     . TYR   A 1 244 ? -8.050  8.216   124.358 1.00 39.89  ? 1154 TYR   A N     1 
ATOM   1877 C  CA    . TYR   A 1 244 ? -8.366  9.405   123.575 1.00 45.94  ? 1154 TYR   A CA    1 
ATOM   1878 C  C     . TYR   A 1 244 ? -7.863  10.676  124.246 1.00 45.29  ? 1154 TYR   A C     1 
ATOM   1879 O  O     . TYR   A 1 244 ? -7.547  11.656  123.568 1.00 44.43  ? 1154 TYR   A O     1 
ATOM   1880 C  CB    . TYR   A 1 244 ? -9.885  9.505   123.358 1.00 48.40  ? 1154 TYR   A CB    1 
ATOM   1881 C  CG    . TYR   A 1 244 ? -10.459 8.538   122.333 1.00 47.46  ? 1154 TYR   A CG    1 
ATOM   1882 C  CD1   . TYR   A 1 244 ? -9.659  7.596   121.702 1.00 44.79  ? 1154 TYR   A CD1   1 
ATOM   1883 C  CD2   . TYR   A 1 244 ? -11.808 8.581   121.992 1.00 48.59  ? 1154 TYR   A CD2   1 
ATOM   1884 C  CE1   . TYR   A 1 244 ? -10.183 6.717   120.768 1.00 41.49  ? 1154 TYR   A CE1   1 
ATOM   1885 C  CE2   . TYR   A 1 244 ? -12.339 7.711   121.056 1.00 47.69  ? 1154 TYR   A CE2   1 
ATOM   1886 C  CZ    . TYR   A 1 244 ? -11.514 6.782   120.444 1.00 44.83  ? 1154 TYR   A CZ    1 
ATOM   1887 O  OH    . TYR   A 1 244 ? -12.029 5.918   119.507 1.00 44.11  ? 1154 TYR   A OH    1 
ATOM   1888 N  N     . GLY   A 1 245 ? -7.789  10.685  125.567 1.00 46.04  ? 1155 GLY   A N     1 
ATOM   1889 C  CA    . GLY   A 1 245 ? -7.408  11.869  126.301 1.00 50.62  ? 1155 GLY   A CA    1 
ATOM   1890 C  C     . GLY   A 1 245 ? -8.619  12.651  126.763 1.00 58.87  ? 1155 GLY   A C     1 
ATOM   1891 O  O     . GLY   A 1 245 ? -9.763  12.396  126.375 1.00 58.89  ? 1155 GLY   A O     1 
ATOM   1892 N  N     . ASP   A 1 246 ? -8.346  13.633  127.615 1.00 61.91  ? 1156 ASP   A N     1 
ATOM   1893 C  CA    . ASP   A 1 246 ? -9.426  14.410  128.201 1.00 66.12  ? 1156 ASP   A CA    1 
ATOM   1894 C  C     . ASP   A 1 246 ? -10.020 15.430  127.235 1.00 67.89  ? 1156 ASP   A C     1 
ATOM   1895 O  O     . ASP   A 1 246 ? -11.190 15.788  127.393 1.00 73.96  ? 1156 ASP   A O     1 
ATOM   1896 C  CB    . ASP   A 1 246 ? -8.933  15.087  129.482 1.00 68.99  ? 1156 ASP   A CB    1 
ATOM   1897 C  CG    . ASP   A 1 246 ? -8.730  14.093  130.621 1.00 72.66  ? 1156 ASP   A CG    1 
ATOM   1898 O  OD1   . ASP   A 1 246 ? -9.371  13.021  130.587 1.00 65.89  ? 1156 ASP   A OD1   1 
ATOM   1899 O  OD2   . ASP   A 1 246 ? -7.937  14.375  131.547 1.00 76.17  ? 1156 ASP   A OD2   1 
ATOM   1900 N  N     . ARG   A 1 247 ? -9.263  15.886  126.229 1.00 66.75  ? 1157 ARG   A N     1 
ATOM   1901 C  CA    . ARG   A 1 247 ? -9.825  16.810  125.243 1.00 67.26  ? 1157 ARG   A CA    1 
ATOM   1902 C  C     . ARG   A 1 247 ? -11.074 16.226  124.592 1.00 67.95  ? 1157 ARG   A C     1 
ATOM   1903 O  O     . ARG   A 1 247 ? -12.103 16.907  124.466 1.00 68.10  ? 1157 ARG   A O     1 
ATOM   1904 C  CB    . ARG   A 1 247 ? -8.788  17.157  124.171 1.00 62.77  ? 1157 ARG   A CB    1 
ATOM   1905 C  CG    . ARG   A 1 247 ? -9.411  17.785  122.931 1.00 62.67  ? 1157 ARG   A CG    1 
ATOM   1906 C  CD    . ARG   A 1 247 ? -8.416  18.574  122.097 1.00 61.77  ? 1157 ARG   A CD    1 
ATOM   1907 N  NE    . ARG   A 1 247 ? -9.060  19.724  121.471 1.00 62.70  ? 1157 ARG   A NE    1 
ATOM   1908 C  CZ    . ARG   A 1 247 ? -8.452  20.584  120.664 1.00 63.54  ? 1157 ARG   A CZ    1 
ATOM   1909 N  NH1   . ARG   A 1 247 ? -7.187  20.427  120.312 1.00 61.70  ? 1157 ARG   A NH1   1 
ATOM   1910 N  NH2   . ARG   A 1 247 ? -9.129  21.636  120.205 1.00 65.59  ? 1157 ARG   A NH2   1 
ATOM   1911 N  N     . PHE   A 1 248 ? -11.000 14.958  124.184 1.00 59.54  ? 1158 PHE   A N     1 
ATOM   1912 C  CA    . PHE   A 1 248 ? -12.127 14.305  123.529 1.00 60.33  ? 1158 PHE   A CA    1 
ATOM   1913 C  C     . PHE   A 1 248 ? -13.332 14.228  124.454 1.00 68.79  ? 1158 PHE   A C     1 
ATOM   1914 O  O     . PHE   A 1 248 ? -14.453 14.568  124.061 1.00 72.03  ? 1158 PHE   A O     1 
ATOM   1915 C  CB    . PHE   A 1 248 ? -11.718 12.907  123.071 1.00 55.23  ? 1158 PHE   A CB    1 
ATOM   1916 C  CG    . PHE   A 1 248 ? -12.846 12.102  122.514 1.00 57.14  ? 1158 PHE   A CG    1 
ATOM   1917 C  CD1   . PHE   A 1 248 ? -13.186 12.199  121.179 1.00 55.13  ? 1158 PHE   A CD1   1 
ATOM   1918 C  CD2   . PHE   A 1 248 ? -13.572 11.246  123.325 1.00 57.78  ? 1158 PHE   A CD2   1 
ATOM   1919 C  CE1   . PHE   A 1 248 ? -14.228 11.459  120.663 1.00 57.19  ? 1158 PHE   A CE1   1 
ATOM   1920 C  CE2   . PHE   A 1 248 ? -14.613 10.504  122.814 1.00 55.03  ? 1158 PHE   A CE2   1 
ATOM   1921 C  CZ    . PHE   A 1 248 ? -14.938 10.606  121.481 1.00 53.00  ? 1158 PHE   A CZ    1 
ATOM   1922 N  N     . TRP   A 1 249 ? -13.119 13.771  125.687 1.00 67.39  ? 1159 TRP   A N     1 
ATOM   1923 C  CA    . TRP   A 1 249 ? -14.204 13.599  126.639 1.00 69.25  ? 1159 TRP   A CA    1 
ATOM   1924 C  C     . TRP   A 1 249 ? -14.667 14.904  127.265 1.00 77.98  ? 1159 TRP   A C     1 
ATOM   1925 O  O     . TRP   A 1 249 ? -15.736 14.928  127.880 1.00 71.84  ? 1159 TRP   A O     1 
ATOM   1926 C  CB    . TRP   A 1 249 ? -13.786 12.630  127.735 1.00 64.45  ? 1159 TRP   A CB    1 
ATOM   1927 C  CG    . TRP   A 1 249 ? -13.748 11.254  127.234 1.00 61.08  ? 1159 TRP   A CG    1 
ATOM   1928 C  CD1   . TRP   A 1 249 ? -12.644 10.538  126.891 1.00 62.73  ? 1159 TRP   A CD1   1 
ATOM   1929 C  CD2   . TRP   A 1 249 ? -14.873 10.417  126.970 1.00 61.04  ? 1159 TRP   A CD2   1 
ATOM   1930 N  NE1   . TRP   A 1 249 ? -13.011 9.289   126.448 1.00 62.11  ? 1159 TRP   A NE1   1 
ATOM   1931 C  CE2   . TRP   A 1 249 ? -14.378 9.194   126.484 1.00 60.72  ? 1159 TRP   A CE2   1 
ATOM   1932 C  CE3   . TRP   A 1 249 ? -16.256 10.579  127.107 1.00 66.70  ? 1159 TRP   A CE3   1 
ATOM   1933 C  CZ2   . TRP   A 1 249 ? -15.214 8.138   126.131 1.00 58.00  ? 1159 TRP   A CZ2   1 
ATOM   1934 C  CZ3   . TRP   A 1 249 ? -17.088 9.527   126.756 1.00 64.63  ? 1159 TRP   A CZ3   1 
ATOM   1935 C  CH2   . TRP   A 1 249 ? -16.561 8.321   126.274 1.00 61.69  ? 1159 TRP   A CH2   1 
ATOM   1936 N  N     . ASP   A 1 250 ? -13.893 15.980  127.144 1.00 86.93  ? 1160 ASP   A N     1 
ATOM   1937 C  CA    . ASP   A 1 250 ? -14.390 17.272  127.598 1.00 90.05  ? 1160 ASP   A CA    1 
ATOM   1938 C  C     . ASP   A 1 250 ? -15.377 17.889  126.620 1.00 88.80  ? 1160 ASP   A C     1 
ATOM   1939 O  O     . ASP   A 1 250 ? -16.037 18.871  126.971 1.00 93.16  ? 1160 ASP   A O     1 
ATOM   1940 C  CB    . ASP   A 1 250 ? -13.231 18.239  127.848 1.00 91.50  ? 1160 ASP   A CB    1 
ATOM   1941 C  CG    . ASP   A 1 250 ? -12.409 17.862  129.072 1.00 93.98  ? 1160 ASP   A CG    1 
ATOM   1942 O  OD1   . ASP   A 1 250 ? -12.682 16.801  129.676 1.00 95.56  ? 1160 ASP   A OD1   1 
ATOM   1943 O  OD2   . ASP   A 1 250 ? -11.486 18.623  129.428 1.00 94.87  ? 1160 ASP   A OD2   1 
ATOM   1944 N  N     . ILE   A 1 251 ? -15.499 17.340  125.414 1.00 82.15  ? 1161 ILE   A N     1 
ATOM   1945 C  CA    . ILE   A 1 251 ? -16.542 17.759  124.489 1.00 83.93  ? 1161 ILE   A CA    1 
ATOM   1946 C  C     . ILE   A 1 251 ? -17.544 16.650  124.178 1.00 83.26  ? 1161 ILE   A C     1 
ATOM   1947 O  O     . ILE   A 1 251 ? -18.664 16.956  123.730 1.00 82.02  ? 1161 ILE   A O     1 
ATOM   1948 C  CB    . ILE   A 1 251 ? -15.939 18.320  123.180 1.00 79.35  ? 1161 ILE   A CB    1 
ATOM   1949 C  CG1   . ILE   A 1 251 ? -15.648 17.207  122.177 1.00 71.69  ? 1161 ILE   A CG1   1 
ATOM   1950 C  CG2   . ILE   A 1 251 ? -14.683 19.123  123.470 1.00 80.58  ? 1161 ILE   A CG2   1 
ATOM   1951 C  CD1   . ILE   A 1 251 ? -16.622 17.180  121.014 1.00 70.92  ? 1161 ILE   A CD1   1 
ATOM   1952 N  N     . LYS   A 1 252 ? -17.208 15.377  124.417 1.00 78.76  ? 1162 LYS   A N     1 
ATOM   1953 C  CA    . LYS   A 1 252 ? -18.096 14.270  124.086 1.00 77.91  ? 1162 LYS   A CA    1 
ATOM   1954 C  C     . LYS   A 1 252 ? -18.897 13.729  125.266 1.00 78.45  ? 1162 LYS   A C     1 
ATOM   1955 O  O     . LYS   A 1 252 ? -19.930 13.093  125.038 1.00 79.66  ? 1162 LYS   A O     1 
ATOM   1956 C  CB    . LYS   A 1 252 ? -17.299 13.115  123.475 1.00 69.60  ? 1162 LYS   A CB    1 
ATOM   1957 C  CG    . LYS   A 1 252 ? -16.797 13.375  122.069 1.00 71.10  ? 1162 LYS   A CG    1 
ATOM   1958 C  CD    . LYS   A 1 252 ? -17.937 13.651  121.106 1.00 72.07  ? 1162 LYS   A CD    1 
ATOM   1959 C  CE    . LYS   A 1 252 ? -17.488 13.430  119.668 1.00 64.30  ? 1162 LYS   A CE    1 
ATOM   1960 N  NZ    . LYS   A 1 252 ? -18.433 14.063  118.705 1.00 70.51  ? 1162 LYS   A NZ    1 
ATOM   1961 N  N     . SER   A 1 253 ? -18.461 13.959  126.510 1.00 76.07  ? 1163 SER   A N     1 
ATOM   1962 C  CA    . SER   A 1 253 ? -19.085 13.279  127.644 1.00 74.33  ? 1163 SER   A CA    1 
ATOM   1963 C  C     . SER   A 1 253 ? -20.523 13.743  127.860 1.00 83.87  ? 1163 SER   A C     1 
ATOM   1964 O  O     . SER   A 1 253 ? -21.389 12.941  128.233 1.00 79.34  ? 1163 SER   A O     1 
ATOM   1965 C  CB    . SER   A 1 253 ? -18.262 13.496  128.914 1.00 73.64  ? 1163 SER   A CB    1 
ATOM   1966 O  OG    . SER   A 1 253 ? -18.415 14.818  129.412 1.00 77.25  ? 1163 SER   A OG    1 
ATOM   1967 N  N     . LYS   A 1 254 ? -20.796 15.033  127.639 1.00 82.46  ? 1164 LYS   A N     1 
ATOM   1968 C  CA    . LYS   A 1 254 ? -22.151 15.546  127.805 1.00 86.85  ? 1164 LYS   A CA    1 
ATOM   1969 C  C     . LYS   A 1 254 ? -23.138 14.840  126.881 1.00 93.44  ? 1164 LYS   A C     1 
ATOM   1970 O  O     . LYS   A 1 254 ? -24.323 14.718  127.217 1.00 90.17  ? 1164 LYS   A O     1 
ATOM   1971 C  CB    . LYS   A 1 254 ? -22.168 17.056  127.559 1.00 89.60  ? 1164 LYS   A CB    1 
ATOM   1972 N  N     . TYR   A 1 255 ? -22.666 14.359  125.725 1.00 96.66  ? 1165 TYR   A N     1 
ATOM   1973 C  CA    . TYR   A 1 255 ? -23.510 13.604  124.799 1.00 95.01  ? 1165 TYR   A CA    1 
ATOM   1974 C  C     . TYR   A 1 255 ? -23.586 12.130  125.192 1.00 90.08  ? 1165 TYR   A C     1 
ATOM   1975 O  O     . TYR   A 1 255 ? -24.663 11.609  125.497 1.00 89.52  ? 1165 TYR   A O     1 
ATOM   1976 C  CB    . TYR   A 1 255 ? -22.982 13.745  123.365 1.00 97.03  ? 1165 TYR   A CB    1 
ATOM   1977 C  CG    . TYR   A 1 255 ? -23.152 15.118  122.746 1.00 107.28 ? 1165 TYR   A CG    1 
ATOM   1978 C  CD1   . TYR   A 1 255 ? -24.383 15.527  122.244 1.00 113.81 ? 1165 TYR   A CD1   1 
ATOM   1979 C  CD2   . TYR   A 1 255 ? -22.079 15.997  122.641 1.00 108.95 ? 1165 TYR   A CD2   1 
ATOM   1980 C  CE1   . TYR   A 1 255 ? -24.547 16.778  121.670 1.00 113.32 ? 1165 TYR   A CE1   1 
ATOM   1981 C  CE2   . TYR   A 1 255 ? -22.234 17.251  122.065 1.00 113.43 ? 1165 TYR   A CE2   1 
ATOM   1982 C  CZ    . TYR   A 1 255 ? -23.473 17.634  121.582 1.00 114.89 ? 1165 TYR   A CZ    1 
ATOM   1983 O  OH    . TYR   A 1 255 ? -23.646 18.874  121.007 1.00 117.51 ? 1165 TYR   A OH    1 
ATOM   1984 N  N     . PHE   A 1 256 ? -22.449 11.440  125.181 1.00 82.74  ? 1166 PHE   A N     1 
ATOM   1985 C  CA    . PHE   A 1 256 ? -22.392 10.027  125.529 1.00 75.98  ? 1166 PHE   A CA    1 
ATOM   1986 C  C     . PHE   A 1 256 ? -21.312 9.785   126.574 1.00 74.78  ? 1166 PHE   A C     1 
ATOM   1987 O  O     . PHE   A 1 256 ? -20.235 10.383  126.522 1.00 69.20  ? 1166 PHE   A O     1 
ATOM   1988 C  CB    . PHE   A 1 256 ? -22.134 9.158   124.292 1.00 69.89  ? 1166 PHE   A CB    1 
ATOM   1989 C  CG    . PHE   A 1 256 ? -20.901 9.542   123.512 1.00 68.21  ? 1166 PHE   A CG    1 
ATOM   1990 C  CD1   . PHE   A 1 256 ? -19.658 9.022   123.846 1.00 63.57  ? 1166 PHE   A CD1   1 
ATOM   1991 C  CD2   . PHE   A 1 256 ? -20.994 10.392  122.426 1.00 65.61  ? 1166 PHE   A CD2   1 
ATOM   1992 C  CE1   . PHE   A 1 256 ? -18.528 9.365   123.125 1.00 61.43  ? 1166 PHE   A CE1   1 
ATOM   1993 C  CE2   . PHE   A 1 256 ? -19.868 10.733  121.696 1.00 62.57  ? 1166 PHE   A CE2   1 
ATOM   1994 C  CZ    . PHE   A 1 256 ? -18.634 10.220  122.046 1.00 61.46  ? 1166 PHE   A CZ    1 
ATOM   1995 N  N     . THR   A 1 257 ? -21.615 8.911   127.522 1.00 74.05  ? 1167 THR   A N     1 
ATOM   1996 C  CA    . THR   A 1 257 ? -20.701 8.539   128.591 1.00 72.49  ? 1167 THR   A CA    1 
ATOM   1997 C  C     . THR   A 1 257 ? -19.948 7.270   128.200 1.00 70.42  ? 1167 THR   A C     1 
ATOM   1998 O  O     . THR   A 1 257 ? -20.285 6.599   127.222 1.00 70.04  ? 1167 THR   A O     1 
ATOM   1999 C  CB    . THR   A 1 257 ? -21.477 8.365   129.908 1.00 81.20  ? 1167 THR   A CB    1 
ATOM   2000 O  OG1   . THR   A 1 257 ? -20.796 7.444   130.772 1.00 81.18  ? 1167 THR   A OG1   1 
ATOM   2001 C  CG2   . THR   A 1 257 ? -22.913 7.876   129.647 1.00 80.13  ? 1167 THR   A CG2   1 
ATOM   2002 N  N     . CYS   A 1 258 ? -18.909 6.948   128.975 1.00 70.22  ? 1168 CYS   A N     1 
ATOM   2003 C  CA    . CYS   A 1 258 ? -17.998 5.864   128.614 1.00 67.73  ? 1168 CYS   A CA    1 
ATOM   2004 C  C     . CYS   A 1 258 ? -18.650 4.500   128.819 1.00 64.66  ? 1168 CYS   A C     1 
ATOM   2005 O  O     . CYS   A 1 258 ? -19.614 4.342   129.569 1.00 72.99  ? 1168 CYS   A O     1 
ATOM   2006 C  CB    . CYS   A 1 258 ? -16.701 5.942   129.429 1.00 66.70  ? 1168 CYS   A CB    1 
ATOM   2007 S  SG    . CYS   A 1 258 ? -15.392 4.738   128.961 1.00 60.22  ? 1168 CYS   A SG    1 
ATOM   2008 N  N     . GLN   A 1 259 ? -18.108 3.502   128.120 1.00 67.06  ? 1169 GLN   A N     1 
ATOM   2009 C  CA    . GLN   A 1 259 ? -18.590 2.130   128.240 1.00 62.35  ? 1169 GLN   A CA    1 
ATOM   2010 C  C     . GLN   A 1 259 ? -17.459 1.113   128.350 1.00 63.81  ? 1169 GLN   A C     1 
ATOM   2011 O  O     . GLN   A 1 259 ? -17.711 -0.083  128.160 1.00 65.53  ? 1169 GLN   A O     1 
ATOM   2012 C  CB    . GLN   A 1 259 ? -19.471 1.749   127.042 1.00 61.45  ? 1169 GLN   A CB    1 
ATOM   2013 C  CG    . GLN   A 1 259 ? -20.578 2.733   126.736 1.00 67.84  ? 1169 GLN   A CG    1 
ATOM   2014 C  CD    . GLN   A 1 259 ? -21.607 2.794   127.834 1.00 67.15  ? 1169 GLN   A CD    1 
ATOM   2015 O  OE1   . GLN   A 1 259 ? -21.852 1.805   128.521 1.00 68.55  ? 1169 GLN   A OE1   1 
ATOM   2016 N  NE2   . GLN   A 1 259 ? -22.201 3.962   128.021 1.00 69.74  ? 1169 GLN   A NE2   1 
ATOM   2017 N  N     . CYS   A 1 260 ? -16.216 1.535   128.598 1.00 59.24  ? 1170 CYS   A N     1 
ATOM   2018 C  CA    . CYS   A 1 260 ? -15.147 0.549   128.717 1.00 60.82  ? 1170 CYS   A CA    1 
ATOM   2019 C  C     . CYS   A 1 260 ? -15.395 -0.370  129.903 1.00 61.64  ? 1170 CYS   A C     1 
ATOM   2020 O  O     . CYS   A 1 260 ? -15.205 -1.587  129.807 1.00 65.63  ? 1170 CYS   A O     1 
ATOM   2021 C  CB    . CYS   A 1 260 ? -13.788 1.239   128.828 1.00 56.58  ? 1170 CYS   A CB    1 
ATOM   2022 S  SG    . CYS   A 1 260 ? -13.401 1.946   130.446 1.00 59.19  ? 1170 CYS   A SG    1 
ATOM   2023 N  N     . GLY   A 1 261 ? -15.848 0.190   131.018 1.00 63.12  ? 1171 GLY   A N     1 
ATOM   2024 C  CA    . GLY   A 1 261 ? -16.165 -0.618  132.168 1.00 65.86  ? 1171 GLY   A CA    1 
ATOM   2025 C  C     . GLY   A 1 261 ? -14.980 -1.157  132.925 1.00 69.73  ? 1171 GLY   A C     1 
ATOM   2026 O  O     . GLY   A 1 261 ? -15.153 -2.067  133.738 1.00 78.24  ? 1171 GLY   A O     1 
ATOM   2027 N  N     . SER   A 1 262 ? -13.777 -0.647  132.684 1.00 70.88  ? 1172 SER   A N     1 
ATOM   2028 C  CA    . SER   A 1 262 ? -12.650 -1.037  133.516 1.00 74.06  ? 1172 SER   A CA    1 
ATOM   2029 C  C     . SER   A 1 262 ? -12.822 -0.455  134.909 1.00 76.99  ? 1172 SER   A C     1 
ATOM   2030 O  O     . SER   A 1 262 ? -13.291 0.676   135.068 1.00 75.86  ? 1172 SER   A O     1 
ATOM   2031 C  CB    . SER   A 1 262 ? -11.331 -0.565  132.913 1.00 74.71  ? 1172 SER   A CB    1 
ATOM   2032 O  OG    . SER   A 1 262 ? -10.258 -0.804  133.810 1.00 76.92  ? 1172 SER   A OG    1 
ATOM   2033 N  N     . GLU   A 1 263 ? -12.436 -1.241  135.920 1.00 79.06  ? 1173 GLU   A N     1 
ATOM   2034 C  CA    . GLU   A 1 263 ? -12.605 -0.827  137.311 1.00 80.56  ? 1173 GLU   A CA    1 
ATOM   2035 C  C     . GLU   A 1 263 ? -12.063 0.578   137.549 1.00 84.30  ? 1173 GLU   A C     1 
ATOM   2036 O  O     . GLU   A 1 263 ? -12.630 1.345   138.337 1.00 81.61  ? 1173 GLU   A O     1 
ATOM   2037 C  CB    . GLU   A 1 263 ? -11.920 -1.830  138.241 1.00 80.67  ? 1173 GLU   A CB    1 
ATOM   2038 N  N     . LYS   A 1 264 ? -10.974 0.935   136.867 1.00 85.59  ? 1174 LYS   A N     1 
ATOM   2039 C  CA    . LYS   A 1 264 ? -10.411 2.283   136.933 1.00 83.32  ? 1174 LYS   A CA    1 
ATOM   2040 C  C     . LYS   A 1 264 ? -10.834 3.067   135.691 1.00 78.88  ? 1174 LYS   A C     1 
ATOM   2041 O  O     . LYS   A 1 264 ? -10.047 3.341   134.788 1.00 81.29  ? 1174 LYS   A O     1 
ATOM   2042 C  CB    . LYS   A 1 264 ? -8.890  2.214   137.069 1.00 89.70  ? 1174 LYS   A CB    1 
ATOM   2043 C  CG    . LYS   A 1 264 ? -8.216  3.515   137.504 1.00 92.09  ? 1174 LYS   A CG    1 
ATOM   2044 C  CD    . LYS   A 1 264 ? -6.693  3.403   137.420 1.00 90.99  ? 1174 LYS   A CD    1 
ATOM   2045 C  CE    . LYS   A 1 264 ? -5.982  4.644   137.971 1.00 89.22  ? 1174 LYS   A CE    1 
ATOM   2046 N  NZ    . LYS   A 1 264 ? -6.005  4.717   139.460 1.00 91.18  ? 1174 LYS   A NZ    1 
ATOM   2047 N  N     . CYS   A 1 265 ? -12.117 3.417   135.658 1.00 79.10  ? 1175 CYS   A N     1 
ATOM   2048 C  CA    . CYS   A 1 265 ? -12.685 4.208   134.573 1.00 77.06  ? 1175 CYS   A CA    1 
ATOM   2049 C  C     . CYS   A 1 265 ? -12.659 5.692   134.933 1.00 76.88  ? 1175 CYS   A C     1 
ATOM   2050 O  O     . CYS   A 1 265 ? -12.979 6.077   136.062 1.00 78.25  ? 1175 CYS   A O     1 
ATOM   2051 C  CB    . CYS   A 1 265 ? -14.118 3.756   134.276 1.00 68.47  ? 1175 CYS   A CB    1 
ATOM   2052 S  SG    . CYS   A 1 265 ? -14.864 4.465   132.788 1.00 66.73  ? 1175 CYS   A SG    1 
ATOM   2053 N  N     . LYS   A 1 266 ? -12.275 6.524   133.963 1.00 74.04  ? 1176 LYS   A N     1 
ATOM   2054 C  CA    . LYS   A 1 266 ? -12.092 7.952   134.194 1.00 74.61  ? 1176 LYS   A CA    1 
ATOM   2055 C  C     . LYS   A 1 266 ? -13.272 8.804   133.731 1.00 73.43  ? 1176 LYS   A C     1 
ATOM   2056 O  O     . LYS   A 1 266 ? -13.458 9.913   134.250 1.00 73.09  ? 1176 LYS   A O     1 
ATOM   2057 C  CB    . LYS   A 1 266 ? -10.810 8.431   133.494 1.00 73.71  ? 1176 LYS   A CB    1 
ATOM   2058 C  CG    . LYS   A 1 266 ? -10.182 9.689   134.090 1.00 76.40  ? 1176 LYS   A CG    1 
ATOM   2059 C  CD    . LYS   A 1 266 ? -8.904  10.090  133.352 1.00 78.62  ? 1176 LYS   A CD    1 
ATOM   2060 C  CE    . LYS   A 1 266 ? -8.352  11.416  133.887 1.00 83.31  ? 1176 LYS   A CE    1 
ATOM   2061 N  NZ    . LYS   A 1 266 ? -7.303  11.994  133.002 1.00 73.23  ? 1176 LYS   A NZ    1 
ATOM   2062 N  N     . HIS   A 1 267 ? -14.076 8.314   132.785 1.00 68.45  ? 1177 HIS   A N     1 
ATOM   2063 C  CA    . HIS   A 1 267 ? -15.144 9.097   132.177 1.00 70.54  ? 1177 HIS   A CA    1 
ATOM   2064 C  C     . HIS   A 1 267 ? -16.473 8.353   132.239 1.00 75.21  ? 1177 HIS   A C     1 
ATOM   2065 O  O     . HIS   A 1 267 ? -17.369 8.590   131.422 1.00 74.13  ? 1177 HIS   A O     1 
ATOM   2066 C  CB    . HIS   A 1 267 ? -14.786 9.461   130.737 1.00 66.56  ? 1177 HIS   A CB    1 
ATOM   2067 C  CG    . HIS   A 1 267 ? -13.412 10.032  130.592 1.00 68.09  ? 1177 HIS   A CG    1 
ATOM   2068 N  ND1   . HIS   A 1 267 ? -12.305 9.250   130.337 1.00 64.33  ? 1177 HIS   A ND1   1 
ATOM   2069 C  CD2   . HIS   A 1 267 ? -12.958 11.304  130.698 1.00 66.59  ? 1177 HIS   A CD2   1 
ATOM   2070 C  CE1   . HIS   A 1 267 ? -11.232 10.018  130.272 1.00 64.91  ? 1177 HIS   A CE1   1 
ATOM   2071 N  NE2   . HIS   A 1 267 ? -11.601 11.269  130.486 1.00 67.22  ? 1177 HIS   A NE2   1 
ATOM   2072 N  N     . SER   A 1 268 ? -16.618 7.464   133.219 1.00 74.56  ? 1178 SER   A N     1 
ATOM   2073 C  CA    . SER   A 1 268 ? -17.818 6.661   133.359 1.00 74.42  ? 1178 SER   A CA    1 
ATOM   2074 C  C     . SER   A 1 268 ? -19.008 7.528   133.752 1.00 83.68  ? 1178 SER   A C     1 
ATOM   2075 O  O     . SER   A 1 268 ? -18.882 8.715   134.069 1.00 83.72  ? 1178 SER   A O     1 
ATOM   2076 C  CB    . SER   A 1 268 ? -17.619 5.574   134.411 1.00 75.40  ? 1178 SER   A CB    1 
ATOM   2077 O  OG    . SER   A 1 268 ? -18.696 4.661   134.392 1.00 79.68  ? 1178 SER   A OG    1 
ATOM   2078 N  N     . ALA   A 1 269 ? -20.186 6.908   133.730 1.00 79.06  ? 1179 ALA   A N     1 
ATOM   2079 C  CA    . ALA   A 1 269 ? -21.360 7.536   134.317 1.00 88.46  ? 1179 ALA   A CA    1 
ATOM   2080 C  C     . ALA   A 1 269 ? -21.147 7.787   135.806 1.00 91.57  ? 1179 ALA   A C     1 
ATOM   2081 O  O     . ALA   A 1 269 ? -21.183 8.933   136.270 1.00 90.44  ? 1179 ALA   A O     1 
ATOM   2082 C  CB    . ALA   A 1 269 ? -22.592 6.661   134.079 1.00 84.47  ? 1179 ALA   A CB    1 
ATOM   2083 N  N     . GLU   A 1 270 ? -20.891 6.718   136.569 1.00 100.00 ? 1180 GLU   A N     1 
ATOM   2084 C  CA    . GLU   A 1 270 ? -20.775 6.843   138.020 1.00 103.10 ? 1180 GLU   A CA    1 
ATOM   2085 C  C     . GLU   A 1 270 ? -19.504 7.567   138.455 1.00 103.85 ? 1180 GLU   A C     1 
ATOM   2086 O  O     . GLU   A 1 270 ? -19.478 8.131   139.556 1.00 105.35 ? 1180 GLU   A O     1 
ATOM   2087 C  CB    . GLU   A 1 270 ? -20.850 5.459   138.682 1.00 106.85 ? 1180 GLU   A CB    1 
ATOM   2088 C  CG    . GLU   A 1 270 ? -19.945 4.388   138.066 1.00 106.66 ? 1180 GLU   A CG    1 
ATOM   2089 C  CD    . GLU   A 1 270 ? -20.063 3.037   138.767 1.00 104.13 ? 1180 GLU   A CD    1 
ATOM   2090 O  OE1   . GLU   A 1 270 ? -20.316 3.012   139.992 1.00 105.83 ? 1180 GLU   A OE1   1 
ATOM   2091 O  OE2   . GLU   A 1 270 ? -19.909 1.998   138.091 1.00 103.25 ? 1180 GLU   A OE2   1 
ATOM   2092 N  N     . ALA   A 1 271 ? -18.454 7.568   137.627 1.00 97.76  ? 1181 ALA   A N     1 
ATOM   2093 C  CA    . ALA   A 1 271 ? -17.241 8.308   137.962 1.00 95.42  ? 1181 ALA   A CA    1 
ATOM   2094 C  C     . ALA   A 1 271 ? -17.425 9.814   137.809 1.00 95.48  ? 1181 ALA   A C     1 
ATOM   2095 O  O     . ALA   A 1 271 ? -16.674 10.585  138.420 1.00 96.94  ? 1181 ALA   A O     1 
ATOM   2096 C  CB    . ALA   A 1 271 ? -16.074 7.827   137.097 1.00 88.98  ? 1181 ALA   A CB    1 
ATOM   2097 N  N     . ILE   A 1 272 ? -18.399 10.244  137.004 1.00 93.53  ? 1182 ILE   A N     1 
ATOM   2098 C  CA    . ILE   A 1 272 ? -18.722 11.663  136.902 1.00 91.91  ? 1182 ILE   A CA    1 
ATOM   2099 C  C     . ILE   A 1 272 ? -19.403 12.146  138.176 1.00 105.96 ? 1182 ILE   A C     1 
ATOM   2100 O  O     . ILE   A 1 272 ? -19.132 13.253  138.661 1.00 110.12 ? 1182 ILE   A O     1 
ATOM   2101 C  CB    . ILE   A 1 272 ? -19.594 11.911  135.657 1.00 87.64  ? 1182 ILE   A CB    1 
ATOM   2102 C  CG1   . ILE   A 1 272 ? -18.743 11.860  134.389 1.00 88.85  ? 1182 ILE   A CG1   1 
ATOM   2103 C  CG2   . ILE   A 1 272 ? -20.345 13.229  135.763 1.00 94.59  ? 1182 ILE   A CG2   1 
ATOM   2104 C  CD1   . ILE   A 1 272 ? -19.554 11.784  133.112 1.00 84.90  ? 1182 ILE   A CD1   1 
ATOM   2105 N  N     . ALA   A 1 273 ? -20.284 11.317  138.748 1.00 110.23 ? 1183 ALA   A N     1 
ATOM   2106 C  CA    . ALA   A 1 273 ? -21.055 11.722  139.920 1.00 111.51 ? 1183 ALA   A CA    1 
ATOM   2107 C  C     . ALA   A 1 273 ? -20.189 11.849  141.168 1.00 114.56 ? 1183 ALA   A C     1 
ATOM   2108 O  O     . ALA   A 1 273 ? -20.510 12.643  142.058 1.00 119.09 ? 1183 ALA   A O     1 
ATOM   2109 C  CB    . ALA   A 1 273 ? -22.191 10.731  140.168 1.00 111.06 ? 1183 ALA   A CB    1 
ATOM   2110 N  N     . LEU   A 1 274 ? -19.102 11.078  141.262 1.00 109.52 ? 1184 LEU   A N     1 
ATOM   2111 C  CA    . LEU   A 1 274 ? -18.234 11.179  142.433 1.00 108.31 ? 1184 LEU   A CA    1 
ATOM   2112 C  C     . LEU   A 1 274 ? -17.506 12.516  142.463 1.00 112.73 ? 1184 LEU   A C     1 
ATOM   2113 O  O     . LEU   A 1 274 ? -17.461 13.185  143.502 1.00 115.67 ? 1184 LEU   A O     1 
ATOM   2114 C  CB    . LEU   A 1 274 ? -17.231 10.028  142.460 1.00 98.48  ? 1184 LEU   A CB    1 
ATOM   2115 C  CG    . LEU   A 1 274 ? -16.285 10.127  143.658 1.00 98.80  ? 1184 LEU   A CG    1 
ATOM   2116 C  CD1   . LEU   A 1 274 ? -17.050 9.922   144.960 1.00 103.44 ? 1184 LEU   A CD1   1 
ATOM   2117 C  CD2   . LEU   A 1 274 ? -15.128 9.147   143.534 1.00 99.58  ? 1184 LEU   A CD2   1 
ATOM   2118 N  N     . GLU   A 1 275 ? -16.921 12.919  141.332 1.00 112.94 ? 1185 GLU   A N     1 
ATOM   2119 C  CA    . GLU   A 1 275 ? -16.294 14.233  141.262 1.00 115.18 ? 1185 GLU   A CA    1 
ATOM   2120 C  C     . GLU   A 1 275 ? -17.324 15.351  141.332 1.00 122.76 ? 1185 GLU   A C     1 
ATOM   2121 O  O     . GLU   A 1 275 ? -17.033 16.426  141.869 1.00 122.53 ? 1185 GLU   A O     1 
ATOM   2122 C  CB    . GLU   A 1 275 ? -15.460 14.358  139.989 1.00 113.63 ? 1185 GLU   A CB    1 
ATOM   2123 C  CG    . GLU   A 1 275 ? -14.095 13.694  140.076 1.00 112.85 ? 1185 GLU   A CG    1 
ATOM   2124 C  CD    . GLU   A 1 275 ? -13.173 14.380  141.069 1.00 111.79 ? 1185 GLU   A CD    1 
ATOM   2125 O  OE1   . GLU   A 1 275 ? -13.437 15.547  141.429 1.00 112.04 ? 1185 GLU   A OE1   1 
ATOM   2126 O  OE2   . GLU   A 1 275 ? -12.182 13.751  141.490 1.00 110.46 ? 1185 GLU   A OE2   1 
ATOM   2127 N  N     . GLN   A 1 276 ? -18.531 15.119  140.807 1.00 138.73 ? 1186 GLN   A N     1 
ATOM   2128 C  CA    . GLN   A 1 276 ? -19.586 16.121  140.915 1.00 139.79 ? 1186 GLN   A CA    1 
ATOM   2129 C  C     . GLN   A 1 276 ? -20.151 16.189  142.330 1.00 144.99 ? 1186 GLN   A C     1 
ATOM   2130 O  O     . GLN   A 1 276 ? -20.583 17.262  142.772 1.00 149.92 ? 1186 GLN   A O     1 
ATOM   2131 C  CB    . GLN   A 1 276 ? -20.697 15.826  139.905 1.00 139.56 ? 1186 GLN   A CB    1 
ATOM   2132 C  CG    . GLN   A 1 276 ? -21.790 16.895  139.824 1.00 145.23 ? 1186 GLN   A CG    1 
ATOM   2133 C  CD    . GLN   A 1 276 ? -21.549 17.911  138.717 1.00 143.42 ? 1186 GLN   A CD    1 
ATOM   2134 O  OE1   . GLN   A 1 276 ? -20.765 17.671  137.796 1.00 144.65 ? 1186 GLN   A OE1   1 
ATOM   2135 N  NE2   . GLN   A 1 276 ? -22.227 19.052  138.803 1.00 142.01 ? 1186 GLN   A NE2   1 
ATOM   2136 N  N     . SER   A 1 277 ? -20.156 15.066  143.057 1.00 128.30 ? 1187 SER   A N     1 
ATOM   2137 C  CA    . SER   A 1 277 ? -20.649 15.086  144.432 1.00 127.78 ? 1187 SER   A CA    1 
ATOM   2138 C  C     . SER   A 1 277 ? -19.573 15.549  145.405 1.00 124.76 ? 1187 SER   A C     1 
ATOM   2139 O  O     . SER   A 1 277 ? -19.858 16.335  146.316 1.00 125.91 ? 1187 SER   A O     1 
ATOM   2140 C  CB    . SER   A 1 277 ? -21.168 13.706  144.839 1.00 127.53 ? 1187 SER   A CB    1 
ATOM   2141 O  OG    . SER   A 1 277 ? -21.735 13.740  146.138 1.00 129.50 ? 1187 SER   A OG    1 
ATOM   2142 N  N     . ARG   A 1 278 ? -18.338 15.070  145.238 1.00 121.81 ? 1188 ARG   A N     1 
ATOM   2143 C  CA    . ARG   A 1 278 ? -17.244 15.570  146.064 1.00 117.90 ? 1188 ARG   A CA    1 
ATOM   2144 C  C     . ARG   A 1 278 ? -17.048 17.064  145.850 1.00 119.41 ? 1188 ARG   A C     1 
ATOM   2145 O  O     . ARG   A 1 278 ? -17.005 17.842  146.811 1.00 119.56 ? 1188 ARG   A O     1 
ATOM   2146 C  CB    . ARG   A 1 278 ? -15.953 14.815  145.760 1.00 114.03 ? 1188 ARG   A CB    1 
ATOM   2147 C  CG    . ARG   A 1 278 ? -14.718 15.542  146.257 1.00 111.29 ? 1188 ARG   A CG    1 
ATOM   2148 C  CD    . ARG   A 1 278 ? -13.449 14.788  145.932 1.00 109.29 ? 1188 ARG   A CD    1 
ATOM   2149 N  NE    . ARG   A 1 278 ? -12.264 15.570  146.266 1.00 108.75 ? 1188 ARG   A NE    1 
ATOM   2150 C  CZ    . ARG   A 1 278 ? -11.511 16.212  145.381 1.00 110.08 ? 1188 ARG   A CZ    1 
ATOM   2151 N  NH1   . ARG   A 1 278 ? -11.785 16.178  144.086 1.00 105.86 ? 1188 ARG   A NH1   1 
ATOM   2152 N  NH2   . ARG   A 1 278 ? -10.451 16.897  145.804 1.00 107.67 ? 1188 ARG   A NH2   1 
ATOM   2153 N  N     . LEU   A 1 279 ? -16.934 17.483  144.594 1.00 117.40 ? 1189 LEU   A N     1 
ATOM   2154 C  CA    . LEU   A 1 279 ? -16.849 18.901  144.268 1.00 117.40 ? 1189 LEU   A CA    1 
ATOM   2155 C  C     . LEU   A 1 279 ? -18.249 19.471  144.016 1.00 118.93 ? 1189 LEU   A C     1 
ATOM   2156 O  O     . LEU   A 1 279 ? -18.565 20.592  144.420 1.00 121.57 ? 1189 LEU   A O     1 
ATOM   2157 C  CB    . LEU   A 1 279 ? -15.952 19.123  143.045 1.00 111.80 ? 1189 LEU   A CB    1 
ATOM   2158 C  CG    . LEU   A 1 279 ? -14.565 18.466  143.041 1.00 109.89 ? 1189 LEU   A CG    1 
ATOM   2159 C  CD1   . LEU   A 1 279 ? -13.788 18.850  141.788 1.00 104.59 ? 1189 LEU   A CD1   1 
ATOM   2160 C  CD2   . LEU   A 1 279 ? -13.775 18.824  144.292 1.00 109.61 ? 1189 LEU   A CD2   1 
ATOM   2161 N  N     . ARG   B 1 7   ? 38.640  -14.264 81.329  1.00 77.50  ? 917  ARG   B N     1 
ATOM   2162 C  CA    . ARG   B 1 7   ? 38.397  -13.555 82.581  1.00 78.09  ? 917  ARG   B CA    1 
ATOM   2163 C  C     . ARG   B 1 7   ? 37.103  -14.041 83.232  1.00 83.40  ? 917  ARG   B C     1 
ATOM   2164 O  O     . ARG   B 1 7   ? 36.061  -14.141 82.574  1.00 80.61  ? 917  ARG   B O     1 
ATOM   2165 C  CB    . ARG   B 1 7   ? 38.346  -12.041 82.336  1.00 75.64  ? 917  ARG   B CB    1 
ATOM   2166 C  CG    . ARG   B 1 7   ? 38.077  -11.192 83.574  1.00 65.92  ? 917  ARG   B CG    1 
ATOM   2167 C  CD    . ARG   B 1 7   ? 38.192  -9.715  83.236  1.00 62.71  ? 917  ARG   B CD    1 
ATOM   2168 N  NE    . ARG   B 1 7   ? 39.572  -9.288  83.022  1.00 65.52  ? 917  ARG   B NE    1 
ATOM   2169 C  CZ    . ARG   B 1 7   ? 40.206  -8.390  83.767  1.00 65.33  ? 917  ARG   B CZ    1 
ATOM   2170 N  NH1   . ARG   B 1 7   ? 39.606  -7.788  84.784  1.00 62.53  ? 917  ARG   B NH1   1 
ATOM   2171 N  NH2   . ARG   B 1 7   ? 41.468  -8.079  83.477  1.00 68.27  ? 917  ARG   B NH2   1 
ATOM   2172 N  N     . THR   B 1 8   ? 37.173  -14.363 84.521  1.00 90.45  ? 918  THR   B N     1 
ATOM   2173 C  CA    . THR   B 1 8   ? 35.973  -14.771 85.233  1.00 90.62  ? 918  THR   B CA    1 
ATOM   2174 C  C     . THR   B 1 8   ? 35.002  -13.602 85.346  1.00 85.10  ? 918  THR   B C     1 
ATOM   2175 O  O     . THR   B 1 8   ? 35.387  -12.430 85.287  1.00 86.81  ? 918  THR   B O     1 
ATOM   2176 C  CB    . THR   B 1 8   ? 36.312  -15.285 86.630  1.00 95.44  ? 918  THR   B CB    1 
ATOM   2177 O  OG1   . THR   B 1 8   ? 35.104  -15.670 87.296  1.00 92.94  ? 918  THR   B OG1   1 
ATOM   2178 C  CG2   . THR   B 1 8   ? 37.001  -14.194 87.443  1.00 98.70  ? 918  THR   B CG2   1 
ATOM   2179 N  N     . GLU   B 1 9   ? 33.728  -13.931 85.523  1.00 78.69  ? 919  GLU   B N     1 
ATOM   2180 C  CA    . GLU   B 1 9   ? 32.667  -12.936 85.613  1.00 67.25  ? 919  GLU   B CA    1 
ATOM   2181 C  C     . GLU   B 1 9   ? 32.230  -12.862 87.076  1.00 72.02  ? 919  GLU   B C     1 
ATOM   2182 O  O     . GLU   B 1 9   ? 31.377  -13.632 87.525  1.00 77.24  ? 919  GLU   B O     1 
ATOM   2183 C  CB    . GLU   B 1 9   ? 31.513  -13.297 84.680  1.00 65.47  ? 919  GLU   B CB    1 
ATOM   2184 C  CG    . GLU   B 1 9   ? 30.685  -12.105 84.234  1.00 61.55  ? 919  GLU   B CG    1 
ATOM   2185 C  CD    . GLU   B 1 9   ? 29.330  -12.508 83.698  1.00 58.39  ? 919  GLU   B CD    1 
ATOM   2186 O  OE1   . GLU   B 1 9   ? 28.627  -13.278 84.392  1.00 54.31  ? 919  GLU   B OE1   1 
ATOM   2187 O  OE2   . GLU   B 1 9   ? 28.978  -12.057 82.582  1.00 54.25  ? 919  GLU   B OE2   1 
ATOM   2188 N  N     . LYS   B 1 10  ? 32.799  -11.907 87.812  1.00 65.81  ? 920  LYS   B N     1 
ATOM   2189 C  CA    . LYS   B 1 10  ? 32.707  -11.883 89.268  1.00 69.70  ? 920  LYS   B CA    1 
ATOM   2190 C  C     . LYS   B 1 10  ? 31.468  -11.133 89.741  1.00 62.10  ? 920  LYS   B C     1 
ATOM   2191 O  O     . LYS   B 1 10  ? 31.256  -9.981  89.354  1.00 59.20  ? 920  LYS   B O     1 
ATOM   2192 C  CB    . LYS   B 1 10  ? 33.958  -11.233 89.864  1.00 73.09  ? 920  LYS   B CB    1 
ATOM   2193 C  CG    . LYS   B 1 10  ? 33.934  -11.139 91.383  1.00 73.80  ? 920  LYS   B CG    1 
ATOM   2194 C  CD    . LYS   B 1 10  ? 34.936  -10.130 91.915  1.00 75.67  ? 920  LYS   B CD    1 
ATOM   2195 C  CE    . LYS   B 1 10  ? 34.981  -10.169 93.436  1.00 80.91  ? 920  LYS   B CE    1 
ATOM   2196 N  NZ    . LYS   B 1 10  ? 35.494  -11.480 93.934  1.00 85.40  ? 920  LYS   B NZ    1 
ATOM   2197 N  N     . ILE   B 1 11  ? 30.665  -11.780 90.589  1.00 67.08  ? 921  ILE   B N     1 
ATOM   2198 C  CA    . ILE   B 1 11  ? 29.549  -11.098 91.245  1.00 61.80  ? 921  ILE   B CA    1 
ATOM   2199 C  C     . ILE   B 1 11  ? 30.117  -10.112 92.257  1.00 63.32  ? 921  ILE   B C     1 
ATOM   2200 O  O     . ILE   B 1 11  ? 30.848  -10.501 93.175  1.00 64.55  ? 921  ILE   B O     1 
ATOM   2201 C  CB    . ILE   B 1 11  ? 28.603  -12.097 91.931  1.00 64.94  ? 921  ILE   B CB    1 
ATOM   2202 C  CG1   . ILE   B 1 11  ? 28.072  -13.136 90.939  1.00 69.46  ? 921  ILE   B CG1   1 
ATOM   2203 C  CG2   . ILE   B 1 11  ? 27.444  -11.355 92.613  1.00 59.82  ? 921  ILE   B CG2   1 
ATOM   2204 C  CD1   . ILE   B 1 11  ? 26.903  -13.967 91.482  1.00 69.53  ? 921  ILE   B CD1   1 
ATOM   2205 N  N     . ILE   B 1 12  ? 29.779  -8.833  92.104  1.00 53.02  ? 922  ILE   B N     1 
ATOM   2206 C  CA    . ILE   B 1 12  ? 30.371  -7.785  92.929  1.00 48.60  ? 922  ILE   B CA    1 
ATOM   2207 C  C     . ILE   B 1 12  ? 29.365  -7.036  93.789  1.00 40.41  ? 922  ILE   B C     1 
ATOM   2208 O  O     . ILE   B 1 12  ? 29.782  -6.328  94.711  1.00 40.97  ? 922  ILE   B O     1 
ATOM   2209 C  CB    . ILE   B 1 12  ? 31.191  -6.789  92.081  1.00 50.83  ? 922  ILE   B CB    1 
ATOM   2210 C  CG1   . ILE   B 1 12  ? 30.425  -6.350  90.841  1.00 47.38  ? 922  ILE   B CG1   1 
ATOM   2211 C  CG2   . ILE   B 1 12  ? 32.509  -7.415  91.672  1.00 51.69  ? 922  ILE   B CG2   1 
ATOM   2212 C  CD1   . ILE   B 1 12  ? 31.262  -5.511  89.889  1.00 45.12  ? 922  ILE   B CD1   1 
ATOM   2213 N  N     . CYS   B 1 13  ? 28.062  -7.175  93.560  1.00 40.89  ? 923  CYS   B N     1 
ATOM   2214 C  CA    . CYS   B 1 13  ? 27.075  -6.597  94.473  1.00 40.24  ? 923  CYS   B CA    1 
ATOM   2215 C  C     . CYS   B 1 13  ? 25.836  -7.470  94.390  1.00 35.28  ? 923  CYS   B C     1 
ATOM   2216 O  O     . CYS   B 1 13  ? 25.308  -7.682  93.300  1.00 34.21  ? 923  CYS   B O     1 
ATOM   2217 C  CB    . CYS   B 1 13  ? 26.759  -5.130  94.125  1.00 34.45  ? 923  CYS   B CB    1 
ATOM   2218 S  SG    . CYS   B 1 13  ? 25.488  -4.244  95.170  1.00 38.71  ? 923  CYS   B SG    1 
ATOM   2219 N  N     . ARG   B 1 14  ? 25.402  -8.015  95.522  1.00 35.83  ? 924  ARG   B N     1 
ATOM   2220 C  CA    . ARG   B 1 14  ? 24.245  -8.892  95.476  1.00 37.25  ? 924  ARG   B CA    1 
ATOM   2221 C  C     . ARG   B 1 14  ? 22.945  -8.127  95.240  1.00 32.30  ? 924  ARG   B C     1 
ATOM   2222 O  O     . ARG   B 1 14  ? 21.977  -8.739  94.792  1.00 33.34  ? 924  ARG   B O     1 
ATOM   2223 C  CB    . ARG   B 1 14  ? 24.184  -9.740  96.748  1.00 40.68  ? 924  ARG   B CB    1 
ATOM   2224 C  CG    . ARG   B 1 14  ? 25.473  -10.557 96.958  1.00 43.79  ? 924  ARG   B CG    1 
ATOM   2225 C  CD    . ARG   B 1 14  ? 25.206  -11.966 97.446  1.00 41.99  ? 924  ARG   B CD    1 
ATOM   2226 N  NE    . ARG   B 1 14  ? 26.307  -12.868 97.133  1.00 46.16  ? 924  ARG   B NE    1 
ATOM   2227 C  CZ    . ARG   B 1 14  ? 26.427  -13.537 95.993  1.00 52.12  ? 924  ARG   B CZ    1 
ATOM   2228 N  NH1   . ARG   B 1 14  ? 25.531  -13.420 95.026  1.00 54.77  ? 924  ARG   B NH1   1 
ATOM   2229 N  NH2   . ARG   B 1 14  ? 27.474  -14.341 95.817  1.00 49.04  ? 924  ARG   B NH2   1 
ATOM   2230 N  N     . ASP   B 1 15  ? 22.918  -6.804  95.467  1.00 32.18  ? 925  ASP   B N     1 
ATOM   2231 C  CA    . ASP   B 1 15  ? 21.739  -5.978  95.162  1.00 33.17  ? 925  ASP   B CA    1 
ATOM   2232 C  C     . ASP   B 1 15  ? 22.065  -4.490  95.188  1.00 32.80  ? 925  ASP   B C     1 
ATOM   2233 O  O     . ASP   B 1 15  ? 22.170  -3.891  96.264  1.00 30.22  ? 925  ASP   B O     1 
ATOM   2234 C  CB    . ASP   B 1 15  ? 20.601  -6.262  96.158  1.00 31.96  ? 925  ASP   B CB    1 
ATOM   2235 C  CG    . ASP   B 1 15  ? 19.256  -5.601  95.767  1.00 33.42  ? 925  ASP   B CG    1 
ATOM   2236 O  OD1   . ASP   B 1 15  ? 18.979  -5.351  94.573  1.00 30.03  ? 925  ASP   B OD1   1 
ATOM   2237 O  OD2   . ASP   B 1 15  ? 18.457  -5.348  96.684  1.00 30.90  ? 925  ASP   B OD2   1 
ATOM   2238 N  N     . VAL   B 1 16  ? 22.217  -3.872  94.014  1.00 32.78  ? 926  VAL   B N     1 
ATOM   2239 C  CA    . VAL   B 1 16  ? 22.494  -2.445  94.011  1.00 29.71  ? 926  VAL   B CA    1 
ATOM   2240 C  C     . VAL   B 1 16  ? 21.274  -1.682  94.507  1.00 32.63  ? 926  VAL   B C     1 
ATOM   2241 O  O     . VAL   B 1 16  ? 21.397  -0.555  94.997  1.00 30.65  ? 926  VAL   B O     1 
ATOM   2242 C  CB    . VAL   B 1 16  ? 22.904  -1.963  92.608  1.00 31.52  ? 926  VAL   B CB    1 
ATOM   2243 C  CG1   . VAL   B 1 16  ? 24.158  -2.671  92.119  1.00 28.35  ? 926  VAL   B CG1   1 
ATOM   2244 C  CG2   . VAL   B 1 16  ? 21.747  -2.162  91.628  1.00 30.41  ? 926  VAL   B CG2   1 
ATOM   2245 N  N     . ALA   B 1 17  ? 20.095  -2.296  94.423  1.00 32.08  ? 927  ALA   B N     1 
ATOM   2246 C  CA    . ALA   B 1 17  ? 18.874  -1.684  94.929  1.00 30.77  ? 927  ALA   B CA    1 
ATOM   2247 C  C     . ALA   B 1 17  ? 18.825  -1.618  96.451  1.00 32.53  ? 927  ALA   B C     1 
ATOM   2248 O  O     . ALA   B 1 17  ? 17.933  -0.964  96.991  1.00 34.73  ? 927  ALA   B O     1 
ATOM   2249 C  CB    . ALA   B 1 17  ? 17.666  -2.444  94.400  1.00 29.71  ? 927  ALA   B CB    1 
ATOM   2250 N  N     . ARG   B 1 18  ? 19.776  -2.236  97.153  1.00 35.56  ? 928  ARG   B N     1 
ATOM   2251 C  CA    . ARG   B 1 18  ? 19.773  -2.247  98.621  1.00 38.56  ? 928  ARG   B CA    1 
ATOM   2252 C  C     . ARG   B 1 18  ? 18.402  -2.642  99.167  1.00 35.83  ? 928  ARG   B C     1 
ATOM   2253 O  O     . ARG   B 1 18  ? 17.953  -2.125  100.188 1.00 38.09  ? 928  ARG   B O     1 
ATOM   2254 C  CB    . ARG   B 1 18  ? 20.204  -0.891  99.208  1.00 36.17  ? 928  ARG   B CB    1 
ATOM   2255 C  CG    . ARG   B 1 18  ? 21.485  -0.294  98.619  1.00 37.99  ? 928  ARG   B CG    1 
ATOM   2256 C  CD    . ARG   B 1 18  ? 22.074  0.837   99.510  1.00 38.70  ? 928  ARG   B CD    1 
ATOM   2257 N  NE    . ARG   B 1 18  ? 21.058  1.666   100.161 1.00 38.54  ? 928  ARG   B NE    1 
ATOM   2258 C  CZ    . ARG   B 1 18  ? 20.243  2.508   99.532  1.00 37.22  ? 928  ARG   B CZ    1 
ATOM   2259 N  NH1   . ARG   B 1 18  ? 20.287  2.664   98.218  1.00 30.89  ? 928  ARG   B NH1   1 
ATOM   2260 N  NH2   . ARG   B 1 18  ? 19.360  3.212   100.240 1.00 38.93  ? 928  ARG   B NH2   1 
ATOM   2261 N  N     . GLY   B 1 19  ? 17.716  -3.547  98.474  1.00 42.30  ? 929  GLY   B N     1 
ATOM   2262 C  CA    . GLY   B 1 19  ? 16.491  -4.135  98.981  1.00 40.04  ? 929  GLY   B CA    1 
ATOM   2263 C  C     . GLY   B 1 19  ? 15.215  -3.359  98.719  1.00 37.16  ? 929  GLY   B C     1 
ATOM   2264 O  O     . GLY   B 1 19  ? 14.142  -3.834  99.114  1.00 40.49  ? 929  GLY   B O     1 
ATOM   2265 N  N     . TYR   B 1 20  ? 15.285  -2.191  98.063  1.00 34.88  ? 930  TYR   B N     1 
ATOM   2266 C  CA    . TYR   B 1 20  ? 14.102  -1.360  97.809  1.00 33.97  ? 930  TYR   B CA    1 
ATOM   2267 C  C     . TYR   B 1 20  ? 13.218  -1.880  96.687  1.00 30.61  ? 930  TYR   B C     1 
ATOM   2268 O  O     . TYR   B 1 20  ? 12.094  -1.400  96.545  1.00 35.58  ? 930  TYR   B O     1 
ATOM   2269 C  CB    . TYR   B 1 20  ? 14.506  0.085   97.482  1.00 32.64  ? 930  TYR   B CB    1 
ATOM   2270 C  CG    . TYR   B 1 20  ? 14.655  0.949   98.704  1.00 30.34  ? 930  TYR   B CG    1 
ATOM   2271 C  CD1   . TYR   B 1 20  ? 15.809  0.912   99.456  1.00 32.79  ? 930  TYR   B CD1   1 
ATOM   2272 C  CD2   . TYR   B 1 20  ? 13.638  1.790   99.113  1.00 32.99  ? 930  TYR   B CD2   1 
ATOM   2273 C  CE1   . TYR   B 1 20  ? 15.954  1.694   100.578 1.00 29.64  ? 930  TYR   B CE1   1 
ATOM   2274 C  CE2   . TYR   B 1 20  ? 13.778  2.581   100.234 1.00 32.57  ? 930  TYR   B CE2   1 
ATOM   2275 C  CZ    . TYR   B 1 20  ? 14.946  2.522   100.961 1.00 32.89  ? 930  TYR   B CZ    1 
ATOM   2276 O  OH    . TYR   B 1 20  ? 15.106  3.286   102.090 1.00 34.26  ? 930  TYR   B OH    1 
ATOM   2277 N  N     . GLU   B 1 21  ? 13.684  -2.819  95.877  1.00 30.37  ? 931  GLU   B N     1 
ATOM   2278 C  CA    . GLU   B 1 21  ? 12.851  -3.368  94.822  1.00 29.51  ? 931  GLU   B CA    1 
ATOM   2279 C  C     . GLU   B 1 21  ? 12.270  -4.705  95.268  1.00 30.60  ? 931  GLU   B C     1 
ATOM   2280 O  O     . GLU   B 1 21  ? 12.611  -5.234  96.329  1.00 28.20  ? 931  GLU   B O     1 
ATOM   2281 C  CB    . GLU   B 1 21  ? 13.642  -3.502  93.521  1.00 28.35  ? 931  GLU   B CB    1 
ATOM   2282 C  CG    . GLU   B 1 21  ? 14.394  -2.227  93.102  1.00 28.96  ? 931  GLU   B CG    1 
ATOM   2283 C  CD    . GLU   B 1 21  ? 13.465  -1.107  92.616  1.00 31.29  ? 931  GLU   B CD    1 
ATOM   2284 O  OE1   . GLU   B 1 21  ? 12.241  -1.328  92.616  1.00 29.14  ? 931  GLU   B OE1   1 
ATOM   2285 O  OE2   . GLU   B 1 21  ? 13.963  -0.020  92.226  1.00 31.16  ? 931  GLU   B OE2   1 
ATOM   2286 N  N     . ASN   B 1 22  ? 11.324  -5.216  94.475  1.00 29.09  ? 932  ASN   B N     1 
ATOM   2287 C  CA    . ASN   B 1 22  ? 10.714  -6.496  94.814  1.00 30.63  ? 932  ASN   B CA    1 
ATOM   2288 C  C     . ASN   B 1 22  ? 11.704  -7.642  94.680  1.00 30.14  ? 932  ASN   B C     1 
ATOM   2289 O  O     . ASN   B 1 22  ? 11.565  -8.664  95.359  1.00 32.84  ? 932  ASN   B O     1 
ATOM   2290 C  CB    . ASN   B 1 22  ? 9.501   -6.764  93.925  1.00 30.01  ? 932  ASN   B CB    1 
ATOM   2291 C  CG    . ASN   B 1 22  ? 8.339   -5.893  94.267  1.00 28.27  ? 932  ASN   B CG    1 
ATOM   2292 O  OD1   . ASN   B 1 22  ? 7.707   -5.315  93.389  1.00 26.06  ? 932  ASN   B OD1   1 
ATOM   2293 N  ND2   . ASN   B 1 22  ? 8.060   -5.768  95.559  1.00 27.94  ? 932  ASN   B ND2   1 
ATOM   2294 N  N     . VAL   B 1 23  ? 12.683  -7.511  93.793  1.00 34.67  ? 933  VAL   B N     1 
ATOM   2295 C  CA    . VAL   B 1 23  ? 13.684  -8.557  93.588  1.00 29.93  ? 933  VAL   B CA    1 
ATOM   2296 C  C     . VAL   B 1 23  ? 15.060  -7.914  93.666  1.00 28.09  ? 933  VAL   B C     1 
ATOM   2297 O  O     . VAL   B 1 23  ? 15.204  -6.704  93.448  1.00 34.61  ? 933  VAL   B O     1 
ATOM   2298 C  CB    . VAL   B 1 23  ? 13.484  -9.274  92.235  1.00 30.90  ? 933  VAL   B CB    1 
ATOM   2299 C  CG1   . VAL   B 1 23  ? 12.085  -9.842  92.147  1.00 34.21  ? 933  VAL   B CG1   1 
ATOM   2300 C  CG2   . VAL   B 1 23  ? 13.741  -8.317  91.090  1.00 30.80  ? 933  VAL   B CG2   1 
ATOM   2301 N  N     . PRO   B 1 24  ? 16.091  -8.685  93.996  1.00 33.49  ? 934  PRO   B N     1 
ATOM   2302 C  CA    . PRO   B 1 24  ? 17.443  -8.109  94.017  1.00 30.64  ? 934  PRO   B CA    1 
ATOM   2303 C  C     . PRO   B 1 24  ? 17.963  -7.869  92.613  1.00 30.04  ? 934  PRO   B C     1 
ATOM   2304 O  O     . PRO   B 1 24  ? 17.646  -8.598  91.673  1.00 31.79  ? 934  PRO   B O     1 
ATOM   2305 C  CB    . PRO   B 1 24  ? 18.276  -9.160  94.756  1.00 30.05  ? 934  PRO   B CB    1 
ATOM   2306 C  CG    . PRO   B 1 24  ? 17.512  -10.439 94.621  1.00 35.84  ? 934  PRO   B CG    1 
ATOM   2307 C  CD    . PRO   B 1 24  ? 16.056  -10.079 94.489  1.00 29.23  ? 934  PRO   B CD    1 
ATOM   2308 N  N     . ILE   B 1 25  ? 18.742  -6.802  92.472  1.00 28.33  ? 935  ILE   B N     1 
ATOM   2309 C  CA    . ILE   B 1 25  ? 19.407  -6.502  91.205  1.00 31.46  ? 935  ILE   B CA    1 
ATOM   2310 C  C     . ILE   B 1 25  ? 20.927  -6.626  91.386  1.00 30.26  ? 935  ILE   B C     1 
ATOM   2311 O  O     . ILE   B 1 25  ? 21.607  -5.662  91.777  1.00 31.06  ? 935  ILE   B O     1 
ATOM   2312 C  CB    . ILE   B 1 25  ? 18.969  -5.123  90.686  1.00 28.65  ? 935  ILE   B CB    1 
ATOM   2313 C  CG1   . ILE   B 1 25  ? 17.456  -5.138  90.432  1.00 31.75  ? 935  ILE   B CG1   1 
ATOM   2314 C  CG2   . ILE   B 1 25  ? 19.692  -4.749  89.409  1.00 27.92  ? 935  ILE   B CG2   1 
ATOM   2315 C  CD1   . ILE   B 1 25  ? 16.891  -3.809  89.992  1.00 28.42  ? 935  ILE   B CD1   1 
ATOM   2316 N  N     . PRO   B 1 26  ? 21.501  -7.801  91.134  1.00 32.74  ? 936  PRO   B N     1 
ATOM   2317 C  CA    . PRO   B 1 26  ? 22.951  -7.987  91.329  1.00 33.60  ? 936  PRO   B CA    1 
ATOM   2318 C  C     . PRO   B 1 26  ? 23.796  -7.298  90.258  1.00 33.43  ? 936  PRO   B C     1 
ATOM   2319 O  O     . PRO   B 1 26  ? 23.337  -7.002  89.155  1.00 38.15  ? 936  PRO   B O     1 
ATOM   2320 C  CB    . PRO   B 1 26  ? 23.123  -9.507  91.269  1.00 34.83  ? 936  PRO   B CB    1 
ATOM   2321 C  CG    . PRO   B 1 26  ? 21.885  -10.009 90.542  1.00 39.19  ? 936  PRO   B CG    1 
ATOM   2322 C  CD    . PRO   B 1 26  ? 20.789  -9.067  90.882  1.00 33.30  ? 936  PRO   B CD    1 
ATOM   2323 N  N     . CYS   B 1 27  ? 25.063  -7.050  90.608  1.00 33.97  ? 937  CYS   B N     1 
ATOM   2324 C  CA    . CYS   B 1 27  ? 26.059  -6.463  89.709  1.00 40.91  ? 937  CYS   B CA    1 
ATOM   2325 C  C     . CYS   B 1 27  ? 27.241  -7.409  89.484  1.00 41.51  ? 937  CYS   B C     1 
ATOM   2326 O  O     . CYS   B 1 27  ? 27.745  -8.020  90.433  1.00 41.34  ? 937  CYS   B O     1 
ATOM   2327 C  CB    . CYS   B 1 27  ? 26.606  -5.140  90.262  1.00 41.04  ? 937  CYS   B CB    1 
ATOM   2328 S  SG    . CYS   B 1 27  ? 27.811  -4.295  89.189  1.00 34.39  ? 937  CYS   B SG    1 
ATOM   2329 N  N     . VAL   B 1 28  ? 27.683  -7.515  88.221  1.00 39.48  ? 938  VAL   B N     1 
ATOM   2330 C  CA    . VAL   B 1 28  ? 28.803  -8.363  87.818  1.00 44.00  ? 938  VAL   B CA    1 
ATOM   2331 C  C     . VAL   B 1 28  ? 29.719  -7.599  86.867  1.00 40.68  ? 938  VAL   B C     1 
ATOM   2332 O  O     . VAL   B 1 28  ? 29.318  -6.632  86.218  1.00 39.79  ? 938  VAL   B O     1 
ATOM   2333 C  CB    . VAL   B 1 28  ? 28.341  -9.681  87.140  1.00 45.41  ? 938  VAL   B CB    1 
ATOM   2334 C  CG1   . VAL   B 1 28  ? 27.331  -10.415 88.015  1.00 46.07  ? 938  VAL   B CG1   1 
ATOM   2335 C  CG2   . VAL   B 1 28  ? 27.769  -9.416  85.745  1.00 42.67  ? 938  VAL   B CG2   1 
ATOM   2336 N  N     . ASN   B 1 29  ? 30.969  -8.050  86.783  1.00 44.40  ? 939  ASN   B N     1 
ATOM   2337 C  CA    . ASN   B 1 29  ? 31.903  -7.516  85.793  1.00 41.54  ? 939  ASN   B CA    1 
ATOM   2338 C  C     . ASN   B 1 29  ? 32.866  -8.634  85.418  1.00 47.31  ? 939  ASN   B C     1 
ATOM   2339 O  O     . ASN   B 1 29  ? 33.715  -9.026  86.223  1.00 51.06  ? 939  ASN   B O     1 
ATOM   2340 C  CB    . ASN   B 1 29  ? 32.644  -6.288  86.327  1.00 41.32  ? 939  ASN   B CB    1 
ATOM   2341 C  CG    . ASN   B 1 29  ? 33.525  -5.615  85.264  1.00 38.42  ? 939  ASN   B CG    1 
ATOM   2342 O  OD1   . ASN   B 1 29  ? 33.865  -6.220  84.256  1.00 39.25  ? 939  ASN   B OD1   1 
ATOM   2343 N  ND2   . ASN   B 1 29  ? 33.881  -4.363  85.492  1.00 37.99  ? 939  ASN   B ND2   1 
ATOM   2344 N  N     . GLY   B 1 30  ? 32.726  -9.151  84.204  1.00 48.15  ? 940  GLY   B N     1 
ATOM   2345 C  CA    . GLY   B 1 30  ? 33.663  -10.138 83.713  1.00 49.77  ? 940  GLY   B CA    1 
ATOM   2346 C  C     . GLY   B 1 30  ? 34.440  -9.577  82.550  1.00 48.59  ? 940  GLY   B C     1 
ATOM   2347 O  O     . GLY   B 1 30  ? 35.006  -10.315 81.741  1.00 52.73  ? 940  GLY   B O     1 
ATOM   2348 N  N     . VAL   B 1 31  ? 34.466  -8.251  82.456  1.00 43.83  ? 941  VAL   B N     1 
ATOM   2349 C  CA    . VAL   B 1 31  ? 35.062  -7.547  81.325  1.00 42.11  ? 941  VAL   B CA    1 
ATOM   2350 C  C     . VAL   B 1 31  ? 36.372  -6.860  81.721  1.00 42.33  ? 941  VAL   B C     1 
ATOM   2351 O  O     . VAL   B 1 31  ? 37.425  -7.162  81.165  1.00 43.53  ? 941  VAL   B O     1 
ATOM   2352 C  CB    . VAL   B 1 31  ? 34.063  -6.542  80.711  1.00 42.32  ? 941  VAL   B CB    1 
ATOM   2353 C  CG1   . VAL   B 1 31  ? 34.729  -5.752  79.603  1.00 41.84  ? 941  VAL   B CG1   1 
ATOM   2354 C  CG2   . VAL   B 1 31  ? 32.815  -7.265  80.205  1.00 41.18  ? 941  VAL   B CG2   1 
ATOM   2355 N  N     . ASP   B 1 32  ? 36.320  -5.925  82.666  1.00 41.30  ? 942  ASP   B N     1 
ATOM   2356 C  CA    . ASP   B 1 32  ? 37.491  -5.133  83.049  1.00 41.53  ? 942  ASP   B CA    1 
ATOM   2357 C  C     . ASP   B 1 32  ? 37.558  -5.069  84.571  1.00 41.06  ? 942  ASP   B C     1 
ATOM   2358 O  O     . ASP   B 1 32  ? 36.901  -5.845  85.276  1.00 42.13  ? 942  ASP   B O     1 
ATOM   2359 C  CB    . ASP   B 1 32  ? 37.446  -3.734  82.417  1.00 41.12  ? 942  ASP   B CB    1 
ATOM   2360 C  CG    . ASP   B 1 32  ? 36.206  -2.939  82.823  1.00 39.81  ? 942  ASP   B CG    1 
ATOM   2361 O  OD1   . ASP   B 1 32  ? 35.377  -3.457  83.611  1.00 41.05  ? 942  ASP   B OD1   1 
ATOM   2362 O  OD2   . ASP   B 1 32  ? 36.058  -1.794  82.340  1.00 39.59  ? 942  ASP   B OD2   1 
ATOM   2363 N  N     . GLY   B 1 33  ? 38.348  -4.132  85.087  1.00 41.07  ? 943  GLY   B N     1 
ATOM   2364 C  CA    . GLY   B 1 33  ? 38.506  -3.943  86.511  1.00 40.89  ? 943  GLY   B CA    1 
ATOM   2365 C  C     . GLY   B 1 33  ? 37.694  -2.824  87.135  1.00 39.81  ? 943  GLY   B C     1 
ATOM   2366 O  O     . GLY   B 1 33  ? 37.979  -2.446  88.278  1.00 39.88  ? 943  GLY   B O     1 
ATOM   2367 N  N     . GLU   B 1 34  ? 36.694  -2.280  86.434  1.00 38.98  ? 944  GLU   B N     1 
ATOM   2368 C  CA    . GLU   B 1 34  ? 35.865  -1.226  87.012  1.00 38.07  ? 944  GLU   B CA    1 
ATOM   2369 C  C     . GLU   B 1 34  ? 35.157  -1.763  88.255  1.00 37.66  ? 944  GLU   B C     1 
ATOM   2370 O  O     . GLU   B 1 34  ? 34.621  -2.876  88.219  1.00 43.76  ? 944  GLU   B O     1 
ATOM   2371 C  CB    . GLU   B 1 34  ? 34.835  -0.736  85.983  1.00 38.70  ? 944  GLU   B CB    1 
ATOM   2372 C  CG    . GLU   B 1 34  ? 34.045  0.520   86.386  1.00 36.69  ? 944  GLU   B CG    1 
ATOM   2373 C  CD    . GLU   B 1 34  ? 34.935  1.738   86.537  1.00 37.49  ? 944  GLU   B CD    1 
ATOM   2374 O  OE1   . GLU   B 1 34  ? 35.872  1.869   85.727  1.00 37.99  ? 944  GLU   B OE1   1 
ATOM   2375 O  OE2   . GLU   B 1 34  ? 34.688  2.549   87.462  1.00 37.01  ? 944  GLU   B OE2   1 
ATOM   2376 N  N     . PRO   B 1 35  ? 35.145  -1.037  89.359  1.00 37.54  ? 945  PRO   B N     1 
ATOM   2377 C  CA    . PRO   B 1 35  ? 34.414  -1.486  90.544  1.00 37.30  ? 945  PRO   B CA    1 
ATOM   2378 C  C     . PRO   B 1 35  ? 32.927  -1.132  90.445  1.00 36.19  ? 945  PRO   B C     1 
ATOM   2379 O  O     . PRO   B 1 35  ? 32.478  -0.486  89.504  1.00 35.89  ? 945  PRO   B O     1 
ATOM   2380 C  CB    . PRO   B 1 35  ? 35.081  -0.709  91.668  1.00 37.87  ? 945  PRO   B CB    1 
ATOM   2381 C  CG    . PRO   B 1 35  ? 35.358  0.613   91.025  1.00 37.74  ? 945  PRO   B CG    1 
ATOM   2382 C  CD    . PRO   B 1 35  ? 35.763  0.278   89.582  1.00 37.81  ? 945  PRO   B CD    1 
ATOM   2383 N  N     . CYS   B 1 36  ? 32.186  -1.524  91.474  1.00 35.99  ? 946  CYS   B N     1 
ATOM   2384 C  CA    . CYS   B 1 36  ? 30.739  -1.312  91.499  1.00 35.02  ? 946  CYS   B CA    1 
ATOM   2385 C  C     . CYS   B 1 36  ? 30.427  0.182   91.448  1.00 37.76  ? 946  CYS   B C     1 
ATOM   2386 O  O     . CYS   B 1 36  ? 30.956  0.953   92.264  1.00 35.09  ? 946  CYS   B O     1 
ATOM   2387 C  CB    . CYS   B 1 36  ? 30.135  -1.942  92.755  1.00 38.90  ? 946  CYS   B CB    1 
ATOM   2388 S  SG    . CYS   B 1 36  ? 28.326  -1.847  92.895  1.00 44.23  ? 946  CYS   B SG    1 
ATOM   2389 N  N     . PRO   B 1 37  ? 29.609  0.631   90.502  1.00 33.90  ? 947  PRO   B N     1 
ATOM   2390 C  CA    . PRO   B 1 37  ? 29.335  2.066   90.384  1.00 37.02  ? 947  PRO   B CA    1 
ATOM   2391 C  C     . PRO   B 1 37  ? 28.732  2.616   91.672  1.00 36.22  ? 947  PRO   B C     1 
ATOM   2392 O  O     . PRO   B 1 37  ? 27.874  1.991   92.290  1.00 33.25  ? 947  PRO   B O     1 
ATOM   2393 C  CB    . PRO   B 1 37  ? 28.348  2.138   89.213  1.00 37.02  ? 947  PRO   B CB    1 
ATOM   2394 C  CG    . PRO   B 1 37  ? 27.792  0.758   89.100  1.00 35.77  ? 947  PRO   B CG    1 
ATOM   2395 C  CD    . PRO   B 1 37  ? 28.907  -0.147  89.477  1.00 35.85  ? 947  PRO   B CD    1 
ATOM   2396 N  N     . GLU   B 1 38  ? 29.230  3.786   92.101  1.00 34.22  ? 948  GLU   B N     1 
ATOM   2397 C  CA    . GLU   B 1 38  ? 28.800  4.339   93.382  1.00 35.63  ? 948  GLU   B CA    1 
ATOM   2398 C  C     . GLU   B 1 38  ? 28.938  5.856   93.430  1.00 38.63  ? 948  GLU   B C     1 
ATOM   2399 O  O     . GLU   B 1 38  ? 28.957  6.427   94.528  1.00 40.22  ? 948  GLU   B O     1 
ATOM   2400 C  CB    . GLU   B 1 38  ? 29.572  3.695   94.562  1.00 39.18  ? 948  GLU   B CB    1 
ATOM   2401 C  CG    . GLU   B 1 38  ? 28.840  2.500   95.200  1.00 45.90  ? 948  GLU   B CG    1 
ATOM   2402 C  CD    . GLU   B 1 38  ? 29.675  1.753   96.247  1.00 55.67  ? 948  GLU   B CD    1 
ATOM   2403 O  OE1   . GLU   B 1 38  ? 30.740  2.268   96.663  1.00 46.97  ? 948  GLU   B OE1   1 
ATOM   2404 O  OE2   . GLU   B 1 38  ? 29.251  0.641   96.651  1.00 58.53  ? 948  GLU   B OE2   1 
ATOM   2405 N  N     . ASP   B 1 39  ? 29.054  6.520   92.278  1.00 34.98  ? 949  ASP   B N     1 
ATOM   2406 C  CA    . ASP   B 1 39  ? 28.932  7.966   92.179  1.00 35.55  ? 949  ASP   B CA    1 
ATOM   2407 C  C     . ASP   B 1 39  ? 27.467  8.426   92.165  1.00 39.31  ? 949  ASP   B C     1 
ATOM   2408 O  O     . ASP   B 1 39  ? 27.178  9.514   91.650  1.00 40.06  ? 949  ASP   B O     1 
ATOM   2409 C  CB    . ASP   B 1 39  ? 29.648  8.461   90.918  1.00 40.77  ? 949  ASP   B CB    1 
ATOM   2410 C  CG    . ASP   B 1 39  ? 30.150  9.912   91.038  1.00 49.49  ? 949  ASP   B CG    1 
ATOM   2411 O  OD1   . ASP   B 1 39  ? 29.611  10.690  91.860  1.00 45.05  ? 949  ASP   B OD1   1 
ATOM   2412 O  OD2   . ASP   B 1 39  ? 31.097  10.279  90.295  1.00 57.20  ? 949  ASP   B OD2   1 
ATOM   2413 N  N     . TYR   B 1 40  ? 26.548  7.624   92.703  1.00 34.21  ? 950  TYR   B N     1 
ATOM   2414 C  CA    . TYR   B 1 40  ? 25.130  7.935   92.624  1.00 35.23  ? 950  TYR   B CA    1 
ATOM   2415 C  C     . TYR   B 1 40  ? 24.424  7.379   93.853  1.00 33.36  ? 950  TYR   B C     1 
ATOM   2416 O  O     . TYR   B 1 40  ? 24.958  6.536   94.575  1.00 33.52  ? 950  TYR   B O     1 
ATOM   2417 C  CB    . TYR   B 1 40  ? 24.501  7.373   91.338  1.00 33.44  ? 950  TYR   B CB    1 
ATOM   2418 C  CG    . TYR   B 1 40  ? 24.185  5.876   91.385  1.00 34.73  ? 950  TYR   B CG    1 
ATOM   2419 C  CD1   . TYR   B 1 40  ? 25.191  4.912   91.316  1.00 33.98  ? 950  TYR   B CD1   1 
ATOM   2420 C  CD2   . TYR   B 1 40  ? 22.878  5.437   91.483  1.00 32.35  ? 950  TYR   B CD2   1 
ATOM   2421 C  CE1   . TYR   B 1 40  ? 24.874  3.549   91.358  1.00 35.83  ? 950  TYR   B CE1   1 
ATOM   2422 C  CE2   . TYR   B 1 40  ? 22.563  4.104   91.520  1.00 31.00  ? 950  TYR   B CE2   1 
ATOM   2423 C  CZ    . TYR   B 1 40  ? 23.547  3.166   91.464  1.00 30.96  ? 950  TYR   B CZ    1 
ATOM   2424 O  OH    . TYR   B 1 40  ? 23.180  1.836   91.517  1.00 33.48  ? 950  TYR   B OH    1 
ATOM   2425 N  N     . LYS   B 1 41  ? 23.207  7.858   94.075  1.00 33.09  ? 951  LYS   B N     1 
ATOM   2426 C  CA    . LYS   B 1 41  ? 22.342  7.380   95.150  1.00 32.86  ? 951  LYS   B CA    1 
ATOM   2427 C  C     . LYS   B 1 41  ? 21.229  6.541   94.534  1.00 33.88  ? 951  LYS   B C     1 
ATOM   2428 O  O     . LYS   B 1 41  ? 20.356  7.081   93.842  1.00 32.55  ? 951  LYS   B O     1 
ATOM   2429 C  CB    . LYS   B 1 41  ? 21.770  8.556   95.939  1.00 33.59  ? 951  LYS   B CB    1 
ATOM   2430 C  CG    . LYS   B 1 41  ? 20.832  8.181   97.054  1.00 33.54  ? 951  LYS   B CG    1 
ATOM   2431 C  CD    . LYS   B 1 41  ? 21.527  7.322   98.062  1.00 34.04  ? 951  LYS   B CD    1 
ATOM   2432 C  CE    . LYS   B 1 41  ? 20.636  7.013   99.256  1.00 36.74  ? 951  LYS   B CE    1 
ATOM   2433 N  NZ    . LYS   B 1 41  ? 21.172  5.822   100.038 1.00 37.09  ? 951  LYS   B NZ    1 
ATOM   2434 N  N     . TYR   B 1 42  ? 21.247  5.229   94.786  1.00 31.33  ? 952  TYR   B N     1 
ATOM   2435 C  CA    . TYR   B 1 42  ? 20.147  4.397   94.319  1.00 35.38  ? 952  TYR   B CA    1 
ATOM   2436 C  C     . TYR   B 1 42  ? 18.862  4.733   95.090  1.00 30.28  ? 952  TYR   B C     1 
ATOM   2437 O  O     . TYR   B 1 42  ? 18.830  4.710   96.324  1.00 30.82  ? 952  TYR   B O     1 
ATOM   2438 C  CB    . TYR   B 1 42  ? 20.481  2.899   94.435  1.00 30.30  ? 952  TYR   B CB    1 
ATOM   2439 C  CG    . TYR   B 1 42  ? 19.516  2.070   93.603  1.00 32.74  ? 952  TYR   B CG    1 
ATOM   2440 C  CD1   . TYR   B 1 42  ? 18.199  1.902   94.014  1.00 30.10  ? 952  TYR   B CD1   1 
ATOM   2441 C  CD2   . TYR   B 1 42  ? 19.893  1.510   92.389  1.00 29.32  ? 952  TYR   B CD2   1 
ATOM   2442 C  CE1   . TYR   B 1 42  ? 17.292  1.201   93.269  1.00 29.61  ? 952  TYR   B CE1   1 
ATOM   2443 C  CE2   . TYR   B 1 42  ? 18.977  0.797   91.630  1.00 30.27  ? 952  TYR   B CE2   1 
ATOM   2444 C  CZ    . TYR   B 1 42  ? 17.668  0.661   92.082  1.00 28.37  ? 952  TYR   B CZ    1 
ATOM   2445 O  OH    . TYR   B 1 42  ? 16.713  -0.031  91.384  1.00 30.23  ? 952  TYR   B OH    1 
ATOM   2446 N  N     . ILE   B 1 43  ? 17.805  5.069   94.362  1.00 29.70  ? 953  ILE   B N     1 
ATOM   2447 C  CA    . ILE   B 1 43  ? 16.487  5.264   94.962  1.00 29.49  ? 953  ILE   B CA    1 
ATOM   2448 C  C     . ILE   B 1 43  ? 15.447  4.562   94.104  1.00 28.62  ? 953  ILE   B C     1 
ATOM   2449 O  O     . ILE   B 1 43  ? 15.542  4.535   92.875  1.00 28.33  ? 953  ILE   B O     1 
ATOM   2450 C  CB    . ILE   B 1 43  ? 16.127  6.758   95.134  1.00 32.66  ? 953  ILE   B CB    1 
ATOM   2451 C  CG1   . ILE   B 1 43  ? 16.674  7.577   93.969  1.00 31.09  ? 953  ILE   B CG1   1 
ATOM   2452 C  CG2   . ILE   B 1 43  ? 16.641  7.295   96.462  1.00 31.05  ? 953  ILE   B CG2   1 
ATOM   2453 C  CD1   . ILE   B 1 43  ? 15.826  8.738   93.605  1.00 30.52  ? 953  ILE   B CD1   1 
ATOM   2454 N  N     . SER   B 1 44  ? 14.432  4.006   94.763  1.00 29.50  ? 954  SER   B N     1 
ATOM   2455 C  CA    . SER   B 1 44  ? 13.420  3.227   94.065  1.00 29.91  ? 954  SER   B CA    1 
ATOM   2456 C  C     . SER   B 1 44  ? 12.298  4.077   93.476  1.00 27.80  ? 954  SER   B C     1 
ATOM   2457 O  O     . SER   B 1 44  ? 11.733  3.689   92.453  1.00 27.20  ? 954  SER   B O     1 
ATOM   2458 C  CB    . SER   B 1 44  ? 12.841  2.168   95.004  1.00 31.97  ? 954  SER   B CB    1 
ATOM   2459 O  OG    . SER   B 1 44  ? 12.520  2.737   96.253  1.00 30.59  ? 954  SER   B OG    1 
ATOM   2460 N  N     . GLU   B 1 45  ? 11.987  5.229   94.069  1.00 27.96  ? 955  GLU   B N     1 
ATOM   2461 C  CA    . GLU   B 1 45  ? 10.998  6.172   93.555  1.00 31.54  ? 955  GLU   B CA    1 
ATOM   2462 C  C     . GLU   B 1 45  ? 11.603  7.562   93.351  1.00 29.99  ? 955  GLU   B C     1 
ATOM   2463 O  O     . GLU   B 1 45  ? 12.658  7.899   93.893  1.00 29.82  ? 955  GLU   B O     1 
ATOM   2464 C  CB    . GLU   B 1 45  ? 9.791   6.261   94.499  1.00 31.45  ? 955  GLU   B CB    1 
ATOM   2465 C  CG    . GLU   B 1 45  ? 9.118   4.902   94.744  1.00 34.06  ? 955  GLU   B CG    1 
ATOM   2466 C  CD    . GLU   B 1 45  ? 8.413   4.854   96.083  1.00 40.05  ? 955  GLU   B CD    1 
ATOM   2467 O  OE1   . GLU   B 1 45  ? 7.997   5.931   96.569  1.00 40.34  ? 955  GLU   B OE1   1 
ATOM   2468 O  OE2   . GLU   B 1 45  ? 8.293   3.749   96.654  1.00 45.49  ? 955  GLU   B OE2   1 
ATOM   2469 N  N     . ASN   B 1 46  ? 10.895  8.379   92.572  1.00 29.78  ? 956  ASN   B N     1 
ATOM   2470 C  CA    . ASN   B 1 46  ? 11.366  9.711   92.213  1.00 32.37  ? 956  ASN   B CA    1 
ATOM   2471 C  C     . ASN   B 1 46  ? 11.535  10.608  93.439  1.00 32.33  ? 956  ASN   B C     1 
ATOM   2472 O  O     . ASN   B 1 46  ? 10.814  10.500  94.430  1.00 30.60  ? 956  ASN   B O     1 
ATOM   2473 C  CB    . ASN   B 1 46  ? 10.407  10.364  91.213  1.00 29.94  ? 956  ASN   B CB    1 
ATOM   2474 C  CG    . ASN   B 1 46  ? 10.415  9.659   89.867  1.00 32.63  ? 956  ASN   B CG    1 
ATOM   2475 O  OD1   . ASN   B 1 46  ? 11.437  9.050   89.485  1.00 29.28  ? 956  ASN   B OD1   1 
ATOM   2476 N  ND2   . ASN   B 1 46  ? 9.279   9.714   89.142  1.00 29.41  ? 956  ASN   B ND2   1 
ATOM   2477 N  N     . CYS   B 1 47  ? 12.539  11.479  93.382  1.00 31.54  ? 957  CYS   B N     1 
ATOM   2478 C  CA    . CYS   B 1 47  ? 12.812  12.384  94.478  1.00 32.68  ? 957  CYS   B CA    1 
ATOM   2479 C  C     . CYS   B 1 47  ? 12.695  13.814  93.974  1.00 33.90  ? 957  CYS   B C     1 
ATOM   2480 O  O     . CYS   B 1 47  ? 12.768  14.073  92.770  1.00 33.94  ? 957  CYS   B O     1 
ATOM   2481 C  CB    . CYS   B 1 47  ? 14.207  12.150  95.054  1.00 33.03  ? 957  CYS   B CB    1 
ATOM   2482 S  SG    . CYS   B 1 47  ? 15.512  12.713  93.918  1.00 37.25  ? 957  CYS   B SG    1 
ATOM   2483 N  N     . GLU   B 1 48  ? 12.529  14.750  94.900  1.00 35.11  ? 958  GLU   B N     1 
ATOM   2484 C  CA    . GLU   B 1 48  ? 12.612  16.155  94.545  1.00 36.64  ? 958  GLU   B CA    1 
ATOM   2485 C  C     . GLU   B 1 48  ? 13.644  16.851  95.411  1.00 39.43  ? 958  GLU   B C     1 
ATOM   2486 O  O     . GLU   B 1 48  ? 13.906  16.456  96.553  1.00 38.09  ? 958  GLU   B O     1 
ATOM   2487 C  CB    . GLU   B 1 48  ? 11.269  16.898  94.656  1.00 41.25  ? 958  GLU   B CB    1 
ATOM   2488 C  CG    . GLU   B 1 48  ? 10.317  16.401  95.714  1.00 38.70  ? 958  GLU   B CG    1 
ATOM   2489 C  CD    . GLU   B 1 48  ? 8.961   17.078  95.614  1.00 43.04  ? 958  GLU   B CD    1 
ATOM   2490 O  OE1   . GLU   B 1 48  ? 8.886   18.284  95.928  1.00 51.33  ? 958  GLU   B OE1   1 
ATOM   2491 O  OE2   . GLU   B 1 48  ? 7.979   16.422  95.203  1.00 42.46  ? 958  GLU   B OE2   1 
ATOM   2492 N  N     . THR   B 1 49  ? 14.207  17.912  94.831  1.00 39.36  ? 959  THR   B N     1 
ATOM   2493 C  CA    . THR   B 1 49  ? 15.269  18.715  95.420  1.00 40.96  ? 959  THR   B CA    1 
ATOM   2494 C  C     . THR   B 1 49  ? 14.958  20.206  95.349  1.00 43.00  ? 959  THR   B C     1 
ATOM   2495 O  O     . THR   B 1 49  ? 15.809  21.017  95.689  1.00 44.63  ? 959  THR   B O     1 
ATOM   2496 C  CB    . THR   B 1 49  ? 16.582  18.412  94.706  1.00 42.47  ? 959  THR   B CB    1 
ATOM   2497 O  OG1   . THR   B 1 49  ? 16.356  18.483  93.290  1.00 42.40  ? 959  THR   B OG1   1 
ATOM   2498 C  CG2   . THR   B 1 49  ? 17.081  16.995  95.067  1.00 39.11  ? 959  THR   B CG2   1 
ATOM   2499 N  N     . SER   B 1 50  ? 13.759  20.579  94.908  1.00 48.30  ? 960  SER   B N     1 
ATOM   2500 C  CA    . SER   B 1 50  ? 13.281  21.956  94.925  1.00 45.19  ? 960  SER   B CA    1 
ATOM   2501 C  C     . SER   B 1 50  ? 11.777  21.910  95.165  1.00 44.86  ? 960  SER   B C     1 
ATOM   2502 O  O     . SER   B 1 50  ? 11.186  20.835  95.234  1.00 44.40  ? 960  SER   B O     1 
ATOM   2503 C  CB    . SER   B 1 50  ? 13.625  22.671  93.618  1.00 46.13  ? 960  SER   B CB    1 
ATOM   2504 O  OG    . SER   B 1 50  ? 12.976  22.037  92.527  1.00 44.74  ? 960  SER   B OG    1 
ATOM   2505 N  N     . THR   B 1 51  ? 11.143  23.077  95.287  1.00 46.75  ? 961  THR   B N     1 
ATOM   2506 C  CA    . THR   B 1 51  ? 9.693   23.113  95.518  1.00 46.63  ? 961  THR   B CA    1 
ATOM   2507 C  C     . THR   B 1 51  ? 8.956   22.713  94.239  1.00 45.46  ? 961  THR   B C     1 
ATOM   2508 O  O     . THR   B 1 51  ? 9.128   23.343  93.194  1.00 46.41  ? 961  THR   B O     1 
ATOM   2509 C  CB    . THR   B 1 51  ? 9.264   24.500  95.998  1.00 49.23  ? 961  THR   B CB    1 
ATOM   2510 O  OG1   . THR   B 1 51  ? 9.718   24.705  97.341  1.00 50.24  ? 961  THR   B OG1   1 
ATOM   2511 C  CG2   . THR   B 1 51  ? 7.728   24.649  95.967  1.00 49.27  ? 961  THR   B CG2   1 
ATOM   2512 N  N     . MET   B 1 52  ? 8.173   21.633  94.306  1.00 43.92  ? 962  MET   B N     1 
ATOM   2513 C  CA    . MET   B 1 52  ? 7.480   21.062  93.151  1.00 42.34  ? 962  MET   B CA    1 
ATOM   2514 C  C     . MET   B 1 52  ? 5.966   21.108  93.266  1.00 44.02  ? 962  MET   B C     1 
ATOM   2515 O  O     . MET   B 1 52  ? 5.286   21.335  92.260  1.00 42.52  ? 962  MET   B O     1 
ATOM   2516 C  CB    . MET   B 1 52  ? 7.893   19.595  92.924  1.00 42.39  ? 962  MET   B CB    1 
ATOM   2517 C  CG    . MET   B 1 52  ? 9.098   19.367  92.026  1.00 50.44  ? 962  MET   B CG    1 
ATOM   2518 S  SD    . MET   B 1 52  ? 9.110   20.518  90.629  1.00 68.10  ? 962  MET   B SD    1 
ATOM   2519 C  CE    . MET   B 1 52  ? 10.702  20.162  89.899  1.00 41.32  ? 962  MET   B CE    1 
ATOM   2520 N  N     . ASN   B 1 53  ? 5.429   20.867  94.465  1.00 43.64  ? 963  ASN   B N     1 
ATOM   2521 C  CA    . ASN   B 1 53  ? 3.999   20.751  94.735  1.00 41.82  ? 963  ASN   B CA    1 
ATOM   2522 C  C     . ASN   B 1 53  ? 3.316   19.867  93.700  1.00 43.63  ? 963  ASN   B C     1 
ATOM   2523 O  O     . ASN   B 1 53  ? 2.518   20.350  92.886  1.00 40.87  ? 963  ASN   B O     1 
ATOM   2524 C  CB    . ASN   B 1 53  ? 3.316   22.121  94.771  1.00 44.05  ? 963  ASN   B CB    1 
ATOM   2525 C  CG    . ASN   B 1 53  ? 3.920   23.063  95.805  1.00 45.98  ? 963  ASN   B CG    1 
ATOM   2526 O  OD1   . ASN   B 1 53  ? 4.616   24.003  95.446  1.00 47.61  ? 963  ASN   B OD1   1 
ATOM   2527 N  ND2   . ASN   B 1 53  ? 3.627   22.834  97.084  1.00 46.01  ? 963  ASN   B ND2   1 
ATOM   2528 N  N     . ILE   B 1 54  ? 3.651   18.573  93.708  1.00 38.33  ? 964  ILE   B N     1 
ATOM   2529 C  CA    . ILE   B 1 54  ? 2.859   17.614  92.963  1.00 36.89  ? 964  ILE   B CA    1 
ATOM   2530 C  C     . ILE   B 1 54  ? 1.448   17.629  93.531  1.00 39.16  ? 964  ILE   B C     1 
ATOM   2531 O  O     . ILE   B 1 54  ? 1.250   17.501  94.747  1.00 36.95  ? 964  ILE   B O     1 
ATOM   2532 C  CB    . ILE   B 1 54  ? 3.474   16.212  93.060  1.00 38.94  ? 964  ILE   B CB    1 
ATOM   2533 C  CG1   . ILE   B 1 54  ? 4.937   16.230  92.578  1.00 36.11  ? 964  ILE   B CG1   1 
ATOM   2534 C  CG2   . ILE   B 1 54  ? 2.626   15.200  92.301  1.00 33.80  ? 964  ILE   B CG2   1 
ATOM   2535 C  CD1   . ILE   B 1 54  ? 5.645   14.958  92.828  1.00 33.74  ? 964  ILE   B CD1   1 
ATOM   2536 N  N     . ASP   B 1 55  ? 0.461   17.788  92.649  1.00 37.09  ? 965  ASP   B N     1 
ATOM   2537 C  CA    . ASP   B 1 55  ? -0.943  17.793  93.036  1.00 37.16  ? 965  ASP   B CA    1 
ATOM   2538 C  C     . ASP   B 1 55  ? -1.313  16.439  93.625  1.00 35.42  ? 965  ASP   B C     1 
ATOM   2539 O  O     . ASP   B 1 55  ? -1.572  15.487  92.881  1.00 34.20  ? 965  ASP   B O     1 
ATOM   2540 C  CB    . ASP   B 1 55  ? -1.794  18.141  91.811  1.00 37.69  ? 965  ASP   B CB    1 
ATOM   2541 C  CG    . ASP   B 1 55  ? -3.278  18.191  92.106  1.00 40.42  ? 965  ASP   B CG    1 
ATOM   2542 O  OD1   . ASP   B 1 55  ? -3.667  18.261  93.292  1.00 38.06  ? 965  ASP   B OD1   1 
ATOM   2543 O  OD2   . ASP   B 1 55  ? -4.052  18.159  91.123  1.00 41.59  ? 965  ASP   B OD2   1 
ATOM   2544 N  N     . ARG   B 1 56  ? -1.313  16.326  94.957  1.00 35.48  ? 966  ARG   B N     1 
ATOM   2545 C  CA    . ARG   B 1 56  ? -1.698  15.085  95.624  1.00 35.23  ? 966  ARG   B CA    1 
ATOM   2546 C  C     . ARG   B 1 56  ? -3.095  15.145  96.235  1.00 34.42  ? 966  ARG   B C     1 
ATOM   2547 O  O     . ARG   B 1 56  ? -3.414  14.323  97.097  1.00 35.61  ? 966  ARG   B O     1 
ATOM   2548 C  CB    . ARG   B 1 56  ? -0.694  14.711  96.714  1.00 35.49  ? 966  ARG   B CB    1 
ATOM   2549 C  CG    . ARG   B 1 56  ? 0.734   14.378  96.198  1.00 44.47  ? 966  ARG   B CG    1 
ATOM   2550 C  CD    . ARG   B 1 56  ? 1.681   14.066  97.358  1.00 44.88  ? 966  ARG   B CD    1 
ATOM   2551 N  NE    . ARG   B 1 56  ? 3.076   13.933  96.946  1.00 53.07  ? 966  ARG   B NE    1 
ATOM   2552 C  CZ    . ARG   B 1 56  ? 3.587   12.838  96.400  1.00 50.44  ? 966  ARG   B CZ    1 
ATOM   2553 N  NH1   . ARG   B 1 56  ? 2.835   11.784  96.138  1.00 52.48  ? 966  ARG   B NH1   1 
ATOM   2554 N  NH2   . ARG   B 1 56  ? 4.884   12.805  96.098  1.00 52.12  ? 966  ARG   B NH2   1 
ATOM   2555 N  N     . ASN   B 1 57  ? -3.923  16.109  95.840  1.00 35.54  ? 967  ASN   B N     1 
ATOM   2556 C  CA    . ASN   B 1 57  ? -5.291  16.165  96.353  1.00 35.86  ? 967  ASN   B CA    1 
ATOM   2557 C  C     . ASN   B 1 57  ? -6.036  14.908  95.910  1.00 34.71  ? 967  ASN   B C     1 
ATOM   2558 O  O     . ASN   B 1 57  ? -6.167  14.643  94.710  1.00 35.99  ? 967  ASN   B O     1 
ATOM   2559 C  CB    . ASN   B 1 57  ? -5.986  17.443  95.871  1.00 39.36  ? 967  ASN   B CB    1 
ATOM   2560 C  CG    . ASN   B 1 57  ? -7.312  17.716  96.595  1.00 38.53  ? 967  ASN   B CG    1 
ATOM   2561 O  OD1   . ASN   B 1 57  ? -8.124  16.815  96.784  1.00 38.41  ? 967  ASN   B OD1   1 
ATOM   2562 N  ND2   . ASN   B 1 57  ? -7.530  18.964  96.986  1.00 40.16  ? 967  ASN   B ND2   1 
ATOM   2563 N  N     . ILE   B 1 58  ? -6.478  14.100  96.878  1.00 33.69  ? 968  ILE   B N     1 
ATOM   2564 C  CA    . ILE   B 1 58  ? -7.189  12.868  96.535  1.00 33.81  ? 968  ILE   B CA    1 
ATOM   2565 C  C     . ILE   B 1 58  ? -8.514  13.170  95.837  1.00 35.60  ? 968  ILE   B C     1 
ATOM   2566 O  O     . ILE   B 1 58  ? -9.010  12.347  95.062  1.00 34.05  ? 968  ILE   B O     1 
ATOM   2567 C  CB    . ILE   B 1 58  ? -7.401  11.984  97.786  1.00 35.75  ? 968  ILE   B CB    1 
ATOM   2568 C  CG1   . ILE   B 1 58  ? -7.889  10.582  97.405  1.00 31.54  ? 968  ILE   B CG1   1 
ATOM   2569 C  CG2   . ILE   B 1 58  ? -8.396  12.621  98.743  1.00 33.08  ? 968  ILE   B CG2   1 
ATOM   2570 C  CD1   . ILE   B 1 58  ? -7.882  9.611   98.565  1.00 30.30  ? 968  ILE   B CD1   1 
ATOM   2571 N  N     . THR   B 1 59  ? -9.101  14.347  96.072  1.00 34.10  ? 969  THR   B N     1 
ATOM   2572 C  CA    . THR   B 1 59  ? -10.347 14.661  95.381  1.00 36.00  ? 969  THR   B CA    1 
ATOM   2573 C  C     . THR   B 1 59  ? -10.114 15.002  93.914  1.00 37.55  ? 969  THR   B C     1 
ATOM   2574 O  O     . THR   B 1 59  ? -11.062 14.973  93.124  1.00 41.58  ? 969  THR   B O     1 
ATOM   2575 C  CB    . THR   B 1 59  ? -11.110 15.809  96.079  1.00 39.30  ? 969  THR   B CB    1 
ATOM   2576 O  OG1   . THR   B 1 59  ? -10.456 17.079  95.885  1.00 37.71  ? 969  THR   B OG1   1 
ATOM   2577 C  CG2   . THR   B 1 59  ? -11.254 15.530  97.565  1.00 37.19  ? 969  THR   B CG2   1 
ATOM   2578 N  N     . HIS   B 1 60  ? -8.880  15.300  93.523  1.00 39.12  ? 970  HIS   B N     1 
ATOM   2579 C  CA    . HIS   B 1 60  ? -8.590  15.655  92.140  1.00 36.99  ? 970  HIS   B CA    1 
ATOM   2580 C  C     . HIS   B 1 60  ? -8.420  14.438  91.253  1.00 36.23  ? 970  HIS   B C     1 
ATOM   2581 O  O     . HIS   B 1 60  ? -8.127  14.599  90.063  1.00 36.25  ? 970  HIS   B O     1 
ATOM   2582 C  CB    . HIS   B 1 60  ? -7.330  16.515  92.070  1.00 39.28  ? 970  HIS   B CB    1 
ATOM   2583 C  CG    . HIS   B 1 60  ? -7.534  17.924  92.533  1.00 41.35  ? 970  HIS   B CG    1 
ATOM   2584 N  ND1   . HIS   B 1 60  ? -6.597  18.913  92.328  1.00 39.35  ? 970  HIS   B ND1   1 
ATOM   2585 C  CD2   . HIS   B 1 60  ? -8.569  18.511  93.182  1.00 39.08  ? 970  HIS   B CD2   1 
ATOM   2586 C  CE1   . HIS   B 1 60  ? -7.052  20.050  92.826  1.00 41.15  ? 970  HIS   B CE1   1 
ATOM   2587 N  NE2   . HIS   B 1 60  ? -8.236  19.828  93.364  1.00 41.01  ? 970  HIS   B NE2   1 
ATOM   2588 N  N     . LEU   B 1 61  ? -8.605  13.240  91.800  1.00 35.76  ? 971  LEU   B N     1 
ATOM   2589 C  CA    . LEU   B 1 61  ? -8.271  11.999  91.110  1.00 33.33  ? 971  LEU   B CA    1 
ATOM   2590 C  C     . LEU   B 1 61  ? -9.487  11.477  90.358  1.00 34.26  ? 971  LEU   B C     1 
ATOM   2591 O  O     . LEU   B 1 61  ? -10.504 11.125  90.972  1.00 34.46  ? 971  LEU   B O     1 
ATOM   2592 C  CB    . LEU   B 1 61  ? -7.786  10.943  92.099  1.00 30.23  ? 971  LEU   B CB    1 
ATOM   2593 C  CG    . LEU   B 1 61  ? -6.362  11.090  92.637  1.00 30.34  ? 971  LEU   B CG    1 
ATOM   2594 C  CD1   . LEU   B 1 61  ? -6.108  10.033  93.681  1.00 29.15  ? 971  LEU   B CD1   1 
ATOM   2595 C  CD2   . LEU   B 1 61  ? -5.369  10.996  91.493  1.00 29.89  ? 971  LEU   B CD2   1 
ATOM   2596 N  N     . GLN   B 1 62  ? -9.377  11.420  89.037  1.00 31.47  ? 972  GLN   B N     1 
ATOM   2597 C  CA    . GLN   B 1 62  ? -10.293 10.604  88.263  1.00 31.23  ? 972  GLN   B CA    1 
ATOM   2598 C  C     . GLN   B 1 62  ? -10.118 9.142   88.654  1.00 31.12  ? 972  GLN   B C     1 
ATOM   2599 O  O     . GLN   B 1 62  ? -8.995  8.666   88.854  1.00 30.59  ? 972  GLN   B O     1 
ATOM   2600 C  CB    . GLN   B 1 62  ? -10.032 10.828  86.783  1.00 32.03  ? 972  GLN   B CB    1 
ATOM   2601 C  CG    . GLN   B 1 62  ? -10.132 12.310  86.423  1.00 33.64  ? 972  GLN   B CG    1 
ATOM   2602 C  CD    . GLN   B 1 62  ? -10.387 12.532  84.959  1.00 34.81  ? 972  GLN   B CD    1 
ATOM   2603 O  OE1   . GLN   B 1 62  ? -11.425 12.140  84.435  1.00 43.07  ? 972  GLN   B OE1   1 
ATOM   2604 N  NE2   . GLN   B 1 62  ? -9.447  13.166  84.286  1.00 35.68  ? 972  GLN   B NE2   1 
ATOM   2605 N  N     . HIS   B 1 63  ? -11.236 8.440   88.812  1.00 29.56  ? 973  HIS   B N     1 
ATOM   2606 C  CA    . HIS   B 1 63  ? -11.230 7.116   89.423  1.00 28.50  ? 973  HIS   B CA    1 
ATOM   2607 C  C     . HIS   B 1 63  ? -12.484 6.363   89.009  1.00 31.46  ? 973  HIS   B C     1 
ATOM   2608 O  O     . HIS   B 1 63  ? -13.510 6.961   88.658  1.00 29.27  ? 973  HIS   B O     1 
ATOM   2609 C  CB    . HIS   B 1 63  ? -11.137 7.203   90.951  1.00 28.17  ? 973  HIS   B CB    1 
ATOM   2610 C  CG    . HIS   B 1 63  ? -12.378 7.723   91.610  1.00 32.32  ? 973  HIS   B CG    1 
ATOM   2611 N  ND1   . HIS   B 1 63  ? -12.573 9.060   91.876  1.00 36.04  ? 973  HIS   B ND1   1 
ATOM   2612 C  CD2   . HIS   B 1 63  ? -13.485 7.086   92.061  1.00 34.45  ? 973  HIS   B CD2   1 
ATOM   2613 C  CE1   . HIS   B 1 63  ? -13.747 9.228   92.458  1.00 30.01  ? 973  HIS   B CE1   1 
ATOM   2614 N  NE2   . HIS   B 1 63  ? -14.319 8.044   92.585  1.00 37.66  ? 973  HIS   B NE2   1 
ATOM   2615 N  N     . CYS   B 1 64  ? -12.391 5.037   89.060  1.00 32.06  ? 974  CYS   B N     1 
ATOM   2616 C  CA    . CYS   B 1 64  ? -13.445 4.174   88.550  1.00 29.82  ? 974  CYS   B CA    1 
ATOM   2617 C  C     . CYS   B 1 64  ? -14.372 3.723   89.686  1.00 28.18  ? 974  CYS   B C     1 
ATOM   2618 O  O     . CYS   B 1 64  ? -14.072 3.885   90.873  1.00 27.33  ? 974  CYS   B O     1 
ATOM   2619 C  CB    . CYS   B 1 64  ? -12.824 2.978   87.812  1.00 27.68  ? 974  CYS   B CB    1 
ATOM   2620 S  SG    . CYS   B 1 64  ? -11.976 1.807   88.855  1.00 26.78  ? 974  CYS   B SG    1 
ATOM   2621 N  N     . THR   B 1 65  ? -15.529 3.170   89.310  1.00 28.11  ? 975  THR   B N     1 
ATOM   2622 C  CA    . THR   B 1 65  ? -16.480 2.653   90.292  1.00 30.20  ? 975  THR   B CA    1 
ATOM   2623 C  C     . THR   B 1 65  ? -16.628 1.135   90.240  1.00 30.96  ? 975  THR   B C     1 
ATOM   2624 O  O     . THR   B 1 65  ? -17.523 0.588   90.897  1.00 35.31  ? 975  THR   B O     1 
ATOM   2625 C  CB    . THR   B 1 65  ? -17.862 3.304   90.119  1.00 31.15  ? 975  THR   B CB    1 
ATOM   2626 O  OG1   . THR   B 1 65  ? -18.369 3.036   88.803  1.00 31.43  ? 975  THR   B OG1   1 
ATOM   2627 C  CG2   . THR   B 1 65  ? -17.807 4.814   90.365  1.00 29.06  ? 975  THR   B CG2   1 
ATOM   2628 N  N     . CYS   B 1 66  ? -15.770 0.455   89.485  1.00 32.89  ? 976  CYS   B N     1 
ATOM   2629 C  CA    . CYS   B 1 66  ? -15.868 -0.977  89.211  1.00 29.28  ? 976  CYS   B CA    1 
ATOM   2630 C  C     . CYS   B 1 66  ? -15.985 -1.815  90.478  1.00 30.16  ? 976  CYS   B C     1 
ATOM   2631 O  O     . CYS   B 1 66  ? -15.315 -1.551  91.479  1.00 31.82  ? 976  CYS   B O     1 
ATOM   2632 C  CB    . CYS   B 1 66  ? -14.611 -1.397  88.438  1.00 29.97  ? 976  CYS   B CB    1 
ATOM   2633 S  SG    . CYS   B 1 66  ? -14.313 -0.308  87.035  1.00 32.49  ? 976  CYS   B SG    1 
ATOM   2634 N  N     . VAL   B 1 67  ? -16.794 -2.871  90.410  1.00 30.77  ? 977  VAL   B N     1 
ATOM   2635 C  CA    . VAL   B 1 67  ? -16.896 -3.843  91.493  1.00 31.14  ? 977  VAL   B CA    1 
ATOM   2636 C  C     . VAL   B 1 67  ? -16.329 -5.203  91.100  1.00 34.61  ? 977  VAL   B C     1 
ATOM   2637 O  O     . VAL   B 1 67  ? -16.467 -6.169  91.863  1.00 34.77  ? 977  VAL   B O     1 
ATOM   2638 C  CB    . VAL   B 1 67  ? -18.341 -3.986  91.998  1.00 36.04  ? 977  VAL   B CB    1 
ATOM   2639 C  CG1   . VAL   B 1 67  ? -18.841 -2.655  92.509  1.00 33.47  ? 977  VAL   B CG1   1 
ATOM   2640 C  CG2   . VAL   B 1 67  ? -19.267 -4.586  90.917  1.00 32.25  ? 977  VAL   B CG2   1 
ATOM   2641 N  N     . ASP   B 1 68  ? -15.691 -5.305  89.932  1.00 34.80  ? 978  ASP   B N     1 
ATOM   2642 C  CA    . ASP   B 1 68  ? -15.005 -6.491  89.440  1.00 32.79  ? 978  ASP   B CA    1 
ATOM   2643 C  C     . ASP   B 1 68  ? -13.497 -6.231  89.535  1.00 35.47  ? 978  ASP   B C     1 
ATOM   2644 O  O     . ASP   B 1 68  ? -13.067 -5.388  90.338  1.00 33.32  ? 978  ASP   B O     1 
ATOM   2645 C  CB    . ASP   B 1 68  ? -15.496 -6.810  88.024  1.00 29.23  ? 978  ASP   B CB    1 
ATOM   2646 C  CG    . ASP   B 1 68  ? -15.076 -5.752  87.008  1.00 33.09  ? 978  ASP   B CG    1 
ATOM   2647 O  OD1   . ASP   B 1 68  ? -14.736 -4.630  87.428  1.00 28.44  ? 978  ASP   B OD1   1 
ATOM   2648 O  OD2   . ASP   B 1 68  ? -15.104 -6.026  85.796  1.00 34.66  ? 978  ASP   B OD2   1 
ATOM   2649 N  N     . ASP   B 1 69  ? -12.707 -6.916  88.715  1.00 29.86  ? 979  ASP   B N     1 
ATOM   2650 C  CA    . ASP   B 1 69  ? -11.265 -6.713  88.728  1.00 33.59  ? 979  ASP   B CA    1 
ATOM   2651 C  C     . ASP   B 1 69  ? -10.822 -5.617  87.755  1.00 32.24  ? 979  ASP   B C     1 
ATOM   2652 O  O     . ASP   B 1 69  ? -9.620  -5.479  87.497  1.00 31.68  ? 979  ASP   B O     1 
ATOM   2653 C  CB    . ASP   B 1 69  ? -10.543 -8.027  88.424  1.00 29.09  ? 979  ASP   B CB    1 
ATOM   2654 C  CG    . ASP   B 1 69  ? -10.960 -8.622  87.112  1.00 29.52  ? 979  ASP   B CG    1 
ATOM   2655 O  OD1   . ASP   B 1 69  ? -11.767 -7.999  86.390  1.00 32.36  ? 979  ASP   B OD1   1 
ATOM   2656 O  OD2   . ASP   B 1 69  ? -10.471 -9.718  86.790  1.00 37.29  ? 979  ASP   B OD2   1 
ATOM   2657 N  N     . CYS   B 1 70  ? -11.765 -4.821  87.246  1.00 31.89  ? 980  CYS   B N     1 
ATOM   2658 C  CA    . CYS   B 1 70  ? -11.501 -3.757  86.279  1.00 33.16  ? 980  CYS   B CA    1 
ATOM   2659 C  C     . CYS   B 1 70  ? -11.030 -4.304  84.939  1.00 34.38  ? 980  CYS   B C     1 
ATOM   2660 O  O     . CYS   B 1 70  ? -10.336 -3.614  84.191  1.00 37.02  ? 980  CYS   B O     1 
ATOM   2661 C  CB    . CYS   B 1 70  ? -10.496 -2.726  86.807  1.00 27.25  ? 980  CYS   B CB    1 
ATOM   2662 S  SG    . CYS   B 1 70  ? -11.085 -1.876  88.264  1.00 28.27  ? 980  CYS   B SG    1 
ATOM   2663 N  N     . SER   B 1 71  ? -11.405 -5.532  84.615  1.00 29.80  ? 981  SER   B N     1 
ATOM   2664 C  CA    . SER   B 1 71  ? -11.179 -6.056  83.277  1.00 33.37  ? 981  SER   B CA    1 
ATOM   2665 C  C     . SER   B 1 71  ? -12.298 -5.696  82.293  1.00 36.35  ? 981  SER   B C     1 
ATOM   2666 O  O     . SER   B 1 71  ? -12.295 -6.193  81.161  1.00 35.64  ? 981  SER   B O     1 
ATOM   2667 C  CB    . SER   B 1 71  ? -11.015 -7.580  83.334  1.00 37.48  ? 981  SER   B CB    1 
ATOM   2668 O  OG    . SER   B 1 71  ? -12.199 -8.196  83.821  1.00 33.74  ? 981  SER   B OG    1 
ATOM   2669 N  N     . SER   B 1 72  ? -13.259 -4.863  82.673  1.00 31.36  ? 982  SER   B N     1 
ATOM   2670 C  CA    . SER   B 1 72  ? -14.339 -4.530  81.754  1.00 38.23  ? 982  SER   B CA    1 
ATOM   2671 C  C     . SER   B 1 72  ? -14.039 -3.211  81.059  1.00 39.15  ? 982  SER   B C     1 
ATOM   2672 O  O     . SER   B 1 72  ? -13.298 -2.373  81.573  1.00 38.21  ? 982  SER   B O     1 
ATOM   2673 C  CB    . SER   B 1 72  ? -15.680 -4.444  82.485  1.00 35.89  ? 982  SER   B CB    1 
ATOM   2674 O  OG    . SER   B 1 72  ? -15.658 -3.414  83.454  1.00 35.21  ? 982  SER   B OG    1 
ATOM   2675 N  N     . SER   B 1 73  ? -14.634 -3.029  79.878  1.00 35.93  ? 983  SER   B N     1 
ATOM   2676 C  CA    . SER   B 1 73  ? -14.413 -1.793  79.140  1.00 38.00  ? 983  SER   B CA    1 
ATOM   2677 C  C     . SER   B 1 73  ? -15.188 -0.625  79.734  1.00 38.49  ? 983  SER   B C     1 
ATOM   2678 O  O     . SER   B 1 73  ? -15.135 0.491   79.202  1.00 37.38  ? 983  SER   B O     1 
ATOM   2679 C  CB    . SER   B 1 73  ? -14.783 -1.988  77.668  1.00 36.33  ? 983  SER   B CB    1 
ATOM   2680 O  OG    . SER   B 1 73  ? -16.160 -2.250  77.525  1.00 43.94  ? 983  SER   B OG    1 
ATOM   2681 N  N     . ASN   B 1 74  ? -15.911 -0.865  80.816  1.00 39.69  ? 984  ASN   B N     1 
ATOM   2682 C  CA    . ASN   B 1 74  ? -16.679 0.161   81.492  1.00 35.61  ? 984  ASN   B CA    1 
ATOM   2683 C  C     . ASN   B 1 74  ? -15.869 0.847   82.579  1.00 34.62  ? 984  ASN   B C     1 
ATOM   2684 O  O     . ASN   B 1 74  ? -16.264 1.915   83.055  1.00 32.31  ? 984  ASN   B O     1 
ATOM   2685 C  CB    . ASN   B 1 74  ? -17.932 -0.477  82.078  1.00 36.35  ? 984  ASN   B CB    1 
ATOM   2686 C  CG    . ASN   B 1 74  ? -18.936 0.533   82.566  1.00 35.71  ? 984  ASN   B CG    1 
ATOM   2687 O  OD1   . ASN   B 1 74  ? -19.263 0.569   83.753  1.00 34.84  ? 984  ASN   B OD1   1 
ATOM   2688 N  ND2   . ASN   B 1 74  ? -19.457 1.342   81.649  1.00 37.44  ? 984  ASN   B ND2   1 
ATOM   2689 N  N     . CYS   B 1 75  ? -14.736 0.264   82.963  1.00 31.09  ? 985  CYS   B N     1 
ATOM   2690 C  CA    . CYS   B 1 75  ? -13.842 0.904   83.918  1.00 31.79  ? 985  CYS   B CA    1 
ATOM   2691 C  C     . CYS   B 1 75  ? -13.460 2.290   83.421  1.00 30.57  ? 985  CYS   B C     1 
ATOM   2692 O  O     . CYS   B 1 75  ? -13.044 2.445   82.272  1.00 31.58  ? 985  CYS   B O     1 
ATOM   2693 C  CB    . CYS   B 1 75  ? -12.593 0.041   84.119  1.00 31.01  ? 985  CYS   B CB    1 
ATOM   2694 S  SG    . CYS   B 1 75  ? -11.463 0.746   85.253  1.00 28.24  ? 985  CYS   B SG    1 
ATOM   2695 N  N     . LEU   B 1 76  ? -13.663 3.311   84.269  1.00 30.08  ? 986  LEU   B N     1 
ATOM   2696 C  CA    . LEU   B 1 76  ? -13.377 4.676   83.839  1.00 30.81  ? 986  LEU   B CA    1 
