data_9CQA
# 
_entry.id   9CQA 
# 
_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   9CQA         pdb_00009cqa 10.2210/pdb9cqa/pdb 
WWPDB D_1000285967 ?            ?                   
# 
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 2025-02-19 ? 
2 'Structure model' 1 1 2025-04-02 ? 
# 
_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_CSD'          
4  2 'Structure model' '_citation.journal_id_ISSN'         
5  2 'Structure model' '_citation.journal_volume'          
6  2 'Structure model' '_citation.page_first'              
7  2 'Structure model' '_citation.page_last'               
8  2 'Structure model' '_citation.pdbx_database_id_DOI'    
9  2 'Structure model' '_citation.pdbx_database_id_PubMed' 
10 2 'Structure model' '_citation.title'                   
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                        9CQA 
_pdbx_database_status.recvd_initial_deposition_date   2024-07-19 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              rmdubois@ucsc.edu 
_pdbx_contact_author.name_first         DuBois 
_pdbx_contact_author.name_last          Rebecca 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-4185-5673 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Juarez, M.G.' 1 0000-0002-0771-1492 
'DuBois, R.M.' 2 0000-0003-4185-5673 
# 
_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                   UK 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Sci Rep' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2045-2322 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            15 
_citation.language                  ? 
_citation.page_first                8666 
_citation.page_last                 8666 
_citation.title                     
'Structures of respiratory syncytial virus G bound to broadly reactive antibodies provide insights into vaccine design.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1038/s41598-025-92886-w 
_citation.pdbx_database_id_PubMed   40082629 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Juarez, M.G.'        1 ? 
primary 
;O'Rourke, S.M.
;
2 ? 
primary 'Dzimianski, J.V.'    3 ? 
primary 'Gagnon, D.'          4 ? 
primary 'Penunuri, G.'        5 ? 
primary 'Serrao, V.H.B.'      6 ? 
primary 'Corbett-Detig, R.B.' 7 ? 
primary 'Kauvar, L.M.'        8 ? 
primary 'DuBois, R.M.'        9 ? 
# 
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 'Fab 1G1 Heavy Chain'            28290.494 2   ? ? ? ? 
2 polymer     man 'Fab1G1 Light Chain'             23331.760 2   ? ? ? ? 
3 polymer     man 'Mature secreted glycoprotein G' 5735.633  2   ? ? ? ? 
4 non-polymer syn 'SULFATE ION'                    96.063    4   ? ? ? ? 
5 water       nat water                            18.015    393 ? ? ? ? 
# 
_entity_name_com.entity_id   3 
_entity_name_com.name        'Mature sG' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no 
;QVHLVQSGVEVKKPGASVRVSCKASGYTFATYGITWVRQAPGRGLEWVGWITPYNDRTSYAQIFHGRVTMTTDTSTNTAY
MELRSLRSDDTAMYYCARNHCNFYHDFWSGLDYWGQGTLVSVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEP
VTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCASLVPRGSGWSHP
QFEKGGGSGGGSGGGSWSHPQFEK
;
;QVHLVQSGVEVKKPGASVRVSCKASGYTFATYGITWVRQAPGRGLEWVGWITPYNDRTSYAQIFHGRVTMTTDTSTNTAY
MELRSLRSDDTAMYYCARNHCNFYHDFWSGLDYWGQGTLVSVSSASTKGPSVFPLAPSSKSTSGGTAALGCLVKDYFPEP
VTVSWNSGALTSGVHTFPAVLQSSGLYSLSSVVTVPSSSLGTQTYICNVNHKPSNTKVDKKVEPKSCASLVPRGSGWSHP
QFEKGGGSGGGSGGGSWSHPQFEK
;
E,D ? 
2 'polypeptide(L)' no no 
;SFELTQPPSVSVSPGQTARITCSGDALPKQYVYWYQQKPGQAPVLVIYKTTERPSGIPERFSDSSSGTTVTLTISAAQAE
DEADYYCQSVDSSGTYVFGIGTKVTVLGRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNS
QESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
;SFELTQPPSVSVSPGQTARITCSGDALPKQYVYWYQQKPGQAPVLVIYKTTERPSGIPERFSDSSSGTTVTLTISAAQAE
DEADYYCQSVDSSGTYVFGIGTKVTVLGRTVAAPSVFIFPPSDEQLKSGTASVVCLLNNFYPREAKVQWKVDNALQSGNS
QESVTEQDSKDSTYSLSSTLTLSKADYEKHKVYACEVTHQGLSSPVTKSFNRGEC
;
F,G ? 
3 'polypeptide(L)' no no MGSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKKHHHHHH MGSKPNNDFHFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKKHHHHHH A,B ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
4 'SULFATE ION' SO4 
5 water         HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLN n 
1 2   VAL n 
1 3   HIS n 
1 4   LEU n 
1 5   VAL n 
1 6   GLN n 
1 7   SER n 
1 8   GLY n 
1 9   VAL n 
1 10  GLU n 
1 11  VAL n 
1 12  LYS n 
1 13  LYS n 
1 14  PRO n 
1 15  GLY n 
1 16  ALA n 
1 17  SER n 
1 18  VAL n 
1 19  ARG n 
1 20  VAL n 
1 21  SER n 
1 22  CYS n 
1 23  LYS n 
1 24  ALA n 
1 25  SER n 
1 26  GLY n 
1 27  TYR n 
1 28  THR n 
1 29  PHE n 
1 30  ALA n 
1 31  THR n 
1 32  TYR n 
1 33  GLY n 
1 34  ILE n 
1 35  THR n 
1 36  TRP n 
1 37  VAL n 
1 38  ARG n 
1 39  GLN n 
1 40  ALA n 
1 41  PRO n 
1 42  GLY n 
1 43  ARG n 
1 44  GLY n 
1 45  LEU n 
1 46  GLU n 
1 47  TRP n 
1 48  VAL n 
1 49  GLY n 
1 50  TRP n 
1 51  ILE n 
1 52  THR n 
1 53  PRO n 
1 54  TYR n 
1 55  ASN n 
1 56  ASP n 
1 57  ARG n 
1 58  THR n 
1 59  SER n 
1 60  TYR n 
1 61  ALA n 
1 62  GLN n 
1 63  ILE n 
1 64  PHE n 
1 65  HIS n 
1 66  GLY n 
1 67  ARG n 
1 68  VAL n 
1 69  THR n 
1 70  MET n 
1 71  THR n 
1 72  THR n 
1 73  ASP n 
1 74  THR n 
1 75  SER n 
1 76  THR n 
1 77  ASN n 
1 78  THR n 
1 79  ALA n 
1 80  TYR n 
1 81  MET n 
1 82  GLU n 
1 83  LEU n 
1 84  ARG n 
1 85  SER n 
1 86  LEU n 
1 87  ARG n 
1 88  SER n 
1 89  ASP n 
1 90  ASP n 
1 91  THR n 
1 92  ALA n 
1 93  MET n 
1 94  TYR n 
1 95  TYR n 
1 96  CYS n 
1 97  ALA n 
1 98  ARG n 
1 99  ASN n 
1 100 HIS n 
1 101 CYS n 
1 102 ASN n 
1 103 PHE n 
1 104 TYR n 
1 105 HIS n 
1 106 ASP n 
1 107 PHE n 
1 108 TRP n 
1 109 SER n 
1 110 GLY n 
1 111 LEU n 
1 112 ASP n 
1 113 TYR n 
1 114 TRP n 
1 115 GLY n 
1 116 GLN n 
1 117 GLY n 
1 118 THR n 
1 119 LEU n 
1 120 VAL n 
1 121 SER n 
1 122 VAL n 
1 123 SER n 
1 124 SER n 
1 125 ALA n 
1 126 SER n 
1 127 THR n 
1 128 LYS n 
1 129 GLY n 
1 130 PRO n 
1 131 SER n 
1 132 VAL n 
1 133 PHE n 
1 134 PRO n 
1 135 LEU n 
1 136 ALA n 
1 137 PRO n 
1 138 SER n 
1 139 SER n 
1 140 LYS n 
1 141 SER n 
1 142 THR n 
1 143 SER n 
1 144 GLY n 
1 145 GLY n 
1 146 THR n 
1 147 ALA n 
1 148 ALA n 
1 149 LEU n 
1 150 GLY n 
1 151 CYS n 
1 152 LEU n 
1 153 VAL n 
1 154 LYS n 
1 155 ASP n 
1 156 TYR n 
1 157 PHE n 
1 158 PRO n 
1 159 GLU n 
1 160 PRO n 
1 161 VAL n 
1 162 THR n 
1 163 VAL n 
1 164 SER n 
1 165 TRP n 
1 166 ASN n 
1 167 SER n 
1 168 GLY n 
1 169 ALA n 
1 170 LEU n 
1 171 THR n 
1 172 SER n 
1 173 GLY n 
1 174 VAL n 
1 175 HIS n 
1 176 THR n 
1 177 PHE n 
1 178 PRO n 
1 179 ALA n 
1 180 VAL n 
1 181 LEU n 
1 182 GLN n 
1 183 SER n 
1 184 SER n 
1 185 GLY n 
1 186 LEU n 
1 187 TYR n 
1 188 SER n 
1 189 LEU n 
1 190 SER n 
1 191 SER n 
1 192 VAL n 
1 193 VAL n 
1 194 THR n 
1 195 VAL n 
1 196 PRO n 
1 197 SER n 
1 198 SER n 
1 199 SER n 
1 200 LEU n 
1 201 GLY n 
1 202 THR n 
1 203 GLN n 
1 204 THR n 
1 205 TYR n 
1 206 ILE n 
1 207 CYS n 
1 208 ASN n 
1 209 VAL n 
1 210 ASN n 
1 211 HIS n 
1 212 LYS n 
1 213 PRO n 
1 214 SER n 
1 215 ASN n 
1 216 THR n 
1 217 LYS n 
1 218 VAL n 
1 219 ASP n 
1 220 LYS n 
1 221 LYS n 
1 222 VAL n 
1 223 GLU n 
1 224 PRO n 
1 225 LYS n 
1 226 SER n 
1 227 CYS n 
1 228 ALA n 
1 229 SER n 
1 230 LEU n 
1 231 VAL n 
1 232 PRO n 
1 233 ARG n 
1 234 GLY n 
1 235 SER n 
1 236 GLY n 
1 237 TRP n 
1 238 SER n 
1 239 HIS n 
1 240 PRO n 
1 241 GLN n 
1 242 PHE n 
1 243 GLU n 
1 244 LYS n 
1 245 GLY n 
1 246 GLY n 
1 247 GLY n 
1 248 SER n 
1 249 GLY n 
1 250 GLY n 
1 251 GLY n 
1 252 SER n 
1 253 GLY n 
1 254 GLY n 
1 255 GLY n 
1 256 SER n 
1 257 TRP n 
1 258 SER n 
1 259 HIS n 
1 260 PRO n 
1 261 GLN n 
1 262 PHE n 
1 263 GLU n 
1 264 LYS n 
2 1   SER n 
2 2   PHE n 
2 3   GLU n 
2 4   LEU n 
2 5   THR n 
2 6   GLN n 
2 7   PRO n 
2 8   PRO n 
2 9   SER n 
2 10  VAL n 
2 11  SER n 
2 12  VAL n 
2 13  SER n 
2 14  PRO n 
2 15  GLY n 
2 16  GLN n 
2 17  THR n 
2 18  ALA n 
2 19  ARG n 
2 20  ILE n 
2 21  THR n 
2 22  CYS n 
2 23  SER n 
2 24  GLY n 
2 25  ASP n 
2 26  ALA n 
2 27  LEU n 
2 28  PRO n 
2 29  LYS n 
2 30  GLN n 
2 31  TYR n 
2 32  VAL n 
2 33  TYR n 
2 34  TRP n 
2 35  TYR n 
2 36  GLN n 
2 37  GLN n 
2 38  LYS n 
2 39  PRO n 
2 40  GLY n 
2 41  GLN n 
2 42  ALA n 
2 43  PRO n 
2 44  VAL n 
2 45  LEU n 
2 46  VAL n 
2 47  ILE n 
2 48  TYR n 
2 49  LYS n 
2 50  THR n 
2 51  THR n 
2 52  GLU n 
2 53  ARG n 
2 54  PRO n 
2 55  SER n 
2 56  GLY n 
2 57  ILE n 
2 58  PRO n 
2 59  GLU n 
2 60  ARG n 
2 61  PHE n 
2 62  SER n 
2 63  ASP n 
2 64  SER n 
2 65  SER n 
2 66  SER n 
2 67  GLY n 
2 68  THR n 
2 69  THR n 
2 70  VAL n 
2 71  THR n 
2 72  LEU n 
2 73  THR n 
2 74  ILE n 
2 75  SER n 
2 76  ALA n 
2 77  ALA n 
2 78  GLN n 
2 79  ALA n 
2 80  GLU n 
2 81  ASP n 
2 82  GLU n 
2 83  ALA n 
2 84  ASP n 
2 85  TYR n 
2 86  TYR n 
2 87  CYS n 
2 88  GLN n 
2 89  SER n 
2 90  VAL n 
2 91  ASP n 
2 92  SER n 
2 93  SER n 
2 94  GLY n 
2 95  THR n 
2 96  TYR n 
2 97  VAL n 
2 98  PHE n 
2 99  GLY n 
2 100 ILE n 
2 101 GLY n 
2 102 THR n 
2 103 LYS n 
2 104 VAL n 
2 105 THR n 
2 106 VAL n 
2 107 LEU n 
2 108 GLY n 
2 109 ARG n 
2 110 THR n 
2 111 VAL n 
2 112 ALA n 
2 113 ALA n 
2 114 PRO n 
2 115 SER n 
2 116 VAL n 
2 117 PHE n 
2 118 ILE n 
2 119 PHE n 
2 120 PRO n 
2 121 PRO n 
2 122 SER n 
2 123 ASP n 
2 124 GLU n 
2 125 GLN n 
2 126 LEU n 
2 127 LYS n 
2 128 SER n 
2 129 GLY n 
2 130 THR n 
2 131 ALA n 
2 132 SER n 
2 133 VAL n 
2 134 VAL n 
2 135 CYS n 
2 136 LEU n 
2 137 LEU n 
2 138 ASN n 
2 139 ASN n 
2 140 PHE n 
2 141 TYR n 
2 142 PRO n 
2 143 ARG n 
2 144 GLU n 
2 145 ALA n 
2 146 LYS n 
2 147 VAL n 
2 148 GLN n 
2 149 TRP n 
2 150 LYS n 
2 151 VAL n 
2 152 ASP n 
2 153 ASN n 
2 154 ALA n 
2 155 LEU n 
2 156 GLN n 
2 157 SER n 
2 158 GLY n 
2 159 ASN n 
2 160 SER n 
2 161 GLN n 
2 162 GLU n 
2 163 SER n 
2 164 VAL n 
2 165 THR n 
2 166 GLU n 
2 167 GLN n 
2 168 ASP n 
2 169 SER n 
2 170 LYS n 
2 171 ASP n 
2 172 SER n 
2 173 THR n 
2 174 TYR n 
2 175 SER n 
2 176 LEU n 
2 177 SER n 
2 178 SER n 
2 179 THR n 
2 180 LEU n 
2 181 THR n 
2 182 LEU n 
2 183 SER n 
2 184 LYS n 
2 185 ALA n 
2 186 ASP n 
2 187 TYR n 
2 188 GLU n 
2 189 LYS n 
2 190 HIS n 
2 191 LYS n 
2 192 VAL n 
2 193 TYR n 
2 194 ALA n 
2 195 CYS n 
2 196 GLU n 
2 197 VAL n 
2 198 THR n 
2 199 HIS n 
2 200 GLN n 
2 201 GLY n 
2 202 LEU n 
2 203 SER n 
2 204 SER n 
2 205 PRO n 
2 206 VAL n 
2 207 THR n 
2 208 LYS n 
2 209 SER n 
2 210 PHE n 
2 211 ASN n 
2 212 ARG n 
2 213 GLY n 
2 214 GLU n 
2 215 CYS n 
3 1   MET n 
3 2   GLY n 
3 3   SER n 
3 4   LYS n 
3 5   PRO n 
3 6   ASN n 
3 7   ASN n 
3 8   ASP n 
3 9   PHE n 
3 10  HIS n 
3 11  PHE n 
3 12  GLU n 
3 13  VAL n 
3 14  PHE n 
3 15  ASN n 
3 16  PHE n 
3 17  VAL n 
3 18  PRO n 
3 19  CYS n 
3 20  SER n 
3 21  ILE n 
3 22  CYS n 
3 23  SER n 
3 24  ASN n 
3 25  ASN n 
3 26  PRO n 
3 27  THR n 
3 28  CYS n 
3 29  TRP n 
3 30  ALA n 
3 31  ILE n 
3 32  CYS n 
3 33  LYS n 
3 34  ARG n 
3 35  ILE n 
3 36  PRO n 
3 37  ASN n 
3 38  LYS n 
3 39  LYS n 
3 40  PRO n 
3 41  GLY n 
3 42  LYS n 
3 43  LYS n 
3 44  HIS n 
3 45  HIS n 
3 46  HIS n 
3 47  HIS n 
3 48  HIS n 
3 49  HIS n 
# 
loop_
_entity_src_gen.entity_id 
_entity_src_gen.pdbx_src_id 
_entity_src_gen.pdbx_alt_source_flag 
_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 
_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 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id 
_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 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id 
_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 
1 1 sample 'Biological sequence' 1 264 human ? ? ? ? ? ? ? ? 'Homo sapiens'                   9606    ? ? ? ? ? ? ? 
'Chinese hamster' 'Cricetulus griseus' 10029 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
2 1 sample 'Biological sequence' 1 215 human ? ? ? ? ? ? ? ? 'Homo sapiens'                   9606    ? ? ? ? ? ? ? 
'Chinese hamster' 'Cricetulus griseus' 10029 ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
3 1 sample 'Biological sequence' 1 49  ?     ? ? ? ? ? ? ? ? 'Respiratory syncytial virus A2' 1972429 ? ? ? ? ? ? ? ? 
'Escherichia coli'   562   ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE         ? 'C3 H7 N O2'     89.093  
ARG 'L-peptide linking' y ARGININE        ? 'C6 H15 N4 O2 1' 175.209 
ASN 'L-peptide linking' y ASPARAGINE      ? 'C4 H8 N2 O3'    132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'     133.103 
CYS 'L-peptide linking' y CYSTEINE        ? 'C3 H7 N O2 S'   121.158 
GLN 'L-peptide linking' y GLUTAMINE       ? 'C5 H10 N2 O3'   146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'     147.129 
GLY 'peptide linking'   y GLYCINE         ? 'C2 H5 N O2'     75.067  
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 
SO4 non-polymer         . 'SULFATE ION'   ? 'O4 S -2'        96.063  
THR 'L-peptide linking' y THREONINE       ? 'C4 H9 N O3'     119.119 
TRP 'L-peptide linking' y TRYPTOPHAN      ? 'C11 H12 N2 O2'  204.225 
TYR 'L-peptide linking' y TYROSINE        ? 'C9 H11 N O3'    181.189 
VAL 'L-peptide linking' y VALINE          ? 'C5 H11 N O2'    117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLN 1   1   1   GLN GLN E . n 
A 1 2   VAL 2   2   2   VAL VAL E . n 
A 1 3   HIS 3   3   3   HIS HIS E . n 
A 1 4   LEU 4   4   4   LEU LEU E . n 
A 1 5   VAL 5   5   5   VAL VAL E . n 
A 1 6   GLN 6   6   6   GLN GLN E . n 
A 1 7   SER 7   7   7   SER SER E . n 
A 1 8   GLY 8   8   8   GLY GLY E . n 
A 1 9   VAL 9   9   9   VAL VAL E . n 
A 1 10  GLU 10  10  10  GLU GLU E . n 
A 1 11  VAL 11  11  11  VAL VAL E . n 
A 1 12  LYS 12  12  12  LYS LYS E . n 
A 1 13  LYS 13  13  13  LYS LYS E . n 
A 1 14  PRO 14  14  14  PRO PRO E . n 
A 1 15  GLY 15  15  15  GLY GLY E . n 
A 1 16  ALA 16  16  16  ALA ALA E . n 
A 1 17  SER 17  17  17  SER SER E . n 
A 1 18  VAL 18  18  18  VAL VAL E . n 
A 1 19  ARG 19  19  19  ARG ARG E . n 
A 1 20  VAL 20  20  20  VAL VAL E . n 
A 1 21  SER 21  21  21  SER SER E . n 
A 1 22  CYS 22  22  22  CYS CYS E . n 
A 1 23  LYS 23  23  23  LYS LYS E . n 
A 1 24  ALA 24  24  24  ALA ALA E . n 
A 1 25  SER 25  25  25  SER SER E . n 
A 1 26  GLY 26  26  26  GLY GLY E . n 
A 1 27  TYR 27  27  27  TYR TYR E . n 
A 1 28  THR 28  28  28  THR THR E . n 
A 1 29  PHE 29  29  29  PHE PHE E . n 
A 1 30  ALA 30  30  30  ALA ALA E . n 
A 1 31  THR 31  31  31  THR THR E . n 
A 1 32  TYR 32  32  32  TYR TYR E . n 
A 1 33  GLY 33  33  33  GLY GLY E . n 
A 1 34  ILE 34  34  34  ILE ILE E . n 
A 1 35  THR 35  35  35  THR THR E . n 
A 1 36  TRP 36  36  36  TRP TRP E . n 
A 1 37  VAL 37  37  37  VAL VAL E . n 
A 1 38  ARG 38  38  38  ARG ARG E . n 
A 1 39  GLN 39  39  39  GLN GLN E . n 
A 1 40  ALA 40  40  40  ALA ALA E . n 
A 1 41  PRO 41  41  41  PRO PRO E . n 
A 1 42  GLY 42  42  42  GLY GLY E . n 
A 1 43  ARG 43  43  43  ARG ARG E . n 
A 1 44  GLY 44  44  44  GLY GLY E . n 
A 1 45  LEU 45  45  45  LEU LEU E . n 
A 1 46  GLU 46  46  46  GLU GLU E . n 
A 1 47  TRP 47  47  47  TRP TRP E . n 
A 1 48  VAL 48  48  48  VAL VAL E . n 
A 1 49  GLY 49  49  49  GLY GLY E . n 
A 1 50  TRP 50  50  50  TRP TRP E . n 
A 1 51  ILE 51  51  51  ILE ILE E . n 
A 1 52  THR 52  52  52  THR THR E . n 
A 1 53  PRO 53  53  53  PRO PRO E . n 
A 1 54  TYR 54  54  54  TYR TYR E . n 
A 1 55  ASN 55  55  55  ASN ASN E . n 
A 1 56  ASP 56  56  56  ASP ASP E . n 
A 1 57  ARG 57  57  57  ARG ARG E . n 
A 1 58  THR 58  58  58  THR THR E . n 
A 1 59  SER 59  59  59  SER SER E . n 
A 1 60  TYR 60  60  60  TYR TYR E . n 
A 1 61  ALA 61  61  61  ALA ALA E . n 
A 1 62  GLN 62  62  62  GLN GLN E . n 
A 1 63  ILE 63  63  63  ILE ILE E . n 
A 1 64  PHE 64  64  64  PHE PHE E . n 
A 1 65  HIS 65  65  65  HIS HIS E . n 
A 1 66  GLY 66  66  66  GLY GLY E . n 
A 1 67  ARG 67  67  67  ARG ARG E . n 
A 1 68  VAL 68  68  68  VAL VAL E . n 
A 1 69  THR 69  69  69  THR THR E . n 
A 1 70  MET 70  70  70  MET MET E . n 
A 1 71  THR 71  71  71  THR THR E . n 
A 1 72  THR 72  72  72  THR THR E . n 
A 1 73  ASP 73  73  73  ASP ASP E . n 
A 1 74  THR 74  74  74  THR THR E . n 
A 1 75  SER 75  75  75  SER SER E . n 
A 1 76  THR 76  76  76  THR THR E . n 
A 1 77  ASN 77  77  77  ASN ASN E . n 
A 1 78  THR 78  78  78  THR THR E . n 
A 1 79  ALA 79  79  79  ALA ALA E . n 
A 1 80  TYR 80  80  80  TYR TYR E . n 
A 1 81  MET 81  81  81  MET MET E . n 
A 1 82  GLU 82  82  82  GLU GLU E . n 
A 1 83  LEU 83  83  83  LEU LEU E . n 
A 1 84  ARG 84  84  84  ARG ARG E . n 
A 1 85  SER 85  85  85  SER SER E . n 
A 1 86  LEU 86  86  86  LEU LEU E . n 
A 1 87  ARG 87  87  87  ARG ARG E . n 
A 1 88  SER 88  88  88  SER SER E . n 
A 1 89  ASP 89  89  89  ASP ASP E . n 
A 1 90  ASP 90  90  90  ASP ASP E . n 
A 1 91  THR 91  91  91  THR THR E . n 
A 1 92  ALA 92  92  92  ALA ALA E . n 
A 1 93  MET 93  93  93  MET MET E . n 
A 1 94  TYR 94  94  94  TYR TYR E . n 
A 1 95  TYR 95  95  95  TYR TYR E . n 
A 1 96  CYS 96  96  96  CYS CYS E . n 
A 1 97  ALA 97  97  97  ALA ALA E . n 
A 1 98  ARG 98  98  98  ARG ARG E . n 
A 1 99  ASN 99  99  99  ASN ASN E . n 
A 1 100 HIS 100 100 100 HIS HIS E . n 
A 1 101 CYS 101 101 101 CYS CYS E . n 
A 1 102 ASN 102 102 102 ASN ASN E . n 
A 1 103 PHE 103 103 103 PHE PHE E . n 
A 1 104 TYR 104 104 104 TYR TYR E . n 
A 1 105 HIS 105 105 105 HIS HIS E . n 
A 1 106 ASP 106 106 106 ASP ASP E . n 
A 1 107 PHE 107 107 107 PHE PHE E . n 
A 1 108 TRP 108 108 108 TRP TRP E . n 
A 1 109 SER 109 109 109 SER SER E . n 
A 1 110 GLY 110 110 110 GLY GLY E . n 
A 1 111 LEU 111 111 111 LEU LEU E . n 
A 1 112 ASP 112 112 112 ASP ASP E . n 
A 1 113 TYR 113 113 113 TYR TYR E . n 
A 1 114 TRP 114 114 114 TRP TRP E . n 
A 1 115 GLY 115 115 115 GLY GLY E . n 
A 1 116 GLN 116 116 116 GLN GLN E . n 
A 1 117 GLY 117 117 117 GLY GLY E . n 
A 1 118 THR 118 118 118 THR THR E . n 
A 1 119 LEU 119 119 119 LEU LEU E . n 
A 1 120 VAL 120 120 120 VAL VAL E . n 
A 1 121 SER 121 121 121 SER SER E . n 
A 1 122 VAL 122 122 122 VAL VAL E . n 
A 1 123 SER 123 123 123 SER SER E . n 
A 1 124 SER 124 124 124 SER SER E . n 
A 1 125 ALA 125 125 125 ALA ALA E . n 
A 1 126 SER 126 126 126 SER SER E . n 
A 1 127 THR 127 127 127 THR THR E . n 
A 1 128 LYS 128 128 128 LYS LYS E . n 
A 1 129 GLY 129 129 129 GLY GLY E . n 
A 1 130 PRO 130 130 130 PRO PRO E . n 
A 1 131 SER 131 131 131 SER SER E . n 
A 1 132 VAL 132 132 132 VAL VAL E . n 
A 1 133 PHE 133 133 133 PHE PHE E . n 
A 1 134 PRO 134 134 134 PRO PRO E . n 
A 1 135 LEU 135 135 135 LEU LEU E . n 
A 1 136 ALA 136 136 136 ALA ALA E . n 
A 1 137 PRO 137 137 137 PRO PRO E . n 
A 1 138 SER 138 138 ?   ?   ?   E . n 
A 1 139 SER 139 139 ?   ?   ?   E . n 
A 1 140 LYS 140 140 ?   ?   ?   E . n 
A 1 141 SER 141 141 ?   ?   ?   E . n 
A 1 142 THR 142 142 ?   ?   ?   E . n 
A 1 143 SER 143 143 ?   ?   ?   E . n 
A 1 144 GLY 144 144 ?   ?   ?   E . n 
A 1 145 GLY 145 145 145 GLY GLY E . n 
A 1 146 THR 146 146 146 THR THR E . n 
A 1 147 ALA 147 147 147 ALA ALA E . n 
A 1 148 ALA 148 148 148 ALA ALA E . n 
A 1 149 LEU 149 149 149 LEU LEU E . n 
A 1 150 GLY 150 150 150 GLY GLY E . n 
A 1 151 CYS 151 151 151 CYS CYS E . n 
A 1 152 LEU 152 152 152 LEU LEU E . n 
A 1 153 VAL 153 153 153 VAL VAL E . n 
A 1 154 LYS 154 154 154 LYS LYS E . n 
A 1 155 ASP 155 155 155 ASP ASP E . n 
A 1 156 TYR 156 156 156 TYR TYR E . n 
A 1 157 PHE 157 157 157 PHE PHE E . n 
A 1 158 PRO 158 158 158 PRO PRO E . n 
A 1 159 GLU 159 159 159 GLU GLU E . n 
A 1 160 PRO 160 160 160 PRO PRO E . n 
A 1 161 VAL 161 161 161 VAL VAL E . n 
A 1 162 THR 162 162 162 THR THR E . n 
A 1 163 VAL 163 163 163 VAL VAL E . n 
A 1 164 SER 164 164 164 SER SER E . n 
A 1 165 TRP 165 165 165 TRP TRP E . n 
A 1 166 ASN 166 166 166 ASN ASN E . n 
A 1 167 SER 167 167 167 SER SER E . n 
A 1 168 GLY 168 168 168 GLY GLY E . n 
A 1 169 ALA 169 169 169 ALA ALA E . n 
A 1 170 LEU 170 170 170 LEU LEU E . n 
A 1 171 THR 171 171 171 THR THR E . n 
A 1 172 SER 172 172 172 SER SER E . n 
A 1 173 GLY 173 173 173 GLY GLY E . n 
A 1 174 VAL 174 174 174 VAL VAL E . n 
A 1 175 HIS 175 175 175 HIS HIS E . n 
A 1 176 THR 176 176 176 THR THR E . n 
A 1 177 PHE 177 177 177 PHE PHE E . n 
A 1 178 PRO 178 178 178 PRO PRO E . n 
A 1 179 ALA 179 179 179 ALA ALA E . n 
A 1 180 VAL 180 180 180 VAL VAL E . n 
A 1 181 LEU 181 181 181 LEU LEU E . n 
A 1 182 GLN 182 182 182 GLN GLN E . n 
A 1 183 SER 183 183 183 SER SER E . n 
A 1 184 SER 184 184 184 SER SER E . n 
A 1 185 GLY 185 185 185 GLY GLY E . n 
A 1 186 LEU 186 186 186 LEU LEU E . n 
A 1 187 TYR 187 187 187 TYR TYR E . n 
A 1 188 SER 188 188 188 SER SER E . n 
A 1 189 LEU 189 189 189 LEU LEU E . n 
A 1 190 SER 190 190 190 SER SER E . n 
A 1 191 SER 191 191 191 SER SER E . n 
A 1 192 VAL 192 192 192 VAL VAL E . n 
A 1 193 VAL 193 193 193 VAL VAL E . n 
A 1 194 THR 194 194 194 THR THR E . n 
A 1 195 VAL 195 195 195 VAL VAL E . n 
A 1 196 PRO 196 196 196 PRO PRO E . n 
A 1 197 SER 197 197 197 SER SER E . n 
A 1 198 SER 198 198 198 SER SER E . n 
A 1 199 SER 199 199 199 SER SER E . n 
A 1 200 LEU 200 200 200 LEU LEU E . n 
A 1 201 GLY 201 201 201 GLY GLY E . n 
A 1 202 THR 202 202 202 THR THR E . n 
A 1 203 GLN 203 203 203 GLN GLN E . n 
A 1 204 THR 204 204 204 THR THR E . n 
A 1 205 TYR 205 205 205 TYR TYR E . n 
A 1 206 ILE 206 206 206 ILE ILE E . n 
A 1 207 CYS 207 207 207 CYS CYS E . n 
A 1 208 ASN 208 208 208 ASN ASN E . n 
A 1 209 VAL 209 209 209 VAL VAL E . n 
A 1 210 ASN 210 210 210 ASN ASN E . n 
A 1 211 HIS 211 211 211 HIS HIS E . n 
A 1 212 LYS 212 212 212 LYS LYS E . n 
A 1 213 PRO 213 213 213 PRO PRO E . n 
A 1 214 SER 214 214 214 SER SER E . n 
A 1 215 ASN 215 215 215 ASN ASN E . n 
A 1 216 THR 216 216 216 THR THR E . n 
A 1 217 LYS 217 217 217 LYS LYS E . n 
A 1 218 VAL 218 218 218 VAL VAL E . n 
A 1 219 ASP 219 219 219 ASP ASP E . n 
A 1 220 LYS 220 220 220 LYS LYS E . n 
A 1 221 LYS 221 221 221 LYS LYS E . n 
A 1 222 VAL 222 222 222 VAL VAL E . n 
A 1 223 GLU 223 223 223 GLU GLU E . n 
A 1 224 PRO 224 224 224 PRO PRO E . n 
A 1 225 LYS 225 225 ?   ?   ?   E . n 
A 1 226 SER 226 226 ?   ?   ?   E . n 
A 1 227 CYS 227 227 ?   ?   ?   E . n 
A 1 228 ALA 228 228 ?   ?   ?   E . n 
A 1 229 SER 229 229 ?   ?   ?   E . n 
A 1 230 LEU 230 230 ?   ?   ?   E . n 
A 1 231 VAL 231 231 ?   ?   ?   E . n 
A 1 232 PRO 232 232 ?   ?   ?   E . n 
A 1 233 ARG 233 233 ?   ?   ?   E . n 
A 1 234 GLY 234 234 ?   ?   ?   E . n 
A 1 235 SER 235 235 ?   ?   ?   E . n 
A 1 236 GLY 236 236 ?   ?   ?   E . n 
A 1 237 TRP 237 237 ?   ?   ?   E . n 
A 1 238 SER 238 238 ?   ?   ?   E . n 
A 1 239 HIS 239 239 ?   ?   ?   E . n 
A 1 240 PRO 240 240 ?   ?   ?   E . n 
A 1 241 GLN 241 241 ?   ?   ?   E . n 
A 1 242 PHE 242 242 ?   ?   ?   E . n 
A 1 243 GLU 243 243 ?   ?   ?   E . n 
A 1 244 LYS 244 244 ?   ?   ?   E . n 
A 1 245 GLY 245 245 ?   ?   ?   E . n 
A 1 246 GLY 246 246 ?   ?   ?   E . n 
A 1 247 GLY 247 247 ?   ?   ?   E . n 
A 1 248 SER 248 248 ?   ?   ?   E . n 
A 1 249 GLY 249 249 ?   ?   ?   E . n 
A 1 250 GLY 250 250 ?   ?   ?   E . n 
A 1 251 GLY 251 251 ?   ?   ?   E . n 
A 1 252 SER 252 252 ?   ?   ?   E . n 
A 1 253 GLY 253 253 ?   ?   ?   E . n 
A 1 254 GLY 254 254 ?   ?   ?   E . n 
A 1 255 GLY 255 255 ?   ?   ?   E . n 
A 1 256 SER 256 256 ?   ?   ?   E . n 
A 1 257 TRP 257 257 ?   ?   ?   E . n 
A 1 258 SER 258 258 ?   ?   ?   E . n 
A 1 259 HIS 259 259 ?   ?   ?   E . n 
A 1 260 PRO 260 260 ?   ?   ?   E . n 
A 1 261 GLN 261 261 ?   ?   ?   E . n 
A 1 262 PHE 262 262 ?   ?   ?   E . n 
A 1 263 GLU 263 263 ?   ?   ?   E . n 
A 1 264 LYS 264 264 ?   ?   ?   E . n 
B 2 1   SER 1   1   1   SER SER F . n 
B 2 2   PHE 2   2   2   PHE PHE F . n 
B 2 3   GLU 3   3   3   GLU GLU F . n 
B 2 4   LEU 4   4   4   LEU LEU F . n 
B 2 5   THR 5   5   5   THR THR F . n 
B 2 6   GLN 6   6   6   GLN GLN F . n 
B 2 7   PRO 7   7   7   PRO PRO F . n 
B 2 8   PRO 8   8   8   PRO PRO F . n 
B 2 9   SER 9   9   9   SER SER F . n 
B 2 10  VAL 10  10  10  VAL VAL F . n 
B 2 11  SER 11  11  11  SER SER F . n 
B 2 12  VAL 12  12  12  VAL VAL F . n 
B 2 13  SER 13  13  13  SER SER F . n 
B 2 14  PRO 14  14  14  PRO PRO F . n 
B 2 15  GLY 15  15  15  GLY GLY F . n 
B 2 16  GLN 16  16  16  GLN GLN F . n 
B 2 17  THR 17  17  17  THR THR F . n 
B 2 18  ALA 18  18  18  ALA ALA F . n 
B 2 19  ARG 19  19  19  ARG ARG F . n 
B 2 20  ILE 20  20  20  ILE ILE F . n 
B 2 21  THR 21  21  21  THR THR F . n 
B 2 22  CYS 22  22  22  CYS CYS F . n 
B 2 23  SER 23  23  23  SER SER F . n 
B 2 24  GLY 24  24  24  GLY GLY F . n 
B 2 25  ASP 25  25  25  ASP ASP F . n 
B 2 26  ALA 26  26  26  ALA ALA F . n 
B 2 27  LEU 27  27  27  LEU LEU F . n 
B 2 28  PRO 28  28  28  PRO PRO F . n 
B 2 29  LYS 29  29  29  LYS LYS F . n 
B 2 30  GLN 30  30  30  GLN GLN F . n 
B 2 31  TYR 31  31  31  TYR TYR F . n 
B 2 32  VAL 32  32  32  VAL VAL F . n 
B 2 33  TYR 33  33  33  TYR TYR F . n 
B 2 34  TRP 34  34  34  TRP TRP F . n 
B 2 35  TYR 35  35  35  TYR TYR F . n 
B 2 36  GLN 36  36  36  GLN GLN F . n 
B 2 37  GLN 37  37  37  GLN GLN F . n 
B 2 38  LYS 38  38  38  LYS LYS F . n 
B 2 39  PRO 39  39  39  PRO PRO F . n 
B 2 40  GLY 40  40  40  GLY GLY F . n 
B 2 41  GLN 41  41  41  GLN GLN F . n 
B 2 42  ALA 42  42  42  ALA ALA F . n 
B 2 43  PRO 43  43  43  PRO PRO F . n 
B 2 44  VAL 44  44  44  VAL VAL F . n 
B 2 45  LEU 45  45  45  LEU LEU F . n 
B 2 46  VAL 46  46  46  VAL VAL F . n 
B 2 47  ILE 47  47  47  ILE ILE F . n 
B 2 48  TYR 48  48  48  TYR TYR F . n 
B 2 49  LYS 49  49  49  LYS LYS F . n 
B 2 50  THR 50  50  50  THR THR F . n 
B 2 51  THR 51  51  51  THR THR F . n 
B 2 52  GLU 52  52  52  GLU GLU F . n 
B 2 53  ARG 53  53  53  ARG ARG F . n 
B 2 54  PRO 54  54  54  PRO PRO F . n 
B 2 55  SER 55  55  55  SER SER F . n 
B 2 56  GLY 56  56  56  GLY GLY F . n 
B 2 57  ILE 57  57  57  ILE ILE F . n 
B 2 58  PRO 58  58  58  PRO PRO F . n 
B 2 59  GLU 59  59  59  GLU GLU F . n 
B 2 60  ARG 60  60  60  ARG ARG F . n 
B 2 61  PHE 61  61  61  PHE PHE F . n 
B 2 62  SER 62  62  62  SER SER F . n 
B 2 63  ASP 63  63  63  ASP ASP F . n 
B 2 64  SER 64  64  64  SER SER F . n 
B 2 65  SER 65  65  65  SER SER F . n 
B 2 66  SER 66  66  66  SER SER F . n 
B 2 67  GLY 67  67  67  GLY GLY F . n 
B 2 68  THR 68  68  68  THR THR F . n 
B 2 69  THR 69  69  69  THR THR F . n 
B 2 70  VAL 70  70  70  VAL VAL F . n 
B 2 71  THR 71  71  71  THR THR F . n 
B 2 72  LEU 72  72  72  LEU LEU F . n 
B 2 73  THR 73  73  73  THR THR F . n 
B 2 74  ILE 74  74  74  ILE ILE F . n 
B 2 75  SER 75  75  75  SER SER F . n 
B 2 76  ALA 76  76  76  ALA ALA F . n 
B 2 77  ALA 77  77  77  ALA ALA F . n 
B 2 78  GLN 78  78  78  GLN GLN F . n 
B 2 79  ALA 79  79  79  ALA ALA F . n 
B 2 80  GLU 80  80  80  GLU GLU F . n 
B 2 81  ASP 81  81  81  ASP ASP F . n 
B 2 82  GLU 82  82  82  GLU GLU F . n 
B 2 83  ALA 83  83  83  ALA ALA F . n 
B 2 84  ASP 84  84  84  ASP ASP F . n 
B 2 85  TYR 85  85  85  TYR TYR F . n 
B 2 86  TYR 86  86  86  TYR TYR F . n 
B 2 87  CYS 87  87  87  CYS CYS F . n 
B 2 88  GLN 88  88  88  GLN GLN F . n 
B 2 89  SER 89  89  89  SER SER F . n 
B 2 90  VAL 90  90  90  VAL VAL F . n 
B 2 91  ASP 91  91  91  ASP ASP F . n 
B 2 92  SER 92  92  92  SER SER F . n 
B 2 93  SER 93  93  93  SER SER F . n 
B 2 94  GLY 94  94  94  GLY GLY F . n 
B 2 95  THR 95  95  95  THR THR F . n 
B 2 96  TYR 96  96  96  TYR TYR F . n 
B 2 97  VAL 97  97  97  VAL VAL F . n 
B 2 98  PHE 98  98  98  PHE PHE F . n 
B 2 99  GLY 99  99  99  GLY GLY F . n 
B 2 100 ILE 100 100 100 ILE ILE F . n 
B 2 101 GLY 101 101 101 GLY GLY F . n 
B 2 102 THR 102 102 102 THR THR F . n 
B 2 103 LYS 103 103 103 LYS LYS F . n 
B 2 104 VAL 104 104 104 VAL VAL F . n 
B 2 105 THR 105 105 105 THR THR F . n 
B 2 106 VAL 106 106 106 VAL VAL F . n 
B 2 107 LEU 107 107 107 LEU LEU F . n 
B 2 108 GLY 108 108 108 GLY GLY F . n 
B 2 109 ARG 109 109 109 ARG ARG F . n 
B 2 110 THR 110 110 110 THR THR F . n 
B 2 111 VAL 111 111 111 VAL VAL F . n 
B 2 112 ALA 112 112 112 ALA ALA F . n 
B 2 113 ALA 113 113 113 ALA ALA F . n 
B 2 114 PRO 114 114 114 PRO PRO F . n 
B 2 115 SER 115 115 115 SER SER F . n 
B 2 116 VAL 116 116 116 VAL VAL F . n 
B 2 117 PHE 117 117 117 PHE PHE F . n 
B 2 118 ILE 118 118 118 ILE ILE F . n 
B 2 119 PHE 119 119 119 PHE PHE F . n 
B 2 120 PRO 120 120 120 PRO PRO F . n 
B 2 121 PRO 121 121 121 PRO PRO F . n 
B 2 122 SER 122 122 122 SER SER F . n 
B 2 123 ASP 123 123 123 ASP ASP F . n 
B 2 124 GLU 124 124 124 GLU GLU F . n 
B 2 125 GLN 125 125 125 GLN GLN F . n 
B 2 126 LEU 126 126 126 LEU LEU F . n 
B 2 127 LYS 127 127 127 LYS LYS F . n 
B 2 128 SER 128 128 128 SER SER F . n 
B 2 129 GLY 129 129 129 GLY GLY F . n 
B 2 130 THR 130 130 130 THR THR F . n 
B 2 131 ALA 131 131 131 ALA ALA F . n 
B 2 132 SER 132 132 132 SER SER F . n 
B 2 133 VAL 133 133 133 VAL VAL F . n 
B 2 134 VAL 134 134 134 VAL VAL F . n 
B 2 135 CYS 135 135 135 CYS CYS F . n 
B 2 136 LEU 136 136 136 LEU LEU F . n 
B 2 137 LEU 137 137 137 LEU LEU F . n 
B 2 138 ASN 138 138 138 ASN ASN F . n 
B 2 139 ASN 139 139 139 ASN ASN F . n 
B 2 140 PHE 140 140 140 PHE PHE F . n 
B 2 141 TYR 141 141 141 TYR TYR F . n 
B 2 142 PRO 142 142 142 PRO PRO F . n 
B 2 143 ARG 143 143 143 ARG ARG F . n 
B 2 144 GLU 144 144 144 GLU GLU F . n 
B 2 145 ALA 145 145 145 ALA ALA F . n 
B 2 146 LYS 146 146 146 LYS LYS F . n 
B 2 147 VAL 147 147 147 VAL VAL F . n 
B 2 148 GLN 148 148 148 GLN GLN F . n 
B 2 149 TRP 149 149 149 TRP TRP F . n 
B 2 150 LYS 150 150 150 LYS LYS F . n 
B 2 151 VAL 151 151 151 VAL VAL F . n 
B 2 152 ASP 152 152 152 ASP ASP F . n 
B 2 153 ASN 153 153 153 ASN ASN F . n 
B 2 154 ALA 154 154 154 ALA ALA F . n 
B 2 155 LEU 155 155 155 LEU LEU F . n 
B 2 156 GLN 156 156 156 GLN GLN F . n 
B 2 157 SER 157 157 157 SER SER F . n 
B 2 158 GLY 158 158 158 GLY GLY F . n 
B 2 159 ASN 159 159 159 ASN ASN F . n 
B 2 160 SER 160 160 160 SER SER F . n 
B 2 161 GLN 161 161 161 GLN GLN F . n 
B 2 162 GLU 162 162 162 GLU GLU F . n 
B 2 163 SER 163 163 163 SER SER F . n 
B 2 164 VAL 164 164 164 VAL VAL F . n 
B 2 165 THR 165 165 165 THR THR F . n 
B 2 166 GLU 166 166 166 GLU GLU F . n 
B 2 167 GLN 167 167 167 GLN GLN F . n 
B 2 168 ASP 168 168 168 ASP ASP F . n 
B 2 169 SER 169 169 169 SER SER F . n 
B 2 170 LYS 170 170 170 LYS LYS F . n 
B 2 171 ASP 171 171 171 ASP ASP F . n 
B 2 172 SER 172 172 172 SER SER F . n 
B 2 173 THR 173 173 173 THR THR F . n 
B 2 174 TYR 174 174 174 TYR TYR F . n 
B 2 175 SER 175 175 175 SER SER F . n 
B 2 176 LEU 176 176 176 LEU LEU F . n 
B 2 177 SER 177 177 177 SER SER F . n 
B 2 178 SER 178 178 178 SER SER F . n 
B 2 179 THR 179 179 179 THR THR F . n 
B 2 180 LEU 180 180 180 LEU LEU F . n 
B 2 181 THR 181 181 181 THR THR F . n 
B 2 182 LEU 182 182 182 LEU LEU F . n 
B 2 183 SER 183 183 183 SER SER F . n 
B 2 184 LYS 184 184 184 LYS LYS F . n 
B 2 185 ALA 185 185 185 ALA ALA F . n 
B 2 186 ASP 186 186 186 ASP ASP F . n 
B 2 187 TYR 187 187 187 TYR TYR F . n 
B 2 188 GLU 188 188 188 GLU GLU F . n 
B 2 189 LYS 189 189 189 LYS LYS F . n 
B 2 190 HIS 190 190 190 HIS HIS F . n 
B 2 191 LYS 191 191 191 LYS LYS F . n 
B 2 192 VAL 192 192 192 VAL VAL F . n 
B 2 193 TYR 193 193 193 TYR TYR F . n 
B 2 194 ALA 194 194 194 ALA ALA F . n 
B 2 195 CYS 195 195 195 CYS CYS F . n 
B 2 196 GLU 196 196 196 GLU GLU F . n 
B 2 197 VAL 197 197 197 VAL VAL F . n 
B 2 198 THR 198 198 198 THR THR F . n 
B 2 199 HIS 199 199 199 HIS HIS F . n 
B 2 200 GLN 200 200 200 GLN GLN F . n 
B 2 201 GLY 201 201 201 GLY GLY F . n 
B 2 202 LEU 202 202 202 LEU LEU F . n 
B 2 203 SER 203 203 203 SER SER F . n 
B 2 204 SER 204 204 204 SER SER F . n 
B 2 205 PRO 205 205 205 PRO PRO F . n 
B 2 206 VAL 206 206 206 VAL VAL F . n 
B 2 207 THR 207 207 207 THR THR F . n 
B 2 208 LYS 208 208 208 LYS LYS F . n 
B 2 209 SER 209 209 209 SER SER F . n 
B 2 210 PHE 210 210 210 PHE PHE F . n 
B 2 211 ASN 211 211 211 ASN ASN F . n 
B 2 212 ARG 212 212 212 ARG ARG F . n 
B 2 213 GLY 213 213 213 GLY GLY F . n 
B 2 214 GLU 214 214 ?   ?   ?   F . n 
B 2 215 CYS 215 215 ?   ?   ?   F . n 
C 1 1   GLN 1   1   1   GLN GLN D . n 
C 1 2   VAL 2   2   2   VAL VAL D . n 
C 1 3   HIS 3   3   3   HIS HIS D . n 
C 1 4   LEU 4   4   4   LEU LEU D . n 
C 1 5   VAL 5   5   5   VAL VAL D . n 
C 1 6   GLN 6   6   6   GLN GLN D . n 
C 1 7   SER 7   7   7   SER SER D . n 
C 1 8   GLY 8   8   8   GLY GLY D . n 
C 1 9   VAL 9   9   9   VAL VAL D . n 
C 1 10  GLU 10  10  10  GLU GLU D . n 
C 1 11  VAL 11  11  11  VAL VAL D . n 
C 1 12  LYS 12  12  12  LYS LYS D . n 
C 1 13  LYS 13  13  13  LYS LYS D . n 
C 1 14  PRO 14  14  14  PRO PRO D . n 
C 1 15  GLY 15  15  15  GLY GLY D . n 
C 1 16  ALA 16  16  16  ALA ALA D . n 
C 1 17  SER 17  17  17  SER SER D . n 
C 1 18  VAL 18  18  18  VAL VAL D . n 
C 1 19  ARG 19  19  19  ARG ARG D . n 
C 1 20  VAL 20  20  20  VAL VAL D . n 
C 1 21  SER 21  21  21  SER SER D . n 
C 1 22  CYS 22  22  22  CYS CYS D . n 
C 1 23  LYS 23  23  23  LYS LYS D . n 
C 1 24  ALA 24  24  24  ALA ALA D . n 
C 1 25  SER 25  25  25  SER SER D . n 
C 1 26  GLY 26  26  26  GLY GLY D . n 
C 1 27  TYR 27  27  27  TYR TYR D . n 
C 1 28  THR 28  28  28  THR THR D . n 
C 1 29  PHE 29  29  29  PHE PHE D . n 
C 1 30  ALA 30  30  30  ALA ALA D . n 
C 1 31  THR 31  31  31  THR THR D . n 
C 1 32  TYR 32  32  32  TYR TYR D . n 
C 1 33  GLY 33  33  33  GLY GLY D . n 
C 1 34  ILE 34  34  34  ILE ILE D . n 
C 1 35  THR 35  35  35  THR THR D . n 
C 1 36  TRP 36  36  36  TRP TRP D . n 
C 1 37  VAL 37  37  37  VAL VAL D . n 
C 1 38  ARG 38  38  38  ARG ARG D . n 
C 1 39  GLN 39  39  39  GLN GLN D . n 
C 1 40  ALA 40  40  40  ALA ALA D . n 
C 1 41  PRO 41  41  41  PRO PRO D . n 
C 1 42  GLY 42  42  42  GLY GLY D . n 
C 1 43  ARG 43  43  43  ARG ARG D . n 
C 1 44  GLY 44  44  44  GLY GLY D . n 
C 1 45  LEU 45  45  45  LEU LEU D . n 
C 1 46  GLU 46  46  46  GLU GLU D . n 
C 1 47  TRP 47  47  47  TRP TRP D . n 
C 1 48  VAL 48  48  48  VAL VAL D . n 
C 1 49  GLY 49  49  49  GLY GLY D . n 
C 1 50  TRP 50  50  50  TRP TRP D . n 
C 1 51  ILE 51  51  51  ILE ILE D . n 
C 1 52  THR 52  52  52  THR THR D . n 
C 1 53  PRO 53  53  53  PRO PRO D . n 
C 1 54  TYR 54  54  54  TYR TYR D . n 
C 1 55  ASN 55  55  55  ASN ASN D . n 
C 1 56  ASP 56  56  56  ASP ASP D . n 
C 1 57  ARG 57  57  57  ARG ARG D . n 
C 1 58  THR 58  58  58  THR THR D . n 
C 1 59  SER 59  59  59  SER SER D . n 
C 1 60  TYR 60  60  60  TYR TYR D . n 
C 1 61  ALA 61  61  61  ALA ALA D . n 
C 1 62  GLN 62  62  62  GLN GLN D . n 
C 1 63  ILE 63  63  63  ILE ILE D . n 
C 1 64  PHE 64  64  64  PHE PHE D . n 
C 1 65  HIS 65  65  65  HIS HIS D . n 
C 1 66  GLY 66  66  66  GLY GLY D . n 
C 1 67  ARG 67  67  67  ARG ARG D . n 
C 1 68  VAL 68  68  68  VAL VAL D . n 
C 1 69  THR 69  69  69  THR THR D . n 
C 1 70  MET 70  70  70  MET MET D . n 
C 1 71  THR 71  71  71  THR THR D . n 
C 1 72  THR 72  72  72  THR THR D . n 
C 1 73  ASP 73  73  73  ASP ASP D . n 
C 1 74  THR 74  74  74  THR THR D . n 
C 1 75  SER 75  75  75  SER SER D . n 
C 1 76  THR 76  76  76  THR THR D . n 
C 1 77  ASN 77  77  77  ASN ASN D . n 
C 1 78  THR 78  78  78  THR THR D . n 
C 1 79  ALA 79  79  79  ALA ALA D . n 
C 1 80  TYR 80  80  80  TYR TYR D . n 
C 1 81  MET 81  81  81  MET MET D . n 
C 1 82  GLU 82  82  82  GLU GLU D . n 
C 1 83  LEU 83  83  83  LEU LEU D . n 
C 1 84  ARG 84  84  84  ARG ARG D . n 
C 1 85  SER 85  85  85  SER SER D . n 
C 1 86  LEU 86  86  86  LEU LEU D . n 
C 1 87  ARG 87  87  87  ARG ARG D . n 
C 1 88  SER 88  88  88  SER SER D . n 
C 1 89  ASP 89  89  89  ASP ASP D . n 
C 1 90  ASP 90  90  90  ASP ASP D . n 
C 1 91  THR 91  91  91  THR THR D . n 
C 1 92  ALA 92  92  92  ALA ALA D . n 
C 1 93  MET 93  93  93  MET MET D . n 
C 1 94  TYR 94  94  94  TYR TYR D . n 
C 1 95  TYR 95  95  95  TYR TYR D . n 
C 1 96  CYS 96  96  96  CYS CYS D . n 
C 1 97  ALA 97  97  97  ALA ALA D . n 
C 1 98  ARG 98  98  98  ARG ARG D . n 
C 1 99  ASN 99  99  99  ASN ASN D . n 
C 1 100 HIS 100 100 100 HIS HIS D . n 
C 1 101 CYS 101 101 101 CYS CYS D . n 
C 1 102 ASN 102 102 102 ASN ASN D . n 
C 1 103 PHE 103 103 103 PHE PHE D . n 
C 1 104 TYR 104 104 104 TYR TYR D . n 
C 1 105 HIS 105 105 105 HIS HIS D . n 
C 1 106 ASP 106 106 106 ASP ASP D . n 
C 1 107 PHE 107 107 107 PHE PHE D . n 
C 1 108 TRP 108 108 108 TRP TRP D . n 
C 1 109 SER 109 109 109 SER SER D . n 
C 1 110 GLY 110 110 110 GLY GLY D . n 
C 1 111 LEU 111 111 111 LEU LEU D . n 
C 1 112 ASP 112 112 112 ASP ASP D . n 
C 1 113 TYR 113 113 113 TYR TYR D . n 
C 1 114 TRP 114 114 114 TRP TRP D . n 
C 1 115 GLY 115 115 115 GLY GLY D . n 
C 1 116 GLN 116 116 116 GLN GLN D . n 
C 1 117 GLY 117 117 117 GLY GLY D . n 
C 1 118 THR 118 118 118 THR THR D . n 
C 1 119 LEU 119 119 119 LEU LEU D . n 
C 1 120 VAL 120 120 120 VAL VAL D . n 
C 1 121 SER 121 121 121 SER SER D . n 
C 1 122 VAL 122 122 122 VAL VAL D . n 
C 1 123 SER 123 123 123 SER SER D . n 
C 1 124 SER 124 124 124 SER SER D . n 
C 1 125 ALA 125 125 125 ALA ALA D . n 
C 1 126 SER 126 126 126 SER SER D . n 
C 1 127 THR 127 127 127 THR THR D . n 
C 1 128 LYS 128 128 128 LYS LYS D . n 
C 1 129 GLY 129 129 129 GLY GLY D . n 
C 1 130 PRO 130 130 130 PRO PRO D . n 
C 1 131 SER 131 131 131 SER SER D . n 
C 1 132 VAL 132 132 132 VAL VAL D . n 
C 1 133 PHE 133 133 133 PHE PHE D . n 
C 1 134 PRO 134 134 134 PRO PRO D . n 
C 1 135 LEU 135 135 135 LEU LEU D . n 
C 1 136 ALA 136 136 136 ALA ALA D . n 
C 1 137 PRO 137 137 137 PRO PRO D . n 
C 1 138 SER 138 138 ?   ?   ?   D . n 
C 1 139 SER 139 139 ?   ?   ?   D . n 
C 1 140 LYS 140 140 ?   ?   ?   D . n 
C 1 141 SER 141 141 ?   ?   ?   D . n 
C 1 142 THR 142 142 ?   ?   ?   D . n 
C 1 143 SER 143 143 ?   ?   ?   D . n 
C 1 144 GLY 144 144 ?   ?   ?   D . n 
C 1 145 GLY 145 145 145 GLY GLY D . n 
C 1 146 THR 146 146 146 THR THR D . n 
C 1 147 ALA 147 147 147 ALA ALA D . n 
C 1 148 ALA 148 148 148 ALA ALA D . n 
C 1 149 LEU 149 149 149 LEU LEU D . n 
C 1 150 GLY 150 150 150 GLY GLY D . n 
C 1 151 CYS 151 151 151 CYS CYS D . n 
C 1 152 LEU 152 152 152 LEU LEU D . n 
C 1 153 VAL 153 153 153 VAL VAL D . n 
C 1 154 LYS 154 154 154 LYS LYS D . n 
C 1 155 ASP 155 155 155 ASP ASP D . n 