ATOM   2697 C  C     . LEU   B 1 76  ? -11.873 4.890   83.671  1.00 30.58  ? 986  LEU   B C     1 
ATOM   2698 O  O     . LEU   B 1 76  ? -11.424 5.545   82.726  1.00 31.50  ? 986  LEU   B O     1 
ATOM   2699 C  CB    . LEU   B 1 76  ? -13.942 5.678   84.837  1.00 32.79  ? 986  LEU   B CB    1 
ATOM   2700 C  CG    . LEU   B 1 76  ? -13.461 7.116   84.573  1.00 34.51  ? 986  LEU   B CG    1 
ATOM   2701 C  CD1   . LEU   B 1 76  ? -14.066 7.653   83.288  1.00 33.43  ? 986  LEU   B CD1   1 
ATOM   2702 C  CD2   . LEU   B 1 76  ? -13.721 8.056   85.740  1.00 36.13  ? 986  LEU   B CD2   1 
ATOM   2703 N  N     . CYS   B 1 77  ? -11.088 4.336   84.584  1.00 30.63  ? 987  CYS   B N     1 
ATOM   2704 C  CA    . CYS   B 1 77  ? -9.636  4.393   84.467  1.00 29.21  ? 987  CYS   B CA    1 
ATOM   2705 C  C     . CYS   B 1 77  ? -9.177  3.926   83.098  1.00 33.31  ? 987  CYS   B C     1 
ATOM   2706 O  O     . CYS   B 1 77  ? -8.378  4.599   82.440  1.00 32.93  ? 987  CYS   B O     1 
ATOM   2707 C  CB    . CYS   B 1 77  ? -9.042  3.548   85.571  1.00 28.08  ? 987  CYS   B CB    1 
ATOM   2708 S  SG    . CYS   B 1 77  ? -9.615  4.202   87.112  1.00 27.62  ? 987  CYS   B SG    1 
ATOM   2709 N  N     . GLY   B 1 78  ? -9.743  2.817   82.620  1.00 32.77  ? 988  GLY   B N     1 
ATOM   2710 C  CA    . GLY   B 1 78  ? -9.361  2.304   81.317  1.00 31.31  ? 988  GLY   B CA    1 
ATOM   2711 C  C     . GLY   B 1 78  ? -9.699  3.265   80.198  1.00 35.34  ? 988  GLY   B C     1 
ATOM   2712 O  O     . GLY   B 1 78  ? -8.863  3.549   79.334  1.00 35.03  ? 988  GLY   B O     1 
ATOM   2713 N  N     . GLN   B 1 79  ? -10.930 3.788   80.205  1.00 34.54  ? 989  GLN   B N     1 
ATOM   2714 C  CA    . GLN   B 1 79  ? -11.385 4.641   79.111  1.00 37.86  ? 989  GLN   B CA    1 
ATOM   2715 C  C     . GLN   B 1 79  ? -10.554 5.910   79.022  1.00 35.04  ? 989  GLN   B C     1 
ATOM   2716 O  O     . GLN   B 1 79  ? -10.306 6.421   77.924  1.00 36.52  ? 989  GLN   B O     1 
ATOM   2717 C  CB    . GLN   B 1 79  ? -12.880 4.985   79.277  1.00 35.07  ? 989  GLN   B CB    1 
ATOM   2718 C  CG    . GLN   B 1 79  ? -13.775 3.785   79.544  1.00 34.59  ? 989  GLN   B CG    1 
ATOM   2719 C  CD    . GLN   B 1 79  ? -15.234 4.183   79.751  1.00 40.80  ? 989  GLN   B CD    1 
ATOM   2720 O  OE1   . GLN   B 1 79  ? -15.555 5.372   79.826  1.00 39.60  ? 989  GLN   B OE1   1 
ATOM   2721 N  NE2   . GLN   B 1 79  ? -16.123 3.186   79.835  1.00 37.54  ? 989  GLN   B NE2   1 
ATOM   2722 N  N     . LEU   B 1 80  ? -10.152 6.455   80.172  1.00 33.98  ? 990  LEU   B N     1 
ATOM   2723 C  CA    . LEU   B 1 80  ? -9.148  7.512   80.193  1.00 34.31  ? 990  LEU   B CA    1 
ATOM   2724 C  C     . LEU   B 1 80  ? -7.949  7.127   79.334  1.00 35.15  ? 990  LEU   B C     1 
ATOM   2725 O  O     . LEU   B 1 80  ? -7.496  7.917   78.503  1.00 35.96  ? 990  LEU   B O     1 
ATOM   2726 C  CB    . LEU   B 1 80  ? -8.708  7.796   81.637  1.00 36.98  ? 990  LEU   B CB    1 
ATOM   2727 C  CG    . LEU   B 1 80  ? -9.687  8.576   82.530  1.00 35.79  ? 990  LEU   B CG    1 
ATOM   2728 C  CD1   . LEU   B 1 80  ? -9.289  8.570   84.025  1.00 31.73  ? 990  LEU   B CD1   1 
ATOM   2729 C  CD2   . LEU   B 1 80  ? -9.844  9.993   82.014  1.00 34.59  ? 990  LEU   B CD2   1 
ATOM   2730 N  N     . SER   B 1 81  ? -7.467  5.891   79.483  1.00 35.50  ? 991  SER   B N     1 
ATOM   2731 C  CA    . SER   B 1 81  ? -6.314  5.354   78.765  1.00 38.55  ? 991  SER   B CA    1 
ATOM   2732 C  C     . SER   B 1 81  ? -6.641  4.949   77.347  1.00 43.03  ? 991  SER   B C     1 
ATOM   2733 O  O     . SER   B 1 81  ? -5.871  4.167   76.779  1.00 49.20  ? 991  SER   B O     1 
ATOM   2734 C  CB    . SER   B 1 81  ? -5.754  4.130   79.495  1.00 33.05  ? 991  SER   B CB    1 
ATOM   2735 O  OG    . SER   B 1 81  ? -5.629  4.344   80.898  1.00 34.42  ? 991  SER   B OG    1 
ATOM   2736 N  N     . ILE   B 1 82  ? -7.755  5.443   76.801  1.00 37.56  ? 992  ILE   B N     1 
ATOM   2737 C  CA    . ILE   B 1 82  ? -8.430  4.925   75.609  1.00 46.42  ? 992  ILE   B CA    1 
ATOM   2738 C  C     . ILE   B 1 82  ? -9.105  3.597   75.948  1.00 45.65  ? 992  ILE   B C     1 
ATOM   2739 O  O     . ILE   B 1 82  ? -10.303 3.406   75.686  1.00 40.32  ? 992  ILE   B O     1 
ATOM   2740 C  CB    . ILE   B 1 82  ? -7.480  4.771   74.405  1.00 49.29  ? 992  ILE   B CB    1 
ATOM   2741 C  CG1   . ILE   B 1 82  ? -6.671  6.052   74.165  1.00 55.52  ? 992  ILE   B CG1   1 
ATOM   2742 C  CG2   . ILE   B 1 82  ? -8.284  4.433   73.157  1.00 49.92  ? 992  ILE   B CG2   1 
ATOM   2743 C  CD1   . ILE   B 1 82  ? -5.713  5.976   72.948  1.00 55.07  ? 992  ILE   B CD1   1 
ATOM   2744 N  N     . ARG   B 1 83  ? -8.330  2.685   76.533  1.00 43.99  ? 993  ARG   B N     1 
ATOM   2745 C  CA    . ARG   B 1 83  ? -8.727  1.380   77.055  1.00 40.39  ? 993  ARG   B CA    1 
ATOM   2746 C  C     . ARG   B 1 83  ? -7.568  0.899   77.915  1.00 39.23  ? 993  ARG   B C     1 
ATOM   2747 O  O     . ARG   B 1 83  ? -6.455  1.418   77.809  1.00 40.81  ? 993  ARG   B O     1 
ATOM   2748 C  CB    . ARG   B 1 83  ? -9.013  0.373   75.936  1.00 43.52  ? 993  ARG   B CB    1 
ATOM   2749 C  CG    . ARG   B 1 83  ? -7.747  -0.039  75.192  1.00 45.26  ? 993  ARG   B CG    1 
ATOM   2750 C  CD    . ARG   B 1 83  ? -8.025  -0.783  73.894  1.00 51.96  ? 993  ARG   B CD    1 
ATOM   2751 N  NE    . ARG   B 1 83  ? -8.188  -2.219  74.092  1.00 60.71  ? 993  ARG   B NE    1 
ATOM   2752 C  CZ    . ARG   B 1 83  ? -7.956  -3.134  73.157  1.00 64.59  ? 993  ARG   B CZ    1 
ATOM   2753 N  NH1   . ARG   B 1 83  ? -7.521  -2.800  71.951  1.00 58.39  ? 993  ARG   B NH1   1 
ATOM   2754 N  NH2   . ARG   B 1 83  ? -8.165  -4.417  73.440  1.00 68.88  ? 993  ARG   B NH2   1 
ATOM   2755 N  N     . CYS   B 1 84  ? -7.828  -0.089  78.764  1.00 36.47  ? 994  CYS   B N     1 
ATOM   2756 C  CA    . CYS   B 1 84  ? -6.741  -0.715  79.506  1.00 38.37  ? 994  CYS   B CA    1 
ATOM   2757 C  C     . CYS   B 1 84  ? -5.915  -1.582  78.554  1.00 41.88  ? 994  CYS   B C     1 
ATOM   2758 O  O     . CYS   B 1 84  ? -6.407  -2.581  78.014  1.00 42.34  ? 994  CYS   B O     1 
ATOM   2759 C  CB    . CYS   B 1 84  ? -7.271  -1.534  80.676  1.00 32.45  ? 994  CYS   B CB    1 
ATOM   2760 S  SG    . CYS   B 1 84  ? -5.955  -2.352  81.629  1.00 32.79  ? 994  CYS   B SG    1 
ATOM   2761 N  N     . TRP   B 1 85  ? -4.652  -1.205  78.349  1.00 39.49  ? 995  TRP   B N     1 
ATOM   2762 C  CA    . TRP   B 1 85  ? -3.785  -1.877  77.391  1.00 41.15  ? 995  TRP   B CA    1 
ATOM   2763 C  C     . TRP   B 1 85  ? -3.089  -3.077  77.975  1.00 40.39  ? 995  TRP   B C     1 
ATOM   2764 O  O     . TRP   B 1 85  ? -2.104  -3.561  77.397  1.00 41.72  ? 995  TRP   B O     1 
ATOM   2765 C  CB    . TRP   B 1 85  ? -2.760  -0.890  76.842  1.00 41.16  ? 995  TRP   B CB    1 
ATOM   2766 C  CG    . TRP   B 1 85  ? -3.413  0.226   76.130  1.00 40.77  ? 995  TRP   B CG    1 
ATOM   2767 C  CD1   . TRP   B 1 85  ? -3.652  1.476   76.613  1.00 39.37  ? 995  TRP   B CD1   1 
ATOM   2768 C  CD2   . TRP   B 1 85  ? -3.958  0.190   74.809  1.00 43.98  ? 995  TRP   B CD2   1 
ATOM   2769 N  NE1   . TRP   B 1 85  ? -4.285  2.234   75.661  1.00 42.23  ? 995  TRP   B NE1   1 
ATOM   2770 C  CE2   . TRP   B 1 85  ? -4.493  1.464   74.546  1.00 45.98  ? 995  TRP   B CE2   1 
ATOM   2771 C  CE3   . TRP   B 1 85  ? -4.040  -0.796  73.819  1.00 45.18  ? 995  TRP   B CE3   1 
ATOM   2772 C  CZ2   . TRP   B 1 85  ? -5.114  1.779   73.332  1.00 51.26  ? 995  TRP   B CZ2   1 
ATOM   2773 C  CZ3   . TRP   B 1 85  ? -4.641  -0.480  72.614  1.00 50.79  ? 995  TRP   B CZ3   1 
ATOM   2774 C  CH2   . TRP   B 1 85  ? -5.175  0.796   72.381  1.00 52.00  ? 995  TRP   B CH2   1 
ATOM   2775 N  N     . TYR   B 1 86  ? -3.577  -3.554  79.110  1.00 37.53  ? 996  TYR   B N     1 
ATOM   2776 C  CA    . TYR   B 1 86  ? -2.994  -4.682  79.813  1.00 39.72  ? 996  TYR   B CA    1 
ATOM   2777 C  C     . TYR   B 1 86  ? -3.853  -5.915  79.569  1.00 39.31  ? 996  TYR   B C     1 
ATOM   2778 O  O     . TYR   B 1 86  ? -5.082  -5.857  79.667  1.00 42.65  ? 996  TYR   B O     1 
ATOM   2779 C  CB    . TYR   B 1 86  ? -2.917  -4.410  81.318  1.00 36.18  ? 996  TYR   B CB    1 
ATOM   2780 C  CG    . TYR   B 1 86  ? -2.113  -3.201  81.752  1.00 29.37  ? 996  TYR   B CG    1 
ATOM   2781 C  CD1   . TYR   B 1 86  ? -0.893  -2.895  81.147  1.00 35.14  ? 996  TYR   B CD1   1 
ATOM   2782 C  CD2   . TYR   B 1 86  ? -2.539  -2.411  82.811  1.00 28.44  ? 996  TYR   B CD2   1 
ATOM   2783 C  CE1   . TYR   B 1 86  ? -0.131  -1.805  81.574  1.00 34.89  ? 996  TYR   B CE1   1 
ATOM   2784 C  CE2   . TYR   B 1 86  ? -1.797  -1.320  83.246  1.00 27.93  ? 996  TYR   B CE2   1 
ATOM   2785 C  CZ    . TYR   B 1 86  ? -0.590  -1.015  82.623  1.00 32.71  ? 996  TYR   B CZ    1 
ATOM   2786 O  OH    . TYR   B 1 86  ? 0.166   0.067   83.041  1.00 31.29  ? 996  TYR   B OH    1 
ATOM   2787 N  N     . ASP   B 1 87  ? -3.207  -7.028  79.257  1.00 39.73  ? 997  ASP   B N     1 
ATOM   2788 C  CA    . ASP   B 1 87  ? -3.930  -8.277  79.128  1.00 37.39  ? 997  ASP   B CA    1 
ATOM   2789 C  C     . ASP   B 1 87  ? -4.085  -8.920  80.500  1.00 38.51  ? 997  ASP   B C     1 
ATOM   2790 O  O     . ASP   B 1 87  ? -3.803  -8.314  81.539  1.00 33.73  ? 997  ASP   B O     1 
ATOM   2791 C  CB    . ASP   B 1 87  ? -3.242  -9.212  78.133  1.00 39.24  ? 997  ASP   B CB    1 
ATOM   2792 C  CG    . ASP   B 1 87  ? -1.822  -9.634  78.566  1.00 37.73  ? 997  ASP   B CG    1 
ATOM   2793 O  OD1   . ASP   B 1 87  ? -1.447  -9.521  79.751  1.00 37.21  ? 997  ASP   B OD1   1 
ATOM   2794 O  OD2   . ASP   B 1 87  ? -1.075  -10.087 77.684  1.00 38.79  ? 997  ASP   B OD2   1 
ATOM   2795 N  N     . LYS   B 1 88  ? -4.528  -10.180 80.484  1.00 43.33  ? 998  LYS   B N     1 
ATOM   2796 C  CA    . LYS   B 1 88  ? -4.884  -10.907 81.699  1.00 43.95  ? 998  LYS   B CA    1 
ATOM   2797 C  C     . LYS   B 1 88  ? -3.692  -11.030 82.641  1.00 41.15  ? 998  LYS   B C     1 
ATOM   2798 O  O     . LYS   B 1 88  ? -3.846  -10.962 83.867  1.00 39.14  ? 998  LYS   B O     1 
ATOM   2799 C  CB    . LYS   B 1 88  ? -5.423  -12.284 81.298  1.00 46.37  ? 998  LYS   B CB    1 
ATOM   2800 C  CG    . LYS   B 1 88  ? -5.963  -13.157 82.406  1.00 52.35  ? 998  LYS   B CG    1 
ATOM   2801 C  CD    . LYS   B 1 88  ? -6.497  -14.485 81.826  1.00 53.70  ? 998  LYS   B CD    1 
ATOM   2802 C  CE    . LYS   B 1 88  ? -5.384  -15.314 81.152  1.00 58.69  ? 998  LYS   B CE    1 
ATOM   2803 N  NZ    . LYS   B 1 88  ? -4.391  -15.885 82.119  1.00 58.79  ? 998  LYS   B NZ    1 
ATOM   2804 N  N     . ASP   B 1 89  ? -2.493  -11.180 82.078  1.00 40.88  ? 999  ASP   B N     1 
ATOM   2805 C  CA    . ASP   B 1 89  ? -1.270  -11.408 82.832  1.00 38.34  ? 999  ASP   B CA    1 
ATOM   2806 C  C     . ASP   B 1 89  ? -0.482  -10.133 83.080  1.00 39.88  ? 999  ASP   B C     1 
ATOM   2807 O  O     . ASP   B 1 89  ? 0.698   -10.202 83.470  1.00 36.37  ? 999  ASP   B O     1 
ATOM   2808 C  CB    . ASP   B 1 89  ? -0.408  -12.422 82.092  1.00 39.98  ? 999  ASP   B CB    1 
ATOM   2809 C  CG    . ASP   B 1 89  ? -1.185  -13.644 81.736  1.00 36.82  ? 999  ASP   B CG    1 
ATOM   2810 O  OD1   . ASP   B 1 89  ? -1.856  -14.161 82.654  1.00 35.75  ? 999  ASP   B OD1   1 
ATOM   2811 O  OD2   . ASP   B 1 89  ? -1.155  -14.049 80.551  1.00 37.29  ? 999  ASP   B OD2   1 
ATOM   2812 N  N     . GLY   B 1 90  ? -1.090  -8.975  82.847  1.00 34.95  ? 1000 GLY   B N     1 
ATOM   2813 C  CA    . GLY   B 1 90  ? -0.393  -7.745  83.116  1.00 36.43  ? 1000 GLY   B CA    1 
ATOM   2814 C  C     . GLY   B 1 90  ? 0.486   -7.249  82.000  1.00 31.76  ? 1000 GLY   B C     1 
ATOM   2815 O  O     . GLY   B 1 90  ? 1.214   -6.279  82.206  1.00 33.52  ? 1000 GLY   B O     1 
ATOM   2816 N  N     . ARG   B 1 91  ? 0.408   -7.838  80.817  1.00 32.53  ? 1001 ARG   B N     1 
ATOM   2817 C  CA    . ARG   B 1 91  ? 1.301   -7.467  79.732  1.00 35.37  ? 1001 ARG   B CA    1 
ATOM   2818 C  C     . ARG   B 1 91  ? 0.619   -6.539  78.739  1.00 35.18  ? 1001 ARG   B C     1 
ATOM   2819 O  O     . ARG   B 1 91  ? -0.594  -6.606  78.508  1.00 38.44  ? 1001 ARG   B O     1 
ATOM   2820 C  CB    . ARG   B 1 91  ? 1.849   -8.708  79.015  1.00 34.06  ? 1001 ARG   B CB    1 
ATOM   2821 C  CG    . ARG   B 1 91  ? 2.894   -9.456  79.840  1.00 35.23  ? 1001 ARG   B CG    1 
ATOM   2822 C  CD    . ARG   B 1 91  ? 3.302   -10.763 79.188  1.00 40.05  ? 1001 ARG   B CD    1 
ATOM   2823 N  NE    . ARG   B 1 91  ? 4.253   -11.513 80.007  1.00 45.83  ? 1001 ARG   B NE    1 
ATOM   2824 C  CZ    . ARG   B 1 91  ? 3.957   -12.631 80.664  1.00 46.22  ? 1001 ARG   B CZ    1 
ATOM   2825 N  NH1   . ARG   B 1 91  ? 2.729   -13.125 80.667  1.00 43.22  ? 1001 ARG   B NH1   1 
ATOM   2826 N  NH2   . ARG   B 1 91  ? 4.921   -13.279 81.319  1.00 41.11  ? 1001 ARG   B NH2   1 
ATOM   2827 N  N     . LEU   B 1 92  ? 1.437   -5.682  78.145  1.00 34.65  ? 1002 LEU   B N     1 
ATOM   2828 C  CA    . LEU   B 1 92  ? 0.991   -4.573  77.316  1.00 38.27  ? 1002 LEU   B CA    1 
ATOM   2829 C  C     . LEU   B 1 92  ? 0.577   -5.081  75.941  1.00 44.35  ? 1002 LEU   B C     1 
ATOM   2830 O  O     . LEU   B 1 92  ? 1.418   -5.604  75.198  1.00 47.24  ? 1002 LEU   B O     1 
ATOM   2831 C  CB    . LEU   B 1 92  ? 2.126   -3.565  77.206  1.00 42.58  ? 1002 LEU   B CB    1 
ATOM   2832 C  CG    . LEU   B 1 92  ? 1.909   -2.361  76.317  1.00 43.47  ? 1002 LEU   B CG    1 
ATOM   2833 C  CD1   . LEU   B 1 92  ? 0.908   -1.459  76.986  1.00 40.83  ? 1002 LEU   B CD1   1 
ATOM   2834 C  CD2   . LEU   B 1 92  ? 3.251   -1.684  76.121  1.00 39.62  ? 1002 LEU   B CD2   1 
ATOM   2835 N  N     . LEU   B 1 93  ? -0.712  -4.906  75.603  1.00 46.25  ? 1003 LEU   B N     1 
ATOM   2836 C  CA    . LEU   B 1 93  ? -1.325  -5.533  74.432  1.00 48.36  ? 1003 LEU   B CA    1 
ATOM   2837 C  C     . LEU   B 1 93  ? -0.509  -5.304  73.167  1.00 49.47  ? 1003 LEU   B C     1 
ATOM   2838 O  O     . LEU   B 1 93  ? 0.103   -4.249  72.980  1.00 48.45  ? 1003 LEU   B O     1 
ATOM   2839 C  CB    . LEU   B 1 93  ? -2.737  -4.986  74.205  1.00 47.65  ? 1003 LEU   B CB    1 
ATOM   2840 C  CG    . LEU   B 1 93  ? -3.788  -5.236  75.282  1.00 48.30  ? 1003 LEU   B CG    1 
ATOM   2841 C  CD1   . LEU   B 1 93  ? -5.122  -4.598  74.905  1.00 51.35  ? 1003 LEU   B CD1   1 
ATOM   2842 C  CD2   . LEU   B 1 93  ? -3.951  -6.728  75.503  1.00 47.26  ? 1003 LEU   B CD2   1 
ATOM   2843 N  N     . GLN   B 1 94  ? -0.550  -6.296  72.267  1.00 48.65  ? 1004 GLN   B N     1 
ATOM   2844 C  CA    . GLN   B 1 94  ? 0.256   -6.228  71.050  1.00 61.43  ? 1004 GLN   B CA    1 
ATOM   2845 C  C     . GLN   B 1 94  ? -0.178  -5.085  70.145  1.00 64.63  ? 1004 GLN   B C     1 
ATOM   2846 O  O     . GLN   B 1 94  ? 0.644   -4.528  69.411  1.00 66.78  ? 1004 GLN   B O     1 
ATOM   2847 C  CB    . GLN   B 1 94  ? 0.185   -7.553  70.286  1.00 64.91  ? 1004 GLN   B CB    1 
ATOM   2848 C  CG    . GLN   B 1 94  ? -1.156  -7.828  69.611  1.00 65.99  ? 1004 GLN   B CG    1 
ATOM   2849 C  CD    . GLN   B 1 94  ? -1.011  -8.700  68.378  1.00 66.02  ? 1004 GLN   B CD    1 
ATOM   2850 O  OE1   . GLN   B 1 94  ? 0.105   -8.952  67.916  1.00 72.40  ? 1004 GLN   B OE1   1 
ATOM   2851 N  NE2   . GLN   B 1 94  ? -2.134  -9.168  67.841  1.00 67.90  ? 1004 GLN   B NE2   1 
ATOM   2852 N  N     . GLU   B 1 95  ? -1.455  -4.719  70.187  1.00 74.54  ? 1005 GLU   B N     1 
ATOM   2853 C  CA    . GLU   B 1 95  ? -1.988  -3.658  69.347  1.00 76.70  ? 1005 GLU   B CA    1 
ATOM   2854 C  C     . GLU   B 1 95  ? -1.635  -2.269  69.856  1.00 77.33  ? 1005 GLU   B C     1 
ATOM   2855 O  O     . GLU   B 1 95  ? -1.903  -1.287  69.152  1.00 79.07  ? 1005 GLU   B O     1 
ATOM   2856 C  CB    . GLU   B 1 95  ? -3.503  -3.818  69.246  1.00 75.20  ? 1005 GLU   B CB    1 
ATOM   2857 C  CG    . GLU   B 1 95  ? -3.895  -5.238  68.890  1.00 76.62  ? 1005 GLU   B CG    1 
ATOM   2858 C  CD    . GLU   B 1 95  ? -5.159  -5.685  69.579  1.00 89.42  ? 1005 GLU   B CD    1 
ATOM   2859 O  OE1   . GLU   B 1 95  ? -5.487  -5.107  70.639  1.00 85.74  ? 1005 GLU   B OE1   1 
ATOM   2860 O  OE2   . GLU   B 1 95  ? -5.826  -6.608  69.057  1.00 91.58  ? 1005 GLU   B OE2   1 
ATOM   2861 N  N     . PHE   B 1 96  ? -1.057  -2.177  71.053  1.00 63.49  ? 1006 PHE   B N     1 
ATOM   2862 C  CA    . PHE   B 1 96  ? -0.589  -0.922  71.621  1.00 59.35  ? 1006 PHE   B CA    1 
ATOM   2863 C  C     . PHE   B 1 96  ? 0.222   -0.141  70.599  1.00 67.55  ? 1006 PHE   B C     1 
ATOM   2864 O  O     . PHE   B 1 96  ? 1.212   -0.647  70.063  1.00 68.28  ? 1006 PHE   B O     1 
ATOM   2865 C  CB    . PHE   B 1 96  ? 0.258   -1.232  72.858  1.00 56.16  ? 1006 PHE   B CB    1 
ATOM   2866 C  CG    . PHE   B 1 96  ? 0.514   -0.056  73.744  1.00 52.47  ? 1006 PHE   B CG    1 
ATOM   2867 C  CD1   . PHE   B 1 96  ? -0.498  0.477   74.520  1.00 48.32  ? 1006 PHE   B CD1   1 
ATOM   2868 C  CD2   . PHE   B 1 96  ? 1.776   0.501   73.822  1.00 50.95  ? 1006 PHE   B CD2   1 
ATOM   2869 C  CE1   . PHE   B 1 96  ? -0.256  1.553   75.345  1.00 50.06  ? 1006 PHE   B CE1   1 
ATOM   2870 C  CE2   . PHE   B 1 96  ? 2.025   1.566   74.643  1.00 48.55  ? 1006 PHE   B CE2   1 
ATOM   2871 C  CZ    . PHE   B 1 96  ? 1.022   2.100   75.404  1.00 47.09  ? 1006 PHE   B CZ    1 
ATOM   2872 N  N     . ASN   B 1 97  ? -0.222  1.084   70.306  1.00 68.42  ? 1007 ASN   B N     1 
ATOM   2873 C  CA    . ASN   B 1 97  ? 0.492   1.963   69.389  1.00 73.27  ? 1007 ASN   B CA    1 
ATOM   2874 C  C     . ASN   B 1 97  ? 1.885   2.226   69.939  1.00 80.58  ? 1007 ASN   B C     1 
ATOM   2875 O  O     . ASN   B 1 97  ? 2.133   3.281   70.532  1.00 82.27  ? 1007 ASN   B O     1 
ATOM   2876 C  CB    . ASN   B 1 97  ? -0.270  3.275   69.190  1.00 79.70  ? 1007 ASN   B CB    1 
ATOM   2877 C  CG    . ASN   B 1 97  ? 0.263   4.097   68.025  1.00 86.15  ? 1007 ASN   B CG    1 
ATOM   2878 O  OD1   . ASN   B 1 97  ? 1.410   3.935   67.599  1.00 88.96  ? 1007 ASN   B OD1   1 
ATOM   2879 N  ND2   . ASN   B 1 97  ? -0.571  4.993   67.507  1.00 85.74  ? 1007 ASN   B ND2   1 
ATOM   2880 N  N     . LYS   B 1 98  ? 2.801   1.274   69.740  1.00 82.98  ? 1008 LYS   B N     1 
ATOM   2881 C  CA    . LYS   B 1 98  ? 4.089   1.272   70.420  1.00 84.56  ? 1008 LYS   B CA    1 
ATOM   2882 C  C     . LYS   B 1 98  ? 5.097   2.254   69.819  1.00 92.35  ? 1008 LYS   B C     1 
ATOM   2883 O  O     . LYS   B 1 98  ? 6.303   2.096   70.044  1.00 88.47  ? 1008 LYS   B O     1 
ATOM   2884 C  CB    . LYS   B 1 98  ? 4.669   -0.145  70.443  1.00 82.72  ? 1008 LYS   B CB    1 
ATOM   2885 C  CG    . LYS   B 1 98  ? 4.831   -0.797  69.087  1.00 89.16  ? 1008 LYS   B CG    1 
ATOM   2886 C  CD    . LYS   B 1 98  ? 5.671   -2.062  69.206  1.00 85.54  ? 1008 LYS   B CD    1 
ATOM   2887 C  CE    . LYS   B 1 98  ? 6.627   -2.190  68.036  1.00 85.38  ? 1008 LYS   B CE    1 
ATOM   2888 N  NZ    . LYS   B 1 98  ? 7.502   -0.990  67.926  1.00 89.70  ? 1008 LYS   B NZ    1 
ATOM   2889 N  N     . ILE   B 1 99  ? 4.633   3.258   69.074  1.00 97.39  ? 1009 ILE   B N     1 
ATOM   2890 C  CA    . ILE   B 1 99  ? 5.486   4.347   68.608  1.00 100.49 ? 1009 ILE   B CA    1 
ATOM   2891 C  C     . ILE   B 1 99  ? 4.782   5.663   68.920  1.00 98.60  ? 1009 ILE   B C     1 
ATOM   2892 O  O     . ILE   B 1 99  ? 5.429   6.695   69.127  1.00 102.08 ? 1009 ILE   B O     1 
ATOM   2893 C  CB    . ILE   B 1 99  ? 5.817   4.210   67.107  1.00 108.11 ? 1009 ILE   B CB    1 
ATOM   2894 C  CG1   . ILE   B 1 99  ? 6.639   2.941   66.857  1.00 107.32 ? 1009 ILE   B CG1   1 
ATOM   2895 C  CG2   . ILE   B 1 99  ? 6.584   5.427   66.593  1.00 109.47 ? 1009 ILE   B CG2   1 
ATOM   2896 C  CD1   . ILE   B 1 99  ? 7.109   2.779   65.422  1.00 107.56 ? 1009 ILE   B CD1   1 
ATOM   2897 N  N     . GLU   B 1 100 ? 3.451   5.630   68.986  1.00 94.22  ? 1010 GLU   B N     1 
ATOM   2898 C  CA    . GLU   B 1 100 ? 2.644   6.770   69.418  1.00 93.38  ? 1010 GLU   B CA    1 
ATOM   2899 C  C     . GLU   B 1 100 ? 1.789   6.348   70.613  1.00 90.29  ? 1010 GLU   B C     1 
ATOM   2900 O  O     . GLU   B 1 100 ? 0.559   6.252   70.510  1.00 88.81  ? 1010 GLU   B O     1 
ATOM   2901 C  CB    . GLU   B 1 100 ? 1.778   7.290   68.271  1.00 96.07  ? 1010 GLU   B CB    1 
ATOM   2902 C  CG    . GLU   B 1 100 ? 1.021   8.576   68.573  1.00 101.83 ? 1010 GLU   B CG    1 
ATOM   2903 C  CD    . GLU   B 1 100 ? 1.940   9.756   68.811  1.00 106.34 ? 1010 GLU   B CD    1 
ATOM   2904 O  OE1   . GLU   B 1 100 ? 3.138   9.661   68.468  1.00 102.15 ? 1010 GLU   B OE1   1 
ATOM   2905 O  OE2   . GLU   B 1 100 ? 1.462   10.780  69.340  1.00 110.01 ? 1010 GLU   B OE2   1 
ATOM   2906 N  N     . PRO   B 1 101 ? 2.409   6.091   71.764  1.00 81.30  ? 1011 PRO   B N     1 
ATOM   2907 C  CA    . PRO   B 1 101 ? 1.672   5.499   72.883  1.00 70.02  ? 1011 PRO   B CA    1 
ATOM   2908 C  C     . PRO   B 1 101 ? 0.976   6.562   73.712  1.00 70.42  ? 1011 PRO   B C     1 
ATOM   2909 O  O     . PRO   B 1 101 ? 1.600   7.557   74.108  1.00 70.46  ? 1011 PRO   B O     1 
ATOM   2910 C  CB    . PRO   B 1 101 ? 2.768   4.789   73.687  1.00 67.45  ? 1011 PRO   B CB    1 
ATOM   2911 C  CG    . PRO   B 1 101 ? 4.013   5.590   73.414  1.00 76.27  ? 1011 PRO   B CG    1 
ATOM   2912 C  CD    . PRO   B 1 101 ? 3.837   6.282   72.079  1.00 82.25  ? 1011 PRO   B CD    1 
ATOM   2913 N  N     . PRO   B 1 102 ? -0.310  6.382   74.006  1.00 65.12  ? 1012 PRO   B N     1 
ATOM   2914 C  CA    . PRO   B 1 102 ? -1.047  7.373   74.792  1.00 58.50  ? 1012 PRO   B CA    1 
ATOM   2915 C  C     . PRO   B 1 102 ? -0.823  7.180   76.285  1.00 54.73  ? 1012 PRO   B C     1 
ATOM   2916 O  O     . PRO   B 1 102 ? -0.394  6.121   76.743  1.00 58.21  ? 1012 PRO   B O     1 
ATOM   2917 C  CB    . PRO   B 1 102 ? -2.502  7.081   74.421  1.00 60.23  ? 1012 PRO   B CB    1 
ATOM   2918 C  CG    . PRO   B 1 102 ? -2.500  5.587   74.281  1.00 61.57  ? 1012 PRO   B CG    1 
ATOM   2919 C  CD    . PRO   B 1 102 ? -1.148  5.212   73.694  1.00 62.91  ? 1012 PRO   B CD    1 
ATOM   2920 N  N     . LEU   B 1 103 ? -1.108  8.242   77.039  1.00 46.14  ? 1013 LEU   B N     1 
ATOM   2921 C  CA    . LEU   B 1 103 ? -1.046  8.185   78.497  1.00 38.03  ? 1013 LEU   B CA    1 
ATOM   2922 C  C     . LEU   B 1 103 ? -1.860  7.009   79.019  1.00 40.97  ? 1013 LEU   B C     1 
ATOM   2923 O  O     . LEU   B 1 103 ? -2.984  6.770   78.567  1.00 46.30  ? 1013 LEU   B O     1 
ATOM   2924 C  CB    . LEU   B 1 103 ? -1.601  9.479   79.116  1.00 37.12  ? 1013 LEU   B CB    1 
ATOM   2925 C  CG    . LEU   B 1 103 ? -1.083  10.880  78.774  1.00 44.62  ? 1013 LEU   B CG    1 
ATOM   2926 C  CD1   . LEU   B 1 103 ? 0.443   10.867  78.587  1.00 37.32  ? 1013 LEU   B CD1   1 
ATOM   2927 C  CD2   . LEU   B 1 103 ? -1.791  11.470  77.563  1.00 43.37  ? 1013 LEU   B CD2   1 
ATOM   2928 N  N     . ILE   B 1 104 ? -1.310  6.298   80.003  1.00 32.30  ? 1014 ILE   B N     1 
ATOM   2929 C  CA    . ILE   B 1 104 ? -2.036  5.265   80.730  1.00 34.04  ? 1014 ILE   B CA    1 
ATOM   2930 C  C     . ILE   B 1 104 ? -2.317  5.783   82.133  1.00 33.29  ? 1014 ILE   B C     1 
ATOM   2931 O  O     . ILE   B 1 104 ? -1.393  6.158   82.864  1.00 31.70  ? 1014 ILE   B O     1 
ATOM   2932 C  CB    . ILE   B 1 104 ? -1.269  3.932   80.788  1.00 38.98  ? 1014 ILE   B CB    1 
ATOM   2933 C  CG1   . ILE   B 1 104 ? -1.132  3.304   79.394  1.00 38.73  ? 1014 ILE   B CG1   1 
ATOM   2934 C  CG2   . ILE   B 1 104 ? -1.958  2.954   81.777  1.00 29.45  ? 1014 ILE   B CG2   1 
ATOM   2935 C  CD1   . ILE   B 1 104 ? -0.250  2.048   79.376  1.00 40.07  ? 1014 ILE   B CD1   1 
ATOM   2936 N  N     . PHE   B 1 105 ? -3.596  5.805   82.508  1.00 35.02  ? 1015 PHE   B N     1 
ATOM   2937 C  CA    . PHE   B 1 105 ? -4.018  6.080   83.875  1.00 31.38  ? 1015 PHE   B CA    1 
ATOM   2938 C  C     . PHE   B 1 105 ? -4.325  4.742   84.539  1.00 31.44  ? 1015 PHE   B C     1 
ATOM   2939 O  O     . PHE   B 1 105 ? -5.255  4.041   84.126  1.00 32.30  ? 1015 PHE   B O     1 
ATOM   2940 C  CB    . PHE   B 1 105 ? -5.242  6.991   83.901  1.00 29.96  ? 1015 PHE   B CB    1 
ATOM   2941 C  CG    . PHE   B 1 105 ? -4.976  8.407   83.447  1.00 33.51  ? 1015 PHE   B CG    1 
ATOM   2942 C  CD1   . PHE   B 1 105 ? -4.825  8.709   82.093  1.00 33.59  ? 1015 PHE   B CD1   1 
ATOM   2943 C  CD2   . PHE   B 1 105 ? -4.918  9.449   84.372  1.00 31.84  ? 1015 PHE   B CD2   1 
ATOM   2944 C  CE1   . PHE   B 1 105 ? -4.596  10.012  81.674  1.00 33.68  ? 1015 PHE   B CE1   1 
ATOM   2945 C  CE2   . PHE   B 1 105 ? -4.697  10.748  83.955  1.00 32.54  ? 1015 PHE   B CE2   1 
ATOM   2946 C  CZ    . PHE   B 1 105 ? -4.535  11.026  82.608  1.00 33.76  ? 1015 PHE   B CZ    1 
ATOM   2947 N  N     . GLU   B 1 106 ? -3.535  4.377   85.545  1.00 27.48  ? 1016 GLU   B N     1 
ATOM   2948 C  CA    . GLU   B 1 106 ? -3.828  3.176   86.308  1.00 28.76  ? 1016 GLU   B CA    1 
ATOM   2949 C  C     . GLU   B 1 106 ? -4.815  3.508   87.420  1.00 26.46  ? 1016 GLU   B C     1 
ATOM   2950 O  O     . GLU   B 1 106 ? -5.017  4.674   87.759  1.00 30.45  ? 1016 GLU   B O     1 
ATOM   2951 C  CB    . GLU   B 1 106 ? -2.540  2.565   86.891  1.00 26.22  ? 1016 GLU   B CB    1 
ATOM   2952 C  CG    . GLU   B 1 106 ? -1.706  1.870   85.841  1.00 26.51  ? 1016 GLU   B CG    1 
ATOM   2953 C  CD    . GLU   B 1 106 ? -0.506  1.095   86.399  1.00 26.09  ? 1016 GLU   B CD    1 
ATOM   2954 O  OE1   . GLU   B 1 106 ? -0.232  1.124   87.617  1.00 25.84  ? 1016 GLU   B OE1   1 
ATOM   2955 O  OE2   . GLU   B 1 106 ? 0.137   0.416   85.593  1.00 26.40  ? 1016 GLU   B OE2   1 
ATOM   2956 N  N     . CYS   B 1 107 ? -5.418  2.473   88.004  1.00 26.04  ? 1017 CYS   B N     1 
ATOM   2957 C  CA    . CYS   B 1 107 ? -6.354  2.735   89.095  1.00 27.02  ? 1017 CYS   B CA    1 
ATOM   2958 C  C     . CYS   B 1 107 ? -5.581  3.247   90.298  1.00 29.23  ? 1017 CYS   B C     1 
ATOM   2959 O  O     . CYS   B 1 107 ? -4.349  3.125   90.378  1.00 28.66  ? 1017 CYS   B O     1 
ATOM   2960 C  CB    . CYS   B 1 107 ? -7.149  1.486   89.482  1.00 25.64  ? 1017 CYS   B CB    1 
ATOM   2961 S  SG    . CYS   B 1 107 ? -8.279  0.946   88.212  1.00 27.46  ? 1017 CYS   B SG    1 
ATOM   2962 N  N     . ASN   B 1 108 ? -6.299  3.836   91.246  1.00 25.76  ? 1018 ASN   B N     1 
ATOM   2963 C  CA    . ASN   B 1 108 ? -5.580  4.561   92.284  1.00 29.95  ? 1018 ASN   B CA    1 
ATOM   2964 C  C     . ASN   B 1 108 ? -6.292  4.378   93.615  1.00 29.76  ? 1018 ASN   B C     1 
ATOM   2965 O  O     . ASN   B 1 108 ? -7.131  3.488   93.777  1.00 30.49  ? 1018 ASN   B O     1 
ATOM   2966 C  CB    . ASN   B 1 108 ? -5.438  6.025   91.882  1.00 29.46  ? 1018 ASN   B CB    1 
ATOM   2967 C  CG    . ASN   B 1 108 ? -6.741  6.610   91.486  1.00 27.93  ? 1018 ASN   B CG    1 
ATOM   2968 O  OD1   . ASN   B 1 108 ? -7.616  6.790   92.324  1.00 29.51  ? 1018 ASN   B OD1   1 
ATOM   2969 N  ND2   . ASN   B 1 108 ? -6.903  6.885   90.195  1.00 28.32  ? 1018 ASN   B ND2   1 
ATOM   2970 N  N     . GLN   B 1 109 ? -5.922  5.201   94.592  1.00 28.89  ? 1019 GLN   B N     1 
ATOM   2971 C  CA    . GLN   B 1 109 ? -6.479  5.032   95.923  1.00 28.94  ? 1019 GLN   B CA    1 
ATOM   2972 C  C     . GLN   B 1 109 ? -7.892  5.586   96.028  1.00 32.00  ? 1019 GLN   B C     1 
ATOM   2973 O  O     . GLN   B 1 109 ? -8.594  5.273   96.999  1.00 30.98  ? 1019 GLN   B O     1 
ATOM   2974 C  CB    . GLN   B 1 109 ? -5.567  5.676   96.973  1.00 28.41  ? 1019 GLN   B CB    1 
ATOM   2975 C  CG    . GLN   B 1 109 ? -5.308  7.166   96.797  1.00 29.63  ? 1019 GLN   B CG    1 
ATOM   2976 C  CD    . GLN   B 1 109 ? -4.105  7.489   95.913  1.00 28.61  ? 1019 GLN   B CD    1 
ATOM   2977 O  OE1   . GLN   B 1 109 ? -3.706  6.699   95.046  1.00 30.79  ? 1019 GLN   B OE1   1 
ATOM   2978 N  NE2   . GLN   B 1 109 ? -3.533  8.667   96.124  1.00 28.41  ? 1019 GLN   B NE2   1 
ATOM   2979 N  N     . ALA   B 1 110 ? -8.335  6.364   95.036  1.00 28.32  ? 1020 ALA   B N     1 
ATOM   2980 C  CA    . ALA   B 1 110 ? -9.712  6.827   95.006  1.00 30.99  ? 1020 ALA   B CA    1 
ATOM   2981 C  C     . ALA   B 1 110 ? -10.670 5.803   94.405  1.00 32.20  ? 1020 ALA   B C     1 
ATOM   2982 O  O     . ALA   B 1 110 ? -11.882 5.896   94.654  1.00 30.20  ? 1020 ALA   B O     1 
ATOM   2983 C  CB    . ALA   B 1 110 ? -9.818  8.138   94.227  1.00 29.56  ? 1020 ALA   B CB    1 
ATOM   2984 N  N     . CYS   B 1 111 ? -10.161 4.850   93.617  1.00 30.58  ? 1021 CYS   B N     1 
ATOM   2985 C  CA    . CYS   B 1 111 ? -11.024 3.889   92.942  1.00 33.89  ? 1021 CYS   B CA    1 
ATOM   2986 C  C     . CYS   B 1 111 ? -11.714 2.992   93.967  1.00 31.06  ? 1021 CYS   B C     1 
ATOM   2987 O  O     . CYS   B 1 111 ? -11.221 2.781   95.078  1.00 31.42  ? 1021 CYS   B O     1 
ATOM   2988 C  CB    . CYS   B 1 111 ? -10.208 3.040   91.947  1.00 31.62  ? 1021 CYS   B CB    1 
ATOM   2989 S  SG    . CYS   B 1 111 ? -9.408  3.965   90.578  1.00 26.36  ? 1021 CYS   B SG    1 
ATOM   2990 N  N     . SER   B 1 112 ? -12.876 2.477   93.600  1.00 27.52  ? 1022 SER   B N     1 
ATOM   2991 C  CA    . SER   B 1 112 ? -13.504 1.501   94.476  1.00 28.19  ? 1022 SER   B CA    1 
ATOM   2992 C  C     . SER   B 1 112 ? -12.882 0.108   94.353  1.00 28.59  ? 1022 SER   B C     1 
ATOM   2993 O  O     . SER   B 1 112 ? -13.058 -0.718  95.254  1.00 28.14  ? 1022 SER   B O     1 
ATOM   2994 C  CB    . SER   B 1 112 ? -15.012 1.446   94.202  1.00 29.84  ? 1022 SER   B CB    1 
ATOM   2995 O  OG    . SER   B 1 112 ? -15.268 1.160   92.839  1.00 31.56  ? 1022 SER   B OG    1 
ATOM   2996 N  N     . CYS   B 1 113 ? -12.136 -0.158  93.287  1.00 30.73  ? 1023 CYS   B N     1 
ATOM   2997 C  CA    . CYS   B 1 113 ? -11.602 -1.486  93.036  1.00 32.18  ? 1023 CYS   B CA    1 
ATOM   2998 C  C     . CYS   B 1 113 ? -10.528 -1.867  94.061  1.00 30.12  ? 1023 CYS   B C     1 
ATOM   2999 O  O     . CYS   B 1 113 ? -10.084 -1.068  94.896  1.00 25.68  ? 1023 CYS   B O     1 
ATOM   3000 C  CB    . CYS   B 1 113 ? -11.029 -1.571  91.625  1.00 28.16  ? 1023 CYS   B CB    1 
ATOM   3001 S  SG    . CYS   B 1 113 ? -9.570  -0.523  91.397  1.00 25.51  ? 1023 CYS   B SG    1 
ATOM   3002 N  N     . TRP   B 1 114 ? -10.134 -3.130  93.999  1.00 29.13  ? 1024 TRP   B N     1 
ATOM   3003 C  CA    . TRP   B 1 114 ? -9.145  -3.665  94.920  1.00 32.46  ? 1024 TRP   B CA    1 
ATOM   3004 C  C     . TRP   B 1 114 ? -7.733  -3.439  94.375  1.00 30.34  ? 1024 TRP   B C     1 
ATOM   3005 O  O     . TRP   B 1 114 ? -7.526  -3.296  93.166  1.00 30.50  ? 1024 TRP   B O     1 
ATOM   3006 C  CB    . TRP   B 1 114 ? -9.386  -5.153  95.151  1.00 34.04  ? 1024 TRP   B CB    1 
ATOM   3007 C  CG    . TRP   B 1 114 ? -10.597 -5.460  95.982  1.00 35.01  ? 1024 TRP   B CG    1 
ATOM   3008 C  CD1   . TRP   B 1 114 ? -11.862 -5.004  95.792  1.00 37.39  ? 1024 TRP   B CD1   1 
ATOM   3009 C  CD2   . TRP   B 1 114 ? -10.642 -6.310  97.129  1.00 35.54  ? 1024 TRP   B CD2   1 
ATOM   3010 N  NE1   . TRP   B 1 114 ? -12.699 -5.508  96.764  1.00 39.37  ? 1024 TRP   B NE1   1 
ATOM   3011 C  CE2   . TRP   B 1 114 ? -11.966 -6.316  97.594  1.00 36.57  ? 1024 TRP   B CE2   1 
ATOM   3012 C  CE3   . TRP   B 1 114 ? -9.683  -7.061  97.814  1.00 33.69  ? 1024 TRP   B CE3   1 
ATOM   3013 C  CZ2   . TRP   B 1 114 ? -12.361 -7.050  98.713  1.00 37.64  ? 1024 TRP   B CZ2   1 
ATOM   3014 C  CZ3   . TRP   B 1 114 ? -10.076 -7.772  98.929  1.00 35.74  ? 1024 TRP   B CZ3   1 
ATOM   3015 C  CH2   . TRP   B 1 114 ? -11.403 -7.767  99.365  1.00 34.10  ? 1024 TRP   B CH2   1 
ATOM   3016 N  N     . ARG   B 1 115 ? -6.757  -3.426  95.290  1.00 30.40  ? 1025 ARG   B N     1 
ATOM   3017 C  CA    . ARG   B 1 115 ? -5.343  -3.177  94.963  1.00 30.49  ? 1025 ARG   B CA    1 
ATOM   3018 C  C     . ARG   B 1 115 ? -4.773  -4.182  93.963  1.00 33.04  ? 1025 ARG   B C     1 
ATOM   3019 O  O     . ARG   B 1 115 ? -3.719  -3.919  93.365  1.00 32.23  ? 1025 ARG   B O     1 
ATOM   3020 C  CB    . ARG   B 1 115 ? -4.527  -3.189  96.265  1.00 27.60  ? 1025 ARG   B CB    1 
ATOM   3021 C  CG    . ARG   B 1 115 ? -2.986  -3.160  96.133  1.00 36.75  ? 1025 ARG   B CG    1 
ATOM   3022 C  CD    . ARG   B 1 115 ? -2.481  -1.872  95.528  1.00 32.65  ? 1025 ARG   B CD    1 
ATOM   3023 N  NE    . ARG   B 1 115 ? -1.024  -1.802  95.488  1.00 36.32  ? 1025 ARG   B NE    1 
ATOM   3024 C  CZ    . ARG   B 1 115 ? -0.271  -2.280  94.506  1.00 35.40  ? 1025 ARG   B CZ    1 
ATOM   3025 N  NH1   . ARG   B 1 115 ? -0.800  -2.916  93.472  1.00 28.77  ? 1025 ARG   B NH1   1 
ATOM   3026 N  NH2   . ARG   B 1 115 ? 1.052   -2.112  94.562  1.00 39.25  ? 1025 ARG   B NH2   1 
ATOM   3027 N  N     . ASN   B 1 116 ? -5.449  -5.313  93.758  1.00 29.93  ? 1026 ASN   B N     1 
ATOM   3028 C  CA    . ASN   B 1 116 ? -5.006  -6.366  92.858  1.00 32.66  ? 1026 ASN   B CA    1 
ATOM   3029 C  C     . ASN   B 1 116 ? -5.756  -6.360  91.534  1.00 28.98  ? 1026 ASN   B C     1 
ATOM   3030 O  O     . ASN   B 1 116 ? -5.853  -7.408  90.882  1.00 29.06  ? 1026 ASN   B O     1 
ATOM   3031 C  CB    . ASN   B 1 116 ? -5.180  -7.723  93.533  1.00 34.95  ? 1026 ASN   B CB    1 
ATOM   3032 C  CG    . ASN   B 1 116 ? -6.576  -7.908  94.089  1.00 35.95  ? 1026 ASN   B CG    1 
ATOM   3033 O  OD1   . ASN   B 1 116 ? -7.495  -8.277  93.365  1.00 44.14  ? 1026 ASN   B OD1   1 
ATOM   3034 N  ND2   . ASN   B 1 116 ? -6.746  -7.640  95.380  1.00 36.87  ? 1026 ASN   B ND2   1 
ATOM   3035 N  N     . CYS   B 1 117 ? -6.313  -5.224  91.142  1.00 29.62  ? 1027 CYS   B N     1 
ATOM   3036 C  CA    . CYS   B 1 117 ? -7.123  -5.176  89.935  1.00 29.29  ? 1027 CYS   B CA    1 
ATOM   3037 C  C     . CYS   B 1 117 ? -6.235  -5.304  88.708  1.00 28.67  ? 1027 CYS   B C     1 
ATOM   3038 O  O     . CYS   B 1 117 ? -5.024  -5.147  88.781  1.00 29.95  ? 1027 CYS   B O     1 
ATOM   3039 C  CB    . CYS   B 1 117 ? -7.939  -3.881  89.884  1.00 27.70  ? 1027 CYS   B CB    1 
ATOM   3040 S  SG    . CYS   B 1 117 ? -7.189  -2.373  89.186  1.00 30.94  ? 1027 CYS   B SG    1 
ATOM   3041 N  N     . LYS   B 1 118 ? -6.850  -5.598  87.570  1.00 28.63  ? 1028 LYS   B N     1 
ATOM   3042 C  CA    . LYS   B 1 118 ? -6.066  -5.749  86.348  1.00 29.88  ? 1028 LYS   B CA    1 
ATOM   3043 C  C     . LYS   B 1 118 ? -5.412  -4.458  85.874  1.00 28.35  ? 1028 LYS   B C     1 
ATOM   3044 O  O     . LYS   B 1 118 ? -4.803  -4.477  84.801  1.00 30.31  ? 1028 LYS   B O     1 
ATOM   3045 C  CB    . LYS   B 1 118 ? -6.938  -6.286  85.208  1.00 31.13  ? 1028 LYS   B CB    1 
ATOM   3046 C  CG    . LYS   B 1 118 ? -7.490  -7.704  85.417  1.00 33.51  ? 1028 LYS   B CG    1 
ATOM   3047 C  CD    . LYS   B 1 118 ? -6.396  -8.659  85.815  1.00 34.52  ? 1028 LYS   B CD    1 
ATOM   3048 C  CE    . LYS   B 1 118 ? -6.876  -10.084 85.896  1.00 33.88  ? 1028 LYS   B CE    1 
ATOM   3049 N  NZ    . LYS   B 1 118 ? -5.712  -10.936 86.280  1.00 41.95  ? 1028 LYS   B NZ    1 
ATOM   3050 N  N     . ASN   B 1 119 ? -5.522  -3.345  86.591  1.00 26.66  ? 1029 ASN   B N     1 
ATOM   3051 C  CA    . ASN   B 1 119 ? -5.111  -2.050  86.041  1.00 30.05  ? 1029 ASN   B CA    1 
ATOM   3052 C  C     . ASN   B 1 119 ? -4.109  -1.372  86.966  1.00 28.54  ? 1029 ASN   B C     1 
ATOM   3053 O  O     . ASN   B 1 119 ? -4.247  -0.191  87.317  1.00 27.98  ? 1029 ASN   B O     1 
ATOM   3054 C  CB    . ASN   B 1 119 ? -6.310  -1.135  85.788  1.00 29.17  ? 1029 ASN   B CB    1 
ATOM   3055 C  CG    . ASN   B 1 119 ? -5.925  0.131   85.047  1.00 28.03  ? 1029 ASN   B CG    1 
ATOM   3056 O  OD1   . ASN   B 1 119 ? -4.881  0.190   84.403  1.00 27.46  ? 1029 ASN   B OD1   1 
ATOM   3057 N  ND2   . ASN   B 1 119 ? -6.772  1.159   85.143  1.00 29.69  ? 1029 ASN   B ND2   1 
ATOM   3058 N  N     . ARG   B 1 120 ? -3.070  -2.133  87.345  1.00 27.82  ? 1030 ARG   B N     1 
ATOM   3059 C  CA    . ARG   B 1 120 ? -2.144  -1.735  88.397  1.00 28.99  ? 1030 ARG   B CA    1 
ATOM   3060 C  C     . ARG   B 1 120 ? -0.769  -2.366  88.166  1.00 27.13  ? 1030 ARG   B C     1 
ATOM   3061 O  O     . ARG   B 1 120 ? -0.084  -2.754  89.118  1.00 25.41  ? 1030 ARG   B O     1 
ATOM   3062 C  CB    . ARG   B 1 120 ? -2.689  -2.114  89.779  1.00 28.72  ? 1030 ARG   B CB    1 
ATOM   3063 C  CG    . ARG   B 1 120 ? -3.866  -1.265  90.202  1.00 29.54  ? 1030 ARG   B CG    1 
ATOM   3064 C  CD    . ARG   B 1 120 ? -4.541  -1.791  91.427  1.00 30.61  ? 1030 ARG   B CD    1 
ATOM   3065 N  NE    . ARG   B 1 120 ? -5.794  -1.093  91.697  1.00 29.03  ? 1030 ARG   B NE    1 
ATOM   3066 C  CZ    . ARG   B 1 120 ? -5.890  -0.007  92.453  1.00 29.72  ? 1030 ARG   B CZ    1 
ATOM   3067 N  NH1   . ARG   B 1 120 ? -4.812  0.578   92.962  1.00 28.34  ? 1030 ARG   B NH1   1 
ATOM   3068 N  NH2   . ARG   B 1 120 ? -7.088  0.505   92.703  1.00 25.57  ? 1030 ARG   B NH2   1 
ATOM   3069 N  N     . VAL   B 1 121 ? -0.360  -2.484  86.902  1.00 26.03  ? 1031 VAL   B N     1 
ATOM   3070 C  CA    . VAL   B 1 121 ? 0.902   -3.143  86.584  1.00 27.31  ? 1031 VAL   B CA    1 
ATOM   3071 C  C     . VAL   B 1 121 ? 2.081   -2.315  87.075  1.00 28.44  ? 1031 VAL   B C     1 
ATOM   3072 O  O     . VAL   B 1 121 ? 2.906   -2.778  87.878  1.00 27.85  ? 1031 VAL   B O     1 
ATOM   3073 C  CB    . VAL   B 1 121 ? 1.021   -3.409  85.073  1.00 31.34  ? 1031 VAL   B CB    1 
ATOM   3074 C  CG1   . VAL   B 1 121 ? 2.420   -4.040  84.761  1.00 29.17  ? 1031 VAL   B CG1   1 
ATOM   3075 C  CG2   . VAL   B 1 121 ? -0.087  -4.308  84.602  1.00 27.59  ? 1031 VAL   B CG2   1 
ATOM   3076 N  N     . VAL   B 1 122 ? 2.196   -1.083  86.582  1.00 26.95  ? 1032 VAL   B N     1 
ATOM   3077 C  CA    . VAL   B 1 122 ? 3.402   -0.319  86.880  1.00 27.39  ? 1032 VAL   B CA    1 
ATOM   3078 C  C     . VAL   B 1 122 ? 3.517   -0.068  88.377  1.00 28.20  ? 1032 VAL   B C     1 
ATOM   3079 O  O     . VAL   B 1 122 ? 4.611   -0.162  88.954  1.00 27.84  ? 1032 VAL   B O     1 
ATOM   3080 C  CB    . VAL   B 1 122 ? 3.434   0.984   86.069  1.00 26.25  ? 1032 VAL   B CB    1 
ATOM   3081 C  CG1   . VAL   B 1 122 ? 4.696   1.794   86.428  1.00 26.25  ? 1032 VAL   B CG1   1 
ATOM   3082 C  CG2   . VAL   B 1 122 ? 3.380   0.668   84.586  1.00 26.96  ? 1032 VAL   B CG2   1 
ATOM   3083 N  N     . GLN   B 1 123 ? 2.392   0.206   89.045  1.00 27.21  ? 1033 GLN   B N     1 
ATOM   3084 C  CA    . GLN   B 1 123 ? 2.481   0.505   90.468  1.00 25.01  ? 1033 GLN   B CA    1 
ATOM   3085 C  C     . GLN   B 1 123 ? 2.920   -0.685  91.305  1.00 25.46  ? 1033 GLN   B C     1 
ATOM   3086 O  O     . GLN   B 1 123 ? 3.130   -0.507  92.503  1.00 25.06  ? 1033 GLN   B O     1 
ATOM   3087 C  CB    . GLN   B 1 123 ? 1.143   1.041   90.999  1.00 24.94  ? 1033 GLN   B CB    1 
ATOM   3088 C  CG    . GLN   B 1 123 ? -0.073  0.227   90.656  1.00 28.95  ? 1033 GLN   B CG    1 
ATOM   3089 C  CD    . GLN   B 1 123 ? -1.370  0.992   90.945  1.00 24.90  ? 1033 GLN   B CD    1 
ATOM   3090 O  OE1   . GLN   B 1 123 ? -1.840  1.026   92.081  1.00 24.86  ? 1033 GLN   B OE1   1 
ATOM   3091 N  NE2   . GLN   B 1 123 ? -1.924  1.633   89.919  1.00 25.60  ? 1033 GLN   B NE2   1 
ATOM   3092 N  N     . SER   B 1 124 ? 3.038   -1.884  90.723  1.00 26.17  ? 1034 SER   B N     1 
ATOM   3093 C  CA    . SER   B 1 124 ? 3.312   -3.091  91.486  1.00 27.30  ? 1034 SER   B CA    1 
ATOM   3094 C  C     . SER   B 1 124 ? 4.793   -3.466  91.520  1.00 27.38  ? 1034 SER   B C     1 
ATOM   3095 O  O     . SER   B 1 124 ? 5.150   -4.451  92.174  1.00 26.25  ? 1034 SER   B O     1 
ATOM   3096 C  CB    . SER   B 1 124 ? 2.496   -4.272  90.940  1.00 30.25  ? 1034 SER   B CB    1 
ATOM   3097 O  OG    . SER   B 1 124 ? 1.105   -4.126  91.204  1.00 29.88  ? 1034 SER   B OG    1 
ATOM   3098 N  N     . GLY   B 1 125 ? 5.655   -2.723  90.836  1.00 25.62  ? 1035 GLY   B N     1 
ATOM   3099 C  CA    . GLY   B 1 125 ? 7.086   -2.888  91.005  1.00 27.46  ? 1035 GLY   B CA    1 
ATOM   3100 C  C     . GLY   B 1 125 ? 7.702   -3.859  90.011  1.00 28.82  ? 1035 GLY   B C     1 
ATOM   3101 O  O     . GLY   B 1 125 ? 7.023   -4.506  89.208  1.00 29.37  ? 1035 GLY   B O     1 
ATOM   3102 N  N     . ILE   B 1 126 ? 9.038   -3.919  90.048  1.00 28.82  ? 1036 ILE   B N     1 
ATOM   3103 C  CA    . ILE   B 1 126 ? 9.785   -4.836  89.198  1.00 27.52  ? 1036 ILE   B CA    1 
ATOM   3104 C  C     . ILE   B 1 126 ? 9.411   -6.267  89.533  1.00 28.15  ? 1036 ILE   B C     1 
ATOM   3105 O  O     . ILE   B 1 126 ? 9.319   -6.644  90.709  1.00 30.52  ? 1036 ILE   B O     1 
ATOM   3106 C  CB    . ILE   B 1 126 ? 11.293  -4.618  89.398  1.00 29.61  ? 1036 ILE   B CB    1 
ATOM   3107 C  CG1   . ILE   B 1 126 ? 11.724  -3.242  88.895  1.00 27.58  ? 1036 ILE   B CG1   1 
ATOM   3108 C  CG2   . ILE   B 1 126 ? 12.114  -5.748  88.737  1.00 29.82  ? 1036 ILE   B CG2   1 
ATOM   3109 C  CD1   . ILE   B 1 126 ? 13.231  -2.980  89.140  1.00 29.62  ? 1036 ILE   B CD1   1 
ATOM   3110 N  N     . LYS   B 1 127 ? 9.216   -7.083  88.500  1.00 28.86  ? 1037 LYS   B N     1 
ATOM   3111 C  CA    . LYS   B 1 127 ? 9.018   -8.517  88.683  1.00 29.97  ? 1037 LYS   B CA    1 
ATOM   3112 C  C     . LYS   B 1 127 ? 10.103  -9.383  88.053  1.00 32.74  ? 1037 LYS   B C     1 
ATOM   3113 O  O     . LYS   B 1 127 ? 10.392  -10.460 88.583  1.00 36.01  ? 1037 LYS   B O     1 
ATOM   3114 C  CB    . LYS   B 1 127 ? 7.653   -8.964  88.120  1.00 31.20  ? 1037 LYS   B CB    1 
ATOM   3115 C  CG    . LYS   B 1 127 ? 6.418   -8.413  88.861  1.00 35.25  ? 1037 LYS   B CG    1 
ATOM   3116 C  CD    . LYS   B 1 127 ? 6.442   -8.769  90.338  1.00 33.80  ? 1037 LYS   B CD    1 
ATOM   3117 C  CE    . LYS   B 1 127 ? 5.352   -8.037  91.109  1.00 37.55  ? 1037 LYS   B CE    1 
ATOM   3118 N  NZ    . LYS   B 1 127 ? 5.440   -8.385  92.564  1.00 39.90  ? 1037 LYS   B NZ    1 
ATOM   3119 N  N     . VAL   B 1 128 ? 10.703  -8.957  86.938  1.00 34.86  ? 1038 VAL   B N     1 
ATOM   3120 C  CA    . VAL   B 1 128 ? 11.724  -9.756  86.273  1.00 34.06  ? 1038 VAL   B CA    1 
ATOM   3121 C  C     . VAL   B 1 128 ? 13.045  -9.631  87.019  1.00 34.99  ? 1038 VAL   B C     1 
ATOM   3122 O  O     . VAL   B 1 128 ? 13.333  -8.620  87.666  1.00 30.37  ? 1038 VAL   B O     1 
ATOM   3123 C  CB    . VAL   B 1 128 ? 11.905  -9.342  84.797  1.00 35.80  ? 1038 VAL   B CB    1 
ATOM   3124 C  CG1   . VAL   B 1 128 ? 10.695  -9.702  83.976  1.00 31.86  ? 1038 VAL   B CG1   1 
ATOM   3125 C  CG2   . VAL   B 1 128 ? 12.247  -7.871  84.677  1.00 30.57  ? 1038 VAL   B CG2   1 
ATOM   3126 N  N     . ARG   B 1 129 ? 13.864  -10.670 86.911  1.00 32.46  ? 1039 ARG   B N     1 
ATOM   3127 C  CA    . ARG   B 1 129 ? 15.201  -10.664 87.487  1.00 35.31  ? 1039 ARG   B CA    1 
ATOM   3128 C  C     . ARG   B 1 129 ? 16.130  -9.994  86.485  1.00 32.57  ? 1039 ARG   B C     1 
ATOM   3129 O  O     . ARG   B 1 129 ? 16.373  -10.541 85.407  1.00 36.96  ? 1039 ARG   B O     1 
ATOM   3130 C  CB    . ARG   B 1 129 ? 15.649  -12.090 87.799  1.00 41.91  ? 1039 ARG   B CB    1 
ATOM   3131 C  CG    . ARG   B 1 129 ? 14.689  -12.849 88.707  1.00 41.62  ? 1039 ARG   B CG    1 
ATOM   3132 C  CD    . ARG   B 1 129 ? 14.286  -11.998 89.910  1.00 41.69  ? 1039 ARG   B CD    1 
ATOM   3133 N  NE    . ARG   B 1 129 ? 13.826  -12.834 91.011  1.00 45.24  ? 1039 ARG   B NE    1 
ATOM   3134 C  CZ    . ARG   B 1 129 ? 14.626  -13.343 91.940  1.00 47.25  ? 1039 ARG   B CZ    1 
ATOM   3135 N  NH1   . ARG   B 1 129 ? 15.918  -13.051 91.971  1.00 41.85  ? 1039 ARG   B NH1   1 
ATOM   3136 N  NH2   . ARG   B 1 129 ? 14.117  -14.168 92.855  1.00 46.00  ? 1039 ARG   B NH2   1 
ATOM   3137 N  N     . LEU   B 1 130 ? 16.601  -8.795  86.810  1.00 34.36  ? 1040 LEU   B N     1 
ATOM   3138 C  CA    . LEU   B 1 130 ? 17.527  -8.053  85.965  1.00 34.52  ? 1040 LEU   B CA    1 
ATOM   3139 C  C     . LEU   B 1 130 ? 18.928  -8.162  86.541  1.00 35.26  ? 1040 LEU   B C     1 
ATOM   3140 O  O     . LEU   B 1 130 ? 19.121  -8.674  87.647  1.00 35.32  ? 1040 LEU   B O     1 
ATOM   3141 C  CB    . LEU   B 1 130 ? 17.114  -6.581  85.846  1.00 30.73  ? 1040 LEU   B CB    1 
ATOM   3142 C  CG    . LEU   B 1 130 ? 15.797  -6.238  85.144  1.00 33.41  ? 1040 LEU   B CG    1 
ATOM   3143 C  CD1   . LEU   B 1 130 ? 15.584  -4.720  85.124  1.00 29.61  ? 1040 LEU   B CD1   1 
ATOM   3144 C  CD2   . LEU   B 1 130 ? 15.776  -6.808  83.740  1.00 31.31  ? 1040 LEU   B CD2   1 
ATOM   3145 N  N     . GLN   B 1 131 ? 19.913  -7.661  85.780  1.00 38.33  ? 1041 GLN   B N     1 
ATOM   3146 C  CA    . GLN   B 1 131 ? 21.311  -7.673  86.209  1.00 32.87  ? 1041 GLN   B CA    1 
ATOM   3147 C  C     . GLN   B 1 131 ? 22.079  -6.504  85.595  1.00 33.31  ? 1041 GLN   B C     1 
ATOM   3148 O  O     . GLN   B 1 131 ? 22.028  -6.290  84.381  1.00 33.25  ? 1041 GLN   B O     1 
ATOM   3149 C  CB    . GLN   B 1 131 ? 22.002  -8.989  85.834  1.00 34.20  ? 1041 GLN   B CB    1 
ATOM   3150 C  CG    . GLN   B 1 131 ? 23.542  -8.961  86.119  1.00 35.25  ? 1041 GLN   B CG    1 
ATOM   3151 C  CD    . GLN   B 1 131 ? 24.246  -10.220 85.667  1.00 36.28  ? 1041 GLN   B CD    1 
ATOM   3152 O  OE1   . GLN   B 1 131 ? 24.526  -10.385 84.480  1.00 37.69  ? 1041 GLN   B OE1   1 
ATOM   3153 N  NE2   . GLN   B 1 131 ? 24.519  -11.127 86.609  1.00 37.02  ? 1041 GLN   B NE2   1 
ATOM   3154 N  N     . LEU   B 1 132 ? 22.785  -5.753  86.436  1.00 32.34  ? 1042 LEU   B N     1 
ATOM   3155 C  CA    . LEU   B 1 132 ? 23.706  -4.712  85.987  1.00 36.33  ? 1042 LEU   B CA    1 
ATOM   3156 C  C     . LEU   B 1 132 ? 25.049  -5.365  85.672  1.00 37.48  ? 1042 LEU   B C     1 
ATOM   3157 O  O     . LEU   B 1 132 ? 25.615  -6.045  86.535  1.00 39.34  ? 1042 LEU   B O     1 
ATOM   3158 C  CB    . LEU   B 1 132 ? 23.864  -3.646  87.073  1.00 35.67  ? 1042 LEU   B CB    1 
ATOM   3159 C  CG    . LEU   B 1 132 ? 24.917  -2.534  87.022  1.00 31.95  ? 1042 LEU   B CG    1 
ATOM   3160 C  CD1   . LEU   B 1 132 ? 24.700  -1.634  85.823  1.00 31.90  ? 1042 LEU   B CD1   1 
ATOM   3161 C  CD2   . LEU   B 1 132 ? 24.871  -1.715  88.308  1.00 31.57  ? 1042 LEU   B CD2   1 
ATOM   3162 N  N     . TYR   B 1 133 ? 25.553  -5.185  84.446  1.00 33.94  ? 1043 TYR   B N     1 
ATOM   3163 C  CA    . TYR   B 1 133 ? 26.782  -5.873  84.030  1.00 35.51  ? 1043 TYR   B CA    1 
ATOM   3164 C  C     . TYR   B 1 133 ? 27.685  -4.945  83.228  1.00 35.39  ? 1043 TYR   B C     1 
ATOM   3165 O  O     . TYR   B 1 133 ? 27.246  -3.936  82.678  1.00 35.00  ? 1043 TYR   B O     1 
ATOM   3166 C  CB    . TYR   B 1 133 ? 26.481  -7.118  83.185  1.00 38.50  ? 1043 TYR   B CB    1 
ATOM   3167 C  CG    . TYR   B 1 133 ? 26.157  -6.826  81.728  1.00 36.40  ? 1043 TYR   B CG    1 
ATOM   3168 C  CD1   . TYR   B 1 133 ? 25.008  -6.114  81.371  1.00 35.67  ? 1043 TYR   B CD1   1 
ATOM   3169 C  CD2   . TYR   B 1 133 ? 26.993  -7.279  80.711  1.00 37.70  ? 1043 TYR   B CD2   1 
ATOM   3170 C  CE1   . TYR   B 1 133 ? 24.723  -5.857  80.037  1.00 36.30  ? 1043 TYR   B CE1   1 
ATOM   3171 C  CE2   . TYR   B 1 133 ? 26.717  -7.027  79.389  1.00 38.34  ? 1043 TYR   B CE2   1 
ATOM   3172 C  CZ    . TYR   B 1 133 ? 25.575  -6.324  79.050  1.00 37.68  ? 1043 TYR   B CZ    1 
ATOM   3173 O  OH    . TYR   B 1 133 ? 25.316  -6.081  77.720  1.00 38.56  ? 1043 TYR   B OH    1 
ATOM   3174 N  N     . ARG   B 1 134 ? 28.964  -5.310  83.148  1.00 36.64  ? 1044 ARG   B N     1 
ATOM   3175 C  CA    . ARG   B 1 134 ? 29.916  -4.517  82.387  1.00 36.78  ? 1044 ARG   B CA    1 
ATOM   3176 C  C     . ARG   B 1 134 ? 29.823  -4.884  80.915  1.00 37.71  ? 1044 ARG   B C     1 
ATOM   3177 O  O     . ARG   B 1 134 ? 29.855  -6.064  80.561  1.00 38.55  ? 1044 ARG   B O     1 
ATOM   3178 C  CB    . ARG   B 1 134 ? 31.334  -4.735  82.909  1.00 38.76  ? 1044 ARG   B CB    1 
ATOM   3179 C  CG    . ARG   B 1 134 ? 32.373  -3.730  82.370  1.00 37.87  ? 1044 ARG   B CG    1 
ATOM   3180 C  CD    . ARG   B 1 134 ? 32.155  -2.321  82.927  1.00 37.03  ? 1044 ARG   B CD    1 
ATOM   3181 N  NE    . ARG   B 1 134 ? 33.256  -1.401  82.654  1.00 38.73  ? 1044 ARG   B NE    1 
ATOM   3182 C  CZ    . ARG   B 1 134 ? 33.176  -0.087  82.824  1.00 37.83  ? 1044 ARG   B CZ    1 
ATOM   3183 N  NH1   . ARG   B 1 134 ? 32.046  0.486   83.224  1.00 37.15  ? 1044 ARG   B NH1   1 
ATOM   3184 N  NH2   . ARG   B 1 134 ? 34.242  0.669   82.572  1.00 37.97  ? 1044 ARG   B NH2   1 
ATOM   3185 N  N     . THR   B 1 135 ? 29.704  -3.880  80.058  1.00 37.79  ? 1045 THR   B N     1 
ATOM   3186 C  CA    . THR   B 1 135 ? 29.590  -4.096  78.623  1.00 38.88  ? 1045 THR   B CA    1 
ATOM   3187 C  C     . THR   B 1 135 ? 30.934  -3.899  77.945  1.00 40.06  ? 1045 THR   B C     1 
ATOM   3188 O  O     . THR   B 1 135 ? 31.851  -3.285  78.490  1.00 39.89  ? 1045 THR   B O     1 
ATOM   3189 C  CB    . THR   B 1 135 ? 28.583  -3.137  77.978  1.00 41.81  ? 1045 THR   B CB    1 
ATOM   3190 O  OG1   . THR   B 1 135 ? 29.119  -1.806  78.012  1.00 39.81  ? 1045 THR   B OG1   1 
ATOM   3191 C  CG2   . THR   B 1 135 ? 27.240  -3.171  78.707  1.00 37.34  ? 1045 THR   B CG2   1 
ATOM   3192 N  N     . ALA   B 1 136 ? 31.006  -4.380  76.707  1.00 41.39  ? 1046 ALA   B N     1 
ATOM   3193 C  CA    . ALA   B 1 136 ? 32.262  -4.379  75.971  1.00 43.06  ? 1046 ALA   B CA    1 
ATOM   3194 C  C     . ALA   B 1 136 ? 32.708  -2.962  75.628  1.00 45.81  ? 1046 ALA   B C     1 
ATOM   3195 O  O     . ALA   B 1 136 ? 33.883  -2.614  75.805  1.00 47.46  ? 1046 ALA   B O     1 
ATOM   3196 C  CB    . ALA   B 1 136 ? 32.125  -5.226  74.707  1.00 44.39  ? 1046 ALA   B CB    1 
ATOM   3197 N  N     . LYS   B 1 137 ? 31.793  -2.130  75.121  1.00 43.91  ? 1047 LYS   B N     1 
ATOM   3198 C  CA    . LYS   B 1 137 ? 32.210  -0.819  74.634  1.00 47.46  ? 1047 LYS   B CA    1 
ATOM   3199 C  C     . LYS   B 1 137 ? 31.280  0.300   75.082  1.00 47.01  ? 1047 LYS   B C     1 
ATOM   3200 O  O     . LYS   B 1 137 ? 31.298  1.384   74.481  1.00 51.44  ? 1047 LYS   B O     1 
ATOM   3201 C  CB    . LYS   B 1 137 ? 32.284  -0.785  73.097  1.00 47.31  ? 1047 LYS   B CB    1 
ATOM   3202 C  CG    . LYS   B 1 137 ? 33.041  -1.922  72.442  1.00 46.38  ? 1047 LYS   B CG    1 
ATOM   3203 C  CD    . LYS   B 1 137 ? 33.108  -1.705  70.931  1.00 50.35  ? 1047 LYS   B CD    1 
ATOM   3204 C  CE    . LYS   B 1 137 ? 33.715  -2.899  70.206  1.00 51.88  ? 1047 LYS   B CE    1 
ATOM   3205 N  NZ    . LYS   B 1 137 ? 33.865  -2.669  68.738  1.00 52.22  ? 1047 LYS   B NZ    1 
ATOM   3206 N  N     . MET   B 1 138 ? 30.480  0.085   76.125  1.00 41.45  ? 1048 MET   B N     1 
ATOM   3207 C  CA    . MET   B 1 138 ? 29.465  1.059   76.517  1.00 45.04  ? 1048 MET   B CA    1 
ATOM   3208 C  C     . MET   B 1 138 ? 29.451  1.347   78.014  1.00 44.32  ? 1048 MET   B C     1 
ATOM   3209 O  O     . MET   B 1 138 ? 28.518  2.011   78.492  1.00 41.57  ? 1048 MET   B O     1 
ATOM   3210 C  CB    . MET   B 1 138 ? 28.069  0.582   76.094  1.00 41.22  ? 1048 MET   B CB    1 
ATOM   3211 C  CG    . MET   B 1 138 ? 27.797  0.580   74.594  1.00 42.29  ? 1048 MET   B CG    1 
ATOM   3212 S  SD    . MET   B 1 138 ? 26.071  0.170   74.239  1.00 52.09  ? 1048 MET   B SD    1 
ATOM   3213 C  CE    . MET   B 1 138 ? 26.006  -1.579  74.672  1.00 44.05  ? 1048 MET   B CE    1 
ATOM   3214 N  N     . GLY   B 1 139 ? 30.430  0.856   78.769  1.00 38.19  ? 1049 GLY   B N     1 
ATOM   3215 C  CA    . GLY   B 1 139 ? 30.360  0.968   80.212  1.00 37.09  ? 1049 GLY   B CA    1 
ATOM   3216 C  C     . GLY   B 1 139 ? 29.399  -0.027  80.838  1.00 38.68  ? 1049 GLY   B C     1 
ATOM   3217 O  O     . GLY   B 1 139 ? 29.294  -1.173  80.384  1.00 36.61  ? 1049 GLY   B O     1 
ATOM   3218 N  N     . TRP   B 1 140 ? 28.700  0.390   81.894  1.00 35.22  ? 1050 TRP   B N     1 
ATOM   3219 C  CA    . TRP   B 1 140 ? 27.747  -0.518  82.511  1.00 34.49  ? 1050 TRP   B CA    1 
ATOM   3220 C  C     . TRP   B 1 140 ? 26.486  -0.626  81.659  1.00 34.37  ? 1050 TRP   B C     1 
ATOM   3221 O  O     . TRP   B 1 140 ? 26.189  0.232   80.823  1.00 34.75  ? 1050 TRP   B O     1 
ATOM   3222 C  CB    . TRP   B 1 140 ? 27.389  -0.058  83.924  1.00 33.62  ? 1050 TRP   B CB    1 
ATOM   3223 C  CG    . TRP   B 1 140 ? 28.579  0.117   84.796  1.00 36.05  ? 1050 TRP   B CG    1 
ATOM   3224 C  CD1   . TRP   B 1 140 ? 29.230  1.280   85.064  1.00 35.26  ? 1050 TRP   B CD1   1 
ATOM   3225 C  CD2   . TRP   B 1 140 ? 29.266  -0.905  85.519  1.00 34.17  ? 1050 TRP   B CD2   1 
ATOM   3226 N  NE1   . TRP   B 1 140 ? 30.288  1.050   85.913  1.00 34.48  ? 1050 TRP   B NE1   1 
ATOM   3227 C  CE2   . TRP   B 1 140 ? 30.329  -0.284  86.210  1.00 34.52  ? 1050 TRP   B CE2   1 
ATOM   3228 C  CE3   . TRP   B 1 140 ? 29.090  -2.282  85.649  1.00 34.33  ? 1050 TRP   B CE3   1 
ATOM   3229 C  CZ2   . TRP   B 1 140 ? 31.212  -0.997  87.012  1.00 36.47  ? 1050 TRP   B CZ2   1 
ATOM   3230 C  CZ3   . TRP   B 1 140 ? 29.964  -2.991  86.456  1.00 34.86  ? 1050 TRP   B CZ3   1 
ATOM   3231 C  CH2   . TRP   B 1 140 ? 31.018  -2.346  87.126  1.00 35.19  ? 1050 TRP   B CH2   1 
ATOM   3232 N  N     . GLY   B 1 141 ? 25.740  -1.701  81.884  1.00 34.06  ? 1051 GLY   B N     1 
ATOM   3233 C  CA    . GLY   B 1 141 ? 24.465  -1.875  81.217  1.00 34.49  ? 1051 GLY   B CA    1 
ATOM   3234 C  C     . GLY   B 1 141 ? 23.579  -2.787  82.037  1.00 33.95  ? 1051 GLY   B C     1 
ATOM   3235 O  O     . GLY   B 1 141 ? 23.977  -3.293  83.088  1.00 35.75  ? 1051 GLY   B O     1 
ATOM   3236 N  N     . VAL   B 1 142 ? 22.367  -3.003  81.534  1.00 34.38  ? 1052 VAL   B N     1 
ATOM   3237 C  CA    . VAL   B 1 142 ? 21.381  -3.862  82.178  1.00 32.68  ? 1052 VAL   B CA    1 
ATOM   3238 C  C     . VAL   B 1 142 ? 20.993  -4.950  81.195  1.00 33.58  ? 1052 VAL   B C     1 
ATOM   3239 O  O     . VAL   B 1 142 ? 20.734  -4.666  80.020  1.00 34.20  ? 1052 VAL   B O     1 
ATOM   3240 C  CB    . VAL   B 1 142 ? 20.137  -3.072  82.620  1.00 31.72  ? 1052 VAL   B CB    1 
ATOM   3241 C  CG1   . VAL   B 1 142 ? 19.220  -3.960  83.458  1.00 31.23  ? 1052 VAL   B CG1   1 
ATOM   3242 C  CG2   . VAL   B 1 142 ? 20.541  -1.813  83.361  1.00 31.16  ? 1052 VAL   B CG2   1 
ATOM   3243 N  N     . ARG   B 1 143 ? 20.950  -6.190  81.668  1.00 33.86  ? 1053 ARG   B N     1 
ATOM   3244 C  CA    . ARG   B 1 143 ? 20.526  -7.296  80.826  1.00 34.89  ? 1053 ARG   B CA    1 
ATOM   3245 C  C     . ARG   B 1 143 ? 19.595  -8.194  81.619  1.00 34.61  ? 1053 ARG   B C     1 
ATOM   3246 O  O     . ARG   B 1 143 ? 19.560  -8.158  82.852  1.00 33.85  ? 1053 ARG   B O     1 
ATOM   3247 C  CB    . ARG   B 1 143 ? 21.707  -8.120  80.305  1.00 40.92  ? 1053 ARG   B CB    1 
ATOM   3248 C  CG    . ARG   B 1 143 ? 22.308  -9.032  81.360  1.00 38.56  ? 1053 ARG   B CG    1 
ATOM   3249 C  CD    . ARG   B 1 143 ? 23.522  -9.743  80.799  1.00 38.05  ? 1053 ARG   B CD    1 
ATOM   3250 N  NE    . ARG   B 1 143 ? 24.543  -9.975  81.806  1.00 37.86  ? 1053 ARG   B NE    1 
ATOM   3251 C  CZ    . ARG   B 1 143 ? 25.729  -10.503 81.537  1.00 40.12  ? 1053 ARG   B CZ    1 
ATOM   3252 N  NH1   . ARG   B 1 143 ? 26.053  -10.880 80.310  1.00 40.30  ? 1053 ARG   B NH1   1 
ATOM   3253 N  NH2   . ARG   B 1 143 ? 26.605  -10.666 82.521  1.00 45.99  ? 1053 ARG   B NH2   1 
ATOM   3254 N  N     . ALA   B 1 144 ? 18.852  -9.015  80.889  1.00 35.43  ? 1054 ALA   B N     1 
ATOM   3255 C  CA    . ALA   B 1 144 ? 17.846  -9.870  81.490  1.00 35.48  ? 1054 ALA   B CA    1 
ATOM   3256 C  C     . ALA   B 1 144 ? 18.444  -11.208 81.901  1.00 36.72  ? 1054 ALA   B C     1 
ATOM   3257 O  O     . ALA   B 1 144 ? 19.243  -11.796 81.168  1.00 40.09  ? 1054 ALA   B O     1 
ATOM   3258 C  CB    . ALA   B 1 144 ? 16.685  -10.088 80.519  1.00 41.04  ? 1054 ALA   B CB    1 
ATOM   3259 N  N     . LEU   B 1 145 ? 18.047  -11.678 83.086  1.00 36.06  ? 1055 LEU   B N     1 
ATOM   3260 C  CA    . LEU   B 1 145 ? 18.417  -12.990 83.604  1.00 41.95  ? 1055 LEU   B CA    1 
ATOM   3261 C  C     . LEU   B 1 145 ? 17.363  -14.062 83.340  1.00 41.77  ? 1055 LEU   B C     1 
ATOM   3262 O  O     . LEU   B 1 145 ? 17.561  -15.210 83.748  1.00 43.03  ? 1055 LEU   B O     1 
ATOM   3263 C  CB    . LEU   B 1 145 ? 18.689  -12.911 85.113  1.00 38.07  ? 1055 LEU   B CB    1 
ATOM   3264 C  CG    . LEU   B 1 145 ? 19.943  -12.177 85.589  1.00 37.91  ? 1055 LEU   B CG    1 
ATOM   3265 C  CD1   . LEU   B 1 145 ? 20.111  -12.344 87.097  1.00 36.48  ? 1055 LEU   B CD1   1 
ATOM   3266 C  CD2   . LEU   B 1 145 ? 21.188  -12.663 84.857  1.00 37.89  ? 1055 LEU   B CD2   1 
ATOM   3267 N  N     . GLN   B 1 146 ? 16.256  -13.719 82.677  1.00 38.03  ? 1056 GLN   B N     1 
ATOM   3268 C  CA    . GLN   B 1 146 ? 15.231  -14.672 82.273  1.00 44.03  ? 1056 GLN   B CA    1 
ATOM   3269 C  C     . GLN   B 1 146 ? 14.769  -14.326 80.865  1.00 42.17  ? 1056 GLN   B C     1 
ATOM   3270 O  O     . GLN   B 1 146 ? 15.111  -13.277 80.313  1.00 41.38  ? 1056 GLN   B O     1 
ATOM   3271 C  CB    . GLN   B 1 146 ? 14.022  -14.648 83.224  1.00 40.47  ? 1056 GLN   B CB    1 
ATOM   3272 C  CG    . GLN   B 1 146 ? 13.309  -13.311 83.201  1.00 40.29  ? 1056 GLN   B CG    1 
ATOM   3273 C  CD    . GLN   B 1 146 ? 12.294  -13.146 84.306  1.00 41.48  ? 1056 GLN   B CD    1 
ATOM   3274 O  OE1   . GLN   B 1 146 ? 12.653  -12.995 85.474  1.00 41.96  ? 1056 GLN   B OE1   1 
ATOM   3275 N  NE2   . GLN   B 1 146 ? 11.011  -13.156 83.944  1.00 40.97  ? 1056 GLN   B NE2   1 
ATOM   3276 N  N     . THR   B 1 147 ? 13.978  -15.213 80.279  1.00 42.10  ? 1057 THR   B N     1 
ATOM   3277 C  CA    . THR   B 1 147 ? 13.241  -14.833 79.085  1.00 46.16  ? 1057 THR   B CA    1 
ATOM   3278 C  C     . THR   B 1 147 ? 12.097  -13.895 79.477  1.00 39.17  ? 1057 THR   B C     1 
ATOM   3279 O  O     . THR   B 1 147 ? 11.458  -14.072 80.516  1.00 38.38  ? 1057 THR   B O     1 
ATOM   3280 C  CB    . THR   B 1 147 ? 12.714  -16.073 78.358  1.00 45.86  ? 1057 THR   B CB    1 
ATOM   3281 O  OG1   . THR   B 1 147 ? 12.070  -16.939 79.296  1.00 50.25  ? 1057 THR   B OG1   1 
ATOM   3282 C  CG2   . THR   B 1 147 ? 13.851  -16.834 77.673  1.00 46.48  ? 1057 THR   B CG2   1 
ATOM   3283 N  N     . ILE   B 1 148 ? 11.882  -12.860 78.671  1.00 42.22  ? 1058 ILE   B N     1 
ATOM   3284 C  CA    . ILE   B 1 148 ? 10.865  -11.843 78.943  1.00 37.33  ? 1058 ILE   B CA    1 
ATOM   3285 C  C     . ILE   B 1 148 ? 9.917   -11.778 77.753  1.00 40.28  ? 1058 ILE   B C     1 
ATOM   3286 O  O     . ILE   B 1 148 ? 10.324  -11.334 76.669  1.00 42.54  ? 1058 ILE   B O     1 
ATOM   3287 C  CB    . ILE   B 1 148 ? 11.480  -10.454 79.189  1.00 38.81  ? 1058 ILE   B CB    1 
ATOM   3288 C  CG1   . ILE   B 1 148 ? 12.497  -10.474 80.329  1.00 36.22  ? 1058 ILE   B CG1   1 
ATOM   3289 C  CG2   . ILE   B 1 148 ? 10.372  -9.410  79.440  1.00 34.77  ? 1058 ILE   B CG2   1 
ATOM   3290 C  CD1   . ILE   B 1 148 ? 13.226  -9.160  80.508  1.00 34.24  ? 1058 ILE   B CD1   1 
ATOM   3291 N  N     . PRO   B 1 149 ? 8.657   -12.193 77.899  1.00 39.55  ? 1059 PRO   B N     1 
ATOM   3292 C  CA    . PRO   B 1 149 ? 7.720   -12.061 76.784  1.00 39.30  ? 1059 PRO   B CA    1 
ATOM   3293 C  C     . PRO   B 1 149 ? 7.532   -10.597 76.429  1.00 38.41  ? 1059 PRO   B C     1 
ATOM   3294 O  O     . PRO   B 1 149 ? 7.635   -9.709  77.280  1.00 36.77  ? 1059 PRO   B O     1 
ATOM   3295 C  CB    . PRO   B 1 149 ? 6.424   -12.684 77.327  1.00 42.31  ? 1059 PRO   B CB    1 
ATOM   3296 C  CG    . PRO   B 1 149 ? 6.815   -13.401 78.592  1.00 39.96  ? 1059 PRO   B CG    1 
ATOM   3297 C  CD    . PRO   B 1 149 ? 7.995   -12.663 79.125  1.00 37.53  ? 1059 PRO   B CD    1 
ATOM   3298 N  N     . GLN   B 1 150 ? 7.259   -10.348 75.152  1.00 39.72  ? 1060 GLN   B N     1 
ATOM   3299 C  CA    . GLN   B 1 150 ? 6.948   -8.992  74.716  1.00 40.40  ? 1060 GLN   B CA    1 
ATOM   3300 C  C     . GLN   B 1 150 ? 5.870   -8.357  75.591  1.00 39.42  ? 1060 GLN   B C     1 
ATOM   3301 O  O     . GLN   B 1 150 ? 4.968   -9.038  76.104  1.00 37.48  ? 1060 GLN   B O     1 
ATOM   3302 C  CB    . GLN   B 1 150 ? 6.476   -8.984  73.263  1.00 41.18  ? 1060 GLN   B CB    1 
ATOM   3303 C  CG    . GLN   B 1 150 ? 6.238   -7.582  72.735  1.00 42.73  ? 1060 GLN   B CG    1 
ATOM   3304 C  CD    . GLN   B 1 150 ? 5.624   -7.572  71.359  1.00 48.32  ? 1060 GLN   B CD    1 
ATOM   3305 O  OE1   . GLN   B 1 150 ? 6.083   -8.277  70.456  1.00 48.94  ? 1060 GLN   B OE1   1 
ATOM   3306 N  NE2   . GLN   B 1 150 ? 4.563   -6.781  71.189  1.00 52.67  ? 1060 GLN   B NE2   1 
ATOM   3307 N  N     . GLY   B 1 151 ? 5.981   -7.034  75.759  1.00 36.70  ? 1061 GLY   B N     1 
ATOM   3308 C  CA    . GLY   B 1 151 ? 4.961   -6.239  76.402  1.00 36.64  ? 1061 GLY   B CA    1 
ATOM   3309 C  C     . GLY   B 1 151 ? 4.941   -6.324  77.905  1.00 38.01  ? 1061 GLY   B C     1 
ATOM   3310 O  O     . GLY   B 1 151 ? 3.998   -5.811  78.529  1.00 40.34  ? 1061 GLY   B O     1 
ATOM   3311 N  N     . THR   B 1 152 ? 5.935   -6.981  78.493  1.00 33.64  ? 1062 THR   B N     1 
ATOM   3312 C  CA    . THR   B 1 152 ? 6.120   -7.071  79.934  1.00 34.46  ? 1062 THR   B CA    1 
ATOM   3313 C  C     . THR   B 1 152 ? 6.709   -5.770  80.478  1.00 35.22  ? 1062 THR   B C     1 
ATOM   3314 O  O     . THR   B 1 152 ? 7.552   -5.133  79.843  1.00 34.80  ? 1062 THR   B O     1 
ATOM   3315 C  CB    . THR   B 1 152 ? 7.076   -8.234  80.266  1.00 35.19  ? 1062 THR   B CB    1 
ATOM   3316 O  OG1   . THR   B 1 152 ? 6.607   -9.450  79.690  1.00 36.23  ? 1062 THR   B OG1   1 
ATOM   3317 C  CG2   . THR   B 1 152 ? 7.242   -8.437  81.754  1.00 37.12  ? 1062 THR   B CG2   1 
ATOM   3318 N  N     . PHE   B 1 153 ? 6.295   -5.403  81.683  1.00 33.44  ? 1063 PHE   B N     1 
ATOM   3319 C  CA    . PHE   B 1 153 ? 6.886   -4.251  82.344  1.00 32.85  ? 1063 PHE   B CA    1 
ATOM   3320 C  C     . PHE   B 1 153 ? 8.282   -4.588  82.857  1.00 32.38  ? 1063 PHE   B C     1 
ATOM   3321 O  O     . PHE   B 1 153 ? 8.505   -5.653  83.443  1.00 32.49  ? 1063 PHE   B O     1 
ATOM   3322 C  CB    . PHE   B 1 153 ? 6.007   -3.807  83.502  1.00 28.29  ? 1063 PHE   B CB    1 
ATOM   3323 C  CG    . PHE   B 1 153 ? 6.655   -2.786  84.388  1.00 27.58  ? 1063 PHE   B CG    1 
ATOM   3324 C  CD1   . PHE   B 1 153 ? 6.910   -1.513  83.924  1.00 27.64  ? 1063 PHE   B CD1   1 
ATOM   3325 C  CD2   . PHE   B 1 153 ? 6.980   -3.090  85.694  1.00 27.06  ? 1063 PHE   B CD2   1 
ATOM   3326 C  CE1   . PHE   B 1 153 ? 7.491   -0.566  84.749  1.00 27.17  ? 1063 PHE   B CE1   1 
ATOM   3327 C  CE2   . PHE   B 1 153 ? 7.548   -2.155  86.511  1.00 26.79  ? 1063 PHE   B CE2   1 
ATOM   3328 C  CZ    . PHE   B 1 153 ? 7.809   -0.890  86.041  1.00 26.65  ? 1063 PHE   B CZ    1 
ATOM   3329 N  N     . ILE   B 1 154 ? 9.225   -3.665  82.658  1.00 30.06  ? 1064 ILE   B N     1 
ATOM   3330 C  CA    . ILE   B 1 154 ? 10.612  -3.923  83.044  1.00 29.21  ? 1064 ILE   B CA    1 
ATOM   3331 C  C     . ILE   B 1 154 ? 10.908  -3.215  84.355  1.00 28.32  ? 1064 ILE   B C     1 
ATOM   3332 O  O     . ILE   B 1 154 ? 11.061  -3.850  85.403  1.00 28.06  ? 1064 ILE   B O     1 
ATOM   3333 C  CB    . ILE   B 1 154 ? 11.593  -3.483  81.945  1.00 29.96  ? 1064 ILE   B CB    1 
ATOM   3334 C  CG1   . ILE   B 1 154 ? 11.226  -4.147  80.614  1.00 31.77  ? 1064 ILE   B CG1   1 
ATOM   3335 C  CG2   . ILE   B 1 154 ? 13.037  -3.822  82.351  1.00 32.63  ? 1064 ILE   B CG2   1 
ATOM   3336 C  CD1   . ILE   B 1 154 ? 11.277  -5.667  80.641  1.00 31.68  ? 1064 ILE   B CD1   1 
ATOM   3337 N  N     . CYS   B 1 155 ? 10.950  -1.893  84.305  1.00 28.07  ? 1065 CYS   B N     1 
ATOM   3338 C  CA    . CYS   B 1 155 ? 11.275  -1.055  85.450  1.00 28.06  ? 1065 CYS   B CA    1 
ATOM   3339 C  C     . CYS   B 1 155 ? 10.874  0.358   85.075  1.00 27.50  ? 1065 CYS   B C     1 
ATOM   3340 O  O     . CYS   B 1 155 ? 10.493  0.619   83.934  1.00 28.61  ? 1065 CYS   B O     1 
ATOM   3341 C  CB    . CYS   B 1 155 ? 12.771  -1.121  85.773  1.00 31.64  ? 1065 CYS   B CB    1 
ATOM   3342 S  SG    . CYS   B 1 155 ? 13.735  -0.712  84.303  1.00 29.87  ? 1065 CYS   B SG    1 
ATOM   3343 N  N     . GLU   B 1 156 ? 11.000  1.272   86.030  1.00 27.16  ? 1066 GLU   B N     1 
ATOM   3344 C  CA    . GLU   B 1 156 ? 10.625  2.675   85.842  1.00 28.18  ? 1066 GLU   B CA    1 
ATOM   3345 C  C     . GLU   B 1 156 ? 11.871  3.552   85.750  1.00 27.80  ? 1066 GLU   B C     1 
ATOM   3346 O  O     . GLU   B 1 156 ? 12.841  3.333   86.482  1.00 27.69  ? 1066 GLU   B O     1 
ATOM   3347 C  CB    . GLU   B 1 156 ? 9.732   3.150   87.000  1.00 26.88  ? 1066 GLU   B CB    1 
ATOM   3348 C  CG    . GLU   B 1 156 ? 9.357   4.643   87.007  1.00 27.23  ? 1066 GLU   B CG    1 
ATOM   3349 C  CD    . GLU   B 1 156 ? 8.535   5.035   88.239  1.00 29.27  ? 1066 GLU   B CD    1 
ATOM   3350 O  OE1   . GLU   B 1 156 ? 8.204   4.125   89.057  1.00 27.55  ? 1066 GLU   B OE1   1 
ATOM   3351 O  OE2   . GLU   B 1 156 ? 8.212   6.248   88.388  1.00 27.34  ? 1066 GLU   B OE2   1 
ATOM   3352 N  N     . TYR   B 1 157 ? 11.852  4.541   84.850  1.00 29.01  ? 1067 TYR   B N     1 
ATOM   3353 C  CA    . TYR   B 1 157 ? 12.940  5.529   84.801  1.00 30.13  ? 1067 TYR   B CA    1 
ATOM   3354 C  C     . TYR   B 1 157 ? 12.824  6.456   86.003  1.00 30.48  ? 1067 TYR   B C     1 
ATOM   3355 O  O     . TYR   B 1 157 ? 12.077  7.439   85.970  1.00 29.30  ? 1067 TYR   B O     1 
ATOM   3356 C  CB    . TYR   B 1 157 ? 12.916  6.346   83.508  1.00 30.08  ? 1067 TYR   B CB    1 
ATOM   3357 C  CG    . TYR   B 1 157 ? 14.228  7.051   83.256  1.00 32.87  ? 1067 TYR   B CG    1 
ATOM   3358 C  CD1   . TYR   B 1 157 ? 14.520  8.252   83.890  1.00 32.96  ? 1067 TYR   B CD1   1 
ATOM   3359 C  CD2   . TYR   B 1 157 ? 15.193  6.502   82.418  1.00 31.28  ? 1067 TYR   B CD2   1 
ATOM   3360 C  CE1   . TYR   B 1 157 ? 15.721  8.888   83.691  1.00 33.30  ? 1067 TYR   B CE1   1 
ATOM   3361 C  CE2   . TYR   B 1 157 ? 16.435  7.143   82.208  1.00 32.02  ? 1067 TYR   B CE2   1 
ATOM   3362 C  CZ    . TYR   B 1 157 ? 16.676  8.328   82.852  1.00 35.96  ? 1067 TYR   B CZ    1 
ATOM   3363 O  OH    . TYR   B 1 157 ? 17.851  9.000   82.661  1.00 34.17  ? 1067 TYR   B OH    1 
ATOM   3364 N  N     . VAL   B 1 158 ? 13.590  6.170   87.056  1.00 28.63  ? 1068 VAL   B N     1 
ATOM   3365 C  CA    . VAL   B 1 158 ? 13.487  6.856   88.340  1.00 28.63  ? 1068 VAL   B CA    1 
ATOM   3366 C  C     . VAL   B 1 158 ? 14.659  7.817   88.502  1.00 30.87  ? 1068 VAL   B C     1 
ATOM   3367 O  O     . VAL   B 1 158 ? 15.787  7.509   88.100  1.00 29.60  ? 1068 VAL   B O     1 
ATOM   3368 C  CB    . VAL   B 1 158 ? 13.453  5.833   89.492  1.00 28.00  ? 1068 VAL   B CB    1 
ATOM   3369 C  CG1   . VAL   B 1 158 ? 13.625  6.511   90.837  1.00 28.30  ? 1068 VAL   B CG1   1 
ATOM   3370 C  CG2   . VAL   B 1 158 ? 12.179  5.001   89.446  1.00 27.68  ? 1068 VAL   B CG2   1 
ATOM   3371 N  N     . GLY   B 1 159 ? 14.394  8.968   89.116  1.00 29.94  ? 1069 GLY   B N     1 
ATOM   3372 C  CA    . GLY   B 1 159 ? 15.434  9.909   89.459  1.00 30.83  ? 1069 GLY   B CA    1 
ATOM   3373 C  C     . GLY   B 1 159 ? 14.921  11.182  90.101  1.00 34.17  ? 1069 GLY   B C     1 
ATOM   3374 O  O     . GLY   B 1 159 ? 13.897  11.192  90.802  1.00 32.66  ? 1069 GLY   B O     1 
ATOM   3375 N  N     . GLU   B 1 160 ? 15.641  12.270  89.850  1.00 35.42  ? 1070 GLU   B N     1 
ATOM   3376 C  CA    . GLU   B 1 160 ? 15.414  13.550  90.496  1.00 33.91  ? 1070 GLU   B CA    1 
ATOM   3377 C  C     . GLU   B 1 160 ? 14.518  14.393  89.597  1.00 34.60  ? 1070 GLU   B C     1 
ATOM   3378 O  O     . GLU   B 1 160 ? 14.868  14.667  88.441  1.00 35.13  ? 1070 GLU   B O     1 
ATOM   3379 C  CB    . GLU   B 1 160 ? 16.750  14.252  90.755  1.00 35.01  ? 1070 GLU   B CB    1 
ATOM   3380 C  CG    . GLU   B 1 160 ? 16.641  15.668  91.306  1.00 36.57  ? 1070 GLU   B CG    1 
ATOM   3381 C  CD    . GLU   B 1 160 ? 17.998  16.385  91.356  1.00 37.84  ? 1070 GLU   B CD    1 
ATOM   3382 O  OE1   . GLU   B 1 160 ? 19.000  15.775  90.957  1.00 37.42  ? 1070 GLU   B OE1   1 
ATOM   3383 O  OE2   . GLU   B 1 160 ? 18.058  17.555  91.788  1.00 39.37  ? 1070 GLU   B OE2   1 
ATOM   3384 N  N     . LEU   B 1 161 ? 13.359  14.783  90.116  1.00 34.72  ? 1071 LEU   B N     1 
ATOM   3385 C  CA    . LEU   B 1 161 ? 12.425  15.587  89.342  1.00 35.51  ? 1071 LEU   B CA    1 
ATOM   3386 C  C     . LEU   B 1 161 ? 12.910  17.032  89.312  1.00 37.38  ? 1071 LEU   B C     1 
ATOM   3387 O  O     . LEU   B 1 161 ? 13.027  17.676  90.358  1.00 38.15  ? 1071 LEU   B O     1 
ATOM   3388 C  CB    . LEU   B 1 161 ? 11.021  15.475  89.938  1.00 38.51  ? 1071 LEU   B CB    1 
ATOM   3389 C  CG    . LEU   B 1 161 ? 10.441  14.057  89.959  1.00 33.37  ? 1071 LEU   B CG    1 
ATOM   3390 C  CD1   . LEU   B 1 161 ? 9.278   13.981  90.897  1.00 37.68  ? 1071 LEU   B CD1   1 
ATOM   3391 C  CD2   . LEU   B 1 161 ? 10.014  13.643  88.568  1.00 33.08  ? 1071 LEU   B CD2   1 
ATOM   3392 N  N     . ILE   B 1 162 ? 13.190  17.542  88.110  1.00 38.31  ? 1072 ILE   B N     1 
ATOM   3393 C  CA    . ILE   B 1 162 ? 13.724  18.885  87.918  1.00 40.77  ? 1072 ILE   B CA    1 
ATOM   3394 C  C     . ILE   B 1 162 ? 12.984  19.561  86.775  1.00 41.48  ? 1072 ILE   B C     1 
ATOM   3395 O  O     . ILE   B 1 162 ? 12.316  18.915  85.971  1.00 51.34  ? 1072 ILE   B O     1 
ATOM   3396 C  CB    . ILE   B 1 162 ? 15.251  18.894  87.634  1.00 40.71  ? 1072 ILE   B CB    1 
ATOM   3397 C  CG1   . ILE   B 1 162 ? 15.547  18.305  86.248  1.00 40.37  ? 1072 ILE   B CG1   1 
ATOM   3398 C  CG2   . ILE   B 1 162 ? 16.021  18.191  88.740  1.00 39.69  ? 1072 ILE   B CG2   1 
ATOM   3399 C  CD1   . ILE   B 1 162 ? 16.995  18.396  85.825  1.00 40.99  ? 1072 ILE   B CD1   1 
ATOM   3400 N  N     . SER   B 1 163 ? 13.142  20.879  86.694  1.00 43.55  ? 1073 SER   B N     1 
ATOM   3401 C  CA    . SER   B 1 163 ? 12.405  21.685  85.732  1.00 48.83  ? 1073 SER   B CA    1 
ATOM   3402 C  C     . SER   B 1 163 ? 13.143  21.761  84.401  1.00 52.59  ? 1073 SER   B C     1 
ATOM   3403 O  O     . SER   B 1 163 ? 14.343  21.483  84.308  1.00 51.83  ? 1073 SER   B O     1 
ATOM   3404 C  CB    . SER   B 1 163 ? 12.180  23.093  86.268  1.00 50.68  ? 1073 SER   B CB    1 
ATOM   3405 O  OG    . SER   B 1 163 ? 13.300  23.915  86.002  1.00 49.01  ? 1073 SER   B OG    1 
ATOM   3406 N  N     . ASP   B 1 164 ? 12.401  22.148  83.358  1.00 53.53  ? 1074 ASP   B N     1 
ATOM   3407 C  CA    . ASP   B 1 164 ? 13.026  22.346  82.055  1.00 58.67  ? 1074 ASP   B CA    1 
ATOM   3408 C  C     . ASP   B 1 164 ? 14.167  23.348  82.155  1.00 59.31  ? 1074 ASP   B C     1 
ATOM   3409 O  O     . ASP   B 1 164 ? 15.221  23.167  81.533  1.00 57.60  ? 1074 ASP   B O     1 
ATOM   3410 C  CB    . ASP   B 1 164 ? 11.986  22.804  81.033  1.00 65.59  ? 1074 ASP   B CB    1 
ATOM   3411 C  CG    . ASP   B 1 164 ? 12.505  22.754  79.607  1.00 70.64  ? 1074 ASP   B CG    1 
ATOM   3412 O  OD1   . ASP   B 1 164 ? 12.923  21.657  79.165  1.00 71.75  ? 1074 ASP   B OD1   1 
ATOM   3413 O  OD2   . ASP   B 1 164 ? 12.483  23.809  78.928  1.00 70.03  ? 1074 ASP   B OD2   1 
ATOM   3414 N  N     . ALA   B 1 165 ? 13.983  24.393  82.971  1.00 57.64  ? 1075 ALA   B N     1 
ATOM   3415 C  CA    . ALA   B 1 165 ? 15.043  25.376  83.190  1.00 54.81  ? 1075 ALA   B CA    1 
ATOM   3416 C  C     . ALA   B 1 165 ? 16.252  24.757  83.882  1.00 54.80  ? 1075 ALA   B C     1 
ATOM   3417 O  O     . ALA   B 1 165 ? 17.396  25.030  83.503  1.00 59.15  ? 1075 ALA   B O     1 
ATOM   3418 C  CB    . ALA   B 1 165 ? 14.512  26.547  84.015  1.00 55.23  ? 1075 ALA   B CB    1 
ATOM   3419 N  N     . GLU   B 1 166 ? 16.017  23.944  84.916  1.00 50.02  ? 1076 GLU   B N     1 
ATOM   3420 C  CA    . GLU   B 1 166 ? 17.112  23.295  85.627  1.00 53.32  ? 1076 GLU   B CA    1 
ATOM   3421 C  C     . GLU   B 1 166 ? 17.873  22.329  84.726  1.00 51.85  ? 1076 GLU   B C     1 
ATOM   3422 O  O     . GLU   B 1 166 ? 19.079  22.125  84.914  1.00 54.94  ? 1076 GLU   B O     1 
ATOM   3423 C  CB    . GLU   B 1 166 ? 16.565  22.586  86.869  1.00 46.99  ? 1076 GLU   B CB    1 
ATOM   3424 C  CG    . GLU   B 1 166 ? 17.539  21.666  87.588  1.00 45.50  ? 1076 GLU   B CG    1 
ATOM   3425 C  CD    . GLU   B 1 166 ? 18.664  22.400  88.275  1.00 49.17  ? 1076 GLU   B CD    1 
ATOM   3426 O  OE1   . GLU   B 1 166 ? 18.392  23.142  89.242  1.00 53.01  ? 1076 GLU   B OE1   1 
ATOM   3427 O  OE2   . GLU   B 1 166 ? 19.828  22.228  87.849  1.00 51.39  ? 1076 GLU   B OE2   1 
ATOM   3428 N  N     . ALA   B 1 167 ? 17.202  21.757  83.725  1.00 53.98  ? 1077 ALA   B N     1 
ATOM   3429 C  CA    . ALA   B 1 167 ? 17.878  20.835  82.817  1.00 58.07  ? 1077 ALA   B CA    1 
ATOM   3430 C  C     . ALA   B 1 167 ? 18.811  21.582  81.871  1.00 62.16  ? 1077 ALA   B C     1 
ATOM   3431 O  O     . ALA   B 1 167 ? 19.888  21.079  81.531  1.00 60.57  ? 1077 ALA   B O     1 
ATOM   3432 C  CB    . ALA   B 1 167 ? 16.847  20.012  82.039  1.00 53.38  ? 1077 ALA   B CB    1 
ATOM   3433 N  N     . ASP   B 1 168 ? 18.409  22.788  81.448  1.00 72.07  ? 1078 ASP   B N     1 
ATOM   3434 C  CA    . ASP   B 1 168 ? 19.267  23.662  80.650  1.00 69.54  ? 1078 ASP   B CA    1 
ATOM   3435 C  C     . ASP   B 1 168 ? 20.587  23.953  81.341  1.00 68.63  ? 1078 ASP   B C     1 
ATOM   3436 O  O     . ASP   B 1 168 ? 21.607  24.145  80.673  1.00 72.44  ? 1078 ASP   B O     1 
ATOM   3437 C  CB    . ASP   B 1 168 ? 18.553  24.986  80.371  1.00 73.73  ? 1078 ASP   B CB    1 
ATOM   3438 C  CG    . ASP   B 1 168 ? 17.509  24.871  79.288  1.00 80.00  ? 1078 ASP   B CG    1 
ATOM   3439 O  OD1   . ASP   B 1 168 ? 17.892  24.874  78.101  1.00 89.18  ? 1078 ASP   B OD1   1 
ATOM   3440 O  OD2   . ASP   B 1 168 ? 16.307  24.770  79.614  1.00 78.85  ? 1078 ASP   B OD2   1 
ATOM   3441 N  N     . VAL   B 1 169 ? 20.584  24.001  82.672  1.00 63.16  ? 1079 VAL   B N     1 
ATOM   3442 C  CA    . VAL   B 1 169 ? 21.758  24.448  83.412  1.00 60.62  ? 1079 VAL   B CA    1 
ATOM   3443 C  C     . VAL   B 1 169 ? 22.748  23.310  83.648  1.00 60.38  ? 1079 VAL   B C     1 
ATOM   3444 O  O     . VAL   B 1 169 ? 23.956  23.550  83.787  1.00 63.35  ? 1079 VAL   B O     1 
ATOM   3445 C  CB    . VAL   B 1 169 ? 21.296  25.096  84.732  1.00 61.45  ? 1079 VAL   B CB    1 
ATOM   3446 C  CG1   . VAL   B 1 169 ? 22.482  25.515  85.589  1.00 68.23  ? 1079 VAL   B CG1   1 
ATOM   3447 C  CG2   . VAL   B 1 169 ? 20.435  26.301  84.430  1.00 59.91  ? 1079 VAL   B CG2   1 
ATOM   3448 N  N     . ARG   B 1 170 ? 22.279  22.067  83.666  1.00 56.88  ? 1080 ARG   B N     1 
ATOM   3449 C  CA    . ARG   B 1 170 ? 23.103  20.973  84.146  1.00 56.72  ? 1080 ARG   B CA    1 
ATOM   3450 C  C     . ARG   B 1 170 ? 24.125  20.544  83.099  1.00 55.58  ? 1080 ARG   B C     1 
ATOM   3451 O  O     . ARG   B 1 170 ? 23.782  20.294  81.939  1.00 55.78  ? 1080 ARG   B O     1 
ATOM   3452 C  CB    . ARG   B 1 170 ? 22.213  19.814  84.573  1.00 52.19  ? 1080 ARG   B CB    1 
ATOM   3453 C  CG    . ARG   B 1 170 ? 21.480  20.151  85.863  1.00 55.87  ? 1080 ARG   B CG    1 
ATOM   3454 C  CD    . ARG   B 1 170 ? 20.895  18.940  86.575  1.00 45.92  ? 1080 ARG   B CD    1 
ATOM   3455 N  NE    . ARG   B 1 170 ? 20.448  19.306  87.914  1.00 45.51  ? 1080 ARG   B NE    1 
ATOM   3456 C  CZ    . ARG   B 1 170 ? 20.030  18.449  88.835  1.00 42.98  ? 1080 ARG   B CZ    1 
ATOM   3457 N  NH1   . ARG   B 1 170 ? 19.997  17.145  88.605  1.00 40.58  ? 1080 ARG   B NH1   1 
ATOM   3458 N  NH2   . ARG   B 1 170 ? 19.631  18.913  90.016  1.00 43.12  ? 1080 ARG   B NH2   1 
ATOM   3459 N  N     . GLU   B 1 171 ? 25.392  20.479  83.516  1.00 59.63  ? 1081 GLU   B N     1 
ATOM   3460 C  CA    . GLU   B 1 171 ? 26.489  20.211  82.596  1.00 58.17  ? 1081 GLU   B CA    1 
ATOM   3461 C  C     . GLU   B 1 171 ? 26.621  18.735  82.259  1.00 60.14  ? 1081 GLU   B C     1 
ATOM   3462 O  O     . GLU   B 1 171 ? 27.218  18.405  81.229  1.00 56.61  ? 1081 GLU   B O     1 
ATOM   3463 C  CB    . GLU   B 1 171 ? 27.805  20.730  83.182  1.00 61.15  ? 1081 GLU   B CB    1 
ATOM   3464 N  N     . ASP   B 1 172 ? 26.068  17.846  83.085  1.00 58.15  ? 1082 ASP   B N     1 
ATOM   3465 C  CA    . ASP   B 1 172 ? 26.121  16.403  82.850  1.00 60.14  ? 1082 ASP   B CA    1 
ATOM   3466 C  C     . ASP   B 1 172 ? 24.712  15.934  82.490  1.00 57.70  ? 1082 ASP   B C     1 
ATOM   3467 O  O     . ASP   B 1 172 ? 23.896  15.627  83.363  1.00 58.40  ? 1082 ASP   B O     1 
ATOM   3468 C  CB    . ASP   B 1 172 ? 26.671  15.656  84.067  1.00 58.03  ? 1082 ASP   B CB    1 
ATOM   3469 C  CG    . ASP   B 1 172 ? 26.918  14.176  83.786  1.00 58.41  ? 1082 ASP   B CG    1 
ATOM   3470 O  OD1   . ASP   B 1 172 ? 26.321  13.619  82.831  1.00 55.43  ? 1082 ASP   B OD1   1 
ATOM   3471 O  OD2   . ASP   B 1 172 ? 27.714  13.565  84.532  1.00 58.44  ? 1082 ASP   B OD2   1 
ATOM   3472 N  N     . ASP   B 1 173 ? 24.436  15.874  81.187  1.00 58.31  ? 1083 ASP   B N     1 
ATOM   3473 C  CA    . ASP   B 1 173 ? 23.147  15.433  80.674  1.00 55.94  ? 1083 ASP   B CA    1 
ATOM   3474 C  C     . ASP   B 1 173 ? 23.201  14.014  80.128  1.00 51.96  ? 1083 ASP   B C     1 
ATOM   3475 O  O     . ASP   B 1 173 ? 22.476  13.679  79.187  1.00 54.09  ? 1083 ASP   B O     1 
ATOM   3476 C  CB    . ASP   B 1 173 ? 22.637  16.401  79.608  1.00 58.35  ? 1083 ASP   B CB    1 
ATOM   3477 C  CG    . ASP   B 1 173 ? 23.676  16.703  78.552  1.00 63.68  ? 1083 ASP   B CG    1 
ATOM   3478 O  OD1   . ASP   B 1 173 ? 24.859  16.332  78.742  1.00 67.23  ? 1083 ASP   B OD1   1 
ATOM   3479 O  OD2   . ASP   B 1 173 ? 23.314  17.319  77.525  1.00 64.87  ? 1083 ASP   B OD2   1 
ATOM   3480 N  N     . SER   B 1 174 ? 24.033  13.164  80.718  1.00 48.86  ? 1084 SER   B N     1 
ATOM   3481 C  CA    . SER   B 1 174 ? 24.105  11.778  80.292  1.00 47.08  ? 1084 SER   B CA    1 
ATOM   3482 C  C     . SER   B 1 174 ? 22.975  10.924  80.856  1.00 38.47  ? 1084 SER   B C     1 
ATOM   3483 O  O     . SER   B 1 174 ? 22.826  9.777   80.431  1.00 37.25  ? 1084 SER   B O     1 
ATOM   3484 C  CB    . SER   B 1 174 ? 25.462  11.177  80.691  1.00 41.74  ? 1084 SER   B CB    1 
ATOM   3485 O  OG    . SER   B 1 174 ? 26.540  12.045  80.356  1.00 50.28  ? 1084 SER   B OG    1 
ATOM   3486 N  N     . TYR   B 1 175 ? 22.169  11.452  81.783  1.00 41.76  ? 1085 TYR   B N     1 
ATOM   3487 C  CA    . TYR   B 1 175 ? 21.129  10.679  82.463  1.00 39.00  ? 1085 TYR   B CA    1 
ATOM   3488 C  C     . TYR   B 1 175 ? 19.808  11.448  82.521  1.00 39.56  ? 1085 TYR   B C     1 
ATOM   3489 O  O     . TYR   B 1 175 ? 18.972  11.231  83.414  1.00 34.04  ? 1085 TYR   B O     1 
ATOM   3490 C  CB    . TYR   B 1 175 ? 21.602  10.281  83.863  1.00 34.04  ? 1085 TYR   B CB    1 
ATOM   3491 C  CG    . TYR   B 1 175 ? 22.923  9.519   83.853  1.00 36.87  ? 1085 TYR   B CG    1 
ATOM   3492 C  CD1   . TYR   B 1 175 ? 24.142  10.191  83.903  1.00 37.11  ? 1085 TYR   B CD1   1 
ATOM   3493 C  CD2   . TYR   B 1 175 ? 22.950  8.120   83.791  1.00 34.56  ? 1085 TYR   B CD2   1 
ATOM   3494 C  CE1   . TYR   B 1 175 ? 25.348  9.497   83.892  1.00 37.00  ? 1085 TYR   B CE1   1 
ATOM   3495 C  CE2   . TYR   B 1 175 ? 24.156  7.417   83.791  1.00 34.16  ? 1085 TYR   B CE2   1 
ATOM   3496 C  CZ    . TYR   B 1 175 ? 25.348  8.110   83.836  1.00 35.64  ? 1085 TYR   B CZ    1 
ATOM   3497 O  OH    . TYR   B 1 175 ? 26.551  7.409   83.828  1.00 36.70  ? 1085 TYR   B OH    1 
ATOM   3498 N  N     . LEU   B 1 176 ? 19.584  12.324  81.554  1.00 40.53  ? 1086 LEU   B N     1 
ATOM   3499 C  CA    . LEU   B 1 176 ? 18.483  13.274  81.607  1.00 40.51  ? 1086 LEU   B CA    1 
ATOM   3500 C  C     . LEU   B 1 176 ? 17.360  12.786  80.698  1.00 40.97  ? 1086 LEU   B C     1 
ATOM   3501 O  O     . LEU   B 1 176 ? 17.519  12.715  79.476  1.00 43.16  ? 1086 LEU   B O     1 
ATOM   3502 C  CB    . LEU   B 1 176 ? 18.970  14.669  81.221  1.00 45.13  ? 1086 LEU   B CB    1 
ATOM   3503 C  CG    . LEU   B 1 176 ? 18.058  15.872  81.433  1.00 44.48  ? 1086 LEU   B CG    1 
ATOM   3504 C  CD1   . LEU   B 1 176 ? 17.088  15.648  82.552  1.00 42.71  ? 1086 LEU   B CD1   1 
ATOM   3505 C  CD2   . LEU   B 1 176 ? 18.905  17.086  81.739  1.00 49.62  ? 1086 LEU   B CD2   1 
ATOM   3506 N  N     . PHE   B 1 177 ? 16.233  12.441  81.299  1.00 37.16  ? 1087 PHE   B N     1 
ATOM   3507 C  CA    . PHE   B 1 177 ? 15.055  12.022  80.560  1.00 43.20  ? 1087 PHE   B CA    1 
ATOM   3508 C  C     . PHE   B 1 177 ? 14.093  13.196  80.469  1.00 40.27  ? 1087 PHE   B C     1 
ATOM   3509 O  O     . PHE   B 1 177 ? 13.774  13.828  81.481  1.00 39.72  ? 1087 PHE   B O     1 
ATOM   3510 C  CB    . PHE   B 1 177 ? 14.382  10.827  81.232  1.00 41.08  ? 1087 PHE   B CB    1 
ATOM   3511 C  CG    . PHE   B 1 177 ? 13.471  10.071  80.335  1.00 41.20  ? 1087 PHE   B CG    1 
ATOM   3512 C  CD1   . PHE   B 1 177 ? 12.195  10.546  80.059  1.00 39.21  ? 1087 PHE   B CD1   1 
ATOM   3513 C  CD2   . PHE   B 1 177 ? 13.872  8.871   79.776  1.00 38.75  ? 1087 PHE   B CD2   1 
ATOM   3514 C  CE1   . PHE   B 1 177 ? 11.353  9.857   79.228  1.00 39.76  ? 1087 PHE   B CE1   1 
ATOM   3515 C  CE2   . PHE   B 1 177 ? 13.014  8.169   78.947  1.00 36.68  ? 1087 PHE   B CE2   1 
ATOM   3516 C  CZ    . PHE   B 1 177 ? 11.754  8.664   78.678  1.00 42.88  ? 1087 PHE   B CZ    1 
ATOM   3517 N  N     . ASP   B 1 178 ? 13.663  13.504  79.258  1.00 41.77  ? 1088 ASP   B N     1 
ATOM   3518 C  CA    . ASP   B 1 178 ? 12.741  14.608  79.028  1.00 50.94  ? 1088 ASP   B CA    1 
ATOM   3519 C  C     . ASP   B 1 178 ? 11.320  14.050  79.021  1.00 48.01  ? 1088 ASP   B C     1 
ATOM   3520 O  O     . ASP   B 1 178 ? 10.942  13.307  78.108  1.00 45.63  ? 1088 ASP   B O     1 
ATOM   3521 C  CB    . ASP   B 1 178 ? 13.086  15.318  77.722  1.00 53.45  ? 1088 ASP   B CB    1 
ATOM   3522 C  CG    . ASP   B 1 178 ? 12.563  16.714  77.678  1.00 59.26  ? 1088 ASP   B CG    1 
ATOM   3523 O  OD1   . ASP   B 1 178 ? 11.347  16.890  77.897  1.00 63.68  ? 1088 ASP   B OD1   1 
ATOM   3524 O  OD2   . ASP   B 1 178 ? 13.362  17.639  77.435  1.00 63.39  ? 1088 ASP   B OD2   1 
ATOM   3525 N  N     . LEU   B 1 179 ? 10.542  14.379  80.057  1.00 51.55  ? 1089 LEU   B N     1 
ATOM   3526 C  CA    . LEU   B 1 179 ? 9.158   13.910  80.102  1.00 55.98  ? 1089 LEU   B CA    1 
ATOM   3527 C  C     . LEU   B 1 179 ? 8.348   14.470  78.938  1.00 62.23  ? 1089 LEU   B C     1 
ATOM   3528 O  O     . LEU   B 1 179 ? 7.488   13.773  78.390  1.00 56.74  ? 1089 LEU   B O     1 
ATOM   3529 C  CB    . LEU   B 1 179 ? 8.507   14.267  81.443  1.00 54.85  ? 1089 LEU   B CB    1 
ATOM   3530 C  CG    . LEU   B 1 179 ? 9.208   13.707  82.686  1.00 41.46  ? 1089 LEU   B CG    1 
ATOM   3531 C  CD1   . LEU   B 1 179 ? 8.394   13.893  83.946  1.00 41.45  ? 1089 LEU   B CD1   1 
ATOM   3532 C  CD2   . LEU   B 1 179 ? 9.592   12.243  82.500  1.00 39.96  ? 1089 LEU   B CD2   1 
ATOM   3533 N  N     . ASP   B 1 180 ? 8.626   15.721  78.541  1.00 68.99  ? 1090 ASP   B N     1 
ATOM   3534 C  CA    . ASP   B 1 180 ? 8.045   16.395  77.378  1.00 79.08  ? 1090 ASP   B CA    1 
ATOM   3535 C  C     . ASP   B 1 180 ? 6.572   16.738  77.599  1.00 94.37  ? 1090 ASP   B C     1 
ATOM   3536 O  O     . ASP   B 1 180 ? 5.700   16.313  76.832  1.00 93.65  ? 1090 ASP   B O     1 
ATOM   3537 C  CB    . ASP   B 1 180 ? 8.222   15.549  76.111  1.00 74.62  ? 1090 ASP   B CB    1 
ATOM   3538 C  CG    . ASP   B 1 180 ? 8.094   16.366  74.829  1.00 87.79  ? 1090 ASP   B CG    1 
ATOM   3539 O  OD1   . ASP   B 1 180 ? 7.508   17.474  74.869  1.00 93.28  ? 1090 ASP   B OD1   1 
ATOM   3540 O  OD2   . ASP   B 1 180 ? 8.576   15.890  73.776  1.00 89.07  ? 1090 ASP   B OD2   1 
ATOM   3541 N  N     . ASN   B 1 181 ? 6.293   17.537  78.629  1.00 118.47 ? 1091 ASN   B N     1 
ATOM   3542 C  CA    . ASN   B 1 181 ? 4.917   17.842  79.012  1.00 123.81 ? 1091 ASN   B CA    1 
ATOM   3543 C  C     . ASN   B 1 181 ? 4.223   18.664  77.930  1.00 125.85 ? 1091 ASN   B C     1 
ATOM   3544 O  O     . ASN   B 1 181 ? 4.615   19.803  77.653  1.00 130.69 ? 1091 ASN   B O     1 
ATOM   3545 C  CB    . ASN   B 1 181 ? 4.892   18.591  80.344  1.00 126.69 ? 1091 ASN   B CB    1 
ATOM   3546 C  CG    . ASN   B 1 181 ? 5.596   17.833  81.459  1.00 123.55 ? 1091 ASN   B CG    1 
ATOM   3547 O  OD1   . ASN   B 1 181 ? 6.636   18.264  81.957  1.00 120.27 ? 1091 ASN   B OD1   1 
ATOM   3548 N  ND2   . ASN   B 1 181 ? 5.025   16.706  81.862  1.00 124.64 ? 1091 ASN   B ND2   1 
ATOM   3549 N  N     . LYS   B 1 182 ? 3.177   18.089  77.331  1.00 116.96 ? 1092 LYS   B N     1 
ATOM   3550 C  CA    . LYS   B 1 182 ? 2.407   18.820  76.330  1.00 115.64 ? 1092 LYS   B CA    1 
ATOM   3551 C  C     . LYS   B 1 182 ? 1.622   19.960  76.965  1.00 119.98 ? 1092 LYS   B C     1 
ATOM   3552 O  O     . LYS   B 1 182 ? 1.454   21.023  76.355  1.00 121.20 ? 1092 LYS   B O     1 
ATOM   3553 N  N     . ASP   B 1 183 ? 1.134   19.761  78.186  1.00 117.90 ? 1093 ASP   B N     1 
ATOM   3554 C  CA    . ASP   B 1 183 ? 0.413   20.798  78.913  1.00 113.90 ? 1093 ASP   B CA    1 
ATOM   3555 C  C     . ASP   B 1 183 ? 1.412   21.580  79.758  1.00 114.08 ? 1093 ASP   B C     1 
ATOM   3556 O  O     . ASP   B 1 183 ? 2.129   20.997  80.579  1.00 111.93 ? 1093 ASP   B O     1 
ATOM   3557 N  N     . GLY   B 1 184 ? 1.458   22.896  79.555  1.00 116.64 ? 1094 GLY   B N     1 
ATOM   3558 C  CA    . GLY   B 1 184 ? 2.404   23.712  80.291  1.00 113.37 ? 1094 GLY   B CA    1 
ATOM   3559 C  C     . GLY   B 1 184 ? 3.845   23.389  79.923  1.00 111.17 ? 1094 GLY   B C     1 
ATOM   3560 O  O     . GLY   B 1 184 ? 4.162   22.998  78.793  1.00 111.79 ? 1094 GLY   B O     1 
ATOM   3561 N  N     . GLU   B 1 185 ? 4.728   23.535  80.907  1.00 99.88  ? 1095 GLU   B N     1 
ATOM   3562 C  CA    . GLU   B 1 185 ? 6.162   23.434  80.687  1.00 91.73  ? 1095 GLU   B CA    1 
ATOM   3563 C  C     . GLU   B 1 185 ? 6.641   21.999  80.800  1.00 94.50  ? 1095 GLU   B C     1 
ATOM   3564 O  O     . GLU   B 1 185 ? 6.117   21.205  81.585  1.00 92.15  ? 1095 GLU   B O     1 
ATOM   3565 C  CB    . GLU   B 1 185 ? 6.923   24.297  81.690  1.00 88.35  ? 1095 GLU   B CB    1 
ATOM   3566 C  CG    . GLU   B 1 185 ? 6.555   25.761  81.635  1.00 88.24  ? 1095 GLU   B CG    1 
ATOM   3567 C  CD    . GLU   B 1 185 ? 6.587   26.399  83.001  1.00 84.72  ? 1095 GLU   B CD    1 
ATOM   3568 O  OE1   . GLU   B 1 185 ? 6.637   25.645  83.998  1.00 83.99  ? 1095 GLU   B OE1   1 
ATOM   3569 O  OE2   . GLU   B 1 185 ? 6.558   27.644  83.077  1.00 86.57  ? 1095 GLU   B OE2   1 
ATOM   3570 N  N     . VAL   B 1 186 ? 7.661   21.684  80.001  1.00 94.97  ? 1096 VAL   B N     1 
ATOM   3571 C  CA    . VAL   B 1 186 ? 8.348   20.403  80.101  1.00 92.27  ? 1096 VAL   B CA    1 
ATOM   3572 C  C     . VAL   B 1 186 ? 8.944   20.235  81.494  1.00 84.96  ? 1096 VAL   B C     1 
ATOM   3573 O  O     . VAL   B 1 186 ? 9.479   21.184  82.080  1.00 89.04  ? 1096 VAL   B O     1 
ATOM   3574 C  CB    . VAL   B 1 186 ? 9.436   20.321  79.014  1.00 92.23  ? 1096 VAL   B CB    1 
ATOM   3575 C  CG1   . VAL   B 1 186 ? 10.584  19.438  79.455  1.00 91.44  ? 1096 VAL   B CG1   1 
ATOM   3576 C  CG2   . VAL   B 1 186 ? 8.854   19.827  77.698  1.00 93.77  ? 1096 VAL   B CG2   1 
ATOM   3577 N  N     . TYR   B 1 187 ? 8.836   19.026  82.041  1.00 74.43  ? 1097 TYR   B N     1 
ATOM   3578 C  CA    . TYR   B 1 187 ? 9.632   18.618  83.188  1.00 65.03  ? 1097 TYR   B CA    1 
ATOM   3579 C  C     . TYR   B 1 187 ? 10.521  17.451  82.786  1.00 57.86  ? 1097 TYR   B C     1 
ATOM   3580 O  O     . TYR   B 1 187 ? 10.361  16.862  81.715  1.00 59.01  ? 1097 TYR   B O     1 
ATOM   3581 C  CB    . TYR   B 1 187 ? 8.760   18.258  84.393  1.00 59.05  ? 1097 TYR   B CB    1 
ATOM   3582 C  CG    . TYR   B 1 187 ? 8.352   19.486  85.165  1.00 62.88  ? 1097 TYR   B CG    1 
ATOM   3583 C  CD1   . TYR   B 1 187 ? 7.294   20.275  84.733  1.00 63.99  ? 1097 TYR   B CD1   1 
ATOM   3584 C  CD2   . TYR   B 1 187 ? 9.042   19.883  86.307  1.00 59.17  ? 1097 TYR   B CD2   1 
ATOM   3585 C  CE1   . TYR   B 1 187 ? 6.921   21.409  85.418  1.00 62.19  ? 1097 TYR   B CE1   1 
ATOM   3586 C  CE2   . TYR   B 1 187 ? 8.664   21.027  87.009  1.00 54.69  ? 1097 TYR   B CE2   1 
ATOM   3587 C  CZ    . TYR   B 1 187 ? 7.606   21.782  86.552  1.00 59.06  ? 1097 TYR   B CZ    1 
ATOM   3588 O  OH    . TYR   B 1 187 ? 7.209   22.924  87.212  1.00 68.52  ? 1097 TYR   B OH    1 
ATOM   3589 N  N     . CYS   B 1 188 ? 11.483  17.131  83.647  1.00 47.26  ? 1098 CYS   B N     1 
ATOM   3590 C  CA    . CYS   B 1 188 ? 12.508  16.165  83.291  1.00 43.50  ? 1098 CYS   B CA    1 
ATOM   3591 C  C     . CYS   B 1 188 ? 12.901  15.330  84.504  1.00 44.26  ? 1098 CYS   B C     1 
ATOM   3592 O  O     . CYS   B 1 188 ? 12.643  15.697  85.656  1.00 39.65  ? 1098 CYS   B O     1 
ATOM   3593 C  CB    . CYS   B 1 188 ? 13.762  16.846  82.714  1.00 44.02  ? 1098 CYS   B CB    1 
ATOM   3594 S  SG    . CYS   B 1 188 ? 13.526  18.110  81.420  1.00 48.24  ? 1098 CYS   B SG    1 
ATOM   3595 N  N     . ILE   B 1 189 ? 13.548  14.202  84.219  1.00 37.83  ? 1099 ILE   B N     1 
ATOM   3596 C  CA    . ILE   B 1 189 ? 14.085  13.312  85.232  1.00 35.44  ? 1099 ILE   B CA    1 
ATOM   3597 C  C     . ILE   B 1 189 ? 15.586  13.185  84.999  1.00 39.29  ? 1099 ILE   B C     1 
ATOM   3598 O  O     . ILE   B 1 189 ? 16.030  12.711  83.942  1.00 36.40  ? 1099 ILE   B O     1 
ATOM   3599 C  CB    . ILE   B 1 189 ? 13.412  11.933  85.207  1.00 38.08  ? 1099 ILE   B CB    1 
ATOM   3600 C  CG1   . ILE   B 1 189 ? 11.912  12.062  85.456  1.00 34.46  ? 1099 ILE   B CG1   1 
ATOM   3601 C  CG2   . ILE   B 1 189 ? 13.987  11.072  86.286  1.00 33.88  ? 1099 ILE   B CG2   1 
ATOM   3602 C  CD1   . ILE   B 1 189 ? 11.208  10.719  85.539  1.00 36.51  ? 1099 ILE   B CD1   1 
ATOM   3603 N  N     . ASP   B 1 190 ? 16.359  13.622  85.973  1.00 36.59  ? 1100 ASP   B N     1 
ATOM   3604 C  CA    . ASP   B 1 190 ? 17.805  13.510  85.937  1.00 37.75  ? 1100 ASP   B CA    1 
ATOM   3605 C  C     . ASP   B 1 190 ? 18.194  12.437  86.937  1.00 33.14  ? 1100 ASP   B C     1 
ATOM   3606 O  O     . ASP   B 1 190 ? 18.017  12.611  88.145  1.00 32.76  ? 1100 ASP   B O     1 
ATOM   3607 C  CB    . ASP   B 1 190 ? 18.450  14.855  86.268  1.00 37.95  ? 1100 ASP   B CB    1 
ATOM   3608 C  CG    . ASP   B 1 190 ? 19.915  14.888  85.955  1.00 38.12  ? 1100 ASP   B CG    1 
ATOM   3609 O  OD1   . ASP   B 1 190 ? 20.515  13.815  85.773  1.00 37.48  ? 1100 ASP   B OD1   1 
ATOM   3610 O  OD2   . ASP   B 1 190 ? 20.462  16.003  85.888  1.00 40.40  ? 1100 ASP   B OD2   1 
ATOM   3611 N  N     . ALA   B 1 191 ? 18.701  11.322  86.438  1.00 32.12  ? 1101 ALA   B N     1 
ATOM   3612 C  CA    . ALA   B 1 191 ? 19.129  10.249  87.318  1.00 30.65  ? 1101 ALA   B CA    1 
ATOM   3613 C  C     . ALA   B 1 191 ? 20.649  10.229  87.512  1.00 32.52  ? 1101 ALA   B C     1 
ATOM   3614 O  O     . ALA   B 1 191 ? 21.220  9.159   87.740  1.00 33.97  ? 1101 ALA   B O     1 
ATOM   3615 C  CB    . ALA   B 1 191 ? 18.626  8.909   86.789  1.00 29.30  ? 1101 ALA   B CB    1 
ATOM   3616 N  N     . ARG   B 1 192 ? 21.306  11.400  87.440  1.00 33.22  ? 1102 ARG   B N     1 
ATOM   3617 C  CA    . ARG   B 1 192 ? 22.760  11.491  87.592  1.00 34.96  ? 1102 ARG   B CA    1 
ATOM   3618 C  C     . ARG   B 1 192 ? 23.194  11.389  89.051  1.00 37.77  ? 1102 ARG   B C     1 
ATOM   3619 O  O     . ARG   B 1 192 ? 24.193  10.729  89.357  1.00 34.67  ? 1102 ARG   B O     1 
ATOM   3620 C  CB    . ARG   B 1 192 ? 23.278  12.799  86.986  1.00 36.97  ? 1102 ARG   B CB    1 
ATOM   3621 C  CG    . ARG   B 1 192 ? 24.706  13.182  87.416  1.00 40.71  ? 1102 ARG   B CG    1 
ATOM   3622 C  CD    . ARG   B 1 192 ? 25.745  12.154  86.974  1.00 39.08  ? 1102 ARG   B CD    1 
ATOM   3623 N  NE    . ARG   B 1 192 ? 27.084  12.488  87.452  1.00 45.64  ? 1102 ARG   B NE    1 
ATOM   3624 C  CZ    . ARG   B 1 192 ? 27.561  12.146  88.641  1.00 41.98  ? 1102 ARG   B CZ    1 
ATOM   3625 N  NH1   . ARG   B 1 192 ? 26.837  11.445  89.501  1.00 41.10  ? 1102 ARG   B NH1   1 
ATOM   3626 N  NH2   . ARG   B 1 192 ? 28.792  12.520  88.980  1.00 43.74  ? 1102 ARG   B NH2   1 
ATOM   3627 N  N     . TYR   B 1 193 ? 22.481  12.045  89.968  1.00 35.29  ? 1103 TYR   B N     1 
ATOM   3628 C  CA    . TYR   B 1 193 ? 22.820  11.929  91.384  1.00 39.22  ? 1103 TYR   B CA    1 
ATOM   3629 C  C     . TYR   B 1 193 ? 21.870  11.031  92.147  1.00 33.77  ? 1103 TYR   B C     1 
ATOM   3630 O  O     . TYR   B 1 193 ? 22.298  10.323  93.056  1.00 32.54  ? 1103 TYR   B O     1 
ATOM   3631 C  CB    . TYR   B 1 193 ? 22.860  13.307  92.057  1.00 35.88  ? 1103 TYR   B CB    1 
ATOM   3632 C  CG    . TYR   B 1 193 ? 23.701  14.304  91.298  1.00 38.19  ? 1103 TYR   B CG    1 
ATOM   3633 C  CD1   . TYR   B 1 193 ? 25.084  14.394  91.498  1.00 44.37  ? 1103 TYR   B CD1   1 
ATOM   3634 C  CD2   . TYR   B 1 193 ? 23.114  15.157  90.375  1.00 39.01  ? 1103 TYR   B CD2   1 
ATOM   3635 C  CE1   . TYR   B 1 193 ? 25.853  15.319  90.785  1.00 42.50  ? 1103 TYR   B CE1   1 
ATOM   3636 C  CE2   . TYR   B 1 193 ? 23.849  16.063  89.669  1.00 41.46  ? 1103 TYR   B CE2   1 
ATOM   3637 C  CZ    . TYR   B 1 193 ? 25.220  16.149  89.875  1.00 43.20  ? 1103 TYR   B CZ    1 
ATOM   3638 O  OH    . TYR   B 1 193 ? 25.915  17.071  89.138  1.00 46.01  ? 1103 TYR   B OH    1 
ATOM   3639 N  N     . TYR   B 1 194 ? 20.589  11.050  91.805  1.00 34.70  ? 1104 TYR   B N     1 
ATOM   3640 C  CA    . TYR   B 1 194 ? 19.634  10.100  92.347  1.00 29.87  ? 1104 TYR   B CA    1 
ATOM   3641 C  C     . TYR   B 1 194 ? 18.979  9.390   91.173  1.00 32.62  ? 1104 TYR   B C     1 
ATOM   3642 O  O     . TYR   B 1 194 ? 18.506  10.042  90.234  1.00 29.39  ? 1104 TYR   B O     1 
ATOM   3643 C  CB    . TYR   B 1 194 ? 18.601  10.799  93.230  1.00 30.08  ? 1104 TYR   B CB    1 
ATOM   3644 C  CG    . TYR   B 1 194 ? 19.155  11.738  94.289  1.00 31.40  ? 1104 TYR   B CG    1 
ATOM   3645 C  CD1   . TYR   B 1 194 ? 19.491  13.051  93.981  1.00 33.00  ? 1104 TYR   B CD1   1 
ATOM   3646 C  CD2   . TYR   B 1 194 ? 19.293  11.328  95.611  1.00 32.20  ? 1104 TYR   B CD2   1 
ATOM   3647 C  CE1   . TYR   B 1 194 ? 19.976  13.920  94.961  1.00 34.47  ? 1104 TYR   B CE1   1 
ATOM   3648 C  CE2   . TYR   B 1 194 ? 19.770  12.191  96.593  1.00 32.79  ? 1104 TYR   B CE2   1 
ATOM   3649 C  CZ    . TYR   B 1 194 ? 20.108  13.475  96.265  1.00 34.29  ? 1104 TYR   B CZ    1 
ATOM   3650 O  OH    . TYR   B 1 194 ? 20.588  14.312  97.253  1.00 35.94  ? 1104 TYR   B OH    1 
ATOM   3651 N  N     . GLY   B 1 195 ? 18.970  8.061   91.220  1.00 31.04  ? 1105 GLY   B N     1 
ATOM   3652 C  CA    . GLY   B 1 195 ? 18.399  7.271   90.144  1.00 27.32  ? 1105 GLY   B CA    1 
ATOM   3653 C  C     . GLY   B 1 195 ? 18.276  5.814   90.544  1.00 28.95  ? 1105 GLY   B C     1 
ATOM   3654 O  O     . GLY   B 1 195 ? 18.636  5.414   91.653  1.00 28.35  ? 1105 GLY   B O     1 
ATOM   3655 N  N     . ASN   B 1 196 ? 17.715  5.024   89.633  1.00 31.42  ? 1106 ASN   B N     1 
ATOM   3656 C  CA    . ASN   B 1 196 ? 17.482  3.603   89.862  1.00 30.13  ? 1106 ASN   B CA    1 
ATOM   3657 C  C     . ASN   B 1 196 ? 18.196  2.809   88.771  1.00 25.82  ? 1106 ASN   B C     1 
ATOM   3658 O  O     . ASN   B 1 196 ? 19.004  3.354   88.014  1.00 27.21  ? 1106 ASN   B O     1 
ATOM   3659 C  CB    . ASN   B 1 196 ? 15.971  3.306   89.924  1.00 27.94  ? 1106 ASN   B CB    1 
ATOM   3660 C  CG    . ASN   B 1 196 ? 15.342  3.121   88.546  1.00 30.66  ? 1106 ASN   B CG    1 
ATOM   3661 O  OD1   . ASN   B 1 196 ? 15.825  3.664   87.540  1.00 28.55  ? 1106 ASN   B OD1   1 
ATOM   3662 N  ND2   . ASN   B 1 196 ? 14.251  2.350   88.492  1.00 25.93  ? 1106 ASN   B ND2   1 
ATOM   3663 N  N     . ILE   B 1 197 ? 17.857  1.524   88.660  1.00 28.37  ? 1107 ILE   B N     1 
ATOM   3664 C  CA    . ILE   B 1 197 ? 18.486  0.645   87.673  1.00 25.32  ? 1107 ILE   B CA    1 
ATOM   3665 C  C     . ILE   B 1 197 ? 18.357  1.191   86.246  1.00 30.00  ? 1107 ILE   B C     1 
ATOM   3666 O  O     . ILE   B 1 197 ? 19.200  0.888   85.384  1.00 26.00  ? 1107 ILE   B O     1 
ATOM   3667 C  CB    . ILE   B 1 197 ? 17.877  -0.772  87.809  1.00 33.82  ? 1107 ILE   B CB    1 
ATOM   3668 C  CG1   . ILE   B 1 197 ? 18.644  -1.798  86.959  1.00 30.09  ? 1107 ILE   B CG1   1 
ATOM   3669 C  CG2   . ILE   B 1 197 ? 16.386  -0.771  87.454  1.00 25.01  ? 1107 ILE   B CG2   1 
ATOM   3670 C  CD1   . ILE   B 1 197 ? 20.103  -1.796  87.214  1.00 26.59  ? 1107 ILE   B CD1   1 
ATOM   3671 N  N     . SER   B 1 198 ? 17.310  2.001   85.972  1.00 29.51  ? 1108 SER   B N     1 
ATOM   3672 C  CA    . SER   B 1 198 ? 17.063  2.548   84.629  1.00 26.60  ? 1108 SER   B CA    1 
ATOM   3673 C  C     . SER   B 1 198 ? 18.196  3.444   84.128  1.00 27.03  ? 1108 SER   B C     1 
ATOM   3674 O  O     . SER   B 1 198 ? 18.403  3.553   82.914  1.00 27.66  ? 1108 SER   B O     1 
ATOM   3675 C  CB    . SER   B 1 198 ? 15.768  3.368   84.606  1.00 26.07  ? 1108 SER   B CB    1 
ATOM   3676 O  OG    . SER   B 1 198 ? 14.637  2.636   85.090  1.00 36.99  ? 1108 SER   B OG    1 
ATOM   3677 N  N     . ARG   B 1 199 ? 18.891  4.140   85.029  1.00 26.80  ? 1109 ARG   B N     1 
ATOM   3678 C  CA    . ARG   B 1 199 ? 19.970  5.028   84.601  1.00 28.78  ? 1109 ARG   B CA    1 
ATOM   3679 C  C     . ARG   B 1 199 ? 21.079  4.271   83.895  1.00 30.10  ? 1109 ARG   B C     1 
ATOM   3680 O  O     . ARG   B 1 199 ? 21.900  4.890   83.216  1.00 31.29  ? 1109 ARG   B O     1 
ATOM   3681 C  CB    . ARG   B 1 199 ? 20.557  5.770   85.794  1.00 28.24  ? 1109 ARG   B CB    1 
ATOM   3682 C  CG    . ARG   B 1 199 ? 21.499  4.915   86.601  1.00 30.40  ? 1109 ARG   B CG    1 
ATOM   3683 C  CD    . ARG   B 1 199 ? 21.785  5.494   87.990  1.00 28.40  ? 1109 ARG   B CD    1 
ATOM   3684 N  NE    . ARG   B 1 199 ? 22.457  6.785   87.961  1.00 29.75  ? 1109 ARG   B NE    1 
ATOM   3685 C  CZ    . ARG   B 1 199 ? 23.767  6.944   87.825  1.00 36.28  ? 1109 ARG   B CZ    1 
ATOM   3686 N  NH1   . ARG   B 1 199 ? 24.575  5.911   87.617  1.00 34.25  ? 1109 ARG   B NH1   1 
ATOM   3687 N  NH2   . ARG   B 1 199 ? 24.281  8.168   87.899  1.00 32.70  ? 1109 ARG   B NH2   1 
ATOM   3688 N  N     . PHE   B 1 200 ? 21.128  2.948   84.033  1.00 32.19  ? 1110 PHE   B N     1 
ATOM   3689 C  CA    . PHE   B 1 200 ? 22.236  2.171   83.482  1.00 28.91  ? 1110 PHE   B CA    1 
ATOM   3690 C  C     . PHE   B 1 200 ? 21.926  1.562   82.123  1.00 29.17  ? 1110 PHE   B C     1 
ATOM   3691 O  O     . PHE   B 1 200 ? 22.806  0.928   81.530  1.00 35.18  ? 1110 PHE   B O     1 
ATOM   3692 C  CB    . PHE   B 1 200 ? 22.644  1.076   84.464  1.00 28.71  ? 1110 PHE   B CB    1 
ATOM   3693 C  CG    . PHE   B 1 200 ? 23.339  1.600   85.685  1.00 29.75  ? 1110 PHE   B CG    1 
ATOM   3694 C  CD1   . PHE   B 1 200 ? 24.610  2.174   85.584  1.00 30.69  ? 1110 PHE   B CD1   1 
ATOM   3695 C  CD2   . PHE   B 1 200 ? 22.750  1.510   86.928  1.00 28.31  ? 1110 PHE   B CD2   1 
ATOM   3696 C  CE1   . PHE   B 1 200 ? 25.263  2.653   86.704  1.00 31.40  ? 1110 PHE   B CE1   1 
ATOM   3697 C  CE2   . PHE   B 1 200 ? 23.408  1.981   88.058  1.00 30.55  ? 1110 PHE   B CE2   1 
ATOM   3698 C  CZ    . PHE   B 1 200 ? 24.672  2.553   87.945  1.00 30.49  ? 1110 PHE   B CZ    1 
ATOM   3699 N  N     . ILE   B 1 201 ? 20.718  1.770   81.610  1.00 28.63  ? 1111 ILE   B N     1 
ATOM   3700 C  CA    . ILE   B 1 201 ? 20.295  1.198   80.335  1.00 31.50  ? 1111 ILE   B CA    1 
ATOM   3701 C  C     . ILE   B 1 201 ? 20.891  2.004   79.187  1.00 34.48  ? 1111 ILE   B C     1 
ATOM   3702 O  O     . ILE   B 1 201 ? 20.739  3.228   79.125  1.00 35.27  ? 1111 ILE   B O     1 
ATOM   3703 C  CB    . ILE   B 1 201 ? 18.755  1.157   80.237  1.00 29.15  ? 1111 ILE   B CB    1 
ATOM   3704 C  CG1   . ILE   B 1 201 ? 18.136  0.456   81.441  1.00 27.26  ? 1111 ILE   B CG1   1 
ATOM   3705 C  CG2   . ILE   B 1 201 ? 18.346  0.438   79.001  1.00 31.29  ? 1111 ILE   B CG2   1 
ATOM   3706 C  CD1   . ILE   B 1 201 ? 16.562  0.279   81.347  1.00 30.19  ? 1111 ILE   B CD1   1 
ATOM   3707 N  N     . ASN   B 1 202 ? 21.546  1.317   78.257  1.00 34.09  ? 1112 ASN   B N     1 
ATOM   3708 C  CA    . ASN   B 1 202 ? 22.170  1.992   77.135  1.00 33.35  ? 1112 ASN   B CA    1 
ATOM   3709 C  C     . ASN   B 1 202 ? 21.167  2.233   76.007  1.00 36.00  ? 1112 ASN   B C     1 
ATOM   3710 O  O     . ASN   B 1 202 ? 20.025  1.766   76.036  1.00 36.13  ? 1112 ASN   B O     1 
ATOM   3711 C  CB    . ASN   B 1 202 ? 23.381  1.173   76.662  1.00 38.27  ? 1112 ASN   B CB    1 
ATOM   3712 C  CG    . ASN   B 1 202 ? 24.438  1.012   77.757  1.00 34.63  ? 1112 ASN   B CG    1 
ATOM   3713 O  OD1   . ASN   B 1 202 ? 24.784  1.976   78.434  1.00 35.66  ? 1112 ASN   B OD1   1 
ATOM   3714 N  ND2   . ASN   B 1 202 ? 24.920  -0.216  77.957  1.00 34.75  ? 1112 ASN   B ND2   1 
ATOM   3715 N  N     . HIS   B 1 203 ? 21.604  2.995   75.007  1.00 37.54  ? 1113 HIS   B N     1 
ATOM   3716 C  CA    . HIS   B 1 203 ? 20.797  3.287   73.826  1.00 38.78  ? 1113 HIS   B CA    1 
ATOM   3717 C  C     . HIS   B 1 203 ? 21.038  2.225   72.768  1.00 39.69  ? 1113 HIS   B C     1 
ATOM   3718 O  O     . HIS   B 1 203 ? 22.189  1.933   72.432  1.00 38.94  ? 1113 HIS   B O     1 
ATOM   3719 C  CB    . HIS   B 1 203 ? 21.154  4.656   73.244  1.00 40.15  ? 1113 HIS   B CB    1 
ATOM   3720 C  CG    . HIS   B 1 203 ? 20.892  4.783   71.774  1.00 41.20  ? 1113 HIS   B CG    1 
ATOM   3721 N  ND1   . HIS   B 1 203 ? 19.728  5.324   71.269  1.00 42.73  ? 1113 HIS   B ND1   1 
ATOM   3722 C  CD2   . HIS   B 1 203 ? 21.649  4.456   70.698  1.00 43.08  ? 1113 HIS   B CD2   1 
ATOM   3723 C  CE1   . HIS   B 1 203 ? 19.774  5.316   69.949  1.00 44.18  ? 1113 HIS   B CE1   1 
ATOM   3724 N  NE2   . HIS   B 1 203 ? 20.930  4.796   69.576  1.00 44.86  ? 1113 HIS   B NE2   1 
ATOM   3725 N  N     . LEU   B 1 204 ? 19.968  1.675   72.211  1.00 37.72  ? 1114 LEU   B N     1 
ATOM   3726 C  CA    . LEU   B 1 204 ? 20.102  0.722   71.120  1.00 38.87  ? 1114 LEU   B CA    1 
ATOM   3727 C  C     . LEU   B 1 204 ? 19.369  1.231   69.891  1.00 42.29  ? 1114 LEU   B C     1 
ATOM   3728 O  O     . LEU   B 1 204 ? 18.179  1.570   69.961  1.00 47.88  ? 1114 LEU   B O     1 
ATOM   3729 C  CB    . LEU   B 1 204 ? 19.588  -0.656  71.511  1.00 37.51  ? 1114 LEU   B CB    1 
ATOM   3730 C  CG    . LEU   B 1 204 ? 20.400  -1.390  72.558  1.00 39.14  ? 1114 LEU   B CG    1 
ATOM   3731 C  CD1   . LEU   B 1 204 ? 19.753  -2.736  72.867  1.00 40.40  ? 1114 LEU   B CD1   1 
ATOM   3732 C  CD2   . LEU   B 1 204 ? 21.878  -1.556  72.103  1.00 37.80  ? 1114 LEU   B CD2   1 
ATOM   3733 N  N     . CYS   B 1 205 ? 20.078  1.271   68.761  1.00 42.93  ? 1115 CYS   B N     1 
ATOM   3734 C  CA    . CYS   B 1 205 ? 19.411  1.540   67.494  1.00 45.09  ? 1115 CYS   B CA    1 
ATOM   3735 C  C     . CYS   B 1 205 ? 18.402  0.451   67.131  1.00 46.89  ? 1115 CYS   B C     1 
ATOM   3736 O  O     . CYS   B 1 205 ? 17.478  0.716   66.351  1.00 48.42  ? 1115 CYS   B O     1 
ATOM   3737 C  CB    . CYS   B 1 205 ? 20.454  1.719   66.397  1.00 47.71  ? 1115 CYS   B CB    1 
ATOM   3738 S  SG    . CYS   B 1 205 ? 21.425  3.242   66.577  1.00 53.93  ? 1115 CYS   B SG    1 
ATOM   3739 N  N     . ASP   B 1 206 ? 18.553  -0.762  67.683  1.00 46.54  ? 1116 ASP   B N     1 
ATOM   3740 C  CA    . ASP   B 1 206 ? 17.561  -1.830  67.570  1.00 45.47  ? 1116 ASP   B CA    1 
ATOM   3741 C  C     . ASP   B 1 206 ? 17.054  -2.118  68.975  1.00 42.59  ? 1116 ASP   B C     1 
ATOM   3742 O  O     . ASP   B 1 206 ? 17.376  -3.161  69.562  1.00 42.10  ? 1116 ASP   B O     1 
ATOM   3743 C  CB    . ASP   B 1 206 ? 18.133  -3.088  66.919  1.00 49.31  ? 1116 ASP   B CB    1 
ATOM   3744 C  CG    . ASP   B 1 206 ? 17.049  -4.069  66.485  1.00 56.04  ? 1116 ASP   B CG    1 
ATOM   3745 O  OD1   . ASP   B 1 206 ? 15.842  -3.790  66.681  1.00 47.56  ? 1116 ASP   B OD1   1 
ATOM   3746 O  OD2   . ASP   B 1 206 ? 17.410  -5.132  65.931  1.00 64.78  ? 1116 ASP   B OD2   1 
ATOM   3747 N  N     . PRO   B 1 207 ? 16.239  -1.228  69.534  1.00 45.06  ? 1117 PRO   B N     1 
ATOM   3748 C  CA    . PRO   B 1 207 ? 15.868  -1.346  70.944  1.00 41.57  ? 1117 PRO   B CA    1 
ATOM   3749 C  C     . PRO   B 1 207 ? 14.941  -2.526  71.172  1.00 41.31  ? 1117 PRO   B C     1 
ATOM   3750 O  O     . PRO   B 1 207 ? 14.351  -3.080  70.243  1.00 39.42  ? 1117 PRO   B O     1 
ATOM   3751 C  CB    . PRO   B 1 207 ? 15.160  -0.019  71.228  1.00 39.85  ? 1117 PRO   B CB    1 
ATOM   3752 C  CG    . PRO   B 1 207 ? 14.542  0.349   69.894  1.00 40.16  ? 1117 PRO   B CG    1 
ATOM   3753 C  CD    . PRO   B 1 207 ? 15.497  -0.152  68.846  1.00 44.82  ? 1117 PRO   B CD    1 
ATOM   3754 N  N     . ASN   B 1 208 ? 14.839  -2.919  72.440  1.00 37.76  ? 1118 ASN   B N     1 
ATOM   3755 C  CA    . ASN   B 1 208 ? 13.945  -3.988  72.851  1.00 40.19  ? 1118 ASN   B CA    1 
ATOM   3756 C  C     . ASN   B 1 208 ? 12.980  -3.582  73.963  1.00 37.27  ? 1118 ASN   B C     1 
ATOM   3757 O  O     . ASN   B 1 208 ? 12.153  -4.404  74.367  1.00 35.56  ? 1118 ASN   B O     1 
ATOM   3758 C  CB    . ASN   B 1 208 ? 14.761  -5.198  73.309  1.00 39.53  ? 1118 ASN   B CB    1 
ATOM   3759 C  CG    . ASN   B 1 208 ? 15.704  -4.850  74.420  1.00 42.01  ? 1118 ASN   B CG    1 
ATOM   3760 O  OD1   . ASN   B 1 208 ? 15.963  -3.671  74.674  1.00 41.28  ? 1118 ASN   B OD1   1 
ATOM   3761 N  ND2   . ASN   B 1 208 ? 16.226  -5.863  75.098  1.00 42.56  ? 1118 ASN   B ND2   1 
ATOM   3762 N  N     . ILE   B 1 209 ? 13.074  -2.356  74.483  1.00 37.25  ? 1119 ILE   B N     1 
ATOM   3763 C  CA    . ILE   B 1 209 ? 12.134  -1.822  75.463  1.00 35.95  ? 1119 ILE   B CA    1 
ATOM   3764 C  C     . ILE   B 1 209 ? 11.678  -0.451  74.983  1.00 37.57  ? 1119 ILE   B C     1 
ATOM   3765 O  O     . ILE   B 1 209 ? 12.413  0.248   74.277  1.00 39.52  ? 1119 ILE   B O     1 
ATOM   3766 C  CB    . ILE   B 1 209 ? 12.745  -1.728  76.888  1.00 33.89  ? 1119 ILE   B CB    1 
ATOM   3767 C  CG1   . ILE   B 1 209 ? 13.711  -0.544  77.002  1.00 36.96  ? 1119 ILE   B CG1   1 
ATOM   3768 C  CG2   . ILE   B 1 209 ? 13.485  -3.021  77.242  1.00 39.11  ? 1119 ILE   B CG2   1 
ATOM   3769 C  CD1   . ILE   B 1 209 ? 14.445  -0.484  78.338  1.00 33.71  ? 1119 ILE   B CD1   1 
ATOM   3770 N  N     . ILE   B 1 210 ? 10.461  -0.060  75.369  1.00 35.98  ? 1120 ILE   B N     1 
ATOM   3771 C  CA    . ILE   B 1 210 ? 9.939   1.263   75.015  1.00 34.25  ? 1120 ILE   B CA    1 
ATOM   3772 C  C     . ILE   B 1 210 ? 9.438   2.002   76.248  1.00 38.43  ? 1120 ILE   B C     1 
ATOM   3773 O  O     . ILE   B 1 210 ? 8.923   1.372   77.186  1.00 35.38  ? 1120 ILE   B O     1 
ATOM   3774 C  CB    . ILE   B 1 210 ? 8.802   1.178   73.984  1.00 39.18  ? 1120 ILE   B CB    1 
ATOM   3775 C  CG1   . ILE   B 1 210 ? 7.611   0.374   74.543  1.00 35.00  ? 1120 ILE   B CG1   1 
ATOM   3776 C  CG2   . ILE   B 1 210 ? 9.311   0.643   72.650  1.00 40.89  ? 1120 ILE   B CG2   1 
ATOM   3777 C  CD1   . ILE   B 1 210 ? 6.494   0.195   73.561  1.00 38.26  ? 1120 ILE   B CD1   1 
ATOM   3778 N  N     . PRO   B 1 211 ? 9.528   3.335   76.268  1.00 36.76  ? 1121 PRO   B N     1 
ATOM   3779 C  CA    . PRO   B 1 211 ? 8.997   4.106   77.396  1.00 36.00  ? 1121 PRO   B CA    1 
ATOM   3780 C  C     . PRO   B 1 211 ? 7.550   4.532   77.185  1.00 36.55  ? 1121 PRO   B C     1 
ATOM   3781 O  O     . PRO   B 1 211 ? 7.139   4.937   76.096  1.00 40.07  ? 1121 PRO   B O     1 
ATOM   3782 C  CB    . PRO   B 1 211 ? 9.927   5.325   77.430  1.00 36.91  ? 1121 PRO   B CB    1 
ATOM   3783 C  CG    . PRO   B 1 211 ? 10.296  5.535   75.984  1.00 36.50  ? 1121 PRO   B CG    1 
ATOM   3784 C  CD    . PRO   B 1 211 ? 10.226  4.190   75.293  1.00 35.77  ? 1121 PRO   B CD    1 
ATOM   3785 N  N     . VAL   B 1 212 ? 6.766   4.438   78.260  1.00 35.38  ? 1122 VAL   B N     1 
ATOM   3786 C  CA    . VAL   B 1 212 ? 5.366   4.842   78.261  1.00 34.91  ? 1122 VAL   B CA    1 
ATOM   3787 C  C     . VAL   B 1 212 ? 5.125   5.794   79.429  1.00 35.47  ? 1122 VAL   B C     1 
ATOM   3788 O  O     . VAL   B 1 212 ? 5.575   5.544   80.553  1.00 33.53  ? 1122 VAL   B O     1 
ATOM   3789 C  CB    . VAL   B 1 212 ? 4.420   3.626   78.352  1.00 36.30  ? 1122 VAL   B CB    1 
ATOM   3790 C  CG1   . VAL   B 1 212 ? 2.970   4.064   78.192  1.00 38.48  ? 1122 VAL   B CG1   1 
ATOM   3791 C  CG2   . VAL   B 1 212 ? 4.782   2.581   77.306  1.00 38.17  ? 1122 VAL   B CG2   1 
ATOM   3792 N  N     . ARG   B 1 213 ? 4.408   6.880   79.171  1.00 36.96  ? 1123 ARG   B N     1 
ATOM   3793 C  CA    . ARG   B 1 213 ? 4.007   7.775   80.250  1.00 38.76  ? 1123 ARG   B CA    1 
ATOM   3794 C  C     . ARG   B 1 213 ? 2.820   7.179   81.004  1.00 32.77  ? 1123 ARG   B C     1 
ATOM   3795 O  O     . ARG   B 1 213 ? 1.862   6.699   80.387  1.00 35.17  ? 1123 ARG   B O     1 
ATOM   3796 C  CB    . ARG   B 1 213 ? 3.668   9.163   79.694  1.00 37.87  ? 1123 ARG   B CB    1 
ATOM   3797 C  CG    . ARG   B 1 213 ? 4.900   9.976   79.323  1.00 47.05  ? 1123 ARG   B CG    1 
ATOM   3798 C  CD    . ARG   B 1 213 ? 4.972   10.307  77.842  1.00 53.45  ? 1123 ARG   B CD    1 
ATOM   3799 N  NE    . ARG   B 1 213 ? 6.143   11.122  77.528  1.00 55.16  ? 1123 ARG   B NE    1 
ATOM   3800 C  CZ    . ARG   B 1 213 ? 7.340   10.635  77.215  1.00 53.64  ? 1123 ARG   B CZ    1 
ATOM   3801 N  NH1   . ARG   B 1 213 ? 7.561   9.331   77.137  1.00 48.01  ? 1123 ARG   B NH1   1 
ATOM   3802 N  NH2   . ARG   B 1 213 ? 8.341   11.477  76.972  1.00 51.63  ? 1123 ARG   B NH2   1 
ATOM   3803 N  N     . VAL   B 1 214 ? 2.889   7.201   82.341  1.00 30.57  ? 1124 VAL   B N     1 
ATOM   3804 C  CA    . VAL   B 1 214 ? 1.914   6.531   83.200  1.00 32.28  ? 1124 VAL   B CA    1 
ATOM   3805 C  C     . VAL   B 1 214 ? 1.525   7.425   84.382  1.00 31.99  ? 1124 VAL   B C     1 
ATOM   3806 O  O     . VAL   B 1 214 ? 2.351   8.171   84.925  1.00 30.47  ? 1124 VAL   B O     1 
ATOM   3807 C  CB    . VAL   B 1 214 ? 2.463   5.177   83.711  1.00 28.86  ? 1124 VAL   B CB    1 
ATOM   3808 C  CG1   . VAL   B 1 214 ? 1.439   4.448   84.534  1.00 29.02  ? 1124 VAL   B CG1   1 
ATOM   3809 C  CG2   . VAL   B 1 214 ? 2.906   4.291   82.557  1.00 31.73  ? 1124 VAL   B CG2   1 
ATOM   3810 N  N     . PHE   B 1 215 ? 0.262   7.311   84.810  1.00 30.28  ? 1125 PHE   B N     1 
ATOM   3811 C  CA    . PHE   B 1 215 ? -0.235  7.956   86.020  1.00 27.59  ? 1125 PHE   B CA    1 
ATOM   3812 C  C     . PHE   B 1 215 ? -0.809  6.938   86.992  1.00 27.37  ? 1125 PHE   B C     1 
ATOM   3813 O  O     . PHE   B 1 215 ? -1.528  6.014   86.603  1.00 28.00  ? 1125 PHE   B O     1 
ATOM   3814 C  CB    . PHE   B 1 215 ? -1.289  8.995   85.693  1.00 28.02  ? 1125 PHE   B CB    1 
ATOM   3815 C  CG    . PHE   B 1 215 ? -0.709  10.236  85.132  1.00 32.57  ? 1125 PHE   B CG    1 
ATOM   3816 C  CD1   . PHE   B 1 215 ? -0.031  11.117  85.957  1.00 28.69  ? 1125 PHE   B CD1   1 
ATOM   3817 C  CD2   . PHE   B 1 215 ? -0.771  10.498  83.778  1.00 31.50  ? 1125 PHE   B CD2   1 
ATOM   3818 C  CE1   . PHE   B 1 215 ? 0.524   12.231  85.456  1.00 28.62  ? 1125 PHE   B CE1   1 
ATOM   3819 C  CE2   . PHE   B 1 215 ? -0.183  11.635  83.268  1.00 32.85  ? 1125 PHE   B CE2   1 
ATOM   3820 C  CZ    . PHE   B 1 215 ? 0.452   12.498  84.107  1.00 29.44  ? 1125 PHE   B CZ    1 
ATOM   3821 N  N     . MET   B 1 216 ? -0.495  7.117   88.265  1.00 27.66  ? 1126 MET   B N     1 
ATOM   3822 C  CA    . MET   B 1 216 ? -0.911  6.146   89.259  1.00 26.91  ? 1126 MET   B CA    1 
ATOM   3823 C  C     . MET   B 1 216 ? -1.459  6.846   90.486  1.00 29.05  ? 1126 MET   B C     1 
ATOM   3824 O  O     . MET   B 1 216 ? -2.666  7.065   90.594  1.00 31.98  ? 1126 MET   B O     1 
ATOM   3825 C  CB    . MET   B 1 216 ? 0.264   5.236   89.658  1.00 26.83  ? 1126 MET   B CB    1 
ATOM   3826 C  CG    . MET   B 1 216 ? 0.604   4.151   88.664  1.00 27.19  ? 1126 MET   B CG    1 
ATOM   3827 S  SD    . MET   B 1 216 ? 2.393   3.711   88.772  1.00 27.29  ? 1126 MET   B SD    1 
ATOM   3828 C  CE    . MET   B 1 216 ? 3.040   5.158   87.935  1.00 26.89  ? 1126 MET   B CE    1 
ATOM   3829 N  N     . LEU   B 1 217 ? -0.593  7.192   91.431  1.00 28.56  ? 1127 LEU   B N     1 
ATOM   3830 C  CA    . LEU   B 1 217 ? -1.125  7.699   92.683  1.00 27.91  ? 1127 LEU   B CA    1 
ATOM   3831 C  C     . LEU   B 1 217 ? -1.442  9.183   92.619  1.00 29.04  ? 1127 LEU   B C     1 
ATOM   3832 O  O     . LEU   B 1 217 ? -2.104  9.700   93.528  1.00 28.87  ? 1127 LEU   B O     1 
ATOM   3833 C  CB    . LEU   B 1 217 ? -0.163  7.379   93.826  1.00 26.44  ? 1127 LEU   B CB    1 
ATOM   3834 C  CG    . LEU   B 1 217 ? -0.469  6.048   94.529  1.00 28.95  ? 1127 LEU   B CG    1 
ATOM   3835 C  CD1   . LEU   B 1 217 ? -0.544  4.903   93.542  1.00 28.91  ? 1127 LEU   B CD1   1 
ATOM   3836 C  CD2   . LEU   B 1 217 ? 0.570   5.706   95.587  1.00 37.65  ? 1127 LEU   B CD2   1 
ATOM   3837 N  N     . HIS   B 1 218 ? -1.011  9.867   91.559  1.00 26.97  ? 1128 HIS   B N     1 
ATOM   3838 C  CA    . HIS   B 1 218 ? -1.438  11.224  91.278  1.00 28.03  ? 1128 HIS   B CA    1 
ATOM   3839 C  C     . HIS   B 1 218 ? -1.688  11.324  89.785  1.00 29.37  ? 1128 HIS   B C     1 
ATOM   3840 O  O     . HIS   B 1 218 ? -1.361  10.412  89.017  1.00 28.01  ? 1128 HIS   B O     1 
ATOM   3841 C  CB    . HIS   B 1 218 ? -0.403  12.256  91.739  1.00 31.28  ? 1128 HIS   B CB    1 
ATOM   3842 C  CG    . HIS   B 1 218 ? 0.843   12.280  90.906  1.00 26.93  ? 1128 HIS   B CG    1 
ATOM   3843 N  ND1   . HIS   B 1 218 ? 0.899   12.889  89.671  1.00 27.37  ? 1128 HIS   B ND1   1 
ATOM   3844 C  CD2   . HIS   B 1 218 ? 2.072   11.745  91.118  1.00 30.69  ? 1128 HIS   B CD2   1 
ATOM   3845 C  CE1   . HIS   B 1 218 ? 2.115   12.753  89.170  1.00 32.03  ? 1128 HIS   B CE1   1 
ATOM   3846 N  NE2   . HIS   B 1 218 ? 2.849   12.064  90.028  1.00 27.67  ? 1128 HIS   B NE2   1 
ATOM   3847 N  N     . GLN   B 1 219 ? -2.272  12.456  89.384  1.00 30.75  ? 1129 GLN   B N     1 
ATOM   3848 C  CA    . GLN   B 1 219 ? -2.599  12.765  87.993  1.00 32.74  ? 1129 GLN   B CA    1 
ATOM   3849 C  C     . GLN   B 1 219 ? -2.167  14.185  87.645  1.00 29.99  ? 1129 GLN   B C     1 
ATOM   3850 O  O     . GLN   B 1 219 ? -2.749  14.836  86.765  1.00 29.60  ? 1129 GLN   B O     1 
ATOM   3851 C  CB    . GLN   B 1 219 ? -4.100  12.552  87.712  1.00 30.17  ? 1129 GLN   B CB    1 
ATOM   3852 C  CG    . GLN   B 1 219 ? -4.463  11.059  87.505  1.00 28.46  ? 1129 GLN   B CG    1 
ATOM   3853 C  CD    . GLN   B 1 219 ? -5.934  10.743  87.732  1.00 32.79  ? 1129 GLN   B CD    1 
ATOM   3854 O  OE1   . GLN   B 1 219 ? -6.776  11.653  87.817  1.00 29.39  ? 1129 GLN   B OE1   1 
ATOM   3855 N  NE2   . GLN   B 1 219 ? -6.255  9.443   87.830  1.00 28.91  ? 1129 GLN   B NE2   1 
ATOM   3856 N  N     . ASP   B 1 220 ? -1.145  14.678  88.339  1.00 30.89  ? 1130 ASP   B N     1 
ATOM   3857 C  CA    . ASP   B 1 220 ? -0.518  15.952  87.999  1.00 29.87  ? 1130 ASP   B CA    1 
ATOM   3858 C  C     . ASP   B 1 220 ? 0.236   15.793  86.683  1.00 30.57  ? 1130 ASP   B C     1 
ATOM   3859 O  O     . ASP   B 1 220 ? 1.254   15.093  86.623  1.00 34.05  ? 1130 ASP   B O     1 
ATOM   3860 C  CB    . ASP   B 1 220 ? 0.413   16.380  89.128  1.00 29.61  ? 1130 ASP   B CB    1 
ATOM   3861 C  CG    . ASP   B 1 220 ? 0.963   17.783  88.938  1.00 33.10  ? 1130 ASP   B CG    1 
ATOM   3862 O  OD1   . ASP   B 1 220 ? 1.233   18.176  87.782  1.00 31.10  ? 1130 ASP   B OD1   1 
ATOM   3863 O  OD2   . ASP   B 1 220 ? 1.108   18.497  89.952  1.00 32.98  ? 1130 ASP   B OD2   1 
ATOM   3864 N  N     . LEU   B 1 221 ? -0.238  16.471  85.635  1.00 30.83  ? 1131 LEU   B N     1 
ATOM   3865 C  CA    . LEU   B 1 221 ? 0.236   16.198  84.282  1.00 31.41  ? 1131 LEU   B CA    1 
ATOM   3866 C  C     . LEU   B 1 221 ? 1.677   16.632  84.036  1.00 38.65  ? 1131 LEU   B C     1 
ATOM   3867 O  O     . LEU   B 1 221 ? 2.258   16.218  83.027  1.00 42.73  ? 1131 LEU   B O     1 
ATOM   3868 C  CB    . LEU   B 1 221 ? -0.661  16.880  83.264  1.00 32.65  ? 1131 LEU   B CB    1 
ATOM   3869 C  CG    . LEU   B 1 221 ? -2.122  16.439  83.309  1.00 38.59  ? 1131 LEU   B CG    1 
ATOM   3870 C  CD1   . LEU   B 1 221 ? -2.890  17.008  82.107  1.00 34.05  ? 1131 LEU   B CD1   1 
ATOM   3871 C  CD2   . LEU   B 1 221 ? -2.247  14.926  83.379  1.00 32.32  ? 1131 LEU   B CD2   1 
ATOM   3872 N  N     . ARG   B 1 222 ? 2.254   17.474  84.898  1.00 37.36  ? 1132 ARG   B N     1 
ATOM   3873 C  CA    . ARG   B 1 222 ? 3.669   17.813  84.756  1.00 43.23  ? 1132 ARG   B CA    1 
ATOM   3874 C  C     . ARG   B 1 222 ? 4.576   16.668  85.157  1.00 44.43  ? 1132 ARG   B C     1 
ATOM   3875 O  O     . ARG   B 1 222 ? 5.791   16.754  84.935  1.00 49.31  ? 1132 ARG   B O     1 
ATOM   3876 C  CB    . ARG   B 1 222 ? 4.044   19.016  85.613  1.00 41.29  ? 1132 ARG   B CB    1 
ATOM   3877 C  CG    . ARG   B 1 222 ? 3.202   20.257  85.424  1.00 44.19  ? 1132 ARG   B CG    1 
ATOM   3878 C  CD    . ARG   B 1 222 ? 3.467   21.207  86.567  1.00 37.97  ? 1132 ARG   B CD    1 
ATOM   3879 N  NE    . ARG   B 1 222 ? 3.181   20.559  87.840  1.00 33.57  ? 1132 ARG   B NE    1 
ATOM   3880 C  CZ    . ARG   B 1 222 ? 3.621   20.991  89.013  1.00 34.70  ? 1132 ARG   B CZ    1 
ATOM   3881 N  NH1   . ARG   B 1 222 ? 4.397   22.056  89.106  1.00 37.89  ? 1132 ARG   B NH1   1 
ATOM   3882 N  NH2   . ARG   B 1 222 ? 3.270   20.341  90.120  1.00 32.60  ? 1132 ARG   B NH2   1 
ATOM   3883 N  N     . PHE   B 1 223 ? 4.027   15.621  85.767  1.00 36.27  ? 1133 PHE   B N     1 
ATOM   3884 C  CA    . PHE   B 1 223 ? 4.824   14.541  86.341  1.00 34.57  ? 1133 PHE   B CA    1 
ATOM   3885 C  C     . PHE   B 1 223 ? 4.287   13.180  85.940  1.00 33.81  ? 1133 PHE   B C     1 
ATOM   3886 O  O     . PHE   B 1 223 ? 3.951   12.358  86.795  1.00 32.30  ? 1133 PHE   B O     1 
ATOM   3887 C  CB    . PHE   B 1 223 ? 4.874   14.675  87.856  1.00 32.86  ? 1133 PHE   B CB    1 
ATOM   3888 C  CG    . PHE   B 1 223 ? 5.538   15.907  88.289  1.00 35.45  ? 1133 PHE   B CG    1 
ATOM   3889 C  CD1   . PHE   B 1 223 ? 6.878   16.091  88.032  1.00 36.73  ? 1133 PHE   B CD1   1 
ATOM   3890 C  CD2   . PHE   B 1 223 ? 4.825   16.919  88.894  1.00 39.03  ? 1133 PHE   B CD2   1 
ATOM   3891 C  CE1   . PHE   B 1 223 ? 7.511   17.243  88.408  1.00 39.22  ? 1133 PHE   B CE1   1 
ATOM   3892 C  CE2   . PHE   B 1 223 ? 5.464   18.081  89.275  1.00 41.20  ? 1133 PHE   B CE2   1 
ATOM   3893 C  CZ    . PHE   B 1 223 ? 6.812   18.238  89.030  1.00 37.85  ? 1133 PHE   B CZ    1 
ATOM   3894 N  N     . PRO   B 1 224 ? 4.215   12.891  84.643  1.00 35.82  ? 1134 PRO   B N     1 
ATOM   3895 C  CA    . PRO   B 1 224 ? 4.018   11.500  84.253  1.00 31.44  ? 1134 PRO   B CA    1 
ATOM   3896 C  C     . PRO   B 1 224 ? 5.238   10.724  84.706  1.00 31.94  ? 1134 PRO   B C     1 
ATOM   3897 O  O     . PRO   B 1 224 ? 6.324   11.282  84.900  1.00 29.40  ? 1134 PRO   B O     1 
ATOM   3898 C  CB    . PRO   B 1 224 ? 3.915   11.555  82.727  1.00 32.43  ? 1134 PRO   B CB    1 
ATOM   3899 C  CG    . PRO   B 1 224 ? 4.745   12.738  82.363  1.00 37.05  ? 1134 PRO   B CG    1 
ATOM   3900 C  CD    . PRO   B 1 224 ? 4.566   13.738  83.484  1.00 36.36  ? 1134 PRO   B CD    1 
ATOM   3901 N  N     . ARG   B 1 225 ? 5.036   9.432   84.919  1.00 31.26  ? 1135 ARG   B N     1 
ATOM   3902 C  CA    . ARG   B 1 225 ? 6.104   8.520   85.273  1.00 27.89  ? 1135 ARG   B CA    1 
ATOM   3903 C  C     . ARG   B 1 225 ? 6.396   7.627   84.077  1.00 31.48  ? 1135 ARG   B C     1 
ATOM   3904 O  O     . ARG   B 1 225 ? 5.477   7.230   83.347  1.00 32.06  ? 1135 ARG   B O     1 
ATOM   3905 C  CB    . ARG   B 1 225 ? 5.729   7.707   86.506  1.00 27.34  ? 1135 ARG   B CB    1 
ATOM   3906 C  CG    . ARG   B 1 225 ? 5.793   8.554   87.765  1.00 27.32  ? 1135 ARG   B CG    1 
ATOM   3907 C  CD    . ARG   B 1 225 ? 5.133   7.862   88.954  1.00 29.73  ? 1135 ARG   B CD    1 
ATOM   3908 N  NE    . ARG   B 1 225 ? 5.768   6.596   89.309  1.00 26.86  ? 1135 ARG   B NE    1 
ATOM   3909 C  CZ    . ARG   B 1 225 ? 5.336   5.797   90.273  1.00 28.47  ? 1135 ARG   B CZ    1 
ATOM   3910 N  NH1   . ARG   B 1 225 ? 4.298   6.122   91.030  1.00 32.69  ? 1135 ARG   B NH1   1 
ATOM   3911 N  NH2   . ARG   B 1 225 ? 5.916   4.618   90.444  1.00 27.08  ? 1135 ARG   B NH2   1 
ATOM   3912 N  N     . ILE   B 1 226 ? 7.681   7.353   83.860  1.00 29.30  ? 1136 ILE   B N     1 
ATOM   3913 C  CA    . ILE   B 1 226 ? 8.142   6.638   82.681  1.00 28.99  ? 1136 ILE   B CA    1 
ATOM   3914 C  C     . ILE   B 1 226 ? 8.185   5.156   83.009  1.00 30.78  ? 1136 ILE   B C     1 
ATOM   3915 O  O     . ILE   B 1 226 ? 8.876   4.741   83.947  1.00 32.25  ? 1136 ILE   B O     1 
ATOM   3916 C  CB    . ILE   B 1 226 ? 9.528   7.133   82.235  1.00 33.93  ? 1136 ILE   B CB    1 
ATOM   3917 C  CG1   . ILE   B 1 226 ? 9.494   8.635   81.955  1.00 36.72  ? 1136 ILE   B CG1   1 
ATOM   3918 C  CG2   . ILE   B 1 226 ? 9.977   6.375   80.992  1.00 33.87  ? 1136 ILE   B CG2   1 
ATOM   3919 C  CD1   . ILE   B 1 226 ? 8.377   9.059   80.989  1.00 33.67  ? 1136 ILE   B CD1   1 
ATOM   3920 N  N     . ALA   B 1 227 ? 7.487   4.355   82.215  1.00 29.00  ? 1137 ALA   B N     1 
ATOM   3921 C  CA    . ALA   B 1 227 ? 7.481   2.908   82.352  1.00 29.28  ? 1137 ALA   B CA    1 
ATOM   3922 C  C     . ALA   B 1 227 ? 8.080   2.282   81.100  1.00 31.22  ? 1137 ALA   B C     1 
ATOM   3923 O  O     . ALA   B 1 227 ? 7.724   2.670   79.983  1.00 35.09  ? 1137 ALA   B O     1 
ATOM   3924 C  CB    . ALA   B 1 227 ? 6.051   2.403   82.575  1.00 30.66  ? 1137 ALA   B CB    1 
ATOM   3925 N  N     . PHE   B 1 228 ? 8.982   1.315   81.282  1.00 30.07  ? 1138 PHE   B N     1 
ATOM   3926 C  CA    . PHE   B 1 228 ? 9.581   0.580   80.172  1.00 30.84  ? 1138 PHE   B CA    1 
ATOM   3927 C  C     . PHE   B 1 228 ? 8.917   -0.778  80.028  1.00 31.27  ? 1138 PHE   B C     1 
ATOM   3928 O  O     . PHE   B 1 228 ? 8.787   -1.510  81.011  1.00 32.66  ? 1138 PHE   B O     1 
ATOM   3929 C  CB    . PHE   B 1 228 ? 11.089  0.374   80.372  1.00 31.70  ? 1138 PHE   B CB    1 
ATOM   3930 C  CG    . PHE   B 1 228 ? 11.891  1.634   80.266  1.00 34.12  ? 1138 PHE   B CG    1 
ATOM   3931 C  CD1   . PHE   B 1 228 ? 12.055  2.263   79.038  1.00 34.95  ? 1138 PHE   B CD1   1 
ATOM   3932 C  CD2   . PHE   B 1 228 ? 12.490  2.180   81.381  1.00 32.29  ? 1138 PHE   B CD2   1 
ATOM   3933 C  CE1   . PHE   B 1 228 ? 12.779  3.418   78.931  1.00 31.91  ? 1138 PHE   B CE1   1 
ATOM   3934 C  CE2   . PHE   B 1 228 ? 13.223  3.338   81.286  1.00 32.31  ? 1138 PHE   B CE2   1 
ATOM   3935 C  CZ    . PHE   B 1 228 ? 13.371  3.959   80.060  1.00 36.75  ? 1138 PHE   B CZ    1 
ATOM   3936 N  N     . PHE   B 1 229 ? 8.530   -1.120  78.801  1.00 34.67  ? 1139 PHE   B N     1 
ATOM   3937 C  CA    . PHE   B 1 229 ? 7.954   -2.419  78.461  1.00 32.76  ? 1139 PHE   B CA    1 
ATOM   3938 C  C     . PHE   B 1 229 ? 8.739   -3.028  77.313  1.00 33.72  ? 1139 PHE   B C     1 
ATOM   3939 O  O     . PHE   B 1 229 ? 9.223   -2.310  76.439  1.00 33.93  ? 1139 PHE   B O     1 
ATOM   3940 C  CB    . PHE   B 1 229 ? 6.481   -2.312  78.016  1.00 33.05  ? 1139 PHE   B CB    1 
ATOM   3941 C  CG    . PHE   B 1 229 ? 5.542   -1.953  79.109  1.00 32.34  ? 1139 PHE   B CG    1 
ATOM   3942 C  CD1   . PHE   B 1 229 ? 5.306   -0.629  79.420  1.00 33.74  ? 1139 PHE   B CD1   1 
ATOM   3943 C  CD2   . PHE   B 1 229 ? 4.884   -2.940  79.823  1.00 33.80  ? 1139 PHE   B CD2   1 
ATOM   3944 C  CE1   . PHE   B 1 229 ? 4.416   -0.278  80.434  1.00 36.18  ? 1139 PHE   B CE1   1 
ATOM   3945 C  CE2   . PHE   B 1 229 ? 3.988   -2.609  80.840  1.00 35.46  ? 1139 PHE   B CE2   1 
ATOM   3946 C  CZ    . PHE   B 1 229 ? 3.760   -1.273  81.152  1.00 33.74  ? 1139 PHE   B CZ    1 
ATOM   3947 N  N     . SER   B 1 230 ? 8.833   -4.357  77.289  1.00 34.49  ? 1140 SER   B N     1 
ATOM   3948 C  CA    . SER   B 1 230 ? 9.528   -5.002  76.184  1.00 35.55  ? 1140 SER   B CA    1 
ATOM   3949 C  C     . SER   B 1 230 ? 8.765   -4.780  74.889  1.00 38.14  ? 1140 SER   B C     1 
ATOM   3950 O  O     . SER   B 1 230 ? 7.550   -4.994  74.827  1.00 38.29  ? 1140 SER   B O     1 
ATOM   3951 C  CB    . SER   B 1 230 ? 9.715   -6.497  76.434  1.00 36.43  ? 1140 SER   B CB    1 
ATOM   3952 O  OG    . SER   B 1 230 ? 8.595   -7.094  77.040  1.00 36.61  ? 1140 SER   B OG    1 
ATOM   3953 N  N     . SER   B 1 231 ? 9.477   -4.313  73.868  1.00 36.75  ? 1141 SER   B N     1 
ATOM   3954 C  CA    . SER   B 1 231 ? 8.920   -4.191  72.529  1.00 37.82  ? 1141 SER   B CA    1 
ATOM   3955 C  C     . SER   B 1 231 ? 8.805   -5.533  71.825  1.00 40.80  ? 1141 SER   B C     1 
ATOM   3956 O  O     . SER   B 1 231 ? 8.100   -5.632  70.819  1.00 45.30  ? 1141 SER   B O     1 
ATOM   3957 C  CB    . SER   B 1 231 ? 9.793   -3.246  71.702  1.00 44.03  ? 1141 SER   B CB    1 
ATOM   3958 O  OG    . SER   B 1 231 ? 11.122  -3.750  71.559  1.00 38.38  ? 1141 SER   B OG    1 
ATOM   3959 N  N     . ARG   B 1 232 ? 9.478   -6.558  72.335  1.00 39.39  ? 1142 ARG   B N     1 
ATOM   3960 C  CA    . ARG   B 1 232 ? 9.542   -7.870  71.708  1.00 40.88  ? 1142 ARG   B CA    1 
ATOM   3961 C  C     . ARG   B 1 232 ? 9.836   -8.877  72.807  1.00 44.11  ? 1142 ARG   B C     1 
ATOM   3962 O  O     . ARG   B 1 232 ? 10.107  -8.507  73.952  1.00 39.61  ? 1142 ARG   B O     1 
ATOM   3963 C  CB    . ARG   B 1 232 ? 10.601  -7.921  70.600  1.00 42.08  ? 1142 ARG   B CB    1 
ATOM   3964 C  CG    . ARG   B 1 232 ? 12.042  -7.535  71.034  1.00 41.04  ? 1142 ARG   B CG    1 
ATOM   3965 C  CD    . ARG   B 1 232 ? 13.006  -7.780  69.883  1.00 42.25  ? 1142 ARG   B CD    1 
ATOM   3966 N  NE    . ARG   B 1 232 ? 14.326  -7.161  70.025  1.00 48.79  ? 1142 ARG   B NE    1 
ATOM   3967 C  CZ    . ARG   B 1 232 ? 15.363  -7.728  70.631  1.00 48.51  ? 1142 ARG   B CZ    1 
ATOM   3968 N  NH1   . ARG   B 1 232 ? 15.237  -8.871  71.284  1.00 49.59  ? 1142 ARG   B NH1   1 
ATOM   3969 N  NH2   . ARG   B 1 232 ? 16.556  -7.131  70.585  1.00 42.22  ? 1142 ARG   B NH2   1 
ATOM   3970 N  N     . ASP   B 1 233 ? 9.736   -10.160 72.459  1.00 48.29  ? 1143 ASP   B N     1 
ATOM   3971 C  CA    . ASP   B 1 233 ? 10.246  -11.190 73.352  1.00 45.60  ? 1143 ASP   B CA    1 
ATOM   3972 C  C     . ASP   B 1 233 ? 11.744  -10.984 73.508  1.00 48.71  ? 1143 ASP   B C     1 
ATOM   3973 O  O     . ASP   B 1 233 ? 12.425  -10.580 72.561  1.00 51.27  ? 1143 ASP   B O     1 
ATOM   3974 C  CB    . ASP   B 1 233 ? 9.947   -12.588 72.804  1.00 45.04  ? 1143 ASP   B CB    1 
ATOM   3975 C  CG    . ASP   B 1 233 ? 8.453   -12.925 72.811  1.00 51.03  ? 1143 ASP   B CG    1 
ATOM   3976 O  OD1   . ASP   B 1 233 ? 7.628   -12.109 73.309  1.00 47.38  ? 1143 ASP   B OD1   1 
ATOM   3977 O  OD2   . ASP   B 1 233 ? 8.108   -14.019 72.309  1.00 52.17  ? 1143 ASP   B OD2   1 
ATOM   3978 N  N     . ILE   B 1 234 ? 12.258  -11.223 74.714  1.00 49.19  ? 1144 ILE   B N     1 
ATOM   3979 C  CA    . ILE   B 1 234 ? 13.665  -10.963 75.019  1.00 44.21  ? 1144 ILE   B CA    1 
ATOM   3980 C  C     . ILE   B 1 234 ? 14.290  -12.226 75.605  1.00 45.64  ? 1144 ILE   B C     1 
ATOM   3981 O  O     . ILE   B 1 234 ? 13.773  -12.785 76.583  1.00 45.47  ? 1144 ILE   B O     1 
ATOM   3982 C  CB    . ILE   B 1 234 ? 13.827  -9.772  75.977  1.00 42.41  ? 1144 ILE   B CB    1 
ATOM   3983 C  CG1   . ILE   B 1 234 ? 13.187  -8.516  75.373  1.00 38.83  ? 1144 ILE   B CG1   1 
ATOM   3984 C  CG2   . ILE   B 1 234 ? 15.309  -9.509  76.256  1.00 48.33  ? 1144 ILE   B CG2   1 
ATOM   3985 C  CD1   . ILE   B 1 234 ? 13.309  -7.293  76.262  1.00 38.16  ? 1144 ILE   B CD1   1 
ATOM   3986 N  N     . ARG   B 1 235 ? 15.399  -12.673 75.009  1.00 45.47  ? 1145 ARG   B N     1 
ATOM   3987 C  CA    . ARG   B 1 235 ? 16.092  -13.869 75.468  1.00 45.16  ? 1145 ARG   B CA    1 
ATOM   3988 C  C     . ARG   B 1 235 ? 16.863  -13.584 76.754  1.00 47.22  ? 1145 ARG   B C     1 
ATOM   3989 O  O     . ARG   B 1 235 ? 17.124  -12.433 77.113  1.00 49.75  ? 1145 ARG   B O     1 
ATOM   3990 C  CB    . ARG   B 1 235 ? 17.065  -14.378 74.402  1.00 48.91  ? 1145 ARG   B CB    1 
ATOM   3991 C  CG    . ARG   B 1 235 ? 16.441  -15.042 73.175  1.00 49.27  ? 1145 ARG   B CG    1 
ATOM   3992 C  CD    . ARG   B 1 235 ? 17.553  -15.561 72.277  1.00 59.22  ? 1145 ARG   B CD    1 
ATOM   3993 N  NE    . ARG   B 1 235 ? 17.106  -16.532 71.288  1.00 63.63  ? 1145 ARG   B NE    1 
ATOM   3994 C  CZ    . ARG   B 1 235 ? 17.922  -17.294 70.572  1.00 65.49  ? 1145 ARG   B CZ    1 
ATOM   3995 N  NH1   . ARG   B 1 235 ? 19.236  -17.240 70.733  1.00 66.62  ? 1145 ARG   B NH1   1 
ATOM   3996 N  NH2   . ARG   B 1 235 ? 17.410  -18.130 69.673  1.00 75.81  ? 1145 ARG   B NH2   1 
ATOM   3997 N  N     . THR   B 1 236 ? 17.247  -14.655 77.442  1.00 45.32  ? 1146 THR   B N     1 
ATOM   3998 C  CA    . THR   B 1 236 ? 18.005  -14.506 78.676  1.00 45.12  ? 1146 THR   B CA    1 
ATOM   3999 C  C     . THR   B 1 236 ? 19.436  -14.057 78.377  1.00 49.17  ? 1146 THR   B C     1 
ATOM   4000 O  O     . THR   B 1 236 ? 20.085  -14.558 77.454  1.00 46.30  ? 1146 THR   B O     1 
ATOM   4001 C  CB    . THR   B 1 236 ? 18.010  -15.823 79.447  1.00 46.74  ? 1146 THR   B CB    1 
ATOM   4002 O  OG1   . THR   B 1 236 ? 16.660  -16.261 79.636  1.00 54.70  ? 1146 THR   B OG1   1 
ATOM   4003 C  CG2   . THR   B 1 236 ? 18.650  -15.652 80.800  1.00 46.68  ? 1146 THR   B CG2   1 
ATOM   4004 N  N     . GLY   B 1 237 ? 19.921  -13.095 79.159  1.00 51.04  ? 1147 GLY   B N     1 
ATOM   4005 C  CA    . GLY   B 1 237 ? 21.245  -12.549 78.964  1.00 51.95  ? 1147 GLY   B CA    1 
ATOM   4006 C  C     . GLY   B 1 237 ? 21.312  -11.382 78.006  1.00 49.28  ? 1147 GLY   B C     1 
ATOM   4007 O  O     . GLY   B 1 237 ? 22.384  -10.780 77.869  1.00 48.21  ? 1147 GLY   B O     1 
ATOM   4008 N  N     . GLU   B 1 238 ? 20.208  -11.032 77.352  1.00 42.59  ? 1148 GLU   B N     1 
ATOM   4009 C  CA    . GLU   B 1 238 ? 20.251  -10.080 76.258  1.00 42.10  ? 1148 GLU   B CA    1 
ATOM   4010 C  C     . GLU   B 1 238 ? 20.103  -8.648  76.781  1.00 44.58  ? 1148 GLU   B C     1 
ATOM   4011 O  O     . GLU   B 1 238 ? 19.430  -8.393  77.787  1.00 40.22  ? 1148 GLU   B O     1 
ATOM   4012 C  CB    . GLU   B 1 238 ? 19.164  -10.423 75.233  1.00 45.02  ? 1148 GLU   B CB    1 
ATOM   4013 C  CG    . GLU   B 1 238 ? 19.007  -9.438  74.074  1.00 47.81  ? 1148 GLU   B CG    1 
ATOM   4014 C  CD    . GLU   B 1 238 ? 17.674  -9.599  73.349  1.00 50.43  ? 1148 GLU   B CD    1 
ATOM   4015 O  OE1   . GLU   B 1 238 ? 17.020  -10.654 73.538  1.00 48.12  ? 1148 GLU   B OE1   1 
ATOM   4016 O  OE2   . GLU   B 1 238 ? 17.285  -8.670  72.598  1.00 48.55  ? 1148 GLU   B OE2   1 
ATOM   4017 N  N     . GLU   B 1 239 ? 20.759  -7.710  76.099  1.00 40.66  ? 1149 GLU   B N     1 
ATOM   4018 C  CA    . GLU   B 1 239 ? 20.901  -6.367  76.642  1.00 39.72  ? 1149 GLU   B CA    1 
ATOM   4019 C  C     . GLU   B 1 239 ? 19.630  -5.555  76.434  1.00 40.64  ? 1149 GLU   B C     1 
ATOM   4020 O  O     . GLU   B 1 239 ? 19.159  -5.389  75.304  1.00 40.26  ? 1149 GLU   B O     1 
ATOM   4021 C  CB    . GLU   B 1 239 ? 22.091  -5.641  76.020  1.00 42.18  ? 1149 GLU   B CB    1 
ATOM   4022 C  CG    . GLU   B 1 239 ? 22.124  -4.152  76.390  1.00 41.43  ? 1149 GLU   B CG    1 
ATOM   4023 C  CD    . GLU   B 1 239 ? 23.524  -3.595  76.464  1.00 41.11  ? 1149 GLU   B CD    1 
ATOM   4024 O  OE1   . GLU   B 1 239 ? 24.401  -4.116  75.753  1.00 44.46  ? 1149 GLU   B OE1   1 
ATOM   4025 O  OE2   . GLU   B 1 239 ? 23.753  -2.651  77.243  1.00 40.15  ? 1149 GLU   B OE2   1 
ATOM   4026 N  N     . LEU   B 1 240 ? 19.100  -5.024  77.525  1.00 37.72  ? 1150 LEU   B N     1 
ATOM   4027 C  CA    . LEU   B 1 240 ? 18.027  -4.054  77.431  1.00 39.24  ? 1150 LEU   B CA    1 
ATOM   4028 C  C     . LEU   B 1 240 ? 18.563  -2.719  76.928  1.00 39.77  ? 1150 LEU   B C     1 
ATOM   4029 O  O     . LEU   B 1 240 ? 19.664  -2.283  77.279  1.00 38.70  ? 1150 LEU   B O     1 
ATOM   4030 C  CB    . LEU   B 1 240 ? 17.348  -3.876  78.790  1.00 35.64  ? 1150 LEU   B CB    1 
ATOM   4031 C  CG    . LEU   B 1 240 ? 16.832  -5.146  79.459  1.00 41.36  ? 1150 LEU   B CG    1 
ATOM   4032 C  CD1   . LEU   B 1 240 ? 15.919  -4.776  80.620  1.00 39.55  ? 1150 LEU   B CD1   1 
ATOM   4033 C  CD2   . LEU   B 1 240 ? 16.111  -6.068  78.468  1.00 39.33  ? 1150 LEU   B CD2   1 
ATOM   4034 N  N     . GLY   B 1 241 ? 17.772  -2.068  76.096  1.00 39.53  ? 1151 GLY   B N     1 
ATOM   4035 C  CA    . GLY   B 1 241 ? 18.122  -0.753  75.627  1.00 37.65  ? 1151 GLY   B CA    1 
ATOM   4036 C  C     . GLY   B 1 241 ? 16.931  -0.121  74.965  1.00 36.19  ? 1151 GLY   B C     1 
ATOM   4037 O  O     . GLY   B 1 241 ? 16.097  -0.835  74.402  1.00 37.39  ? 1151 GLY   B O     1 
ATOM   4038 N  N     . PHE   B 1 242 ? 16.821  1.203   75.046  1.00 36.98  ? 1152 PHE   B N     1 
ATOM   4039 C  CA    . PHE   B 1 242 ? 15.761  1.932   74.373  1.00 36.01  ? 1152 PHE   B CA    1 
ATOM   4040 C  C     . PHE   B 1 242 ? 16.386  2.988   73.479  1.00 37.20  ? 1152 PHE   B C     1 
ATOM   4041 O  O     . PHE   B 1 242 ? 17.541  3.377   73.669  1.00 37.47  ? 1152 PHE   B O     1 
ATOM   4042 C  CB    . PHE   B 1 242 ? 14.768  2.567   75.377  1.00 37.05  ? 1152 PHE   B CB    1 
ATOM   4043 C  CG    . PHE   B 1 242 ? 15.385  3.569   76.320  1.00 36.27  ? 1152 PHE   B CG    1 
ATOM   4044 C  CD1   . PHE   B 1 242 ? 16.186  3.157   77.384  1.00 38.66  ? 1152 PHE   B CD1   1 
ATOM   4045 C  CD2   . PHE   B 1 242 ? 15.155  4.921   76.156  1.00 34.74  ? 1152 PHE   B CD2   1 
ATOM   4046 C  CE1   . PHE   B 1 242 ? 16.739  4.079   78.250  1.00 34.21  ? 1152 PHE   B CE1   1 
ATOM   4047 C  CE2   . PHE   B 1 242 ? 15.717  5.848   77.022  1.00 38.88  ? 1152 PHE   B CE2   1 
ATOM   4048 C  CZ    . PHE   B 1 242 ? 16.506  5.429   78.065  1.00 34.42  ? 1152 PHE   B CZ    1 
ATOM   4049 N  N     . ASP   B 1 243 ? 15.621  3.437   72.482  1.00 37.52  ? 1153 ASP   B N     1 
ATOM   4050 C  CA    . ASP   B 1 243 ? 16.077  4.508   71.591  1.00 41.06  ? 1153 ASP   B CA    1 
ATOM   4051 C  C     . ASP   B 1 243 ? 16.060  5.827   72.358  1.00 39.76  ? 1153 ASP   B C     1 
ATOM   4052 O  O     . ASP   B 1 243 ? 14.998  6.421   72.581  1.00 44.74  ? 1153 ASP   B O     1 
ATOM   4053 C  CB    . ASP   B 1 243 ? 15.211  4.583   70.336  1.00 39.63  ? 1153 ASP   B CB    1 
ATOM   4054 C  CG    . ASP   B 1 243 ? 15.809  5.489   69.252  1.00 42.47  ? 1153 ASP   B CG    1 
ATOM   4055 O  OD1   . ASP   B 1 243 ? 16.791  6.215   69.518  1.00 41.73  ? 1153 ASP   B OD1   1 
ATOM   4056 O  OD2   . ASP   B 1 243 ? 15.287  5.476   68.118  1.00 50.31  ? 1153 ASP   B OD2   1 
ATOM   4057 N  N     . TYR   B 1 244 ? 17.250  6.266   72.776  1.00 38.83  ? 1154 TYR   B N     1 
ATOM   4058 C  CA    . TYR   B 1 244 ? 17.434  7.557   73.432  1.00 42.83  ? 1154 TYR   B CA    1 
ATOM   4059 C  C     . TYR   B 1 244 ? 16.856  8.698   72.615  1.00 40.76  ? 1154 TYR   B C     1 
ATOM   4060 O  O     . TYR   B 1 244 ? 16.467  9.725   73.176  1.00 45.53  ? 1154 TYR   B O     1 
ATOM   4061 C  CB    . TYR   B 1 244 ? 18.929  7.842   73.667  1.00 40.39  ? 1154 TYR   B CB    1 
ATOM   4062 C  CG    . TYR   B 1 244 ? 19.590  7.187   74.870  1.00 39.29  ? 1154 TYR   B CG    1 
ATOM   4063 C  CD1   . TYR   B 1 244 ? 19.008  6.121   75.535  1.00 37.79  ? 1154 TYR   B CD1   1 
ATOM   4064 C  CD2   . TYR   B 1 244 ? 20.805  7.662   75.342  1.00 40.47  ? 1154 TYR   B CD2   1 
ATOM   4065 C  CE1   . TYR   B 1 244 ? 19.621  5.538   76.623  1.00 37.37  ? 1154 TYR   B CE1   1 
ATOM   4066 C  CE2   . TYR   B 1 244 ? 21.422  7.091   76.418  1.00 40.65  ? 1154 TYR   B CE2   1 
ATOM   4067 C  CZ    . TYR   B 1 244 ? 20.837  6.027   77.058  1.00 40.29  ? 1154 TYR   B CZ    1 
ATOM   4068 O  OH    . TYR   B 1 244 ? 21.477  5.465   78.144  1.00 38.09  ? 1154 TYR   B OH    1 
ATOM   4069 N  N     . GLY   B 1 245 ? 16.831  8.564   71.300  1.00 41.09  ? 1155 GLY   B N     1 
ATOM   4070 C  CA    . GLY   B 1 245 ? 16.241  9.570   70.444  1.00 43.45  ? 1155 GLY   B CA    1 
ATOM   4071 C  C     . GLY   B 1 245 ? 17.289  10.353  69.680  1.00 48.95  ? 1155 GLY   B C     1 
ATOM   4072 O  O     . GLY   B 1 245 ? 18.495  10.181  69.856  1.00 54.61  ? 1155 GLY   B O     1 
ATOM   4073 N  N     . ASP   B 1 246 ? 16.794  11.222  68.797  1.00 47.04  ? 1156 ASP   B N     1 
ATOM   4074 C  CA    . ASP   B 1 246 ? 17.659  12.059  67.972  1.00 52.44  ? 1156 ASP   B CA    1 
ATOM   4075 C  C     . ASP   B 1 246 ? 18.064  13.355  68.654  1.00 55.16  ? 1156 ASP   B C     1 
ATOM   4076 O  O     . ASP   B 1 246 ? 19.005  14.006  68.195  1.00 59.66  ? 1156 ASP   B O     1 
ATOM   4077 C  CB    . ASP   B 1 246 ? 16.982  12.413  66.641  1.00 56.46  ? 1156 ASP   B CB    1 
ATOM   4078 C  CG    . ASP   B 1 246 ? 17.060  11.296  65.618  1.00 60.62  ? 1156 ASP   B CG    1 
ATOM   4079 O  OD1   . ASP   B 1 246 ? 17.441  10.159  65.975  1.00 62.39  ? 1156 ASP   B OD1   1 
ATOM   4080 O  OD2   . ASP   B 1 246 ? 16.738  11.566  64.439  1.00 61.98  ? 1156 ASP   B OD2   1 
ATOM   4081 N  N     . ARG   B 1 247 ? 17.362  13.770  69.710  1.00 55.88  ? 1157 ARG   B N     1 
ATOM   4082 C  CA    . ARG   B 1 247 ? 17.796  14.958  70.435  1.00 57.88  ? 1157 ARG   B CA    1 
ATOM   4083 C  C     . ARG   B 1 247 ? 19.033  14.655  71.262  1.00 60.47  ? 1157 ARG   B C     1 
ATOM   4084 O  O     . ARG   B 1 247 ? 19.936  15.492  71.370  1.00 63.02  ? 1157 ARG   B O     1 
ATOM   4085 C  CB    . ARG   B 1 247 ? 16.681  15.487  71.336  1.00 60.07  ? 1157 ARG   B CB    1 
ATOM   4086 C  CG    . ARG   B 1 247 ? 17.024  16.829  71.959  1.00 61.51  ? 1157 ARG   B CG    1 
ATOM   4087 C  CD    . ARG   B 1 247 ? 16.156  17.176  73.157  1.00 59.71  ? 1157 ARG   B CD    1 
ATOM   4088 N  NE    . ARG   B 1 247 ? 16.423  18.542  73.592  1.00 61.88  ? 1157 ARG   B NE    1 
ATOM   4089 C  CZ    . ARG   B 1 247 ? 16.031  19.057  74.749  1.00 61.56  ? 1157 ARG   B CZ    1 
ATOM   4090 N  NH1   . ARG   B 1 247 ? 15.350  18.341  75.626  1.00 62.15  ? 1157 ARG   B NH1   1 
ATOM   4091 N  NH2   . ARG   B 1 247 ? 16.333  20.322  75.032  1.00 59.41  ? 1157 ARG   B NH2   1 
ATOM   4092 N  N     . PHE   B 1 248 ? 19.085  13.461  71.854  1.00 58.14  ? 1158 PHE   B N     1 
ATOM   4093 C  CA    . PHE   B 1 248 ? 20.267  13.050  72.601  1.00 58.75  ? 1158 PHE   B CA    1 
ATOM   4094 C  C     . PHE   B 1 248 ? 21.498  13.006  71.701  1.00 60.71  ? 1158 PHE   B C     1 
ATOM   4095 O  O     . PHE   B 1 248 ? 22.587  13.440  72.098  1.00 58.12  ? 1158 PHE   B O     1 
ATOM   4096 C  CB    . PHE   B 1 248 ? 20.009  11.686  73.250  1.00 51.19  ? 1158 PHE   B CB    1 
ATOM   4097 C  CG    . PHE   B 1 248 ? 21.126  11.200  74.138  1.00 52.54  ? 1158 PHE   B CG    1 
ATOM   4098 C  CD1   . PHE   B 1 248 ? 22.196  10.489  73.611  1.00 50.14  ? 1158 PHE   B CD1   1 
ATOM   4099 C  CD2   . PHE   B 1 248 ? 21.092  11.432  75.506  1.00 52.38  ? 1158 PHE   B CD2   1 
ATOM   4100 C  CE1   . PHE   B 1 248 ? 23.212  10.035  74.428  1.00 49.58  ? 1158 PHE   B CE1   1 
ATOM   4101 C  CE2   . PHE   B 1 248 ? 22.118  10.979  76.327  1.00 50.71  ? 1158 PHE   B CE2   1 
ATOM   4102 C  CZ    . PHE   B 1 248 ? 23.170  10.278  75.787  1.00 47.86  ? 1158 PHE   B CZ    1 
ATOM   4103 N  N     . TRP   B 1 249 ? 21.336  12.511  70.476  1.00 59.87  ? 1159 TRP   B N     1 
ATOM   4104 C  CA    . TRP   B 1 249 ? 22.468  12.254  69.603  1.00 61.50  ? 1159 TRP   B CA    1 
ATOM   4105 C  C     . TRP   B 1 249 ? 22.892  13.454  68.772  1.00 66.78  ? 1159 TRP   B C     1 
ATOM   4106 O  O     . TRP   B 1 249 ? 24.019  13.460  68.268  1.00 71.49  ? 1159 TRP   B O     1 
ATOM   4107 C  CB    . TRP   B 1 249 ? 22.157  11.080  68.679  1.00 56.66  ? 1159 TRP   B CB    1 
ATOM   4108 C  CG    . TRP   B 1 249 ? 22.210  9.776   69.381  1.00 54.05  ? 1159 TRP   B CG    1 
ATOM   4109 C  CD1   . TRP   B 1 249 ? 21.160  8.969   69.683  1.00 50.65  ? 1159 TRP   B CD1   1 
ATOM   4110 C  CD2   . TRP   B 1 249 ? 23.379  9.126   69.894  1.00 52.93  ? 1159 TRP   B CD2   1 
ATOM   4111 N  NE1   . TRP   B 1 249 ? 21.597  7.848   70.343  1.00 52.09  ? 1159 TRP   B NE1   1 
ATOM   4112 C  CE2   . TRP   B 1 249 ? 22.958  7.919   70.485  1.00 51.40  ? 1159 TRP   B CE2   1 
ATOM   4113 C  CE3   . TRP   B 1 249 ? 24.739  9.440   69.899  1.00 55.66  ? 1159 TRP   B CE3   1 
ATOM   4114 C  CZ2   . TRP   B 1 249 ? 23.850  7.027   71.082  1.00 47.92  ? 1159 TRP   B CZ2   1 
ATOM   4115 C  CZ3   . TRP   B 1 249 ? 25.627  8.551   70.496  1.00 55.30  ? 1159 TRP   B CZ3   1 
ATOM   4116 C  CH2   . TRP   B 1 249 ? 25.175  7.360   71.076  1.00 51.31  ? 1159 TRP   B CH2   1 
ATOM   4117 N  N     . ASP   B 1 250 ? 22.031  14.458  68.589  1.00 69.16  ? 1160 ASP   B N     1 
ATOM   4118 C  CA    . ASP   B 1 250 ? 22.549  15.704  68.040  1.00 72.18  ? 1160 ASP   B CA    1 
ATOM   4119 C  C     . ASP   B 1 250 ? 23.374  16.451  69.080  1.00 74.37  ? 1160 ASP   B C     1 
ATOM   4120 O  O     . ASP   B 1 250 ? 24.243  17.251  68.710  1.00 79.59  ? 1160 ASP   B O     1 
ATOM   4121 C  CB    . ASP   B 1 250 ? 21.422  16.587  67.485  1.00 72.86  ? 1160 ASP   B CB    1 
ATOM   4122 C  CG    . ASP   B 1 250 ? 20.446  17.055  68.550  1.00 75.37  ? 1160 ASP   B CG    1 
ATOM   4123 O  OD1   . ASP   B 1 250 ? 20.889  17.547  69.608  1.00 75.15  ? 1160 ASP   B OD1   1 
ATOM   4124 O  OD2   . ASP   B 1 250 ? 19.222  16.960  68.319  1.00 78.00  ? 1160 ASP   B OD2   1 
ATOM   4125 N  N     . ILE   B 1 251 ? 23.132  16.186  70.365  1.00 68.83  ? 1161 ILE   B N     1 
ATOM   4126 C  CA    . ILE   B 1 251 ? 23.955  16.759  71.429  1.00 68.63  ? 1161 ILE   B CA    1 
ATOM   4127 C  C     . ILE   B 1 251 ? 25.279  16.011  71.558  1.00 71.53  ? 1161 ILE   B C     1 
ATOM   4128 O  O     . ILE   B 1 251 ? 26.362  16.594  71.414  1.00 72.32  ? 1161 ILE   B O     1 
ATOM   4129 C  CB    . ILE   B 1 251 ? 23.192  16.748  72.764  1.00 64.98  ? 1161 ILE   B CB    1 
ATOM   4130 C  CG1   . ILE   B 1 251 ? 22.005  17.703  72.722  1.00 62.47  ? 1161 ILE   B CG1   1 
ATOM   4131 C  CG2   . ILE   B 1 251 ? 24.123  17.110  73.914  1.00 61.88  ? 1161 ILE   B CG2   1 
ATOM   4132 C  CD1   . ILE   B 1 251 ? 21.206  17.714  74.004  1.00 56.07  ? 1161 ILE   B CD1   1 
ATOM   4133 N  N     . LYS   B 1 252 ? 25.209  14.709  71.856  1.00 69.95  ? 1162 LYS   B N     1 
ATOM   4134 C  CA    . LYS   B 1 252 ? 26.387  13.910  72.164  1.00 71.61  ? 1162 LYS   B CA    1 
ATOM   4135 C  C     . LYS   B 1 252 ? 27.049  13.402  70.888  1.00 76.24  ? 1162 LYS   B C     1 
ATOM   4136 O  O     . LYS   B 1 252 ? 27.678  12.337  70.895  1.00 74.32  ? 1162 LYS   B O     1 
ATOM   4137 C  CB    . LYS   B 1 252 ? 26.024  12.724  73.075  1.00 65.63  ? 1162 LYS   B CB    1 
ATOM   4138 C  CG    . LYS   B 1 252 ? 25.468  13.084  74.470  1.00 62.66  ? 1162 LYS   B CG    1 
ATOM   4139 C  CD    . LYS   B 1 252 ? 26.570  13.282  75.527  1.00 65.11  ? 1162 LYS   B CD    1 
ATOM   4140 C  CE    . LYS   B 1 252 ? 26.018  13.222  76.957  1.00 57.78  ? 1162 LYS   B CE    1 
ATOM   4141 N  NZ    . LYS   B 1 252 ? 27.101  13.338  77.988  1.00 55.81  ? 1162 LYS   B NZ    1 
ATOM   4142 N  N     . SER   B 1 253 ? 26.898  14.143  69.786  1.00 79.70  ? 1163 SER   B N     1 
ATOM   4143 C  CA    . SER   B 1 253 ? 27.576  13.781  68.545  1.00 84.45  ? 1163 SER   B CA    1 
ATOM   4144 C  C     . SER   B 1 253 ? 28.999  14.329  68.493  1.00 84.45  ? 1163 SER   B C     1 
ATOM   4145 O  O     . SER   B 1 253 ? 29.859  13.760  67.809  1.00 80.99  ? 1163 SER   B O     1 
ATOM   4146 C  CB    . SER   B 1 253 ? 26.771  14.271  67.336  1.00 81.81  ? 1163 SER   B CB    1 
ATOM   4147 O  OG    . SER   B 1 253 ? 26.374  15.626  67.483  1.00 79.65  ? 1163 SER   B OG    1 
ATOM   4148 N  N     . LYS   B 1 254 ? 29.270  15.412  69.210  1.00 92.50  ? 1164 LYS   B N     1 
ATOM   4149 C  CA    . LYS   B 1 254 ? 30.620  15.949  69.264  1.00 97.28  ? 1164 LYS   B CA    1 
ATOM   4150 C  C     . LYS   B 1 254 ? 31.525  15.179  70.214  1.00 98.20  ? 1164 LYS   B C     1 
ATOM   4151 O  O     . LYS   B 1 254 ? 32.741  15.408  70.201  1.00 102.67 ? 1164 LYS   B O     1 
ATOM   4152 C  CB    . LYS   B 1 254 ? 30.587  17.425  69.677  1.00 98.15  ? 1164 LYS   B CB    1 
ATOM   4153 N  N     . TYR   B 1 255 ? 30.976  14.273  71.024  1.00 80.39  ? 1165 TYR   B N     1 
ATOM   4154 C  CA    . TYR   B 1 255 ? 31.722  13.657  72.117  1.00 72.51  ? 1165 TYR   B CA    1 
ATOM   4155 C  C     . TYR   B 1 255 ? 31.961  12.174  71.859  1.00 66.48  ? 1165 TYR   B C     1 
ATOM   4156 O  O     . TYR   B 1 255 ? 33.094  11.778  71.593  1.00 68.38  ? 1165 TYR   B O     1 
ATOM   4157 C  CB    . TYR   B 1 255 ? 30.992  13.895  73.437  1.00 72.85  ? 1165 TYR   B CB    1 
ATOM   4158 C  CG    . TYR   B 1 255 ? 30.792  15.366  73.736  1.00 75.26  ? 1165 TYR   B CG    1 
ATOM   4159 C  CD1   . TYR   B 1 255 ? 31.731  16.311  73.324  1.00 79.24  ? 1165 TYR   B CD1   1 
ATOM   4160 C  CD2   . TYR   B 1 255 ? 29.664  15.814  74.413  1.00 76.54  ? 1165 TYR   B CD2   1 
ATOM   4161 C  CE1   . TYR   B 1 255 ? 31.559  17.663  73.585  1.00 76.30  ? 1165 TYR   B CE1   1 
ATOM   4162 C  CE2   . TYR   B 1 255 ? 29.479  17.167  74.682  1.00 76.81  ? 1165 TYR   B CE2   1 
ATOM   4163 C  CZ    . TYR   B 1 255 ? 30.431  18.087  74.267  1.00 77.20  ? 1165 TYR   B CZ    1 
ATOM   4164 O  OH    . TYR   B 1 255 ? 30.251  19.432  74.532  1.00 72.32  ? 1165 TYR   B OH    1 
ATOM   4165 N  N     . PHE   B 1 256 ? 30.935  11.334  71.935  1.00 66.99  ? 1166 PHE   B N     1 
ATOM   4166 C  CA    . PHE   B 1 256 ? 31.102  9.928   71.585  1.00 58.21  ? 1166 PHE   B CA    1 
ATOM   4167 C  C     . PHE   B 1 256 ? 30.152  9.574   70.447  1.00 59.38  ? 1166 PHE   B C     1 
ATOM   4168 O  O     . PHE   B 1 256 ? 29.363  10.400  69.993  1.00 62.76  ? 1166 PHE   B O     1 
ATOM   4169 C  CB    . PHE   B 1 256 ? 30.913  9.021   72.810  1.00 53.86  ? 1166 PHE   B CB    1 
ATOM   4170 C  CG    . PHE   B 1 256 ? 29.639  9.256   73.568  1.00 60.11  ? 1166 PHE   B CG    1 
ATOM   4171 C  CD1   . PHE   B 1 256 ? 29.597  10.159  74.622  1.00 65.28  ? 1166 PHE   B CD1   1 
ATOM   4172 C  CD2   . PHE   B 1 256 ? 28.493  8.549   73.255  1.00 57.06  ? 1166 PHE   B CD2   1 
ATOM   4173 C  CE1   . PHE   B 1 256 ? 28.424  10.360  75.336  1.00 53.15  ? 1166 PHE   B CE1   1 
ATOM   4174 C  CE2   . PHE   B 1 256 ? 27.314  8.743   73.963  1.00 55.24  ? 1166 PHE   B CE2   1 
ATOM   4175 C  CZ    . PHE   B 1 256 ? 27.282  9.655   74.999  1.00 59.49  ? 1166 PHE   B CZ    1 
ATOM   4176 N  N     . THR   B 1 257 ? 30.268  8.346   69.951  1.00 54.82  ? 1167 THR   B N     1 
ATOM   4177 C  CA    . THR   B 1 257 ? 29.370  7.837   68.927  1.00 54.27  ? 1167 THR   B CA    1 
ATOM   4178 C  C     . THR   B 1 257 ? 28.767  6.523   69.395  1.00 55.18  ? 1167 THR   B C     1 
ATOM   4179 O  O     . THR   B 1 257 ? 29.308  5.844   70.273  1.00 56.36  ? 1167 THR   B O     1 
ATOM   4180 C  CB    . THR   B 1 257 ? 30.067  7.630   67.569  1.00 56.13  ? 1167 THR   B CB    1 
ATOM   4181 O  OG1   . THR   B 1 257 ? 31.300  6.918   67.748  1.00 58.54  ? 1167 THR   B OG1   1 
ATOM   4182 C  CG2   . THR   B 1 257 ? 30.323  8.961   66.891  1.00 58.04  ? 1167 THR   B CG2   1 
ATOM   4183 N  N     . CYS   B 1 258 ? 27.631  6.173   68.794  1.00 51.48  ? 1168 CYS   B N     1 
ATOM   4184 C  CA    . CYS   B 1 258 ? 26.948  4.940   69.156  1.00 54.45  ? 1168 CYS   B CA    1 
ATOM   4185 C  C     . CYS   B 1 258 ? 27.829  3.731   68.865  1.00 49.79  ? 1168 CYS   B C     1 
ATOM   4186 O  O     . CYS   B 1 258 ? 28.424  3.620   67.792  1.00 51.34  ? 1168 CYS   B O     1 
ATOM   4187 C  CB    . CYS   B 1 258 ? 25.626  4.826   68.397  1.00 50.89  ? 1168 CYS   B CB    1 
ATOM   4188 S  SG    . CYS   B 1 258 ? 24.582  3.479   68.966  1.00 47.71  ? 1168 CYS   B SG    1 
ATOM   4189 N  N     . GLN   B 1 259 ? 27.890  2.812   69.826  1.00 49.25  ? 1169 GLN   B N     1 
ATOM   4190 C  CA    . GLN   B 1 259 ? 28.654  1.581   69.696  1.00 51.71  ? 1169 GLN   B CA    1 
ATOM   4191 C  C     . GLN   B 1 259 ? 27.757  0.349   69.709  1.00 49.63  ? 1169 GLN   B C     1 
ATOM   4192 O  O     . GLN   B 1 259 ? 28.226  -0.750  70.013  1.00 51.29  ? 1169 GLN   B O     1 
ATOM   4193 C  CB    . GLN   B 1 259 ? 29.695  1.489   70.813  1.00 52.80  ? 1169 GLN   B CB    1 
ATOM   4194 C  CG    . GLN   B 1 259 ? 30.612  2.707   70.930  1.00 57.09  ? 1169 GLN   B CG    1 
ATOM   4195 C  CD    . GLN   B 1 259 ? 31.770  2.693   69.940  1.00 55.51  ? 1169 GLN   B CD    1 
ATOM   4196 O  OE1   . GLN   B 1 259 ? 32.439  1.677   69.761  1.00 56.53  ? 1169 GLN   B OE1   1 
ATOM   4197 N  NE2   . GLN   B 1 259 ? 32.006  3.828   69.292  1.00 54.44  ? 1169 GLN   B NE2   1 
ATOM   4198 N  N     . CYS   B 1 260 ? 26.474  0.510   69.387  1.00 52.35  ? 1170 CYS   B N     1 
ATOM   4199 C  CA    . CYS   B 1 260 ? 25.545  -0.604  69.537  1.00 52.98  ? 1170 CYS   B CA    1 
ATOM   4200 C  C     . CYS   B 1 260 ? 25.844  -1.721  68.550  1.00 50.28  ? 1170 CYS   B C     1 
ATOM   4201 O  O     . CYS   B 1 260 ? 25.515  -2.880  68.816  1.00 50.64  ? 1170 CYS   B O     1 
ATOM   4202 C  CB    . CYS   B 1 260 ? 24.102  -0.113  69.388  1.00 47.50  ? 1170 CYS   B CB    1 
ATOM   4203 S  SG    . CYS   B 1 260 ? 23.555  0.234   67.705  1.00 50.64  ? 1170 CYS   B SG    1 
ATOM   4204 N  N     . GLY   B 1 261 ? 26.454  -1.398  67.412  1.00 50.54  ? 1171 GLY   B N     1 
ATOM   4205 C  CA    . GLY   B 1 261 ? 26.775  -2.389  66.404  1.00 49.73  ? 1171 GLY   B CA    1 
ATOM   4206 C  C     . GLY   B 1 261 ? 25.662  -2.743  65.432  1.00 55.83  ? 1171 GLY   B C     1 
ATOM   4207 O  O     . GLY   B 1 261 ? 25.942  -3.397  64.423  1.00 52.10  ? 1171 GLY   B O     1 
ATOM   4208 N  N     . SER   B 1 262 ? 24.420  -2.318  65.682  1.00 53.18  ? 1172 SER   B N     1 
ATOM   4209 C  CA    . SER   B 1 262 ? 23.283  -2.741  64.864  1.00 55.28  ? 1172 SER   B CA    1 
ATOM   4210 C  C     . SER   B 1 262 ? 23.510  -2.475  63.378  1.00 61.27  ? 1172 SER   B C     1 
ATOM   4211 O  O     . SER   B 1 262 ? 24.035  -1.429  62.986  1.00 63.54  ? 1172 SER   B O     1 
ATOM   4212 C  CB    . SER   B 1 262 ? 22.019  -2.025  65.315  1.00 59.67  ? 1172 SER   B CB    1 
ATOM   4213 O  OG    . SER   B 1 262 ? 20.901  -2.432  64.531  1.00 66.19  ? 1172 SER   B OG    1 
ATOM   4214 N  N     . GLU   B 1 263 ? 23.090  -3.429  62.542  1.00 63.62  ? 1173 GLU   B N     1 
ATOM   4215 C  CA    . GLU   B 1 263 ? 23.205  -3.258  61.097  1.00 63.86  ? 1173 GLU   B CA    1 
ATOM   4216 C  C     . GLU   B 1 263 ? 22.352  -2.111  60.584  1.00 68.48  ? 1173 GLU   B C     1 
ATOM   4217 O  O     . GLU   B 1 263 ? 22.484  -1.735  59.412  1.00 71.38  ? 1173 GLU   B O     1 
ATOM   4218 C  CB    . GLU   B 1 263 ? 22.819  -4.544  60.368  1.00 60.82  ? 1173 GLU   B CB    1 
ATOM   4219 C  CG    . GLU   B 1 263 ? 23.551  -4.729  59.059  1.00 62.20  ? 1173 GLU   B CG    1 
ATOM   4220 C  CD    . GLU   B 1 263 ? 25.012  -5.090  59.278  1.00 68.69  ? 1173 GLU   B CD    1 
ATOM   4221 O  OE1   . GLU   B 1 263 ? 25.294  -5.802  60.266  1.00 66.24  ? 1173 GLU   B OE1   1 
ATOM   4222 O  OE2   . GLU   B 1 263 ? 25.876  -4.656  58.479  1.00 64.61  ? 1173 GLU   B OE2   1 
ATOM   4223 N  N     . LYS   B 1 264 ? 21.484  -1.557  61.429  1.00 68.10  ? 1174 LYS   B N     1 
ATOM   4224 C  CA    . LYS   B 1 264 ? 20.687  -0.377  61.125  1.00 70.83  ? 1174 LYS   B CA    1 
ATOM   4225 C  C     . LYS   B 1 264 ? 21.036  0.773   62.068  1.00 67.64  ? 1174 LYS   B C     1 
ATOM   4226 O  O     . LYS   B 1 264 ? 20.165  1.564   62.438  1.00 69.12  ? 1174 LYS   B O     1 
ATOM   4227 C  CB    . LYS   B 1 264 ? 19.195  -0.697  61.214  1.00 73.41  ? 1174 LYS   B CB    1 
ATOM   4228 C  CG    . LYS   B 1 264 ? 18.813  -2.083  60.703  1.00 74.77  ? 1174 LYS   B CG    1 
ATOM   4229 C  CD    . LYS   B 1 264 ? 17.400  -2.456  61.122  1.00 77.27  ? 1174 LYS   B CD    1 
ATOM   4230 C  CE    . LYS   B 1 264 ? 16.935  -3.724  60.419  1.00 84.78  ? 1174 LYS   B CE    1 
ATOM   4231 N  NZ    . LYS   B 1 264 ? 15.480  -3.984  60.643  1.00 82.16  ? 1174 LYS   B NZ    1 
ATOM   4232 N  N     . CYS   B 1 265 ? 22.302  0.869   62.473  1.00 61.72  ? 1175 CYS   B N     1 
ATOM   4233 C  CA    . CYS   B 1 265 ? 22.705  1.876   63.446  1.00 60.00  ? 1175 CYS   B CA    1 
ATOM   4234 C  C     . CYS   B 1 265 ? 22.721  3.260   62.813  1.00 57.69  ? 1175 CYS   B C     1 
ATOM   4235 O  O     . CYS   B 1 265 ? 23.299  3.464   61.743  1.00 58.11  ? 1175 CYS   B O     1 
ATOM   4236 C  CB    . CYS   B 1 265 ? 24.077  1.548   64.026  1.00 58.45  ? 1175 CYS   B CB    1 
ATOM   4237 S  SG    . CYS   B 1 265 ? 24.719  2.803   65.156  1.00 56.21  ? 1175 CYS   B SG    1 
ATOM   4238 N  N     . LYS   B 1 266 ? 22.078  4.209   63.486  1.00 57.31  ? 1176 LYS   B N     1 
ATOM   4239 C  CA    . LYS   B 1 266 ? 21.924  5.560   62.975  1.00 55.89  ? 1176 LYS   B CA    1 
ATOM   4240 C  C     . LYS   B 1 266 ? 23.001  6.504   63.482  1.00 54.57  ? 1176 LYS   B C     1 
ATOM   4241 O  O     . LYS   B 1 266 ? 23.264  7.530   62.842  1.00 56.77  ? 1176 LYS   B O     1 
ATOM   4242 C  CB    . LYS   B 1 266 ? 20.539  6.102   63.359  1.00 61.45  ? 1176 LYS   B CB    1 
ATOM   4243 C  CG    . LYS   B 1 266 ? 20.250  7.520   62.873  1.00 66.03  ? 1176 LYS   B CG    1 
ATOM   4244 C  CD    . LYS   B 1 266 ? 18.918  8.040   63.391  1.00 66.86  ? 1176 LYS   B CD    1 
ATOM   4245 C  CE    . LYS   B 1 266 ? 18.677  9.476   62.932  1.00 69.74  ? 1176 LYS   B CE    1 
ATOM   4246 N  NZ    . LYS   B 1 266 ? 17.225  9.812   62.948  1.00 70.77  ? 1176 LYS   B NZ    1 
ATOM   4247 N  N     . HIS   B 1 267 ? 23.653  6.171   64.593  1.00 54.10  ? 1177 HIS   B N     1 
ATOM   4248 C  CA    . HIS   B 1 267 ? 24.542  7.112   65.256  1.00 54.69  ? 1177 HIS   B CA    1 
ATOM   4249 C  C     . HIS   B 1 267 ? 25.968  6.583   65.411  1.00 54.51  ? 1177 HIS   B C     1 
ATOM   4250 O  O     . HIS   B 1 267 ? 26.689  7.017   66.311  1.00 52.99  ? 1177 HIS   B O     1 
ATOM   4251 C  CB    . HIS   B 1 267 ? 23.948  7.500   66.609  1.00 55.87  ? 1177 HIS   B CB    1 
ATOM   4252 C  CG    . HIS   B 1 267 ? 22.516  7.935   66.535  1.00 56.29  ? 1177 HIS   B CG    1 
ATOM   4253 N  ND1   . HIS   B 1 267 ? 22.140  9.203   66.141  1.00 56.55  ? 1177 HIS   B ND1   1 
ATOM   4254 C  CD2   . HIS   B 1 267 ? 21.366  7.265   66.787  1.00 55.09  ? 1177 HIS   B CD2   1 
ATOM   4255 C  CE1   . HIS   B 1 267 ? 20.823  9.295   66.159  1.00 54.24  ? 1177 HIS   B CE1   1 
ATOM   4256 N  NE2   . HIS   B 1 267 ? 20.330  8.135   66.549  1.00 53.42  ? 1177 HIS   B NE2   1 
ATOM   4257 N  N     . SER   B 1 268 ? 26.397  5.659   64.556  1.00 57.88  ? 1178 SER   B N     1 
ATOM   4258 C  CA    . SER   B 1 268 ? 27.798  5.262   64.544  1.00 54.96  ? 1178 SER   B CA    1 
ATOM   4259 C  C     . SER   B 1 268 ? 28.609  6.273   63.752  1.00 60.91  ? 1178 SER   B C     1 
ATOM   4260 O  O     . SER   B 1 268 ? 28.087  6.944   62.857  1.00 60.42  ? 1178 SER   B O     1 
ATOM   4261 C  CB    . SER   B 1 268 ? 27.979  3.879   63.926  1.00 55.08  ? 1178 SER   B CB    1 
ATOM   4262 O  OG    . SER   B 1 268 ? 27.888  3.957   62.519  1.00 56.75  ? 1178 SER   B OG    1 
ATOM   4263 N  N     . ALA   B 1 269 ? 29.905  6.370   64.088  1.00 58.78  ? 1179 ALA   B N     1 
ATOM   4264 C  CA    . ALA   B 1 269 ? 30.799  7.297   63.394  1.00 63.63  ? 1179 ALA   B CA    1 
ATOM   4265 C  C     . ALA   B 1 269 ? 30.696  7.149   61.884  1.00 65.34  ? 1179 ALA   B C     1 
ATOM   4266 O  O     . ALA   B 1 269 ? 30.697  8.145   61.152  1.00 67.19  ? 1179 ALA   B O     1 
ATOM   4267 C  CB    . ALA   B 1 269 ? 32.245  7.078   63.844  1.00 62.18  ? 1179 ALA   B CB    1 
ATOM   4268 N  N     . GLU   B 1 270 ? 30.598  5.909   61.403  1.00 64.18  ? 1180 GLU   B N     1 
ATOM   4269 C  CA    . GLU   B 1 270 ? 30.441  5.674   59.973  1.00 68.64  ? 1180 GLU   B CA    1 
ATOM   4270 C  C     . GLU   B 1 270 ? 29.153  6.294   59.447  1.00 71.16  ? 1180 GLU   B C     1 
ATOM   4271 O  O     . GLU   B 1 270 ? 29.148  6.923   58.384  1.00 71.96  ? 1180 GLU   B O     1 
ATOM   4272 C  CB    . GLU   B 1 270 ? 30.465  4.174   59.697  1.00 73.57  ? 1180 GLU   B CB    1 
ATOM   4273 C  CG    . GLU   B 1 270 ? 30.745  3.807   58.258  1.00 81.65  ? 1180 GLU   B CG    1 
ATOM   4274 C  CD    . GLU   B 1 270 ? 30.732  2.307   58.048  1.00 89.48  ? 1180 GLU   B CD    1 
ATOM   4275 O  OE1   . GLU   B 1 270 ? 29.661  1.689   58.277  1.00 88.15  ? 1180 GLU   B OE1   1 
ATOM   4276 O  OE2   . GLU   B 1 270 ? 31.795  1.753   57.675  1.00 86.86  ? 1180 GLU   B OE2   1 
ATOM   4277 N  N     . ALA   B 1 271 ? 28.051  6.136   60.183  1.00 67.34  ? 1181 ALA   B N     1 
ATOM   4278 C  CA    . ALA   B 1 271 ? 26.775  6.683   59.732  1.00 67.26  ? 1181 ALA   B CA    1 
ATOM   4279 C  C     . ALA   B 1 271 ? 26.845  8.199   59.596  1.00 70.63  ? 1181 ALA   B C     1 
ATOM   4280 O  O     . ALA   B 1 271 ? 26.411  8.763   58.584  1.00 74.34  ? 1181 ALA   B O     1 
ATOM   4281 C  CB    . ALA   B 1 271 ? 25.658  6.272   60.691  1.00 59.48  ? 1181 ALA   B CB    1 
ATOM   4282 N  N     . ILE   B 1 272 ? 27.410  8.876   60.598  1.00 70.58  ? 1182 ILE   B N     1 
ATOM   4283 C  CA    . ILE   B 1 272 ? 27.547  10.331  60.539  1.00 70.83  ? 1182 ILE   B CA    1 
ATOM   4284 C  C     . ILE   B 1 272 ? 28.431  10.745  59.366  1.00 73.38  ? 1182 ILE   B C     1 
ATOM   4285 O  O     . ILE   B 1 272 ? 28.062  11.612  58.566  1.00 72.07  ? 1182 ILE   B O     1 
ATOM   4286 C  CB    . ILE   B 1 272 ? 28.098  10.873  61.868  1.00 68.20  ? 1182 ILE   B CB    1 
ATOM   4287 C  CG1   . ILE   B 1 272 ? 27.066  10.684  62.980  1.00 61.70  ? 1182 ILE   B CG1   1 
ATOM   4288 C  CG2   . ILE   B 1 272 ? 28.516  12.334  61.708  1.00 68.17  ? 1182 ILE   B CG2   1 
ATOM   4289 C  CD1   . ILE   B 1 272 ? 27.448  11.337  64.287  1.00 62.76  ? 1182 ILE   B CD1   1 
ATOM   4290 N  N     . ALA   B 1 273 ? 29.619  10.139  59.252  1.00 74.54  ? 1183 ALA   B N     1 
ATOM   4291 C  CA    . ALA   B 1 273 ? 30.546  10.526  58.191  1.00 77.46  ? 1183 ALA   B CA    1 
ATOM   4292 C  C     . ALA   B 1 273 ? 29.975  10.232  56.809  1.00 77.77  ? 1183 ALA   B C     1 
ATOM   4293 O  O     . ALA   B 1 273 ? 30.269  10.955  55.850  1.00 83.11  ? 1183 ALA   B O     1 
ATOM   4294 C  CB    . ALA   B 1 273 ? 31.892  9.821   58.378  1.00 81.68  ? 1183 ALA   B CB    1 
ATOM   4295 N  N     . LEU   B 1 274 ? 29.162  9.184   56.684  1.00 75.89  ? 1184 LEU   B N     1 
ATOM   4296 C  CA    . LEU   B 1 274 ? 28.468  8.924   55.429  1.00 77.77  ? 1184 LEU   B CA    1 
ATOM   4297 C  C     . LEU   B 1 274 ? 27.299  9.876   55.203  1.00 80.19  ? 1184 LEU   B C     1 
ATOM   4298 O  O     . LEU   B 1 274 ? 26.882  10.061  54.055  1.00 84.52  ? 1184 LEU   B O     1 
ATOM   4299 C  CB    . LEU   B 1 274 ? 27.979  7.472   55.388  1.00 75.99  ? 1184 LEU   B CB    1 
ATOM   4300 C  CG    . LEU   B 1 274 ? 29.093  6.415   55.391  1.00 76.37  ? 1184 LEU   B CG    1 
ATOM   4301 C  CD1   . LEU   B 1 274 ? 28.533  4.998   55.388  1.00 73.49  ? 1184 LEU   B CD1   1 
ATOM   4302 C  CD2   . LEU   B 1 274 ? 30.056  6.628   54.230  1.00 79.90  ? 1184 LEU   B CD2   1 
ATOM   4303 N  N     . GLU   B 1 275 ? 26.770  10.487  56.266  1.00 75.08  ? 1185 GLU   B N     1 
ATOM   4304 C  CA    . GLU   B 1 275 ? 25.695  11.461  56.126  1.00 76.85  ? 1185 GLU   B CA    1 
ATOM   4305 C  C     . GLU   B 1 275 ? 26.199  12.841  55.709  1.00 84.56  ? 1185 GLU   B C     1 
ATOM   4306 O  O     . GLU   B 1 275 ? 25.424  13.634  55.161  1.00 84.34  ? 1185 GLU   B O     1 
ATOM   4307 C  CB    . GLU   B 1 275 ? 24.910  11.557  57.439  1.00 72.13  ? 1185 GLU   B CB    1 
ATOM   4308 C  CG    . GLU   B 1 275 ? 23.772  12.574  57.463  1.00 74.09  ? 1185 GLU   B CG    1 
ATOM   4309 C  CD    . GLU   B 1 275 ? 22.656  12.253  56.481  1.00 73.59  ? 1185 GLU   B CD    1 
ATOM   4310 O  OE1   . GLU   B 1 275 ? 22.905  12.275  55.254  1.00 71.57  ? 1185 GLU   B OE1   1 
ATOM   4311 O  OE2   . GLU   B 1 275 ? 21.526  11.975  56.945  1.00 67.14  ? 1185 GLU   B OE2   1 
ATOM   4312 N  N     . GLN   B 1 276 ? 27.479  13.138  55.929  1.00 84.40  ? 1186 GLN   B N     1 
ATOM   4313 C  CA    . GLN   B 1 276 ? 28.034  14.441  55.590  1.00 86.70  ? 1186 GLN   B CA    1 
ATOM   4314 C  C     . GLN   B 1 276 ? 28.369  14.579  54.106  1.00 94.58  ? 1186 GLN   B C     1 
ATOM   4315 O  O     . GLN   B 1 276 ? 28.973  15.584  53.718  1.00 93.27  ? 1186 GLN   B O     1 
ATOM   4316 C  CB    . GLN   B 1 276 ? 29.280  14.718  56.439  1.00 85.17  ? 1186 GLN   B CB    1 
ATOM   4317 C  CG    . GLN   B 1 276 ? 29.071  14.532  57.939  1.00 82.31  ? 1186 GLN   B CG    1 
ATOM   4318 C  CD    . GLN   B 1 276 ? 27.938  15.381  58.483  1.00 83.81  ? 1186 GLN   B CD    1 
ATOM   4319 O  OE1   . GLN   B 1 276 ? 27.798  16.548  58.119  1.00 82.25  ? 1186 GLN   B OE1   1 
ATOM   4320 N  NE2   . GLN   B 1 276 ? 27.113  14.794  59.352  1.00 80.85  ? 1186 GLN   B NE2   1 
ATOM   4321 N  N     . SER   B 1 277 ? 27.992  13.608  53.275  1.00 104.69 ? 1187 SER   B N     1 
ATOM   4322 C  CA    . SER   B 1 277 ? 28.225  13.694  51.833  1.00 108.46 ? 1187 SER   B CA    1 
ATOM   4323 C  C     . SER   B 1 277 ? 26.920  13.912  51.071  1.00 109.82 ? 1187 SER   B C     1 
ATOM   4324 O  O     . SER   B 1 277 ? 26.038  13.051  51.068  1.00 105.31 ? 1187 SER   B O     1 
ATOM   4325 C  CB    . SER   B 1 277 ? 28.913  12.431  51.320  1.00 109.22 ? 1187 SER   B CB    1 
ATOM   4326 O  OG    . SER   B 1 277 ? 28.012  11.339  51.311  1.00 109.14 ? 1187 SER   B OG    1 
HETATM 4327 ZN ZN    . ZN    C 2 .   ? 19.168  5.670   108.817 1.00 33.18  ? 1201 ZN    A ZN    1 
HETATM 4328 ZN ZN    . ZN    D 2 .   ? 18.945  1.834   108.706 1.00 31.75  ? 1202 ZN    A ZN    1 
HETATM 4329 ZN ZN    . ZN    E 2 .   ? 21.652  3.539   110.441 1.00 34.51  ? 1203 ZN    A ZN    1 
HETATM 4330 ZN ZN    . ZN    F 2 .   ? -13.865 4.213   130.677 1.00 65.73  ? 1204 ZN    A ZN    1 
HETATM 4331 N  N     . SFG   G 3 .   ? -17.063 2.806   117.566 1.00 38.92  ? 1205 SFG   A N     1 
HETATM 4332 C  CA    . SFG   G 3 .   ? -16.769 3.705   116.457 1.00 37.80  ? 1205 SFG   A CA    1 
HETATM 4333 C  C     . SFG   G 3 .   ? -17.609 3.307   115.281 1.00 35.02  ? 1205 SFG   A C     1 
HETATM 4334 O  O     . SFG   G 3 .   ? -18.427 2.384   115.458 1.00 31.61  ? 1205 SFG   A O     1 
HETATM 4335 O  OXT   . SFG   G 3 .   ? -17.461 3.911   114.193 1.00 35.54  ? 1205 SFG   A OXT   1 
HETATM 4336 C  CB    . SFG   G 3 .   ? -15.281 3.672   116.114 1.00 33.65  ? 1205 SFG   A CB    1 
HETATM 4337 C  CG    . SFG   G 3 .   ? -14.484 4.551   117.083 1.00 37.10  ? 1205 SFG   A CG    1 