C 1 156 TYR 156 156 156 TYR TYR D . n 
C 1 157 PHE 157 157 157 PHE PHE D . n 
C 1 158 PRO 158 158 158 PRO PRO D . n 
C 1 159 GLU 159 159 159 GLU GLU D . n 
C 1 160 PRO 160 160 160 PRO PRO D . n 
C 1 161 VAL 161 161 161 VAL VAL D . n 
C 1 162 THR 162 162 162 THR THR D . n 
C 1 163 VAL 163 163 163 VAL VAL D . n 
C 1 164 SER 164 164 164 SER SER D . n 
C 1 165 TRP 165 165 165 TRP TRP D . n 
C 1 166 ASN 166 166 166 ASN ASN D . n 
C 1 167 SER 167 167 167 SER SER D . n 
C 1 168 GLY 168 168 168 GLY GLY D . n 
C 1 169 ALA 169 169 169 ALA ALA D . n 
C 1 170 LEU 170 170 170 LEU LEU D . n 
C 1 171 THR 171 171 171 THR THR D . n 
C 1 172 SER 172 172 172 SER SER D . n 
C 1 173 GLY 173 173 173 GLY GLY D . n 
C 1 174 VAL 174 174 174 VAL VAL D . n 
C 1 175 HIS 175 175 175 HIS HIS D . n 
C 1 176 THR 176 176 176 THR THR D . n 
C 1 177 PHE 177 177 177 PHE PHE D . n 
C 1 178 PRO 178 178 178 PRO PRO D . n 
C 1 179 ALA 179 179 179 ALA ALA D . n 
C 1 180 VAL 180 180 180 VAL VAL D . n 
C 1 181 LEU 181 181 181 LEU LEU D . n 
C 1 182 GLN 182 182 182 GLN GLN D . n 
C 1 183 SER 183 183 183 SER SER D . n 
C 1 184 SER 184 184 184 SER SER D . n 
C 1 185 GLY 185 185 185 GLY GLY D . n 
C 1 186 LEU 186 186 186 LEU LEU D . n 
C 1 187 TYR 187 187 187 TYR TYR D . n 
C 1 188 SER 188 188 188 SER SER D . n 
C 1 189 LEU 189 189 189 LEU LEU D . n 
C 1 190 SER 190 190 190 SER SER D . n 
C 1 191 SER 191 191 191 SER SER D . n 
C 1 192 VAL 192 192 192 VAL VAL D . n 
C 1 193 VAL 193 193 193 VAL VAL D . n 
C 1 194 THR 194 194 194 THR THR D . n 
C 1 195 VAL 195 195 195 VAL VAL D . n 
C 1 196 PRO 196 196 196 PRO PRO D . n 
C 1 197 SER 197 197 197 SER SER D . n 
C 1 198 SER 198 198 198 SER SER D . n 
C 1 199 SER 199 199 199 SER SER D . n 
C 1 200 LEU 200 200 200 LEU LEU D . n 
C 1 201 GLY 201 201 201 GLY GLY D . n 
C 1 202 THR 202 202 202 THR THR D . n 
C 1 203 GLN 203 203 203 GLN GLN D . n 
C 1 204 THR 204 204 204 THR THR D . n 
C 1 205 TYR 205 205 205 TYR TYR D . n 
C 1 206 ILE 206 206 206 ILE ILE D . n 
C 1 207 CYS 207 207 207 CYS CYS D . n 
C 1 208 ASN 208 208 208 ASN ASN D . n 
C 1 209 VAL 209 209 209 VAL VAL D . n 
C 1 210 ASN 210 210 210 ASN ASN D . n 
C 1 211 HIS 211 211 211 HIS HIS D . n 
C 1 212 LYS 212 212 212 LYS LYS D . n 
C 1 213 PRO 213 213 213 PRO PRO D . n 
C 1 214 SER 214 214 214 SER SER D . n 
C 1 215 ASN 215 215 215 ASN ASN D . n 
C 1 216 THR 216 216 216 THR THR D . n 
C 1 217 LYS 217 217 217 LYS LYS D . n 
C 1 218 VAL 218 218 218 VAL VAL D . n 
C 1 219 ASP 219 219 219 ASP ASP D . n 
C 1 220 LYS 220 220 220 LYS LYS D . n 
C 1 221 LYS 221 221 221 LYS LYS D . n 
C 1 222 VAL 222 222 222 VAL VAL D . n 
C 1 223 GLU 223 223 223 GLU GLU D . n 
C 1 224 PRO 224 224 224 PRO PRO D . n 
C 1 225 LYS 225 225 ?   ?   ?   D . n 
C 1 226 SER 226 226 ?   ?   ?   D . n 
C 1 227 CYS 227 227 ?   ?   ?   D . n 
C 1 228 ALA 228 228 ?   ?   ?   D . n 
C 1 229 SER 229 229 ?   ?   ?   D . n 
C 1 230 LEU 230 230 ?   ?   ?   D . n 
C 1 231 VAL 231 231 ?   ?   ?   D . n 
C 1 232 PRO 232 232 ?   ?   ?   D . n 
C 1 233 ARG 233 233 ?   ?   ?   D . n 
C 1 234 GLY 234 234 ?   ?   ?   D . n 
C 1 235 SER 235 235 ?   ?   ?   D . n 
C 1 236 GLY 236 236 ?   ?   ?   D . n 
C 1 237 TRP 237 237 ?   ?   ?   D . n 
C 1 238 SER 238 238 ?   ?   ?   D . n 
C 1 239 HIS 239 239 ?   ?   ?   D . n 
C 1 240 PRO 240 240 ?   ?   ?   D . n 
C 1 241 GLN 241 241 ?   ?   ?   D . n 
C 1 242 PHE 242 242 ?   ?   ?   D . n 
C 1 243 GLU 243 243 ?   ?   ?   D . n 
C 1 244 LYS 244 244 ?   ?   ?   D . n 
C 1 245 GLY 245 245 ?   ?   ?   D . n 
C 1 246 GLY 246 246 ?   ?   ?   D . n 
C 1 247 GLY 247 247 ?   ?   ?   D . n 
C 1 248 SER 248 248 ?   ?   ?   D . n 
C 1 249 GLY 249 249 ?   ?   ?   D . n 
C 1 250 GLY 250 250 ?   ?   ?   D . n 
C 1 251 GLY 251 251 ?   ?   ?   D . n 
C 1 252 SER 252 252 ?   ?   ?   D . n 
C 1 253 GLY 253 253 ?   ?   ?   D . n 
C 1 254 GLY 254 254 ?   ?   ?   D . n 
C 1 255 GLY 255 255 ?   ?   ?   D . n 
C 1 256 SER 256 256 ?   ?   ?   D . n 
C 1 257 TRP 257 257 ?   ?   ?   D . n 
C 1 258 SER 258 258 ?   ?   ?   D . n 
C 1 259 HIS 259 259 ?   ?   ?   D . n 
C 1 260 PRO 260 260 ?   ?   ?   D . n 
C 1 261 GLN 261 261 ?   ?   ?   D . n 
C 1 262 PHE 262 262 ?   ?   ?   D . n 
C 1 263 GLU 263 263 ?   ?   ?   D . n 
C 1 264 LYS 264 264 ?   ?   ?   D . n 
D 2 1   SER 1   1   1   SER SER G . n 
D 2 2   PHE 2   2   2   PHE PHE G . n 
D 2 3   GLU 3   3   3   GLU GLU G . n 
D 2 4   LEU 4   4   4   LEU LEU G . n 
D 2 5   THR 5   5   5   THR THR G . n 
D 2 6   GLN 6   6   6   GLN GLN G . n 
D 2 7   PRO 7   7   7   PRO PRO G . n 
D 2 8   PRO 8   8   8   PRO PRO G . n 
D 2 9   SER 9   9   9   SER SER G . n 
D 2 10  VAL 10  10  10  VAL VAL G . n 
D 2 11  SER 11  11  11  SER SER G . n 
D 2 12  VAL 12  12  12  VAL VAL G . n 
D 2 13  SER 13  13  13  SER SER G . n 
D 2 14  PRO 14  14  14  PRO PRO G . n 
D 2 15  GLY 15  15  15  GLY GLY G . n 
D 2 16  GLN 16  16  16  GLN GLN G . n 
D 2 17  THR 17  17  17  THR THR G . n 
D 2 18  ALA 18  18  18  ALA ALA G . n 
D 2 19  ARG 19  19  19  ARG ARG G . n 
D 2 20  ILE 20  20  20  ILE ILE G . n 
D 2 21  THR 21  21  21  THR THR G . n 
D 2 22  CYS 22  22  22  CYS CYS G . n 
D 2 23  SER 23  23  23  SER SER G . n 
D 2 24  GLY 24  24  24  GLY GLY G . n 
D 2 25  ASP 25  25  25  ASP ASP G . n 
D 2 26  ALA 26  26  26  ALA ALA G . n 
D 2 27  LEU 27  27  27  LEU LEU G . n 
D 2 28  PRO 28  28  28  PRO PRO G . n 
D 2 29  LYS 29  29  29  LYS LYS G . n 
D 2 30  GLN 30  30  30  GLN GLN G . n 
D 2 31  TYR 31  31  31  TYR TYR G . n 
D 2 32  VAL 32  32  32  VAL VAL G . n 
D 2 33  TYR 33  33  33  TYR TYR G . n 
D 2 34  TRP 34  34  34  TRP TRP G . n 
D 2 35  TYR 35  35  35  TYR TYR G . n 
D 2 36  GLN 36  36  36  GLN GLN G . n 
D 2 37  GLN 37  37  37  GLN GLN G . n 
D 2 38  LYS 38  38  38  LYS LYS G . n 
D 2 39  PRO 39  39  39  PRO PRO G . n 
D 2 40  GLY 40  40  40  GLY GLY G . n 
D 2 41  GLN 41  41  41  GLN GLN G . n 
D 2 42  ALA 42  42  42  ALA ALA G . n 
D 2 43  PRO 43  43  43  PRO PRO G . n 
D 2 44  VAL 44  44  44  VAL VAL G . n 
D 2 45  LEU 45  45  45  LEU LEU G . n 
D 2 46  VAL 46  46  46  VAL VAL G . n 
D 2 47  ILE 47  47  47  ILE ILE G . n 
D 2 48  TYR 48  48  48  TYR TYR G . n 
D 2 49  LYS 49  49  49  LYS LYS G . n 
D 2 50  THR 50  50  50  THR THR G . n 
D 2 51  THR 51  51  51  THR THR G . n 
D 2 52  GLU 52  52  52  GLU GLU G . n 
D 2 53  ARG 53  53  53  ARG ARG G . n 
D 2 54  PRO 54  54  54  PRO PRO G . n 
D 2 55  SER 55  55  55  SER SER G . n 
D 2 56  GLY 56  56  56  GLY GLY G . n 
D 2 57  ILE 57  57  57  ILE ILE G . n 
D 2 58  PRO 58  58  58  PRO PRO G . n 
D 2 59  GLU 59  59  59  GLU GLU G . n 
D 2 60  ARG 60  60  60  ARG ARG G . n 
D 2 61  PHE 61  61  61  PHE PHE G . n 
D 2 62  SER 62  62  62  SER SER G . n 
D 2 63  ASP 63  63  63  ASP ASP G . n 
D 2 64  SER 64  64  64  SER SER G . n 
D 2 65  SER 65  65  65  SER SER G . n 
D 2 66  SER 66  66  66  SER SER G . n 
D 2 67  GLY 67  67  67  GLY GLY G . n 
D 2 68  THR 68  68  68  THR THR G . n 
D 2 69  THR 69  69  69  THR THR G . n 
D 2 70  VAL 70  70  70  VAL VAL G . n 
D 2 71  THR 71  71  71  THR THR G . n 
D 2 72  LEU 72  72  72  LEU LEU G . n 
D 2 73  THR 73  73  73  THR THR G . n 
D 2 74  ILE 74  74  74  ILE ILE G . n 
D 2 75  SER 75  75  75  SER SER G . n 
D 2 76  ALA 76  76  76  ALA ALA G . n 
D 2 77  ALA 77  77  77  ALA ALA G . n 
D 2 78  GLN 78  78  78  GLN GLN G . n 
D 2 79  ALA 79  79  79  ALA ALA G . n 
D 2 80  GLU 80  80  80  GLU GLU G . n 
D 2 81  ASP 81  81  81  ASP ASP G . n 
D 2 82  GLU 82  82  82  GLU GLU G . n 
D 2 83  ALA 83  83  83  ALA ALA G . n 
D 2 84  ASP 84  84  84  ASP ASP G . n 
D 2 85  TYR 85  85  85  TYR TYR G . n 
D 2 86  TYR 86  86  86  TYR TYR G . n 
D 2 87  CYS 87  87  87  CYS CYS G . n 
D 2 88  GLN 88  88  88  GLN GLN G . n 
D 2 89  SER 89  89  89  SER SER G . n 
D 2 90  VAL 90  90  90  VAL VAL G . n 
D 2 91  ASP 91  91  91  ASP ASP G . n 
D 2 92  SER 92  92  92  SER SER G . n 
D 2 93  SER 93  93  93  SER SER G . n 
D 2 94  GLY 94  94  94  GLY GLY G . n 
D 2 95  THR 95  95  95  THR THR G . n 
D 2 96  TYR 96  96  96  TYR TYR G . n 
D 2 97  VAL 97  97  97  VAL VAL G . n 
D 2 98  PHE 98  98  98  PHE PHE G . n 
D 2 99  GLY 99  99  99  GLY GLY G . n 
D 2 100 ILE 100 100 100 ILE ILE G . n 
D 2 101 GLY 101 101 101 GLY GLY G . n 
D 2 102 THR 102 102 102 THR THR G . n 
D 2 103 LYS 103 103 103 LYS LYS G . n 
D 2 104 VAL 104 104 104 VAL VAL G . n 
D 2 105 THR 105 105 105 THR THR G . n 
D 2 106 VAL 106 106 106 VAL VAL G . n 
D 2 107 LEU 107 107 107 LEU LEU G . n 
D 2 108 GLY 108 108 108 GLY GLY G . n 
D 2 109 ARG 109 109 109 ARG ARG G . n 
D 2 110 THR 110 110 110 THR THR G . n 
D 2 111 VAL 111 111 111 VAL VAL G . n 
D 2 112 ALA 112 112 112 ALA ALA G . n 
D 2 113 ALA 113 113 113 ALA ALA G . n 
D 2 114 PRO 114 114 114 PRO PRO G . n 
D 2 115 SER 115 115 115 SER SER G . n 
D 2 116 VAL 116 116 116 VAL VAL G . n 
D 2 117 PHE 117 117 117 PHE PHE G . n 
D 2 118 ILE 118 118 118 ILE ILE G . n 
D 2 119 PHE 119 119 119 PHE PHE G . n 
D 2 120 PRO 120 120 120 PRO PRO G . n 
D 2 121 PRO 121 121 121 PRO PRO G . n 
D 2 122 SER 122 122 122 SER SER G . n 
D 2 123 ASP 123 123 123 ASP ASP G . n 
D 2 124 GLU 124 124 124 GLU GLU G . n 
D 2 125 GLN 125 125 125 GLN GLN G . n 
D 2 126 LEU 126 126 126 LEU LEU G . n 
D 2 127 LYS 127 127 127 LYS LYS G . n 
D 2 128 SER 128 128 128 SER SER G . n 
D 2 129 GLY 129 129 129 GLY GLY G . n 
D 2 130 THR 130 130 130 THR THR G . n 
D 2 131 ALA 131 131 131 ALA ALA G . n 
D 2 132 SER 132 132 132 SER SER G . n 
D 2 133 VAL 133 133 133 VAL VAL G . n 
D 2 134 VAL 134 134 134 VAL VAL G . n 
D 2 135 CYS 135 135 135 CYS CYS G . n 
D 2 136 LEU 136 136 136 LEU LEU G . n 
D 2 137 LEU 137 137 137 LEU LEU G . n 
D 2 138 ASN 138 138 138 ASN ASN G . n 
D 2 139 ASN 139 139 139 ASN ASN G . n 
D 2 140 PHE 140 140 140 PHE PHE G . n 
D 2 141 TYR 141 141 141 TYR TYR G . n 
D 2 142 PRO 142 142 142 PRO PRO G . n 
D 2 143 ARG 143 143 143 ARG ARG G . n 
D 2 144 GLU 144 144 144 GLU GLU G . n 
D 2 145 ALA 145 145 145 ALA ALA G . n 
D 2 146 LYS 146 146 146 LYS LYS G . n 
D 2 147 VAL 147 147 147 VAL VAL G . n 
D 2 148 GLN 148 148 148 GLN GLN G . n 
D 2 149 TRP 149 149 149 TRP TRP G . n 
D 2 150 LYS 150 150 150 LYS LYS G . n 
D 2 151 VAL 151 151 151 VAL VAL G . n 
D 2 152 ASP 152 152 152 ASP ASP G . n 
D 2 153 ASN 153 153 153 ASN ASN G . n 
D 2 154 ALA 154 154 154 ALA ALA G . n 
D 2 155 LEU 155 155 155 LEU LEU G . n 
D 2 156 GLN 156 156 156 GLN GLN G . n 
D 2 157 SER 157 157 157 SER SER G . n 
D 2 158 GLY 158 158 158 GLY GLY G . n 
D 2 159 ASN 159 159 159 ASN ASN G . n 
D 2 160 SER 160 160 160 SER SER G . n 
D 2 161 GLN 161 161 161 GLN GLN G . n 
D 2 162 GLU 162 162 162 GLU GLU G . n 
D 2 163 SER 163 163 163 SER SER G . n 
D 2 164 VAL 164 164 164 VAL VAL G . n 
D 2 165 THR 165 165 165 THR THR G . n 
D 2 166 GLU 166 166 166 GLU GLU G . n 
D 2 167 GLN 167 167 167 GLN GLN G . n 
D 2 168 ASP 168 168 168 ASP ASP G . n 
D 2 169 SER 169 169 169 SER SER G . n 
D 2 170 LYS 170 170 170 LYS LYS G . n 
D 2 171 ASP 171 171 171 ASP ASP G . n 
D 2 172 SER 172 172 172 SER SER G . n 
D 2 173 THR 173 173 173 THR THR G . n 
D 2 174 TYR 174 174 174 TYR TYR G . n 
D 2 175 SER 175 175 175 SER SER G . n 
D 2 176 LEU 176 176 176 LEU LEU G . n 
D 2 177 SER 177 177 177 SER SER G . n 
D 2 178 SER 178 178 178 SER SER G . n 
D 2 179 THR 179 179 179 THR THR G . n 
D 2 180 LEU 180 180 180 LEU LEU G . n 
D 2 181 THR 181 181 181 THR THR G . n 
D 2 182 LEU 182 182 182 LEU LEU G . n 
D 2 183 SER 183 183 183 SER SER G . n 
D 2 184 LYS 184 184 184 LYS LYS G . n 
D 2 185 ALA 185 185 185 ALA ALA G . n 
D 2 186 ASP 186 186 186 ASP ASP G . n 
D 2 187 TYR 187 187 187 TYR TYR G . n 
D 2 188 GLU 188 188 188 GLU GLU G . n 
D 2 189 LYS 189 189 189 LYS LYS G . n 
D 2 190 HIS 190 190 190 HIS HIS G . n 
D 2 191 LYS 191 191 191 LYS LYS G . n 
D 2 192 VAL 192 192 192 VAL VAL G . n 
D 2 193 TYR 193 193 193 TYR TYR G . n 
D 2 194 ALA 194 194 194 ALA ALA G . n 
D 2 195 CYS 195 195 195 CYS CYS G . n 
D 2 196 GLU 196 196 196 GLU GLU G . n 
D 2 197 VAL 197 197 197 VAL VAL G . n 
D 2 198 THR 198 198 198 THR THR G . n 
D 2 199 HIS 199 199 199 HIS HIS G . n 
D 2 200 GLN 200 200 200 GLN GLN G . n 
D 2 201 GLY 201 201 201 GLY GLY G . n 
D 2 202 LEU 202 202 202 LEU LEU G . n 
D 2 203 SER 203 203 203 SER SER G . n 
D 2 204 SER 204 204 204 SER SER G . n 
D 2 205 PRO 205 205 205 PRO PRO G . n 
D 2 206 VAL 206 206 206 VAL VAL G . n 
D 2 207 THR 207 207 207 THR THR G . n 
D 2 208 LYS 208 208 208 LYS LYS G . n 
D 2 209 SER 209 209 209 SER SER G . n 
D 2 210 PHE 210 210 210 PHE PHE G . n 
D 2 211 ASN 211 211 211 ASN ASN G . n 
D 2 212 ARG 212 212 212 ARG ARG G . n 
D 2 213 GLY 213 213 213 GLY GLY G . n 
D 2 214 GLU 214 214 ?   ?   ?   G . n 
D 2 215 CYS 215 215 ?   ?   ?   G . n 
E 3 1   MET 1   155 ?   ?   ?   A . n 
E 3 2   GLY 2   156 ?   ?   ?   A . n 
E 3 3   SER 3   157 ?   ?   ?   A . n 
E 3 4   LYS 4   158 ?   ?   ?   A . n 
E 3 5   PRO 5   159 ?   ?   ?   A . n 
E 3 6   ASN 6   160 ?   ?   ?   A . n 
E 3 7   ASN 7   161 161 ASN ASN A . n 
E 3 8   ASP 8   162 162 ASP ASP A . n 
E 3 9   PHE 9   163 163 PHE PHE A . n 
E 3 10  HIS 10  164 164 HIS HIS A . n 
E 3 11  PHE 11  165 165 PHE PHE A . n 
E 3 12  GLU 12  166 166 GLU GLU A . n 
E 3 13  VAL 13  167 167 VAL VAL A . n 
E 3 14  PHE 14  168 168 PHE PHE A . n 
E 3 15  ASN 15  169 169 ASN ASN A . n 
E 3 16  PHE 16  170 170 PHE PHE A . n 
E 3 17  VAL 17  171 171 VAL VAL A . n 
E 3 18  PRO 18  172 172 PRO PRO A . n 
E 3 19  CYS 19  173 173 CYS CYS A . n 
E 3 20  SER 20  174 174 SER SER A . n 
E 3 21  ILE 21  175 175 ILE ILE A . n 
E 3 22  CYS 22  176 176 CYS CYS A . n 
E 3 23  SER 23  177 177 SER SER A . n 
E 3 24  ASN 24  178 178 ASN ASN A . n 
E 3 25  ASN 25  179 179 ASN ASN A . n 
E 3 26  PRO 26  180 180 PRO PRO A . n 
E 3 27  THR 27  181 181 THR THR A . n 
E 3 28  CYS 28  182 182 CYS CYS A . n 
E 3 29  TRP 29  183 183 TRP TRP A . n 
E 3 30  ALA 30  184 184 ALA ALA A . n 
E 3 31  ILE 31  185 185 ILE ILE A . n 
E 3 32  CYS 32  186 186 CYS CYS A . n 
E 3 33  LYS 33  187 187 LYS LYS A . n 
E 3 34  ARG 34  188 188 ARG ARG A . n 
E 3 35  ILE 35  189 ?   ?   ?   A . n 
E 3 36  PRO 36  190 ?   ?   ?   A . n 
E 3 37  ASN 37  191 ?   ?   ?   A . n 
E 3 38  LYS 38  192 ?   ?   ?   A . n 
E 3 39  LYS 39  193 ?   ?   ?   A . n 
E 3 40  PRO 40  194 ?   ?   ?   A . n 
E 3 41  GLY 41  195 ?   ?   ?   A . n 
E 3 42  LYS 42  196 ?   ?   ?   A . n 
E 3 43  LYS 43  197 ?   ?   ?   A . n 
E 3 44  HIS 44  198 ?   ?   ?   A . n 
E 3 45  HIS 45  199 ?   ?   ?   A . n 
E 3 46  HIS 46  200 ?   ?   ?   A . n 
E 3 47  HIS 47  201 ?   ?   ?   A . n 
E 3 48  HIS 48  202 ?   ?   ?   A . n 
E 3 49  HIS 49  203 ?   ?   ?   A . n 
F 3 1   MET 1   155 ?   ?   ?   B . n 
F 3 2   GLY 2   156 ?   ?   ?   B . n 
F 3 3   SER 3   157 ?   ?   ?   B . n 
F 3 4   LYS 4   158 ?   ?   ?   B . n 
F 3 5   PRO 5   159 ?   ?   ?   B . n 
F 3 6   ASN 6   160 ?   ?   ?   B . n 
F 3 7   ASN 7   161 161 ASN ASN B . n 
F 3 8   ASP 8   162 162 ASP ASP B . n 
F 3 9   PHE 9   163 163 PHE PHE B . n 
F 3 10  HIS 10  164 164 HIS HIS B . n 
F 3 11  PHE 11  165 165 PHE PHE B . n 
F 3 12  GLU 12  166 166 GLU GLU B . n 
F 3 13  VAL 13  167 167 VAL VAL B . n 
F 3 14  PHE 14  168 168 PHE PHE B . n 
F 3 15  ASN 15  169 169 ASN ASN B . n 
F 3 16  PHE 16  170 170 PHE PHE B . n 
F 3 17  VAL 17  171 171 VAL VAL B . n 
F 3 18  PRO 18  172 172 PRO PRO B . n 
F 3 19  CYS 19  173 173 CYS CYS B . n 
F 3 20  SER 20  174 174 SER SER B . n 
F 3 21  ILE 21  175 175 ILE ILE B . n 
F 3 22  CYS 22  176 176 CYS CYS B . n 
F 3 23  SER 23  177 177 SER SER B . n 
F 3 24  ASN 24  178 178 ASN ASN B . n 
F 3 25  ASN 25  179 179 ASN ASN B . n 
F 3 26  PRO 26  180 180 PRO PRO B . n 
F 3 27  THR 27  181 181 THR THR B . n 
F 3 28  CYS 28  182 182 CYS CYS B . n 
F 3 29  TRP 29  183 183 TRP TRP B . n 
F 3 30  ALA 30  184 184 ALA ALA B . n 
F 3 31  ILE 31  185 185 ILE ILE B . n 
F 3 32  CYS 32  186 186 CYS CYS B . n 
F 3 33  LYS 33  187 187 LYS LYS B . n 
F 3 34  ARG 34  188 188 ARG ARG B . n 
F 3 35  ILE 35  189 ?   ?   ?   B . n 
F 3 36  PRO 36  190 ?   ?   ?   B . n 
F 3 37  ASN 37  191 ?   ?   ?   B . n 
F 3 38  LYS 38  192 ?   ?   ?   B . n 
F 3 39  LYS 39  193 ?   ?   ?   B . n 
F 3 40  PRO 40  194 ?   ?   ?   B . n 
F 3 41  GLY 41  195 ?   ?   ?   B . n 
F 3 42  LYS 42  196 ?   ?   ?   B . n 
F 3 43  LYS 43  197 ?   ?   ?   B . n 
F 3 44  HIS 44  198 ?   ?   ?   B . n 
F 3 45  HIS 45  199 ?   ?   ?   B . n 
F 3 46  HIS 46  200 ?   ?   ?   B . n 
F 3 47  HIS 47  201 ?   ?   ?   B . n 
F 3 48  HIS 48  202 ?   ?   ?   B . n 
F 3 49  HIS 49  203 ?   ?   ?   B . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
G 4 SO4 1   301 3   SO4 SO4 E . 
H 4 SO4 1   301 4   SO4 SO4 G . 
I 4 SO4 1   301 1   SO4 SO4 A . 
J 4 SO4 1   301 2   SO4 SO4 B . 
K 5 HOH 1   401 16  HOH HOH E . 
K 5 HOH 2   402 98  HOH HOH E . 
K 5 HOH 3   403 169 HOH HOH E . 
K 5 HOH 4   404 383 HOH HOH E . 
K 5 HOH 5   405 31  HOH HOH E . 
K 5 HOH 6   406 305 HOH HOH E . 
K 5 HOH 7   407 108 HOH HOH E . 
K 5 HOH 8   408 201 HOH HOH E . 
K 5 HOH 9   409 105 HOH HOH E . 
K 5 HOH 10  410 21  HOH HOH E . 
K 5 HOH 11  411 14  HOH HOH E . 
K 5 HOH 12  412 54  HOH HOH E . 
K 5 HOH 13  413 174 HOH HOH E . 
K 5 HOH 14  414 270 HOH HOH E . 
K 5 HOH 15  415 228 HOH HOH E . 
K 5 HOH 16  416 68  HOH HOH E . 
K 5 HOH 17  417 362 HOH HOH E . 
K 5 HOH 18  418 92  HOH HOH E . 
K 5 HOH 19  419 132 HOH HOH E . 
K 5 HOH 20  420 12  HOH HOH E . 
K 5 HOH 21  421 235 HOH HOH E . 
K 5 HOH 22  422 384 HOH HOH E . 
K 5 HOH 23  423 223 HOH HOH E . 
K 5 HOH 24  424 369 HOH HOH E . 
K 5 HOH 25  425 219 HOH HOH E . 
K 5 HOH 26  426 30  HOH HOH E . 
K 5 HOH 27  427 77  HOH HOH E . 
K 5 HOH 28  428 9   HOH HOH E . 
K 5 HOH 29  429 340 HOH HOH E . 
K 5 HOH 30  430 232 HOH HOH E . 
K 5 HOH 31  431 20  HOH HOH E . 
K 5 HOH 32  432 279 HOH HOH E . 
K 5 HOH 33  433 8   HOH HOH E . 
K 5 HOH 34  434 282 HOH HOH E . 
K 5 HOH 35  435 271 HOH HOH E . 
K 5 HOH 36  436 148 HOH HOH E . 
K 5 HOH 37  437 27  HOH HOH E . 
K 5 HOH 38  438 36  HOH HOH E . 
K 5 HOH 39  439 227 HOH HOH E . 
K 5 HOH 40  440 339 HOH HOH E . 
K 5 HOH 41  441 190 HOH HOH E . 
K 5 HOH 42  442 302 HOH HOH E . 
K 5 HOH 43  443 328 HOH HOH E . 
K 5 HOH 44  444 265 HOH HOH E . 
K 5 HOH 45  445 153 HOH HOH E . 
K 5 HOH 46  446 26  HOH HOH E . 
K 5 HOH 47  447 306 HOH HOH E . 
K 5 HOH 48  448 79  HOH HOH E . 
K 5 HOH 49  449 206 HOH HOH E . 
K 5 HOH 50  450 34  HOH HOH E . 
K 5 HOH 51  451 107 HOH HOH E . 
K 5 HOH 52  452 200 HOH HOH E . 
K 5 HOH 53  453 67  HOH HOH E . 
K 5 HOH 54  454 252 HOH HOH E . 
K 5 HOH 55  455 168 HOH HOH E . 
K 5 HOH 56  456 290 HOH HOH E . 
K 5 HOH 57  457 84  HOH HOH E . 
K 5 HOH 58  458 104 HOH HOH E . 
K 5 HOH 59  459 175 HOH HOH E . 
K 5 HOH 60  460 249 HOH HOH E . 
K 5 HOH 61  461 360 HOH HOH E . 
K 5 HOH 62  462 1   HOH HOH E . 
K 5 HOH 63  463 388 HOH HOH E . 
K 5 HOH 64  464 80  HOH HOH E . 
K 5 HOH 65  465 55  HOH HOH E . 
K 5 HOH 66  466 126 HOH HOH E . 
K 5 HOH 67  467 188 HOH HOH E . 
K 5 HOH 68  468 89  HOH HOH E . 
K 5 HOH 69  469 304 HOH HOH E . 
K 5 HOH 70  470 155 HOH HOH E . 
K 5 HOH 71  471 179 HOH HOH E . 
K 5 HOH 72  472 106 HOH HOH E . 
K 5 HOH 73  473 301 HOH HOH E . 
K 5 HOH 74  474 140 HOH HOH E . 
K 5 HOH 75  475 220 HOH HOH E . 
K 5 HOH 76  476 300 HOH HOH E . 
K 5 HOH 77  477 352 HOH HOH E . 
K 5 HOH 78  478 115 HOH HOH E . 
K 5 HOH 79  479 164 HOH HOH E . 
K 5 HOH 80  480 162 HOH HOH E . 
K 5 HOH 81  481 43  HOH HOH E . 
K 5 HOH 82  482 358 HOH HOH E . 
K 5 HOH 83  483 303 HOH HOH E . 
K 5 HOH 84  484 160 HOH HOH E . 
K 5 HOH 85  485 392 HOH HOH E . 
K 5 HOH 86  486 334 HOH HOH E . 
K 5 HOH 87  487 335 HOH HOH E . 
K 5 HOH 88  488 116 HOH HOH E . 
K 5 HOH 89  489 323 HOH HOH E . 
K 5 HOH 90  490 254 HOH HOH E . 
K 5 HOH 91  491 346 HOH HOH E . 
K 5 HOH 92  492 268 HOH HOH E . 
K 5 HOH 93  493 393 HOH HOH E . 
K 5 HOH 94  494 275 HOH HOH E . 
K 5 HOH 95  495 250 HOH HOH E . 
K 5 HOH 96  496 216 HOH HOH E . 
K 5 HOH 97  497 343 HOH HOH E . 
K 5 HOH 98  498 337 HOH HOH E . 
K 5 HOH 99  499 152 HOH HOH E . 
K 5 HOH 100 500 241 HOH HOH E . 
K 5 HOH 101 501 284 HOH HOH E . 
K 5 HOH 102 502 390 HOH HOH E . 
L 5 HOH 1   301 180 HOH HOH F . 
L 5 HOH 2   302 110 HOH HOH F . 
L 5 HOH 3   303 117 HOH HOH F . 
L 5 HOH 4   304 85  HOH HOH F . 
L 5 HOH 5   305 88  HOH HOH F . 
L 5 HOH 6   306 293 HOH HOH F . 
L 5 HOH 7   307 48  HOH HOH F . 
L 5 HOH 8   308 380 HOH HOH F . 
L 5 HOH 9   309 255 HOH HOH F . 
L 5 HOH 10  310 130 HOH HOH F . 
L 5 HOH 11  311 60  HOH HOH F . 
L 5 HOH 12  312 187 HOH HOH F . 
L 5 HOH 13  313 3   HOH HOH F . 
L 5 HOH 14  314 65  HOH HOH F . 
L 5 HOH 15  315 100 HOH HOH F . 
L 5 HOH 16  316 327 HOH HOH F . 
L 5 HOH 17  317 94  HOH HOH F . 
L 5 HOH 18  318 167 HOH HOH F . 
L 5 HOH 19  319 195 HOH HOH F . 
L 5 HOH 20  320 4   HOH HOH F . 
L 5 HOH 21  321 314 HOH HOH F . 
L 5 HOH 22  322 361 HOH HOH F . 
L 5 HOH 23  323 161 HOH HOH F . 
L 5 HOH 24  324 349 HOH HOH F . 
L 5 HOH 25  325 137 HOH HOH F . 
L 5 HOH 26  326 82  HOH HOH F . 
L 5 HOH 27  327 71  HOH HOH F . 
L 5 HOH 28  328 51  HOH HOH F . 
L 5 HOH 29  329 72  HOH HOH F . 
L 5 HOH 30  330 145 HOH HOH F . 
L 5 HOH 31  331 170 HOH HOH F . 
L 5 HOH 32  332 53  HOH HOH F . 
L 5 HOH 33  333 208 HOH HOH F . 
L 5 HOH 34  334 35  HOH HOH F . 
L 5 HOH 35  335 119 HOH HOH F . 
L 5 HOH 36  336 59  HOH HOH F . 
L 5 HOH 37  337 247 HOH HOH F . 
L 5 HOH 38  338 63  HOH HOH F . 
L 5 HOH 39  339 87  HOH HOH F . 
L 5 HOH 40  340 313 HOH HOH F . 
L 5 HOH 41  341 264 HOH HOH F . 
L 5 HOH 42  342 122 HOH HOH F . 
L 5 HOH 43  343 158 HOH HOH F . 
L 5 HOH 44  344 202 HOH HOH F . 
L 5 HOH 45  345 203 HOH HOH F . 
L 5 HOH 46  346 177 HOH HOH F . 
L 5 HOH 47  347 295 HOH HOH F . 
L 5 HOH 48  348 165 HOH HOH F . 
L 5 HOH 49  349 237 HOH HOH F . 
L 5 HOH 50  350 316 HOH HOH F . 
L 5 HOH 51  351 243 HOH HOH F . 
L 5 HOH 52  352 269 HOH HOH F . 
L 5 HOH 53  353 154 HOH HOH F . 
L 5 HOH 54  354 244 HOH HOH F . 
L 5 HOH 55  355 205 HOH HOH F . 
L 5 HOH 56  356 193 HOH HOH F . 
L 5 HOH 57  357 25  HOH HOH F . 
L 5 HOH 58  358 365 HOH HOH F . 
L 5 HOH 59  359 40  HOH HOH F . 
L 5 HOH 60  360 267 HOH HOH F . 
L 5 HOH 61  361 345 HOH HOH F . 
L 5 HOH 62  362 62  HOH HOH F . 
L 5 HOH 63  363 240 HOH HOH F . 
L 5 HOH 64  364 69  HOH HOH F . 
L 5 HOH 65  365 173 HOH HOH F . 
L 5 HOH 66  366 42  HOH HOH F . 
L 5 HOH 67  367 315 HOH HOH F . 
L 5 HOH 68  368 292 HOH HOH F . 
L 5 HOH 69  369 377 HOH HOH F . 
L 5 HOH 70  370 172 HOH HOH F . 
L 5 HOH 71  371 336 HOH HOH F . 
L 5 HOH 72  372 317 HOH HOH F . 
L 5 HOH 73  373 277 HOH HOH F . 
L 5 HOH 74  374 224 HOH HOH F . 
L 5 HOH 75  375 222 HOH HOH F . 
L 5 HOH 76  376 225 HOH HOH F . 
L 5 HOH 77  377 156 HOH HOH F . 
L 5 HOH 78  378 330 HOH HOH F . 
L 5 HOH 79  379 318 HOH HOH F . 
L 5 HOH 80  380 368 HOH HOH F . 
L 5 HOH 81  381 385 HOH HOH F . 
L 5 HOH 82  382 342 HOH HOH F . 
L 5 HOH 83  383 281 HOH HOH F . 
L 5 HOH 84  384 288 HOH HOH F . 
L 5 HOH 85  385 379 HOH HOH F . 
L 5 HOH 86  386 296 HOH HOH F . 
L 5 HOH 87  387 262 HOH HOH F . 
L 5 HOH 88  388 151 HOH HOH F . 
L 5 HOH 89  389 113 HOH HOH F . 
L 5 HOH 90  390 367 HOH HOH F . 
L 5 HOH 91  391 298 HOH HOH F . 
L 5 HOH 92  392 242 HOH HOH F . 
L 5 HOH 93  393 197 HOH HOH F . 
L 5 HOH 94  394 382 HOH HOH F . 
L 5 HOH 95  395 344 HOH HOH F . 
L 5 HOH 96  396 257 HOH HOH F . 
L 5 HOH 97  397 238 HOH HOH F . 
L 5 HOH 98  398 370 HOH HOH F . 
M 5 HOH 1   301 375 HOH HOH D . 
M 5 HOH 2   302 5   HOH HOH D . 
M 5 HOH 3   303 90  HOH HOH D . 
M 5 HOH 4   304 273 HOH HOH D . 
M 5 HOH 5   305 261 HOH HOH D . 
M 5 HOH 6   306 112 HOH HOH D . 
M 5 HOH 7   307 118 HOH HOH D . 
M 5 HOH 8   308 353 HOH HOH D . 
M 5 HOH 9   309 133 HOH HOH D . 
M 5 HOH 10  310 245 HOH HOH D . 
M 5 HOH 11  311 29  HOH HOH D . 
M 5 HOH 12  312 136 HOH HOH D . 
M 5 HOH 13  313 127 HOH HOH D . 
M 5 HOH 14  314 15  HOH HOH D . 
M 5 HOH 15  315 32  HOH HOH D . 
M 5 HOH 16  316 41  HOH HOH D . 
M 5 HOH 17  317 141 HOH HOH D . 
M 5 HOH 18  318 95  HOH HOH D . 
M 5 HOH 19  319 210 HOH HOH D . 
M 5 HOH 20  320 10  HOH HOH D . 
M 5 HOH 21  321 333 HOH HOH D . 
M 5 HOH 22  322 78  HOH HOH D . 
M 5 HOH 23  323 157 HOH HOH D . 
M 5 HOH 24  324 49  HOH HOH D . 
M 5 HOH 25  325 321 HOH HOH D . 
M 5 HOH 26  326 239 HOH HOH D . 
M 5 HOH 27  327 129 HOH HOH D . 
M 5 HOH 28  328 66  HOH HOH D . 
M 5 HOH 29  329 24  HOH HOH D . 
M 5 HOH 30  330 143 HOH HOH D . 
M 5 HOH 31  331 297 HOH HOH D . 
M 5 HOH 32  332 33  HOH HOH D . 
M 5 HOH 33  333 386 HOH HOH D . 
M 5 HOH 34  334 218 HOH HOH D . 
M 5 HOH 35  335 123 HOH HOH D . 
M 5 HOH 36  336 11  HOH HOH D . 
M 5 HOH 37  337 372 HOH HOH D . 
M 5 HOH 38  338 251 HOH HOH D . 
M 5 HOH 39  339 185 HOH HOH D . 
M 5 HOH 40  340 47  HOH HOH D . 
M 5 HOH 41  341 52  HOH HOH D . 
M 5 HOH 42  342 230 HOH HOH D . 
M 5 HOH 43  343 363 HOH HOH D . 
M 5 HOH 44  344 56  HOH HOH D . 
M 5 HOH 45  345 23  HOH HOH D . 
M 5 HOH 46  346 196 HOH HOH D . 
M 5 HOH 47  347 366 HOH HOH D . 
M 5 HOH 48  348 387 HOH HOH D . 
M 5 HOH 49  349 184 HOH HOH D . 
M 5 HOH 50  350 75  HOH HOH D . 
M 5 HOH 51  351 231 HOH HOH D . 
M 5 HOH 52  352 199 HOH HOH D . 
M 5 HOH 53  353 45  HOH HOH D . 
M 5 HOH 54  354 291 HOH HOH D . 
M 5 HOH 55  355 373 HOH HOH D . 
M 5 HOH 56  356 331 HOH HOH D . 
M 5 HOH 57  357 378 HOH HOH D . 
M 5 HOH 58  358 181 HOH HOH D . 
M 5 HOH 59  359 266 HOH HOH D . 
M 5 HOH 60  360 58  HOH HOH D . 
M 5 HOH 61  361 256 HOH HOH D . 
M 5 HOH 62  362 64  HOH HOH D . 
M 5 HOH 63  363 286 HOH HOH D . 
M 5 HOH 64  364 310 HOH HOH D . 
M 5 HOH 65  365 217 HOH HOH D . 
M 5 HOH 66  366 149 HOH HOH D . 
M 5 HOH 67  367 182 HOH HOH D . 
M 5 HOH 68  368 176 HOH HOH D . 
M 5 HOH 69  369 93  HOH HOH D . 
M 5 HOH 70  370 44  HOH HOH D . 
M 5 HOH 71  371 97  HOH HOH D . 
M 5 HOH 72  372 348 HOH HOH D . 
M 5 HOH 73  373 221 HOH HOH D . 
M 5 HOH 74  374 287 HOH HOH D . 
M 5 HOH 75  375 278 HOH HOH D . 
M 5 HOH 76  376 263 HOH HOH D . 
M 5 HOH 77  377 341 HOH HOH D . 
M 5 HOH 78  378 212 HOH HOH D . 
M 5 HOH 79  379 276 HOH HOH D . 
M 5 HOH 80  380 280 HOH HOH D . 
M 5 HOH 81  381 125 HOH HOH D . 
M 5 HOH 82  382 381 HOH HOH D . 
M 5 HOH 83  383 289 HOH HOH D . 
M 5 HOH 84  384 319 HOH HOH D . 
M 5 HOH 85  385 294 HOH HOH D . 
M 5 HOH 86  386 166 HOH HOH D . 
M 5 HOH 87  387 389 HOH HOH D . 
M 5 HOH 88  388 320 HOH HOH D . 
N 5 HOH 1   401 39  HOH HOH G . 
N 5 HOH 2   402 186 HOH HOH G . 
N 5 HOH 3   403 376 HOH HOH G . 
N 5 HOH 4   404 57  HOH HOH G . 
N 5 HOH 5   405 38  HOH HOH G . 
N 5 HOH 6   406 18  HOH HOH G . 
N 5 HOH 7   407 374 HOH HOH G . 
N 5 HOH 8   408 260 HOH HOH G . 
N 5 HOH 9   409 50  HOH HOH G . 
N 5 HOH 10  410 101 HOH HOH G . 
N 5 HOH 11  411 131 HOH HOH G . 
N 5 HOH 12  412 73  HOH HOH G . 
N 5 HOH 13  413 356 HOH HOH G . 
N 5 HOH 14  414 135 HOH HOH G . 
N 5 HOH 15  415 248 HOH HOH G . 
N 5 HOH 16  416 86  HOH HOH G . 
N 5 HOH 17  417 109 HOH HOH G . 
N 5 HOH 18  418 139 HOH HOH G . 
N 5 HOH 19  419 111 HOH HOH G . 
N 5 HOH 20  420 272 HOH HOH G . 
N 5 HOH 21  421 28  HOH HOH G . 
N 5 HOH 22  422 70  HOH HOH G . 
N 5 HOH 23  423 121 HOH HOH G . 
N 5 HOH 24  424 102 HOH HOH G . 
N 5 HOH 25  425 338 HOH HOH G . 
N 5 HOH 26  426 144 HOH HOH G . 
N 5 HOH 27  427 147 HOH HOH G . 
N 5 HOH 28  428 99  HOH HOH G . 
N 5 HOH 29  429 322 HOH HOH G . 
N 5 HOH 30  430 163 HOH HOH G . 
N 5 HOH 31  431 22  HOH HOH G . 
N 5 HOH 32  432 150 HOH HOH G . 
N 5 HOH 33  433 61  HOH HOH G . 
N 5 HOH 34  434 146 HOH HOH G . 
N 5 HOH 35  435 37  HOH HOH G . 
N 5 HOH 36  436 103 HOH HOH G . 
N 5 HOH 37  437 128 HOH HOH G . 
N 5 HOH 38  438 13  HOH HOH G . 
N 5 HOH 39  439 234 HOH HOH G . 
N 5 HOH 40  440 258 HOH HOH G . 
N 5 HOH 41  441 46  HOH HOH G . 
N 5 HOH 42  442 124 HOH HOH G . 
N 5 HOH 43  443 311 HOH HOH G . 
N 5 HOH 44  444 134 HOH HOH G . 
N 5 HOH 45  445 120 HOH HOH G . 
N 5 HOH 46  446 391 HOH HOH G . 
N 5 HOH 47  447 83  HOH HOH G . 
N 5 HOH 48  448 189 HOH HOH G . 
N 5 HOH 49  449 191 HOH HOH G . 
N 5 HOH 50  450 194 HOH HOH G . 
N 5 HOH 51  451 96  HOH HOH G . 
N 5 HOH 52  452 253 HOH HOH G . 
N 5 HOH 53  453 274 HOH HOH G . 
N 5 HOH 54  454 171 HOH HOH G . 
N 5 HOH 55  455 214 HOH HOH G . 
N 5 HOH 56  456 229 HOH HOH G . 
N 5 HOH 57  457 283 HOH HOH G . 
N 5 HOH 58  458 7   HOH HOH G . 
N 5 HOH 59  459 204 HOH HOH G . 
N 5 HOH 60  460 347 HOH HOH G . 
N 5 HOH 61  461 307 HOH HOH G . 
N 5 HOH 62  462 329 HOH HOH G . 
N 5 HOH 63  463 371 HOH HOH G . 
N 5 HOH 64  464 308 HOH HOH G . 
N 5 HOH 65  465 215 HOH HOH G . 
N 5 HOH 66  466 233 HOH HOH G . 
N 5 HOH 67  467 183 HOH HOH G . 
N 5 HOH 68  468 91  HOH HOH G . 
N 5 HOH 69  469 350 HOH HOH G . 
N 5 HOH 70  470 236 HOH HOH G . 
N 5 HOH 71  471 325 HOH HOH G . 
N 5 HOH 72  472 81  HOH HOH G . 
N 5 HOH 73  473 285 HOH HOH G . 
N 5 HOH 74  474 213 HOH HOH G . 
N 5 HOH 75  475 354 HOH HOH G . 
N 5 HOH 76  476 364 HOH HOH G . 
N 5 HOH 77  477 332 HOH HOH G . 
N 5 HOH 78  478 192 HOH HOH G . 
N 5 HOH 79  479 351 HOH HOH G . 
N 5 HOH 80  480 209 HOH HOH G . 
N 5 HOH 81  481 207 HOH HOH G . 
N 5 HOH 82  482 309 HOH HOH G . 
N 5 HOH 83  483 355 HOH HOH G . 
N 5 HOH 84  484 324 HOH HOH G . 
N 5 HOH 85  485 359 HOH HOH G . 
N 5 HOH 86  486 198 HOH HOH G . 
N 5 HOH 87  487 246 HOH HOH G . 
N 5 HOH 88  488 357 HOH HOH G . 
N 5 HOH 89  489 138 HOH HOH G . 
N 5 HOH 90  490 299 HOH HOH G . 
N 5 HOH 91  491 211 HOH HOH G . 
N 5 HOH 92  492 326 HOH HOH G . 
N 5 HOH 93  493 142 HOH HOH G . 
O 5 HOH 1   401 178 HOH HOH A . 
O 5 HOH 2   402 259 HOH HOH A . 
O 5 HOH 3   403 19  HOH HOH A . 
O 5 HOH 4   404 76  HOH HOH A . 
O 5 HOH 5   405 6   HOH HOH A . 
O 5 HOH 6   406 312 HOH HOH A . 
P 5 HOH 1   401 2   HOH HOH B . 
P 5 HOH 2   402 74  HOH HOH B . 
P 5 HOH 3   403 17  HOH HOH B . 
P 5 HOH 4   404 159 HOH HOH B . 
P 5 HOH 5   405 226 HOH HOH B . 
P 5 HOH 6   406 114 HOH HOH B . 
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX  ? ? ? '(1.20.1_4487: 000)' 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? XDS     ? ? ? .                    2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? Aimless ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHASER  ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9CQA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     76.418 
_cell.length_a_esd                 ? 
_cell.length_b                     80.753 
_cell.length_b_esd                 ? 
_cell.length_c                     175.181 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_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                         9CQA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_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                   9CQA 
_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             2.36 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          47.79 
_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 (pH 6.5), 0.2M Ammonium Sulfate, and 24.5% PEG 3350' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            295.15 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS EIGER X 16M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2022-04-22 
_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   1.033167 
_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                        'APS BEAMLINE 23-ID-B' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        1.033167 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       9CQA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.74 
_reflns.d_resolution_low                               47.32 
_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                                     110905 
_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                           99.2 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.2 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.6 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   .999 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.74 
_reflns_shell.d_res_low                                     1.77 
_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                             5008 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  .457 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 9CQA 
_refine.pdbx_refine_id                           'X-RAY DIFFRACTION' 
_refine.ls_abs_structure_details                 ? 
_refine.ls_abs_structure_Flack                   ? 
_refine.ls_abs_structure_Flack_esd               ? 
_refine.ls_abs_structure_Rogers                  ? 
_refine.ls_abs_structure_Rogers_esd              ? 
_refine.ls_d_res_high                            1.74 
_refine.ls_d_res_low                             47.32 
_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                     110700 
_refine.ls_number_reflns_R_free                  2004 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    99.07 
_refine.ls_percent_reflns_R_free                 1.81 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2111 
_refine.ls_R_factor_R_free                       0.2250 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2108 
_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                          1.34 
_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                 26.66 
_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                            0.21 
_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        7038 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         20 
_refine_hist.number_atoms_solvent             393 
_refine_hist.number_atoms_total               7451 
_refine_hist.d_res_high                       1.74 
_refine_hist.d_res_low                        47.32 
# 
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' ? 0.007  ? 7236 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.969  ? 9874 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 14.023 ? 2542 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.063  ? 1108 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.011  ? 1258 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.74 1.78  . . 129 7148 93.00  . . . . 0.3448 . . . . . . . . . . . 0.3247 
'X-RAY DIFFRACTION' 1.78 1.83  . . 142 7673 99.00  . . . . 0.3035 . . . . . . . . . . . 0.3059 
'X-RAY DIFFRACTION' 1.83 1.89  . . 147 7782 100.00 . . . . 0.2669 . . . . . . . . . . . 0.2631 
'X-RAY DIFFRACTION' 1.89 1.95  . . 130 7709 100.00 . . . . 0.2496 . . . . . . . . . . . 0.2683 
'X-RAY DIFFRACTION' 1.95 2.02  . . 148 7766 99.00  . . . . 0.2433 . . . . . . . . . . . 0.2944 
'X-RAY DIFFRACTION' 2.02 2.10  . . 147 7715 100.00 . . . . 0.2262 . . . . . . . . . . . 0.2563 
'X-RAY DIFFRACTION' 2.10 2.19  . . 144 7737 99.00  . . . . 0.2144 . . . . . . . . . . . 0.2314 
'X-RAY DIFFRACTION' 2.19 2.31  . . 134 7770 100.00 . . . . 0.2207 . . . . . . . . . . . 0.2568 
'X-RAY DIFFRACTION' 2.31 2.45  . . 154 7790 100.00 . . . . 0.2171 . . . . . . . . . . . 0.2488 
'X-RAY DIFFRACTION' 2.45 2.64  . . 131 7839 100.00 . . . . 0.2194 . . . . . . . . . . . 0.2263 
'X-RAY DIFFRACTION' 2.64 2.91  . . 159 7785 99.00  . . . . 0.2173 . . . . . . . . . . . 0.2293 
'X-RAY DIFFRACTION' 2.91 3.33  . . 143 7858 99.00  . . . . 0.2091 . . . . . . . . . . . 0.2074 
'X-RAY DIFFRACTION' 3.33 4.19  . . 144 7945 100.00 . . . . 0.1879 . . . . . . . . . . . 0.2115 
'X-RAY DIFFRACTION' 4.19 47.32 . . 152 8179 99.00  . . . . 0.1886 . . . . . . . . . . . 0.1944 
# 
_struct.entry_id                     9CQA 
_struct.title                        'Structure of antibody 1G1 bound to the central conserved region of RSV G' 
_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        9CQA 
_struct_keywords.text            
'antibody, respiratory syncytial virus, G glycoprotein, VIRAL PROTEIN, VIRAL PROTEIN-IMMUNE SYSTEM complex' 
_struct_keywords.pdbx_keywords   'VIRAL PROTEIN/IMMUNE SYSTEM' 
# 
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 2 ? 
C N N 1 ? 
D N N 2 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
I N N 4 ? 
J N N 4 ? 
K N N 5 ? 
L N N 5 ? 
M N N 5 ? 
N N N 5 ? 
O N N 5 ? 
P N N 5 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 PDB 9CQA       9CQA   ? 1 ?                                         1   
2 PDB 9CQA       9CQA   ? 2 ?                                         1   
3 UNP GLYC_HRSVA P03423 ? 3 SKPNNDFHFEVFNFVPCSICSNNPTCWAICKRIPNKKPGKK 157 
# 
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 9CQA E 1 ? 264 ? 9CQA   1   ? 264 ? 1   264 
2 2 9CQA F 1 ? 215 ? 9CQA   1   ? 215 ? 1   215 
3 1 9CQA D 1 ? 264 ? 9CQA   1   ? 264 ? 1   264 
4 2 9CQA G 1 ? 215 ? 9CQA   1   ? 215 ? 1   215 
5 3 9CQA A 3 ? 43  ? P03423 157 ? 197 ? 157 197 
6 3 9CQA B 3 ? 43  ? P03423 157 ? 197 ? 157 197 
# 
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 
5 9CQA MET A 1  ? UNP P03423 ? ? 'initiating methionine' 155 1  
5 9CQA GLY A 2  ? UNP P03423 ? ? 'expression tag'        156 2  
5 9CQA HIS A 44 ? UNP P03423 ? ? 'expression tag'        198 3  
5 9CQA HIS A 45 ? UNP P03423 ? ? 'expression tag'        199 4  
5 9CQA HIS A 46 ? UNP P03423 ? ? 'expression tag'        200 5  
5 9CQA HIS A 47 ? UNP P03423 ? ? 'expression tag'        201 6  
5 9CQA HIS A 48 ? UNP P03423 ? ? 'expression tag'        202 7  
5 9CQA HIS A 49 ? UNP P03423 ? ? 'expression tag'        203 8  
6 9CQA MET B 1  ? UNP P03423 ? ? 'initiating methionine' 155 9  
6 9CQA GLY B 2  ? UNP P03423 ? ? 'expression tag'        156 10 
6 9CQA HIS B 44 ? UNP P03423 ? ? 'expression tag'        198 11 
6 9CQA HIS B 45 ? UNP P03423 ? ? 'expression tag'        199 12 
6 9CQA HIS B 46 ? UNP P03423 ? ? 'expression tag'        200 13 
6 9CQA HIS B 47 ? UNP P03423 ? ? 'expression tag'        201 14 
6 9CQA HIS B 48 ? UNP P03423 ? ? 'expression tag'        202 15 
6 9CQA HIS B 49 ? UNP P03423 ? ? 'expression tag'        203 16 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA trimeric 3 
2 author_and_software_defined_assembly PISA trimeric 3 
# 
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)' 5690  ? 
1 MORE         -71   ? 
1 'SSA (A^2)'  21410 ? 
2 'ABSA (A^2)' 5290  ? 