HETATM 4338 C  CD    . SFG   G 3 .   ? -14.696 6.054   116.814 1.00 39.55  ? 1205 SFG   A CD    1 
HETATM 4339 N  NE    . SFG   G 3 .   ? -13.488 6.620   116.249 1.00 39.28  ? 1205 SFG   A NE    1 
HETATM 4340 C  "C5'" . SFG   G 3 .   ? -15.057 6.815   118.099 1.00 41.37  ? 1205 SFG   A "C5'" 1 
HETATM 4341 C  "C4'" . SFG   G 3 .   ? -16.554 6.686   118.441 1.00 40.92  ? 1205 SFG   A "C4'" 1 
HETATM 4342 O  "O4'" . SFG   G 3 .   ? -16.862 5.382   118.952 1.00 37.81  ? 1205 SFG   A "O4'" 1 
HETATM 4343 C  "C3'" . SFG   G 3 .   ? -17.055 7.650   119.507 1.00 41.47  ? 1205 SFG   A "C3'" 1 
HETATM 4344 O  "O3'" . SFG   G 3 .   ? -17.557 8.831   118.888 1.00 44.04  ? 1205 SFG   A "O3'" 1 
HETATM 4345 C  "C2'" . SFG   G 3 .   ? -18.164 6.866   120.186 1.00 45.12  ? 1205 SFG   A "C2'" 1 
HETATM 4346 O  "O2'" . SFG   G 3 .   ? -19.374 6.857   119.401 1.00 33.45  ? 1205 SFG   A "O2'" 1 
HETATM 4347 C  "C1'" . SFG   G 3 .   ? -17.616 5.454   120.167 1.00 42.38  ? 1205 SFG   A "C1'" 1 
HETATM 4348 N  N9    . SFG   G 3 .   ? -16.733 5.177   121.324 1.00 41.52  ? 1205 SFG   A N9    1 
HETATM 4349 C  C8    . SFG   G 3 .   ? -15.409 5.025   121.290 1.00 41.73  ? 1205 SFG   A C8    1 
HETATM 4350 N  N7    . SFG   G 3 .   ? -14.974 4.754   122.539 1.00 43.14  ? 1205 SFG   A N7    1 
HETATM 4351 C  C5    . SFG   G 3 .   ? -16.030 4.717   123.352 1.00 41.76  ? 1205 SFG   A C5    1 
HETATM 4352 C  C6    . SFG   G 3 .   ? -16.186 4.485   124.706 1.00 50.00  ? 1205 SFG   A C6    1 
HETATM 4353 N  N6    . SFG   G 3 .   ? -15.111 4.230   125.486 1.00 46.98  ? 1205 SFG   A N6    1 
HETATM 4354 N  N1    . SFG   G 3 .   ? -17.429 4.523   125.244 1.00 53.27  ? 1205 SFG   A N1    1 
HETATM 4355 C  C2    . SFG   G 3 .   ? -18.492 4.771   124.477 1.00 49.71  ? 1205 SFG   A C2    1 
HETATM 4356 N  N3    . SFG   G 3 .   ? -18.364 4.992   123.164 1.00 49.37  ? 1205 SFG   A N3    1 
HETATM 4357 C  C4    . SFG   G 3 .   ? -17.141 4.968   122.578 1.00 47.90  ? 1205 SFG   A C4    1 
HETATM 4358 C  C11   . A1L58 H 4 .   ? -8.078  12.188  120.563 1.00 46.57  ? 1206 A1L58 A C11   1 
HETATM 4359 C  C12   . A1L58 H 4 .   ? -8.341  10.833  119.774 1.00 43.13  ? 1206 A1L58 A C12   1 
HETATM 4360 C  C13   . A1L58 H 4 .   ? -9.785  10.683  119.239 1.00 47.51  ? 1206 A1L58 A C13   1 
HETATM 4361 C  C14   . A1L58 H 4 .   ? -10.042 9.376   118.437 1.00 46.13  ? 1206 A1L58 A C14   1 
HETATM 4362 C  C21   . A1L58 H 4 .   ? -2.494  11.059  123.455 1.00 48.53  ? 1206 A1L58 A C21   1 
HETATM 4363 C  C22   . A1L58 H 4 .   ? -1.567  11.507  122.517 1.00 47.97  ? 1206 A1L58 A C22   1 
HETATM 4364 C  C29   . A1L58 H 4 .   ? -0.850  14.306  124.573 1.00 59.45  ? 1206 A1L58 A C29   1 
HETATM 4365 C  C30   . A1L58 H 4 .   ? -0.385  13.881  123.156 1.00 57.41  ? 1206 A1L58 A C30   1 
HETATM 4366 C  C33   . A1L58 H 4 .   ? -11.453 15.564  119.748 1.00 57.52  ? 1206 A1L58 A C33   1 
HETATM 4367 C  C34   . A1L58 H 4 .   ? -12.137 16.553  119.052 1.00 60.77  ? 1206 A1L58 A C34   1 
HETATM 4368 C  C01   . A1L58 H 4 .   ? -11.288 21.898  117.557 1.00 58.07  ? 1206 A1L58 A C01   1 
HETATM 4369 C  C02   . A1L58 H 4 .   ? -10.985 20.589  117.922 1.00 60.35  ? 1206 A1L58 A C02   1 
HETATM 4370 C  C03   . A1L58 H 4 .   ? -9.827  19.962  117.410 1.00 59.80  ? 1206 A1L58 A C03   1 
HETATM 4371 C  C05   . A1L58 H 4 .   ? -10.068 17.594  118.397 1.00 56.16  ? 1206 A1L58 A C05   1 
HETATM 4372 C  C06   . A1L58 H 4 .   ? -9.391  16.584  119.106 1.00 53.60  ? 1206 A1L58 A C06   1 
HETATM 4373 C  C07   . A1L58 H 4 .   ? -10.061 15.560  119.802 1.00 54.76  ? 1206 A1L58 A C07   1 
HETATM 4374 C  C08   . A1L58 H 4 .   ? -9.321  14.469  120.546 1.00 52.71  ? 1206 A1L58 A C08   1 
HETATM 4375 C  C15   . A1L58 H 4 .   ? -11.453 9.294   117.853 1.00 47.62  ? 1206 A1L58 A C15   1 
HETATM 4376 C  C16   . A1L58 H 4 .   ? -6.481  12.370  120.648 1.00 45.00  ? 1206 A1L58 A C16   1 
HETATM 4377 C  C19   . A1L58 H 4 .   ? -4.334  11.640  121.947 1.00 44.04  ? 1206 A1L58 A C19   1 
HETATM 4378 C  C20   . A1L58 H 4 .   ? -3.857  11.128  123.161 1.00 46.90  ? 1206 A1L58 A C20   1 
HETATM 4379 C  C24   . A1L58 H 4 .   ? 0.548   12.652  123.000 1.00 56.26  ? 1206 A1L58 A C24   1 
HETATM 4380 C  C25   . A1L58 H 4 .   ? 1.426   12.549  124.233 1.00 61.04  ? 1206 A1L58 A C25   1 
HETATM 4381 C  C26   . A1L58 H 4 .   ? 0.650   12.530  125.531 1.00 64.14  ? 1206 A1L58 A C26   1 
HETATM 4382 C  C28   . A1L58 H 4 .   ? -1.099  13.522  126.909 1.00 57.45  ? 1206 A1L58 A C28   1 
HETATM 4383 C  C32   . A1L58 H 4 .   ? -3.297  12.058  121.052 1.00 45.29  ? 1206 A1L58 A C32   1 
HETATM 4384 C  C35   . A1L58 H 4 .   ? -11.469 17.555  118.381 1.00 57.18  ? 1206 A1L58 A C35   1 
HETATM 4385 C  C36   . A1L58 H 4 .   ? -9.032  20.735  116.549 1.00 58.77  ? 1206 A1L58 A C36   1 
HETATM 4386 C  C37   . A1L58 H 4 .   ? -9.415  22.041  116.242 1.00 56.49  ? 1206 A1L58 A C37   1 
HETATM 4387 N  N04   . A1L58 H 4 .   ? -9.398  18.634  117.702 1.00 56.28  ? 1206 A1L58 A N04   1 
HETATM 4388 N  N10   . A1L58 H 4 .   ? -8.797  13.312  119.909 1.00 49.46  ? 1206 A1L58 A N10   1 
HETATM 4389 N  N18   . A1L58 H 4 .   ? -5.726  11.696  121.645 1.00 41.89  ? 1206 A1L58 A N18   1 
HETATM 4390 N  N27   . A1L58 H 4 .   ? -0.159  13.749  125.782 1.00 61.83  ? 1206 A1L58 A N27   1 
HETATM 4391 N  N31   . A1L58 H 4 .   ? -1.984  11.998  121.299 1.00 43.08  ? 1206 A1L58 A N31   1 
HETATM 4392 N  N38   . A1L58 H 4 .   ? -10.531 22.632  116.734 1.00 59.13  ? 1206 A1L58 A N38   1 
HETATM 4393 O  O09   . A1L58 H 4 .   ? -9.162  14.579  121.763 1.00 55.25  ? 1206 A1L58 A O09   1 
HETATM 4394 O  O17   . A1L58 H 4 .   ? -5.933  13.072  119.813 1.00 47.44  ? 1206 A1L58 A O17   1 
HETATM 4395 O  O23   . A1L58 H 4 .   ? -0.196  11.431  122.797 1.00 52.84  ? 1206 A1L58 A O23   1 
HETATM 4396 ZN ZN    . ZN    I 2 .   ? -9.750  2.700   88.690  1.00 23.80  ? 1201 ZN    B ZN    1 
HETATM 4397 ZN ZN    . ZN    J 2 .   ? -9.123  -0.990  89.211  1.00 23.11  ? 1202 ZN    B ZN    1 
HETATM 4398 ZN ZN    . ZN    K 2 .   ? -12.019 0.108   87.311  1.00 25.86  ? 1203 ZN    B ZN    1 
HETATM 4399 ZN ZN    . ZN    L 2 .   ? 23.590  2.481   67.156  1.00 55.06  ? 1204 ZN    B ZN    1 
HETATM 4400 N  N     . SFG   M 3 .   ? 26.633  3.802   80.336  1.00 32.33  ? 1205 SFG   B N     1 
HETATM 4401 C  CA    . SFG   M 3 .   ? 26.236  4.469   81.554  1.00 32.84  ? 1205 SFG   B CA    1 
HETATM 4402 C  C     . SFG   M 3 .   ? 27.027  3.981   82.737  1.00 32.43  ? 1205 SFG   B C     1 
HETATM 4403 O  O     . SFG   M 3 .   ? 27.790  2.996   82.625  1.00 30.42  ? 1205 SFG   B O     1 
HETATM 4404 O  OXT   . SFG   M 3 .   ? 26.885  4.590   83.816  1.00 30.50  ? 1205 SFG   B OXT   1 
HETATM 4405 C  CB    . SFG   M 3 .   ? 24.734  4.253   81.782  1.00 34.86  ? 1205 SFG   B CB    1 
HETATM 4406 C  CG    . SFG   M 3 .   ? 23.919  4.720   80.571  1.00 34.21  ? 1205 SFG   B CG    1 
HETATM 4407 C  CD    . SFG   M 3 .   ? 23.819  6.244   80.488  1.00 33.45  ? 1205 SFG   B CD    1 
HETATM 4408 N  NE    . SFG   M 3 .   ? 22.451  6.636   80.750  1.00 31.68  ? 1205 SFG   B NE    1 
HETATM 4409 C  "C5'" . SFG   M 3 .   ? 24.174  6.727   79.086  1.00 36.03  ? 1205 SFG   B "C5'" 1 
HETATM 4410 C  "C4'" . SFG   M 3 .   ? 25.679  6.756   78.848  1.00 40.02  ? 1205 SFG   B "C4'" 1 
HETATM 4411 O  "O4'" . SFG   M 3 .   ? 26.189  5.432   78.591  1.00 37.94  ? 1205 SFG   B "O4'" 1 
HETATM 4412 C  "C3'" . SFG   M 3 .   ? 26.015  7.606   77.633  1.00 41.76  ? 1205 SFG   B "C3'" 1 
HETATM 4413 O  "O3'" . SFG   M 3 .   ? 26.379  8.931   78.014  1.00 43.47  ? 1205 SFG   B "O3'" 1 
HETATM 4414 C  "C2'" . SFG   M 3 .   ? 27.193  6.884   77.029  1.00 43.64  ? 1205 SFG   B "C2'" 1 
HETATM 4415 O  "O2'" . SFG   M 3 .   ? 28.377  7.320   77.695  1.00 39.44  ? 1205 SFG   B "O2'" 1 
HETATM 4416 C  "C1'" . SFG   M 3 .   ? 26.913  5.427   77.359  1.00 43.46  ? 1205 SFG   B "C1'" 1 
HETATM 4417 N  N9    . SFG   M 3 .   ? 26.067  4.847   76.293  1.00 40.07  ? 1205 SFG   B N9    1 
HETATM 4418 C  C8    . SFG   M 3 .   ? 24.766  4.548   76.366  1.00 40.58  ? 1205 SFG   B C8    1 
HETATM 4419 N  N7    . SFG   M 3 .   ? 24.372  4.023   75.183  1.00 39.53  ? 1205 SFG   B N7    1 
HETATM 4420 C  C5    . SFG   M 3 .   ? 25.442  3.983   74.370  1.00 40.56  ? 1205 SFG   B C5    1 
HETATM 4421 C  C6    . SFG   M 3 .   ? 25.659  3.559   73.062  1.00 45.19  ? 1205 SFG   B C6    1 
HETATM 4422 N  N6    . SFG   M 3 .   ? 24.660  3.048   72.307  1.00 39.49  ? 1205 SFG   B N6    1 
HETATM 4423 N  N1    . SFG   M 3 .   ? 26.905  3.668   72.534  1.00 47.22  ? 1205 SFG   B N1    1 
HETATM 4424 C  C2    . SFG   M 3 .   ? 27.913  4.176   73.251  1.00 44.93  ? 1205 SFG   B C2    1 
HETATM 4425 N  N3    . SFG   M 3 .   ? 27.730  4.588   74.508  1.00 43.29  ? 1205 SFG   B N3    1 
HETATM 4426 C  C4    . SFG   M 3 .   ? 26.509  4.500   75.085  1.00 43.00  ? 1205 SFG   B C4    1 
HETATM 4427 C  C11   . A1L58 N 4 .   ? 16.792  10.896  76.108  1.00 45.23  ? 1206 A1L58 B C11   1 
HETATM 4428 C  C12   . A1L58 N 4 .   ? 17.297  9.569   76.811  1.00 43.27  ? 1206 A1L58 B C12   1 
HETATM 4429 C  C13   . A1L58 N 4 .   ? 18.038  9.811   78.159  1.00 41.33  ? 1206 A1L58 B C13   1 
HETATM 4430 C  C14   . A1L58 N 4 .   ? 19.291  8.916   78.411  1.00 41.51  ? 1206 A1L58 B C14   1 
HETATM 4431 C  C21   . A1L58 N 4 .   ? 11.480  8.231   73.686  1.00 48.17  ? 1206 A1L58 B C21   1 
HETATM 4432 C  C22   . A1L58 N 4 .   ? 10.442  8.798   74.420  1.00 50.53  ? 1206 A1L58 B C22   1 
HETATM 4433 C  C29   . A1L58 N 4 .   ? 8.825   10.092  71.318  1.00 65.79  ? 1206 A1L58 B C29   1 
HETATM 4434 C  C30   . A1L58 N 4 .   ? 8.782   10.422  72.819  1.00 59.58  ? 1206 A1L58 B C30   1 
HETATM 4435 C  C33   . A1L58 N 4 .   ? 19.121  14.800  77.306  1.00 52.08  ? 1206 A1L58 B C33   1 
HETATM 4436 C  C34   . A1L58 N 4 .   ? 19.599  15.948  77.935  1.00 56.47  ? 1206 A1L58 B C34   1 
HETATM 4437 C  C01   . A1L58 N 4 .   ? 18.049  21.455  77.636  1.00 67.34  ? 1206 A1L58 B C01   1 
HETATM 4438 C  C02   . A1L58 N 4 .   ? 17.977  20.064  77.712  1.00 62.23  ? 1206 A1L58 B C02   1 
HETATM 4439 C  C03   . A1L58 N 4 .   ? 16.773  19.456  78.112  1.00 62.38  ? 1206 A1L58 B C03   1 
HETATM 4440 C  C05   . A1L58 N 4 .   ? 17.403  16.947  77.904  1.00 58.69  ? 1206 A1L58 B C05   1 
HETATM 4441 C  C06   . A1L58 N 4 .   ? 16.931  15.773  77.260  1.00 54.13  ? 1206 A1L58 B C06   1 
HETATM 4442 C  C07   . A1L58 N 4 .   ? 17.774  14.679  76.945  1.00 53.14  ? 1206 A1L58 B C07   1 
HETATM 4443 C  C08   . A1L58 N 4 .   ? 17.247  13.398  76.255  1.00 49.69  ? 1206 A1L58 B C08   1 
HETATM 4444 C  C15   . A1L58 N 4 .   ? 19.515  8.570   79.891  1.00 39.25  ? 1206 A1L58 B C15   1 
HETATM 4445 C  C16   . A1L58 N 4 .   ? 15.166  10.847  76.032  1.00 44.35  ? 1206 A1L58 B C16   1 
HETATM 4446 C  C19   . A1L58 N 4 .   ? 13.142  9.543   74.926  1.00 44.28  ? 1206 A1L58 B C19   1 
HETATM 4447 C  C20   . A1L58 N 4 .   ? 12.797  8.602   73.946  1.00 45.82  ? 1206 A1L58 B C20   1 
HETATM 4448 C  C24   . A1L58 N 4 .   ? 8.146   9.370   73.757  1.00 61.32  ? 1206 A1L58 B C24   1 
HETATM 4449 C  C25   . A1L58 N 4 .   ? 6.944   8.690   73.052  1.00 65.00  ? 1206 A1L58 B C25   1 
HETATM 4450 C  C26   . A1L58 N 4 .   ? 6.541   9.303   71.725  1.00 72.13  ? 1206 A1L58 B C26   1 
HETATM 4451 C  C28   . A1L58 N 4 .   ? 8.079   7.955   70.361  1.00 74.06  ? 1206 A1L58 B C28   1 
HETATM 4452 C  C32   . A1L58 N 4 .   ? 12.014  10.063  75.640  1.00 46.21  ? 1206 A1L58 B C32   1 
HETATM 4453 C  C35   . A1L58 N 4 .   ? 18.768  17.010  78.235  1.00 57.95  ? 1206 A1L58 B C35   1 
HETATM 4454 C  C36   . A1L58 N 4 .   ? 15.701  20.313  78.408  1.00 62.94  ? 1206 A1L58 B C36   1 
HETATM 4455 C  C37   . A1L58 N 4 .   ? 15.867  21.690  78.302  1.00 66.81  ? 1206 A1L58 B C37   1 
HETATM 4456 N  N04   . A1L58 N 4 .   ? 16.554  18.058  78.234  1.00 60.22  ? 1206 A1L58 B N04   1 
HETATM 4457 N  N10   . A1L58 N 4 .   ? 17.308  12.088  76.806  1.00 46.07  ? 1206 A1L58 B N10   1 
HETATM 4458 N  N18   . A1L58 N 4 .   ? 14.519  9.882   75.195  1.00 43.48  ? 1206 A1L58 B N18   1 
HETATM 4459 N  N27   . A1L58 N 4 .   ? 7.673   9.337   70.760  1.00 73.52  ? 1206 A1L58 B N27   1 
HETATM 4460 N  N31   . A1L58 N 4 .   ? 10.717  9.719   75.418  1.00 47.59  ? 1206 A1L58 B N31   1 
HETATM 4461 N  N38   . A1L58 N 4 .   ? 17.020  22.277  77.917  1.00 68.89  ? 1206 A1L58 B N38   1 
HETATM 4462 O  O09   . A1L58 N 4 .   ? 16.722  13.495  75.148  1.00 53.21  ? 1206 A1L58 B O09   1 
HETATM 4463 O  O17   . A1L58 N 4 .   ? 14.527  11.652  76.702  1.00 42.07  ? 1206 A1L58 B O17   1 
HETATM 4464 O  O23   . A1L58 N 4 .   ? 9.118   8.400   74.166  1.00 53.83  ? 1206 A1L58 B O23   1 
HETATM 4465 O  O     . HOH   O 5 .   ? 15.335  -6.644  108.843 1.00 35.60  ? 1301 HOH   A O     1 
HETATM 4466 O  O     . HOH   O 5 .   ? -7.763  14.296  123.526 1.00 51.58  ? 1302 HOH   A O     1 
HETATM 4467 O  O     . HOH   O 5 .   ? 0.701   15.605  120.954 1.00 51.87  ? 1303 HOH   A O     1 
HETATM 4468 O  O     . HOH   O 5 .   ? -12.959 10.597  136.458 1.00 68.12  ? 1304 HOH   A O     1 
HETATM 4469 O  O     . HOH   O 5 .   ? 0.169   7.422   106.641 1.00 33.18  ? 1305 HOH   A O     1 
HETATM 4470 O  O     . HOH   O 5 .   ? 5.598   11.113  102.367 1.00 40.95  ? 1306 HOH   A O     1 
HETATM 4471 O  O     . HOH   O 5 .   ? -21.395 -7.971  103.473 1.00 40.29  ? 1307 HOH   A O     1 
HETATM 4472 O  O     . HOH   O 5 .   ? -19.407 6.688   116.989 1.00 36.57  ? 1308 HOH   A O     1 
HETATM 4473 O  O     . HOH   O 5 .   ? 13.198  -2.612  110.983 1.00 37.54  ? 1309 HOH   A O     1 
HETATM 4474 O  O     . HOH   O 5 .   ? -17.627 -16.258 112.080 1.00 34.64  ? 1310 HOH   A O     1 
HETATM 4475 O  O     . HOH   O 5 .   ? -1.438  1.209   109.556 1.00 29.69  ? 1311 HOH   A O     1 
HETATM 4476 O  O     . HOH   O 5 .   ? -7.928  6.138   110.849 1.00 33.16  ? 1312 HOH   A O     1 
HETATM 4477 O  O     . HOH   O 5 .   ? -4.946  4.320   141.648 1.00 66.78  ? 1313 HOH   A O     1 
HETATM 4478 O  O     . HOH   O 5 .   ? -1.234  -4.831  99.253  1.00 36.87  ? 1314 HOH   A O     1 
HETATM 4479 O  O     . HOH   O 5 .   ? 1.187   12.693  109.298 1.00 37.47  ? 1315 HOH   A O     1 
HETATM 4480 O  O     . HOH   O 5 .   ? 11.189  3.229   103.261 1.00 31.54  ? 1316 HOH   A O     1 
HETATM 4481 O  O     . HOH   O 5 .   ? 11.393  21.116  106.573 1.00 39.87  ? 1317 HOH   A O     1 
HETATM 4482 O  O     . HOH   O 5 .   ? -2.805  1.890   106.947 1.00 26.98  ? 1318 HOH   A O     1 
HETATM 4483 O  O     . HOH   O 5 .   ? -5.425  -5.902  102.858 1.00 30.39  ? 1319 HOH   A O     1 
HETATM 4484 O  O     . HOH   O 5 .   ? 24.856  1.687   100.889 1.00 39.31  ? 1320 HOH   A O     1 
HETATM 4485 O  O     . HOH   O 5 .   ? 7.749   -3.515  125.280 1.00 51.45  ? 1321 HOH   A O     1 
HETATM 4486 O  O     . HOH   O 5 .   ? 17.963  -1.588  127.232 1.00 57.28  ? 1322 HOH   A O     1 
HETATM 4487 O  O     . HOH   O 5 .   ? -7.245  -8.818  100.767 1.00 33.88  ? 1323 HOH   A O     1 
HETATM 4488 O  O     . HOH   O 5 .   ? -22.064 2.451   106.206 1.00 34.25  ? 1324 HOH   A O     1 
HETATM 4489 O  O     . HOH   O 5 .   ? -19.625 7.049   141.907 1.00 88.24  ? 1325 HOH   A O     1 
HETATM 4490 O  O     . HOH   O 5 .   ? -9.039  -4.482  125.652 1.00 41.87  ? 1326 HOH   A O     1 
HETATM 4491 O  O     . HOH   O 5 .   ? 13.047  9.372   108.652 1.00 28.58  ? 1327 HOH   A O     1 
HETATM 4492 O  O     . HOH   O 5 .   ? 11.480  6.090   125.744 1.00 46.68  ? 1328 HOH   A O     1 
HETATM 4493 O  O     . HOH   O 5 .   ? -6.249  -9.564  110.113 1.00 32.33  ? 1329 HOH   A O     1 
HETATM 4494 O  O     . HOH   O 5 .   ? -18.248 18.949  109.074 1.00 45.14  ? 1330 HOH   A O     1 
HETATM 4495 O  O     . HOH   O 5 .   ? 11.115  16.395  105.243 1.00 34.22  ? 1331 HOH   A O     1 
HETATM 4496 O  O     . HOH   O 5 .   ? 20.723  16.141  105.326 1.00 42.41  ? 1332 HOH   A O     1 
HETATM 4497 O  O     . HOH   O 5 .   ? -20.925 14.941  106.490 1.00 36.61  ? 1333 HOH   A O     1 
HETATM 4498 O  O     . HOH   O 5 .   ? 0.797   -4.991  112.844 1.00 27.33  ? 1334 HOH   A O     1 
HETATM 4499 O  O     . HOH   O 5 .   ? -11.754 12.537  106.526 1.00 33.06  ? 1335 HOH   A O     1 
HETATM 4500 O  O     . HOH   O 5 .   ? 5.937   -9.759  126.019 1.00 42.64  ? 1336 HOH   A O     1 
HETATM 4501 O  O     . HOH   O 5 .   ? -11.623 -0.940  119.517 1.00 32.40  ? 1337 HOH   A O     1 
HETATM 4502 O  O     . HOH   O 5 .   ? -14.313 1.922   98.361  1.00 32.50  ? 1338 HOH   A O     1 
HETATM 4503 O  O     . HOH   O 5 .   ? -22.990 16.460  114.714 1.00 54.64  ? 1339 HOH   A O     1 
HETATM 4504 O  O     . HOH   O 5 .   ? -7.763  16.925  145.695 1.00 68.43  ? 1340 HOH   A O     1 
HETATM 4505 O  O     . HOH   O 5 .   ? 6.102   -3.615  110.810 1.00 26.24  ? 1341 HOH   A O     1 
HETATM 4506 O  O     . HOH   O 5 .   ? 21.298  -2.435  106.397 1.00 36.22  ? 1342 HOH   A O     1 
HETATM 4507 O  O     . HOH   O 5 .   ? -18.214 18.077  136.878 1.00 75.84  ? 1343 HOH   A O     1 
HETATM 4508 O  O     . HOH   O 5 .   ? -2.831  25.063  111.097 1.00 41.42  ? 1344 HOH   A O     1 
HETATM 4509 O  O     . HOH   O 5 .   ? -3.149  8.032   124.337 1.00 33.42  ? 1345 HOH   A O     1 
HETATM 4510 O  O     . HOH   O 5 .   ? -5.584  3.120   100.142 1.00 29.49  ? 1346 HOH   A O     1 
HETATM 4511 O  O     . HOH   O 5 .   ? -25.932 18.784  111.021 1.00 40.38  ? 1347 HOH   A O     1 
HETATM 4512 O  O     . HOH   O 5 .   ? 1.135   -11.610 113.101 1.00 41.93  ? 1348 HOH   A O     1 
HETATM 4513 O  O     . HOH   O 5 .   ? -16.054 1.085   125.865 1.00 52.93  ? 1349 HOH   A O     1 
HETATM 4514 O  O     . HOH   O 5 .   ? -15.384 15.391  110.341 1.00 41.49  ? 1350 HOH   A O     1 
HETATM 4515 O  O     . HOH   O 5 .   ? -20.716 -0.214  139.578 1.00 58.22  ? 1351 HOH   A O     1 
HETATM 4516 O  O     . HOH   O 5 .   ? 6.023   11.572  109.581 1.00 30.76  ? 1352 HOH   A O     1 
HETATM 4517 O  O     . HOH   O 5 .   ? 0.101   -2.886  106.033 1.00 27.26  ? 1353 HOH   A O     1 
HETATM 4518 O  O     . HOH   O 5 .   ? -10.607 0.261   129.948 1.00 50.63  ? 1354 HOH   A O     1 
HETATM 4519 O  O     . HOH   O 5 .   ? -12.993 -13.431 110.479 1.00 31.96  ? 1355 HOH   A O     1 
HETATM 4520 O  O     . HOH   O 5 .   ? -6.523  16.573  126.195 1.00 57.61  ? 1356 HOH   A O     1 
HETATM 4521 O  O     . HOH   O 5 .   ? 25.005  0.931   113.004 1.00 44.94  ? 1357 HOH   A O     1 
HETATM 4522 O  O     . HOH   O 5 .   ? -2.916  19.396  116.745 1.00 40.92  ? 1358 HOH   A O     1 
HETATM 4523 O  O     . HOH   O 5 .   ? -3.215  5.491   124.573 1.00 37.93  ? 1359 HOH   A O     1 
HETATM 4524 O  O     . HOH   O 5 .   ? -17.605 16.680  109.851 1.00 48.29  ? 1360 HOH   A O     1 
HETATM 4525 O  O     . HOH   O 5 .   ? -4.396  -18.057 121.399 1.00 34.26  ? 1361 HOH   A O     1 
HETATM 4526 O  O     . HOH   O 5 .   ? 0.731   9.627   102.249 1.00 35.88  ? 1362 HOH   A O     1 
HETATM 4527 O  O     . HOH   O 5 .   ? 23.403  7.201   101.567 1.00 34.69  ? 1363 HOH   A O     1 
HETATM 4528 O  O     . HOH   O 5 .   ? -14.436 14.629  130.483 1.00 73.29  ? 1364 HOH   A O     1 
HETATM 4529 O  O     . HOH   O 5 .   ? 0.182   0.304   105.112 1.00 33.67  ? 1365 HOH   A O     1 
HETATM 4530 O  O     . HOH   O 5 .   ? 1.963   18.331  100.611 1.00 29.02  ? 1366 HOH   A O     1 
HETATM 4531 O  O     . HOH   O 5 .   ? 6.655   16.586  115.531 1.00 42.55  ? 1367 HOH   A O     1 
HETATM 4532 O  O     . HOH   O 5 .   ? 15.908  9.308   109.756 1.00 32.02  ? 1368 HOH   A O     1 
HETATM 4533 O  O     . HOH   O 5 .   ? 6.626   -4.750  115.819 1.00 29.88  ? 1369 HOH   A O     1 
HETATM 4534 O  O     . HOH   O 5 .   ? 2.274   1.949   108.730 1.00 31.89  ? 1370 HOH   A O     1 
HETATM 4535 O  O     . HOH   O 5 .   ? 10.524  10.938  125.676 1.00 52.41  ? 1371 HOH   A O     1 
HETATM 4536 O  O     . HOH   O 5 .   ? -0.125  1.284   101.846 1.00 38.15  ? 1372 HOH   A O     1 
HETATM 4537 O  O     . HOH   O 5 .   ? -22.054 6.217   120.599 1.00 46.21  ? 1373 HOH   A O     1 
HETATM 4538 O  O     . HOH   O 5 .   ? 5.964   4.765   104.132 1.00 30.21  ? 1374 HOH   A O     1 
HETATM 4539 O  O     . HOH   O 5 .   ? -19.535 -9.284  116.673 1.00 38.39  ? 1375 HOH   A O     1 
HETATM 4540 O  O     . HOH   O 5 .   ? 7.826   22.892  102.620 1.00 36.96  ? 1376 HOH   A O     1 
HETATM 4541 O  O     . HOH   O 5 .   ? 25.421  7.928   110.916 1.00 37.59  ? 1377 HOH   A O     1 
HETATM 4542 O  O     . HOH   O 5 .   ? 5.355   0.676   131.570 1.00 54.74  ? 1378 HOH   A O     1 
HETATM 4543 O  O     . HOH   O 5 .   ? 4.183   25.685  104.105 1.00 30.40  ? 1379 HOH   A O     1 
HETATM 4544 O  O     . HOH   O 5 .   ? -23.682 0.388   119.200 1.00 43.32  ? 1380 HOH   A O     1 
HETATM 4545 O  O     . HOH   O 5 .   ? -20.659 -15.545 107.009 1.00 38.29  ? 1381 HOH   A O     1 
HETATM 4546 O  O     . HOH   O 5 .   ? 20.250  -10.226 123.368 1.00 47.26  ? 1382 HOH   A O     1 
HETATM 4547 O  O     . HOH   O 5 .   ? -27.218 -11.128 107.049 1.00 49.75  ? 1383 HOH   A O     1 
HETATM 4548 O  O     . HOH   O 5 .   ? 4.134   -6.200  113.987 1.00 31.91  ? 1384 HOH   A O     1 
HETATM 4549 O  O     . HOH   O 5 .   ? -7.125  21.507  105.489 1.00 39.27  ? 1385 HOH   A O     1 
HETATM 4550 O  O     . HOH   O 5 .   ? 0.236   -1.666  130.312 1.00 49.86  ? 1386 HOH   A O     1 
HETATM 4551 O  O     . HOH   O 5 .   ? -4.173  -8.169  101.582 1.00 34.72  ? 1387 HOH   A O     1 
HETATM 4552 O  O     . HOH   O 5 .   ? -22.875 -6.322  105.034 1.00 36.89  ? 1388 HOH   A O     1 
HETATM 4553 O  O     . HOH   O 5 .   ? -13.946 1.962   101.052 1.00 32.00  ? 1389 HOH   A O     1 
HETATM 4554 O  O     . HOH   O 5 .   ? -21.475 5.744   123.369 1.00 52.01  ? 1390 HOH   A O     1 
HETATM 4555 O  O     . HOH   O 5 .   ? 11.478  -4.884  107.601 1.00 38.74  ? 1391 HOH   A O     1 
HETATM 4556 O  O     . HOH   O 5 .   ? -15.960 21.786  128.463 1.00 50.06  ? 1392 HOH   A O     1 
HETATM 4557 O  O     . HOH   O 5 .   ? 21.837  15.908  102.190 1.00 42.42  ? 1393 HOH   A O     1 
HETATM 4558 O  O     . HOH   O 5 .   ? -0.557  12.405  100.288 1.00 32.02  ? 1394 HOH   A O     1 
HETATM 4559 O  O     . HOH   O 5 .   ? 7.648   25.112  103.606 1.00 36.82  ? 1395 HOH   A O     1 
HETATM 4560 O  O     . HOH   O 5 .   ? -18.782 -11.628 117.969 1.00 42.70  ? 1396 HOH   A O     1 
HETATM 4561 O  O     . HOH   O 5 .   ? 2.399   12.422  106.644 1.00 35.12  ? 1397 HOH   A O     1 
HETATM 4562 O  O     . HOH   O 5 .   ? -22.228 3.622   120.398 1.00 49.29  ? 1398 HOH   A O     1 
HETATM 4563 O  O     . HOH   O 5 .   ? -8.432  -10.238 97.354  1.00 53.36  ? 1399 HOH   A O     1 
HETATM 4564 O  O     . HOH   O 5 .   ? 1.789   19.996  98.356  1.00 40.01  ? 1400 HOH   A O     1 
HETATM 4565 O  O     . HOH   O 5 .   ? -3.914  5.337   100.215 1.00 24.59  ? 1401 HOH   A O     1 
HETATM 4566 O  O     . HOH   O 5 .   ? -19.119 4.066   108.416 1.00 36.92  ? 1402 HOH   A O     1 
HETATM 4567 O  O     . HOH   O 5 .   ? 2.952   1.377   105.418 1.00 34.69  ? 1403 HOH   A O     1 
HETATM 4568 O  O     . HOH   O 5 .   ? 24.050  14.705  102.360 1.00 47.18  ? 1404 HOH   A O     1 
HETATM 4569 O  O     . HOH   O 5 .   ? -4.483  13.687  125.215 1.00 47.38  ? 1405 HOH   A O     1 
HETATM 4570 O  O     . HOH   O 5 .   ? -4.251  15.155  123.106 1.00 44.14  ? 1406 HOH   A O     1 
HETATM 4571 O  O     . HOH   O 5 .   ? -22.249 3.404   108.330 1.00 43.99  ? 1407 HOH   A O     1 
HETATM 4572 O  O     . HOH   O 5 .   ? -15.971 10.175  100.497 1.00 41.51  ? 1408 HOH   A O     1 
HETATM 4573 O  O     . HOH   O 5 .   ? -3.630  11.479  126.885 1.00 46.29  ? 1409 HOH   A O     1 
HETATM 4574 O  O     . HOH   O 5 .   ? 6.565   -4.960  113.332 1.00 31.48  ? 1410 HOH   A O     1 
HETATM 4575 O  O     . HOH   O 5 .   ? -16.527 11.178  98.224  1.00 35.83  ? 1411 HOH   A O     1 
HETATM 4576 O  O     . HOH   O 5 .   ? 23.053  17.425  100.113 1.00 42.12  ? 1412 HOH   A O     1 
HETATM 4577 O  O     . HOH   O 5 .   ? -28.692 17.997  111.642 1.00 44.93  ? 1413 HOH   A O     1 
HETATM 4578 O  O     . HOH   O 5 .   ? -28.980 18.232  113.870 1.00 44.74  ? 1414 HOH   A O     1 
HETATM 4579 O  O     . HOH   O 5 .   ? -29.350 -6.522  122.529 1.00 48.57  ? 1415 HOH   A O     1 
HETATM 4580 O  O     . HOH   P 5 .   ? 28.482  4.176   85.257  1.00 33.18  ? 1301 HOH   B O     1 
HETATM 4581 O  O     . HOH   P 5 .   ? -14.652 -3.358  85.469  1.00 31.04  ? 1302 HOH   B O     1 
HETATM 4582 O  O     . HOH   P 5 .   ? -3.608  -9.165  66.073  1.00 56.12  ? 1303 HOH   B O     1 
HETATM 4583 O  O     . HOH   P 5 .   ? -6.505  -8.303  97.596  1.00 41.13  ? 1304 HOH   B O     1 
HETATM 4584 O  O     . HOH   P 5 .   ? 29.161  -11.064 80.440  1.00 50.07  ? 1305 HOH   B O     1 
HETATM 4585 O  O     . HOH   P 5 .   ? 13.094  8.803   96.045  1.00 28.39  ? 1306 HOH   B O     1 
HETATM 4586 O  O     . HOH   P 5 .   ? 35.731  4.270   88.763  1.00 32.81  ? 1307 HOH   B O     1 
HETATM 4587 O  O     . HOH   P 5 .   ? 16.088  7.933   61.948  1.00 55.28  ? 1308 HOH   B O     1 
HETATM 4588 O  O     . HOH   P 5 .   ? 3.382   15.525  77.086  1.00 80.63  ? 1309 HOH   B O     1 
HETATM 4589 O  O     . HOH   P 5 .   ? 7.049   11.890  87.183  1.00 28.93  ? 1310 HOH   B O     1 
HETATM 4590 O  O     . HOH   P 5 .   ? 6.044   20.770  75.879  1.00 96.55  ? 1311 HOH   B O     1 
HETATM 4591 O  O     . HOH   P 5 .   ? -18.268 0.960   93.262  1.00 26.00  ? 1312 HOH   B O     1 
HETATM 4592 O  O     . HOH   P 5 .   ? -6.970  13.835  86.595  1.00 35.31  ? 1313 HOH   B O     1 
HETATM 4593 O  O     . HOH   P 5 .   ? 6.580   22.057  77.754  1.00 95.58  ? 1314 HOH   B O     1 
HETATM 4594 O  O     . HOH   P 5 .   ? -3.480  12.622  98.960  1.00 30.08  ? 1315 HOH   B O     1 
HETATM 4595 O  O     . HOH   P 5 .   ? 15.362  -5.312  68.638  1.00 45.20  ? 1316 HOH   B O     1 
HETATM 4596 O  O     . HOH   P 5 .   ? 4.295   -4.899  87.888  1.00 26.00  ? 1317 HOH   B O     1 
HETATM 4597 O  O     . HOH   P 5 .   ? 11.260  0.434   88.416  1.00 21.32  ? 1318 HOH   B O     1 
HETATM 4598 O  O     . HOH   P 5 .   ? 10.149  0.024   92.069  1.00 31.68  ? 1319 HOH   B O     1 
HETATM 4599 O  O     . HOH   P 5 .   ? 7.405   1.673   88.978  1.00 27.46  ? 1320 HOH   B O     1 
HETATM 4600 O  O     . HOH   P 5 .   ? -4.151  7.182   88.471  1.00 23.56  ? 1321 HOH   B O     1 
HETATM 4601 O  O     . HOH   P 5 .   ? 12.572  1.450   90.598  1.00 27.83  ? 1322 HOH   B O     1 
HETATM 4602 O  O     . HOH   P 5 .   ? 22.052  13.784  83.526  1.00 41.58  ? 1323 HOH   B O     1 
HETATM 4603 O  O     . HOH   P 5 .   ? 9.253   3.546   91.643  1.00 34.03  ? 1324 HOH   B O     1 
HETATM 4604 O  O     . HOH   P 5 .   ? 2.692   9.926   86.840  1.00 26.80  ? 1325 HOH   B O     1 
HETATM 4605 O  O     . HOH   P 5 .   ? -7.057  6.145   86.952  1.00 26.76  ? 1326 HOH   B O     1 
HETATM 4606 O  O     . HOH   P 5 .   ? -9.209  -1.335  83.437  1.00 31.00  ? 1327 HOH   B O     1 
HETATM 4607 O  O     . HOH   P 5 .   ? 11.508  -14.087 91.384  1.00 41.57  ? 1328 HOH   B O     1 
HETATM 4608 O  O     . HOH   P 5 .   ? 9.156   7.959   86.580  1.00 25.98  ? 1329 HOH   B O     1 
HETATM 4609 O  O     . HOH   P 5 .   ? -8.820  1.281   94.921  1.00 30.83  ? 1330 HOH   B O     1 
HETATM 4610 O  O     . HOH   P 5 .   ? 7.184   20.297  96.410  1.00 41.96  ? 1331 HOH   B O     1 
HETATM 4611 O  O     . HOH   P 5 .   ? 14.230  21.730  88.995  1.00 40.73  ? 1332 HOH   B O     1 
HETATM 4612 O  O     . HOH   P 5 .   ? -5.153  1.531   82.090  1.00 31.66  ? 1333 HOH   B O     1 
HETATM 4613 O  O     . HOH   P 5 .   ? -3.298  -6.925  83.791  1.00 30.18  ? 1334 HOH   B O     1 
HETATM 4614 O  O     . HOH   P 5 .   ? 15.717  -5.002  95.483  1.00 25.14  ? 1335 HOH   B O     1 
HETATM 4615 O  O     . HOH   P 5 .   ? 8.717   -12.531 85.263  1.00 37.74  ? 1336 HOH   B O     1 
HETATM 4616 O  O     . HOH   P 5 .   ? 9.862   -6.305  85.969  1.00 23.95  ? 1337 HOH   B O     1 
HETATM 4617 O  O     . HOH   P 5 .   ? -16.106 7.747   89.060  1.00 31.04  ? 1338 HOH   B O     1 
HETATM 4618 O  O     . HOH   P 5 .   ? 23.385  3.812   95.757  1.00 31.98  ? 1339 HOH   B O     1 
HETATM 4619 O  O     . HOH   P 5 .   ? 10.141  -3.097  92.423  1.00 25.32  ? 1340 HOH   B O     1 
HETATM 4620 O  O     . HOH   P 5 .   ? -4.806  8.471   77.404  1.00 40.23  ? 1341 HOH   B O     1 
HETATM 4621 O  O     . HOH   P 5 .   ? 21.808  -1.654  78.956  1.00 36.16  ? 1342 HOH   B O     1 
HETATM 4622 O  O     . HOH   P 5 .   ? 8.916   6.996   91.189  1.00 30.09  ? 1343 HOH   B O     1 
HETATM 4623 O  O     . HOH   P 5 .   ? 38.454  1.197   86.545  1.00 31.93  ? 1344 HOH   B O     1 
HETATM 4624 O  O     . HOH   P 5 .   ? -3.138  0.349   80.109  1.00 33.03  ? 1345 HOH   B O     1 
HETATM 4625 O  O     . HOH   P 5 .   ? -2.506  -4.868  87.461  1.00 27.99  ? 1346 HOH   B O     1 
HETATM 4626 O  O     . HOH   P 5 .   ? 3.863   -6.771  83.002  1.00 26.98  ? 1347 HOH   B O     1 
HETATM 4627 O  O     . HOH   P 5 .   ? -11.296 10.894  94.286  1.00 30.47  ? 1348 HOH   B O     1 
HETATM 4628 O  O     . HOH   P 5 .   ? 6.742   -15.525 70.356  1.00 44.01  ? 1349 HOH   B O     1 
HETATM 4629 O  O     . HOH   P 5 .   ? 22.861  1.601   96.083  1.00 32.19  ? 1350 HOH   B O     1 
HETATM 4630 O  O     . HOH   P 5 .   ? 3.093   -4.781  72.553  1.00 44.87  ? 1351 HOH   B O     1 
HETATM 4631 O  O     . HOH   P 5 .   ? 36.431  -1.611  79.536  1.00 36.36  ? 1352 HOH   B O     1 
HETATM 4632 O  O     . HOH   P 5 .   ? -15.976 3.140   86.486  1.00 29.25  ? 1353 HOH   B O     1 
HETATM 4633 O  O     . HOH   P 5 .   ? 7.294   -5.552  98.310  1.00 41.84  ? 1354 HOH   B O     1 
HETATM 4634 O  O     . HOH   P 5 .   ? -17.069 8.125   91.775  1.00 38.32  ? 1355 HOH   B O     1 
HETATM 4635 O  O     . HOH   P 5 .   ? -10.793 -5.302  92.238  1.00 34.66  ? 1356 HOH   B O     1 
HETATM 4636 O  O     . HOH   P 5 .   ? 36.600  -8.679  85.680  1.00 45.48  ? 1357 HOH   B O     1 
HETATM 4637 O  O     . HOH   P 5 .   ? 12.726  2.537   72.552  1.00 32.72  ? 1358 HOH   B O     1 
HETATM 4638 O  O     . HOH   P 5 .   ? 1.295   9.283   89.055  1.00 28.17  ? 1359 HOH   B O     1 
HETATM 4639 O  O     . HOH   P 5 .   ? 7.274   16.928  71.414  1.00 61.64  ? 1360 HOH   B O     1 
HETATM 4640 O  O     . HOH   P 5 .   ? 12.541  5.013   73.167  1.00 39.68  ? 1361 HOH   B O     1 
HETATM 4641 O  O     . HOH   P 5 .   ? -12.093 14.259  90.511  1.00 43.92  ? 1362 HOH   B O     1 
HETATM 4642 O  O     . HOH   P 5 .   ? 31.748  2.282   88.097  1.00 35.73  ? 1363 HOH   B O     1 
HETATM 4643 O  O     . HOH   P 5 .   ? 30.293  -8.201  82.483  1.00 37.24  ? 1364 HOH   B O     1 
HETATM 4644 O  O     . HOH   P 5 .   ? 29.160  5.137   79.782  1.00 33.56  ? 1365 HOH   B O     1 
HETATM 4645 O  O     . HOH   P 5 .   ? 2.096   8.303   91.318  1.00 26.78  ? 1366 HOH   B O     1 
HETATM 4646 O  O     . HOH   P 5 .   ? -14.929 -3.982  95.652  1.00 36.41  ? 1367 HOH   B O     1 
HETATM 4647 O  O     . HOH   P 5 .   ? 22.513  23.361  88.196  1.00 49.58  ? 1368 HOH   B O     1 
HETATM 4648 O  O     . HOH   P 5 .   ? 26.683  -7.437  98.113  1.00 41.77  ? 1369 HOH   B O     1 
HETATM 4649 O  O     . HOH   P 5 .   ? 21.513  20.095  79.277  1.00 55.29  ? 1370 HOH   B O     1 
HETATM 4650 O  O     . HOH   P 5 .   ? -9.732  -7.375  91.656  1.00 35.22  ? 1371 HOH   B O     1 
HETATM 4651 O  O     . HOH   P 5 .   ? 14.055  -7.657  97.230  1.00 35.30  ? 1372 HOH   B O     1 
HETATM 4652 O  O     . HOH   P 5 .   ? -3.777  14.285  91.298  1.00 33.52  ? 1373 HOH   B O     1 
HETATM 4653 O  O     . HOH   P 5 .   ? 18.300  21.887  91.944  1.00 44.94  ? 1374 HOH   B O     1 
HETATM 4654 O  O     . HOH   P 5 .   ? -12.766 7.892   96.736  1.00 34.62  ? 1375 HOH   B O     1 
HETATM 4655 O  O     . HOH   P 5 .   ? -17.339 -0.728  85.693  1.00 33.13  ? 1376 HOH   B O     1 
HETATM 4656 O  O     . HOH   P 5 .   ? -13.754 10.110  88.322  1.00 34.49  ? 1377 HOH   B O     1 
HETATM 4657 O  O     . HOH   P 5 .   ? -3.749  -9.258  87.924  1.00 39.53  ? 1378 HOH   B O     1 
HETATM 4658 O  O     . HOH   P 5 .   ? 22.932  -8.644  74.135  1.00 45.83  ? 1379 HOH   B O     1 
HETATM 4659 O  O     . HOH   P 5 .   ? 32.123  4.771   91.745  1.00 35.45  ? 1380 HOH   B O     1 
HETATM 4660 O  O     . HOH   P 5 .   ? 19.469  14.296  65.157  1.00 53.88  ? 1381 HOH   B O     1 
HETATM 4661 O  O     . HOH   P 5 .   ? 25.134  20.845  86.573  1.00 51.06  ? 1382 HOH   B O     1 
HETATM 4662 O  O     . HOH   P 5 .   ? 13.703  -17.929 81.839  1.00 40.94  ? 1383 HOH   B O     1 
HETATM 4663 O  O     . HOH   P 5 .   ? 15.914  21.599  91.492  1.00 42.70  ? 1384 HOH   B O     1 
HETATM 4664 O  O     . HOH   P 5 .   ? -16.329 -5.640  94.987  1.00 44.66  ? 1385 HOH   B O     1 
HETATM 4665 O  O     . HOH   P 5 .   ? 27.818  8.084   80.930  1.00 37.53  ? 1386 HOH   B O     1 
HETATM 4666 O  O     . HOH   P 5 .   ? -14.081 -4.043  93.182  1.00 35.46  ? 1387 HOH   B O     1 
HETATM 4667 O  O     . HOH   P 5 .   ? -13.531 12.214  90.019  1.00 41.55  ? 1388 HOH   B O     1 
HETATM 4668 O  O     . HOH   P 5 .   ? 9.004   -0.548  89.599  1.00 29.90  ? 1389 HOH   B O     1 
HETATM 4669 O  O     . HOH   P 5 .   ? 27.464  19.968  86.246  1.00 55.42  ? 1390 HOH   B O     1 
HETATM 4670 O  O     . HOH   P 5 .   ? 33.758  -0.429  79.115  1.00 42.94  ? 1391 HOH   B O     1 
HETATM 4671 O  O     . HOH   P 5 .   ? 6.627   8.165   92.710  1.00 32.72  ? 1392 HOH   B O     1 
HETATM 4672 O  O     . HOH   P 5 .   ? 3.429   9.234   93.592  1.00 31.92  ? 1393 HOH   B O     1 
HETATM 4673 O  O     . HOH   P 5 .   ? -2.444  -7.016  86.290  1.00 34.37  ? 1394 HOH   B O     1 
HETATM 4674 O  O     . HOH   P 5 .   ? 1.810   -8.061  90.844  1.00 42.49  ? 1395 HOH   B O     1 
HETATM 4675 O  O     . HOH   P 5 .   ? -21.117 4.532   91.383  1.00 31.28  ? 1396 HOH   B O     1 
HETATM 4676 O  O     . HOH   P 5 .   ? 0.642   -7.086  88.326  1.00 34.27  ? 1397 HOH   B O     1 
HETATM 4677 O  O     . HOH   P 5 .   ? 20.140  -12.443 92.688  1.00 32.42  ? 1398 HOH   B O     1 
HETATM 4678 O  O     . HOH   P 5 .   ? 3.063   -7.836  88.982  1.00 34.45  ? 1399 HOH   B O     1 
HETATM 4679 O  O     . HOH   P 5 .   ? -20.543 7.008   88.121  1.00 38.57  ? 1400 HOH   B O     1 
HETATM 4680 O  O     . HOH   P 5 .   ? 21.529  -15.108 93.053  1.00 51.98  ? 1401 HOH   B O     1 
HETATM 4681 O  O     . HOH   P 5 .   ? 22.444  -13.410 90.368  1.00 33.28  ? 1402 HOH   B O     1 
HETATM 4682 O  O     . HOH   P 5 .   ? 6.307   -5.880  100.215 1.00 48.07  ? 1403 HOH   B O     1 
HETATM 4683 O  O     . HOH   P 5 .   ? 29.121  -5.894  54.233  1.00 43.01  ? 1404 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   . THR A 8   ? 0.3368 0.5559 1.1277 -0.0658 0.0642  0.1661  918  THR A N   
2    C CA  . THR A 8   ? 0.3263 0.5176 1.1234 -0.0636 0.0589  0.1654  918  THR A CA  
3    C C   . THR A 8   ? 0.3218 0.5027 1.1074 -0.0543 0.0565  0.1564  918  THR A C   
4    O O   . THR A 8   ? 0.3047 0.4907 1.0877 -0.0507 0.0532  0.1447  918  THR A O   
5    C CB  . THR A 8   ? 0.3678 0.5502 1.1814 -0.0694 0.0518  0.1588  918  THR A CB  
6    O OG1 . THR A 8   ? 0.4366 0.6172 1.2484 -0.0645 0.0457  0.1450  918  THR A OG1 
7    C CG2 . THR A 8   ? 0.3677 0.5698 1.1903 -0.0781 0.0533  0.1621  918  THR A CG2 
8    N N   . GLU A 9   ? 0.3124 0.4786 1.0920 -0.0503 0.0582  0.1624  919  GLU A N   
9    C CA  . GLU A 9   ? 0.3007 0.4573 1.0686 -0.0422 0.0563  0.1550  919  GLU A CA  
10   C C   . GLU A 9   ? 0.3011 0.4369 1.0789 -0.0419 0.0480  0.1456  919  GLU A C   
11   O O   . GLU A 9   ? 0.3120 0.4327 1.1025 -0.0465 0.0461  0.1487  919  GLU A O   
12   C CB  . GLU A 9   ? 0.3001 0.4526 1.0574 -0.0384 0.0617  0.1657  919  GLU A CB  
13   C CG  . GLU A 9   ? 0.2874 0.4433 1.0251 -0.0311 0.0631  0.1598  919  GLU A CG  
14   C CD  . GLU A 9   ? 0.2868 0.4330 1.0173 -0.0269 0.0659  0.1687  919  GLU A CD  
15   O OE1 . GLU A 9   ? 0.2871 0.4131 1.0253 -0.0247 0.0618  0.1662  919  GLU A OE1 
16   O OE2 . GLU A 9   ? 0.2869 0.4472 1.0043 -0.0264 0.0722  0.1780  919  GLU A OE2 
17   N N   . LYS A 10  ? 0.2909 0.4262 1.0622 -0.0372 0.0431  0.1335  920  LYS A N   
18   C CA  . LYS A 10  ? 0.2903 0.4089 1.0673 -0.0370 0.0345  0.1236  920  LYS A CA  
19   C C   . LYS A 10  ? 0.2792 0.3907 1.0417 -0.0292 0.0335  0.1189  920  LYS A C   
20   O O   . LYS A 10  ? 0.2714 0.3934 1.0191 -0.0240 0.0383  0.1202  920  LYS A O   
21   C CB  . LYS A 10  ? 0.2900 0.4168 1.0741 -0.0395 0.0275  0.1139  920  LYS A CB  
22   C CG  . LYS A 10  ? 0.3233 0.4580 1.1223 -0.0484 0.0277  0.1177  920  LYS A CG  
23   C CD  . LYS A 10  ? 0.3528 0.4988 1.1589 -0.0506 0.0208  0.1091  920  LYS A CD  
24   C CE  . LYS A 10  ? 0.3614 0.5176 1.1811 -0.0599 0.0215  0.1130  920  LYS A CE  
25   N NZ  . LYS A 10  ? 0.4271 0.5978 1.2540 -0.0616 0.0152  0.1057  920  LYS A NZ  
26   N N   . ILE A 11  ? 0.2798 0.3741 1.0455 -0.0292 0.0273  0.1125  921  ILE A N   
27   C CA  . ILE A 11  ? 0.2697 0.3577 1.0223 -0.0226 0.0248  0.1067  921  ILE A CA  
28   C C   . ILE A 11  ? 0.2657 0.3543 1.0180 -0.0222 0.0149  0.0942  921  ILE A C   
29   O O   . ILE A 11  ? 0.2728 0.3545 1.0360 -0.0281 0.0078  0.0883  921  ILE A O   
30   C CB  . ILE A 11  ? 0.2736 0.3432 1.0284 -0.0227 0.0255  0.1087  921  ILE A CB  
31   C CG1 . ILE A 11  ? 0.2784 0.3493 1.0338 -0.0220 0.0355  0.1238  921  ILE A CG1 
32   C CG2 . ILE A 11  ? 0.2627 0.3284 1.0042 -0.0165 0.0220  0.1016  921  ILE A CG2 
33   C CD1 . ILE A 11  ? 0.2851 0.3367 1.0439 -0.0212 0.0377  0.1278  921  ILE A CD1 
34   N N   . ILE A 12  ? 0.2561 0.3527 0.9945 -0.0156 0.0143  0.0902  922  ILE A N   
35   C CA  . ILE A 12  ? 0.3086 0.4084 1.0464 -0.0141 0.0054  0.0809  922  ILE A CA  
36   C C   . ILE A 12  ? 0.2467 0.3380 0.9717 -0.0091 -0.0004 0.0743  922  ILE A C   
37   O O   . ILE A 12  ? 0.2452 0.3382 0.9683 -0.0076 -0.0088 0.0675  922  ILE A O   
38   C CB  . ILE A 12  ? 0.2712 0.3871 1.0059 -0.0110 0.0090  0.0810  922  ILE A CB  
39   C CG1 . ILE A 12  ? 0.2456 0.3655 0.9622 -0.0051 0.0177  0.0834  922  ILE A CG1 
40   C CG2 . ILE A 12  ? 0.2586 0.3851 1.0074 -0.0169 0.0130  0.0863  922  ILE A CG2 
41   C CD1 . ILE A 12  ? 0.2918 0.4281 1.0065 -0.0033 0.0240  0.0830  922  ILE A CD1 
42   N N   . CYS A 13  ? 0.3136 0.3969 1.0294 -0.0064 0.0036  0.0769  923  CYS A N   
43   C CA  . CYS A 13  ? 0.2433 0.3177 0.9462 -0.0022 -0.0024 0.0704  923  CYS A CA  
44   C C   . CYS A 13  ? 0.2441 0.3045 0.9345 -0.0010 0.0028  0.0744  923  CYS A C   
45   O O   . CYS A 13  ? 0.2420 0.3086 0.9334 0.0003  0.0125  0.0840  923  CYS A O   
46   C CB  . CYS A 13  ? 0.2318 0.3119 0.9156 0.0049  -0.0019 0.0679  923  CYS A CB  
47   S SG  . CYS A 13  ? 0.2554 0.3235 0.9172 0.0098  -0.0101 0.0603  923  CYS A SG  
48   N N   . ARG A 14  ? 0.2620 0.3053 0.9419 -0.0017 -0.0034 0.0673  924  ARG A N   
49   C CA  . ARG A 14  ? 0.2575 0.2872 0.9268 0.0007  0.0017  0.0707  924  ARG A CA  
50   C C   . ARG A 14  ? 0.2492 0.2816 0.8947 0.0086  0.0045  0.0722  924  ARG A C   
51   O O   . ARG A 14  ? 0.2494 0.2816 0.8894 0.0119  0.0126  0.0807  924  ARG A O   
52   C CB  . ARG A 14  ? 0.2933 0.3040 0.9605 -0.0031 -0.0046 0.0612  924  ARG A CB  
53   C CG  . ARG A 14  ? 0.3690 0.3780 1.0548 -0.0125 -0.0104 0.0554  924  ARG A CG  
54   C CD  . ARG A 14  ? 0.4312 0.4203 1.1151 -0.0173 -0.0134 0.0460  924  ARG A CD  
55   N NE  . ARG A 14  ? 0.4449 0.4259 1.1055 -0.0117 -0.0160 0.0397  924  ARG A NE  
56   C CZ  . ARG A 14  ? 0.4633 0.4487 1.1095 -0.0115 -0.0254 0.0309  924  ARG A CZ  
57   N NH1 . ARG A 14  ? 0.4012 0.3992 1.0546 -0.0158 -0.0333 0.0281  924  ARG A NH1 
58   N NH2 . ARG A 14  ? 0.4277 0.4062 1.0525 -0.0069 -0.0270 0.0258  924  ARG A NH2 
59   N N   . ASP A 15  ? 0.2426 0.2786 0.8745 0.0114  -0.0019 0.0649  925  ASP A N   
60   C CA  . ASP A 15  ? 0.2356 0.2742 0.8442 0.0176  0.0005  0.0654  925  ASP A CA  
61   C C   . ASP A 15  ? 0.2280 0.2757 0.8321 0.0195  -0.0039 0.0606  925  ASP A C   
62   O O   . ASP A 15  ? 0.2296 0.2718 0.8275 0.0191  -0.0138 0.0528  925  ASP A O   
63   C CB  . ASP A 15  ? 0.2412 0.2651 0.8312 0.0195  -0.0038 0.0597  925  ASP A CB  
64   C CG  . ASP A 15  ? 0.2348 0.2623 0.8000 0.0251  -0.0009 0.0610  925  ASP A CG  
65   O OD1 . ASP A 15  ? 0.2276 0.2680 0.7905 0.0272  0.0068  0.0678  925  ASP A OD1 
66   O OD2 . ASP A 15  ? 0.2376 0.2562 0.7854 0.0266  -0.0061 0.0547  925  ASP A OD2 
67   N N   . VAL A 16  ? 0.2209 0.2829 0.8277 0.0215  0.0039  0.0655  926  VAL A N   
68   C CA  . VAL A 16  ? 0.2156 0.2846 0.8202 0.0241  0.0012  0.0608  926  VAL A CA  
69   C C   . VAL A 16  ? 0.2151 0.2758 0.7946 0.0275  -0.0039 0.0553  926  VAL A C   
70   O O   . VAL A 16  ? 0.2140 0.2751 0.7920 0.0292  -0.0097 0.0506  926  VAL A O   
71   C CB  . VAL A 16  ? 0.2395 0.3216 0.8423 0.0241  0.0123  0.0647  926  VAL A CB  
72   C CG1 . VAL A 16  ? 0.2172 0.3069 0.8405 0.0197  0.0156  0.0687  926  VAL A CG1 
73   C CG2 . VAL A 16  ? 0.2099 0.2975 0.7984 0.0254  0.0220  0.0706  926  VAL A CG2 
74   N N   . ALA A 17  ? 0.2300 0.2838 0.7906 0.0285  -0.0020 0.0566  927  ALA A N   
75   C CA  . ALA A 17  ? 0.2163 0.2636 0.7516 0.0310  -0.0064 0.0518  927  ALA A CA  
76   C C   . ALA A 17  ? 0.2222 0.2573 0.7523 0.0291  -0.0183 0.0450  927  ALA A C   
77   O O   . ALA A 17  ? 0.2226 0.2532 0.7332 0.0302  -0.0240 0.0405  927  ALA A O   
78   C CB  . ALA A 17  ? 0.2146 0.2643 0.7319 0.0329  0.0020  0.0568  927  ALA A CB  
79   N N   . ARG A 18  ? 0.2278 0.2583 0.7743 0.0253  -0.0219 0.0438  928  ARG A N   
80   C CA  . ARG A 18  ? 0.2569 0.2787 0.8011 0.0216  -0.0332 0.0359  928  ARG A CA  
81   C C   . ARG A 18  ? 0.2389 0.2515 0.7610 0.0226  -0.0341 0.0322  928  ARG A C   
82   O O   . ARG A 18  ? 0.2693 0.2785 0.7774 0.0211  -0.0431 0.0254  928  ARG A O   
83   C CB  . ARG A 18  ? 0.2332 0.2593 0.7771 0.0208  -0.0435 0.0320  928  ARG A CB  
84   C CG  . ARG A 18  ? 0.2295 0.2663 0.7963 0.0211  -0.0425 0.0356  928  ARG A CG  
85   C CD  . ARG A 18  ? 0.2299 0.2707 0.7989 0.0210  -0.0535 0.0332  928  ARG A CD  
86   N NE  . ARG A 18  ? 0.2366 0.2716 0.7808 0.0228  -0.0586 0.0304  928  ARG A NE  
87   C CZ  . ARG A 18  ? 0.2718 0.3073 0.8045 0.0277  -0.0554 0.0320  928  ARG A CZ  
88   N NH1 . ARG A 18  ? 0.2568 0.2988 0.8013 0.0316  -0.0471 0.0355  928  ARG A NH1 
89   N NH2 . ARG A 18  ? 0.2287 0.2583 0.7376 0.0279  -0.0601 0.0295  928  ARG A NH2 
90   N N   . GLY A 19  ? 0.2643 0.2744 0.7844 0.0252  -0.0248 0.0373  929  GLY A N   
91   C CA  . GLY A 19  ? 0.2547 0.2580 0.7561 0.0275  -0.0240 0.0349  929  GLY A CA  
92   C C   . GLY A 19  ? 0.2950 0.3034 0.7710 0.0313  -0.0231 0.0358  929  GLY A C   
93   O O   . GLY A 19  ? 0.2395 0.2441 0.6991 0.0332  -0.0227 0.0337  929  GLY A O   
94   N N   . TYR A 20  ? 0.2717 0.2886 0.7444 0.0322  -0.0223 0.0382  930  TYR A N   
95   C CA  . TYR A 20  ? 0.2254 0.2462 0.6733 0.0344  -0.0214 0.0381  930  TYR A CA  
96   C C   . TYR A 20  ? 0.2402 0.2687 0.6785 0.0375  -0.0100 0.0459  930  TYR A C   
97   O O   . TYR A 20  ? 0.2241 0.2562 0.6397 0.0385  -0.0090 0.0455  930  TYR A O   
98   C CB  . TYR A 20  ? 0.2214 0.2469 0.6700 0.0342  -0.0236 0.0372  930  TYR A CB  
99   C CG  . TYR A 20  ? 0.2248 0.2448 0.6674 0.0320  -0.0364 0.0305  930  TYR A CG  
100  C CD1 . TYR A 20  ? 0.2260 0.2436 0.6435 0.0317  -0.0411 0.0274  930  TYR A CD1 
101  C CD2 . TYR A 20  ? 0.2427 0.2619 0.7050 0.0295  -0.0441 0.0284  930  TYR A CD2 
102  C CE1 . TYR A 20  ? 0.2299 0.2442 0.6426 0.0290  -0.0534 0.0229  930  TYR A CE1 
103  C CE2 . TYR A 20  ? 0.2310 0.2482 0.6890 0.0269  -0.0562 0.0242  930  TYR A CE2 
104  C CZ  . TYR A 20  ? 0.2611 0.2757 0.6947 0.0267  -0.0610 0.0218  930  TYR A CZ  
105  O OH  . TYR A 20  ? 0.2453 0.2597 0.6762 0.0234  -0.0737 0.0191  930  TYR A OH  
106  N N   . GLU A 21  ? 0.2326 0.2657 0.6873 0.0382  -0.0015 0.0538  931  GLU A N   
107  C CA  . GLU A 21  ? 0.2771 0.3205 0.7238 0.0406  0.0089  0.0631  931  GLU A CA  
108  C C   . GLU A 21  ? 0.2310 0.2677 0.6800 0.0433  0.0104  0.0664  931  GLU A C   
109  O O   . GLU A 21  ? 0.2527 0.2763 0.7118 0.0425  0.0048  0.0606  931  GLU A O   
110  C CB  . GLU A 21  ? 0.2144 0.2708 0.6770 0.0393  0.0181  0.0716  931  GLU A CB  
111  C CG  . GLU A 21  ? 0.2100 0.2723 0.6758 0.0371  0.0180  0.0673  931  GLU A CG  
112  C CD  . GLU A 21  ? 0.2118 0.2814 0.6541 0.0369  0.0209  0.0648  931  GLU A CD  
113  O OE1 . GLU A 21  ? 0.2372 0.3085 0.6587 0.0379  0.0220  0.0663  931  GLU A OE1 
114  O OE2 . GLU A 21  ? 0.2045 0.2784 0.6497 0.0355  0.0226  0.0611  931  GLU A OE2 
115  N N   . ASN A 22  ? 0.2454 0.2921 0.6851 0.0463  0.0185  0.0756  932  ASN A N   
116  C CA  . ASN A 22  ? 0.2302 0.2716 0.6753 0.0503  0.0215  0.0807  932  ASN A CA  
117  C C   . ASN A 22  ? 0.2485 0.2833 0.7220 0.0498  0.0250  0.0868  932  ASN A C   
118  O O   . ASN A 22  ? 0.2455 0.2698 0.7279 0.0528  0.0263  0.0884  932  ASN A O   
119  C CB  . ASN A 22  ? 0.2973 0.3545 0.7301 0.0537  0.0300  0.0926  932  ASN A CB  
120  C CG  . ASN A 22  ? 0.2243 0.2887 0.6280 0.0537  0.0277  0.0876  932  ASN A CG  
121  O OD1 . ASN A 22  ? 0.2977 0.3797 0.6892 0.0525  0.0337  0.0944  932  ASN A OD1 
122  N ND2 . ASN A 22  ? 0.2600 0.3125 0.6521 0.0539  0.0191  0.0757  932  ASN A ND2 
123  N N   . VAL A 23  ? 0.2617 0.3029 0.7500 0.0461  0.0272  0.0904  933  VAL A N   
124  C CA  . VAL A 23  ? 0.2401 0.2775 0.7556 0.0444  0.0308  0.0974  933  VAL A CA  
125  C C   . VAL A 23  ? 0.2356 0.2731 0.7644 0.0392  0.0267  0.0915  933  VAL A C   
126  O O   . VAL A 23  ? 0.2278 0.2737 0.7474 0.0377  0.0246  0.0868  933  VAL A O   
127  C CB  . VAL A 23  ? 0.2608 0.3149 0.7830 0.0454  0.0416  0.1149  933  VAL A CB  
128  C CG1 . VAL A 23  ? 0.2456 0.2988 0.7626 0.0513  0.0460  0.1236  933  VAL A CG1 
129  C CG2 . VAL A 23  ? 0.2740 0.3495 0.7823 0.0431  0.0455  0.1172  933  VAL A CG2 
130  N N   . PRO A 24  ? 0.2430 0.2710 0.7945 0.0361  0.0257  0.0916  934  PRO A N   
131  C CA  . PRO A 24  ? 0.2542 0.2854 0.8209 0.0310  0.0222  0.0876  934  PRO A CA  
132  C C   . PRO A 24  ? 0.2352 0.2860 0.8095 0.0295  0.0302  0.0975  934  PRO A C   
133  O O   . PRO A 24  ? 0.2333 0.2935 0.8111 0.0302  0.0388  0.1103  934  PRO A O   
134  C CB  . PRO A 24  ? 0.2596 0.2764 0.8479 0.0274  0.0205  0.0864  934  PRO A CB  
135  C CG  . PRO A 24  ? 0.2606 0.2713 0.8507 0.0310  0.0274  0.0958  934  PRO A CG  
136  C CD  . PRO A 24  ? 0.2556 0.2683 0.8205 0.0369  0.0272  0.0940  934  PRO A CD  
137  N N   . ILE A 25  ? 0.2269 0.2853 0.8047 0.0272  0.0274  0.0916  935  ILE A N   
138  C CA  . ILE A 25  ? 0.2205 0.2983 0.8075 0.0249  0.0347  0.0978  935  ILE A CA  
139  C C   . ILE A 25  ? 0.2223 0.3006 0.8337 0.0205  0.0316  0.0952  935  ILE A C   
140  O O   . ILE A 25  ? 0.2192 0.2984 0.8326 0.0203  0.0259  0.0865  935  ILE A O   
141  C CB  . ILE A 25  ? 0.2124 0.3007 0.7813 0.0267  0.0363  0.0927  935  ILE A CB  
142  C CG1 . ILE A 25  ? 0.2113 0.3006 0.7554 0.0299  0.0394  0.0957  935  ILE A CG1 
143  C CG2 . ILE A 25  ? 0.2087 0.3165 0.7843 0.0236  0.0451  0.0970  935  ILE A CG2 
144  C CD1 . ILE A 25  ? 0.2054 0.3037 0.7297 0.0305  0.0415  0.0904  935  ILE A CD1 
145  N N   . PRO A 26  ? 0.2282 0.3062 0.8590 0.0168  0.0349  0.1033  936  PRO A N   
146  C CA  . PRO A 26  ? 0.2311 0.3095 0.8848 0.0116  0.0313  0.1006  936  PRO A CA  
147  C C   . PRO A 26  ? 0.2286 0.3239 0.8827 0.0093  0.0364  0.1025  936  PRO A C   
148  O O   . PRO A 26  ? 0.2416 0.3488 0.8809 0.0104  0.0440  0.1070  936  PRO A O   
149  C CB  . PRO A 26  ? 0.2630 0.3326 0.9320 0.0080  0.0343  0.1094  936  PRO A CB  
150  C CG  . PRO A 26  ? 0.2406 0.3177 0.9010 0.0110  0.0435  0.1221  936  PRO A CG  
151  C CD  . PRO A 26  ? 0.2474 0.3247 0.8811 0.0170  0.0420  0.1162  936  PRO A CD  
152  N N   . CYS A 27  ? 0.2801 0.3760 0.9486 0.0058  0.0319  0.0979  937  CYS A N   
153  C CA  . CYS A 27  ? 0.2328 0.3429 0.9019 0.0039  0.0362  0.0982  937  CYS A CA  
154  C C   . CYS A 27  ? 0.2407 0.3536 0.9299 -0.0022 0.0370  0.1038  937  CYS A C   
155  O O   . CYS A 27  ? 0.2673 0.3711 0.9720 -0.0053 0.0298  0.1003  937  CYS A O   
156  C CB  . CYS A 27  ? 0.2298 0.3407 0.8961 0.0065  0.0300  0.0872  937  CYS A CB  
157  S SG  . CYS A 27  ? 0.2639 0.3929 0.9327 0.0057  0.0364  0.0860  937  CYS A SG  
158  N N   . VAL A 28  ? 0.2440 0.3705 0.9321 -0.0047 0.0454  0.1120  938  VAL A N   
159  C CA  . VAL A 28  ? 0.2524 0.3843 0.9573 -0.0107 0.0466  0.1175  938  VAL A CA  
160  C C   . VAL A 28  ? 0.2525 0.4037 0.9549 -0.0119 0.0509  0.1152  938  VAL A C   
161  O O   . VAL A 28  ? 0.2477 0.4092 0.9347 -0.0088 0.0559  0.1121  938  VAL A O   
162  C CB  . VAL A 28  ? 0.2594 0.3906 0.9686 -0.0139 0.0525  0.1318  938  VAL A CB  
163  C CG1 . VAL A 28  ? 0.2585 0.3732 0.9668 -0.0108 0.0512  0.1350  938  VAL A CG1 
164  C CG2 . VAL A 28  ? 0.2871 0.4378 0.9822 -0.0144 0.0615  0.1392  938  VAL A CG2 
165  N N   . ASN A 29  ? 0.2592 0.4160 0.9776 -0.0169 0.0494  0.1163  939  ASN A N   
166  C CA  . ASN A 29  ? 0.2612 0.4385 0.9808 -0.0191 0.0543  0.1151  939  ASN A CA  
167  C C   . ASN A 29  ? 0.2709 0.4547 1.0051 -0.0266 0.0557  0.1237  939  ASN A C   
168  O O   . ASN A 29  ? 0.2759 0.4513 1.0258 -0.0302 0.0495  0.1228  939  ASN A O   
169  C CB  . ASN A 29  ? 0.2582 0.4383 0.9827 -0.0158 0.0492  0.1036  939  ASN A CB  
170  C CG  . ASN A 29  ? 0.2707 0.4732 0.9972 -0.0168 0.0553  0.1008  939  ASN A CG  
171  O OD1 . ASN A 29  ? 0.2653 0.4820 0.9939 -0.0221 0.0614  0.1074  939  ASN A OD1 
172  N ND2 . ASN A 29  ? 0.2569 0.4626 0.9834 -0.0116 0.0536  0.0912  939  ASN A ND2 
173  N N   . GLY A 30  ? 0.2746 0.4744 1.0028 -0.0300 0.0638  0.1318  940  GLY A N   
174  C CA  . GLY A 30  ? 0.2843 0.4953 1.0246 -0.0376 0.0659  0.1394  940  GLY A CA  
175  C C   . GLY A 30  ? 0.2850 0.5226 1.0211 -0.0401 0.0723  0.1367  940  GLY A C   
176  O O   . GLY A 30  ? 0.2926 0.5448 1.0304 -0.0466 0.0770  0.1453  940  GLY A O   
177  N N   . VAL A 31  ? 0.2782 0.5227 1.0098 -0.0351 0.0726  0.1246  941  VAL A N   
178  C CA  . VAL A 31  ? 0.2786 0.5483 1.0058 -0.0363 0.0798  0.1193  941  VAL A CA  
179  C C   . VAL A 31  ? 0.2797 0.5575 1.0222 -0.0356 0.0767  0.1109  941  VAL A C   
180  O O   . VAL A 31  ? 0.2972 0.5959 1.0468 -0.0407 0.0807  0.1114  941  VAL A O   
181  C CB  . VAL A 31  ? 0.2717 0.5455 0.9802 -0.0311 0.0853  0.1124  941  VAL A CB  
182  C CG1 . VAL A 31  ? 0.3353 0.6311 1.0444 -0.0306 0.0915  0.1019  941  VAL A CG1 
183  C CG2 . VAL A 31  ? 0.2733 0.5530 0.9659 -0.0347 0.0912  0.1218  941  VAL A CG2 
184  N N   . ASP A 32  ? 0.2751 0.5384 1.0229 -0.0294 0.0696  0.1034  942  ASP A N   
185  C CA  . ASP A 32  ? 0.3075 0.5782 1.0700 -0.0275 0.0657  0.0961  942  ASP A CA  
186  C C   . ASP A 32  ? 0.3067 0.5565 1.0758 -0.0240 0.0546  0.0934  942  ASP A C   
187  O O   . ASP A 32  ? 0.2728 0.5040 1.0379 -0.0250 0.0504  0.0975  942  ASP A O   
188  C CB  . ASP A 32  ? 0.2740 0.5596 1.0323 -0.0218 0.0722  0.0864  942  ASP A CB  
189  C CG  . ASP A 32  ? 0.3325 0.6057 1.0745 -0.0151 0.0740  0.0813  942  ASP A CG  
190  O OD1 . ASP A 32  ? 0.2633 0.5150 1.0022 -0.0116 0.0666  0.0815  942  ASP A OD1 
191  O OD2 . ASP A 32  ? 0.3546 0.6407 1.0871 -0.0138 0.0830  0.0762  942  ASP A OD2 
192  N N   . GLY A 33  ? 0.2808 0.5346 1.0598 -0.0200 0.0499  0.0865  943  GLY A N   
193  C CA  . GLY A 33  ? 0.2838 0.5230 1.0697 -0.0180 0.0387  0.0841  943  GLY A CA  
194  C C   . GLY A 33  ? 0.2668 0.4923 1.0426 -0.0096 0.0351  0.0779  943  GLY A C   
195  O O   . GLY A 33  ? 0.2666 0.4842 1.0480 -0.0076 0.0254  0.0752  943  GLY A O   
196  N N   . GLU A 34  ? 0.2624 0.4863 1.0233 -0.0054 0.0423  0.0758  944  GLU A N   
197  C CA  . GLU A 34  ? 0.2575 0.4679 1.0081 0.0019  0.0390  0.0701  944  GLU A CA  
198  C C   . GLU A 34  ? 0.2655 0.4559 1.0106 0.0007  0.0305  0.0723  944  GLU A C   
199  O O   . GLU A 34  ? 0.2533 0.4376 0.9915 -0.0029 0.0333  0.0775  944  GLU A O   
200  C CB  . GLU A 34  ? 0.2860 0.5002 1.0212 0.0051  0.0494  0.0672  944  GLU A CB  
201  C CG  . GLU A 34  ? 0.3232 0.5278 1.0505 0.0128  0.0480  0.0601  944  GLU A CG  
202  C CD  . GLU A 34  ? 0.2577 0.4688 0.9986 0.0179  0.0459  0.0548  944  GLU A CD  
203  O OE1 . GLU A 34  ? 0.3043 0.5327 1.0583 0.0162  0.0498  0.0549  944  GLU A OE1 
204  O OE2 . GLU A 34  ? 0.2554 0.4553 0.9943 0.0238  0.0403  0.0512  944  GLU A OE2 
205  N N   . PRO A 35  ? 0.3054 0.4868 1.0541 0.0033  0.0202  0.0689  945  PRO A N   
206  C CA  . PRO A 35  ? 0.2518 0.4159 0.9952 0.0017  0.0120  0.0693  945  PRO A CA  
207  C C   . PRO A 35  ? 0.2457 0.3990 0.9699 0.0067  0.0147  0.0672  945  PRO A C   
208  O O   . PRO A 35  ? 0.2814 0.4403 0.9969 0.0108  0.0228  0.0651  945  PRO A O   
209  C CB  . PRO A 35  ? 0.2596 0.4231 1.0123 0.0026  0.0002  0.0661  945  PRO A CB  
210  C CG  . PRO A 35  ? 0.2764 0.4517 1.0334 0.0085  0.0032  0.0635  945  PRO A CG  
211  C CD  . PRO A 35  ? 0.2603 0.4492 1.0197 0.0074  0.0153  0.0651  945  PRO A CD  
212  N N   . CYS A 36  ? 0.2489 0.3877 0.9671 0.0059  0.0079  0.0668  946  CYS A N   
213  C CA  . CYS A 36  ? 0.2377 0.3666 0.9372 0.0100  0.0096  0.0651  946  CYS A CA  
214  C C   . CYS A 36  ? 0.2546 0.3840 0.9466 0.0165  0.0087  0.0595  946  CYS A C   
215  O O   . CYS A 36  ? 0.2393 0.3683 0.9385 0.0181  0.0001  0.0570  946  CYS A O   
216  C CB  . CYS A 36  ? 0.2384 0.3531 0.9349 0.0083  0.0011  0.0643  946  CYS A CB  
217  S SG  . CYS A 36  ? 0.2655 0.3704 0.9388 0.0125  0.0049  0.0640  946  CYS A SG  
218  N N   . PRO A 37  ? 0.2335 0.3649 0.9121 0.0200  0.0177  0.0580  947  PRO A N   
219  C CA  . PRO A 37  ? 0.2521 0.3826 0.9255 0.0259  0.0179  0.0524  947  PRO A CA  
220  C C   . PRO A 37  ? 0.2697 0.3861 0.9336 0.0283  0.0073  0.0502  947  PRO A C   
221  O O   . PRO A 37  ? 0.2285 0.3364 0.8805 0.0270  0.0052  0.0512  947  PRO A O   
222  C CB  . PRO A 37  ? 0.2312 0.3675 0.8922 0.0270  0.0307  0.0510  947  PRO A CB  
223  C CG  . PRO A 37  ? 0.2277 0.3640 0.8816 0.0225  0.0340  0.0570  947  PRO A CG  
224  C CD  . PRO A 37  ? 0.2306 0.3664 0.8993 0.0180  0.0281  0.0618  947  PRO A CD  
225  N N   . GLU A 38  ? 0.2367 0.3517 0.9066 0.0316  0.0000  0.0480  948  GLU A N   
226  C CA  . GLU A 38  ? 0.2367 0.3406 0.8978 0.0332  -0.0111 0.0467  948  GLU A CA  
227  C C   . GLU A 38  ? 0.2414 0.3438 0.9021 0.0392  -0.0119 0.0443  948  GLU A C   
228  O O   . GLU A 38  ? 0.2527 0.3502 0.9132 0.0404  -0.0229 0.0451  948  GLU A O   
229  C CB  . GLU A 38  ? 0.2638 0.3675 0.9351 0.0289  -0.0236 0.0487  948  GLU A CB  
230  C CG  . GLU A 38  ? 0.3128 0.4145 0.9858 0.0228  -0.0233 0.0503  948  GLU A CG  
231  C CD  . GLU A 38  ? 0.3796 0.4840 1.0678 0.0170  -0.0338 0.0510  948  GLU A CD  
232  O OE1 . GLU A 38  ? 0.3783 0.4823 1.0675 0.0169  -0.0451 0.0497  948  GLU A OE1 
233  O OE2 . GLU A 38  ? 0.4594 0.5673 1.1588 0.0118  -0.0307 0.0530  948  GLU A OE2 
234  N N   . ASP A 39  ? 0.2427 0.3498 0.9043 0.0425  -0.0002 0.0415  949  ASP A N   
235  C CA  . ASP A 39  ? 0.2565 0.3609 0.9196 0.0486  0.0017  0.0384  949  ASP A CA  
236  C C   . ASP A 39  ? 0.2467 0.3407 0.8910 0.0507  0.0052  0.0349  949  ASP A C   
237  O O   . ASP A 39  ? 0.2696 0.3632 0.9143 0.0546  0.0140  0.0304  949  ASP A O   
238  C CB  . ASP A 39  ? 0.2837 0.4000 0.9613 0.0508  0.0132  0.0358  949  ASP A CB  
239  C CG  . ASP A 39  ? 0.2959 0.4098 0.9820 0.0575  0.0143  0.0331  949  ASP A CG  
240  O OD1 . ASP A 39  ? 0.2663 0.3710 0.9501 0.0601  0.0040  0.0355  949  ASP A OD1 
241  O OD2 . ASP A 39  ? 0.3434 0.4652 1.0390 0.0602  0.0258  0.0286  949  ASP A OD2 
242  N N   . TYR A 40  ? 0.2405 0.3266 0.8692 0.0481  -0.0011 0.0363  950  TYR A N   
243  C CA  . TYR A 40  ? 0.2373 0.3148 0.8467 0.0494  0.0012  0.0336  950  TYR A CA  
244  C C   . TYR A 40  ? 0.2332 0.3032 0.8301 0.0467  -0.0102 0.0362  950  TYR A C   
245  O O   . TYR A 40  ? 0.2307 0.3037 0.8327 0.0427  -0.0146 0.0389  950  TYR A O   
246  C CB  . TYR A 40  ? 0.2317 0.3164 0.8346 0.0481  0.0158  0.0312  950  TYR A CB  
247  C CG  . TYR A 40  ? 0.2245 0.3129 0.8214 0.0433  0.0158  0.0355  950  TYR A CG  
248  C CD1 . TYR A 40  ? 0.2247 0.3201 0.8349 0.0398  0.0150  0.0393  950  TYR A CD1 
249  C CD2 . TYR A 40  ? 0.2411 0.3258 0.8201 0.0425  0.0167  0.0361  950  TYR A CD2 
250  C CE1 . TYR A 40  ? 0.2203 0.3170 0.8272 0.0357  0.0153  0.0438  950  TYR A CE1 
251  C CE2 . TYR A 40  ? 0.2138 0.3012 0.7891 0.0389  0.0171  0.0408  950  TYR A CE2 
252  C CZ  . TYR A 40  ? 0.2507 0.3430 0.8403 0.0356  0.0166  0.0447  950  TYR A CZ  
253  O OH  . TYR A 40  ? 0.3048 0.3979 0.8927 0.0323  0.0175  0.0500  950  TYR A OH  
254  N N   . LYS A 41  ? 0.2335 0.2938 0.8149 0.0485  -0.0148 0.0349  951  LYS A N   
255  C CA  . LYS A 41  ? 0.2798 0.3341 0.8471 0.0460  -0.0239 0.0360  951  LYS A CA  
256  C C   . LYS A 41  ? 0.2222 0.2782 0.7767 0.0451  -0.0146 0.0354  951  LYS A C   
257  O O   . LYS A 41  ? 0.2207 0.2774 0.7674 0.0473  -0.0055 0.0330  951  LYS A O   
258  C CB  . LYS A 41  ? 0.2336 0.2781 0.7892 0.0480  -0.0339 0.0358  951  LYS A CB  
259  C CG  . LYS A 41  ? 0.2306 0.2705 0.7733 0.0452  -0.0449 0.0363  951  LYS A CG  
260  C CD  . LYS A 41  ? 0.2312 0.2758 0.7869 0.0410  -0.0546 0.0380  951  LYS A CD  
261  C CE  . LYS A 41  ? 0.2435 0.2839 0.7868 0.0381  -0.0661 0.0368  951  LYS A CE  
262  N NZ  . LYS A 41  ? 0.2310 0.2757 0.7843 0.0325  -0.0736 0.0361  951  LYS A NZ  
263  N N   . TYR A 42  ? 0.2183 0.2762 0.7730 0.0417  -0.0161 0.0377  952  TYR A N   
264  C CA  . TYR A 42  ? 0.2124 0.2717 0.7537 0.0412  -0.0093 0.0389  952  TYR A CA  
265  C C   . TYR A 42  ? 0.2151 0.2633 0.7282 0.0409  -0.0155 0.0365  952  TYR A C   
266  O O   . TYR A 42  ? 0.2189 0.2600 0.7285 0.0398  -0.0277 0.0354  952  TYR A O   
267  C CB  . TYR A 42  ? 0.2108 0.2721 0.7593 0.0378  -0.0095 0.0425  952  TYR A CB  
268  C CG  . TYR A 42  ? 0.2927 0.3570 0.8258 0.0366  0.0004  0.0459  952  TYR A CG  
269  C CD1 . TYR A 42  ? 0.2094 0.2660 0.7166 0.0365  -0.0019 0.0451  952  TYR A CD1 
270  C CD2 . TYR A 42  ? 0.2226 0.2997 0.7667 0.0354  0.0120  0.0506  952  TYR A CD2 
271  C CE1 . TYR A 42  ? 0.2073 0.2690 0.7015 0.0358  0.0069  0.0494  952  TYR A CE1 
272  C CE2 . TYR A 42  ? 0.2245 0.3070 0.7546 0.0340  0.0206  0.0555  952  TYR A CE2 
273  C CZ  . TYR A 42  ? 0.2043 0.2791 0.7099 0.0346  0.0179  0.0552  952  TYR A CZ  
274  O OH  . TYR A 42  ? 0.2027 0.2851 0.6958 0.0337  0.0261  0.0614  952  TYR A OH  
275  N N   . ILE A 43  ? 0.2144 0.2632 0.7068 0.0407  -0.0071 0.0356  953  ILE A N   
276  C CA  . ILE A 43  ? 0.2166 0.2572 0.6803 0.0396  -0.0115 0.0339  953  ILE A CA  
277  C C   . ILE A 43  ? 0.2132 0.2601 0.6599 0.0378  -0.0019 0.0364  953  ILE A C   
278  O O   . ILE A 43  ? 0.2108 0.2681 0.6596 0.0371  0.0101  0.0379  953  ILE A O   
279  C CB  . ILE A 43  ? 0.2215 0.2560 0.6741 0.0407  -0.0125 0.0303  953  ILE A CB  
280  C CG1 . ILE A 43  ? 0.2219 0.2631 0.6820 0.0417  0.0008  0.0283  953  ILE A CG1 
281  C CG2 . ILE A 43  ? 0.2263 0.2531 0.6887 0.0422  -0.0260 0.0300  953  ILE A CG2 
282  C CD1 . ILE A 43  ? 0.2290 0.2622 0.6754 0.0419  0.0022  0.0240  953  ILE A CD1 
283  N N   . SER A 44  ? 0.2137 0.2559 0.6435 0.0368  -0.0070 0.0370  954  SER A N   
284  C CA  . SER A 44  ? 0.2516 0.3011 0.6658 0.0359  0.0016  0.0408  954  SER A CA  
285  C C   . SER A 44  ? 0.2790 0.3321 0.6689 0.0343  0.0072  0.0389  954  SER A C   
286  O O   . SER A 44  ? 0.3184 0.3834 0.6997 0.0327  0.0175  0.0428  954  SER A O   
287  C CB  . SER A 44  ? 0.2172 0.2612 0.6228 0.0362  -0.0045 0.0417  954  SER A CB  
288  O OG  . SER A 44  ? 0.2311 0.2649 0.6263 0.0355  -0.0164 0.0360  954  SER A OG  
289  N N   . GLU A 45  ? 0.1852 0.3463 0.6956 0.0382  -0.0297 -0.0176 955  GLU A N   
290  C CA  . GLU A 45  ? 0.1847 0.3347 0.6853 0.0437  -0.0193 -0.0208 955  GLU A CA  
291  C C   . GLU A 45  ? 0.1867 0.3428 0.6892 0.0479  -0.0068 -0.0107 955  GLU A C   
292  O O   . GLU A 45  ? 0.1879 0.3598 0.6962 0.0490  -0.0071 -0.0014 955  GLU A O   
293  C CB  . GLU A 45  ? 0.1844 0.3324 0.6746 0.0471  -0.0228 -0.0274 955  GLU A CB  
294  C CG  . GLU A 45  ? 0.2870 0.4263 0.7731 0.0465  -0.0326 -0.0385 955  GLU A CG  
295  C CD  . GLU A 45  ? 0.2964 0.4395 0.7753 0.0502  -0.0378 -0.0438 955  GLU A CD  
296  O OE1 . GLU A 45  ? 0.3053 0.4592 0.7840 0.0516  -0.0354 -0.0386 955  GLU A OE1 
297  O OE2 . GLU A 45  ? 0.2755 0.4116 0.7497 0.0525  -0.0443 -0.0529 955  GLU A OE2 
298  N N   . ASN A 46  ? 0.1886 0.3321 0.6867 0.0505  0.0040  -0.0124 956  ASN A N   
299  C CA  . ASN A 46  ? 0.1940 0.3384 0.6934 0.0562  0.0170  -0.0040 956  ASN A CA  
300  C C   . ASN A 46  ? 0.1955 0.3504 0.6927 0.0609  0.0167  0.0018  956  ASN A C   
301  O O   . ASN A 46  ? 0.1923 0.3481 0.6835 0.0601  0.0100  -0.0034 956  ASN A O   
302  C CB  . ASN A 46  ? 0.1977 0.3239 0.6914 0.0573  0.0277  -0.0088 956  ASN A CB  
303  C CG  . ASN A 46  ? 0.2405 0.3567 0.7375 0.0524  0.0291  -0.0139 956  ASN A CG  
304  O OD1 . ASN A 46  ? 0.1957 0.3183 0.7011 0.0499  0.0268  -0.0109 956  ASN A OD1 
305  N ND2 . ASN A 46  ? 0.2349 0.3375 0.7271 0.0501  0.0325  -0.0216 956  ASN A ND2 
306  N N   . CYS A 47  ? 0.2016 0.3650 0.7042 0.0666  0.0246  0.0128  957  CYS A N   
307  C CA  . CYS A 47  ? 0.2045 0.3800 0.7077 0.0718  0.0249  0.0206  957  CYS A CA  
308  C C   . CYS A 47  ? 0.2152 0.3799 0.7159 0.0803  0.0393  0.0258  957  CYS A C   
309  O O   . CYS A 47  ? 0.2828 0.4334 0.7825 0.0822  0.0497  0.0250  957  CYS A O   
310  C CB  . CYS A 47  ? 0.2044 0.4039 0.7183 0.0713  0.0195  0.0311  957  CYS A CB  
311  S SG  . CYS A 47  ? 0.2137 0.4215 0.7370 0.0779  0.0316  0.0434  957  CYS A SG  
312  N N   . GLU A 48  ? 0.2191 0.3895 0.7192 0.0855  0.0404  0.0315  958  GLU A N   
313  C CA  . GLU A 48  ? 0.2541 0.4125 0.7518 0.0946  0.0540  0.0374  958  GLU A CA  
314  C C   . GLU A 48  ? 0.2399 0.4161 0.7448 0.1025  0.0552  0.0511  958  GLU A C   
315  O O   . GLU A 48  ? 0.2333 0.4280 0.7422 0.1000  0.0449  0.0540  958  GLU A O   
316  C CB  . GLU A 48  ? 0.2332 0.3776 0.7236 0.0940  0.0556  0.0313  958  GLU A CB  
317  C CG  . GLU A 48  ? 0.2247 0.3577 0.7095 0.0856  0.0519  0.0181  958  GLU A CG  
318  C CD  . GLU A 48  ? 0.2889 0.4155 0.7695 0.0842  0.0521  0.0129  958  GLU A CD  
319  O OE1 . GLU A 48  ? 0.2888 0.4081 0.7695 0.0903  0.0609  0.0189  958  GLU A OE1 
320  O OE2 . GLU A 48  ? 0.3449 0.4744 0.8225 0.0773  0.0437  0.0032  958  GLU A OE2 
321  N N   . THR A 49  ? 0.2551 0.4260 0.7614 0.1122  0.0681  0.0596  959  THR A N   
322  C CA  . THR A 49  ? 0.2650 0.4524 0.7783 0.1215  0.0705  0.0736  959  THR A CA  
323  C C   . THR A 49  ? 0.2822 0.4520 0.7895 0.1319  0.0817  0.0787  959  THR A C   
324  O O   . THR A 49  ? 0.2943 0.4745 0.8068 0.1416  0.0856  0.0911  959  THR A O   
325  C CB  . THR A 49  ? 0.2724 0.4729 0.7937 0.1267  0.0761  0.0824  959  THR A CB  
326  O OG1 . THR A 49  ? 0.2813 0.4593 0.7962 0.1292  0.0885  0.0776  959  THR A OG1 
327  C CG2 . THR A 49  ? 0.2573 0.4838 0.7881 0.1168  0.0628  0.0824  959  THR A CG2 
328  N N   . SER A 50  ? 0.2852 0.4287 0.7822 0.1300  0.0872  0.0699  960  SER A N   
329  C CA  . SER A 50  ? 0.3017 0.4262 0.7921 0.1378  0.0965  0.0739  960  SER A CA  
330  C C   . SER A 50  ? 0.3070 0.4140 0.7904 0.1291  0.0950  0.0615  960  SER A C   
331  O O   . SER A 50  ? 0.3615 0.4725 0.8453 0.1186  0.0869  0.0509  960  SER A O   
332  C CB  . SER A 50  ? 0.3297 0.4321 0.8121 0.1505  0.1148  0.0808  960  SER A CB  
333  O OG  . SER A 50  ? 0.3331 0.4209 0.8098 0.1479  0.1223  0.0740  960  SER A OG  
334  N N   . THR A 51  ? 0.3078 0.3959 0.7851 0.1336  0.1027  0.0634  961  THR A N   
335  C CA  . THR A 51  ? 0.3309 0.4070 0.8048 0.1253  0.1010  0.0530  961  THR A CA  
336  C C   . THR A 51  ? 0.3083 0.3572 0.7720 0.1210  0.1112  0.0433  961  THR A C   
337  O O   . THR A 51  ? 0.3763 0.3948 0.8269 0.1278  0.1273  0.0463  961  THR A O   
338  C CB  . THR A 51  ? 0.3155 0.3784 0.7866 0.1315  0.1073  0.0593  961  THR A CB  
339  O OG1 . THR A 51  ? 0.3524 0.4408 0.8333 0.1361  0.0987  0.0699  961  THR A OG1 
340  C CG2 . THR A 51  ? 0.3366 0.3951 0.8091 0.1223  0.1040  0.0495  961  THR A CG2 
341  N N   . MET A 52  ? 0.3325 0.3901 0.7998 0.1096  0.1021  0.0319  962  MET A N   
342  C CA  . MET A 52  ? 0.2940 0.3285 0.7536 0.1040  0.1104  0.0224  962  MET A CA  
343  C C   . MET A 52  ? 0.3226 0.3426 0.7670 0.0926  0.1096  0.0137  962  MET A C   
344  O O   . MET A 52  ? 0.3342 0.3284 0.7570 0.0836  0.1163  0.0072  962  MET A O   
345  C CB  . MET A 52  ? 0.2752 0.3256 0.7403 0.0962  0.1003  0.0157  962  MET A CB  
346  C CG  . MET A 52  ? 0.3145 0.3812 0.7844 0.1005  0.0966  0.0231  962  MET A CG  
347  S SD  . MET A 52  ? 0.3910 0.4365 0.8532 0.1104  0.1156  0.0304  962  MET A SD  
348  C CE  . MET A 52  ? 0.3416 0.3943 0.8050 0.1239  0.1192  0.0450  962  MET A CE  
349  N N   . ASN A 53  ? 0.2887 0.3252 0.7353 0.0888  0.0995  0.0135  963  ASN A N   
350  C CA  . ASN A 53  ? 0.3085 0.3354 0.7330 0.0747  0.0964  0.0066  963  ASN A CA  
351  C C   . ASN A 53  ? 0.3328 0.3599 0.7501 0.0619  0.0918  -0.0045 963  ASN A C   
352  O O   . ASN A 53  ? 0.3376 0.3418 0.7300 0.0502  0.0972  -0.0085 963  ASN A O   
353  C CB  . ASN A 53  ? 0.3326 0.3215 0.7285 0.0733  0.1100  0.0110  963  ASN A CB  
354  C CG  . ASN A 53  ? 0.3772 0.3639 0.7538 0.0595  0.1049  0.0079  963  ASN A CG  
355  O OD1 . ASN A 53  ? 0.3184 0.3357 0.7080 0.0572  0.0926  0.0066  963  ASN A OD1 
356  N ND2 . ASN A 53  ? 0.3726 0.3229 0.7162 0.0492  0.1145  0.0067  963  ASN A ND2 
357  N N   . ILE A 54  ? 0.2852 0.3380 0.7232 0.0634  0.0814  -0.0086 964  ILE A N   
358  C CA  . ILE A 54  ? 0.2607 0.3177 0.6944 0.0530  0.0752  -0.0181 964  ILE A CA  
359  C C   . ILE A 54  ? 0.2490 0.3184 0.6734 0.0428  0.0672  -0.0230 964  ILE A C   
360  O O   . ILE A 54  ? 0.2358 0.3278 0.6707 0.0460  0.0589  -0.0225 964  ILE A O   
361  C CB  . ILE A 54  ? 0.2554 0.3342 0.7116 0.0581  0.0656  -0.0206 964  ILE A CB  
362  C CG1 . ILE A 54  ? 0.2552 0.3259 0.7213 0.0671  0.0737  -0.0145 964  ILE A CG1 
363  C CG2 . ILE A 54  ? 0.2557 0.3386 0.7073 0.0486  0.0584  -0.0297 964  ILE A CG2 
364  C CD1 . ILE A 54  ? 0.2346 0.3212 0.7081 0.0669  0.0625  -0.0154 964  ILE A CD1 
365  N N   . ASP A 55  ? 0.2987 0.3543 0.7022 0.0296  0.0700  -0.0271 965  ASP A N   
366  C CA  . ASP A 55  ? 0.2586 0.3304 0.6535 0.0186  0.0626  -0.0310 965  ASP A CA  
367  C C   . ASP A 55  ? 0.2545 0.3588 0.6689 0.0223  0.0494  -0.0367 965  ASP A C   
368  O O   . ASP A 55  ? 0.2259 0.3323 0.6425 0.0196  0.0462  -0.0410 965  ASP A O   
369  C CB  . ASP A 55  ? 0.2796 0.3314 0.6481 0.0021  0.0680  -0.0329 965  ASP A CB  
370  C CG  . ASP A 55  ? 0.3504 0.4243 0.7103 -0.0110 0.0602  -0.0354 965  ASP A CG  
371  O OD1 . ASP A 55  ? 0.3179 0.4158 0.6872 -0.0073 0.0536  -0.0350 965  ASP A OD1 
372  O OD2 . ASP A 55  ? 0.2873 0.3557 0.6306 -0.0255 0.0608  -0.0372 965  ASP A OD2 
373  N N   . ARG A 56  ? 0.2180 0.3457 0.6450 0.0287  0.0419  -0.0367 966  ARG A N   
374  C CA  . ARG A 56  ? 0.1980 0.3532 0.6392 0.0331  0.0303  -0.0425 966  ARG A CA  
375  C C   . ARG A 56  ? 0.2412 0.4186 0.6765 0.0271  0.0252  -0.0452 966  ARG A C   
376  O O   . ARG A 56  ? 0.1837 0.3849 0.6298 0.0333  0.0167  -0.0495 966  ARG A O   
377  C CB  . ARG A 56  ? 0.2064 0.3721 0.6656 0.0450  0.0252  -0.0412 966  ARG A CB  
378  C CG  . ARG A 56  ? 0.2745 0.4251 0.7421 0.0509  0.0295  -0.0373 966  ARG A CG  
379  C CD  . ARG A 56  ? 0.3256 0.4810 0.7936 0.0574  0.0251  -0.0316 966  ARG A CD  
380  N NE  . ARG A 56  ? 0.3715 0.5145 0.8400 0.0610  0.0284  -0.0260 966  ARG A NE  
381  C CZ  . ARG A 56  ? 0.3953 0.5352 0.8606 0.0600  0.0235  -0.0286 966  ARG A CZ  
382  N NH1 . ARG A 56  ? 0.3425 0.4869 0.8032 0.0568  0.0158  -0.0364 966  ARG A NH1 
383  N NH2 . ARG A 56  ? 0.3765 0.5099 0.8442 0.0626  0.0266  -0.0225 966  ARG A NH2 
384  N N   . ASN A 57  ? 0.2107 0.3806 0.6276 0.0149  0.0305  -0.0425 967  ASN A N   
385  C CA  . ASN A 57  ? 0.2498 0.4442 0.6604 0.0071  0.0260  -0.0440 967  ASN A CA  
386  C C   . ASN A 57  ? 0.1980 0.4146 0.6150 0.0071  0.0190  -0.0491 967  ASN A C   
387  O O   . ASN A 57  ? 0.2044 0.4121 0.6134 -0.0009 0.0208  -0.0492 967  ASN A O   
388  C CB  . ASN A 57  ? 0.2322 0.4105 0.6180 -0.0094 0.0330  -0.0394 967  ASN A CB  
389  C CG  . ASN A 57  ? 0.2324 0.4382 0.6114 -0.0187 0.0286  -0.0390 967  ASN A CG  
390  O OD1 . ASN A 57  ? 0.2179 0.4566 0.6087 -0.0148 0.0212  -0.0428 967  ASN A OD1 
391  N ND2 . ASN A 57  ? 0.2736 0.4654 0.6325 -0.0305 0.0336  -0.0340 967  ASN A ND2 
392  N N   . ILE A 58  ? 0.1922 0.4366 0.6225 0.0168  0.0113  -0.0531 968  ILE A N   
393  C CA  . ILE A 58  ? 0.1790 0.4448 0.6155 0.0200  0.0051  -0.0573 968  ILE A CA  
394  C C   . ILE A 58  ? 0.2038 0.4820 0.6275 0.0051  0.0062  -0.0544 968  ILE A C   
395  O O   . ILE A 58  ? 0.1863 0.4697 0.6109 0.0032  0.0036  -0.0550 968  ILE A O   
396  C CB  . ILE A 58  ? 0.1774 0.4698 0.6257 0.0330  -0.0015 -0.0619 968  ILE A CB  
397  C CG1 . ILE A 58  ? 0.1644 0.4626 0.6077 0.0410  -0.0071 -0.0641 968  ILE A CG1 
398  C CG2 . ILE A 58  ? 0.1655 0.4834 0.6083 0.0275  -0.0014 -0.0604 968  ILE A CG2 
399  C CD1 . ILE A 58  ? 0.1683 0.4678 0.6026 0.0546  -0.0118 -0.0661 968  ILE A CD1 
400  N N   . THR A 59  ? 0.1936 0.4750 0.6037 -0.0075 0.0097  -0.0503 969  THR A N   
401  C CA  . THR A 59  ? 0.2031 0.4988 0.5995 -0.0243 0.0098  -0.0466 969  THR A CA  
402  C C   . THR A 59  ? 0.2307 0.4965 0.6113 -0.0378 0.0148  -0.0441 969  THR A C   
403  O O   . THR A 59  ? 0.2279 0.5045 0.5961 -0.0536 0.0139  -0.0407 969  THR A O   
404  C CB  . THR A 59  ? 0.2319 0.5388 0.6143 -0.0375 0.0117  -0.0424 969  THR A CB  
405  O OG1 . THR A 59  ? 0.2318 0.5006 0.5974 -0.0453 0.0191  -0.0392 969  THR A OG1 
406  C CG2 . THR A 59  ? 0.2003 0.5378 0.5961 -0.0257 0.0074  -0.0449 969  THR A CG2 
407  N N   . HIS A 60  ? 0.2232 0.4532 0.6031 -0.0327 0.0201  -0.0451 970  HIS A N   
408  C CA  . HIS A 60  ? 0.2396 0.4403 0.6036 -0.0446 0.0256  -0.0436 970  HIS A CA  
409  C C   . HIS A 60  ? 0.2591 0.4631 0.6357 -0.0377 0.0212  -0.0467 970  HIS A C   
410  O O   . HIS A 60  ? 0.2710 0.4547 0.6348 -0.0484 0.0248  -0.0456 970  HIS A O   
411  C CB  . HIS A 60  ? 0.2928 0.4512 0.6458 -0.0437 0.0358  -0.0421 970  HIS A CB  
412  C CG  . HIS A 60  ? 0.2722 0.4205 0.6091 -0.0509 0.0407  -0.0381 970  HIS A CG  
413  N ND1 . HIS A 60  ? 0.3178 0.4310 0.6455 -0.0470 0.0499  -0.0354 970  HIS A ND1 
414  C CD2 . HIS A 60  ? 0.2764 0.4454 0.6043 -0.0613 0.0377  -0.0357 970  HIS A CD2 
415  C CE1 . HIS A 60  ? 0.3142 0.4241 0.6268 -0.0548 0.0520  -0.0317 970  HIS A CE1 
416  N NE2 . HIS A 60  ? 0.3406 0.4843 0.6529 -0.0645 0.0445  -0.0320 970  HIS A NE2 
417  N N   . LEU A 61  ? 0.2586 0.4856 0.6573 -0.0210 0.0136  -0.0504 971  LEU A N   
418  C CA  . LEU A 61  ? 0.2303 0.4605 0.6393 -0.0144 0.0084  -0.0529 971  LEU A CA  
419  C C   . LEU A 61  ? 0.2240 0.4745 0.6262 -0.0265 0.0046  -0.0498 971  LEU A C   
420  O O   . LEU A 61  ? 0.2204 0.5037 0.6241 -0.0288 0.0007  -0.0477 971  LEU A O   
421  C CB  . LEU A 61  ? 0.1823 0.4304 0.6117 0.0056  0.0010  -0.0576 971  LEU A CB  
422  C CG  . LEU A 61  ? 0.1774 0.4069 0.6154 0.0172  0.0027  -0.0601 971  LEU A CG  
423  C CD1 . LEU A 61  ? 0.1807 0.4230 0.6338 0.0339  -0.0055 -0.0651 971  LEU A CD1 
424  C CD2 . LEU A 61  ? 0.1853 0.3818 0.6182 0.0128  0.0088  -0.0587 971  LEU A CD2 
425  N N   . GLN A 62  ? 0.2408 0.4739 0.6356 -0.0349 0.0057  -0.0488 972  GLN A N   
426  C CA  . GLN A 62  ? 0.2425 0.4979 0.6361 -0.0427 -0.0004 -0.0455 972  GLN A CA  
427  C C   . GLN A 62  ? 0.2273 0.5011 0.6422 -0.0228 -0.0090 -0.0485 972  GLN A C   
428  O O   . GLN A 62  ? 0.2254 0.4778 0.6472 -0.0127 -0.0095 -0.0524 972  GLN A O   
429  C CB  . GLN A 62  ? 0.2384 0.4665 0.6139 -0.0602 0.0038  -0.0432 972  GLN A CB  
430  C CG  . GLN A 62  ? 0.2711 0.4846 0.6191 -0.0838 0.0111  -0.0391 972  GLN A CG  
431  C CD  . GLN A 62  ? 0.3121 0.5037 0.6388 -0.1039 0.0141  -0.0364 972  GLN A CD  
432  O OE1 . GLN A 62  ? 0.3935 0.6075 0.7134 -0.1186 0.0087  -0.0311 972  GLN A OE1 
433  N NE2 . GLN A 62  ? 0.3517 0.5008 0.6671 -0.1052 0.0232  -0.0394 972  GLN A NE2 
434  N N   . HIS A 63  ? 0.1896 0.5022 0.6135 -0.0169 -0.0154 -0.0464 973  HIS A N   
435  C CA  . HIS A 63  ? 0.2022 0.5313 0.6437 0.0046  -0.0227 -0.0495 973  HIS A CA  
436  C C   . HIS A 63  ? 0.2479 0.6092 0.6932 0.0034  -0.0291 -0.0434 973  HIS A C   
437  O O   . HIS A 63  ? 0.3145 0.6928 0.7502 -0.0149 -0.0286 -0.0365 973  HIS A O   
438  C CB  . HIS A 63  ? 0.1699 0.5161 0.6210 0.0200  -0.0230 -0.0535 973  HIS A CB  
439  C CG  . HIS A 63  ? 0.2344 0.6168 0.6833 0.0130  -0.0224 -0.0490 973  HIS A CG  
440  N ND1 . HIS A 63  ? 0.2642 0.6432 0.7032 0.0010  -0.0169 -0.0480 973  HIS A ND1 
441  C CD2 . HIS A 63  ? 0.1970 0.6215 0.6520 0.0159  -0.0266 -0.0443 973  HIS A CD2 
442  C CE1 . HIS A 63  ? 0.2175 0.6344 0.6557 -0.0047 -0.0181 -0.0434 973  HIS A CE1 
443  N NE2 . HIS A 63  ? 0.2097 0.6568 0.6587 0.0045  -0.0237 -0.0408 973  HIS A NE2 
444  N N   . CYS A 64  ? 0.2616 0.6314 0.7197 0.0229  -0.0353 -0.0454 974  CYS A N   
445  C CA  . CYS A 64  ? 0.2202 0.6197 0.6839 0.0259  -0.0418 -0.0388 974  CYS A CA  
446  C C   . CYS A 64  ? 0.1771 0.6085 0.6443 0.0449  -0.0436 -0.0359 974  CYS A C   
447  O O   . CYS A 64  ? 0.1794 0.6000 0.6403 0.0577  -0.0403 -0.0397 974  CYS A O   
448  C CB  . CYS A 64  ? 0.1802 0.5568 0.6460 0.0330  -0.0468 -0.0398 974  CYS A CB  
449  S SG  . CYS A 64  ? 0.1840 0.5410 0.6506 0.0619  -0.0498 -0.0464 974  CYS A SG  
450  N N   . THR A 65  ? 0.2109 0.6769 0.6826 0.0454  -0.0478 -0.0263 975  THR A N   
451  C CA  . THR A 65  ? 0.1880 0.6788 0.6605 0.0611  -0.0476 -0.0194 975  THR A CA  
452  C C   . THR A 65  ? 0.1979 0.6870 0.6741 0.0822  -0.0519 -0.0159 975  THR A C   
453  O O   . THR A 65  ? 0.2993 0.8081 0.7794 0.0945  -0.0520 -0.0109 975  THR A O   
454  C CB  . THR A 65  ? 0.1907 0.7187 0.6636 0.0446  -0.0481 -0.0114 975  THR A CB  
455  O OG1 . THR A 65  ? 0.1950 0.7402 0.6708 0.0372  -0.0539 -0.0038 975  THR A OG1 
456  C CG2 . THR A 65  ? 0.1843 0.7108 0.6495 0.0198  -0.0441 -0.0138 975  THR A CG2 
457  N N   . CYS A 66  ? 0.2633 0.7257 0.7377 0.0864  -0.0553 -0.0206 976  CYS A N   
458  C CA  . CYS A 66  ? 0.2430 0.7002 0.7186 0.1061  -0.0597 -0.0177 976  CYS A CA  
459  C C   . CYS A 66  ? 0.3146 0.7577 0.7826 0.1289  -0.0555 -0.0212 976  CYS A C   
460  O O   . CYS A 66  ? 0.2379 0.6635 0.6973 0.1295  -0.0507 -0.0290 976  CYS A O   
461  C CB  . CYS A 66  ? 0.3155 0.7377 0.7894 0.1037  -0.0645 -0.0247 976  CYS A CB  
462  S SG  . CYS A 66  ? 0.1960 0.6149 0.6773 0.0729  -0.0660 -0.0260 976  CYS A SG  
463  N N   . VAL A 67  ? 0.5096 0.9593 0.9808 0.1472  -0.0577 -0.0156 977  VAL A N   
464  C CA  . VAL A 67  ? 0.5448 0.9778 1.0079 0.1698  -0.0539 -0.0197 977  VAL A CA  
465  C C   . VAL A 67  ? 0.5747 0.9774 1.0306 0.1844  -0.0585 -0.0225 977  VAL A C   
466  O O   . VAL A 67  ? 0.6308 1.0024 1.0736 0.1986  -0.0565 -0.0306 977  VAL A O   
467  C CB  . VAL A 67  ? 0.5041 0.9693 0.9766 0.1795  -0.0513 -0.0133 977  VAL A CB  
468  C CG1 . VAL A 67  ? 0.4934 0.9402 0.9571 0.2040  -0.0472 -0.0184 977  VAL A CG1 
469  C CG2 . VAL A 67  ? 0.4990 0.9881 0.9741 0.1647  -0.0473 -0.0138 977  VAL A CG2 
470  N N   . ASP A 68  ? 0.4591 0.8685 0.9222 0.1795  -0.0654 -0.0164 978  ASP A N   
471  C CA  . ASP A 68  ? 0.4637 0.8401 0.9190 0.1907  -0.0712 -0.0201 978  ASP A CA  
472  C C   . ASP A 68  ? 0.4135 0.7480 0.8594 0.1797  -0.0731 -0.0333 978  ASP A C   
473  O O   . ASP A 68  ? 0.4302 0.7558 0.8710 0.1730  -0.0679 -0.0403 978  ASP A O   
474  C CB  . ASP A 68  ? 0.4001 0.7962 0.8669 0.1879  -0.0792 -0.0095 978  ASP A CB  
475  C CG  . ASP A 68  ? 0.4358 0.8472 0.9119 0.1611  -0.0832 -0.0087 978  ASP A CG  
476  O OD1 . ASP A 68  ? 0.4291 0.8391 0.9042 0.1455  -0.0785 -0.0148 978  ASP A OD1 
477  O OD2 . ASP A 68  ? 0.4158 0.8395 0.9005 0.1548  -0.0910 -0.0018 978  ASP A OD2 
478  N N   . ASP A 69  ? 0.3941 0.7022 0.8395 0.1770  -0.0807 -0.0358 979  ASP A N   
479  C CA  . ASP A 69  ? 0.3744 0.6419 0.8146 0.1659  -0.0826 -0.0464 979  ASP A CA  
480  C C   . ASP A 69  ? 0.3338 0.6070 0.7865 0.1412  -0.0834 -0.0461 979  ASP A C   
481  O O   . ASP A 69  ? 0.3292 0.5721 0.7826 0.1313  -0.0860 -0.0516 979  ASP A O   
482  C CB  . ASP A 69  ? 0.3791 0.6098 0.8114 0.1758  -0.0903 -0.0492 979  ASP A CB  
483  C CG  . ASP A 69  ? 0.3759 0.6169 0.8182 0.1743  -0.0985 -0.0407 979  ASP A CG  
484  O OD1 . ASP A 69  ? 0.4190 0.7004 0.8709 0.1758  -0.0979 -0.0307 979  ASP A OD1 
485  O OD2 . ASP A 69  ? 0.4127 0.6233 0.8539 0.1705  -0.1062 -0.0430 979  ASP A OD2 
486  N N   . CYS A 70  ? 0.3424 0.6539 0.8050 0.1306  -0.0808 -0.0393 980  CYS A N   
487  C CA  . CYS A 70  ? 0.2720 0.5900 0.7455 0.1059  -0.0808 -0.0382 980  CYS A CA  
488  C C   . CYS A 70  ? 0.2939 0.5925 0.7675 0.0960  -0.0874 -0.0352 980  CYS A C   
489  O O   . CYS A 70  ? 0.3559 0.6269 0.8219 0.0785  -0.0848 -0.0382 980  CYS A O   
490  C CB  . CYS A 70  ? 0.3184 0.6150 0.7880 0.0950  -0.0738 -0.0465 980  CYS A CB  
491  S SG  . CYS A 70  ? 0.2117 0.5231 0.6725 0.1009  -0.0650 -0.0489 980  CYS A SG  
492  N N   . SER A 71  ? 0.3294 0.6405 0.8058 0.1065  -0.0948 -0.0276 981  SER A N   
493  C CA  . SER A 71  ? 0.3136 0.6082 0.7838 0.0945  -0.1008 -0.0220 981  SER A CA  
494  C C   . SER A 71  ? 0.3040 0.6331 0.7768 0.0779  -0.1028 -0.0096 981  SER A C   
495  O O   . SER A 71  ? 0.3327 0.6515 0.7998 0.0659  -0.1079 -0.0038 981  SER A O   
496  C CB  . SER A 71  ? 0.3090 0.5850 0.7769 0.1159  -0.1091 -0.0216 981  SER A CB  
497  O OG  . SER A 71  ? 0.3396 0.6318 0.8135 0.1435  -0.1093 -0.0227 981  SER A OG  
498  N N   . SER A 72  ? 0.3278 0.6979 0.8078 0.0752  -0.0993 -0.0048 982  SER A N   
499  C CA  . SER A 72  ? 0.2609 0.6671 0.7419 0.0569  -0.1017 0.0080  982  SER A CA  
500  C C   . SER A 72  ? 0.3279 0.7219 0.7961 0.0250  -0.0952 0.0064  982  SER A C   
501  O O   . SER A 72  ? 0.2760 0.6377 0.7372 0.0200  -0.0881 -0.0041 982  SER A O   
502  C CB  . SER A 72  ? 0.2310 0.6913 0.7252 0.0689  -0.1016 0.0156  982  SER A CB  
503  O OG  . SER A 72  ? 0.2205 0.6928 0.7118 0.0539  -0.0939 0.0124  982  SER A OG  
504  N N   . SER A 73  ? 0.3332 0.7541 0.7970 0.0033  -0.0972 0.0175  983  SER A N   
505  C CA  . SER A 73  ? 0.3575 0.7643 0.8042 -0.0282 -0.0907 0.0166  983  SER A CA  
506  C C   . SER A 73  ? 0.3308 0.7604 0.7761 -0.0363 -0.0840 0.0161  983  SER A C   
507  O O   . SER A 73  ? 0.3818 0.7945 0.8099 -0.0611 -0.0774 0.0144  983  SER A O   
508  C CB  . SER A 73  ? 0.3909 0.8094 0.8278 -0.0522 -0.0962 0.0285  983  SER A CB  
509  O OG  . SER A 73  ? 0.4018 0.8750 0.8496 -0.0496 -0.1029 0.0421  983  SER A OG  
510  N N   . ASN A 74  ? 0.2407 0.7060 0.7015 -0.0162 -0.0850 0.0176  984  ASN A N   
511  C CA  . ASN A 74  ? 0.2531 0.7388 0.7123 -0.0231 -0.0787 0.0165  984  ASN A CA  
512  C C   . ASN A 74  ? 0.2607 0.7159 0.7202 -0.0108 -0.0713 0.0028  984  ASN A C   
513  O O   . ASN A 74  ? 0.2398 0.7114 0.7001 -0.0114 -0.0666 0.0010  984  ASN A O   
514  C CB  . ASN A 74  ? 0.2289 0.7746 0.7042 -0.0102 -0.0829 0.0263  984  ASN A CB  
515  C CG  . ASN A 74  ? 0.2339 0.8103 0.7041 -0.0274 -0.0890 0.0409  984  ASN A CG  
516  O OD1 . ASN A 74  ? 0.2714 0.8324 0.7314 -0.0494 -0.0919 0.0450  984  ASN A OD1 
517  N ND2 . ASN A 74  ? 0.2872 0.8960 0.7571 -0.0184 -0.0897 0.0477  984  ASN A ND2 
518  N N   . CYS A 75  ? 0.2592 0.6719 0.7176 -0.0012 -0.0707 -0.0060 985  CYS A N   
519  C CA  . CYS A 75  ? 0.2507 0.6329 0.7080 0.0068  -0.0641 -0.0178 985  CYS A CA  
520  C C   . CYS A 75  ? 0.2532 0.6114 0.6936 -0.0184 -0.0558 -0.0198 985  CYS A C   
521  O O   . CYS A 75  ? 0.2605 0.5894 0.6890 -0.0333 -0.0542 -0.0200 985  CYS A O   
522  C CB  . CYS A 75  ? 0.2557 0.6026 0.7159 0.0226  -0.0669 -0.0249 985  CYS A CB  
523  S SG  . CYS A 75  ? 0.2068 0.5281 0.6699 0.0374  -0.0614 -0.0372 985  CYS A SG  
524  N N   . LEU A 76  ? 0.2839 0.6095 0.6300 0.0009  -0.0436 -0.0292 986  LEU A N   
525  C CA  . LEU A 76  ? 0.3617 0.6656 0.6861 -0.0181 -0.0431 -0.0401 986  LEU A CA  
526  C C   . LEU A 76  ? 0.3097 0.5738 0.6087 -0.0125 -0.0375 -0.0449 986  LEU A C   
527  O O   . LEU A 76  ? 0.3452 0.5916 0.6220 -0.0232 -0.0388 -0.0518 986  LEU A O   
528  C CB  . LEU A 76  ? 0.3617 0.6634 0.6935 -0.0295 -0.0342 -0.0450 986  LEU A CB  
529  C CG  . LEU A 76  ? 0.3493 0.6201 0.6558 -0.0475 -0.0315 -0.0559 986  LEU A CG  
530  C CD1 . LEU A 76  ? 0.3547 0.6433 0.6662 -0.0721 -0.0360 -0.0600 986  LEU A CD1 
531  C CD2 . LEU A 76  ? 0.3289 0.5649 0.6253 -0.0412 -0.0180 -0.0586 986  LEU A CD2 
532  N N   . CYS A 77  ? 0.2957 0.5463 0.5976 0.0037  -0.0309 -0.0412 987  CYS A N   
533  C CA  . CYS A 77  ? 0.3429 0.5627 0.6268 0.0084  -0.0260 -0.0441 987  CYS A CA  
534  C C   . CYS A 77  ? 0.3122 0.5305 0.5832 0.0104  -0.0319 -0.0413 987  CYS A C   
535  O O   . CYS A 77  ? 0.3737 0.5708 0.6280 0.0093  -0.0277 -0.0449 987  CYS A O   
536  C CB  . CYS A 77  ? 0.3193 0.5276 0.6091 0.0213  -0.0195 -0.0412 987  CYS A CB  
537  S SG  . CYS A 77  ? 0.3558 0.5718 0.6595 0.0214  -0.0125 -0.0418 987  CYS A SG  
538  N N   . GLY A 78  ? 0.3222 0.5638 0.6010 0.0144  -0.0408 -0.0335 988  GLY A N   
539  C CA  . GLY A 78  ? 0.3714 0.6127 0.6332 0.0136  -0.0475 -0.0300 988  GLY A CA  
540  C C   . GLY A 78  ? 0.3944 0.6376 0.6376 -0.0039 -0.0531 -0.0378 988  GLY A C   
541  O O   . GLY A 78  ? 0.4134 0.6406 0.6315 -0.0077 -0.0523 -0.0407 988  GLY A O   
542  N N   . GLN A 79  ? 0.3699 0.6313 0.6232 -0.0163 -0.0577 -0.0417 989  GLN A N   
543  C CA  . GLN A 79  ? 0.3523 0.6114 0.5847 -0.0369 -0.0632 -0.0511 989  GLN A CA  
544  C C   . GLN A 79  ? 0.3593 0.5775 0.5675 -0.0424 -0.0503 -0.0632 989  GLN A C   
545  O O   . GLN A 79  ? 0.3947 0.5954 0.5729 -0.0524 -0.0504 -0.0708 989  GLN A O   
546  C CB  . GLN A 79  ? 0.3018 0.5891 0.5536 -0.0513 -0.0697 -0.0525 989  GLN A CB  
547  C CG  . GLN A 79  ? 0.3762 0.7103 0.6568 -0.0440 -0.0821 -0.0390 989  GLN A CG  
548  C CD  . GLN A 79  ? 0.3176 0.6859 0.6197 -0.0609 -0.0889 -0.0397 989  GLN A CD  
549  O OE1 . GLN A 79  ? 0.4006 0.7641 0.6858 -0.0850 -0.0937 -0.0499 989  GLN A OE1 
550  N NE2 . GLN A 79  ? 0.4129 0.8151 0.7522 -0.0494 -0.0880 -0.0293 989  GLN A NE2 
551  N N   . LEU A 80  ? 0.3683 0.5701 0.5875 -0.0351 -0.0386 -0.0645 990  LEU A N   
552  C CA  . LEU A 80  ? 0.3649 0.5298 0.5656 -0.0355 -0.0257 -0.0727 990  LEU A CA  
553  C C   . LEU A 80  ? 0.4246 0.5742 0.6075 -0.0268 -0.0211 -0.0720 990  LEU A C   
554  O O   . LEU A 80  ? 0.4170 0.5391 0.5778 -0.0297 -0.0115 -0.0799 990  LEU A O   
555  C CB  . LEU A 80  ? 0.3531 0.5091 0.5706 -0.0256 -0.0167 -0.0700 990  LEU A CB  
556  C CG  . LEU A 80  ? 0.3741 0.5436 0.6077 -0.0340 -0.0179 -0.0700 990  LEU A CG  
557  C CD1 . LEU A 80  ? 0.3250 0.4926 0.5745 -0.0213 -0.0115 -0.0644 990  LEU A CD1 
558  C CD2 . LEU A 80  ? 0.2940 0.4420 0.5107 -0.0517 -0.0133 -0.0797 990  LEU A CD2 
559  N N   . SER A 81  ? 0.3965 0.5621 0.5884 -0.0159 -0.0262 -0.0621 991  SER A N   
560  C CA  . SER A 81  ? 0.4167 0.5710 0.5946 -0.0084 -0.0211 -0.0591 991  SER A CA  
561  C C   . SER A 81  ? 0.4742 0.6360 0.6292 -0.0153 -0.0296 -0.0579 991  SER A C   
562  O O   . SER A 81  ? 0.4704 0.6292 0.6158 -0.0084 -0.0274 -0.0515 991  SER A O   
563  C CB  . SER A 81  ? 0.4138 0.5749 0.6119 0.0060  -0.0201 -0.0485 991  SER A CB  
564  O OG  . SER A 81  ? 0.3700 0.5315 0.5891 0.0107  -0.0174 -0.0483 991  SER A OG  
565  N N   . ILE A 82  ? 0.4791 0.6516 0.6243 -0.0303 -0.0400 -0.0634 992  ILE A N   
566  C CA  . ILE A 82  ? 0.4900 0.6796 0.6168 -0.0386 -0.0542 -0.0601 992  ILE A CA  
567  C C   . ILE A 82  ? 0.4793 0.7026 0.6332 -0.0277 -0.0665 -0.0443 992  ILE A C   
568  O O   . ILE A 82  ? 0.4322 0.6860 0.5998 -0.0342 -0.0805 -0.0407 992  ILE A O   
569  C CB  . ILE A 82  ? 0.5603 0.7295 0.6512 -0.0380 -0.0482 -0.0612 992  ILE A CB  
570  C CG1 . ILE A 82  ? 0.5507 0.6854 0.6101 -0.0487 -0.0351 -0.0779 992  ILE A CG1 
571  C CG2 . ILE A 82  ? 0.4516 0.6422 0.5241 -0.0439 -0.0654 -0.0534 992  ILE A CG2 
572  C CD1 . ILE A 82  ? 0.5609 0.6713 0.6316 -0.0370 -0.0154 -0.0813 992  ILE A CD1 
573  N N   . ARG A 83  ? 0.5039 0.7215 0.6660 -0.0110 -0.0607 -0.0343 993  ARG A N   
574  C CA  . ARG A 83  ? 0.4992 0.7379 0.6877 0.0031  -0.0671 -0.0201 993  ARG A CA  
575  C C   . ARG A 83  ? 0.5073 0.7259 0.7077 0.0162  -0.0540 -0.0177 993  ARG A C   
576  O O   . ARG A 83  ? 0.5746 0.7701 0.7628 0.0149  -0.0427 -0.0235 993  ARG A O   
577  C CB  . ARG A 83  ? 0.5317 0.7854 0.7082 0.0076  -0.0792 -0.0065 993  ARG A CB  
578  C CG  . ARG A 83  ? 0.6173 0.8460 0.7697 0.0132  -0.0708 -0.0016 993  ARG A CG  
579  C CD  . ARG A 83  ? 0.6219 0.8624 0.7590 0.0185  -0.0825 0.0144  993  ARG A CD  
580  N NE  . ARG A 83  ? 0.6507 0.9029 0.8139 0.0362  -0.0863 0.0303  993  ARG A NE  
581  C CZ  . ARG A 83  ? 0.7199 0.9790 0.8752 0.0463  -0.0947 0.0480  993  ARG A CZ  
582  N NH1 . ARG A 83  ? 0.7805 1.0379 0.9010 0.0396  -0.1013 0.0530  993  ARG A NH1 
583  N NH2 . ARG A 83  ? 0.7084 0.9734 0.8885 0.0644  -0.0956 0.0616  993  ARG A NH2 
584  N N   . CYS A 84  ? 0.4413 0.6694 0.6656 0.0285  -0.0551 -0.0093 994  CYS A N   
585  C CA  . CYS A 84  ? 0.4162 0.6241 0.6460 0.0391  -0.0455 -0.0055 994  CYS A CA  
586  C C   . CYS A 84  ? 0.4442 0.6403 0.6549 0.0422  -0.0447 0.0035  994  CYS A C   
587  O O   . CYS A 84  ? 0.4390 0.6458 0.6453 0.0480  -0.0532 0.0152  994  CYS A O   
588  C CB  . CYS A 84  ? 0.4105 0.6259 0.6636 0.0516  -0.0459 0.0009  994  CYS A CB  
589  S SG  . CYS A 84  ? 0.3922 0.5777 0.6474 0.0605  -0.0349 0.0031  994  CYS A SG  
590  N N   . TRP A 85  ? 0.4477 0.6236 0.6479 0.0388  -0.0341 -0.0005 995  TRP A N   
591  C CA  . TRP A 85  ? 0.4375 0.6013 0.6187 0.0394  -0.0299 0.0077  995  TRP A CA  
592  C C   . TRP A 85  ? 0.4126 0.5624 0.6030 0.0475  -0.0252 0.0175  995  TRP A C   
593  O O   . TRP A 85  ? 0.4493 0.5871 0.6253 0.0472  -0.0204 0.0259  995  TRP A O   
594  C CB  . TRP A 85  ? 0.3942 0.5465 0.5612 0.0315  -0.0186 -0.0009 995  TRP A CB  
595  C CG  . TRP A 85  ? 0.4519 0.6089 0.6009 0.0225  -0.0217 -0.0111 995  TRP A CG  
596  C CD1 . TRP A 85  ? 0.4665 0.6229 0.6212 0.0171  -0.0198 -0.0236 995  TRP A CD1 
597  C CD2 . TRP A 85  ? 0.4751 0.6348 0.5937 0.0162  -0.0277 -0.0098 995  TRP A CD2 
598  N NE1 . TRP A 85  ? 0.4618 0.6176 0.5916 0.0066  -0.0233 -0.0314 995  TRP A NE1 
599  C CE2 . TRP A 85  ? 0.4863 0.6452 0.5926 0.0053  -0.0289 -0.0237 995  TRP A CE2 
600  C CE3 . TRP A 85  ? 0.5022 0.6626 0.5993 0.0179  -0.0322 0.0023  995  TRP A CE3 
601  C CZ2 . TRP A 85  ? 0.5369 0.6959 0.6092 -0.0056 -0.0354 -0.0278 995  TRP A CZ2 
602  C CZ3 . TRP A 85  ? 0.5095 0.6726 0.5729 0.0086  -0.0392 -0.0002 995  TRP A CZ3 
603  C CH2 . TRP A 85  ? 0.5070 0.6696 0.5576 -0.0039 -0.0412 -0.0161 995  TRP A CH2 
604  N N   . TYR A 86  ? 0.3272 0.4754 0.5378 0.0534  -0.0256 0.0164  996  TYR A N   
605  C CA  . TYR A 86  ? 0.3653 0.4942 0.5810 0.0591  -0.0208 0.0233  996  TYR A CA  
606  C C   . TYR A 86  ? 0.4082 0.5363 0.6212 0.0713  -0.0264 0.0370  996  TYR A C   
607  O O   . TYR A 86  ? 0.4668 0.6144 0.6893 0.0786  -0.0343 0.0386  996  TYR A O   
608  C CB  . TYR A 86  ? 0.3487 0.4722 0.5815 0.0597  -0.0178 0.0146  996  TYR A CB  
609  C CG  . TYR A 86  ? 0.2968 0.4223 0.5344 0.0501  -0.0135 0.0038  996  TYR A CG  
610  C CD1 . TYR A 86  ? 0.3651 0.4883 0.5959 0.0430  -0.0076 0.0041  996  TYR A CD1 
611  C CD2 . TYR A 86  ? 0.2941 0.4245 0.5431 0.0497  -0.0141 -0.0051 996  TYR A CD2 
612  C CE1 . TYR A 86  ? 0.2485 0.3758 0.4869 0.0376  -0.0030 -0.0036 996  TYR A CE1 
613  C CE2 . TYR A 86  ? 0.2890 0.4210 0.5422 0.0431  -0.0107 -0.0124 996  TYR A CE2 
614  C CZ  . TYR A 86  ? 0.2775 0.4087 0.5269 0.0381  -0.0054 -0.0112 996  TYR A CZ  
615  O OH  . TYR A 86  ? 0.2849 0.4200 0.5418 0.0349  -0.0015 -0.0163 996  TYR A OH  
616  N N   . ASP A 87  ? 0.4057 0.5121 0.6070 0.0739  -0.0220 0.0481  997  ASP A N   
617  C CA  . ASP A 87  ? 0.3987 0.4973 0.5981 0.0887  -0.0253 0.0629  997  ASP A CA  
618  C C   . ASP A 87  ? 0.4392 0.5156 0.6510 0.0962  -0.0188 0.0603  997  ASP A C   
619  O O   . ASP A 87  ? 0.4383 0.5067 0.6571 0.0876  -0.0135 0.0474  997  ASP A O   
620  C CB  . ASP A 87  ? 0.4208 0.5024 0.5974 0.0885  -0.0231 0.0780  997  ASP A CB  
621  C CG  . ASP A 87  ? 0.4302 0.4810 0.6009 0.0785  -0.0106 0.0774  997  ASP A CG  
622  O OD1 . ASP A 87  ? 0.4486 0.4866 0.6322 0.0745  -0.0053 0.0677  997  ASP A OD1 
623  O OD2 . ASP A 87  ? 0.4595 0.5001 0.6114 0.0732  -0.0062 0.0871  997  ASP A OD2 
624  N N   . LYS A 88  ? 0.4985 0.5634 0.7107 0.1131  -0.0189 0.0729  998  LYS A N   
625  C CA  . LYS A 88  ? 0.5155 0.5567 0.7361 0.1229  -0.0110 0.0694  998  LYS A CA  
626  C C   . LYS A 88  ? 0.5027 0.5066 0.7136 0.1095  -0.0012 0.0609  998  LYS A C   
627  O O   . LYS A 88  ? 0.4989 0.4845 0.7132 0.1109  0.0047  0.0514  998  LYS A O   
628  C CB  . LYS A 88  ? 0.5069 0.5350 0.7262 0.1455  -0.0100 0.0870  998  LYS A CB  
629  C CG  . LYS A 88  ? 0.5236 0.5283 0.7213 0.1458  -0.0092 0.1037  998  LYS A CG  
630  C CD  . LYS A 88  ? 0.6217 0.6221 0.8195 0.1710  -0.0113 0.1245  998  LYS A CD  
631  C CE  . LYS A 88  ? 0.5966 0.6508 0.8145 0.1828  -0.0252 0.1302  998  LYS A CE  
632  N NZ  . LYS A 88  ? 0.5131 0.5701 0.7316 0.2079  -0.0301 0.1552  998  LYS A NZ  
633  N N   . ASP A 89  ? 0.4724 0.4661 0.6708 0.0953  0.0007  0.0641  999  ASP A N   
634  C CA  . ASP A 89  ? 0.4963 0.4614 0.6891 0.0791  0.0084  0.0574  999  ASP A CA  
635  C C   . ASP A 89  ? 0.4516 0.4396 0.6539 0.0615  0.0067  0.0447  999  ASP A C   
636  O O   . ASP A 89  ? 0.4626 0.4405 0.6629 0.0457  0.0112  0.0436  999  ASP A O   
637  C CB  . ASP A 89  ? 0.5485 0.4858 0.7241 0.0745  0.0142  0.0716  999  ASP A CB  
638  C CG  . ASP A 89  ? 0.6088 0.5098 0.7729 0.0911  0.0187  0.0839  999  ASP A CG  
639  O OD1 . ASP A 89  ? 0.7034 0.6120 0.8756 0.1105  0.0160  0.0848  999  ASP A OD1 
640  O OD2 . ASP A 89  ? 0.6723 0.5367 0.8203 0.0853  0.0263  0.0934  999  ASP A OD2 
641  N N   . GLY A 90  ? 0.4005 0.4197 0.6146 0.0641  0.0009  0.0362  1000 GLY A N   
642  C CA  . GLY A 90  ? 0.4313 0.4699 0.6545 0.0510  0.0002  0.0256  1000 GLY A CA  
643  C C   . GLY A 90  ? 0.3972 0.4506 0.6167 0.0432  0.0022  0.0295  1000 GLY A C   
644  O O   . GLY A 90  ? 0.3534 0.4245 0.5817 0.0362  0.0028  0.0217  1000 GLY A O   
645  N N   . ARG A 91  ? 0.4118 0.4577 0.6170 0.0457  0.0042  0.0419  1001 ARG A N   
646  C CA  . ARG A 91  ? 0.3897 0.4455 0.5862 0.0383  0.0091  0.0460  1001 ARG A CA  
647  C C   . ARG A 91  ? 0.4195 0.4976 0.6077 0.0433  0.0036  0.0440  1001 ARG A C   
648  O O   . ARG A 91  ? 0.4290 0.5137 0.6140 0.0531  -0.0052 0.0469  1001 ARG A O   
649  C CB  . ARG A 91  ? 0.4350 0.4686 0.6146 0.0370  0.0148  0.0612  1001 ARG A CB  
650  C CG  . ARG A 91  ? 0.4408 0.4450 0.6243 0.0317  0.0191  0.0632  1001 ARG A CG  
651  C CD  . ARG A 91  ? 0.4548 0.4396 0.6264 0.0213  0.0290  0.0754  1001 ARG A CD  
652  N NE  . ARG A 91  ? 0.4692 0.4300 0.6479 0.0082  0.0335  0.0727  1001 ARG A NE  
653  C CZ  . ARG A 91  ? 0.5381 0.4620 0.7075 0.0119  0.0340  0.0758  1001 ARG A CZ  
654  N NH1 . ARG A 91  ? 0.5348 0.4447 0.6920 0.0315  0.0308  0.0837  1001 ARG A NH1 
655  N NH2 . ARG A 91  ? 0.4959 0.3965 0.6684 -0.0044 0.0378  0.0711  1001 ARG A NH2 
656  N N   . LEU A 92  ? 0.4333 0.5230 0.6179 0.0360  0.0096  0.0392  1002 LEU A N   
657  C CA  . LEU A 92  ? 0.4399 0.5438 0.6091 0.0372  0.0061  0.0358  1002 LEU A CA  
658  C C   . LEU A 92  ? 0.5103 0.6095 0.6542 0.0412  0.0019  0.0491  1002 LEU A C   
659  O O   . LEU A 92  ? 0.4898 0.5730 0.6239 0.0407  0.0076  0.0615  1002 LEU A O   
660  C CB  . LEU A 92  ? 0.4446 0.5543 0.6105 0.0302  0.0173  0.0286  1002 LEU A CB  
661  C CG  . LEU A 92  ? 0.4306 0.5484 0.6202 0.0283  0.0206  0.0171  1002 LEU A CG  
662  C CD1 . LEU A 92  ? 0.3631 0.4856 0.5502 0.0249  0.0346  0.0137  1002 LEU A CD1 
663  C CD2 . LEU A 92  ? 0.3958 0.5213 0.5890 0.0316  0.0108  0.0076  1002 LEU A CD2 
664  N N   . LEU A 93  ? 0.4923 0.6062 0.6248 0.0438  -0.0089 0.0474  1003 LEU A N   
665  C CA  . LEU A 93  ? 0.5869 0.7014 0.6929 0.0470  -0.0160 0.0605  1003 LEU A CA  
666  C C   . LEU A 93  ? 0.6460 0.7514 0.7232 0.0389  -0.0046 0.0627  1003 LEU A C   
667  O O   . LEU A 93  ? 0.6680 0.7735 0.7450 0.0317  0.0067  0.0510  1003 LEU A O   
668  C CB  . LEU A 93  ? 0.5973 0.7350 0.6986 0.0479  -0.0319 0.0568  1003 LEU A CB  
669  C CG  . LEU A 93  ? 0.5091 0.6621 0.6392 0.0568  -0.0425 0.0566  1003 LEU A CG  
670  C CD1 . LEU A 93  ? 0.6178 0.7988 0.7419 0.0556  -0.0595 0.0577  1003 LEU A CD1 
671  C CD2 . LEU A 93  ? 0.4777 0.6168 0.6182 0.0704  -0.0416 0.0716  1003 LEU A CD2 
672  N N   . GLN A 94  ? 0.6927 0.7893 0.7447 0.0418  -0.0066 0.0792  1004 GLN A N   
673  C CA  . GLN A 94  ? 0.7633 0.8498 0.7827 0.0345  0.0056  0.0834  1004 GLN A CA  
674  C C   . GLN A 94  ? 0.7624 0.8590 0.7581 0.0269  0.0050  0.0693  1004 GLN A C   
675  O O   . GLN A 94  ? 0.7925 0.8814 0.7721 0.0203  0.0218  0.0631  1004 GLN A O   
676  C CB  . GLN A 94  ? 0.8282 0.9038 0.8205 0.0399  0.0004  0.1054  1004 GLN A CB  
677  C CG  . GLN A 94  ? 0.9043 0.9634 0.8637 0.0329  0.0164  0.1145  1004 GLN A CG  
678  C CD  . GLN A 94  ? 1.0055 1.0481 0.9431 0.0399  0.0121  0.1394  1004 GLN A CD  
679  O OE1 . GLN A 94  ? 1.0937 1.1386 1.0417 0.0519  -0.0033 0.1496  1004 GLN A OE1 
680  N NE2 . GLN A 94  ? 1.0068 1.0322 0.9145 0.0337  0.0271  0.1505  1004 GLN A NE2 
681  N N   . GLU A 95  ? 0.7153 0.8287 0.7090 0.0273  -0.0129 0.0635  1005 GLU A N   
682  C CA  . GLU A 95  ? 0.7197 0.8385 0.6856 0.0173  -0.0158 0.0494  1005 GLU A CA  
683  C C   . GLU A 95  ? 0.6951 0.8120 0.6783 0.0125  -0.0051 0.0287  1005 GLU A C   
684  O O   . GLU A 95  ? 0.6880 0.8032 0.6481 0.0037  -0.0056 0.0147  1005 GLU A O   
685  C CB  . GLU A 95  ? 0.7521 0.8928 0.7119 0.0167  -0.0409 0.0523  1005 GLU A CB  
686  C CG  . GLU A 95  ? 0.6839 0.8433 0.6842 0.0192  -0.0510 0.0441  1005 GLU A CG  
687  C CD  . GLU A 95  ? 0.7924 0.9799 0.8008 0.0236  -0.0747 0.0551  1005 GLU A CD  
688  O OE1 . GLU A 95  ? 0.7836 0.9733 0.7934 0.0358  -0.0808 0.0752  1005 GLU A OE1 
689  O OE2 . GLU A 95  ? 0.7988 1.0067 0.8137 0.0151  -0.0867 0.0446  1005 GLU A OE2 
690  N N   . PHE A 96  ? 0.6879 0.8028 0.7083 0.0175  0.0043  0.0269  1006 PHE A N   
691  C CA  . PHE A 96  ? 0.6422 0.7567 0.6815 0.0154  0.0129  0.0104  1006 PHE A CA  
692  C C   . PHE A 96  ? 0.6696 0.7705 0.6841 0.0110  0.0322  0.0014  1006 PHE A C   
693  O O   . PHE A 96  ? 0.6925 0.7862 0.6993 0.0121  0.0473  0.0090  1006 PHE A O   
694  C CB  . PHE A 96  ? 0.5468 0.6630 0.6272 0.0212  0.0180  0.0130  1006 PHE A CB  
695  C CG  . PHE A 96  ? 0.5318 0.6489 0.6327 0.0210  0.0260  -0.0005 1006 PHE A CG  
696  C CD1 . PHE A 96  ? 0.5351 0.6588 0.6505 0.0209  0.0158  -0.0093 1006 PHE A CD1 
697  C CD2 . PHE A 96  ? 0.5745 0.6872 0.6816 0.0216  0.0444  -0.0027 1006 PHE A CD2 
698  C CE1 . PHE A 96  ? 0.5275 0.6492 0.6592 0.0216  0.0231  -0.0196 1006 PHE A CE1 
699  C CE2 . PHE A 96  ? 0.5326 0.6468 0.6593 0.0241  0.0511  -0.0124 1006 PHE A CE2 
700  C CZ  . PHE A 96  ? 0.5279 0.6444 0.6649 0.0242  0.0402  -0.0206 1006 PHE A CZ  
701  N N   . ASN A 97  ? 0.6807 0.7763 0.6822 0.0060  0.0332  -0.0147 1007 ASN A N   
702  C CA  . ASN A 97  ? 0.6963 0.7741 0.6718 0.0038  0.0535  -0.0256 1007 ASN A CA  
703  C C   . ASN A 97  ? 0.6903 0.7685 0.6972 0.0123  0.0737  -0.0237 1007 ASN A C   
704  O O   . ASN A 97  ? 0.6651 0.7470 0.7026 0.0166  0.0750  -0.0297 1007 ASN A O   
705  C CB  . ASN A 97  ? 0.7289 0.7959 0.6889 -0.0032 0.0506  -0.0439 1007 ASN A CB  
706  C CG  . ASN A 97  ? 0.7650 0.8062 0.6855 -0.0059 0.0714  -0.0565 1007 ASN A CG  
707  O OD1 . ASN A 97  ? 0.7724 0.8066 0.7007 0.0029  0.0944  -0.0557 1007 ASN A OD1 
708  N ND2 . ASN A 97  ? 0.7818 0.8091 0.6592 -0.0186 0.0639  -0.0685 1007 ASN A ND2 
709  N N   . LYS A 98  ? 0.7347 0.8114 0.7347 0.0142  0.0893  -0.0142 1008 LYS A N   
710  C CA  . LYS A 98  ? 0.7512 0.8372 0.7882 0.0206  0.1060  -0.0090 1008 LYS A CA  
711  C C   . LYS A 98  ? 0.7416 0.8195 0.7746 0.0264  0.1296  -0.0194 1008 LYS A C   
712  O O   . LYS A 98  ? 0.6841 0.7736 0.7555 0.0338  0.1380  -0.0192 1008 LYS A O   
713  C CB  . LYS A 98  ? 0.7378 0.8284 0.7753 0.0185  0.1128  0.0078  1008 LYS A CB  
714  C CG  . LYS A 98  ? 0.7300 0.8257 0.7817 0.0164  0.0930  0.0197  1008 LYS A CG  
715  C CD  . LYS A 98  ? 0.7841 0.8706 0.8031 0.0126  0.0923  0.0338  1008 LYS A CD  
716  C CE  . LYS A 98  ? 0.7682 0.8550 0.8019 0.0135  0.0752  0.0467  1008 LYS A CE  
717  N NZ  . LYS A 98  ? 0.7654 0.8402 0.7661 0.0118  0.0747  0.0631  1008 LYS A NZ  
718  N N   . ILE A 99  ? 0.7847 0.8424 0.7706 0.0238  0.1408  -0.0282 1009 ILE A N   
719  C CA  . ILE A 99  ? 0.7996 0.8429 0.7768 0.0314  0.1657  -0.0398 1009 ILE A CA  
720  C C   . ILE A 99  ? 0.8113 0.8491 0.8081 0.0358  0.1596  -0.0514 1009 ILE A C   
721  O O   . ILE A 99  ? 0.7910 0.8367 0.8233 0.0473  0.1719  -0.0504 1009 ILE A O   
722  C CB  . ILE A 99  ? 0.8559 0.8711 0.7691 0.0255  0.1770  -0.0500 1009 ILE A CB  
723  C CG1 . ILE A 99  ? 0.8531 0.8719 0.7442 0.0224  0.1873  -0.0370 1009 ILE A CG1 
724  C CG2 . ILE A 99  ? 0.9019 0.8944 0.8025 0.0347  0.2037  -0.0646 1009 ILE A CG2 
725  C CD1 . ILE A 99  ? 0.8879 0.8792 0.7082 0.0140  0.1929  -0.0459 1009 ILE A CD1 
726  N N   . GLU A 100 ? 0.7857 0.8113 0.7599 0.0263  0.1402  -0.0611 1010 GLU A N   
727  C CA  . GLU A 100 ? 0.8297 0.8459 0.8161 0.0273  0.1342  -0.0722 1010 GLU A CA  
728  C C   . GLU A 100 ? 0.7579 0.7936 0.7687 0.0210  0.1062  -0.0668 1010 GLU A C   
729  O O   . GLU A 100 ? 0.7239 0.7566 0.7119 0.0092  0.0887  -0.0718 1010 GLU A O   
730  C CB  . GLU A 100 ? 0.8956 0.8765 0.8314 0.0194  0.1401  -0.0908 1010 GLU A CB  
731  C CG  . GLU A 100 ? 0.9546 0.9144 0.9000 0.0265  0.1509  -0.1018 1010 GLU A CG  
732  C CD  . GLU A 100 ? 0.9563 0.9253 0.9401 0.0469  0.1727  -0.0936 1010 GLU A CD  
733  O OE1 . GLU A 100 ? 0.9615 0.9268 0.9343 0.0550  0.1959  -0.0918 1010 GLU A OE1 
734  O OE2 . GLU A 100 ? 0.9355 0.9184 0.9611 0.0546  0.1665  -0.0879 1010 GLU A OE2 
735  N N   . PRO A 101 ? 0.7153 0.7727 0.7727 0.0283  0.1016  -0.0564 1011 PRO A N   
736  C CA  . PRO A 101 ? 0.5948 0.6677 0.6732 0.0238  0.0783  -0.0520 1011 PRO A CA  
737  C C   . PRO A 101 ? 0.5982 0.6610 0.6737 0.0193  0.0701  -0.0635 1011 PRO A C   
738  O O   . PRO A 101 ? 0.5935 0.6377 0.6639 0.0230  0.0831  -0.0728 1011 PRO A O   
739  C CB  . PRO A 101 ? 0.5537 0.6456 0.6770 0.0322  0.0799  -0.0412 1011 PRO A CB  
740  C CG  . PRO A 101 ? 0.5438 0.6323 0.6755 0.0418  0.1026  -0.0420 1011 PRO A CG  
741  C CD  . PRO A 101 ? 0.6267 0.6973 0.7174 0.0396  0.1174  -0.0477 1011 PRO A CD  
742  N N   . PRO A 102 ? 0.5616 0.6356 0.6406 0.0117  0.0499  -0.0626 1012 PRO A N   
743  C CA  . PRO A 102 ? 0.5304 0.5997 0.6152 0.0064  0.0423  -0.0712 1012 PRO A CA  
744  C C   . PRO A 102 ? 0.4864 0.5674 0.6107 0.0148  0.0401  -0.0652 1012 PRO A C   
745  O O   . PRO A 102 ? 0.4969 0.5942 0.6437 0.0208  0.0367  -0.0546 1012 PRO A O   
746  C CB  . PRO A 102 ? 0.5929 0.6768 0.6674 -0.0051 0.0222  -0.0703 1012 PRO A CB  
747  C CG  . PRO A 102 ? 0.5568 0.6592 0.6430 0.0015  0.0161  -0.0555 1012 PRO A CG  
748  C CD  . PRO A 102 ? 0.5449 0.6366 0.6233 0.0084  0.0342  -0.0523 1012 PRO A CD  
749  N N   . LEU A 103 ? 0.4386 0.5080 0.5677 0.0140  0.0422  -0.0722 1013 LEU A N   
750  C CA  . LEU A 103 ? 0.3672 0.4467 0.5284 0.0209  0.0389  -0.0665 1013 LEU A CA  
751  C C   . LEU A 103 ? 0.3849 0.4866 0.5622 0.0182  0.0228  -0.0598 1013 LEU A C   
752  O O   . LEU A 103 ? 0.4106 0.5200 0.5776 0.0099  0.0124  -0.0611 1013 LEU A O   
753  C CB  . LEU A 103 ? 0.3294 0.3909 0.4882 0.0188  0.0425  -0.0738 1013 LEU A CB  
754  C CG  . LEU A 103 ? 0.4441 0.4760 0.5867 0.0240  0.0603  -0.0807 1013 LEU A CG  
755  C CD1 . LEU A 103 ? 0.3733 0.3847 0.5115 0.0191  0.0612  -0.0866 1013 LEU A CD1 
756  C CD2 . LEU A 103 ? 0.3529 0.3900 0.5158 0.0411  0.0726  -0.0722 1013 LEU A CD2 
757  N N   . ILE A 104 ? 0.3430 0.4555 0.5453 0.0255  0.0209  -0.0521 1014 ILE A N   
758  C CA  . ILE A 104 ? 0.3406 0.4683 0.5566 0.0254  0.0093  -0.0463 1014 ILE A CA  
759  C C   . ILE A 104 ? 0.3216 0.4505 0.5526 0.0265  0.0063  -0.0474 1014 ILE A C   
760  O O   . ILE A 104 ? 0.2770 0.4024 0.5185 0.0316  0.0107  -0.0455 1014 ILE A O   
761  C CB  . ILE A 104 ? 0.3281 0.4620 0.5543 0.0303  0.0097  -0.0374 1014 ILE A CB  
762  C CG1 . ILE A 104 ? 0.3268 0.4600 0.5358 0.0286  0.0117  -0.0339 1014 ILE A CG1 
763  C CG2 . ILE A 104 ? 0.3165 0.4578 0.5562 0.0321  0.0006  -0.0331 1014 ILE A CG2 
764  C CD1 . ILE A 104 ? 0.3642 0.5009 0.5815 0.0311  0.0113  -0.0238 1014 ILE A CD1 
765  N N   . PHE A 105 ? 0.3359 0.4727 0.5685 0.0219  -0.0012 -0.0490 1015 PHE A N   
766  C CA  . PHE A 105 ? 0.2868 0.4256 0.5311 0.0222  -0.0028 -0.0495 1015 PHE A CA  
767  C C   . PHE A 105 ? 0.2887 0.4395 0.5450 0.0270  -0.0084 -0.0440 1015 PHE A C   
768  O O   . PHE A 105 ? 0.3260 0.4900 0.5852 0.0261  -0.0139 -0.0423 1015 PHE A O   
769  C CB  . PHE A 105 ? 0.3307 0.4694 0.5694 0.0125  -0.0037 -0.0555 1015 PHE A CB  
770  C CG  . PHE A 105 ? 0.2873 0.4046 0.5113 0.0082  0.0044  -0.0619 1015 PHE A CG  
771  C CD1 . PHE A 105 ? 0.3159 0.4235 0.5212 0.0042  0.0074  -0.0667 1015 PHE A CD1 
772  C CD2 . PHE A 105 ? 0.2507 0.3539 0.4766 0.0096  0.0103  -0.0625 1015 PHE A CD2 
773  C CE1 . PHE A 105 ? 0.3064 0.3886 0.4956 0.0022  0.0177  -0.0734 1015 PHE A CE1 
774  C CE2 . PHE A 105 ? 0.2734 0.3522 0.4853 0.0085  0.0195  -0.0671 1015 PHE A CE2 
775  C CZ  . PHE A 105 ? 0.3216 0.3885 0.5152 0.0051  0.0241  -0.0734 1015 PHE A CZ  
776  N N   . GLU A 106 ? 0.2175 0.3634 0.4806 0.0323  -0.0071 -0.0410 1016 GLU A N   
777  C CA  . GLU A 106 ? 0.2499 0.3980 0.5194 0.0367  -0.0099 -0.0378 1016 GLU A CA  
778  C C   . GLU A 106 ? 0.2928 0.4431 0.5660 0.0367  -0.0091 -0.0404 1016 GLU A C   
779  O O   . GLU A 106 ? 0.2880 0.4347 0.5591 0.0331  -0.0064 -0.0433 1016 GLU A O   
780  C CB  . GLU A 106 ? 0.2648 0.4045 0.5360 0.0381  -0.0094 -0.0352 1016 GLU A CB  
781  C CG  . GLU A 106 ? 0.2463 0.3849 0.5158 0.0381  -0.0090 -0.0304 1016 GLU A CG  
782  C CD  . GLU A 106 ? 0.2770 0.4087 0.5502 0.0362  -0.0094 -0.0274 1016 GLU A CD  
783  O OE1 . GLU A 106 ? 0.2620 0.3885 0.5363 0.0349  -0.0117 -0.0297 1016 GLU A OE1 
784  O OE2 . GLU A 106 ? 0.2813 0.4123 0.5544 0.0341  -0.0073 -0.0228 1016 GLU A OE2 
785  N N   . CYS A 107 ? 0.2501 0.4045 0.5280 0.0418  -0.0096 -0.0386 1017 CYS A N   
786  C CA  . CYS A 107 ? 0.2577 0.4159 0.5394 0.0429  -0.0060 -0.0405 1017 CYS A CA  
787  C C   . CYS A 107 ? 0.2837 0.4267 0.5569 0.0420  -0.0036 -0.0429 1017 CYS A C   
788  O O   . CYS A 107 ? 0.2918 0.4244 0.5600 0.0419  -0.0061 -0.0423 1017 CYS A O   
789  C CB  . CYS A 107 ? 0.2086 0.3730 0.4974 0.0521  -0.0044 -0.0373 1017 CYS A CB  
790  S SG  . CYS A 107 ? 0.3423 0.5352 0.6460 0.0552  -0.0092 -0.0312 1017 CYS A SG  
791  N N   . ASN A 108 ? 0.2356 0.3792 0.5068 0.0400  0.0008  -0.0447 1018 ASN A N   
792  C CA  . ASN A 108 ? 0.2601 0.3904 0.5197 0.0379  0.0015  -0.0454 1018 ASN A CA  
793  C C   . ASN A 108 ? 0.2631 0.3894 0.5151 0.0397  0.0079  -0.0472 1018 ASN A C   
794  O O   . ASN A 108 ? 0.2820 0.4162 0.5407 0.0443  0.0133  -0.0479 1018 ASN A O   
795  C CB  . ASN A 108 ? 0.2821 0.4105 0.5403 0.0330  0.0021  -0.0443 1018 ASN A CB  
796  C CG  . ASN A 108 ? 0.2734 0.4102 0.5367 0.0277  0.0068  -0.0456 1018 ASN A CG  
797  O OD1 . ASN A 108 ? 0.2724 0.4119 0.5348 0.0263  0.0124  -0.0457 1018 ASN A OD1 
798  N ND2 . ASN A 108 ? 0.2378 0.3794 0.5052 0.0234  0.0050  -0.0470 1018 ASN A ND2 
799  N N   . GLN A 109 ? 0.2739 0.3888 0.5114 0.0371  0.0081  -0.0469 1019 GLN A N   
800  C CA  . GLN A 109 ? 0.2712 0.3785 0.4946 0.0380  0.0154  -0.0489 1019 GLN A CA  
801  C C   . GLN A 109 ? 0.2483 0.3662 0.4782 0.0361  0.0254  -0.0477 1019 GLN A C   
802  O O   . GLN A 109 ? 0.2970 0.4102 0.5156 0.0372  0.0344  -0.0488 1019 GLN A O   
803  C CB  . GLN A 109 ? 0.2632 0.3561 0.4655 0.0347  0.0108  -0.0474 1019 GLN A CB  
804  C CG  . GLN A 109 ? 0.2625 0.3551 0.4641 0.0317  0.0088  -0.0412 1019 GLN A CG  
805  C CD  . GLN A 109 ? 0.2853 0.3825 0.4996 0.0325  0.0006  -0.0380 1019 GLN A CD  
806  O OE1 . GLN A 109 ? 0.2983 0.4017 0.5236 0.0337  -0.0034 -0.0402 1019 GLN A OE1 
807  N NE2 . GLN A 109 ? 0.2645 0.3572 0.4766 0.0329  -0.0003 -0.0319 1019 GLN A NE2 
808  N N   . ALA A 110 ? 0.2358 0.3666 0.4812 0.0315  0.0248  -0.0459 1020 ALA A N   
809  C CA  . ALA A 110 ? 0.3029 0.4483 0.5587 0.0267  0.0337  -0.0449 1020 ALA A CA  
810  C C   . ALA A 110 ? 0.2822 0.4527 0.5609 0.0305  0.0345  -0.0450 1020 ALA A C   
811  O O   . ALA A 110 ? 0.3336 0.5236 0.6262 0.0275  0.0422  -0.0434 1020 ALA A O   
812  C CB  . ALA A 110 ? 0.2443 0.3867 0.5006 0.0159  0.0332  -0.0433 1020 ALA A CB  
813  N N   . CYS A 111 ? 0.2401 0.4126 0.5242 0.0368  0.0267  -0.0453 1021 CYS A N   
814  C CA  . CYS A 111 ? 0.2208 0.4161 0.5249 0.0435  0.0263  -0.0429 1021 CYS A CA  
815  C C   . CYS A 111 ? 0.2766 0.4744 0.5835 0.0547  0.0380  -0.0425 1021 CYS A C   
816  O O   . CYS A 111 ? 0.3059 0.4797 0.5926 0.0587  0.0434  -0.0460 1021 CYS A O   
817  C CB  . CYS A 111 ? 0.2696 0.4595 0.5730 0.0489  0.0170  -0.0418 1021 CYS A CB  
818  S SG  . CYS A 111 ? 0.2084 0.3976 0.5086 0.0382  0.0067  -0.0425 1021 CYS A SG  
819  N N   . SER A 112 ? 0.2213 0.4494 0.5530 0.0596  0.0422  -0.0380 1022 SER A N   
820  C CA  . SER A 112 ? 0.3011 0.5329 0.6389 0.0745  0.0557  -0.0367 1022 SER A CA  
821  C C   . SER A 112 ? 0.2679 0.4835 0.6010 0.0900  0.0541  -0.0360 1022 SER A C   
822  O O   . SER A 112 ? 0.2996 0.5021 0.6267 0.1035  0.0670  -0.0374 1022 SER A O   
823  C CB  . SER A 112 ? 0.2312 0.5069 0.6029 0.0760  0.0618  -0.0300 1022 SER A CB  
824  O OG  . SER A 112 ? 0.2178 0.5213 0.6120 0.0767  0.0487  -0.0237 1022 SER A OG  
825  N N   . CYS A 113 ? 0.2329 0.4451 0.5655 0.0879  0.0403  -0.0339 1023 CYS A N   
826  C CA  . CYS A 113 ? 0.2571 0.4512 0.5840 0.1004  0.0386  -0.0317 1023 CYS A CA  
827  C C   . CYS A 113 ? 0.3137 0.4657 0.6109 0.1010  0.0440  -0.0397 1023 CYS A C   
828  O O   . CYS A 113 ? 0.3176 0.4574 0.5982 0.0922  0.0472  -0.0461 1023 CYS A O   
829  C CB  . CYS A 113 ? 0.2303 0.4283 0.5587 0.0946  0.0236  -0.0278 1023 CYS A CB  
830  S SG  . CYS A 113 ? 0.2211 0.3954 0.5267 0.0774  0.0150  -0.0348 1023 CYS A SG  
831  N N   . TRP A 114 ? 0.3205 0.4488 0.6088 0.1104  0.0448  -0.0389 1024 TRP A N   
832  C CA  . TRP A 114 ? 0.3406 0.4274 0.5986 0.1070  0.0482  -0.0475 1024 TRP A CA  
833  C C   . TRP A 114 ? 0.3530 0.4287 0.6006 0.0924  0.0342  -0.0488 1024 TRP A C   
834  O O   . TRP A 114 ? 0.3305 0.4241 0.5919 0.0889  0.0247  -0.0427 1024 TRP A O   
835  C CB  . TRP A 114 ? 0.3628 0.4223 0.6130 0.1231  0.0586  -0.0471 1024 TRP A CB  
836  C CG  . TRP A 114 ? 0.4291 0.4864 0.6792 0.1377  0.0772  -0.0496 1024 TRP A CG  
837  C CD1 . TRP A 114 ? 0.3938 0.4881 0.6678 0.1439  0.0846  -0.0453 1024 TRP A CD1 
838  C CD2 . TRP A 114 ? 0.4064 0.4212 0.6304 0.1475  0.0926  -0.0573 1024 TRP A CD2 
839  N NE1 . TRP A 114 ? 0.4527 0.5332 0.7196 0.1589  0.1051  -0.0489 1024 TRP A NE1 
840  C CE2 . TRP A 114 ? 0.4338 0.4627 0.6675 0.1619  0.1108  -0.0571 1024 TRP A CE2 
841  C CE3 . TRP A 114 ? 0.4532 0.4177 0.6451 0.1440  0.0937  -0.0650 1024 TRP A CE3 
842  C CZ2 . TRP A 114 ? 0.4658 0.4580 0.6761 0.1755  0.1315  -0.0648 1024 TRP A CZ2 
843  C CZ3 . TRP A 114 ? 0.4909 0.4159 0.6571 0.1550  0.1125  -0.0736 1024 TRP A CZ3 
844  C CH2 . TRP A 114 ? 0.5033 0.4412 0.6779 0.1720  0.1321  -0.0737 1024 TRP A CH2 
845  N N   . ARG A 115 ? 0.3335 0.3808 0.5559 0.0833  0.0334  -0.0567 1025 ARG A N   
846  C CA  . ARG A 115 ? 0.3818 0.4218 0.5972 0.0693  0.0211  -0.0573 1025 ARG A CA  
847  C C   . ARG A 115 ? 0.4333 0.4620 0.6519 0.0707  0.0177  -0.0525 1025 ARG A C   
848  O O   . ARG A 115 ? 0.4098 0.4393 0.6286 0.0594  0.0088  -0.0510 1025 ARG A O   
849  C CB  . ARG A 115 ? 0.3961 0.4112 0.5841 0.0587  0.0199  -0.0661 1025 ARG A CB  
850  C CG  . ARG A 115 ? 0.3682 0.3818 0.5520 0.0430  0.0064  -0.0660 1025 ARG A CG  
851  C CD  . ARG A 115 ? 0.3894 0.4336 0.5937 0.0400  -0.0013 -0.0593 1025 ARG A CD  
852  N NE  . ARG A 115 ? 0.3873 0.4350 0.5906 0.0277  -0.0123 -0.0581 1025 ARG A NE  
853  C CZ  . ARG A 115 ? 0.3751 0.4212 0.5848 0.0212  -0.0173 -0.0554 1025 ARG A CZ  
854  N NH1 . ARG A 115 ? 0.3468 0.3823 0.5595 0.0256  -0.0126 -0.0535 1025 ARG A NH1 
855  N NH2 . ARG A 115 ? 0.4067 0.4638 0.6212 0.0105  -0.0269 -0.0529 1025 ARG A NH2 
856  N N   . ASN A 116 ? 0.3815 0.5400 0.7179 0.0379  0.0399  -0.1570 1026 ASN A N   
857  C CA  . ASN A 116 ? 0.3864 0.5322 0.7597 0.0485  0.0352  -0.1453 1026 ASN A CA  
858  C C   . ASN A 116 ? 0.3217 0.4795 0.7148 0.0533  0.0303  -0.1201 1026 ASN A C   
859  O O   . ASN A 116 ? 0.3197 0.4761 0.7555 0.0624  0.0287  -0.1105 1026 ASN A O   
860  C CB  . ASN A 116 ? 0.3962 0.5354 0.8101 0.0570  0.0444  -0.1649 1026 ASN A CB  
861  C CG  . ASN A 116 ? 0.4508 0.6057 0.8908 0.0626  0.0552  -0.1698 1026 ASN A CG  
862  O OD1 . ASN A 116 ? 0.3908 0.5692 0.8203 0.0598  0.0598  -0.1693 1026 ASN A OD1 
863  N ND2 . ASN A 116 ? 0.5207 0.6616 0.9923 0.0688  0.0584  -0.1723 1026 ASN A ND2 
864  N N   . CYS A 117 ? 0.3330 0.5017 0.6951 0.0455  0.0264  -0.1077 1027 CYS A N   
865  C CA  . CYS A 117 ? 0.2944 0.4766 0.6686 0.0458  0.0210  -0.0839 1027 CYS A CA  
866  C C   . CYS A 117 ? 0.2980 0.4679 0.6651 0.0433  0.0107  -0.0646 1027 CYS A C   
867  O O   . CYS A 117 ? 0.3542 0.5060 0.7066 0.0423  0.0081  -0.0692 1027 CYS A O   
868  C CB  . CYS A 117 ? 0.3000 0.4985 0.6426 0.0362  0.0215  -0.0803 1027 CYS A CB  
869  S SG  . CYS A 117 ? 0.3503 0.5346 0.6345 0.0232  0.0141  -0.0760 1027 CYS A SG  
870  N N   . LYS A 118 ? 0.2656 0.4480 0.6430 0.0408  0.0047  -0.0420 1028 LYS A N   
871  C CA  . LYS A 118 ? 0.2769 0.4522 0.6519 0.0370  -0.0038 -0.0233 1028 LYS A CA  
872  C C   . LYS A 118 ? 0.3185 0.4823 0.6445 0.0273  -0.0056 -0.0235 1028 LYS A C   
873  O O   . LYS A 118 ? 0.3221 0.4800 0.6430 0.0236  -0.0101 -0.0115 1028 LYS A O   
874  C CB  . LYS A 118 ? 0.2831 0.4781 0.6792 0.0330  -0.0105 0.0023  1028 LYS A CB  
875  C CG  . LYS A 118 ? 0.3705 0.5751 0.8271 0.0438  -0.0111 0.0091  1028 LYS A CG  
876  C CD  . LYS A 118 ? 0.4059 0.5881 0.8796 0.0500  -0.0131 0.0073  1028 LYS A CD  
877  C CE  . LYS A 118 ? 0.4845 0.6628 0.9952 0.0556  -0.0149 0.0183  1028 LYS A CE  
878  N NZ  . LYS A 118 ? 0.5146 0.6697 1.0410 0.0585  -0.0181 0.0188  1028 LYS A NZ  
879  N N   . ASN A 119 ? 0.2761 0.4372 0.5689 0.0227  -0.0020 -0.0362 1029 ASN A N   
880  C CA  . ASN A 119 ? 0.3049 0.4547 0.5569 0.0141  -0.0035 -0.0355 1029 ASN A CA  
881  C C   . ASN A 119 ? 0.3031 0.4365 0.5418 0.0164  -0.0015 -0.0514 1029 ASN A C   
882  O O   . ASN A 119 ? 0.3151 0.4444 0.5253 0.0104  -0.0012 -0.0575 1029 ASN A O   
883  C CB  . ASN A 119 ? 0.2891 0.4490 0.5147 0.0043  -0.0038 -0.0323 1029 ASN A CB  
884  C CG  . ASN A 119 ? 0.3452 0.4943 0.5353 -0.0060 -0.0056 -0.0268 1029 ASN A CG  
885  O OD1 . ASN A 119 ? 0.3319 0.4748 0.5206 -0.0079 -0.0065 -0.0190 1029 ASN A OD1 
886  N ND2 . ASN A 119 ? 0.3272 0.4745 0.4888 -0.0137 -0.0055 -0.0313 1029 ASN A ND2 
887  N N   . ARG A 120 ? 0.2702 0.3948 0.5307 0.0236  -0.0015 -0.0564 1030 ARG A N   
888  C CA  . ARG A 120 ? 0.2828 0.3948 0.5335 0.0239  -0.0012 -0.0701 1030 ARG A CA  
889  C C   . ARG A 120 ? 0.2857 0.3852 0.5516 0.0282  -0.0039 -0.0668 1030 ARG A C   
890  O O   . ARG A 120 ? 0.2440 0.3362 0.5199 0.0305  -0.0044 -0.0773 1030 ARG A O   
891  C CB  . ARG A 120 ? 0.2481 0.3663 0.5068 0.0253  0.0031  -0.0871 1030 ARG A CB  
892  C CG  . ARG A 120 ? 0.2984 0.4294 0.5343 0.0183  0.0055  -0.0907 1030 ARG A CG  
893  C CD  . ARG A 120 ? 0.3463 0.4866 0.5846 0.0168  0.0115  -0.1093 1030 ARG A CD  
894  N NE  . ARG A 120 ? 0.2770 0.4354 0.5016 0.0108  0.0147  -0.1099 1030 ARG A NE  
895  C CZ  . ARG A 120 ? 0.3058 0.4680 0.4987 -0.0001 0.0130  -0.1136 1030 ARG A CZ  
896  N NH1 . ARG A 120 ? 0.3105 0.4598 0.4830 -0.0064 0.0075  -0.1158 1030 ARG A NH1 
897  N NH2 . ARG A 120 ? 0.3045 0.4854 0.4881 -0.0059 0.0158  -0.1127 1030 ARG A NH2 
898  N N   . VAL A 121 ? 0.2552 0.3534 0.5209 0.0273  -0.0056 -0.0524 1031 VAL A N   
899  C CA  . VAL A 121 ? 0.2780 0.3684 0.5607 0.0305  -0.0080 -0.0469 1031 VAL A CA  
900  C C   . VAL A 121 ? 0.2546 0.3329 0.5232 0.0294  -0.0087 -0.0528 1031 VAL A C   
901  O O   . VAL A 121 ? 0.2122 0.2839 0.4928 0.0314  -0.0112 -0.0596 1031 VAL A O   
902  C CB  . VAL A 121 ? 0.2812 0.3779 0.5660 0.0273  -0.0087 -0.0295 1031 VAL A CB  
903  C CG1 . VAL A 121 ? 0.1838 0.2740 0.4816 0.0289  -0.0104 -0.0236 1031 VAL A CG1 
904  C CG2 . VAL A 121 ? 0.2567 0.3670 0.5645 0.0278  -0.0114 -0.0191 1031 VAL A CG2 
905  N N   . VAL A 122 ? 0.2483 0.3236 0.4932 0.0253  -0.0066 -0.0498 1032 VAL A N   
906  C CA  . VAL A 122 ? 0.2606 0.3258 0.5008 0.0254  -0.0074 -0.0509 1032 VAL A CA  
907  C C   . VAL A 122 ? 0.2651 0.3268 0.5015 0.0235  -0.0117 -0.0611 1032 VAL A C   
908  O O   . VAL A 122 ? 0.2837 0.3404 0.5305 0.0239  -0.0157 -0.0619 1032 VAL A O   
909  C CB  . VAL A 122 ? 0.2749 0.3359 0.4949 0.0222  -0.0029 -0.0473 1032 VAL A CB  
910  C CG1 . VAL A 122 ? 0.2167 0.2682 0.4397 0.0238  -0.0033 -0.0468 1032 VAL A CG1 
911  C CG2 . VAL A 122 ? 0.2654 0.3324 0.4863 0.0206  0.0020  -0.0384 1032 VAL A CG2 
912  N N   . GLN A 123 ? 0.2406 0.3073 0.4618 0.0195  -0.0115 -0.0684 1033 GLN A N   
913  C CA  . GLN A 123 ? 0.2720 0.3392 0.4854 0.0141  -0.0153 -0.0784 1033 GLN A CA  
914  C C   . GLN A 123 ? 0.3099 0.3772 0.5414 0.0155  -0.0162 -0.0878 1033 GLN A C   
915  O O   . GLN A 123 ? 0.3406 0.4077 0.5646 0.0085  -0.0198 -0.0965 1033 GLN A O   
916  C CB  . GLN A 123 ? 0.2756 0.3521 0.4696 0.0083  -0.0136 -0.0842 1033 GLN A CB  
917  C CG  . GLN A 123 ? 0.2956 0.3836 0.5006 0.0116  -0.0081 -0.0906 1033 GLN A CG  
918  C CD  . GLN A 123 ? 0.2727 0.3725 0.4591 0.0059  -0.0060 -0.0919 1033 GLN A CD  
919  O OE1 . GLN A 123 ? 0.2043 0.3129 0.3806 -0.0004 -0.0051 -0.1021 1033 GLN A OE1 
920  N NE2 . GLN A 123 ? 0.2838 0.3848 0.4640 0.0060  -0.0052 -0.0814 1033 GLN A NE2 
921  N N   . SER A 124 ? 0.2331 0.3001 0.4883 0.0226  -0.0139 -0.0859 1034 SER A N   
922  C CA  . SER A 124 ? 0.2509 0.3142 0.5266 0.0240  -0.0145 -0.0959 1034 SER A CA  
923  C C   . SER A 124 ? 0.2882 0.3418 0.5755 0.0236  -0.0205 -0.0905 1034 SER A C   
924  O O   . SER A 124 ? 0.3366 0.3845 0.6380 0.0224  -0.0223 -0.0998 1034 SER A O   
925  C CB  . SER A 124 ? 0.2629 0.3301 0.5655 0.0317  -0.0105 -0.0952 1034 SER A CB  
926  O OG  . SER A 124 ? 0.2681 0.3464 0.5651 0.0317  -0.0048 -0.1024 1034 SER A OG  
927  N N   . GLY A 125 ? 0.2720 0.3239 0.5556 0.0243  -0.0228 -0.0766 1035 GLY A N   
928  C CA  . GLY A 125 ? 0.2705 0.3167 0.5651 0.0229  -0.0285 -0.0704 1035 GLY A CA  
929  C C   . GLY A 125 ? 0.2927 0.3374 0.6131 0.0282  -0.0289 -0.0605 1035 GLY A C   
930  O O   . GLY A 125 ? 0.2531 0.3011 0.5852 0.0327  -0.0258 -0.0567 1035 GLY A O   
931  N N   . ILE A 126 ? 0.2715 0.3131 0.6026 0.0262  -0.0342 -0.0538 1036 ILE A N   
932  C CA  . ILE A 126 ? 0.2706 0.3129 0.6256 0.0292  -0.0357 -0.0416 1036 ILE A CA  
933  C C   . ILE A 126 ? 0.2609 0.2971 0.6368 0.0300  -0.0386 -0.0475 1036 ILE A C   
934  O O   . ILE A 126 ? 0.2824 0.3106 0.6589 0.0260  -0.0417 -0.0617 1036 ILE A O   
935  C CB  . ILE A 126 ? 0.2820 0.3243 0.6451 0.0260  -0.0410 -0.0329 1036 ILE A CB  
936  C CG1 . ILE A 126 ? 0.2485 0.2965 0.6005 0.0279  -0.0361 -0.0253 1036 ILE A CG1 
937  C CG2 . ILE A 126 ? 0.2338 0.2776 0.6232 0.0269  -0.0440 -0.0210 1036 ILE A CG2 
938  C CD1 . ILE A 126 ? 0.2784 0.3270 0.6364 0.0240  -0.0424 -0.0197 1036 ILE A CD1 
939  N N   . LYS A 127 ? 0.2540 0.2942 0.6482 0.0339  -0.0376 -0.0365 1037 LYS A N   
940  C CA  . LYS A 127 ? 0.2405 0.2739 0.6630 0.0358  -0.0413 -0.0385 1037 LYS A CA  
941  C C   . LYS A 127 ? 0.2509 0.2849 0.6995 0.0346  -0.0475 -0.0212 1037 LYS A C   
942  O O   . LYS A 127 ? 0.3349 0.3580 0.8081 0.0338  -0.0534 -0.0241 1037 LYS A O   
943  C CB  . LYS A 127 ? 0.2663 0.3053 0.6954 0.0407  -0.0369 -0.0386 1037 LYS A CB  
944  C CG  . LYS A 127 ? 0.2947 0.3332 0.7058 0.0416  -0.0309 -0.0577 1037 LYS A CG  
945  C CD  . LYS A 127 ? 0.3678 0.3936 0.7862 0.0397  -0.0314 -0.0785 1037 LYS A CD  
946  C CE  . LYS A 127 ? 0.4112 0.4404 0.8062 0.0376  -0.0245 -0.0980 1037 LYS A CE  
947  N NZ  . LYS A 127 ? 0.4076 0.4486 0.8030 0.0431  -0.0182 -0.0957 1037 LYS A NZ  
948  N N   . VAL A 128 ? 0.2927 0.3395 0.7370 0.0335  -0.0458 -0.0038 1038 VAL A N   
949  C CA  . VAL A 128 ? 0.2748 0.3261 0.7424 0.0303  -0.0515 0.0140  1038 VAL A CA  
950  C C   . VAL A 128 ? 0.2558 0.3014 0.7273 0.0266  -0.0565 0.0126  1038 VAL A C   
951  O O   . VAL A 128 ? 0.2534 0.2968 0.7062 0.0259  -0.0547 0.0029  1038 VAL A O   
952  C CB  . VAL A 128 ? 0.2869 0.3569 0.7456 0.0278  -0.0459 0.0311  1038 VAL A CB  
953  C CG1 . VAL A 128 ? 0.2580 0.3352 0.7111 0.0284  -0.0429 0.0344  1038 VAL A CG1 
954  C CG2 . VAL A 128 ? 0.2398 0.3145 0.6737 0.0280  -0.0378 0.0267  1038 VAL A CG2 
955  N N   . ARG A 129 ? 0.3115 0.3558 0.8079 0.0227  -0.0642 0.0247  1039 ARG A N   
956  C CA  . ARG A 129 ? 0.2270 0.2683 0.7317 0.0177  -0.0709 0.0268  1039 ARG A CA  
957  C C   . ARG A 129 ? 0.2333 0.2925 0.7320 0.0158  -0.0660 0.0429  1039 ARG A C   
958  O O   . ARG A 129 ? 0.2185 0.2885 0.7199 0.0137  -0.0629 0.0584  1039 ARG A O   
959  C CB  . ARG A 129 ? 0.2394 0.2691 0.7751 0.0133  -0.0819 0.0315  1039 ARG A CB  
960  C CG  . ARG A 129 ? 0.2750 0.2835 0.8181 0.0153  -0.0839 0.0114  1039 ARG A CG  
961  C CD  . ARG A 129 ? 0.2634 0.2629 0.7811 0.0128  -0.0815 -0.0117 1039 ARG A CD  
962  N NE  . ARG A 129 ? 0.3086 0.3019 0.8280 0.0030  -0.0904 -0.0124 1039 ARG A NE  
963  C CZ  . ARG A 129 ? 0.3128 0.2869 0.8418 -0.0039 -0.0967 -0.0268 1039 ARG A CZ  
964  N NH1 . ARG A 129 ? 0.3442 0.3023 0.8842 -0.0002 -0.0932 -0.0441 1039 ARG A NH1 
965  N NH2 . ARG A 129 ? 0.3307 0.3016 0.8597 -0.0153 -0.1061 -0.0245 1039 ARG A NH2 
966  N N   . LEU A 130 ? 0.2217 0.2844 0.7121 0.0157  -0.0649 0.0393  1040 LEU A N   
967  C CA  . LEU A 130 ? 0.2335 0.3116 0.7192 0.0159  -0.0572 0.0509  1040 LEU A CA  
968  C C   . LEU A 130 ? 0.1886 0.2676 0.6876 0.0106  -0.0652 0.0580  1040 LEU A C   
969  O O   . LEU A 130 ? 0.1935 0.2630 0.6999 0.0064  -0.0764 0.0504  1040 LEU A O   
970  C CB  . LEU A 130 ? 0.1755 0.2578 0.6418 0.0221  -0.0471 0.0422  1040 LEU A CB  
971  C CG  . LEU A 130 ? 0.1867 0.2691 0.6326 0.0261  -0.0378 0.0351  1040 LEU A CG  
972  C CD1 . LEU A 130 ? 0.1817 0.2682 0.6103 0.0302  -0.0266 0.0306  1040 LEU A CD1 
973  C CD2 . LEU A 130 ? 0.2022 0.2961 0.6554 0.0236  -0.0346 0.0473  1040 LEU A CD2 
974  N N   . GLN A 131 ? 0.1887 0.2817 0.6923 0.0097  -0.0592 0.0724  1041 GLN A N   
975  C CA  . GLN A 131 ? 0.2372 0.3335 0.7541 0.0044  -0.0662 0.0822  1041 GLN A CA  
976  C C   . GLN A 131 ? 0.1925 0.3038 0.7085 0.0087  -0.0545 0.0891  1041 GLN A C   
977  O O   . GLN A 131 ? 0.2112 0.3364 0.7263 0.0123  -0.0412 0.0937  1041 GLN A O   
978  C CB  . GLN A 131 ? 0.2688 0.3663 0.8027 -0.0028 -0.0736 0.0962  1041 GLN A CB  
979  C CG  . GLN A 131 ? 0.2228 0.3231 0.7705 -0.0097 -0.0825 0.1077  1041 GLN A CG  
980  C CD  . GLN A 131 ? 0.2426 0.3456 0.8056 -0.0165 -0.0883 0.1231  1041 GLN A CD  
981  O OE1 . GLN A 131 ? 0.2980 0.4176 0.8628 -0.0157 -0.0789 0.1350  1041 GLN A OE1 
982  N NE2 . GLN A 131 ? 0.2329 0.3204 0.8080 -0.0242 -0.1041 0.1228  1041 GLN A NE2 
983  N N   . LEU A 132 ? 0.1954 0.3056 0.7149 0.0076  -0.0597 0.0901  1042 LEU A N   
984  C CA  . LEU A 132 ? 0.2625 0.3860 0.7905 0.0112  -0.0506 0.0999  1042 LEU A CA  
985  C C   . LEU A 132 ? 0.2047 0.3395 0.7508 0.0057  -0.0532 0.1166  1042 LEU A C   
986  O O   . LEU A 132 ? 0.2386 0.3676 0.7930 -0.0030 -0.0684 0.1230  1042 LEU A O   
987  C CB  . LEU A 132 ? 0.2601 0.3795 0.7895 0.0104  -0.0578 0.0997  1042 LEU A CB  
988  C CG  . LEU A 132 ? 0.2043 0.3342 0.7457 0.0158  -0.0483 0.1087  1042 LEU A CG  
989  C CD1 . LEU A 132 ? 0.1999 0.3340 0.7347 0.0265  -0.0281 0.1001  1042 LEU A CD1 
990  C CD2 . LEU A 132 ? 0.2090 0.3343 0.7535 0.0123  -0.0599 0.1119  1042 LEU A CD2 
991  N N   . TYR A 133 ? 0.2185 0.3706 0.7714 0.0097  -0.0385 0.1234  1043 TYR A N   
992  C CA  . TYR A 133 ? 0.2413 0.4078 0.8123 0.0046  -0.0398 0.1402  1043 TYR A CA  
993  C C   . TYR A 133 ? 0.2314 0.4178 0.8154 0.0114  -0.0228 0.1453  1043 TYR A C   
994  O O   . TYR A 133 ? 0.2121 0.4011 0.7910 0.0202  -0.0079 0.1349  1043 TYR A O   
995  C CB  . TYR A 133 ? 0.2130 0.3851 0.7845 -0.0011 -0.0412 0.1463  1043 TYR A CB  
996  C CG  . TYR A 133 ? 0.2692 0.4604 0.8369 0.0029  -0.0229 0.1445  1043 TYR A CG  
997  C CD1 . TYR A 133 ? 0.2316 0.4187 0.7837 0.0092  -0.0132 0.1297  1043 TYR A CD1 
998  C CD2 . TYR A 133 ? 0.2246 0.4405 0.8043 -0.0014 -0.0151 0.1579  1043 TYR A CD2 
999  C CE1 . TYR A 133 ? 0.1987 0.4057 0.7475 0.0101  0.0040  0.1278  1043 TYR A CE1 
1000 C CE2 . TYR A 133 ? 0.2192 0.4568 0.7948 -0.0010 0.0025  0.1556  1043 TYR A CE2 
1001 C CZ  . TYR A 133 ? 0.2054 0.4382 0.7654 0.0042  0.0121  0.1403  1043 TYR A CZ  
1002 O OH  . TYR A 133 ? 0.2067 0.4627 0.7615 0.0015  0.0305  0.1377  1043 TYR A OH  
1003 N N   . ARG A 134 ? 0.2371 0.4373 0.8398 0.0072  -0.0249 0.1611  1044 ARG A N   
1004 C CA  . ARG A 134 ? 0.2301 0.4514 0.8511 0.0134  -0.0088 0.1669  1044 ARG A CA  
1005 C C   . ARG A 134 ? 0.2308 0.4753 0.8534 0.0129  0.0070  0.1680  1044 ARG A C   
1006 O O   . ARG A 134 ? 0.2339 0.4872 0.8599 0.0038  -0.0004 0.1800  1044 ARG A O   
1007 C CB  . ARG A 134 ? 0.2405 0.4674 0.8820 0.0082  -0.0195 0.1846  1044 ARG A CB  
1008 C CG  . ARG A 134 ? 0.2494 0.4962 0.9148 0.0155  -0.0044 0.1911  1044 ARG A CG  
1009 C CD  . ARG A 134 ? 0.2503 0.4861 0.9185 0.0243  -0.0001 0.1834  1044 ARG A CD  
1010 N NE  . ARG A 134 ? 0.2837 0.5348 0.9806 0.0311  0.0114  0.1915  1044 ARG A NE  
1011 C CZ  . ARG A 134 ? 0.2908 0.5359 0.9975 0.0403  0.0198  0.1859  1044 ARG A CZ  
1012 N NH1 . ARG A 134 ? 0.2608 0.4864 0.9488 0.0433  0.0182  0.1723  1044 ARG A NH1 
1013 N NH2 . ARG A 134 ? 0.2814 0.5404 1.0191 0.0464  0.0296  0.1946  1044 ARG A NH2 
1014 N N   . THR A 135 ? 0.2303 0.4856 0.8507 0.0210  0.0284  0.1558  1045 THR A N   
1015 C CA  . THR A 135 ? 0.2337 0.5154 0.8539 0.0176  0.0454  0.1556  1045 THR A CA  
1016 C C   . THR A 135 ? 0.2466 0.5553 0.8904 0.0177  0.0570  0.1656  1045 THR A C   
1017 O O   . THR A 135 ? 0.2526 0.5589 0.9151 0.0230  0.0543  0.1715  1045 THR A O   
1018 C CB  . THR A 135 ? 0.2320 0.5158 0.8385 0.0236  0.0659  0.1366  1045 THR A CB  
1019 O OG1 . THR A 135 ? 0.2428 0.5327 0.8629 0.0339  0.0848  0.1280  1045 THR A OG1 
1020 C CG2 . THR A 135 ? 0.2208 0.4760 0.8078 0.0269  0.0553  0.1256  1045 THR A CG2 
1021 N N   . ALA A 136 ? 0.2526 0.5896 0.8955 0.0102  0.0704  0.1681  1046 ALA A N   
1022 C CA  . ALA A 136 ? 0.3102 0.6772 0.9742 0.0086  0.0831  0.1764  1046 ALA A CA  
1023 C C   . ALA A 136 ? 0.3076 0.6822 0.9858 0.0216  0.1072  0.1618  1046 ALA A C   
1024 O O   . ALA A 136 ? 0.2888 0.6773 0.9925 0.0256  0.1123  0.1691  1046 ALA A O   
1025 C CB  . ALA A 136 ? 0.2736 0.6707 0.9285 -0.0057 0.0920  0.1818  1046 ALA A CB  
1026 N N   . LYS A 137 ? 0.2766 0.6407 0.9401 0.0283  0.1218  0.1414  1047 LYS A N   
1027 C CA  . LYS A 137 ? 0.2929 0.6634 0.9677 0.0395  0.1479  0.1246  1047 LYS A CA  
1028 C C   . LYS A 137 ? 0.3334 0.6716 1.0015 0.0517  0.1483  0.1097  1047 LYS A C   
1029 O O   . LYS A 137 ? 0.3709 0.7065 1.0554 0.0627  0.1638  0.0999  1047 LYS A O   
1030 C CB  . LYS A 137 ? 0.3072 0.7064 0.9682 0.0319  0.1759  0.1104  1047 LYS A CB  
1031 C CG  . LYS A 137 ? 0.4082 0.8426 1.0713 0.0161  0.1766  0.1252  1047 LYS A CG  
1032 C CD  . LYS A 137 ? 0.4482 0.9148 1.0955 0.0055  0.2069  0.1100  1047 LYS A CD  
1033 C CE  . LYS A 137 ? 0.4425 0.9480 1.0985 -0.0095 0.2103  0.1248  1047 LYS A CE  
1034 N NZ  . LYS A 137 ? 0.4825 1.0235 1.1213 -0.0227 0.2419  0.1088  1047 LYS A NZ  
1035 N N   . MET A 138 ? 0.2910 0.6044 0.9376 0.0500  0.1316  0.1080  1048 MET A N   
1036 C CA  . MET A 138 ? 0.3111 0.5964 0.9463 0.0590  0.1334  0.0927  1048 MET A CA  
1037 C C   . MET A 138 ? 0.2808 0.5398 0.9210 0.0623  0.1086  0.1026  1048 MET A C   
1038 O O   . MET A 138 ? 0.3069 0.5427 0.9289 0.0639  0.1004  0.0945  1048 MET A O   
1039 C CB  . MET A 138 ? 0.2986 0.5781 0.9025 0.0532  0.1362  0.0807  1048 MET A CB  
1040 C CG  . MET A 138 ? 0.3317 0.6341 0.9233 0.0474  0.1639  0.0670  1048 MET A CG  
1041 S SD  . MET A 138 ? 0.3795 0.6735 0.9352 0.0383  0.1642  0.0566  1048 MET A SD  
1042 C CE  . MET A 138 ? 0.3291 0.6364 0.8845 0.0240  0.1388  0.0816  1048 MET A CE  
1043 N N   . GLY A 139 ? 0.2664 0.5305 0.9290 0.0610  0.0962  0.1203  1049 GLY A N   
1044 C CA  . GLY A 139 ? 0.2593 0.5018 0.9218 0.0590  0.0718  0.1305  1049 GLY A CA  
1045 C C   . GLY A 139 ? 0.2432 0.4732 0.8793 0.0500  0.0535  0.1306  1049 GLY A C   
1046 O O   . GLY A 139 ? 0.2382 0.4797 0.8681 0.0423  0.0504  0.1356  1049 GLY A O   
1047 N N   . TRP A 140 ? 0.2415 0.4484 0.8632 0.0503  0.0412  0.1252  1050 TRP A N   
1048 C CA  . TRP A 140 ? 0.2332 0.4267 0.8312 0.0428  0.0249  0.1224  1050 TRP A CA  
1049 C C   . TRP A 140 ? 0.2173 0.4087 0.7937 0.0451  0.0362  0.1066  1050 TRP A C   
1050 O O   . TRP A 140 ? 0.2218 0.4131 0.7954 0.0526  0.0536  0.0944  1050 TRP A O   
1051 C CB  . TRP A 140 ? 0.2536 0.4272 0.8452 0.0404  0.0072  0.1228  1050 TRP A CB  
1052 C CG  . TRP A 140 ? 0.2562 0.4326 0.8684 0.0351  -0.0065 0.1402  1050 TRP A CG  
1053 C CD1 . TRP A 140 ? 0.2398 0.4161 0.8709 0.0385  -0.0062 0.1475  1050 TRP A CD1 
1054 C CD2 . TRP A 140 ? 0.2320 0.4113 0.8490 0.0242  -0.0232 0.1535  1050 TRP A CD2 
1055 N NE1 . TRP A 140 ? 0.2466 0.4276 0.8935 0.0300  -0.0219 0.1657  1050 TRP A NE1 
1056 C CE2 . TRP A 140 ? 0.2781 0.4603 0.9154 0.0210  -0.0323 0.1687  1050 TRP A CE2 
1057 C CE3 . TRP A 140 ? 0.2534 0.4319 0.8611 0.0162  -0.0320 0.1547  1050 TRP A CE3 
1058 C CZ2 . TRP A 140 ? 0.2814 0.4669 0.9274 0.0095  -0.0494 0.1845  1050 TRP A CZ2 
1059 C CZ3 . TRP A 140 ? 0.2353 0.4145 0.8525 0.0054  -0.0489 0.1691  1050 TRP A CZ3 
1060 C CH2 . TRP A 140 ? 0.2456 0.4286 0.8804 0.0020  -0.0572 0.1834  1050 TRP A CH2 
1061 N N   . GLY A 141 ? 0.2085 0.3975 0.7711 0.0378  0.0258  0.1074  1051 GLY A N   
1062 C CA  . GLY A 141 ? 0.2659 0.4521 0.8088 0.0378  0.0317  0.0955  1051 GLY A CA  
1063 C C   . GLY A 141 ? 0.1930 0.3619 0.7214 0.0323  0.0123  0.0941  1051 GLY A C   
1064 O O   . GLY A 141 ? 0.2031 0.3626 0.7360 0.0275  -0.0044 0.1007  1051 GLY A O   
1065 N N   . VAL A 142 ? 0.2829 0.4488 0.7952 0.0323  0.0157  0.0847  1052 VAL A N   
1066 C CA  . VAL A 142 ? 0.2123 0.3626 0.7122 0.0283  0.0002  0.0810  1052 VAL A CA  
1067 C C   . VAL A 142 ? 0.2571 0.4190 0.7579 0.0219  0.0004  0.0877  1052 VAL A C   
1068 O O   . VAL A 142 ? 0.2597 0.4366 0.7560 0.0215  0.0143  0.0856  1052 VAL A O   
1069 C CB  . VAL A 142 ? 0.1816 0.3172 0.6629 0.0336  0.0016  0.0656  1052 VAL A CB  
1070 C CG1 . VAL A 142 ? 0.2257 0.3485 0.6966 0.0300  -0.0115 0.0606  1052 VAL A CG1 
1071 C CG2 . VAL A 142 ? 0.1798 0.3048 0.6617 0.0372  -0.0021 0.0627  1052 VAL A CG2 
1072 N N   . ARG A 143 ? 0.2019 0.3574 0.7094 0.0152  -0.0149 0.0966  1053 ARG A N   
1073 C CA  . ARG A 143 ? 0.2377 0.4022 0.7486 0.0078  -0.0181 0.1066  1053 ARG A CA  
1074 C C   . ARG A 143 ? 0.2529 0.3966 0.7579 0.0071  -0.0313 0.1007  1053 ARG A C   
1075 O O   . ARG A 143 ? 0.2782 0.4017 0.7813 0.0095  -0.0405 0.0910  1053 ARG A O   
1076 C CB  . ARG A 143 ? 0.2660 0.4418 0.7940 0.0000  -0.0236 0.1249  1053 ARG A CB  
1077 C CG  . ARG A 143 ? 0.2741 0.4307 0.8123 -0.0038 -0.0416 0.1294  1053 ARG A CG  
1078 C CD  . ARG A 143 ? 0.2378 0.4074 0.7916 -0.0126 -0.0465 0.1493  1053 ARG A CD  
1079 N NE  . ARG A 143 ? 0.2667 0.4272 0.8326 -0.0157 -0.0576 0.1549  1053 ARG A NE  
1080 C CZ  . ARG A 143 ? 0.2623 0.4372 0.8417 -0.0216 -0.0591 0.1716  1053 ARG A CZ  
1081 N NH1 . ARG A 143 ? 0.2275 0.4282 0.8096 -0.0251 -0.0492 0.1833  1053 ARG A NH1 
1082 N NH2 . ARG A 143 ? 0.2728 0.4380 0.8628 -0.0256 -0.0711 0.1769  1053 ARG A NH2 
1083 N N   . ALA A 144 ? 0.1828 0.3338 0.6866 0.0028  -0.0314 0.1067  1054 ALA A N   
1084 C CA  . ALA A 144 ? 0.2594 0.3919 0.7635 0.0026  -0.0430 0.1033  1054 ALA A CA  
1085 C C   . ALA A 144 ? 0.3173 0.4370 0.8401 -0.0029 -0.0576 0.1132  1054 ALA A C   
1086 O O   . ALA A 144 ? 0.2867 0.4184 0.8207 -0.0099 -0.0598 0.1302  1054 ALA A O   
1087 C CB  . ALA A 144 ? 0.3229 0.4687 0.8223 -0.0013 -0.0400 0.1101  1054 ALA A CB  
1088 N N   . LEU A 145 ? 0.2804 0.3471 0.8808 -0.0241 -0.0730 0.1116  1055 LEU A N   
1089 C CA  . LEU A 145 ? 0.2520 0.3007 0.8557 -0.0283 -0.0970 0.1245  1055 LEU A CA  
1090 C C   . LEU A 145 ? 0.2564 0.3057 0.8437 -0.0292 -0.1083 0.1145  1055 LEU A C   
1091 O O   . LEU A 145 ? 0.2762 0.3060 0.8600 -0.0323 -0.1306 0.1209  1055 LEU A O   
1092 C CB  . LEU A 145 ? 0.2801 0.3003 0.8687 -0.0283 -0.1175 0.1168  1055 LEU A CB  
1093 C CG  . LEU A 145 ? 0.2597 0.2771 0.8693 -0.0270 -0.1128 0.1323  1055 LEU A CG  
1094 C CD1 . LEU A 145 ? 0.2566 0.2514 0.8485 -0.0265 -0.1343 0.1246  1055 LEU A CD1 
1095 C CD2 . LEU A 145 ? 0.2605 0.2888 0.9073 -0.0286 -0.1082 0.1657  1055 LEU A CD2 
1096 N N   . GLN A 146 ? 0.2876 0.3579 0.8649 -0.0253 -0.0946 0.0989  1056 GLN A N   
1097 C CA  . GLN A 146 ? 0.3329 0.4045 0.8883 -0.0238 -0.1065 0.0842  1056 GLN A CA  
1098 C C   . GLN A 146 ? 0.2807 0.3755 0.8255 -0.0163 -0.0837 0.0753  1056 GLN A C   
1099 O O   . GLN A 146 ? 0.2536 0.3569 0.7972 -0.0118 -0.0604 0.0728  1056 GLN A O   
1100 C CB  . GLN A 146 ? 0.3097 0.3601 0.8260 -0.0228 -0.1236 0.0582  1056 GLN A CB  
1101 C CG  . GLN A 146 ? 0.3097 0.3685 0.8101 -0.0200 -0.1107 0.0362  1056 GLN A CG  
1102 C CD  . GLN A 146 ? 0.3476 0.3900 0.8094 -0.0169 -0.1249 0.0151  1056 GLN A CD  
1103 O OE1 . GLN A 146 ? 0.3787 0.3991 0.8316 -0.0160 -0.1367 0.0170  1056 GLN A OE1 
1104 N NE2 . GLN A 146 ? 0.3747 0.4291 0.8143 -0.0139 -0.1231 -0.0036 1056 GLN A NE2 
1105 N N   . THR A 147 ? 0.2374 0.3303 0.7541 -0.0127 -0.0883 0.0691  1057 THR A N   
1106 C CA  . THR A 147 ? 0.3783 0.4782 0.8560 -0.0041 -0.0689 0.0532  1057 THR A CA  
1107 C C   . THR A 147 ? 0.2867 0.3828 0.7382 -0.0043 -0.0693 0.0246  1057 THR A C   
1108 O O   . THR A 147 ? 0.2654 0.3536 0.7146 -0.0087 -0.0892 0.0131  1057 THR A O   
1109 C CB  . THR A 147 ? 0.3499 0.4484 0.8035 -0.0007 -0.0769 0.0522  1057 THR A CB  
1110 O OG1 . THR A 147 ? 0.3780 0.4867 0.8468 0.0038  -0.0620 0.0774  1057 THR A OG1 
1111 C CG2 . THR A 147 ? 0.4098 0.5096 0.8170 0.0051  -0.0708 0.0260  1057 THR A CG2 
1112 N N   . ILE A 148 ? 0.3124 0.4133 0.7460 0.0012  -0.0474 0.0150  1058 ILE A N   
1113 C CA  . ILE A 148 ? 0.3183 0.4160 0.7315 0.0000  -0.0460 -0.0091 1058 ILE A CA  
1114 C C   . ILE A 148 ? 0.3692 0.4678 0.7426 0.0069  -0.0337 -0.0239 1058 ILE A C   
1115 O O   . ILE A 148 ? 0.3645 0.4638 0.7311 0.0149  -0.0129 -0.0189 1058 ILE A O   
1116 C CB  . ILE A 148 ? 0.2934 0.3904 0.7283 -0.0013 -0.0337 -0.0062 1058 ILE A CB  
1117 C CG1 . ILE A 148 ? 0.2881 0.3835 0.7628 -0.0084 -0.0472 0.0079  1058 ILE A CG1 
1118 C CG2 . ILE A 148 ? 0.2891 0.3818 0.7015 -0.0031 -0.0328 -0.0304 1058 ILE A CG2 
1119 C CD1 . ILE A 148 ? 0.2006 0.2954 0.6939 -0.0100 -0.0371 0.0073  1058 ILE A CD1 
1120 N N   . PRO A 149 ? 0.3018 0.4001 0.6472 0.0054  -0.0462 -0.0415 1059 PRO A N   
1121 C CA  . PRO A 149 ? 0.3466 0.4448 0.6543 0.0109  -0.0379 -0.0561 1059 PRO A CA  
1122 C C   . PRO A 149 ? 0.3800 0.4720 0.6770 0.0103  -0.0281 -0.0707 1059 PRO A C   
1123 O O   . PRO A 149 ? 0.3709 0.4613 0.6859 0.0038  -0.0318 -0.0743 1059 PRO A O   
1124 C CB  . PRO A 149 ? 0.3890 0.4909 0.6770 0.0078  -0.0571 -0.0687 1059 PRO A CB  
1125 C CG  . PRO A 149 ? 0.3472 0.4488 0.6594 0.0039  -0.0743 -0.0584 1059 PRO A CG  
1126 C CD  . PRO A 149 ? 0.3226 0.4206 0.6690 0.0002  -0.0694 -0.0476 1059 PRO A CD  
1127 N N   . GLN A 150 ? 0.4252 0.5119 0.6909 0.0179  -0.0167 -0.0793 1060 GLN A N   
1128 C CA  . GLN A 150 ? 0.3880 0.4634 0.6363 0.0185  -0.0096 -0.0948 1060 GLN A CA  
1129 C C   . GLN A 150 ? 0.4088 0.4855 0.6557 0.0066  -0.0265 -0.1114 1060 GLN A C   
1130 O O   . GLN A 150 ? 0.3594 0.4452 0.5981 0.0022  -0.0414 -0.1170 1060 GLN A O   
1131 C CB  . GLN A 150 ? 0.4203 0.4868 0.6277 0.0297  -0.0005 -0.1031 1060 GLN A CB  
1132 C CG  . GLN A 150 ? 0.5094 0.5574 0.6932 0.0329  0.0057  -0.1189 1060 GLN A CG  
1133 C CD  . GLN A 150 ? 0.6067 0.6439 0.7445 0.0397  0.0031  -0.1342 1060 GLN A CD  
1134 O OE1 . GLN A 150 ? 0.6783 0.6976 0.7877 0.0528  0.0152  -0.1394 1060 GLN A OE1 
1135 N NE2 . GLN A 150 ? 0.6887 0.7358 0.8170 0.0323  -0.0136 -0.1418 1060 GLN A NE2 
1136 N N   . GLY A 151 ? 0.4003 0.4693 0.6564 0.0022  -0.0235 -0.1176 1061 GLY A N   
1137 C CA  . GLY A 151 ? 0.3953 0.4671 0.6534 -0.0088 -0.0375 -0.1305 1061 GLY A CA  
1138 C C   . GLY A 151 ? 0.3208 0.4027 0.6124 -0.0155 -0.0458 -0.1231 1061 GLY A C   
1139 O O   . GLY A 151 ? 0.3292 0.4135 0.6276 -0.0231 -0.0533 -0.1306 1061 GLY A O   
1140 N N   . THR A 152 ? 0.2905 0.3773 0.6028 -0.0126 -0.0457 -0.1078 1062 THR A N   
1141 C CA  . THR A 152 ? 0.3023 0.3945 0.6442 -0.0169 -0.0548 -0.1004 1062 THR A CA  
1142 C C   . THR A 152 ? 0.2943 0.3802 0.6561 -0.0197 -0.0459 -0.0996 1062 THR A C   
1143 O O   . THR A 152 ? 0.2831 0.3607 0.6482 -0.0153 -0.0298 -0.0942 1062 THR A O   
1144 C CB  . THR A 152 ? 0.2848 0.3783 0.6445 -0.0133 -0.0576 -0.0831 1062 THR A CB  
1145 O OG1 . THR A 152 ? 0.3075 0.4046 0.6470 -0.0097 -0.0637 -0.0831 1062 THR A OG1 
1146 C CG2 . THR A 152 ? 0.2348 0.3302 0.6181 -0.0165 -0.0724 -0.0776 1062 THR A CG2 
1147 N N   . PHE A 153 ? 0.2478 0.3384 0.6225 -0.0253 -0.0558 -0.1035 1063 PHE A N   
1148 C CA  . PHE A 153 ? 0.2471 0.3330 0.6448 -0.0278 -0.0493 -0.1004 1063 PHE A CA  
1149 C C   . PHE A 153 ? 0.2187 0.3037 0.6445 -0.0250 -0.0474 -0.0834 1063 PHE A C   
1150 O O   . PHE A 153 ? 0.2866 0.3692 0.7050 -0.0217 -0.0579 -0.0739 1063 PHE A O   
1151 C CB  . PHE A 153 ? 0.2114 0.2961 0.5943 -0.0285 -0.0568 -0.1016 1063 PHE A CB  
1152 C CG  . PHE A 153 ? 0.2160 0.2916 0.6093 -0.0270 -0.0503 -0.0941 1063 PHE A CG  
1153 C CD1 . PHE A 153 ? 0.2537 0.3244 0.6591 -0.0308 -0.0399 -0.1003 1063 PHE A CD1 
1154 C CD2 . PHE A 153 ? 0.2118 0.2814 0.6016 -0.0215 -0.0557 -0.0824 1063 PHE A CD2 
1155 C CE1 . PHE A 153 ? 0.2248 0.2878 0.6392 -0.0286 -0.0342 -0.0933 1063 PHE A CE1 
1156 C CE2 . PHE A 153 ? 0.2088 0.2703 0.6071 -0.0198 -0.0507 -0.0766 1063 PHE A CE2 
1157 C CZ  . PHE A 153 ? 0.1962 0.2556 0.6066 -0.0230 -0.0397 -0.0812 1063 PHE A CZ  
1158 N N   . ILE A 154 ? 0.2258 0.3045 0.6674 -0.0236 -0.0326 -0.0767 1064 ILE A N   
1159 C CA  . ILE A 154 ? 0.1911 0.2697 0.6613 -0.0214 -0.0295 -0.0575 1064 ILE A CA  
1160 C C   . ILE A 154 ? 0.1720 0.2367 0.6363 -0.0201 -0.0316 -0.0522 1064 ILE A C   
1161 O O   . ILE A 154 ? 0.1913 0.2473 0.6459 -0.0176 -0.0435 -0.0440 1064 ILE A O   
1162 C CB  . ILE A 154 ? 0.1907 0.2670 0.6653 -0.0147 -0.0080 -0.0473 1064 ILE A CB  
1163 C CG1 . ILE A 154 ? 0.2431 0.3184 0.6861 -0.0088 -0.0021 -0.0522 1064 ILE A CG1 
1164 C CG2 . ILE A 154 ? 0.1834 0.2656 0.6938 -0.0136 -0.0065 -0.0235 1064 ILE A CG2 
1165 C CD1 . ILE A 154 ? 0.2304 0.3126 0.6710 -0.0101 -0.0164 -0.0469 1064 ILE A CD1 
1166 N N   . CYS A 155 ? 0.1889 0.2513 0.6612 -0.0209 -0.0199 -0.0576 1065 CYS A N   
1167 C CA  . CYS A 155 ? 0.2189 0.2706 0.6883 -0.0187 -0.0204 -0.0529 1065 CYS A CA  
1168 C C   . CYS A 155 ? 0.2053 0.2554 0.6764 -0.0211 -0.0105 -0.0653 1065 CYS A C   
1169 O O   . CYS A 155 ? 0.1841 0.2387 0.6629 -0.0250 -0.0022 -0.0768 1065 CYS A O   
1170 C CB  . CYS A 155 ? 0.2189 0.2658 0.7095 -0.0158 -0.0153 -0.0342 1065 CYS A CB  
1171 S SG  . CYS A 155 ? 0.1929 0.2518 0.7161 -0.0142 0.0073  -0.0253 1065 CYS A SG  
1172 N N   . GLU A 156 ? 0.1724 0.2151 0.6377 -0.0190 -0.0120 -0.0635 1066 GLU A N   
1173 C CA  . GLU A 156 ? 0.1920 0.2311 0.6610 -0.0210 -0.0035 -0.0724 1066 GLU A CA  
1174 C C   . GLU A 156 ? 0.1937 0.2270 0.6878 -0.0181 0.0108  -0.0639 1066 GLU A C   
1175 O O   . GLU A 156 ? 0.2037 0.2340 0.7040 -0.0140 0.0091  -0.0492 1066 GLU A O   
1176 C CB  . GLU A 156 ? 0.1869 0.2245 0.6365 -0.0198 -0.0125 -0.0736 1066 GLU A CB  
1177 C CG  . GLU A 156 ? 0.1920 0.2264 0.6440 -0.0223 -0.0066 -0.0807 1066 GLU A CG  
1178 C CD  . GLU A 156 ? 0.2146 0.2510 0.6507 -0.0213 -0.0148 -0.0785 1066 GLU A CD  
1179 O OE1 . GLU A 156 ? 0.1734 0.2132 0.5960 -0.0184 -0.0242 -0.0735 1066 GLU A OE1 
1180 O OE2 . GLU A 156 ? 0.2570 0.2912 0.6960 -0.0235 -0.0113 -0.0816 1066 GLU A OE2 
1181 N N   . TYR A 157 ? 0.2121 0.2422 0.7208 -0.0208 0.0246  -0.0731 1067 TYR A N   
1182 C CA  . TYR A 157 ? 0.1966 0.2211 0.7283 -0.0167 0.0404  -0.0652 1067 TYR A CA  
1183 C C   . TYR A 157 ? 0.2090 0.2266 0.7312 -0.0145 0.0341  -0.0640 1067 TYR A C   
1184 O O   . TYR A 157 ? 0.1938 0.2082 0.7095 -0.0176 0.0339  -0.0754 1067 TYR A O   
1185 C CB  . TYR A 157 ? 0.2533 0.2625 0.7701 -0.0113 0.0571  -0.0745 1067 TYR A CB  
1186 C CG  . TYR A 157 ? 0.2473 0.2523 0.7790 0.0002  0.0769  -0.0607 1067 TYR A CG  
1187 C CD1 . TYR A 157 ? 0.2291 0.2283 0.7775 -0.0008 0.0810  -0.0598 1067 TYR A CD1 
1188 C CD2 . TYR A 157 ? 0.2473 0.2568 0.7781 0.0129  0.0920  -0.0463 1067 TYR A CD2 
1189 C CE1 . TYR A 157 ? 0.2390 0.2362 0.8016 0.0108  0.0996  -0.0459 1067 TYR A CE1 
1190 C CE2 . TYR A 157 ? 0.2570 0.2670 0.8039 0.0250  0.1113  -0.0304 1067 TYR A CE2 
1191 C CZ  . TYR A 157 ? 0.2651 0.2687 0.8274 0.0240  0.1148  -0.0307 1067 TYR A CZ  
1192 O OH  . TYR A 157 ? 0.2837 0.2863 0.8489 0.0333  0.1313  -0.0131 1067 TYR A OH  
1193 N N   . VAL A 158 ? 0.1955 0.2104 0.7170 -0.0096 0.0287  -0.0493 1068 VAL A N   
1194 C CA  . VAL A 158 ? 0.1934 0.2035 0.7068 -0.0066 0.0225  -0.0475 1068 VAL A CA  
1195 C C   . VAL A 158 ? 0.1834 0.1850 0.7161 -0.0030 0.0341  -0.0380 1068 VAL A C   
1196 O O   . VAL A 158 ? 0.1881 0.1876 0.7336 -0.0022 0.0397  -0.0244 1068 VAL A O   
1197 C CB  . VAL A 158 ? 0.2182 0.2280 0.7140 -0.0044 0.0061  -0.0408 1068 VAL A CB  
1198 C CG1 . VAL A 158 ? 0.1834 0.1866 0.6770 -0.0005 0.0025  -0.0362 1068 VAL A CG1 
1199 C CG2 . VAL A 158 ? 0.2509 0.2680 0.7253 -0.0074 -0.0041 -0.0499 1068 VAL A CG2 
1200 N N   . GLY A 159 ? 0.1926 0.1929 0.7234 -0.0026 0.0371  -0.0424 1069 GLY A N   
1201 C CA  . GLY A 159 ? 0.1903 0.1865 0.7282 -0.0017 0.0456  -0.0321 1069 GLY A CA  
1202 C C   . GLY A 159 ? 0.2225 0.2192 0.7544 -0.0016 0.0455  -0.0377 1069 GLY A C   
1203 O O   . GLY A 159 ? 0.2493 0.2493 0.7680 -0.0016 0.0349  -0.0436 1069 GLY A O   
1204 N N   . GLU A 160 ? 0.2300 0.2230 0.7737 -0.0014 0.0584  -0.0346 1070 GLU A N   
1205 C CA  . GLU A 160 ? 0.2072 0.2014 0.7491 -0.0009 0.0591  -0.0373 1070 GLU A CA  
1206 C C   . GLU A 160 ? 0.2033 0.2018 0.7610 -0.0044 0.0678  -0.0518 1070 GLU A C   
1207 O O   . GLU A 160 ? 0.2143 0.2097 0.7905 -0.0076 0.0830  -0.0558 1070 GLU A O   
1208 C CB  . GLU A 160 ? 0.2473 0.2346 0.7944 0.0004  0.0675  -0.0250 1070 GLU A CB  
1209 C CG  . GLU A 160 ? 0.2260 0.2169 0.7786 0.0013  0.0730  -0.0286 1070 GLU A CG  
1210 C CD  . GLU A 160 ? 0.2772 0.2542 0.8345 -0.0040 0.0831  -0.0160 1070 GLU A CD  
1211 O OE1 . GLU A 160 ? 0.3113 0.2903 0.8845 -0.0044 0.0939  -0.0054 1070 GLU A OE1 
1212 O OE2 . GLU A 160 ? 0.2673 0.2425 0.8208 -0.0007 0.0822  -0.0159 1070 GLU A OE2 
1213 N N   . LEU A 161 ? 0.2158 0.2167 0.7682 -0.0053 0.0587  -0.0593 1071 LEU A N   
1214 C CA  . LEU A 161 ? 0.2132 0.2076 0.7672 -0.0123 0.0613  -0.0717 1071 LEU A CA  
1215 C C   . LEU A 161 ? 0.2250 0.2118 0.7892 -0.0126 0.0724  -0.0696 1071 LEU A C   
1216 O O   . LEU A 161 ? 0.2101 0.2079 0.7870 -0.0076 0.0717  -0.0620 1071 LEU A O   
1217 C CB  . LEU A 161 ? 0.2431 0.2389 0.7770 -0.0165 0.0454  -0.0752 1071 LEU A CB  
1218 C CG  . LEU A 161 ? 0.2710 0.2724 0.7879 -0.0182 0.0340  -0.0768 1071 LEU A CG  
1219 C CD1 . LEU A 161 ? 0.2925 0.2991 0.7942 -0.0203 0.0213  -0.0738 1071 LEU A CD1 
1220 C CD2 . LEU A 161 ? 0.2294 0.2216 0.7354 -0.0262 0.0339  -0.0881 1071 LEU A CD2 
1221 N N   . ILE A 162 ? 0.2595 0.2185 0.8084 -0.0149 0.0820  -0.0765 1072 ILE A N   
1222 C CA  . ILE A 162 ? 0.3081 0.2479 0.8526 -0.0119 0.0921  -0.0754 1072 ILE A CA  
1223 C C   . ILE A 162 ? 0.3940 0.2950 0.9017 -0.0132 0.0875  -0.0905 1072 ILE A C   
1224 O O   . ILE A 162 ? 0.3432 0.2323 0.8307 -0.0162 0.0794  -0.1008 1072 ILE A O   
1225 C CB  . ILE A 162 ? 0.2919 0.2267 0.8437 -0.0027 0.1109  -0.0648 1072 ILE A CB  
1226 C CG1 . ILE A 162 ? 0.3192 0.2335 0.8482 0.0065  0.1188  -0.0694 1072 ILE A CG1 
1227 C CG2 . ILE A 162 ? 0.2501 0.2208 0.8392 -0.0060 0.1115  -0.0485 1072 ILE A CG2 
1228 C CD1 . ILE A 162 ? 0.3321 0.2445 0.8634 0.0206  0.1384  -0.0548 1072 ILE A CD1 
1229 N N   . SER A 163 ? 0.3542 0.2345 0.8523 -0.0109 0.0907  -0.0918 1073 SER A N   
1230 C CA  . SER A 163 ? 0.4045 0.2425 0.8650 -0.0110 0.0837  -0.1060 1073 SER A CA  
1231 C C   . SER A 163 ? 0.4631 0.2660 0.8919 0.0060  0.0972  -0.1124 1073 SER A C   
1232 O O   . SER A 163 ? 0.4786 0.2934 0.9177 0.0176  0.1136  -0.1031 1073 SER A O   
1233 C CB  . SER A 163 ? 0.4179 0.2447 0.8783 -0.0146 0.0794  -0.1048 1073 SER A CB  
1234 O OG  . SER A 163 ? 0.4447 0.2567 0.9019 -0.0020 0.0953  -0.1001 1073 SER A OG  
1235 N N   . ASP A 164 ? 0.5156 0.2743 0.9030 0.0095  0.0895  -0.1274 1074 ASP A N   
1236 C CA  . ASP A 164 ? 0.5544 0.2752 0.9021 0.0315  0.1018  -0.1349 1074 ASP A CA  
1237 C C   . ASP A 164 ? 0.6219 0.3339 0.9680 0.0480  0.1193  -0.1259 1074 ASP A C   
1238 O O   . ASP A 164 ? 0.6358 0.3443 0.9704 0.0693  0.1383  -0.1201 1074 ASP A O   
1239 C CB  . ASP A 164 ? 0.6398 0.3121 0.9395 0.0311  0.0849  -0.1544 1074 ASP A CB  
1240 C CG  . ASP A 164 ? 0.6997 0.3345 0.9523 0.0561  0.0949  -0.1649 1074 ASP A CG  
1241 O OD1 . ASP A 164 ? 0.6496 0.3051 0.9098 0.0670  0.1097  -0.1593 1074 ASP A OD1 
1242 O OD2 . ASP A 164 ? 0.7379 0.3219 0.9438 0.0658  0.0869  -0.1785 1074 ASP A OD2 
1243 N N   . ALA A 165 ? 0.6074 0.3186 0.9653 0.0395  0.1137  -0.1226 1075 ALA A N   
1244 C CA  . ALA A 165 ? 0.6115 0.3168 0.9698 0.0541  0.1296  -0.1134 1075 ALA A CA  
1245 C C   . ALA A 165 ? 0.5776 0.3292 0.9775 0.0563  0.1466  -0.0932 1075 ALA A C   
1246 O O   . ALA A 165 ? 0.6009 0.3508 0.9950 0.0750  0.1651  -0.0834 1075 ALA A O   
1247 C CB  . ALA A 165 ? 0.5859 0.2813 0.9493 0.0431  0.1187  -0.1143 1075 ALA A CB  
1248 N N   . GLU A 166 ? 0.4987 0.2920 0.9391 0.0382  0.1395  -0.0858 1076 GLU A N   
1249 C CA  . GLU A 166 ? 0.5120 0.3456 0.9902 0.0381  0.1510  -0.0669 1076 GLU A CA  
1250 C C   . GLU A 166 ? 0.5201 0.3543 0.9886 0.0532  0.1648  -0.0609 1076 GLU A C   
1251 O O   . GLU A 166 ? 0.4906 0.3373 0.9695 0.0641  0.1806  -0.0442 1076 GLU A O   
1252 C CB  . GLU A 166 ? 0.4658 0.3386 0.9813 0.0187  0.1375  -0.0628 1076 GLU A CB  
1253 C CG  . GLU A 166 ? 0.4240 0.3331 0.9754 0.0164  0.1445  -0.0441 1076 GLU A CG  
1254 C CD  . GLU A 166 ? 0.4347 0.3502 1.0009 0.0190  0.1541  -0.0307 1076 GLU A CD  
1255 O OE1 . GLU A 166 ? 0.4383 0.3452 1.0011 0.0169  0.1507  -0.0361 1076 GLU A OE1 
1256 O OE2 . GLU A 166 ? 0.4284 0.3559 1.0082 0.0228  0.1642  -0.0139 1076 GLU A OE2 
1257 N N   . ALA A 167 ? 0.5391 0.3612 0.9874 0.0541  0.1588  -0.0729 1077 ALA A N   
1258 C CA  . ALA A 167 ? 0.5616 0.3848 0.9982 0.0706  0.1725  -0.0671 1077 ALA A CA  
1259 C C   . ALA A 167 ? 0.5784 0.3782 0.9833 0.0973  0.1915  -0.0629 1077 ALA A C   
1260 O O   . ALA A 167 ? 0.6208 0.4337 1.0252 0.1129  0.2073  -0.0491 1077 ALA A O   
1261 C CB  . ALA A 167 ? 0.4826 0.2901 0.8953 0.0686  0.1622  -0.0841 1077 ALA A CB  
1262 N N   . ASP A 168 ? 0.5574 0.3239 0.9351 0.1037  0.1896  -0.0731 1078 ASP A N   
1263 C CA  . ASP A 168 ? 0.6762 0.4201 1.0215 0.1313  0.2068  -0.0693 1078 ASP A CA  
1264 C C   . ASP A 168 ? 0.6007 0.3789 0.9793 0.1360  0.2236  -0.0433 1078 ASP A C   
1265 O O   . ASP A 168 ? 0.6058 0.3900 0.9739 0.1576  0.2420  -0.0295 1078 ASP A O   
1266 C CB  . ASP A 168 ? 0.6871 0.3855 0.9970 0.1353  0.1971  -0.0864 1078 ASP A CB  
1267 C CG  . ASP A 168 ? 0.6936 0.3498 0.9622 0.1329  0.1786  -0.1115 1078 ASP A CG  
1268 O OD1 . ASP A 168 ? 0.6833 0.3486 0.9535 0.1261  0.1734  -0.1163 1078 ASP A OD1 
1269 O OD2 . ASP A 168 ? 0.7529 0.3651 0.9864 0.1371  0.1675  -0.1262 1078 ASP A OD2 
1270 N N   . VAL A 169 ? 0.5581 0.3594 0.9758 0.1158  0.2167  -0.0356 1079 VAL A N   
1271 C CA  . VAL A 169 ? 0.5576 0.3861 1.0051 0.1170  0.2286  -0.0127 1079 VAL A CA  
1272 C C   . VAL A 169 ? 0.5294 0.3990 1.0172 0.1052  0.2290  0.0068  1079 VAL A C   
1273 O O   . VAL A 169 ? 0.5165 0.4100 1.0348 0.0987  0.2323  0.0261  1079 VAL A O   
1274 C CB  . VAL A 169 ? 0.5689 0.3979 1.0340 0.1023  0.2198  -0.0148 1079 VAL A CB  
1275 C CG1 . VAL A 169 ? 0.5541 0.3386 0.9784 0.1130  0.2167  -0.0330 1079 VAL A CG1 
1276 C CG2 . VAL A 169 ? 0.4547 0.3047 0.9505 0.0755  0.2012  -0.0199 1079 VAL A CG2 
1277 N N   . ARG A 170 ? 0.5165 0.3916 1.0032 0.1016  0.2234  0.0017  1080 ARG A N   
1278 C CA  . ARG A 170 ? 0.4803 0.3889 1.0004 0.0914  0.2213  0.0195  1080 ARG A CA  
1279 C C   . ARG A 170 ? 0.5253 0.4411 1.0359 0.1130  0.2405  0.0382  1080 ARG A C   
1280 O O   . ARG A 170 ? 0.5612 0.4615 1.0393 0.1306  0.2486  0.0302  1080 ARG A O   
1281 C CB  . ARG A 170 ? 0.4605 0.3727 0.9844 0.0776  0.2056  0.0058  1080 ARG A CB  
1282 C CG  . ARG A 170 ? 0.4176 0.3346 0.9599 0.0542  0.1854  -0.0065 1080 ARG A CG  
1283 C CD  . ARG A 170 ? 0.3252 0.2703 0.9059 0.0371  0.1764  0.0103  1080 ARG A CD  
1284 N NE  . ARG A 170 ? 0.2981 0.2497 0.8941 0.0197  0.1614  0.0022  1080 ARG A NE  
1285 C CZ  . ARG A 170 ? 0.2977 0.2642 0.9107 0.0035  0.1442  -0.0003 1080 ARG A CZ  
1286 N NH1 . ARG A 170 ? 0.2550 0.2256 0.8698 0.0007  0.1377  0.0029  1080 ARG A NH1 
1287 N NH2 . ARG A 170 ? 0.2493 0.2238 0.8581 -0.0027 0.1297  -0.0064 1080 ARG A NH2 
1288 N N   . GLU A 171 ? 0.4998 0.4380 1.0367 0.1121  0.2473  0.0640  1081 GLU A N   
1289 C CA  . GLU A 171 ? 0.5277 0.4758 1.0578 0.1331  0.2667  0.0857  1081 GLU A CA  
1290 C C   . GLU A 171 ? 0.5713 0.5359 1.1085 0.1327  0.2658  0.0945  1081 GLU A C   
1291 O O   . GLU A 171 ? 0.5840 0.5453 1.0959 0.1541  0.2807  0.0981  1081 GLU A O   
1292 C CB  . GLU A 171 ? 0.5234 0.4900 1.0815 0.1306  0.2722  0.1125  1081 GLU A CB  
1293 C CG  . GLU A 171 ? 0.5384 0.5242 1.1020 0.1460  0.2880  0.1414  1081 GLU A CG  
1294 C CD  . GLU A 171 ? 0.5657 0.5673 1.1559 0.1448  0.2932  0.1696  1081 GLU A CD  
1295 O OE1 . GLU A 171 ? 0.5698 0.5664 1.1722 0.1327  0.2849  0.1654  1081 GLU A OE1 
1296 O OE2 . GLU A 171 ? 0.4906 0.5093 1.0892 0.1563  0.3055  0.1968  1081 GLU A OE2 
1297 N N   . ASP A 172 ? 0.5409 0.5217 1.1095 0.1097  0.2477  0.0986  1082 ASP A N   
1298 C CA  . ASP A 172 ? 0.5526 0.5500 1.1321 0.1073  0.2444  0.1097  1082 ASP A CA  
1299 C C   . ASP A 172 ? 0.5426 0.5288 1.1053 0.1027  0.2344  0.0837  1082 ASP A C   
1300 O O   . ASP A 172 ? 0.4886 0.4781 1.0676 0.0822  0.2146  0.0746  1082 ASP A O   
1301 C CB  . ASP A 172 ? 0.5099 0.5241 1.1267 0.0874  0.2278  0.1289  1082 ASP A CB  
1302 C CG  . ASP A 172 ? 0.5086 0.5369 1.1361 0.0841  0.2213  0.1401  1082 ASP A CG  
1303 O OD1 . ASP A 172 ? 0.5103 0.5408 1.1193 0.0987  0.2339  0.1378  1082 ASP A OD1 
1304 O OD2 . ASP A 172 ? 0.4871 0.5210 1.1378 0.0685  0.2024  0.1507  1082 ASP A OD2 
1305 N N   . ASP A 173 ? 0.6051 0.5750 1.1312 0.1233  0.2476  0.0716  1083 ASP A N   
1306 C CA  . ASP A 173 ? 0.6207 0.5743 1.1250 0.1215  0.2388  0.0458  1083 ASP A CA  
1307 C C   . ASP A 173 ? 0.6055 0.5756 1.1134 0.1241  0.2397  0.0543  1083 ASP A C   
1308 O O   . ASP A 173 ? 0.6355 0.5901 1.1101 0.1387  0.2458  0.0408  1083 ASP A O   
1309 C CB  . ASP A 173 ? 0.6638 0.5803 1.1182 0.1417  0.2478  0.0241  1083 ASP A CB  
1310 C CG  . ASP A 173 ? 0.7454 0.6579 1.1728 0.1710  0.2711  0.0386  1083 ASP A CG  
1311 O OD1 . ASP A 173 ? 0.7626 0.6991 1.2141 0.1738  0.2815  0.0659  1083 ASP A OD1 
1312 O OD2 . ASP A 173 ? 0.7834 0.6663 1.1624 0.1916  0.2777  0.0224  1083 ASP A OD2 
1313 N N   . SER A 174 ? 0.4998 0.4973 1.0447 0.1099  0.2317  0.0757  1084 SER A N   
1314 C CA  . SER A 174 ? 0.4430 0.4574 0.9950 0.1104  0.2306  0.0865  1084 SER A CA  
1315 C C   . SER A 174 ? 0.4185 0.4361 0.9846 0.0891  0.2072  0.0721  1084 SER A C   
1316 O O   . SER A 174 ? 0.4092 0.4415 0.9854 0.0858  0.2021  0.0816  1084 SER A O   
1317 C CB  . SER A 174 ? 0.4601 0.4986 1.0402 0.1101  0.2353  0.1220  1084 SER A CB  
1318 O OG  . SER A 174 ? 0.4430 0.4808 1.0129 0.1290  0.2562  0.1371  1084 SER A OG  
1319 N N   . TYR A 175 ? 0.3982 0.4025 0.9639 0.0754  0.1928  0.0503  1085 TYR A N   
1320 C CA  . TYR A 175 ? 0.3068 0.3136 0.8829 0.0563  0.1700  0.0362  1085 TYR A CA  
1321 C C   . TYR A 175 ? 0.3743 0.3601 0.9314 0.0534  0.1642  0.0064  1085 TYR A C   
1322 O O   . TYR A 175 ? 0.3293 0.3166 0.8959 0.0367  0.1451  -0.0060 1085 TYR A O   
1323 C CB  . TYR A 175 ? 0.2786 0.2932 0.8805 0.0381  0.1516  0.0493  1085 TYR A CB  
1324 C CG  . TYR A 175 ? 0.2810 0.3093 0.9000 0.0404  0.1535  0.0793  1085 TYR A CG  
1325 C CD1 . TYR A 175 ? 0.2724 0.3105 0.8981 0.0365  0.1432  0.0879  1085 TYR A CD1 
1326 C CD2 . TYR A 175 ? 0.2939 0.3246 0.9224 0.0467  0.1648  0.0993  1085 TYR A CD2 
1327 C CE1 . TYR A 175 ? 0.2768 0.3254 0.9193 0.0379  0.1426  0.1149  1085 TYR A CE1 
1328 C CE2 . TYR A 175 ? 0.3144 0.3574 0.9613 0.0485  0.1649  0.1280  1085 TYR A CE2 
1329 C CZ  . TYR A 175 ? 0.2899 0.3413 0.9443 0.0438  0.1534  0.1357  1085 TYR A CZ  
1330 O OH  . TYR A 175 ? 0.2958 0.3580 0.9701 0.0449  0.1512  0.1644  1085 TYR A OH  
1331 N N   . LEU A 176 ? 0.3732 0.3361 0.8986 0.0706  0.1791  -0.0048 1086 LEU A N   
1332 C CA  . LEU A 176 ? 0.3909 0.3248 0.8921 0.0683  0.1729  -0.0308 1086 LEU A CA  
1333 C C   . LEU A 176 ? 0.4150 0.3286 0.8846 0.0732  0.1688  -0.0522 1086 LEU A C   
1334 O O   . LEU A 176 ? 0.4227 0.3242 0.8631 0.0934  0.1836  -0.0521 1086 LEU A O   
1335 C CB  . LEU A 176 ? 0.4392 0.3520 0.9173 0.0841  0.1883  -0.0297 1086 LEU A CB  
1336 C CG  . LEU A 176 ? 0.4955 0.3807 0.9564 0.0787  0.1805  -0.0484 1086 LEU A CG  
1337 C CD1 . LEU A 176 ? 0.4276 0.3331 0.9255 0.0560  0.1657  -0.0444 1086 LEU A CD1 
1338 C CD2 . LEU A 176 ? 0.5468 0.4129 0.9834 0.0990  0.1978  -0.0433 1086 LEU A CD2 
1339 N N   . PHE A 177 ? 0.3799 0.2903 0.8526 0.0551  0.1483  -0.0694 1087 PHE A N   
1340 C CA  . PHE A 177 ? 0.3870 0.2832 0.8218 0.0510  0.1361  -0.0879 1087 PHE A CA  
1341 C C   . PHE A 177 ? 0.4132 0.2763 0.8208 0.0440  0.1241  -0.1106 1087 PHE A C   
1342 O O   . PHE A 177 ? 0.3934 0.2577 0.8235 0.0307  0.1151  -0.1129 1087 PHE A O   
1343 C CB  . PHE A 177 ? 0.3762 0.2998 0.8313 0.0336  0.1184  -0.0860 1087 PHE A CB  
1344 C CG  . PHE A 177 ? 0.4153 0.3305 0.8348 0.0310  0.1077  -0.1009 1087 PHE A CG  
1345 C CD1 . PHE A 177 ? 0.3954 0.2894 0.7901 0.0208  0.0921  -0.1220 1087 PHE A CD1 
1346 C CD2 . PHE A 177 ? 0.3975 0.3266 0.8103 0.0382  0.1124  -0.0925 1087 PHE A CD2 
1347 C CE1 . PHE A 177 ? 0.3985 0.2853 0.7618 0.0184  0.0813  -0.1348 1087 PHE A CE1 
1348 C CE2 . PHE A 177 ? 0.3805 0.3022 0.7602 0.0363  0.1025  -0.1061 1087 PHE A CE2 
1349 C CZ  . PHE A 177 ? 0.3972 0.2977 0.7519 0.0265  0.0867  -0.1277 1087 PHE A CZ  
1350 N N   . ASP A 178 ? 0.4595 0.2927 0.8187 0.0528  0.1225  -0.1266 1088 ASP A N   
1351 C CA  . ASP A 178 ? 0.4945 0.2903 0.8235 0.0469  0.1087  -0.1482 1088 ASP A CA  
1352 C C   . ASP A 178 ? 0.5206 0.3219 0.8464 0.0256  0.0838  -0.1609 1088 ASP A C   
1353 O O   . ASP A 178 ? 0.5176 0.3211 0.8204 0.0279  0.0793  -0.1659 1088 ASP A O   
1354 C CB  . ASP A 178 ? 0.5601 0.3153 0.8337 0.0700  0.1178  -0.1595 1088 ASP A CB  
1355 C CG  . ASP A 178 ? 0.6344 0.3683 0.9015 0.0895  0.1366  -0.1544 1088 ASP A CG  
1356 O OD1 . ASP A 178 ? 0.5835 0.3338 0.8856 0.0809  0.1384  -0.1428 1088 ASP A OD1 
1357 O OD2 . ASP A 178 ? 0.6496 0.3530 0.8705 0.1141  0.1479  -0.1602 1088 ASP A OD2 
1358 N N   . LEU A 179 ? 0.5179 0.3217 0.8648 0.0061  0.0680  -0.1650 1089 LEU A N   
1359 C CA  . LEU A 179 ? 0.5954 0.4043 0.9339 -0.0124 0.0441  -0.1745 1089 LEU A CA  
1360 C C   . LEU A 179 ? 0.6655 0.4315 0.9557 -0.0102 0.0324  -0.1929 1089 LEU A C   
1361 O O   . LEU A 179 ? 0.7211 0.4818 0.9902 -0.0145 0.0198  -0.2038 1089 LEU A O   
1362 C CB  . LEU A 179 ? 0.4721 0.3110 0.8401 -0.0304 0.0313  -0.1633 1089 LEU A CB  
1363 C CG  . LEU A 179 ? 0.4019 0.2808 0.8124 -0.0315 0.0390  -0.1454 1089 LEU A CG  
1364 C CD1 . LEU A 179 ? 0.3861 0.2868 0.8140 -0.0412 0.0295  -0.1357 1089 LEU A CD1 
1365 C CD2 . LEU A 179 ? 0.3523 0.2579 0.7756 -0.0339 0.0357  -0.1417 1089 LEU A CD2 
1366 N N   . ASP A 180 ? 0.7396 0.4737 1.0104 -0.0038 0.0344  -0.1961 1090 ASP A N   
1367 C CA  . ASP A 180 ? 0.7752 0.4585 0.9940 0.0032  0.0244  -0.2130 1090 ASP A CA  
1368 C C   . ASP A 180 ? 0.9803 0.6574 1.1908 -0.0194 -0.0039 -0.2179 1090 ASP A C   
1369 O O   . ASP A 180 ? 0.9334 0.6389 1.1586 -0.0347 -0.0170 -0.2156 1090 ASP A O   
1370 C CB  . ASP A 180 ? 0.8002 0.4612 0.9796 0.0227  0.0312  -0.2264 1090 ASP A CB  
1371 N N   . ASN A 181 ? 1.0835 0.7233 1.2698 -0.0204 -0.0130 -0.2229 1091 ASN A N   
1372 C CA  . ASN A 181 ? 1.1390 0.7680 1.3161 -0.0412 -0.0389 -0.2253 1091 ASN A CA  
1373 C C   . ASN A 181 ? 1.2099 0.7799 1.3424 -0.0349 -0.0464 -0.2366 1091 ASN A C   
1374 O O   . ASN A 181 ? 1.2215 0.7482 1.3043 -0.0188 -0.0464 -0.2524 1091 ASN A O   
1375 C CB  . ASN A 181 ? 1.1239 0.7969 1.3497 -0.0606 -0.0437 -0.2070 1091 ASN A CB  
1376 N N   . GLY A 184 ? 1.3257 0.9164 1.5047 -0.0892 -0.0878 -0.2151 1094 GLY A N   
1377 C CA  . GLY A 184 ? 1.3533 0.9221 1.5338 -0.0887 -0.0853 -0.2115 1094 GLY A CA  
1378 C C   . GLY A 184 ? 1.3332 0.9215 1.5387 -0.0750 -0.0623 -0.2023 1094 GLY A C   
1379 O O   . GLY A 184 ? 1.3914 0.9449 1.5718 -0.0561 -0.0495 -0.2095 1094 GLY A O   
1380 N N   . GLU A 185 ? 1.0853 0.7301 1.3391 -0.0828 -0.0566 -0.1856 1095 GLU A N   
1381 C CA  . GLU A 185 ? 0.8812 0.5522 1.1648 -0.0721 -0.0358 -0.1752 1095 GLU A CA  
1382 C C   . GLU A 185 ? 0.8017 0.4941 1.0923 -0.0591 -0.0196 -0.1765 1095 GLU A C   
1383 O O   . GLU A 185 ? 0.8123 0.5293 1.1098 -0.0650 -0.0249 -0.1763 1095 GLU A O   
1384 C CB  . GLU A 185 ? 0.7688 0.4875 1.0972 -0.0845 -0.0375 -0.1569 1095 GLU A CB  
1385 C CG  . GLU A 185 ? 0.6924 0.4124 1.0383 -0.0795 -0.0267 -0.1485 1095 GLU A CG  
1386 C CD  . GLU A 185 ? 0.5824 0.3395 0.9626 -0.0914 -0.0327 -0.1324 1095 GLU A CD  
1387 O OE1 . GLU A 185 ? 0.4840 0.2869 0.8938 -0.0891 -0.0252 -0.1213 1095 GLU A OE1 
1388 O OE2 . GLU A 185 ? 0.6025 0.3407 0.9773 -0.1022 -0.0456 -0.1311 1095 GLU A OE2 
1389 N N   . VAL A 186 ? 0.7331 0.4179 1.0240 -0.0414 0.0008  -0.1758 1096 VAL A N   
1390 C CA  . VAL A 186 ? 0.6534 0.3473 0.9440 -0.0258 0.0183  -0.1775 1096 VAL A CA  
1391 C C   . VAL A 186 ? 0.5941 0.3340 0.9312 -0.0241 0.0348  -0.1606 1096 VAL A C   
1392 O O   . VAL A 186 ? 0.5665 0.3074 0.9168 -0.0202 0.0435  -0.1527 1096 VAL A O   
1393 C CB  . VAL A 186 ? 0.7326 0.3769 0.9788 -0.0020 0.0300  -0.1891 1096 VAL A CB  
1394 C CG1 . VAL A 186 ? 0.6536 0.3163 0.9112 0.0173  0.0554  -0.1826 1096 VAL A CG1 
1395 C CG2 . VAL A 186 ? 0.8638 0.4645 1.0594 -0.0006 0.0136  -0.2077 1096 VAL A CG2 
1396 N N   . TYR A 187 ? 0.4059 0.3515 0.8330 0.0244  0.1040  -0.1155 1097 TYR A N   
1397 C CA  . TYR A 187 ? 0.4149 0.3694 0.8511 0.0243  0.1032  -0.1013 1097 TYR A CA  
1398 C C   . TYR A 187 ? 0.4060 0.3686 0.8324 0.0280  0.1071  -0.0985 1097 TYR A C   
1399 O O   . TYR A 187 ? 0.4341 0.3970 0.8438 0.0298  0.1099  -0.1063 1097 TYR A O   
1400 C CB  . TYR A 187 ? 0.3124 0.2730 0.7483 0.0185  0.0940  -0.0943 1097 TYR A CB  
1401 C CG  . TYR A 187 ? 0.3396 0.2948 0.7907 0.0153  0.0912  -0.0917 1097 TYR A CG  
1402 C CD1 . TYR A 187 ? 0.3584 0.3129 0.8284 0.0168  0.0925  -0.0819 1097 TYR A CD1 
1403 C CD2 . TYR A 187 ? 0.3594 0.3103 0.8075 0.0108  0.0871  -0.0985 1097 TYR A CD2 
1404 C CE1 . TYR A 187 ? 0.3512 0.3010 0.8359 0.0140  0.0902  -0.0781 1097 TYR A CE1 
1405 C CE2 . TYR A 187 ? 0.3973 0.3439 0.8617 0.0076  0.0847  -0.0947 1097 TYR A CE2 
1406 C CZ  . TYR A 187 ? 0.3722 0.3183 0.8545 0.0092  0.0865  -0.0841 1097 TYR A CZ  
1407 O OH  . TYR A 187 ? 0.3012 0.2434 0.8003 0.0059  0.0841  -0.0788 1097 TYR A OH  
1408 N N   . CYS A 188 ? 0.2949 0.2641 0.7327 0.0291  0.1069  -0.0864 1098 CYS A N   
1409 C CA  . CYS A 188 ? 0.3423 0.3195 0.7771 0.0323  0.1104  -0.0812 1098 CYS A CA  
1410 C C   . CYS A 188 ? 0.3115 0.2973 0.7503 0.0297  0.1022  -0.0700 1098 CYS A C   
1411 O O   . CYS A 188 ? 0.3229 0.3089 0.7701 0.0272  0.0957  -0.0648 1098 CYS A O   
1412 C CB  . CYS A 188 ? 0.2988 0.2748 0.7482 0.0384  0.1203  -0.0784 1098 CYS A CB  
1413 S SG  . CYS A 188 ? 0.3702 0.3375 0.8115 0.0438  0.1306  -0.0931 1098 CYS A SG  
1414 N N   . ILE A 189 ? 0.2943 0.2875 0.7273 0.0308  0.1023  -0.0661 1099 ILE A N   
1415 C CA  . ILE A 189 ? 0.2588 0.2595 0.6987 0.0296  0.0945  -0.0557 1099 ILE A CA  
1416 C C   . ILE A 189 ? 0.3162 0.3207 0.7720 0.0337  0.1006  -0.0473 1099 ILE A C   
1417 O O   . ILE A 189 ? 0.3643 0.3724 0.8155 0.0362  0.1074  -0.0473 1099 ILE A O   
1418 C CB  . ILE A 189 ? 0.2543 0.2606 0.6783 0.0269  0.0877  -0.0567 1099 ILE A CB  
1419 C CG1 . ILE A 189 ? 0.3155 0.3194 0.7253 0.0229  0.0813  -0.0645 1099 ILE A CG1 
1420 C CG2 . ILE A 189 ? 0.2423 0.2553 0.6758 0.0266  0.0791  -0.0466 1099 ILE A CG2 
1421 C CD1 . ILE A 189 ? 0.2475 0.2574 0.6442 0.0206  0.0731  -0.0646 1099 ILE A CD1 
1422 N N   . ASP A 190 ? 0.2684 0.2730 0.7432 0.0347  0.0983  -0.0394 1100 ASP A N   
1423 C CA  . ASP A 190 ? 0.2763 0.2854 0.7695 0.0383  0.1027  -0.0303 1100 ASP A CA  
1424 C C   . ASP A 190 ? 0.2403 0.2561 0.7399 0.0366  0.0917  -0.0212 1100 ASP A C   
1425 O O   . ASP A 190 ? 0.2326 0.2481 0.7393 0.0355  0.0822  -0.0173 1100 ASP A O   
1426 C CB  . ASP A 190 ? 0.2925 0.2972 0.8050 0.0412  0.1071  -0.0274 1100 ASP A CB  
1427 C CG  . ASP A 190 ? 0.2593 0.2677 0.7840 0.0435  0.1129  -0.0187 1100 ASP A CG  
1428 O OD1 . ASP A 190 ? 0.2643 0.2802 0.7901 0.0446  0.1147  -0.0144 1100 ASP A OD1 
1429 O OD2 . ASP A 190 ? 0.2833 0.2876 0.8177 0.0440  0.1154  -0.0155 1100 ASP A OD2 
1430 N N   . ALA A 191 ? 0.2402 0.2622 0.7374 0.0368  0.0925  -0.0178 1101 ALA A N   
1431 C CA  . ALA A 191 ? 0.2308 0.2587 0.7363 0.0354  0.0817  -0.0093 1101 ALA A CA  
1432 C C   . ALA A 191 ? 0.2283 0.2605 0.7606 0.0380  0.0828  0.0021  1101 ALA A C   
1433 O O   . ALA A 191 ? 0.2230 0.2596 0.7638 0.0366  0.0739  0.0098  1101 ALA A O   
1434 C CB  . ALA A 191 ? 0.2323 0.2647 0.7242 0.0337  0.0808  -0.0102 1101 ALA A CB  
1435 N N   . ARG A 192 ? 0.2359 0.2645 0.7750 0.0397  0.0915  0.0035  1102 ARG A N   
1436 C CA  . ARG A 192 ? 0.2389 0.2691 0.7945 0.0397  0.0920  0.0147  1102 ARG A CA  
1437 C C   . ARG A 192 ? 0.2325 0.2606 0.7957 0.0366  0.0769  0.0210  1102 ARG A C   
1438 O O   . ARG A 192 ? 0.2306 0.2619 0.8047 0.0352  0.0700  0.0297  1102 ARG A O   
1439 C CB  . ARG A 192 ? 0.2496 0.2759 0.8092 0.0424  0.1042  0.0135  1102 ARG A CB  
1440 C CG  . ARG A 192 ? 0.2866 0.3118 0.8636 0.0416  0.1015  0.0236  1102 ARG A CG  
1441 C CD  . ARG A 192 ? 0.3187 0.3509 0.9087 0.0421  0.1039  0.0342  1102 ARG A CD  
1442 N NE  . ARG A 192 ? 0.3479 0.3789 0.9554 0.0408  0.1002  0.0437  1102 ARG A NE  
1443 C CZ  . ARG A 192 ? 0.3557 0.3869 0.9727 0.0372  0.0864  0.0511  1102 ARG A CZ  
1444 N NH1 . ARG A 192 ? 0.2417 0.2738 0.8519 0.0347  0.0744  0.0498  1102 ARG A NH1 
1445 N NH2 . ARG A 192 ? 0.3267 0.3570 0.9603 0.0362  0.0841  0.0593  1102 ARG A NH2 
1446 N N   . TYR A 193 ? 0.2308 0.2537 0.7891 0.0358  0.0719  0.0170  1103 TYR A N   
1447 C CA  . TYR A 193 ? 0.2267 0.2483 0.7894 0.0339  0.0579  0.0220  1103 TYR A CA  
1448 C C   . TYR A 193 ? 0.2191 0.2426 0.7708 0.0331  0.0451  0.0184  1103 TYR A C   
1449 O O   . TYR A 193 ? 0.2169 0.2411 0.7717 0.0321  0.0321  0.0227  1103 TYR A O   
1450 C CB  . TYR A 193 ? 0.2300 0.2465 0.7941 0.0342  0.0594  0.0212  1103 TYR A CB  
1451 C CG  . TYR A 193 ? 0.2383 0.2529 0.8141 0.0353  0.0708  0.0245  1103 TYR A CG  
1452 C CD1 . TYR A 193 ? 0.2408 0.2572 0.8323 0.0347  0.0689  0.0339  1103 TYR A CD1 
1453 C CD2 . TYR A 193 ? 0.2486 0.2593 0.8203 0.0371  0.0830  0.0178  1103 TYR A CD2 
1454 C CE1 . TYR A 193 ? 0.2684 0.2838 0.8714 0.0363  0.0796  0.0369  1103 TYR A CE1 
1455 C CE2 . TYR A 193 ? 0.2571 0.2661 0.8388 0.0390  0.0931  0.0199  1103 TYR A CE2 
1456 C CZ  . TYR A 193 ? 0.3102 0.3220 0.9077 0.0387  0.0917  0.0298  1103 TYR A CZ  
1457 O OH  . TYR A 193 ? 0.3640 0.3748 0.9720 0.0411  0.1019  0.0320  1103 TYR A OH  
1458 N N   . TYR A 194 ? 0.2164 0.2404 0.7550 0.0337  0.0482  0.0098  1104 TYR A N   
1459 C CA  . TYR A 194 ? 0.2099 0.2362 0.7372 0.0334  0.0371  0.0052  1104 TYR A CA  
1460 C C   . TYR A 194 ? 0.2079 0.2378 0.7288 0.0336  0.0422  -0.0001 1104 TYR A C   
1461 O O   . TYR A 194 ? 0.2137 0.2410 0.7241 0.0329  0.0535  -0.0058 1104 TYR A O   
1462 C CB  . TYR A 194 ? 0.2086 0.2328 0.7269 0.0341  0.0350  0.0001  1104 TYR A CB  
1463 C CG  . TYR A 194 ? 0.2135 0.2353 0.7376 0.0345  0.0299  0.0058  1104 TYR A CG  
1464 C CD1 . TYR A 194 ? 0.2572 0.2811 0.7793 0.0354  0.0155  0.0088  1104 TYR A CD1 
1465 C CD2 . TYR A 194 ? 0.2164 0.2339 0.7475 0.0345  0.0388  0.0076  1104 TYR A CD2 
1466 C CE1 . TYR A 194 ? 0.2125 0.2352 0.7391 0.0365  0.0106  0.0140  1104 TYR A CE1 
1467 C CE2 . TYR A 194 ? 0.2189 0.2348 0.7562 0.0350  0.0338  0.0136  1104 TYR A CE2 
1468 C CZ  . TYR A 194 ? 0.2169 0.2358 0.7516 0.0361  0.0198  0.0169  1104 TYR A CZ  
1469 O OH  . TYR A 194 ? 0.3048 0.3229 0.8447 0.0373  0.0145  0.0229  1104 TYR A OH  
1470 N N   . GLY A 195 ? 0.2043 0.2378 0.7242 0.0326  0.0329  0.0018  1105 GLY A N   
1471 C CA  . GLY A 195 ? 0.2067 0.2421 0.7134 0.0306  0.0370  -0.0016 1105 GLY A CA  
1472 C C   . GLY A 195 ? 0.2021 0.2402 0.7052 0.0294  0.0231  -0.0013 1105 GLY A C   
1473 O O   . GLY A 195 ? 0.1977 0.2367 0.7122 0.0307  0.0105  0.0024  1105 GLY A O   
1474 N N   . ASN A 196 ? 0.2186 0.2577 0.7056 0.0273  0.0246  -0.0059 1106 ASN A N   
1475 C CA  . ASN A 196 ? 0.2045 0.2461 0.6899 0.0262  0.0125  -0.0051 1106 ASN A CA  
1476 C C   . ASN A 196 ? 0.2358 0.2814 0.7315 0.0253  0.0176  0.0032  1106 ASN A C   
1477 O O   . ASN A 196 ? 0.2501 0.2975 0.7597 0.0264  0.0280  0.0101  1106 ASN A O   
1478 C CB  . ASN A 196 ? 0.2009 0.2416 0.6623 0.0246  0.0088  -0.0152 1106 ASN A CB  
1479 C CG  . ASN A 196 ? 0.2218 0.2626 0.6681 0.0227  0.0196  -0.0188 1106 ASN A CG  
1480 O OD1 . ASN A 196 ? 0.2129 0.2538 0.6624 0.0232  0.0324  -0.0162 1106 ASN A OD1 
1481 N ND2 . ASN A 196 ? 0.2069 0.2481 0.6362 0.0210  0.0140  -0.0254 1106 ASN A ND2 
1482 N N   . ILE A 197 ? 0.2290 0.2765 0.7186 0.0235  0.0105  0.0032  1107 ILE A N   
1483 C CA  . ILE A 197 ? 0.2246 0.2767 0.7255 0.0225  0.0139  0.0131  1107 ILE A CA  
1484 C C   . ILE A 197 ? 0.2326 0.2869 0.7216 0.0227  0.0317  0.0127  1107 ILE A C   
1485 O O   . ILE A 197 ? 0.2212 0.2809 0.7221 0.0233  0.0402  0.0227  1107 ILE A O   
1486 C CB  . ILE A 197 ? 0.2058 0.2586 0.7036 0.0206  0.0003  0.0131  1107 ILE A CB  
1487 C CG1 . ILE A 197 ? 0.2098 0.2681 0.7218 0.0192  0.0029  0.0255  1107 ILE A CG1 
1488 C CG2 . ILE A 197 ? 0.2073 0.2580 0.6768 0.0195  0.0001  0.0014  1107 ILE A CG2 
1489 C CD1 . ILE A 197 ? 0.2223 0.2832 0.7655 0.0197  -0.0007 0.0376  1107 ILE A CD1 
1490 N N   . SER A 198 ? 0.2196 0.2701 0.6854 0.0226  0.0374  0.0013  1108 SER A N   
1491 C CA  . SER A 198 ? 0.2415 0.2927 0.6928 0.0236  0.0529  -0.0019 1108 SER A CA  
1492 C C   . SER A 198 ? 0.2355 0.2891 0.7008 0.0268  0.0668  0.0042  1108 SER A C   