2 MORE         -44   ? 
2 'SSA (A^2)'  21310 ? 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,B,E,G,I,K,L,O 
2 1 C,D,F,H,J,M,N,P 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   'gel filtration' 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1  AA1 THR A 28  ? TYR A 32  ? THR E 28  TYR E 32  5 ? 5 
HELX_P HELX_P2  AA2 GLN A 62  ? HIS A 65  ? GLN E 62  HIS E 65  5 ? 4 
HELX_P HELX_P3  AA3 ARG A 87  ? THR A 91  ? ARG E 87  THR E 91  5 ? 5 
HELX_P HELX_P4  AA4 SER A 167 ? ALA A 169 ? SER E 167 ALA E 169 5 ? 3 
HELX_P HELX_P5  AA5 SER A 198 ? GLY A 201 ? SER E 198 GLY E 201 5 ? 4 
HELX_P HELX_P6  AA6 LYS A 212 ? ASN A 215 ? LYS E 212 ASN E 215 5 ? 4 
HELX_P HELX_P7  AA7 GLN B 78  ? GLU B 82  ? GLN F 78  GLU F 82  5 ? 5 
HELX_P HELX_P8  AA8 SER B 122 ? SER B 128 ? SER F 122 SER F 128 1 ? 7 
HELX_P HELX_P9  AA9 LYS B 184 ? LYS B 189 ? LYS F 184 LYS F 189 1 ? 6 
HELX_P HELX_P10 AB1 THR C 28  ? TYR C 32  ? THR D 28  TYR D 32  5 ? 5 
HELX_P HELX_P11 AB2 GLN C 62  ? HIS C 65  ? GLN D 62  HIS D 65  5 ? 4 
HELX_P HELX_P12 AB3 ARG C 87  ? THR C 91  ? ARG D 87  THR D 91  5 ? 5 
HELX_P HELX_P13 AB4 SER C 167 ? ALA C 169 ? SER D 167 ALA D 169 5 ? 3 
HELX_P HELX_P14 AB5 SER C 198 ? LEU C 200 ? SER D 198 LEU D 200 5 ? 3 
HELX_P HELX_P15 AB6 LYS C 212 ? ASN C 215 ? LYS D 212 ASN D 215 5 ? 4 
HELX_P HELX_P16 AB7 GLN D 78  ? GLU D 82  ? GLN G 78  GLU G 82  5 ? 5 
HELX_P HELX_P17 AB8 SER D 122 ? SER D 128 ? SER G 122 SER G 128 1 ? 7 
HELX_P HELX_P18 AB9 LYS D 184 ? GLU D 188 ? LYS G 184 GLU G 188 1 ? 5 
HELX_P HELX_P19 AC1 PRO E 18  ? CYS E 22  ? PRO A 172 CYS A 176 5 ? 5 
HELX_P HELX_P20 AC2 ASN E 25  ? CYS E 32  ? ASN A 179 CYS A 186 1 ? 8 
HELX_P HELX_P21 AC3 PRO F 18  ? CYS F 22  ? PRO B 172 CYS B 176 5 ? 5 
HELX_P HELX_P22 AC4 ASN F 25  ? CYS F 32  ? ASN B 179 CYS B 186 1 ? 8 
# 
_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 
disulf1  disulf ? ? A CYS 22  SG ? ? ? 1_555 A CYS 96  SG ? ? E CYS 22  E CYS 96  1_555 ? ? ? ? ? ? ? 2.084 ? ? 
disulf2  disulf ? ? A CYS 151 SG ? ? ? 1_555 A CYS 207 SG ? ? E CYS 151 E CYS 207 1_555 ? ? ? ? ? ? ? 2.037 ? ? 
disulf3  disulf ? ? B CYS 22  SG ? ? ? 1_555 B CYS 87  SG ? ? F CYS 22  F CYS 87  1_555 ? ? ? ? ? ? ? 2.087 ? ? 
disulf4  disulf ? ? B CYS 135 SG ? ? ? 1_555 B CYS 195 SG ? ? F CYS 135 F CYS 195 1_555 ? ? ? ? ? ? ? 2.065 ? ? 
disulf5  disulf ? ? C CYS 22  SG ? ? ? 1_555 C CYS 96  SG ? ? D CYS 22  D CYS 96  1_555 ? ? ? ? ? ? ? 2.081 ? ? 
disulf6  disulf ? ? C CYS 151 SG ? ? ? 1_555 C CYS 207 SG ? ? D CYS 151 D CYS 207 1_555 ? ? ? ? ? ? ? 2.032 ? ? 
disulf7  disulf ? ? D CYS 22  SG ? ? ? 1_555 D CYS 87  SG ? ? G CYS 22  G CYS 87  1_555 ? ? ? ? ? ? ? 2.088 ? ? 
disulf8  disulf ? ? D CYS 135 SG ? ? ? 1_555 D CYS 195 SG ? ? G CYS 135 G CYS 195 1_555 ? ? ? ? ? ? ? 2.055 ? ? 
disulf9  disulf ? ? E CYS 19  SG ? ? ? 1_555 E CYS 32  SG ? ? A CYS 173 A CYS 186 1_555 ? ? ? ? ? ? ? 2.041 ? ? 
disulf10 disulf ? ? E CYS 22  SG ? ? ? 1_555 E CYS 28  SG ? ? A CYS 176 A CYS 182 1_555 ? ? ? ? ? ? ? 2.060 ? ? 
disulf11 disulf ? ? F CYS 19  SG ? ? ? 1_555 F CYS 32  SG ? ? B CYS 173 B CYS 186 1_555 ? ? ? ? ? ? ? 2.038 ? ? 
disulf12 disulf ? ? F CYS 22  SG ? ? ? 1_555 F CYS 28  SG ? ? B CYS 176 B CYS 182 1_555 ? ? ? ? ? ? ? 2.064 ? ? 
# 
_struct_conn_type.id          disulf 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1  CYS A 22  ? CYS A 96  ? CYS E 22  ? 1_555 CYS E 96  ? 1_555 SG SG . . . None 'Disulfide bridge' 
2  CYS A 151 ? CYS A 207 ? CYS E 151 ? 1_555 CYS E 207 ? 1_555 SG SG . . . None 'Disulfide bridge' 
3  CYS B 22  ? CYS B 87  ? CYS F 22  ? 1_555 CYS F 87  ? 1_555 SG SG . . . None 'Disulfide bridge' 
4  CYS B 135 ? CYS B 195 ? CYS F 135 ? 1_555 CYS F 195 ? 1_555 SG SG . . . None 'Disulfide bridge' 
5  CYS C 22  ? CYS C 96  ? CYS D 22  ? 1_555 CYS D 96  ? 1_555 SG SG . . . None 'Disulfide bridge' 
6  CYS C 151 ? CYS C 207 ? CYS D 151 ? 1_555 CYS D 207 ? 1_555 SG SG . . . None 'Disulfide bridge' 
7  CYS D 22  ? CYS D 87  ? CYS G 22  ? 1_555 CYS G 87  ? 1_555 SG SG . . . None 'Disulfide bridge' 
8  CYS D 135 ? CYS D 195 ? CYS G 135 ? 1_555 CYS G 195 ? 1_555 SG SG . . . None 'Disulfide bridge' 
9  CYS E 19  ? CYS E 32  ? CYS A 173 ? 1_555 CYS A 186 ? 1_555 SG SG . . . None 'Disulfide bridge' 
10 CYS E 22  ? CYS E 28  ? CYS A 176 ? 1_555 CYS A 182 ? 1_555 SG SG . . . None 'Disulfide bridge' 
11 CYS F 19  ? CYS F 32  ? CYS B 173 ? 1_555 CYS B 186 ? 1_555 SG SG . . . None 'Disulfide bridge' 
12 CYS F 22  ? CYS F 28  ? CYS B 176 ? 1_555 CYS B 182 ? 1_555 SG SG . . . None 'Disulfide bridge' 
# 
loop_
_struct_mon_prot_cis.pdbx_id 
_struct_mon_prot_cis.label_comp_id 
_struct_mon_prot_cis.label_seq_id 
_struct_mon_prot_cis.label_asym_id 
_struct_mon_prot_cis.label_alt_id 
_struct_mon_prot_cis.pdbx_PDB_ins_code 
_struct_mon_prot_cis.auth_comp_id 
_struct_mon_prot_cis.auth_seq_id 
_struct_mon_prot_cis.auth_asym_id 
_struct_mon_prot_cis.pdbx_label_comp_id_2 
_struct_mon_prot_cis.pdbx_label_seq_id_2 
_struct_mon_prot_cis.pdbx_label_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_ins_code_2 
_struct_mon_prot_cis.pdbx_auth_comp_id_2 
_struct_mon_prot_cis.pdbx_auth_seq_id_2 
_struct_mon_prot_cis.pdbx_auth_asym_id_2 
_struct_mon_prot_cis.pdbx_PDB_model_num 
_struct_mon_prot_cis.pdbx_omega_angle 
1 PHE 157 A . ? PHE 157 E PRO 158 A ? PRO 158 E 1 -5.10 
2 GLU 159 A . ? GLU 159 E PRO 160 A ? PRO 160 E 1 -2.29 
3 TYR 141 B . ? TYR 141 F PRO 142 B ? PRO 142 F 1 0.68  
4 PHE 157 C . ? PHE 157 D PRO 158 C ? PRO 158 D 1 -8.15 
5 GLU 159 C . ? GLU 159 D PRO 160 C ? PRO 160 D 1 -0.47 
6 TYR 141 D . ? TYR 141 G PRO 142 D ? PRO 142 G 1 4.76  
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 6 ? 
AA3 ? 2 ? 
AA4 ? 4 ? 
AA5 ? 4 ? 
AA6 ? 3 ? 
AA7 ? 5 ? 
AA8 ? 4 ? 
AA9 ? 3 ? 
AB1 ? 4 ? 
AB2 ? 4 ? 
AB3 ? 4 ? 
AB4 ? 6 ? 
AB5 ? 2 ? 
AB6 ? 4 ? 
AB7 ? 4 ? 
AB8 ? 3 ? 
AB9 ? 5 ? 
AC1 ? 4 ? 
AC2 ? 3 ? 
AC3 ? 4 ? 
AC4 ? 3 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? parallel      
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? anti-parallel 
AA4 3 4 ? anti-parallel 
AA5 1 2 ? anti-parallel 
AA5 2 3 ? anti-parallel 
AA5 3 4 ? anti-parallel 
AA6 1 2 ? anti-parallel 
AA6 2 3 ? anti-parallel 
AA7 1 2 ? parallel      
AA7 2 3 ? anti-parallel 
AA7 3 4 ? anti-parallel 
AA7 4 5 ? anti-parallel 
AA8 1 2 ? parallel      
AA8 2 3 ? anti-parallel 
AA8 3 4 ? anti-parallel 
AA9 1 2 ? anti-parallel 
AA9 2 3 ? anti-parallel 
AB1 1 2 ? anti-parallel 
AB1 2 3 ? anti-parallel 
AB1 3 4 ? anti-parallel 
AB2 1 2 ? anti-parallel 
AB2 2 3 ? anti-parallel 
AB2 3 4 ? anti-parallel 
AB3 1 2 ? anti-parallel 
AB3 2 3 ? anti-parallel 
AB3 3 4 ? anti-parallel 
AB4 1 2 ? parallel      
AB4 2 3 ? anti-parallel 
AB4 3 4 ? anti-parallel 
AB4 4 5 ? anti-parallel 
AB4 5 6 ? anti-parallel 
AB5 1 2 ? anti-parallel 
AB6 1 2 ? anti-parallel 
AB6 2 3 ? anti-parallel 
AB6 3 4 ? anti-parallel 
AB7 1 2 ? anti-parallel 
AB7 2 3 ? anti-parallel 
AB7 3 4 ? anti-parallel 
AB8 1 2 ? anti-parallel 
AB8 2 3 ? anti-parallel 
AB9 1 2 ? parallel      
AB9 2 3 ? anti-parallel 
AB9 3 4 ? anti-parallel 
AB9 4 5 ? anti-parallel 
AC1 1 2 ? parallel      
AC1 2 3 ? anti-parallel 
AC1 3 4 ? anti-parallel 
AC2 1 2 ? anti-parallel 
AC2 2 3 ? anti-parallel 
AC3 1 2 ? anti-parallel 
AC3 2 3 ? anti-parallel 
AC3 3 4 ? anti-parallel 
AC4 1 2 ? anti-parallel 
AC4 2 3 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 HIS A 3   ? GLN A 6   ? HIS E 3   GLN E 6   
AA1 2 VAL A 18  ? SER A 25  ? VAL E 18  SER E 25  
AA1 3 THR A 78  ? LEU A 83  ? THR E 78  LEU E 83  
AA1 4 VAL A 68  ? ASP A 73  ? VAL E 68  ASP E 73  
AA2 1 GLU A 10  ? LYS A 12  ? GLU E 10  LYS E 12  
AA2 2 THR A 118 ? VAL A 122 ? THR E 118 VAL E 122 
AA2 3 ALA A 92  ? ASN A 99  ? ALA E 92  ASN E 99  
AA2 4 GLY A 33  ? GLN A 39  ? GLY E 33  GLN E 39  
AA2 5 GLU A 46  ? THR A 52  ? GLU E 46  THR E 52  
AA2 6 ARG A 57  ? TYR A 60  ? ARG E 57  TYR E 60  
AA3 1 CYS A 101 ? ASN A 102 ? CYS E 101 ASN E 102 
AA3 2 PHE A 107 ? TRP A 108 ? PHE E 107 TRP E 108 
AA4 1 SER A 131 ? LEU A 135 ? SER E 131 LEU E 135 
AA4 2 THR A 146 ? TYR A 156 ? THR E 146 TYR E 156 
AA4 3 TYR A 187 ? PRO A 196 ? TYR E 187 PRO E 196 
AA4 4 VAL A 174 ? THR A 176 ? VAL E 174 THR E 176 
AA5 1 SER A 131 ? LEU A 135 ? SER E 131 LEU E 135 
AA5 2 THR A 146 ? TYR A 156 ? THR E 146 TYR E 156 
AA5 3 TYR A 187 ? PRO A 196 ? TYR E 187 PRO E 196 
AA5 4 VAL A 180 ? LEU A 181 ? VAL E 180 LEU E 181 
AA6 1 THR A 162 ? TRP A 165 ? THR E 162 TRP E 165 
AA6 2 ILE A 206 ? HIS A 211 ? ILE E 206 HIS E 211 
AA6 3 THR A 216 ? LYS A 221 ? THR E 216 LYS E 221 
AA7 1 SER B 9   ? VAL B 12  ? SER F 9   VAL F 12  
AA7 2 THR B 102 ? VAL B 106 ? THR F 102 VAL F 106 
AA7 3 ALA B 83  ? VAL B 90  ? ALA F 83  VAL F 90  
AA7 4 TYR B 33  ? GLN B 37  ? TYR F 33  GLN F 37  
AA7 5 VAL B 44  ? ILE B 47  ? VAL F 44  ILE F 47  
AA8 1 SER B 9   ? VAL B 12  ? SER F 9   VAL F 12  
AA8 2 THR B 102 ? VAL B 106 ? THR F 102 VAL F 106 
AA8 3 ALA B 83  ? VAL B 90  ? ALA F 83  VAL F 90  
AA8 4 TYR B 96  ? PHE B 98  ? TYR F 96  PHE F 98  
AA9 1 ALA B 18  ? SER B 23  ? ALA F 18  SER F 23  
AA9 2 THR B 69  ? ILE B 74  ? THR F 69  ILE F 74  
AA9 3 PHE B 61  ? SER B 66  ? PHE F 61  SER F 66  
AB1 1 SER B 115 ? PHE B 119 ? SER F 115 PHE F 119 
AB1 2 THR B 130 ? PHE B 140 ? THR F 130 PHE F 140 
AB1 3 TYR B 174 ? SER B 183 ? TYR F 174 SER F 183 
AB1 4 SER B 160 ? VAL B 164 ? SER F 160 VAL F 164 
AB2 1 ALA B 154 ? LEU B 155 ? ALA F 154 LEU F 155 
AB2 2 LYS B 146 ? VAL B 151 ? LYS F 146 VAL F 151 
AB2 3 VAL B 192 ? THR B 198 ? VAL F 192 THR F 198 
AB2 4 VAL B 206 ? ASN B 211 ? VAL F 206 ASN F 211 
AB3 1 HIS C 3   ? GLN C 6   ? HIS D 3   GLN D 6   
AB3 2 VAL C 18  ? SER C 25  ? VAL D 18  SER D 25  
AB3 3 THR C 78  ? LEU C 83  ? THR D 78  LEU D 83  
AB3 4 VAL C 68  ? ASP C 73  ? VAL D 68  ASP D 73  
AB4 1 GLU C 10  ? LYS C 12  ? GLU D 10  LYS D 12  
AB4 2 THR C 118 ? VAL C 122 ? THR D 118 VAL D 122 
AB4 3 ALA C 92  ? ASN C 99  ? ALA D 92  ASN D 99  
AB4 4 GLY C 33  ? GLN C 39  ? GLY D 33  GLN D 39  
AB4 5 GLU C 46  ? THR C 52  ? GLU D 46  THR D 52  
AB4 6 ARG C 57  ? TYR C 60  ? ARG D 57  TYR D 60  
AB5 1 CYS C 101 ? ASN C 102 ? CYS D 101 ASN D 102 
AB5 2 PHE C 107 ? TRP C 108 ? PHE D 107 TRP D 108 
AB6 1 SER C 131 ? LEU C 135 ? SER D 131 LEU D 135 
AB6 2 THR C 146 ? TYR C 156 ? THR D 146 TYR D 156 
AB6 3 TYR C 187 ? PRO C 196 ? TYR D 187 PRO D 196 
AB6 4 VAL C 174 ? THR C 176 ? VAL D 174 THR D 176 
AB7 1 SER C 131 ? LEU C 135 ? SER D 131 LEU D 135 
AB7 2 THR C 146 ? TYR C 156 ? THR D 146 TYR D 156 
AB7 3 TYR C 187 ? PRO C 196 ? TYR D 187 PRO D 196 
AB7 4 VAL C 180 ? LEU C 181 ? VAL D 180 LEU D 181 
AB8 1 THR C 162 ? TRP C 165 ? THR D 162 TRP D 165 
AB8 2 ILE C 206 ? HIS C 211 ? ILE D 206 HIS D 211 
AB8 3 THR C 216 ? LYS C 221 ? THR D 216 LYS D 221 
AB9 1 SER D 9   ? VAL D 12  ? SER G 9   VAL G 12  
AB9 2 THR D 102 ? VAL D 106 ? THR G 102 VAL G 106 
AB9 3 ALA D 83  ? VAL D 90  ? ALA G 83  VAL G 90  
AB9 4 TYR D 33  ? GLN D 37  ? TYR G 33  GLN G 37  
AB9 5 VAL D 44  ? ILE D 47  ? VAL G 44  ILE G 47  
AC1 1 SER D 9   ? VAL D 12  ? SER G 9   VAL G 12  
AC1 2 THR D 102 ? VAL D 106 ? THR G 102 VAL G 106 
AC1 3 ALA D 83  ? VAL D 90  ? ALA G 83  VAL G 90  
AC1 4 TYR D 96  ? PHE D 98  ? TYR G 96  PHE G 98  
AC2 1 ALA D 18  ? SER D 23  ? ALA G 18  SER G 23  
AC2 2 THR D 69  ? ILE D 74  ? THR G 69  ILE G 74  
AC2 3 PHE D 61  ? SER D 66  ? PHE G 61  SER G 66  
AC3 1 SER D 115 ? PHE D 119 ? SER G 115 PHE G 119 
AC3 2 THR D 130 ? PHE D 140 ? THR G 130 PHE G 140 
AC3 3 TYR D 174 ? SER D 183 ? TYR G 174 SER G 183 
AC3 4 SER D 160 ? VAL D 164 ? SER G 160 VAL G 164 
AC4 1 ALA D 145 ? VAL D 151 ? ALA G 145 VAL G 151 
AC4 2 VAL D 192 ? HIS D 199 ? VAL G 192 HIS G 199 
AC4 3 VAL D 206 ? ASN D 211 ? VAL G 206 ASN G 211 
# 
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 VAL A 5   ? N VAL E 5   O LYS A 23  ? O LYS E 23  
AA1 2 3 N CYS A 22  ? N CYS E 22  O ALA A 79  ? O ALA E 79  
AA1 3 4 O THR A 78  ? O THR E 78  N ASP A 73  ? N ASP E 73  
AA2 1 2 N LYS A 12  ? N LYS E 12  O SER A 121 ? O SER E 121 
AA2 2 3 O THR A 118 ? O THR E 118 N TYR A 94  ? N TYR E 94  
AA2 3 4 O TYR A 95  ? O TYR E 95  N VAL A 37  ? N VAL E 37  
AA2 4 5 N ARG A 38  ? N ARG E 38  O GLU A 46  ? O GLU E 46  
AA2 5 6 N THR A 52  ? N THR E 52  O ARG A 57  ? O ARG E 57  
AA3 1 2 N ASN A 102 ? N ASN E 102 O PHE A 107 ? O PHE E 107 
AA4 1 2 N LEU A 135 ? N LEU E 135 O GLY A 150 ? O GLY E 150 
AA4 2 3 N ALA A 147 ? N ALA E 147 O VAL A 195 ? O VAL E 195 
AA4 3 4 O VAL A 192 ? O VAL E 192 N HIS A 175 ? N HIS E 175 
AA5 1 2 N LEU A 135 ? N LEU E 135 O GLY A 150 ? O GLY E 150 
AA5 2 3 N ALA A 147 ? N ALA E 147 O VAL A 195 ? O VAL E 195 
AA5 3 4 O SER A 188 ? O SER E 188 N VAL A 180 ? N VAL E 180 
AA6 1 2 N SER A 164 ? N SER E 164 O ASN A 208 ? O ASN E 208 
AA6 2 3 N VAL A 209 ? N VAL E 209 O VAL A 218 ? O VAL E 218 
AA7 1 2 N VAL B 12  ? N VAL F 12  O THR B 105 ? O THR F 105 
AA7 2 3 O VAL B 104 ? O VAL F 104 N ALA B 83  ? N ALA F 83  
AA7 3 4 O ASP B 84  ? O ASP F 84  N GLN B 37  ? N GLN F 37  
AA7 4 5 N TRP B 34  ? N TRP F 34  O VAL B 46  ? O VAL F 46  
AA8 1 2 N VAL B 12  ? N VAL F 12  O THR B 105 ? O THR F 105 
AA8 2 3 O VAL B 104 ? O VAL F 104 N ALA B 83  ? N ALA F 83  
AA8 3 4 N SER B 89  ? N SER F 89  O VAL B 97  ? O VAL F 97  
AA9 1 2 N ILE B 20  ? N ILE F 20  O LEU B 72  ? O LEU F 72  
AA9 2 3 O THR B 73  ? O THR F 73  N SER B 62  ? N SER F 62  
AB1 1 2 N PHE B 117 ? N PHE F 117 O LEU B 136 ? O LEU F 136 
AB1 2 3 N ALA B 131 ? N ALA F 131 O LEU B 182 ? O LEU F 182 
AB1 3 4 O SER B 177 ? O SER F 177 N SER B 163 ? N SER F 163 
AB2 1 2 O ALA B 154 ? O ALA F 154 N VAL B 151 ? N VAL F 151 
AB2 2 3 N GLN B 148 ? N GLN F 148 O GLU B 196 ? O GLU F 196 
AB2 3 4 N VAL B 197 ? N VAL F 197 O VAL B 206 ? O VAL F 206 
AB3 1 2 N VAL C 5   ? N VAL D 5   O LYS C 23  ? O LYS D 23  
AB3 2 3 N VAL C 20  ? N VAL D 20  O MET C 81  ? O MET D 81  
AB3 3 4 O THR C 78  ? O THR D 78  N ASP C 73  ? N ASP D 73  
AB4 1 2 N LYS C 12  ? N LYS D 12  O SER C 121 ? O SER D 121 
AB4 2 3 O THR C 118 ? O THR D 118 N TYR C 94  ? N TYR D 94  
AB4 3 4 O TYR C 95  ? O TYR D 95  N VAL C 37  ? N VAL D 37  
AB4 4 5 N ARG C 38  ? N ARG D 38  O GLU C 46  ? O GLU D 46  
AB4 5 6 N THR C 52  ? N THR D 52  O ARG C 57  ? O ARG D 57  
AB5 1 2 N ASN C 102 ? N ASN D 102 O PHE C 107 ? O PHE D 107 
AB6 1 2 N PHE C 133 ? N PHE D 133 O LEU C 152 ? O LEU D 152 
AB6 2 3 N ALA C 147 ? N ALA D 147 O VAL C 195 ? O VAL D 195 
AB6 3 4 O VAL C 192 ? O VAL D 192 N HIS C 175 ? N HIS D 175 
AB7 1 2 N PHE C 133 ? N PHE D 133 O LEU C 152 ? O LEU D 152 
AB7 2 3 N ALA C 147 ? N ALA D 147 O VAL C 195 ? O VAL D 195 
AB7 3 4 O SER C 188 ? O SER D 188 N VAL C 180 ? N VAL D 180 
AB8 1 2 N SER C 164 ? N SER D 164 O ASN C 208 ? O ASN D 208 
AB8 2 3 N VAL C 209 ? N VAL D 209 O VAL C 218 ? O VAL D 218 
AB9 1 2 N VAL D 12  ? N VAL G 12  O THR D 105 ? O THR G 105 
AB9 2 3 O VAL D 104 ? O VAL G 104 N ALA D 83  ? N ALA G 83  
AB9 3 4 O ASP D 84  ? O ASP G 84  N GLN D 37  ? N GLN G 37  
AB9 4 5 N TRP D 34  ? N TRP G 34  O VAL D 46  ? O VAL G 46  
AC1 1 2 N VAL D 12  ? N VAL G 12  O THR D 105 ? O THR G 105 
AC1 2 3 O VAL D 104 ? O VAL G 104 N ALA D 83  ? N ALA G 83  
AC1 3 4 N SER D 89  ? N SER G 89  O VAL D 97  ? O VAL G 97  
AC2 1 2 N ILE D 20  ? N ILE G 20  O LEU D 72  ? O LEU G 72  
AC2 2 3 O THR D 73  ? O THR G 73  N SER D 62  ? N SER G 62  
AC3 1 2 N PHE D 117 ? N PHE G 117 O LEU D 136 ? O LEU G 136 
AC3 2 3 N VAL D 133 ? N VAL G 133 O LEU D 180 ? O LEU G 180 
AC3 3 4 O SER D 177 ? O SER G 177 N SER D 163 ? N SER G 163 
AC4 1 2 N GLN D 148 ? N GLN G 148 O GLU D 196 ? O GLU G 196 
AC4 2 3 N VAL D 197 ? N VAL G 197 O VAL D 206 ? O VAL G 206 
# 
_pdbx_entry_details.entry_id                   9CQA 
_pdbx_entry_details.has_ligand_of_interest     N 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_torsion.id 
_pdbx_validate_torsion.PDB_model_num 
_pdbx_validate_torsion.auth_comp_id 
_pdbx_validate_torsion.auth_asym_id 
_pdbx_validate_torsion.auth_seq_id 
_pdbx_validate_torsion.PDB_ins_code 
_pdbx_validate_torsion.label_alt_id 
_pdbx_validate_torsion.phi 
_pdbx_validate_torsion.psi 
1 1 ASP E 155 ? ? 62.52   68.18   
2 1 THR F 50  ? ? 68.76   -41.54  
3 1 SER F 66  ? ? -167.03 94.12   
4 1 ALA F 83  ? ? 179.91  170.96  
5 1 ASP D 155 ? ? 62.80   62.44   
6 1 THR G 50  ? ? 70.85   -43.55  
7 1 SER A 177 ? ? 53.15   -119.58 
8 1 SER B 177 ? ? 53.81   -120.01 
# 
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 E SER 138 ? A SER 138 
2   1 Y 1 E SER 139 ? A SER 139 
3   1 Y 1 E LYS 140 ? A LYS 140 
4   1 Y 1 E SER 141 ? A SER 141 
5   1 Y 1 E THR 142 ? A THR 142 
6   1 Y 1 E SER 143 ? A SER 143 
7   1 Y 1 E GLY 144 ? A GLY 144 
8   1 Y 1 E LYS 225 ? A LYS 225 
9   1 Y 1 E SER 226 ? A SER 226 
10  1 Y 1 E CYS 227 ? A CYS 227 
11  1 Y 1 E ALA 228 ? A ALA 228 
12  1 Y 1 E SER 229 ? A SER 229 
13  1 Y 1 E LEU 230 ? A LEU 230 
14  1 Y 1 E VAL 231 ? A VAL 231 
15  1 Y 1 E PRO 232 ? A PRO 232 
16  1 Y 1 E ARG 233 ? A ARG 233 
17  1 Y 1 E GLY 234 ? A GLY 234 
18  1 Y 1 E SER 235 ? A SER 235 
19  1 Y 1 E GLY 236 ? A GLY 236 
20  1 Y 1 E TRP 237 ? A TRP 237 
21  1 Y 1 E SER 238 ? A SER 238 
22  1 Y 1 E HIS 239 ? A HIS 239 
23  1 Y 1 E PRO 240 ? A PRO 240 
24  1 Y 1 E GLN 241 ? A GLN 241 
25  1 Y 1 E PHE 242 ? A PHE 242 
26  1 Y 1 E GLU 243 ? A GLU 243 
27  1 Y 1 E LYS 244 ? A LYS 244 
28  1 Y 1 E GLY 245 ? A GLY 245 
29  1 Y 1 E GLY 246 ? A GLY 246 
30  1 Y 1 E GLY 247 ? A GLY 247 
31  1 Y 1 E SER 248 ? A SER 248 
32  1 Y 1 E GLY 249 ? A GLY 249 
33  1 Y 1 E GLY 250 ? A GLY 250 
34  1 Y 1 E GLY 251 ? A GLY 251 
35  1 Y 1 E SER 252 ? A SER 252 
36  1 Y 1 E GLY 253 ? A GLY 253 
37  1 Y 1 E GLY 254 ? A GLY 254 
38  1 Y 1 E GLY 255 ? A GLY 255 
39  1 Y 1 E SER 256 ? A SER 256 
40  1 Y 1 E TRP 257 ? A TRP 257 
41  1 Y 1 E SER 258 ? A SER 258 
42  1 Y 1 E HIS 259 ? A HIS 259 
43  1 Y 1 E PRO 260 ? A PRO 260 
44  1 Y 1 E GLN 261 ? A GLN 261 
45  1 Y 1 E PHE 262 ? A PHE 262 
46  1 Y 1 E GLU 263 ? A GLU 263 
47  1 Y 1 E LYS 264 ? A LYS 264 
48  1 Y 1 F GLU 214 ? B GLU 214 
49  1 Y 1 F CYS 215 ? B CYS 215 
50  1 Y 1 D SER 138 ? C SER 138 
51  1 Y 1 D SER 139 ? C SER 139 
52  1 Y 1 D LYS 140 ? C LYS 140 
53  1 Y 1 D SER 141 ? C SER 141 
54  1 Y 1 D THR 142 ? C THR 142 
55  1 Y 1 D SER 143 ? C SER 143 
56  1 Y 1 D GLY 144 ? C GLY 144 
57  1 Y 1 D LYS 225 ? C LYS 225 
58  1 Y 1 D SER 226 ? C SER 226 
59  1 Y 1 D CYS 227 ? C CYS 227 
60  1 Y 1 D ALA 228 ? C ALA 228 
61  1 Y 1 D SER 229 ? C SER 229 
62  1 Y 1 D LEU 230 ? C LEU 230 
63  1 Y 1 D VAL 231 ? C VAL 231 
64  1 Y 1 D PRO 232 ? C PRO 232 
65  1 Y 1 D ARG 233 ? C ARG 233 
66  1 Y 1 D GLY 234 ? C GLY 234 
67  1 Y 1 D SER 235 ? C SER 235 
68  1 Y 1 D GLY 236 ? C GLY 236 
69  1 Y 1 D TRP 237 ? C TRP 237 
70  1 Y 1 D SER 238 ? C SER 238 
71  1 Y 1 D HIS 239 ? C HIS 239 
72  1 Y 1 D PRO 240 ? C PRO 240 
73  1 Y 1 D GLN 241 ? C GLN 241 
74  1 Y 1 D PHE 242 ? C PHE 242 
75  1 Y 1 D GLU 243 ? C GLU 243 
76  1 Y 1 D LYS 244 ? C LYS 244 
77  1 Y 1 D GLY 245 ? C GLY 245 
78  1 Y 1 D GLY 246 ? C GLY 246 
79  1 Y 1 D GLY 247 ? C GLY 247 
80  1 Y 1 D SER 248 ? C SER 248 
81  1 Y 1 D GLY 249 ? C GLY 249 
82  1 Y 1 D GLY 250 ? C GLY 250 
83  1 Y 1 D GLY 251 ? C GLY 251 
84  1 Y 1 D SER 252 ? C SER 252 
85  1 Y 1 D GLY 253 ? C GLY 253 
86  1 Y 1 D GLY 254 ? C GLY 254 
87  1 Y 1 D GLY 255 ? C GLY 255 
88  1 Y 1 D SER 256 ? C SER 256 
89  1 Y 1 D TRP 257 ? C TRP 257 
90  1 Y 1 D SER 258 ? C SER 258 
91  1 Y 1 D HIS 259 ? C HIS 259 
92  1 Y 1 D PRO 260 ? C PRO 260 
93  1 Y 1 D GLN 261 ? C GLN 261 
94  1 Y 1 D PHE 262 ? C PHE 262 
95  1 Y 1 D GLU 263 ? C GLU 263 
96  1 Y 1 D LYS 264 ? C LYS 264 
97  1 Y 1 G GLU 214 ? D GLU 214 
98  1 Y 1 G CYS 215 ? D CYS 215 
99  1 Y 1 A MET 155 ? E MET 1   
100 1 Y 1 A GLY 156 ? E GLY 2   
101 1 Y 1 A SER 157 ? E SER 3   
102 1 Y 1 A LYS 158 ? E LYS 4   
103 1 Y 1 A PRO 159 ? E PRO 5   
104 1 Y 1 A ASN 160 ? E ASN 6   
105 1 Y 1 A ILE 189 ? E ILE 35  
106 1 Y 1 A PRO 190 ? E PRO 36  
107 1 Y 1 A ASN 191 ? E ASN 37  
108 1 Y 1 A LYS 192 ? E LYS 38  
109 1 Y 1 A LYS 193 ? E LYS 39  
110 1 Y 1 A PRO 194 ? E PRO 40  
111 1 Y 1 A GLY 195 ? E GLY 41  
112 1 Y 1 A LYS 196 ? E LYS 42  
113 1 Y 1 A LYS 197 ? E LYS 43  
114 1 Y 1 A HIS 198 ? E HIS 44  
115 1 Y 1 A HIS 199 ? E HIS 45  
116 1 Y 1 A HIS 200 ? E HIS 46  
117 1 Y 1 A HIS 201 ? E HIS 47  
118 1 Y 1 A HIS 202 ? E HIS 48  
119 1 Y 1 A HIS 203 ? E HIS 49  
120 1 Y 1 B MET 155 ? F MET 1   
121 1 Y 1 B GLY 156 ? F GLY 2   
122 1 Y 1 B SER 157 ? F SER 3   
123 1 Y 1 B LYS 158 ? F LYS 4   
124 1 Y 1 B PRO 159 ? F PRO 5   
125 1 Y 1 B ASN 160 ? F ASN 6   
126 1 Y 1 B ILE 189 ? F ILE 35  
127 1 Y 1 B PRO 190 ? F PRO 36  
128 1 Y 1 B ASN 191 ? F ASN 37  
129 1 Y 1 B LYS 192 ? F LYS 38  
130 1 Y 1 B LYS 193 ? F LYS 39  
131 1 Y 1 B PRO 194 ? F PRO 40  
132 1 Y 1 B GLY 195 ? F GLY 41  
133 1 Y 1 B LYS 196 ? F LYS 42  
134 1 Y 1 B LYS 197 ? F LYS 43  
135 1 Y 1 B HIS 198 ? F HIS 44  
136 1 Y 1 B HIS 199 ? F HIS 45  
137 1 Y 1 B HIS 200 ? F HIS 46  
138 1 Y 1 B HIS 201 ? F HIS 47  
139 1 Y 1 B HIS 202 ? F HIS 48  
140 1 Y 1 B HIS 203 ? F HIS 49  
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N N N 1   
ALA CA   C N S 2   
ALA C    C N N 3   
ALA O    O N N 4   
ALA CB   C N N 5   
ALA OXT  O N N 6   
ALA H    H N N 7   
ALA H2   H N N 8   
ALA HA   H N N 9   
ALA HB1  H N N 10  
ALA HB2  H N N 11  
ALA HB3  H N N 12  
ALA HXT  H N N 13  
ARG N    N N N 14  
ARG CA   C N S 15  
ARG C    C N N 16  
ARG O    O N N 17  
ARG CB   C N N 18  
ARG CG   C N N 19  
ARG CD   C N N 20  
ARG NE   N N N 21  
ARG CZ   C N N 22  
ARG NH1  N N N 23  
ARG NH2  N N N 24  
ARG OXT  O N N 25  
ARG H    H N N 26  
ARG H2   H N N 27  
ARG HA   H N N 28  
ARG HB2  H N N 29  
ARG HB3  H N N 30  
ARG HG2  H N N 31  
ARG HG3  H N N 32  
ARG HD2  H N N 33  
ARG HD3  H N N 34  
ARG HE   H N N 35  
ARG HH11 H N N 36  
ARG HH12 H N N 37  
ARG HH21 H N N 38  
ARG HH22 H N N 39  
ARG HXT  H N N 40  
ASN N    N N N 41  
ASN CA   C N S 42  
ASN C    C N N 43  
ASN O    O N N 44  
ASN CB   C N N 45  
ASN CG   C N N 46  
ASN OD1  O N N 47  
ASN ND2  N N N 48  
ASN OXT  O N N 49  
ASN H    H N N 50  
ASN H2   H N N 51  
ASN HA   H N N 52  
ASN HB2  H N N 53  
ASN HB3  H N N 54  
ASN HD21 H N N 55  
ASN HD22 H N N 56  
ASN HXT  H N N 57  
ASP N    N N N 58  
ASP CA   C N S 59  
ASP C    C N N 60  
ASP O    O N N 61  
ASP CB   C N N 62  
ASP CG   C N N 63  
ASP OD1  O N N 64  
ASP OD2  O N N 65  
ASP OXT  O N N 66  
ASP H    H N N 67  
ASP H2   H N N 68  
ASP HA   H N N 69  
ASP HB2  H N N 70  
ASP HB3  H N N 71  
ASP HD2  H N N 72  
ASP HXT  H N N 73  
CYS N    N N N 74  
CYS CA   C N R 75  
CYS C    C N N 76  
CYS O    O N N 77  
CYS CB   C N N 78  
CYS SG   S N N 79  
CYS OXT  O N N 80  
CYS H    H N N 81  
CYS H2   H N N 82  
CYS HA   H N N 83  
CYS HB2  H N N 84  
CYS HB3  H N N 85  
CYS HG   H N N 86  
CYS HXT  H N N 87  
GLN N    N N N 88  
GLN CA   C N S 89  
GLN C    C N N 90  
GLN O    O N N 91  
GLN CB   C N N 92  
GLN CG   C N N 93  
GLN CD   C N N 94  
GLN OE1  O N N 95  
GLN NE2  N N N 96  
GLN OXT  O N N 97  
GLN H    H N N 98  
GLN H2   H N N 99  
GLN HA   H N N 100 
GLN HB2  H N N 101 
GLN HB3  H N N 102 
GLN HG2  H N N 103 
GLN HG3  H N N 104 
GLN HE21 H N N 105 
GLN HE22 H N N 106 
GLN HXT  H N N 107 
GLU N    N N N 108 
GLU CA   C N S 109 
GLU C    C N N 110 
GLU O    O N N 111 
GLU CB   C N N 112 
GLU CG   C N N 113 
GLU CD   C N N 114 
GLU OE1  O N N 115 
GLU OE2  O N N 116 
GLU OXT  O N N 117 
GLU H    H N N 118 
GLU H2   H N N 119 
GLU HA   H N N 120 
GLU HB2  H N N 121 
GLU HB3  H N N 122 
GLU HG2  H N N 123 
GLU HG3  H N N 124 
GLU HE2  H N N 125 
GLU HXT  H N N 126 
GLY N    N N N 127 
GLY CA   C N N 128 
GLY C    C N N 129 
GLY O    O N N 130 
GLY OXT  O N N 131 
GLY H    H N N 132 
GLY H2   H N N 133 
GLY HA2  H N N 134 
GLY HA3  H N N 135 
GLY HXT  H N N 136 
HIS N    N N N 137 
HIS CA   C N S 138 
HIS C    C N N 139 
HIS O    O N N 140 
HIS CB   C N N 141 
HIS CG   C Y N 142 
HIS ND1  N Y N 143 
HIS CD2  C Y N 144 
HIS CE1  C Y N 145 
HIS NE2  N Y N 146 
HIS OXT  O N N 147 
HIS H    H N N 148 
HIS H2   H N N 149 
HIS HA   H N N 150 
HIS HB2  H N N 151 
HIS HB3  H N N 152 
HIS HD1  H N N 153 
HIS HD2  H N N 154 
HIS HE1  H N N 155 
HIS HE2  H N N 156 
HIS HXT  H N N 157 
HOH O    O N N 158 
HOH H1   H N N 159 
HOH H2   H N N 160 
ILE N    N N N 161 
ILE CA   C N S 162 
ILE C    C N N 163 
ILE O    O N N 164 
ILE CB   C N S 165 
ILE CG1  C N N 166 
ILE CG2  C N N 167 
ILE CD1  C N N 168 
ILE OXT  O N N 169 
ILE H    H N N 170 
ILE H2   H N N 171 
ILE HA   H N N 172 
ILE HB   H N N 173 
ILE HG12 H N N 174 
ILE HG13 H N N 175 
ILE HG21 H N N 176 
ILE HG22 H N N 177 
ILE HG23 H N N 178 
ILE HD11 H N N 179 
ILE HD12 H N N 180 
ILE HD13 H N N 181 
ILE HXT  H N N 182 
LEU N    N N N 183 
LEU CA   C N S 184 
LEU C    C N N 185 
LEU O    O N N 186 
LEU CB   C N N 187 
LEU CG   C N N 188 
LEU CD1  C N N 189 
LEU CD2  C N N 190 
LEU OXT  O N N 191 
LEU H    H N N 192 
LEU H2   H N N 193 
LEU HA   H N N 194 
LEU HB2  H N N 195 
LEU HB3  H N N 196 
LEU HG   H N N 197 
LEU HD11 H N N 198 
LEU HD12 H N N 199 
LEU HD13 H N N 200 
LEU HD21 H N N 201 
LEU HD22 H N N 202 
LEU HD23 H N N 203 
LEU HXT  H N N 204 
LYS N    N N N 205 
LYS CA   C N S 206 
LYS C    C N N 207 
LYS O    O N N 208 
LYS CB   C N N 209 
LYS CG   C N N 210 
LYS CD   C N N 211 
LYS CE   C N N 212 
LYS NZ   N N N 213 
LYS OXT  O N N 214 
LYS H    H N N 215 
LYS H2   H N N 216 
LYS HA   H N N 217 
LYS HB2  H N N 218 
LYS HB3  H N N 219 
LYS HG2  H N N 220 
LYS HG3  H N N 221 
LYS HD2  H N N 222 
LYS HD3  H N N 223 
LYS HE2  H N N 224 
LYS HE3  H N N 225 
LYS HZ1  H N N 226 
LYS HZ2  H N N 227 
LYS HZ3  H N N 228 
LYS HXT  H N N 229 
MET N    N N N 230 
MET CA   C N S 231 
MET C    C N N 232 
MET O    O N N 233 
MET CB   C N N 234 
MET CG   C N N 235 
MET SD   S N N 236 
MET CE   C N N 237 
MET OXT  O N N 238 
MET H    H N N 239 
MET H2   H N N 240 
MET HA   H N N 241 
MET HB2  H N N 242 
MET HB3  H N N 243 
MET HG2  H N N 244 
MET HG3  H N N 245 
MET HE1  H N N 246 
MET HE2  H N N 247 
MET HE3  H N N 248 
MET HXT  H N N 249 
PHE N    N N N 250 
PHE CA   C N S 251 
PHE C    C N N 252 
PHE O    O N N 253 
PHE CB   C N N 254 
PHE CG   C Y N 255 
PHE CD1  C Y N 256 
PHE CD2  C Y N 257 
PHE CE1  C Y N 258 
PHE CE2  C Y N 259 
PHE CZ   C Y N 260 
PHE OXT  O N N 261 
PHE H    H N N 262 
PHE H2   H N N 263 
PHE HA   H N N 264 
PHE HB2  H N N 265 
PHE HB3  H N N 266 
PHE HD1  H N N 267 
PHE HD2  H N N 268 
PHE HE1  H N N 269 
PHE HE2  H N N 270 
PHE HZ   H N N 271 
PHE HXT  H N N 272 
PRO N    N N N 273 
PRO CA   C N S 274 
PRO C    C N N 275 
PRO O    O N N 276 
PRO CB   C N N 277 
PRO CG   C N N 278 
PRO CD   C N N 279 
PRO OXT  O N N 280 
PRO H    H N N 281 
PRO HA   H N N 282 
PRO HB2  H N N 283 
PRO HB3  H N N 284 
PRO HG2  H N N 285 
PRO HG3  H N N 286 
PRO HD2  H N N 287 
PRO HD3  H N N 288 
PRO HXT  H N N 289 
SER N    N N N 290 
SER CA   C N S 291 
SER C    C N N 292 
SER O    O N N 293 
SER CB   C N N 294 
SER OG   O N N 295 
SER OXT  O N N 296 
SER H    H N N 297 
SER H2   H N N 298 
SER HA   H N N 299 
SER HB2  H N N 300 
SER HB3  H N N 301 
SER HG   H N N 302 
SER HXT  H N N 303 
SO4 S    S N N 304 
SO4 O1   O N N 305 
SO4 O2   O N N 306 
SO4 O3   O N N 307 
SO4 O4   O N N 308 
THR N    N N N 309 
THR CA   C N S 310 
THR C    C N N 311 
THR O    O N N 312 
THR CB   C N R 313 
THR OG1  O N N 314 
THR CG2  C N N 315 
THR OXT  O N N 316 
THR H    H N N 317 
THR H2   H N N 318 
THR HA   H N N 319 
THR HB   H N N 320 
THR HG1  H N N 321 
THR HG21 H N N 322 
THR HG22 H N N 323 
THR HG23 H N N 324 
THR HXT  H N N 325 
TRP N    N N N 326 
TRP CA   C N S 327 
TRP C    C N N 328 
TRP O    O N N 329 
TRP CB   C N N 330 
TRP CG   C Y N 331 
TRP CD1  C Y N 332 
TRP CD2  C Y N 333 
TRP NE1  N Y N 334 
TRP CE2  C Y N 335 
TRP CE3  C Y N 336 
TRP CZ2  C Y N 337 
TRP CZ3  C Y N 338 
TRP CH2  C Y N 339 
TRP OXT  O N N 340 
TRP H    H N N 341 
TRP H2   H N N 342 
TRP HA   H N N 343 
TRP HB2  H N N 344 
TRP HB3  H N N 345 
TRP HD1  H N N 346 
TRP HE1  H N N 347 
TRP HE3  H N N 348 
TRP HZ2  H N N 349 
TRP HZ3  H N N 350 
TRP HH2  H N N 351 
TRP HXT  H N N 352 
TYR N    N N N 353 
TYR CA   C N S 354 
TYR C    C N N 355 
TYR O    O N N 356 
TYR CB   C N N 357 
TYR CG   C Y N 358 
TYR CD1  C Y N 359 
TYR CD2  C Y N 360 
TYR CE1  C Y N 361 
TYR CE2  C Y N 362 
TYR CZ   C Y N 363 
TYR OH   O N N 364 
TYR OXT  O N N 365 
TYR H    H N N 366 
TYR H2   H N N 367 
TYR HA   H N N 368 
TYR HB2  H N N 369 
TYR HB3  H N N 370 
TYR HD1  H N N 371 
TYR HD2  H N N 372 
TYR HE1  H N N 373 
TYR HE2  H N N 374 
TYR HH   H N N 375 
TYR HXT  H N N 376 
VAL N    N N N 377 
VAL CA   C N S 378 
VAL C    C N N 379 
VAL O    O N N 380 
VAL CB   C N N 381 
VAL CG1  C N N 382 
VAL CG2  C N N 383 
VAL OXT  O N N 384 
VAL H    H N N 385 
VAL H2   H N N 386 
VAL HA   H N N 387 
VAL HB   H N N 388 
VAL HG11 H N N 389 
VAL HG12 H N N 390 
VAL HG13 H N N 391 
VAL HG21 H N N 392 
VAL HG22 H N N 393 
VAL HG23 H N N 394 
VAL HXT  H N N 395 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SER N   CA   sing N N 277 
SER N   H    sing N N 278 
SER N   H2   sing N N 279 
SER CA  C    sing N N 280 
SER CA  CB   sing N N 281 
SER CA  HA   sing N N 282 
SER C   O    doub N N 283 
SER C   OXT  sing N N 284 
SER CB  OG   sing N N 285 
SER CB  HB2  sing N N 286 
SER CB  HB3  sing N N 287 
SER OG  HG   sing N N 288 
SER OXT HXT  sing N N 289 
SO4 S   O1   doub N N 290 
SO4 S   O2   doub N N 291 
SO4 S   O3   sing N N 292 
SO4 S   O4   sing N N 293 
THR N   CA   sing N N 294 
THR N   H    sing N N 295 
THR N   H2   sing N N 296 
THR CA  C    sing N N 297 
THR CA  CB   sing N N 298 
THR CA  HA   sing N N 299 
THR C   O    doub N N 300 
THR C   OXT  sing N N 301 
THR CB  OG1  sing N N 302 
THR CB  CG2  sing N N 303 
THR CB  HB   sing N N 304 
THR OG1 HG1  sing N N 305 
THR CG2 HG21 sing N N 306 
THR CG2 HG22 sing N N 307 
THR CG2 HG23 sing N N 308 
THR OXT HXT  sing N N 309 
TRP N   CA   sing N N 310 
TRP N   H    sing N N 311 
TRP N   H2   sing N N 312 
TRP CA  C    sing N N 313 
TRP CA  CB   sing N N 314 
TRP CA  HA   sing N N 315 
TRP C   O    doub N N 316 
TRP C   OXT  sing N N 317 
TRP CB  CG   sing N N 318 
TRP CB  HB2  sing N N 319 
TRP CB  HB3  sing N N 320 
TRP CG  CD1  doub Y N 321 
TRP CG  CD2  sing Y N 322 
TRP CD1 NE1  sing Y N 323 
TRP CD1 HD1  sing N N 324 
TRP CD2 CE2  doub Y N 325 
TRP CD2 CE3  sing Y N 326 
TRP NE1 CE2  sing Y N 327 
TRP NE1 HE1  sing N N 328 
TRP CE2 CZ2  sing Y N 329 
TRP CE3 CZ3  doub Y N 330 
TRP CE3 HE3  sing N N 331 
TRP CZ2 CH2  doub Y N 332 
TRP CZ2 HZ2  sing N N 333 
TRP CZ3 CH2  sing Y N 334 
TRP CZ3 HZ3  sing N N 335 
TRP CH2 HH2  sing N N 336 
TRP OXT HXT  sing N N 337 
TYR N   CA   sing N N 338 
TYR N   H    sing N N 339 
TYR N   H2   sing N N 340 
TYR CA  C    sing N N 341 
TYR CA  CB   sing N N 342 
TYR CA  HA   sing N N 343 
TYR C   O    doub N N 344 
TYR C   OXT  sing N N 345 
TYR CB  CG   sing N N 346 
TYR CB  HB2  sing N N 347 
TYR CB  HB3  sing N N 348 
TYR CG  CD1  doub Y N 349 
TYR CG  CD2  sing Y N 350 
TYR CD1 CE1  sing Y N 351 
TYR CD1 HD1  sing N N 352 
TYR CD2 CE2  doub Y N 353 
TYR CD2 HD2  sing N N 354 
TYR CE1 CZ   doub Y N 355 
TYR CE1 HE1  sing N N 356 
TYR CE2 CZ   sing Y N 357 
TYR CE2 HE2  sing N N 358 
TYR CZ  OH   sing N N 359 
TYR OH  HH   sing N N 360 
TYR OXT HXT  sing N N 361 
VAL N   CA   sing N N 362 
VAL N   H    sing N N 363 
VAL N   H2   sing N N 364 
VAL CA  C    sing N N 365 
VAL CA  CB   sing N N 366 
VAL CA  HA   sing N N 367 
VAL C   O    doub N N 368 
VAL C   OXT  sing N N 369 
VAL CB  CG1  sing N N 370 
VAL CB  CG2  sing N N 371 
VAL CB  HB   sing N N 372 
VAL CG1 HG11 sing N N 373 
VAL CG1 HG12 sing N N 374 
VAL CG1 HG13 sing N N 375 
VAL CG2 HG21 sing N N 376 
VAL CG2 HG22 sing N N 377 
VAL CG2 HG23 sing N N 378 
VAL OXT HXT  sing N N 379 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute Of Allergy and Infectious Diseases (NIH/NIAID)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           AI166066 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'in silico model' 
_pdbx_initial_refinement_model.source_name      SwissModel 
_pdbx_initial_refinement_model.accession_code   ? 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9CQA 
_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]   0.013086 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.012383 
_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]   0.005708 
_atom_sites.fract_transf_vector[1]      0.00000 
_atom_sites.fract_transf_vector[2]      0.00000 
_atom_sites.fract_transf_vector[3]      0.00000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C 
N 
O 
S 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N N   . GLN A 1 1   ? 42.951  -21.691 -47.623 1.00 41.95 ?  1   GLN E N   1 
ATOM   2    C CA  . GLN A 1 1   ? 44.145  -20.825 -47.686 1.00 32.01 ?  1   GLN E CA  1 
ATOM   3    C C   . GLN A 1 1   ? 43.756  -19.405 -47.251 1.00 26.97 ?  1   GLN E C   1 
ATOM   4    O O   . GLN A 1 1   ? 44.643  -18.631 -47.006 1.00 28.58 ?  1   GLN E O   1 
ATOM   5    C CB  . GLN A 1 1   ? 44.768  -20.936 -49.076 1.00 28.33 ?  1   GLN E CB  1 
ATOM   6    C CG  . GLN A 1 1   ? 45.785  -22.060 -49.187 1.00 38.96 ?  1   GLN E CG  1 
ATOM   7    C CD  . GLN A 1 1   ? 45.763  -22.707 -50.549 1.00 45.25 ?  1   GLN E CD  1 
ATOM   8    O OE1 . GLN A 1 1   ? 45.432  -22.077 -51.550 1.00 61.87 ?  1   GLN E OE1 1 
ATOM   9    N NE2 . GLN A 1 1   ? 46.105  -23.985 -50.596 1.00 44.66 ?  1   GLN E NE2 1 
ATOM   10   N N   . VAL A 1 2   ? 42.460  -19.120 -47.135 1.00 27.97 ?  2   VAL E N   1 
ATOM   11   C CA  . VAL A 1 2   ? 42.027  -17.795 -46.605 1.00 23.37 ?  2   VAL E CA  1 
ATOM   12   C C   . VAL A 1 2   ? 41.890  -17.873 -45.084 1.00 23.55 ?  2   VAL E C   1 
ATOM   13   O O   . VAL A 1 2   ? 41.300  -18.837 -44.607 1.00 26.64 ?  2   VAL E O   1 
ATOM   14   C CB  . VAL A 1 2   ? 40.732  -17.283 -47.263 1.00 26.41 ?  2   VAL E CB  1 
ATOM   15   C CG1 . VAL A 1 2   ? 40.225  -16.023 -46.581 1.00 27.45 ?  2   VAL E CG1 1 
ATOM   16   C CG2 . VAL A 1 2   ? 40.925  -17.038 -48.749 1.00 28.36 ?  2   VAL E CG2 1 
ATOM   17   N N   . HIS A 1 3   ? 42.438  -16.896 -44.366 1.00 21.77 ?  3   HIS E N   1 
ATOM   18   C CA  . HIS A 1 3   ? 42.301  -16.809 -42.917 1.00 21.59 ?  3   HIS E CA  1 
ATOM   19   C C   . HIS A 1 3   ? 41.995  -15.365 -42.531 1.00 22.89 ?  3   HIS E C   1 
ATOM   20   O O   . HIS A 1 3   ? 42.567  -14.424 -43.092 1.00 24.11 ?  3   HIS E O   1 
ATOM   21   C CB  . HIS A 1 3   ? 43.576  -17.283 -42.182 1.00 23.91 ?  3   HIS E CB  1 
ATOM   22   C CG  . HIS A 1 3   ? 43.804  -18.762 -42.268 1.00 26.68 ?  3   HIS E CG  1 
ATOM   23   N ND1 . HIS A 1 3   ? 43.295  -19.648 -41.339 1.00 31.34 ?  3   HIS E ND1 1 
ATOM   24   C CD2 . HIS A 1 3   ? 44.465  -19.512 -43.180 1.00 24.46 ?  3   HIS E CD2 1 
ATOM   25   C CE1 . HIS A 1 3   ? 43.649  -20.879 -41.668 1.00 32.93 ?  3   HIS E CE1 1 
ATOM   26   N NE2 . HIS A 1 3   ? 44.357  -20.824 -42.783 1.00 26.16 ?  3   HIS E NE2 1 
ATOM   27   N N   . LEU A 1 4   ? 41.107  -15.200 -41.558 1.00 20.83 ?  4   LEU E N   1 
ATOM   28   C CA  . LEU A 1 4   ? 40.867  -13.920 -40.901 1.00 22.23 ?  4   LEU E CA  1 
ATOM   29   C C   . LEU A 1 4   ? 41.140  -14.135 -39.424 1.00 22.80 ?  4   LEU E C   1 
ATOM   30   O O   . LEU A 1 4   ? 40.534  -15.025 -38.814 1.00 25.19 ?  4   LEU E O   1 
ATOM   31   C CB  . LEU A 1 4   ? 39.424  -13.441 -41.106 1.00 24.33 ?  4   LEU E CB  1 
ATOM   32   C CG  . LEU A 1 4   ? 38.962  -13.177 -42.536 1.00 24.04 ?  4   LEU E CG  1 
ATOM   33   C CD1 . LEU A 1 4   ? 37.448  -12.887 -42.557 1.00 22.86 ?  4   LEU E CD1 1 
ATOM   34   C CD2 . LEU A 1 4   ? 39.718  -12.014 -43.137 1.00 26.66 ?  4   LEU E CD2 1 
ATOM   35   N N   . VAL A 1 5   ? 42.048  -13.344 -38.856 1.00 22.77 ?  5   VAL E N   1 
ATOM   36   C CA  . VAL A 1 5   ? 42.462  -13.513 -37.468 1.00 23.30 ?  5   VAL E CA  1 
ATOM   37   C C   . VAL A 1 5   ? 42.181  -12.220 -36.717 1.00 21.57 ?  5   VAL E C   1 
ATOM   38   O O   . VAL A 1 5   ? 42.692  -11.154 -37.089 1.00 24.23 ?  5   VAL E O   1 
ATOM   39   C CB  . VAL A 1 5   ? 43.953  -13.882 -37.342 1.00 25.38 ?  5   VAL E CB  1 
ATOM   40   C CG1 . VAL A 1 5   ? 44.321  -13.962 -35.863 1.00 24.05 ?  5   VAL E CG1 1 
ATOM   41   C CG2 . VAL A 1 5   ? 44.239  -15.211 -38.054 1.00 27.68 ?  5   VAL E CG2 1 
ATOM   42   N N   . GLN A 1 6   ? 41.402  -12.324 -35.640 1.00 22.15 ?  6   GLN E N   1 