1493 O O   . SER A 198 ? 0.2459 0.3032 0.7047 0.0288  0.0793  0.0058  1108 SER A O   
1494 C CB  . SER A 198 ? 0.2321 0.2775 0.6620 0.0231  0.0548  -0.0155 1108 SER A CB  
1495 O OG  . SER A 198 ? 0.2526 0.2968 0.6695 0.0206  0.0431  -0.0215 1108 SER A OG  
1496 N N   . ARG A 199 ? 0.2298 0.2817 0.7133 0.0281  0.0651  0.0071  1109 ARG A N   
1497 C CA  . ARG A 199 ? 0.2353 0.2892 0.7323 0.0315  0.0787  0.0118  1109 ARG A CA  
1498 C C   . ARG A 199 ? 0.2394 0.3024 0.7521 0.0328  0.0850  0.0251  1109 ARG A C   
1499 O O   . ARG A 199 ? 0.2471 0.3139 0.7668 0.0365  0.0993  0.0287  1109 ARG A O   
1500 C CB  . ARG A 199 ? 0.2282 0.2788 0.7437 0.0325  0.0740  0.0137  1109 ARG A CB  
1501 C CG  . ARG A 199 ? 0.2508 0.3055 0.7919 0.0319  0.0636  0.0254  1109 ARG A CG  
1502 C CD  . ARG A 199 ? 0.2321 0.2825 0.7856 0.0325  0.0541  0.0251  1109 ARG A CD  
1503 N NE  . ARG A 199 ? 0.2782 0.3258 0.8396 0.0342  0.0637  0.0279  1109 ARG A NE  
1504 C CZ  . ARG A 199 ? 0.2241 0.2728 0.8016 0.0338  0.0657  0.0386  1109 ARG A CZ  
1505 N NH1 . ARG A 199 ? 0.2237 0.2763 0.8135 0.0318  0.0594  0.0485  1109 ARG A NH1 
1506 N NH2 . ARG A 199 ? 0.2301 0.2755 0.8125 0.0353  0.0739  0.0397  1109 ARG A NH2 
1507 N N   . PHE A 200 ? 0.2355 0.3024 0.7542 0.0300  0.0751  0.0325  1110 PHE A N   
1508 C CA  . PHE A 200 ? 0.2391 0.3155 0.7755 0.0304  0.0798  0.0472  1110 PHE A CA  
1509 C C   . PHE A 200 ? 0.2534 0.3350 0.7709 0.0308  0.0885  0.0481  1110 PHE A C   
1510 O O   . PHE A 200 ? 0.2552 0.3463 0.7858 0.0316  0.0949  0.0615  1110 PHE A O   
1511 C CB  . PHE A 200 ? 0.2298 0.3073 0.7877 0.0272  0.0627  0.0561  1110 PHE A CB  
1512 C CG  . PHE A 200 ? 0.2213 0.2954 0.8008 0.0276  0.0539  0.0576  1110 PHE A CG  
1513 C CD1 . PHE A 200 ? 0.2233 0.3011 0.8263 0.0294  0.0608  0.0677  1110 PHE A CD1 
1514 C CD2 . PHE A 200 ? 0.2137 0.2804 0.7872 0.0264  0.0385  0.0489  1110 PHE A CD2 
1515 C CE1 . PHE A 200 ? 0.2463 0.3148 0.8555 0.0277  0.0508  0.0685  1110 PHE A CE1 
1516 C CE2 . PHE A 200 ? 0.2111 0.2720 0.7956 0.0262  0.0296  0.0501  1110 PHE A CE2 
1517 C CZ  . PHE A 200 ? 0.2252 0.2855 0.8247 0.0261  0.0352  0.0596  1110 PHE A CZ  
1518 N N   . ILE A 201 ? 0.2540 0.3303 0.7420 0.0302  0.0882  0.0351  1111 ILE A N   
1519 C CA  . ILE A 201 ? 0.2660 0.3466 0.7330 0.0309  0.0958  0.0347  1111 ILE A CA  
1520 C C   . ILE A 201 ? 0.2800 0.3660 0.7427 0.0366  0.1154  0.0358  1111 ILE A C   
1521 O O   . ILE A 201 ? 0.2842 0.3646 0.7374 0.0395  0.1225  0.0248  1111 ILE A O   
1522 C CB  . ILE A 201 ? 0.2695 0.3426 0.7075 0.0290  0.0897  0.0196  1111 ILE A CB  
1523 C CG1 . ILE A 201 ? 0.2710 0.3407 0.7125 0.0244  0.0709  0.0189  1111 ILE A CG1 
1524 C CG2 . ILE A 201 ? 0.2966 0.3738 0.7110 0.0309  0.0989  0.0178  1111 ILE A CG2 
1525 C CD1 . ILE A 201 ? 0.2539 0.3167 0.6699 0.0225  0.0641  0.0039  1111 ILE A CD1 
1526 N N   . ASN A 202 ? 0.2962 0.3932 0.7659 0.0386  0.1241  0.0493  1112 ASN A N   
1527 C CA  . ASN A 202 ? 0.3036 0.4079 0.7700 0.0452  0.1435  0.0517  1112 ASN A CA  
1528 C C   . ASN A 202 ? 0.3198 0.4224 0.7505 0.0485  0.1513  0.0394  1112 ASN A C   
1529 O O   . ASN A 202 ? 0.3354 0.4322 0.7456 0.0451  0.1418  0.0310  1112 ASN A O   
1530 C CB  . ASN A 202 ? 0.3076 0.4265 0.7957 0.0465  0.1506  0.0721  1112 ASN A CB  
1531 C CG  . ASN A 202 ? 0.3018 0.4229 0.8282 0.0445  0.1452  0.0840  1112 ASN A CG  
1532 O OD1 . ASN A 202 ? 0.3001 0.4169 0.8371 0.0466  0.1477  0.0790  1112 ASN A OD1 
1533 N ND2 . ASN A 202 ? 0.2887 0.4164 0.8373 0.0404  0.1368  0.0999  1112 ASN A ND2 
1534 N N   . HIS A 203 ? 0.3356 0.4437 0.7594 0.0558  0.1685  0.0383  1113 HIS A N   
1535 C CA  . HIS A 203 ? 0.3883 0.4954 0.7784 0.0607  0.1772  0.0265  1113 HIS A CA  
1536 C C   . HIS A 203 ? 0.4062 0.5266 0.7876 0.0629  0.1840  0.0393  1113 HIS A C   
1537 O O   . HIS A 203 ? 0.3874 0.5206 0.7888 0.0655  0.1933  0.0561  1113 HIS A O   
1538 C CB  . HIS A 203 ? 0.4469 0.5529 0.8332 0.0688  0.1922  0.0175  1113 HIS A CB  
1539 C CG  . HIS A 203 ? 0.4727 0.5815 0.8273 0.0762  0.2038  0.0084  1113 HIS A CG  
1540 N ND1 . HIS A 203 ? 0.4818 0.5787 0.8111 0.0780  0.2019  -0.0119 1113 HIS A ND1 
1541 C CD2 . HIS A 203 ? 0.5167 0.6389 0.8607 0.0828  0.2171  0.0169  1113 HIS A CD2 
1542 C CE1 . HIS A 203 ? 0.5161 0.6181 0.8196 0.0855  0.2126  -0.0169 1113 HIS A CE1 
1543 N NE2 . HIS A 203 ? 0.5259 0.6437 0.8365 0.0888  0.2224  0.0006  1113 HIS A NE2 
1544 N N   . LEU A 204 ? 0.4247 0.5427 0.7772 0.0620  0.1797  0.0320  1114 LEU A N   
1545 C CA  . LEU A 204 ? 0.4639 0.5942 0.8028 0.0650  0.1867  0.0429  1114 LEU A CA  
1546 C C   . LEU A 204 ? 0.5106 0.6390 0.8120 0.0718  0.1951  0.0278  1114 LEU A C   
1547 O O   . LEU A 204 ? 0.5395 0.6554 0.8209 0.0696  0.1860  0.0103  1114 LEU A O   
1548 C CB  . LEU A 204 ? 0.4439 0.5744 0.7849 0.0572  0.1715  0.0514  1114 LEU A CB  
1549 C CG  . LEU A 204 ? 0.3630 0.4952 0.7407 0.0507  0.1611  0.0664  1114 LEU A CG  
1550 C CD1 . LEU A 204 ? 0.3781 0.5122 0.7558 0.0449  0.1483  0.0755  1114 LEU A CD1 
1551 C CD2 . LEU A 204 ? 0.4723 0.6178 0.8770 0.0545  0.1743  0.0839  1114 LEU A CD2 
1552 N N   . CYS A 205 ? 0.5459 0.6872 0.8380 0.0805  0.2120  0.0347  1115 CYS A N   
1553 C CA  . CYS A 205 ? 0.6180 0.7583 0.8724 0.0883  0.2196  0.0205  1115 CYS A CA  
1554 C C   . CYS A 205 ? 0.6212 0.7588 0.8504 0.0843  0.2082  0.0173  1115 CYS A C   
1555 O O   . CYS A 205 ? 0.6684 0.7988 0.8667 0.0878  0.2068  -0.0001 1115 CYS A O   
1556 C CB  . CYS A 205 ? 0.6962 0.8532 0.9455 0.0993  0.2403  0.0304  1115 CYS A CB  
1557 S SG  . CYS A 205 ? 0.7600 0.9172 1.0265 0.1076  0.2554  0.0245  1115 CYS A SG  
1558 N N   . ASP A 206 ? 0.5730 0.7157 0.8161 0.0771  0.1990  0.0335  1116 ASP A N   
1559 C CA  . ASP A 206 ? 0.5486 0.6880 0.7731 0.0722  0.1859  0.0316  1116 ASP A CA  
1560 C C   . ASP A 206 ? 0.5164 0.6444 0.7595 0.0617  0.1669  0.0289  1116 ASP A C   
1561 O O   . ASP A 206 ? 0.4952 0.6274 0.7571 0.0558  0.1583  0.0440  1116 ASP A O   
1562 C CB  . ASP A 206 ? 0.6127 0.7678 0.8367 0.0732  0.1905  0.0531  1116 ASP A CB  
1563 C CG  . ASP A 206 ? 0.5777 0.7303 0.7766 0.0703  0.1793  0.0500  1116 ASP A CG  
1564 O OD1 . ASP A 206 ? 0.5160 0.6551 0.6984 0.0676  0.1683  0.0310  1116 ASP A OD1 
1565 O OD2 . ASP A 206 ? 0.6777 0.8422 0.8744 0.0708  0.1816  0.0674  1116 ASP A OD2 
1566 N N   . PRO A 207 ? 0.4930 0.6071 0.7321 0.0596  0.1598  0.0102  1117 PRO A N   
1567 C CA  . PRO A 207 ? 0.4620 0.5669 0.7211 0.0510  0.1439  0.0083  1117 PRO A CA  
1568 C C   . PRO A 207 ? 0.4200 0.5231 0.6726 0.0448  0.1285  0.0103  1117 PRO A C   
1569 O O   . PRO A 207 ? 0.4584 0.5633 0.6860 0.0463  0.1277  0.0074  1117 PRO A O   
1570 C CB  . PRO A 207 ? 0.4026 0.4944 0.6527 0.0515  0.1421  -0.0124 1117 PRO A CB  
1571 C CG  . PRO A 207 ? 0.4493 0.5409 0.6684 0.0584  0.1509  -0.0241 1117 PRO A CG  
1572 C CD  . PRO A 207 ? 0.4948 0.6010 0.7118 0.0653  0.1660  -0.0098 1117 PRO A CD  
1573 N N   . ASN A 208 ? 0.3676 0.4671 0.6434 0.0383  0.1155  0.0150  1118 ASN A N   
1574 C CA  . ASN A 208 ? 0.4078 0.5039 0.6806 0.0324  0.0992  0.0146  1118 ASN A CA  
1575 C C   . ASN A 208 ? 0.3588 0.4436 0.6361 0.0279  0.0862  0.0011  1118 ASN A C   
1576 O O   . ASN A 208 ? 0.3945 0.4767 0.6745 0.0232  0.0718  0.0011  1118 ASN A O   
1577 C CB  . ASN A 208 ? 0.3718 0.4758 0.6683 0.0293  0.0937  0.0348  1118 ASN A CB  
1578 C CG  . ASN A 208 ? 0.3510 0.4552 0.6812 0.0275  0.0921  0.0431  1118 ASN A CG  
1579 O OD1 . ASN A 208 ? 0.3481 0.4446 0.6849 0.0268  0.0894  0.0328  1118 ASN A OD1 
1580 N ND2 . ASN A 208 ? 0.3626 0.4759 0.7156 0.0267  0.0930  0.0627  1118 ASN A ND2 
1581 N N   . ILE A 209 ? 0.3381 0.4168 0.6175 0.0294  0.0910  -0.0094 1119 ILE A N   
1582 C CA  . ILE A 209 ? 0.3249 0.3938 0.6048 0.0259  0.0808  -0.0228 1119 ILE A CA  
1583 C C   . ILE A 209 ? 0.3625 0.4252 0.6275 0.0291  0.0892  -0.0377 1119 ILE A C   
1584 O O   . ILE A 209 ? 0.3920 0.4572 0.6546 0.0343  0.1029  -0.0369 1119 ILE A O   
1585 C CB  . ILE A 209 ? 0.3055 0.3725 0.6133 0.0231  0.0740  -0.0176 1119 ILE A CB  
1586 C CG1 . ILE A 209 ? 0.3267 0.3942 0.6490 0.0266  0.0857  -0.0152 1119 ILE A CG1 
1587 C CG2 . ILE A 209 ? 0.3485 0.4210 0.6744 0.0205  0.0653  -0.0030 1119 ILE A CG2 
1588 C CD1 . ILE A 209 ? 0.2880 0.3529 0.6356 0.0242  0.0780  -0.0115 1119 ILE A CD1 
1589 N N   . ILE A 210 ? 0.3331 0.3877 0.5890 0.0261  0.0809  -0.0512 1120 ILE A N   
1590 C CA  . ILE A 210 ? 0.3379 0.3852 0.5829 0.0284  0.0866  -0.0657 1120 ILE A CA  
1591 C C   . ILE A 210 ? 0.3218 0.3624 0.5795 0.0245  0.0793  -0.0719 1120 ILE A C   
1592 O O   . ILE A 210 ? 0.3296 0.3705 0.5945 0.0203  0.0676  -0.0697 1120 ILE A O   
1593 C CB  . ILE A 210 ? 0.3834 0.4281 0.6008 0.0293  0.0853  -0.0771 1120 ILE A CB  
1594 C CG1 . ILE A 210 ? 0.3599 0.4042 0.5722 0.0240  0.0707  -0.0788 1120 ILE A CG1 
1595 C CG2 . ILE A 210 ? 0.3747 0.4263 0.5769 0.0351  0.0957  -0.0721 1120 ILE A CG2 
1596 C CD1 . ILE A 210 ? 0.4748 0.5161 0.6619 0.0244  0.0676  -0.0904 1120 ILE A CD1 
1597 N N   . PRO A 211 ? 0.3245 0.3592 0.5858 0.0264  0.0856  -0.0793 1121 PRO A N   
1598 C CA  . PRO A 211 ? 0.3256 0.3544 0.5978 0.0229  0.0791  -0.0846 1121 PRO A CA  
1599 C C   . PRO A 211 ? 0.3463 0.3690 0.6033 0.0204  0.0733  -0.0983 1121 PRO A C   
1600 O O   . PRO A 211 ? 0.3569 0.3764 0.5970 0.0227  0.0775  -0.1074 1121 PRO A O   
1601 C CB  . PRO A 211 ? 0.3359 0.3615 0.6208 0.0264  0.0894  -0.0844 1121 PRO A CB  
1602 C CG  . PRO A 211 ? 0.3346 0.3607 0.6047 0.0320  0.1008  -0.0885 1121 PRO A CG  
1603 C CD  . PRO A 211 ? 0.3404 0.3742 0.5978 0.0325  0.0995  -0.0821 1121 PRO A CD  
1604 N N   . VAL A 212 ? 0.3527 0.3744 0.6163 0.0159  0.0632  -0.0997 1122 VAL A N   
1605 C CA  . VAL A 212 ? 0.3187 0.3358 0.5732 0.0127  0.0569  -0.1110 1122 VAL A CA  
1606 C C   . VAL A 212 ? 0.2928 0.3067 0.5628 0.0106  0.0553  -0.1120 1122 VAL A C   
1607 O O   . VAL A 212 ? 0.2942 0.3114 0.5789 0.0103  0.0530  -0.1035 1122 VAL A O   
1608 C CB  . VAL A 212 ? 0.3356 0.3572 0.5820 0.0095  0.0457  -0.1107 1122 VAL A CB  
1609 C CG1 . VAL A 212 ? 0.3135 0.3315 0.5523 0.0062  0.0394  -0.1220 1122 VAL A CG1 
1610 C CG2 . VAL A 212 ? 0.3258 0.3515 0.5586 0.0116  0.0469  -0.1071 1122 VAL A CG2 
1611 N N   . ARG A 213 ? 0.2996 0.3070 0.5669 0.0093  0.0558  -0.1220 1123 ARG A N   
1612 C CA  . ARG A 213 ? 0.2910 0.2956 0.5730 0.0070  0.0542  -0.1221 1123 ARG A CA  
1613 C C   . ARG A 213 ? 0.3043 0.3131 0.5856 0.0027  0.0440  -0.1231 1123 ARG A C   
1614 O O   . ARG A 213 ? 0.3090 0.3172 0.5788 0.0006  0.0394  -0.1307 1123 ARG A O   
1615 C CB  . ARG A 213 ? 0.3140 0.3095 0.5971 0.0074  0.0593  -0.1314 1123 ARG A CB  
1616 C CG  . ARG A 213 ? 0.3955 0.3864 0.6708 0.0126  0.0686  -0.1360 1123 ARG A CG  
1617 C CD  . ARG A 213 ? 0.3755 0.3700 0.6607 0.0165  0.0762  -0.1258 1123 ARG A CD  
1618 N NE  . ARG A 213 ? 0.4568 0.4450 0.7462 0.0211  0.0860  -0.1299 1123 ARG A NE  
1619 C CZ  . ARG A 213 ? 0.5162 0.5063 0.8006 0.0269  0.0953  -0.1283 1123 ARG A CZ  
1620 N NH1 . ARG A 213 ? 0.5033 0.5016 0.7790 0.0283  0.0963  -0.1215 1123 ARG A NH1 
1621 N NH2 . ARG A 213 ? 0.5256 0.5099 0.8151 0.0317  0.1039  -0.1331 1123 ARG A NH2 
1622 N N   . VAL A 214 ? 0.2868 0.3004 0.5803 0.0019  0.0402  -0.1157 1124 VAL A N   
1623 C CA  . VAL A 214 ? 0.3054 0.3251 0.5985 -0.0007 0.0311  -0.1155 1124 VAL A CA  
1624 C C   . VAL A 214 ? 0.3086 0.3292 0.6150 -0.0021 0.0307  -0.1131 1124 VAL A C   
1625 O O   . VAL A 214 ? 0.2486 0.2664 0.5661 -0.0006 0.0359  -0.1084 1124 VAL A O   
1626 C CB  . VAL A 214 ? 0.2707 0.2974 0.5634 0.0008  0.0250  -0.1086 1124 VAL A CB  
1627 C CG1 . VAL A 214 ? 0.3052 0.3381 0.5936 -0.0010 0.0154  -0.1111 1124 VAL A CG1 
1628 C CG2 . VAL A 214 ? 0.2568 0.2828 0.5406 0.0025  0.0273  -0.1074 1124 VAL A CG2 
1629 N N   . PHE A 215 ? 0.2632 0.2886 0.5687 -0.0048 0.0245  -0.1154 1125 PHE A N   
1630 C CA  . PHE A 215 ? 0.2389 0.2681 0.5559 -0.0059 0.0237  -0.1116 1125 PHE A CA  
1631 C C   . PHE A 215 ? 0.2608 0.3005 0.5757 -0.0050 0.0160  -0.1086 1125 PHE A C   
1632 O O   . PHE A 215 ? 0.2780 0.3211 0.5837 -0.0058 0.0105  -0.1130 1125 PHE A O   
1633 C CB  . PHE A 215 ? 0.2834 0.3086 0.6042 -0.0099 0.0251  -0.1174 1125 PHE A CB  
1634 C CG  . PHE A 215 ? 0.2998 0.3138 0.6239 -0.0099 0.0320  -0.1213 1125 PHE A CG  
1635 C CD1 . PHE A 215 ? 0.2568 0.2673 0.5941 -0.0086 0.0375  -0.1157 1125 PHE A CD1 
1636 C CD2 . PHE A 215 ? 0.2766 0.2838 0.5899 -0.0104 0.0327  -0.1310 1125 PHE A CD2 
1637 C CE1 . PHE A 215 ? 0.2678 0.2681 0.6088 -0.0078 0.0438  -0.1198 1125 PHE A CE1 
1638 C CE2 . PHE A 215 ? 0.3004 0.2973 0.6156 -0.0091 0.0389  -0.1358 1125 PHE A CE2 
1639 C CZ  . PHE A 215 ? 0.3243 0.3177 0.6541 -0.0077 0.0446  -0.1304 1125 PHE A CZ  
1640 N N   . MET A 216 ? 0.2214 0.2664 0.5447 -0.0027 0.0153  -0.1014 1126 MET A N   
1641 C CA  . MET A 216 ? 0.2476 0.3026 0.5682 0.0000  0.0078  -0.0990 1126 MET A CA  
1642 C C   . MET A 216 ? 0.2603 0.3230 0.5886 0.0008  0.0081  -0.0941 1126 MET A C   
1643 O O   . MET A 216 ? 0.2476 0.3159 0.5760 -0.0015 0.0072  -0.0962 1126 MET A O   
1644 C CB  . MET A 216 ? 0.2093 0.2643 0.5294 0.0041  0.0044  -0.0950 1126 MET A CB  
1645 C CG  . MET A 216 ? 0.2355 0.2879 0.5468 0.0038  0.0012  -0.0986 1126 MET A CG  
1646 S SD  . MET A 216 ? 0.2765 0.3252 0.5925 0.0068  0.0011  -0.0923 1126 MET A SD  
1647 C CE  . MET A 216 ? 0.2173 0.2575 0.5396 0.0055  0.0133  -0.0910 1126 MET A CE  
1648 N N   . LEU A 217 ? 0.2070 0.2708 0.5419 0.0041  0.0093  -0.0870 1127 LEU A N   
1649 C CA  . LEU A 217 ? 0.2429 0.3157 0.5830 0.0058  0.0094  -0.0813 1127 LEU A CA  
1650 C C   . LEU A 217 ? 0.2637 0.3336 0.6143 0.0015  0.0164  -0.0785 1127 LEU A C   
1651 O O   . LEU A 217 ? 0.2420 0.3208 0.5973 0.0017  0.0171  -0.0735 1127 LEU A O   
1652 C CB  . LEU A 217 ? 0.2694 0.3451 0.6120 0.0114  0.0070  -0.0744 1127 LEU A CB  
1653 C CG  . LEU A 217 ? 0.3065 0.3852 0.6426 0.0166  -0.0017 -0.0757 1127 LEU A CG  
1654 C CD1 . LEU A 217 ? 0.3159 0.3953 0.6576 0.0215  -0.0033 -0.0686 1127 LEU A CD1 
1655 C CD2 . LEU A 217 ? 0.2311 0.3204 0.5586 0.0195  -0.0085 -0.0795 1127 LEU A CD2 
1656 N N   . HIS A 218 ? 0.2150 0.2731 0.5701 -0.0017 0.0216  -0.0812 1128 HIS A N   
1657 C CA  . HIS A 218 ? 0.2585 0.3115 0.6248 -0.0060 0.0271  -0.0803 1128 HIS A CA  
1658 C C   . HIS A 218 ? 0.2298 0.2724 0.5925 -0.0098 0.0286  -0.0902 1128 HIS A C   
1659 O O   . HIS A 218 ? 0.2458 0.2845 0.5980 -0.0085 0.0273  -0.0958 1128 HIS A O   
1660 C CB  . HIS A 218 ? 0.2519 0.2995 0.6298 -0.0046 0.0321  -0.0730 1128 HIS A CB  
1661 C CG  . HIS A 218 ? 0.2281 0.2652 0.6050 -0.0031 0.0350  -0.0760 1128 HIS A CG  
1662 N ND1 . HIS A 218 ? 0.2342 0.2604 0.6116 -0.0056 0.0391  -0.0835 1128 HIS A ND1 
1663 C CD2 . HIS A 218 ? 0.2220 0.2587 0.5977 0.0011  0.0343  -0.0727 1128 HIS A CD2 
1664 C CE1 . HIS A 218 ? 0.2354 0.2560 0.6116 -0.0028 0.0420  -0.0840 1128 HIS A CE1 
1665 N NE2 . HIS A 218 ? 0.2668 0.2935 0.6430 0.0009  0.0390  -0.0771 1128 HIS A NE2 
1666 N N   . GLN A 219 ? 0.2451 0.2835 0.6170 -0.0141 0.0308  -0.0923 1129 GLN A N   
1667 C CA  . GLN A 219 ? 0.2589 0.2866 0.6268 -0.0169 0.0315  -0.1028 1129 GLN A CA  
1668 C C   . GLN A 219 ? 0.2634 0.2795 0.6441 -0.0183 0.0368  -0.1034 1129 GLN A C   
1669 O O   . GLN A 219 ? 0.3494 0.3581 0.7345 -0.0219 0.0363  -0.1105 1129 GLN A O   
1670 C CB  . GLN A 219 ? 0.2470 0.2788 0.6123 -0.0209 0.0265  -0.1086 1129 GLN A CB  
1671 C CG  . GLN A 219 ? 0.2387 0.2815 0.5913 -0.0189 0.0208  -0.1091 1129 GLN A CG  
1672 C CD  . GLN A 219 ? 0.2818 0.3322 0.6357 -0.0225 0.0159  -0.1120 1129 GLN A CD  
1673 O OE1 . GLN A 219 ? 0.2446 0.2931 0.6104 -0.0270 0.0164  -0.1127 1129 GLN A OE1 
1674 N NE2 . GLN A 219 ? 0.2324 0.2917 0.5757 -0.0205 0.0106  -0.1135 1129 GLN A NE2 
1675 N N   . ASP A 220 ? 0.2847 0.2987 0.6724 -0.0153 0.0411  -0.0963 1130 ASP A N   
1676 C CA  . ASP A 220 ? 0.2920 0.2946 0.6928 -0.0156 0.0462  -0.0966 1130 ASP A CA  
1677 C C   . ASP A 220 ? 0.2744 0.2668 0.6656 -0.0133 0.0491  -0.1068 1130 ASP A C   
1678 O O   . ASP A 220 ? 0.2971 0.2904 0.6809 -0.0092 0.0513  -0.1052 1130 ASP A O   
1679 C CB  . ASP A 220 ? 0.2557 0.2605 0.6675 -0.0128 0.0494  -0.0850 1130 ASP A CB  
1680 C CG  . ASP A 220 ? 0.2802 0.2738 0.7089 -0.0134 0.0540  -0.0840 1130 ASP A CG  
1681 O OD1 . ASP A 220 ? 0.2974 0.2798 0.7247 -0.0127 0.0568  -0.0935 1130 ASP A OD1 
1682 O OD2 . ASP A 220 ? 0.2631 0.2593 0.7065 -0.0143 0.0548  -0.0738 1130 ASP A OD2 
1683 N N   . LEU A 221 ? 0.2825 0.2656 0.6740 -0.0156 0.0488  -0.1170 1131 LEU A N   
1684 C CA  . LEU A 221 ? 0.3324 0.3077 0.7100 -0.0128 0.0507  -0.1282 1131 LEU A CA  
1685 C C   . LEU A 221 ? 0.2983 0.2670 0.6790 -0.0078 0.0582  -0.1275 1131 LEU A C   
1686 O O   . LEU A 221 ? 0.3373 0.3018 0.7055 -0.0042 0.0613  -0.1351 1131 LEU A O   
1687 C CB  . LEU A 221 ? 0.3081 0.2743 0.6858 -0.0158 0.0476  -0.1403 1131 LEU A CB  
1688 C CG  . LEU A 221 ? 0.3046 0.2778 0.6761 -0.0202 0.0400  -0.1429 1131 LEU A CG  
1689 C CD1 . LEU A 221 ? 0.3161 0.2817 0.6991 -0.0249 0.0356  -0.1501 1131 LEU A CD1 
1690 C CD2 . LEU A 221 ? 0.3070 0.2824 0.6559 -0.0178 0.0381  -0.1498 1131 LEU A CD2 
1691 N N   . ARG A 222 ? 0.3092 0.2774 0.7065 -0.0070 0.0613  -0.1183 1132 ARG A N   
1692 C CA  . ARG A 222 ? 0.3349 0.2979 0.7375 -0.0020 0.0683  -0.1166 1132 ARG A CA  
1693 C C   . ARG A 222 ? 0.3576 0.3293 0.7541 0.0014  0.0697  -0.1086 1132 ARG A C   
1694 O O   . ARG A 222 ? 0.3619 0.3310 0.7627 0.0058  0.0756  -0.1066 1132 ARG A O   
1695 C CB  . ARG A 222 ? 0.3243 0.2826 0.7489 -0.0027 0.0702  -0.1098 1132 ARG A CB  
1696 C CG  . ARG A 222 ? 0.3647 0.3142 0.7999 -0.0068 0.0677  -0.1158 1132 ARG A CG  
1697 C CD  . ARG A 222 ? 0.4012 0.3487 0.8595 -0.0082 0.0686  -0.1055 1132 ARG A CD  
1698 N NE  . ARG A 222 ? 0.3272 0.2870 0.7890 -0.0109 0.0653  -0.0923 1132 ARG A NE  
1699 C CZ  . ARG A 222 ? 0.3573 0.3203 0.8335 -0.0104 0.0665  -0.0795 1132 ARG A CZ  
1700 N NH1 . ARG A 222 ? 0.2941 0.2485 0.7842 -0.0076 0.0708  -0.0774 1132 ARG A NH1 
1701 N NH2 . ARG A 222 ? 0.2776 0.2531 0.7536 -0.0120 0.0634  -0.0687 1132 ARG A NH2 
1702 N N   . PHE A 223 ? 0.3154 0.2973 0.7036 -0.0003 0.0640  -0.1043 1133 PHE A N   
1703 C CA  . PHE A 223 ? 0.2641 0.2539 0.6495 0.0026  0.0632  -0.0963 1133 PHE A CA  
1704 C C   . PHE A 223 ? 0.2791 0.2755 0.6478 0.0020  0.0581  -0.0993 1133 PHE A C   
1705 O O   . PHE A 223 ? 0.2495 0.2545 0.6161 0.0014  0.0521  -0.0941 1133 PHE A O   
1706 C CB  . PHE A 223 ? 0.2536 0.2496 0.6506 0.0023  0.0600  -0.0852 1133 PHE A CB  
1707 C CG  . PHE A 223 ? 0.3254 0.3154 0.7398 0.0031  0.0645  -0.0804 1133 PHE A CG  
1708 C CD1 . PHE A 223 ? 0.3076 0.2953 0.7303 0.0072  0.0689  -0.0757 1133 PHE A CD1 
1709 C CD2 . PHE A 223 ? 0.2889 0.2757 0.7133 -0.0003 0.0641  -0.0799 1133 PHE A CD2 
1710 C CE1 . PHE A 223 ? 0.3077 0.2896 0.7474 0.0082  0.0726  -0.0712 1133 PHE A CE1 
1711 C CE2 . PHE A 223 ? 0.2655 0.2464 0.7072 0.0004  0.0676  -0.0748 1133 PHE A CE2 
1712 C CZ  . PHE A 223 ? 0.3437 0.3220 0.7927 0.0048  0.0718  -0.0708 1133 PHE A CZ  
1713 N N   . PRO A 224 ? 0.3034 0.2962 0.6595 0.0027  0.0602  -0.1077 1134 PRO A N   
1714 C CA  . PRO A 224 ? 0.2658 0.2649 0.6075 0.0030  0.0560  -0.1083 1134 PRO A CA  
1715 C C   . PRO A 224 ? 0.2897 0.2941 0.6355 0.0061  0.0563  -0.0990 1134 PRO A C   
1716 O O   . PRO A 224 ? 0.2905 0.2925 0.6472 0.0089  0.0619  -0.0941 1134 PRO A O   
1717 C CB  . PRO A 224 ? 0.2806 0.2740 0.6090 0.0042  0.0599  -0.1181 1134 PRO A CB  
1718 C CG  . PRO A 224 ? 0.3398 0.3247 0.6770 0.0069  0.0680  -0.1205 1134 PRO A CG  
1719 C CD  . PRO A 224 ? 0.3564 0.3394 0.7102 0.0042  0.0664  -0.1168 1134 PRO A CD  
1720 N N   . ARG A 225 ? 0.4220 0.3663 0.4217 0.0492  0.1556  0.0115  1135 ARG A N   
1721 C CA  . ARG A 225 ? 0.4290 0.3981 0.4481 0.0643  0.1357  0.0135  1135 ARG A CA  
1722 C C   . ARG A 225 ? 0.4186 0.3917 0.4546 0.0592  0.1287  0.0051  1135 ARG A C   
1723 O O   . ARG A 225 ? 0.4505 0.4253 0.4846 0.0439  0.1295  -0.0062 1135 ARG A O   
1724 C CB  . ARG A 225 ? 0.3424 0.3460 0.3653 0.0665  0.1198  0.0059  1135 ARG A CB  
1725 C CG  . ARG A 225 ? 0.3665 0.3717 0.3703 0.0739  0.1252  0.0180  1135 ARG A CG  
1726 C CD  . ARG A 225 ? 0.3728 0.4145 0.3759 0.0728  0.1134  0.0068  1135 ARG A CD  
1727 N NE  . ARG A 225 ? 0.3296 0.4022 0.3570 0.0824  0.0914  -0.0037 1135 ARG A NE  
1728 C CZ  . ARG A 225 ? 0.3241 0.4309 0.3580 0.0827  0.0794  -0.0187 1135 ARG A CZ  
1729 N NH1 . ARG A 225 ? 0.3559 0.4746 0.3723 0.0745  0.0870  -0.0244 1135 ARG A NH1 
1730 N NH2 . ARG A 225 ? 0.2965 0.4266 0.3569 0.0903  0.0605  -0.0301 1135 ARG A NH2 
1731 N N   . ILE A 226 ? 0.3651 0.3413 0.4171 0.0711  0.1222  0.0118  1136 ILE A N   
1732 C CA  . ILE A 226 ? 0.4140 0.3901 0.4786 0.0657  0.1199  0.0082  1136 ILE A CA  
1733 C C   . ILE A 226 ? 0.3893 0.3941 0.4762 0.0669  0.0974  0.0022  1136 ILE A C   
1734 O O   . ILE A 226 ? 0.3561 0.3772 0.4600 0.0791  0.0852  0.0050  1136 ILE A O   
1735 C CB  . ILE A 226 ? 0.3795 0.3417 0.4511 0.0762  0.1295  0.0180  1136 ILE A CB  
1736 C CG1 . ILE A 226 ? 0.4287 0.3592 0.4824 0.0775  0.1517  0.0238  1136 ILE A CG1 
1737 C CG2 . ILE A 226 ? 0.3817 0.3428 0.4599 0.0667  0.1323  0.0138  1136 ILE A CG2 
1738 C CD1 . ILE A 226 ? 0.4715 0.3811 0.5098 0.0588  0.1683  0.0134  1136 ILE A CD1 
1739 N N   . ALA A 227 ? 0.3704 0.3818 0.4592 0.0540  0.0916  -0.0062 1137 ALA A N   
1740 C CA  . ALA A 227 ? 0.3332 0.3667 0.4458 0.0544  0.0711  -0.0111 1137 ALA A CA  
1741 C C   . ALA A 227 ? 0.3383 0.3689 0.4594 0.0481  0.0690  -0.0057 1137 ALA A C   
1742 O O   . ALA A 227 ? 0.3895 0.4094 0.4938 0.0365  0.0798  -0.0054 1137 ALA A O   
1743 C CB  . ALA A 227 ? 0.3664 0.4132 0.4786 0.0467  0.0638  -0.0229 1137 ALA A CB  
1744 N N   . PHE A 228 ? 0.3443 0.3859 0.4909 0.0542  0.0557  -0.0020 1138 PHE A N   
1745 C CA  . PHE A 228 ? 0.3525 0.3933 0.5084 0.0476  0.0531  0.0059  1138 PHE A CA  
1746 C C   . PHE A 228 ? 0.3216 0.3735 0.4929 0.0421  0.0357  0.0043  1138 PHE A C   
1747 O O   . PHE A 228 ? 0.3016 0.3649 0.4934 0.0488  0.0215  -0.0033 1138 PHE A O   
1748 C CB  . PHE A 228 ? 0.2869 0.3319 0.4647 0.0558  0.0508  0.0126  1138 PHE A CB  
1749 C CG  . PHE A 228 ? 0.3271 0.3617 0.4936 0.0610  0.0688  0.0172  1138 PHE A CG  
1750 C CD1 . PHE A 228 ? 0.3514 0.3734 0.5007 0.0520  0.0854  0.0207  1138 PHE A CD1 
1751 C CD2 . PHE A 228 ? 0.3240 0.3635 0.4986 0.0753  0.0687  0.0175  1138 PHE A CD2 
1752 C CE1 . PHE A 228 ? 0.3715 0.3829 0.5154 0.0583  0.1030  0.0230  1138 PHE A CE1 
1753 C CE2 . PHE A 228 ? 0.3150 0.3449 0.4839 0.0826  0.0844  0.0230  1138 PHE A CE2 
1754 C CZ  . PHE A 228 ? 0.3425 0.3569 0.4980 0.0746  0.1022  0.0251  1138 PHE A CZ  
1755 N N   . PHE A 229 ? 0.3254 0.3751 0.4871 0.0306  0.0367  0.0110  1139 PHE A N   
1756 C CA  . PHE A 229 ? 0.3703 0.4295 0.5473 0.0263  0.0196  0.0150  1139 PHE A CA  
1757 C C   . PHE A 229 ? 0.3693 0.4259 0.5470 0.0186  0.0200  0.0315  1139 PHE A C   
1758 O O   . PHE A 229 ? 0.3448 0.3953 0.5000 0.0115  0.0363  0.0353  1139 PHE A O   
1759 C CB  . PHE A 229 ? 0.3174 0.3834 0.4777 0.0181  0.0183  0.0082  1139 PHE A CB  
1760 C CG  . PHE A 229 ? 0.3485 0.4196 0.5075 0.0230  0.0197  -0.0078 1139 PHE A CG  
1761 C CD1 . PHE A 229 ? 0.3554 0.4162 0.4898 0.0213  0.0381  -0.0140 1139 PHE A CD1 
1762 C CD2 . PHE A 229 ? 0.3434 0.4293 0.5266 0.0290  0.0038  -0.0164 1139 PHE A CD2 
1763 C CE1 . PHE A 229 ? 0.3228 0.3888 0.4538 0.0240  0.0407  -0.0260 1139 PHE A CE1 
1764 C CE2 . PHE A 229 ? 0.3213 0.4156 0.5020 0.0319  0.0069  -0.0317 1139 PHE A CE2 
1765 C CZ  . PHE A 229 ? 0.3420 0.4268 0.4949 0.0286  0.0255  -0.0353 1139 PHE A CZ  
1766 N N   . SER A 230 ? 0.3820 0.4430 0.5863 0.0194  0.0029  0.0410  1140 SER A N   
1767 C CA  . SER A 230 ? 0.4118 0.4713 0.6162 0.0104  0.0023  0.0603  1140 SER A CA  
1768 C C   . SER A 230 ? 0.4506 0.5159 0.6232 -0.0025 0.0056  0.0668  1140 SER A C   
1769 O O   . SER A 230 ? 0.4344 0.5083 0.6052 -0.0032 -0.0056 0.0635  1140 SER A O   
1770 C CB  . SER A 230 ? 0.3999 0.4590 0.6425 0.0143  -0.0172 0.0705  1140 SER A CB  
1771 O OG  . SER A 230 ? 0.3308 0.3953 0.5887 0.0205  -0.0333 0.0631  1140 SER A OG  
1772 N N   . SER A 231 ? 0.5122 0.5765 0.6602 -0.0131 0.0213  0.0740  1141 SER A N   
1773 C CA  . SER A 231 ? 0.5416 0.6158 0.6572 -0.0275 0.0244  0.0792  1141 SER A CA  
1774 C C   . SER A 231 ? 0.5267 0.6095 0.6486 -0.0337 0.0088  0.1034  1141 SER A C   
1775 O O   . SER A 231 ? 0.5730 0.6694 0.6676 -0.0458 0.0075  0.1107  1141 SER A O   
1776 C CB  . SER A 231 ? 0.5561 0.6276 0.6418 -0.0370 0.0494  0.0736  1141 SER A CB  
1777 O OG  . SER A 231 ? 0.6110 0.6787 0.7095 -0.0361 0.0570  0.0842  1141 SER A OG  
1778 N N   . ARG A 232 ? 0.4708 0.5464 0.6284 -0.0262 -0.0034 0.1159  1142 ARG A N   
1779 C CA  . ARG A 232 ? 0.4823 0.5600 0.6519 -0.0309 -0.0182 0.1427  1142 ARG A CA  
1780 C C   . ARG A 232 ? 0.4526 0.5176 0.6715 -0.0184 -0.0331 0.1453  1142 ARG A C   
1781 O O   . ARG A 232 ? 0.4143 0.4736 0.6528 -0.0078 -0.0312 0.1255  1142 ARG A O   
1782 C CB  . ARG A 232 ? 0.5284 0.6087 0.6784 -0.0450 -0.0038 0.1603  1142 ARG A CB  
1783 C CG  . ARG A 232 ? 0.5305 0.6020 0.6946 -0.0428 0.0133  0.1529  1142 ARG A CG  
1784 C CD  . ARG A 232 ? 0.4886 0.5640 0.6473 -0.0564 0.0232  0.1746  1142 ARG A CD  
1785 N NE  . ARG A 232 ? 0.5245 0.5969 0.6999 -0.0547 0.0398  0.1668  1142 ARG A NE  
1786 C CZ  . ARG A 232 ? 0.5394 0.6054 0.7537 -0.0524 0.0353  0.1751  1142 ARG A CZ  
1787 N NH1 . ARG A 232 ? 0.5010 0.5575 0.7442 -0.0509 0.0155  0.1908  1142 ARG A NH1 
1788 N NH2 . ARG A 232 ? 0.5554 0.6251 0.7829 -0.0518 0.0513  0.1667  1142 ARG A NH2 
1789 N N   . ASP A 233 ? 0.4489 0.5099 0.6876 -0.0202 -0.0482 0.1701  1143 ASP A N   
1790 C CA  . ASP A 233 ? 0.4789 0.5242 0.7676 -0.0113 -0.0601 0.1737  1143 ASP A CA  
1791 C C   . ASP A 233 ? 0.4930 0.5309 0.7943 -0.0152 -0.0456 0.1716  1143 ASP A C   
1792 O O   . ASP A 233 ? 0.5287 0.5703 0.8085 -0.0280 -0.0313 0.1855  1143 ASP A O   
1793 C CB  . ASP A 233 ? 0.5046 0.5431 0.8115 -0.0137 -0.0775 0.2050  1143 ASP A CB  
1794 C CG  . ASP A 233 ? 0.4844 0.5324 0.7918 -0.0060 -0.0964 0.2073  1143 ASP A CG  
1795 O OD1 . ASP A 233 ? 0.4443 0.5001 0.7552 0.0038  -0.0989 0.1808  1143 ASP A OD1 
1796 O OD2 . ASP A 233 ? 0.5652 0.6147 0.8703 -0.0098 -0.1089 0.2371  1143 ASP A OD2 
1797 N N   . ILE A 234 ? 0.4860 0.5171 0.8237 -0.0047 -0.0493 0.1531  1144 ILE A N   
1798 C CA  . ILE A 234 ? 0.3908 0.4201 0.7459 -0.0070 -0.0379 0.1476  1144 ILE A CA  
1799 C C   . ILE A 234 ? 0.4315 0.4469 0.8369 -0.0070 -0.0501 0.1561  1144 ILE A C   
1800 O O   . ILE A 234 ? 0.3822 0.3910 0.8204 0.0037  -0.0650 0.1429  1144 ILE A O   
1801 C CB  . ILE A 234 ? 0.3771 0.4143 0.7311 0.0038  -0.0311 0.1181  1144 ILE A CB  
1802 C CG1 . ILE A 234 ? 0.3804 0.4259 0.6869 0.0022  -0.0162 0.1115  1144 ILE A CG1 
1803 C CG2 . ILE A 234 ? 0.4338 0.4738 0.8119 0.0028  -0.0228 0.1129  1144 ILE A CG2 
1804 C CD1 . ILE A 234 ? 0.3477 0.3984 0.6500 0.0131  -0.0092 0.0876  1144 ILE A CD1 
1805 N N   . ARG A 235 ? 0.4534 0.4647 0.8665 -0.0199 -0.0420 0.1760  1145 ARG A N   
1806 C CA  . ARG A 235 ? 0.4170 0.4122 0.8783 -0.0239 -0.0506 0.1869  1145 ARG A CA  
1807 C C   . ARG A 235 ? 0.4117 0.4106 0.9104 -0.0183 -0.0497 0.1593  1145 ARG A C   
1808 O O   . ARG A 235 ? 0.4111 0.4269 0.8947 -0.0131 -0.0400 0.1386  1145 ARG A O   
1809 C CB  . ARG A 235 ? 0.4175 0.4097 0.8704 -0.0423 -0.0400 0.2192  1145 ARG A CB  
1810 C CG  . ARG A 235 ? 0.4966 0.4869 0.9154 -0.0484 -0.0451 0.2494  1145 ARG A CG  
1811 C CD  . ARG A 235 ? 0.5415 0.5431 0.9247 -0.0670 -0.0271 0.2735  1145 ARG A CD  
1812 N NE  . ARG A 235 ? 0.6011 0.5936 1.0159 -0.0803 -0.0201 0.2904  1145 ARG A NE  
1813 C CZ  . ARG A 235 ? 0.6966 0.7006 1.1205 -0.0874 -0.0022 0.2785  1145 ARG A CZ  
1814 N NH1 . ARG A 235 ? 0.7258 0.7490 1.1293 -0.0811 0.0105  0.2517  1145 ARG A NH1 
1815 N NH2 . ARG A 235 ? 0.7977 0.7940 1.2547 -0.1012 0.0032  0.2944  1145 ARG A NH2 
1816 N N   . THR A 236 ? 0.4186 0.4018 0.9678 -0.0189 -0.0609 0.1588  1146 THR A N   
1817 C CA  . THR A 236 ? 0.3669 0.3564 0.9553 -0.0152 -0.0625 0.1306  1146 THR A CA  
1818 C C   . THR A 236 ? 0.3621 0.3670 0.9503 -0.0264 -0.0459 0.1323  1146 THR A C   
1819 O O   . THR A 236 ? 0.3914 0.3888 0.9883 -0.0419 -0.0384 0.1567  1146 THR A O   
1820 C CB  . THR A 236 ? 0.3585 0.3254 1.0040 -0.0164 -0.0765 0.1296  1146 THR A CB  
1821 O OG1 . THR A 236 ? 0.3464 0.3040 0.9991 -0.0022 -0.0920 0.1198  1146 THR A OG1 
1822 C CG2 . THR A 236 ? 0.3363 0.3137 1.0232 -0.0176 -0.0763 0.1007  1146 THR A CG2 
1823 N N   . GLY A 237 ? 0.3613 0.3893 0.9422 -0.0183 -0.0403 0.1072  1147 GLY A N   
1824 C CA  . GLY A 237 ? 0.3138 0.3617 0.8986 -0.0253 -0.0257 0.1052  1147 GLY A CA  
1825 C C   . GLY A 237 ? 0.3416 0.4027 0.8779 -0.0248 -0.0082 0.1132  1147 GLY A C   
1826 O O   . GLY A 237 ? 0.2839 0.3651 0.8232 -0.0263 0.0046  0.1076  1147 GLY A O   
1827 N N   . GLU A 238 ? 0.3468 0.3985 0.8415 -0.0226 -0.0073 0.1241  1148 GLU A N   
1828 C CA  . GLU A 238 ? 0.3396 0.4015 0.7888 -0.0238 0.0103  0.1294  1148 GLU A CA  
1829 C C   . GLU A 238 ? 0.3360 0.4136 0.7753 -0.0094 0.0160  0.1058  1148 GLU A C   
1830 O O   . GLU A 238 ? 0.3341 0.4127 0.7811 0.0035  0.0039  0.0875  1148 GLU A O   
1831 C CB  . GLU A 238 ? 0.3970 0.4479 0.8064 -0.0246 0.0073  0.1414  1148 GLU A CB  
1832 C CG  . GLU A 238 ? 0.4641 0.5079 0.8610 -0.0409 0.0105  0.1716  1148 GLU A CG  
1833 C CD  . GLU A 238 ? 0.4691 0.5134 0.8176 -0.0421 0.0119  0.1791  1148 GLU A CD  
1834 O OE1 . GLU A 238 ? 0.4773 0.5223 0.8118 -0.0302 0.0067  0.1611  1148 GLU A OE1 
1835 O OE2 . GLU A 238 ? 0.5435 0.5900 0.8678 -0.0561 0.0185  0.2022  1148 GLU A OE2 
1836 N N   . GLU A 239 ? 0.3480 0.4388 0.7704 -0.0112 0.0351  0.1069  1149 GLU A N   
1837 C CA  . GLU A 239 ? 0.3699 0.4725 0.7801 0.0038  0.0419  0.0893  1149 GLU A CA  
1838 C C   . GLU A 239 ? 0.3574 0.4486 0.7228 0.0092  0.0454  0.0870  1149 GLU A C   
1839 O O   . GLU A 239 ? 0.3648 0.4481 0.7013 -0.0011 0.0529  0.0992  1149 GLU A O   
1840 C CB  . GLU A 239 ? 0.2802 0.4008 0.6953 0.0021  0.0616  0.0899  1149 GLU A CB  
1841 C CG  . GLU A 239 ? 0.2676 0.4018 0.6838 0.0206  0.0648  0.0732  1149 GLU A CG  
1842 C CD  . GLU A 239 ? 0.3391 0.4922 0.7633 0.0224  0.0848  0.0728  1149 GLU A CD  
1843 O OE1 . GLU A 239 ? 0.3432 0.5028 0.7749 0.0075  0.0973  0.0831  1149 GLU A OE1 
1844 O OE2 . GLU A 239 ? 0.3176 0.4801 0.7417 0.0391  0.0884  0.0628  1149 GLU A OE2 
1845 N N   . LEU A 240 ? 0.3616 0.4540 0.7214 0.0241  0.0397  0.0712  1150 LEU A N   
1846 C CA  . LEU A 240 ? 0.3299 0.4120 0.6506 0.0288  0.0446  0.0667  1150 LEU A CA  
1847 C C   . LEU A 240 ? 0.3730 0.4566 0.6711 0.0314  0.0665  0.0655  1150 LEU A C   
1848 O O   . LEU A 240 ? 0.3525 0.4477 0.6669 0.0408  0.0727  0.0604  1150 LEU A O   
1849 C CB  . LEU A 240 ? 0.3561 0.4396 0.6798 0.0425  0.0320  0.0515  1150 LEU A CB  
1850 C CG  . LEU A 240 ? 0.4022 0.4861 0.7519 0.0432  0.0111  0.0457  1150 LEU A CG  
1851 C CD1 . LEU A 240 ? 0.3974 0.4896 0.7463 0.0568  0.0033  0.0281  1150 LEU A CD1 
1852 C CD2 . LEU A 240 ? 0.4078 0.4782 0.7456 0.0346  0.0045  0.0545  1150 LEU A CD2 
1853 N N   . GLY A 241 ? 0.3983 0.4715 0.6611 0.0236  0.0780  0.0686  1151 GLY A N   
1854 C CA  . GLY A 241 ? 0.3797 0.4503 0.6214 0.0261  0.1000  0.0637  1151 GLY A CA  
1855 C C   . GLY A 241 ? 0.3871 0.4433 0.5900 0.0214  0.1066  0.0588  1151 GLY A C   
1856 O O   . GLY A 241 ? 0.4001 0.4536 0.5892 0.0113  0.0969  0.0632  1151 GLY A O   
1857 N N   . PHE A 242 ? 0.4092 0.4566 0.5973 0.0287  0.1229  0.0495  1152 PHE A N   
1858 C CA  . PHE A 242 ? 0.4546 0.4883 0.6072 0.0209  0.1348  0.0424  1152 PHE A CA  
1859 C C   . PHE A 242 ? 0.4954 0.5251 0.6379 0.0192  0.1609  0.0362  1152 PHE A C   
1860 O O   . PHE A 242 ? 0.4367 0.4746 0.6015 0.0271  0.1695  0.0376  1152 PHE A O   
1861 C CB  . PHE A 242 ? 0.4268 0.4473 0.5696 0.0299  0.1301  0.0343  1152 PHE A CB  
1862 C CG  . PHE A 242 ? 0.4020 0.4152 0.5547 0.0475  0.1386  0.0310  1152 PHE A CG  
1863 C CD1 . PHE A 242 ? 0.3581 0.3835 0.5384 0.0618  0.1253  0.0348  1152 PHE A CD1 
1864 C CD2 . PHE A 242 ? 0.4224 0.4165 0.5571 0.0497  0.1589  0.0239  1152 PHE A CD2 
1865 C CE1 . PHE A 242 ? 0.3576 0.3795 0.5454 0.0790  0.1306  0.0346  1152 PHE A CE1 
1866 C CE2 . PHE A 242 ? 0.4630 0.4481 0.6077 0.0677  0.1657  0.0246  1152 PHE A CE2 
1867 C CZ  . PHE A 242 ? 0.4204 0.4211 0.5905 0.0829  0.1506  0.0314  1152 PHE A CZ  
1868 N N   . ASP A 243 ? 0.4646 0.4835 0.5756 0.0083  0.1740  0.0272  1153 ASP A N   
1869 C CA  . ASP A 243 ? 0.4979 0.5113 0.5980 0.0051  0.2009  0.0166  1153 ASP A CA  
1870 C C   . ASP A 243 ? 0.5131 0.5046 0.6183 0.0216  0.2122  0.0077  1153 ASP A C   
1871 O O   . ASP A 243 ? 0.4830 0.4562 0.5693 0.0196  0.2140  0.0003  1153 ASP A O   
1872 C CB  . ASP A 243 ? 0.5086 0.5230 0.5731 -0.0160 0.2102  0.0083  1153 ASP A CB  
1873 C CG  . ASP A 243 ? 0.5497 0.5660 0.6056 -0.0225 0.2382  -0.0040 1153 ASP A CG  
1874 O OD1 . ASP A 243 ? 0.5716 0.5747 0.6436 -0.0081 0.2542  -0.0123 1153 ASP A OD1 
1875 O OD2 . ASP A 243 ? 0.5686 0.6012 0.6030 -0.0411 0.2443  -0.0050 1153 ASP A OD2 
1876 N N   . TYR A 244 ? 0.4629 0.4575 0.5954 0.0379  0.2196  0.0099  1154 TYR A N   
1877 C CA  . TYR A 244 ? 0.5438 0.5176 0.6842 0.0560  0.2314  0.0053  1154 TYR A CA  
1878 C C   . TYR A 244 ? 0.5519 0.5006 0.6683 0.0479  0.2553  -0.0105 1154 TYR A C   
1879 O O   . TYR A 244 ? 0.5508 0.4733 0.6642 0.0577  0.2622  -0.0133 1154 TYR A O   
1880 C CB  . TYR A 244 ? 0.5590 0.5459 0.7342 0.0731  0.2385  0.0087  1154 TYR A CB  
1881 C CG  . TYR A 244 ? 0.5302 0.5388 0.7343 0.0858  0.2155  0.0216  1154 TYR A CG  
1882 C CD1 . TYR A 244 ? 0.4962 0.5103 0.6951 0.0814  0.1914  0.0280  1154 TYR A CD1 
1883 C CD2 . TYR A 244 ? 0.5269 0.5530 0.7662 0.1022  0.2183  0.0248  1154 TYR A CD2 
1884 C CE1 . TYR A 244 ? 0.4385 0.4733 0.6646 0.0915  0.1713  0.0355  1154 TYR A CE1 
1885 C CE2 . TYR A 244 ? 0.4987 0.5483 0.7652 0.1120  0.1970  0.0335  1154 TYR A CE2 
1886 C CZ  . TYR A 244 ? 0.4639 0.5167 0.7225 0.1060  0.1738  0.0379  1154 TYR A CZ  
1887 O OH  . TYR A 244 ? 0.4377 0.5144 0.7238 0.1144  0.1534  0.0426  1154 TYR A OH  
1888 N N   . GLY A 245 ? 0.5645 0.5211 0.6637 0.0292  0.2686  -0.0209 1155 GLY A N   
1889 C CA  . GLY A 245 ? 0.6362 0.5725 0.7146 0.0193  0.2926  -0.0406 1155 GLY A CA  
1890 C C   . GLY A 245 ? 0.7368 0.6696 0.8305 0.0266  0.3070  -0.0491 1155 GLY A C   
1891 O O   . GLY A 245 ? 0.7230 0.6680 0.8465 0.0426  0.3050  -0.0402 1155 GLY A O   
1892 N N   . ASP A 246 ? 0.7035 0.5519 1.0971 -0.0056 0.2686  -0.1751 1156 ASP A N   
1893 C CA  . ASP A 246 ? 0.7502 0.6071 1.1551 0.0179  0.2758  -0.2037 1156 ASP A CA  
1894 C C   . ASP A 246 ? 0.7865 0.5824 1.2106 0.0291  0.2615  -0.2162 1156 ASP A C   
1895 O O   . ASP A 246 ? 0.8526 0.6591 1.2983 0.0529  0.2670  -0.2306 1156 ASP A O   
1896 C CB  . ASP A 246 ? 0.7902 0.6657 1.1653 0.0204  0.2806  -0.2370 1156 ASP A CB  
1897 C CG  . ASP A 246 ? 0.8189 0.7644 1.1775 0.0166  0.2975  -0.2271 1156 ASP A CG  
1898 O OD1 . ASP A 246 ? 0.7154 0.6985 1.0896 0.0187  0.3088  -0.2005 1156 ASP A OD1 
1899 O OD2 . ASP A 246 ? 0.8681 0.8298 1.1964 0.0103  0.2987  -0.2451 1156 ASP A OD2 
1900 N N   . ARG A 247 ? 0.7948 0.5298 1.2115 0.0127  0.2430  -0.2103 1157 ARG A N   
1901 C CA  . ARG A 247 ? 0.8174 0.4890 1.2490 0.0221  0.2272  -0.2181 1157 ARG A CA  
1902 C C   . ARG A 247 ? 0.8088 0.4948 1.2780 0.0379  0.2313  -0.1987 1157 ARG A C   
1903 O O   . ARG A 247 ? 0.8090 0.4843 1.2941 0.0610  0.2260  -0.2134 1157 ARG A O   
1904 C CB  . ARG A 247 ? 0.7852 0.4036 1.1963 -0.0041 0.2052  -0.2030 1157 ARG A CB  
1905 C CG  . ARG A 247 ? 0.7961 0.3865 1.1984 0.0013  0.1772  -0.1849 1157 ARG A CG  
1906 C CD  . ARG A 247 ? 0.8129 0.3630 1.1710 -0.0198 0.1495  -0.1753 1157 ARG A CD  
1907 N NE  . ARG A 247 ? 0.8462 0.3528 1.1832 -0.0075 0.1257  -0.1791 1157 ARG A NE  
1908 C CZ  . ARG A 247 ? 0.8867 0.3483 1.1792 -0.0219 0.1000  -0.1712 1157 ARG A CZ  
1909 N NH1 . ARG A 247 ? 0.8719 0.3326 1.1398 -0.0493 0.0935  -0.1583 1157 ARG A NH1 
1910 N NH2 . ARG A 247 ? 0.9356 0.3511 1.2053 -0.0081 0.0812  -0.1766 1157 ARG A NH2 
1911 N N   . PHE A 248 ? 0.6891 0.4047 1.1684 0.0254  0.2376  -0.1640 1158 PHE A N   
1912 C CA  . PHE A 248 ? 0.6827 0.4133 1.1962 0.0355  0.2406  -0.1430 1158 PHE A CA  
1913 C C   . PHE A 248 ? 0.7639 0.5524 1.2973 0.0593  0.2575  -0.1575 1158 PHE A C   
1914 O O   . PHE A 248 ? 0.7958 0.5823 1.3587 0.0791  0.2551  -0.1634 1158 PHE A O   
1915 C CB  . PHE A 248 ? 0.6112 0.3624 1.1248 0.0159  0.2445  -0.1050 1158 PHE A CB  
1916 C CG  . PHE A 248 ? 0.6178 0.3900 1.1633 0.0224  0.2488  -0.0823 1158 PHE A CG  
1917 C CD1 . PHE A 248 ? 0.5996 0.3446 1.1505 0.0185  0.2286  -0.0651 1158 PHE A CD1 
1918 C CD2 . PHE A 248 ? 0.6010 0.4376 1.1567 0.0277  0.2670  -0.0747 1158 PHE A CD2 
1919 C CE1 . PHE A 248 ? 0.6091 0.3756 1.1884 0.0225  0.2314  -0.0453 1158 PHE A CE1 
1920 C CE2 . PHE A 248 ? 0.5495 0.4070 1.1342 0.0301  0.2704  -0.0536 1158 PHE A CE2 
1921 C CZ  . PHE A 248 ? 0.5318 0.3460 1.1358 0.0292  0.2551  -0.0405 1158 PHE A CZ  
1922 N N   . TRP A 249 ? 0.7328 0.5773 1.2503 0.0576  0.2746  -0.1633 1159 TRP A N   
1923 C CA  . TRP A 249 ? 0.7295 0.6389 1.2628 0.0764  0.2933  -0.1755 1159 TRP A CA  
1924 C C   . TRP A 249 ? 0.8417 0.7459 1.3753 0.1024  0.2933  -0.2190 1159 TRP A C   
1925 O O   . TRP A 249 ? 0.7398 0.6964 1.2933 0.1231  0.3073  -0.2331 1159 TRP A O   
1926 C CB  . TRP A 249 ? 0.6562 0.6252 1.1674 0.0636  0.3109  -0.1645 1159 TRP A CB  
1927 C CG  . TRP A 249 ? 0.6069 0.5906 1.1233 0.0454  0.3135  -0.1232 1159 TRP A CG  
1928 C CD1 . TRP A 249 ? 0.6417 0.6053 1.1362 0.0241  0.3065  -0.0989 1159 TRP A CD1 
1929 C CD2 . TRP A 249 ? 0.5848 0.6046 1.1298 0.0469  0.3223  -0.1015 1159 TRP A CD2 
1930 N NE1 . TRP A 249 ? 0.6250 0.6050 1.1301 0.0138  0.3100  -0.0639 1159 TRP A NE1 
1931 C CE2 . TRP A 249 ? 0.5860 0.5994 1.1216 0.0254  0.3195  -0.0641 1159 TRP A CE2 
1932 C CE3 . TRP A 249 ? 0.6323 0.6919 1.2102 0.0645  0.3319  -0.1110 1159 TRP A CE3 
1933 C CZ2 . TRP A 249 ? 0.5366 0.5757 1.0916 0.0184  0.3253  -0.0353 1159 TRP A CZ2 
1934 C CZ3 . TRP A 249 ? 0.5876 0.6802 1.1878 0.0560  0.3386  -0.0818 1159 TRP A CZ3 
1935 C CH2 . TRP A 249 ? 0.5592 0.6382 1.1464 0.0319  0.3349  -0.0440 1159 TRP A CH2 
1936 N N   . ASP A 250 ? 0.9828 0.8263 1.4937 0.1016  0.2778  -0.2414 1160 ASP A N   
1937 C CA  . ASP A 250 ? 1.0286 0.8537 1.5390 0.1287  0.2739  -0.2835 1160 ASP A CA  
1938 C C   . ASP A 250 ? 1.0156 0.8034 1.5550 0.1501  0.2588  -0.2865 1160 ASP A C   
1939 O O   . ASP A 250 ? 1.0742 0.8581 1.6075 0.1754  0.2503  -0.3138 1160 ASP A O   
1940 C CB  . ASP A 250 ? 1.0788 0.8477 1.5501 0.1181  0.2605  -0.3069 1160 ASP A CB  
1941 C CG  . ASP A 250 ? 1.1052 0.9203 1.5452 0.1042  0.2744  -0.3135 1160 ASP A CG  
1942 O OD1 . ASP A 250 ? 1.0997 0.9855 1.5457 0.1014  0.2935  -0.2966 1160 ASP A OD1 
1943 O OD2 . ASP A 250 ? 1.1391 0.9188 1.5466 0.0947  0.2651  -0.3349 1160 ASP A OD2 
1944 N N   . ILE A 251 ? 0.9334 0.7011 1.4870 0.1366  0.2470  -0.2510 1161 ILE A N   
1945 C CA  . ILE A 251 ? 0.9564 0.7087 1.5238 0.1513  0.2270  -0.2424 1161 ILE A CA  
1946 C C   . ILE A 251 ? 0.9148 0.7224 1.5262 0.1549  0.2415  -0.2193 1161 ILE A C   
1947 O O   . ILE A 251 ? 0.8894 0.7066 1.5204 0.1741  0.2317  -0.2204 1161 ILE A O   
1948 C CB  . ILE A 251 ? 0.9329 0.6131 1.4689 0.1324  0.1939  -0.2216 1161 ILE A CB  
1949 C CG1 . ILE A 251 ? 0.8315 0.5159 1.3764 0.1064  0.1922  -0.1807 1161 ILE A CG1 
1950 C CG2 . ILE A 251 ? 0.9793 0.6119 1.4705 0.1177  0.1830  -0.2357 1161 ILE A CG2 
1951 C CD1 . ILE A 251 ? 0.8188 0.4990 1.3770 0.1122  0.1752  -0.1611 1161 ILE A CD1 
1952 N N   . LYS A 252 ? 0.8402 0.6859 1.4665 0.1379  0.2642  -0.1983 1162 LYS A N   
1953 C CA  . LYS A 252 ? 0.8013 0.6980 1.4609 0.1346  0.2747  -0.1706 1162 LYS A CA  
1954 C C   . LYS A 252 ? 0.7735 0.7620 1.4452 0.1432  0.2999  -0.1777 1162 LYS A C   
1955 O O   . LYS A 252 ? 0.7622 0.7978 1.4668 0.1462  0.3074  -0.1627 1162 LYS A O   
1956 C CB  . LYS A 252 ? 0.7049 0.5885 1.3509 0.1017  0.2726  -0.1305 1162 LYS A CB  
1957 C CG  . LYS A 252 ? 0.7507 0.5600 1.3908 0.0898  0.2480  -0.1142 1162 LYS A CG  
1958 C CD  . LYS A 252 ? 0.7578 0.5642 1.4163 0.0995  0.2300  -0.1064 1162 LYS A CD  
1959 C CE  . LYS A 252 ? 0.6801 0.4489 1.3142 0.0752  0.2043  -0.0759 1162 LYS A CE  
1960 N NZ  . LYS A 252 ? 0.7615 0.5179 1.3998 0.0865  0.1821  -0.0753 1162 LYS A NZ  
1961 N N   . SER A 253 ? 0.7424 0.7600 1.3880 0.1455  0.3132  -0.1997 1163 SER A N   
1962 C CA  . SER A 253 ? 0.6888 0.7962 1.3391 0.1466  0.3385  -0.2007 1163 SER A CA  
1963 C C   . SER A 253 ? 0.7793 0.9387 1.4686 0.1773  0.3469  -0.2238 1163 SER A C   
1964 O O   . SER A 253 ? 0.6896 0.9248 1.4000 0.1739  0.3647  -0.2113 1163 SER A O   
1965 C CB  . SER A 253 ? 0.6876 0.8122 1.2981 0.1428  0.3493  -0.2208 1163 SER A CB  
1966 O OG  . SER A 253 ? 0.7392 0.8502 1.3457 0.1707  0.3463  -0.2659 1163 SER A OG  
1967 N N   . LYS A 254 ? 0.7745 0.8935 1.4652 0.2052  0.3299  -0.2551 1164 LYS A N   
1968 C CA  . LYS A 254 ? 0.8082 0.9721 1.5195 0.2349  0.3278  -0.2736 1164 LYS A CA  
1969 C C   . LYS A 254 ? 0.8701 1.0601 1.6202 0.2308  0.3242  -0.2451 1164 LYS A C   
1970 O O   . LYS A 254 ? 0.7970 1.0591 1.5699 0.2458  0.3331  -0.2508 1164 LYS A O   
1971 C CB  . LYS A 254 ? 0.8706 0.9692 1.5645 0.2629  0.3026  -0.3047 1164 LYS A CB  
1972 N N   . TYR A 255 ? 0.9270 1.0623 1.6834 0.2099  0.3113  -0.2143 1165 TYR A N   
1973 C CA  . TYR A 255 ? 0.8880 1.0434 1.6787 0.2019  0.3072  -0.1852 1165 TYR A CA  
1974 C C   . TYR A 255 ? 0.8014 1.0205 1.6008 0.1732  0.3308  -0.1546 1165 TYR A C   
1975 O O   . TYR A 255 ? 0.7622 1.0566 1.5827 0.1736  0.3420  -0.1489 1165 TYR A O   
1976 C CB  . TYR A 255 ? 0.9443 1.0113 1.7310 0.1907  0.2809  -0.1648 1165 TYR A CB  
1977 C CG  . TYR A 255 ? 1.0996 1.1045 1.8720 0.2135  0.2516  -0.1853 1165 TYR A CG  
1978 C CD1 . TYR A 255 ? 1.1681 1.1914 1.9646 0.2366  0.2392  -0.1910 1165 TYR A CD1 
1979 C CD2 . TYR A 255 ? 1.1599 1.0891 1.8905 0.2100  0.2349  -0.1965 1165 TYR A CD2 
1980 C CE1 . TYR A 255 ? 1.1881 1.1529 1.9647 0.2576  0.2114  -0.2068 1165 TYR A CE1 
1981 C CE2 . TYR A 255 ? 1.2434 1.1148 1.9516 0.2273  0.2066  -0.2107 1165 TYR A CE2 
1982 C CZ  . TYR A 255 ? 1.2492 1.1368 1.9794 0.2520  0.1952  -0.2153 1165 TYR A CZ  
1983 O OH  . TYR A 255 ? 1.3110 1.1395 2.0144 0.2705  0.1676  -0.2271 1165 TYR A OH  
1984 N N   . PHE A 256 ? 0.7259 0.9147 1.5031 0.1465  0.3361  -0.1329 1166 PHE A N   
1985 C CA  . PHE A 256 ? 0.6291 0.8621 1.3958 0.1154  0.3510  -0.0990 1166 PHE A CA  
1986 C C   . PHE A 256 ? 0.6285 0.8639 1.3490 0.1014  0.3616  -0.1008 1166 PHE A C   
1987 O O   . PHE A 256 ? 0.5867 0.7637 1.2790 0.1024  0.3504  -0.1121 1166 PHE A O   
1988 C CB  . PHE A 256 ? 0.5666 0.7536 1.3354 0.0912  0.3363  -0.0596 1166 PHE A CB  
1989 C CG  . PHE A 256 ? 0.5841 0.6812 1.3263 0.0851  0.3159  -0.0556 1166 PHE A CG  
1990 C CD1 . PHE A 256 ? 0.5468 0.6207 1.2479 0.0643  0.3173  -0.0425 1166 PHE A CD1 
1991 C CD2 . PHE A 256 ? 0.5653 0.6040 1.3235 0.0994  0.2949  -0.0638 1166 PHE A CD2 
1992 C CE1 . PHE A 256 ? 0.5516 0.5520 1.2305 0.0573  0.2997  -0.0394 1166 PHE A CE1 
1993 C CE2 . PHE A 256 ? 0.5615 0.5217 1.2941 0.0901  0.2771  -0.0589 1166 PHE A CE2 
1994 C CZ  . PHE A 256 ? 0.5656 0.5098 1.2597 0.0685  0.2803  -0.0472 1166 PHE A CZ  
1995 N N   . THR A 257 ? 0.5989 0.9036 1.3110 0.0871  0.3826  -0.0892 1167 THR A N   
1996 C CA  . THR A 257 ? 0.5899 0.9067 1.2578 0.0729  0.3936  -0.0876 1167 THR A CA  
1997 C C   . THR A 257 ? 0.5817 0.8696 1.2244 0.0412  0.3881  -0.0450 1167 THR A C   
1998 O O   . THR A 257 ? 0.5771 0.8465 1.2375 0.0289  0.3795  -0.0173 1167 THR A O   
1999 C CB  . THR A 257 ? 0.6690 1.0783 1.3377 0.0764  0.4194  -0.1005 1167 THR A CB  
2000 O OG1 . THR A 257 ? 0.6762 1.1050 1.3034 0.0517  0.4303  -0.0801 1167 THR A OG1 
2001 C CG2 . THR A 257 ? 0.6275 1.0926 1.3247 0.0742  0.4205  -0.0870 1167 THR A CG2 
2002 N N   . CYS A 258 ? 0.5949 0.8783 1.1949 0.0293  0.3920  -0.0411 1168 CYS A N   
2003 C CA  . CYS A 258 ? 0.5850 0.8320 1.1565 0.0047  0.3834  -0.0053 1168 CYS A CA  
2004 C C   . CYS A 258 ? 0.5328 0.8210 1.1031 -0.0174 0.3942  0.0294  1168 CYS A C   
2005 O O   . CYS A 258 ? 0.6150 0.9679 1.1904 -0.0180 0.4081  0.0253  1168 CYS A O   
2006 C CB  . CYS A 258 ? 0.5910 0.8257 1.1177 0.0008  0.3832  -0.0127 1168 CYS A CB  
2007 S SG  . CYS A 258 ? 0.5371 0.7233 1.0278 -0.0226 0.3692  0.0259  1168 CYS A SG  
2008 N N   . GLN A 259 ? 0.5844 0.8280 1.1357 -0.0361 0.3797  0.0630  1169 GLN A N   
2009 C CA  . GLN A 259 ? 0.5282 0.7872 1.0536 -0.0584 0.3737  0.0958  1169 GLN A CA  
2010 C C   . GLN A 259 ? 0.5758 0.7967 1.0521 -0.0737 0.3619  0.1210  1169 GLN A C   
2011 O O   . GLN A 259 ? 0.6091 0.8203 1.0603 -0.0911 0.3494  0.1483  1169 GLN A O   
2012 C CB  . GLN A 259 ? 0.5159 0.7550 1.0639 -0.0632 0.3580  0.1108  1169 GLN A CB  
2013 C CG  . GLN A 259 ? 0.5685 0.8399 1.1690 -0.0455 0.3656  0.0877  1169 GLN A CG  
2014 C CD  . GLN A 259 ? 0.5291 0.8851 1.1372 -0.0447 0.3849  0.0756  1169 GLN A CD  
2015 O OE1 . GLN A 259 ? 0.5456 0.9353 1.1239 -0.0661 0.3893  0.0948  1169 GLN A OE1 
2016 N NE2 . GLN A 259 ? 0.5382 0.9285 1.1832 -0.0193 0.3950  0.0420  1169 GLN A NE2 
2017 N N   . CYS A 260 ? 0.5307 0.7278 0.9923 -0.0670 0.3635  0.1113  1170 CYS A N   
2018 C CA  . CYS A 260 ? 0.5761 0.7422 0.9926 -0.0783 0.3513  0.1346  1170 CYS A CA  
2019 C C   . CYS A 260 ? 0.5839 0.7926 0.9657 -0.0930 0.3608  0.1509  1170 CYS A C   
2020 O O   . CYS A 260 ? 0.6533 0.8391 1.0012 -0.1072 0.3462  0.1782  1170 CYS A O   
2021 C CB  . CYS A 260 ? 0.5321 0.6754 0.9423 -0.0692 0.3534  0.1191  1170 CYS A CB  
2022 S SG  . CYS A 260 ? 0.5565 0.7504 0.9421 -0.0612 0.3690  0.0905  1170 CYS A SG  
2023 N N   . GLY A 261 ? 0.5807 0.8500 0.9678 -0.0895 0.3840  0.1326  1171 GLY A N   
2024 C CA  . GLY A 261 ? 0.6115 0.9260 0.9648 -0.1055 0.3941  0.1476  1171 GLY A CA  
2025 C C   . GLY A 261 ? 0.6797 0.9828 0.9868 -0.1105 0.3940  0.1606  1171 GLY A C   
2026 O O   . GLY A 261 ? 0.7922 1.1175 1.0633 -0.1275 0.3970  0.1809  1171 GLY A O   
2027 N N   . SER A 262 ? 0.7061 0.9755 1.0115 -0.0978 0.3901  0.1503  1172 SER A N   
2028 C CA  . SER A 262 ? 0.7630 1.0299 1.0210 -0.0989 0.3857  0.1566  1172 SER A CA  
2029 C C   . SER A 262 ? 0.7855 1.1129 1.0270 -0.0955 0.4033  0.1333  1172 SER A C   
2030 O O   . SER A 262 ? 0.7532 1.1079 1.0213 -0.0828 0.4134  0.0991  1172 SER A O   
2031 C CB  . SER A 262 ? 0.7877 1.0085 1.0426 -0.0860 0.3674  0.1438  1172 SER A CB  
2032 O OG  . SER A 262 ? 0.8274 1.0560 1.0392 -0.0846 0.3630  0.1446  1172 SER A OG  
2033 N N   . GLU A 263 ? 0.8211 1.1671 1.0158 -0.1060 0.4058  0.1519  1173 GLU A N   
2034 C CA  . GLU A 263 ? 0.8274 1.2338 0.9998 -0.1055 0.4229  0.1332  1173 GLU A CA  
2035 C C   . GLU A 263 ? 0.8686 1.2829 1.0516 -0.0852 0.4232  0.0880  1173 GLU A C   
2036 O O   . GLU A 263 ? 0.8161 1.2804 1.0042 -0.0789 0.4402  0.0596  1173 GLU A O   
2037 C CB  . GLU A 263 ? 0.8468 1.2570 0.9613 -0.1173 0.4187  0.1600  1173 GLU A CB  
2038 N N   . LYS A 264 ? 0.9004 1.2659 1.0858 -0.0757 0.4045  0.0800  1174 LYS A N   
2039 C CA  . LYS A 264 ? 0.8694 1.2315 1.0649 -0.0599 0.4016  0.0385  1174 LYS A CA  
2040 C C   . LYS A 264 ? 0.8089 1.1359 1.0525 -0.0506 0.3962  0.0233  1174 LYS A C   
2041 O O   . LYS A 264 ? 0.8524 1.1313 1.1051 -0.0472 0.3794  0.0212  1174 LYS A O   
2042 C CB  . LYS A 264 ? 0.9686 1.3068 1.1329 -0.0585 0.3845  0.0386  1174 LYS A CB  
2043 C CG  . LYS A 264 ? 0.9978 1.3424 1.1588 -0.0479 0.3826  -0.0035 1174 LYS A CG  
2044 C CD  . LYS A 264 ? 0.9997 1.3209 1.1367 -0.0486 0.3635  -0.0010 1174 LYS A CD  
2045 C CE  . LYS A 264 ? 0.9769 1.3078 1.1051 -0.0427 0.3611  -0.0418 1174 LYS A CE  
2046 N NZ  . LYS A 264 ? 0.9962 1.3792 1.0890 -0.0429 0.3727  -0.0546 1174 LYS A NZ  
2047 N N   . CYS A 265 ? 0.7921 1.1471 1.0664 -0.0466 0.4106  0.0132  1175 CYS A N   
2048 C CA  . CYS A 265 ? 0.7604 1.0873 1.0803 -0.0355 0.4060  -0.0025 1175 CYS A CA  
2049 C C   . CYS A 265 ? 0.7530 1.0860 1.0821 -0.0170 0.4088  -0.0492 1175 CYS A C   
2050 O O   . CYS A 265 ? 0.7583 1.1407 1.0741 -0.0111 0.4239  -0.0711 1175 CYS A O   
2051 C CB  . CYS A 265 ? 0.6318 0.9870 0.9827 -0.0398 0.4179  0.0123  1175 CYS A CB  
2052 S SG  . CYS A 265 ? 0.6036 0.9212 1.0104 -0.0274 0.4087  0.0024  1175 CYS A SG  
2053 N N   . LYS A 266 ? 0.7279 1.0081 1.0770 -0.0084 0.3936  -0.0646 1176 LYS A N   
2054 C CA  . LYS A 266 ? 0.7377 1.0068 1.0902 0.0075  0.3913  -0.1079 1176 LYS A CA  
2055 C C   . LYS A 266 ? 0.7096 0.9781 1.1025 0.0258  0.3952  -0.1301 1176 LYS A C   
2056 O O   . LYS A 266 ? 0.7027 0.9783 1.0961 0.0426  0.3988  -0.1687 1176 LYS A O   
2057 C CB  . LYS A 266 ? 0.7497 0.9585 1.0924 0.0032  0.3704  -0.1126 1176 LYS A CB  
2058 C CG  . LYS A 266 ? 0.7927 0.9920 1.1180 0.0111  0.3665  -0.1534 1176 LYS A CG  
2059 C CD  . LYS A 266 ? 0.8424 0.9865 1.1583 0.0014  0.3460  -0.1547 1176 LYS A CD  
2060 C CE  . LYS A 266 ? 0.9125 1.0416 1.2113 0.0063  0.3406  -0.1964 1176 LYS A CE  
2061 N NZ  . LYS A 266 ? 0.8048 0.8766 1.1008 -0.0049 0.3204  -0.1999 1176 LYS A NZ  
2062 N N   . HIS A 267 ? 0.6384 0.8985 1.0640 0.0240  0.3937  -0.1076 1177 HIS A N   
2063 C CA  . HIS A 267 ? 0.6528 0.9078 1.1195 0.0426  0.3933  -0.1262 1177 HIS A CA  
2064 C C   . HIS A 267 ? 0.6844 0.9954 1.1778 0.0411  0.4088  -0.1089 1177 HIS A C   
2065 O O   . HIS A 267 ? 0.6599 0.9648 1.1920 0.0511  0.4053  -0.1095 1177 HIS A O   
2066 C CB  . HIS A 267 ? 0.6210 0.8025 1.1056 0.0426  0.3715  -0.1195 1177 HIS A CB  
2067 C CG  . HIS A 267 ? 0.6668 0.7962 1.1241 0.0371  0.3562  -0.1302 1177 HIS A CG  
2068 N ND1 . HIS A 267 ? 0.6339 0.7427 1.0675 0.0175  0.3478  -0.1042 1177 HIS A ND1 
2069 C CD2 . HIS A 267 ? 0.6617 0.7578 1.1105 0.0477  0.3475  -0.1649 1177 HIS A CD2 
2070 C CE1 . HIS A 267 ? 0.6602 0.7313 1.0749 0.0151  0.3354  -0.1220 1177 HIS A CE1 
2071 N NE2 . HIS A 267 ? 0.6907 0.7506 1.1127 0.0314  0.3347  -0.1582 1177 HIS A NE2 
2072 N N   . SER A 268 ? 0.6646 1.0320 1.1364 0.0275  0.4253  -0.0933 1178 SER A N   
2073 C CA  . SER A 268 ? 0.6368 1.0619 1.1287 0.0194  0.4408  -0.0737 1178 SER A CA  
2074 C C   . SER A 268 ? 0.7253 1.2046 1.2494 0.0428  0.4551  -0.1081 1178 SER A C   
2075 O O   . SER A 268 ? 0.7281 1.2000 1.2528 0.0664  0.4538  -0.1481 1178 SER A O   
2076 C CB  . SER A 268 ? 0.6470 1.1169 1.1008 -0.0024 0.4546  -0.0498 1178 SER A CB  
2077 O OG  . SER A 268 ? 0.6806 1.1965 1.1502 -0.0175 0.4661  -0.0237 1178 SER A OG  
2078 N N   . ALA A 269 ? 0.6412 1.1746 1.1883 0.0361  0.4653  -0.0918 1179 ALA A N   
2079 C CA  . ALA A 269 ? 0.7319 1.3319 1.2971 0.0568  0.4751  -0.1192 1179 ALA A CA  
2080 C C   . ALA A 269 ? 0.7669 1.4167 1.2955 0.0613  0.4909  -0.1400 1179 ALA A C   
2081 O O   . ALA A 269 ? 0.7510 1.4056 1.2797 0.0885  0.4924  -0.1813 1179 ALA A O   
2082 C CB  . ALA A 269 ? 0.6573 1.3096 1.2424 0.0427  0.4779  -0.0911 1179 ALA A CB  
2083 N N   . GLU A 270 ? 0.8753 1.5564 1.3679 0.0347  0.5004  -0.1107 1180 GLU A N   
2084 C CA  . GLU A 270 ? 0.9107 1.6409 1.3656 0.0368  0.5154  -0.1246 1180 GLU A CA  
2085 C C   . GLU A 270 ? 0.9429 1.6350 1.3681 0.0451  0.5120  -0.1531 1180 GLU A C   
2086 O O   . GLU A 270 ? 0.9591 1.6839 1.3596 0.0572  0.5207  -0.1798 1180 GLU A O   
2087 C CB  . GLU A 270 ? 0.9579 1.7218 1.3801 0.0050  0.5247  -0.0812 1180 GLU A CB  
2088 C CG  . GLU A 270 ? 0.9787 1.6918 1.3822 -0.0229 0.5131  -0.0421 1180 GLU A CG  
2089 C CD  . GLU A 270 ? 0.9507 1.6877 1.3182 -0.0521 0.5206  0.0009  1180 GLU A CD  
2090 O OE1 . GLU A 270 ? 0.9679 1.7444 1.3087 -0.0539 0.5354  -0.0063 1180 GLU A OE1 
2091 O OE2 . GLU A 270 ? 0.9509 1.6588 1.3135 -0.0748 0.5093  0.0395  1180 GLU A OE2 
2092 N N   . ALA A 271 ? 0.8887 1.5108 1.3150 0.0385  0.4994  -0.1474 1181 ALA A N   
2093 C CA  . ALA A 271 ? 0.8833 1.4633 1.2790 0.0461  0.4893  -0.1719 1181 ALA A CA  
2094 C C   . ALA A 271 ? 0.8843 1.4429 1.3004 0.0773  0.4840  -0.2207 1181 ALA A C   
2095 O O   . ALA A 271 ? 0.9176 1.4603 1.3055 0.0858  0.4801  -0.2504 1181 ALA A O   
2096 C CB  . ALA A 271 ? 0.8315 1.3364 1.2130 0.0305  0.4666  -0.1430 1181 ALA A CB  
2097 N N   . ILE A 272 ? 0.8452 1.4006 1.3077 0.0944  0.4820  -0.2296 1182 ILE A N   
2098 C CA  . ILE A 272 ? 0.8253 1.3609 1.3058 0.1274  0.4758  -0.2760 1182 ILE A CA  
2099 C C   . ILE A 272 ? 0.9879 1.5880 1.4502 0.1455  0.4877  -0.3033 1182 ILE A C   
2100 O O   . ILE A 272 ? 1.0521 1.6336 1.4985 0.1665  0.4833  -0.3437 1182 ILE A O   
2101 C CB  . ILE A 272 ? 0.7635 1.2737 1.2927 0.1414  0.4640  -0.2710 1182 ILE A CB  
2102 C CG1 . ILE A 272 ? 0.8074 1.2284 1.3402 0.1297  0.4408  -0.2499 1182 ILE A CG1 
2103 C CG2 . ILE A 272 ? 0.8472 1.3565 1.3902 0.1789  0.4570  -0.3132 1182 ILE A CG2 
2104 C CD1 . ILE A 272 ? 0.7490 1.1491 1.3276 0.1357  0.4307  -0.2346 1182 ILE A CD1 
2105 N N   . ALA A 273 ? 1.0180 1.6906 1.4797 0.1360  0.5027  -0.2803 1183 ALA A N   
2106 C CA  . ALA A 273 ? 1.0180 1.7527 1.4662 0.1524  0.5162  -0.3022 1183 ALA A CA  
2107 C C   . ALA A 273 ? 1.0704 1.8153 1.4671 0.1458  0.5231  -0.3171 1183 ALA A C   
2108 O O   . ALA A 273 ? 1.1244 1.8937 1.5066 0.1661  0.5287  -0.3506 1183 ALA A O   
2109 C CB  . ALA A 273 ? 0.9846 1.7892 1.4460 0.1386  0.5311  -0.2699 1183 ALA A CB  
2110 N N   . LEU A 274 ? 1.0223 1.7492 1.3898 0.1182  0.5220  -0.2930 1184 LEU A N   
2111 C CA  . LEU A 274 ? 1.0202 1.7577 1.3372 0.1114  0.5264  -0.3061 1184 LEU A CA  
2112 C C   . LEU A 274 ? 1.0959 1.7844 1.4031 0.1322  0.5146  -0.3533 1184 LEU A C   
2113 O O   . LEU A 274 ? 1.1360 1.8441 1.4148 0.1445  0.5187  -0.3842 1184 LEU A O   
2114 C CB  . LEU A 274 ? 0.9087 1.6363 1.1967 0.0787  0.5254  -0.2678 1184 LEU A CB  
2115 C CG  . LEU A 274 ? 0.9268 1.6661 1.1610 0.0719  0.5275  -0.2807 1184 LEU A CG  
2116 C CD1 . LEU A 274 ? 0.9716 1.7770 1.1817 0.0721  0.5431  -0.2812 1184 LEU A CD1 
2117 C CD2 . LEU A 274 ? 0.9530 1.6713 1.1594 0.0443  0.5216  -0.2471 1184 LEU A CD2 
2118 N N   . GLU A 275 ? 1.1141 1.7343 1.4429 0.1343  0.4993  -0.3590 1185 GLU A N   
2119 C CA  . GLU A 275 ? 1.1642 1.7278 1.4844 0.1524  0.4858  -0.4031 1185 GLU A CA  
2120 C C   . GLU A 275 ? 1.2541 1.8180 1.5924 0.1875  0.4823  -0.4383 1185 GLU A C   
2121 O O   . GLU A 275 ? 1.2666 1.8067 1.5823 0.2045  0.4756  -0.4782 1185 GLU A O   
2122 C CB  . GLU A 275 ? 1.1675 1.6476 1.5022 0.1429  0.4654  -0.3917 1185 GLU A CB  
2123 C CG  . GLU A 275 ? 1.1784 1.6334 1.4761 0.1133  0.4550  -0.3636 1185 GLU A CG  
2124 C CD  . GLU A 275 ? 1.1812 1.6319 1.4345 0.1130  0.4519  -0.3960 1185 GLU A CD  
2125 O OE1 . GLU A 275 ? 1.1883 1.6292 1.4394 0.1357  0.4516  -0.4421 1185 GLU A OE1 
2126 O OE2 . GLU A 275 ? 1.1738 1.6299 1.3932 0.0910  0.4486  -0.3759 1185 GLU A OE2 
2127 N N   . GLN A 276 ? 1.4347 2.0246 1.8119 0.1987  0.4859  -0.4241 1186 GLN A N   
2128 C CA  . GLN A 276 ? 1.4399 2.0375 1.8340 0.2339  0.4833  -0.4554 1186 GLN A CA  
2129 C C   . GLN A 276 ? 1.4904 2.1589 1.8596 0.2419  0.5009  -0.4704 1186 GLN A C   
2130 O O   . GLN A 276 ? 1.5560 2.2199 1.9202 0.2710  0.4980  -0.5084 1186 GLN A O   
2131 C CB  . GLN A 276 ? 1.4167 2.0252 1.8606 0.2426  0.4812  -0.4349 1186 GLN A CB  
2132 C CG  . GLN A 276 ? 1.4812 2.0906 1.9465 0.2815  0.4753  -0.4657 1186 GLN A CG  
2133 C CD  . GLN A 276 ? 1.4836 2.0018 1.9640 0.3010  0.4490  -0.4839 1186 GLN A CD  
2134 O OE1 . GLN A 276 ? 1.5164 1.9764 2.0032 0.2833  0.4365  -0.4670 1186 GLN A OE1 
2135 N NE2 . GLN A 276 ? 1.4698 1.9718 1.9540 0.3366  0.4401  -0.5169 1186 GLN A NE2 
2136 N N   . SER A 277 ? 1.2646 1.9942 1.6158 0.2160  0.5183  -0.4404 1187 SER A N   
2137 C CA  . SER A 277 ? 1.2449 2.0399 1.5702 0.2198  0.5352  -0.4529 1187 SER A CA  
2138 C C   . SER A 277 ? 1.2287 2.0081 1.5034 0.2160  0.5330  -0.4780 1187 SER A C   
2139 O O   . SER A 277 ? 1.2432 2.0415 1.4993 0.2350  0.5373  -0.5126 1187 SER A O   
2140 C CB  . SER A 277 ? 1.2197 2.0821 1.5436 0.1919  0.5531  -0.4094 1187 SER A CB  
2141 O OG  . SER A 277 ? 1.2311 2.1569 1.5325 0.1946  0.5695  -0.4219 1187 SER A OG  
2142 N N   . ARG A 278 ? 1.2098 1.9567 1.4616 0.1914  0.5262  -0.4615 1188 ARG A N   
2143 C CA  . ARG A 278 ? 1.1821 1.9104 1.3872 0.1874  0.5213  -0.4868 1188 ARG A CA  
2144 C C   . ARG A 278 ? 1.2211 1.8893 1.4266 0.2150  0.5054  -0.5355 1188 ARG A C   
2145 O O   . ARG A 278 ? 1.2303 1.9059 1.4065 0.2286  0.5063  -0.5702 1188 ARG A O   
2146 C CB  . ARG A 278 ? 1.1484 1.8500 1.3341 0.1573  0.5148  -0.4602 1188 ARG A CB  
2147 C CG  . ARG A 278 ? 1.1391 1.8045 1.2851 0.1548  0.5038  -0.4912 1188 ARG A CG  
2148 C CD  . ARG A 278 ? 1.1265 1.7707 1.2554 0.1257  0.4974  -0.4651 1188 ARG A CD  
2149 N NE  . ARG A 278 ? 1.1434 1.7498 1.2388 0.1227  0.4849  -0.4972 1188 ARG A NE  
2150 C CZ  . ARG A 278 ? 1.1797 1.7173 1.2854 0.1216  0.4689  -0.5140 1188 ARG A CZ  
2151 N NH1 . ARG A 278 ? 1.1291 1.6180 1.2752 0.1237  0.4580  -0.4947 1188 ARG A NH1 
2152 N NH2 . ARG A 278 ? 1.1721 1.6768 1.2419 0.1149  0.4546  -0.5390 1188 ARG A NH2 
2153 N N   . LEU A 279 ? 1.2068 1.8107 1.4433 0.2228  0.4896  -0.5380 1189 LEU A N   
2154 C CA  . LEU A 279 ? 1.2293 1.7649 1.4665 0.2487  0.4712  -0.5801 1189 LEU A CA  
2155 C C   . LEU A 279 ? 1.2335 1.7812 1.5039 0.2821  0.4720  -0.5930 1189 LEU A C   
2156 O O   . LEU A 279 ? 1.2775 1.8047 1.5367 0.3093  0.4654  -0.6311 1189 LEU A O   
2157 C CB  . LEU A 279 ? 1.1824 1.6340 1.4316 0.2380  0.4512  -0.5758 1189 LEU A CB  
2158 C CG  . LEU A 279 ? 1.1706 1.6091 1.3957 0.2036  0.4502  -0.5586 1189 LEU A CG  
2159 C CD1 . LEU A 279 ? 1.1276 1.4786 1.3677 0.1952  0.4304  -0.5588 1189 LEU A CD1 
2160 C CD2 . LEU A 279 ? 1.1796 1.6325 1.3527 0.1970  0.4516  -0.5840 1189 LEU A CD2 
2161 N N   . ARG B 7   ? 0.5368 1.0917 1.3163 0.2356  0.2328  -0.1255 917  ARG B N   
2162 C CA  . ARG B 7   ? 0.5419 1.1068 1.3185 0.2314  0.1978  -0.0962 917  ARG B CA  
2163 C C   . ARG B 7   ? 0.6454 1.1270 1.3966 0.2321  0.1928  -0.0993 917  ARG B C   
2164 O O   . ARG B 7   ? 0.6375 1.0661 1.3593 0.2118  0.2036  -0.1270 917  ARG B O   
2165 C CB  . ARG B 7   ? 0.5006 1.1108 1.2626 0.1925  0.1747  -0.0933 917  ARG B CB  
2166 C CG  . ARG B 7   ? 0.3767 0.9968 1.1312 0.1831  0.1371  -0.0664 917  ARG B CG  
2167 C CD  . ARG B 7   ? 0.3259 0.9898 1.0669 0.1427  0.1141  -0.0639 917  ARG B CD  
2168 N NE  . ARG B 7   ? 0.3253 1.0672 1.0968 0.1407  0.1116  -0.0428 917  ARG B NE  
2169 C CZ  . ARG B 7   ? 0.3047 1.0831 1.0946 0.1254  0.0820  -0.0124 917  ARG B CZ  
2170 N NH1 . ARG B 7   ? 0.2852 1.0364 1.0542 0.1124  0.0505  -0.0041 917  ARG B NH1 
2171 N NH2 . ARG B 7   ? 0.3131 1.1371 1.1438 0.1170  0.0805  -0.0116 917  ARG B NH2 
2172 N N   . THR B 8   ? 0.7338 1.2074 1.4953 0.2533  0.1757  -0.0708 918  THR B N   
2173 C CA  . THR B 8   ? 0.7685 1.1696 1.5052 0.2528  0.1688  -0.0678 918  THR B CA  
2174 C C   . THR B 8   ? 0.7117 1.1051 1.4167 0.2199  0.1468  -0.0721 918  THR B C   
2175 O O   . THR B 8   ? 0.7148 1.1626 1.4209 0.2008  0.1282  -0.0666 918  THR B O   
2176 C CB  . THR B 8   ? 0.8240 1.2252 1.5772 0.2789  0.1529  -0.0338 918  THR B CB  
2177 O OG1 . THR B 8   ? 0.8239 1.1573 1.5501 0.2759  0.1469  -0.0297 918  THR B OG1 
2178 C CG2 . THR B 8   ? 0.8392 1.3097 1.6013 0.2719  0.1206  -0.0080 918  THR B CG2 
2179 N N   . GLU B 9   ? 0.6625 0.9881 1.3392 0.2122  0.1479  -0.0816 919  GLU B N   
2180 C CA  . GLU B 9   ? 0.5326 0.8436 1.1790 0.1835  0.1290  -0.0887 919  GLU B CA  
2181 C C   . GLU B 9   ? 0.6017 0.8957 1.2389 0.1934  0.1044  -0.0589 919  GLU B C   
2182 O O   . GLU B 9   ? 0.6920 0.9293 1.3133 0.2007  0.1091  -0.0566 919  GLU B O   
2183 C CB  . GLU B 9   ? 0.5378 0.7933 1.1565 0.1642  0.1477  -0.1225 919  GLU B CB  
2184 C CG  . GLU B 9   ? 0.4943 0.7571 1.0870 0.1299  0.1334  -0.1394 919  GLU B CG  
2185 C CD  . GLU B 9   ? 0.4840 0.6892 1.0453 0.1126  0.1458  -0.1642 919  GLU B CD  
2186 O OE1 . GLU B 9   ? 0.4527 0.6067 1.0040 0.1244  0.1467  -0.1540 919  GLU B OE1 
2187 O OE2 . GLU B 9   ? 0.4335 0.6495 0.9781 0.0849  0.1537  -0.1920 919  GLU B OE2 
2188 N N   . LYS B 10  ? 0.5037 0.8492 1.1474 0.1899  0.0770  -0.0366 920  LYS B N   
2189 C CA  . LYS B 10  ? 0.5560 0.8996 1.1927 0.2011  0.0535  -0.0057 920  LYS B CA  
2190 C C   . LYS B 10  ? 0.4819 0.7936 1.0840 0.1818  0.0341  -0.0078 920  LYS B C   
2191 O O   . LYS B 10  ? 0.4424 0.7730 1.0341 0.1566  0.0196  -0.0197 920  LYS B O   
2192 C CB  . LYS B 10  ? 0.5682 0.9847 1.2243 0.2030  0.0320  0.0177  920  LYS B CB  
2193 C CG  . LYS B 10  ? 0.5799 1.0000 1.2242 0.2094  0.0060  0.0472  920  LYS B CG  
2194 C CD  . LYS B 10  ? 0.5794 1.0668 1.2288 0.1962  -0.0216 0.0634  920  LYS B CD  
2195 C CE  . LYS B 10  ? 0.6495 1.1393 1.2853 0.2014  -0.0443 0.0914  920  LYS B CE  
2196 N NZ  . LYS B 10  ? 0.6992 1.1837 1.3618 0.2313  -0.0308 0.1096  920  LYS B NZ  
2197 N N   . ILE B 11  ? 0.5666 0.8317 1.1503 0.1926  0.0326  0.0039  921  ILE B N   
2198 C CA  . ILE B 11  ? 0.5194 0.7593 1.0697 0.1785  0.0125  0.0067  921  ILE B CA  
2199 C C   . ILE B 11  ? 0.5242 0.8114 1.0701 0.1733  -0.0192 0.0295  921  ILE B C   
2200 O O   . ILE B 11  ? 0.5285 0.8405 1.0835 0.1888  -0.0267 0.0543  921  ILE B O   
2201 C CB  . ILE B 11  ? 0.5840 0.7687 1.1149 0.1902  0.0197  0.0156  921  ILE B CB  
2202 C CG1 . ILE B 11  ? 0.6568 0.7938 1.1887 0.1907  0.0498  -0.0071 921  ILE B CG1 
2203 C CG2 . ILE B 11  ? 0.5383 0.7016 1.0331 0.1766  -0.0001 0.0185  921  ILE B CG2 
2204 C CD1 . ILE B 11  ? 0.6840 0.7657 1.1919 0.1926  0.0545  -0.0019 921  ILE B CD1 
2205 N N   . ILE B 12  ? 0.3957 0.6943 0.9245 0.1486  -0.0397 0.0194  922  ILE B N   
2206 C CA  . ILE B 12  ? 0.3305 0.6710 0.8449 0.1352  -0.0706 0.0360  922  ILE B CA  
2207 C C   . ILE B 12  ? 0.2557 0.5635 0.7164 0.1208  -0.0916 0.0371  922  ILE B C   
2208 O O   . ILE B 12  ? 0.2586 0.5947 0.7033 0.1119  -0.1162 0.0517  922  ILE B O   
2209 C CB  . ILE B 12  ? 0.3460 0.7266 0.8588 0.1102  -0.0778 0.0238  922  ILE B CB  
2210 C CG1 . ILE B 12  ? 0.3228 0.6688 0.8084 0.0885  -0.0666 -0.0066 922  ILE B CG1 
2211 C CG2 . ILE B 12  ? 0.3212 0.7555 0.8873 0.1267  -0.0636 0.0328  922  ILE B CG2 
2212 C CD1 . ILE B 12  ? 0.2789 0.6669 0.7686 0.0647  -0.0701 -0.0167 922  ILE B CD1 
2213 N N   . CYS B 13  ? 0.2897 0.5420 0.7220 0.1180  -0.0824 0.0223  923  CYS B N   
2214 C CA  . CYS B 13  ? 0.3065 0.5298 0.6926 0.1103  -0.0991 0.0254  923  CYS B CA  
2215 C C   . CYS B 13  ? 0.2624 0.4354 0.6427 0.1219  -0.0812 0.0205  923  CYS B C   
2216 O O   . CYS B 13  ? 0.2574 0.4050 0.6373 0.1151  -0.0637 0.0001  923  CYS B O   
2217 C CB  . CYS B 13  ? 0.2508 0.4649 0.5932 0.0803  -0.1146 0.0080  923  CYS B CB  
2218 S SG  . CYS B 13  ? 0.3378 0.5124 0.6206 0.0711  -0.1320 0.0066  923  CYS B SG  
2219 N N   . ARG B 14  ? 0.2738 0.4370 0.6507 0.1376  -0.0854 0.0403  924  ARG B N   
2220 C CA  . ARG B 14  ? 0.3081 0.4258 0.6814 0.1470  -0.0687 0.0381  924  ARG B CA  
2221 C C   . ARG B 14  ? 0.2727 0.3560 0.5985 0.1283  -0.0722 0.0205  924  ARG B C   
2222 O O   . ARG B 14  ? 0.2984 0.3471 0.6211 0.1289  -0.0562 0.0123  924  ARG B O   
2223 C CB  . ARG B 14  ? 0.3545 0.4710 0.7202 0.1630  -0.0686 0.0645  924  ARG B CB  
2224 C CG  . ARG B 14  ? 0.3729 0.5195 0.7713 0.1787  -0.0625 0.0809  924  ARG B CG  
2225 C CD  . ARG B 14  ? 0.3571 0.4778 0.7605 0.1942  -0.0476 0.0947  924  ARG B CD  
2226 N NE  . ARG B 14  ? 0.3927 0.5275 0.8339 0.2091  -0.0343 0.1013  924  ARG B NE  
2227 C CZ  . ARG B 14  ? 0.4684 0.5815 0.9304 0.2123  -0.0111 0.0844  924  ARG B CZ  
2228 N NH1 . ARG B 14  ? 0.5180 0.5962 0.9668 0.1991  0.0012  0.0596  924  ARG B NH1 
2229 N NH2 . ARG B 14  ? 0.4130 0.5408 0.9095 0.2283  0.0004  0.0920  924  ARG B NH2 
2230 N N   . ASP B 15  ? 0.2800 0.3719 0.5708 0.1112  -0.0916 0.0143  925  ASP B N   
2231 C CA  . ASP B 15  ? 0.3164 0.3776 0.5665 0.0956  -0.0939 -0.0012 925  ASP B CA  
2232 C C   . ASP B 15  ? 0.3177 0.3890 0.5395 0.0767  -0.1129 -0.0096 925  ASP B C   
2233 O O   . ASP B 15  ? 0.2903 0.3686 0.4892 0.0759  -0.1297 -0.0022 925  ASP B O   
2234 C CB  . ASP B 15  ? 0.3164 0.3547 0.5432 0.1053  -0.0950 0.0093  925  ASP B CB  
2235 C CG  . ASP B 15  ? 0.3565 0.3646 0.5487 0.0936  -0.0927 -0.0044 925  ASP B CG  
2236 O OD1 . ASP B 15  ? 0.3165 0.3152 0.5094 0.0806  -0.0844 -0.0199 925  ASP B OD1 
2237 O OD2 . ASP B 15  ? 0.3371 0.3348 0.5021 0.0982  -0.0988 0.0021  925  ASP B OD2 
2238 N N   . VAL B 16  ? 0.3175 0.3888 0.5390 0.0594  -0.1102 -0.0253 926  VAL B N   
2239 C CA  . VAL B 16  ? 0.2864 0.3609 0.4817 0.0400  -0.1278 -0.0320 926  VAL B CA  
2240 C C   . VAL B 16  ? 0.3486 0.3881 0.5031 0.0375  -0.1335 -0.0360 926  VAL B C   
2241 O O   . VAL B 16  ? 0.3346 0.3682 0.4618 0.0267  -0.1489 -0.0395 926  VAL B O   
2242 C CB  . VAL B 16  ? 0.3026 0.3869 0.5081 0.0212  -0.1234 -0.0445 926  VAL B CB  
2243 C CG1 . VAL B 16  ? 0.2356 0.3592 0.4825 0.0249  -0.1160 -0.0419 926  VAL B CG1 
2244 C CG2 . VAL B 16  ? 0.2993 0.3577 0.4983 0.0170  -0.1080 -0.0546 926  VAL B CG2 
2245 N N   . ALA B 17  ? 0.3509 0.3669 0.5011 0.0473  -0.1203 -0.0358 927  ALA B N   
2246 C CA  . ALA B 17  ? 0.3552 0.3429 0.4709 0.0489  -0.1230 -0.0374 927  ALA B CA  
2247 C C   . ALA B 17  ? 0.3839 0.3725 0.4793 0.0600  -0.1333 -0.0287 927  ALA B C   
2248 O O   . ALA B 17  ? 0.4293 0.3969 0.4934 0.0617  -0.1360 -0.0321 927  ALA B O   
2249 C CB  . ALA B 17  ? 0.3460 0.3171 0.4659 0.0545  -0.1061 -0.0373 927  ALA B CB  
2250 N N   . ARG B 18  ? 0.4076 0.4235 0.5200 0.0673  -0.1388 -0.0170 928  ARG B N   
2251 C CA  . ARG B 18  ? 0.4491 0.4742 0.5418 0.0757  -0.1493 -0.0064 928  ARG B CA  
2252 C C   . ARG B 18  ? 0.4276 0.4313 0.5024 0.0883  -0.1402 -0.0019 928  ARG B C   
2253 O O   . ARG B 18  ? 0.4685 0.4681 0.5106 0.0902  -0.1473 -0.0023 928  ARG B O   
2254 C CB  . ARG B 18  ? 0.4298 0.4556 0.4887 0.0605  -0.1673 -0.0165 928  ARG B CB  
2255 C CG  . ARG B 18  ? 0.4416 0.4879 0.5137 0.0426  -0.1778 -0.0217 928  ARG B CG  
2256 C CD  . ARG B 18  ? 0.4596 0.5122 0.4985 0.0259  -0.1977 -0.0285 928  ARG B CD  
2257 N NE  . ARG B 18  ? 0.4848 0.5006 0.4789 0.0251  -0.1987 -0.0413 928  ARG B NE  
2258 C CZ  . ARG B 18  ? 0.4876 0.4623 0.4645 0.0206  -0.1927 -0.0559 928  ARG B CZ  
2259 N NH1 . ARG B 18  ? 0.4031 0.3697 0.4007 0.0136  -0.1869 -0.0589 928  ARG B NH1 
2260 N NH2 . ARG B 18  ? 0.5322 0.4759 0.4710 0.0238  -0.1919 -0.0667 928  ARG B NH2 
2261 N N   . GLY B 19  ? 0.5070 0.4984 0.6018 0.0951  -0.1238 0.0011  929  GLY B N   
2262 C CA  . GLY B 19  ? 0.4863 0.4644 0.5707 0.1062  -0.1146 0.0095  929  GLY B CA  
2263 C C   . GLY B 19  ? 0.4671 0.4215 0.5234 0.1024  -0.1102 -0.0013 929  GLY B C   
2264 O O   . GLY B 19  ? 0.5141 0.4620 0.5625 0.1108  -0.1021 0.0066  929  GLY B O   
2265 N N   . TYR B 20  ? 0.4462 0.3895 0.4897 0.0904  -0.1151 -0.0165 930  TYR B N   
2266 C CA  . TYR B 20  ? 0.4493 0.3715 0.4698 0.0894  -0.1109 -0.0238 930  TYR B CA  
2267 C C   . TYR B 20  ? 0.4030 0.3203 0.4396 0.0861  -0.0969 -0.0223 930  TYR B C   
2268 O O   . TYR B 20  ? 0.4742 0.3812 0.4964 0.0881  -0.0920 -0.0225 930  TYR B O   
2269 C CB  . TYR B 20  ? 0.4425 0.3514 0.4464 0.0776  -0.1209 -0.0376 930  TYR B CB  
2270 C CG  . TYR B 20  ? 0.4270 0.3280 0.3978 0.0803  -0.1314 -0.0439 930  TYR B CG  
2271 C CD1 . TYR B 20  ? 0.4530 0.3720 0.4210 0.0756  -0.1439 -0.0434 930  TYR B CD1 
2272 C CD2 . TYR B 20  ? 0.4777 0.3557 0.4202 0.0873  -0.1277 -0.0505 930  TYR B CD2 
2273 C CE1 . TYR B 20  ? 0.4262 0.3401 0.3600 0.0740  -0.1535 -0.0516 930  TYR B CE1 
2274 C CE2 . TYR B 20  ? 0.4869 0.3549 0.3960 0.0885  -0.1351 -0.0606 930  TYR B CE2 
2275 C CZ  . TYR B 20  ? 0.4869 0.3729 0.3899 0.0800  -0.1484 -0.0622 930  TYR B CZ  
2276 O OH  . TYR B 20  ? 0.5190 0.3977 0.3850 0.0771  -0.1559 -0.0744 930  TYR B OH  
2277 N N   . GLU B 21  ? 0.3874 0.3133 0.4531 0.0804  -0.0897 -0.0213 931  GLU B N   
2278 C CA  . GLU B 21  ? 0.3735 0.2967 0.4510 0.0730  -0.0761 -0.0221 931  GLU B CA  
2279 C C   . GLU B 21  ? 0.3842 0.3067 0.4718 0.0815  -0.0652 -0.0110 931  GLU B C   
2280 O O   . GLU B 21  ? 0.3521 0.2779 0.4415 0.0940  -0.0683 -0.0007 931  GLU B O   
2281 C CB  . GLU B 21  ? 0.3489 0.2799 0.4483 0.0578  -0.0724 -0.0323 931  GLU B CB  
2282 C CG  . GLU B 21  ? 0.3580 0.2922 0.4503 0.0472  -0.0845 -0.0404 931  GLU B CG  
2283 C CD  . GLU B 21  ? 0.3969 0.3215 0.4704 0.0402  -0.0868 -0.0413 931  GLU B CD  
2284 O OE1 . GLU B 21  ? 0.3732 0.2939 0.4400 0.0444  -0.0792 -0.0352 931  GLU B OE1 
2285 O OE2 . GLU B 21  ? 0.3981 0.3204 0.4656 0.0303  -0.0961 -0.0459 931  GLU B OE2 
2286 N N   . ASN B 22  ? 0.3642 0.2840 0.4571 0.0727  -0.0532 -0.0113 932  ASN B N   
2287 C CA  . ASN B 22  ? 0.3820 0.2975 0.4844 0.0766  -0.0422 -0.0010 932  ASN B CA  
2288 C C   . ASN B 22  ? 0.3679 0.2784 0.4990 0.0785  -0.0352 -0.0017 932  ASN B C   
2289 O O   . ASN B 22  ? 0.4010 0.3047 0.5421 0.0876  -0.0296 0.0112  932  ASN B O   
2290 C CB  . ASN B 22  ? 0.3744 0.2908 0.4752 0.0620  -0.0314 -0.0023 932  ASN B CB  
2291 C CG  . ASN B 22  ? 0.3574 0.2815 0.4353 0.0659  -0.0353 0.0052  932  ASN B CG  
2292 O OD1 . ASN B 22  ? 0.3280 0.2607 0.4016 0.0545  -0.0340 0.0023  932  ASN B OD1 
2293 N ND2 . ASN B 22  ? 0.3579 0.2823 0.4215 0.0829  -0.0398 0.0160  932  ASN B ND2 
2294 N N   . VAL B 23  ? 0.4188 0.3330 0.5654 0.0706  -0.0341 -0.0152 933  VAL B N   
2295 C CA  . VAL B 23  ? 0.3496 0.2604 0.5274 0.0751  -0.0249 -0.0172 933  VAL B CA  
2296 C C   . VAL B 23  ? 0.3176 0.2455 0.5042 0.0797  -0.0360 -0.0204 933  VAL B C   
2297 O O   . VAL B 23  ? 0.4027 0.3404 0.5719 0.0716  -0.0477 -0.0271 933  VAL B O   
2298 C CB  . VAL B 23  ? 0.3601 0.2619 0.5522 0.0582  -0.0069 -0.0336 933  VAL B CB  
2299 C CG1 . VAL B 23  ? 0.4099 0.2989 0.5909 0.0489  0.0022  -0.0299 933  VAL B CG1 
2300 C CG2 . VAL B 23  ? 0.3560 0.2733 0.5410 0.0406  -0.0101 -0.0500 933  VAL B CG2 
2301 N N   . PRO B 24  ? 0.3749 0.3078 0.5897 0.0924  -0.0329 -0.0138 934  PRO B N   
2302 C CA  . PRO B 24  ? 0.3271 0.2839 0.5533 0.0948  -0.0434 -0.0154 934  PRO B CA  
2303 C C   . PRO B 24  ? 0.3129 0.2777 0.5508 0.0794  -0.0355 -0.0354 934  PRO B C   
2304 O O   . PRO B 24  ? 0.3352 0.2879 0.5848 0.0719  -0.0175 -0.0476 934  PRO B O   
2305 C CB  . PRO B 24  ? 0.3066 0.2703 0.5649 0.1151  -0.0398 0.0019  934  PRO B CB  
2306 C CG  . PRO B 24  ? 0.3868 0.3233 0.6516 0.1174  -0.0204 0.0050  934  PRO B CG  
2307 C CD  . PRO B 24  ? 0.3178 0.2365 0.5562 0.1064  -0.0208 -0.0003 934  PRO B CD  
2308 N N   . ILE B 25  ? 0.2862 0.2723 0.5180 0.0719  -0.0494 -0.0394 935  ILE B N   
2309 C CA  . ILE B 25  ? 0.3165 0.3185 0.5604 0.0567  -0.0438 -0.0555 935  ILE B CA  
2310 C C   . ILE B 25  ? 0.2816 0.3134 0.5547 0.0654  -0.0473 -0.0508 935  ILE B C   
2311 O O   . ILE B 25  ? 0.2877 0.3402 0.5522 0.0605  -0.0655 -0.0459 935  ILE B O   
2312 C CB  . ILE B 25  ? 0.2901 0.2938 0.5047 0.0368  -0.0557 -0.0626 935  ILE B CB  
2313 C CG1 . ILE B 25  ? 0.3441 0.3254 0.5370 0.0305  -0.0498 -0.0643 935  ILE B CG1 
2314 C CG2 . ILE B 25  ? 0.2697 0.2954 0.4957 0.0189  -0.0518 -0.0759 935  ILE B CG2 
2315 C CD1 . ILE B 25  ? 0.3106 0.2915 0.4778 0.0151  -0.0605 -0.0664 935  ILE B CD1 
2316 N N   . PRO B 26  ? 0.1942 0.3267 0.7232 0.0354  -0.0345 -0.0222 936  PRO B N   
2317 C CA  . PRO B 26  ? 0.1974 0.3382 0.7411 0.0365  -0.0358 -0.0211 936  PRO B CA  
2318 C C   . PRO B 26  ? 0.1944 0.3398 0.7361 0.0340  -0.0295 -0.0369 936  PRO B C   
2319 O O   . PRO B 26  ? 0.2587 0.4003 0.7906 0.0320  -0.0230 -0.0491 936  PRO B O   
2320 C CB  . PRO B 26  ? 0.2080 0.3398 0.7755 0.0399  -0.0351 -0.0176 936  PRO B CB  
2321 C CG  . PRO B 26  ? 0.2672 0.3867 0.8351 0.0395  -0.0307 -0.0258 936  PRO B CG  
2322 C CD  . PRO B 26  ? 0.1997 0.3211 0.7445 0.0379  -0.0330 -0.0218 936  PRO B CD  
2323 N N   . CYS B 27  ? 0.1960 0.3508 0.7438 0.0336  -0.0314 -0.0352 937  CYS B N   
2324 C CA  . CYS B 27  ? 0.2815 0.4424 0.8305 0.0312  -0.0254 -0.0480 937  CYS B CA  
2325 C C   . CYS B 27  ? 0.2817 0.4436 0.8518 0.0338  -0.0242 -0.0509 937  CYS B C   
2326 O O   . CYS B 27  ? 0.2747 0.4392 0.8568 0.0367  -0.0303 -0.0388 937  CYS B O   
2327 C CB  . CYS B 27  ? 0.2849 0.4549 0.8197 0.0267  -0.0273 -0.0460 937  CYS B CB  
2328 S SG  . CYS B 27  ? 0.1980 0.3750 0.7338 0.0226  -0.0188 -0.0591 937  CYS B SG  
2329 N N   . VAL B 28  ? 0.2539 0.4168 0.8293 0.0327  -0.0160 -0.0665 938  VAL B N   
2330 C CA  . VAL B 28  ? 0.3036 0.4678 0.9003 0.0346  -0.0133 -0.0732 938  VAL B CA  
2331 C C   . VAL B 28  ? 0.2588 0.4345 0.8522 0.0312  -0.0061 -0.0861 938  VAL B C   
2332 O O   . VAL B 28  ? 0.2511 0.4326 0.8282 0.0275  -0.0013 -0.0916 938  VAL B O   
2333 C CB  . VAL B 28  ? 0.3190 0.4735 0.9327 0.0366  -0.0093 -0.0825 938  VAL B CB  
2334 C CG1 . VAL B 28  ? 0.3300 0.4725 0.9481 0.0391  -0.0151 -0.0687 938  VAL B CG1 
2335 C CG2 . VAL B 28  ? 0.2860 0.4455 0.8898 0.0336  -0.0008 -0.1012 938  VAL B CG2 
2336 N N   . ASN B 29  ? 0.2988 0.4789 0.9095 0.0324  -0.0051 -0.0896 939  ASN B N   
2337 C CA  . ASN B 29  ? 0.2585 0.4505 0.8694 0.0293  0.0027  -0.1026 939  ASN B CA  
2338 C C   . ASN B 29  ? 0.3233 0.5153 0.9591 0.0319  0.0053  -0.1112 939  ASN B C   
2339 O O   . ASN B 29  ? 0.3659 0.5573 1.0169 0.0347  -0.0001 -0.1024 939  ASN B O   
2340 C CB  . ASN B 29  ? 0.2556 0.4566 0.8579 0.0261  0.0007  -0.0961 939  ASN B CB  
2341 C CG  . ASN B 29  ? 0.2148 0.4285 0.8165 0.0220  0.0100  -0.1075 939  ASN B CG  
2342 O OD1 . ASN B 29  ? 0.2208 0.4394 0.8312 0.0224  0.0169  -0.1202 939  ASN B OD1 
2343 N ND2 . ASN B 29  ? 0.2101 0.4304 0.8028 0.0174  0.0107  -0.1035 939  ASN B ND2 
2344 N N   . GLY B 30  ? 0.3310 0.5261 0.9722 0.0309  0.0135  -0.1289 940  GLY B N   
2345 C CA  . GLY B 30  ? 0.3426 0.5392 1.0091 0.0323  0.0173  -0.1409 940  GLY B CA  
2346 C C   . GLY B 30  ? 0.3232 0.5381 0.9848 0.0286  0.0266  -0.1565 940  GLY B C   
2347 O O   . GLY B 30  ? 0.3682 0.5889 1.0466 0.0283  0.0327  -0.1731 940  GLY B O   
2348 N N   . VAL B 31  ? 0.2666 0.4919 0.9067 0.0250  0.0284  -0.1511 941  VAL B N   
2349 C CA  . VAL B 31  ? 0.2406 0.4862 0.8732 0.0206  0.0383  -0.1621 941  VAL B CA  
2350 C C   . VAL B 31  ? 0.2399 0.4911 0.8772 0.0191  0.0377  -0.1558 941  VAL B C   
2351 O O   . VAL B 31  ? 0.2475 0.5085 0.8978 0.0187  0.0429  -0.1660 941  VAL B O   
2352 C CB  . VAL B 31  ? 0.2480 0.5040 0.8559 0.0166  0.0429  -0.1603 941  VAL B CB  
2353 C CG1 . VAL B 31  ? 0.2361 0.5165 0.8372 0.0116  0.0535  -0.1669 941  VAL B CG1 
2354 C CG2 . VAL B 31  ? 0.2354 0.4899 0.8393 0.0177  0.0439  -0.1693 941  VAL B CG2 
2355 N N   . ASP B 32  ? 0.2318 0.4781 0.8593 0.0179  0.0318  -0.1406 942  ASP B N   
2356 C CA  . ASP B 32  ? 0.2312 0.4844 0.8624 0.0154  0.0315  -0.1358 942  ASP B CA  
2357 C C   . ASP B 32  ? 0.2275 0.4712 0.8614 0.0177  0.0197  -0.1217 942  ASP B C   
2358 O O   . ASP B 32  ? 0.2437 0.4764 0.8806 0.0221  0.0123  -0.1151 942  ASP B O   
2359 C CB  . ASP B 32  ? 0.2271 0.4921 0.8433 0.0087  0.0394  -0.1345 942  ASP B CB  
2360 C CG  . ASP B 32  ? 0.2188 0.4762 0.8178 0.0068  0.0367  -0.1243 942  ASP B CG  
2361 O OD1 . ASP B 32  ? 0.2398 0.4839 0.8362 0.0106  0.0283  -0.1190 942  ASP B OD1 
2362 O OD2 . ASP B 32  ? 0.2165 0.4816 0.8063 0.0014  0.0434  -0.1207 942  ASP B OD2 
2363 N N   . GLY B 33  ? 0.2256 0.4760 0.8589 0.0142  0.0181  -0.1170 943  GLY B N   
2364 C CA  . GLY B 33  ? 0.2232 0.4723 0.8579 0.0153  0.0072  -0.1058 943  GLY B CA  
2365 C C   . GLY B 33  ? 0.2159 0.4628 0.8336 0.0109  0.0042  -0.0993 943  GLY B C   
2366 O O   . GLY B 33  ? 0.2150 0.4670 0.8333 0.0100  -0.0037 -0.0931 943  GLY B O   
2367 N N   . GLU B 34  ? 0.2118 0.4536 0.8155 0.0081  0.0104  -0.1009 944  GLU B N   
2368 C CA  . GLU B 34  ? 0.2061 0.4440 0.7964 0.0040  0.0082  -0.0951 944  GLU B CA  
2369 C C   . GLU B 34  ? 0.2036 0.4366 0.7905 0.0079  -0.0033 -0.0868 944  GLU B C   
2370 O O   . GLU B 34  ? 0.2824 0.5088 0.8714 0.0135  -0.0061 -0.0842 944  GLU B O   
2371 C CB  . GLU B 34  ? 0.2192 0.4535 0.7977 0.0016  0.0168  -0.0962 944  GLU B CB  
2372 C CG  . GLU B 34  ? 0.2000 0.4282 0.7659 -0.0035 0.0172  -0.0903 944  GLU B CG  
2373 C CD  . GLU B 34  ? 0.2055 0.4397 0.7793 -0.0103 0.0213  -0.0915 944  GLU B CD  
2374 O OE1 . GLU B 34  ? 0.2061 0.4488 0.7884 -0.0122 0.0289  -0.0952 944  GLU B OE1 
2375 O OE2 . GLU B 34  ? 0.2022 0.4320 0.7721 -0.0139 0.0173  -0.0896 944  GLU B OE2 
2376 N N   . PRO B 35  ? 0.2019 0.4397 0.7849 0.0048  -0.0096 -0.0829 945  PRO B N   
2377 C CA  . PRO B 35  ? 0.2001 0.4386 0.7783 0.0080  -0.0201 -0.0741 945  PRO B CA  
2378 C C   . PRO B 35  ? 0.1948 0.4222 0.7582 0.0069  -0.0188 -0.0720 945  PRO B C   
2379 O O   . PRO B 35  ? 0.1969 0.4155 0.7511 0.0037  -0.0101 -0.0761 945  PRO B O   
2380 C CB  . PRO B 35  ? 0.2016 0.4559 0.7814 0.0036  -0.0261 -0.0746 945  PRO B CB  
2381 C CG  . PRO B 35  ? 0.2014 0.4530 0.7796 -0.0040 -0.0168 -0.0841 945  PRO B CG  
2382 C CD  . PRO B 35  ? 0.2027 0.4475 0.7863 -0.0025 -0.0068 -0.0875 945  PRO B CD  
2383 N N   . CYS B 36  ? 0.1935 0.4223 0.7518 0.0094  -0.0275 -0.0637 946  CYS B N   
2384 C CA  . CYS B 36  ? 0.1929 0.4076 0.7301 0.0090  -0.0270 -0.0603 946  CYS B CA  
2385 C C   . CYS B 36  ? 0.2346 0.4441 0.7560 0.0016  -0.0218 -0.0658 946  CYS B C   
2386 O O   . CYS B 36  ? 0.1958 0.4171 0.7202 -0.0029 -0.0246 -0.0696 946  CYS B O   
2387 C CB  . CYS B 36  ? 0.2409 0.4618 0.7755 0.0123  -0.0373 -0.0495 946  CYS B CB  
2388 S SG  . CYS B 36  ? 0.3222 0.5265 0.8317 0.0123  -0.0372 -0.0444 946  CYS B SG  
2389 N N   . PRO B 37  ? 0.1953 0.3896 0.7031 0.0003  -0.0140 -0.0666 947  PRO B N   
2390 C CA  . PRO B 37  ? 0.2396 0.4281 0.7390 -0.0061 -0.0079 -0.0696 947  PRO B CA  
2391 C C   . PRO B 37  ? 0.2313 0.4220 0.7230 -0.0088 -0.0139 -0.0700 947  PRO B C   
2392 O O   . PRO B 37  ? 0.1976 0.3869 0.6790 -0.0055 -0.0202 -0.0647 947  PRO B O   
2393 C CB  . PRO B 37  ? 0.2487 0.4233 0.7347 -0.0050 -0.0006 -0.0659 947  PRO B CB  
2394 C CG  . PRO B 37  ? 0.2345 0.4068 0.7177 0.0014  -0.0052 -0.0631 947  PRO B CG  
2395 C CD  . PRO B 37  ? 0.2250 0.4093 0.7278 0.0044  -0.0101 -0.0650 947  PRO B CD  
2396 N N   . GLU B 38  ? 0.2015 0.3980 0.7005 -0.0154 -0.0115 -0.0778 948  GLU B N   
2397 C CA  . GLU B 38  ? 0.2180 0.4229 0.7130 -0.0190 -0.0168 -0.0829 948  GLU B CA  
2398 C C   . GLU B 38  ? 0.2533 0.4559 0.7584 -0.0269 -0.0094 -0.0934 948  GLU B C   
2399 O O   . GLU B 38  ? 0.2677 0.4837 0.7767 -0.0315 -0.0130 -0.1036 948  GLU B O   
2400 C CB  . GLU B 38  ? 0.2522 0.4827 0.7539 -0.0180 -0.0276 -0.0842 948  GLU B CB  
2401 C CG  . GLU B 38  ? 0.3395 0.5746 0.8299 -0.0116 -0.0366 -0.0727 948  GLU B CG  
2402 C CD  . GLU B 38  ? 0.4505 0.7141 0.9507 -0.0095 -0.0472 -0.0684 948  GLU B CD  
2403 O OE1 . GLU B 38  ? 0.3297 0.6127 0.8423 -0.0137 -0.0488 -0.0773 948  GLU B OE1 
2404 O OE2 . GLU B 38  ? 0.4861 0.7541 0.9835 -0.0034 -0.0539 -0.0551 948  GLU B OE2 
2405 N N   . ASP B 39  ? 0.2095 0.3981 0.7215 -0.0287 0.0011  -0.0912 949  ASP B N   
2406 C CA  . ASP B 39  ? 0.2147 0.3959 0.7401 -0.0354 0.0099  -0.0971 949  ASP B CA  
2407 C C   . ASP B 39  ? 0.2713 0.4367 0.7856 -0.0346 0.0126  -0.0929 949  ASP B C   
2408 O O   . ASP B 39  ? 0.2807 0.4343 0.8073 -0.0381 0.0220  -0.0915 949  ASP B O   
2409 C CB  . ASP B 39  ? 0.2781 0.4533 0.8177 -0.0372 0.0206  -0.0919 949  ASP B CB  
2410 C CG  . ASP B 39  ? 0.3797 0.5543 0.9466 -0.0455 0.0291  -0.1004 949  ASP B CG  
2411 O OD1 . ASP B 39  ? 0.3215 0.4945 0.8958 -0.0496 0.0292  -0.1099 949  ASP B OD1 
2412 O OD2 . ASP B 39  ? 0.4709 0.6477 1.0547 -0.0483 0.0365  -0.0982 949  ASP B OD2 
2413 N N   . TYR B 40  ? 0.2134 0.3787 0.7076 -0.0301 0.0048  -0.0896 950  TYR B N   
2414 C CA  . TYR B 40  ? 0.2350 0.3859 0.7178 -0.0287 0.0071  -0.0849 950  TYR B CA  
2415 C C   . TYR B 40  ? 0.2128 0.3730 0.6815 -0.0273 -0.0023 -0.0886 950  TYR B C   
2416 O O   . TYR B 40  ? 0.2105 0.3877 0.6754 -0.0258 -0.0109 -0.0898 950  TYR B O   
2417 C CB  . TYR B 40  ? 0.2213 0.3586 0.6907 -0.0230 0.0104  -0.0702 950  TYR B CB  
2418 C CG  . TYR B 40  ? 0.2424 0.3827 0.6945 -0.0166 0.0022  -0.0647 950  TYR B CG  
2419 C CD1 . TYR B 40  ? 0.2279 0.3789 0.6842 -0.0142 -0.0019 -0.0650 950  TYR B CD1 
2420 C CD2 . TYR B 40  ? 0.2203 0.3527 0.6562 -0.0130 -0.0006 -0.0593 950  TYR B CD2 
2421 C CE1 . TYR B 40  ? 0.2538 0.4061 0.7014 -0.0082 -0.0084 -0.0598 950  TYR B CE1 
2422 C CE2 . TYR B 40  ? 0.2060 0.3400 0.6316 -0.0076 -0.0070 -0.0544 950  TYR B CE2 
2423 C CZ  . TYR B 40  ? 0.2000 0.3434 0.6328 -0.0052 -0.0106 -0.0545 950  TYR B CZ  
2424 O OH  . TYR B 40  ? 0.2332 0.3769 0.6620 0.0002  -0.0161 -0.0494 950  TYR B OH  
2425 N N   . LYS B 41  ? 0.2147 0.3654 0.6770 -0.0276 -0.0003 -0.0889 951  LYS B N   
2426 C CA  . LYS B 41  ? 0.2139 0.3733 0.6614 -0.0263 -0.0077 -0.0908 951  LYS B CA  
2427 C C   . LYS B 41  ? 0.2379 0.3827 0.6668 -0.0197 -0.0090 -0.0766 951  LYS B C   
2428 O O   . LYS B 41  ? 0.2269 0.3552 0.6545 -0.0190 -0.0028 -0.0723 951  LYS B O   
2429 C CB  . LYS B 41  ? 0.2191 0.3813 0.6759 -0.0321 -0.0041 -0.1050 951  LYS B CB  
2430 C CG  . LYS B 41  ? 0.2194 0.3941 0.6610 -0.0316 -0.0105 -0.1082 951  LYS B CG  
2431 C CD  . LYS B 41  ? 0.2186 0.4217 0.6531 -0.0315 -0.0206 -0.1096 951  LYS B CD  
2432 C CE  . LYS B 41  ? 0.2513 0.4731 0.6714 -0.0319 -0.0265 -0.1119 951  LYS B CE  
2433 N NZ  . LYS B 41  ? 0.2501 0.4987 0.6606 -0.0291 -0.0374 -0.1025 951  LYS B NZ  
2434 N N   . TYR B 42  ? 0.2068 0.3589 0.6246 -0.0150 -0.0168 -0.0691 952  TYR B N   
2435 C CA  . TYR B 42  ? 0.2669 0.4070 0.6704 -0.0096 -0.0182 -0.0582 952  TYR B CA  
2436 C C   . TYR B 42  ? 0.2058 0.3450 0.5995 -0.0105 -0.0192 -0.0599 952  TYR B C   
2437 O O   . TYR B 42  ? 0.2076 0.3642 0.5990 -0.0128 -0.0243 -0.0650 952  TYR B O   
2438 C CB  . TYR B 42  ? 0.2009 0.3482 0.6021 -0.0045 -0.0254 -0.0500 952  TYR B CB  
2439 C CG  . TYR B 42  ? 0.2394 0.3724 0.6322 0.0006  -0.0245 -0.0415 952  TYR B CG  
2440 C CD1 . TYR B 42  ? 0.2114 0.3396 0.5926 0.0018  -0.0262 -0.0376 952  TYR B CD1 
2441 C CD2 . TYR B 42  ? 0.1968 0.3232 0.5941 0.0035  -0.0212 -0.0394 952  TYR B CD2 
2442 C CE1 . TYR B 42  ? 0.2109 0.3277 0.5863 0.0057  -0.0253 -0.0318 952  TYR B CE1 
2443 C CE2 . TYR B 42  ? 0.2140 0.3311 0.6051 0.0073  -0.0202 -0.0352 952  TYR B CE2 
2444 C CZ  . TYR B 42  ? 0.1953 0.3070 0.5757 0.0083  -0.0224 -0.0313 952  TYR B CZ  
2445 O OH  . TYR B 42  ? 0.2230 0.3269 0.5986 0.0114  -0.0216 -0.0284 952  TYR B OH  
2446 N N   . ILE B 43  ? 0.2059 0.3282 0.5942 -0.0089 -0.0141 -0.0558 953  ILE B N   
2447 C CA  . ILE B 43  ? 0.2071 0.3270 0.5864 -0.0089 -0.0147 -0.0563 953  ILE B CA  
2448 C C   . ILE B 43  ? 0.2044 0.3105 0.5725 -0.0037 -0.0145 -0.0453 953  ILE B C   
2449 O O   . ILE B 43  ? 0.2036 0.3001 0.5729 -0.0016 -0.0104 -0.0401 953  ILE B O   
2450 C CB  . ILE B 43  ? 0.2451 0.3602 0.6357 -0.0136 -0.0077 -0.0662 953  ILE B CB  
2451 C CG1 . ILE B 43  ? 0.2244 0.3273 0.6295 -0.0144 0.0005  -0.0638 953  ILE B CG1 
2452 C CG2 . ILE B 43  ? 0.2154 0.3506 0.6140 -0.0194 -0.0097 -0.0818 953  ILE B CG2 
2453 C CD1 . ILE B 43  ? 0.2178 0.3078 0.6340 -0.0155 0.0084  -0.0636 953  ILE B CD1 
2454 N N   . SER B 44  ? 0.2183 0.3266 0.5760 -0.0021 -0.0185 -0.0423 954  SER B N   
2455 C CA  . SER B 44  ? 0.2299 0.3277 0.5787 0.0024  -0.0190 -0.0335 954  SER B CA  
2456 C C   . SER B 44  ? 0.2080 0.2937 0.5545 0.0027  -0.0134 -0.0327 954  SER B C   
2457 O O   . SER B 44  ? 0.2046 0.2826 0.5464 0.0060  -0.0121 -0.0264 954  SER B O   
2458 C CB  . SER B 44  ? 0.2557 0.3616 0.5976 0.0042  -0.0256 -0.0284 954  SER B CB  
2459 O OG  . SER B 44  ? 0.2350 0.3531 0.5740 0.0007  -0.0268 -0.0339 954  SER B OG  
2460 N N   . GLU B 45  ? 0.2082 0.2940 0.5602 -0.0007 -0.0099 -0.0396 955  GLU B N   
2461 C CA  . GLU B 45  ? 0.2559 0.3305 0.6120 -0.0003 -0.0040 -0.0380 955  GLU B CA  
2462 C C   . GLU B 45  ? 0.2310 0.3019 0.6065 -0.0038 0.0033  -0.0433 955  GLU B C   
2463 O O   . GLU B 45  ? 0.2230 0.3018 0.6083 -0.0078 0.0035  -0.0524 955  GLU B O   
2464 C CB  . GLU B 45  ? 0.2558 0.3326 0.6067 -0.0007 -0.0052 -0.0418 955  GLU B CB  
2465 C CG  . GLU B 45  ? 0.2929 0.3731 0.6282 0.0024  -0.0116 -0.0350 955  GLU B CG  
2466 C CD  . GLU B 45  ? 0.3666 0.4580 0.6969 0.0004  -0.0140 -0.0402 955  GLU B CD  
2467 O OE1 . GLU B 45  ? 0.3673 0.4602 0.7051 -0.0025 -0.0096 -0.0498 955  GLU B OE1 
2468 O OE2 . GLU B 45  ? 0.4354 0.5360 0.7570 0.0015  -0.0197 -0.0347 955  GLU B OE2 
2469 N N   . ASN B 46  ? 0.2290 0.2893 0.6131 -0.0023 0.0095  -0.0367 956  ASN B N   
2470 C CA  . ASN B 46  ? 0.2555 0.3103 0.6640 -0.0049 0.0178  -0.0375 956  ASN B CA  
2471 C C   . ASN B 46  ? 0.2477 0.3064 0.6743 -0.0105 0.0204  -0.0553 956  ASN B C   
2472 O O   . ASN B 46  ? 0.2257 0.2901 0.6468 -0.0115 0.0178  -0.0648 956  ASN B O   
2473 C CB  . ASN B 46  ? 0.2255 0.2705 0.6418 -0.0014 0.0234  -0.0234 956  ASN B CB  
2474 C CG  . ASN B 46  ? 0.2635 0.3110 0.6651 0.0030  0.0221  -0.0077 956  ASN B CG  
2475 O OD1 . ASN B 46  ? 0.2213 0.2750 0.6163 0.0024  0.0202  -0.0077 956  ASN B OD1 
2476 N ND2 . ASN B 46  ? 0.2248 0.2706 0.6221 0.0071  0.0229  0.0044  956  ASN B ND2 
2477 N N   . CYS B 47  ? 0.2301 0.2887 0.6798 -0.0147 0.0260  -0.0613 957  CYS B N   
2478 C CA  . CYS B 47  ? 0.2349 0.3000 0.7067 -0.0209 0.0295  -0.0819 957  CYS B CA  
2479 C C   . CYS B 47  ? 0.2425 0.2944 0.7510 -0.0225 0.0407  -0.0807 957  CYS B C   
2480 O O   . CYS B 47  ? 0.2442 0.2855 0.7600 -0.0194 0.0452  -0.0618 957  CYS B O   
2481 C CB  . CYS B 47  ? 0.2340 0.3143 0.7068 -0.0257 0.0260  -0.0940 957  CYS B CB  
2482 S SG  . CYS B 47  ? 0.2829 0.3554 0.7770 -0.0271 0.0328  -0.0855 957  CYS B SG  
2483 N N   . GLU B 48  ? 0.2482 0.3033 0.7825 -0.0276 0.0457  -0.1009 958  GLU B N   
2484 C CA  . GLU B 48  ? 0.2567 0.2997 0.8356 -0.0301 0.0574  -0.1024 958  GLU B CA  
2485 C C   . GLU B 48  ? 0.2791 0.3333 0.8856 -0.0387 0.0610  -0.1284 958  GLU B C   
2486 O O   . GLU B 48  ? 0.2598 0.3342 0.8532 -0.0431 0.0551  -0.1498 958  GLU B O   
2487 C CB  . GLU B 48  ? 0.3118 0.3447 0.9108 -0.0280 0.0633  -0.1030 958  GLU B CB  
2488 C CG  . GLU B 48  ? 0.2827 0.3265 0.8611 -0.0280 0.0577  -0.1178 958  GLU B CG  
2489 C CD  . GLU B 48  ? 0.3350 0.3672 0.9332 -0.0247 0.0638  -0.1146 958  GLU B CD  
2490 O OE1 . GLU B 48  ? 0.4268 0.4543 1.0692 -0.0283 0.0736  -0.1289 958  GLU B OE1 
2491 O OE2 . GLU B 48  ? 0.3374 0.3654 0.9105 -0.0185 0.0592  -0.0984 958  GLU B OE2 
2492 N N   . THR B 49  ? 0.2685 0.3115 0.9155 -0.0413 0.0713  -0.1254 959  THR B N   
2493 C CA  . THR B 49  ? 0.2782 0.3269 0.9510 -0.0471 0.0763  -0.1474 959  THR B CA  
2494 C C   . THR B 49  ? 0.2956 0.3283 1.0100 -0.0443 0.0891  -0.1519 959  THR B C   
2495 O O   . THR B 49  ? 0.3076 0.3424 1.0455 -0.0462 0.0951  -0.1677 959  THR B O   
2496 C CB  . THR B 49  ? 0.2984 0.3483 0.9671 -0.0481 0.0753  -0.1357 959  THR B CB  
2497 O OG1 . THR B 49  ? 0.3006 0.3348 0.9754 -0.0434 0.0800  -0.1040 959  THR B OG1 
2498 C CG2 . THR B 49  ? 0.2623 0.3323 0.8915 -0.0492 0.0624  -0.1378 959  THR B CG2 
2499 N N   . SER B 50  ? 0.3630 0.3823 1.0900 -0.0389 0.0936  -0.1378 960  SER B N   
2500 C CA  . SER B 50  ? 0.3122 0.3216 1.0833 -0.0345 0.1056  -0.1417 960  SER B CA  
2501 C C   . SER B 50  ? 0.3091 0.3162 1.0791 -0.0313 0.1052  -0.1408 960  SER B C   
2502 O O   . SER B 50  ? 0.3137 0.3244 1.0488 -0.0326 0.0960  -0.1358 960  SER B O   
2503 C CB  . SER B 50  ? 0.3197 0.3149 1.1183 -0.0290 0.1138  -0.1118 960  SER B CB  
2504 O OG  . SER B 50  ? 0.3110 0.2988 1.0902 -0.0250 0.1101  -0.0786 960  SER B OG  
2505 N N   . THR B 51  ? 0.3201 0.3243 1.1320 -0.0270 0.1157  -0.1454 961  THR B N   
2506 C CA  . THR B 51  ? 0.3173 0.3217 1.1326 -0.0242 0.1161  -0.1448 961  THR B CA  
2507 C C   . THR B 51  ? 0.3105 0.3021 1.1148 -0.0185 0.1135  -0.1056 961  THR B C   
2508 O O   . THR B 51  ? 0.3165 0.3016 1.1452 -0.0139 0.1195  -0.0793 961  THR B O   
2509 C CB  . THR B 51  ? 0.3307 0.3414 1.1982 -0.0231 0.1282  -0.1603 961  THR B CB  
2510 O OG1 . THR B 51  ? 0.3375 0.3643 1.2071 -0.0290 0.1294  -0.2007 961  THR B OG1 
2511 C CG2 . THR B 51  ? 0.3309 0.3391 1.2021 -0.0215 0.1284  -0.1513 961  THR B CG2 
2512 N N   . MET B 52  ? 0.3039 0.2942 1.0707 -0.0189 0.1042  -0.1012 962  MET B N   
2513 C CA  . MET B 52  ? 0.2933 0.2734 1.0421 -0.0135 0.1003  -0.0667 962  MET B CA  
2514 C C   . MET B 52  ? 0.3150 0.2930 1.0645 -0.0092 0.1000  -0.0626 962  MET B C   
2515 O O   . MET B 52  ? 0.2957 0.2687 1.0512 -0.0032 0.1016  -0.0331 962  MET B O   
2516 C CB  . MET B 52  ? 0.3105 0.2972 1.0029 -0.0138 0.0880  -0.0597 962  MET B CB  
2517 C CG  . MET B 52  ? 0.4147 0.4023 1.0994 -0.0143 0.0875  -0.0429 962  MET B CG  
2518 S SD  . MET B 52  ? 0.6272 0.6021 1.3581 -0.0102 0.0992  -0.0089 962  MET B SD  
2519 C CE  . MET B 52  ? 0.2900 0.2718 1.0083 -0.0132 0.0984  0.0015  962  MET B CE  
2520 N N   . ASN B 53  ? 0.3107 0.2956 1.0519 -0.0127 0.0976  -0.0911 963  ASN B N   
2521 C CA  . ASN B 53  ? 0.2896 0.2742 1.0252 -0.0091 0.0962  -0.0914 963  ASN B CA  
2522 C C   . ASN B 53  ? 0.3261 0.3046 1.0270 -0.0001 0.0887  -0.0599 963  ASN B C   
2523 O O   . ASN B 53  ? 0.2879 0.2608 1.0042 0.0048  0.0918  -0.0362 963  ASN B O   
2524 C CB  . ASN B 53  ? 0.3009 0.2885 1.0842 -0.0105 0.1065  -0.0913 963  ASN B CB  
2525 C CG  . ASN B 53  ? 0.3082 0.3099 1.1288 -0.0170 0.1148  -0.1243 963  ASN B CG  
2526 O OD1 . ASN B 53  ? 0.3190 0.3190 1.1710 -0.0168 0.1221  -0.1194 963  ASN B OD1 
2527 N ND2 . ASN B 53  ? 0.3073 0.3219 1.1188 -0.0216 0.1133  -0.1576 963  ASN B ND2 
2528 N N   . ILE B 54  ? 0.2733 0.2622 0.9210 -0.0002 0.0777  -0.0578 964  ILE B N   
2529 C CA  . ILE B 54  ? 0.2668 0.2575 0.8773 0.0066  0.0696  -0.0355 964  ILE B CA  
2530 C C   . ILE B 54  ? 0.2949 0.2863 0.9067 0.0091  0.0695  -0.0429 964  ILE B C   
2531 O O   . ILE B 54  ? 0.2656 0.2653 0.8729 0.0044  0.0689  -0.0688 964  ILE B O   
2532 C CB  . ILE B 54  ? 0.3058 0.3073 0.8662 0.0051  0.0588  -0.0372 964  ILE B CB  
2533 C CG1 . ILE B 54  ? 0.2695 0.2714 0.8312 0.0022  0.0595  -0.0328 964  ILE B CG1 
2534 C CG2 . ILE B 54  ? 0.2512 0.2555 0.7776 0.0114  0.0512  -0.0178 964  ILE B CG2 
2535 C CD1 . ILE B 54  ? 0.2494 0.2618 0.7707 0.0003  0.0501  -0.0380 964  ILE B CD1 
2536 N N   . ASP B 55  ? 0.2682 0.2545 0.8865 0.0163  0.0701  -0.0197 965  ASP B N   
2537 C CA  . ASP B 55  ? 0.2680 0.2551 0.8888 0.0196  0.0700  -0.0234 965  ASP B CA  
2538 C C   . ASP B 55  ? 0.2586 0.2569 0.8303 0.0183  0.0599  -0.0328 965  ASP B C   
2539 O O   . ASP B 55  ? 0.2527 0.2548 0.7920 0.0222  0.0523  -0.0154 965  ASP B O   
2540 C CB  . ASP B 55  ? 0.2715 0.2543 0.9064 0.0280  0.0712  0.0076  965  ASP B CB  
2541 C CG  . ASP B 55  ? 0.3048 0.2888 0.9423 0.0310  0.0709  0.0061  965  ASP B CG  
2542 O OD1 . ASP B 55  ? 0.2728 0.2585 0.9150 0.0270  0.0729  -0.0202 965  ASP B OD1 
2543 O OD2 . ASP B 55  ? 0.3201 0.3065 0.9535 0.0366  0.0684  0.0316  965  ASP B OD2 
2544 N N   . ARG B 56  ? 0.2579 0.2645 0.8256 0.0126  0.0602  -0.0603 966  ARG B N   
2545 C CA  . ARG B 56  ? 0.2645 0.2837 0.7904 0.0112  0.0516  -0.0674 966  ARG B CA  
2546 C C   . ARG B 56  ? 0.2514 0.2749 0.7816 0.0127  0.0533  -0.0755 966  ARG B C   
2547 O O   . ARG B 56  ? 0.2709 0.3077 0.7745 0.0099  0.0486  -0.0863 966  ARG B O   
2548 C CB  . ARG B 56  ? 0.2679 0.3009 0.7795 0.0037  0.0493  -0.0889 966  ARG B CB  
2549 C CG  . ARG B 56  ? 0.3859 0.4174 0.8864 0.0021  0.0459  -0.0816 966  ARG B CG  
2550 C CD  . ARG B 56  ? 0.3891 0.4378 0.8784 -0.0052 0.0433  -0.1031 966  ARG B CD  
2551 N NE  . ARG B 56  ? 0.4942 0.5418 0.9804 -0.0071 0.0414  -0.0990 966  ARG B NE  
2552 C CZ  . ARG B 56  ? 0.4707 0.5188 0.9272 -0.0048 0.0336  -0.0840 966  ARG B CZ  
2553 N NH1 . ARG B 56  ? 0.5053 0.5539 0.9347 -0.0007 0.0272  -0.0715 966  ARG B NH1 
2554 N NH2 . ARG B 56  ? 0.4915 0.5400 0.9489 -0.0070 0.0328  -0.0829 966  ARG B NH2 
2555 N N   . ASN B 57  ? 0.2570 0.2710 0.8223 0.0169  0.0602  -0.0699 967  ASN B N   
2556 C CA  . ASN B 57  ? 0.2577 0.2761 0.8287 0.0188  0.0619  -0.0770 967  ASN B CA  
2557 C C   . ASN B 57  ? 0.2550 0.2777 0.7860 0.0228  0.0524  -0.0604 967  ASN B C   
2558 O O   . ASN B 57  ? 0.2756 0.2925 0.7992 0.0283  0.0485  -0.0362 967  ASN B O   
2559 C CB  . ASN B 57  ? 0.2894 0.2958 0.9104 0.0237  0.0711  -0.0703 967  ASN B CB  
2560 C CG  . ASN B 57  ? 0.2727 0.2841 0.9072 0.0241  0.0750  -0.0840 967  ASN B CG  
2561 O OD1 . ASN B 57  ? 0.2780 0.2981 0.8832 0.0260  0.0691  -0.0818 967  ASN B OD1 
2562 N ND2 . ASN B 57  ? 0.2830 0.2892 0.9537 0.0184  0.0835  -0.0963 967  ASN B ND2 
2563 N N   . ILE B 58  ? 0.2461 0.2820 0.7520 0.0194  0.0487  -0.0736 968  ILE B N   
2564 C CA  . ILE B 58  ? 0.2575 0.2974 0.7299 0.0224  0.0404  -0.0597 968  ILE B CA  
2565 C C   . ILE B 58  ? 0.2770 0.3117 0.7640 0.0291  0.0417  -0.0464 968  ILE B C   
2566 O O   . ILE B 58  ? 0.2638 0.2994 0.7304 0.0329  0.0351  -0.0299 968  ILE B O   
2567 C CB  . ILE B 58  ? 0.2848 0.3415 0.7320 0.0172  0.0373  -0.0744 968  ILE B CB  
2568 C CG1 . ILE B 58  ? 0.2413 0.3007 0.6563 0.0194  0.0287  -0.0594 968  ILE B CG1 
2569 C CG2 . ILE B 58  ? 0.2416 0.3073 0.7080 0.0155  0.0441  -0.0924 968  ILE B CG2 
2570 C CD1 . ILE B 58  ? 0.2279 0.3043 0.6191 0.0143  0.0254  -0.0681 968  ILE B CD1 
2571 N N   . THR B 59  ? 0.2466 0.2774 0.7717 0.0306  0.0502  -0.0539 969  THR B N   
2572 C CA  . THR B 59  ? 0.2662 0.2935 0.8081 0.0376  0.0511  -0.0391 969  THR B CA  
2573 C C   . THR B 59  ? 0.2849 0.3044 0.8372 0.0439  0.0496  -0.0118 969  THR B C   
2574 O O   . THR B 59  ? 0.3340 0.3558 0.8903 0.0502  0.0473  0.0060  969  THR B O   
2575 C CB  . THR B 59  ? 0.2941 0.3203 0.8786 0.0380  0.0613  -0.0551 969  THR B CB  
2576 O OG1 . THR B 59  ? 0.2663 0.2807 0.8858 0.0358  0.0687  -0.0561 969  THR B OG1 
2577 C CG2 . THR B 59  ? 0.2663 0.3064 0.8401 0.0308  0.0636  -0.0841 969  THR B CG2 
2578 N N   . HIS B 60  ? 0.3055 0.3194 0.8617 0.0423  0.0508  -0.0073 970  HIS B N   
2579 C CA  . HIS B 60  ? 0.2761 0.2870 0.8424 0.0477  0.0501  0.0199  970  HIS B CA  
2580 C C   . HIS B 60  ? 0.2772 0.2974 0.8018 0.0491  0.0400  0.0348  970  HIS B C   
2581 O O   . HIS B 60  ? 0.2755 0.2994 0.8024 0.0530  0.0387  0.0570  970  HIS B O   
2582 C CB  . HIS B 60  ? 0.2999 0.3020 0.8907 0.0449  0.0565  0.0188  970  HIS B CB  
2583 C CG  . HIS B 60  ? 0.3161 0.3089 0.9461 0.0399  0.0664  0.0103  970  HIS B CG  
2584 N ND1 . HIS B 60  ? 0.2839 0.2693 0.9419 0.0355  0.0733  0.0127  970  HIS B ND1 
2585 C CD2 . HIS B 60  ? 0.2813 0.2729 0.9308 0.0380  0.0710  -0.0013 970  HIS B CD2 
2586 C CE1 . HIS B 60  ? 0.2959 0.2766 0.9909 0.0309  0.0816  0.0028  970  HIS B CE1 
2587 N NE2 . HIS B 60  ? 0.2948 0.2788 0.9847 0.0323  0.0804  -0.0065 970  HIS B NE2 
2588 N N   . LEU B 61  ? 0.2809 0.3070 0.7706 0.0458  0.0336  0.0231  971  LEU B N   
2589 C CA  . LEU B 61  ? 0.2594 0.2936 0.7133 0.0456  0.0249  0.0313  971  LEU B CA  
2590 C C   . LEU B 61  ? 0.2708 0.3153 0.7156 0.0505  0.0198  0.0438  971  LEU B C   
2591 O O   . LEU B 61  ? 0.2737 0.3204 0.7152 0.0503  0.0188  0.0356  971  LEU B O   
2592 C CB  . LEU B 61  ? 0.2289 0.2643 0.6554 0.0395  0.0211  0.0137  971  LEU B CB  
2593 C CG  . LEU B 61  ? 0.2320 0.2632 0.6574 0.0343  0.0230  0.0031  971  LEU B CG  
2594 C CD1 . LEU B 61  ? 0.2233 0.2602 0.6242 0.0292  0.0188  -0.0109 971  LEU B CD1 
2595 C CD2 . LEU B 61  ? 0.2283 0.2594 0.6482 0.0357  0.0211  0.0172  971  LEU B CD2 
2596 N N   . GLN B 62  ? 0.2335 0.2877 0.6745 0.0544  0.0167  0.0631  972  GLN B N   
2597 C CA  . GLN B 62  ? 0.2307 0.3007 0.6551 0.0574  0.0099  0.0714  972  GLN B CA  
2598 C C   . GLN B 62  ? 0.2390 0.3110 0.6323 0.0526  0.0039  0.0569  972  GLN B C   
2599 O O   . GLN B 62  ? 0.2382 0.3058 0.6183 0.0486  0.0031  0.0499  972  GLN B O   
2600 C CB  . GLN B 62  ? 0.2353 0.3214 0.6601 0.0616  0.0079  0.0933  972  GLN B CB  
2601 C CG  . GLN B 62  ? 0.2444 0.3280 0.7056 0.0666  0.0147  0.1117  972  GLN B CG  
2602 C CD  . GLN B 62  ? 0.2504 0.3581 0.7140 0.0722  0.0119  0.1384  972  GLN B CD  
2603 O OE1 . GLN B 62  ? 0.3513 0.4773 0.8079 0.0756  0.0066  0.1451  972  GLN B OE1 
2604 N NE2 . GLN B 62  ? 0.2567 0.3679 0.7309 0.0730  0.0155  0.1543  972  GLN B NE2 
2605 N N   . HIS B 63  ? 0.2197 0.2983 0.6052 0.0530  0.0002  0.0528  973  HIS B N   
2606 C CA  . HIS B 63  ? 0.2135 0.2915 0.5780 0.0484  -0.0039 0.0393  973  HIS B CA  
2607 C C   . HIS B 63  ? 0.2485 0.3393 0.6077 0.0499  -0.0086 0.0404  973  HIS B C   
2608 O O   . HIS B 63  ? 0.2140 0.3117 0.5865 0.0543  -0.0080 0.0484  973  HIS B O   
2609 C CB  . HIS B 63  ? 0.2123 0.2787 0.5792 0.0442  0.0000  0.0251  973  HIS B CB  
2610 C CG  . HIS B 63  ? 0.2601 0.3263 0.6417 0.0456  0.0034  0.0215  973  HIS B CG  
2611 N ND1 . HIS B 63  ? 0.3005 0.3610 0.7077 0.0480  0.0100  0.0218  973  HIS B ND1 
2612 C CD2 . HIS B 63  ? 0.2867 0.3581 0.6640 0.0450  0.0018  0.0168  973  HIS B CD2 
2613 C CE1 . HIS B 63  ? 0.2200 0.2828 0.6372 0.0489  0.0123  0.0165  973  HIS B CE1 
2614 N NE2 . HIS B 63  ? 0.3210 0.3908 0.7190 0.0470  0.0073  0.0140  973  HIS B NE2 
2615 N N   . CYS B 64  ? 0.2604 0.3546 0.6033 0.0463  -0.0129 0.0323  974  CYS B N   
2616 C CA  . CYS B 64  ? 0.2286 0.3365 0.5679 0.0468  -0.0175 0.0311  974  CYS B CA  
2617 C C   . CYS B 64  ? 0.2090 0.3111 0.5508 0.0444  -0.0164 0.0228  974  CYS B C   
2618 O O   . CYS B 64  ? 0.2019 0.2923 0.5442 0.0416  -0.0126 0.0171  974  CYS B O   
2619 C CB  . CYS B 64  ? 0.2027 0.3197 0.5293 0.0441  -0.0221 0.0259  974  CYS B CB  
2620 S SG  . CYS B 64  ? 0.1986 0.3013 0.5178 0.0382  -0.0219 0.0141  974  CYS B SG  
2621 N N   . THR B 65  ? 0.2034 0.3174 0.5474 0.0451  -0.0194 0.0221  975  THR B N   
2622 C CA  . THR B 65  ? 0.2297 0.3408 0.5769 0.0425  -0.0182 0.0155  975  THR B CA  
2623 C C   . THR B 65  ? 0.2395 0.3550 0.5817 0.0382  -0.0216 0.0083  975  THR B C   
2624 O O   . THR B 65  ? 0.2928 0.4088 0.6398 0.0360  -0.0208 0.0046  975  THR B O   
2625 C CB  . THR B 65  ? 0.2345 0.3543 0.5948 0.0466  -0.0175 0.0197  975  THR B CB  
2626 O OG1 . THR B 65  ? 0.2316 0.3703 0.5923 0.0493  -0.0230 0.0244  975  THR B OG1 
2627 C CG2 . THR B 65  ? 0.2059 0.3189 0.5795 0.0507  -0.0125 0.0259  975  THR B CG2 
2628 N N   . CYS B 66  ? 0.2650 0.3840 0.6009 0.0369  -0.0248 0.0059  976  CYS B N   
2629 C CA  . CYS B 66  ? 0.2167 0.3412 0.5547 0.0331  -0.0276 -0.0026 976  CYS B CA  
2630 C C   . CYS B 66  ? 0.2301 0.3434 0.5725 0.0288  -0.0252 -0.0053 976  CYS B C   
2631 O O   . CYS B 66  ? 0.2565 0.3584 0.5942 0.0276  -0.0223 -0.0022 976  CYS B O   
2632 C CB  . CYS B 66  ? 0.2266 0.3534 0.5589 0.0322  -0.0296 -0.0059 976  CYS B CB  
2633 S SG  . CYS B 66  ? 0.2550 0.3986 0.5808 0.0371  -0.0314 0.0015  976  CYS B SG  
2634 N N   . VAL B 67  ? 0.2324 0.3516 0.5853 0.0260  -0.0263 -0.0108 977  VAL B N   
2635 C CA  . VAL B 67  ? 0.2370 0.3482 0.5980 0.0217  -0.0239 -0.0105 977  VAL B CA  
2636 C C   . VAL B 67  ? 0.2772 0.3879 0.6500 0.0184  -0.0253 -0.0168 977  VAL B C   
2637 O O   . VAL B 67  ? 0.2765 0.3820 0.6624 0.0148  -0.0232 -0.0147 977  VAL B O   
2638 C CB  . VAL B 67  ? 0.2942 0.4106 0.6646 0.0205  -0.0221 -0.0101 977  VAL B CB  
2639 C CG1 . VAL B 67  ? 0.2642 0.3804 0.6272 0.0237  -0.0196 -0.0053 977  VAL B CG1 
2640 C CG2 . VAL B 67  ? 0.2374 0.3678 0.6199 0.0200  -0.0254 -0.0188 977  VAL B CG2 
2641 N N   . ASP B 68  ? 0.2779 0.3953 0.6489 0.0194  -0.0282 -0.0241 978  ASP B N   
2642 C CA  . ASP B 68  ? 0.2479 0.3658 0.6324 0.0165  -0.0289 -0.0334 978  ASP B CA  
2643 C C   . ASP B 68  ? 0.2882 0.3971 0.6626 0.0177  -0.0286 -0.0296 978  ASP B C   
2644 O O   . ASP B 68  ? 0.2685 0.3681 0.6295 0.0193  -0.0273 -0.0194 978  ASP B O   
2645 C CB  . ASP B 68  ? 0.1936 0.3323 0.5846 0.0161  -0.0320 -0.0478 978  ASP B CB  
2646 C CG  . ASP B 68  ? 0.2443 0.3965 0.6163 0.0200  -0.0346 -0.0467 978  ASP B CG  
2647 O OD1 . ASP B 68  ? 0.1935 0.3370 0.5502 0.0234  -0.0337 -0.0341 978  ASP B OD1 
2648 O OD2 . ASP B 68  ? 0.2563 0.4301 0.6305 0.0195  -0.0372 -0.0582 978  ASP B OD2 
2649 N N   . ASP B 69  ? 0.2129 0.3264 0.5952 0.0166  -0.0296 -0.0397 979  ASP B N   
2650 C CA  . ASP B 69  ? 0.2651 0.3714 0.6396 0.0177  -0.0294 -0.0371 979  ASP B CA  
2651 C C   . ASP B 69  ? 0.2508 0.3677 0.6065 0.0208  -0.0309 -0.0373 979  ASP B C   
2652 O O   . ASP B 69  ? 0.2461 0.3608 0.5966 0.0213  -0.0306 -0.0376 979  ASP B O   
2653 C CB  . ASP B 69  ? 0.2013 0.3065 0.5976 0.0150  -0.0287 -0.0474 979  ASP B CB  
2654 C CG  . ASP B 69  ? 0.1963 0.3206 0.6047 0.0133  -0.0298 -0.0662 979  ASP B CG  
2655 O OD1 . ASP B 69  ? 0.2306 0.3715 0.6275 0.0144  -0.0319 -0.0694 979  ASP B OD1 
2656 O OD2 . ASP B 69  ? 0.2867 0.4119 0.7182 0.0107  -0.0284 -0.0786 979  ASP B OD2 
2657 N N   . CYS B 70  ? 0.2451 0.3741 0.5925 0.0229  -0.0322 -0.0351 980  CYS B N   
2658 C CA  . CYS B 70  ? 0.2614 0.4040 0.5946 0.0263  -0.0334 -0.0311 980  CYS B CA  
2659 C C   . CYS B 70  ? 0.2690 0.4334 0.6039 0.0251  -0.0351 -0.0435 980  CYS B C   
2660 O O   . CYS B 70  ? 0.3026 0.4778 0.6263 0.0271  -0.0352 -0.0394 980  CYS B O   
2661 C CB  . CYS B 70  ? 0.1951 0.3233 0.5169 0.0284  -0.0312 -0.0198 980  CYS B CB  
2662 S SG  . CYS B 70  ? 0.2145 0.3251 0.5346 0.0295  -0.0286 -0.0091 980  CYS B SG  
2663 N N   . SER B 71  ? 0.2027 0.3760 0.5536 0.0216  -0.0358 -0.0593 981  SER B N   
2664 C CA  . SER B 71  ? 0.2374 0.4385 0.5920 0.0198  -0.0372 -0.0756 981  SER B CA  
2665 C C   . SER B 71  ? 0.2662 0.4992 0.6159 0.0207  -0.0407 -0.0784 981  SER B C   
2666 O O   . SER B 71  ? 0.2457 0.5094 0.5990 0.0184  -0.0422 -0.0946 981  SER B O   
2667 C CB  . SER B 71  ? 0.2818 0.4800 0.6624 0.0150  -0.0357 -0.0949 981  SER B CB  
2668 O OG  . SER B 71  ? 0.2301 0.4243 0.6273 0.0128  -0.0358 -0.0987 981  SER B OG  
2669 N N   . SER B 72  ? 0.2062 0.4362 0.5492 0.0239  -0.0419 -0.0642 982  SER B N   
2670 C CA  . SER B 72  ? 0.2832 0.5456 0.6235 0.0253  -0.0457 -0.0648 982  SER B CA  
2671 C C   . SER B 72  ? 0.2953 0.5740 0.6181 0.0304  -0.0468 -0.0470 982  SER B C   
2672 O O   . SER B 72  ? 0.2931 0.5506 0.6082 0.0332  -0.0441 -0.0319 982  SER B O   
2673 C CB  . SER B 72  ? 0.2541 0.5074 0.6021 0.0259  -0.0463 -0.0599 982  SER B CB  
2674 O OG  . SER B 72  ? 0.2564 0.4844 0.5969 0.0298  -0.0440 -0.0407 982  SER B OG  
2675 N N   . SER B 73  ? 0.2422 0.5615 0.5613 0.0314  -0.0507 -0.0482 983  SER B N   
2676 C CA  . SER B 73  ? 0.2661 0.6058 0.5720 0.0366  -0.0517 -0.0274 983  SER B CA  
2677 C C   . SER B 73  ? 0.2766 0.6016 0.5842 0.0423  -0.0515 -0.0045 983  SER B C   
2678 O O   . SER B 73  ? 0.2593 0.5988 0.5623 0.0474  -0.0517 0.0165  983  SER B O   
2679 C CB  . SER B 73  ? 0.2281 0.6229 0.5294 0.0359  -0.0562 -0.0343 983  SER B CB  
2680 O OG  . SER B 73  ? 0.3156 0.7293 0.6248 0.0357  -0.0604 -0.0398 983  SER B OG  
2681 N N   . ASN B 74  ? 0.2976 0.5959 0.6146 0.0416  -0.0504 -0.0079 984  ASN B N   
2682 C CA  . ASN B 74  ? 0.2492 0.5325 0.5713 0.0464  -0.0492 0.0095  984  ASN B CA  
2683 C C   . ASN B 74  ? 0.2494 0.4948 0.5711 0.0476  -0.0436 0.0186  984  ASN B C   
2684 O O   . ASN B 74  ? 0.2219 0.4558 0.5498 0.0519  -0.0413 0.0332  984  ASN B O   
2685 C CB  . ASN B 74  ? 0.2564 0.5355 0.5893 0.0444  -0.0504 -0.0006 984  ASN B CB  
2686 C CG  . ASN B 74  ? 0.2478 0.5208 0.5884 0.0496  -0.0496 0.0149  984  ASN B CG  
2687 O OD1 . ASN B 74  ? 0.2438 0.4892 0.5907 0.0488  -0.0460 0.0138  984  ASN B OD1 
2688 N ND2 . ASN B 74  ? 0.2596 0.5614 0.6016 0.0549  -0.0528 0.0296  984  ASN B ND2 
2689 N N   . CYS B 75  ? 0.2122 0.4400 0.5290 0.0438  -0.0414 0.0093  985  CYS B N   
2690 C CA  . CYS B 75  ? 0.2316 0.4290 0.5471 0.0443  -0.0367 0.0164  985  CYS B CA  
2691 C C   . CYS B 75  ? 0.2145 0.4172 0.5298 0.0493  -0.0348 0.0354  985  CYS B C   
2692 O O   . CYS B 75  ? 0.2209 0.4483 0.5307 0.0506  -0.0365 0.0410  985  CYS B O   
2693 C CB  . CYS B 75  ? 0.2270 0.4133 0.5378 0.0399  -0.0356 0.0049  985  CYS B CB  
2694 S SG  . CYS B 75  ? 0.2030 0.3580 0.5119 0.0399  -0.0307 0.0116  985  CYS B SG  
2695 N N   . LEU B 76  ? 0.2120 0.3945 0.5363 0.0521  -0.0309 0.0452  986  LEU B N   
2696 C CA  . LEU B 76  ? 0.2177 0.4032 0.5498 0.0570  -0.0280 0.0643  986  LEU B CA  
2697 C C   . LEU B 76  ? 0.2190 0.3974 0.5453 0.0554  -0.0253 0.0663  986  LEU B C   
2698 O O   . LEU B 76  ? 0.2249 0.4196 0.5524 0.0582  -0.0246 0.0809  986  LEU B O   
2699 C CB  . LEU B 76  ? 0.2440 0.4089 0.5929 0.0597  -0.0234 0.0701  986  LEU B CB  
2700 C CG  . LEU B 76  ? 0.2617 0.4230 0.6263 0.0642  -0.0186 0.0885  986  LEU B CG  
2701 C CD1 . LEU B 76  ? 0.2357 0.4270 0.6076 0.0700  -0.0213 0.1089  986  LEU B CD1 
2702 C CD2 . LEU B 76  ? 0.2837 0.4206 0.6685 0.0652  -0.0122 0.0873  986  LEU B CD2 
2703 N N   . CYS B 77  ? 0.2288 0.3852 0.5498 0.0509  -0.0236 0.0530  987  CYS B N   
2704 C CA  . CYS B 77  ? 0.2147 0.3648 0.5302 0.0489  -0.0214 0.0524  987  CYS B CA  
2705 C C   . CYS B 77  ? 0.2608 0.4385 0.5665 0.0487  -0.0242 0.0536  987  CYS B C   
2706 O O   . CYS B 77  ? 0.2532 0.4392 0.5590 0.0501  -0.0219 0.0650  987  CYS B O   
2707 C CB  . CYS B 77  ? 0.2090 0.3384 0.5194 0.0442  -0.0210 0.0371  987  CYS B CB  
2708 S SG  . CYS B 77  ? 0.2074 0.3140 0.5280 0.0441  -0.0173 0.0357  987  CYS B SG  
2709 N N   . GLY B 78  ? 0.2500 0.4455 0.5495 0.0468  -0.0288 0.0416  988  GLY B N   
2710 C CA  . GLY B 78  ? 0.2237 0.4511 0.5147 0.0458  -0.0312 0.0380  988  GLY B CA  
2711 C C   . GLY B 78  ? 0.2646 0.5224 0.5558 0.0503  -0.0318 0.0580  988  GLY B C   
2712 O O   . GLY B 78  ? 0.2561 0.5329 0.5418 0.0506  -0.0305 0.0655  988  GLY B O   
2713 N N   . GLN B 79  ? 0.2497 0.5142 0.5486 0.0542  -0.0336 0.0687  989  GLN B N   
2714 C CA  . GLN B 79  ? 0.2794 0.5778 0.5812 0.0592  -0.0349 0.0907  989  GLN B CA  
2715 C C   . GLN B 79  ? 0.2437 0.5336 0.5543 0.0625  -0.0294 0.1135  989  GLN B C   
2716 O O   . GLN B 79  ? 0.2521 0.5740 0.5616 0.0650  -0.0295 0.1317  989  GLN B O   
2717 C CB  . GLN B 79  ? 0.2386 0.5424 0.5514 0.0632  -0.0376 0.0984  989  GLN B CB  
2718 C CG  . GLN B 79  ? 0.2329 0.5400 0.5415 0.0596  -0.0421 0.0758  989  GLN B CG  
2719 C CD  . GLN B 79  ? 0.3059 0.6177 0.6267 0.0637  -0.0444 0.0838  989  GLN B CD  
2720 O OE1 . GLN B 79  ? 0.2874 0.5952 0.6218 0.0695  -0.0421 0.1055  989  GLN B OE1 
2721 N NE2 . GLN B 79  ? 0.2622 0.5827 0.5816 0.0606  -0.0484 0.0660  989  GLN B NE2 
2722 N N   . LEU B 80  ? 0.2399 0.4897 0.5615 0.0623  -0.0244 0.1130  990  LEU B N   
2723 C CA  . LEU B 80  ? 0.2445 0.4821 0.5769 0.0637  -0.0182 0.1287  990  LEU B CA  
2724 C C   . LEU B 80  ? 0.2536 0.5102 0.5718 0.0608  -0.0179 0.1276  990  LEU B C   
2725 O O   . LEU B 80  ? 0.2557 0.5312 0.5794 0.0633  -0.0152 0.1490  990  LEU B O   
2726 C CB  . LEU B 80  ? 0.2895 0.4841 0.6316 0.0614  -0.0135 0.1179  990  LEU B CB  
2727 C CG  . LEU B 80  ? 0.2740 0.4492 0.6368 0.0645  -0.0109 0.1216  990  LEU B CG  
2728 C CD1 . LEU B 80  ? 0.2328 0.3731 0.5997 0.0606  -0.0071 0.1039  990  LEU B CD1 
2729 C CD2 . LEU B 80  ? 0.2480 0.4295 0.6365 0.0703  -0.0063 0.1484  990  LEU B CD2 
2730 N N   . SER B 81  ? 0.2642 0.5185 0.5663 0.0556  -0.0204 0.1035  991  SER B N   
2731 C CA  . SER B 81  ? 0.3013 0.5724 0.5910 0.0522  -0.0198 0.0967  991  SER B CA  
2732 C C   . SER B 81  ? 0.3452 0.6662 0.6237 0.0525  -0.0235 0.0989  991  SER B C   
2733 O O   . SER B 81  ? 0.4211 0.7597 0.6885 0.0486  -0.0237 0.0845  991  SER B O   
2734 C CB  . SER B 81  ? 0.2410 0.4914 0.5235 0.0469  -0.0209 0.0695  991  SER B CB  
2735 O OG  . SER B 81  ? 0.2690 0.4791 0.5596 0.0462  -0.0187 0.0653  991  SER B OG  
2736 N N   . ILE B 82  ? 0.2662 0.6121 0.5489 0.0568  -0.0264 0.1150  992  ILE B N   
2737 C CA  . ILE B 82  ? 0.3647 0.7622 0.6368 0.0568  -0.0317 0.1131  992  ILE B CA  
2738 C C   . ILE B 82  ? 0.3575 0.7525 0.6245 0.0527  -0.0365 0.0826  992  ILE B C   
2739 O O   . ILE B 82  ? 0.2827 0.6984 0.5509 0.0541  -0.0412 0.0816  992  ILE B O   
2740 C CB  . ILE B 82  ? 0.3916 0.8301 0.6512 0.0545  -0.0305 0.1150  992  ILE B CB  
2741 C CG1 . ILE B 82  ? 0.4685 0.9049 0.7363 0.0579  -0.0245 0.1458  992  ILE B CG1 
2742 C CG2 . ILE B 82  ? 0.3825 0.8820 0.6323 0.0549  -0.0361 0.1157  992  ILE B CG2 
2743 C CD1 . ILE B 82  ? 0.4520 0.9329 0.7074 0.0556  -0.0225 0.1507  992  ILE B CD1 
2744 N N   . ARG B 83  ? 0.3457 0.7159 0.6098 0.0477  -0.0349 0.0589  993  ARG B N   
2745 C CA  . ARG B 83  ? 0.3036 0.6619 0.5692 0.0433  -0.0375 0.0305  993  ARG B CA  
2746 C C   . ARG B 83  ? 0.3005 0.6219 0.5681 0.0400  -0.0337 0.0180  993  ARG B C   
2747 O O   . ARG B 83  ? 0.3232 0.6393 0.5880 0.0402  -0.0300 0.0267  993  ARG B O   
2748 C CB  . ARG B 83  ? 0.3296 0.7342 0.5896 0.0396  -0.0411 0.0104  993  ARG B CB  
2749 C CG  . ARG B 83  ? 0.3473 0.7720 0.6003 0.0361  -0.0384 -0.0006 993  ARG B CG  
2750 C CD  . ARG B 83  ? 0.4148 0.8970 0.6622 0.0326  -0.0413 -0.0189 993  ARG B CD  
2751 N NE  . ARG B 83  ? 0.5235 1.0016 0.7815 0.0270  -0.0421 -0.0538 993  ARG B NE  
2752 C CZ  . ARG B 83  ? 0.5589 1.0773 0.8180 0.0219  -0.0422 -0.0805 993  ARG B CZ  
2753 N NH1 . ARG B 83  ? 0.4677 1.0369 0.7138 0.0215  -0.0417 -0.0769 993  ARG B NH1 
2754 N NH2 . ARG B 83  ? 0.6105 1.1199 0.8866 0.0170  -0.0422 -0.1119 993  ARG B NH2 
2755 N N   . CYS B 84  ? 0.2712 0.5689 0.5454 0.0369  -0.0347 -0.0008 994  CYS B N   
2756 C CA  . CYS B 84  ? 0.3037 0.5728 0.5816 0.0339  -0.0320 -0.0127 994  CYS B CA  
2757 C C   . CYS B 84  ? 0.3399 0.6349 0.6164 0.0302  -0.0314 -0.0308 994  CYS B C   
2758 O O   . CYS B 84  ? 0.3366 0.6538 0.6183 0.0272  -0.0335 -0.0507 994  CYS B O   
2759 C CB  . CYS B 84  ? 0.2349 0.4751 0.5231 0.0319  -0.0329 -0.0239 994  CYS B CB  
2760 S SG  . CYS B 84  ? 0.2471 0.4560 0.5428 0.0288  -0.0302 -0.0348 994  CYS B SG  
2761 N N   . TRP B 85  ? 0.3118 0.6051 0.5837 0.0302  -0.0279 -0.0257 995  TRP B N   
2762 C CA  . TRP B 85  ? 0.3240 0.6449 0.5947 0.0270  -0.0263 -0.0418 995  TRP B CA  
2763 C C   . TRP B 85  ? 0.3169 0.6164 0.6012 0.0235  -0.0250 -0.0636 995  TRP B C   
2764 O O   . TRP B 85  ? 0.3282 0.6420 0.6149 0.0211  -0.0224 -0.0766 995  TRP B O   
2765 C CB  . TRP B 85  ? 0.3237 0.6556 0.5848 0.0285  -0.0227 -0.0248 995  TRP B CB  
2766 C CG  . TRP B 85  ? 0.3127 0.6711 0.5653 0.0321  -0.0236 -0.0012 995  TRP B CG  
2767 C CD1 . TRP B 85  ? 0.3008 0.6400 0.5549 0.0364  -0.0224 0.0250  995  TRP B CD1 
2768 C CD2 . TRP B 85  ? 0.3383 0.7501 0.5826 0.0319  -0.0257 -0.0012 995  TRP B CD2 
2769 N NE1 . TRP B 85  ? 0.3266 0.7020 0.5760 0.0395  -0.0235 0.0443  995  TRP B NE1 
2770 C CE2 . TRP B 85  ? 0.3611 0.7835 0.6024 0.0369  -0.0261 0.0296  995  TRP B CE2 
2771 C CE3 . TRP B 85  ? 0.3401 0.7949 0.5815 0.0279  -0.0272 -0.0252 995  TRP B CE3 
2772 C CZ2 . TRP B 85  ? 0.4127 0.8888 0.6462 0.0384  -0.0286 0.0406  995  TRP B CZ2 
2773 C CZ3 . TRP B 85  ? 0.3960 0.9063 0.6274 0.0286  -0.0296 -0.0176 995  TRP B CZ3 
2774 C CH2 . TRP B 85  ? 0.4093 0.9307 0.6358 0.0341  -0.0307 0.0167  995  TRP B CH2 
2775 N N   . TYR B 86  ? 0.2880 0.5553 0.5829 0.0234  -0.0263 -0.0663 996  TYR B N   
2776 C CA  . TYR B 86  ? 0.3174 0.5622 0.6296 0.0208  -0.0252 -0.0817 996  TYR B CA  
2777 C C   . TYR B 86  ? 0.3025 0.5591 0.6319 0.0177  -0.0266 -0.1035 996  TYR B C   
2778 O O   . TYR B 86  ? 0.3438 0.6040 0.6728 0.0181  -0.0293 -0.1012 996  TYR B O   
2779 C CB  . TYR B 86  ? 0.2853 0.4894 0.6000 0.0224  -0.0253 -0.0680 996  TYR B CB  
2780 C CG  . TYR B 86  ? 0.2080 0.3974 0.5106 0.0248  -0.0235 -0.0493 996  TYR B CG  
2781 C CD1 . TYR B 86  ? 0.2793 0.4783 0.5775 0.0245  -0.0208 -0.0490 996  TYR B CD1 
2782 C CD2 . TYR B 86  ? 0.2051 0.3714 0.5039 0.0267  -0.0239 -0.0343 996  TYR B CD2 
2783 C CE1 . TYR B 86  ? 0.2832 0.4680 0.5746 0.0261  -0.0186 -0.0331 996  TYR B CE1 
2784 C CE2 . TYR B 86  ? 0.2051 0.3584 0.4978 0.0281  -0.0217 -0.0207 996  TYR B CE2 
2785 C CZ  . TYR B 86  ? 0.2638 0.4256 0.5535 0.0278  -0.0190 -0.0197 996  TYR B CZ  
2786 O OH  . TYR B 86  ? 0.2508 0.3999 0.5382 0.0286  -0.0163 -0.0073 996  TYR B OH  
2787 N N   . ASP B 87  ? 0.2997 0.5622 0.6478 0.0145  -0.0244 -0.1253 997  ASP B N   
2788 C CA  . ASP B 87  ? 0.2594 0.5291 0.6320 0.0110  -0.0246 -0.1481 997  ASP B CA  
2789 C C   . ASP B 87  ? 0.2801 0.5104 0.6726 0.0112  -0.0243 -0.1428 997  ASP B C   
2790 O O   . ASP B 87  ? 0.2322 0.4343 0.6150 0.0140  -0.0249 -0.1216 997  ASP B O   
2791 C CB  . ASP B 87  ? 0.2681 0.5648 0.6581 0.0072  -0.0213 -0.1767 997  ASP B CB  
2792 C CG  . ASP B 87  ? 0.2514 0.5267 0.6555 0.0075  -0.0176 -0.1790 997  ASP B CG  
2793 O OD1 . ASP B 87  ? 0.2562 0.4947 0.6631 0.0100  -0.0179 -0.1616 997  ASP B OD1 
2794 O OD2 . ASP B 87  ? 0.2538 0.5533 0.6668 0.0051  -0.0143 -0.1992 997  ASP B OD2 
2795 N N   . LYS B 88  ? 0.3305 0.5621 0.7537 0.0078  -0.0231 -0.1628 998  LYS B N   
2796 C CA  . LYS B 88  ? 0.3410 0.5411 0.7877 0.0076  -0.0226 -0.1567 998  LYS B CA  
2797 C C   . LYS B 88  ? 0.3126 0.4846 0.7662 0.0096  -0.0209 -0.1439 998  LYS B C   
2798 O O   . LYS B 88  ? 0.2955 0.4418 0.7500 0.0112  -0.0218 -0.1251 998  LYS B O   
2799 C CB  . LYS B 88  ? 0.3553 0.5659 0.8405 0.0030  -0.0203 -0.1832 998  LYS B CB  
2800 C CG  . LYS B 88  ? 0.4300 0.6133 0.9458 0.0021  -0.0190 -0.1773 998  LYS B CG  
2801 C CD  . LYS B 88  ? 0.4291 0.6249 0.9862 -0.0030 -0.0156 -0.2065 998  LYS B CD  
2802 C CE  . LYS B 88  ? 0.4855 0.6839 1.0607 -0.0045 -0.0108 -0.2282 998  LYS B CE  
2803 N NZ  . LYS B 88  ? 0.4902 0.6557 1.0880 -0.0022 -0.0080 -0.2148 998  LYS B NZ  
2804 N N   . ASP B 89  ? 0.3052 0.4851 0.7628 0.0095  -0.0186 -0.1537 999  ASP B N   
2805 C CA  . ASP B 89  ? 0.2768 0.4348 0.7451 0.0114  -0.0171 -0.1446 999  ASP B CA  
2806 C C   . ASP B 89  ? 0.3091 0.4616 0.7445 0.0144  -0.0185 -0.1255 999  ASP B C   
2807 O O   . ASP B 89  ? 0.2666 0.4080 0.7075 0.0157  -0.0174 -0.1207 999  ASP B O   
2808 C CB  . ASP B 89  ? 0.2834 0.4532 0.7823 0.0094  -0.0130 -0.1689 999  ASP B CB  
2809 C CG  . ASP B 89  ? 0.2283 0.4063 0.7645 0.0057  -0.0106 -0.1918 999  ASP B CG  
2810 O OD1 . ASP B 89  ? 0.2152 0.3729 0.7704 0.0057  -0.0111 -0.1819 999  ASP B OD1 
2811 O OD2 . ASP B 89  ? 0.2211 0.4282 0.7677 0.0025  -0.0080 -0.2196 999  ASP B OD2 
2812 N N   . GLY B 90  ? 0.2541 0.4148 0.6589 0.0155  -0.0207 -0.1149 1000 GLY B N   
2813 C CA  . GLY B 90  ? 0.2835 0.4376 0.6631 0.0179  -0.0211 -0.0973 1000 GLY B CA  
2814 C C   . GLY B 90  ? 0.2210 0.3968 0.5889 0.0177  -0.0190 -0.1031 1000 GLY B C   
2815 O O   . GLY B 90  ? 0.2507 0.4202 0.6027 0.0194  -0.0185 -0.0891 1000 GLY B O   
2816 N N   . ARG B 91  ? 0.2187 0.4228 0.5944 0.0154  -0.0174 -0.1235 1001 ARG B N   
2817 C CA  . ARG B 91  ? 0.2494 0.4793 0.6152 0.0148  -0.0147 -0.1300 1001 ARG B CA  
2818 C C   . ARG B 91  ? 0.2447 0.5055 0.5864 0.0151  -0.0157 -0.1240 1001 ARG B C   
2819 O O   . ARG B 91  ? 0.2827 0.5556 0.6223 0.0146  -0.0183 -0.1264 1001 ARG B O   
2820 C CB  . ARG B 91  ? 0.2183 0.4659 0.6099 0.0117  -0.0113 -0.1585 1001 ARG B CB  
2821 C CG  . ARG B 91  ? 0.2338 0.4545 0.6504 0.0124  -0.0094 -0.1605 1001 ARG B CG  
2822 C CD  . ARG B 91  ? 0.2784 0.5144 0.7290 0.0095  -0.0054 -0.1904 1001 ARG B CD  
2823 N NE  . ARG B 91  ? 0.3505 0.5606 0.8301 0.0110  -0.0037 -0.1896 1001 ARG B NE  
2824 C CZ  . ARG B 91  ? 0.3495 0.5414 0.8653 0.0109  -0.0033 -0.1949 1001 ARG B CZ  
2825 N NH1 . ARG B 91  ? 0.3071 0.5007 0.8343 0.0089  -0.0042 -0.2021 1001 ARG B NH1 
2826 N NH2 . ARG B 91  ? 0.2817 0.4545 0.8257 0.0128  -0.0017 -0.1919 1001 ARG B NH2 
2827 N N   . LEU B 92  ? 0.2386 0.5140 0.5642 0.0158  -0.0135 -0.1148 1002 LEU B N   
2828 C CA  . LEU B 92  ? 0.2826 0.5854 0.5859 0.0171  -0.0140 -0.1001 1002 LEU B CA  
2829 C C   . LEU B 92  ? 0.3436 0.6957 0.6458 0.0142  -0.0137 -0.1193 1002 LEU B C   
2830 O O   . LEU B 92  ? 0.3705 0.7460 0.6784 0.0115  -0.0102 -0.1371 1002 LEU B O   
2831 C CB  . LEU B 92  ? 0.3417 0.6425 0.6337 0.0185  -0.0107 -0.0831 1002 LEU B CB  
2832 C CG  . LEU B 92  ? 0.3495 0.6791 0.6231 0.0201  -0.0098 -0.0633 1002 LEU B CG  
2833 C CD1 . LEU B 92  ? 0.3244 0.6343 0.5928 0.0235  -0.0126 -0.0417 1002 LEU B CD1 
2834 C CD2 . LEU B 92  ? 0.3020 0.6317 0.5717 0.0201  -0.0050 -0.0527 1002 LEU B CD2 
2835 N N   . LEU B 93  ? 0.3637 0.7344 0.6591 0.0147  -0.0174 -0.1165 1003 LEU B N   
2836 C CA  . LEU B 93  ? 0.3736 0.7931 0.6706 0.0113  -0.0182 -0.1385 1003 LEU B CA  
2837 C C   . LEU B 93  ? 0.3758 0.8422 0.6617 0.0094  -0.0148 -0.1436 1003 LEU B C   
2838 O O   . LEU B 93  ? 0.3672 0.8367 0.6371 0.0119  -0.0129 -0.1196 1003 LEU B O   
2839 C CB  . LEU B 93  ? 0.3625 0.7995 0.6483 0.0132  -0.0231 -0.1259 1003 LEU B CB  
2840 C CG  . LEU B 93  ? 0.3793 0.7806 0.6754 0.0145  -0.0265 -0.1230 1003 LEU B CG  
2841 C CD1 . LEU B 93  ? 0.4138 0.8384 0.6987 0.0167  -0.0310 -0.1099 1003 LEU B CD1 
2842 C CD2 . LEU B 93  ? 0.3595 0.7542 0.6821 0.0100  -0.0258 -0.1543 1003 LEU B CD2 
2843 N N   . GLN B 94  ? 0.3486 0.8549 0.6449 0.0046  -0.0134 -0.1759 1004 GLN B N   
2844 C CA  . GLN B 94  ? 0.4968 1.0533 0.7840 0.0018  -0.0094 -0.1858 1004 GLN B CA  
2845 C C   . GLN B 94  ? 0.5314 1.1330 0.7911 0.0038  -0.0113 -0.1605 1004 GLN B C   
2846 O O   . GLN B 94  ? 0.5531 1.1846 0.7996 0.0036  -0.0076 -0.1508 1004 GLN B O   
2847 C CB  . GLN B 94  ? 0.5217 1.1158 0.8289 -0.0044 -0.0072 -0.2299 1004 GLN B CB  
2848 C CG  . GLN B 94  ? 0.5216 1.1587 0.8269 -0.0069 -0.0117 -0.2436 1004 GLN B CG  
2849 C CD  . GLN B 94  ? 0.4978 1.1979 0.8127 -0.0137 -0.0084 -0.2840 1004 GLN B CD  
2850 O OE1 . GLN B 94  ? 0.5730 1.2873 0.8907 -0.0161 -0.0025 -0.2982 1004 GLN B OE1 
2851 N NE2 . GLN B 94  ? 0.5134 1.2405 0.8258 -0.0167 -0.0114 -0.3017 1004 GLN B NE2 
2852 N N   . GLU B 95  ? 0.6571 1.2652 0.9099 0.0060  -0.0169 -0.1479 1005 GLU B N   
2853 C CA  . GLU B 95  ? 0.6769 1.3294 0.9078 0.0087  -0.0194 -0.1210 1005 GLU B CA  
2854 C C   . GLU B 95  ? 0.6987 1.3202 0.9194 0.0146  -0.0183 -0.0784 1005 GLU B C   
2855 O O   . GLU B 95  ? 0.7136 1.3704 0.9202 0.0174  -0.0191 -0.0508 1005 GLU B O   
2856 C CB  . GLU B 95  ? 0.6519 1.3220 0.8834 0.0091  -0.0259 -0.1240 1005 GLU B CB  
2857 C CG  . GLU B 95  ? 0.6563 1.3503 0.9045 0.0026  -0.0266 -0.1690 1005 GLU B CG  
2858 C CD  . GLU B 95  ? 0.8222 1.4917 1.0838 0.0030  -0.0315 -0.1760 1005 GLU B CD  
2859 O OE1 . GLU B 95  ? 0.7927 1.4109 1.0542 0.0078  -0.0332 -0.1509 1005 GLU B OE1 
2860 O OE2 . GLU B 95  ? 0.8342 1.5378 1.1077 -0.0020 -0.0333 -0.2078 1005 GLU B OE2 
2861 N N   . PHE B 96  ? 0.5409 1.1003 0.7713 0.0163  -0.0163 -0.0728 1006 PHE B N   
2862 C CA  . PHE B 96  ? 0.5005 1.0278 0.7266 0.0208  -0.0141 -0.0382 1006 PHE B CA  
2863 C C   . PHE B 96  ? 0.5950 1.1622 0.8094 0.0209  -0.0096 -0.0200 1006 PHE B C   
2864 O O   . PHE B 96  ? 0.5977 1.1854 0.8113 0.0171  -0.0054 -0.0371 1006 PHE B O   
2865 C CB  . PHE B 96  ? 0.4757 0.9441 0.7142 0.0205  -0.0117 -0.0454 1006 PHE B CB  
2866 C CG  . PHE B 96  ? 0.4423 0.8699 0.6813 0.0246  -0.0102 -0.0160 1006 PHE B CG  
2867 C CD1 . PHE B 96  ? 0.3976 0.7988 0.6394 0.0281  -0.0135 -0.0012 1006 PHE B CD1 
2868 C CD2 . PHE B 96  ? 0.4267 0.8430 0.6662 0.0244  -0.0051 -0.0056 1006 PHE B CD2 
2869 C CE1 . PHE B 96  ? 0.4302 0.7957 0.6762 0.0312  -0.0114 0.0217  1006 PHE B CE1 
2870 C CE2 . PHE B 96  ? 0.4068 0.7871 0.6508 0.0273  -0.0032 0.0177  1006 PHE B CE2 
2871 C CZ  . PHE B 96  ? 0.3954 0.7506 0.6432 0.0306  -0.0062 0.0305  1006 PHE B CZ  
2872 N N   . ASN B 97  ? 0.6037 1.1843 0.8115 0.0254  -0.0101 0.0155  1007 ASN B N   
2873 C CA  . ASN B 97  ? 0.6556 1.2731 0.8553 0.0260  -0.0054 0.0403  1007 ASN B CA  
2874 C C   . ASN B 97  ? 0.7582 1.3386 0.9647 0.0251  0.0010  0.0430  1007 ASN B C   
2875 O O   . ASN B 97  ? 0.7883 1.3351 1.0024 0.0285  0.0036  0.0702  1007 ASN B O   
2876 C CB  . ASN B 97  ? 0.7336 1.3614 0.9332 0.0319  -0.0067 0.0819  1007 ASN B CB  
2877 C CG  . ASN B 97  ? 0.8002 1.4806 0.9924 0.0326  -0.0022 0.1103  1007 ASN B CG  
2878 O OD1 . ASN B 97  ? 0.8323 1.5275 1.0204 0.0290  0.0034  0.1035  1007 ASN B OD1 
2879 N ND2 . ASN B 97  ? 0.7851 1.4953 0.9773 0.0374  -0.0044 0.1440  1007 ASN B ND2 
2880 N N   . LYS B 98  ? 0.7862 1.3739 0.9929 0.0203  0.0038  0.0136  1008 LYS B N   
2881 C CA  . LYS B 98  ? 0.8164 1.3645 1.0320 0.0191  0.0087  0.0094  1008 LYS B CA  
2882 C C   . LYS B 98  ? 0.9097 1.4772 1.1220 0.0192  0.0156  0.0346  1008 LYS B C   
2883 O O   . LYS B 98  ? 0.8640 1.4155 1.0820 0.0169  0.0203  0.0261  1008 LYS B O   
2884 C CB  . LYS B 98  ? 0.7908 1.3392 1.0130 0.0145  0.0095  -0.0310 1008 LYS B CB  
2885 C CG  . LYS B 98  ? 0.8531 1.4671 1.0676 0.0102  0.0117  -0.0520 1008 LYS B CG  
2886 C CD  . LYS B 98  ? 0.8050 1.4116 1.0336 0.0060  0.0145  -0.0904 1008 LYS B CD  
2887 C CE  . LYS B 98  ? 0.7870 1.4473 1.0098 0.0020  0.0211  -0.1011 1008 LYS B CE  
2888 N NZ  . LYS B 98  ? 0.8450 1.5034 1.0598 0.0037  0.0261  -0.0675 1008 LYS B NZ  
2889 N N   . ILE B 99  ? 0.9642 1.5663 1.1699 0.0219  0.0163  0.0668  1009 ILE B N   
2890 C CA  . ILE B 99  ? 0.9983 1.6140 1.2060 0.0225  0.0233  0.0979  1009 ILE B CA  
2891 C C   . ILE B 99  ? 0.9768 1.5750 1.1944 0.0281  0.0229  0.1375  1009 ILE B C   
2892 O O   . ILE B 99  ? 1.0228 1.6022 1.2534 0.0295  0.0288  0.1637  1009 ILE B O   
2893 C CB  . ILE B 99  ? 1.0744 1.7659 1.2674 0.0195  0.0268  0.0994  1009 ILE B CB  
2894 C CG1 . ILE B 99  ? 1.0610 1.7664 1.2502 0.0137  0.0288  0.0573  1009 ILE B CG1 
2895 C CG2 . ILE B 99  ? 1.0845 1.7932 1.2816 0.0206  0.0344  0.1380  1009 ILE B CG2 
2896 C CD1 . ILE B 99  ? 1.0431 1.8251 1.2186 0.0098  0.0335  0.0541  1009 ILE B CD1 
2897 N N   . GLU B 100 ? 0.9206 1.5234 1.1359 0.0313  0.0164  0.1409  1010 GLU B N   
2898 C CA  . GLU B 100 ? 0.9127 1.4936 1.1419 0.0371  0.0155  0.1739  1010 GLU B CA  
2899 C C   . GLU B 100 ? 0.8880 1.4196 1.1229 0.0385  0.0097  0.1556  1010 GLU B C   
2900 O O   . GLU B 100 ? 0.8658 1.4105 1.0980 0.0412  0.0039  0.1579  1010 GLU B O   
2901 C CB  . GLU B 100 ? 0.9286 1.5698 1.1518 0.0404  0.0135  0.2023  1010 GLU B CB  
2902 C CG  . GLU B 100 ? 1.0006 1.6243 1.2440 0.0471  0.0139  0.2415  1010 GLU B CG  
2903 C CD  . GLU B 100 ? 1.0588 1.6572 1.3245 0.0484  0.0228  0.2708  1010 GLU B CD  
2904 O OE1 . GLU B 100 ? 1.0037 1.6121 1.2653 0.0444  0.0286  0.2671  1010 GLU B OE1 
2905 O OE2 . GLU B 100 ? 1.1069 1.6758 1.3971 0.0534  0.0245  0.2965  1010 GLU B OE2 
2906 N N   . PRO B 101 ? 0.7895 1.2670 1.0325 0.0367  0.0110  0.1382  1011 PRO B N   
2907 C CA  . PRO B 101 ? 0.6592 1.0959 0.9052 0.0372  0.0056  0.1179  1011 PRO B CA  
2908 C C   . PRO B 101 ? 0.6704 1.0724 0.9328 0.0418  0.0058  0.1399  1011 PRO B C   
2909 O O   . PRO B 101 ? 0.6736 1.0520 0.9515 0.0428  0.0114  0.1577  1011 PRO B O   
2910 C CB  . PRO B 101 ? 0.6376 1.0394 0.8859 0.0332  0.0074  0.0927  1011 PRO B CB  
2911 C CG  . PRO B 101 ? 0.7467 1.1500 1.0011 0.0323  0.0147  0.1092  1011 PRO B CG  
2912 C CD  . PRO B 101 ? 0.8067 1.2623 1.0563 0.0339  0.0173  0.1359  1011 PRO B CD  
2913 N N   . PRO B 102 ? 0.6046 1.0030 0.8669 0.0443  0.0003  0.1373  1012 PRO B N   
2914 C CA  . PRO B 102 ? 0.5251 0.8924 0.8052 0.0487  0.0009  0.1558  1012 PRO B CA  
2915 C C   . PRO B 102 ? 0.4928 0.8058 0.7808 0.0469  0.0012  0.1376  1012 PRO B C   
2916 O O   . PRO B 102 ? 0.5442 0.8444 0.8229 0.0431  -0.0009 0.1111  1012 PRO B O   
2917 C CB  . PRO B 102 ? 0.5406 0.9325 0.8152 0.0515  -0.0056 0.1568  1012 PRO B CB  
2918 C CG  . PRO B 102 ? 0.5593 0.9636 0.8164 0.0468  -0.0102 0.1229  1012 PRO B CG  
2919 C CD  . PRO B 102 ? 0.5735 0.9945 0.8223 0.0427  -0.0063 0.1141  1012 PRO B CD  
2920 N N   . LEU B 103 ? 0.3870 0.6708 0.6951 0.0498  0.0043  0.1526  1013 LEU B N   
2921 C CA  . LEU B 103 ? 0.2969 0.5351 0.6131 0.0482  0.0047  0.1365  1013 LEU B CA  
2922 C C   . LEU B 103 ? 0.3405 0.5727 0.6436 0.0470  -0.0019 0.1133  1013 LEU B C   
2923 O O   . LEU B 103 ? 0.4028 0.6550 0.7013 0.0493  -0.0061 0.1160  1013 LEU B O   
2924 C CB  . LEU B 103 ? 0.2841 0.5002 0.6261 0.0519  0.0087  0.1539  1013 LEU B CB  
2925 C CG  . LEU B 103 ? 0.3707 0.5865 0.7382 0.0541  0.0165  0.1807  1013 LEU B CG  
2926 C CD1 . LEU B 103 ? 0.2793 0.4940 0.6446 0.0499  0.0210  0.1778  1013 LEU B CD1 
2927 C CD2 . LEU B 103 ? 0.3406 0.5929 0.7144 0.0593  0.0165  0.2110  1013 LEU B CD2 
2928 N N   . ILE B 104 ? 0.2407 0.4464 0.5402 0.0433  -0.0027 0.0921  1014 ILE B N   
2929 C CA  . ILE B 104 ? 0.2688 0.4628 0.5617 0.0420  -0.0077 0.0728  1014 ILE B CA  
2930 C C   . ILE B 104 ? 0.2669 0.4266 0.5712 0.0422  -0.0062 0.0713  1014 ILE B C   
2931 O O   . ILE B 104 ? 0.2514 0.3908 0.5622 0.0402  -0.0029 0.0686  1014 ILE B O   
2932 C CB  . ILE B 104 ? 0.3346 0.5288 0.6177 0.0379  -0.0099 0.0509  1014 ILE B CB  
2933 C CG1 . ILE B 104 ? 0.3219 0.5546 0.5951 0.0370  -0.0112 0.0466  1014 ILE B CG1 
2934 C CG2 . ILE B 104 ? 0.2199 0.3961 0.5027 0.0365  -0.0139 0.0345  1014 ILE B CG2 
2935 C CD1 . ILE B 104 ? 0.3397 0.5731 0.6096 0.0331  -0.0118 0.0241  1014 ILE B CD1 
2936 N N   . PHE B 105 ? 0.2889 0.4453 0.5962 0.0443  -0.0086 0.0717  1015 PHE B N   
2937 C CA  . PHE B 105 ? 0.2490 0.3783 0.5651 0.0438  -0.0075 0.0658  1015 PHE B CA  
2938 C C   . PHE B 105 ? 0.2553 0.3784 0.5608 0.0409  -0.0120 0.0475  1015 PHE B C   
2939 O O   . PHE B 105 ? 0.2634 0.4000 0.5637 0.0415  -0.0159 0.0438  1015 PHE B O   
2940 C CB  . PHE B 105 ? 0.2262 0.3563 0.5558 0.0480  -0.0063 0.0784  1015 PHE B CB  
2941 C CG  . PHE B 105 ? 0.2643 0.3959 0.6132 0.0512  -0.0007 0.0987  1015 PHE B CG  
2942 C CD1 . PHE B 105 ? 0.2566 0.4151 0.6047 0.0539  -0.0005 0.1170  1015 PHE B CD1 
2943 C CD2 . PHE B 105 ? 0.2433 0.3522 0.6142 0.0514  0.0051  0.0999  1015 PHE B CD2 
2944 C CE1 . PHE B 105 ? 0.2497 0.4102 0.6198 0.0571  0.0053  0.1395  1015 PHE B CE1 
2945 C CE2 . PHE B 105 ? 0.2440 0.3528 0.6396 0.0544  0.0112  0.1189  1015 PHE B CE2 
2946 C CZ  . PHE B 105 ? 0.2510 0.3846 0.6469 0.0574  0.0114  0.1405  1015 PHE B CZ  
2947 N N   . GLU B 106 ? 0.2116 0.3166 0.5161 0.0376  -0.0114 0.0369  1016 GLU B N   
2948 C CA  . GLU B 106 ? 0.2317 0.3301 0.5309 0.0351  -0.0149 0.0238  1016 GLU B CA  
2949 C C   . GLU B 106 ? 0.2048 0.2912 0.5093 0.0353  -0.0143 0.0231  1016 GLU B C   
2950 O O   . GLU B 106 ? 0.2544 0.3342 0.5682 0.0368  -0.0106 0.0293  1016 GLU B O   
2951 C CB  . GLU B 106 ? 0.2033 0.2923 0.5005 0.0319  -0.0150 0.0154  1016 GLU B CB  
2952 C CG  . GLU B 106 ? 0.2040 0.3064 0.4970 0.0312  -0.0160 0.0114  1016 GLU B CG  
2953 C CD  . GLU B 106 ? 0.2010 0.2951 0.4952 0.0285  -0.0166 0.0029  1016 GLU B CD  
2954 O OE1 . GLU B 106 ? 0.2017 0.2816 0.4983 0.0271  -0.0167 0.0016  1016 GLU B OE1 
2955 O OE2 . GLU B 106 ? 0.2015 0.3065 0.4952 0.0279  -0.0170 -0.0030 1016 GLU B OE2 
2956 N N   . CYS B 107 ? 0.2012 0.2856 0.5027 0.0337  -0.0173 0.0152  1017 CYS B N   
2957 C CA  . CYS B 107 ? 0.2150 0.2912 0.5206 0.0334  -0.0162 0.0141  1017 CYS B CA  
2958 C C   . CYS B 107 ? 0.2461 0.3107 0.5539 0.0310  -0.0133 0.0109  1017 CYS B C   
2959 O O   . CYS B 107 ? 0.2406 0.3025 0.5460 0.0292  -0.0132 0.0088  1017 CYS B O   
2960 C CB  . CYS B 107 ? 0.1974 0.2755 0.5012 0.0317  -0.0193 0.0081  1017 CYS B CB  
2961 S SG  . CYS B 107 ? 0.2146 0.3097 0.5191 0.0337  -0.0226 0.0079  1017 CYS B SG  
2962 N N   . ASN B 108 ? 0.2017 0.2621 0.5149 0.0306  -0.0107 0.0089  1018 ASN B N   
2963 C CA  . ASN B 108 ? 0.2552 0.3099 0.5728 0.0281  -0.0072 0.0035  1018 ASN B CA  
2964 C C   . ASN B 108 ? 0.2524 0.3092 0.5693 0.0256  -0.0064 -0.0031 1018 ASN B C   
2965 O O   . ASN B 108 ? 0.2620 0.3226 0.5740 0.0254  -0.0089 -0.0021 1018 ASN B O   
2966 C CB  . ASN B 108 ? 0.2454 0.2961 0.5778 0.0301  -0.0021 0.0071  1018 ASN B CB  
2967 C CG  . ASN B 108 ? 0.2220 0.2744 0.5649 0.0339  -0.0004 0.0129  1018 ASN B CG  
2968 O OD1 . ASN B 108 ? 0.2405 0.2924 0.5884 0.0334  0.0015  0.0071  1018 ASN B OD1 
2969 N ND2 . ASN B 108 ? 0.2241 0.2815 0.5703 0.0379  -0.0010 0.0250  1018 ASN B ND2 
2970 N N   . GLN B 109 ? 0.2392 0.2962 0.5624 0.0230  -0.0024 -0.0109 1019 GLN B N   
2971 C CA  . GLN B 109 ? 0.2379 0.3029 0.5588 0.0198  -0.0012 -0.0184 1019 GLN B CA  
2972 C C   . GLN B 109 ? 0.2732 0.3390 0.6037 0.0217  0.0022  -0.0201 1019 GLN B C   
2973 O O   . GLN B 109 ? 0.2582 0.3331 0.5857 0.0194  0.0031  -0.0249 1019 GLN B O   
2974 C CB  . GLN B 109 ? 0.2280 0.2994 0.5521 0.0156  0.0017  -0.0296 1019 GLN B CB  
2975 C CG  . GLN B 109 ? 0.2390 0.3042 0.5826 0.0159  0.0079  -0.0368 1019 GLN B CG  
2976 C CD  . GLN B 109 ? 0.2276 0.2841 0.5752 0.0168  0.0076  -0.0319 1019 GLN B CD  
2977 O OE1 . GLN B 109 ? 0.2600 0.3132 0.5966 0.0188  0.0031  -0.0216 1019 GLN B OE1 
2978 N NE2 . GLN B 109 ? 0.2197 0.2737 0.5859 0.0151  0.0132  -0.0405 1019 GLN B NE2 
2979 N N   . ALA B 110 ? 0.2248 0.2836 0.5678 0.0261  0.0041  -0.0146 1020 ALA B N   
2980 C CA  . ALA B 110 ? 0.2544 0.3143 0.6087 0.0288  0.0068  -0.0141 1020 ALA B CA  
2981 C C   . ALA B 110 ? 0.2716 0.3352 0.6166 0.0309  0.0019  -0.0062 1020 ALA B C   
2982 O O   . ALA B 110 ? 0.2429 0.3104 0.5942 0.0321  0.0033  -0.0073 1020 ALA B O   
2983 C CB  . ALA B 110 ? 0.2311 0.2843 0.6077 0.0331  0.0111  -0.0089 1020 ALA B CB  
2984 N N   . CYS B 111 ? 0.2550 0.3190 0.5880 0.0312  -0.0034 -0.0001 1021 CYS B N   
2985 C CA  . CYS B 111 ? 0.2967 0.3661 0.6248 0.0326  -0.0078 0.0045  1021 CYS B CA  
2986 C C   . CYS B 111 ? 0.2610 0.3343 0.5850 0.0293  -0.0081 0.0002  1021 CYS B C   
2987 O O   . CYS B 111 ? 0.2666 0.3410 0.5861 0.0256  -0.0068 -0.0040 1021 CYS B O   
2988 C CB  . CYS B 111 ? 0.2704 0.3413 0.5897 0.0327  -0.0123 0.0077  1021 CYS B CB  
2989 S SG  . CYS B 111 ? 0.2023 0.2746 0.5247 0.0363  -0.0119 0.0156  1021 CYS B SG  
2990 N N   . SER B 112 ? 0.2136 0.2919 0.5402 0.0305  -0.0099 0.0021  1022 SER B N   
2991 C CA  . SER B 112 ? 0.2213 0.3038 0.5461 0.0271  -0.0100 0.0003  1022 SER B CA  
2992 C C   . SER B 112 ? 0.2279 0.3099 0.5483 0.0245  -0.0138 0.0021  1022 SER B C   
2993 O O   . SER B 112 ? 0.2211 0.3061 0.5419 0.0212  -0.0133 0.0036  1022 SER B O   
2994 C CB  . SER B 112 ? 0.2376 0.3259 0.5701 0.0288  -0.0100 0.0008  1022 SER B CB  
2995 O OG  . SER B 112 ? 0.2576 0.3496 0.5919 0.0317  -0.0142 0.0035  1022 SER B OG  
2996 N N   . CYS B 113 ? 0.2564 0.3362 0.5749 0.0259  -0.0169 0.0026  1023 CYS B N   
2997 C CA  . CYS B 113 ? 0.2743 0.3538 0.5947 0.0238  -0.0198 0.0021  1023 CYS B CA  
2998 C C   . CYS B 113 ? 0.2503 0.3262 0.5678 0.0211  -0.0193 0.0047  1023 CYS B C   
2999 O O   . CYS B 113 ? 0.1962 0.2721 0.5076 0.0204  -0.0170 0.0050  1023 CYS B O   
3000 C CB  . CYS B 113 ? 0.2228 0.3048 0.5424 0.0258  -0.0226 -0.0006 1023 CYS B CB  
3001 S SG  . CYS B 113 ? 0.1937 0.2706 0.5050 0.0273  -0.0215 0.0015  1023 CYS B SG  
3002 N N   . TRP B 114 ? 0.2356 0.3108 0.5605 0.0194  -0.0212 0.0060  1024 TRP B N   
3003 C CA  . TRP B 114 ? 0.2778 0.3523 0.6033 0.0174  -0.0214 0.0115  1024 TRP B CA  
3004 C C   . TRP B 114 ? 0.2536 0.3240 0.5751 0.0185  -0.0229 0.0092  1024 TRP B C   
3005 O O   . TRP B 114 ? 0.2561 0.3249 0.5776 0.0204  -0.0239 0.0036  1024 TRP B O   
3006 C CB  . TRP B 114 ? 0.2920 0.3671 0.6342 0.0155  -0.0220 0.0165  1024 TRP B CB  
3007 C CG  . TRP B 114 ? 0.3007 0.3815 0.6480 0.0135  -0.0198 0.0221  1024 TRP B CG  
3008 C CD1 . TRP B 114 ? 0.3306 0.4140 0.6763 0.0138  -0.0184 0.0180  1024 TRP B CD1 
3009 C CD2 . TRP B 114 ? 0.3023 0.3892 0.6587 0.0109  -0.0186 0.0344  1024 TRP B CD2 
3010 N NE1 . TRP B 114 ? 0.3511 0.4411 0.7035 0.0113  -0.0160 0.0254  1024 TRP B NE1 
3011 C CE2 . TRP B 114 ? 0.3125 0.4056 0.6714 0.0094  -0.0159 0.0365  1024 TRP B CE2 
3012 C CE3 . TRP B 114 ? 0.2754 0.3653 0.6395 0.0100  -0.0194 0.0458  1024 TRP B CE3 
3013 C CZ2 . TRP B 114 ? 0.3197 0.4226 0.6876 0.0065  -0.0136 0.0501  1024 TRP B CZ2 
3014 C CZ3 . TRP B 114 ? 0.2947 0.3952 0.6682 0.0076  -0.0175 0.0609  1024 TRP B CZ3 
3015 C CH2 . TRP B 114 ? 0.2711 0.3783 0.6461 0.0057  -0.0144 0.0631  1024 TRP B CH2 
3016 N N   . ARG B 115 ? 0.2549 0.3271 0.5732 0.0172  -0.0230 0.0137  1025 ARG B N   
3017 C CA  . ARG B 115 ? 0.2579 0.3273 0.5731 0.0179  -0.0242 0.0119  1025 ARG B CA  
3018 C C   . ARG B 115 ? 0.2879 0.3533 0.6144 0.0189  -0.0261 0.0094  1025 ARG B C   
3019 O O   . ARG B 115 ? 0.2790 0.3425 0.6032 0.0198  -0.0266 0.0058  1025 ARG B O   
3020 C CB  . ARG B 115 ? 0.2199 0.2967 0.5321 0.0159  -0.0247 0.0179  1025 ARG B CB  
3021 C CG  . ARG B 115 ? 0.3361 0.4121 0.6481 0.0162  -0.0264 0.0174  1025 ARG B CG  
3022 C CD  . ARG B 115 ? 0.2885 0.3601 0.5920 0.0169  -0.0247 0.0092  1025 ARG B CD  
3023 N NE  . ARG B 115 ? 0.3345 0.4068 0.6385 0.0167  -0.0260 0.0085  1025 ARG B NE  
3024 C CZ  . ARG B 115 ? 0.3228 0.3898 0.6324 0.0182  -0.0270 0.0069  1025 ARG B CZ  
3025 N NH1 . ARG B 115 ? 0.2382 0.3012 0.5538 0.0198  -0.0271 0.0046  1025 ARG B NH1 
3026 N NH2 . ARG B 115 ? 0.3709 0.4395 0.6811 0.0179  -0.0278 0.0060  1025 ARG B NH2 
3027 N N   . ASN B 116 ? 0.2435 0.3087 0.5848 0.0183  -0.0265 0.0097  1026 ASN B N   
3028 C CA  . ASN B 116 ? 0.2732 0.3364 0.6313 0.0186  -0.0273 0.0038  1026 ASN B CA  
3029 C C   . ASN B 116 ? 0.2249 0.2920 0.5844 0.0191  -0.0272 -0.0079 1026 ASN B C   
3030 O O   . ASN B 116 ? 0.2189 0.2880 0.5971 0.0183  -0.0272 -0.0160 1026 ASN B O   
3031 C CB  . ASN B 116 ? 0.2949 0.3569 0.6763 0.0172  -0.0271 0.0112  1026 ASN B CB  
3032 C CG  . ASN B 116 ? 0.3057 0.3700 0.6903 0.0157  -0.0257 0.0160  1026 ASN B CG  
3033 O OD1 . ASN B 116 ? 0.4062 0.4710 0.8001 0.0151  -0.0251 0.0078  1026 ASN B OD1 
3034 N ND2 . ASN B 116 ? 0.3182 0.3872 0.6952 0.0147  -0.0252 0.0285  1026 ASN B ND2 
3035 N N   . CYS B 117 ? 0.2373 0.3079 0.5804 0.0204  -0.0270 -0.0092 1027 CYS B N   
3036 C CA  . CYS B 117 ? 0.2299 0.3098 0.5733 0.0211  -0.0276 -0.0178 1027 CYS B CA  
3037 C C   . CYS B 117 ? 0.2192 0.3070 0.5630 0.0217  -0.0281 -0.0268 1027 CYS B C   
3038 O O   . CYS B 117 ? 0.2378 0.3215 0.5787 0.0220  -0.0277 -0.0253 1027 CYS B O   
3039 C CB  . CYS B 117 ? 0.2135 0.2964 0.5426 0.0231  -0.0271 -0.0133 1027 CYS B CB  
3040 S SG  . CYS B 117 ? 0.2585 0.3442 0.5728 0.0260  -0.0263 -0.0097 1027 CYS B SG  
3041 N N   . LYS B 118 ? 0.2126 0.3151 0.5603 0.0215  -0.0290 -0.0370 1028 LYS B N   
3042 C CA  . LYS B 118 ? 0.2237 0.3401 0.5713 0.0214  -0.0290 -0.0473 1028 LYS B CA  
3043 C C   . LYS B 118 ? 0.2092 0.3304 0.5376 0.0238  -0.0285 -0.0396 1028 LYS B C   
3044 O O   . LYS B 118 ? 0.2295 0.3665 0.5556 0.0238  -0.0281 -0.0465 1028 LYS B O   
3045 C CB  . LYS B 118 ? 0.2299 0.3683 0.5846 0.0201  -0.0301 -0.0615 1028 LYS B CB  
3046 C CG  . LYS B 118 ? 0.2518 0.3882 0.6331 0.0168  -0.0297 -0.0737 1028 LYS B CG  
3047 C CD  . LYS B 118 ? 0.2622 0.3862 0.6631 0.0155  -0.0277 -0.0778 1028 LYS B CD  
3048 C CE  . LYS B 118 ? 0.2433 0.3659 0.6780 0.0123  -0.0262 -0.0899 1028 LYS B CE  
3049 N NZ  . LYS B 118 ? 0.3422 0.4525 0.7993 0.0120  -0.0240 -0.0910 1028 LYS B NZ  
3050 N N   . ASN B 119 ? 0.1950 0.3056 0.5125 0.0257  -0.0278 -0.0264 1029 ASN B N   
3051 C CA  . ASN B 119 ? 0.2401 0.3562 0.5453 0.0280  -0.0265 -0.0180 1029 ASN B CA  
3052 C C   . ASN B 119 ? 0.2277 0.3270 0.5298 0.0280  -0.0244 -0.0110 1029 ASN B C   
3053 O O   . ASN B 119 ? 0.2238 0.3176 0.5217 0.0295  -0.0226 -0.0022 1029 ASN B O   
3054 C CB  . ASN B 119 ? 0.2281 0.3516 0.5289 0.0306  -0.0268 -0.0098 1029 ASN B CB  
3055 C CG  . ASN B 119 ? 0.2128 0.3452 0.5072 0.0334  -0.0250 0.0013  1029 ASN B CG  
3056 O OD1 . ASN B 119 ? 0.2042 0.3437 0.4953 0.0330  -0.0239 0.0008  1029 ASN B OD1 
3057 N ND2 . ASN B 119 ? 0.2336 0.3658 0.5289 0.0363  -0.0241 0.0123  1029 ASN B ND2 
3058 N N   . ARG B 120 ? 0.2190 0.3118 0.5263 0.0262  -0.0246 -0.0158 1030 ARG B N   
3059 C CA  . ARG B 120 ? 0.2387 0.3183 0.5447 0.0255  -0.0236 -0.0110 1030 ARG B CA  
3060 C C   . ARG B 120 ? 0.2132 0.2933 0.5245 0.0246  -0.0236 -0.0159 1030 ARG B C   
3061 O O   . ARG B 120 ? 0.1924 0.2644 0.5086 0.0236  -0.0244 -0.0143 1030 ARG B O   
3062 C CB  . ARG B 120 ? 0.2371 0.3075 0.5465 0.0243  -0.0245 -0.0082 1030 ARG B CB  
3063 C CG  . ARG B 120 ? 0.2496 0.3188 0.5542 0.0250  -0.0234 -0.0038 1030 ARG B CG  
3064 C CD  . ARG B 120 ? 0.2632 0.3287 0.5711 0.0234  -0.0239 -0.0018 1030 ARG B CD  
3065 N NE  . ARG B 120 ? 0.2438 0.3102 0.5492 0.0242  -0.0225 0.0000  1030 ARG B NE  
3066 C CZ  . ARG B 120 ? 0.2544 0.3185 0.5565 0.0241  -0.0199 0.0016  1030 ARG B CZ  
3067 N NH1 . ARG B 120 ? 0.2385 0.3000 0.5383 0.0229  -0.0186 0.0010  1030 ARG B NH1 
3068 N NH2 . ARG B 120 ? 0.2009 0.2664 0.5044 0.0249  -0.0183 0.0022  1030 ARG B NH2 
3069 N N   . VAL B 121 ? 0.1951 0.2878 0.5061 0.0249  -0.0228 -0.0216 1031 VAL B N   
3070 C CA  . VAL B 121 ? 0.2081 0.3031 0.5265 0.0241  -0.0223 -0.0285 1031 VAL B CA  
3071 C C   . VAL B 121 ? 0.2264 0.3140 0.5403 0.0240  -0.0208 -0.0221 1031 VAL B C   
3072 O O   . VAL B 121 ? 0.2191 0.2989 0.5402 0.0233  -0.0218 -0.0221 1031 VAL B O   
3073 C CB  . VAL B 121 ? 0.2522 0.3679 0.5706 0.0239  -0.0210 -0.0381 1031 VAL B CB  
3074 C CG1 . VAL B 121 ? 0.2205 0.3392 0.5487 0.0230  -0.0195 -0.0468 1031 VAL B CG1 
3075 C CG2 . VAL B 121 ? 0.1986 0.3247 0.5248 0.0232  -0.0225 -0.0483 1031 VAL B CG2 
3076 N N   . VAL B 122 ? 0.2092 0.3008 0.5138 0.0247  -0.0184 -0.0158 1032 VAL B N   
3077 C CA  . VAL B 122 ? 0.2166 0.3031 0.5208 0.0239  -0.0162 -0.0120 1032 VAL B CA  
3078 C C   . VAL B 122 ? 0.2309 0.3039 0.5367 0.0228  -0.0175 -0.0092 1032 VAL B C   
3079 O O   . VAL B 122 ? 0.2260 0.2959 0.5357 0.0216  -0.0179 -0.0105 1032 VAL B O   
3080 C CB  . VAL B 122 ? 0.2015 0.2948 0.5009 0.0248  -0.0124 -0.0037 1032 VAL B CB  
3081 C CG1 . VAL B 122 ? 0.2025 0.2894 0.5055 0.0233  -0.0095 -0.0008 1032 VAL B CG1 
3082 C CG2 . VAL B 122 ? 0.2046 0.3190 0.5006 0.0255  -0.0115 -0.0059 1032 VAL B CG2 
3083 N N   . GLN B 123 ? 0.2209 0.2890 0.5240 0.0231  -0.0182 -0.0062 1033 GLN B N   
3084 C CA  . GLN B 123 ? 0.1951 0.2566 0.4987 0.0214  -0.0188 -0.0052 1033 GLN B CA  
3085 C C   . GLN B 123 ? 0.1991 0.2609 0.5074 0.0205  -0.0224 -0.0061 1033 GLN B C   
3086 O O   . GLN B 123 ? 0.1940 0.2565 0.5017 0.0189  -0.0235 -0.0044 1033 GLN B O   
3087 C CB  . GLN B 123 ? 0.1958 0.2549 0.4968 0.0217  -0.0181 -0.0030 1033 GLN B CB  
3088 C CG  . GLN B 123 ? 0.2460 0.3074 0.5465 0.0231  -0.0200 -0.0027 1033 GLN B CG  
3089 C CD  . GLN B 123 ? 0.1957 0.2558 0.4946 0.0239  -0.0184 -0.0002 1033 GLN B CD  
3090 O OE1 . GLN B 123 ? 0.1959 0.2542 0.4946 0.0225  -0.0184 -0.0007 1033 GLN B OE1 
3091 N NE2 . GLN B 123 ? 0.2035 0.2671 0.5023 0.0262  -0.0168 0.0030  1033 GLN B NE2 
3092 N N   . SER B 124 ? 0.2050 0.2688 0.5206 0.0215  -0.0241 -0.0085 1034 SER B N   
3093 C CA  . SER B 124 ? 0.2156 0.2792 0.5423 0.0213  -0.0270 -0.0064 1034 SER B CA  
3094 C C   . SER B 124 ? 0.2132 0.2787 0.5484 0.0214  -0.0278 -0.0072 1034 SER B C   
3095 O O   . SER B 124 ? 0.1943 0.2608 0.5424 0.0219  -0.0303 -0.0028 1034 SER B O   
3096 C CB  . SER B 124 ? 0.2492 0.3130 0.5872 0.0222  -0.0275 -0.0096 1034 SER B CB  
3097 O OG  . SER B 124 ? 0.2466 0.3093 0.5795 0.0219  -0.0275 -0.0073 1034 SER B OG  
3098 N N   . GLY B 125 ? 0.1919 0.2590 0.5227 0.0212  -0.0256 -0.0112 1035 GLY B N   
3099 C CA  . GLY B 125 ? 0.2119 0.2815 0.5500 0.0209  -0.0263 -0.0119 1035 GLY B CA  
3100 C C   . GLY B 125 ? 0.2236 0.2961 0.5753 0.0223  -0.0254 -0.0187 1035 GLY B C   
3101 O O   . GLY B 125 ? 0.2283 0.3024 0.5852 0.0230  -0.0244 -0.0246 1035 GLY B O   
3102 N N   . ILE B 126 ? 0.2202 0.2956 0.5793 0.0223  -0.0254 -0.0199 1036 ILE B N   
3103 C CA  . ILE B 126 ? 0.1968 0.2763 0.5724 0.0234  -0.0240 -0.0280 1036 ILE B CA  
3104 C C   . ILE B 126 ? 0.1985 0.2754 0.5958 0.0251  -0.0261 -0.0275 1036 ILE B C   
3105 O O   . ILE B 126 ? 0.2272 0.3014 0.6310 0.0258  -0.0296 -0.0164 1036 ILE B O   
3106 C CB  . ILE B 126 ? 0.2202 0.3032 0.6016 0.0233  -0.0241 -0.0278 1036 ILE B CB  
3107 C CG1 . ILE B 126 ? 0.1988 0.2845 0.5646 0.0212  -0.0206 -0.0290 1036 ILE B CG1 
3108 C CG2 . ILE B 126 ? 0.2137 0.3011 0.6184 0.0249  -0.0227 -0.0363 1036 ILE B CG2 
3109 C CD1 . ILE B 126 ? 0.2210 0.3107 0.5938 0.0204  -0.0205 -0.0295 1036 ILE B CD1 
3110 N N   . LYS B 127 ? 0.2016 0.2820 0.6131 0.0256  -0.0234 -0.0396 1037 LYS B N   
3111 C CA  . LYS B 127 ? 0.2066 0.2840 0.6481 0.0270  -0.0240 -0.0416 1037 LYS B CA  
3112 C C   . LYS B 127 ? 0.2309 0.3130 0.6999 0.0282  -0.0214 -0.0530 1037 LYS B C   
3113 O O   . LYS B 127 ? 0.2636 0.3413 0.7635 0.0302  -0.0223 -0.0489 1037 LYS B O   
3114 C CB  . LYS B 127 ? 0.2211 0.2990 0.6653 0.0260  -0.0226 -0.0497 1037 LYS B CB  
3115 C CG  . LYS B 127 ? 0.2805 0.3529 0.7060 0.0253  -0.0249 -0.0383 1037 LYS B CG  
3116 C CD  . LYS B 127 ? 0.2615 0.3273 0.6953 0.0263  -0.0283 -0.0209 1037 LYS B CD  
3117 C CE  . LYS B 127 ? 0.3170 0.3807 0.7291 0.0252  -0.0300 -0.0111 1037 LYS B CE  
3118 N NZ  . LYS B 127 ? 0.3443 0.4084 0.7631 0.0257  -0.0332 0.0062  1037 LYS B NZ  
3119 N N   . VAL B 128 ? 0.2570 0.3494 0.7182 0.0271  -0.0178 -0.0663 1038 VAL B N   
3120 C CA  . VAL B 128 ? 0.2356 0.3351 0.7236 0.0279  -0.0144 -0.0801 1038 VAL B CA  
3121 C C   . VAL B 128 ? 0.2460 0.3423 0.7412 0.0297  -0.0165 -0.0698 1038 VAL B C   
3122 O O   . VAL B 128 ? 0.1957 0.2899 0.6681 0.0291  -0.0192 -0.0574 1038 VAL B O   
3123 C CB  . VAL B 128 ? 0.2557 0.3730 0.7317 0.0256  -0.0093 -0.0980 1038 VAL B CB  
3124 C CG1 . VAL B 128 ? 0.2029 0.3296 0.6782 0.0238  -0.0074 -0.1114 1038 VAL B CG1 
3125 C CG2 . VAL B 128 ? 0.1993 0.3204 0.6418 0.0243  -0.0092 -0.0888 1038 VAL B CG2 
3126 N N   . ARG B 129 ? 0.2018 0.2995 0.7322 0.0318  -0.0149 -0.0765 1039 ARG B N   
3127 C CA  . ARG B 129 ? 0.2339 0.3320 0.7756 0.0339  -0.0167 -0.0683 1039 ARG B CA  
3128 C C   . ARG B 129 ? 0.1992 0.3091 0.7292 0.0321  -0.0123 -0.0815 1039 ARG B C   
3129 O O   . ARG B 129 ? 0.2464 0.3659 0.7921 0.0315  -0.0069 -0.1008 1039 ARG B O   
3130 C CB  . ARG B 129 ? 0.3111 0.3984 0.8829 0.0345  -0.0163 -0.0666 1039 ARG B CB  
3131 C CG  . ARG B 129 ? 0.3078 0.3831 0.8904 0.0348  -0.0192 -0.0520 1039 ARG B CG  
3132 C CD  . ARG B 129 ? 0.3154 0.3924 0.8764 0.0361  -0.0254 -0.0304 1039 ARG B CD  
3133 N NE  . ARG B 129 ? 0.3581 0.4277 0.9331 0.0368  -0.0283 -0.0109 1039 ARG B NE  
3134 C CZ  . ARG B 129 ? 0.3788 0.4491 0.9674 0.0383  -0.0313 0.0067  1039 ARG B CZ  
3135 N NH1 . ARG B 129 ? 0.3082 0.3852 0.8967 0.0395  -0.0325 0.0066  1039 ARG B NH1 
3136 N NH2 . ARG B 129 ? 0.3592 0.4255 0.9629 0.0385  -0.0330 0.0257  1039 ARG B NH2 
3137 N N   . LEU B 130 ? 0.2304 0.3415 0.7334 0.0306  -0.0140 -0.0722 1040 LEU B N   
3138 C CA  . LEU B 130 ? 0.2323 0.3545 0.7246 0.0286  -0.0096 -0.0806 1040 LEU B CA  
3139 C C   . LEU B 130 ? 0.2357 0.3593 0.7447 0.0303  -0.0113 -0.0758 1040 LEU B C   
3140 O O   . LEU B 130 ? 0.2331 0.3508 0.7579 0.0330  -0.0167 -0.0636 1040 LEU B O   
3141 C CB  . LEU B 130 ? 0.1962 0.3189 0.6523 0.0254  -0.0090 -0.0738 1040 LEU B CB  
3142 C CG  . LEU B 130 ? 0.2358 0.3610 0.6725 0.0238  -0.0071 -0.0768 1040 LEU B CG  
3143 C CD1 . LEU B 130 ? 0.1973 0.3222 0.6056 0.0215  -0.0061 -0.0669 1040 LEU B CD1 
3144 C CD2 . LEU B 130 ? 0.2009 0.3431 0.6455 0.0230  -0.0014 -0.0953 1040 LEU B CD2 
3145 N N   . GLN B 131 ? 0.2719 0.4064 0.7780 0.0286  -0.0067 -0.0843 1041 GLN B N   
3146 C CA  . GLN B 131 ? 0.1964 0.3346 0.7181 0.0298  -0.0078 -0.0815 1041 GLN B CA  
3147 C C   . GLN B 131 ? 0.2050 0.3525 0.7083 0.0261  -0.0033 -0.0845 1041 GLN B C   
3148 O O   . GLN B 131 ? 0.2030 0.3616 0.6989 0.0240  0.0034  -0.0958 1041 GLN B O   
3149 C CB  . GLN B 131 ? 0.2021 0.3416 0.7559 0.0322  -0.0054 -0.0923 1041 GLN B CB  
3150 C CG  . GLN B 131 ? 0.2108 0.3536 0.7749 0.0328  -0.0059 -0.0899 1041 GLN B CG  
3151 C CD  . GLN B 131 ? 0.2162 0.3562 0.8062 0.0340  -0.0027 -0.1008 1041 GLN B CD  
3152 O OE1 . GLN B 131 ? 0.2294 0.3793 0.8234 0.0321  0.0045  -0.1197 1041 GLN B OE1 
3153 N NE2 . GLN B 131 ? 0.2229 0.3516 0.8320 0.0367  -0.0076 -0.0887 1041 GLN B NE2 
3154 N N   . LEU B 132 ? 0.1950 0.3410 0.6927 0.0251  -0.0068 -0.0742 1042 LEU B N   
3155 C CA  . LEU B 132 ? 0.2458 0.4001 0.7346 0.0216  -0.0023 -0.0763 1042 LEU B CA  
3156 C C   . LEU B 132 ? 0.2480 0.4127 0.7634 0.0233  0.0000  -0.0848 1042 LEU B C   
3157 O O   . LEU B 132 ? 0.2648 0.4283 0.8016 0.0266  -0.0055 -0.0802 1042 LEU B O   
3158 C CB  . LEU B 132 ? 0.2433 0.3929 0.7191 0.0192  -0.0067 -0.0648 1042 LEU B CB  
3159 C CG  . LEU B 132 ? 0.1949 0.3509 0.6681 0.0152  -0.0035 -0.0649 1042 LEU B CG  
3160 C CD1 . LEU B 132 ? 0.1979 0.3574 0.6567 0.0117  0.0052  -0.0672 1042 LEU B CD1 
3161 C CD2 . LEU B 132 ? 0.1939 0.3462 0.6594 0.0129  -0.0091 -0.0569 1042 LEU B CD2 
3162 N N   . TYR B 133 ? 0.1988 0.3764 0.7144 0.0212  0.0082  -0.0964 1043 TYR B N   
3163 C CA  . TYR B 133 ? 0.2057 0.3949 0.7488 0.0227  0.0116  -0.1075 1043 TYR B CA  
3164 C C   . TYR B 133 ? 0.2021 0.4055 0.7370 0.0185  0.0190  -0.1113 1043 TYR B C   
3165 O O   . TYR B 133 ? 0.2042 0.4109 0.7148 0.0146  0.0232  -0.1070 1043 TYR B O   
3166 C CB  . TYR B 133 ? 0.2379 0.4303 0.7948 0.0246  0.0155  -0.1233 1043 TYR B CB  
3167 C CG  . TYR B 133 ? 0.2071 0.4208 0.7550 0.0214  0.0246  -0.1377 1043 TYR B CG  
3168 C CD1 . TYR B 133 ? 0.2080 0.4216 0.7257 0.0188  0.0253  -0.1320 1043 TYR B CD1 
3169 C CD2 . TYR B 133 ? 0.2154 0.4448 0.7723 0.0201  0.0319  -0.1543 1043 TYR B CD2 
3170 C CE1 . TYR B 133 ? 0.2132 0.4490 0.7171 0.0157  0.0329  -0.1419 1043 TYR B CE1 
3171 C CE2 . TYR B 133 ? 0.2182 0.4736 0.7651 0.0168  0.0403  -0.1671 1043 TYR B CE2 
3172 C CZ  . TYR B 133 ? 0.2175 0.4771 0.7370 0.0146  0.0405  -0.1599 1043 TYR B CZ  
3173 O OH  . TYR B 133 ? 0.2239 0.5125 0.7288 0.0111  0.0482  -0.1697 1043 TYR B OH  
3174 N N   . ARG B 134 ? 0.2082 0.4197 0.7643 0.0193  0.0209  -0.1177 1044 ARG B N   
3175 C CA  . ARG B 134 ? 0.2049 0.4329 0.7597 0.0153  0.0287  -0.1218 1044 ARG B CA  
3176 C C   . ARG B 134 ? 0.2104 0.4581 0.7644 0.0139  0.0382  -0.1374 1044 ARG B C   
3177 O O   . ARG B 134 ? 0.2176 0.4646 0.7825 0.0163  0.0388  -0.1505 1044 ARG B O   
3178 C CB  . ARG B 134 ? 0.2255 0.4519 0.7953 0.0161  0.0264  -0.1215 1044 ARG B CB  
3179 C CG  . ARG B 134 ? 0.2094 0.4509 0.7787 0.0114  0.0336  -0.1225 1044 ARG B CG  
3180 C CD  . ARG B 134 ? 0.2049 0.4416 0.7604 0.0071  0.0324  -0.1093 1044 ARG B CD  
3181 N NE  . ARG B 134 ? 0.2214 0.4686 0.7815 0.0023  0.0384  -0.1084 1044 ARG B NE  
3182 C CZ  . ARG B 134 ? 0.2158 0.4584 0.7632 -0.0027 0.0405  -0.0985 1044 ARG B CZ  
3183 N NH1 . ARG B 134 ? 0.2182 0.4467 0.7467 -0.0036 0.0374  -0.0894 1044 ARG B NH1 
3184 N NH2 . ARG B 134 ? 0.2110 0.4635 0.7682 -0.0072 0.0466  -0.0983 1044 ARG B NH2 
3185 N N   . THR B 135 ? 0.2141 0.4750 0.7465 0.0092  0.0453  -0.1339 1045 THR B N   
3186 C CA  . THR B 135 ? 0.2206 0.5083 0.7483 0.0071  0.0546  -0.1472 1045 THR B CA  
3187 C C   . THR B 135 ? 0.2242 0.5338 0.7641 0.0044  0.0630  -0.1545 1045 THR B C   
3188 O O   . THR B 135 ? 0.2220 0.5252 0.7682 0.0032  0.0623  -0.1458 1045 THR B O   
3189 C CB  . THR B 135 ? 0.2658 0.5609 0.7619 0.0037  0.0577  -0.1358 1045 THR B CB  
3190 O OG1 . THR B 135 ? 0.2437 0.5389 0.7298 -0.0001 0.0611  -0.1193 1045 THR B OG1 
3191 C CG2 . THR B 135 ? 0.2211 0.4937 0.7040 0.0060  0.0495  -0.1270 1045 THR B CG2 
3192 N N   . ALA B 136 ? 0.2309 0.5693 0.7724 0.0029  0.0713  -0.1713 1046 ALA B N   
3193 C CA  . ALA B 136 ? 0.2434 0.6016 0.7911 0.0003  0.0792  -0.1799 1046 ALA B CA  
3194 C C   . ALA B 136 ? 0.2761 0.6504 0.8141 -0.0047 0.0862  -0.1638 1046 ALA B C   
3195 O O   . ALA B 136 ? 0.2930 0.6675 0.8425 -0.0062 0.0887  -0.1612 1046 ALA B O   
3196 C CB  . ALA B 136 ? 0.2521 0.6373 0.7972 -0.0009 0.0858  -0.2020 1046 ALA B CB  
3197 N N   . LYS B 137 ? 0.2590 0.6405 0.7690 -0.0074 0.0884  -0.1494 1047 LYS B N   
3198 C CA  . LYS B 137 ? 0.3035 0.6981 0.8015 -0.0124 0.0958  -0.1308 1047 LYS B CA  
3199 C C   . LYS B 137 ? 0.3111 0.6857 0.7895 -0.0132 0.0920  -0.1060 1047 LYS B C   
3200 O O   . LYS B 137 ? 0.3659 0.7545 0.8340 -0.0171 0.0990  -0.0880 1047 LYS B O   
3201 C CB  . LYS B 137 ? 0.2896 0.7307 0.7774 -0.0161 0.1072  -0.1362 1047 LYS B CB  
3202 C CG  . LYS B 137 ? 0.2623 0.7308 0.7691 -0.0158 0.1127  -0.1652 1047 LYS B CG  
3203 C CD  . LYS B 137 ? 0.2998 0.8205 0.7929 -0.0205 0.1246  -0.1686 1047 LYS B CD  
3204 C CE  . LYS B 137 ? 0.3111 0.8495 0.8104 -0.0202 0.1275  -0.1975 1047 LYS B CE  
3205 N NZ  . LYS B 137 ? 0.3043 0.8940 0.7857 -0.0252 0.1381  -0.2002 1047 LYS B NZ  
3206 N N   . MET B 138 ? 0.2520 0.5953 0.7277 -0.0098 0.0818  -0.1036 1048 MET B N   
3207 C CA  . MET B 138 ? 0.3090 0.6348 0.7676 -0.0103 0.0785  -0.0833 1048 MET B CA  
3208 C C   . MET B 138 ? 0.3093 0.5994 0.7751 -0.0089 0.0696  -0.0776 1048 MET B C   
3209 O O   . MET B 138 ? 0.2841 0.5572 0.7383 -0.0088 0.0660  -0.0647 1048 MET B O   
3210 C CB  . MET B 138 ? 0.2647 0.5961 0.7054 -0.0080 0.0757  -0.0857 1048 MET B CB  
3211 C CG  . MET B 138 ? 0.2690 0.6413 0.6964 -0.0101 0.0841  -0.0871 1048 MET B CG  
3212 S SD  . MET B 138 ? 0.3979 0.7763 0.8048 -0.0078 0.0793  -0.0884 1048 MET B SD  
3213 C CE  . MET B 138 ? 0.2934 0.6623 0.7178 -0.0041 0.0732  -0.1196 1048 MET B CE  
3214 N N   . GLY B 139 ? 0.2282 0.5095 0.7133 -0.0078 0.0658  -0.0873 1049 GLY B N   
3215 C CA  . GLY B 139 ? 0.2214 0.4758 0.7121 -0.0063 0.0563  -0.0837 1049 GLY B CA  
3216 C C   . GLY B 139 ? 0.2475 0.4880 0.7343 -0.0014 0.0472  -0.0889 1049 GLY B C   
3217 O O   . GLY B 139 ? 0.2162 0.4655 0.7094 0.0017  0.0471  -0.1017 1049 GLY B O   
3218 N N   . TRP B 140 ? 0.2130 0.4329 0.6922 -0.0009 0.0401  -0.0800 1050 TRP B N   
3219 C CA  . TRP B 140 ? 0.2089 0.4167 0.6848 0.0035  0.0320  -0.0825 1050 TRP B CA  
3220 C C   . TRP B 140 ? 0.2119 0.4239 0.6700 0.0041  0.0346  -0.0817 1050 TRP B C   
3221 O O   . TRP B 140 ? 0.2178 0.4396 0.6629 0.0012  0.0411  -0.0744 1050 TRP B O   
3222 C CB  . TRP B 140 ? 0.2051 0.3943 0.6778 0.0034  0.0238  -0.0741 1050 TRP B CB  
3223 C CG  . TRP B 140 ? 0.2303 0.4203 0.7192 0.0023  0.0205  -0.0751 1050 TRP B CG  
3224 C CD1 . TRP B 140 ? 0.2190 0.4097 0.7109 -0.0025 0.0233  -0.0717 1050 TRP B CD1 
3225 C CD2 . TRP B 140 ? 0.1995 0.3918 0.7069 0.0060  0.0138  -0.0797 1050 TRP B CD2 
3226 N NE1 . TRP B 140 ? 0.2020 0.3972 0.7109 -0.0024 0.0183  -0.0756 1050 TRP B NE1 
3227 C CE2 . TRP B 140 ? 0.1990 0.3958 0.7170 0.0031  0.0121  -0.0790 1050 TRP B CE2 
3228 C CE3 . TRP B 140 ? 0.1976 0.3895 0.7173 0.0115  0.0094  -0.0837 1050 TRP B CE3 
3229 C CZ2 . TRP B 140 ? 0.2148 0.4183 0.7525 0.0060  0.0054  -0.0808 1050 TRP B CZ2 
3230 C CZ3 . TRP B 140 ? 0.1955 0.3915 0.7376 0.0147  0.0032  -0.0837 1050 TRP B CZ3 
3231 C CH2 . TRP B 140 ? 0.1949 0.3979 0.7444 0.0121  0.0009  -0.0816 1050 TRP B CH2 
3232 N N   . GLY B 141 ? 0.2093 0.4157 0.6694 0.0079  0.0294  -0.0883 1051 GLY B N   
3233 C CA  . GLY B 141 ? 0.2185 0.4289 0.6630 0.0084  0.0305  -0.0890 1051 GLY B CA  
3234 C C   . GLY B 141 ? 0.2157 0.4102 0.6641 0.0121  0.0226  -0.0910 1051 GLY B C   
3235 O O   . GLY B 141 ? 0.2376 0.4202 0.7007 0.0144  0.0165  -0.0900 1051 GLY B O   
3236 N N   . VAL B 142 ? 0.2243 0.4216 0.6605 0.0126  0.0227  -0.0926 1052 VAL B N   
3237 C CA  . VAL B 142 ? 0.2060 0.3896 0.6461 0.0156  0.0164  -0.0942 1052 VAL B CA  
3238 C C   . VAL B 142 ? 0.2089 0.4080 0.6590 0.0164  0.0197  -0.1119 1052 VAL B C   
3239 O O   . VAL B 142 ? 0.2138 0.4342 0.6516 0.0141  0.0254  -0.1177 1052 VAL B O   
3240 C CB  . VAL B 142 ? 0.2051 0.3766 0.6234 0.0151  0.0132  -0.0810 1052 VAL B CB  
3241 C CG1 . VAL B 142 ? 0.2018 0.3588 0.6261 0.0180  0.0066  -0.0809 1052 VAL B CG1 
3242 C CG2 . VAL B 142 ? 0.2041 0.3656 0.6143 0.0130  0.0124  -0.0675 1052 VAL B CG2 
3243 N N   . ARG B 143 ? 0.2070 0.3979 0.6815 0.0195  0.0164  -0.1204 1053 ARG B N   
3244 C CA  . ARG B 143 ? 0.2102 0.4145 0.7009 0.0199  0.0197  -0.1404 1053 ARG B CA  
3245 C C   . ARG B 143 ? 0.2079 0.3942 0.7130 0.0227  0.0141  -0.1389 1053 ARG B C   
3246 O O   . ARG B 143 ? 0.2041 0.3703 0.7117 0.0249  0.0078  -0.1230 1053 ARG B O   
3247 C CB  . ARG B 143 ? 0.2720 0.4900 0.7928 0.0205  0.0248  -0.1586 1053 ARG B CB  
3248 C CG  . ARG B 143 ? 0.2394 0.4366 0.7892 0.0243  0.0200  -0.1549 1053 ARG B CG  
3249 C CD  . ARG B 143 ? 0.2248 0.4283 0.7927 0.0238  0.0249  -0.1699 1053 ARG B CD  
3250 N NE  . ARG B 143 ? 0.2232 0.4099 0.8053 0.0264  0.0203  -0.1578 1053 ARG B NE  
3251 C CZ  . ARG B 143 ? 0.2452 0.4346 0.8448 0.0264  0.0233  -0.1668 1053 ARG B CZ  
3252 N NH1 . ARG B 143 ? 0.2396 0.4467 0.8447 0.0238  0.0311  -0.1891 1053 ARG B NH1 
3253 N NH2 . ARG B 143 ? 0.3197 0.4962 0.9315 0.0290  0.0183  -0.1534 1053 ARG B NH2 
3254 N N   . ALA B 144 ? 0.2111 0.4079 0.7270 0.0221  0.0168  -0.1563 1054 ALA B N   
3255 C CA  . ALA B 144 ? 0.2116 0.3933 0.7430 0.0240  0.0127  -0.1559 1054 ALA B CA  
3256 C C   . ALA B 144 ? 0.2213 0.3879 0.7861 0.0257  0.0124  -0.1619 1054 ALA B C   
3257 O O   . ALA B 144 ? 0.2563 0.4316 0.8354 0.0243  0.0174  -0.1792 1054 ALA B O   
3258 C CB  . ALA B 144 ? 0.2794 0.4774 0.8027 0.0214  0.0155  -0.1712 1054 ALA B CB  
3259 N N   . LEU B 145 ? 0.2175 0.3607 0.7917 0.0280  0.0065  -0.1456 1055 LEU B N   
3260 C CA  . LEU B 145 ? 0.2878 0.4134 0.8928 0.0288  0.0055  -0.1449 1055 LEU B CA  
3261 C C   . LEU B 145 ? 0.2814 0.4004 0.9051 0.0267  0.0070  -0.1566 1055 LEU B C   
3262 O O   . LEU B 145 ? 0.2922 0.3961 0.9467 0.0263  0.0069  -0.1554 1055 LEU B O   
3263 C CB  . LEU B 145 ? 0.2437 0.3526 0.8501 0.0318  -0.0016 -0.1171 1055 LEU B CB  
3264 C CG  . LEU B 145 ? 0.2431 0.3560 0.8415 0.0334  -0.0039 -0.1060 1055 LEU B CG  
3265 C CD1 . LEU B 145 ? 0.2273 0.3286 0.8304 0.0360  -0.0112 -0.0804 1055 LEU B CD1 
3266 C CD2 . LEU B 145 ? 0.2347 0.3539 0.8511 0.0328  0.0011  -0.1213 1055 LEU B CD2 
3267 N N   . GLN B 146 ? 0.2353 0.3663 0.8435 0.0250  0.0086  -0.1672 1056 GLN B N   
3268 C CA  . GLN B 146 ? 0.3062 0.4351 0.9317 0.0222  0.0106  -0.1826 1056 GLN B CA  
3269 C C   . GLN B 146 ? 0.2779 0.4360 0.8883 0.0191  0.0155  -0.2077 1056 GLN B C   
3270 O O   . GLN B 146 ? 0.2693 0.4485 0.8545 0.0192  0.0170  -0.2079 1056 GLN B O   
3271 C CB  . GLN B 146 ? 0.2676 0.3813 0.8887 0.0235  0.0055  -0.1639 1056 GLN B CB  
3272 C CG  . GLN B 146 ? 0.2731 0.3989 0.8587 0.0247  0.0029  -0.1550 1056 GLN B CG  
3273 C CD  . GLN B 146 ? 0.2956 0.4060 0.8746 0.0263  -0.0025 -0.1337 1056 GLN B CD  
3274 O OE1 . GLN B 146 ? 0.3066 0.4032 0.8845 0.0287  -0.0069 -0.1113 1056 GLN B OE1 
3275 N NE2 . GLN B 146 ? 0.2889 0.4050 0.8627 0.0247  -0.0023 -0.1409 1056 GLN B NE2 
3276 N N   . THR B 147 ? 0.2702 0.4322 0.8973 0.0156  0.0181  -0.2286 1057 THR B N   
3277 C CA  . THR B 147 ? 0.3173 0.5109 0.9256 0.0125  0.0212  -0.2490 1057 THR B CA  
3278 C C   . THR B 147 ? 0.2368 0.4327 0.8186 0.0142  0.0165  -0.2310 1057 THR B C   
3279 O O   . THR B 147 ? 0.2329 0.4045 0.8208 0.0162  0.0121  -0.2134 1057 THR B O   
3280 C CB  . THR B 147 ? 0.3028 0.5016 0.9380 0.0075  0.0250  -0.2792 1057 THR B CB  
3281 O OG1 . THR B 147 ? 0.3596 0.5278 1.0216 0.0076  0.0222  -0.2696 1057 THR B OG1 
3282 C CG2 . THR B 147 ? 0.3006 0.5061 0.9592 0.0043  0.0304  -0.3026 1057 THR B CG2 
3283 N N   . ILE B 148 ? 0.2748 0.5016 0.8279 0.0132  0.0176  -0.2334 1058 ILE B N   
3284 C CA  . ILE B 148 ? 0.2224 0.4507 0.7453 0.0139  0.0130  -0.2148 1058 ILE B CA  
3285 C C   . ILE B 148 ? 0.2530 0.5154 0.7621 0.0100  0.0149  -0.2330 1058 ILE B C   
3286 O O   . ILE B 148 ? 0.2760 0.5716 0.7687 0.0077  0.0186  -0.2432 1058 ILE B O   
3287 C CB  . ILE B 148 ? 0.2549 0.4787 0.7410 0.0152  0.0112  -0.1904 1058 ILE B CB  
3288 C CG1 . ILE B 148 ? 0.2270 0.4234 0.7257 0.0185  0.0090  -0.1744 1058 ILE B CG1 
3289 C CG2 . ILE B 148 ? 0.2171 0.4360 0.6680 0.0153  0.0067  -0.1703 1058 ILE B CG2 
3290 C CD1 . ILE B 148 ? 0.2126 0.4070 0.6814 0.0188  0.0083  -0.1555 1058 ILE B CD1 
3291 N N   . PRO B 149 ? 0.2429 0.5019 0.7579 0.0091  0.0124  -0.2368 1059 PRO B N   
3292 C CA  . PRO B 149 ? 0.2327 0.5280 0.7326 0.0054  0.0131  -0.2529 1059 PRO B CA  
3293 C C   . PRO B 149 ? 0.2325 0.5419 0.6849 0.0060  0.0107  -0.2308 1059 PRO B C   
3294 O O   . PRO B 149 ? 0.2272 0.5101 0.6599 0.0091  0.0072  -0.2022 1059 PRO B O   
3295 C CB  . PRO B 149 ? 0.2706 0.5506 0.7864 0.0050  0.0099  -0.2544 1059 PRO B CB  
3296 C CG  . PRO B 149 ? 0.2454 0.4827 0.7900 0.0079  0.0090  -0.2432 1059 PRO B CG  
3297 C CD  . PRO B 149 ? 0.2232 0.4477 0.7550 0.0113  0.0082  -0.2229 1059 PRO B CD  
3298 N N   . GLN B 150 ? 0.2394 0.5936 0.6760 0.0028  0.0130  -0.2445 1060 GLN B N   
3299 C CA  . GLN B 150 ? 0.2556 0.6275 0.6518 0.0036  0.0110  -0.2215 1060 GLN B CA  
3300 C C   . GLN B 150 ? 0.2576 0.6017 0.6384 0.0065  0.0049  -0.1962 1060 GLN B C   
3301 O O   . GLN B 150 ? 0.2330 0.5619 0.6292 0.0063  0.0021  -0.2028 1060 GLN B O   
3302 C CB  . GLN B 150 ? 0.2504 0.6797 0.6347 -0.0002 0.0131  -0.2394 1060 GLN B CB  
3303 C CG  . GLN B 150 ? 0.2751 0.7270 0.6216 0.0011  0.0116  -0.2120 1060 GLN B CG  
3304 C CD  . GLN B 150 ? 0.3297 0.8431 0.6630 -0.0024 0.0124  -0.2259 1060 GLN B CD  
3305 O OE1 . GLN B 150 ? 0.3208 0.8733 0.6653 -0.0066 0.0172  -0.2556 1060 GLN B OE1 
3306 N NE2 . GLN B 150 ? 0.3881 0.9139 0.6993 -0.0008 0.0078  -0.2054 1060 GLN B NE2 
3307 N N   . GLY B 151 ? 0.2345 0.5725 0.5876 0.0089  0.0035  -0.1676 1061 GLY B N   
3308 C CA  . GLY B 151 ? 0.2453 0.5645 0.5824 0.0115  -0.0012 -0.1443 1061 GLY B CA  
3309 C C   . GLY B 151 ? 0.2755 0.5469 0.6221 0.0139  -0.0041 -0.1321 1061 GLY B C   
3310 O O   . GLY B 151 ? 0.3135 0.5689 0.6505 0.0157  -0.0078 -0.1166 1061 GLY B O   
3311 N N   . THR B 152 ? 0.2200 0.4717 0.5863 0.0140  -0.0026 -0.1388 1062 THR B N   
3312 C CA  . THR B 152 ? 0.2405 0.4529 0.6158 0.0162  -0.0053 -0.1257 1062 THR B CA  
3313 C C   . THR B 152 ? 0.2615 0.4596 0.6171 0.0180  -0.0057 -0.1025 1062 THR B C   
3314 O O   . THR B 152 ? 0.2546 0.4669 0.6008 0.0175  -0.0024 -0.0997 1062 THR B O   
3315 C CB  . THR B 152 ? 0.2429 0.4451 0.6492 0.0161  -0.0034 -0.1397 1062 THR B CB  
3316 O OG1 . THR B 152 ? 0.2429 0.4593 0.6743 0.0140  -0.0017 -0.1644 1062 THR B OG1 
3317 C CG2 . THR B 152 ? 0.2751 0.4430 0.6923 0.0184  -0.0067 -0.1247 1062 THR B CG2 
3318 N N   . PHE B 153 ? 0.2490 0.4203 0.6011 0.0196  -0.0091 -0.0871 1063 PHE B N   
3319 C CA  . PHE B 153 ? 0.2506 0.4074 0.5902 0.0206  -0.0091 -0.0692 1063 PHE B CA  
3320 C C   . PHE B 153 ? 0.2437 0.3903 0.5963 0.0206  -0.0082 -0.0713 1063 PHE B C   
3321 O O   . PHE B 153 ? 0.2418 0.3785 0.6142 0.0211  -0.0099 -0.0779 1063 PHE B O   
3322 C CB  . PHE B 153 ? 0.2018 0.3375 0.5355 0.0217  -0.0126 -0.0560 1063 PHE B CB  
3323 C CG  . PHE B 153 ? 0.2001 0.3204 0.5272 0.0220  -0.0125 -0.0425 1063 PHE B CG  
3324 C CD1 . PHE B 153 ? 0.2028 0.3289 0.5184 0.0219  -0.0095 -0.0330 1063 PHE B CD1 
3325 C CD2 . PHE B 153 ? 0.1969 0.2997 0.5315 0.0222  -0.0152 -0.0389 1063 PHE B CD2 
3326 C CE1 . PHE B 153 ? 0.2019 0.3143 0.5161 0.0215  -0.0087 -0.0237 1063 PHE B CE1 
3327 C CE2 . PHE B 153 ? 0.1984 0.2917 0.5279 0.0217  -0.0152 -0.0300 1063 PHE B CE2 
3328 C CZ  . PHE B 153 ? 0.1984 0.2954 0.5188 0.0211  -0.0117 -0.0240 1063 PHE B CZ  
3329 N N   . ILE B 154 ? 0.2161 0.3659 0.5602 0.0202  -0.0056 -0.0642 1064 ILE B N   
3330 C CA  . ILE B 154 ? 0.2031 0.3470 0.5596 0.0201  -0.0047 -0.0667 1064 ILE B CA  
3331 C C   . ILE B 154 ? 0.1999 0.3234 0.5529 0.0204  -0.0074 -0.0529 1064 ILE B C   
3332 O O   . ILE B 154 ? 0.1970 0.3079 0.5614 0.0213  -0.0111 -0.0517 1064 ILE B O   
3333 C CB  . ILE B 154 ? 0.2071 0.3710 0.5601 0.0186  0.0007  -0.0705 1064 ILE B CB  
3334 C CG1 . ILE B 154 ? 0.2202 0.4119 0.5749 0.0176  0.0036  -0.0864 1064 ILE B CG1 
3335 C CG2 . ILE B 154 ? 0.2376 0.3959 0.6060 0.0186  0.0015  -0.0744 1064 ILE B CG2 
3336 C CD1 . ILE B 154 ? 0.2108 0.4025 0.5902 0.0178  0.0029  -0.1061 1064 ILE B CD1 
3337 N N   . CYS B 155 ? 0.2013 0.3243 0.5408 0.0195  -0.0053 -0.0423 1065 CYS B N   
3338 C CA  . CYS B 155 ? 0.2067 0.3148 0.5445 0.0189  -0.0067 -0.0329 1065 CYS B CA  
3339 C C   . CYS B 155 ? 0.2027 0.3122 0.5299 0.0181  -0.0031 -0.0229 1065 CYS B C   
3340 O O   . CYS B 155 ? 0.2141 0.3378 0.5352 0.0185  0.0000  -0.0207 1065 CYS B O   
3341 C CB  . CYS B 155 ? 0.2487 0.3565 0.5968 0.0180  -0.0062 -0.0355 1065 CYS B CB  
3342 S SG  . CYS B 155 ? 0.2202 0.3464 0.5682 0.0166  0.0007  -0.0386 1065 CYS B SG  
3343 N N   . GLU B 156 ? 0.2022 0.2997 0.5301 0.0169  -0.0032 -0.0168 1066 GLU B N   
3344 C CA  . GLU B 156 ? 0.2165 0.3120 0.5423 0.0163  0.0009  -0.0070 1066 GLU B CA  
3345 C C   . GLU B 156 ? 0.2085 0.3048 0.5430 0.0138  0.0056  -0.0045 1066 GLU B C   
3346 O O   . GLU B 156 ? 0.2062 0.2987 0.5471 0.0122  0.0039  -0.0107 1066 GLU B O   
3347 C CB  . GLU B 156 ? 0.2046 0.2868 0.5298 0.0161  -0.0013 -0.0051 1066 GLU B CB  
3348 C CG  . GLU B 156 ? 0.2089 0.2861 0.5396 0.0154  0.0036  0.0033  1066 GLU B CG  
3349 C CD  . GLU B 156 ? 0.2378 0.3042 0.5702 0.0149  0.0019  0.0007  1066 GLU B CD  
3350 O OE1 . GLU B 156 ? 0.2186 0.2834 0.5448 0.0150  -0.0034 -0.0051 1066 GLU B OE1 
3351 O OE2 . GLU B 156 ? 0.2118 0.2727 0.5542 0.0142  0.0063  0.0048  1066 GLU B OE2 
3352 N N   . TYR B 157 ? 0.2208 0.3239 0.5574 0.0136  0.0115  0.0058  1067 TYR B N   
3353 C CA  . TYR B 157 ? 0.2311 0.3334 0.5802 0.0108  0.0171  0.0100  1067 TYR B CA  
3354 C C   . TYR B 157 ? 0.2371 0.3234 0.5974 0.0088  0.0175  0.0088  1067 TYR B C   
3355 O O   . TYR B 157 ? 0.2216 0.3026 0.5891 0.0092  0.0211  0.0172  1067 TYR B O   
3356 C CB  . TYR B 157 ? 0.2250 0.3409 0.5769 0.0112  0.0240  0.0249  1067 TYR B CB  
3357 C CG  . TYR B 157 ? 0.2547 0.3737 0.6205 0.0081  0.0303  0.0285  1067 TYR B CG  
3358 C CD1 . TYR B 157 ? 0.2539 0.3597 0.6388 0.0055  0.0346  0.0325  1067 TYR B CD1 
3359 C CD2 . TYR B 157 ? 0.2299 0.3660 0.5926 0.0073  0.0324  0.0259  1067 TYR B CD2 
3360 C CE1 . TYR B 157 ? 0.2521 0.3604 0.6528 0.0021  0.0406  0.0350  1067 TYR B CE1 
3361 C CE2 . TYR B 157 ? 0.2335 0.3730 0.6102 0.0041  0.0385  0.0292  1067 TYR B CE2 
3362 C CZ  . TYR B 157 ? 0.2819 0.4069 0.6775 0.0015  0.0424  0.0343  1067 TYR B CZ  
3363 O OH  . TYR B 157 ? 0.2525 0.3805 0.6653 -0.0021 0.0489  0.0376  1067 TYR B OH  
3364 N N   . VAL B 158 ? 0.2140 0.2954 0.5784 0.0064  0.0142  -0.0023 1068 VAL B N   
3365 C CA  . VAL B 158 ? 0.2141 0.2863 0.5874 0.0038  0.0136  -0.0086 1068 VAL B CA  
3366 C C   . VAL B 158 ? 0.2362 0.3083 0.6284 -0.0005 0.0188  -0.0115 1068 VAL B C   
3367 O O   . VAL B 158 ? 0.2171 0.2960 0.6116 -0.0016 0.0195  -0.0127 1068 VAL B O   
3368 C CB  . VAL B 158 ? 0.2088 0.2819 0.5733 0.0039  0.0056  -0.0182 1068 VAL B CB  
3369 C CG1 . VAL B 158 ? 0.2099 0.2820 0.5832 0.0001  0.0049  -0.0274 1068 VAL B CG1 
3370 C CG2 . VAL B 158 ? 0.2099 0.2812 0.5605 0.0075  0.0014  -0.0153 1068 VAL B CG2 
3371 N N   . GLY B 159 ? 0.2215 0.2864 0.6298 -0.0033 0.0229  -0.0142 1069 GLY B N   
3372 C CA  . GLY B 159 ? 0.2253 0.2900 0.6562 -0.0083 0.0279  -0.0206 1069 GLY B CA  
3373 C C   . GLY B 159 ? 0.2627 0.3192 0.7163 -0.0112 0.0334  -0.0259 1069 GLY B C   
3374 O O   . GLY B 159 ? 0.2462 0.2994 0.6952 -0.0104 0.0309  -0.0312 1069 GLY B O   
3375 N N   . GLU B 160 ? 0.2701 0.3239 0.7517 -0.0150 0.0416  -0.0252 1070 GLU B N   
3376 C CA  . GLU B 160 ? 0.2430 0.2895 0.7560 -0.0190 0.0483  -0.0342 1070 GLU B CA  
3377 C C   . GLU B 160 ? 0.2495 0.2858 0.7793 -0.0156 0.0561  -0.0152 1070 GLU B C   
3378 O O   . GLU B 160 ? 0.2535 0.2908 0.7907 -0.0141 0.0614  0.0038  1070 GLU B O   
3379 C CB  . GLU B 160 ? 0.2469 0.2966 0.7869 -0.0254 0.0535  -0.0448 1070 GLU B CB  
3380 C CG  . GLU B 160 ? 0.2551 0.2976 0.8368 -0.0305 0.0625  -0.0562 1070 GLU B CG  
3381 C CD  . GLU B 160 ? 0.2598 0.3053 0.8726 -0.0372 0.0688  -0.0650 1070 GLU B CD  