ATOM   43   C CA  . GLN A 1 6   ? 40.955  -11.176 -34.868 1.00 22.40 ?  6   GLN E CA  1 
ATOM   44   C C   . GLN A 1 6   ? 41.795  -10.992 -33.606 1.00 22.70 ?  6   GLN E C   1 
ATOM   45   O O   . GLN A 1 6   ? 42.450  -11.918 -33.115 1.00 22.69 ?  6   GLN E O   1 
ATOM   46   C CB  . GLN A 1 6   ? 39.475  -11.352 -34.504 1.00 24.33 ?  6   GLN E CB  1 
ATOM   47   C CG  . GLN A 1 6   ? 38.584  -11.471 -35.733 1.00 23.47 ?  6   GLN E CG  1 
ATOM   48   C CD  . GLN A 1 6   ? 37.102  -11.499 -35.382 1.00 22.52 ?  6   GLN E CD  1 
ATOM   49   O OE1 . GLN A 1 6   ? 36.334  -12.273 -35.951 1.00 22.88 ?  6   GLN E OE1 1 
ATOM   50   N NE2 . GLN A 1 6   ? 36.704  -10.668 -34.426 1.00 23.47 ?  6   GLN E NE2 1 
ATOM   51   N N   . SER A 1 7   ? 41.763  -9.771  -33.084 1.00 23.31 ?  7   SER E N   1 
ATOM   52   C CA  . SER A 1 7   ? 42.436  -9.415  -31.843 1.00 25.35 ?  7   SER E CA  1 
ATOM   53   C C   . SER A 1 7   ? 41.713  -10.049 -30.645 1.00 25.44 ?  7   SER E C   1 
ATOM   54   O O   . SER A 1 7   ? 40.611  -10.580 -30.766 1.00 24.89 ?  7   SER E O   1 
ATOM   55   C CB  . SER A 1 7   ? 42.517  -7.885  -31.725 1.00 25.38 ?  7   SER E CB  1 
ATOM   56   O OG  . SER A 1 7   ? 41.229  -7.308  -31.968 1.00 23.76 ?  7   SER E OG  1 
ATOM   57   N N   . GLY A 1 8   ? 42.349  -9.976  -29.469 1.00 27.54 ?  8   GLY E N   1 
ATOM   58   C CA  . GLY A 1 8   ? 41.902  -10.719 -28.310 1.00 28.54 ?  8   GLY E CA  1 
ATOM   59   C C   . GLY A 1 8   ? 40.829  -10.024 -27.477 1.00 29.51 ?  8   GLY E C   1 
ATOM   60   O O   . GLY A 1 8   ? 40.361  -8.926  -27.782 1.00 26.90 ?  8   GLY E O   1 
ATOM   61   N N   . VAL A 1 9   ? 40.483  -10.693 -26.372 1.00 28.45 ?  9   VAL E N   1 
ATOM   62   C CA  . VAL A 1 9   ? 39.328  -10.316 -25.564 1.00 26.45 ?  9   VAL E CA  1 
ATOM   63   C C   . VAL A 1 9   ? 39.513  -8.909  -25.024 1.00 31.35 ?  9   VAL E C   1 
ATOM   64   O O   . VAL A 1 9   ? 40.627  -8.493  -24.682 1.00 27.80 ?  9   VAL E O   1 
ATOM   65   C CB  . VAL A 1 9   ? 39.128  -11.336 -24.426 1.00 28.08 ?  9   VAL E CB  1 
ATOM   66   C CG1 . VAL A 1 9   ? 40.352  -11.364 -23.504 1.00 33.92 ?  9   VAL E CG1 1 
ATOM   67   C CG2 . VAL A 1 9   ? 37.872  -11.040 -23.630 1.00 31.19 ?  9   VAL E CG2 1 
ATOM   68   N N   . GLU A 1 10  ? 38.418  -8.162  -24.963 1.00 28.52 ?  10  GLU E N   1 
ATOM   69   C CA  . GLU A 1 10  ? 38.424  -6.799  -24.438 1.00 27.53 ?  10  GLU E CA  1 
ATOM   70   C C   . GLU A 1 10  ? 37.459  -6.707  -23.271 1.00 31.02 ?  10  GLU E C   1 
ATOM   71   O O   . GLU A 1 10  ? 36.332  -7.206  -23.362 1.00 31.82 ?  10  GLU E O   1 
ATOM   72   C CB  . GLU A 1 10  ? 38.037  -5.787  -25.510 1.00 28.42 ?  10  GLU E CB  1 
ATOM   73   C CG  . GLU A 1 10  ? 38.842  -5.861  -26.785 1.00 28.41 ?  10  GLU E CG  1 
ATOM   74   C CD  . GLU A 1 10  ? 40.117  -5.051  -26.656 1.00 35.01 ?  10  GLU E CD  1 
ATOM   75   O OE1 . GLU A 1 10  ? 40.314  -4.454  -25.578 1.00 34.28 ?  10  GLU E OE1 1 
ATOM   76   O OE2 . GLU A 1 10  ? 40.862  -4.927  -27.650 1.00 34.68 ?  10  GLU E OE2 1 
ATOM   77   N N   . VAL A 1 11  ? 37.909  -6.096  -22.177 1.00 27.18 ?  11  VAL E N   1 
ATOM   78   C CA  . VAL A 1 11  ? 37.067  -5.824  -21.018 1.00 30.37 ?  11  VAL E CA  1 
ATOM   79   C C   . VAL A 1 11  ? 37.102  -4.317  -20.794 1.00 33.16 ?  11  VAL E C   1 
ATOM   80   O O   . VAL A 1 11  ? 38.147  -3.765  -20.430 1.00 30.62 ?  11  VAL E O   1 
ATOM   81   C CB  . VAL A 1 11  ? 37.534  -6.583  -19.766 1.00 31.85 ?  11  VAL E CB  1 
ATOM   82   C CG1 . VAL A 1 11  ? 36.608  -6.276  -18.595 1.00 35.44 ?  11  VAL E CG1 1 
ATOM   83   C CG2 . VAL A 1 11  ? 37.587  -8.097  -20.031 1.00 32.74 ?  11  VAL E CG2 1 
ATOM   84   N N   . LYS A 1 12  ? 35.967  -3.656  -21.002 1.00 28.71 ?  12  LYS E N   1 
ATOM   85   C CA  . LYS A 1 12  ? 35.905  -2.204  -21.030 1.00 32.64 ?  12  LYS E CA  1 
ATOM   86   C C   . LYS A 1 12  ? 34.878  -1.683  -20.035 1.00 34.61 ?  12  LYS E C   1 
ATOM   87   O O   . LYS A 1 12  ? 33.908  -2.370  -19.703 1.00 33.61 ?  12  LYS E O   1 
ATOM   88   C CB  . LYS A 1 12  ? 35.561  -1.709  -22.426 1.00 32.06 ?  12  LYS E CB  1 
ATOM   89   C CG  . LYS A 1 12  ? 36.640  -2.045  -23.441 1.00 33.58 ?  12  LYS E CG  1 
ATOM   90   C CD  . LYS A 1 12  ? 37.763  -1.027  -23.419 1.00 35.53 ?  12  LYS E CD  1 
ATOM   91   C CE  . LYS A 1 12  ? 38.856  -1.435  -24.380 1.00 37.65 ?  12  LYS E CE  1 
ATOM   92   N NZ  . LYS A 1 12  ? 39.966  -0.453  -24.345 1.00 40.58 ?  12  LYS E NZ  1 
ATOM   93   N N   . LYS A 1 13  ? 35.102  -0.459  -19.552 1.00 32.39 ?  13  LYS E N   1 
ATOM   94   C CA  . LYS A 1 13  ? 34.107  0.168   -18.692 1.00 36.19 ?  13  LYS E CA  1 
ATOM   95   C C   . LYS A 1 13  ? 33.105  0.956   -19.521 1.00 34.22 ?  13  LYS E C   1 
ATOM   96   O O   . LYS A 1 13  ? 33.408  1.376   -20.640 1.00 33.79 ?  13  LYS E O   1 
ATOM   97   C CB  . LYS A 1 13  ? 34.805  1.074   -17.674 1.00 40.02 ?  13  LYS E CB  1 
ATOM   98   C CG  . LYS A 1 13  ? 35.397  0.264   -16.532 1.00 42.80 ?  13  LYS E CG  1 
ATOM   99   C CD  . LYS A 1 13  ? 36.618  0.887   -15.916 1.00 49.90 ?  13  LYS E CD  1 
ATOM   100  C CE  . LYS A 1 13  ? 37.147  -0.027  -14.813 1.00 50.20 ?  13  LYS E CE  1 
ATOM   101  N NZ  . LYS A 1 13  ? 36.055  -0.498  -13.906 1.00 49.36 ?  13  LYS E NZ  1 
ATOM   102  N N   . PRO A 1 14  ? 31.882  1.150   -19.012 1.00 33.03 ?  14  PRO E N   1 
ATOM   103  C CA  . PRO A 1 14  ? 30.890  1.939   -19.749 1.00 32.33 ?  14  PRO E CA  1 
ATOM   104  C C   . PRO A 1 14  ? 31.458  3.303   -20.112 1.00 34.43 ?  14  PRO E C   1 
ATOM   105  O O   . PRO A 1 14  ? 32.239  3.889   -19.359 1.00 35.22 ?  14  PRO E O   1 
ATOM   106  C CB  . PRO A 1 14  ? 29.726  2.049   -18.760 1.00 32.68 ?  14  PRO E CB  1 
ATOM   107  C CG  . PRO A 1 14  ? 29.841  0.802   -17.941 1.00 36.15 ?  14  PRO E CG  1 
ATOM   108  C CD  . PRO A 1 14  ? 31.328  0.615   -17.759 1.00 34.51 ?  14  PRO E CD  1 
ATOM   109  N N   . GLY A 1 15  ? 31.111  3.779   -21.308 1.00 34.15 ?  15  GLY E N   1 
ATOM   110  C CA  . GLY A 1 15  ? 31.635  5.028   -21.820 1.00 36.06 ?  15  GLY E CA  1 
ATOM   111  C C   . GLY A 1 15  ? 32.964  4.941   -22.537 1.00 37.61 ?  15  GLY E C   1 
ATOM   112  O O   . GLY A 1 15  ? 33.312  5.870   -23.281 1.00 37.21 ?  15  GLY E O   1 
ATOM   113  N N   . ALA A 1 16  ? 33.734  3.876   -22.337 1.00 34.65 ?  16  ALA E N   1 
ATOM   114  C CA  . ALA A 1 16  ? 35.006  3.742   -23.039 1.00 34.24 ?  16  ALA E CA  1 
ATOM   115  C C   . ALA A 1 16  ? 34.760  3.399   -24.508 1.00 34.07 ?  16  ALA E C   1 
ATOM   116  O O   . ALA A 1 16  ? 33.625  3.213   -24.957 1.00 31.89 ?  16  ALA E O   1 
ATOM   117  C CB  . ALA A 1 16  ? 35.880  2.681   -22.374 1.00 33.80 ?  16  ALA E CB  1 
ATOM   118  N N   . SER A 1 17  ? 35.840  3.323   -25.276 1.00 31.50 ?  17  SER E N   1 
ATOM   119  C CA  . SER A 1 17  ? 35.773  2.857   -26.649 1.00 33.57 ?  17  SER E CA  1 
ATOM   120  C C   . SER A 1 17  ? 36.645  1.615   -26.799 1.00 33.21 ?  17  SER E C   1 
ATOM   121  O O   . SER A 1 17  ? 37.530  1.348   -25.978 1.00 32.18 ?  17  SER E O   1 
ATOM   122  C CB  . SER A 1 17  ? 36.215  3.946   -27.633 1.00 33.75 ?  17  SER E CB  1 
ATOM   123  O OG  . SER A 1 17  ? 37.595  4.226   -27.467 1.00 45.95 ?  17  SER E OG  1 
ATOM   124  N N   . VAL A 1 18  ? 36.371  0.837   -27.850 1.00 29.36 ?  18  VAL E N   1 
ATOM   125  C CA  . VAL A 1 18  ? 37.122  -0.378  -28.130 1.00 31.16 ?  18  VAL E CA  1 
ATOM   126  C C   . VAL A 1 18  ? 37.434  -0.405  -29.621 1.00 29.51 ?  18  VAL E C   1 
ATOM   127  O O   . VAL A 1 18  ? 36.657  0.089   -30.445 1.00 28.99 ?  18  VAL E O   1 
ATOM   128  C CB  . VAL A 1 18  ? 36.341  -1.650  -27.692 1.00 30.57 ?  18  VAL E CB  1 
ATOM   129  C CG1 . VAL A 1 18  ? 35.052  -1.815  -28.484 1.00 31.19 ?  18  VAL E CG1 1 
ATOM   130  C CG2 . VAL A 1 18  ? 37.213  -2.908  -27.804 1.00 32.80 ?  18  VAL E CG2 1 
ATOM   131  N N   . ARG A 1 19  ? 38.598  -0.949  -29.960 1.00 30.24 ?  19  ARG E N   1 
ATOM   132  C CA  . ARG A 1 19  ? 38.982  -1.203  -31.342 1.00 30.25 ?  19  ARG E CA  1 
ATOM   133  C C   . ARG A 1 19  ? 39.298  -2.682  -31.506 1.00 27.96 ?  19  ARG E C   1 
ATOM   134  O O   . ARG A 1 19  ? 40.059  -3.247  -30.712 1.00 27.37 ?  19  ARG E O   1 
ATOM   135  C CB  . ARG A 1 19  ? 40.188  -0.365  -31.751 1.00 28.82 ?  19  ARG E CB  1 
ATOM   136  C CG  . ARG A 1 19  ? 40.444  -0.356  -33.250 1.00 33.58 ?  19  ARG E CG  1 
ATOM   137  C CD  . ARG A 1 19  ? 41.822  0.224   -33.564 1.00 35.26 ?  19  ARG E CD  1 
ATOM   138  N NE  . ARG A 1 19  ? 42.838  -0.353  -32.694 1.00 41.69 ?  19  ARG E NE  1 
ATOM   139  C CZ  . ARG A 1 19  ? 43.591  0.345   -31.853 1.00 46.30 ?  19  ARG E CZ  1 
ATOM   140  N NH1 . ARG A 1 19  ? 43.519  1.667   -31.790 1.00 47.13 ?  19  ARG E NH1 1 
ATOM   141  N NH2 . ARG A 1 19  ? 44.432  -0.301  -31.049 1.00 44.68 ?  19  ARG E NH2 1 
ATOM   142  N N   . VAL A 1 20  ? 38.709  -3.304  -32.522 1.00 25.07 ?  20  VAL E N   1 
ATOM   143  C CA  . VAL A 1 20  ? 38.949  -4.711  -32.826 1.00 24.72 ?  20  VAL E CA  1 
ATOM   144  C C   . VAL A 1 20  ? 39.599  -4.792  -34.198 1.00 24.08 ?  20  VAL E C   1 
ATOM   145  O O   . VAL A 1 20  ? 39.154  -4.125  -35.138 1.00 24.33 ?  20  VAL E O   1 
ATOM   146  C CB  . VAL A 1 20  ? 37.631  -5.520  -32.790 1.00 23.48 ?  20  VAL E CB  1 
ATOM   147  C CG1 . VAL A 1 20  ? 37.897  -7.014  -33.137 1.00 23.66 ?  20  VAL E CG1 1 
ATOM   148  C CG2 . VAL A 1 20  ? 36.995  -5.401  -31.420 1.00 26.81 ?  20  VAL E CG2 1 
ATOM   149  N N   . SER A 1 21  ? 40.636  -5.606  -34.325 1.00 21.72 ?  21  SER E N   1 
ATOM   150  C CA  . SER A 1 21  ? 41.272  -5.770  -35.622 1.00 23.56 ?  21  SER E CA  1 
ATOM   151  C C   . SER A 1 21  ? 40.946  -7.132  -36.227 1.00 22.17 ?  21  SER E C   1 
ATOM   152  O O   . SER A 1 21  ? 40.565  -8.078  -35.537 1.00 22.55 ?  21  SER E O   1 
ATOM   153  C CB  . SER A 1 21  ? 42.795  -5.616  -35.519 1.00 22.36 ?  21  SER E CB  1 
ATOM   154  O OG  . SER A 1 21  ? 43.352  -6.694  -34.765 1.00 23.83 ?  21  SER E OG  1 
ATOM   155  N N   . CYS A 1 22  ? 41.158  -7.216  -37.536 1.00 21.86 ?  22  CYS E N   1 
ATOM   156  C CA  . CYS A 1 22  ? 40.839  -8.397  -38.332 1.00 20.97 ?  22  CYS E CA  1 
ATOM   157  C C   . CYS A 1 22  ? 41.915  -8.468  -39.404 1.00 23.54 ?  22  CYS E C   1 
ATOM   158  O O   . CYS A 1 22  ? 41.894  -7.660  -40.343 1.00 23.65 ?  22  CYS E O   1 
ATOM   159  C CB  . CYS A 1 22  ? 39.438  -8.263  -38.946 1.00 22.29 ?  22  CYS E CB  1 
ATOM   160  S SG  . CYS A 1 22  ? 38.939  -9.587  -40.098 1.00 26.54 ?  22  CYS E SG  1 
ATOM   161  N N   . LYS A 1 23  ? 42.867  -9.398  -39.251 1.00 22.80 ?  23  LYS E N   1 
ATOM   162  C CA  . LYS A 1 23  ? 44.015  -9.526  -40.145 1.00 21.92 ?  23  LYS E CA  1 
ATOM   163  C C   . LYS A 1 23  ? 43.786  -10.613 -41.182 1.00 21.62 ?  23  LYS E C   1 
ATOM   164  O O   . LYS A 1 23  ? 43.594  -11.785 -40.835 1.00 24.29 ?  23  LYS E O   1 
ATOM   165  C CB  . LYS A 1 23  ? 45.293  -9.823  -39.348 1.00 22.66 ?  23  LYS E CB  1 
ATOM   166  C CG  . LYS A 1 23  ? 45.612  -8.741  -38.306 1.00 24.45 ?  23  LYS E CG  1 
ATOM   167  C CD  . LYS A 1 23  ? 46.859  -9.047  -37.537 1.00 26.79 ?  23  LYS E CD  1 
ATOM   168  C CE  . LYS A 1 23  ? 47.211  -7.903  -36.601 1.00 29.85 ?  23  LYS E CE  1 
ATOM   169  N NZ  . LYS A 1 23  ? 48.179  -8.342  -35.557 1.00 28.52 ?  23  LYS E NZ  1 
ATOM   170  N N   . ALA A 1 24  ? 43.893  -10.242 -42.452 1.00 21.80 ?  24  ALA E N   1 
ATOM   171  C CA  . ALA A 1 24  ? 43.593  -11.137 -43.563 1.00 20.18 ?  24  ALA E CA  1 
ATOM   172  C C   . ALA A 1 24  ? 44.846  -11.812 -44.103 1.00 25.11 ?  24  ALA E C   1 
ATOM   173  O O   . ALA A 1 24  ? 45.938  -11.236 -44.093 1.00 22.24 ?  24  ALA E O   1 
ATOM   174  C CB  . ALA A 1 24  ? 42.915  -10.346 -44.695 1.00 24.32 ?  24  ALA E CB  1 
ATOM   175  N N   . SER A 1 25  ? 44.675  -13.041 -44.591 1.00 18.08 ?  25  SER E N   1 
ATOM   176  C CA  . SER A 1 25  ? 45.740  -13.708 -45.329 1.00 20.67 ?  25  SER E CA  1 
ATOM   177  C C   . SER A 1 25  ? 45.100  -14.601 -46.377 1.00 23.23 ?  25  SER E C   1 
ATOM   178  O O   . SER A 1 25  ? 43.957  -15.040 -46.220 1.00 22.00 ?  25  SER E O   1 
ATOM   179  C CB  . SER A 1 25  ? 46.670  -14.525 -44.405 1.00 23.03 ?  25  SER E CB  1 
ATOM   180  O OG  . SER A 1 25  ? 45.996  -15.669 -43.909 1.00 25.69 ?  25  SER E OG  1 
ATOM   181  N N   . GLY A 1 26  ? 45.825  -14.810 -47.479 1.00 21.65 ?  26  GLY E N   1 
ATOM   182  C CA  . GLY A 1 26  ? 45.447  -15.822 -48.452 1.00 22.70 ?  26  GLY E CA  1 
ATOM   183  C C   . GLY A 1 26  ? 44.589  -15.341 -49.598 1.00 24.98 ?  26  GLY E C   1 
ATOM   184  O O   . GLY A 1 26  ? 44.066  -16.175 -50.352 1.00 26.40 ?  26  GLY E O   1 
ATOM   185  N N   . TYR A 1 27  ? 44.378  -14.032 -49.730 1.00 25.43 ?  27  TYR E N   1 
ATOM   186  C CA  . TYR A 1 27  ? 43.602  -13.529 -50.851 1.00 21.92 ?  27  TYR E CA  1 
ATOM   187  C C   . TYR A 1 27  ? 43.973  -12.073 -51.070 1.00 23.77 ?  27  TYR E C   1 
ATOM   188  O O   . TYR A 1 27  ? 44.703  -11.470 -50.277 1.00 24.21 ?  27  TYR E O   1 
ATOM   189  C CB  . TYR A 1 27  ? 42.088  -13.693 -50.619 1.00 22.48 ?  27  TYR E CB  1 
ATOM   190  C CG  . TYR A 1 27  ? 41.518  -12.804 -49.529 1.00 20.62 ?  27  TYR E CG  1 
ATOM   191  C CD1 . TYR A 1 27  ? 41.664  -13.131 -48.192 1.00 20.75 ?  27  TYR E CD1 1 
ATOM   192  C CD2 . TYR A 1 27  ? 40.814  -11.645 -49.849 1.00 22.62 ?  27  TYR E CD2 1 
ATOM   193  C CE1 . TYR A 1 27  ? 41.123  -12.340 -47.196 1.00 21.20 ?  27  TYR E CE1 1 
ATOM   194  C CE2 . TYR A 1 27  ? 40.276  -10.837 -48.857 1.00 24.72 ?  27  TYR E CE2 1 
ATOM   195  C CZ  . TYR A 1 27  ? 40.432  -11.198 -47.537 1.00 23.22 ?  27  TYR E CZ  1 
ATOM   196  O OH  . TYR A 1 27  ? 39.895  -10.416 -46.550 1.00 23.33 ?  27  TYR E OH  1 
ATOM   197  N N   . THR A 1 28  ? 43.478  -11.516 -52.176 1.00 24.14 ?  28  THR E N   1 
ATOM   198  C CA  . THR A 1 28  ? 43.766  -10.120 -52.502 1.00 24.93 ?  28  THR E CA  1 
ATOM   199  C C   . THR A 1 28  ? 42.799  -9.241  -51.724 1.00 26.15 ?  28  THR E C   1 
ATOM   200  O O   . THR A 1 28  ? 41.664  -8.994  -52.152 1.00 23.22 ?  28  THR E O   1 
ATOM   201  C CB  . THR A 1 28  ? 43.692  -9.877  -54.001 1.00 29.55 ?  28  THR E CB  1 
ATOM   202  O OG1 . THR A 1 28  ? 44.670  -10.710 -54.646 1.00 30.05 ?  28  THR E OG1 1 
ATOM   203  C CG2 . THR A 1 28  ? 43.991  -8.413  -54.320 1.00 23.63 ?  28  THR E CG2 1 
ATOM   204  N N   . PHE A 1 29  ? 43.292  -8.745  -50.590 1.00 25.92 ?  29  PHE E N   1 
ATOM   205  C CA  . PHE A 1 29  ? 42.463  -8.066  -49.604 1.00 26.17 ?  29  PHE E CA  1 
ATOM   206  C C   . PHE A 1 29  ? 41.675  -6.919  -50.220 1.00 27.34 ?  29  PHE E C   1 
ATOM   207  O O   . PHE A 1 29  ? 40.505  -6.705  -49.884 1.00 25.06 ?  29  PHE E O   1 
ATOM   208  C CB  . PHE A 1 29  ? 43.379  -7.586  -48.485 1.00 28.12 ?  29  PHE E CB  1 
ATOM   209  C CG  . PHE A 1 29  ? 42.704  -6.790  -47.416 1.00 27.61 ?  29  PHE E CG  1 
ATOM   210  C CD1 . PHE A 1 29  ? 41.863  -7.408  -46.495 1.00 27.58 ?  29  PHE E CD1 1 
ATOM   211  C CD2 . PHE A 1 29  ? 42.971  -5.430  -47.279 1.00 28.31 ?  29  PHE E CD2 1 
ATOM   212  C CE1 . PHE A 1 29  ? 41.262  -6.670  -45.477 1.00 27.71 ?  29  PHE E CE1 1 
ATOM   213  C CE2 . PHE A 1 29  ? 42.385  -4.693  -46.264 1.00 29.41 ?  29  PHE E CE2 1 
ATOM   214  C CZ  . PHE A 1 29  ? 41.533  -5.317  -45.358 1.00 25.83 ?  29  PHE E CZ  1 
ATOM   215  N N   . ALA A 1 30  ? 42.279  -6.206  -51.162 1.00 25.64 ?  30  ALA E N   1 
ATOM   216  C CA  . ALA A 1 30  ? 41.673  -4.977  -51.667 1.00 29.76 ?  30  ALA E CA  1 
ATOM   217  C C   . ALA A 1 30  ? 40.546  -5.224  -52.667 1.00 27.34 ?  30  ALA E C   1 
ATOM   218  O O   . ALA A 1 30  ? 39.917  -4.254  -53.102 1.00 29.66 ?  30  ALA E O   1 
ATOM   219  C CB  . ALA A 1 30  ? 42.761  -4.082  -52.295 1.00 27.54 ?  30  ALA E CB  1 
ATOM   220  N N   . THR A 1 31  ? 40.245  -6.478  -53.038 1.00 24.44 ?  31  THR E N   1 
ATOM   221  C CA  . THR A 1 31  ? 39.131  -6.713  -53.949 1.00 23.29 ?  31  THR E CA  1 
ATOM   222  C C   . THR A 1 31  ? 37.861  -7.209  -53.250 1.00 23.56 ?  31  THR E C   1 
ATOM   223  O O   . THR A 1 31  ? 36.818  -7.331  -53.912 1.00 25.70 ?  31  THR E O   1 
ATOM   224  C CB  . THR A 1 31  ? 39.523  -7.710  -55.056 1.00 25.89 ?  31  THR E CB  1 
ATOM   225  O OG1 . THR A 1 31  ? 39.762  -9.021  -54.507 1.00 25.23 ?  31  THR E OG1 1 
ATOM   226  C CG2 . THR A 1 31  ? 40.769  -7.230  -55.798 1.00 25.97 ?  31  THR E CG2 1 
ATOM   227  N N   . TYR A 1 32  ? 37.918  -7.490  -51.947 1.00 22.63 ?  32  TYR E N   1 
ATOM   228  C CA  . TYR A 1 32  ? 36.775  -7.968  -51.168 1.00 21.82 ?  32  TYR E CA  1 
ATOM   229  C C   . TYR A 1 32  ? 36.441  -6.947  -50.095 1.00 25.04 ?  32  TYR E C   1 
ATOM   230  O O   . TYR A 1 32  ? 37.264  -6.102  -49.748 1.00 28.54 ?  32  TYR E O   1 
ATOM   231  C CB  . TYR A 1 32  ? 37.077  -9.328  -50.486 1.00 20.49 ?  32  TYR E CB  1 
ATOM   232  C CG  . TYR A 1 32  ? 37.060  -10.485 -51.442 1.00 24.34 ?  32  TYR E CG  1 
ATOM   233  C CD1 . TYR A 1 32  ? 38.159  -10.759 -52.256 1.00 23.64 ?  32  TYR E CD1 1 
ATOM   234  C CD2 . TYR A 1 32  ? 35.959  -11.314 -51.523 1.00 24.30 ?  32  TYR E CD2 1 
ATOM   235  C CE1 . TYR A 1 32  ? 38.130  -11.826 -53.140 1.00 21.84 ?  32  TYR E CE1 1 
ATOM   236  C CE2 . TYR A 1 32  ? 35.923  -12.381 -52.389 1.00 23.16 ?  32  TYR E CE2 1 
ATOM   237  C CZ  . TYR A 1 32  ? 37.007  -12.625 -53.193 1.00 25.34 ?  32  TYR E CZ  1 
ATOM   238  O OH  . TYR A 1 32  ? 36.949  -13.688 -54.048 1.00 23.63 ?  32  TYR E OH  1 
ATOM   239  N N   . GLY A 1 33  ? 35.225  -7.035  -49.558 1.00 23.44 ?  33  GLY E N   1 
ATOM   240  C CA  . GLY A 1 33  ? 34.891  -6.270  -48.375 1.00 20.55 ?  33  GLY E CA  1 
ATOM   241  C C   . GLY A 1 33  ? 35.125  -7.035  -47.100 1.00 21.59 ?  33  GLY E C   1 
ATOM   242  O O   . GLY A 1 33  ? 35.393  -8.241  -47.083 1.00 22.05 ?  33  GLY E O   1 
ATOM   243  N N   . ILE A 1 34  ? 35.049  -6.311  -45.997 1.00 19.74 ?  34  ILE E N   1 
ATOM   244  C CA  . ILE A 1 34  ? 35.029  -6.899  -44.672 1.00 20.10 ?  34  ILE E CA  1 
ATOM   245  C C   . ILE A 1 34  ? 33.714  -6.508  -44.019 1.00 20.38 ?  34  ILE E C   1 
ATOM   246  O O   . ILE A 1 34  ? 33.350  -5.317  -43.993 1.00 20.90 ?  34  ILE E O   1 
ATOM   247  C CB  . ILE A 1 34  ? 36.208  -6.440  -43.804 1.00 21.58 ?  34  ILE E CB  1 
ATOM   248  C CG1 . ILE A 1 34  ? 37.531  -7.065  -44.304 1.00 21.79 ?  34  ILE E CG1 1 
ATOM   249  C CG2 . ILE A 1 34  ? 35.936  -6.832  -42.344 1.00 23.13 ?  34  ILE E CG2 1 
ATOM   250  C CD1 . ILE A 1 34  ? 37.620  -8.603  -44.158 1.00 20.60 ?  34  ILE E CD1 1 
ATOM   251  N N   . THR A 1 35  ? 33.023  -7.503  -43.480 1.00 18.22 ?  35  THR E N   1 
ATOM   252  C CA  . THR A 1 35  ? 31.742  -7.327  -42.799 1.00 21.19 ?  35  THR E CA  1 
ATOM   253  C C   . THR A 1 35  ? 31.968  -7.574  -41.316 1.00 21.17 ?  35  THR E C   1 
ATOM   254  O O   . THR A 1 35  ? 32.813  -8.394  -40.938 1.00 21.54 ?  35  THR E O   1 
ATOM   255  C CB  . THR A 1 35  ? 30.703  -8.321  -43.366 1.00 20.17 ?  35  THR E CB  1 
ATOM   256  O OG1 . THR A 1 35  ? 30.467  -8.035  -44.753 1.00 22.56 ?  35  THR E OG1 1 
ATOM   257  C CG2 . THR A 1 35  ? 29.373  -8.300  -42.601 1.00 18.93 ?  35  THR E CG2 1 
ATOM   258  N N   . TRP A 1 36  ? 31.263  -6.842  -40.469 1.00 19.91 ?  36  TRP E N   1 
ATOM   259  C CA  . TRP A 1 36  ? 31.279  -7.120  -39.042 1.00 18.58 ?  36  TRP E CA  1 
ATOM   260  C C   . TRP A 1 36  ? 29.880  -7.518  -38.592 1.00 21.47 ?  36  TRP E C   1 
ATOM   261  O O   . TRP A 1 36  ? 28.881  -6.937  -39.025 1.00 20.23 ?  36  TRP E O   1 
ATOM   262  C CB  . TRP A 1 36  ? 31.779  -5.913  -38.230 1.00 19.95 ?  36  TRP E CB  1 
ATOM   263  C CG  . TRP A 1 36  ? 33.237  -5.594  -38.483 1.00 22.52 ?  36  TRP E CG  1 
ATOM   264  C CD1 . TRP A 1 36  ? 33.756  -4.798  -39.472 1.00 21.72 ?  36  TRP E CD1 1 
ATOM   265  C CD2 . TRP A 1 36  ? 34.352  -6.096  -37.742 1.00 23.11 ?  36  TRP E CD2 1 
ATOM   266  N NE1 . TRP A 1 36  ? 35.131  -4.778  -39.383 1.00 24.49 ?  36  TRP E NE1 1 
ATOM   267  C CE2 . TRP A 1 36  ? 35.520  -5.571  -38.329 1.00 22.33 ?  36  TRP E CE2 1 
ATOM   268  C CE3 . TRP A 1 36  ? 34.472  -6.928  -36.627 1.00 21.91 ?  36  TRP E CE3 1 
ATOM   269  C CZ2 . TRP A 1 36  ? 36.801  -5.839  -37.828 1.00 21.43 ?  36  TRP E CZ2 1 
ATOM   270  C CZ3 . TRP A 1 36  ? 35.750  -7.211  -36.136 1.00 23.28 ?  36  TRP E CZ3 1 
ATOM   271  C CH2 . TRP A 1 36  ? 36.899  -6.651  -36.740 1.00 22.69 ?  36  TRP E CH2 1 
ATOM   272  N N   . VAL A 1 37  ? 29.822  -8.539  -37.757 1.00 19.71 ?  37  VAL E N   1 
ATOM   273  C CA  . VAL A 1 37  ? 28.570  -9.073  -37.237 1.00 20.81 ?  37  VAL E CA  1 
ATOM   274  C C   . VAL A 1 37  ? 28.761  -9.249  -35.740 1.00 23.56 ?  37  VAL E C   1 
ATOM   275  O O   . VAL A 1 37  ? 29.841  -9.631  -35.282 1.00 25.56 ?  37  VAL E O   1 
ATOM   276  C CB  . VAL A 1 37  ? 28.218  -10.416 -37.917 1.00 23.70 ?  37  VAL E CB  1 
ATOM   277  C CG1 . VAL A 1 37  ? 27.005  -11.074 -37.242 1.00 22.15 ?  37  VAL E CG1 1 
ATOM   278  C CG2 . VAL A 1 37  ? 27.969  -10.213 -39.420 1.00 23.21 ?  37  VAL E CG2 1 
ATOM   279  N N   . ARG A 1 38  ? 27.714  -8.990  -34.984 1.00 23.59 ?  38  ARG E N   1 
ATOM   280  C CA  . ARG A 1 38  ? 27.751  -8.966  -33.535 1.00 24.00 ?  38  ARG E CA  1 
ATOM   281  C C   . ARG A 1 38  ? 26.804  -10.024 -32.981 1.00 25.09 ?  38  ARG E C   1 
ATOM   282  O O   . ARG A 1 38  ? 25.756  -10.289 -33.574 1.00 23.95 ?  38  ARG E O   1 
ATOM   283  C CB  . ARG A 1 38  ? 27.331  -7.548  -33.068 1.00 32.30 ?  38  ARG E CB  1 
ATOM   284  C CG  . ARG A 1 38  ? 27.117  -7.465  -31.637 1.00 35.32 ?  38  ARG E CG  1 
ATOM   285  C CD  . ARG A 1 38  ? 27.027  -6.074  -31.134 1.00 33.98 ?  38  ARG E CD  1 
ATOM   286  N NE  . ARG A 1 38  ? 25.729  -5.430  -31.186 1.00 34.10 ?  38  ARG E NE  1 
ATOM   287  C CZ  . ARG A 1 38  ? 25.519  -4.283  -30.559 1.00 38.04 ?  38  ARG E CZ  1 
ATOM   288  N NH1 . ARG A 1 38  ? 26.502  -3.673  -29.912 1.00 32.46 ?  38  ARG E NH1 1 
ATOM   289  N NH2 . ARG A 1 38  ? 24.295  -3.765  -30.540 1.00 37.68 ?  38  ARG E NH2 1 
ATOM   290  N N   . GLN A 1 39  ? 27.165  -10.639 -31.846 1.00 22.92 ?  39  GLN E N   1 
ATOM   291  C CA  . GLN A 1 39  ? 26.290  -11.628 -31.209 1.00 24.41 ?  39  GLN E CA  1 
ATOM   292  C C   . GLN A 1 39  ? 26.325  -11.476 -29.694 1.00 28.28 ?  39  GLN E C   1 
ATOM   293  O O   . GLN A 1 39  ? 27.298  -11.877 -29.052 1.00 27.13 ?  39  GLN E O   1 
ATOM   294  C CB  . GLN A 1 39  ? 26.689  -13.047 -31.607 1.00 26.27 ?  39  GLN E CB  1 
ATOM   295  C CG  . GLN A 1 39  ? 25.704  -14.104 -31.156 1.00 26.85 ?  39  GLN E CG  1 
ATOM   296  C CD  . GLN A 1 39  ? 26.020  -15.430 -31.782 1.00 26.55 ?  39  GLN E CD  1 
ATOM   297  O OE1 . GLN A 1 39  ? 27.193  -15.835 -31.872 1.00 27.40 ?  39  GLN E OE1 1 
ATOM   298  N NE2 . GLN A 1 39  ? 24.989  -16.116 -32.245 1.00 28.06 ?  39  GLN E NE2 1 
ATOM   299  N N   . ALA A 1 40  ? 25.250  -10.934 -29.117 1.00 28.21 ?  40  ALA E N   1 
ATOM   300  C CA  . ALA A 1 40  ? 25.135  -10.846 -27.669 1.00 30.46 ?  40  ALA E CA  1 
ATOM   301  C C   . ALA A 1 40  ? 24.944  -12.239 -27.072 1.00 32.14 ?  40  ALA E C   1 
ATOM   302  O O   . ALA A 1 40  ? 24.483  -13.156 -27.756 1.00 30.56 ?  40  ALA E O   1 
ATOM   303  C CB  . ALA A 1 40  ? 23.964  -9.943  -27.283 1.00 28.74 ?  40  ALA E CB  1 
ATOM   304  N N   . PRO A 1 41  ? 25.302  -12.428 -25.799 1.00 32.71 ?  41  PRO E N   1 
ATOM   305  C CA  . PRO A 1 41  ? 25.205  -13.767 -25.206 1.00 35.59 ?  41  PRO E CA  1 
ATOM   306  C C   . PRO A 1 41  ? 23.780  -14.288 -25.294 1.00 33.31 ?  41  PRO E C   1 
ATOM   307  O O   . PRO A 1 41  ? 22.825  -13.600 -24.926 1.00 37.51 ?  41  PRO E O   1 
ATOM   308  C CB  . PRO A 1 41  ? 25.641  -13.544 -23.753 1.00 37.70 ?  41  PRO E CB  1 
ATOM   309  C CG  . PRO A 1 41  ? 26.525  -12.352 -23.810 1.00 35.51 ?  41  PRO E CG  1 
ATOM   310  C CD  . PRO A 1 41  ? 25.867  -11.462 -24.838 1.00 35.30 ?  41  PRO E CD  1 
ATOM   311  N N   . GLY A 1 42  ? 23.645  -15.492 -25.833 1.00 35.65 ?  42  GLY E N   1 
ATOM   312  C CA  . GLY A 1 42  ? 22.353  -16.133 -25.972 1.00 37.50 ?  42  GLY E CA  1 
ATOM   313  C C   . GLY A 1 42  ? 21.473  -15.602 -27.080 1.00 39.01 ?  42  GLY E C   1 
ATOM   314  O O   . GLY A 1 42  ? 20.325  -16.050 -27.196 1.00 35.30 ?  42  GLY E O   1 
ATOM   315  N N   . ARG A 1 43  ? 21.955  -14.664 -27.899 1.00 31.65 ?  43  ARG E N   1 
ATOM   316  C CA  . ARG A 1 43  ? 21.111  -14.035 -28.915 1.00 29.36 ?  43  ARG E CA  1 
ATOM   317  C C   . ARG A 1 43  ? 21.650  -14.323 -30.315 1.00 27.57 ?  43  ARG E C   1 
ATOM   318  O O   . ARG A 1 43  ? 22.609  -15.077 -30.498 1.00 26.99 ?  43  ARG E O   1 
ATOM   319  C CB  . ARG A 1 43  ? 20.973  -12.534 -28.660 1.00 31.73 ?  43  ARG E CB  1 
ATOM   320  C CG  . ARG A 1 43  ? 20.451  -12.201 -27.269 1.00 41.24 ?  43  ARG E CG  1 
ATOM   321  C CD  . ARG A 1 43  ? 18.924  -12.284 -27.258 1.00 49.81 ?  43  ARG E CD  1 
ATOM   322  N NE  . ARG A 1 43  ? 18.310  -11.334 -28.184 1.00 56.51 ?  43  ARG E NE  1 
ATOM   323  C CZ  . ARG A 1 43  ? 17.456  -10.382 -27.827 1.00 62.53 ?  43  ARG E CZ  1 
ATOM   324  N NH1 . ARG A 1 43  ? 17.076  -10.233 -26.569 1.00 64.22 ?  43  ARG E NH1 1 
ATOM   325  N NH2 . ARG A 1 43  ? 16.970  -9.564  -28.758 1.00 62.67 ?  43  ARG E NH2 1 
ATOM   326  N N   . GLY A 1 44  ? 21.013  -13.718 -31.314 1.00 25.67 ?  44  GLY E N   1 
ATOM   327  C CA  . GLY A 1 44  ? 21.285  -14.053 -32.693 1.00 28.29 ?  44  GLY E CA  1 
ATOM   328  C C   . GLY A 1 44  ? 22.327  -13.151 -33.327 1.00 28.89 ?  44  GLY E C   1 
ATOM   329  O O   . GLY A 1 44  ? 22.882  -12.243 -32.709 1.00 29.42 ?  44  GLY E O   1 
ATOM   330  N N   . LEU A 1 45  ? 22.579  -13.408 -34.606 1.00 25.40 ?  45  LEU E N   1 
ATOM   331  C CA  . LEU A 1 45  ? 23.564  -12.633 -35.348 1.00 26.34 ?  45  LEU E CA  1 
ATOM   332  C C   . LEU A 1 45  ? 22.968  -11.289 -35.761 1.00 27.96 ?  45  LEU E C   1 
ATOM   333  O O   . LEU A 1 45  ? 21.857  -11.219 -36.301 1.00 25.72 ?  45  LEU E O   1 
ATOM   334  C CB  . LEU A 1 45  ? 24.032  -13.407 -36.579 1.00 20.12 ?  45  LEU E CB  1 
ATOM   335  C CG  . LEU A 1 45  ? 24.671  -14.777 -36.343 1.00 23.99 ?  45  LEU E CG  1 
ATOM   336  C CD1 . LEU A 1 45  ? 25.063  -15.351 -37.697 1.00 22.64 ?  45  LEU E CD1 1 
ATOM   337  C CD2 . LEU A 1 45  ? 25.896  -14.697 -35.419 1.00 23.48 ?  45  LEU E CD2 1 
ATOM   338  N N   . GLU A 1 46  ? 23.713  -10.222 -35.501 1.00 22.19 ?  46  GLU E N   1 
ATOM   339  C CA  . GLU A 1 46  ? 23.298  -8.854  -35.805 1.00 24.88 ?  46  GLU E CA  1 
ATOM   340  C C   . GLU A 1 46  ? 24.328  -8.223  -36.735 1.00 25.33 ?  46  GLU E C   1 
ATOM   341  O O   . GLU A 1 46  ? 25.499  -8.072  -36.362 1.00 23.20 ?  46  GLU E O   1 
ATOM   342  C CB  . GLU A 1 46  ? 23.167  -8.040  -34.520 1.00 28.98 ?  46  GLU E CB  1 
ATOM   343  C CG  . GLU A 1 46  ? 22.915  -6.530  -34.721 1.00 32.44 ?  46  GLU E CG  1 
ATOM   344  C CD  . GLU A 1 46  ? 22.623  -5.779  -33.410 1.00 38.23 ?  46  GLU E CD  1 
ATOM   345  O OE1 . GLU A 1 46  ? 23.390  -5.933  -32.434 1.00 41.70 ?  46  GLU E OE1 1 
ATOM   346  O OE2 . GLU A 1 46  ? 21.621  -5.024  -33.357 1.00 47.09 ?  46  GLU E OE2 1 
ATOM   347  N N   . TRP A 1 47  ? 23.897  -7.875  -37.944 1.00 22.71 ?  47  TRP E N   1 
ATOM   348  C CA  . TRP A 1 47  ? 24.760  -7.166  -38.885 1.00 22.76 ?  47  TRP E CA  1 
ATOM   349  C C   . TRP A 1 47  ? 25.171  -5.809  -38.317 1.00 23.13 ?  47  TRP E C   1 
ATOM   350  O O   . TRP A 1 47  ? 24.326  -5.024  -37.878 1.00 23.95 ?  47  TRP E O   1 
ATOM   351  C CB  . TRP A 1 47  ? 24.024  -6.977  -40.215 1.00 22.10 ?  47  TRP E CB  1 
ATOM   352  C CG  . TRP A 1 47  ? 24.823  -6.286  -41.311 1.00 22.70 ?  47  TRP E CG  1 
ATOM   353  C CD1 . TRP A 1 47  ? 25.989  -6.716  -41.875 1.00 21.76 ?  47  TRP E CD1 1 
ATOM   354  C CD2 . TRP A 1 47  ? 24.461  -5.086  -42.005 1.00 21.52 ?  47  TRP E CD2 1 
ATOM   355  N NE1 . TRP A 1 47  ? 26.394  -5.837  -42.860 1.00 23.18 ?  47  TRP E NE1 1 
ATOM   356  C CE2 . TRP A 1 47  ? 25.469  -4.831  -42.961 1.00 21.18 ?  47  TRP E CE2 1 
ATOM   357  C CE3 . TRP A 1 47  ? 23.378  -4.196  -41.908 1.00 21.34 ?  47  TRP E CE3 1 
ATOM   358  C CZ2 . TRP A 1 47  ? 25.438  -3.718  -43.806 1.00 22.49 ?  47  TRP E CZ2 1 
ATOM   359  C CZ3 . TRP A 1 47  ? 23.349  -3.084  -42.754 1.00 20.96 ?  47  TRP E CZ3 1 
ATOM   360  C CH2 . TRP A 1 47  ? 24.367  -2.868  -43.696 1.00 21.95 ?  47  TRP E CH2 1 
ATOM   361  N N   . VAL A 1 48  ? 26.470  -5.528  -38.322 1.00 22.70 ?  48  VAL E N   1 
ATOM   362  C CA  . VAL A 1 48  ? 26.983  -4.209  -37.942 1.00 20.89 ?  48  VAL E CA  1 
ATOM   363  C C   . VAL A 1 48  ? 27.207  -3.333  -39.164 1.00 24.21 ?  48  VAL E C   1 
ATOM   364  O O   . VAL A 1 48  ? 26.756  -2.181  -39.203 1.00 21.38 ?  48  VAL E O   1 
ATOM   365  C CB  . VAL A 1 48  ? 28.278  -4.343  -37.102 1.00 22.68 ?  48  VAL E CB  1 
ATOM   366  C CG1 . VAL A 1 48  ? 28.841  -2.938  -36.731 1.00 20.40 ?  48  VAL E CG1 1 
ATOM   367  C CG2 . VAL A 1 48  ? 27.982  -5.099  -35.846 1.00 22.11 ?  48  VAL E CG2 1 
ATOM   368  N N   . GLY A 1 49  ? 27.895  -3.872  -40.168 1.00 20.35 ?  49  GLY E N   1 
ATOM   369  C CA  . GLY A 1 49  ? 28.138  -3.138  -41.392 1.00 20.75 ?  49  GLY E CA  1 
ATOM   370  C C   . GLY A 1 49  ? 29.229  -3.786  -42.218 1.00 23.17 ?  49  GLY E C   1 
ATOM   371  O O   . GLY A 1 49  ? 29.733  -4.868  -41.890 1.00 20.58 ?  49  GLY E O   1 
ATOM   372  N N   . TRP A 1 50  ? 29.554  -3.129  -43.333 1.00 19.00 ?  50  TRP E N   1 
ATOM   373  C CA  . TRP A 1 50  ? 30.686  -3.560  -44.143 1.00 20.55 ?  50  TRP E CA  1 
ATOM   374  C C   . TRP A 1 50  ? 31.472  -2.348  -44.603 1.00 24.46 ?  50  TRP E C   1 
ATOM   375  O O   . TRP A 1 50  ? 30.978  -1.208  -44.591 1.00 21.29 ?  50  TRP E O   1 
ATOM   376  C CB  . TRP A 1 50  ? 30.298  -4.400  -45.382 1.00 19.60 ?  50  TRP E CB  1 
ATOM   377  C CG  . TRP A 1 50  ? 29.230  -3.824  -46.291 1.00 21.74 ?  50  TRP E CG  1 
ATOM   378  C CD1 . TRP A 1 50  ? 27.914  -4.267  -46.393 1.00 20.84 ?  50  TRP E CD1 1 
ATOM   379  C CD2 . TRP A 1 50  ? 29.365  -2.756  -47.249 1.00 22.30 ?  50  TRP E CD2 1 
ATOM   380  N NE1 . TRP A 1 50  ? 27.250  -3.531  -47.337 1.00 21.18 ?  50  TRP E NE1 1 
ATOM   381  C CE2 . TRP A 1 50  ? 28.104  -2.598  -47.875 1.00 24.07 ?  50  TRP E CE2 1 
ATOM   382  C CE3 . TRP A 1 50  ? 30.426  -1.916  -47.633 1.00 23.74 ?  50  TRP E CE3 1 
ATOM   383  C CZ2 . TRP A 1 50  ? 27.863  -1.619  -48.850 1.00 23.81 ?  50  TRP E CZ2 1 
ATOM   384  C CZ3 . TRP A 1 50  ? 30.197  -0.949  -48.610 1.00 25.36 ?  50  TRP E CZ3 1 
ATOM   385  C CH2 . TRP A 1 50  ? 28.916  -0.808  -49.209 1.00 25.12 ?  50  TRP E CH2 1 
ATOM   386  N N   . ILE A 1 51  ? 32.713  -2.624  -45.002 1.00 21.00 ?  51  ILE E N   1 
ATOM   387  C CA  . ILE A 1 51  ? 33.618  -1.638  -45.587 1.00 20.34 ?  51  ILE E CA  1 
ATOM   388  C C   . ILE A 1 51  ? 34.282  -2.251  -46.810 1.00 22.11 ?  51  ILE E C   1 
ATOM   389  O O   . ILE A 1 51  ? 34.778  -3.380  -46.755 1.00 22.57 ?  51  ILE E O   1 
ATOM   390  C CB  . ILE A 1 51  ? 34.678  -1.145  -44.571 1.00 23.22 ?  51  ILE E CB  1 
ATOM   391  C CG1 . ILE A 1 51  ? 35.575  -0.087  -45.223 1.00 23.79 ?  51  ILE E CG1 1 
ATOM   392  C CG2 . ILE A 1 51  ? 35.484  -2.334  -43.975 1.00 25.22 ?  51  ILE E CG2 1 
ATOM   393  C CD1 . ILE A 1 51  ? 36.343  0.797   -44.220 1.00 23.76 ?  51  ILE E CD1 1 
ATOM   394  N N   . THR A 1 52  ? 34.279  -1.525  -47.924 1.00 22.11 ?  52  THR E N   1 
ATOM   395  C CA  . THR A 1 52  ? 35.013  -1.978  -49.102 1.00 22.40 ?  52  THR E CA  1 
ATOM   396  C C   . THR A 1 52  ? 36.242  -1.087  -49.303 1.00 25.89 ?  52  THR E C   1 
ATOM   397  O O   . THR A 1 52  ? 36.113  0.143   -49.416 1.00 27.67 ?  52  THR E O   1 
ATOM   398  C CB  . THR A 1 52  ? 34.124  -1.995  -50.355 1.00 23.44 ?  52  THR E CB  1 
ATOM   399  O OG1 . THR A 1 52  ? 33.347  -0.790  -50.434 1.00 26.26 ?  52  THR E OG1 1 
ATOM   400  C CG2 . THR A 1 52  ? 33.151  -3.205  -50.323 1.00 26.13 ?  52  THR E CG2 1 
ATOM   401  N N   . PRO A 1 53  ? 37.446  -1.672  -49.324 1.00 25.83 ?  53  PRO E N   1 
ATOM   402  C CA  . PRO A 1 53  ? 38.682  -0.855  -49.371 1.00 30.58 ?  53  PRO E CA  1 
ATOM   403  C C   . PRO A 1 53  ? 38.943  -0.159  -50.700 1.00 34.45 ?  53  PRO E C   1 
ATOM   404  O O   . PRO A 1 53  ? 39.652  0.857   -50.714 1.00 36.94 ?  53  PRO E O   1 
ATOM   405  C CB  . PRO A 1 53  ? 39.789  -1.883  -49.075 1.00 28.59 ?  53  PRO E CB  1 
ATOM   406  C CG  . PRO A 1 53  ? 39.186  -3.208  -49.398 1.00 31.01 ?  53  PRO E CG  1 
ATOM   407  C CD  . PRO A 1 53  ? 37.733  -3.079  -49.021 1.00 28.17 ?  53  PRO E CD  1 
ATOM   408  N N   . TYR A 1 54  ? 38.405  -0.650  -51.812 1.00 30.75 ?  54  TYR E N   1 
ATOM   409  C CA  . TYR A 1 54  ? 38.691  -0.043  -53.108 1.00 32.50 ?  54  TYR E CA  1 
ATOM   410  C C   . TYR A 1 54  ? 37.911  1.237   -53.371 1.00 37.61 ?  54  TYR E C   1 
ATOM   411  O O   . TYR A 1 54  ? 38.082  1.834   -54.439 1.00 40.17 ?  54  TYR E O   1 
ATOM   412  C CB  . TYR A 1 54  ? 38.397  -1.036  -54.229 1.00 31.03 ?  54  TYR E CB  1 
ATOM   413  C CG  . TYR A 1 54  ? 37.051  -1.711  -54.111 1.00 31.98 ?  54  TYR E CG  1 
ATOM   414  C CD1 . TYR A 1 54  ? 35.884  -1.096  -54.576 1.00 30.15 ?  54  TYR E CD1 1 
ATOM   415  C CD2 . TYR A 1 54  ? 36.946  -2.966  -53.534 1.00 29.25 ?  54  TYR E CD2 1 
ATOM   416  C CE1 . TYR A 1 54  ? 34.646  -1.722  -54.458 1.00 28.69 ?  54  TYR E CE1 1 
ATOM   417  C CE2 . TYR A 1 54  ? 35.733  -3.600  -53.426 1.00 27.56 ?  54  TYR E CE2 1 
ATOM   418  C CZ  . TYR A 1 54  ? 34.586  -2.990  -53.884 1.00 29.84 ?  54  TYR E CZ  1 
ATOM   419  O OH  . TYR A 1 54  ? 33.391  -3.661  -53.752 1.00 25.22 ?  54  TYR E OH  1 
ATOM   420  N N   . ASN A 1 55  ? 37.032  1.651   -52.467 1.00 35.48 ?  55  ASN E N   1 
ATOM   421  C CA  . ASN A 1 55  ? 36.394  2.954   -52.571 1.00 35.50 ?  55  ASN E CA  1 
ATOM   422  C C   . ASN A 1 55  ? 36.190  3.562   -51.190 1.00 35.81 ?  55  ASN E C   1 
ATOM   423  O O   . ASN A 1 55  ? 35.509  4.587   -51.080 1.00 41.28 ?  55  ASN E O   1 
ATOM   424  C CB  . ASN A 1 55  ? 35.052  2.851   -53.333 1.00 37.36 ?  55  ASN E CB  1 
ATOM   425  C CG  . ASN A 1 55  ? 34.134  1.779   -52.764 1.00 32.43 ?  55  ASN E CG  1 
ATOM   426  O OD1 . ASN A 1 55  ? 34.368  1.287   -51.663 1.00 36.08 ?  55  ASN E OD1 1 
ATOM   427  N ND2 . ASN A 1 55  ? 33.108  1.396   -53.516 1.00 32.01 ?  55  ASN E ND2 1 
ATOM   428  N N   . ASP A 1 56  ? 36.739  2.944   -50.139 1.00 35.08 ?  56  ASP E N   1 
ATOM   429  C CA  . ASP A 1 56  ? 36.561  3.403   -48.756 1.00 37.54 ?  56  ASP E CA  1 
ATOM   430  C C   . ASP A 1 56  ? 35.088  3.622   -48.394 1.00 36.83 ?  56  ASP E C   1 
ATOM   431  O O   . ASP A 1 56  ? 34.762  4.452   -47.536 1.00 40.58 ?  56  ASP E O   1 
ATOM   432  C CB  . ASP A 1 56  ? 37.369  4.684   -48.487 1.00 39.98 ?  56  ASP E CB  1 
ATOM   433  C CG  . ASP A 1 56  ? 38.860  4.500   -48.744 1.00 48.81 ?  56  ASP E CG  1 
ATOM   434  O OD1 . ASP A 1 56  ? 39.387  3.405   -48.439 1.00 52.09 ?  56  ASP E OD1 1 
ATOM   435  O OD2 . ASP A 1 56  ? 39.505  5.451   -49.248 1.00 57.58 ?  56  ASP E OD2 1 
ATOM   436  N N   . ARG A 1 57  ? 34.169  2.904   -49.034 1.00 29.02 ?  57  ARG E N   1 
ATOM   437  C CA  . ARG A 1 57  ? 32.769  3.104   -48.696 1.00 30.28 ?  57  ARG E CA  1 
ATOM   438  C C   . ARG A 1 57  ? 32.387  2.180   -47.552 1.00 28.90 ?  57  ARG E C   1 
ATOM   439  O O   . ARG A 1 57  ? 32.948  1.089   -47.398 1.00 25.70 ?  57  ARG E O   1 
ATOM   440  C CB  . ARG A 1 57  ? 31.874  2.887   -49.911 1.00 33.64 ?  57  ARG E CB  1 
ATOM   441  C CG  . ARG A 1 57  ? 32.285  3.917   -50.954 1.00 40.77 ?  57  ARG E CG  1 
ATOM   442  C CD  . ARG A 1 57  ? 31.276  5.010   -51.202 1.00 45.26 ?  57  ARG E CD  1 
ATOM   443  N NE  . ARG A 1 57  ? 30.004  4.527   -51.708 1.00 53.18 ?  57  ARG E NE  1 
ATOM   444  C CZ  . ARG A 1 57  ? 29.409  5.025   -52.784 1.00 53.21 ?  57  ARG E CZ  1 
ATOM   445  N NH1 . ARG A 1 57  ? 29.954  6.011   -53.478 1.00 54.20 ?  57  ARG E NH1 1 
ATOM   446  N NH2 . ARG A 1 57  ? 28.239  4.524   -53.172 1.00 55.70 ?  57  ARG E NH2 1 
ATOM   447  N N   . THR A 1 58  ? 31.474  2.657   -46.712 1.00 24.99 ?  58  THR E N   1 
ATOM   448  C CA  . THR A 1 58  ? 31.000  1.908   -45.558 1.00 23.07 ?  58  THR E CA  1 
ATOM   449  C C   . THR A 1 58  ? 29.479  1.969   -45.497 1.00 26.69 ?  58  THR E C   1 
ATOM   450  O O   . THR A 1 58  ? 28.857  2.953   -45.899 1.00 29.89 ?  58  THR E O   1 
ATOM   451  C CB  . THR A 1 58  ? 31.566  2.456   -44.240 1.00 28.67 ?  58  THR E CB  1 
ATOM   452  O OG1 . THR A 1 58  ? 31.262  3.856   -44.121 1.00 29.58 ?  58  THR E OG1 1 
ATOM   453  C CG2 . THR A 1 58  ? 33.074  2.283   -44.188 1.00 27.71 ?  58  THR E CG2 1 
ATOM   454  N N   . SER A 1 59  ? 28.885  0.910   -44.969 1.00 22.80 ?  59  SER E N   1 
ATOM   455  C CA  . SER A 1 59  ? 27.450  0.879   -44.727 1.00 20.65 ?  59  SER E CA  1 
ATOM   456  C C   . SER A 1 59  ? 27.295  0.261   -43.354 1.00 24.36 ?  59  SER E C   1 
ATOM   457  O O   . SER A 1 59  ? 27.863  -0.806  -43.102 1.00 22.05 ?  59  SER E O   1 
ATOM   458  C CB  . SER A 1 59  ? 26.734  0.076   -45.809 1.00 22.91 ?  59  SER E CB  1 
ATOM   459  O OG  . SER A 1 59  ? 25.330  -0.051  -45.529 1.00 23.85 ?  59  SER E OG  1 
ATOM   460  N N   . TYR A 1 60  ? 26.614  0.968   -42.457 1.00 20.83 ?  60  TYR E N   1 
ATOM   461  C CA  . TYR A 1 60  ? 26.358  0.513   -41.099 1.00 23.75 ?  60  TYR E CA  1 
ATOM   462  C C   . TYR A 1 60  ? 24.861  0.370   -40.879 1.00 27.36 ?  60  TYR E C   1 
ATOM   463  O O   . TYR A 1 60  ? 24.065  1.138   -41.427 1.00 24.52 ?  60  TYR E O   1 
ATOM   464  C CB  . TYR A 1 60  ? 26.892  1.494   -40.043 1.00 25.25 ?  60  TYR E CB  1 
ATOM   465  C CG  . TYR A 1 60  ? 28.345  1.942   -40.187 1.00 26.86 ?  60  TYR E CG  1 
ATOM   466  C CD1 . TYR A 1 60  ? 29.359  1.033   -40.462 1.00 26.04 ?  60  TYR E CD1 1 
ATOM   467  C CD2 . TYR A 1 60  ? 28.678  3.279   -40.113 1.00 29.08 ?  60  TYR E CD2 1 
ATOM   468  C CE1 . TYR A 1 60  ? 30.700  1.455   -40.605 1.00 27.24 ?  60  TYR E CE1 1 
ATOM   469  C CE2 . TYR A 1 60  ? 30.003  3.710   -40.255 1.00 32.54 ?  60  TYR E CE2 1 
ATOM   470  C CZ  . TYR A 1 60  ? 30.999  2.811   -40.497 1.00 27.27 ?  60  TYR E CZ  1 
ATOM   471  O OH  . TYR A 1 60  ? 32.299  3.264   -40.635 1.00 27.51 ?  60  TYR E OH  1 
ATOM   472  N N   . ALA A 1 61  ? 24.477  -0.605  -40.060 1.00 23.38 ?  61  ALA E N   1 
ATOM   473  C CA  . ALA A 1 61  ? 23.100  -0.637  -39.590 1.00 23.90 ?  61  ALA E CA  1 
ATOM   474  C C   . ALA A 1 61  ? 22.804  0.647   -38.817 1.00 25.50 ?  61  ALA E C   1 
ATOM   475  O O   . ALA A 1 61  ? 23.632  1.129   -38.039 1.00 23.50 ?  61  ALA E O   1 
ATOM   476  C CB  . ALA A 1 61  ? 22.857  -1.854  -38.699 1.00 25.06 ?  61  ALA E CB  1 
ATOM   477  N N   . GLN A 1 62  ? 21.621  1.219   -39.061 1.00 28.56 ?  62  GLN E N   1 
ATOM   478  C CA  . GLN A 1 62  ? 21.229  2.549   -38.505 1.00 30.43 ?  62  GLN E CA  1 
ATOM   479  C C   . GLN A 1 62  ? 21.543  2.693   -37.017 1.00 29.33 ?  62  GLN E C   1 
ATOM   480  O O   . GLN A 1 62  ? 21.992  3.769   -36.609 1.00 29.23 ?  62  GLN E O   1 
ATOM   481  C CB  . GLN A 1 62  ? 19.732  2.752   -38.765 1.00 32.25 ?  62  GLN E CB  1 
ATOM   482  C CG  . GLN A 1 62  ? 19.038  3.747   -37.843 1.00 35.33 ?  62  GLN E CG  1 
ATOM   483  C CD  . GLN A 1 62  ? 17.551  3.499   -37.749 1.00 41.71 ?  62  GLN E CD  1 
ATOM   484  O OE1 . GLN A 1 62  ? 16.787  3.804   -38.662 1.00 33.73 ?  62  GLN E OE1 1 
ATOM   485  N NE2 . GLN A 1 62  ? 17.128  2.933   -36.631 1.00 43.00 ?  62  GLN E NE2 1 
ATOM   486  N N   . ILE A 1 63  ? 21.312  1.639   -36.251 1.00 26.54 ?  63  ILE E N   1 
ATOM   487  C CA  . ILE A 1 63  ? 21.506  1.757   -34.814 1.00 30.53 ?  63  ILE E CA  1 
ATOM   488  C C   . ILE A 1 63  ? 22.959  2.052   -34.453 1.00 32.23 ?  63  ILE E C   1 
ATOM   489  O O   . ILE A 1 63  ? 23.243  2.526   -33.345 1.00 32.66 ?  63  ILE E O   1 
ATOM   490  C CB  . ILE A 1 63  ? 21.017  0.462   -34.151 1.00 35.13 ?  63  ILE E CB  1 
ATOM   491  C CG1 . ILE A 1 63  ? 21.119  0.535   -32.629 1.00 41.70 ?  63  ILE E CG1 1 
ATOM   492  C CG2 . ILE A 1 63  ? 21.836  -0.720  -34.662 1.00 30.94 ?  63  ILE E CG2 1 
ATOM   493  C CD1 . ILE A 1 63  ? 19.986  1.279   -31.975 1.00 40.39 ?  63  ILE E CD1 1 
ATOM   494  N N   . PHE A 1 64  ? 23.896  1.821   -35.367 1.00 29.14 ?  64  PHE E N   1 
ATOM   495  C CA  . PHE A 1 64  ? 25.300  2.054   -35.061 1.00 27.44 ?  64  PHE E CA  1 
ATOM   496  C C   . PHE A 1 64  ? 25.812  3.373   -35.621 1.00 30.79 ?  64  PHE E C   1 
ATOM   497  O O   . PHE A 1 64  ? 26.974  3.727   -35.381 1.00 32.30 ?  64  PHE E O   1 
ATOM   498  C CB  . PHE A 1 64  ? 26.141  0.900   -35.599 1.00 28.69 ?  64  PHE E CB  1 
ATOM   499  C CG  . PHE A 1 64  ? 25.824  -0.406  -34.951 1.00 28.36 ?  64  PHE E CG  1 
ATOM   500  C CD1 . PHE A 1 64  ? 26.005  -0.589  -33.596 1.00 31.01 ?  64  PHE E CD1 1 
ATOM   501  C CD2 . PHE A 1 64  ? 25.270  -1.431  -35.700 1.00 26.77 ?  64  PHE E CD2 1 
ATOM   502  C CE1 . PHE A 1 64  ? 25.682  -1.817  -33.010 1.00 34.69 ?  64  PHE E CE1 1 
ATOM   503  C CE2 . PHE A 1 64  ? 24.936  -2.636  -35.122 1.00 27.85 ?  64  PHE E CE2 1 
ATOM   504  C CZ  . PHE A 1 64  ? 25.145  -2.826  -33.776 1.00 32.71 ?  64  PHE E CZ  1 
ATOM   505  N N   . HIS A 1 65  ? 24.986  4.102   -36.361 1.00 29.63 ?  65  HIS E N   1 
ATOM   506  C CA  . HIS A 1 65  ? 25.427  5.375   -36.921 1.00 29.99 ?  65  HIS E CA  1 
ATOM   507  C C   . HIS A 1 65  ? 25.924  6.315   -35.824 1.00 31.88 ?  65  HIS E C   1 
ATOM   508  O O   . HIS A 1 65  ? 25.261  6.502   -34.798 1.00 31.62 ?  65  HIS E O   1 
ATOM   509  C CB  . HIS A 1 65  ? 24.281  6.016   -37.693 1.00 29.06 ?  65  HIS E CB  1 
ATOM   510  C CG  . HIS A 1 65  ? 24.014  5.381   -39.022 1.00 29.03 ?  65  HIS E CG  1 
ATOM   511  N ND1 . HIS A 1 65  ? 23.514  6.085   -40.096 1.00 25.29 ?  65  HIS E ND1 1 
ATOM   512  C CD2 . HIS A 1 65  ? 24.158  4.100   -39.444 1.00 29.61 ?  65  HIS E CD2 1 
ATOM   513  C CE1 . HIS A 1 65  ? 23.382  5.270   -41.131 1.00 28.40 ?  65  HIS E CE1 1 
ATOM   514  N NE2 . HIS A 1 65  ? 23.746  4.055   -40.757 1.00 30.03 ?  65  HIS E NE2 1 
ATOM   515  N N   . GLY A 1 66  ? 27.096  6.906   -36.046 1.00 30.53 ?  66  GLY E N   1 
ATOM   516  C CA  . GLY A 1 66  ? 27.683  7.824   -35.094 1.00 35.08 ?  66  GLY E CA  1 
ATOM   517  C C   . GLY A 1 66  ? 28.452  7.178   -33.963 1.00 38.32 ?  66  GLY E C   1 
ATOM   518  O O   . GLY A 1 66  ? 29.190  7.883   -33.259 1.00 39.36 ?  66  GLY E O   1 
ATOM   519  N N   . ARG A 1 67  ? 28.315  5.866   -33.765 1.00 31.92 ?  67  ARG E N   1 
ATOM   520  C CA  . ARG A 1 67  ? 29.012  5.156   -32.705 1.00 34.43 ?  67  ARG E CA  1 
ATOM   521  C C   . ARG A 1 67  ? 30.074  4.187   -33.203 1.00 31.96 ?  67  ARG E C   1 
ATOM   522  O O   . ARG A 1 67  ? 30.990  3.863   -32.448 1.00 36.17 ?  67  ARG E O   1 
ATOM   523  C CB  . ARG A 1 67  ? 28.017  4.371   -31.843 1.00 35.92 ?  67  ARG E CB  1 
ATOM   524  C CG  . ARG A 1 67  ? 27.312  5.193   -30.777 1.00 42.46 ?  67  ARG E CG  1 
ATOM   525  C CD  . ARG A 1 67  ? 27.209  4.419   -29.456 1.00 41.33 ?  67  ARG E CD  1 
ATOM   526  N NE  . ARG A 1 67  ? 26.507  3.150   -29.609 1.00 41.24 ?  67  ARG E NE  1 
ATOM   527  C CZ  . ARG A 1 67  ? 26.863  2.010   -29.026 1.00 42.65 ?  67  ARG E CZ  1 
ATOM   528  N NH1 . ARG A 1 67  ? 27.941  1.930   -28.258 1.00 37.52 ?  67  ARG E NH1 1 
ATOM   529  N NH2 . ARG A 1 67  ? 26.114  0.924   -29.210 1.00 40.73 ?  67  ARG E NH2 1 
ATOM   530  N N   . VAL A 1 68  ? 29.951  3.689   -34.429 1.00 31.54 ?  68  VAL E N   1 
ATOM   531  C CA  . VAL A 1 68  ? 30.871  2.708   -34.985 1.00 28.17 ?  68  VAL E CA  1 
ATOM   532  C C   . VAL A 1 68  ? 31.625  3.368   -36.121 1.00 28.32 ?  68  VAL E C   1 
ATOM   533  O O   . VAL A 1 68  ? 31.072  4.197   -36.852 1.00 29.44 ?  68  VAL E O   1 
ATOM   534  C CB  . VAL A 1 68  ? 30.139  1.447   -35.481 1.00 28.50 ?  68  VAL E CB  1 
ATOM   535  C CG1 . VAL A 1 68  ? 29.269  1.782   -36.694 1.00 30.68 ?  68  VAL E CG1 1 
ATOM   536  C CG2 . VAL A 1 68  ? 31.128  0.361   -35.844 1.00 30.43 ?  68  VAL E CG2 1 
ATOM   537  N N   . THR A 1 69  ? 32.905  3.020   -36.248 1.00 25.63 ?  69  THR E N   1 
ATOM   538  C CA  . THR A 1 69  ? 33.712  3.408   -37.393 1.00 23.15 ?  69  THR E CA  1 
ATOM   539  C C   . THR A 1 69  ? 34.449  2.172   -37.867 1.00 26.97 ?  69  THR E C   1 
ATOM   540  O O   . THR A 1 69  ? 35.171  1.550   -37.083 1.00 27.50 ?  69  THR E O   1 
ATOM   541  C CB  . THR A 1 69  ? 34.732  4.501   -37.041 1.00 29.77 ?  69  THR E CB  1 
ATOM   542  O OG1 . THR A 1 69  ? 34.032  5.626   -36.511 1.00 29.61 ?  69  THR E OG1 1 
ATOM   543  C CG2 . THR A 1 69  ? 35.500  4.910   -38.285 1.00 29.00 ?  69  THR E CG2 1 
ATOM   544  N N   . MET A 1 70  ? 34.294  1.830   -39.133 1.00 25.22 ?  70  MET E N   1 
ATOM   545  C CA  . MET A 1 70  ? 35.148  0.828   -39.745 1.00 26.14 ?  70  MET E CA  1 
ATOM   546  C C   . MET A 1 70  ? 36.201  1.486   -40.619 1.00 26.91 ?  70  MET E C   1 
ATOM   547  O O   . MET A 1 70  ? 35.927  2.459   -41.332 1.00 24.52 ?  70  MET E O   1 
ATOM   548  C CB  . MET A 1 70  ? 34.349  -0.189  -40.564 1.00 22.72 ?  70  MET E CB  1 
ATOM   549  C CG  . MET A 1 70  ? 33.267  -0.850  -39.737 1.00 23.72 ?  70  MET E CG  1 
ATOM   550  S SD  . MET A 1 70  ? 32.124  -1.784  -40.776 1.00 25.65 ?  70  MET E SD  1 
ATOM   551  C CE  . MET A 1 70  ? 31.197  -2.498  -39.430 1.00 25.26 ?  70  MET E CE  1 
ATOM   552  N N   . THR A 1 71  ? 37.413  0.951   -40.553 1.00 24.63 ?  71  THR E N   1 
ATOM   553  C CA  . THR A 1 71  ? 38.483  1.396   -41.426 1.00 25.98 ?  71  THR E CA  1 
ATOM   554  C C   . THR A 1 71  ? 39.191  0.172   -41.972 1.00 26.52 ?  71  THR E C   1 
ATOM   555  O O   . THR A 1 71  ? 39.112  -0.919  -41.399 1.00 24.70 ?  71  THR E O   1 
ATOM   556  C CB  . THR A 1 71  ? 39.500  2.273   -40.695 1.00 27.85 ?  71  THR E CB  1 
ATOM   557  O OG1 . THR A 1 71  ? 39.962  1.556   -39.552 1.00 27.72 ?  71  THR E OG1 1 
ATOM   558  C CG2 . THR A 1 71  ? 38.875  3.561   -40.239 1.00 30.92 ?  71  THR E CG2 1 
ATOM   559  N N   . THR A 1 72  ? 39.899  0.351   -43.085 1.00 25.18 ?  72  THR E N   1 
ATOM   560  C CA  . THR A 1 72  ? 40.793  -0.689  -43.563 1.00 27.95 ?  72  THR E CA  1 
ATOM   561  C C   . THR A 1 72  ? 42.152  -0.074  -43.832 1.00 30.98 ?  72  THR E C   1 
ATOM   562  O O   . THR A 1 72  ? 42.260  1.092   -44.231 1.00 29.29 ?  72  THR E O   1 
ATOM   563  C CB  . THR A 1 72  ? 40.267  -1.392  -44.814 1.00 32.41 ?  72  THR E CB  1 
ATOM   564  O OG1 . THR A 1 72  ? 39.843  -0.408  -45.764 1.00 38.61 ?  72  THR E OG1 1 
ATOM   565  C CG2 . THR A 1 72  ? 39.099  -2.300  -44.458 1.00 32.77 ?  72  THR E CG2 1 
ATOM   566  N N   . ASP A 1 73  ? 43.187  -0.843  -43.550 1.00 24.04 ?  73  ASP E N   1 
ATOM   567  C CA  . ASP A 1 73  ? 44.564  -0.424  -43.761 1.00 26.38 ?  73  ASP E CA  1 
ATOM   568  C C   . ASP A 1 73  ? 45.112  -1.370  -44.814 1.00 29.35 ?  73  ASP E C   1 
ATOM   569  O O   . ASP A 1 73  ? 45.531  -2.487  -44.496 1.00 25.23 ?  73  ASP E O   1 
ATOM   570  C CB  . ASP A 1 73  ? 45.355  -0.502  -42.472 1.00 28.01 ?  73  ASP E CB  1 
ATOM   571  C CG  . ASP A 1 73  ? 46.761  0.040   -42.616 1.00 34.35 ?  73  ASP E CG  1 
ATOM   572  O OD1 . ASP A 1 73  ? 47.266  0.093   -43.755 1.00 34.73 ?  73  ASP E OD1 1 
ATOM   573  O OD2 . ASP A 1 73  ? 47.378  0.359   -41.581 1.00 36.24 ?  73  ASP E OD2 1 
ATOM   574  N N   . THR A 1 74  ? 45.091  -0.938  -46.068 1.00 26.77 ?  74  THR E N   1 
ATOM   575  C CA  . THR A 1 74  ? 45.603  -1.775  -47.140 1.00 30.97 ?  74  THR E CA  1 
ATOM   576  C C   . THR A 1 74  ? 47.112  -1.971  -47.071 1.00 35.56 ?  74  THR E C   1 
ATOM   577  O O   . THR A 1 74  ? 47.629  -2.895  -47.713 1.00 35.89 ?  74  THR E O   1 
ATOM   578  C CB  . THR A 1 74  ? 45.195  -1.172  -48.482 1.00 37.01 ?  74  THR E CB  1 
ATOM   579  O OG1 . THR A 1 74  ? 45.674  0.185   -48.546 1.00 34.43 ?  74  THR E OG1 1 
ATOM   580  C CG2 . THR A 1 74  ? 43.692  -1.207  -48.651 1.00 36.56 ?  74  THR E CG2 1 
ATOM   581  N N   . SER A 1 75  ? 47.829  -1.160  -46.288 1.00 29.66 ?  75  SER E N   1 
ATOM   582  C CA  . SER A 1 75  ? 49.258  -1.406  -46.161 1.00 32.50 ?  75  SER E CA  1 
ATOM   583  C C   . SER A 1 75  ? 49.563  -2.562  -45.215 1.00 31.82 ?  75  SER E C   1 
ATOM   584  O O   . SER A 1 75  ? 50.608  -3.199  -45.363 1.00 28.18 ?  75  SER E O   1 
ATOM   585  C CB  . SER A 1 75  ? 49.996  -0.143  -45.703 1.00 31.26 ?  75  SER E CB  1 
ATOM   586  O OG  . SER A 1 75  ? 49.748  0.146   -44.334 1.00 32.16 ?  75  SER E OG  1 
ATOM   587  N N   . THR A 1 76  ? 48.699  -2.847  -44.238 1.00 30.59 ?  76  THR E N   1 
ATOM   588  C CA  . THR A 1 76  ? 48.880  -4.016  -43.375 1.00 27.85 ?  76  THR E CA  1 
ATOM   589  C C   . THR A 1 76  ? 47.846  -5.104  -43.618 1.00 25.07 ?  76  THR E C   1 
ATOM   590  O O   . THR A 1 76  ? 47.848  -6.107  -42.895 1.00 26.12 ?  76  THR E O   1 
ATOM   591  C CB  . THR A 1 76  ? 48.829  -3.628  -41.899 1.00 28.08 ?  76  THR E CB  1 
ATOM   592  O OG1 . THR A 1 76  ? 47.512  -3.156  -41.600 1.00 27.16 ?  76  THR E OG1 1 
ATOM   593  C CG2 . THR A 1 76  ? 49.831  -2.536  -41.590 1.00 29.59 ?  76  THR E CG2 1 
ATOM   594  N N   . ASN A 1 77  ? 46.975  -4.930  -44.606 1.00 27.09 ?  77  ASN E N   1 
ATOM   595  C CA  . ASN A 1 77  ? 45.892  -5.856  -44.913 1.00 29.59 ?  77  ASN E CA  1 
ATOM   596  C C   . ASN A 1 77  ? 45.126  -6.240  -43.651 1.00 26.86 ?  77  ASN E C   1 
ATOM   597  O O   . ASN A 1 77  ? 44.947  -7.418  -43.334 1.00 27.71 ?  77  ASN E O   1 
ATOM   598  C CB  . ASN A 1 77  ? 46.443  -7.077  -45.642 1.00 31.38 ?  77  ASN E CB  1 
ATOM   599  C CG  . ASN A 1 77  ? 47.049  -6.688  -46.961 1.00 35.08 ?  77  ASN E CG  1 
ATOM   600  O OD1 . ASN A 1 77  ? 46.331  -6.247  -47.850 1.00 36.33 ?  77  ASN E OD1 1 
ATOM   601  N ND2 . ASN A 1 77  ? 48.384  -6.821  -47.093 1.00 33.68 ?  77  ASN E ND2 1 
ATOM   602  N N   . THR A 1 78  ? 44.695  -5.204  -42.923 1.00 25.58 ?  78  THR E N   1 
ATOM   603  C CA  . THR A 1 78  ? 43.976  -5.322  -41.659 1.00 22.58 ?  78  THR E CA  1 
ATOM   604  C C   . THR A 1 78  ? 42.737  -4.443  -41.712 1.00 25.22 ?  78  THR E C   1 
ATOM   605  O O   . THR A 1 78  ? 42.811  -3.294  -42.171 1.00 23.87 ?  78  THR E O   1 
ATOM   606  C CB  . THR A 1 78  ? 44.841  -4.858  -40.487 1.00 24.65 ?  78  THR E CB  1 
ATOM   607  O OG1 . THR A 1 78  ? 46.112  -5.518  -40.543 1.00 27.95 ?  78  THR E OG1 1 
ATOM   608  C CG2 . THR A 1 78  ? 44.155  -5.184  -39.162 1.00 26.40 ?  78  THR E CG2 1 
ATOM   609  N N   . ALA A 1 79  ? 41.610  -4.968  -41.223 1.00 24.42 ?  79  ALA E N   1 
ATOM   610  C CA  . ALA A 1 79  ? 40.398  -4.173  -41.052 1.00 20.84 ?  79  ALA E CA  1 
ATOM   611  C C   . ALA A 1 79  ? 40.185  -3.907  -39.567 1.00 22.29 ?  79  ALA E C   1 
ATOM   612  O O   . ALA A 1 79  ? 40.579  -4.717  -38.723 1.00 22.85 ?  79  ALA E O   1 
ATOM   613  C CB  . ALA A 1 79  ? 39.178  -4.892  -41.645 1.00 23.63 ?  79  ALA E CB  1 
ATOM   614  N N   . TYR A 1 80  ? 39.579  -2.750  -39.244 1.00 20.88 ?  80  TYR E N   1 
ATOM   615  C CA  . TYR A 1 80  ? 39.306  -2.385  -37.855 1.00 22.80 ?  80  TYR E CA  1 
ATOM   616  C C   . TYR A 1 80  ? 37.859  -1.965  -37.685 1.00 21.89 ?  80  TYR E C   1 
ATOM   617  O O   . TYR A 1 80  ? 37.268  -1.375  -38.590 1.00 22.98 ?  80  TYR E O   1 
ATOM   618  C CB  . TYR A 1 80  ? 40.173  -1.228  -37.364 1.00 22.59 ?  80  TYR E CB  1 
ATOM   619  C CG  . TYR A 1 80  ? 41.653  -1.496  -37.499 1.00 22.95 ?  80  TYR E CG  1 
ATOM   620  C CD1 . TYR A 1 80  ? 42.357  -2.102  -36.470 1.00 25.76 ?  80  TYR E CD1 1 
ATOM   621  C CD2 . TYR A 1 80  ? 42.335  -1.139  -38.651 1.00 25.72 ?  80  TYR E CD2 1 
ATOM   622  C CE1 . TYR A 1 80  ? 43.726  -2.338  -36.579 1.00 25.39 ?  80  TYR E CE1 1 
ATOM   623  C CE2 . TYR A 1 80  ? 43.702  -1.379  -38.778 1.00 25.26 ?  80  TYR E CE2 1 
ATOM   624  C CZ  . TYR A 1 80  ? 44.386  -1.972  -37.739 1.00 27.04 ?  80  TYR E CZ  1 
ATOM   625  O OH  . TYR A 1 80  ? 45.739  -2.208  -37.860 1.00 28.60 ?  80  TYR E OH  1 
ATOM   626  N N   . MET A 1 81  ? 37.287  -2.312  -36.534 1.00 23.68 ?  81  MET E N   1 
ATOM   627  C CA  . MET A 1 81  ? 35.999  -1.787  -36.106 1.00 23.15 ?  81  MET E CA  1 
ATOM   628  C C   . MET A 1 81  ? 36.229  -1.097  -34.774 1.00 27.80 ?  81  MET E C   1 
ATOM   629  O O   . MET A 1 81  ? 36.743  -1.719  -33.836 1.00 25.74 ?  81  MET E O   1 
ATOM   630  C CB  . MET A 1 81  ? 34.947  -2.897  -35.968 1.00 21.54 ?  81  MET E CB  1 
ATOM   631  C CG  . MET A 1 81  ? 33.592  -2.384  -35.433 1.00 28.65 ?  81  MET E CG  1 
ATOM   632  S SD  . MET A 1 81  ? 32.658  -3.755  -34.729 1.00 40.19 ?  81  MET E SD  1 
ATOM   633  C CE  . MET A 1 81  ? 33.445  -3.868  -33.109 1.00 34.45 ?  81  MET E CE  1 
ATOM   634  N N   . GLU A 1 82  ? 35.892  0.191   -34.703 1.00 23.72 ?  82  GLU E N   1 
ATOM   635  C CA  . GLU A 1 82  ? 35.897  0.934   -33.447 1.00 25.97 ?  82  GLU E CA  1 
ATOM   636  C C   . GLU A 1 82  ? 34.469  1.199   -32.997 1.00 28.03 ?  82  GLU E C   1 
ATOM   637  O O   . GLU A 1 82  ? 33.635  1.617   -33.799 1.00 26.43 ?  82  GLU E O   1 
ATOM   638  C CB  . GLU A 1 82  ? 36.636  2.262   -33.584 1.00 31.77 ?  82  GLU E CB  1 
ATOM   639  C CG  . GLU A 1 82  ? 36.773  2.968   -32.254 1.00 32.32 ?  82  GLU E CG  1 
ATOM   640  C CD  . GLU A 1 82  ? 37.367  4.345   -32.401 1.00 43.28 ?  82  GLU E CD  1 
ATOM   641  O OE1 . GLU A 1 82  ? 38.615  4.418   -32.450 1.00 50.53 ?  82  GLU E OE1 1 
ATOM   642  O OE2 . GLU A 1 82  ? 36.596  5.336   -32.458 1.00 46.67 ?  82  GLU E OE2 1 
ATOM   643  N N   . LEU A 1 83  ? 34.186  0.942   -31.726 1.00 26.18 ?  83  LEU E N   1 
ATOM   644  C CA  . LEU A 1 83  ? 32.868  1.199   -31.161 1.00 28.79 ?  83  LEU E CA  1 
ATOM   645  C C   . LEU A 1 83  ? 33.055  2.148   -29.987 1.00 32.71 ?  83  LEU E C   1 
ATOM   646  O O   . LEU A 1 83  ? 33.816  1.846   -29.061 1.00 30.08 ?  83  LEU E O   1 
ATOM   647  C CB  . LEU A 1 83  ? 32.195  -0.101  -30.698 1.00 32.18 ?  83  LEU E CB  1 
ATOM   648  C CG  . LEU A 1 83  ? 30.695  -0.028  -30.355 1.00 32.86 ?  83  LEU E CG  1 
ATOM   649  C CD1 . LEU A 1 83  ? 29.881  0.802   -31.365 1.00 34.94 ?  83  LEU E CD1 1 
ATOM   650  C CD2 . LEU A 1 83  ? 30.068  -1.418  -30.136 1.00 32.77 ?  83  LEU E CD2 1 
ATOM   651  N N   . ARG A 1 84  ? 32.365  3.289   -30.020 1.00 31.10 ?  84  ARG E N   1 
ATOM   652  C CA  . ARG A 1 84  ? 32.546  4.320   -29.010 1.00 34.36 ?  84  ARG E CA  1 
ATOM   653  C C   . ARG A 1 84  ? 31.357  4.328   -28.058 1.00 34.92 ?  84  ARG E C   1 
ATOM   654  O O   . ARG A 1 84  ? 30.304  3.746   -28.342 1.00 36.31 ?  84  ARG E O   1 
ATOM   655  C CB  . ARG A 1 84  ? 32.711  5.694   -29.669 1.00 36.50 ?  84  ARG E CB  1 
ATOM   656  C CG  . ARG A 1 84  ? 33.829  5.733   -30.695 1.00 39.90 ?  84  ARG E CG  1 
ATOM   657  C CD  . ARG A 1 84  ? 34.044  7.144   -31.279 1.00 46.52 ?  84  ARG E CD  1 
ATOM   658  N NE  . ARG A 1 84  ? 33.070  7.486   -32.317 1.00 46.02 ?  84  ARG E NE  1 
ATOM   659  C CZ  . ARG A 1 84  ? 32.904  6.814   -33.451 1.00 45.14 ?  84  ARG E CZ  1 
ATOM   660  N NH1 . ARG A 1 84  ? 33.661  5.766   -33.758 1.00 38.08 ?  84  ARG E NH1 1 
ATOM   661  N NH2 . ARG A 1 84  ? 31.962  7.207   -34.303 1.00 42.33 ?  84  ARG E NH2 1 
ATOM   662  N N   . SER A 1 85  ? 31.547  4.989   -26.914 1.00 34.32 ?  85  SER E N   1 
ATOM   663  C CA  . SER A 1 85  ? 30.478  5.226   -25.942 1.00 35.85 ?  85  SER E CA  1 
ATOM   664  C C   . SER A 1 85  ? 29.832  3.909   -25.527 1.00 35.36 ?  85  SER E C   1 
ATOM   665  O O   . SER A 1 85  ? 28.617  3.714   -25.622 1.00 34.51 ?  85  SER E O   1 
ATOM   666  C CB  . SER A 1 85  ? 29.429  6.188   -26.510 1.00 39.72 ?  85  SER E CB  1 
ATOM   667  O OG  . SER A 1 85  ? 30.034  7.399   -26.912 1.00 43.29 ?  85  SER E OG  1 
ATOM   668  N N   . LEU A 1 86  ? 30.683  2.961   -25.128 1.00 34.79 ?  86  LEU E N   1 
ATOM   669  C CA  . LEU A 1 86  ? 30.196  1.586   -24.837 1.00 34.23 ?  86  LEU E CA  1 
ATOM   670  C C   . LEU A 1 86  ? 29.150  1.553   -23.722 1.00 37.75 ?  86  LEU E C   1 
ATOM   671  O O   . LEU A 1 86  ? 29.282  2.327   -22.757 1.00 37.42 ?  86  LEU E O   1 
ATOM   672  C CB  . LEU A 1 86  ? 31.404  0.716   -24.474 1.00 32.93 ?  86  LEU E CB  1 
ATOM   673  C CG  . LEU A 1 86  ? 32.325  0.366   -25.641 1.00 31.09 ?  86  LEU E CG  1 
ATOM   674  C CD1 . LEU A 1 86  ? 33.469  -0.521  -25.178 1.00 34.15 ?  86  LEU E CD1 1 
ATOM   675  C CD2 . LEU A 1 86  ? 31.545  -0.313  -26.753 1.00 32.41 ?  86  LEU E CD2 1 
ATOM   676  N N   . ARG A 1 87  ? 28.162  0.667   -23.862 1.00 36.80 ?  87  ARG E N   1 
ATOM   677  C CA  . ARG A 1 87  ? 27.136  0.478   -22.806 1.00 40.48 ?  87  ARG E CA  1 
ATOM   678  C C   . ARG A 1 87  ? 27.066  -1.023  -22.509 1.00 42.59 ?  87  ARG E C   1 
ATOM   679  O O   . ARG A 1 87  ? 27.507  -1.808  -23.366 1.00 35.95 ?  87  ARG E O   1 
ATOM   680  C CB  . ARG A 1 87  ? 25.794  1.059   -23.260 1.00 43.15 ?  87  ARG E CB  1 
ATOM   681  C CG  . ARG A 1 87  ? 25.570  1.002   -24.764 1.00 45.11 ?  87  ARG E CG  1 
ATOM   682  C CD  . ARG A 1 87  ? 24.298  1.696   -25.207 1.00 50.03 ?  87  ARG E CD  1 
ATOM   683  N NE  . ARG A 1 87  ? 23.102  1.038   -24.698 1.00 56.71 ?  87  ARG E NE  1 
ATOM   684  C CZ  . ARG A 1 87  ? 21.863  1.453   -24.929 1.00 56.50 ?  87  ARG E CZ  1 
ATOM   685  N NH1 . ARG A 1 87  ? 21.654  2.612   -25.527 1.00 56.68 ?  87  ARG E NH1 1 
ATOM   686  N NH2 . ARG A 1 87  ? 20.835  0.710   -24.555 1.00 60.21 ?  87  ARG E NH2 1 
ATOM   687  N N   . SER A 1 88  ? 26.560  -1.405  -21.336 1.00 41.96 ?  88  SER E N   1 
ATOM   688  C CA  . SER A 1 88  ? 26.535  -2.838  -20.940 1.00 40.37 ?  88  SER E CA  1 
ATOM   689  C C   . SER A 1 88  ? 26.009  -3.714  -22.083 1.00 39.89 ?  88  SER E C   1 
ATOM   690  O O   . SER A 1 88  ? 26.563  -4.810  -22.278 1.00 38.90 ?  88  SER E O   1 
ATOM   691  C CB  . SER A 1 88  ? 25.717  -3.030  -19.691 1.00 44.34 ?  88  SER E CB  1 
ATOM   692  O OG  . SER A 1 88  ? 24.389  -2.566  -19.882 1.00 51.75 ?  88  SER E OG  1 
ATOM   693  N N   . ASP A 1 89  ? 24.983  -3.257  -22.805 1.00 37.78 ?  89  ASP E N   1 
ATOM   694  C CA  . ASP A 1 89  ? 24.388  -4.097  -23.835 1.00 35.94 ?  89  ASP E CA  1 
ATOM   695  C C   . ASP A 1 89  ? 25.191  -4.104  -25.143 1.00 37.10 ?  89  ASP E C   1 
ATOM   696  O O   . ASP A 1 89  ? 24.758  -4.722  -26.122 1.00 35.88 ?  89  ASP E O   1 
ATOM   697  C CB  . ASP A 1 89  ? 22.920  -3.700  -24.073 1.00 42.46 ?  89  ASP E CB  1 
ATOM   698  C CG  . ASP A 1 89  ? 22.763  -2.351  -24.739 1.00 49.53 ?  89  ASP E CG  1 
ATOM   699  O OD1 . ASP A 1 89  ? 23.765  -1.635  -24.903 1.00 48.92 ?  89  ASP E OD1 1 
ATOM   700  O OD2 . ASP A 1 89  ? 21.618  -1.996  -25.096 1.00 54.67 ?  89  ASP E OD2 1 
ATOM   701  N N   . ASP A 1 90  ? 26.364  -3.468  -25.166 1.00 35.02 ?  90  ASP E N   1 
ATOM   702  C CA  . ASP A 1 90  ? 27.326  -3.698  -26.237 1.00 34.01 ?  90  ASP E CA  1 
ATOM   703  C C   . ASP A 1 90  ? 28.159  -4.957  -26.008 1.00 29.40 ?  90  ASP E C   1 
ATOM   704  O O   . ASP A 1 90  ? 28.941  -5.330  -26.890 1.00 29.16 ?  90  ASP E O   1 
ATOM   705  C CB  . ASP A 1 90  ? 28.241  -2.481  -26.383 1.00 33.24 ?  90  ASP E CB  1 
ATOM   706  C CG  . ASP A 1 90  ? 27.527  -1.291  -27.009 1.00 37.87 ?  90  ASP E CG  1 
ATOM   707  O OD1 . ASP A 1 90  ? 26.697  -1.500  -27.927 1.00 36.11 ?  90  ASP E OD1 1 
ATOM   708  O OD2 . ASP A 1 90  ? 27.787  -0.154  -26.566 1.00 38.60 ?  90  ASP E OD2 1 
ATOM   709  N N   . THR A 1 91  ? 28.005  -5.612  -24.852 1.00 29.50 ?  91  THR E N   1 
ATOM   710  C CA  . THR A 1 91  ? 28.687  -6.868  -24.583 1.00 30.60 ?  91  THR E CA  1 
ATOM   711  C C   . THR A 1 91  ? 28.259  -7.888  -25.616 1.00 31.63 ?  91  THR E C   1 
ATOM   712  O O   . THR A 1 91  ? 27.064  -8.186  -25.736 1.00 27.44 ?  91  THR E O   1 
ATOM   713  C CB  . THR A 1 91  ? 28.349  -7.388  -23.185 1.00 32.73 ?  91  THR E CB  1 
ATOM   714  O OG1 . THR A 1 91  ? 28.863  -6.491  -22.196 1.00 32.37 ?  91  THR E OG1 1 
ATOM   715  C CG2 . THR A 1 91  ? 28.937  -8.785  -22.979 1.00 30.17 ?  91  THR E CG2 1 
ATOM   716  N N   . ALA A 1 92  ? 29.227  -8.418  -26.360 1.00 27.10 ?  92  ALA E N   1 
ATOM   717  C CA  . ALA A 1 92  ? 28.900  -9.333  -27.443 1.00 26.85 ?  92  ALA E CA  1 
ATOM   718  C C   . ALA A 1 92  ? 30.177  -9.934  -27.998 1.00 29.29 ?  92  ALA E C   1 
ATOM   719  O O   . ALA A 1 92  ? 31.280  -9.411  -27.783 1.00 26.35 ?  92  ALA E O   1 
ATOM   720  C CB  . ALA A 1 92  ? 28.144  -8.626  -28.564 1.00 27.22 ?  92  ALA E CB  1 
ATOM   721  N N   . MET A 1 93  ? 30.006  -11.046 -28.718 1.00 23.76 ?  93  MET E N   1 
ATOM   722  C CA  . MET A 1 93  ? 31.039  -11.528 -29.625 1.00 24.79 ?  93  MET E CA  1 
ATOM   723  C C   . MET A 1 93  ? 30.965  -10.755 -30.930 1.00 27.11 ?  93  MET E C   1 
ATOM   724  O O   . MET A 1 93  ? 29.892  -10.637 -31.535 1.00 28.15 ?  93  MET E O   1 
ATOM   725  C CB  . MET A 1 93  ? 30.877  -13.020 -29.901 1.00 25.88 ?  93  MET E CB  1 
ATOM   726  C CG  . MET A 1 93  ? 32.080  -13.593 -30.615 1.00 29.52 ?  93  MET E CG  1 
ATOM   727  S SD  . MET A 1 93  ? 33.531  -13.830 -29.551 1.00 31.21 ?  93  MET E SD  1 
ATOM   728  C CE  . MET A 1 93  ? 33.015  -15.225 -28.555 1.00 38.06 ?  93  MET E CE  1 
ATOM   729  N N   . TYR A 1 94  ? 32.094  -10.217 -31.360 1.00 23.14 ?  94  TYR E N   1 
ATOM   730  C CA  . TYR A 1 94  ? 32.176  -9.452  -32.596 1.00 24.65 ?  94  TYR E CA  1 
ATOM   731  C C   . TYR A 1 94  ? 32.964  -10.272 -33.606 1.00 23.72 ?  94  TYR E C   1 
ATOM   732  O O   . TYR A 1 94  ? 34.095  -10.680 -33.323 1.00 23.73 ?  94  TYR E O   1 
ATOM   733  C CB  . TYR A 1 94  ? 32.834  -8.090  -32.350 1.00 24.35 ?  94  TYR E CB  1 
ATOM   734  C CG  . TYR A 1 94  ? 31.925  -7.168  -31.573 1.00 29.10 ?  94  TYR E CG  1 
ATOM   735  C CD1 . TYR A 1 94  ? 31.766  -7.311  -30.201 1.00 26.98 ?  94  TYR E CD1 1 
ATOM   736  C CD2 . TYR A 1 94  ? 31.194  -6.188  -32.220 1.00 28.53 ?  94  TYR E CD2 1 
ATOM   737  C CE1 . TYR A 1 94  ? 30.918  -6.468  -29.488 1.00 26.05 ?  94  TYR E CE1 1 
ATOM   738  C CE2 . TYR A 1 94  ? 30.335  -5.335  -31.512 1.00 29.40 ?  94  TYR E CE2 1 
ATOM   739  C CZ  . TYR A 1 94  ? 30.202  -5.491  -30.152 1.00 28.64 ?  94  TYR E CZ  1 
ATOM   740  O OH  . TYR A 1 94  ? 29.340  -4.677  -29.441 1.00 29.70 ?  94  TYR E OH  1 
ATOM   741  N N   . TYR A 1 95  ? 32.359  -10.540 -34.764 1.00 21.39 ?  95  TYR E N   1 
ATOM   742  C CA  . TYR A 1 95  ? 33.015  -11.302 -35.827 1.00 22.34 ?  95  TYR E CA  1 
ATOM   743  C C   . TYR A 1 95  ? 33.328  -10.404 -37.004 1.00 20.57 ?  95  TYR E C   1 
ATOM   744  O O   . TYR A 1 95  ? 32.499  -9.581  -37.388 1.00 22.29 ?  95  TYR E O   1 
ATOM   745  C CB  . TYR A 1 95  ? 32.124  -12.429 -36.349 1.00 20.20 ?  95  TYR E CB  1 
ATOM   746  C CG  . TYR A 1 95  ? 31.846  -13.511 -35.354 1.00 21.55 ?  95  TYR E CG  1 
ATOM   747  C CD1 . TYR A 1 95  ? 32.761  -14.527 -35.156 1.00 23.02 ?  95  TYR E CD1 1 
ATOM   748  C CD2 . TYR A 1 95  ? 30.665  -13.514 -34.608 1.00 24.19 ?  95  TYR E CD2 1 
ATOM   749  C CE1 . TYR A 1 95  ? 32.510  -15.549 -34.250 1.00 23.81 ?  95  TYR E CE1 1 
ATOM   750  C CE2 . TYR A 1 95  ? 30.407  -14.539 -33.693 1.00 26.57 ?  95  TYR E CE2 1 
ATOM   751  C CZ  . TYR A 1 95  ? 31.339  -15.545 -33.524 1.00 26.11 ?  95  TYR E CZ  1 
ATOM   752  O OH  . TYR A 1 95  ? 31.115  -16.569 -32.629 1.00 28.64 ?  95  TYR E OH  1 
ATOM   753  N N   . CYS A 1 96  ? 34.489  -10.613 -37.634 1.00 20.36 ?  96  CYS E N   1 
ATOM   754  C CA  . CYS A 1 96  ? 34.664  -10.100 -38.982 1.00 20.53 ?  96  CYS E CA  1 
ATOM   755  C C   . CYS A 1 96  ? 34.448  -11.243 -39.966 1.00 23.02 ?  96  CYS E C   1 
ATOM   756  O O   . CYS A 1 96  ? 34.631  -12.414 -39.630 1.00 23.43 ?  96  CYS E O   1 
ATOM   757  C CB  . CYS A 1 96  ? 36.039  -9.453  -39.178 1.00 22.53 ?  96  CYS E CB  1 
ATOM   758  S SG  . CYS A 1 96  ? 37.428  -10.607 -39.089 1.00 24.44 ?  96  CYS E SG  1 
ATOM   759  N N   . ALA A 1 97  ? 34.042  -10.897 -41.183 1.00 20.65 ?  97  ALA E N   1 
ATOM   760  C CA  . ALA A 1 97  ? 33.800  -11.901 -42.214 1.00 19.04 ?  97  ALA E CA  1 
ATOM   761  C C   . ALA A 1 97  ? 34.043  -11.262 -43.571 1.00 22.51 ?  97  ALA E C   1 
ATOM   762  O O   . ALA A 1 97  ? 33.981  -10.038 -43.721 1.00 23.05 ?  97  ALA E O   1 
ATOM   763  C CB  . ALA A 1 97  ? 32.371  -12.458 -42.134 1.00 22.60 ?  97  ALA E CB  1 
ATOM   764  N N   . ARG A 1 98  ? 34.282  -12.098 -44.573 1.00 21.46 ?  98  ARG E N   1 
ATOM   765  C CA  . ARG A 1 98  ? 34.622  -11.616 -45.906 1.00 21.11 ?  98  ARG E CA  1 
ATOM   766  C C   . ARG A 1 98  ? 33.389  -11.610 -46.802 1.00 22.97 ?  98  ARG E C   1 
ATOM   767  O O   . ARG A 1 98  ? 32.762  -12.649 -47.007 1.00 21.88 ?  98  ARG E O   1 
ATOM   768  C CB  . ARG A 1 98  ? 35.714  -12.477 -46.532 1.00 19.72 ?  98  ARG E CB  1 
ATOM   769  C CG  . ARG A 1 98  ? 36.236  -11.883 -47.830 1.00 24.08 ?  98  ARG E CG  1 
ATOM   770  C CD  . ARG A 1 98  ? 37.304  -12.755 -48.439 1.00 22.74 ?  98  ARG E CD  1 
ATOM   771  N NE  . ARG A 1 98  ? 36.712  -13.850 -49.203 1.00 23.89 ?  98  ARG E NE  1 
ATOM   772  C CZ  . ARG A 1 98  ? 37.362  -14.534 -50.134 1.00 24.70 ?  98  ARG E CZ  1 
ATOM   773  N NH1 . ARG A 1 98  ? 38.620  -14.248 -50.439 1.00 25.33 ?  98  ARG E NH1 1 
ATOM   774  N NH2 . ARG A 1 98  ? 36.743  -15.537 -50.760 1.00 20.73 ?  98  ARG E NH2 1 
ATOM   775  N N   . ASN A 1 99  ? 33.045  -10.445 -47.344 1.00 22.81 ?  99  ASN E N   1 
ATOM   776  C CA  . ASN A 1 99  ? 32.015  -10.351 -48.371 1.00 20.98 ?  99  ASN E CA  1 
ATOM   777  C C   . ASN A 1 99  ? 32.603  -9.670  -49.604 1.00 22.48 ?  99  ASN E C   1 
ATOM   778  O O   . ASN A 1 99  ? 33.788  -9.327  -49.636 1.00 21.09 ?  99  ASN E O   1 
ATOM   779  C CB  . ASN A 1 99  ? 30.771  -9.606  -47.835 1.00 21.07 ?  99  ASN E CB  1 
ATOM   780  C CG  . ASN A 1 99  ? 30.979  -8.118  -47.702 1.00 22.70 ?  99  ASN E CG  1 
ATOM   781  O OD1 . ASN A 1 99  ? 32.018  -7.654  -47.209 1.00 22.85 ?  99  ASN E OD1 1 
ATOM   782  N ND2 . ASN A 1 99  ? 29.928  -7.345  -48.022 1.00 24.00 ?  99  ASN E ND2 1 
ATOM   783  N N   . HIS A 1 100 ? 31.776  -9.520  -50.639 1.00 22.14 ?  100 HIS E N   1 
ATOM   784  C CA  . HIS A 1 100 ? 32.197  -8.842  -51.861 1.00 21.68 ?  100 HIS E CA  1 
ATOM   785  C C   . HIS A 1 100 ? 30.947  -8.445  -52.629 1.00 24.77 ?  100 HIS E C   1 
ATOM   786  O O   . HIS A 1 100 ? 29.847  -8.901  -52.322 1.00 21.02 ?  100 HIS E O   1 
ATOM   787  C CB  . HIS A 1 100 ? 33.106  -9.717  -52.725 1.00 22.09 ?  100 HIS E CB  1 
ATOM   788  C CG  . HIS A 1 100 ? 32.462  -10.962 -53.255 1.00 24.65 ?  100 HIS E CG  1 
ATOM   789  N ND1 . HIS A 1 100 ? 32.355  -12.126 -52.521 1.00 24.90 ?  100 HIS E ND1 1 
ATOM   790  C CD2 . HIS A 1 100 ? 31.925  -11.232 -54.468 1.00 24.17 ?  100 HIS E CD2 1 
ATOM   791  C CE1 . HIS A 1 100 ? 31.781  -13.060 -53.260 1.00 24.81 ?  100 HIS E CE1 1 
ATOM   792  N NE2 . HIS A 1 100 ? 31.499  -12.540 -54.442 1.00 25.35 ?  100 HIS E NE2 1 
ATOM   793  N N   . CYS A 1 101 ? 31.157  -7.620  -53.657 1.00 24.23 ?  101 CYS E N   1 
ATOM   794  C CA  . CYS A 1 101 ? 30.047  -7.273  -54.574 1.00 22.86 ?  101 CYS E CA  1 
ATOM   795  C C   . CYS A 1 101 ? 30.408  -7.871  -55.935 1.00 28.60 ?  101 CYS E C   1 
ATOM   796  O O   . CYS A 1 101 ? 31.476  -7.519  -56.462 1.00 28.73 ?  101 CYS E O   1 
ATOM   797  C CB  . CYS A 1 101 ? 29.876  -5.767  -54.720 1.00 28.98 ?  101 CYS E CB  1 
ATOM   798  S SG  . CYS A 1 101 ? 28.464  -5.315  -55.763 1.00 43.12 ?  101 CYS E SG  1 
ATOM   799  N N   . ASN A 1 102 ? 29.589  -8.787  -56.442 1.00 26.71 ?  102 ASN E N   1 
ATOM   800  C CA  . ASN A 1 102 ? 29.816  -9.381  -57.752 1.00 27.69 ?  102 ASN E CA  1 
ATOM   801  C C   . ASN A 1 102 ? 29.404  -8.357  -58.801 1.00 31.03 ?  102 ASN E C   1 
ATOM   802  O O   . ASN A 1 102 ? 28.213  -8.069  -58.966 1.00 30.08 ?  102 ASN E O   1 
ATOM   803  C CB  . ASN A 1 102 ? 29.028  -10.676 -57.902 1.00 27.36 ?  102 ASN E CB  1 
ATOM   804  C CG  . ASN A 1 102 ? 29.319  -11.374 -59.207 1.00 31.99 ?  102 ASN E CG  1 
ATOM   805  O OD1 . ASN A 1 102 ? 29.095  -10.820 -60.290 1.00 31.88 ?  102 ASN E OD1 1 
ATOM   806  N ND2 . ASN A 1 102 ? 29.830  -12.601 -59.120 1.00 28.28 ?  102 ASN E ND2 1 
ATOM   807  N N   . PHE A 1 103 ? 30.383  -7.821  -59.526 1.00 29.93 ?  103 PHE E N   1 
ATOM   808  C CA  . PHE A 1 103 ? 30.095  -6.727  -60.442 1.00 30.91 ?  103 PHE E CA  1 
ATOM   809  C C   . PHE A 1 103 ? 29.536  -7.224  -61.767 1.00 33.44 ?  103 PHE E C   1 
ATOM   810  O O   . PHE A 1 103 ? 28.768  -6.499  -62.407 1.00 41.47 ?  103 PHE E O   1 
ATOM   811  C CB  . PHE A 1 103 ? 31.361  -5.906  -60.675 1.00 29.95 ?  103 PHE E CB  1 
ATOM   812  C CG  . PHE A 1 103 ? 31.674  -4.971  -59.553 1.00 29.95 ?  103 PHE E CG  1 
ATOM   813  C CD1 . PHE A 1 103 ? 32.447  -5.403  -58.485 1.00 28.81 ?  103 PHE E CD1 1 
ATOM   814  C CD2 . PHE A 1 103 ? 31.232  -3.653  -59.571 1.00 31.74 ?  103 PHE E CD2 1 
ATOM   815  C CE1 . PHE A 1 103 ? 32.747  -4.554  -57.442 1.00 32.81 ?  103 PHE E CE1 1 
ATOM   816  C CE2 . PHE A 1 103 ? 31.540  -2.794  -58.536 1.00 33.00 ?  103 PHE E CE2 1 
ATOM   817  C CZ  . PHE A 1 103 ? 32.302  -3.243  -57.469 1.00 34.33 ?  103 PHE E CZ  1 
ATOM   818  N N   . TYR A 1 104 ? 29.904  -8.434  -62.195 1.00 36.25 ?  104 TYR E N   1 
ATOM   819  C CA  . TYR A 1 104 ? 29.315  -9.020  -63.395 1.00 40.25 ?  104 TYR E CA  1 
ATOM   820  C C   . TYR A 1 104 ? 27.795  -9.070  -63.290 1.00 41.65 ?  104 TYR E C   1 
ATOM   821  O O   . TYR A 1 104 ? 27.078  -8.534  -64.143 1.00 40.78 ?  104 TYR E O   1 
ATOM   822  C CB  . TYR A 1 104 ? 29.858  -10.436 -63.631 1.00 42.95 ?  104 TYR E CB  1 
ATOM   823  C CG  . TYR A 1 104 ? 31.311  -10.551 -64.053 1.00 52.26 ?  104 TYR E CG  1 
ATOM   824  C CD1 . TYR A 1 104 ? 31.679  -10.431 -65.392 1.00 56.62 ?  104 TYR E CD1 1 
ATOM   825  C CD2 . TYR A 1 104 ? 32.312  -10.822 -63.123 1.00 51.17 ?  104 TYR E CD2 1 
ATOM   826  C CE1 . TYR A 1 104 ? 33.010  -10.553 -65.790 1.00 56.58 ?  104 TYR E CE1 1 
ATOM   827  C CE2 . TYR A 1 104 ? 33.643  -10.946 -63.512 1.00 51.90 ?  104 TYR E CE2 1 
ATOM   828  C CZ  . TYR A 1 104 ? 33.985  -10.810 -64.849 1.00 57.95 ?  104 TYR E CZ  1 
ATOM   829  O OH  . TYR A 1 104 ? 35.304  -10.929 -65.241 1.00 59.61 ?  104 TYR E OH  1 
ATOM   830  N N   . HIS A 1 105 ? 27.290  -9.717  -62.239 1.00 37.08 ?  105 HIS E N   1 
ATOM   831  C CA  . HIS A 1 105 ? 25.872  -9.992  -62.057 1.00 36.29 ?  105 HIS E CA  1 
ATOM   832  C C   . HIS A 1 105 ? 25.191  -9.046  -61.081 1.00 37.30 ?  105 HIS E C   1 
ATOM   833  O O   . HIS A 1 105 ? 23.990  -9.199  -60.828 1.00 37.20 ?  105 HIS E O   1 
ATOM   834  C CB  . HIS A 1 105 ? 25.687  -11.434 -61.588 1.00 35.89 ?  105 HIS E CB  1 
ATOM   835  C CG  . HIS A 1 105 ? 26.352  -12.436 -62.471 1.00 39.99 ?  105 HIS E CG  1 
ATOM   836  N ND1 . HIS A 1 105 ? 25.883  -12.742 -63.730 1.00 43.46 ?  105 HIS E ND1 1 
ATOM   837  C CD2 . HIS A 1 105 ? 27.455  -13.199 -62.284 1.00 41.35 ?  105 HIS E CD2 1 
ATOM   838  C CE1 . HIS A 1 105 ? 26.664  -13.656 -64.279 1.00 46.18 ?  105 HIS E CE1 1 
ATOM   839  N NE2 . HIS A 1 105 ? 27.625  -13.951 -63.421 1.00 47.31 ?  105 HIS E NE2 1 
ATOM   840  N N   . ASP A 1 106 ? 25.927  -8.089  -60.518 1.00 34.90 ?  106 ASP E N   1 
ATOM   841  C CA  . ASP A 1 106 ? 25.375  -7.016  -59.690 1.00 33.91 ?  106 ASP E CA  1 
ATOM   842  C C   . ASP A 1 106 ? 24.599  -7.558  -58.482 1.00 36.98 ?  106 ASP E C   1 
ATOM   843  O O   . ASP A 1 106 ? 23.393  -7.331  -58.327 1.00 36.18 ?  106 ASP E O   1 
ATOM   844  C CB  . ASP A 1 106 ? 24.505  -6.076  -60.539 1.00 37.75 ?  106 ASP E CB  1 
ATOM   845  C CG  . ASP A 1 106 ? 24.256  -4.748  -59.857 1.00 45.80 ?  106 ASP E CG  1 
ATOM   846  O OD1 . ASP A 1 106 ? 25.128  -4.314  -59.079 1.00 50.94 ?  106 ASP E OD1 1 
ATOM   847  O OD2 . ASP A 1 106 ? 23.200  -4.122  -60.105 1.00 53.85 ?  106 ASP E OD2 1 
ATOM   848  N N   . PHE A 1 107 ? 25.314  -8.276  -57.610 1.00 30.32 ?  107 PHE E N   1 
ATOM   849  C CA  . PHE A 1 107 ? 24.728  -8.685  -56.338 1.00 27.76 ?  107 PHE E CA  1 
ATOM   850  C C   . PHE A 1 107 ? 25.801  -8.690  -55.251 1.00 27.30 ?  107 PHE E C   1 
ATOM   851  O O   . PHE A 1 107 ? 26.973  -8.970  -55.511 1.00 25.62 ?  107 PHE E O   1 
ATOM   852  C CB  . PHE A 1 107 ? 24.033  -10.058 -56.443 1.00 27.44 ?  107 PHE E CB  1 
ATOM   853  C CG  . PHE A 1 107 ? 24.975  -11.217 -56.696 1.00 31.83 ?  107 PHE E CG  1 
ATOM   854  C CD1 . PHE A 1 107 ? 25.637  -11.840 -55.644 1.00 28.30 ?  107 PHE E CD1 1 
ATOM   855  C CD2 . PHE A 1 107 ? 25.182  -11.698 -57.986 1.00 32.70 ?  107 PHE E CD2 1 
ATOM   856  C CE1 . PHE A 1 107 ? 26.508  -12.908 -55.864 1.00 27.07 ?  107 PHE E CE1 1 
ATOM   857  C CE2 . PHE A 1 107 ? 26.054  -12.778 -58.223 1.00 29.63 ?  107 PHE E CE2 1 
ATOM   858  C CZ  . PHE A 1 107 ? 26.722  -13.376 -57.152 1.00 31.11 ?  107 PHE E CZ  1 