3382 O OE1 . GLU B 160 ? 0.2562 0.3098 0.8558 -0.0374 0.0659  -0.0610 1070 GLU B OE1 
3383 O OE2 . GLU B 160 ? 0.2674 0.3077 0.9207 -0.0423 0.0772  -0.0768 1070 GLU B OE2 
3384 N N   . LEU B 161 ? 0.2511 0.2806 0.7874 -0.0143 0.0567  -0.0191 1071 LEU B N   
3385 C CA  . LEU B 161 ? 0.2576 0.2786 0.8129 -0.0104 0.0635  0.0000  1071 LEU B CA  
3386 C C   . LEU B 161 ? 0.2675 0.2804 0.8723 -0.0145 0.0753  0.0005  1071 LEU B C   
3387 O O   . LEU B 161 ? 0.2702 0.2793 0.9001 -0.0196 0.0784  -0.0218 1071 LEU B O   
3388 C CB  . LEU B 161 ? 0.2996 0.3166 0.8471 -0.0075 0.0603  -0.0053 1071 LEU B CB  
3389 C CG  . LEU B 161 ? 0.2468 0.2710 0.7503 -0.0036 0.0496  -0.0046 1071 LEU B CG  
3390 C CD1 . LEU B 161 ? 0.3038 0.3255 0.8026 -0.0029 0.0467  -0.0161 1071 LEU B CD1 
3391 C CD2 . LEU B 161 ? 0.2469 0.2752 0.7349 0.0022  0.0487  0.0197  1071 LEU B CD2 
3392 N N   . ILE B 162 ? 0.2740 0.2866 0.8950 -0.0124 0.0822  0.0256  1072 ILE B N   
3393 C CA  . ILE B 162 ? 0.2906 0.2954 0.9632 -0.0160 0.0944  0.0313  1072 ILE B CA  
3394 C C   . ILE B 162 ? 0.2935 0.2962 0.9862 -0.0103 0.1013  0.0648  1072 ILE B C   
3395 O O   . ILE B 162 ? 0.4255 0.4375 1.0876 -0.0042 0.0962  0.0840  1072 ILE B O   
3396 C CB  . ILE B 162 ? 0.2855 0.2967 0.9646 -0.0211 0.0973  0.0300  1072 ILE B CB  
3397 C CG1 . ILE B 162 ? 0.2853 0.3092 0.9393 -0.0168 0.0962  0.0574  1072 ILE B CG1 
3398 C CG2 . ILE B 162 ? 0.2772 0.2943 0.9366 -0.0262 0.0895  -0.0008 1072 ILE B CG2 
3399 C CD1 . ILE B 162 ? 0.2875 0.3187 0.9510 -0.0214 0.1006  0.0595  1072 ILE B CD1 
3400 N N   . SER B 163 ? 0.3059 0.2985 1.0504 -0.0113 0.1128  0.0718  1073 SER B N   
3401 C CA  . SER B 163 ? 0.3655 0.3572 1.1327 -0.0033 0.1190  0.1042  1073 SER B CA  
3402 C C   . SER B 163 ? 0.4090 0.4137 1.1757 -0.0019 0.1232  0.1359  1073 SER B C   
3403 O O   . SER B 163 ? 0.4002 0.4101 1.1588 -0.0069 0.1235  0.1295  1073 SER B O   
3404 C CB  . SER B 163 ? 0.3763 0.3580 1.1913 0.0011  0.1273  0.0949  1073 SER B CB  
3405 O OG  . SER B 163 ? 0.3458 0.3269 1.1893 0.0009  0.1349  0.0979  1073 SER B OG  
3406 N N   . ASP B 164 ? 0.4150 0.4284 1.1904 0.0052  0.1262  0.1708  1074 ASP B N   
3407 C CA  . ASP B 164 ? 0.4739 0.5048 1.2505 0.0073  0.1307  0.2037  1074 ASP B CA  
3408 C C   . ASP B 164 ? 0.4735 0.4956 1.2843 0.0069  0.1385  0.1991  1074 ASP B C   
3409 O O   . ASP B 164 ? 0.4511 0.4840 1.2533 0.0037  0.1407  0.2084  1074 ASP B O   
3410 C CB  . ASP B 164 ? 0.5537 0.5985 1.3401 0.0163  0.1326  0.2418  1074 ASP B CB  
3411 C CG  . ASP B 164 ? 0.6117 0.6842 1.3880 0.0181  0.1354  0.2775  1074 ASP B CG  
3412 O OD1 . ASP B 164 ? 0.6317 0.7249 1.3697 0.0129  0.1317  0.2773  1074 ASP B OD1 
3413 O OD2 . ASP B 164 ? 0.5910 0.6701 1.3997 0.0252  0.1414  0.3047  1074 ASP B OD2 
3414 N N   . ALA B 165 ? 0.4441 0.4502 1.2958 0.0096  0.1434  0.1823  1075 ALA B N   
3415 C CA  . ALA B 165 ? 0.3980 0.3971 1.2875 0.0089  0.1516  0.1736  1075 ALA B CA  
3416 C C   . ALA B 165 ? 0.4065 0.4005 1.2750 -0.0004 0.1484  0.1431  1075 ALA B C   
3417 O O   . ALA B 165 ? 0.4577 0.4543 1.3355 -0.0028 0.1528  0.1477  1075 ALA B O   
3418 C CB  . ALA B 165 ? 0.3897 0.3794 1.3296 0.0128  0.1581  0.1569  1075 ALA B CB  
3419 N N   . GLU B 166 ? 0.3564 0.3456 1.1984 -0.0057 0.1406  0.1121  1076 GLU B N   
3420 C CA  . GLU B 166 ? 0.4049 0.3945 1.2267 -0.0141 0.1362  0.0833  1076 GLU B CA  
3421 C C   . GLU B 166 ? 0.3920 0.3971 1.1812 -0.0177 0.1330  0.0995  1076 GLU B C   
3422 O O   . GLU B 166 ? 0.4313 0.4397 1.2164 -0.0230 0.1328  0.0859  1076 GLU B O   
3423 C CB  . GLU B 166 ? 0.3329 0.3198 1.1327 -0.0178 0.1278  0.0511  1076 GLU B CB  
3424 C CG  . GLU B 166 ? 0.3208 0.3150 1.0932 -0.0257 0.1204  0.0246  1076 GLU B CG  
3425 C CD  . GLU B 166 ? 0.3601 0.3510 1.1571 -0.0293 0.1249  0.0011  1076 GLU B CD  
3426 O OE1 . GLU B 166 ? 0.4027 0.3880 1.2236 -0.0289 0.1279  -0.0223 1076 GLU B OE1 
3427 O OE2 . GLU B 166 ? 0.3876 0.3843 1.1808 -0.0325 0.1258  0.0051  1076 GLU B OE2 
3428 N N   . ALA B 167 ? 0.4214 0.4401 1.1893 -0.0146 0.1310  0.1277  1077 ALA B N   
3429 C CA  . ALA B 167 ? 0.4753 0.5165 1.2145 -0.0173 0.1292  0.1415  1077 ALA B CA  
3430 C C   . ALA B 167 ? 0.5186 0.5661 1.2771 -0.0164 0.1379  0.1643  1077 ALA B C   
3431 O O   . ALA B 167 ? 0.4987 0.5593 1.2435 -0.0208 0.1381  0.1619  1077 ALA B O   
3432 C CB  . ALA B 167 ? 0.4200 0.4800 1.1283 -0.0128 0.1243  0.1616  1077 ALA B CB  
3433 N N   . ASP B 168 ? 0.6351 0.6752 1.4279 -0.0101 0.1451  0.1863  1078 ASP B N   
3434 C CA  . ASP B 168 ? 0.5928 0.6378 1.4116 -0.0084 0.1538  0.2080  1078 ASP B CA  
3435 C C   . ASP B 168 ? 0.5798 0.6134 1.4143 -0.0144 0.1566  0.1815  1078 ASP B C   
3436 O O   . ASP B 168 ? 0.6231 0.6662 1.4630 -0.0164 0.1616  0.1940  1078 ASP B O   
3437 C CB  . ASP B 168 ? 0.6336 0.6713 1.4964 0.0007  0.1606  0.2300  1078 ASP B CB  
3438 C CG  . ASP B 168 ? 0.7102 0.7679 1.5614 0.0076  0.1593  0.2676  1078 ASP B CG  
3439 O OD1 . ASP B 168 ? 0.8211 0.9024 1.6648 0.0091  0.1622  0.2988  1078 ASP B OD1 
3440 O OD2 . ASP B 168 ? 0.6979 0.7513 1.5468 0.0115  0.1553  0.2660  1078 ASP B OD2 
3441 N N   . VAL B 169 ? 0.5138 0.5301 1.3557 -0.0174 0.1535  0.1450  1079 VAL B N   
3442 C CA  . VAL B 169 ? 0.4779 0.4853 1.3400 -0.0223 0.1564  0.1186  1079 VAL B CA  
3443 C C   . VAL B 169 ? 0.4830 0.5012 1.3101 -0.0302 0.1498  0.1002  1079 VAL B C   
3444 O O   . VAL B 169 ? 0.5166 0.5351 1.3552 -0.0345 0.1528  0.0894  1079 VAL B O   
3445 C CB  . VAL B 169 ? 0.4852 0.4764 1.3732 -0.0215 0.1568  0.0871  1079 VAL B CB  
3446 C CG1 . VAL B 169 ? 0.5662 0.5527 1.4735 -0.0269 0.1593  0.0562  1079 VAL B CG1 
3447 C CG2 . VAL B 169 ? 0.4535 0.4379 1.3849 -0.0128 0.1649  0.1056  1079 VAL B CG2 
3448 N N   . ARG B 170 ? 0.5234 0.5072 1.1305 -0.2035 0.1191  0.0743  1080 ARG B N   
3449 C CA  . ARG B 170 ? 0.4971 0.5544 1.1036 -0.2036 0.1116  0.0460  1080 ARG B CA  
3450 C C   . ARG B 170 ? 0.4721 0.5734 1.0664 -0.2212 0.1221  0.0550  1080 ARG B C   
3451 O O   . ARG B 170 ? 0.4761 0.5766 1.0665 -0.2173 0.1265  0.0833  1080 ARG B O   
3452 C CB  . ARG B 170 ? 0.4273 0.5126 1.0431 -0.1717 0.0924  0.0356  1080 ARG B CB  
3453 C CG  . ARG B 170 ? 0.4811 0.5360 1.1056 -0.1587 0.0849  0.0161  1080 ARG B CG  
3454 C CD  . ARG B 170 ? 0.3466 0.4314 0.9670 -0.1340 0.0688  -0.0034 1080 ARG B CD  
3455 N NE  . ARG B 170 ? 0.3494 0.4079 0.9718 -0.1274 0.0662  -0.0252 1080 ARG B NE  
3456 C CZ  . ARG B 170 ? 0.3171 0.3882 0.9277 -0.1112 0.0565  -0.0456 1080 ARG B CZ  
3457 N NH1 . ARG B 170 ? 0.2819 0.3865 0.8735 -0.0993 0.0473  -0.0482 1080 ARG B NH1 
3458 N NH2 . ARG B 170 ? 0.3269 0.3721 0.9395 -0.1078 0.0578  -0.0636 1080 ARG B NH2 
3459 N N   . GLU B 171 ? 0.5114 0.6531 1.1009 -0.2403 0.1257  0.0320  1081 GLU B N   
3460 C CA  . GLU B 171 ? 0.4805 0.6677 1.0620 -0.2605 0.1382  0.0365  1081 GLU B CA  
3461 C C   . GLU B 171 ? 0.4842 0.7357 1.0650 -0.2386 0.1269  0.0298  1081 GLU B C   
3462 O O   . GLU B 171 ? 0.4304 0.7159 1.0045 -0.2488 0.1383  0.0398  1081 GLU B O   
3463 C CB  . GLU B 171 ? 0.5088 0.7208 1.0938 -0.2877 0.1438  0.0157  1081 GLU B CB  
3464 N N   . ASP B 172 ? 0.4546 0.7184 1.0365 -0.2092 0.1063  0.0134  1082 ASP B N   
3465 C CA  . ASP B 172 ? 0.4665 0.7796 1.0388 -0.1860 0.0941  0.0063  1082 ASP B CA  
3466 C C   . ASP B 172 ? 0.4445 0.7334 1.0145 -0.1621 0.0852  0.0220  1082 ASP B C   
3467 O O   . ASP B 172 ? 0.4606 0.7299 1.0284 -0.1430 0.0711  0.0113  1082 ASP B O   
3468 C CB  . ASP B 172 ? 0.4326 0.7732 0.9989 -0.1718 0.0777  -0.0221 1082 ASP B CB  
3469 C CG  . ASP B 172 ? 0.4278 0.8125 0.9789 -0.1487 0.0669  -0.0278 1082 ASP B CG  
3470 O OD1 . ASP B 172 ? 0.3912 0.7810 0.9339 -0.1388 0.0683  -0.0136 1082 ASP B OD1 
3471 O OD2 . ASP B 172 ? 0.4205 0.8310 0.9689 -0.1392 0.0571  -0.0466 1082 ASP B OD2 
3472 N N   . ASP B 173 ? 0.4511 0.7432 1.0212 -0.1640 0.0940  0.0491  1083 ASP B N   
3473 C CA  . ASP B 173 ? 0.4277 0.7046 0.9932 -0.1407 0.0826  0.0689  1083 ASP B CA  
3474 C C   . ASP B 173 ? 0.3687 0.6914 0.9139 -0.1227 0.0740  0.0637  1083 ASP B C   
3475 O O   . ASP B 173 ? 0.4081 0.7226 0.9244 -0.1084 0.0677  0.0833  1083 ASP B O   
3476 C CB  . ASP B 173 ? 0.4828 0.7109 1.0234 -0.1445 0.0893  0.1046  1083 ASP B CB  
3477 C CG  . ASP B 173 ? 0.5522 0.7926 1.0749 -0.1691 0.1101  0.1196  1083 ASP B CG  
3478 O OD1 . ASP B 173 ? 0.5741 0.8653 1.1149 -0.1864 0.1215  0.0992  1083 ASP B OD1 
3479 O OD2 . ASP B 173 ? 0.5920 0.7918 1.0810 -0.1706 0.1153  0.1512  1083 ASP B OD2 
3480 N N   . SER B 174 ? 0.3194 0.6796 0.8577 -0.1187 0.0699  0.0349  1084 SER B N   
3481 C CA  . SER B 174 ? 0.2915 0.6882 0.8090 -0.1002 0.0623  0.0274  1084 SER B CA  
3482 C C   . SER B 174 ? 0.1947 0.5723 0.6947 -0.0762 0.0440  0.0189  1084 SER B C   
3483 O O   . SER B 174 ? 0.1790 0.5771 0.6591 -0.0614 0.0378  0.0153  1084 SER B O   
3484 C CB  . SER B 174 ? 0.2123 0.6518 0.7216 -0.1006 0.0625  0.0044  1084 SER B CB  
3485 O OG  . SER B 174 ? 0.3084 0.7672 0.8347 -0.1263 0.0793  0.0080  1084 SER B OG  
3486 N N   . TYR B 175 ? 0.2475 0.5857 0.7535 -0.0738 0.0375  0.0148  1085 TYR B N   
3487 C CA  . TYR B 175 ? 0.2255 0.5443 0.7120 -0.0560 0.0241  0.0031  1085 TYR B CA  
3488 C C   . TYR B 175 ? 0.2368 0.5229 0.7434 -0.0531 0.0211  0.0152  1085 TYR B C   
3489 O O   . TYR B 175 ? 0.1775 0.4405 0.6755 -0.0448 0.0146  0.0015  1085 TYR B O   
3490 C CB  . TYR B 175 ? 0.1714 0.4806 0.6413 -0.0529 0.0192  -0.0216 1085 TYR B CB  
3491 C CG  . TYR B 175 ? 0.1996 0.5441 0.6573 -0.0505 0.0188  -0.0319 1085 TYR B CG  
3492 C CD1 . TYR B 175 ? 0.1897 0.5556 0.6647 -0.0645 0.0259  -0.0342 1085 TYR B CD1 
3493 C CD2 . TYR B 175 ? 0.1756 0.5305 0.6071 -0.0335 0.0114  -0.0400 1085 TYR B CD2 
3494 C CE1 . TYR B 175 ? 0.1784 0.5790 0.6485 -0.0588 0.0244  -0.0440 1085 TYR B CE1 
3495 C CE2 . TYR B 175 ? 0.1637 0.5460 0.5883 -0.0260 0.0101  -0.0504 1085 TYR B CE2 
3496 C CZ  . TYR B 175 ? 0.1673 0.5740 0.6128 -0.0374 0.0161  -0.0522 1085 TYR B CZ  
3497 O OH  . TYR B 175 ? 0.1723 0.6081 0.6140 -0.0276 0.0141  -0.0657 1085 TYR B OH  
3498 N N   . LEU B 176 ? 0.2408 0.5252 0.7741 -0.0591 0.0262  0.0428  1086 LEU B N   
3499 C CA  . LEU B 176 ? 0.2490 0.4957 0.7946 -0.0529 0.0223  0.0555  1086 LEU B CA  
3500 C C   . LEU B 176 ? 0.2595 0.5112 0.7859 -0.0343 0.0095  0.0690  1086 LEU B C   
3501 O O   . LEU B 176 ? 0.2928 0.5526 0.7946 -0.0329 0.0089  0.0900  1086 LEU B O   
3502 C CB  . LEU B 176 ? 0.3153 0.5314 0.8678 -0.0676 0.0339  0.0761  1086 LEU B CB  
3503 C CG  . LEU B 176 ? 0.3192 0.4856 0.8853 -0.0609 0.0318  0.0878  1086 LEU B CG  
3504 C CD1 . LEU B 176 ? 0.2907 0.4529 0.8791 -0.0476 0.0232  0.0652  1086 LEU B CD1 
3505 C CD2 . LEU B 176 ? 0.3915 0.5249 0.9689 -0.0840 0.0479  0.0918  1086 LEU B CD2 
3506 N N   . PHE B 177 ? 0.2084 0.4579 0.7457 -0.0218 -0.0001 0.0550  1087 PHE B N   
3507 C CA  . PHE B 177 ? 0.2845 0.5449 0.8118 -0.0054 -0.0136 0.0624  1087 PHE B CA  
3508 C C   . PHE B 177 ? 0.2493 0.4830 0.7979 0.0072  -0.0201 0.0759  1087 PHE B C   
3509 O O   . PHE B 177 ? 0.2397 0.4524 0.8170 0.0074  -0.0162 0.0635  1087 PHE B O   
3510 C CB  . PHE B 177 ? 0.2529 0.5313 0.7766 -0.0018 -0.0184 0.0352  1087 PHE B CB  
3511 C CG  . PHE B 177 ? 0.2515 0.5541 0.7600 0.0086  -0.0308 0.0387  1087 PHE B CG  
3512 C CD1 . PHE B 177 ? 0.2187 0.5245 0.7468 0.0224  -0.0424 0.0434  1087 PHE B CD1 
3513 C CD2 . PHE B 177 ? 0.2251 0.5485 0.6988 0.0056  -0.0316 0.0346  1087 PHE B CD2 
3514 C CE1 . PHE B 177 ? 0.2207 0.5543 0.7357 0.0307  -0.0556 0.0437  1087 PHE B CE1 
3515 C CE2 . PHE B 177 ? 0.1975 0.5420 0.6540 0.0126  -0.0430 0.0353  1087 PHE B CE2 
3516 C CZ  . PHE B 177 ? 0.2663 0.6183 0.7446 0.0239  -0.0555 0.0394  1087 PHE B CZ  
3517 N N   . ASP B 178 ? 0.2745 0.5065 0.8061 0.0195  -0.0303 0.1011  1088 ASP B N   
3518 C CA  . ASP B 178 ? 0.3950 0.5996 0.9410 0.0381  -0.0402 0.1165  1088 ASP B CA  
3519 C C   . ASP B 178 ? 0.3418 0.5780 0.9046 0.0578  -0.0575 0.1024  1088 ASP B C   
3520 O O   . ASP B 178 ? 0.3086 0.5751 0.8502 0.0645  -0.0698 0.1074  1088 ASP B O   
3521 C CB  . ASP B 178 ? 0.4467 0.6258 0.9583 0.0419  -0.0428 0.1528  1088 ASP B CB  
3522 C CG  . ASP B 178 ? 0.5342 0.6634 1.0539 0.0576  -0.0476 0.1710  1088 ASP B CG  
3523 O OD1 . ASP B 178 ? 0.5800 0.7151 1.1245 0.0821  -0.0632 0.1635  1088 ASP B OD1 
3524 O OD2 . ASP B 178 ? 0.6079 0.6913 1.1091 0.0453  -0.0348 0.1914  1088 ASP B OD2 
3525 N N   . LEU B 179 ? 0.3748 0.6073 0.9764 0.0648  -0.0571 0.0819  1089 LEU B N   
3526 C CA  . LEU B 179 ? 0.4109 0.6802 1.0360 0.0811  -0.0711 0.0645  1089 LEU B CA  
3527 C C   . LEU B 179 ? 0.4897 0.7637 1.1112 0.1085  -0.0931 0.0873  1089 LEU B C   
3528 O O   . LEU B 179 ? 0.4052 0.7230 1.0278 0.1183  -0.1087 0.0796  1089 LEU B O   
3529 C CB  . LEU B 179 ? 0.3922 0.6485 1.0433 0.0806  -0.0615 0.0363  1089 LEU B CB  
3530 C CG  . LEU B 179 ? 0.2330 0.4743 0.8678 0.0546  -0.0416 0.0124  1089 LEU B CG  
3531 C CD1 . LEU B 179 ? 0.2338 0.4623 0.8786 0.0528  -0.0328 -0.0154 1089 LEU B CD1 
3532 C CD2 . LEU B 179 ? 0.2221 0.4845 0.8117 0.0391  -0.0389 0.0027  1089 LEU B CD2 
3533 N N   . ASP B 180 ? 0.5943 0.8204 1.2066 0.1205  -0.0950 0.1150  1090 ASP B N   
3534 C CA  . ASP B 180 ? 0.7319 0.9459 1.3268 0.1490  -0.1168 0.1433  1090 ASP B CA  
3535 C C   . ASP B 180 ? 0.9030 1.1410 1.5416 0.1814  -0.1360 0.1287  1090 ASP B C   
3536 O O   . ASP B 180 ? 0.8807 1.1610 1.5166 0.1996  -0.1581 0.1275  1090 ASP B O   
3537 C CB  . ASP B 180 ? 0.6801 0.9234 1.2316 0.1462  -0.1281 0.1581  1090 ASP B CB  
3538 C CG  . ASP B 180 ? 0.8710 1.0818 1.3829 0.1691  -0.1458 0.1960  1090 ASP B CG  
3539 O OD1 . ASP B 180 ? 0.9481 1.1238 1.4722 0.1958  -0.1566 0.2076  1090 ASP B OD1 
3540 O OD2 . ASP B 180 ? 0.9010 1.1181 1.3653 0.1616  -0.1488 0.2140  1090 ASP B OD2 
3541 N N   . ASN B 181 ? 1.2042 1.4166 1.8806 0.1885  -0.1273 0.1154  1091 ASN B N   
3542 C CA  . ASN B 181 ? 1.2592 1.4917 1.9532 0.2104  -0.1353 0.0905  1091 ASN B CA  
3543 C C   . ASN B 181 ? 1.2945 1.5141 1.9734 0.2505  -0.1620 0.1152  1091 ASN B C   
3544 O O   . ASN B 181 ? 1.3816 1.5357 2.0483 0.2671  -0.1653 0.1449  1091 ASN B O   
3545 C CB  . ASN B 181 ? 1.2978 1.4960 2.0200 0.2059  -0.1164 0.0715  1091 ASN B CB  
3546 C CG  . ASN B 181 ? 1.2540 1.4582 1.9823 0.1682  -0.0917 0.0475  1091 ASN B CG  
3547 O OD1 . ASN B 181 ? 1.2236 1.3870 1.9592 0.1537  -0.0771 0.0555  1091 ASN B OD1 
3548 N ND2 . ASN B 181 ? 1.2546 1.5058 1.9754 0.1525  -0.0867 0.0183  1091 ASN B ND2 
3549 N N   . LYS B 182 ? 1.1638 1.4420 1.8380 0.2658  -0.1802 0.1027  1092 LYS B N   
3550 C CA  . LYS B 182 ? 1.1546 1.4278 1.8115 0.3078  -0.2078 0.1222  1092 LYS B CA  
3551 C C   . LYS B 182 ? 1.2099 1.4591 1.8899 0.3369  -0.2075 0.1130  1092 LYS B C   
3552 O O   . LYS B 182 ? 1.2489 1.4501 1.9059 0.3720  -0.2236 0.1390  1092 LYS B O   
3553 N N   . ASP B 183 ? 1.1615 1.4380 1.8801 0.3229  -0.1885 0.0771  1093 ASP B N   
3554 C CA  . ASP B 183 ? 1.1094 1.3656 1.8528 0.3473  -0.1848 0.0651  1093 ASP B CA  
3555 C C   . ASP B 183 ? 1.1371 1.3158 1.8817 0.3321  -0.1643 0.0714  1093 ASP B C   
3556 O O   . ASP B 183 ? 1.1061 1.2852 1.8616 0.2938  -0.1424 0.0569  1093 ASP B O   
3557 N N   . GLY B 184 ? 1.1976 1.3072 1.9268 0.3617  -0.1707 0.0934  1094 GLY B N   
3558 C CA  . GLY B 184 ? 1.1834 1.2141 1.9101 0.3455  -0.1502 0.1010  1094 GLY B CA  
3559 C C   . GLY B 184 ? 1.1748 1.1701 1.8792 0.3127  -0.1407 0.1278  1094 GLY B C   
3560 O O   . GLY B 184 ? 1.1906 1.1917 1.8652 0.3150  -0.1554 0.1551  1094 GLY B O   
3561 N N   . GLU B 185 ? 1.0378 0.9998 1.7572 0.2812  -0.1150 0.1192  1095 GLU B N   
3562 C CA  . GLU B 185 ? 0.9534 0.8754 1.6564 0.2506  -0.1013 0.1445  1095 GLU B CA  
3563 C C   . GLU B 185 ? 0.9619 0.9514 1.6774 0.2197  -0.0948 0.1304  1095 GLU B C   
3564 O O   . GLU B 185 ? 0.9040 0.9505 1.6468 0.2098  -0.0897 0.0943  1095 GLU B O   
3565 C CB  . GLU B 185 ? 0.9311 0.7858 1.6401 0.2300  -0.0761 0.1391  1095 GLU B CB  
3566 C CG  . GLU B 185 ? 0.9640 0.7409 1.6477 0.2557  -0.0785 0.1514  1095 GLU B CG  
3567 C CD  . GLU B 185 ? 0.9220 0.6706 1.6265 0.2433  -0.0577 0.1223  1095 GLU B CD  
3568 O OE1 . GLU B 185 ? 0.8837 0.6832 1.6241 0.2203  -0.0452 0.0896  1095 GLU B OE1 
3569 O OE2 . GLU B 185 ? 0.9794 0.6522 1.6577 0.2561  -0.0539 0.1318  1095 GLU B OE2 
3570 N N   . VAL B 186 ? 0.9877 0.9656 1.6551 0.1962  -0.0903 0.1552  1096 VAL B N   
3571 C CA  . VAL B 186 ? 0.9385 0.9680 1.5993 0.1628  -0.0802 0.1421  1096 VAL B CA  
3572 C C   . VAL B 186 ? 0.8383 0.8662 1.5236 0.1336  -0.0566 0.1129  1096 VAL B C   
3573 O O   . VAL B 186 ? 0.9082 0.8807 1.5943 0.1239  -0.0420 0.1146  1096 VAL B O   
3574 C CB  . VAL B 186 ? 0.9636 0.9723 1.5686 0.1442  -0.0762 0.1744  1096 VAL B CB  
3575 C CG1 . VAL B 186 ? 0.9468 0.9817 1.5460 0.1050  -0.0563 0.1600  1096 VAL B CG1 
3576 C CG2 . VAL B 186 ? 0.9814 1.0216 1.5598 0.1655  -0.1002 0.1931  1096 VAL B CG2 
3577 N N   . TYR B 187 ? 0.6805 0.7655 1.3819 0.1195  -0.0532 0.0851  1097 TYR B N   
3578 C CA  . TYR B 187 ? 0.5590 0.6448 1.2669 0.0890  -0.0330 0.0614  1097 TYR B CA  
3579 C C   . TYR B 187 ? 0.4672 0.5861 1.1452 0.0664  -0.0299 0.0631  1097 TYR B C   
3580 O O   . TYR B 187 ? 0.4799 0.6260 1.1364 0.0735  -0.0421 0.0778  1097 TYR B O   
3581 C CB  . TYR B 187 ? 0.4620 0.5731 1.2087 0.0922  -0.0285 0.0243  1097 TYR B CB  
3582 C CG  . TYR B 187 ? 0.5156 0.5833 1.2904 0.1048  -0.0222 0.0164  1097 TYR B CG  
3583 C CD1 . TYR B 187 ? 0.5300 0.5871 1.3140 0.1367  -0.0356 0.0240  1097 TYR B CD1 
3584 C CD2 . TYR B 187 ? 0.4784 0.5125 1.2572 0.0834  -0.0035 0.0003  1097 TYR B CD2 
3585 C CE1 . TYR B 187 ? 0.5175 0.5313 1.3142 0.1476  -0.0292 0.0158  1097 TYR B CE1 
3586 C CE2 . TYR B 187 ? 0.4288 0.4186 1.2305 0.0947  0.0033  -0.0084 1097 TYR B CE2 
3587 C CZ  . TYR B 187 ? 0.4864 0.4657 1.2919 0.1255  -0.0090 -0.0001 1097 TYR B CZ  
3588 O OH  . TYR B 187 ? 0.6187 0.5548 1.4299 0.1351  -0.0025 -0.0089 1097 TYR B OH  
3589 N N   . CYS B 188 ? 0.3349 0.4507 1.0099 0.0406  -0.0143 0.0472  1098 CYS B N   
3590 C CA  . CYS B 188 ? 0.2885 0.4295 0.9347 0.0216  -0.0105 0.0492  1098 CYS B CA  
3591 C C   . CYS B 188 ? 0.2913 0.4483 0.9419 0.0054  -0.0014 0.0180  1098 CYS B C   
3592 O O   . CYS B 188 ? 0.2316 0.3715 0.9036 0.0026  0.0056  -0.0025 1098 CYS B O   
3593 C CB  . CYS B 188 ? 0.3112 0.4251 0.9364 0.0057  -0.0013 0.0725  1098 CYS B CB  
3594 S SG  . CYS B 188 ? 0.3861 0.4547 0.9923 0.0201  -0.0070 0.1131  1098 CYS B SG  
3595 N N   . ILE B 189 ? 0.2092 0.3948 0.8333 -0.0039 -0.0018 0.0147  1099 ILE B N   
3596 C CA  . ILE B 189 ? 0.1961 0.3744 0.7761 -0.0150 0.0041  -0.0107 1099 ILE B CA  
3597 C C   . ILE B 189 ? 0.2476 0.4335 0.8118 -0.0282 0.0092  -0.0049 1099 ILE B C   
3598 O O   . ILE B 189 ? 0.2060 0.4176 0.7595 -0.0283 0.0067  0.0097  1099 ILE B O   
3599 C CB  . ILE B 189 ? 0.2376 0.4317 0.7776 -0.0103 -0.0011 -0.0238 1099 ILE B CB  
3600 C CG1 . ILE B 189 ? 0.1870 0.3801 0.7421 -0.0006 -0.0043 -0.0332 1099 ILE B CG1 
3601 C CG2 . ILE B 189 ? 0.2006 0.3825 0.7040 -0.0186 0.0042  -0.0450 1099 ILE B CG2 
3602 C CD1 . ILE B 189 ? 0.2199 0.4274 0.7400 -0.0022 -0.0057 -0.0484 1099 ILE B CD1 
3603 N N   . ASP B 190 ? 0.2199 0.3871 0.7833 -0.0389 0.0164  -0.0179 1100 ASP B N   
3604 C CA  . ASP B 190 ? 0.2358 0.4153 0.7834 -0.0511 0.0207  -0.0190 1100 ASP B CA  
3605 C C   . ASP B 190 ? 0.1893 0.3710 0.6989 -0.0485 0.0172  -0.0425 1100 ASP B C   
3606 O O   . ASP B 190 ? 0.1927 0.3516 0.7006 -0.0491 0.0185  -0.0600 1100 ASP B O   
3607 C CB  . ASP B 190 ? 0.2357 0.3949 0.8112 -0.0663 0.0301  -0.0163 1100 ASP B CB  
3608 C CG  . ASP B 190 ? 0.2342 0.4148 0.7994 -0.0818 0.0358  -0.0150 1100 ASP B CG  
3609 O OD1 . ASP B 190 ? 0.2248 0.4363 0.7631 -0.0777 0.0313  -0.0215 1100 ASP B OD1 
3610 O OD2 . ASP B 190 ? 0.2616 0.4274 0.8461 -0.0988 0.0458  -0.0083 1100 ASP B OD2 
3611 N N   . ALA B 191 ? 0.1766 0.3845 0.6593 -0.0447 0.0130  -0.0425 1101 ALA B N   
3612 C CA  . ALA B 191 ? 0.1674 0.3761 0.6211 -0.0405 0.0088  -0.0622 1101 ALA B CA  
3613 C C   . ALA B 191 ? 0.1844 0.4146 0.6367 -0.0456 0.0087  -0.0685 1101 ALA B C   
3614 O O   . ALA B 191 ? 0.2048 0.4493 0.6366 -0.0377 0.0030  -0.0799 1101 ALA B O   
3615 C CB  . ALA B 191 ? 0.1551 0.3752 0.5830 -0.0306 0.0039  -0.0624 1101 ALA B CB  
3616 N N   . ARG B 192 ? 0.1841 0.4174 0.6606 -0.0588 0.0149  -0.0632 1102 ARG B N   
3617 C CA  . ARG B 192 ? 0.1957 0.4565 0.6759 -0.0667 0.0156  -0.0707 1102 ARG B CA  
3618 C C   . ARG B 192 ? 0.2366 0.4869 0.7117 -0.0654 0.0098  -0.0946 1102 ARG B C   
3619 O O   . ARG B 192 ? 0.1912 0.4675 0.6585 -0.0603 0.0033  -0.1076 1102 ARG B O   
3620 C CB  . ARG B 192 ? 0.2102 0.4767 0.7180 -0.0864 0.0267  -0.0581 1102 ARG B CB  
3621 C CG  . ARG B 192 ? 0.2461 0.5375 0.7632 -0.1000 0.0289  -0.0702 1102 ARG B CG  
3622 C CD  . ARG B 192 ? 0.2128 0.5518 0.7201 -0.0922 0.0245  -0.0745 1102 ARG B CD  
3623 N NE  . ARG B 192 ? 0.2818 0.6491 0.8032 -0.1029 0.0249  -0.0888 1102 ARG B NE  
3624 C CZ  . ARG B 192 ? 0.2361 0.6056 0.7534 -0.0951 0.0142  -0.1116 1102 ARG B CZ  
3625 N NH1 . ARG B 192 ? 0.2406 0.5832 0.7379 -0.0782 0.0039  -0.1228 1102 ARG B NH1 
3626 N NH2 . ARG B 192 ? 0.2422 0.6428 0.7768 -0.1057 0.0142  -0.1251 1102 ARG B NH2 
3627 N N   . TYR B 193 ? 0.2148 0.4294 0.6966 -0.0685 0.0119  -0.1022 1103 TYR B N   
3628 C CA  . TYR B 193 ? 0.2698 0.4744 0.7460 -0.0674 0.0067  -0.1263 1103 TYR B CA  
3629 C C   . TYR B 193 ? 0.2156 0.3962 0.6714 -0.0553 0.0024  -0.1390 1103 TYR B C   
3630 O O   . TYR B 193 ? 0.2033 0.3870 0.6459 -0.0494 -0.0059 -0.1598 1103 TYR B O   
3631 C CB  . TYR B 193 ? 0.2278 0.4112 0.7243 -0.0815 0.0137  -0.1308 1103 TYR B CB  
3632 C CG  . TYR B 193 ? 0.2441 0.4450 0.7619 -0.0989 0.0210  -0.1190 1103 TYR B CG  
3633 C CD1 . TYR B 193 ? 0.3091 0.5436 0.8331 -0.1089 0.0185  -0.1298 1103 TYR B CD1 
3634 C CD2 . TYR B 193 ? 0.2545 0.4393 0.7884 -0.1063 0.0309  -0.0984 1103 TYR B CD2 
3635 C CE1 . TYR B 193 ? 0.2734 0.5245 0.8168 -0.1295 0.0282  -0.1200 1103 TYR B CE1 
3636 C CE2 . TYR B 193 ? 0.2764 0.4714 0.8275 -0.1257 0.0401  -0.0878 1103 TYR B CE2 
3637 C CZ  . TYR B 193 ? 0.2864 0.5144 0.8407 -0.1392 0.0399  -0.0987 1103 TYR B CZ  
3638 O OH  . TYR B 193 ? 0.3137 0.5506 0.8838 -0.1628 0.0520  -0.0883 1103 TYR B OH  
3639 N N   . TYR B 194 ? 0.2349 0.3938 0.6896 -0.0522 0.0077  -0.1290 1104 TYR B N   
3640 C CA  . TYR B 194 ? 0.1863 0.3274 0.6214 -0.0443 0.0066  -0.1407 1104 TYR B CA  
3641 C C   . TYR B 194 ? 0.2207 0.3722 0.6466 -0.0385 0.0061  -0.1254 1104 TYR B C   
3642 O O   . TYR B 194 ? 0.1737 0.3285 0.6146 -0.0400 0.0095  -0.1061 1104 TYR B O   
3643 C CB  . TYR B 194 ? 0.1967 0.3063 0.6401 -0.0467 0.0154  -0.1484 1104 TYR B CB  
3644 C CG  . TYR B 194 ? 0.2135 0.3128 0.6669 -0.0533 0.0179  -0.1601 1104 TYR B CG  
3645 C CD1 . TYR B 194 ? 0.2255 0.3236 0.7047 -0.0615 0.0224  -0.1502 1104 TYR B CD1 
3646 C CD2 . TYR B 194 ? 0.2334 0.3225 0.6675 -0.0527 0.0161  -0.1808 1104 TYR B CD2 
3647 C CE1 . TYR B 194 ? 0.2451 0.3333 0.7313 -0.0695 0.0252  -0.1621 1104 TYR B CE1 
3648 C CE2 . TYR B 194 ? 0.2418 0.3233 0.6808 -0.0594 0.0175  -0.1907 1104 TYR B CE2 
3649 C CZ  . TYR B 194 ? 0.2517 0.3336 0.7177 -0.0679 0.0222  -0.1824 1104 TYR B CZ  
3650 O OH  . TYR B 194 ? 0.2742 0.3481 0.7431 -0.0766 0.0238  -0.1940 1104 TYR B OH  
3651 N N   . GLY B 195 ? 0.2064 0.3639 0.6090 -0.0316 0.0008  -0.1358 1105 GLY B N   
3652 C CA  . GLY B 195 ? 0.1594 0.3285 0.5503 -0.0267 0.0001  -0.1245 1105 GLY B CA  
3653 C C   . GLY B 195 ? 0.1887 0.3558 0.5553 -0.0213 -0.0043 -0.1450 1105 GLY B C   
3654 O O   . GLY B 195 ? 0.1917 0.3430 0.5425 -0.0202 -0.0085 -0.1664 1105 GLY B O   
3655 N N   . ASN B 196 ? 0.2206 0.3975 0.5756 -0.0183 -0.0041 -0.1388 1106 ASN B N   
3656 C CA  . ASN B 196 ? 0.2303 0.3830 0.5315 -0.0128 -0.0057 -0.1520 1106 ASN B CA  
3657 C C   . ASN B 196 ? 0.1755 0.3502 0.4555 0.0004  -0.0120 -0.1433 1106 ASN B C   
3658 O O   . ASN B 196 ? 0.1699 0.3833 0.4808 0.0042  -0.0148 -0.1309 1106 ASN B O   
3659 C CB  . ASN B 196 ? 0.2121 0.3447 0.5049 -0.0247 0.0040  -0.1568 1106 ASN B CB  
3660 C CG  . ASN B 196 ? 0.2330 0.3940 0.5380 -0.0252 0.0037  -0.1423 1106 ASN B CG  
3661 O OD1 . ASN B 196 ? 0.1852 0.3807 0.5188 -0.0196 -0.0012 -0.1241 1106 ASN B OD1 
3662 N ND2 . ASN B 196 ? 0.1860 0.3322 0.4669 -0.0339 0.0097  -0.1513 1106 ASN B ND2 
3663 N N   . ILE B 197 ? 0.2352 0.3825 0.4603 0.0054  -0.0120 -0.1504 1107 ILE B N   
3664 C CA  . ILE B 197 ? 0.2012 0.3624 0.3984 0.0195  -0.0171 -0.1453 1107 ILE B CA  
3665 C C   . ILE B 197 ? 0.2324 0.4395 0.4680 0.0157  -0.0154 -0.1252 1107 ILE B C   
3666 O O   . ILE B 197 ? 0.1748 0.4082 0.4048 0.0269  -0.0184 -0.1188 1107 ILE B O   
3667 C CB  . ILE B 197 ? 0.3481 0.4607 0.4764 0.0206  -0.0145 -0.1569 1107 ILE B CB  
3668 C CG1 . ILE B 197 ? 0.3126 0.4288 0.4019 0.0393  -0.0202 -0.1559 1107 ILE B CG1 
3669 C CG2 . ILE B 197 ? 0.2352 0.3436 0.3714 0.0000  -0.0049 -0.1554 1107 ILE B CG2 
3670 C CD1 . ILE B 197 ? 0.2623 0.3956 0.3524 0.0619  -0.0304 -0.1600 1107 ILE B CD1 
3671 N N   . SER B 198 ? 0.2107 0.4276 0.4831 0.0017  -0.0108 -0.1156 1108 SER B N   
3672 C CA  . SER B 198 ? 0.1523 0.4052 0.4533 -0.0004 -0.0112 -0.0949 1108 SER B CA  
3673 C C   . SER B 198 ? 0.1369 0.4210 0.4689 0.0026  -0.0114 -0.0800 1108 SER B C   
3674 O O   . SER B 198 ? 0.1347 0.4456 0.4708 0.0042  -0.0112 -0.0640 1108 SER B O   
3675 C CB  . SER B 198 ? 0.1333 0.3881 0.4693 -0.0109 -0.0092 -0.0888 1108 SER B CB  
3676 O OG  . SER B 198 ? 0.2855 0.5189 0.6010 -0.0186 -0.0059 -0.1054 1108 SER B OG  
3677 N N   . ARG B 199 ? 0.1340 0.4071 0.4770 0.0005  -0.0102 -0.0827 1109 ARG B N   
3678 C CA  . ARG B 199 ? 0.1463 0.4402 0.5071 -0.0023 -0.0074 -0.0682 1109 ARG B CA  
3679 C C   . ARG B 199 ? 0.1568 0.4820 0.5051 0.0080  -0.0083 -0.0705 1109 ARG B C   
3680 O O   . ARG B 199 ? 0.1575 0.5087 0.5229 0.0032  -0.0030 -0.0577 1109 ARG B O   
3681 C CB  . ARG B 199 ? 0.1403 0.4199 0.5127 -0.0075 -0.0069 -0.0774 1109 ARG B CB  
3682 C CG  . ARG B 199 ? 0.1718 0.4555 0.5278 0.0038  -0.0137 -0.1000 1109 ARG B CG  
3683 C CD  . ARG B 199 ? 0.1493 0.4151 0.5149 -0.0009 -0.0161 -0.1152 1109 ARG B CD  
3684 N NE  . ARG B 199 ? 0.1541 0.4306 0.5456 -0.0135 -0.0110 -0.1050 1109 ARG B NE  
3685 C CZ  . ARG B 199 ? 0.2236 0.5308 0.6238 -0.0134 -0.0121 -0.1074 1109 ARG B CZ  
3686 N NH1 . ARG B 199 ? 0.1954 0.5264 0.5794 0.0023  -0.0186 -0.1175 1109 ARG B NH1 
3687 N NH2 . ARG B 199 ? 0.1674 0.4820 0.5931 -0.0291 -0.0061 -0.1017 1109 ARG B NH2 
3688 N N   . PHE B 200 ? 0.1935 0.5179 0.5118 0.0225  -0.0138 -0.0889 1110 PHE B N   
3689 C CA  . PHE B 200 ? 0.1490 0.5004 0.4491 0.0378  -0.0153 -0.0950 1110 PHE B CA  
3690 C C   . PHE B 200 ? 0.1544 0.5204 0.4336 0.0413  -0.0122 -0.0849 1110 PHE B C   
3691 O O   . PHE B 200 ? 0.2281 0.6175 0.4909 0.0544  -0.0112 -0.0895 1110 PHE B O   
3692 C CB  . PHE B 200 ? 0.1661 0.4959 0.4290 0.0574  -0.0247 -0.1194 1110 PHE B CB  
3693 C CG  . PHE B 200 ? 0.1726 0.5029 0.4550 0.0585  -0.0305 -0.1324 1110 PHE B CG  
3694 C CD1 . PHE B 200 ? 0.1694 0.5270 0.4698 0.0564  -0.0290 -0.1289 1110 PHE B CD1 
3695 C CD2 . PHE B 200 ? 0.1745 0.4614 0.4397 0.0569  -0.0352 -0.1442 1110 PHE B CD2 
3696 C CE1 . PHE B 200 ? 0.1749 0.5309 0.4872 0.0554  -0.0351 -0.1412 1110 PHE B CE1 
3697 C CE2 . PHE B 200 ? 0.1970 0.4862 0.4777 0.0586  -0.0422 -0.1581 1110 PHE B CE2 
3698 C CZ  . PHE B 200 ? 0.1764 0.5014 0.4805 0.0580  -0.0431 -0.1567 1110 PHE B CZ  
3699 N N   . ILE B 201 ? 0.1526 0.5048 0.4304 0.0304  -0.0110 -0.0717 1111 ILE B N   
3700 C CA  . ILE B 201 ? 0.1954 0.5552 0.4463 0.0318  -0.0101 -0.0618 1111 ILE B CA  
3701 C C   . ILE B 201 ? 0.2126 0.6110 0.4866 0.0264  -0.0033 -0.0417 1111 ILE B C   
3702 O O   . ILE B 201 ? 0.2082 0.6131 0.5187 0.0142  -0.0003 -0.0260 1111 ILE B O   
3703 C CB  . ILE B 201 ? 0.1750 0.5128 0.4196 0.0220  -0.0136 -0.0578 1111 ILE B CB  
3704 C CG1 . ILE B 201 ? 0.1722 0.4694 0.3942 0.0213  -0.0155 -0.0785 1111 ILE B CG1 
3705 C CG2 . ILE B 201 ? 0.2104 0.5560 0.4223 0.0235  -0.0150 -0.0522 1111 ILE B CG2 
3706 C CD1 . ILE B 201 ? 0.2154 0.4985 0.4331 0.0087  -0.0166 -0.0804 1111 ILE B CD1 
3707 N N   . ASN B 202 ? 0.2094 0.6285 0.4573 0.0349  0.0005  -0.0421 1112 ASN B N   
3708 C CA  . ASN B 202 ? 0.1838 0.6377 0.4455 0.0277  0.0103  -0.0242 1112 ASN B CA  
3709 C C   . ASN B 202 ? 0.2246 0.6728 0.4704 0.0202  0.0083  -0.0027 1112 ASN B C   
3710 O O   . ASN B 202 ? 0.2398 0.6657 0.4671 0.0214  -0.0013 -0.0050 1112 ASN B O   
3711 C CB  . ASN B 202 ? 0.2425 0.7261 0.4854 0.0410  0.0171  -0.0370 1112 ASN B CB  
3712 C CG  . ASN B 202 ? 0.1852 0.6824 0.4480 0.0522  0.0156  -0.0591 1112 ASN B CG  
3713 O OD1 . ASN B 202 ? 0.1885 0.6813 0.4850 0.0402  0.0169  -0.0564 1112 ASN B OD1 
3714 N ND2 . ASN B 202 ? 0.1988 0.6927 0.4289 0.0751  0.0109  -0.0798 1112 ASN B ND2 
3715 N N   . HIS B 203 ? 0.2349 0.7042 0.4872 0.0114  0.0175  0.0175  1113 HIS B N   
3716 C CA  . HIS B 203 ? 0.2591 0.7240 0.4903 0.0067  0.0142  0.0402  1113 HIS B CA  
3717 C C   . HIS B 203 ? 0.2815 0.7604 0.4663 0.0139  0.0169  0.0359  1113 HIS B C   
3718 O O   . HIS B 203 ? 0.2656 0.7695 0.4443 0.0163  0.0300  0.0293  1113 HIS B O   
3719 C CB  . HIS B 203 ? 0.2690 0.7385 0.5182 -0.0071 0.0240  0.0663  1113 HIS B CB  
3720 C CG  . HIS B 203 ? 0.2937 0.7654 0.5061 -0.0097 0.0252  0.0890  1113 HIS B CG  
3721 N ND1 . HIS B 203 ? 0.3234 0.7743 0.5259 -0.0083 0.0115  0.1095  1113 HIS B ND1 
3722 C CD2 . HIS B 203 ? 0.3210 0.8137 0.5022 -0.0124 0.0381  0.0938  1113 HIS B CD2 
3723 C CE1 . HIS B 203 ? 0.3535 0.8093 0.5159 -0.0099 0.0140  0.1272  1113 HIS B CE1 
3724 N NE2 . HIS B 203 ? 0.3589 0.8387 0.5067 -0.0140 0.0317  0.1182  1113 HIS B NE2 
3725 N N   . LEU B 204 ? 0.2709 0.7373 0.4249 0.0167  0.0051  0.0381  1114 LEU B N   
3726 C CA  . LEU B 204 ? 0.2984 0.7744 0.4039 0.0216  0.0073  0.0346  1114 LEU B CA  
3727 C C   . LEU B 204 ? 0.3482 0.8260 0.4325 0.0157  0.0007  0.0590  1114 LEU B C   
3728 O O   . LEU B 204 ? 0.4203 0.8864 0.5127 0.0144  -0.0152 0.0663  1114 LEU B O   
3729 C CB  . LEU B 204 ? 0.2976 0.7548 0.3729 0.0300  -0.0006 0.0094  1114 LEU B CB  
3730 C CG  . LEU B 204 ? 0.3206 0.7689 0.3976 0.0414  0.0046  -0.0150 1114 LEU B CG  
3731 C CD1 . LEU B 204 ? 0.3616 0.7769 0.3966 0.0471  -0.0023 -0.0370 1114 LEU B CD1 
3732 C CD2 . LEU B 204 ? 0.2948 0.7733 0.3680 0.0504  0.0195  -0.0194 1114 LEU B CD2 
3733 N N   . CYS B 205 ? 0.3604 0.8547 0.4161 0.0132  0.0126  0.0703  1115 CYS B N   
3734 C CA  . CYS B 205 ? 0.4003 0.8928 0.4201 0.0100  0.0046  0.0917  1115 CYS B CA  
3735 C C   . CYS B 205 ? 0.4363 0.9243 0.4210 0.0154  -0.0119 0.0775  1115 CYS B C   
3736 O O   . CYS B 205 ? 0.4626 0.9494 0.4275 0.0146  -0.0273 0.0920  1115 CYS B O   
3737 C CB  . CYS B 205 ? 0.4381 0.9469 0.4279 0.0041  0.0244  0.1041  1115 CYS B CB  
3738 S SG  . CYS B 205 ? 0.5042 1.0151 0.5300 -0.0111 0.0446  0.1260  1115 CYS B SG  
3739 N N   . ASP B 206 ? 0.4371 0.9203 0.4111 0.0210  -0.0097 0.0486  1116 ASP B N   
3740 C CA  . ASP B 206 ? 0.4373 0.9094 0.3810 0.0213  -0.0233 0.0305  1116 ASP B CA  
3741 C C   . ASP B 206 ? 0.3973 0.8500 0.3710 0.0211  -0.0285 0.0115  1116 ASP B C   
3742 O O   . ASP B 206 ? 0.4034 0.8377 0.3586 0.0256  -0.0226 -0.0124 1116 ASP B O   
3743 C CB  . ASP B 206 ? 0.5042 0.9745 0.3948 0.0264  -0.0139 0.0124  1116 ASP B CB  
3744 C CG  . ASP B 206 ? 0.6067 1.0652 0.4574 0.0214  -0.0275 -0.0030 1116 ASP B CG  
3745 O OD1 . ASP B 206 ? 0.4932 0.9523 0.3616 0.0137  -0.0446 -0.0011 1116 ASP B OD1 
3746 O OD2 . ASP B 206 ? 0.7362 1.1868 0.5384 0.0249  -0.0204 -0.0192 1116 ASP B OD2 
3747 N N   . PRO B 207 ? 0.4148 0.8673 0.4300 0.0168  -0.0391 0.0211  1117 PRO B N   
3748 C CA  . PRO B 207 ? 0.3663 0.8007 0.4124 0.0150  -0.0401 0.0042  1117 PRO B CA  
3749 C C   . PRO B 207 ? 0.3774 0.7958 0.3964 0.0085  -0.0463 -0.0209 1117 PRO B C   
3750 O O   . PRO B 207 ? 0.3616 0.7882 0.3479 0.0040  -0.0539 -0.0243 1117 PRO B O   
3751 C CB  . PRO B 207 ? 0.3260 0.7679 0.4203 0.0126  -0.0495 0.0222  1117 PRO B CB  
3752 C CG  . PRO B 207 ? 0.3299 0.7901 0.4059 0.0134  -0.0625 0.0414  1117 PRO B CG  
3753 C CD  . PRO B 207 ? 0.4027 0.8685 0.4319 0.0151  -0.0523 0.0464  1117 PRO B CD  
3754 N N   . ASN B 208 ? 0.3376 0.7304 0.3667 0.0062  -0.0419 -0.0396 1118 ASN B N   
3755 C CA  . ASN B 208 ? 0.3849 0.7541 0.3882 -0.0049 -0.0436 -0.0648 1118 ASN B CA  
3756 C C   . ASN B 208 ? 0.3366 0.6999 0.3794 -0.0154 -0.0463 -0.0734 1118 ASN B C   
3757 O O   . ASN B 208 ? 0.3274 0.6721 0.3517 -0.0295 -0.0450 -0.0955 1118 ASN B O   
3758 C CB  . ASN B 208 ? 0.4059 0.7351 0.3611 0.0016  -0.0322 -0.0843 1118 ASN B CB  
3759 C CG  . ASN B 208 ? 0.4353 0.7496 0.4115 0.0132  -0.0250 -0.0843 1118 ASN B CG  
3760 O OD1 . ASN B 208 ? 0.4019 0.7395 0.4272 0.0155  -0.0262 -0.0678 1118 ASN B OD1 
3761 N ND2 . ASN B 208 ? 0.4694 0.7421 0.4057 0.0212  -0.0186 -0.1031 1118 ASN B ND2 
3762 N N   . ILE B 209 ? 0.2319 0.4977 0.6859 0.0084  0.0098  -0.1020 1119 ILE B N   
3763 C CA  . ILE B 209 ? 0.2219 0.4689 0.6752 0.0049  0.0061  -0.0925 1119 ILE B CA  
3764 C C   . ILE B 209 ? 0.2450 0.4991 0.6836 0.0018  0.0052  -0.0811 1119 ILE B C   
3765 O O   . ILE B 209 ? 0.2681 0.5357 0.6980 0.0014  0.0092  -0.0757 1119 ILE B O   
3766 C CB  . ILE B 209 ? 0.1990 0.4295 0.6592 0.0051  0.0061  -0.0838 1119 ILE B CB  
3767 C CG1 . ILE B 209 ? 0.2362 0.4758 0.6924 0.0017  0.0078  -0.0731 1119 ILE B CG1 
3768 C CG2 . ILE B 209 ? 0.2629 0.4888 0.7343 0.0119  0.0084  -0.0927 1119 ILE B CG2 
3769 C CD1 . ILE B 209 ? 0.1951 0.4264 0.6595 0.0032  0.0066  -0.0685 1119 ILE B CD1 
3770 N N   . ILE B 210 ? 0.2292 0.4731 0.6648 0.0002  0.0011  -0.0770 1120 ILE B N   
3771 C CA  . ILE B 210 ? 0.2114 0.4582 0.6319 -0.0003 0.0005  -0.0648 1120 ILE B CA  
3772 C C   . ILE B 210 ? 0.2708 0.4970 0.6925 -0.0037 -0.0016 -0.0534 1120 ILE B C   
3773 O O   . ILE B 210 ? 0.2331 0.4459 0.6652 -0.0045 -0.0042 -0.0572 1120 ILE B O   
3774 C CB  . ILE B 210 ? 0.2714 0.5338 0.6834 0.0042  -0.0033 -0.0722 1120 ILE B CB  
3775 C CG1 . ILE B 210 ? 0.2166 0.4719 0.6414 0.0029  -0.0083 -0.0832 1120 ILE B CG1 
3776 C CG2 . ILE B 210 ? 0.2869 0.5730 0.6937 0.0087  -0.0012 -0.0831 1120 ILE B CG2 
3777 C CD1 . ILE B 210 ? 0.2522 0.5286 0.6730 0.0070  -0.0130 -0.0950 1120 ILE B CD1 
3778 N N   . PRO B 211 ? 0.2548 0.4767 0.6654 -0.0053 0.0008  -0.0393 1121 PRO B N   
3779 C CA  . PRO B 211 ? 0.2513 0.4543 0.6624 -0.0080 -0.0012 -0.0297 1121 PRO B CA  
3780 C C   . PRO B 211 ? 0.2614 0.4633 0.6641 -0.0042 -0.0053 -0.0271 1121 PRO B C   
3781 O O   . PRO B 211 ? 0.3062 0.5209 0.6956 0.0011  -0.0051 -0.0252 1121 PRO B O   
3782 C CB  . PRO B 211 ? 0.2661 0.4649 0.6713 -0.0123 0.0053  -0.0180 1121 PRO B CB  
3783 C CG  . PRO B 211 ? 0.2595 0.4747 0.6528 -0.0095 0.0107  -0.0167 1121 PRO B CG  
3784 C CD  . PRO B 211 ? 0.2431 0.4753 0.6408 -0.0050 0.0073  -0.0315 1121 PRO B CD  
3785 N N   . VAL B 212 ? 0.2488 0.4369 0.6586 -0.0055 -0.0090 -0.0269 1122 VAL B N   
3786 C CA  . VAL B 212 ? 0.2444 0.4324 0.6497 -0.0020 -0.0131 -0.0252 1122 VAL B CA  
3787 C C   . VAL B 212 ? 0.2586 0.4264 0.6625 -0.0040 -0.0129 -0.0139 1122 VAL B C   
3788 O O   . VAL B 212 ? 0.2354 0.3904 0.6483 -0.0081 -0.0123 -0.0137 1122 VAL B O   
3789 C CB  . VAL B 212 ? 0.2555 0.4497 0.6740 -0.0020 -0.0168 -0.0401 1122 VAL B CB  
3790 C CG1 . VAL B 212 ? 0.2817 0.4833 0.6971 0.0021  -0.0214 -0.0408 1122 VAL B CG1 
3791 C CG2 . VAL B 212 ? 0.2718 0.4841 0.6945 -0.0010 -0.0164 -0.0543 1122 VAL B CG2 
3792 N N   . ARG B 213 ? 0.2823 0.4480 0.6740 0.0004  -0.0134 -0.0049 1123 ARG B N   
3793 C CA  . ARG B 213 ? 0.3117 0.4586 0.7024 -0.0007 -0.0134 0.0040  1123 ARG B CA  
3794 C C   . ARG B 213 ? 0.2329 0.3789 0.6335 0.0002  -0.0182 -0.0026 1123 ARG B C   
3795 O O   . ARG B 213 ? 0.2574 0.4190 0.6601 0.0042  -0.0218 -0.0105 1123 ARG B O   
3796 C CB  . ARG B 213 ? 0.3078 0.4498 0.6813 0.0051  -0.0107 0.0168  1123 ARG B CB  
3797 C CG  . ARG B 213 ? 0.4294 0.5633 0.7951 0.0013  -0.0021 0.0259  1123 ARG B CG  
3798 C CD  . ARG B 213 ? 0.5121 0.6579 0.8610 0.0086  0.0021  0.0316  1123 ARG B CD  
3799 N NE  . ARG B 213 ? 0.5392 0.6747 0.8819 0.0034  0.0133  0.0411  1123 ARG B NE  
3800 C CZ  . ARG B 213 ? 0.5147 0.6591 0.8642 -0.0033 0.0177  0.0363  1123 ARG B CZ  
3801 N NH1 . ARG B 213 ? 0.4339 0.5957 0.7946 -0.0043 0.0118  0.0228  1123 ARG B NH1 
3802 N NH2 . ARG B 213 ? 0.4934 0.6286 0.8394 -0.0093 0.0296  0.0446  1123 ARG B NH2 
3803 N N   . VAL B 214 ? 0.2080 0.3378 0.6156 -0.0036 -0.0177 -0.0005 1124 VAL B N   
3804 C CA  . VAL B 214 ? 0.2274 0.3537 0.6453 -0.0039 -0.0195 -0.0061 1124 VAL B CA  
3805 C C   . VAL B 214 ? 0.2302 0.3402 0.6452 -0.0034 -0.0195 0.0021  1124 VAL B C   
3806 O O   . VAL B 214 ? 0.2163 0.3148 0.6267 -0.0053 -0.0178 0.0086  1124 VAL B O   
3807 C CB  . VAL B 214 ? 0.1812 0.3043 0.6111 -0.0075 -0.0173 -0.0138 1124 VAL B CB  
3808 C CG1 . VAL B 214 ? 0.1817 0.2988 0.6220 -0.0083 -0.0160 -0.0185 1124 VAL B CG1 
3809 C CG2 . VAL B 214 ? 0.2114 0.3495 0.6448 -0.0079 -0.0169 -0.0232 1124 VAL B CG2 
3810 N N   . PHE B 215 ? 0.2067 0.3176 0.6263 -0.0012 -0.0209 -0.0004 1125 PHE B N   
3811 C CA  . PHE B 215 ? 0.1777 0.2746 0.5962 -0.0002 -0.0205 0.0053  1125 PHE B CA  
3812 C C   . PHE B 215 ? 0.1724 0.2654 0.6024 -0.0023 -0.0181 0.0000  1125 PHE B C   
3813 O O   . PHE B 215 ? 0.1733 0.2767 0.6138 -0.0038 -0.0171 -0.0089 1125 PHE B O   
3814 C CB  . PHE B 215 ? 0.1843 0.2847 0.5958 0.0061  -0.0228 0.0095  1125 PHE B CB  
3815 C CG  . PHE B 215 ? 0.2489 0.3425 0.6462 0.0090  -0.0219 0.0191  1125 PHE B CG  
3816 C CD1 . PHE B 215 ? 0.2076 0.2822 0.6004 0.0063  -0.0191 0.0256  1125 PHE B CD1 
3817 C CD2 . PHE B 215 ? 0.2341 0.3401 0.6225 0.0143  -0.0227 0.0209  1125 PHE B CD2 
3818 C CE1 . PHE B 215 ? 0.2133 0.2786 0.5954 0.0071  -0.0155 0.0337  1125 PHE B CE1 
3819 C CE2 . PHE B 215 ? 0.2595 0.3551 0.6337 0.0170  -0.0188 0.0316  1125 PHE B CE2 
3820 C CZ  . PHE B 215 ? 0.2242 0.2980 0.5964 0.0124  -0.0144 0.0380  1125 PHE B CZ  
3821 N N   . MET B 216 ? 0.1816 0.2597 0.6095 -0.0023 -0.0163 0.0048  1126 MET B N   
3822 C CA  . MET B 216 ? 0.1720 0.2431 0.6075 -0.0028 -0.0117 0.0025  1126 MET B CA  
3823 C C   . MET B 216 ? 0.2040 0.2650 0.6349 0.0002  -0.0109 0.0080  1126 MET B C   
3824 O O   . MET B 216 ? 0.2386 0.3033 0.6732 0.0013  -0.0101 0.0068  1126 MET B O   
3825 C CB  . MET B 216 ? 0.1731 0.2371 0.6091 -0.0030 -0.0090 0.0024  1126 MET B CB  
3826 C CG  . MET B 216 ? 0.1725 0.2442 0.6163 -0.0057 -0.0073 -0.0051 1126 MET B CG  
3827 S SD  . MET B 216 ? 0.1761 0.2448 0.6159 -0.0034 -0.0076 -0.0038 1126 MET B SD  
3828 C CE  . MET B 216 ? 0.1702 0.2494 0.6023 -0.0056 -0.0134 -0.0010 1126 MET B CE  
3829 N N   . LEU B 217 ? 0.2037 0.2545 0.6270 0.0023  -0.0113 0.0126  1127 LEU B N   
3830 C CA  . LEU B 217 ? 0.1999 0.2422 0.6185 0.0059  -0.0100 0.0162  1127 LEU B CA  
3831 C C   . LEU B 217 ? 0.2167 0.2576 0.6292 0.0072  -0.0137 0.0186  1127 LEU B C   
3832 O O   . LEU B 217 ? 0.2174 0.2527 0.6267 0.0106  -0.0127 0.0203  1127 LEU B O   
3833 C CB  . LEU B 217 ? 0.1857 0.2206 0.5982 0.0097  -0.0090 0.0184  1127 LEU B CB  
3834 C CG  . LEU B 217 ? 0.2190 0.2472 0.6336 0.0129  -0.0016 0.0199  1127 LEU B CG  
3835 C CD1 . LEU B 217 ? 0.2140 0.2451 0.6392 0.0086  0.0022  0.0157  1127 LEU B CD1 
3836 C CD2 . LEU B 217 ? 0.3340 0.3572 0.7392 0.0205  -0.0014 0.0231  1127 LEU B CD2 
3837 N N   . HIS B 218 ? 0.1901 0.2345 0.6001 0.0053  -0.0166 0.0192  1128 HIS B N   
3838 C CA  . HIS B 218 ? 0.2072 0.2472 0.6108 0.0077  -0.0180 0.0229  1128 HIS B CA  
3839 C C   . HIS B 218 ? 0.2211 0.2710 0.6239 0.0085  -0.0192 0.0237  1128 HIS B C   
3840 O O   . HIS B 218 ? 0.1988 0.2593 0.6063 0.0059  -0.0195 0.0200  1128 HIS B O   
3841 C CB  . HIS B 218 ? 0.2541 0.2828 0.6518 0.0055  -0.0179 0.0243  1128 HIS B CB  
3842 C CG  . HIS B 218 ? 0.1979 0.2295 0.5959 0.0001  -0.0175 0.0240  1128 HIS B CG  
3843 N ND1 . HIS B 218 ? 0.2049 0.2364 0.5985 -0.0003 -0.0158 0.0282  1128 HIS B ND1 
3844 C CD2 . HIS B 218 ? 0.2428 0.2789 0.6446 -0.0040 -0.0179 0.0200  1128 HIS B CD2 
3845 C CE1 . HIS B 218 ? 0.2622 0.2972 0.6577 -0.0060 -0.0143 0.0268  1128 HIS B CE1 
3846 N NE2 . HIS B 218 ? 0.2035 0.2426 0.6051 -0.0084 -0.0160 0.0211  1128 HIS B NE2 
3847 N N   . GLN B 219 ? 0.2422 0.2885 0.6377 0.0138  -0.0196 0.0285  1129 GLN B N   
3848 C CA  . GLN B 219 ? 0.2661 0.3219 0.6560 0.0187  -0.0207 0.0314  1129 GLN B CA  
3849 C C   . GLN B 219 ? 0.2409 0.2805 0.6180 0.0217  -0.0175 0.0405  1129 GLN B C   
3850 O O   . GLN B 219 ? 0.2385 0.2802 0.6061 0.0306  -0.0173 0.0464  1129 GLN B O   
3851 C CB  . GLN B 219 ? 0.2268 0.2987 0.6208 0.0262  -0.0238 0.0280  1129 GLN B CB  
3852 C CG  . GLN B 219 ? 0.1940 0.2849 0.6024 0.0216  -0.0250 0.0173  1129 GLN B CG  
3853 C CD  . GLN B 219 ? 0.2402 0.3463 0.6593 0.0252  -0.0261 0.0105  1129 GLN B CD  
3854 O OE1 . GLN B 219 ? 0.1982 0.3058 0.6125 0.0338  -0.0278 0.0138  1129 GLN B OE1 
3855 N NE2 . GLN B 219 ? 0.1821 0.2994 0.6170 0.0185  -0.0241 0.0002  1129 GLN B NE2 
3856 N N   . ASP B 220 ? 0.2577 0.2813 0.6346 0.0148  -0.0141 0.0412  1130 ASP B N   
3857 C CA  . ASP B 220 ? 0.2538 0.2592 0.6218 0.0139  -0.0081 0.0482  1130 ASP B CA  
3858 C C   . ASP B 220 ? 0.2622 0.2739 0.6256 0.0120  -0.0050 0.0520  1130 ASP B C   
3859 O O   . ASP B 220 ? 0.3013 0.3207 0.6718 0.0037  -0.0049 0.0469  1130 ASP B O   
3860 C CB  . ASP B 220 ? 0.2530 0.2453 0.6267 0.0051  -0.0056 0.0434  1130 ASP B CB  
3861 C CG  . ASP B 220 ? 0.3064 0.2767 0.6746 0.0021  0.0028  0.0483  1130 ASP B CG  
3862 O OD1 . ASP B 220 ? 0.2851 0.2508 0.6456 0.0032  0.0087  0.0563  1130 ASP B OD1 
3863 O OD2 . ASP B 220 ? 0.3083 0.2650 0.6796 -0.0010 0.0047  0.0439  1130 ASP B OD2 
3864 N N   . LEU B 221 ? 0.2708 0.2796 0.6211 0.0211  -0.0019 0.0614  1131 LEU B N   
3865 C CA  . LEU B 221 ? 0.2769 0.2964 0.6199 0.0226  0.0005  0.0654  1131 LEU B CA  
3866 C C   . LEU B 221 ? 0.3727 0.3800 0.7156 0.0121  0.0097  0.0682  1131 LEU B C   
3867 O O   . LEU B 221 ? 0.4219 0.4406 0.7612 0.0112  0.0120  0.0696  1131 LEU B O   
3868 C CB  . LEU B 221 ? 0.2983 0.3183 0.6238 0.0382  0.0018  0.0759  1131 LEU B CB  
3869 C CG  . LEU B 221 ? 0.3665 0.4060 0.6938 0.0496  -0.0077 0.0711  1131 LEU B CG  
3870 C CD1 . LEU B 221 ? 0.3125 0.3601 0.6210 0.0678  -0.0077 0.0806  1131 LEU B CD1 
3871 C CD2 . LEU B 221 ? 0.2731 0.3388 0.6161 0.0433  -0.0154 0.0570  1131 LEU B CD2 
3872 N N   . ARG B 222 ? 0.3619 0.3481 0.7096 0.0041  0.0156  0.0679  1132 ARG B N   
3873 C CA  . ARG B 222 ? 0.4369 0.4158 0.7900 -0.0084 0.0247  0.0669  1132 ARG B CA  
3874 C C   . ARG B 222 ? 0.4401 0.4393 0.8086 -0.0178 0.0190  0.0546  1132 ARG B C   
3875 O O   . ARG B 222 ? 0.4992 0.5001 0.8744 -0.0277 0.0253  0.0517  1132 ARG B O   
3876 C CB  . ARG B 222 ? 0.4192 0.3727 0.7768 -0.0158 0.0325  0.0659  1132 ARG B CB  
3877 C CG  . ARG B 222 ? 0.4694 0.3967 0.8128 -0.0064 0.0398  0.0777  1132 ARG B CG  
3878 C CD  . ARG B 222 ? 0.3950 0.3003 0.7473 -0.0145 0.0448  0.0712  1132 ARG B CD  
3879 N NE  . ARG B 222 ? 0.3310 0.2503 0.6945 -0.0159 0.0326  0.0583  1132 ARG B NE  
3880 C CZ  . ARG B 222 ? 0.3438 0.2560 0.7186 -0.0244 0.0329  0.0469  1132 ARG B CZ  
3881 N NH1 . ARG B 222 ? 0.3891 0.2810 0.7696 -0.0348 0.0447  0.0441  1132 ARG B NH1 
3882 N NH2 . ARG B 222 ? 0.3105 0.2368 0.6914 -0.0223 0.0220  0.0374  1132 ARG B NH2 
3883 N N   . PHE B 223 ? 0.3300 0.3437 0.7044 -0.0144 0.0085  0.0473  1133 PHE B N   
3884 C CA  . PHE B 223 ? 0.2991 0.3281 0.6865 -0.0205 0.0035  0.0367  1133 PHE B CA  
3885 C C   . PHE B 223 ? 0.2831 0.3299 0.6717 -0.0150 -0.0032 0.0336  1133 PHE B C   
3886 O O   . PHE B 223 ? 0.2602 0.3118 0.6554 -0.0136 -0.0088 0.0278  1133 PHE B O   
3887 C CB  . PHE B 223 ? 0.2766 0.3001 0.6717 -0.0230 -0.0001 0.0297  1133 PHE B CB  
3888 C CG  . PHE B 223 ? 0.3133 0.3222 0.7113 -0.0305 0.0064  0.0282  1133 PHE B CG  
3889 C CD1 . PHE B 223 ? 0.3250 0.3389 0.7317 -0.0406 0.0119  0.0233  1133 PHE B CD1 
3890 C CD2 . PHE B 223 ? 0.3663 0.3568 0.7599 -0.0280 0.0083  0.0305  1133 PHE B CD2 
3891 C CE1 . PHE B 223 ? 0.3587 0.3597 0.7717 -0.0498 0.0196  0.0194  1133 PHE B CE1 
3892 C CE2 . PHE B 223 ? 0.3974 0.3725 0.7957 -0.0363 0.0158  0.0270  1133 PHE B CE2 
3893 C CZ  . PHE B 223 ? 0.3495 0.3300 0.7584 -0.0481 0.0218  0.0209  1133 PHE B CZ  
3894 N N   . PRO B 224 ? 0.3072 0.3641 0.6896 -0.0118 -0.0018 0.0367  1134 PRO B N   
3895 C CA  . PRO B 224 ? 0.2439 0.3192 0.6315 -0.0095 -0.0071 0.0296  1134 PRO B CA  
3896 C C   . PRO B 224 ? 0.2446 0.3259 0.6431 -0.0160 -0.0072 0.0222  1134 PRO B C   
3897 O O   . PRO B 224 ? 0.2126 0.2905 0.6141 -0.0223 -0.0030 0.0222  1134 PRO B O   
3898 C CB  . PRO B 224 ? 0.2564 0.3424 0.6336 -0.0048 -0.0048 0.0335  1134 PRO B CB  
3899 C CG  . PRO B 224 ? 0.3217 0.3949 0.6912 -0.0084 0.0043  0.0424  1134 PRO B CG  
3900 C CD  . PRO B 224 ? 0.3194 0.3718 0.6904 -0.0110 0.0061  0.0456  1134 PRO B CD  
3901 N N   . ARG B 225 ? 0.2305 0.3208 0.6363 -0.0141 -0.0114 0.0151  1135 ARG B N   
3902 C CA  . ARG B 225 ? 0.1827 0.2797 0.5974 -0.0166 -0.0117 0.0085  1135 ARG B CA  
3903 C C   . ARG B 225 ? 0.2228 0.3344 0.6388 -0.0157 -0.0110 0.0039  1135 ARG B C   
3904 O O   . ARG B 225 ? 0.2291 0.3466 0.6426 -0.0124 -0.0124 0.0021  1135 ARG B O   
3905 C CB  . ARG B 225 ? 0.1756 0.2674 0.5959 -0.0135 -0.0148 0.0052  1135 ARG B CB  
3906 C CG  . ARG B 225 ? 0.1793 0.2605 0.5982 -0.0140 -0.0157 0.0078  1135 ARG B CG  
3907 C CD  . ARG B 225 ? 0.2116 0.2863 0.6317 -0.0089 -0.0175 0.0071  1135 ARG B CD  
3908 N NE  . ARG B 225 ? 0.1724 0.2511 0.5971 -0.0052 -0.0173 0.0033  1135 ARG B NE  
3909 C CZ  . ARG B 225 ? 0.1953 0.2666 0.6197 0.0005  -0.0163 0.0041  1135 ARG B CZ  
3910 N NH1 . ARG B 225 ? 0.2531 0.3150 0.6741 0.0021  -0.0157 0.0076  1135 ARG B NH1 
3911 N NH2 . ARG B 225 ? 0.1765 0.2488 0.6036 0.0054  -0.0146 0.0019  1135 ARG B NH2 
3912 N N   . ILE B 226 ? 0.1909 0.3107 0.6116 -0.0186 -0.0088 0.0005  1136 ILE B N   
3913 C CA  . ILE B 226 ? 0.1819 0.3162 0.6032 -0.0178 -0.0070 -0.0043 1136 ILE B CA  
3914 C C   . ILE B 226 ? 0.2007 0.3381 0.6308 -0.0144 -0.0094 -0.0129 1136 ILE B C   
3915 O O   . ILE B 226 ? 0.2181 0.3527 0.6545 -0.0131 -0.0101 -0.0149 1136 ILE B O   
3916 C CB  . ILE B 226 ? 0.2412 0.3839 0.6641 -0.0227 -0.0019 -0.0039 1136 ILE B CB  
3917 C CG1 . ILE B 226 ? 0.2823 0.4162 0.6968 -0.0270 0.0037  0.0056  1136 ILE B CG1 
3918 C CG2 . ILE B 226 ? 0.2352 0.3942 0.6575 -0.0210 0.0003  -0.0090 1136 ILE B CG2 
3919 C CD1 . ILE B 226 ? 0.2494 0.3808 0.6492 -0.0217 0.0045  0.0128  1136 ILE B CD1 
3920 N N   . ALA B 227 ? 0.1758 0.3195 0.6064 -0.0120 -0.0100 -0.0187 1137 ALA B N   
3921 C CA  . ALA B 227 ? 0.1763 0.3200 0.6162 -0.0094 -0.0097 -0.0279 1137 ALA B CA  
3922 C C   . ALA B 227 ? 0.1951 0.3548 0.6362 -0.0087 -0.0080 -0.0360 1137 ALA B C   
3923 O O   . ALA B 227 ? 0.2424 0.4143 0.6766 -0.0089 -0.0083 -0.0370 1137 ALA B O   
3924 C CB  . ALA B 227 ? 0.1947 0.3318 0.6384 -0.0090 -0.0105 -0.0315 1137 ALA B CB  
3925 N N   . PHE B 228 ? 0.1778 0.3382 0.6263 -0.0062 -0.0060 -0.0419 1138 PHE B N   
3926 C CA  . PHE B 228 ? 0.1818 0.3570 0.6329 -0.0046 -0.0040 -0.0514 1138 PHE B CA  
3927 C C   . PHE B 228 ? 0.1861 0.3563 0.6458 -0.0027 -0.0025 -0.0630 1138 PHE B C   
3928 O O   . PHE B 228 ? 0.2073 0.3603 0.6735 -0.0003 -0.0004 -0.0630 1138 PHE B O   
3929 C CB  . PHE B 228 ? 0.1892 0.3707 0.6444 -0.0022 -0.0020 -0.0519 1138 PHE B CB  
3930 C CG  . PHE B 228 ? 0.2183 0.4090 0.6690 -0.0065 -0.0011 -0.0445 1138 PHE B CG  
3931 C CD1 . PHE B 228 ? 0.2268 0.4311 0.6701 -0.0096 0.0020  -0.0433 1138 PHE B CD1 
3932 C CD2 . PHE B 228 ? 0.1955 0.3817 0.6495 -0.0073 -0.0022 -0.0395 1138 PHE B CD2 
3933 C CE1 . PHE B 228 ? 0.1877 0.3969 0.6280 -0.0149 0.0060  -0.0361 1138 PHE B CE1 
3934 C CE2 . PHE B 228 ? 0.1934 0.3874 0.6468 -0.0135 0.0003  -0.0351 1138 PHE B CE2 
3935 C CZ  . PHE B 228 ? 0.2485 0.4522 0.6957 -0.0180 0.0054  -0.0329 1138 PHE B CZ  
3936 N N   . PHE B 229 ? 0.2242 0.4093 0.6838 -0.0033 -0.0026 -0.0734 1139 PHE B N   
3937 C CA  . PHE B 229 ? 0.1969 0.3803 0.6674 -0.0032 -0.0003 -0.0888 1139 PHE B CA  
3938 C C   . PHE B 229 ? 0.2031 0.4037 0.6744 -0.0006 0.0014  -0.1004 1139 PHE B C   
3939 O O   . PHE B 229 ? 0.2029 0.4223 0.6639 0.0003  -0.0002 -0.0977 1139 PHE B O   
3940 C CB  . PHE B 229 ? 0.1975 0.3884 0.6699 -0.0068 -0.0031 -0.0961 1139 PHE B CB  
3941 C CG  . PHE B 229 ? 0.1931 0.3678 0.6679 -0.0094 -0.0035 -0.0882 1139 PHE B CG  
3942 C CD1 . PHE B 229 ? 0.2144 0.3896 0.6779 -0.0091 -0.0076 -0.0744 1139 PHE B CD1 
3943 C CD2 . PHE B 229 ? 0.2126 0.3703 0.7012 -0.0121 0.0017  -0.0948 1139 PHE B CD2 
3944 C CE1 . PHE B 229 ? 0.2492 0.4107 0.7147 -0.0109 -0.0079 -0.0678 1139 PHE B CE1 
3945 C CE2 . PHE B 229 ? 0.2376 0.3815 0.7283 -0.0145 0.0024  -0.0874 1139 PHE B CE2 
3946 C CZ  . PHE B 229 ? 0.2186 0.3657 0.6975 -0.0135 -0.0031 -0.0743 1139 PHE B CZ  
3947 N N   . SER B 230 ? 0.2114 0.4043 0.6946 0.0010  0.0059  -0.1134 1140 SER B N   
3948 C CA  . SER B 230 ? 0.2188 0.4282 0.7035 0.0040  0.0077  -0.1266 1140 SER B CA  
3949 C C   . SER B 230 ? 0.2449 0.4792 0.7251 0.0020  0.0039  -0.1382 1140 SER B C   
3950 O O   . SER B 230 ? 0.2445 0.4794 0.7311 -0.0019 0.0022  -0.1471 1140 SER B O   
3951 C CB  . SER B 230 ? 0.2310 0.4235 0.7298 0.0067  0.0145  -0.1391 1140 SER B CB  
3952 O OG  . SER B 230 ? 0.2363 0.4089 0.7459 0.0021  0.0180  -0.1440 1140 SER B OG  
3953 N N   . SER B 231 ? 0.2235 0.4806 0.6924 0.0053  0.0029  -0.1380 1141 SER B N   
3954 C CA  . SER B 231 ? 0.2304 0.5150 0.6917 0.0070  -0.0005 -0.1496 1141 SER B CA  
3955 C C   . SER B 231 ? 0.2610 0.5543 0.7348 0.0076  0.0015  -0.1745 1141 SER B C   
3956 O O   . SER B 231 ? 0.3109 0.6281 0.7821 0.0087  -0.0023 -0.1894 1141 SER B O   
3957 C CB  . SER B 231 ? 0.3087 0.6125 0.7517 0.0112  0.0003  -0.1390 1141 SER B CB  
3958 O OG  . SER B 231 ? 0.2353 0.5411 0.6820 0.0135  0.0056  -0.1415 1141 SER B OG  
3959 N N   . ARG B 232 ? 0.2450 0.5197 0.7317 0.0081  0.0075  -0.1801 1142 ARG B N   
3960 C CA  . ARG B 232 ? 0.2585 0.5367 0.7579 0.0090  0.0115  -0.2038 1142 ARG B CA  
3961 C C   . ARG B 232 ? 0.3061 0.5494 0.8207 0.0090  0.0192  -0.2036 1142 ARG B C   
3962 O O   . ARG B 232 ? 0.2567 0.4792 0.7692 0.0099  0.0202  -0.1848 1142 ARG B O   
3963 C CB  . ARG B 232 ? 0.2686 0.5713 0.7589 0.0157  0.0123  -0.2099 1142 ARG B CB  
3964 C CG  . ARG B 232 ? 0.2592 0.5568 0.7435 0.0204  0.0156  -0.1928 1142 ARG B CG  
3965 C CD  . ARG B 232 ? 0.2678 0.5907 0.7466 0.0265  0.0182  -0.2027 1142 ARG B CD  
3966 N NE  . ARG B 232 ? 0.3508 0.6800 0.8230 0.0298  0.0211  -0.1877 1142 ARG B NE  
3967 C CZ  . ARG B 232 ? 0.3475 0.6662 0.8294 0.0344  0.0252  -0.1866 1142 ARG B CZ  
3968 N NH1 . ARG B 232 ? 0.3645 0.6593 0.8604 0.0374  0.0278  -0.1952 1142 ARG B NH1 
3969 N NH2 . ARG B 232 ? 0.2646 0.5973 0.7424 0.0368  0.0277  -0.1766 1142 ARG B NH2 
3970 N N   . ASP B 233 ? 0.3562 0.5928 0.8856 0.0087  0.0253  -0.2249 1143 ASP B N   
3971 C CA  . ASP B 233 ? 0.3300 0.5322 0.8705 0.0124  0.0348  -0.2237 1143 ASP B CA  
3972 C C   . ASP B 233 ? 0.3715 0.5767 0.9025 0.0229  0.0349  -0.2107 1143 ASP B C   
3973 O O   . ASP B 233 ? 0.3973 0.6312 0.9196 0.0261  0.0314  -0.2138 1143 ASP B O   
3974 C CB  . ASP B 233 ? 0.3198 0.5138 0.8779 0.0105  0.0429  -0.2506 1143 ASP B CB  
3975 C CG  . ASP B 233 ? 0.3921 0.5814 0.9656 -0.0016 0.0449  -0.2661 1143 ASP B CG  
3976 O OD1 . ASP B 233 ? 0.3464 0.5375 0.9165 -0.0073 0.0399  -0.2546 1143 ASP B OD1 
3977 O OD2 . ASP B 233 ? 0.4023 0.5869 0.9930 -0.0058 0.0520  -0.2914 1143 ASP B OD2 
3978 N N   . ILE B 234 ? 0.3863 0.5642 0.9185 0.0290  0.0392  -0.1961 1144 ILE B N   
3979 C CA  . ILE B 234 ? 0.3234 0.5076 0.8487 0.0395  0.0382  -0.1841 1144 ILE B CA  
3980 C C   . ILE B 234 ? 0.3478 0.5051 0.8811 0.0511  0.0472  -0.1870 1144 ILE B C   
3981 O O   . ILE B 234 ? 0.3553 0.4793 0.8931 0.0526  0.0533  -0.1815 1144 ILE B O   
3982 C CB  . ILE B 234 ? 0.3038 0.4881 0.8194 0.0387  0.0324  -0.1615 1144 ILE B CB  
3983 C CG1 . ILE B 234 ? 0.2541 0.4609 0.7606 0.0286  0.0252  -0.1577 1144 ILE B CG1 
3984 C CG2 . ILE B 234 ? 0.3759 0.5724 0.8879 0.0485  0.0312  -0.1529 1144 ILE B CG2 
3985 C CD1 . ILE B 234 ? 0.2488 0.4544 0.7468 0.0266  0.0204  -0.1374 1144 ILE B CD1 
3986 N N   . ARG B 235 ? 0.3407 0.5119 0.8750 0.0605  0.0489  -0.1948 1145 ARG B N   
3987 C CA  . ARG B 235 ? 0.3426 0.4901 0.8832 0.0747  0.0576  -0.1977 1145 ARG B CA  
3988 C C   . ARG B 235 ? 0.3740 0.5121 0.9082 0.0868  0.0559  -0.1769 1145 ARG B C   
3989 O O   . ARG B 235 ? 0.4022 0.5592 0.9290 0.0837  0.0476  -0.1636 1145 ARG B O   
3990 C CB  . ARG B 235 ? 0.3818 0.5511 0.9254 0.0822  0.0593  -0.2133 1145 ARG B CB  
3991 C CG  . ARG B 235 ? 0.3819 0.5570 0.9332 0.0749  0.0630  -0.2385 1145 ARG B CG  
3992 C CD  . ARG B 235 ? 0.5005 0.6960 1.0535 0.0852  0.0653  -0.2521 1145 ARG B CD  
3993 N NE  . ARG B 235 ? 0.5538 0.7475 1.1165 0.0823  0.0712  -0.2789 1145 ARG B NE  
3994 C CZ  . ARG B 235 ? 0.5730 0.7754 1.1398 0.0922  0.0760  -0.2947 1145 ARG B CZ  
3995 N NH1 . ARG B 235 ? 0.5847 0.7989 1.1477 0.1063  0.0759  -0.2861 1145 ARG B NH1 
3996 N NH2 . ARG B 235 ? 0.7008 0.9023 1.2772 0.0880  0.0810  -0.3214 1145 ARG B NH2 
3997 N N   . THR B 236 ? 0.3586 0.4676 0.8956 0.1018  0.0643  -0.1749 1146 THR B N   
3998 C CA  . THR B 236 ? 0.3609 0.4631 0.8904 0.1173  0.0625  -0.1566 1146 THR B CA  
3999 C C   . THR B 236 ? 0.3999 0.5400 0.9283 0.1268  0.0555  -0.1569 1146 THR B C   
4000 O O   . THR B 236 ? 0.3566 0.5118 0.8906 0.1315  0.0580  -0.1708 1146 THR B O   
4001 C CB  . THR B 236 ? 0.3955 0.4548 0.9257 0.1337  0.0749  -0.1534 1146 THR B CB  
4002 O OG1 . THR B 236 ? 0.5063 0.5310 1.0409 0.1220  0.0839  -0.1555 1146 THR B OG1 
4003 C CG2 . THR B 236 ? 0.4005 0.4534 0.9198 0.1517  0.0723  -0.1334 1146 THR B CG2 
4004 N N   . GLY B 237 ? 0.4197 0.5771 0.9424 0.1291  0.0472  -0.1429 1147 GLY B N   
4005 C CA  . GLY B 237 ? 0.4176 0.6140 0.9424 0.1354  0.0410  -0.1439 1147 GLY B CA  
4006 C C   . GLY B 237 ? 0.3717 0.6030 0.8978 0.1175  0.0357  -0.1481 1147 GLY B C   
4007 O O   . GLY B 237 ? 0.3457 0.6106 0.8753 0.1195  0.0320  -0.1485 1147 GLY B O   
4008 N N   . GLU B 238 ? 0.2899 0.5152 0.8133 0.1009  0.0361  -0.1510 1148 GLU B N   
4009 C CA  . GLU B 238 ? 0.2741 0.5298 0.7957 0.0871  0.0334  -0.1551 1148 GLU B CA  
4010 C C   . GLU B 238 ? 0.3039 0.5696 0.8203 0.0763  0.0274  -0.1411 1148 GLU B C   
4011 O O   . GLU B 238 ? 0.2568 0.5017 0.7697 0.0747  0.0247  -0.1306 1148 GLU B O   
4012 C CB  . GLU B 238 ? 0.3140 0.5625 0.8341 0.0774  0.0362  -0.1667 1148 GLU B CB  
4013 C CG  . GLU B 238 ? 0.3419 0.6194 0.8554 0.0652  0.0338  -0.1691 1148 GLU B CG  
4014 C CD  . GLU B 238 ? 0.3784 0.6491 0.8887 0.0563  0.0337  -0.1783 1148 GLU B CD  
4015 O OE1 . GLU B 238 ? 0.3549 0.6014 0.8722 0.0584  0.0372  -0.1879 1148 GLU B OE1 
4016 O OE2 . GLU B 238 ? 0.3513 0.6412 0.8523 0.0477  0.0308  -0.1762 1148 GLU B OE2 
4017 N N   . GLU B 239 ? 0.2440 0.5408 0.7601 0.0691  0.0266  -0.1411 1149 GLU B N   
4018 C CA  . GLU B 239 ? 0.2294 0.5363 0.7435 0.0600  0.0228  -0.1292 1149 GLU B CA  
4019 C C   . GLU B 239 ? 0.2485 0.5431 0.7527 0.0466  0.0212  -0.1221 1149 GLU B C   
4020 O O   . GLU B 239 ? 0.2432 0.5453 0.7412 0.0403  0.0234  -0.1265 1149 GLU B O   
4021 C CB  . GLU B 239 ? 0.2470 0.5892 0.7663 0.0560  0.0254  -0.1317 1149 GLU B CB  
4022 C CG  . GLU B 239 ? 0.2353 0.5854 0.7534 0.0430  0.0242  -0.1210 1149 GLU B CG  
4023 C CD  . GLU B 239 ? 0.2180 0.5980 0.7460 0.0415  0.0264  -0.1232 1149 GLU B CD  
4024 O OE1 . GLU B 239 ? 0.2530 0.6521 0.7841 0.0467  0.0306  -0.1318 1149 GLU B OE1 
4025 O OE2 . GLU B 239 ? 0.2055 0.5866 0.7335 0.0344  0.0240  -0.1163 1149 GLU B OE2 
4026 N N   . LEU B 240 ? 0.2177 0.4958 0.7195 0.0439  0.0171  -0.1113 1150 LEU B N   
4027 C CA  . LEU B 240 ? 0.2427 0.5125 0.7357 0.0320  0.0152  -0.1032 1150 LEU B CA  
4028 C C   . LEU B 240 ? 0.2434 0.5342 0.7336 0.0223  0.0170  -0.0977 1150 LEU B C   
4029 O O   . LEU B 240 ? 0.2218 0.5288 0.7197 0.0221  0.0179  -0.0970 1150 LEU B O   
4030 C CB  . LEU B 240 ? 0.2054 0.4518 0.6968 0.0327  0.0111  -0.0937 1150 LEU B CB  
4031 C CG  . LEU B 240 ? 0.2856 0.5066 0.7792 0.0423  0.0122  -0.0962 1150 LEU B CG  
4032 C CD1 . LEU B 240 ? 0.2716 0.4705 0.7607 0.0404  0.0095  -0.0855 1150 LEU B CD1 
4033 C CD2 . LEU B 240 ? 0.2619 0.4758 0.7567 0.0412  0.0162  -0.1077 1150 LEU B CD2 
4034 N N   . GLY B 241 ? 0.2438 0.5347 0.7234 0.0145  0.0184  -0.0943 1151 GLY B N   
4035 C CA  . GLY B 241 ? 0.2176 0.5212 0.6919 0.0055  0.0226  -0.0863 1151 GLY B CA  
4036 C C   . GLY B 241 ? 0.2065 0.5026 0.6657 0.0010  0.0226  -0.0799 1151 GLY B C   
4037 O O   . GLY B 241 ? 0.2242 0.5178 0.6786 0.0050  0.0202  -0.0869 1151 GLY B O   
4038 N N   . PHE B 242 ? 0.2200 0.5127 0.6724 -0.0066 0.0254  -0.0678 1152 PHE B N   
4039 C CA  . PHE B 242 ? 0.2152 0.5022 0.6509 -0.0083 0.0260  -0.0598 1152 PHE B CA  
4040 C C   . PHE B 242 ? 0.2296 0.5280 0.6559 -0.0130 0.0364  -0.0513 1152 PHE B C   
4041 O O   . PHE B 242 ? 0.2269 0.5336 0.6630 -0.0186 0.0430  -0.0505 1152 PHE B O   
4042 C CB  . PHE B 242 ? 0.2365 0.5012 0.6699 -0.0112 0.0208  -0.0508 1152 PHE B CB  
4043 C CG  . PHE B 242 ? 0.2271 0.4843 0.6668 -0.0184 0.0234  -0.0427 1152 PHE B CG  
4044 C CD1 . PHE B 242 ? 0.2518 0.5104 0.7069 -0.0182 0.0205  -0.0481 1152 PHE B CD1 
4045 C CD2 . PHE B 242 ? 0.2136 0.4628 0.6437 -0.0244 0.0289  -0.0306 1152 PHE B CD2 
4046 C CE1 . PHE B 242 ? 0.1938 0.4499 0.6563 -0.0250 0.0220  -0.0440 1152 PHE B CE1 
4047 C CE2 . PHE B 242 ? 0.2657 0.5078 0.7039 -0.0326 0.0320  -0.0259 1152 PHE B CE2 
4048 C CZ  . PHE B 242 ? 0.2017 0.4492 0.6569 -0.0335 0.0280  -0.0339 1152 PHE B CZ  
4049 N N   . ASP B 243 ? 0.2393 0.5395 0.6466 -0.0099 0.0386  -0.0453 1153 ASP B N   
4050 C CA  . ASP B 243 ? 0.2868 0.5930 0.6804 -0.0126 0.0508  -0.0337 1153 ASP B CA  
4051 C C   . ASP B 243 ? 0.2770 0.5629 0.6709 -0.0212 0.0556  -0.0196 1153 ASP B C   
4052 O O   . ASP B 243 ? 0.3494 0.6185 0.7322 -0.0191 0.0521  -0.0107 1153 ASP B O   
4053 C CB  . ASP B 243 ? 0.2738 0.5882 0.6437 -0.0032 0.0511  -0.0307 1153 ASP B CB  
4054 C CG  . ASP B 243 ? 0.3127 0.6354 0.6654 -0.0030 0.0661  -0.0185 1153 ASP B CG  
4055 O OD1 . ASP B 243 ? 0.3024 0.6203 0.6628 -0.0127 0.0776  -0.0112 1153 ASP B OD1 
4056 O OD2 . ASP B 243 ? 0.4151 0.7500 0.7463 0.0073  0.0672  -0.0166 1153 ASP B OD2 
4057 N N   . TYR B 244 ? 0.2594 0.5483 0.6679 -0.0308 0.0638  -0.0194 1154 TYR B N   
4058 C CA  . TYR B 244 ? 0.3145 0.5862 0.7266 -0.0412 0.0711  -0.0090 1154 TYR B CA  
4059 C C   . TYR B 244 ? 0.3008 0.5582 0.6897 -0.0402 0.0818  0.0082  1154 TYR B C   
4060 O O   . TYR B 244 ? 0.3695 0.6045 0.7559 -0.0452 0.0850  0.0182  1154 TYR B O   
4061 C CB  . TYR B 244 ? 0.2723 0.5575 0.7047 -0.0525 0.0811  -0.0145 1154 TYR B CB  
4062 C CG  . TYR B 244 ? 0.2468 0.5419 0.7039 -0.0545 0.0716  -0.0286 1154 TYR B CG  
4063 C CD1 . TYR B 244 ? 0.2280 0.5205 0.6873 -0.0450 0.0565  -0.0359 1154 TYR B CD1 
4064 C CD2 . TYR B 244 ? 0.2506 0.5582 0.7287 -0.0655 0.0788  -0.0347 1154 TYR B CD2 
4065 C CE1 . TYR B 244 ? 0.2137 0.5144 0.6916 -0.0437 0.0488  -0.0465 1154 TYR B CE1 
4066 C CE2 . TYR B 244 ? 0.2417 0.5624 0.7404 -0.0645 0.0693  -0.0478 1154 TYR B CE2 
4067 C CZ  . TYR B 244 ? 0.2391 0.5556 0.7359 -0.0523 0.0543  -0.0525 1154 TYR B CZ  
4068 O OH  . TYR B 244 ? 0.2013 0.5304 0.7155 -0.0484 0.0457  -0.0637 1154 TYR B OH  
4069 N N   . GLY B 245 ? 0.3069 0.5767 0.6778 -0.0328 0.0883  0.0121  1155 GLY B N   
4070 C CA  . GLY B 245 ? 0.3498 0.6072 0.6940 -0.0273 0.0985  0.0300  1155 GLY B CA  
4071 C C   . GLY B 245 ? 0.4203 0.6796 0.7599 -0.0341 0.1201  0.0398  1155 GLY B C   
4072 O O   . GLY B 245 ? 0.4808 0.7530 0.8411 -0.0450 0.1272  0.0313  1155 GLY B O   
4073 N N   . ASP B 246 ? 0.4096 0.6567 0.7210 -0.0264 0.1316  0.0582  1156 ASP B N   
4074 C CA  . ASP B 246 ? 0.4822 0.7260 0.7842 -0.0315 0.1557  0.0714  1156 ASP B CA  
4075 C C   . ASP B 246 ? 0.5231 0.7371 0.8357 -0.0470 0.1715  0.0819  1156 ASP B C   
4076 O O   . ASP B 246 ? 0.5803 0.7912 0.8952 -0.0570 0.1938  0.0892  1156 ASP B O   
4077 C CB  . ASP B 246 ? 0.5463 0.7897 0.8090 -0.0135 0.1632  0.0884  1156 ASP B CB  
4078 C CG  . ASP B 246 ? 0.5909 0.8693 0.8432 -0.0012 0.1567  0.0775  1156 ASP B CG  
4079 O OD1 . ASP B 246 ? 0.5986 0.8985 0.8734 -0.0052 0.1440  0.0566  1156 ASP B OD1 
4080 O OD2 . ASP B 246 ? 0.6169 0.9011 0.8370 0.0137  0.1648  0.0901  1156 ASP B OD2 
4081 N N   . ARG B 247 ? 0.5373 0.7291 0.8567 -0.0497 0.1621  0.0825  1157 ARG B N   
4082 C CA  . ARG B 247 ? 0.5672 0.7317 0.9004 -0.0659 0.1766  0.0885  1157 ARG B CA  
4083 C C   . ARG B 247 ? 0.5817 0.7630 0.9528 -0.0846 0.1769  0.0693  1157 ARG B C   
4084 O O   . ARG B 247 ? 0.6117 0.7847 0.9980 -0.1010 0.1962  0.0705  1157 ARG B O   
4085 C CB  . ARG B 247 ? 0.6053 0.7427 0.9345 -0.0622 0.1661  0.0933  1157 ARG B CB  
4086 C CG  . ARG B 247 ? 0.6307 0.7360 0.9704 -0.0775 0.1832  0.1003  1157 ARG B CG  
4087 C CD  . ARG B 247 ? 0.6128 0.6975 0.9584 -0.0773 0.1701  0.0977  1157 ARG B CD  
4088 N NE  . ARG B 247 ? 0.6492 0.7003 1.0016 -0.0906 0.1888  0.1051  1157 ARG B NE  
4089 C CZ  . ARG B 247 ? 0.6475 0.6796 1.0121 -0.0964 0.1827  0.0999  1157 ARG B CZ  
4090 N NH1 . ARG B 247 ? 0.6493 0.6923 1.0199 -0.0900 0.1589  0.0887  1157 ARG B NH1 
4091 N NH2 . ARG B 247 ? 0.6285 0.6291 0.9998 -0.1092 0.2023  0.1056  1157 ARG B NH2 
4092 N N   . PHE B 248 ? 0.5388 0.7442 0.9260 -0.0817 0.1562  0.0510  1158 PHE B N   
4093 C CA  . PHE B 248 ? 0.5280 0.7550 0.9491 -0.0950 0.1543  0.0321  1158 PHE B CA  
4094 C C   . PHE B 248 ? 0.5430 0.7920 0.9716 -0.1021 0.1720  0.0297  1158 PHE B C   
4095 O O   . PHE B 248 ? 0.4986 0.7560 0.9536 -0.1188 0.1833  0.0210  1158 PHE B O   
4096 C CB  . PHE B 248 ? 0.4227 0.6691 0.8533 -0.0858 0.1302  0.0162  1158 PHE B CB  
4097 C CG  . PHE B 248 ? 0.4212 0.6907 0.8842 -0.0947 0.1252  -0.0029 1158 PHE B CG  
4098 C CD1 . PHE B 248 ? 0.3764 0.6770 0.8516 -0.0953 0.1291  -0.0135 1158 PHE B CD1 
4099 C CD2 . PHE B 248 ? 0.4156 0.6785 0.8960 -0.1005 0.1159  -0.0109 1158 PHE B CD2 
4100 C CE1 . PHE B 248 ? 0.3514 0.6764 0.8559 -0.1007 0.1236  -0.0314 1158 PHE B CE1 
4101 C CE2 . PHE B 248 ? 0.3767 0.6649 0.8852 -0.1058 0.1101  -0.0290 1158 PHE B CE2 
4102 C CZ  . PHE B 248 ? 0.3262 0.6457 0.8468 -0.1054 0.1137  -0.0391 1158 PHE B CZ  
4103 N N   . TRP B 249 ? 0.5362 0.7967 0.9421 -0.0898 0.1751  0.0364  1159 TRP B N   
4104 C CA  . TRP B 249 ? 0.5461 0.8323 0.9582 -0.0940 0.1898  0.0324  1159 TRP B CA  
4105 C C   . TRP B 249 ? 0.6221 0.8924 1.0228 -0.1024 0.2191  0.0500  1159 TRP B C   
4106 O O   . TRP B 249 ? 0.6708 0.9609 1.0844 -0.1117 0.2354  0.0455  1159 TRP B O   
4107 C CB  . TRP B 249 ? 0.4833 0.7922 0.8772 -0.0763 0.1795  0.0286  1159 TRP B CB  
4108 C CG  . TRP B 249 ? 0.4374 0.7667 0.8497 -0.0713 0.1574  0.0083  1159 TRP B CG  
4109 C CD1 . TRP B 249 ? 0.3986 0.7240 0.8020 -0.0586 0.1368  0.0039  1159 TRP B CD1 
4110 C CD2 . TRP B 249 ? 0.4040 0.7599 0.8472 -0.0782 0.1547  -0.0102 1159 TRP B CD2 
4111 N NE1 . TRP B 249 ? 0.4034 0.7472 0.8286 -0.0570 0.1230  -0.0146 1159 TRP B NE1 
4112 C CE2 . TRP B 249 ? 0.3802 0.7437 0.8289 -0.0675 0.1328  -0.0232 1159 TRP B CE2 
4113 C CE3 . TRP B 249 ? 0.4240 0.7994 0.8914 -0.0919 0.1695  -0.0175 1159 TRP B CE3 
4114 C CZ2 . TRP B 249 ? 0.3195 0.7073 0.7939 -0.0674 0.1249  -0.0413 1159 TRP B CZ2 
4115 C CZ3 . TRP B 249 ? 0.4005 0.8049 0.8956 -0.0923 0.1600  -0.0376 1159 TRP B CZ3 
4116 C CH2 . TRP B 249 ? 0.3479 0.7572 0.8446 -0.0789 0.1377  -0.0483 1159 TRP B CH2 
4117 N N   . ASP B 250 ? 0.6722 0.9070 1.0485 -0.0987 0.2276  0.0704  1160 ASP B N   
4118 C CA  . ASP B 250 ? 0.7195 0.9327 1.0903 -0.1098 0.2586  0.0870  1160 ASP B CA  
4119 C C   . ASP B 250 ? 0.7377 0.9420 1.1459 -0.1345 0.2688  0.0763  1160 ASP B C   
4120 O O   . ASP B 250 ? 0.8027 1.0005 1.2210 -0.1502 0.2963  0.0812  1160 ASP B O   
4121 C CB  . ASP B 250 ? 0.7537 0.9297 1.0852 -0.0960 0.2669  0.1135  1160 ASP B CB  
4122 C CG  . ASP B 250 ? 0.7944 0.9419 1.1274 -0.0951 0.2532  0.1149  1160 ASP B CG  
4123 O OD1 . ASP B 250 ? 0.7852 0.9221 1.1480 -0.1135 0.2555  0.1048  1160 ASP B OD1 
4124 O OD2 . ASP B 250 ? 0.8407 0.9780 1.1452 -0.0757 0.2405  0.1254  1160 ASP B OD2 
4125 N N   . ILE B 251 ? 0.6598 0.8658 1.0896 -0.1385 0.2478  0.0607  1161 ILE B N   
4126 C CA  . ILE B 251 ? 0.6444 0.8509 1.1125 -0.1608 0.2535  0.0451  1161 ILE B CA  
4127 C C   . ILE B 251 ? 0.6550 0.9064 1.1564 -0.1706 0.2521  0.0225  1161 ILE B C   
4128 O O   . ILE B 251 ? 0.6575 0.9150 1.1756 -0.1873 0.2703  0.0168  1161 ILE B O   
4129 C CB  . ILE B 251 ? 0.5997 0.7937 1.0756 -0.1589 0.2312  0.0369  1161 ILE B CB  
4130 C CG1 . ILE B 251 ? 0.5921 0.7407 1.0405 -0.1522 0.2362  0.0580  1161 ILE B CG1 
4131 C CG2 . ILE B 251 ? 0.5432 0.7487 1.0594 -0.1793 0.2317  0.0152  1161 ILE B CG2 
4132 C CD1 . ILE B 251 ? 0.5131 0.6496 0.9678 -0.1496 0.2153  0.0504  1161 ILE B CD1 
4133 N N   . LYS B 252 ? 0.6241 0.9046 1.1291 -0.1577 0.2271  0.0087  1162 LYS B N   
4134 C CA  . LYS B 252 ? 0.6200 0.9440 1.1569 -0.1631 0.2215  -0.0142 1162 LYS B CA  
4135 C C   . LYS B 252 ? 0.6730 1.0212 1.2027 -0.1590 0.2342  -0.0119 1162 LYS B C   
4136 O O   . LYS B 252 ? 0.6318 1.0163 1.1756 -0.1530 0.2234  -0.0280 1162 LYS B O   
4137 C CB  . LYS B 252 ? 0.5369 0.8774 1.0794 -0.1492 0.1909  -0.0285 1162 LYS B CB  
4138 C CG  . LYS B 252 ? 0.5035 0.8252 1.0521 -0.1512 0.1754  -0.0335 1162 LYS B CG  
4139 C CD  . LYS B 252 ? 0.5255 0.8601 1.0885 -0.1592 0.1663  -0.0523 1162 LYS B CD  
4140 C CE  . LYS B 252 ? 0.4360 0.7601 0.9992 -0.1540 0.1452  -0.0597 1162 LYS B CE  
4141 N NZ  . LYS B 252 ? 0.4004 0.7426 0.9777 -0.1589 0.1365  -0.0788 1162 LYS B NZ  
4142 N N   . SER B 253 ? 0.7314 1.0595 1.2374 -0.1602 0.2575  0.0085  1163 SER B N   
4143 C CA  . SER B 253 ? 0.7866 1.1376 1.2846 -0.1571 0.2729  0.0115  1163 SER B CA  
4144 C C   . SER B 253 ? 0.7711 1.1396 1.2982 -0.1782 0.2943  0.0018  1163 SER B C   
4145 O O   . SER B 253 ? 0.7150 1.1153 1.2469 -0.1766 0.2999  -0.0053 1163 SER B O   
4146 C CB  . SER B 253 ? 0.7771 1.1007 1.2307 -0.1450 0.2872  0.0388  1163 SER B CB  
4147 O OG  . SER B 253 ? 0.7666 1.0480 1.2116 -0.1545 0.3049  0.0564  1163 SER B OG  
4148 N N   . LYS B 254 ? 0.8790 1.2222 1.4132 -0.1935 0.2980  0.0008  1164 LYS B N   
4149 C CA  . LYS B 254 ? 0.9302 1.2844 1.4816 -0.2096 0.3083  -0.0101 1164 LYS B CA  
4150 C C   . LYS B 254 ? 0.9205 1.3117 1.4988 -0.2095 0.2845  -0.0374 1164 LYS B C   
4151 O O   . LYS B 254 ? 0.9651 1.3751 1.5610 -0.2203 0.2916  -0.0490 1164 LYS B O   
4152 C CB  . LYS B 254 ? 0.9553 1.2683 1.5056 -0.2255 0.3221  -0.0033 1164 LYS B CB  
4153 N N   . TYR B 255 ? 0.6907 1.0921 1.2715 -0.1963 0.2576  -0.0469 1165 TYR B N   
4154 C CA  . TYR B 255 ? 0.5752 1.0035 1.1761 -0.1936 0.2346  -0.0699 1165 TYR B CA  
4155 C C   . TYR B 255 ? 0.4868 0.9499 1.0891 -0.1762 0.2197  -0.0787 1165 TYR B C   
4156 O O   . TYR B 255 ? 0.4966 0.9898 1.1117 -0.1767 0.2219  -0.0899 1165 TYR B O   
4157 C CB  . TYR B 255 ? 0.5863 0.9943 1.1872 -0.1920 0.2159  -0.0742 1165 TYR B CB  
4158 C CG  . TYR B 255 ? 0.6290 1.0015 1.2290 -0.2084 0.2302  -0.0678 1165 TYR B CG  
4159 C CD1 . TYR B 255 ? 0.6772 1.0469 1.2868 -0.2255 0.2519  -0.0692 1165 TYR B CD1 
4160 C CD2 . TYR B 255 ? 0.6595 0.9998 1.2490 -0.2064 0.2228  -0.0606 1165 TYR B CD2 
4161 C CE1 . TYR B 255 ? 0.6522 0.9862 1.2608 -0.2399 0.2661  -0.0641 1165 TYR B CE1 
4162 C CE2 . TYR B 255 ? 0.6751 0.9806 1.2628 -0.2200 0.2363  -0.0552 1165 TYR B CE2 
4163 C CZ  . TYR B 255 ? 0.6782 0.9797 1.2754 -0.2367 0.2580  -0.0572 1165 TYR B CZ  
4164 O OH  . TYR B 255 ? 0.6294 0.8936 1.2249 -0.2496 0.2722  -0.0527 1165 TYR B OH  
4165 N N   . PHE B 256 ? 0.4986 0.9577 1.0889 -0.1604 0.2049  -0.0747 1166 PHE B N   
4166 C CA  . PHE B 256 ? 0.3782 0.8657 0.9679 -0.1431 0.1928  -0.0826 1166 PHE B CA  
4167 C C   . PHE B 256 ? 0.4003 0.8831 0.9727 -0.1344 0.2020  -0.0694 1166 PHE B C   
4168 O O   . PHE B 256 ? 0.4555 0.9133 1.0160 -0.1404 0.2173  -0.0530 1166 PHE B O   
4169 C CB  . PHE B 256 ? 0.3205 0.8124 0.9135 -0.1294 0.1646  -0.0947 1166 PHE B CB  
4170 C CG  . PHE B 256 ? 0.4127 0.8750 0.9962 -0.1268 0.1537  -0.0874 1166 PHE B CG  
4171 C CD1 . PHE B 256 ? 0.4825 0.9272 1.0707 -0.1368 0.1501  -0.0892 1166 PHE B CD1 
4172 C CD2 . PHE B 256 ? 0.3813 0.8345 0.9522 -0.1137 0.1464  -0.0804 1166 PHE B CD2 
4173 C CE1 . PHE B 256 ? 0.3408 0.7587 0.9200 -0.1335 0.1399  -0.0827 1166 PHE B CE1 
4174 C CE2 . PHE B 256 ? 0.3695 0.7962 0.9331 -0.1109 0.1362  -0.0739 1166 PHE B CE2 
4175 C CZ  . PHE B 256 ? 0.4282 0.8368 0.9952 -0.1207 0.1332  -0.0742 1166 PHE B CZ  
4176 N N   . THR B 257 ? 0.3352 0.8424 0.9053 -0.1191 0.1939  -0.0771 1167 THR B N   
4177 C CA  . THR B 257 ? 0.3370 0.8407 0.8842 -0.1065 0.1964  -0.0680 1167 THR B CA  
4178 C C   . THR B 257 ? 0.3497 0.8552 0.8916 -0.0877 0.1705  -0.0773 1167 THR B C   
4179 O O   . THR B 257 ? 0.3531 0.8739 0.9144 -0.0835 0.1563  -0.0923 1167 THR B O   
4180 C CB  . THR B 257 ? 0.3551 0.8824 0.8951 -0.1046 0.2144  -0.0670 1167 THR B CB  
4181 O OG1 . THR B 257 ? 0.3667 0.9282 0.9294 -0.1032 0.2101  -0.0852 1167 THR B OG1 
4182 C CG2 . THR B 257 ? 0.3860 0.8999 0.9193 -0.1203 0.2431  -0.0507 1167 THR B CG2 
4183 N N   . CYS B 258 ? 0.3199 0.8057 0.8304 -0.0749 0.1638  -0.0670 1168 CYS B N   
4184 C CA  . CYS B 258 ? 0.3603 0.8434 0.8652 -0.0586 0.1420  -0.0754 1168 CYS B CA  
4185 C C   . CYS B 258 ? 0.2858 0.8015 0.8043 -0.0489 0.1386  -0.0929 1168 CYS B C   
4186 O O   . CYS B 258 ? 0.3000 0.8365 0.8143 -0.0479 0.1514  -0.0945 1168 CYS B O   
4187 C CB  . CYS B 258 ? 0.3334 0.7956 0.8046 -0.0482 0.1378  -0.0640 1168 CYS B CB  
4188 S SG  . CYS B 258 ? 0.2982 0.7496 0.7650 -0.0325 0.1132  -0.0739 1168 CYS B SG  
4189 N N   . GLN B 259 ? 0.2730 0.7921 0.8063 -0.0403 0.1218  -0.1052 1169 GLN B N   
4190 C CA  . GLN B 259 ? 0.2917 0.8364 0.8368 -0.0279 0.1168  -0.1215 1169 GLN B CA  
4191 C C   . GLN B 259 ? 0.2743 0.8044 0.8069 -0.0114 0.1021  -0.1264 1169 GLN B C   
4192 O O   . GLN B 259 ? 0.2909 0.8278 0.8301 0.0008  0.0937  -0.1378 1169 GLN B O   
4193 C CB  . GLN B 259 ? 0.3004 0.8481 0.8577 -0.0282 0.1084  -0.1273 1169 GLN B CB  
4194 C CG  . GLN B 259 ? 0.3479 0.9051 0.9163 -0.0457 0.1208  -0.1241 1169 GLN B CG  
4195 C CD  . GLN B 259 ? 0.3164 0.9020 0.8906 -0.0486 0.1355  -0.1292 1169 GLN B CD  
4196 O OE1 . GLN B 259 ? 0.3228 0.9256 0.8994 -0.0361 0.1302  -0.1399 1169 GLN B OE1 
4197 N NE2 . GLN B 259 ? 0.3012 0.8902 0.8772 -0.0649 0.1554  -0.1210 1169 GLN B NE2 
4198 N N   . CYS B 260 ? 0.3254 0.8292 0.8344 -0.0104 0.0984  -0.1163 1170 CYS B N   
4199 C CA  . CYS B 260 ? 0.3418 0.8290 0.8422 0.0023  0.0849  -0.1222 1170 CYS B CA  
4200 C C   . CYS B 260 ? 0.3026 0.8078 0.7999 0.0140  0.0865  -0.1358 1170 CYS B C   
4201 O O   . CYS B 260 ? 0.3090 0.8058 0.8091 0.0251  0.0771  -0.1463 1170 CYS B O   
4202 C CB  . CYS B 260 ? 0.2887 0.7490 0.7671 0.0000  0.0809  -0.1103 1170 CYS B CB  
4203 S SG  . CYS B 260 ? 0.3354 0.8033 0.7855 0.0020  0.0903  -0.1046 1170 CYS B SG  
4204 N N   . GLY B 261 ? 0.3003 0.8287 0.7915 0.0117  0.0995  -0.1359 1171 GLY B N   
4205 C CA  . GLY B 261 ? 0.2848 0.8329 0.7720 0.0228  0.1020  -0.1498 1171 GLY B CA  
4206 C C   . GLY B 261 ? 0.3727 0.9133 0.8353 0.0293  0.0991  -0.1514 1171 GLY B C   
4207 O O   . GLY B 261 ? 0.3209 0.8813 0.7775 0.0375  0.1031  -0.1630 1171 GLY B O   
4208 N N   . SER B 262 ? 0.3520 0.8679 0.8007 0.0265  0.0921  -0.1417 1172 SER B N   
4209 C CA  . SER B 262 ? 0.3865 0.8987 0.8150 0.0337  0.0867  -0.1469 1172 SER B CA  
4210 C C   . SER B 262 ? 0.4608 0.9984 0.8689 0.0378  0.0975  -0.1468 1172 SER B C   
4211 O O   . SER B 262 ? 0.4895 1.0355 0.8892 0.0318  0.1106  -0.1323 1172 SER B O   
4212 C CB  . SER B 262 ? 0.4544 0.9417 0.8710 0.0290  0.0799  -0.1336 1172 SER B CB  
4213 O OG  . SER B 262 ? 0.5423 1.0311 0.9416 0.0364  0.0737  -0.1409 1172 SER B OG  
4214 N N   . GLU B 263 ? 0.4894 1.0388 0.8890 0.0484  0.0931  -0.1635 1173 GLU B N   
4215 C CA  . GLU B 263 ? 0.4912 1.0670 0.8680 0.0551  0.1020  -0.1651 1173 GLU B CA  
4216 C C   . GLU B 263 ? 0.5608 1.1320 0.9092 0.0546  0.1049  -0.1463 1173 GLU B C   
4217 O O   . GLU B 263 ? 0.5984 1.1903 0.9234 0.0609  0.1146  -0.1419 1173 GLU B O   
4218 C CB  . GLU B 263 ? 0.4490 1.0386 0.8234 0.0666  0.0949  -0.1901 1173 GLU B CB  
4219 C CG  . GLU B 263 ? 0.4595 1.0829 0.8210 0.0748  0.1057  -0.1982 1173 GLU B CG  
4220 C CD  . GLU B 263 ? 0.5303 1.1665 0.9133 0.0735  0.1147  -0.2035 1173 GLU B CD  
4221 O OE1 . GLU B 263 ? 0.4954 1.1175 0.9037 0.0724  0.1080  -0.2122 1173 GLU B OE1 
4222 O OE2 . GLU B 263 ? 0.4731 1.1341 0.8476 0.0744  0.1291  -0.1988 1173 GLU B OE2 
4223 N N   . LYS B 264 ? 0.5647 1.1094 0.9134 0.0488  0.0972  -0.1346 1174 LYS B N   
4224 C CA  . LYS B 264 ? 0.6107 1.1465 0.9342 0.0490  0.1001  -0.1144 1174 LYS B CA  
4225 C C   . LYS B 264 ? 0.5752 1.0879 0.9070 0.0360  0.1072  -0.0933 1174 LYS B C   
4226 O O   . LYS B 264 ? 0.6042 1.0964 0.9255 0.0341  0.1040  -0.0791 1174 LYS B O   
4227 C CB  . LYS B 264 ? 0.6489 1.1759 0.9644 0.0549  0.0843  -0.1211 1174 LYS B CB  
4228 C CG  . LYS B 264 ? 0.6588 1.2030 0.9792 0.0636  0.0743  -0.1490 1174 LYS B CG  
4229 C CD  . LYS B 264 ? 0.6935 1.2256 1.0169 0.0647  0.0591  -0.1579 1174 LYS B CD  
4230 C CE  . LYS B 264 ? 0.7808 1.3330 1.1075 0.0727  0.0511  -0.1873 1174 LYS B CE  
4231 N NZ  . LYS B 264 ? 0.7489 1.2954 1.0775 0.0734  0.0379  -0.1973 1174 LYS B NZ  
4232 N N   . CYS B 265 ? 0.4919 1.0093 0.8439 0.0272  0.1169  -0.0930 1175 CYS B N   
4233 C CA  . CYS B 265 ? 0.4721 0.9705 0.8373 0.0134  0.1230  -0.0781 1175 CYS B CA  
4234 C C   . CYS B 265 ? 0.4522 0.9447 0.7952 0.0096  0.1402  -0.0554 1175 CYS B C   
4235 O O   . CYS B 265 ? 0.4559 0.9671 0.7849 0.0129  0.1551  -0.0516 1175 CYS B O   
4236 C CB  . CYS B 265 ? 0.4381 0.9494 0.8334 0.0058  0.1279  -0.0874 1175 CYS B CB  
4237 S SG  . CYS B 265 ? 0.4082 0.9041 0.8233 -0.0123 0.1366  -0.0740 1175 CYS B SG  
4238 N N   . LYS B 266 ? 0.4578 0.9227 0.7969 0.0034  0.1392  -0.0400 1176 LYS B N   
4239 C CA  . LYS B 266 ? 0.4520 0.9032 0.7683 0.0012  0.1557  -0.0166 1176 LYS B CA  
4240 C C   . LYS B 266 ? 0.4319 0.8747 0.7670 -0.0164 0.1734  -0.0075 1176 LYS B C   
4241 O O   . LYS B 266 ? 0.4674 0.9032 0.7863 -0.0196 0.1940  0.0104  1176 LYS B O   
4242 C CB  . LYS B 266 ? 0.5366 0.9615 0.8367 0.0059  0.1454  -0.0051 1176 LYS B CB  
4243 C CG  . LYS B 266 ? 0.6101 1.0154 0.8836 0.0067  0.1622  0.0210  1176 LYS B CG  
4244 C CD  . LYS B 266 ? 0.6331 1.0129 0.8944 0.0118  0.1510  0.0309  1176 LYS B CD  
4245 C CE  . LYS B 266 ? 0.6862 1.0429 0.9205 0.0143  0.1692  0.0582  1176 LYS B CE  
4246 N NZ  . LYS B 266 ? 0.7116 1.0541 0.9232 0.0282  0.1574  0.0671  1176 LYS B NZ  
4247 N N   . HIS B 267 ? 0.4139 0.8586 0.7829 -0.0273 0.1670  -0.0202 1177 HIS B N   
4248 C CA  . HIS B 267 ? 0.4165 0.8539 0.8075 -0.0454 0.1810  -0.0149 1177 HIS B CA  
4249 C C   . HIS B 267 ? 0.3939 0.8616 0.8155 -0.0528 0.1863  -0.0316 1177 HIS B C   
4250 O O   . HIS B 267 ? 0.3652 0.8335 0.8148 -0.0671 0.1899  -0.0362 1177 HIS B O   
4251 C CB  . HIS B 267 ? 0.4360 0.8472 0.8396 -0.0521 0.1687  -0.0135 1177 HIS B CB  
4252 C CG  . HIS B 267 ? 0.4594 0.8435 0.8356 -0.0436 0.1616  0.0007  1177 HIS B CG  
4253 N ND1 . HIS B 267 ? 0.4774 0.8382 0.8329 -0.0460 0.1769  0.0220  1177 HIS B ND1 
4254 C CD2 . HIS B 267 ? 0.4496 0.8270 0.8164 -0.0320 0.1417  -0.0039 1177 HIS B CD2 
4255 C CE1 . HIS B 267 ? 0.4611 0.8045 0.7952 -0.0348 0.1652  0.0299  1177 HIS B CE1 
4256 N NE2 . HIS B 267 ? 0.4445 0.7989 0.7862 -0.0272 0.1439  0.0137  1177 HIS B NE2 
4257 N N   . SER B 268 ? 0.4287 0.9242 0.8464 -0.0428 0.1867  -0.0422 1178 SER B N   
4258 C CA  . SER B 268 ? 0.3721 0.8991 0.8170 -0.0488 0.1949  -0.0566 1178 SER B CA  
4259 C C   . SER B 268 ? 0.4459 0.9804 0.8880 -0.0602 0.2232  -0.0448 1178 SER B C   
4260 O O   . SER B 268 ? 0.4548 0.9749 0.8658 -0.0568 0.2361  -0.0264 1178 SER B O   
4261 C CB  . SER B 268 ? 0.3656 0.9190 0.8082 -0.0332 0.1859  -0.0733 1178 SER B CB  
4262 O OG  . SER B 268 ? 0.3927 0.9565 0.8071 -0.0255 0.1987  -0.0662 1178 SER B OG  
4263 N N   . ALA B 269 ? 0.4001 0.9582 0.8752 -0.0730 0.2335  -0.0559 1179 ALA B N   
4264 C CA  . ALA B 269 ? 0.4573 1.0243 0.9359 -0.0868 0.2632  -0.0470 1179 ALA B CA  
4265 C C   . ALA B 269 ? 0.4871 1.0634 0.9322 -0.0748 0.2769  -0.0372 1179 ALA B C   
4266 O O   . ALA B 269 ? 0.5216 1.0841 0.9471 -0.0802 0.3007  -0.0174 1179 ALA B O   
4267 C CB  . ALA B 269 ? 0.4126 1.0159 0.9341 -0.0987 0.2693  -0.0667 1179 ALA B CB  
4268 N N   . GLU B 270 ? 0.4676 1.0663 0.9047 -0.0574 0.2628  -0.0508 1180 GLU B N   
4269 C CA  . GLU B 270 ? 0.5311 1.1421 0.9348 -0.0436 0.2730  -0.0444 1180 GLU B CA  
4270 C C   . GLU B 270 ? 0.5871 1.1678 0.9487 -0.0341 0.2731  -0.0226 1180 GLU B C   
4271 O O   . GLU B 270 ? 0.6074 1.1868 0.9400 -0.0302 0.2936  -0.0053 1180 GLU B O   
4272 C CB  . GLU B 270 ? 0.5840 1.2217 0.9895 -0.0268 0.2548  -0.0665 1180 GLU B CB  
4273 C CG  . GLU B 270 ? 0.6857 1.3495 1.0672 -0.0145 0.2675  -0.0673 1180 GLU B CG  
4274 C CD  . GLU B 270 ? 0.7758 1.4630 1.1612 0.0016  0.2491  -0.0915 1180 GLU B CD  
4275 O OE1 . GLU B 270 ? 0.7675 1.4400 1.1417 0.0125  0.2276  -0.0972 1180 GLU B OE1 
4276 O OE2 . GLU B 270 ? 0.7263 1.4461 1.1279 0.0030  0.2572  -0.1057 1180 GLU B OE2 
4277 N N   . ALA B 271 ? 0.5482 1.1052 0.9053 -0.0292 0.2509  -0.0226 1181 ALA B N   
4278 C CA  . ALA B 271 ? 0.5683 1.1001 0.8870 -0.0183 0.2486  -0.0038 1181 ALA B CA  
4279 C C   . ALA B 271 ? 0.6242 1.1290 0.9305 -0.0289 0.2733  0.0224  1181 ALA B C   
4280 O O   . ALA B 271 ? 0.6861 1.1834 0.9549 -0.0181 0.2869  0.0417  1181 ALA B O   
4281 C CB  . ALA B 271 ? 0.4750 0.9873 0.7978 -0.0139 0.2216  -0.0101 1181 ALA B CB  
4282 N N   . ILE B 272 ? 0.6180 1.1084 0.9554 -0.0494 0.2804  0.0230  1182 ILE B N   
4283 C CA  . ILE B 272 ? 0.6332 1.0945 0.9637 -0.0622 0.3063  0.0459  1182 ILE B CA  
4284 C C   . ILE B 272 ? 0.6647 1.1401 0.9831 -0.0645 0.3375  0.0566  1182 ILE B C   
4285 O O   . ILE B 272 ? 0.6669 1.1209 0.9507 -0.0585 0.3575  0.0816  1182 ILE B O   
4286 C CB  . ILE B 272 ? 0.5900 1.0393 0.9619 -0.0854 0.3073  0.0382  1182 ILE B CB  
4287 C CG1 . ILE B 272 ? 0.5134 0.9418 0.8892 -0.0817 0.2800  0.0337  1182 ILE B CG1 
4288 C CG2 . ILE B 272 ? 0.5985 1.0215 0.9700 -0.1023 0.3398  0.0580  1182 ILE B CG2 
4289 C CD1 . ILE B 272 ? 0.5200 0.9339 0.9308 -0.1022 0.2805  0.0278  1182 ILE B CD1 
4290 N N   . ALA B 273 ? 0.6581 1.1697 1.0043 -0.0721 0.3433  0.0384  1183 ALA B N   
4291 C CA  . ALA B 273 ? 0.6924 1.2197 1.0312 -0.0763 0.3750  0.0473  1183 ALA B CA  
4292 C C   . ALA B 273 ? 0.7102 1.2453 0.9996 -0.0518 0.3784  0.0597  1183 ALA B C   
4293 O O   . ALA B 273 ? 0.7876 1.3176 1.0525 -0.0508 0.4078  0.0800  1183 ALA B O   
4294 C CB  . ALA B 273 ? 0.7178 1.2876 1.0979 -0.0872 0.3773  0.0222  1183 ALA B CB  
4295 N N   . LEU B 274 ? 0.6870 1.2351 0.9614 -0.0319 0.3498  0.0474  1184 LEU B N   
4296 C CA  . LEU B 274 ? 0.7237 1.2808 0.9504 -0.0072 0.3495  0.0568  1184 LEU B CA  
4297 C C   . LEU B 274 ? 0.7797 1.3004 0.9668 0.0036  0.3525  0.0840  1184 LEU B C   
4298 O O   . LEU B 274 ? 0.8478 1.3727 0.9908 0.0230  0.3619  0.0993  1184 LEU B O   
4299 C CB  . LEU B 274 ? 0.6919 1.2759 0.9195 0.0090  0.3184  0.0311  1184 LEU B CB  
4300 C CG  . LEU B 274 ? 0.6734 1.2957 0.9327 0.0047  0.3160  0.0048  1184 LEU B CG  
4301 C CD1 . LEU B 274 ? 0.6302 1.2718 0.8902 0.0206  0.2866  -0.0202 1184 LEU B CD1 
4302 C CD2 . LEU B 274 ? 0.7140 1.3611 0.9607 0.0060  0.3447  0.0112  1184 LEU B CD2 
4303 N N   . GLU B 275 ? 0.7220 1.2084 0.9225 -0.0069 0.3447  0.0901  1185 GLU B N   
4304 C CA  . GLU B 275 ? 0.7683 1.2181 0.9336 0.0033  0.3486  0.1163  1185 GLU B CA  
4305 C C   . GLU B 275 ? 0.8801 1.3013 1.0315 -0.0058 0.3867  0.1452  1185 GLU B C   
4306 O O   . GLU B 275 ? 0.8998 1.2950 1.0100 0.0093  0.3967  0.1714  1185 GLU B O   
4307 C CB  . GLU B 275 ? 0.7104 1.1346 0.8956 -0.0037 0.3257  0.1107  1185 GLU B CB  
4308 C CG  . GLU B 275 ? 0.7587 1.1439 0.9123 0.0063  0.3278  0.1360  1185 GLU B CG  
4309 C CD  . GLU B 275 ? 0.7642 1.1609 0.8712 0.0365  0.3157  0.1429  1185 GLU B CD  
4310 O OE1 . GLU B 275 ? 0.7434 1.1570 0.8188 0.0507  0.3314  0.1530  1185 GLU B OE1 
4311 O OE2 . GLU B 275 ? 0.6858 1.0769 0.7883 0.0464  0.2903  0.1372  1185 GLU B OE2 
4312 N N   . GLN B 276 ? 0.8654 1.2915 1.0500 -0.0294 0.4091  0.1408  1186 GLN B N   
4313 C CA  . GLN B 276 ? 0.9066 1.3036 1.0840 -0.0420 0.4486  0.1663  1186 GLN B CA  
4314 C C   . GLN B 276 ? 1.0152 1.4252 1.1530 -0.0270 0.4753  0.1843  1186 GLN B C   
4315 O O   . GLN B 276 ? 1.0078 1.3959 1.1401 -0.0381 0.5126  0.2055  1186 GLN B O   
4316 C CB  . GLN B 276 ? 0.8676 1.2681 1.1005 -0.0750 0.4628  0.1514  1186 GLN B CB  
4317 C CG  . GLN B 276 ? 0.8204 1.2136 1.0936 -0.0891 0.4365  0.1314  1186 GLN B CG  
4318 C CD  . GLN B 276 ? 0.8611 1.2068 1.1164 -0.0854 0.4309  0.1493  1186 GLN B CD  
4319 O OE1 . GLN B 276 ? 0.8610 1.1694 1.0949 -0.0875 0.4584  0.1758  1186 GLN B OE1 
4320 N NE2 . GLN B 276 ? 0.8210 1.1665 1.0843 -0.0789 0.3964  0.1354  1186 GLN B NE2 
4321 N N   . SER B 277 ? 1.1410 1.5854 1.2513 -0.0025 0.4584  0.1761  1187 SER B N   
4322 C CA  . SER B 277 ? 1.1978 1.6577 1.2654 0.0155  0.4816  0.1928  1187 SER B CA  
4323 C C   . SER B 277 ? 1.2387 1.6870 1.2470 0.0483  0.4734  0.2136  1187 SER B C   
4324 O O   . SER B 277 ? 1.1782 1.6471 1.1760 0.0664  0.4399  0.1976  1187 SER B O   
4325 C CB  . SER B 277 ? 1.1853 1.6995 1.2650 0.0201  0.4720  0.1660  1187 SER B CB  
4326 O OG  . SER B 277 ? 1.1801 1.7172 1.2495 0.0401  0.4344  0.1462  1187 SER B OG  
# 