ATOM   859  N N   . TRP A 1 108 ? 25.371  -8.392  -54.028 1.00 24.84 ?  108 TRP E N   1 
ATOM   860  C CA  . TRP A 1 108 ? 26.212  -8.536  -52.848 1.00 22.23 ?  108 TRP E CA  1 
ATOM   861  C C   . TRP A 1 108 ? 26.230  -9.981  -52.369 1.00 24.13 ?  108 TRP E C   1 
ATOM   862  O O   . TRP A 1 108 ? 25.213  -10.678 -52.409 1.00 25.32 ?  108 TRP E O   1 
ATOM   863  C CB  . TRP A 1 108 ? 25.714  -7.620  -51.738 1.00 21.46 ?  108 TRP E CB  1 
ATOM   864  C CG  . TRP A 1 108 ? 26.031  -6.180  -52.024 1.00 23.57 ?  108 TRP E CG  1 
ATOM   865  C CD1 . TRP A 1 108 ? 25.265  -5.267  -52.707 1.00 27.15 ?  108 TRP E CD1 1 
ATOM   866  C CD2 . TRP A 1 108 ? 27.239  -5.518  -51.683 1.00 23.53 ?  108 TRP E CD2 1 
ATOM   867  N NE1 . TRP A 1 108 ? 25.930  -4.053  -52.774 1.00 25.82 ?  108 TRP E NE1 1 
ATOM   868  C CE2 . TRP A 1 108 ? 27.146  -4.191  -52.153 1.00 25.31 ?  108 TRP E CE2 1 
ATOM   869  C CE3 . TRP A 1 108 ? 28.398  -5.912  -51.003 1.00 24.47 ?  108 TRP E CE3 1 
ATOM   870  C CZ2 . TRP A 1 108 ? 28.167  -3.270  -51.972 1.00 27.52 ?  108 TRP E CZ2 1 
ATOM   871  C CZ3 . TRP A 1 108 ? 29.412  -4.994  -50.833 1.00 25.33 ?  108 TRP E CZ3 1 
ATOM   872  C CH2 . TRP A 1 108 ? 29.284  -3.682  -51.302 1.00 24.97 ?  108 TRP E CH2 1 
ATOM   873  N N   . SER A 1 109 ? 27.394  -10.421 -51.897 1.00 23.63 ?  109 SER E N   1 
ATOM   874  C CA  . SER A 1 109 ? 27.648  -11.836 -51.651 1.00 20.21 ?  109 SER E CA  1 
ATOM   875  C C   . SER A 1 109 ? 27.284  -12.257 -50.231 1.00 20.95 ?  109 SER E C   1 
ATOM   876  O O   . SER A 1 109 ? 26.977  -11.440 -49.367 1.00 23.04 ?  109 SER E O   1 
ATOM   877  C CB  . SER A 1 109 ? 29.115  -12.141 -51.874 1.00 23.46 ?  109 SER E CB  1 
ATOM   878  O OG  . SER A 1 109 ? 29.839  -11.688 -50.741 1.00 23.96 ?  109 SER E OG  1 
ATOM   879  N N   . GLY A 1 110 ? 27.381  -13.571 -49.978 1.00 21.52 ?  110 GLY E N   1 
ATOM   880  C CA  . GLY A 1 110 ? 27.355  -14.081 -48.625 1.00 21.10 ?  110 GLY E CA  1 
ATOM   881  C C   . GLY A 1 110 ? 28.723  -13.941 -47.966 1.00 23.60 ?  110 GLY E C   1 
ATOM   882  O O   . GLY A 1 110 ? 29.675  -13.391 -48.533 1.00 22.25 ?  110 GLY E O   1 
ATOM   883  N N   . LEU A 1 111 ? 28.809  -14.437 -46.732 1.00 20.28 ?  111 LEU E N   1 
ATOM   884  C CA  . LEU A 1 111 ? 30.004  -14.269 -45.899 1.00 19.45 ?  111 LEU E CA  1 
ATOM   885  C C   . LEU A 1 111 ? 30.736  -15.611 -45.890 1.00 21.59 ?  111 LEU E C   1 
ATOM   886  O O   . LEU A 1 111 ? 30.344  -16.534 -45.174 1.00 18.70 ?  111 LEU E O   1 
ATOM   887  C CB  . LEU A 1 111 ? 29.623  -13.794 -44.500 1.00 21.07 ?  111 LEU E CB  1 
ATOM   888  C CG  . LEU A 1 111 ? 28.706  -12.547 -44.481 1.00 24.92 ?  111 LEU E CG  1 
ATOM   889  C CD1 . LEU A 1 111 ? 28.250  -12.173 -43.051 1.00 25.57 ?  111 LEU E CD1 1 
ATOM   890  C CD2 . LEU A 1 111 ? 29.383  -11.366 -45.122 1.00 24.80 ?  111 LEU E CD2 1 
ATOM   891  N N   . ASP A 1 112 ? 31.787  -15.729 -46.712 1.00 18.51 ?  112 ASP E N   1 
ATOM   892  C CA  . ASP A 1 112 ? 32.326  -17.071 -46.923 1.00 22.10 ?  112 ASP E CA  1 
ATOM   893  C C   . ASP A 1 112 ? 33.387  -17.454 -45.899 1.00 21.78 ?  112 ASP E C   1 
ATOM   894  O O   . ASP A 1 112 ? 33.404  -18.596 -45.439 1.00 25.31 ?  112 ASP E O   1 
ATOM   895  C CB  . ASP A 1 112 ? 32.870  -17.244 -48.357 1.00 22.32 ?  112 ASP E CB  1 
ATOM   896  C CG  . ASP A 1 112 ? 33.793  -16.101 -48.825 1.00 23.04 ?  112 ASP E CG  1 
ATOM   897  O OD1 . ASP A 1 112 ? 34.245  -15.243 -48.024 1.00 23.02 ?  112 ASP E OD1 1 
ATOM   898  O OD2 . ASP A 1 112 ? 34.091  -16.076 -50.048 1.00 22.61 ?  112 ASP E OD2 1 
ATOM   899  N N   . TYR A 1 113 ? 34.268  -16.539 -45.502 1.00 20.95 ?  113 TYR E N   1 
ATOM   900  C CA  . TYR A 1 113 ? 35.251  -16.824 -44.465 1.00 20.21 ?  113 TYR E CA  1 
ATOM   901  C C   . TYR A 1 113 ? 35.011  -15.909 -43.274 1.00 21.66 ?  113 TYR E C   1 
ATOM   902  O O   . TYR A 1 113 ? 34.718  -14.713 -43.443 1.00 21.15 ?  113 TYR E O   1 
ATOM   903  C CB  . TYR A 1 113 ? 36.676  -16.628 -44.976 1.00 22.66 ?  113 TYR E CB  1 
ATOM   904  C CG  . TYR A 1 113 ? 37.015  -17.617 -46.068 1.00 24.71 ?  113 TYR E CG  1 
ATOM   905  C CD1 . TYR A 1 113 ? 37.303  -18.944 -45.764 1.00 25.96 ?  113 TYR E CD1 1 
ATOM   906  C CD2 . TYR A 1 113 ? 37.013  -17.226 -47.397 1.00 24.84 ?  113 TYR E CD2 1 
ATOM   907  C CE1 . TYR A 1 113 ? 37.615  -19.868 -46.779 1.00 27.57 ?  113 TYR E CE1 1 
ATOM   908  C CE2 . TYR A 1 113 ? 37.317  -18.127 -48.409 1.00 26.82 ?  113 TYR E CE2 1 
ATOM   909  C CZ  . TYR A 1 113 ? 37.612  -19.438 -48.097 1.00 27.78 ?  113 TYR E CZ  1 
ATOM   910  O OH  . TYR A 1 113 ? 37.907  -20.308 -49.121 1.00 32.76 ?  113 TYR E OH  1 
ATOM   911  N N   . TRP A 1 114 ? 35.170  -16.476 -42.076 1.00 20.97 ?  114 TRP E N   1 
ATOM   912  C CA  . TRP A 1 114 ? 34.901  -15.775 -40.829 1.00 23.51 ?  114 TRP E CA  1 
ATOM   913  C C   . TRP A 1 114 ? 36.129  -15.745 -39.937 1.00 23.82 ?  114 TRP E C   1 
ATOM   914  O O   . TRP A 1 114 ? 36.888  -16.722 -39.867 1.00 21.21 ?  114 TRP E O   1 
ATOM   915  C CB  . TRP A 1 114 ? 33.762  -16.459 -40.066 1.00 23.28 ?  114 TRP E CB  1 
ATOM   916  C CG  . TRP A 1 114 ? 32.420  -16.343 -40.739 1.00 22.52 ?  114 TRP E CG  1 
ATOM   917  C CD1 . TRP A 1 114 ? 32.022  -16.919 -41.924 1.00 20.29 ?  114 TRP E CD1 1 
ATOM   918  C CD2 . TRP A 1 114 ? 31.302  -15.593 -40.252 1.00 23.81 ?  114 TRP E CD2 1 
ATOM   919  N NE1 . TRP A 1 114 ? 30.701  -16.573 -42.190 1.00 22.79 ?  114 TRP E NE1 1 
ATOM   920  C CE2 . TRP A 1 114 ? 30.237  -15.770 -41.174 1.00 21.17 ?  114 TRP E CE2 1 
ATOM   921  C CE3 . TRP A 1 114 ? 31.082  -14.815 -39.105 1.00 22.79 ?  114 TRP E CE3 1 
ATOM   922  C CZ2 . TRP A 1 114 ? 28.992  -15.168 -41.002 1.00 23.54 ?  114 TRP E CZ2 1 
ATOM   923  C CZ3 . TRP A 1 114 ? 29.820  -14.227 -38.931 1.00 23.78 ?  114 TRP E CZ3 1 
ATOM   924  C CH2 . TRP A 1 114 ? 28.796  -14.415 -39.874 1.00 22.74 ?  114 TRP E CH2 1 
ATOM   925  N N   . GLY A 1 115 ? 36.296  -14.633 -39.222 1.00 19.64 ?  115 GLY E N   1 
ATOM   926  C CA  . GLY A 1 115 ? 37.242  -14.591 -38.122 1.00 23.01 ?  115 GLY E CA  1 
ATOM   927  C C   . GLY A 1 115 ? 36.765  -15.438 -36.957 1.00 24.83 ?  115 GLY E C   1 
ATOM   928  O O   . GLY A 1 115 ? 35.642  -15.946 -36.936 1.00 23.77 ?  115 GLY E O   1 
ATOM   929  N N   . GLN A 1 116 ? 37.628  -15.586 -35.953 1.00 21.96 ?  116 GLN E N   1 
ATOM   930  C CA  . GLN A 1 116 ? 37.290  -16.446 -34.819 1.00 22.08 ?  116 GLN E CA  1 
ATOM   931  C C   . GLN A 1 116 ? 36.418  -15.757 -33.776 1.00 24.59 ?  116 GLN E C   1 
ATOM   932  O O   . GLN A 1 116 ? 35.987  -16.419 -32.827 1.00 25.16 ?  116 GLN E O   1 
ATOM   933  C CB  . GLN A 1 116 ? 38.566  -16.974 -34.140 1.00 24.47 ?  116 GLN E CB  1 
ATOM   934  C CG  . GLN A 1 116 ? 39.194  -16.011 -33.103 1.00 26.11 ?  116 GLN E CG  1 
ATOM   935  C CD  . GLN A 1 116 ? 40.182  -15.028 -33.725 1.00 27.25 ?  116 GLN E CD  1 
ATOM   936  O OE1 . GLN A 1 116 ? 40.105  -14.722 -34.924 1.00 24.85 ?  116 GLN E OE1 1 
ATOM   937  N NE2 . GLN A 1 116 ? 41.086  -14.494 -32.903 1.00 22.25 ?  116 GLN E NE2 1 
ATOM   938  N N   . GLY A 1 117 ? 36.157  -14.470 -33.922 1.00 22.34 ?  117 GLY E N   1 
ATOM   939  C CA  . GLY A 1 117 ? 35.402  -13.746 -32.909 1.00 25.39 ?  117 GLY E CA  1 
ATOM   940  C C   . GLY A 1 117 ? 36.297  -13.088 -31.875 1.00 23.47 ?  117 GLY E C   1 
ATOM   941  O O   . GLY A 1 117 ? 37.341  -13.614 -31.468 1.00 24.57 ?  117 GLY E O   1 
ATOM   942  N N   . THR A 1 118 ? 35.865  -11.905 -31.445 1.00 23.76 ?  118 THR E N   1 
ATOM   943  C CA  . THR A 1 118 ? 36.462  -11.144 -30.355 1.00 24.88 ?  118 THR E CA  1 
ATOM   944  C C   . THR A 1 118 ? 35.371  -10.857 -29.333 1.00 27.20 ?  118 THR E C   1 
ATOM   945  O O   . THR A 1 118 ? 34.382  -10.191 -29.654 1.00 24.58 ?  118 THR E O   1 
ATOM   946  C CB  . THR A 1 118 ? 37.054  -9.825  -30.869 1.00 25.57 ?  118 THR E CB  1 
ATOM   947  O OG1 . THR A 1 118 ? 38.072  -10.098 -31.844 1.00 24.12 ?  118 THR E OG1 1 
ATOM   948  C CG2 . THR A 1 118 ? 37.631  -8.999  -29.716 1.00 26.42 ?  118 THR E CG2 1 
ATOM   949  N N   . LEU A 1 119 ? 35.553  -11.335 -28.110 1.00 26.51 ?  119 LEU E N   1 
ATOM   950  C CA  . LEU A 1 119 ? 34.597  -11.027 -27.053 1.00 25.67 ?  119 LEU E CA  1 
ATOM   951  C C   . LEU A 1 119 ? 34.883  -9.636  -26.494 1.00 27.04 ?  119 LEU E C   1 
ATOM   952  O O   . LEU A 1 119 ? 36.006  -9.363  -26.063 1.00 29.08 ?  119 LEU E O   1 
ATOM   953  C CB  . LEU A 1 119 ? 34.682  -12.069 -25.946 1.00 26.29 ?  119 LEU E CB  1 
ATOM   954  C CG  . LEU A 1 119 ? 33.740  -11.804 -24.772 1.00 33.07 ?  119 LEU E CG  1 
ATOM   955  C CD1 . LEU A 1 119 ? 32.276  -11.930 -25.214 1.00 34.21 ?  119 LEU E CD1 1 
ATOM   956  C CD2 . LEU A 1 119 ? 34.037  -12.783 -23.654 1.00 33.07 ?  119 LEU E CD2 1 
ATOM   957  N N   . VAL A 1 120 ? 33.878  -8.761  -26.503 1.00 25.35 ?  120 VAL E N   1 
ATOM   958  C CA  . VAL A 1 120 ? 33.970  -7.434  -25.891 1.00 27.41 ?  120 VAL E CA  1 
ATOM   959  C C   . VAL A 1 120 ? 32.993  -7.420  -24.728 1.00 31.97 ?  120 VAL E C   1 
ATOM   960  O O   . VAL A 1 120 ? 31.780  -7.556  -24.930 1.00 29.67 ?  120 VAL E O   1 
ATOM   961  C CB  . VAL A 1 120 ? 33.653  -6.304  -26.885 1.00 28.89 ?  120 VAL E CB  1 
ATOM   962  C CG1 . VAL A 1 120 ? 33.660  -4.940  -26.162 1.00 28.13 ?  120 VAL E CG1 1 
ATOM   963  C CG2 . VAL A 1 120 ? 34.648  -6.298  -28.048 1.00 28.72 ?  120 VAL E CG2 1 
ATOM   964  N N   . SER A 1 121 ? 33.515  -7.274  -23.514 1.00 30.72 ?  121 SER E N   1 
ATOM   965  C CA  . SER A 1 121 ? 32.699  -7.248  -22.309 1.00 31.80 ?  121 SER E CA  1 
ATOM   966  C C   . SER A 1 121 ? 32.700  -5.840  -21.725 1.00 31.58 ?  121 SER E C   1 
ATOM   967  O O   . SER A 1 121 ? 33.760  -5.236  -21.562 1.00 30.53 ?  121 SER E O   1 
ATOM   968  C CB  . SER A 1 121 ? 33.226  -8.259  -21.292 1.00 35.60 ?  121 SER E CB  1 
ATOM   969  O OG  . SER A 1 121 ? 32.709  -7.973  -20.012 1.00 46.06 ?  121 SER E OG  1 
ATOM   970  N N   . VAL A 1 122 ? 31.512  -5.319  -21.417 1.00 31.99 ?  122 VAL E N   1 
ATOM   971  C CA  . VAL A 1 122 ? 31.358  -3.967  -20.884 1.00 32.32 ?  122 VAL E CA  1 
ATOM   972  C C   . VAL A 1 122 ? 30.797  -4.073  -19.479 1.00 34.58 ?  122 VAL E C   1 
ATOM   973  O O   . VAL A 1 122 ? 29.696  -4.599  -19.290 1.00 33.52 ?  122 VAL E O   1 
ATOM   974  C CB  . VAL A 1 122 ? 30.444  -3.103  -21.764 1.00 33.62 ?  122 VAL E CB  1 
ATOM   975  C CG1 . VAL A 1 122 ? 30.365  -1.679  -21.202 1.00 33.84 ?  122 VAL E CG1 1 
ATOM   976  C CG2 . VAL A 1 122 ? 30.967  -3.067  -23.182 1.00 32.08 ?  122 VAL E CG2 1 
ATOM   977  N N   . SER A 1 123 ? 31.548  -3.583  -18.495 1.00 31.75 ?  123 SER E N   1 
ATOM   978  C CA  . SER A 1 123 ? 30.984  -3.432  -17.160 1.00 39.22 ?  123 SER E CA  1 
ATOM   979  C C   . SER A 1 123 ? 31.896  -2.551  -16.323 1.00 37.80 ?  123 SER E C   1 
ATOM   980  O O   . SER A 1 123 ? 33.050  -2.288  -16.669 1.00 36.99 ?  123 SER E O   1 
ATOM   981  C CB  . SER A 1 123 ? 30.754  -4.775  -16.456 1.00 42.48 ?  123 SER E CB  1 
ATOM   982  O OG  . SER A 1 123 ? 31.957  -5.340  -15.988 1.00 41.86 ?  123 SER E OG  1 
ATOM   983  N N   . SER A 1 124 ? 31.342  -2.093  -15.213 1.00 40.83 ?  124 SER E N   1 
ATOM   984  C CA  . SER A 1 124 ? 32.048  -1.228  -14.286 1.00 43.16 ?  124 SER E CA  1 
ATOM   985  C C   . SER A 1 124 ? 32.759  -2.005  -13.185 1.00 45.08 ?  124 SER E C   1 
ATOM   986  O O   . SER A 1 124 ? 33.468  -1.400  -12.377 1.00 44.08 ?  124 SER E O   1 
ATOM   987  C CB  . SER A 1 124 ? 31.063  -0.217  -13.697 1.00 42.04 ?  124 SER E CB  1 
ATOM   988  O OG  . SER A 1 124 ? 29.982  -0.888  -13.070 1.00 50.78 ?  124 SER E OG  1 
ATOM   989  N N   . ALA A 1 125 ? 32.617  -3.327  -13.153 1.00 41.01 ?  125 ALA E N   1 
ATOM   990  C CA  . ALA A 1 125 ? 33.298  -4.125  -12.146 1.00 41.23 ?  125 ALA E CA  1 
ATOM   991  C C   . ALA A 1 125 ? 34.807  -4.044  -12.315 1.00 42.34 ?  125 ALA E C   1 
ATOM   992  O O   . ALA A 1 125 ? 35.322  -3.803  -13.411 1.00 42.50 ?  125 ALA E O   1 
ATOM   993  C CB  . ALA A 1 125 ? 32.842  -5.587  -12.217 1.00 42.17 ?  125 ALA E CB  1 
ATOM   994  N N   . SER A 1 126 ? 35.517  -4.249  -11.208 1.00 40.64 ?  126 SER E N   1 
ATOM   995  C CA  . SER A 1 126 ? 36.971  -4.272  -11.183 1.00 40.94 ?  126 SER E CA  1 
ATOM   996  C C   . SER A 1 126 ? 37.462  -5.690  -10.925 1.00 39.88 ?  126 SER E C   1 
ATOM   997  O O   . SER A 1 126 ? 36.734  -6.529  -10.400 1.00 36.83 ?  126 SER E O   1 
ATOM   998  C CB  . SER A 1 126 ? 37.508  -3.326  -10.107 1.00 45.95 ?  126 SER E CB  1 
ATOM   999  O OG  . SER A 1 126 ? 37.180  -1.980  -10.415 1.00 49.40 ?  126 SER E OG  1 
ATOM   1000 N N   . THR A 1 127 ? 38.718  -5.940  -11.291 1.00 38.25 ?  127 THR E N   1 
ATOM   1001 C CA  . THR A 1 127 ? 39.304  -7.265  -11.123 1.00 37.52 ?  127 THR E CA  1 
ATOM   1002 C C   . THR A 1 127 ? 39.232  -7.709  -9.670  1.00 39.94 ?  127 THR E C   1 
ATOM   1003 O O   . THR A 1 127 ? 39.603  -6.965  -8.760  1.00 39.75 ?  127 THR E O   1 
ATOM   1004 C CB  . THR A 1 127 ? 40.759  -7.256  -11.589 1.00 37.96 ?  127 THR E CB  1 
ATOM   1005 O OG1 . THR A 1 127 ? 40.817  -6.841  -12.955 1.00 39.26 ?  127 THR E OG1 1 
ATOM   1006 C CG2 . THR A 1 127 ? 41.386  -8.641  -11.448 1.00 35.22 ?  127 THR E CG2 1 
ATOM   1007 N N   . LYS A 1 128 ? 38.770  -8.937  -9.459  1.00 36.02 ?  128 LYS E N   1 
ATOM   1008 C CA  . LYS A 1 128 ? 38.660  -9.508  -8.123  1.00 37.31 ?  128 LYS E CA  1 
ATOM   1009 C C   . LYS A 1 128 ? 38.819  -11.017 -8.224  1.00 36.35 ?  128 LYS E C   1 
ATOM   1010 O O   . LYS A 1 128 ? 38.184  -11.646 -9.075  1.00 35.95 ?  128 LYS E O   1 
ATOM   1011 C CB  . LYS A 1 128 ? 37.310  -9.151  -7.485  1.00 36.29 ?  128 LYS E CB  1 
ATOM   1012 C CG  . LYS A 1 128 ? 36.998  -9.970  -6.240  1.00 40.39 ?  128 LYS E CG  1 
ATOM   1013 C CD  . LYS A 1 128 ? 35.701  -9.534  -5.574  1.00 40.64 ?  128 LYS E CD  1 
ATOM   1014 C CE  . LYS A 1 128 ? 35.539  -10.208 -4.208  1.00 44.94 ?  128 LYS E CE  1 
ATOM   1015 N NZ  . LYS A 1 128 ? 35.679  -11.711 -4.275  1.00 46.57 ?  128 LYS E NZ  1 
ATOM   1016 N N   . GLY A 1 129 ? 39.674  -11.588 -7.376  1.00 35.10 ?  129 GLY E N   1 
ATOM   1017 C CA  . GLY A 1 129 ? 39.849  -13.019 -7.309  1.00 33.23 ?  129 GLY E CA  1 
ATOM   1018 C C   . GLY A 1 129 ? 38.689  -13.693 -6.593  1.00 36.35 ?  129 GLY E C   1 
ATOM   1019 O O   . GLY A 1 129 ? 38.019  -13.099 -5.741  1.00 35.00 ?  129 GLY E O   1 
ATOM   1020 N N   . PRO A 1 130 ? 38.432  -14.953 -6.922  1.00 35.61 ?  130 PRO E N   1 
ATOM   1021 C CA  . PRO A 1 130 ? 37.300  -15.658 -6.313  1.00 35.39 ?  130 PRO E CA  1 
ATOM   1022 C C   . PRO A 1 130 ? 37.608  -16.162 -4.912  1.00 37.29 ?  130 PRO E C   1 
ATOM   1023 O O   . PRO A 1 130 ? 38.757  -16.403 -4.539  1.00 38.02 ?  130 PRO E O   1 
ATOM   1024 C CB  . PRO A 1 130 ? 37.070  -16.834 -7.263  1.00 33.42 ?  130 PRO E CB  1 
ATOM   1025 C CG  . PRO A 1 130 ? 38.444  -17.134 -7.808  1.00 34.40 ?  130 PRO E CG  1 
ATOM   1026 C CD  . PRO A 1 130 ? 39.150  -15.788 -7.904  1.00 32.37 ?  130 PRO E CD  1 
ATOM   1027 N N   . SER A 1 131 ? 36.543  -16.322 -4.131  1.00 35.21 ?  131 SER E N   1 
ATOM   1028 C CA  . SER A 1 131 ? 36.583  -17.164 -2.942  1.00 36.08 ?  131 SER E CA  1 
ATOM   1029 C C   . SER A 1 131 ? 36.182  -18.580 -3.341  1.00 38.03 ?  131 SER E C   1 
ATOM   1030 O O   . SER A 1 131 ? 35.331  -18.769 -4.214  1.00 40.88 ?  131 SER E O   1 
ATOM   1031 C CB  . SER A 1 131 ? 35.642  -16.626 -1.862  1.00 39.43 ?  131 SER E CB  1 
ATOM   1032 O OG  . SER A 1 131 ? 36.069  -15.345 -1.408  1.00 41.77 ?  131 SER E OG  1 
ATOM   1033 N N   . VAL A 1 132 ? 36.799  -19.575 -2.709  1.00 33.88 ?  132 VAL E N   1 
ATOM   1034 C CA  . VAL A 1 132 ? 36.604  -20.973 -3.082  1.00 36.62 ?  132 VAL E CA  1 
ATOM   1035 C C   . VAL A 1 132 ? 36.135  -21.746 -1.859  1.00 38.42 ?  132 VAL E C   1 
ATOM   1036 O O   . VAL A 1 132 ? 36.881  -21.885 -0.883  1.00 39.63 ?  132 VAL E O   1 
ATOM   1037 C CB  . VAL A 1 132 ? 37.882  -21.594 -3.659  1.00 38.42 ?  132 VAL E CB  1 
ATOM   1038 C CG1 . VAL A 1 132 ? 37.644  -23.062 -3.998  1.00 35.18 ?  132 VAL E CG1 1 
ATOM   1039 C CG2 . VAL A 1 132 ? 38.348  -20.821 -4.888  1.00 35.13 ?  132 VAL E CG2 1 
ATOM   1040 N N   . PHE A 1 133 ? 34.912  -22.275 -1.924  1.00 34.99 ?  133 PHE E N   1 
ATOM   1041 C CA  . PHE A 1 133 ? 34.264  -22.945 -0.809  1.00 34.00 ?  133 PHE E CA  1 
ATOM   1042 C C   . PHE A 1 133 ? 33.955  -24.395 -1.154  1.00 38.68 ?  133 PHE E C   1 
ATOM   1043 O O   . PHE A 1 133 ? 33.576  -24.689 -2.292  1.00 36.00 ?  133 PHE E O   1 
ATOM   1044 C CB  . PHE A 1 133 ? 32.955  -22.248 -0.441  1.00 36.16 ?  133 PHE E CB  1 
ATOM   1045 C CG  . PHE A 1 133 ? 33.117  -20.810 -0.077  1.00 38.57 ?  133 PHE E CG  1 
ATOM   1046 C CD1 . PHE A 1 133 ? 33.918  -20.439 0.995   1.00 40.18 ?  133 PHE E CD1 1 
ATOM   1047 C CD2 . PHE A 1 133 ? 32.497  -19.826 -0.825  1.00 37.27 ?  133 PHE E CD2 1 
ATOM   1048 C CE1 . PHE A 1 133 ? 34.067  -19.110 1.335   1.00 40.34 ?  133 PHE E CE1 1 
ATOM   1049 C CE2 . PHE A 1 133 ? 32.655  -18.492 -0.498  1.00 39.68 ?  133 PHE E CE2 1 
ATOM   1050 C CZ  . PHE A 1 133 ? 33.447  -18.136 0.583   1.00 37.80 ?  133 PHE E CZ  1 
ATOM   1051 N N   . PRO A 1 134 ? 34.073  -25.313 -0.197  1.00 38.61 ?  134 PRO E N   1 
ATOM   1052 C CA  . PRO A 1 134 ? 33.781  -26.720 -0.486  1.00 38.85 ?  134 PRO E CA  1 
ATOM   1053 C C   . PRO A 1 134 ? 32.287  -26.979 -0.573  1.00 36.13 ?  134 PRO E C   1 
ATOM   1054 O O   . PRO A 1 134 ? 31.487  -26.360 0.130   1.00 36.59 ?  134 PRO E O   1 
ATOM   1055 C CB  . PRO A 1 134 ? 34.395  -27.448 0.715   1.00 42.23 ?  134 PRO E CB  1 
ATOM   1056 C CG  . PRO A 1 134 ? 34.187  -26.481 1.835   1.00 40.41 ?  134 PRO E CG  1 
ATOM   1057 C CD  . PRO A 1 134 ? 34.423  -25.111 1.221   1.00 43.45 ?  134 PRO E CD  1 
ATOM   1058 N N   . LEU A 1 135 ? 31.919  -27.892 -1.467  1.00 37.37 ?  135 LEU E N   1 
ATOM   1059 C CA  . LEU A 1 135 ? 30.562  -28.437 -1.560  1.00 38.54 ?  135 LEU E CA  1 
ATOM   1060 C C   . LEU A 1 135 ? 30.640  -29.885 -1.085  1.00 40.92 ?  135 LEU E C   1 
ATOM   1061 O O   . LEU A 1 135 ? 31.089  -30.767 -1.828  1.00 39.83 ?  135 LEU E O   1 
ATOM   1062 C CB  . LEU A 1 135 ? 30.018  -28.351 -2.984  1.00 36.96 ?  135 LEU E CB  1 
ATOM   1063 C CG  . LEU A 1 135 ? 29.731  -26.956 -3.538  1.00 39.44 ?  135 LEU E CG  1 
ATOM   1064 C CD1 . LEU A 1 135 ? 29.550  -27.046 -5.038  1.00 38.08 ?  135 LEU E CD1 1 
ATOM   1065 C CD2 . LEU A 1 135 ? 28.487  -26.356 -2.892  1.00 38.40 ?  135 LEU E CD2 1 
ATOM   1066 N N   . ALA A 1 136 ? 30.217  -30.126 0.152   1.00 42.76 ?  136 ALA E N   1 
ATOM   1067 C CA  . ALA A 1 136 ? 30.348  -31.443 0.753   1.00 47.95 ?  136 ALA E CA  1 
ATOM   1068 C C   . ALA A 1 136 ? 28.967  -32.022 1.036   1.00 50.44 ?  136 ALA E C   1 
ATOM   1069 O O   . ALA A 1 136 ? 28.045  -31.273 1.386   1.00 50.83 ?  136 ALA E O   1 
ATOM   1070 C CB  . ALA A 1 136 ? 31.156  -31.376 2.055   1.00 45.41 ?  136 ALA E CB  1 
ATOM   1071 N N   . PRO A 1 137 ? 28.790  -33.356 0.897   1.00 53.96 ?  137 PRO E N   1 
ATOM   1072 C CA  . PRO A 1 137 ? 27.518  -34.086 1.024   1.00 56.96 ?  137 PRO E CA  1 
ATOM   1073 C C   . PRO A 1 137 ? 26.534  -33.500 2.042   1.00 58.39 ?  137 PRO E C   1 
ATOM   1074 O O   . PRO A 1 137 ? 26.217  -34.146 3.043   1.00 63.02 ?  137 PRO E O   1 
ATOM   1075 C CB  . PRO A 1 137 ? 27.974  -35.480 1.460   1.00 54.20 ?  137 PRO E CB  1 
ATOM   1076 C CG  . PRO A 1 137 ? 29.287  -35.657 0.757   1.00 55.74 ?  137 PRO E CG  1 
ATOM   1077 C CD  . PRO A 1 137 ? 29.910  -34.276 0.615   1.00 53.60 ?  137 PRO E CD  1 
ATOM   1078 N N   . GLY A 1 145 ? 25.847  -45.981 -3.126  1.00 30.00 ?  145 GLY E N   1 
ATOM   1079 C CA  . GLY A 1 145 ? 25.485  -45.489 -4.467  1.00 30.00 ?  145 GLY E CA  1 
ATOM   1080 C C   . GLY A 1 145 ? 26.456  -44.432 -4.949  1.00 30.00 ?  145 GLY E C   1 
ATOM   1081 O O   . GLY A 1 145 ? 27.671  -44.668 -4.873  1.00 30.00 ?  145 GLY E O   1 
ATOM   1082 N N   . THR A 1 146 ? 25.939  -43.297 -5.416  1.00 45.84 ?  146 THR E N   1 
ATOM   1083 C CA  . THR A 1 146 ? 26.808  -42.227 -5.962  1.00 44.64 ?  146 THR E CA  1 
ATOM   1084 C C   . THR A 1 146 ? 26.777  -41.004 -5.050  1.00 43.49 ?  146 THR E C   1 
ATOM   1085 O O   . THR A 1 146 ? 25.682  -40.616 -4.614  1.00 41.00 ?  146 THR E O   1 
ATOM   1086 C CB  . THR A 1 146 ? 26.402  -41.864 -7.393  1.00 42.73 ?  146 THR E CB  1 
ATOM   1087 O OG1 . THR A 1 146 ? 26.518  -43.042 -8.186  1.00 46.55 ?  146 THR E OG1 1 
ATOM   1088 C CG2 . THR A 1 146 ? 27.250  -40.761 -7.983  1.00 42.61 ?  146 THR E CG2 1 
ATOM   1089 N N   . ALA A 1 147 ? 27.949  -40.439 -4.773  1.00 43.77 ?  147 ALA E N   1 
ATOM   1090 C CA  . ALA A 1 147 ? 28.010  -39.195 -3.986  1.00 43.58 ?  147 ALA E CA  1 
ATOM   1091 C C   . ALA A 1 147 ? 28.408  -38.027 -4.887  1.00 38.73 ?  147 ALA E C   1 
ATOM   1092 O O   . ALA A 1 147 ? 29.028  -38.268 -5.924  1.00 41.38 ?  147 ALA E O   1 
ATOM   1093 C CB  . ALA A 1 147 ? 28.991  -39.352 -2.866  1.00 41.26 ?  147 ALA E CB  1 
ATOM   1094 N N   . ALA A 1 148 ? 28.020  -36.819 -4.505  1.00 38.03 ?  148 ALA E N   1 
ATOM   1095 C CA  . ALA A 1 148 ? 28.441  -35.621 -5.223  1.00 37.87 ?  148 ALA E CA  1 
ATOM   1096 C C   . ALA A 1 148 ? 29.201  -34.695 -4.285  1.00 34.81 ?  148 ALA E C   1 
ATOM   1097 O O   . ALA A 1 148 ? 28.842  -34.536 -3.116  1.00 36.60 ?  148 ALA E O   1 
ATOM   1098 C CB  . ALA A 1 148 ? 27.251  -34.872 -5.837  1.00 34.44 ?  148 ALA E CB  1 
ATOM   1099 N N   . LEU A 1 149 ? 30.259  -34.088 -4.803  1.00 35.13 ?  149 LEU E N   1 
ATOM   1100 C CA  . LEU A 1 149 ? 30.993  -33.085 -4.055  1.00 34.98 ?  149 LEU E CA  1 
ATOM   1101 C C   . LEU A 1 149 ? 31.504  -32.068 -5.055  1.00 36.80 ?  149 LEU E C   1 
ATOM   1102 O O   . LEU A 1 149 ? 31.459  -32.287 -6.269  1.00 32.49 ?  149 LEU E O   1 
ATOM   1103 C CB  . LEU A 1 149 ? 32.117  -33.721 -3.222  1.00 38.00 ?  149 LEU E CB  1 
ATOM   1104 C CG  . LEU A 1 149 ? 33.216  -34.520 -3.917  1.00 40.81 ?  149 LEU E CG  1 
ATOM   1105 C CD1 . LEU A 1 149 ? 34.344  -33.624 -4.369  1.00 42.20 ?  149 LEU E CD1 1 
ATOM   1106 C CD2 . LEU A 1 149 ? 33.734  -35.609 -2.985  1.00 45.34 ?  149 LEU E CD2 1 
ATOM   1107 N N   . GLY A 1 150 ? 31.976  -30.940 -4.545  1.00 33.01 ?  150 GLY E N   1 
ATOM   1108 C CA  . GLY A 1 150 ? 32.432  -29.928 -5.471  1.00 34.66 ?  150 GLY E CA  1 
ATOM   1109 C C   . GLY A 1 150 ? 33.056  -28.747 -4.769  1.00 36.75 ?  150 GLY E C   1 
ATOM   1110 O O   . GLY A 1 150 ? 33.376  -28.800 -3.580  1.00 36.15 ?  150 GLY E O   1 
ATOM   1111 N N   . CYS A 1 151 ? 33.238  -27.678 -5.549  1.00 35.94 ?  151 CYS E N   1 
ATOM   1112 C CA  . CYS A 1 151 ? 33.746  -26.404 -5.065  1.00 36.41 ?  151 CYS E CA  1 
ATOM   1113 C C   . CYS A 1 151 ? 32.923  -25.279 -5.663  1.00 37.96 ?  151 CYS E C   1 
ATOM   1114 O O   . CYS A 1 151 ? 32.625  -25.287 -6.863  1.00 34.20 ?  151 CYS E O   1 
ATOM   1115 C CB  . CYS A 1 151 ? 35.212  -26.206 -5.445  1.00 39.37 ?  151 CYS E CB  1 
ATOM   1116 S SG  . CYS A 1 151 ? 36.325  -27.229 -4.508  1.00 45.83 ?  151 CYS E SG  1 
ATOM   1117 N N   . LEU A 1 152 ? 32.567  -24.312 -4.827  1.00 32.60 ?  152 LEU E N   1 
ATOM   1118 C CA  . LEU A 1 152 ? 31.891  -23.104 -5.267  1.00 35.37 ?  152 LEU E CA  1 
ATOM   1119 C C   . LEU A 1 152 ? 32.936  -22.004 -5.438  1.00 37.27 ?  152 LEU E C   1 
ATOM   1120 O O   . LEU A 1 152 ? 33.660  -21.675 -4.489  1.00 34.82 ?  152 LEU E O   1 
ATOM   1121 C CB  . LEU A 1 152 ? 30.809  -22.711 -4.264  1.00 32.99 ?  152 LEU E CB  1 
ATOM   1122 C CG  . LEU A 1 152 ? 30.047  -21.411 -4.495  1.00 37.49 ?  152 LEU E CG  1 
ATOM   1123 C CD1 . LEU A 1 152 ? 29.281  -21.453 -5.808  1.00 39.17 ?  152 LEU E CD1 1 
ATOM   1124 C CD2 . LEU A 1 152 ? 29.085  -21.158 -3.337  1.00 39.36 ?  152 LEU E CD2 1 
ATOM   1125 N N   . VAL A 1 153 ? 33.027  -21.457 -6.650  1.00 34.89 ?  153 VAL E N   1 
ATOM   1126 C CA  . VAL A 1 153 ? 34.004  -20.433 -7.020  1.00 34.26 ?  153 VAL E CA  1 
ATOM   1127 C C   . VAL A 1 153 ? 33.248  -19.114 -7.154  1.00 35.35 ?  153 VAL E C   1 
ATOM   1128 O O   . VAL A 1 153 ? 32.634  -18.845 -8.193  1.00 33.63 ?  153 VAL E O   1 
ATOM   1129 C CB  . VAL A 1 153 ? 34.729  -20.800 -8.321  1.00 32.61 ?  153 VAL E CB  1 
ATOM   1130 C CG1 . VAL A 1 153 ? 35.771  -19.762 -8.672  1.00 31.28 ?  153 VAL E CG1 1 
ATOM   1131 C CG2 . VAL A 1 153 ? 35.362  -22.178 -8.204  1.00 32.27 ?  153 VAL E CG2 1 
ATOM   1132 N N   . LYS A 1 154 ? 33.297  -18.263 -6.127  1.00 33.83 ?  154 LYS E N   1 
ATOM   1133 C CA  . LYS A 1 154 ? 32.312  -17.199 -5.998  1.00 37.07 ?  154 LYS E CA  1 
ATOM   1134 C C   . LYS A 1 154 ? 32.950  -15.810 -6.035  1.00 38.44 ?  154 LYS E C   1 
ATOM   1135 O O   . LYS A 1 154 ? 34.043  -15.593 -5.489  1.00 35.28 ?  154 LYS E O   1 
ATOM   1136 C CB  . LYS A 1 154 ? 31.497  -17.393 -4.702  1.00 41.77 ?  154 LYS E CB  1 
ATOM   1137 C CG  . LYS A 1 154 ? 30.494  -16.287 -4.440  1.00 45.92 ?  154 LYS E CG  1 
ATOM   1138 C CD  . LYS A 1 154 ? 29.194  -16.810 -3.843  1.00 48.67 ?  154 LYS E CD  1 
ATOM   1139 C CE  . LYS A 1 154 ? 28.204  -15.659 -3.633  1.00 47.17 ?  154 LYS E CE  1 
ATOM   1140 N NZ  . LYS A 1 154 ? 28.677  -14.708 -2.582  1.00 51.24 ?  154 LYS E NZ  1 
ATOM   1141 N N   . ASP A 1 155 ? 32.256  -14.879 -6.705  1.00 38.61 ?  155 ASP E N   1 
ATOM   1142 C CA  . ASP A 1 155 ? 32.536  -13.436 -6.689  1.00 38.43 ?  155 ASP E CA  1 
ATOM   1143 C C   . ASP A 1 155 ? 33.916  -13.112 -7.264  1.00 36.60 ?  155 ASP E C   1 
ATOM   1144 O O   . ASP A 1 155 ? 34.823  -12.656 -6.567  1.00 39.65 ?  155 ASP E O   1 
ATOM   1145 C CB  . ASP A 1 155 ? 32.406  -12.855 -5.274  1.00 41.35 ?  155 ASP E CB  1 
ATOM   1146 C CG  . ASP A 1 155 ? 30.998  -12.952 -4.726  1.00 45.57 ?  155 ASP E CG  1 
ATOM   1147 O OD1 . ASP A 1 155 ? 30.059  -13.059 -5.538  1.00 46.58 ?  155 ASP E OD1 1 
ATOM   1148 O OD2 . ASP A 1 155 ? 30.828  -12.899 -3.489  1.00 48.64 ?  155 ASP E OD2 1 
ATOM   1149 N N   . TYR A 1 156 ? 34.047  -13.331 -8.572  1.00 33.54 ?  156 TYR E N   1 
ATOM   1150 C CA  . TYR A 1 156 ? 35.286  -13.007 -9.267  1.00 33.00 ?  156 TYR E CA  1 
ATOM   1151 C C   . TYR A 1 156 ? 34.980  -12.201 -10.517 1.00 33.16 ?  156 TYR E C   1 
ATOM   1152 O O   . TYR A 1 156 ? 33.839  -12.147 -10.991 1.00 35.19 ?  156 TYR E O   1 
ATOM   1153 C CB  . TYR A 1 156 ? 36.097  -14.256 -9.635  1.00 30.60 ?  156 TYR E CB  1 
ATOM   1154 C CG  . TYR A 1 156 ? 35.450  -15.139 -10.688 1.00 31.18 ?  156 TYR E CG  1 
ATOM   1155 C CD1 . TYR A 1 156 ? 35.669  -14.910 -12.047 1.00 32.01 ?  156 TYR E CD1 1 
ATOM   1156 C CD2 . TYR A 1 156 ? 34.653  -16.219 -10.323 1.00 30.62 ?  156 TYR E CD2 1 
ATOM   1157 C CE1 . TYR A 1 156 ? 35.080  -15.710 -13.014 1.00 33.00 ?  156 TYR E CE1 1 
ATOM   1158 C CE2 . TYR A 1 156 ? 34.075  -17.042 -11.284 1.00 32.09 ?  156 TYR E CE2 1 
ATOM   1159 C CZ  . TYR A 1 156 ? 34.297  -16.779 -12.632 1.00 35.10 ?  156 TYR E CZ  1 
ATOM   1160 O OH  . TYR A 1 156 ? 33.724  -17.579 -13.602 1.00 34.62 ?  156 TYR E OH  1 
ATOM   1161 N N   . PHE A 1 157 ? 36.032  -11.574 -11.052 1.00 31.95 ?  157 PHE E N   1 
ATOM   1162 C CA  . PHE A 1 157 ? 35.923  -10.794 -12.268 1.00 33.29 ?  157 PHE E CA  1 
ATOM   1163 C C   . PHE A 1 157 ? 37.327  -10.545 -12.791 1.00 34.38 ?  157 PHE E C   1 
ATOM   1164 O O   . PHE A 1 157 ? 38.244  -10.323 -11.987 1.00 34.47 ?  157 PHE E O   1 
ATOM   1165 C CB  . PHE A 1 157 ? 35.200  -9.466  -12.019 1.00 32.80 ?  157 PHE E CB  1 
ATOM   1166 C CG  . PHE A 1 157 ? 34.940  -8.678  -13.273 1.00 34.77 ?  157 PHE E CG  1 
ATOM   1167 C CD1 . PHE A 1 157 ? 33.775  -8.873  -14.001 1.00 33.66 ?  157 PHE E CD1 1 
ATOM   1168 C CD2 . PHE A 1 157 ? 35.879  -7.764  -13.739 1.00 36.46 ?  157 PHE E CD2 1 
ATOM   1169 C CE1 . PHE A 1 157 ? 33.540  -8.151  -15.158 1.00 39.45 ?  157 PHE E CE1 1 
ATOM   1170 C CE2 . PHE A 1 157 ? 35.655  -7.048  -14.895 1.00 36.51 ?  157 PHE E CE2 1 
ATOM   1171 C CZ  . PHE A 1 157 ? 34.487  -7.236  -15.605 1.00 37.96 ?  157 PHE E CZ  1 
ATOM   1172 N N   . PRO A 1 158 ? 37.543  -10.611 -14.104 1.00 34.05 ?  158 PRO E N   1 
ATOM   1173 C CA  . PRO A 1 158 ? 36.581  -11.006 -15.137 1.00 33.54 ?  158 PRO E CA  1 
ATOM   1174 C C   . PRO A 1 158 ? 36.672  -12.495 -15.394 1.00 33.98 ?  158 PRO E C   1 
ATOM   1175 O O   . PRO A 1 158 ? 37.422  -13.194 -14.720 1.00 33.08 ?  158 PRO E O   1 
ATOM   1176 C CB  . PRO A 1 158 ? 37.043  -10.184 -16.347 1.00 34.70 ?  158 PRO E CB  1 
ATOM   1177 C CG  . PRO A 1 158 ? 38.559  -10.185 -16.194 1.00 32.50 ?  158 PRO E CG  1 
ATOM   1178 C CD  . PRO A 1 158 ? 38.827  -10.189 -14.696 1.00 33.02 ?  158 PRO E CD  1 
ATOM   1179 N N   . GLU A 1 159 ? 35.924  -13.016 -16.369 1.00 34.48 ?  159 GLU E N   1 
ATOM   1180 C CA  . GLU A 1 159 ? 36.214  -14.341 -16.896 1.00 35.08 ?  159 GLU E CA  1 
ATOM   1181 C C   . GLU A 1 159 ? 37.640  -14.369 -17.441 1.00 35.15 ?  159 GLU E C   1 
ATOM   1182 O O   . GLU A 1 159 ? 38.188  -13.326 -17.803 1.00 33.93 ?  159 GLU E O   1 
ATOM   1183 C CB  . GLU A 1 159 ? 35.234  -14.682 -18.016 1.00 36.89 ?  159 GLU E CB  1 
ATOM   1184 C CG  . GLU A 1 159 ? 33.782  -14.914 -17.637 1.00 37.28 ?  159 GLU E CG  1 
ATOM   1185 C CD  . GLU A 1 159 ? 33.491  -16.293 -17.054 1.00 38.62 ?  159 GLU E CD  1 
ATOM   1186 O OE1 . GLU A 1 159 ? 34.337  -16.892 -16.352 1.00 36.51 ?  159 GLU E OE1 1 
ATOM   1187 O OE2 . GLU A 1 159 ? 32.417  -16.825 -17.397 1.00 38.96 ?  159 GLU E OE2 1 
ATOM   1188 N N   . PRO A 1 160 ? 38.260  -15.555 -17.542 1.00 37.00 ?  160 PRO E N   1 
ATOM   1189 C CA  . PRO A 1 160 ? 37.781  -16.884 -17.155 1.00 33.68 ?  160 PRO E CA  1 
ATOM   1190 C C   . PRO A 1 160 ? 38.443  -17.452 -15.910 1.00 34.73 ?  160 PRO E C   1 
ATOM   1191 O O   . PRO A 1 160 ? 39.432  -16.936 -15.396 1.00 34.11 ?  160 PRO E O   1 
ATOM   1192 C CB  . PRO A 1 160 ? 38.159  -17.736 -18.373 1.00 33.52 ?  160 PRO E CB  1 
ATOM   1193 C CG  . PRO A 1 160 ? 39.471  -17.116 -18.852 1.00 35.99 ?  160 PRO E CG  1 
ATOM   1194 C CD  . PRO A 1 160 ? 39.492  -15.668 -18.341 1.00 35.06 ?  160 PRO E CD  1 
ATOM   1195 N N   . VAL A 1 161 ? 37.874  -18.561 -15.447 1.00 30.54 ?  161 VAL E N   1 
ATOM   1196 C CA  . VAL A 1 161 ? 38.455  -19.424 -14.427 1.00 32.90 ?  161 VAL E CA  1 
ATOM   1197 C C   . VAL A 1 161 ? 38.584  -20.814 -15.033 1.00 34.73 ?  161 VAL E C   1 
ATOM   1198 O O   . VAL A 1 161 ? 37.731  -21.234 -15.833 1.00 31.64 ?  161 VAL E O   1 
ATOM   1199 C CB  . VAL A 1 161 ? 37.581  -19.456 -13.152 1.00 36.96 ?  161 VAL E CB  1 
ATOM   1200 C CG1 . VAL A 1 161 ? 37.881  -20.680 -12.298 1.00 40.12 ?  161 VAL E CG1 1 
ATOM   1201 C CG2 . VAL A 1 161 ? 37.773  -18.194 -12.343 1.00 34.87 ?  161 VAL E CG2 1 
ATOM   1202 N N   . THR A 1 162 ? 39.655  -21.517 -14.669 1.00 33.55 ?  162 THR E N   1 
ATOM   1203 C CA  . THR A 1 162 ? 39.836  -22.927 -14.987 1.00 37.05 ?  162 THR E CA  1 
ATOM   1204 C C   . THR A 1 162 ? 39.791  -23.735 -13.697 1.00 36.13 ?  162 THR E C   1 
ATOM   1205 O O   . THR A 1 162 ? 40.285  -23.294 -12.654 1.00 35.88 ?  162 THR E O   1 
ATOM   1206 C CB  . THR A 1 162 ? 41.173  -23.172 -15.706 1.00 33.02 ?  162 THR E CB  1 
ATOM   1207 O OG1 . THR A 1 162 ? 42.221  -22.544 -14.971 1.00 39.66 ?  162 THR E OG1 1 
ATOM   1208 C CG2 . THR A 1 162 ? 41.156  -22.598 -17.111 1.00 34.94 ?  162 THR E CG2 1 
ATOM   1209 N N   . VAL A 1 163 ? 39.185  -24.912 -13.757 1.00 33.33 ?  163 VAL E N   1 
ATOM   1210 C CA  . VAL A 1 163 ? 39.050  -25.767 -12.587 1.00 34.47 ?  163 VAL E CA  1 
ATOM   1211 C C   . VAL A 1 163 ? 39.443  -27.172 -12.994 1.00 39.27 ?  163 VAL E C   1 
ATOM   1212 O O   . VAL A 1 163 ? 38.935  -27.697 -13.993 1.00 36.31 ?  163 VAL E O   1 
ATOM   1213 C CB  . VAL A 1 163 ? 37.619  -25.757 -12.013 1.00 35.10 ?  163 VAL E CB  1 
ATOM   1214 C CG1 . VAL A 1 163 ? 37.515  -26.710 -10.823 1.00 34.89 ?  163 VAL E CG1 1 
ATOM   1215 C CG2 . VAL A 1 163 ? 37.189  -24.351 -11.627 1.00 35.73 ?  163 VAL E CG2 1 
ATOM   1216 N N   . SER A 1 164 ? 40.361  -27.767 -12.244 1.00 36.27 ?  164 SER E N   1 
ATOM   1217 C CA  . SER A 1 164 ? 40.663  -29.179 -12.375 1.00 35.09 ?  164 SER E CA  1 
ATOM   1218 C C   . SER A 1 164 ? 40.462  -29.841 -11.021 1.00 36.85 ?  164 SER E C   1 
ATOM   1219 O O   . SER A 1 164 ? 40.257  -29.178 -9.999  1.00 37.01 ?  164 SER E O   1 
ATOM   1220 C CB  . SER A 1 164 ? 42.087  -29.407 -12.900 1.00 37.20 ?  164 SER E CB  1 
ATOM   1221 O OG  . SER A 1 164 ? 43.058  -29.049 -11.930 1.00 37.13 ?  164 SER E OG  1 
ATOM   1222 N N   . TRP A 1 165 ? 40.482  -31.167 -11.026 1.00 34.84 ?  165 TRP E N   1 
ATOM   1223 C CA  . TRP A 1 165 ? 40.335  -31.947 -9.808  1.00 36.26 ?  165 TRP E CA  1 
ATOM   1224 C C   . TRP A 1 165 ? 41.532  -32.877 -9.670  1.00 37.81 ?  165 TRP E C   1 
ATOM   1225 O O   . TRP A 1 165 ? 41.928  -33.533 -10.639 1.00 40.45 ?  165 TRP E O   1 
ATOM   1226 C CB  . TRP A 1 165 ? 39.017  -32.721 -9.821  1.00 36.65 ?  165 TRP E CB  1 
ATOM   1227 C CG  . TRP A 1 165 ? 37.839  -31.847 -9.556  1.00 35.49 ?  165 TRP E CG  1 
ATOM   1228 C CD1 . TRP A 1 165 ? 37.145  -31.089 -10.456 1.00 35.62 ?  165 TRP E CD1 1 
ATOM   1229 C CD2 . TRP A 1 165 ? 37.249  -31.599 -8.283  1.00 35.42 ?  165 TRP E CD2 1 
ATOM   1230 N NE1 . TRP A 1 165 ? 36.122  -30.407 -9.820  1.00 32.44 ?  165 TRP E NE1 1 
ATOM   1231 C CE2 . TRP A 1 165 ? 36.176  -30.699 -8.481  1.00 34.07 ?  165 TRP E CE2 1 
ATOM   1232 C CE3 . TRP A 1 165 ? 37.516  -32.059 -6.988  1.00 38.54 ?  165 TRP E CE3 1 
ATOM   1233 C CZ2 . TRP A 1 165 ? 35.379  -30.259 -7.436  1.00 34.04 ?  165 TRP E CZ2 1 
ATOM   1234 C CZ3 . TRP A 1 165 ? 36.720  -31.614 -5.952  1.00 38.24 ?  165 TRP E CZ3 1 
ATOM   1235 C CH2 . TRP A 1 165 ? 35.664  -30.726 -6.182  1.00 35.66 ?  165 TRP E CH2 1 
ATOM   1236 N N   . ASN A 1 166 ? 42.123  -32.902 -8.476  1.00 39.08 ?  166 ASN E N   1 
ATOM   1237 C CA  . ASN A 1 166 ? 43.304  -33.723 -8.206  1.00 42.22 ?  166 ASN E CA  1 
ATOM   1238 C C   . ASN A 1 166 ? 44.381  -33.510 -9.271  1.00 40.87 ?  166 ASN E C   1 
ATOM   1239 O O   . ASN A 1 166 ? 45.013  -34.457 -9.747  1.00 44.14 ?  166 ASN E O   1 
ATOM   1240 C CB  . ASN A 1 166 ? 42.918  -35.199 -8.090  1.00 39.22 ?  166 ASN E CB  1 
ATOM   1241 C CG  . ASN A 1 166 ? 42.063  -35.481 -6.860  1.00 42.77 ?  166 ASN E CG  1 
ATOM   1242 O OD1 . ASN A 1 166 ? 41.741  -34.572 -6.095  1.00 45.12 ?  166 ASN E OD1 1 
ATOM   1243 N ND2 . ASN A 1 166 ? 41.686  -36.742 -6.670  1.00 42.21 ?  166 ASN E ND2 1 
ATOM   1244 N N   . SER A 1 167 ? 44.572  -32.245 -9.660  1.00 40.99 ?  167 SER E N   1 
ATOM   1245 C CA  . SER A 1 167 ? 45.617  -31.829 -10.601 1.00 41.86 ?  167 SER E CA  1 
ATOM   1246 C C   . SER A 1 167 ? 45.448  -32.475 -11.971 1.00 43.98 ?  167 SER E C   1 
ATOM   1247 O O   . SER A 1 167 ? 46.428  -32.713 -12.673 1.00 45.24 ?  167 SER E O   1 
ATOM   1248 C CB  . SER A 1 167 ? 47.023  -32.114 -10.054 1.00 44.24 ?  167 SER E CB  1 
ATOM   1249 O OG  . SER A 1 167 ? 47.174  -31.622 -8.735  1.00 47.49 ?  167 SER E OG  1 
ATOM   1250 N N   . GLY A 1 168 ? 44.210  -32.761 -12.371 1.00 42.59 ?  168 GLY E N   1 
ATOM   1251 C CA  . GLY A 1 168 ? 43.963  -33.355 -13.663 1.00 43.06 ?  168 GLY E CA  1 
ATOM   1252 C C   . GLY A 1 168 ? 43.900  -34.865 -13.665 1.00 43.40 ?  168 GLY E C   1 
ATOM   1253 O O   . GLY A 1 168 ? 43.502  -35.453 -14.679 1.00 45.69 ?  168 GLY E O   1 
ATOM   1254 N N   . ALA A 1 169 ? 44.272  -35.514 -12.560 1.00 43.18 ?  169 ALA E N   1 
ATOM   1255 C CA  . ALA A 1 169 ? 44.180  -36.965 -12.480 1.00 44.56 ?  169 ALA E CA  1 
ATOM   1256 C C   . ALA A 1 169 ? 42.737  -37.455 -12.400 1.00 44.11 ?  169 ALA E C   1 
ATOM   1257 O O   . ALA A 1 169 ? 42.485  -38.633 -12.670 1.00 46.70 ?  169 ALA E O   1 
ATOM   1258 C CB  . ALA A 1 169 ? 44.967  -37.472 -11.273 1.00 43.95 ?  169 ALA E CB  1 
ATOM   1259 N N   . LEU A 1 170 ? 41.793  -36.589 -12.028 1.00 42.33 ?  170 LEU E N   1 
ATOM   1260 C CA  . LEU A 1 170 ? 40.380  -36.941 -11.910 1.00 41.69 ?  170 LEU E CA  1 
ATOM   1261 C C   . LEU A 1 170 ? 39.597  -36.170 -12.971 1.00 43.28 ?  170 LEU E C   1 
ATOM   1262 O O   . LEU A 1 170 ? 39.422  -34.949 -12.859 1.00 38.43 ?  170 LEU E O   1 
ATOM   1263 C CB  . LEU A 1 170 ? 39.866  -36.637 -10.505 1.00 40.13 ?  170 LEU E CB  1 
ATOM   1264 C CG  . LEU A 1 170 ? 38.363  -36.824 -10.259 1.00 42.11 ?  170 LEU E CG  1 
ATOM   1265 C CD1 . LEU A 1 170 ? 37.935  -38.247 -10.585 1.00 46.84 ?  170 LEU E CD1 1 
ATOM   1266 C CD2 . LEU A 1 170 ? 37.963  -36.453 -8.831  1.00 38.47 ?  170 LEU E CD2 1 
ATOM   1267 N N   . THR A 1 171 ? 39.130  -36.877 -14.001 1.00 41.26 ?  171 THR E N   1 
ATOM   1268 C CA  . THR A 1 171 ? 38.356  -36.251 -15.063 1.00 41.89 ?  171 THR E CA  1 
ATOM   1269 C C   . THR A 1 171 ? 36.970  -36.849 -15.256 1.00 40.92 ?  171 THR E C   1 
ATOM   1270 O O   . THR A 1 171 ? 36.051  -36.109 -15.608 1.00 39.46 ?  171 THR E O   1 
ATOM   1271 C CB  . THR A 1 171 ? 39.106  -36.324 -16.403 1.00 43.64 ?  171 THR E CB  1 
ATOM   1272 O OG1 . THR A 1 171 ? 39.432  -37.688 -16.693 1.00 43.39 ?  171 THR E OG1 1 
ATOM   1273 C CG2 . THR A 1 171 ? 40.392  -35.492 -16.352 1.00 43.60 ?  171 THR E CG2 1 
ATOM   1274 N N   . SER A 1 172 ? 36.785  -38.149 -15.026 1.00 41.61 ?  172 SER E N   1 
ATOM   1275 C CA  . SER A 1 172 ? 35.463  -38.739 -15.203 1.00 41.59 ?  172 SER E CA  1 
ATOM   1276 C C   . SER A 1 172 ? 34.523  -38.255 -14.106 1.00 40.74 ?  172 SER E C   1 
ATOM   1277 O O   . SER A 1 172 ? 34.882  -38.240 -12.926 1.00 46.43 ?  172 SER E O   1 
ATOM   1278 C CB  . SER A 1 172 ? 35.540  -40.268 -15.186 1.00 45.59 ?  172 SER E CB  1 
ATOM   1279 O OG  . SER A 1 172 ? 36.470  -40.721 -14.218 1.00 52.61 ?  172 SER E OG  1 
ATOM   1280 N N   . GLY A 1 173 ? 33.318  -37.857 -14.498 1.00 42.60 ?  173 GLY E N   1 
ATOM   1281 C CA  . GLY A 1 173 ? 32.334  -37.382 -13.550 1.00 40.95 ?  173 GLY E CA  1 
ATOM   1282 C C   . GLY A 1 173 ? 32.472  -35.929 -13.145 1.00 40.94 ?  173 GLY E C   1 
ATOM   1283 O O   . GLY A 1 173 ? 31.697  -35.465 -12.291 1.00 39.13 ?  173 GLY E O   1 
ATOM   1284 N N   . VAL A 1 174 ? 33.416  -35.186 -13.725 1.00 36.77 ?  174 VAL E N   1 
ATOM   1285 C CA  . VAL A 1 174 ? 33.595  -33.774 -13.396 1.00 34.96 ?  174 VAL E CA  1 
ATOM   1286 C C   . VAL A 1 174 ? 32.660  -32.934 -14.258 1.00 37.67 ?  174 VAL E C   1 
ATOM   1287 O O   . VAL A 1 174 ? 32.594  -33.116 -15.479 1.00 40.98 ?  174 VAL E O   1 
ATOM   1288 C CB  . VAL A 1 174 ? 35.055  -33.341 -13.609 1.00 37.60 ?  174 VAL E CB  1 
ATOM   1289 C CG1 . VAL A 1 174 ? 35.173  -31.822 -13.479 1.00 34.72 ?  174 VAL E CG1 1 
ATOM   1290 C CG2 . VAL A 1 174 ? 35.986  -34.061 -12.633 1.00 35.84 ?  174 VAL E CG2 1 
ATOM   1291 N N   . HIS A 1 175 ? 31.966  -31.980 -13.634 1.00 34.25 ?  175 HIS E N   1 
ATOM   1292 C CA  . HIS A 1 175 ? 31.118  -31.037 -14.355 1.00 34.88 ?  175 HIS E CA  1 
ATOM   1293 C C   . HIS A 1 175 ? 31.393  -29.637 -13.833 1.00 34.56 ?  175 HIS E C   1 
ATOM   1294 O O   . HIS A 1 175 ? 31.061  -29.320 -12.688 1.00 33.24 ?  175 HIS E O   1 
ATOM   1295 C CB  . HIS A 1 175 ? 29.642  -31.398 -14.196 1.00 38.27 ?  175 HIS E CB  1 
ATOM   1296 C CG  . HIS A 1 175 ? 29.331  -32.807 -14.592 1.00 40.42 ?  175 HIS E CG  1 
ATOM   1297 N ND1 . HIS A 1 175 ? 29.143  -33.186 -15.904 1.00 44.11 ?  175 HIS E ND1 1 
ATOM   1298 C CD2 . HIS A 1 175 ? 29.216  -33.936 -13.853 1.00 42.60 ?  175 HIS E CD2 1 
ATOM   1299 C CE1 . HIS A 1 175 ? 28.905  -34.484 -15.953 1.00 43.48 ?  175 HIS E CE1 1 
ATOM   1300 N NE2 . HIS A 1 175 ? 28.948  -34.965 -14.722 1.00 43.83 ?  175 HIS E NE2 1 
ATOM   1301 N N   . THR A 1 176 ? 31.980  -28.798 -14.669 1.00 34.20 ?  176 THR E N   1 
ATOM   1302 C CA  . THR A 1 176 ? 32.212  -27.404 -14.326 1.00 34.90 ?  176 THR E CA  1 
ATOM   1303 C C   . THR A 1 176 ? 31.237  -26.567 -15.136 1.00 34.33 ?  176 THR E C   1 
ATOM   1304 O O   . THR A 1 176 ? 31.205  -26.669 -16.367 1.00 40.36 ?  176 THR E O   1 
ATOM   1305 C CB  . THR A 1 176 ? 33.666  -27.015 -14.586 1.00 35.82 ?  176 THR E CB  1 
ATOM   1306 O OG1 . THR A 1 176 ? 34.509  -27.897 -13.833 1.00 34.88 ?  176 THR E OG1 1 
ATOM   1307 C CG2 . THR A 1 176 ? 33.929  -25.564 -14.176 1.00 32.89 ?  176 THR E CG2 1 
ATOM   1308 N N   . PHE A 1 177 ? 30.430  -25.762 -14.444 1.00 35.26 ?  177 PHE E N   1 
ATOM   1309 C CA  . PHE A 1 177 ? 29.294  -25.033 -14.989 1.00 33.49 ?  177 PHE E CA  1 
ATOM   1310 C C   . PHE A 1 177 ? 29.700  -23.674 -15.544 1.00 36.53 ?  177 PHE E C   1 
ATOM   1311 O O   . PHE A 1 177 ? 30.633  -23.040 -15.040 1.00 37.74 ?  177 PHE E O   1 
ATOM   1312 C CB  . PHE A 1 177 ? 28.233  -24.840 -13.917 1.00 35.98 ?  177 PHE E CB  1 
ATOM   1313 C CG  . PHE A 1 177 ? 27.494  -26.099 -13.591 1.00 34.29 ?  177 PHE E CG  1 
ATOM   1314 C CD1 . PHE A 1 177 ? 26.359  -26.447 -14.306 1.00 33.40 ?  177 PHE E CD1 1 
ATOM   1315 C CD2 . PHE A 1 177 ? 27.942  -26.940 -12.589 1.00 33.70 ?  177 PHE E CD2 1 
ATOM   1316 C CE1 . PHE A 1 177 ? 25.670  -27.616 -14.018 1.00 32.12 ?  177 PHE E CE1 1 
ATOM   1317 C CE2 . PHE A 1 177 ? 27.264  -28.119 -12.296 1.00 37.65 ?  177 PHE E CE2 1 
ATOM   1318 C CZ  . PHE A 1 177 ? 26.129  -28.454 -13.012 1.00 34.82 ?  177 PHE E CZ  1 
ATOM   1319 N N   . PRO A 1 178 ? 29.008  -23.220 -16.588 1.00 37.53 ?  178 PRO E N   1 
ATOM   1320 C CA  . PRO A 1 178 ? 29.196  -21.841 -17.043 1.00 37.25 ?  178 PRO E CA  1 
ATOM   1321 C C   . PRO A 1 178 ? 28.941  -20.880 -15.895 1.00 37.69 ?  178 PRO E C   1 
ATOM   1322 O O   . PRO A 1 178 ? 28.012  -21.067 -15.105 1.00 38.28 ?  178 PRO E O   1 
ATOM   1323 C CB  . PRO A 1 178 ? 28.148  -21.685 -18.152 1.00 35.73 ?  178 PRO E CB  1 
ATOM   1324 C CG  . PRO A 1 178 ? 27.889  -23.085 -18.617 1.00 37.54 ?  178 PRO E CG  1 
ATOM   1325 C CD  . PRO A 1 178 ? 27.991  -23.932 -17.383 1.00 36.31 ?  178 PRO E CD  1 
ATOM   1326 N N   . ALA A 1 179 ? 29.791  -19.863 -15.791 1.00 35.02 ?  179 ALA E N   1 
ATOM   1327 C CA  . ALA A 1 179 ? 29.613  -18.857 -14.755 1.00 37.48 ?  179 ALA E CA  1 
ATOM   1328 C C   . ALA A 1 179 ? 28.291  -18.130 -14.934 1.00 37.31 ?  179 ALA E C   1 
ATOM   1329 O O   . ALA A 1 179 ? 27.781  -17.981 -16.047 1.00 36.21 ?  179 ALA E O   1 
ATOM   1330 C CB  . ALA A 1 179 ? 30.762  -17.847 -14.787 1.00 36.11 ?  179 ALA E CB  1 
ATOM   1331 N N   . VAL A 1 180 ? 27.738  -17.655 -13.823 1.00 37.84 ?  180 VAL E N   1 
ATOM   1332 C CA  . VAL A 1 180 ? 26.570  -16.786 -13.855 1.00 37.47 ?  180 VAL E CA  1 
ATOM   1333 C C   . VAL A 1 180 ? 27.020  -15.387 -13.462 1.00 37.83 ?  180 VAL E C   1 
ATOM   1334 O O   . VAL A 1 180 ? 27.897  -15.217 -12.605 1.00 34.14 ?  180 VAL E O   1 
ATOM   1335 C CB  . VAL A 1 180 ? 25.432  -17.289 -12.941 1.00 39.94 ?  180 VAL E CB  1 
ATOM   1336 C CG1 . VAL A 1 180 ? 25.010  -18.709 -13.352 1.00 39.69 ?  180 VAL E CG1 1 
ATOM   1337 C CG2 . VAL A 1 180 ? 25.834  -17.245 -11.480 1.00 39.84 ?  180 VAL E CG2 1 
ATOM   1338 N N   . LEU A 1 181 ? 26.461  -14.393 -14.138 1.00 36.11 ?  181 LEU E N   1 
ATOM   1339 C CA  . LEU A 1 181 ? 26.696  -12.998 -13.790 1.00 41.77 ?  181 LEU E CA  1 
ATOM   1340 C C   . LEU A 1 181 ? 25.754  -12.615 -12.658 1.00 43.71 ?  181 LEU E C   1 
ATOM   1341 O O   . LEU A 1 181 ? 24.532  -12.745 -12.786 1.00 43.02 ?  181 LEU E O   1 
ATOM   1342 C CB  . LEU A 1 181 ? 26.474  -12.098 -15.005 1.00 40.43 ?  181 LEU E CB  1 
ATOM   1343 C CG  . LEU A 1 181 ? 26.907  -10.627 -14.940 1.00 43.87 ?  181 LEU E CG  1 
ATOM   1344 C CD1 . LEU A 1 181 ? 28.329  -10.460 -14.382 1.00 40.11 ?  181 LEU E CD1 1 
ATOM   1345 C CD2 . LEU A 1 181 ? 26.759  -9.972  -16.307 1.00 45.44 ?  181 LEU E CD2 1 
ATOM   1346 N N   . GLN A 1 182 ? 26.335  -12.152 -11.562 1.00 43.62 ?  182 GLN E N   1 
ATOM   1347 C CA  . GLN A 1 182 ? 25.522  -11.757 -10.391 1.00 45.17 ?  182 GLN E CA  1 
ATOM   1348 C C   . GLN A 1 182 ? 25.176  -10.271 -10.506 1.00 48.09 ?  182 GLN E C   1 
ATOM   1349 O O   . GLN A 1 182 ? 25.830  -9.561  -11.274 1.00 46.77 ?  182 GLN E O   1 
ATOM   1350 C CB  . GLN A 1 182 ? 26.263  -12.108 -9.101  1.00 44.64 ?  182 GLN E CB  1 
ATOM   1351 C CG  . GLN A 1 182 ? 26.469  -13.608 -8.934  1.00 44.34 ?  182 GLN E CG  1 
ATOM   1352 C CD  . GLN A 1 182 ? 27.490  -13.953 -7.878  1.00 46.07 ?  182 GLN E CD  1 
ATOM   1353 O OE1 . GLN A 1 182 ? 27.231  -14.741 -6.974  1.00 48.37 ?  182 GLN E OE1 1 
ATOM   1354 N NE2 . GLN A 1 182 ? 28.671  -13.370 -7.990  1.00 52.04 ?  182 GLN E NE2 1 
ATOM   1355 N N   . SER A 1 183 ? 24.169  -9.841  -9.756  1.00 48.67 ?  183 SER E N   1 
ATOM   1356 C CA  . SER A 1 183 ? 23.733  -8.451  -9.832  1.00 49.19 ?  183 SER E CA  1 
ATOM   1357 C C   . SER A 1 183 ? 24.836  -7.477  -9.435  1.00 49.39 ?  183 SER E C   1 
ATOM   1358 O O   . SER A 1 183 ? 24.805  -6.319  -9.861  1.00 52.26 ?  183 SER E O   1 
ATOM   1359 C CB  . SER A 1 183 ? 22.494  -8.234  -8.959  1.00 51.73 ?  183 SER E CB  1 
ATOM   1360 O OG  . SER A 1 183 ? 22.671  -8.798  -7.671  1.00 58.64 ?  183 SER E OG  1 
ATOM   1361 N N   . SER A 1 184 ? 25.821  -7.923  -8.655  1.00 49.36 ?  184 SER E N   1 
ATOM   1362 C CA  . SER A 1 184 ? 26.968  -7.081  -8.340  1.00 48.39 ?  184 SER E CA  1 
ATOM   1363 C C   . SER A 1 184 ? 27.866  -6.846  -9.544  1.00 46.28 ?  184 SER E C   1 
ATOM   1364 O O   . SER A 1 184 ? 28.710  -5.945  -9.499  1.00 46.99 ?  184 SER E O   1 
ATOM   1365 C CB  . SER A 1 184 ? 27.800  -7.705  -7.219  1.00 49.63 ?  184 SER E CB  1 
ATOM   1366 O OG  . SER A 1 184 ? 28.134  -9.056  -7.511  1.00 47.82 ?  184 SER E OG  1 
ATOM   1367 N N   . GLY A 1 185 ? 27.704  -7.629  -10.612 1.00 46.82 ?  185 GLY E N   1 
ATOM   1368 C CA  . GLY A 1 185 ? 28.619  -7.607  -11.734 1.00 44.06 ?  185 GLY E CA  1 
ATOM   1369 C C   . GLY A 1 185 ? 29.740  -8.613  -11.643 1.00 41.92 ?  185 GLY E C   1 
ATOM   1370 O O   . GLY A 1 185 ? 30.553  -8.709  -12.576 1.00 39.86 ?  185 GLY E O   1 
ATOM   1371 N N   . LEU A 1 186 ? 29.824  -9.349  -10.545 1.00 39.65 ?  186 LEU E N   1 
ATOM   1372 C CA  . LEU A 1 186 ? 30.825  -10.388 -10.391 1.00 37.78 ?  186 LEU E CA  1 
ATOM   1373 C C   . LEU A 1 186 ? 30.251  -11.721 -10.863 1.00 39.28 ?  186 LEU E C   1 
ATOM   1374 O O   . LEU A 1 186 ? 29.037  -11.891 -10.989 1.00 41.96 ?  186 LEU E O   1 
ATOM   1375 C CB  . LEU A 1 186 ? 31.272  -10.480 -8.934  1.00 38.21 ?  186 LEU E CB  1 
ATOM   1376 C CG  . LEU A 1 186 ? 31.764  -9.169  -8.310  1.00 39.84 ?  186 LEU E CG  1 
ATOM   1377 C CD1 . LEU A 1 186 ? 32.120  -9.380  -6.846  1.00 39.57 ?  186 LEU E CD1 1 
ATOM   1378 C CD2 . LEU A 1 186 ? 32.956  -8.604  -9.082  1.00 37.53 ?  186 LEU E CD2 1 
ATOM   1379 N N   . TYR A 1 187 ? 31.141  -12.668 -11.132 1.00 35.76 ?  187 TYR E N   1 
ATOM   1380 C CA  . TYR A 1 187 ? 30.753  -13.996 -11.584 1.00 33.80 ?  187 TYR E CA  1 
ATOM   1381 C C   . TYR A 1 187 ? 30.848  -14.998 -10.444 1.00 36.43 ?  187 TYR E C   1 
ATOM   1382 O O   . TYR A 1 187 ? 31.636  -14.831 -9.512  1.00 32.98 ?  187 TYR E O   1 
ATOM   1383 C CB  . TYR A 1 187 ? 31.659  -14.459 -12.728 1.00 33.69 ?  187 TYR E CB  1 
ATOM   1384 C CG  . TYR A 1 187 ? 31.498  -13.684 -14.016 1.00 36.11 ?  187 TYR E CG  1 
ATOM   1385 C CD1 . TYR A 1 187 ? 30.526  -14.028 -14.951 1.00 37.92 ?  187 TYR E CD1 1 
ATOM   1386 C CD2 . TYR A 1 187 ? 32.316  -12.598 -14.292 1.00 38.26 ?  187 TYR E CD2 1 
ATOM   1387 C CE1 . TYR A 1 187 ? 30.385  -13.316 -16.135 1.00 40.47 ?  187 TYR E CE1 1 
ATOM   1388 C CE2 . TYR A 1 187 ? 32.179  -11.871 -15.466 1.00 37.66 ?  187 TYR E CE2 1 
ATOM   1389 C CZ  . TYR A 1 187 ? 31.216  -12.234 -16.382 1.00 40.79 ?  187 TYR E CZ  1 
ATOM   1390 O OH  . TYR A 1 187 ? 31.092  -11.510 -17.547 1.00 40.81 ?  187 TYR E OH  1 
ATOM   1391 N N   . SER A 1 188 ? 30.047  -16.061 -10.538 1.00 33.46 ?  188 SER E N   1 
ATOM   1392 C CA  . SER A 1 188 ? 30.242  -17.249 -9.721  1.00 33.04 ?  188 SER E CA  1 
ATOM   1393 C C   . SER A 1 188 ? 29.998  -18.473 -10.581 1.00 33.89 ?  188 SER E C   1 
ATOM   1394 O O   . SER A 1 188 ? 29.187  -18.440 -11.509 1.00 33.45 ?  188 SER E O   1 
ATOM   1395 C CB  . SER A 1 188 ? 29.311  -17.297 -8.498  1.00 38.84 ?  188 SER E CB  1 
ATOM   1396 O OG  . SER A 1 188 ? 29.614  -16.252 -7.586  1.00 43.26 ?  188 SER E OG  1 
ATOM   1397 N N   . LEU A 1 189 ? 30.700  -19.555 -10.254 1.00 33.54 ?  189 LEU E N   1 
ATOM   1398 C CA  . LEU A 1 189 ? 30.440  -20.859 -10.843 1.00 35.05 ?  189 LEU E CA  1 
ATOM   1399 C C   . LEU A 1 189 ? 30.645  -21.936 -9.789  1.00 37.09 ?  189 LEU E C   1 
ATOM   1400 O O   . LEU A 1 189 ? 31.232  -21.710 -8.727  1.00 33.91 ?  189 LEU E O   1 
ATOM   1401 C CB  . LEU A 1 189 ? 31.342  -21.147 -12.048 1.00 34.13 ?  189 LEU E CB  1 
ATOM   1402 C CG  . LEU A 1 189 ? 32.843  -21.346 -11.834 1.00 33.58 ?  189 LEU E CG  1 
ATOM   1403 C CD1 . LEU A 1 189 ? 33.208  -22.780 -11.458 1.00 35.77 ?  189 LEU E CD1 1 
ATOM   1404 C CD2 . LEU A 1 189 ? 33.563  -20.969 -13.109 1.00 36.59 ?  189 LEU E CD2 1 
ATOM   1405 N N   . SER A 1 190 ? 30.183  -23.131 -10.109 1.00 34.91 ?  190 SER E N   1 
ATOM   1406 C CA  . SER A 1 190 ? 30.512  -24.298 -9.318  1.00 34.89 ?  190 SER E CA  1 
ATOM   1407 C C   . SER A 1 190 ? 31.116  -25.341 -10.235 1.00 36.18 ?  190 SER E C   1 
ATOM   1408 O O   . SER A 1 190 ? 30.855  -25.357 -11.444 1.00 37.39 ?  190 SER E O   1 
ATOM   1409 C CB  . SER A 1 190 ? 29.287  -24.883 -8.622  1.00 39.54 ?  190 SER E CB  1 
ATOM   1410 O OG  . SER A 1 190 ? 28.374  -25.356 -9.588  1.00 43.60 ?  190 SER E OG  1 
ATOM   1411 N N   . SER A 1 191 ? 31.931  -26.204 -9.645  1.00 33.39 ?  191 SER E N   1 
ATOM   1412 C CA  . SER A 1 191 ? 32.450  -27.386 -10.299 1.00 29.73 ?  191 SER E CA  1 
ATOM   1413 C C   . SER A 1 191 ? 32.165  -28.554 -9.370  1.00 34.85 ?  191 SER E C   1 
ATOM   1414 O O   . SER A 1 191 ? 32.460  -28.473 -8.176  1.00 35.23 ?  191 SER E O   1 
ATOM   1415 C CB  . SER A 1 191 ? 33.950  -27.250 -10.573 1.00 32.85 ?  191 SER E CB  1 
ATOM   1416 O OG  . SER A 1 191 ? 34.438  -28.428 -11.175 1.00 33.82 ?  191 SER E OG  1 
ATOM   1417 N N   . VAL A 1 192 ? 31.565  -29.620 -9.899  1.00 31.93 ?  192 VAL E N   1 
ATOM   1418 C CA  . VAL A 1 192 ? 31.152  -30.746 -9.072  1.00 33.45 ?  192 VAL E CA  1 
ATOM   1419 C C   . VAL A 1 192 ? 31.681  -32.036 -9.682  1.00 33.87 ?  192 VAL E C   1 
ATOM   1420 O O   . VAL A 1 192 ? 32.015  -32.103 -10.867 1.00 34.04 ?  192 VAL E O   1 
ATOM   1421 C CB  . VAL A 1 192 ? 29.616  -30.822 -8.922  1.00 33.65 ?  192 VAL E CB  1 
ATOM   1422 C CG1 . VAL A 1 192 ? 29.068  -29.563 -8.259  1.00 35.36 ?  192 VAL E CG1 1 
ATOM   1423 C CG2 . VAL A 1 192 ? 28.974  -31.028 -10.296 1.00 31.84 ?  192 VAL E CG2 1 
ATOM   1424 N N   . VAL A 1 193 ? 31.755  -33.073 -8.857  1.00 31.15 ?  193 VAL E N   1 
ATOM   1425 C CA  . VAL A 1 193 ? 32.134  -34.392 -9.346  1.00 33.79 ?  193 VAL E CA  1 
ATOM   1426 C C   . VAL A 1 193 ? 31.248  -35.430 -8.675  1.00 34.63 ?  193 VAL E C   1 
ATOM   1427 O O   . VAL A 1 193 ? 30.867  -35.280 -7.508  1.00 34.44 ?  193 VAL E O   1 
ATOM   1428 C CB  . VAL A 1 193 ? 33.636  -34.660 -9.110  1.00 37.06 ?  193 VAL E CB  1 
ATOM   1429 C CG1 . VAL A 1 193 ? 33.982  -34.444 -7.675  1.00 36.30 ?  193 VAL E CG1 1 
ATOM   1430 C CG2 . VAL A 1 193 ? 34.029  -36.061 -9.565  1.00 35.41 ?  193 VAL E CG2 1 
ATOM   1431 N N   . THR A 1 194 ? 30.883  -36.462 -9.425  1.00 34.62 ?  194 THR E N   1 
ATOM   1432 C CA  . THR A 1 194 ? 30.139  -37.589 -8.879  1.00 37.52 ?  194 THR E CA  1 
ATOM   1433 C C   . THR A 1 194 ? 31.116  -38.727 -8.634  1.00 40.70 ?  194 THR E C   1 
ATOM   1434 O O   . THR A 1 194 ? 31.926  -39.054 -9.510  1.00 40.79 ?  194 THR E O   1 
ATOM   1435 C CB  . THR A 1 194 ? 29.035  -38.042 -9.830  1.00 41.27 ?  194 THR E CB  1 
ATOM   1436 O OG1 . THR A 1 194 ? 29.596  -38.245 -11.129 1.00 41.28 ?  194 THR E OG1 1 
ATOM   1437 C CG2 . THR A 1 194 ? 27.938  -36.985 -9.902  1.00 37.81 ?  194 THR E CG2 1 
ATOM   1438 N N   . VAL A 1 195 ? 31.057  -39.307 -7.441  1.00 38.79 ?  195 VAL E N   1 
ATOM   1439 C CA  . VAL A 1 195 ? 32.011  -40.334 -7.028  1.00 42.47 ?  195 VAL E CA  1 
ATOM   1440 C C   . VAL A 1 195 ? 31.260  -41.422 -6.279  1.00 43.99 ?  195 VAL E C   1 
ATOM   1441 O O   . VAL A 1 195 ? 30.168  -41.182 -5.748  1.00 43.88 ?  195 VAL E O   1 
ATOM   1442 C CB  . VAL A 1 195 ? 33.126  -39.747 -6.136  1.00 44.05 ?  195 VAL E CB  1 
ATOM   1443 C CG1 . VAL A 1 195 ? 33.983  -38.760 -6.930  1.00 42.39 ?  195 VAL E CG1 1 
ATOM   1444 C CG2 . VAL A 1 195 ? 32.534  -39.076 -4.911  1.00 45.54 ?  195 VAL E CG2 1 
ATOM   1445 N N   . PRO A 1 196 ? 31.816  -42.635 -6.224  1.00 47.70 ?  196 PRO E N   1 
ATOM   1446 C CA  . PRO A 1 196 ? 31.196  -43.675 -5.390  1.00 49.87 ?  196 PRO E CA  1 
ATOM   1447 C C   . PRO A 1 196 ? 31.170  -43.234 -3.936  1.00 50.38 ?  196 PRO E C   1 
ATOM   1448 O O   . PRO A 1 196 ? 32.185  -42.793 -3.390  1.00 52.17 ?  196 PRO E O   1 
ATOM   1449 C CB  . PRO A 1 196 ? 32.117  -44.889 -5.585  1.00 51.08 ?  196 PRO E CB  1 
ATOM   1450 C CG  . PRO A 1 196 ? 32.882  -44.610 -6.805  1.00 49.08 ?  196 PRO E CG  1 
ATOM   1451 C CD  . PRO A 1 196 ? 33.043  -43.125 -6.874  1.00 47.40 ?  196 PRO E CD  1 
ATOM   1452 N N   . SER A 1 197 ? 29.999  -43.355 -3.302  1.00 50.28 ?  197 SER E N   1 
ATOM   1453 C CA  . SER A 1 197 ? 29.929  -43.097 -1.864  1.00 52.78 ?  197 SER E CA  1 
ATOM   1454 C C   . SER A 1 197 ? 30.916  -43.970 -1.091  1.00 56.08 ?  197 SER E C   1 
ATOM   1455 O O   . SER A 1 197 ? 31.351  -43.598 0.006   1.00 56.71 ?  197 SER E O   1 
ATOM   1456 C CB  . SER A 1 197 ? 28.504  -43.319 -1.356  1.00 52.62 ?  197 SER E CB  1 
ATOM   1457 O OG  . SER A 1 197 ? 28.196  -44.704 -1.294  1.00 58.82 ?  197 SER E OG  1 
ATOM   1458 N N   . SER A 1 198 ? 31.279  -45.126 -1.658  1.00 55.67 ?  198 SER E N   1 
ATOM   1459 C CA  . SER A 1 198 ? 32.334  -45.968 -1.096  1.00 56.91 ?  198 SER E CA  1 
ATOM   1460 C C   . SER A 1 198 ? 33.597  -45.167 -0.816  1.00 59.09 ?  198 SER E C   1 
ATOM   1461 O O   . SER A 1 198 ? 34.209  -45.298 0.250   1.00 65.09 ?  198 SER E O   1 
ATOM   1462 C CB  . SER A 1 198 ? 32.653  -47.100 -2.072  1.00 56.09 ?  198 SER E CB  1 
ATOM   1463 O OG  . SER A 1 198 ? 31.494  -47.854 -2.383  1.00 60.22 ?  198 SER E OG  1 
ATOM   1464 N N   . SER A 1 199 ? 33.988  -44.316 -1.760  1.00 60.36 ?  199 SER E N   1 
ATOM   1465 C CA  . SER A 1 199 ? 35.297  -43.677 -1.788  1.00 58.42 ?  199 SER E CA  1 
ATOM   1466 C C   . SER A 1 199 ? 35.400  -42.431 -0.917  1.00 59.98 ?  199 SER E C   1 
ATOM   1467 O O   . SER A 1 199 ? 36.479  -41.825 -0.871  1.00 60.56 ?  199 SER E O   1 
ATOM   1468 C CB  . SER A 1 199 ? 35.642  -43.307 -3.231  1.00 56.63 ?  199 SER E CB  1 
ATOM   1469 O OG  . SER A 1 199 ? 35.009  -42.088 -3.589  1.00 54.48 ?  199 SER E OG  1 
ATOM   1470 N N   . LEU A 1 200 ? 34.326  -42.029 -0.233  1.00 59.17 ?  200 LEU E N   1 
ATOM   1471 C CA  . LEU A 1 200 ? 34.340  -40.741 0.453   1.00 57.29 ?  200 LEU E CA  1 
ATOM   1472 C C   . LEU A 1 200 ? 35.329  -40.713 1.614   1.00 62.77 ?  200 LEU E C   1 
ATOM   1473 O O   . LEU A 1 200 ? 35.895  -39.655 1.917   1.00 65.87 ?  200 LEU E O   1 
ATOM   1474 C CB  . LEU A 1 200 ? 32.937  -40.389 0.937   1.00 60.43 ?  200 LEU E CB  1 
ATOM   1475 C CG  . LEU A 1 200 ? 31.916  -40.147 -0.175  1.00 57.95 ?  200 LEU E CG  1 
ATOM   1476 C CD1 . LEU A 1 200 ? 30.553  -39.824 0.411   1.00 56.84 ?  200 LEU E CD1 1 
ATOM   1477 C CD2 . LEU A 1 200 ? 32.390  -39.035 -1.099  1.00 55.48 ?  200 LEU E CD2 1 
ATOM   1478 N N   . GLY A 1 201 ? 35.560  -41.847 2.267   1.00 64.81 ?  201 GLY E N   1 
ATOM   1479 C CA  . GLY A 1 201 ? 36.501  -41.877 3.368   1.00 65.89 ?  201 GLY E CA  1 
ATOM   1480 C C   . GLY A 1 201 ? 37.919  -42.206 2.954   1.00 64.89 ?  201 GLY E C   1 
ATOM   1481 O O   . GLY A 1 201 ? 38.871  -41.834 3.644   1.00 66.78 ?  201 GLY E O   1 
ATOM   1482 N N   . THR A 1 202 ? 38.070  -42.894 1.821   1.00 63.90 ?  202 THR E N   1 
ATOM   1483 C CA  . THR A 1 202 ? 39.361  -43.414 1.380   1.00 63.41 ?  202 THR E CA  1 
ATOM   1484 C C   . THR A 1 202 ? 40.114  -42.442 0.477   1.00 61.78 ?  202 THR E C   1 
ATOM   1485 O O   . THR A 1 202 ? 41.315  -42.226 0.657   1.00 60.08 ?  202 THR E O   1 
ATOM   1486 C CB  . THR A 1 202 ? 39.159  -44.748 0.651   1.00 64.22 ?  202 THR E CB  1 
ATOM   1487 O OG1 . THR A 1 202 ? 38.632  -45.717 1.565   1.00 70.74 ?  202 THR E OG1 1 
ATOM   1488 C CG2 . THR A 1 202 ? 40.476  -45.253 0.066   1.00 62.00 ?  202 THR E CG2 1 
ATOM   1489 N N   . GLN A 1 203 ? 39.430  -41.862 -0.503  1.00 59.44 ?  203 GLN E N   1 
ATOM   1490 C CA  . GLN A 1 203 ? 40.072  -41.025 -1.506  1.00 54.79 ?  203 GLN E CA  1 
ATOM   1491 C C   . GLN A 1 203 ? 39.968  -39.552 -1.129  1.00 53.93 ?  203 GLN E C   1 
ATOM   1492 O O   . GLN A 1 203 ? 38.920  -39.087 -0.672  1.00 54.73 ?  203 GLN E O   1 
ATOM   1493 C CB  . GLN A 1 203 ? 39.430  -41.264 -2.874  1.00 54.60 ?  203 GLN E CB  1 
ATOM   1494 C CG  . GLN A 1 203 ? 39.913  -40.322 -3.957  1.00 51.86 ?  203 GLN E CG  1 
ATOM   1495 C CD  . GLN A 1 203 ? 41.192  -40.786 -4.597  1.00 52.45 ?  203 GLN E CD  1 
ATOM   1496 O OE1 . GLN A 1 203 ? 41.278  -41.912 -5.078  1.00 58.57 ?  203 GLN E OE1 1 
ATOM   1497 N NE2 . GLN A 1 203 ? 42.197  -39.919 -4.613  1.00 52.82 ?  203 GLN E NE2 1 
ATOM   1498 N N   . THR A 1 204 ? 41.057  -38.816 -1.329  1.00 49.85 ?  204 THR E N   1 
ATOM   1499 C CA  . THR A 1 204 ? 41.039  -37.379 -1.108  1.00 50.55 ?  204 THR E CA  1 
ATOM   1500 C C   . THR A 1 204 ? 40.640  -36.664 -2.394  1.00 46.13 ?  204 THR E C   1 
ATOM   1501 O O   . THR A 1 204 ? 40.995  -37.092 -3.498  1.00 43.74 ?  204 THR E O   1 
ATOM   1502 C CB  . THR A 1 204 ? 42.397  -36.870 -0.620  1.00 54.70 ?  204 THR E CB  1 
ATOM   1503 O OG1 . THR A 1 204 ? 43.236  -36.585 -1.744  1.00 57.53 ?  204 THR E OG1 1 
ATOM   1504 C CG2 . THR A 1 204 ? 43.072  -37.909 0.269   1.00 52.10 ?  204 THR E CG2 1 
ATOM   1505 N N   . TYR A 1 205 ? 39.887  -35.578 -2.245  1.00 44.73 ?  205 TYR E N   1 
ATOM   1506 C CA  . TYR A 1 205 ? 39.363  -34.834 -3.382  1.00 42.18 ?  205 TYR E CA  1 
ATOM   1507 C C   . TYR A 1 205 ? 39.733  -33.370 -3.219  1.00 43.14 ?  205 TYR E C   1 
ATOM   1508 O O   . TYR A 1 205 ? 39.340  -32.733 -2.236  1.00 42.27 ?  205 TYR E O   1 
ATOM   1509 C CB  . TYR A 1 205 ? 37.846  -35.004 -3.496  1.00 42.47 ?  205 TYR E CB  1 
ATOM   1510 C CG  . TYR A 1 205 ? 37.449  -36.397 -3.918  1.00 41.62 ?  205 TYR E CG  1 
ATOM   1511 C CD1 . TYR A 1 205 ? 37.654  -36.832 -5.222  1.00 41.47 ?  205 TYR E CD1 1 
ATOM   1512 C CD2 . TYR A 1 205 ? 36.890  -37.286 -3.009  1.00 42.56 ?  205 TYR E CD2 1 
ATOM   1513 C CE1 . TYR A 1 205 ? 37.303  -38.115 -5.610  1.00 44.15 ?  205 TYR E CE1 1 
ATOM   1514 C CE2 . TYR A 1 205 ? 36.532  -38.566 -3.390  1.00 44.24 ?  205 TYR E CE2 1 
ATOM   1515 C CZ  . TYR A 1 205 ? 36.741  -38.976 -4.690  1.00 46.88 ?  205 TYR E CZ  1 
ATOM   1516 O OH  . TYR A 1 205 ? 36.388  -40.254 -5.070  1.00 45.18 ?  205 TYR E OH  1 
ATOM   1517 N N   . ILE A 1 206 ? 40.504  -32.849 -4.171  1.00 40.84 ?  206 ILE E N   1 
ATOM   1518 C CA  . ILE A 1 206 ? 40.957  -31.465 -4.161  1.00 42.98 ?  206 ILE E CA  1 
ATOM   1519 C C   . ILE A 1 206 ? 40.597  -30.819 -5.488  1.00 39.54 ?  206 ILE E C   1 
ATOM   1520 O O   . ILE A 1 206 ? 40.898  -31.365 -6.555  1.00 39.90 ?  206 ILE E O   1 
ATOM   1521 C CB  . ILE A 1 206 ? 42.475  -31.363 -3.906  1.00 42.77 ?  206 ILE E CB  1 
ATOM   1522 C CG1 . ILE A 1 206 ? 42.902  -32.355 -2.819  1.00 44.82 ?  206 ILE E CG1 1 
ATOM   1523 C CG2 . ILE A 1 206 ? 42.875  -29.929 -3.595  1.00 43.39 ?  206 ILE E CG2 1 
ATOM   1524 C CD1 . ILE A 1 206 ? 44.391  -32.325 -2.520  1.00 47.27 ?  206 ILE E CD1 1 
ATOM   1525 N N   . CYS A 1 207 ? 39.966  -29.656 -5.426  1.00 38.45 ?  207 CYS E N   1 
ATOM   1526 C CA  . CYS A 1 207 ? 39.703  -28.871 -6.623  1.00 37.22 ?  207 CYS E CA  1 
ATOM   1527 C C   . CYS A 1 207 ? 40.781  -27.802 -6.766  1.00 37.88 ?  207 CYS E C   1 
ATOM   1528 O O   . CYS A 1 207 ? 41.148  -27.148 -5.785  1.00 39.45 ?  207 CYS E O   1 
ATOM   1529 C CB  . CYS A 1 207 ? 38.308  -28.246 -6.575  1.00 37.13 ?  207 CYS E CB  1 
ATOM   1530 S SG  . CYS A 1 207 ? 38.111  -26.880 -5.424  1.00 43.80 ?  207 CYS E SG  1 
ATOM   1531 N N   . ASN A 1 208 ? 41.295  -27.649 -7.980  1.00 38.28 ?  208 ASN E N   1 
ATOM   1532 C CA  . ASN A 1 208 ? 42.366  -26.710 -8.304  1.00 35.94 ?  208 ASN E CA  1 
ATOM   1533 C C   . ASN A 1 208 ? 41.753  -25.600 -9.140  1.00 37.75 ?  208 ASN E C   1 
ATOM   1534 O O   . ASN A 1 208 ? 41.323  -25.837 -10.272 1.00 38.39 ?  208 ASN E O   1 
ATOM   1535 C CB  . ASN A 1 208 ? 43.476  -27.401 -9.086  1.00 38.84 ?  208 ASN E CB  1 
ATOM   1536 C CG  . ASN A 1 208 ? 43.740  -28.796 -8.595  1.00 39.61 ?  208 ASN E CG  1 
ATOM   1537 O OD1 . ASN A 1 208 ? 43.580  -29.757 -9.339  1.00 42.60 ?  208 ASN E OD1 1 
ATOM   1538 N ND2 . ASN A 1 208 ? 44.186  -28.919 -7.351  1.00 42.59 ?  208 ASN E ND2 1 
ATOM   1539 N N   . VAL A 1 209 ? 41.724  -24.392 -8.599  1.00 32.72 ?  209 VAL E N   1 
ATOM   1540 C CA  . VAL A 1 209 ? 41.061  -23.263 -9.234  1.00 33.63 ?  209 VAL E CA  1 
ATOM   1541 C C   . VAL A 1 209 ? 42.118  -22.248 -9.640  1.00 34.65 ?  209 VAL E C   1 
ATOM   1542 O O   . VAL A 1 209 ? 42.956  -21.860 -8.820  1.00 35.76 ?  209 VAL E O   1 
ATOM   1543 C CB  . VAL A 1 209 ? 40.031  -22.618 -8.293  1.00 35.48 ?  209 VAL E CB  1 
ATOM   1544 C CG1 . VAL A 1 209 ? 39.434  -21.381 -8.944  1.00 33.18 ?  209 VAL E CG1 1 
ATOM   1545 C CG2 . VAL A 1 209 ? 38.967  -23.634 -7.899  1.00 36.14 ?  209 VAL E CG2 1 
ATOM   1546 N N   . ASN A 1 210 ? 42.068  -21.805 -10.893 1.00 32.08 ?  210 ASN E N   1 
ATOM   1547 C CA  . ASN A 1 210 ? 43.033  -20.843 -11.411 1.00 33.54 ?  210 ASN E CA  1 
ATOM   1548 C C   . ASN A 1 210 ? 42.259  -19.681 -12.010 1.00 35.74 ?  210 ASN E C   1 
ATOM   1549 O O   . ASN A 1 210 ? 41.412  -19.885 -12.889 1.00 34.08 ?  210 ASN E O   1 
ATOM   1550 C CB  . ASN A 1 210 ? 43.958  -21.502 -12.448 1.00 34.25 ?  210 ASN E CB  1 
ATOM   1551 C CG  . ASN A 1 210 ? 45.005  -20.541 -13.018 1.00 37.52 ?  210 ASN E CG  1 
ATOM   1552 O OD1 . ASN A 1 210 ? 45.229  -19.448 -12.496 1.00 39.93 ?  210 ASN E OD1 1 
ATOM   1553 N ND2 . ASN A 1 210 ? 45.677  -20.974 -14.084 1.00 42.18 ?  210 ASN E ND2 1 
ATOM   1554 N N   . HIS A 1 211 ? 42.513  -18.474 -11.503 1.00 33.60 ?  211 HIS E N   1 
ATOM   1555 C CA  . HIS A 1 211 ? 41.942  -17.239 -12.042 1.00 31.36 ?  211 HIS E CA  1 
ATOM   1556 C C   . HIS A 1 211 ? 43.106  -16.326 -12.405 1.00 35.42 ?  211 HIS E C   1 
ATOM   1557 O O   . HIS A 1 211 ? 43.556  -15.535 -11.575 1.00 33.86 ?  211 HIS E O   1 
ATOM   1558 C CB  . HIS A 1 211 ? 41.012  -16.543 -11.059 1.00 31.20 ?  211 HIS E CB  1 
ATOM   1559 C CG  . HIS A 1 211 ? 40.364  -15.311 -11.610 1.00 32.04 ?  211 HIS E CG  1 
ATOM   1560 N ND1 . HIS A 1 211 ? 40.454  -14.082 -10.987 1.00 32.17 ?  211 HIS E ND1 1 
ATOM   1561 C CD2 . HIS A 1 211 ? 39.590  -15.120 -12.707 1.00 29.83 ?  211 HIS E CD2 1 
ATOM   1562 C CE1 . HIS A 1 211 ? 39.776  -13.187 -11.684 1.00 32.77 ?  211 HIS E CE1 1 
ATOM   1563 N NE2 . HIS A 1 211 ? 39.240  -13.790 -12.731 1.00 33.59 ?  211 HIS E NE2 1 
ATOM   1564 N N   . LYS A 1 212 ? 43.555  -16.421 -13.654 1.00 34.70 ?  212 LYS E N   1 
ATOM   1565 C CA  . LYS A 1 212 ? 44.749  -15.691 -14.087 1.00 38.15 ?  212 LYS E CA  1 
ATOM   1566 C C   . LYS A 1 212 ? 44.623  -14.172 -13.970 1.00 37.05 ?  212 LYS E C   1 
ATOM   1567 O O   . LYS A 1 212 ? 45.616  -13.532 -13.577 1.00 42.72 ?  212 LYS E O   1 
ATOM   1568 C CB  . LYS A 1 212 ? 45.086  -16.100 -15.529 1.00 38.34 ?  212 LYS E CB  1 
ATOM   1569 C CG  . LYS A 1 212 ? 46.366  -15.506 -16.122 1.00 47.38 ?  212 LYS E CG  1 
ATOM   1570 C CD  . LYS A 1 212 ? 47.545  -16.482 -15.941 1.00 51.58 ?  212 LYS E CD  1 
ATOM   1571 C CE  . LYS A 1 212 ? 48.901  -15.780 -15.867 1.00 52.93 ?  212 LYS E CE  1 
ATOM   1572 N NZ  . LYS A 1 212 ? 49.501  -15.568 -17.220 1.00 58.55 ?  212 LYS E NZ  1 
ATOM   1573 N N   . PRO A 1 213 ? 43.487  -13.535 -14.285 1.00 35.80 ?  213 PRO E N   1 
ATOM   1574 C CA  . PRO A 1 213 ? 43.444  -12.065 -14.201 1.00 39.04 ?  213 PRO E CA  1 
ATOM   1575 C C   . PRO A 1 213 ? 43.786  -11.504 -12.829 1.00 39.45 ?  213 PRO E C   1 
ATOM   1576 O O   . PRO A 1 213 ? 44.250  -10.362 -12.748 1.00 39.11 ?  213 PRO E O   1 
ATOM   1577 C CB  . PRO A 1 213 ? 41.998  -11.741 -14.601 1.00 37.33 ?  213 PRO E CB  1 
ATOM   1578 C CG  . PRO A 1 213 ? 41.626  -12.841 -15.523 1.00 36.06 ?  213 PRO E CG  1 
ATOM   1579 C CD  . PRO A 1 213 ? 42.270  -14.066 -14.938 1.00 35.89 ?  213 PRO E CD  1 
ATOM   1580 N N   . SER A 1 214 ? 43.568  -12.262 -11.752 1.00 38.26 ?  214 SER E N   1 
ATOM   1581 C CA  . SER A 1 214 ? 43.869  -11.823 -10.394 1.00 35.57 ?  214 SER E CA  1 
ATOM   1582 C C   . SER A 1 214 ? 45.064  -12.539 -9.783  1.00 38.71 ?  214 SER E C   1 
ATOM   1583 O O   . SER A 1 214 ? 45.333  -12.349 -8.593  1.00 37.35 ?  214 SER E O   1 
ATOM   1584 C CB  . SER A 1 214 ? 42.646  -12.028 -9.498  1.00 36.55 ?  214 SER E CB  1 
ATOM   1585 O OG  . SER A 1 214 ? 42.411  -13.412 -9.282  1.00 34.39 ?  214 SER E OG  1 
ATOM   1586 N N   . ASN A 1 215 ? 45.776  -13.365 -10.554 1.00 37.08 ?  215 ASN E N   1 
ATOM   1587 C CA  . ASN A 1 215 ? 46.852  -14.213 -10.040 1.00 40.65 ?  215 ASN E CA  1 
ATOM   1588 C C   . ASN A 1 215 ? 46.400  -15.024 -8.831  1.00 41.06 ?  215 ASN E C   1 
ATOM   1589 O O   . ASN A 1 215 ? 47.062  -15.053 -7.788  1.00 39.80 ?  215 ASN E O   1 
ATOM   1590 C CB  . ASN A 1 215 ? 48.092  -13.390 -9.700  1.00 39.93 ?  215 ASN E CB  1 
ATOM   1591 C CG  . ASN A 1 215 ? 48.709  -12.763 -10.918 1.00 43.83 ?  215 ASN E CG  1 
ATOM   1592 O OD1 . ASN A 1 215 ? 49.077  -13.460 -11.862 1.00 45.80 ?  215 ASN E OD1 1 
ATOM   1593 N ND2 . ASN A 1 215 ? 48.837  -11.442 -10.909 1.00 44.15 ?  215 ASN E ND2 1 
ATOM   1594 N N   . THR A 1 216 ? 45.255  -15.693 -8.977  1.00 36.93 ?  216 THR E N   1 
ATOM   1595 C CA  . THR A 1 216 ? 44.720  -16.573 -7.943  1.00 36.31 ?  216 THR E CA  1 
ATOM   1596 C C   . THR A 1 216 ? 44.853  -18.024 -8.386  1.00 38.85 ?  216 THR E C   1 
ATOM   1597 O O   . THR A 1 216 ? 44.325  -18.414 -9.437  1.00 38.33 ?  216 THR E O   1 
ATOM   1598 C CB  . THR A 1 216 ? 43.257  -16.259 -7.635  1.00 38.13 ?  216 THR E CB  1 
ATOM   1599 O OG1 . THR A 1 216 ? 43.134  -14.892 -7.226  1.00 39.82 ?  216 THR E OG1 1 
ATOM   1600 C CG2 . THR A 1 216 ? 42.758  -17.151 -6.504  1.00 37.56 ?  216 THR E CG2 1 
ATOM   1601 N N   . LYS A 1 217 ? 45.545  -18.820 -7.578  1.00 35.47 ?  217 LYS E N   1 
ATOM   1602 C CA  . LYS A 1 217 ? 45.572  -20.267 -7.729  1.00 39.12 ?  217 LYS E CA  1 
ATOM   1603 C C   . LYS A 1 217 ? 45.277  -20.859 -6.366  1.00 41.82 ?  217 LYS E C   1 
ATOM   1604 O O   . LYS A 1 217 ? 46.038  -20.636 -5.419  1.00 39.68 ?  217 LYS E O   1 
ATOM   1605 C CB  . LYS A 1 217 ? 46.918  -20.774 -8.252  1.00 40.00 ?  217 LYS E CB  1 
ATOM   1606 C CG  . LYS A 1 217 ? 47.270  -20.327 -9.657  1.00 40.54 ?  217 LYS E CG  1 
ATOM   1607 C CD  . LYS A 1 217 ? 48.490  -21.094 -10.162 1.00 41.39 ?  217 LYS E CD  1 
ATOM   1608 C CE  . LYS A 1 217 ? 48.615  -20.977 -11.672 1.00 42.35 ?  217 LYS E CE  1 
ATOM   1609 N NZ  . LYS A 1 217 ? 50.025  -21.110 -12.127 1.00 46.23 ?  217 LYS E NZ  1 
ATOM   1610 N N   . VAL A 1 218 ? 44.172  -21.597 -6.263  1.00 36.10 ?  218 VAL E N   1 
ATOM   1611 C CA  . VAL A 1 218 ? 43.724  -22.181 -5.005  1.00 39.43 ?  218 VAL E CA  1 
ATOM   1612 C C   . VAL A 1 218 ? 43.546  -23.679 -5.197  1.00 40.77 ?  218 VAL E C   1 
ATOM   1613 O O   . VAL A 1 218 ? 43.014  -24.118 -6.221  1.00 37.76 ?  218 VAL E O   1 
ATOM   1614 C CB  . VAL A 1 218 ? 42.412  -21.543 -4.520  1.00 41.45 ?  218 VAL E CB  1 
ATOM   1615 C CG1 . VAL A 1 218 ? 42.030  -22.108 -3.171  1.00 42.41 ?  218 VAL E CG1 1 
ATOM   1616 C CG2 . VAL A 1 218 ? 42.558  -20.038 -4.426  1.00 38.30 ?  218 VAL E CG2 1 
ATOM   1617 N N   . ASP A 1 219 ? 44.024  -24.455 -4.229  1.00 40.52 ?  219 ASP E N   1 
ATOM   1618 C CA  . ASP A 1 219 ? 43.625  -25.845 -4.062  1.00 43.14 ?  219 ASP E CA  1 
ATOM   1619 C C   . ASP A 1 219 ? 42.761  -25.935 -2.818  1.00 46.69 ?  219 ASP E C   1 
ATOM   1620 O O   . ASP A 1 219 ? 43.100  -25.363 -1.778  1.00 47.65 ?  219 ASP E O   1 
ATOM   1621 C CB  . ASP A 1 219 ? 44.831  -26.780 -3.961  1.00 43.59 ?  219 ASP E CB  1 
ATOM   1622 C CG  . ASP A 1 219 ? 45.819  -26.567 -5.076  1.00 48.74 ?  219 ASP E CG  1 
ATOM   1623 O OD1 . ASP A 1 219 ? 45.383  -26.512 -6.245  1.00 53.11 ?  219 ASP E OD1 1 
ATOM   1624 O OD2 . ASP A 1 219 ? 47.037  -26.462 -4.788  1.00 57.76 ?  219 ASP E OD2 1 
ATOM   1625 N N   . LYS A 1 220 ? 41.628  -26.615 -2.934  1.00 41.12 ?  220 LYS E N   1 
ATOM   1626 C CA  . LYS A 1 220 ? 40.712  -26.749 -1.815  1.00 43.31 ?  220 LYS E CA  1 
ATOM   1627 C C   . LYS A 1 220 ? 40.408  -28.224 -1.625  1.00 45.15 ?  220 LYS E C   1 
ATOM   1628 O O   . LYS A 1 220 ? 39.953  -28.894 -2.556  1.00 43.31 ?  220 LYS E O   1 
ATOM   1629 C CB  . LYS A 1 220 ? 39.427  -25.952 -2.046  1.00 44.76 ?  220 LYS E CB  1 
ATOM   1630 C CG  . LYS A 1 220 ? 38.612  -25.757 -0.788  1.00 45.90 ?  220 LYS E CG  1 
ATOM   1631 C CD  . LYS A 1 220 ? 39.301  -24.742 0.115   1.00 47.00 ?  220 LYS E CD  1 
ATOM   1632 C CE  . LYS A 1 220 ? 38.634  -24.682 1.472   1.00 51.93 ?  220 LYS E CE  1 
ATOM   1633 N NZ  . LYS A 1 220 ? 38.673  -23.306 2.037   1.00 54.96 ?  220 LYS E NZ  1 
ATOM   1634 N N   . LYS A 1 221 ? 40.687  -28.723 -0.429  1.00 45.47 ?  221 LYS E N   1 
ATOM   1635 C CA  . LYS A 1 221 ? 40.383  -30.095 -0.063  1.00 47.03 ?  221 LYS E CA  1 
ATOM   1636 C C   . LYS A 1 221 ? 38.924  -30.182 0.368   1.00 47.45 ?  221 LYS E C   1 
ATOM   1637 O O   . LYS A 1 221 ? 38.493  -29.457 1.273   1.00 47.94 ?  221 LYS E O   1 
ATOM   1638 C CB  . LYS A 1 221 ? 41.336  -30.525 1.046   1.00 51.78 ?  221 LYS E CB  1 
ATOM   1639 C CG  . LYS A 1 221 ? 41.354  -31.990 1.422   1.00 53.09 ?  221 LYS E CG  1 
ATOM   1640 C CD  . LYS A 1 221 ? 41.824  -32.078 2.871   1.00 58.97 ?  221 LYS E CD  1 
ATOM   1641 C CE  . LYS A 1 221 ? 43.249  -31.505 3.000   1.00 62.97 ?  221 LYS E CE  1 
ATOM   1642 N NZ  . LYS A 1 221 ? 43.482  -30.733 4.264   1.00 66.71 ?  221 LYS E NZ  1 
ATOM   1643 N N   . VAL A 1 222 ? 38.158  -31.039 -0.298  1.00 47.19 ?  222 VAL E N   1 
ATOM   1644 C CA  . VAL A 1 222 ? 36.725  -31.186 -0.055  1.00 47.96 ?  222 VAL E CA  1 
ATOM   1645 C C   . VAL A 1 222 ? 36.510  -32.488 0.705   1.00 48.83 ?  222 VAL E C   1 
ATOM   1646 O O   . VAL A 1 222 ? 36.726  -33.578 0.164   1.00 50.73 ?  222 VAL E O   1 
ATOM   1647 C CB  . VAL A 1 222 ? 35.914  -31.167 -1.360  1.00 43.78 ?  222 VAL E CB  1 
ATOM   1648 C CG1 . VAL A 1 222 ? 34.427  -31.168 -1.050  1.00 42.74 ?  222 VAL E CG1 1 
ATOM   1649 C CG2 . VAL A 1 222 ? 36.291  -29.951 -2.199  1.00 40.46 ?  222 VAL E CG2 1 
ATOM   1650 N N   . GLU A 1 223 ? 36.059  -32.377 1.950   1.00 53.51 ?  223 GLU E N   1 
ATOM   1651 C CA  . GLU A 1 223 ? 35.906  -33.518 2.836   1.00 55.87 ?  223 GLU E CA  1 
ATOM   1652 C C   . GLU A 1 223 ? 34.442  -33.725 3.205   1.00 55.69 ?  223 GLU E C   1 
ATOM   1653 O O   . GLU A 1 223 ? 33.671  -32.763 3.262   1.00 55.94 ?  223 GLU E O   1 
ATOM   1654 C CB  . GLU A 1 223 ? 36.730  -33.312 4.109   1.00 57.89 ?  223 GLU E CB  1 
ATOM   1655 C CG  . GLU A 1 223 ? 38.217  -33.264 3.848   1.00 59.97 ?  223 GLU E CG  1 
ATOM   1656 C CD  . GLU A 1 223 ? 39.013  -33.812 5.003   1.00 64.68 ?  223 GLU E CD  1 
ATOM   1657 O OE1 . GLU A 1 223 ? 38.545  -34.791 5.628   1.00 68.44 ?  223 GLU E OE1 1 
ATOM   1658 O OE2 . GLU A 1 223 ? 40.092  -33.257 5.294   1.00 69.44 ?  223 GLU E OE2 1 
ATOM   1659 N N   . PRO A 1 224 ? 34.028  -34.978 3.460   1.00 59.61 ?  224 PRO E N   1 
ATOM   1660 C CA  . PRO A 1 224 ? 32.655  -35.320 3.853   1.00 59.48 ?  224 PRO E CA  1 
ATOM   1661 C C   . PRO A 1 224 ? 32.187  -34.587 5.109   1.00 61.25 ?  224 PRO E C   1 
ATOM   1662 O O   . PRO A 1 224 ? 32.935  -34.589 6.087   1.00 61.84 ?  224 PRO E O   1 
ATOM   1663 C CB  . PRO A 1 224 ? 32.741  -36.822 4.116   1.00 63.29 ?  224 PRO E CB  1 
ATOM   1664 C CG  . PRO A 1 224 ? 33.814  -37.287 3.198   1.00 60.93 ?  224 PRO E CG  1 
ATOM   1665 C CD  . PRO A 1 224 ? 34.838  -36.182 3.209   1.00 60.09 ?  224 PRO E CD  1 
ATOM   1666 N N   . SER B 2 1   ? 14.779  -2.299  -44.098 1.00 24.21 ?  1   SER F N   1 
ATOM   1667 C CA  . SER B 2 1   ? 15.075  -3.471  -44.920 1.00 26.73 ?  1   SER F CA  1 
ATOM   1668 C C   . SER B 2 1   ? 13.909  -4.439  -44.899 1.00 25.60 ?  1   SER F C   1 
ATOM   1669 O O   . SER B 2 1   ? 13.067  -4.403  -44.007 1.00 23.21 ?  1   SER F O   1 
ATOM   1670 C CB  . SER B 2 1   ? 16.316  -4.206  -44.417 1.00 29.23 ?  1   SER F CB  1 
ATOM   1671 O OG  . SER B 2 1   ? 16.265  -4.378  -43.005 1.00 28.19 ?  1   SER F OG  1 
ATOM   1672 N N   . PHE B 2 2   ? 13.877  -5.327  -45.877 1.00 27.46 ?  2   PHE F N   1 
ATOM   1673 C CA  . PHE B 2 2   ? 12.849  -6.348  -45.866 1.00 30.85 ?  2   PHE F CA  1 
ATOM   1674 C C   . PHE B 2 2   ? 13.189  -7.371  -44.794 1.00 30.95 ?  2   PHE F C   1 
ATOM   1675 O O   . PHE B 2 2   ? 14.347  -7.517  -44.405 1.00 29.13 ?  2   PHE F O   1 
ATOM   1676 C CB  . PHE B 2 2   ? 12.713  -6.941  -47.270 1.00 34.76 ?  2   PHE F CB  1 
ATOM   1677 C CG  . PHE B 2 2   ? 12.398  -5.871  -48.308 1.00 39.43 ?  2   PHE F CG  1 
ATOM   1678 C CD1 . PHE B 2 2   ? 11.114  -5.340  -48.414 1.00 39.69 ?  2   PHE F CD1 1 
ATOM   1679 C CD2 . PHE B 2 2   ? 13.403  -5.322  -49.099 1.00 44.04 ?  2   PHE F CD2 1 
ATOM   1680 C CE1 . PHE B 2 2   ? 10.832  -4.318  -49.323 1.00 35.79 ?  2   PHE F CE1 1 
ATOM   1681 C CE2 . PHE B 2 2   ? 13.120  -4.304  -50.012 1.00 42.25 ?  2   PHE F CE2 1 
ATOM   1682 C CZ  . PHE B 2 2   ? 11.829  -3.812  -50.122 1.00 39.90 ?  2   PHE F CZ  1 
ATOM   1683 N N   . GLU B 2 3   ? 12.159  -7.991  -44.234 1.00 27.27 ?  3   GLU F N   1 
ATOM   1684 C CA  . GLU B 2 3   ? 12.340  -8.950  -43.157 1.00 28.33 ?  3   GLU F CA  1 
ATOM   1685 C C   . GLU B 2 3   ? 12.544  -10.346 -43.713 1.00 26.88 ?  3   GLU F C   1 
ATOM   1686 O O   . GLU B 2 3   ? 12.012  -10.689 -44.770 1.00 27.48 ?  3   GLU F O   1 
ATOM   1687 C CB  . GLU B 2 3   ? 11.140  -8.966  -42.204 1.00 32.88 ?  3   GLU F CB  1 
ATOM   1688 C CG  . GLU B 2 3   ? 11.258  -7.987  -41.063 1.00 34.53 ?  3   GLU F CG  1 
ATOM   1689 C CD  . GLU B 2 3   ? 10.083  -8.053  -40.102 1.00 39.20 ?  3   GLU F CD  1 
ATOM   1690 O OE1 . GLU B 2 3   ? 8.969   -8.463  -40.505 1.00 39.70 ?  3   GLU F OE1 1 
ATOM   1691 O OE2 . GLU B 2 3   ? 10.300  -7.743  -38.910 1.00 43.66 ?  3   GLU F OE2 1 
ATOM   1692 N N   . LEU B 2 4   ? 13.319  -11.144 -42.981 1.00 22.45 ?  4   LEU F N   1 
ATOM   1693 C CA  . LEU B 2 4   ? 13.429  -12.584 -43.201 1.00 23.21 ?  4   LEU F CA  1 
ATOM   1694 C C   . LEU B 2 4   ? 12.825  -13.297 -41.997 1.00 25.11 ?  4   LEU F C   1 
ATOM   1695 O O   . LEU B 2 4   ? 13.230  -13.029 -40.861 1.00 25.84 ?  4   LEU F O   1 
ATOM   1696 C CB  . LEU B 2 4   ? 14.900  -12.994 -43.380 1.00 22.52 ?  4   LEU F CB  1 
ATOM   1697 C CG  . LEU B 2 4   ? 15.610  -12.551 -44.656 1.00 24.48 ?  4   LEU F CG  1 
ATOM   1698 C CD1 . LEU B 2 4   ? 17.091  -12.977 -44.624 1.00 24.21 ?  4   LEU F CD1 1 
ATOM   1699 C CD2 . LEU B 2 4   ? 14.936  -13.102 -45.876 1.00 27.15 ?  4   LEU F CD2 1 
ATOM   1700 N N   . THR B 2 5   ? 11.854  -14.195 -42.238 1.00 21.50 ?  5   THR F N   1 
ATOM   1701 C CA  . THR B 2 5   ? 11.145  -14.890 -41.170 1.00 22.41 ?  5   THR F CA  1 
ATOM   1702 C C   . THR B 2 5   ? 11.530  -16.362 -41.169 1.00 23.14 ?  5   THR F C   1 
ATOM   1703 O O   . THR B 2 5   ? 11.295  -17.063 -42.157 1.00 21.94 ?  5   THR F O   1 
ATOM   1704 C CB  . THR B 2 5   ? 9.623   -14.746 -41.324 1.00 22.69 ?  5   THR F CB  1 
ATOM   1705 O OG1 . THR B 2 5   ? 9.272   -13.362 -41.247 1.00 26.00 ?  5   THR F OG1 1 
ATOM   1706 C CG2 . THR B 2 5   ? 8.892   -15.493 -40.229 1.00 25.51 ?  5   THR F CG2 1 
ATOM   1707 N N   . GLN B 2 6   ? 12.130  -16.813 -40.073 1.00 21.54 ?  6   GLN F N   1 
ATOM   1708 C CA  . GLN B 2 6   ? 12.429  -18.216 -39.841 1.00 21.88 ?  6   GLN F CA  1 
ATOM   1709 C C   . GLN B 2 6   ? 11.975  -18.566 -38.434 1.00 25.12 ?  6   GLN F C   1 
ATOM   1710 O O   . GLN B 2 6   ? 11.923  -17.702 -37.556 1.00 25.36 ?  6   GLN F O   1 
ATOM   1711 C CB  . GLN B 2 6   ? 13.938  -18.526 -40.033 1.00 21.09 ?  6   GLN F CB  1 
ATOM   1712 C CG  . GLN B 2 6   ? 14.902  -17.786 -39.090 1.00 21.80 ?  6   GLN F CG  1 
ATOM   1713 C CD  . GLN B 2 6   ? 16.363  -18.116 -39.388 1.00 23.89 ?  6   GLN F CD  1 
ATOM   1714 O OE1 . GLN B 2 6   ? 17.195  -17.221 -39.583 1.00 23.47 ?  6   GLN F OE1 1 
ATOM   1715 N NE2 . GLN B 2 6   ? 16.678  -19.401 -39.445 1.00 19.63 ?  6   GLN F NE2 1 
ATOM   1716 N N   . PRO B 2 7   ? 11.622  -19.826 -38.193 1.00 21.09 ?  7   PRO F N   1 
ATOM   1717 C CA  . PRO B 2 7   ? 11.080  -20.182 -36.886 1.00 25.88 ?  7   PRO F CA  1 
ATOM   1718 C C   . PRO B 2 7   ? 12.159  -20.139 -35.816 1.00 24.58 ?  7   PRO F C   1 
ATOM   1719 O O   . PRO B 2 7   ? 13.339  -20.404 -36.095 1.00 26.97 ?  7   PRO F O   1 
ATOM   1720 C CB  . PRO B 2 7   ? 10.540  -21.609 -37.100 1.00 26.17 ?  7   PRO F CB  1 
ATOM   1721 C CG  . PRO B 2 7   ? 11.234  -22.099 -38.338 1.00 30.02 ?  7   PRO F CG  1 
ATOM   1722 C CD  . PRO B 2 7   ? 11.481  -20.900 -39.189 1.00 24.76 ?  7   PRO F CD  1 
ATOM   1723 N N   . PRO B 2 8   ? 11.796  -19.810 -34.576 1.00 25.80 ?  8   PRO F N   1 
ATOM   1724 C CA  . PRO B 2 8   ? 12.827  -19.750 -33.533 1.00 26.71 ?  8   PRO F CA  1 
ATOM   1725 C C   . PRO B 2 8   ? 13.373  -21.116 -33.177 1.00 27.07 ?  8   PRO F C   1 
ATOM   1726 O O   . PRO B 2 8   ? 14.523  -21.207 -32.741 1.00 26.48 ?  8   PRO F O   1 
ATOM   1727 C CB  . PRO B 2 8   ? 12.102  -19.091 -32.349 1.00 32.12 ?  8   PRO F CB  1 
ATOM   1728 C CG  . PRO B 2 8   ? 10.647  -19.348 -32.599 1.00 32.81 ?  8   PRO F CG  1 
ATOM   1729 C CD  . PRO B 2 8   ? 10.469  -19.386 -34.088 1.00 30.24 ?  8   PRO F CD  1 
ATOM   1730 N N   . SER B 2 9   ? 12.603  -22.186 -33.369 1.00 27.49 ?  9   SER F N   1 
ATOM   1731 C CA  . SER B 2 9   ? 13.122  -23.497 -33.010 1.00 27.72 ?  9   SER F CA  1 
ATOM   1732 C C   . SER B 2 9   ? 12.498  -24.580 -33.872 1.00 26.60 ?  9   SER F C   1 
ATOM   1733 O O   . SER B 2 9   ? 11.338  -24.479 -34.298 1.00 26.24 ?  9   SER F O   1 
ATOM   1734 C CB  . SER B 2 9   ? 12.889  -23.784 -31.526 1.00 30.76 ?  9   SER F CB  1 
ATOM   1735 O OG  . SER B 2 9   ? 11.515  -23.889 -31.259 1.00 38.30 ?  9   SER F OG  1 
ATOM   1736 N N   . VAL B 2 10  ? 13.305  -25.606 -34.138 1.00 24.76 ?  10  VAL F N   1 
ATOM   1737 C CA  . VAL B 2 10  ? 12.881  -26.806 -34.851 1.00 26.75 ?  10  VAL F CA  1 
ATOM   1738 C C   . VAL B 2 10  ? 13.453  -27.998 -34.105 1.00 27.41 ?  10  VAL F C   1 
ATOM   1739 O O   . VAL B 2 10  ? 14.643  -28.007 -33.765 1.00 25.97 ?  10  VAL F O   1 
ATOM   1740 C CB  . VAL B 2 10  ? 13.363  -26.799 -36.317 1.00 23.99 ?  10  VAL F CB  1 
ATOM   1741 C CG1 . VAL B 2 10  ? 13.250  -28.195 -36.927 1.00 24.50 ?  10  VAL F CG1 1 
ATOM   1742 C CG2 . VAL B 2 10  ? 12.580  -25.777 -37.146 1.00 25.64 ?  10  VAL F CG2 1 
ATOM   1743 N N   . SER B 2 11  ? 12.617  -29.003 -33.845 1.00 24.79 ?  11  SER F N   1 
ATOM   1744 C CA  . SER B 2 11  ? 13.060  -30.243 -33.234 1.00 25.37 ?  11  SER F CA  1 
ATOM   1745 C C   . SER B 2 11  ? 13.004  -31.353 -34.276 1.00 24.67 ?  11  SER F C   1 
ATOM   1746 O O   . SER B 2 11  ? 12.034  -31.452 -35.037 1.00 24.76 ?  11  SER F O   1 
ATOM   1747 C CB  . SER B 2 11  ? 12.167  -30.614 -32.040 1.00 31.80 ?  11  SER F CB  1 
ATOM   1748 O OG  . SER B 2 11  ? 12.679  -30.045 -30.844 1.00 38.44 ?  11  SER F OG  1 
ATOM   1749 N N   . VAL B 2 12  ? 14.035  -32.190 -34.315 1.00 25.63 ?  12  VAL F N   1 
ATOM   1750 C CA  . VAL B 2 12  ? 14.050  -33.323 -35.237 1.00 26.57 ?  12  VAL F CA  1 
ATOM   1751 C C   . VAL B 2 12  ? 14.560  -34.539 -34.476 1.00 26.45 ?  12  VAL F C   1 
ATOM   1752 O O   . VAL B 2 12  ? 15.502  -34.437 -33.685 1.00 26.78 ?  12  VAL F O   1 
ATOM   1753 C CB  . VAL B 2 12  ? 14.906  -33.023 -36.489 1.00 26.88 ?  12  VAL F CB  1 
ATOM   1754 C CG1 . VAL B 2 12  ? 16.394  -32.705 -36.108 1.00 24.47 ?  12  VAL F CG1 1 
ATOM   1755 C CG2 . VAL B 2 12  ? 14.826  -34.174 -37.503 1.00 25.92 ?  12  VAL F CG2 1 
ATOM   1756 N N   . SER B 2 13  ? 13.912  -35.681 -34.675 1.00 25.80 ?  13  SER F N   1 
ATOM   1757 C CA  . SER B 2 13  ? 14.419  -36.901 -34.065 1.00 26.24 ?  13  SER F CA  1 
ATOM   1758 C C   . SER B 2 13  ? 15.647  -37.380 -34.832 1.00 26.73 ?  13  SER F C   1 
ATOM   1759 O O   . SER B 2 13  ? 15.756  -37.175 -36.046 1.00 30.60 ?  13  SER F O   1 
ATOM   1760 C CB  . SER B 2 13  ? 13.352  -38.007 -34.050 1.00 26.14 ?  13  SER F CB  1 
ATOM   1761 O OG  . SER B 2 13  ? 12.200  -37.615 -33.344 1.00 29.37 ?  13  SER F OG  1 
ATOM   1762 N N   . PRO B 2 14  ? 16.605  -37.994 -34.144 1.00 31.85 ?  14  PRO F N   1 
ATOM   1763 C CA  . PRO B 2 14  ? 17.798  -38.493 -34.834 1.00 28.08 ?  14  PRO F CA  1 
ATOM   1764 C C   . PRO B 2 14  ? 17.425  -39.379 -36.024 1.00 26.39 ?  14  PRO F C   1 
ATOM   1765 O O   . PRO B 2 14  ? 16.577  -40.268 -35.915 1.00 27.54 ?  14  PRO F O   1 
ATOM   1766 C CB  . PRO B 2 14  ? 18.523  -39.288 -33.740 1.00 31.45 ?  14  PRO F CB  1 
ATOM   1767 C CG  . PRO B 2 14  ? 18.081  -38.630 -32.462 1.00 31.41 ?  14  PRO F CG  1 
ATOM   1768 C CD  . PRO B 2 14  ? 16.647  -38.245 -32.694 1.00 30.98 ?  14  PRO F CD  1 
ATOM   1769 N N   . GLY B 2 15  ? 18.033  -39.095 -37.179 1.00 24.85 ?  15  GLY F N   1 
ATOM   1770 C CA  . GLY B 2 15  ? 17.778  -39.821 -38.414 1.00 26.25 ?  15  GLY F CA  1 
ATOM   1771 C C   . GLY B 2 15  ? 16.577  -39.358 -39.225 1.00 26.90 ?  15  GLY F C   1 
ATOM   1772 O O   . GLY B 2 15  ? 16.338  -39.892 -40.315 1.00 23.64 ?  15  GLY F O   1 
ATOM   1773 N N   . GLN B 2 16  ? 15.809  -38.400 -38.737 1.00 24.57 ?  16  GLN F N   1 
ATOM   1774 C CA  . GLN B 2 16  ? 14.640  -37.920 -39.458 1.00 23.87 ?  16  GLN F CA  1 
ATOM   1775 C C   . GLN B 2 16  ? 14.996  -36.625 -40.174 1.00 24.84 ?  16  GLN F C   1 
ATOM   1776 O O   . GLN B 2 16  ? 16.096  -36.096 -40.027 1.00 23.98 ?  16  GLN F O   1 
ATOM   1777 C CB  . GLN B 2 16  ? 13.459  -37.757 -38.498 1.00 25.46 ?  16  GLN F CB  1 
ATOM   1778 C CG  . GLN B 2 16  ? 13.069  -39.071 -37.819 1.00 30.43 ?  16  GLN F CG  1 
ATOM   1779 C CD  . GLN B 2 16  ? 11.707  -39.023 -37.139 1.00 32.12 ?  16  GLN F CD  1 
ATOM   1780 O OE1 . GLN B 2 16  ? 11.148  -37.952 -36.909 1.00 37.87 ?  16  GLN F OE1 1 
ATOM   1781 N NE2 . GLN B 2 16  ? 11.152  -40.194 -36.849 1.00 37.16 ?  16  GLN F NE2 1 
ATOM   1782 N N   . THR B 2 17  ? 14.047  -36.100 -40.955 1.00 23.49 ?  17  THR F N   1 
ATOM   1783 C CA  . THR B 2 17  ? 14.298  -34.927 -41.786 1.00 26.33 ?  17  THR F CA  1 
ATOM   1784 C C   . THR B 2 17  ? 13.857  -33.660 -41.067 1.00 23.35 ?  17  THR F C   1 
ATOM   1785 O O   . THR B 2 17  ? 12.710  -33.569 -40.609 1.00 24.28 ?  17  THR F O   1 
ATOM   1786 C CB  . THR B 2 17  ? 13.543  -35.049 -43.113 1.00 28.87 ?  17  THR F CB  1 
ATOM   1787 O OG1 . THR B 2 17  ? 14.053  -36.168 -43.843 1.00 27.72 ?  17  THR F OG1 1 
ATOM   1788 C CG2 . THR B 2 17  ? 13.713  -33.780 -43.975 1.00 24.58 ?  17  THR F CG2 1 
ATOM   1789 N N   . ALA B 2 18  ? 14.767  -32.683 -40.976 1.00 21.65 ?  18  ALA F N   1 
ATOM   1790 C CA  . ALA B 2 18  ? 14.448  -31.358 -40.467 1.00 25.59 ?  18  ALA F CA  1 
ATOM   1791 C C   . ALA B 2 18  ? 14.245  -30.422 -41.645 1.00 22.81 ?  18  ALA F C   1 
ATOM   1792 O O   . ALA B 2 18  ? 14.989  -30.482 -42.631 1.00 22.35 ?  18  ALA F O   1 
ATOM   1793 C CB  . ALA B 2 18  ? 15.570  -30.811 -39.566 1.00 23.44 ?  18  ALA F CB  1 
ATOM   1794 N N   . ARG B 2 19  ? 13.252  -29.542 -41.528 1.00 23.61 ?  19  ARG F N   1 
ATOM   1795 C CA  . ARG B 2 19  ? 13.001  -28.510 -42.527 1.00 20.86 ?  19  ARG F CA  1 
ATOM   1796 C C   . ARG B 2 19  ? 12.960  -27.171 -41.813 1.00 23.49 ?  19  ARG F C   1 
ATOM   1797 O O   . ARG B 2 19  ? 12.159  -26.990 -40.892 1.00 22.80 ?  19  ARG F O   1 
ATOM   1798 C CB  . ARG B 2 19  ? 11.689  -28.758 -43.279 1.00 20.97 ?  19  ARG F CB  1 
ATOM   1799 C CG  . ARG B 2 19  ? 11.775  -29.948 -44.271 1.00 22.37 ?  19  ARG F CG  1 
ATOM   1800 C CD  . ARG B 2 19  ? 10.491  -30.082 -45.123 1.00 23.75 ?  19  ARG F CD  1 
ATOM   1801 N NE  . ARG B 2 19  ? 10.565  -31.328 -45.887 1.00 21.51 ?  19  ARG F NE  1 
ATOM   1802 C CZ  . ARG B 2 19  ? 9.997   -32.461 -45.513 1.00 24.76 ?  19  ARG F CZ  1 
ATOM   1803 N NH1 . ARG B 2 19  ? 9.212   -32.520 -44.453 1.00 25.82 ?  19  ARG F NH1 1 
ATOM   1804 N NH2 . ARG B 2 19  ? 10.227  -33.566 -46.220 1.00 27.05 ?  19  ARG F NH2 1 
ATOM   1805 N N   . ILE B 2 20  ? 13.821  -26.245 -42.233 1.00 22.66 ?  20  ILE F N   1 
ATOM   1806 C CA  . ILE B 2 20  ? 13.871  -24.898 -41.676 1.00 22.44 ?  20  ILE F CA  1 
ATOM   1807 C C   . ILE B 2 20  ? 13.527  -23.926 -42.789 1.00 24.48 ?  20  ILE F C   1 
ATOM   1808 O O   . ILE B 2 20  ? 14.250  -23.840 -43.791 1.00 23.85 ?  20  ILE F O   1 
ATOM   1809 C CB  . ILE B 2 20  ? 15.253  -24.565 -41.083 1.00 24.60 ?  20  ILE F CB  1 
ATOM   1810 C CG1 . ILE B 2 20  ? 15.642  -25.581 -40.005 1.00 25.74 ?  20  ILE F CG1 1 
ATOM   1811 C CG2 . ILE B 2 20  ? 15.205  -23.195 -40.432 1.00 24.58 ?  20  ILE F CG2 1 
ATOM   1812 C CD1 . ILE B 2 20  ? 16.527  -26.695 -40.476 1.00 29.27 ?  20  ILE F CD1 1 
ATOM   1813 N N   . THR B 2 21  ? 12.451  -23.168 -42.606 1.00 22.62 ?  21  THR F N   1 
ATOM   1814 C CA  . THR B 2 21  ? 12.011  -22.254 -43.646 1.00 19.56 ?  21  THR F CA  1 
ATOM   1815 C C   . THR B 2 21  ? 12.511  -20.845 -43.356 1.00 21.26 ?  21  THR F C   1 
ATOM   1816 O O   . THR B 2 21  ? 12.793  -20.464 -42.217 1.00 21.08 ?  21  THR F O   1 
ATOM   1817 C CB  . THR B 2 21  ? 10.482  -22.236 -43.793 1.00 22.79 ?  21  THR F CB  1 
ATOM   1818 O OG1 . THR B 2 21  ? 9.880   -21.968 -42.521 1.00 23.74 ?  21  THR F OG1 1 
ATOM   1819 C CG2 . THR B 2 21  ? 9.984   -23.612 -44.324 1.00 20.66 ?  21  THR F CG2 1 
ATOM   1820 N N   . CYS B 2 22  ? 12.611  -20.081 -44.424 1.00 21.41 ?  22  CYS F N   1 
ATOM   1821 C CA  . CYS B 2 22  ? 13.009  -18.681 -44.367 1.00 20.61 ?  22  CYS F CA  1 
ATOM   1822 C C   . CYS B 2 22  ? 12.198  -17.976 -45.429 1.00 22.51 ?  22  CYS F C   1 
ATOM   1823 O O   . CYS B 2 22  ? 12.331  -18.307 -46.611 1.00 24.84 ?  22  CYS F O   1 
ATOM   1824 C CB  . CYS B 2 22  ? 14.514  -18.535 -44.632 1.00 20.43 ?  22  CYS F CB  1 
ATOM   1825 S SG  . CYS B 2 22  ? 15.089  -16.811 -44.518 1.00 26.06 ?  22  CYS F SG  1 
ATOM   1826 N N   . SER B 2 23  ? 11.346  -17.027 -45.017 1.00 22.37 ?  23  SER F N   1 
ATOM   1827 C CA  . SER B 2 23  ? 10.444  -16.337 -45.934 1.00 25.07 ?  23  SER F CA  1 
ATOM   1828 C C   . SER B 2 23  ? 10.716  -14.848 -45.916 1.00 23.79 ?  23  SER F C   1 
ATOM   1829 O O   . SER B 2 23  ? 11.065  -14.286 -44.875 1.00 25.29 ?  23  SER F O   1 
ATOM   1830 C CB  . SER B 2 23  ? 8.954   -16.558 -45.566 1.00 23.47 ?  23  SER F CB  1 
ATOM   1831 O OG  . SER B 2 23  ? 8.695   -17.942 -45.454 1.00 34.52 ?  23  SER F OG  1 
ATOM   1832 N N   . GLY B 2 24  ? 10.555  -14.226 -47.072 1.00 28.79 ?  24  GLY F N   1 
ATOM   1833 C CA  . GLY B 2 24  ? 10.627  -12.776 -47.173 1.00 31.59 ?  24  GLY F CA  1 
ATOM   1834 C C   . GLY B 2 24  ? 10.113  -12.341 -48.527 1.00 35.05 ?  24  GLY F C   1 
ATOM   1835 O O   . GLY B 2 24  ? 10.330  -13.036 -49.522 1.00 30.22 ?  24  GLY F O   1 
ATOM   1836 N N   . ASP B 2 25  ? 9.410   -11.204 -48.591 1.00 41.47 ?  25  ASP F N   1 
ATOM   1837 C CA  . ASP B 2 25  ? 8.801   -10.809 -49.858 1.00 40.25 ?  25  ASP F CA  1 
ATOM   1838 C C   . ASP B 2 25  ? 9.839   -10.489 -50.918 1.00 39.91 ?  25  ASP F C   1 
ATOM   1839 O O   . ASP B 2 25  ? 9.502   -10.498 -52.109 1.00 38.03 ?  25  ASP F O   1 
ATOM   1840 C CB  . ASP B 2 25  ? 7.879   -9.601  -49.665 1.00 39.14 ?  25  ASP F CB  1 
ATOM   1841 C CG  . ASP B 2 25  ? 6.816   -9.842  -48.623 1.00 47.71 ?  25  ASP F CG  1 
ATOM   1842 O OD1 . ASP B 2 25  ? 6.368   -11.008 -48.468 1.00 49.48 ?  25  ASP F OD1 1 
ATOM   1843 O OD2 . ASP B 2 25  ? 6.422   -8.861  -47.958 1.00 53.51 ?  25  ASP F OD2 1 
ATOM   1844 N N   . ALA B 2 26  ? 11.086  -10.220 -50.511 1.00 34.46 ?  26  ALA F N   1 
ATOM   1845 C CA  . ALA B 2 26  ? 12.189  -9.918  -51.416 1.00 36.35 ?  26  ALA F CA  1 
ATOM   1846 C C   . ALA B 2 26  ? 12.926  -11.156 -51.931 1.00 38.39 ?  26  ALA F C   1 
ATOM   1847 O O   . ALA B 2 26  ? 13.755  -11.035 -52.838 1.00 38.54 ?  26  ALA F O   1 
ATOM   1848 C CB  . ALA B 2 26  ? 13.203  -9.010  -50.715 1.00 43.48 ?  26  ALA F CB  1 
ATOM   1849 N N   . LEU B 2 27  ? 12.666  -12.341 -51.379 1.00 33.56 ?  27  LEU F N   1 
ATOM   1850 C CA  . LEU B 2 27  ? 13.438  -13.506 -51.792 1.00 36.02 ?  27  LEU F CA  1 
ATOM   1851 C C   . LEU B 2 27  ? 13.282  -13.882 -53.264 1.00 37.95 ?  27  LEU F C   1 
ATOM   1852 O O   . LEU B 2 27  ? 14.260  -14.398 -53.831 1.00 38.86 ?  27  LEU F O   1 
ATOM   1853 C CB  . LEU B 2 27  ? 13.106  -14.706 -50.891 1.00 33.03 ?  27  LEU F CB  1 
ATOM   1854 C CG  . LEU B 2 27  ? 13.589  -14.438 -49.459 1.00 34.09 ?  27  LEU F CG  1 
ATOM   1855 C CD1 . LEU B 2 27  ? 13.431  -15.676 -48.566 1.00 33.19 ?  27  LEU F CD1 1 
ATOM   1856 C CD2 . LEU B 2 27  ? 15.030  -13.854 -49.431 1.00 33.55 ?  27  LEU F CD2 1 
ATOM   1857 N N   . PRO B 2 28  ? 12.140  -13.682 -53.936 1.00 39.33 ?  28  PRO F N   1 
ATOM   1858 C CA  . PRO B 2 28  ? 12.105  -14.004 -55.377 1.00 40.64 ?  28  PRO F CA  1 
ATOM   1859 C C   . PRO B 2 28  ? 13.158  -13.269 -56.193 1.00 39.46 ?  28  PRO F C   1 
ATOM   1860 O O   . PRO B 2 28  ? 13.501  -13.736 -57.284 1.00 43.16 ?  28  PRO F O   1 
ATOM   1861 C CB  . PRO B 2 28  ? 10.685  -13.615 -55.808 1.00 39.59 ?  28  PRO F CB  1 
ATOM   1862 C CG  . PRO B 2 28  ? 9.884   -13.485 -54.563 1.00 43.29 ?  28  PRO F CG  1 
ATOM   1863 C CD  . PRO B 2 28  ? 10.798  -13.390 -53.382 1.00 41.82 ?  28  PRO F CD  1 
ATOM   1864 N N   . LYS B 2 29  ? 13.684  -12.134 -55.713 1.00 38.60 ?  29  LYS F N   1 
ATOM   1865 C CA  . LYS B 2 29  ? 14.686  -11.378 -56.451 1.00 39.48 ?  29  LYS F CA  1 
ATOM   1866 C C   . LYS B 2 29  ? 16.092  -11.488 -55.874 1.00 39.33 ?  29  LYS F C   1 
ATOM   1867 O O   . LYS B 2 29  ? 17.045  -11.090 -56.551 1.00 45.82 ?  29  LYS F O   1 
ATOM   1868 C CB  . LYS B 2 29  ? 14.299  -9.890  -56.519 1.00 42.99 ?  29  LYS F CB  1 
ATOM   1869 C CG  . LYS B 2 29  ? 13.016  -9.597  -57.284 1.00 50.12 ?  29  LYS F CG  1 
ATOM   1870 C CD  . LYS B 2 29  ? 13.156  -9.844  -58.786 1.00 53.47 ?  29  LYS F CD  1 
ATOM   1871 C CE  . LYS B 2 29  ? 11.876  -9.441  -59.514 1.00 57.15 ?  29  LYS F CE  1 
ATOM   1872 N NZ  . LYS B 2 29  ? 11.941  -9.713  -60.975 1.00 60.16 ?  29  LYS F NZ  1 
ATOM   1873 N N   . GLN B 2 30  ? 16.259  -12.012 -54.662 1.00 33.27 ?  30  GLN F N   1 
ATOM   1874 C CA  . GLN B 2 30  ? 17.551  -12.006 -53.983 1.00 32.35 ?  30  GLN F CA  1 
ATOM   1875 C C   . GLN B 2 30  ? 17.975  -13.415 -53.576 1.00 29.58 ?  30  GLN F C   1 
ATOM   1876 O O   . GLN B 2 30  ? 17.135  -14.269 -53.282 1.00 28.90 ?  30  GLN F O   1 
ATOM   1877 C CB  . GLN B 2 30  ? 17.504  -11.109 -52.737 1.00 34.40 ?  30  GLN F CB  1 
ATOM   1878 C CG  . GLN B 2 30  ? 17.344  -9.576  -52.977 1.00 33.50 ?  30  GLN F CG  1 
ATOM   1879 C CD  . GLN B 2 30  ? 18.371  -8.954  -53.959 1.00 38.61 ?  30  GLN F CD  1 
ATOM   1880 O OE1 . GLN B 2 30  ? 19.557  -9.322  -53.968 1.00 42.38 ?  30  GLN F OE1 1 
ATOM   1881 N NE2 . GLN B 2 30  ? 17.937  -7.926  -54.705 1.00 42.20 ?  30  GLN F NE2 1 
ATOM   1882 N N   . TYR B 2 31  ? 19.288  -13.643 -53.526 1.00 29.90 ?  31  TYR F N   1 
ATOM   1883 C CA  . TYR B 2 31  ? 19.804  -14.930 -53.061 1.00 25.59 ?  31  TYR F CA  1 
ATOM   1884 C C   . TYR B 2 31  ? 19.658  -15.052 -51.555 1.00 24.35 ?  31  TYR F C   1 
ATOM   1885 O O   . TYR B 2 31  ? 19.662  -14.053 -50.828 1.00 24.46 ?  31  TYR F O   1 
ATOM   1886 C CB  . TYR B 2 31  ? 21.291  -15.087 -53.404 1.00 24.52 ?  31  TYR F CB  1 
ATOM   1887 C CG  . TYR B 2 31  ? 21.584  -15.317 -54.858 1.00 26.37 ?  31  TYR F CG  1 
ATOM   1888 C CD1 . TYR B 2 31  ? 21.043  -16.407 -55.535 1.00 28.17 ?  31  TYR F CD1 1 
ATOM   1889 C CD2 . TYR B 2 31  ? 22.436  -14.454 -55.549 1.00 28.93 ?  31  TYR F CD2 1 
ATOM   1890 C CE1 . TYR B 2 31  ? 21.324  -16.624 -56.870 1.00 31.10 ?  31  TYR F CE1 1 
ATOM   1891 C CE2 . TYR B 2 31  ? 22.730  -14.660 -56.875 1.00 30.94 ?  31  TYR F CE2 1 
ATOM   1892 C CZ  . TYR B 2 31  ? 22.171  -15.751 -57.532 1.00 31.12 ?  31  TYR F CZ  1 
ATOM   1893 O OH  . TYR B 2 31  ? 22.464  -15.953 -58.855 1.00 34.55 ?  31  TYR F OH  1 
ATOM   1894 N N   . VAL B 2 32  ? 19.583  -16.298 -51.079 1.00 23.33 ?  32  VAL F N   1 
ATOM   1895 C CA  . VAL B 2 32  ? 19.559  -16.621 -49.654 1.00 23.09 ?  32  VAL F CA  1 
ATOM   1896 C C   . VAL B 2 32  ? 20.847  -17.354 -49.306 1.00 23.69 ?  32  VAL F C   1 
ATOM   1897 O O   . VAL B 2 32  ? 21.332  -18.183 -50.087 1.00 23.39 ?  32  VAL F O   1 
ATOM   1898 C CB  . VAL B 2 32  ? 18.334  -17.486 -49.283 1.00 25.37 ?  32  VAL F CB  1 
ATOM   1899 C CG1 . VAL B 2 32  ? 18.332  -17.791 -47.780 1.00 26.69 ?  32  VAL F CG1 1 
ATOM   1900 C CG2 . VAL B 2 32  ? 17.070  -16.751 -49.649 1.00 30.78 ?  32  VAL F CG2 1 
ATOM   1901 N N   . TYR B 2 33  ? 21.380  -17.068 -48.125 1.00 22.87 ?  33  TYR F N   1 
ATOM   1902 C CA  . TYR B 2 33  ? 22.549  -17.743 -47.587 1.00 20.91 ?  33  TYR F CA  1 
ATOM   1903 C C   . TYR B 2 33  ? 22.176  -18.346 -46.245 1.00 22.82 ?  33  TYR F C   1 
ATOM   1904 O O   . TYR B 2 33  ? 21.405  -17.748 -45.487 1.00 22.78 ?  33  TYR F O   1 
ATOM   1905 C CB  . TYR B 2 33  ? 23.728  -16.741 -47.441 1.00 19.92 ?  33  TYR F CB  1 
ATOM   1906 C CG  . TYR B 2 33  ? 24.019  -16.070 -48.766 1.00 19.81 ?  33  TYR F CG  1 
ATOM   1907 C CD1 . TYR B 2 33  ? 23.266  -14.980 -49.202 1.00 22.28 ?  33  TYR F CD1 1 
ATOM   1908 C CD2 . TYR B 2 33  ? 25.027  -16.555 -49.598 1.00 21.52 ?  33  TYR F CD2 1 
ATOM   1909 C CE1 . TYR B 2 33  ? 23.510  -14.386 -50.430 1.00 21.91 ?  33  TYR F CE1 1 
ATOM   1910 C CE2 . TYR B 2 33  ? 25.287  -15.961 -50.819 1.00 21.79 ?  33  TYR F CE2 1 
ATOM   1911 C CZ  . TYR B 2 33  ? 24.510  -14.882 -51.230 1.00 24.18 ?  33  TYR F CZ  1 
ATOM   1912 O OH  . TYR B 2 33  ? 24.756  -14.288 -52.438 1.00 22.76 ?  33  TYR F OH  1 
ATOM   1913 N N   . TRP B 2 34  ? 22.681  -19.546 -45.970 1.00 20.33 ?  34  TRP F N   1 
ATOM   1914 C CA  . TRP B 2 34  ? 22.469  -20.191 -44.685 1.00 20.40 ?  34  TRP F CA  1 
ATOM   1915 C C   . TRP B 2 34  ? 23.797  -20.390 -43.979 1.00 20.91 ?  34  TRP F C   1 
ATOM   1916 O O   . TRP B 2 34  ? 24.763  -20.864 -44.586 1.00 21.56 ?  34  TRP F O   1 
ATOM   1917 C CB  . TRP B 2 34  ? 21.820  -21.558 -44.842 1.00 19.45 ?  34  TRP F CB  1 
ATOM   1918 C CG  . TRP B 2 34  ? 20.377  -21.528 -45.215 1.00 20.10 ?  34  TRP F CG  1 
ATOM   1919 C CD1 . TRP B 2 34  ? 19.850  -21.665 -46.472 1.00 22.70 ?  34  TRP F CD1 1 
ATOM   1920 C CD2 . TRP B 2 34  ? 19.263  -21.404 -44.320 1.00 19.84 ?  34  TRP F CD2 1 
ATOM   1921 N NE1 . TRP B 2 34  ? 18.475  -21.613 -46.416 1.00 21.27 ?  34  TRP F NE1 1 
ATOM   1922 C CE2 . TRP B 2 34  ? 18.088  -21.450 -45.108 1.00 20.03 ?  34  TRP F CE2 1 
ATOM   1923 C CE3 . TRP B 2 34  ? 19.146  -21.231 -42.937 1.00 19.32 ?  34  TRP F CE3 1 
ATOM   1924 C CZ2 . TRP B 2 34  ? 16.804  -21.378 -44.550 1.00 22.01 ?  34  TRP F CZ2 1 
ATOM   1925 C CZ3 . TRP B 2 34  ? 17.878  -21.165 -42.378 1.00 20.95 ?  34  TRP F CZ3 1 
ATOM   1926 C CH2 . TRP B 2 34  ? 16.718  -21.217 -43.191 1.00 19.70 ?  34  TRP F CH2 1 
ATOM   1927 N N   . TYR B 2 35  ? 23.809  -20.073 -42.684 1.00 21.75 ?  35  TYR F N   1 
ATOM   1928 C CA  . TYR B 2 35  ? 24.942  -20.281 -41.798 1.00 20.11 ?  35  TYR F CA  1 
ATOM   1929 C C   . TYR B 2 35  ? 24.557  -21.236 -40.685 1.00 21.41 ?  35  TYR F C   1 
ATOM   1930 O O   . TYR B 2 35  ? 23.463  -21.139 -40.121 1.00 23.87 ?  35  TYR F O   1 
ATOM   1931 C CB  . TYR B 2 35  ? 25.433  -18.969 -41.169 1.00 19.66 ?  35  TYR F CB  1 
ATOM   1932 C CG  . TYR B 2 35  ? 25.747  -17.964 -42.231 1.00 21.39 ?  35  TYR F CG  1 
ATOM   1933 C CD1 . TYR B 2 35  ? 27.000  -17.934 -42.826 1.00 19.45 ?  35  TYR F CD1 1 
ATOM   1934 C CD2 . TYR B 2 35  ? 24.769  -17.087 -42.678 1.00 20.62 ?  35  TYR F CD2 1 
ATOM   1935 C CE1 . TYR B 2 35  ? 27.294  -17.008 -43.844 1.00 20.62 ?  35  TYR F CE1 1 
ATOM   1936 C CE2 . TYR B 2 35  ? 25.021  -16.187 -43.682 1.00 23.66 ?  35  TYR F CE2 1 
ATOM   1937 C CZ  . TYR B 2 35  ? 26.276  -16.147 -44.263 1.00 21.27 ?  35  TYR F CZ  1 
ATOM   1938 O OH  . TYR B 2 35  ? 26.489  -15.250 -45.269 1.00 19.27 ?  35  TYR F OH  1 
ATOM   1939 N N   . GLN B 2 36  ? 25.478  -22.142 -40.367 1.00 20.63 ?  36  GLN F N   1 
ATOM   1940 C CA  . GLN B 2 36  ? 25.349  -23.046 -39.242 1.00 20.01 ?  36  GLN F CA  1 
ATOM   1941 C C   . GLN B 2 36  ? 26.258  -22.541 -38.132 1.00 22.06 ?  36  GLN F C   1 
ATOM   1942 O O   . GLN B 2 36  ? 27.438  -22.263 -38.382 1.00 22.95 ?  36  GLN F O   1 
ATOM   1943 C CB  . GLN B 2 36  ? 25.777  -24.462 -39.649 1.00 21.67 ?  36  GLN F CB  1 
ATOM   1944 C CG  . GLN B 2 36  ? 25.629  -25.474 -38.551 1.00 23.78 ?  36  GLN F CG  1 
ATOM   1945 C CD  . GLN B 2 36  ? 26.271  -26.809 -38.910 1.00 27.72 ?  36  GLN F CD  1 
ATOM   1946 O OE1 . GLN B 2 36  ? 25.620  -27.864 -38.904 1.00 26.87 ?  36  GLN F OE1 1 
ATOM   1947 N NE2 . GLN B 2 36  ? 27.556  -26.771 -39.221 1.00 20.66 ?  36  GLN F NE2 1 
ATOM   1948 N N   . GLN B 2 37  ? 25.741  -22.458 -36.902 1.00 21.91 ?  37  GLN F N   1 
ATOM   1949 C CA  . GLN B 2 37  ? 26.603  -22.082 -35.773 1.00 22.92 ?  37  GLN F CA  1 
ATOM   1950 C C   . GLN B 2 37  ? 26.420  -23.101 -34.655 1.00 26.52 ?  37  GLN F C   1 
ATOM   1951 O O   . GLN B 2 37  ? 25.375  -23.134 -33.999 1.00 26.20 ?  37  GLN F O   1 
ATOM   1952 C CB  . GLN B 2 37  ? 26.307  -20.667 -35.278 1.00 22.81 ?  37  GLN F CB  1 
ATOM   1953 C CG  . GLN B 2 37  ? 27.337  -20.196 -34.253 1.00 26.07 ?  37  GLN F CG  1 
ATOM   1954 C CD  . GLN B 2 37  ? 27.039  -18.811 -33.759 1.00 22.64 ?  37  GLN F CD  1 
ATOM   1955 O OE1 . GLN B 2 37  ? 25.877  -18.396 -33.707 1.00 24.96 ?  37  GLN F OE1 1 
ATOM   1956 N NE2 . GLN B 2 37  ? 28.068  -18.101 -33.350 1.00 25.41 ?  37  GLN F NE2 1 
ATOM   1957 N N   . LYS B 2 38  ? 27.430  -23.937 -34.459 1.00 30.20 ?  38  LYS F N   1 
ATOM   1958 C CA  . LYS B 2 38  ? 27.427  -24.892 -33.371 1.00 31.73 ?  38  LYS F CA  1 
ATOM   1959 C C   . LYS B 2 38  ? 27.875  -24.205 -32.086 1.00 36.36 ?  38  LYS F C   1 
ATOM   1960 O O   . LYS B 2 38  ? 28.536  -23.162 -32.122 1.00 34.91 ?  38  LYS F O   1 
ATOM   1961 C CB  . LYS B 2 38  ? 28.333  -26.070 -33.718 1.00 33.08 ?  38  LYS F CB  1 
ATOM   1962 C CG  . LYS B 2 38  ? 27.914  -26.799 -34.998 1.00 32.45 ?  38  LYS F CG  1 
ATOM   1963 C CD  . LYS B 2 38  ? 28.881  -27.912 -35.396 1.00 35.80 ?  38  LYS F CD  1 
ATOM   1964 C CE  . LYS B 2 38  ? 28.254  -28.814 -36.440 1.00 38.50 ?  38  LYS F CE  1 
ATOM   1965 N NZ  . LYS B 2 38  ? 29.104  -29.987 -36.819 1.00 40.05 ?  38  LYS F NZ  1 
ATOM   1966 N N   . PRO B 2 39  ? 27.517  -24.764 -30.931 1.00 40.72 ?  39  PRO F N   1 
ATOM   1967 C CA  . PRO B 2 39  ? 27.855  -24.108 -29.660 1.00 40.87 ?  39  PRO F CA  1 
ATOM   1968 C C   . PRO B 2 39  ? 29.354  -23.871 -29.542 1.00 42.14 ?  39  PRO F C   1 
ATOM   1969 O O   . PRO B 2 39  ? 30.168  -24.778 -29.762 1.00 41.97 ?  39  PRO F O   1 
ATOM   1970 C CB  . PRO B 2 39  ? 27.358  -25.096 -28.598 1.00 45.61 ?  39  PRO F CB  1 
ATOM   1971 C CG  . PRO B 2 39  ? 26.646  -26.192 -29.315 1.00 46.03 ?  39  PRO F CG  1 
ATOM   1972 C CD  . PRO B 2 39  ? 26.608  -25.914 -30.772 1.00 39.48 ?  39  PRO F CD  1 
ATOM   1973 N N   . GLY B 2 40  ? 29.714  -22.633 -29.216 1.00 40.31 ?  40  GLY F N   1 
ATOM   1974 C CA  . GLY B 2 40  ? 31.092  -22.253 -29.006 1.00 41.01 ?  40  GLY F CA  1 
ATOM   1975 C C   . GLY B 2 40  ? 31.917  -22.047 -30.253 1.00 40.02 ?  40  GLY F C   1 
ATOM   1976 O O   . GLY B 2 40  ? 33.140  -21.919 -30.143 1.00 39.16 ?  40  GLY F O   1 
ATOM   1977 N N   . GLN B 2 41  ? 31.301  -22.008 -31.431 1.00 37.28 ?  41  GLN F N   1 
ATOM   1978 C CA  . GLN B 2 41  ? 32.021  -21.864 -32.686 1.00 32.47 ?  41  GLN F CA  1 
ATOM   1979 C C   . GLN B 2 41  ? 31.530  -20.638 -33.446 1.00 29.67 ?  41  GLN F C   1 
ATOM   1980 O O   . GLN B 2 41  ? 30.467  -20.097 -33.158 1.00 30.68 ?  41  GLN F O   1 
ATOM   1981 C CB  . GLN B 2 41  ? 31.859  -23.118 -33.555 1.00 33.15 ?  41  GLN F CB  1 
ATOM   1982 C CG  . GLN B 2 41  ? 32.438  -24.392 -32.928 1.00 36.89 ?  41  GLN F CG  1 
ATOM   1983 C CD  . GLN B 2 41  ? 32.307  -25.581 -33.843 1.00 41.86 ?  41  GLN F CD  1 
ATOM   1984 O OE1 . GLN B 2 41  ? 31.938  -25.437 -35.014 1.00 43.25 ?  41  GLN F OE1 1 
ATOM   1985 N NE2 . GLN B 2 41  ? 32.606  -26.768 -33.324 1.00 44.05 ?  41  GLN F NE2 1 
ATOM   1986 N N   . ALA B 2 42  ? 32.337  -20.199 -34.416 1.00 28.46 ?  42  ALA F N   1 
ATOM   1987 C CA  . ALA B 2 42  ? 31.924  -19.160 -35.348 1.00 28.11 ?  42  ALA F CA  1 
ATOM   1988 C C   . ALA B 2 42  ? 30.907  -19.720 -36.345 1.00 29.02 ?  42  ALA F C   1 
ATOM   1989 O O   . ALA B 2 42  ? 30.861  -20.937 -36.572 1.00 25.55 ?  42  ALA F O   1 
ATOM   1990 C CB  . ALA B 2 42  ? 33.132  -18.620 -36.106 1.00 28.75 ?  42  ALA F CB  1 
ATOM   1991 N N   . PRO B 2 43  ? 30.060  -18.862 -36.934 1.00 25.47 ?  43  PRO F N   1 
ATOM   1992 C CA  . PRO B 2 43  ? 29.161  -19.329 -38.007 1.00 23.93 ?  43  PRO F CA  1 
ATOM   1993 C C   . PRO B 2 43  ? 29.948  -19.854 -39.202 1.00 24.77 ?  43  PRO F C   1 
ATOM   1994 O O   . PRO B 2 43  ? 31.062  -19.408 -39.479 1.00 25.39 ?  43  PRO F O   1 
ATOM   1995 C CB  . PRO B 2 43  ? 28.373  -18.070 -38.386 1.00 22.46 ?  43  PRO F CB  1 
ATOM   1996 C CG  . PRO B 2 43  ? 28.463  -17.152 -37.155 1.00 22.16 ?  43  PRO F CG  1 
ATOM   1997 C CD  . PRO B 2 43  ? 29.830  -17.440 -36.580 1.00 25.72 ?  43  PRO F CD  1 
ATOM   1998 N N   . VAL B 2 44  ? 29.353  -20.804 -39.923 1.00 22.02 ?  44  VAL F N   1 
ATOM   1999 C CA  . VAL B 2 44  ? 29.946  -21.385 -41.122 1.00 19.17 ?  44  VAL F CA  1 
ATOM   2000 C C   . VAL B 2 44  ? 28.903  -21.321 -42.230 1.00 22.27 ?  44  VAL F C   1 
ATOM   2001 O O   . VAL B 2 44  ? 27.735  -21.647 -41.998 1.00 21.46 ?  44  VAL F O   1 
ATOM   2002 C CB  . VAL B 2 44  ? 30.400  -22.845 -40.876 1.00 26.61 ?  44  VAL F CB  1 
ATOM   2003 C CG1 . VAL B 2 44  ? 30.844  -23.512 -42.173 1.00 26.38 ?  44  VAL F CG1 1 
ATOM   2004 C CG2 . VAL B 2 44  ? 31.534  -22.878 -39.859 1.00 27.63 ?  44  VAL F CG2 1 
ATOM   2005 N N   . LEU B 2 45  ? 29.316  -20.903 -43.423 1.00 22.30 ?  45  LEU F N   1 
ATOM   2006 C CA  . LEU B 2 45  ? 28.407  -20.835 -44.564 1.00 22.48 ?  45  LEU F CA  1 
ATOM   2007 C C   . LEU B 2 45  ? 28.142  -22.242 -45.086 1.00 25.38 ?  45  LEU F C   1 
ATOM   2008 O O   . LEU B 2 45  ? 29.091  -22.943 -45.483 1.00 24.71 ?  45  LEU F O   1 
ATOM   2009 C CB  . LEU B 2 45  ? 29.012  -19.957 -45.661 1.00 23.48 ?  45  LEU F CB  1 
ATOM   2010 C CG  . LEU B 2 45  ? 28.250  -19.748 -46.970 1.00 22.51 ?  45  LEU F CG  1 
ATOM   2011 C CD1 . LEU B 2 45  ? 26.921  -19.045 -46.691 1.00 22.81 ?  45  LEU F CD1 1 
ATOM   2012 C CD2 . LEU B 2 45  ? 29.119  -18.856 -47.879 1.00 25.48 ?  45  LEU F CD2 1 
ATOM   2013 N N   . VAL B 2 46  ? 26.872  -22.666 -45.084 1.00 20.23 ?  46  VAL F N   1 
ATOM   2014 C CA  . VAL B 2 46  ? 26.521  -24.020 -45.515 1.00 23.11 ?  46  VAL F CA  1 
ATOM   2015 C C   . VAL B 2 46  ? 25.718  -24.058 -46.816 1.00 22.94 ?  46  VAL F C   1 
ATOM   2016 O O   . VAL B 2 46  ? 25.742  -25.090 -47.505 1.00 23.45 ?  46  VAL F O   1 
ATOM   2017 C CB  . VAL B 2 46  ? 25.778  -24.814 -44.412 1.00 25.17 ?  46  VAL F CB  1 
ATOM   2018 C CG1 . VAL B 2 46  ? 26.670  -24.977 -43.181 1.00 27.42 ?  46  VAL F CG1 1 
ATOM   2019 C CG2 . VAL B 2 46  ? 24.444  -24.177 -44.056 1.00 24.52 ?  46  VAL F CG2 1 
ATOM   2020 N N   . ILE B 2 47  ? 25.035  -22.978 -47.186 1.00 20.55 ?  47  ILE F N   1 
ATOM   2021 C CA  . ILE B 2 47  ? 24.382  -22.856 -48.481 1.00 22.02 ?  47  ILE F CA  1 
ATOM   2022 C C   . ILE B 2 47  ? 24.588  -21.426 -48.942 1.00 22.82 ?  47  ILE F C   1 
ATOM   2023 O O   . ILE B 2 47  ? 24.378  -20.491 -48.161 1.00 21.58 ?  47  ILE F O   1 
ATOM   2024 C CB  . ILE B 2 47  ? 22.867  -23.155 -48.406 1.00 23.70 ?  47  ILE F CB  1 
ATOM   2025 C CG1 . ILE B 2 47  ? 22.581  -24.614 -47.997 1.00 24.18 ?  47  ILE F CG1 1 
ATOM   2026 C CG2 . ILE B 2 47  ? 22.156  -22.745 -49.716 1.00 25.01 ?  47  ILE F CG2 1 
ATOM   2027 C CD1 . ILE B 2 47  ? 22.983  -25.629 -49.051 1.00 25.09 ?  47  ILE F CD1 1 
ATOM   2028 N N   . TYR B 2 48  ? 24.960  -21.240 -50.201 1.00 22.40 ?  48  TYR F N   1 
ATOM   2029 C CA  . TYR B 2 48  ? 25.076  -19.882 -50.725 1.00 22.62 ?  48  TYR F CA  1 
ATOM   2030 C C   . TYR B 2 48  ? 24.383  -19.771 -52.073 1.00 24.91 ?  48  TYR F C   1 
ATOM   2031 O O   . TYR B 2 48  ? 24.173  -20.768 -52.775 1.00 26.47 ?  48  TYR F O   1 
ATOM   2032 C CB  . TYR B 2 48  ? 26.550  -19.435 -50.817 1.00 23.21 ?  48  TYR F CB  1 
ATOM   2033 C CG  . TYR B 2 48  ? 27.436  -20.198 -51.783 1.00 24.10 ?  48  TYR F CG  1 
ATOM   2034 C CD1 . TYR B 2 48  ? 27.908  -21.472 -51.476 1.00 25.35 ?  48  TYR F CD1 1 
ATOM   2035 C CD2 . TYR B 2 48  ? 27.841  -19.616 -52.979 1.00 24.98 ?  48  TYR F CD2 1 
ATOM   2036 C CE1 . TYR B 2 48  ? 28.744  -22.155 -52.349 1.00 27.94 ?  48  TYR F CE1 1 
ATOM   2037 C CE2 . TYR B 2 48  ? 28.672  -20.281 -53.860 1.00 29.27 ?  48  TYR F CE2 1 
ATOM   2038 C CZ  . TYR B 2 48  ? 29.115  -21.561 -53.546 1.00 32.82 ?  48  TYR F CZ  1 
ATOM   2039 O OH  . TYR B 2 48  ? 29.956  -22.253 -54.409 1.00 33.94 ?  48  TYR F OH  1 
ATOM   2040 N N   . LYS B 2 49  ? 24.000  -18.547 -52.422 1.00 22.05 ?  49  LYS F N   1 
ATOM   2041 C CA  . LYS B 2 49  ? 23.299  -18.299 -53.705 1.00 23.11 ?  49  LYS F CA  1 
ATOM   2042 C C   . LYS B 2 49  ? 22.059  -19.203 -53.777 1.00 24.25 ?  49  LYS F C   1 
ATOM   2043 O O   . LYS B 2 49  ? 21.785  -19.715 -54.859 1.00 25.18 ?  49  LYS F O   1 
ATOM   2044 C CB  . LYS B 2 49  ? 24.287  -18.391 -54.869 1.00 25.58 ?  49  LYS F CB  1 
ATOM   2045 C CG  . LYS B 2 49  ? 25.302  -17.264 -54.908 1.00 28.08 ?  49  LYS F CG  1 
ATOM   2046 C CD  . LYS B 2 49  ? 26.281  -17.422 -56.029 1.00 32.58 ?  49  LYS F CD  1 
ATOM   2047 C CE  . LYS B 2 49  ? 25.718  -16.978 -57.359 1.00 36.16 ?  49  LYS F CE  1 
ATOM   2048 N NZ  . LYS B 2 49  ? 26.719  -17.124 -58.438 1.00 37.25 ?  49  LYS F NZ  1 
ATOM   2049 N N   . THR B 2 50  ? 21.397  -19.405 -52.640 1.00 23.30 ?  50  THR F N   1 
ATOM   2050 C CA  . THR B 2 50  ? 20.132  -20.177 -52.543 1.00 24.88 ?  50  THR F CA  1 
ATOM   2051 C C   . THR B 2 50  ? 20.307  -21.682 -52.801 1.00 24.07 ?  50  THR F C   1 
ATOM   2052 O O   . THR B 2 50  ? 19.742  -22.449 -52.060 1.00 26.72 ?  50  THR F O   1 
ATOM   2053 C CB  . THR B 2 50  ? 19.042  -19.517 -53.400 1.00 25.80 ?  50  THR F CB  1 
ATOM   2054 O OG1 . THR B 2 50  ? 18.921  -18.151 -53.013 1.00 24.75 ?  50  THR F OG1 1 
ATOM   2055 C CG2 . THR B 2 50  ? 17.703  -20.206 -53.265 1.00 24.61 ?  50  THR F CG2 1 
ATOM   2056 N N   . THR B 2 51  ? 21.097  -22.097 -53.777 1.00 24.12 ?  51  THR F N   1 
ATOM   2057 C CA  . THR B 2 51  ? 21.122  -23.542 -54.121 1.00 31.11 ?  51  THR F CA  1 
ATOM   2058 C C   . THR B 2 51  ? 22.510  -24.183 -54.057 1.00 33.29 ?  51  THR F C   1 
ATOM   2059 O O   . THR B 2 51  ? 22.579  -25.388 -54.295 1.00 33.92 ?  51  THR F O   1 
ATOM   2060 C CB  . THR B 2 51  ? 20.584  -23.733 -55.543 1.00 31.10 ?  51  THR F CB  1 
ATOM   2061 O OG1 . THR B 2 51  ? 21.423  -22.994 -56.429 1.00 36.53 ?  51  THR F OG1 1 
ATOM   2062 C CG2 . THR B 2 51  ? 19.149  -23.285 -55.693 1.00 30.39 ?  51  THR F CG2 1 
ATOM   2063 N N   . GLU B 2 52  ? 23.556  -23.443 -53.714 1.00 28.12 ?  52  GLU F N   1 
ATOM   2064 C CA  . GLU B 2 52  ? 24.892  -24.024 -53.803 1.00 27.79 ?  52  GLU F CA  1 
ATOM   2065 C C   . GLU B 2 52  ? 25.394  -24.469 -52.441 1.00 29.12 ?  52  GLU F C   1 
ATOM   2066 O O   . GLU B 2 52  ? 25.207  -23.780 -51.435 1.00 28.38 ?  52  GLU F O   1 
ATOM   2067 C CB  . GLU B 2 52  ? 25.870  -23.039 -54.427 1.00 29.30 ?  52  GLU F CB  1 
ATOM   2068 C CG  . GLU B 2 52  ? 25.327  -22.430 -55.718 1.00 33.57 ?  52  GLU F CG  1 
ATOM   2069 C CD  . GLU B 2 52  ? 25.187  -23.464 -56.821 1.00 41.48 ?  52  GLU F CD  1 
ATOM   2070 O OE1 . GLU B 2 52  ? 26.146  -24.238 -57.054 1.00 43.97 ?  52  GLU F OE1 1 
ATOM   2071 O OE2 . GLU B 2 52  ? 24.101  -23.518 -57.439 1.00 48.21 ?  52  GLU F OE2 1 
ATOM   2072 N N   . ARG B 2 53  ? 26.028  -25.642 -52.417 1.00 26.86 ?  53  ARG F N   1 
ATOM   2073 C CA  . ARG B 2 53  ? 26.595  -26.210 -51.202 1.00 25.66 ?  53  ARG F CA  1 
ATOM   2074 C C   . ARG B 2 53  ? 28.111  -26.118 -51.296 1.00 29.58 ?  53  ARG F C   1 
ATOM   2075 O O   . ARG B 2 53  ? 28.677  -26.653 -52.259 1.00 32.41 ?  53  ARG F O   1 
ATOM   2076 C CB  . ARG B 2 53  ? 26.156  -27.676 -51.043 1.00 30.41 ?  53  ARG F CB  1 
ATOM   2077 C CG  . ARG B 2 53  ? 26.258  -28.224 -49.630 1.00 31.89 ?  53  ARG F CG  1 
ATOM   2078 C CD  . ARG B 2 53  ? 25.719  -29.673 -49.542 1.00 33.88 ?  53  ARG F CD  1 
ATOM   2079 N NE  . ARG B 2 53  ? 25.899  -30.366 -50.812 1.00 35.27 ?  53  ARG F NE  1 
ATOM   2080 C CZ  . ARG B 2 53  ? 24.920  -30.858 -51.557 1.00 40.03 ?  53  ARG F CZ  1 
ATOM   2081 N NH1 . ARG B 2 53  ? 23.652  -30.760 -51.190 1.00 35.70 ?  53  ARG F NH1 1 
ATOM   2082 N NH2 . ARG B 2 53  ? 25.222  -31.461 -52.704 1.00 46.43 ?  53  ARG F NH2 1 
ATOM   2083 N N   . PRO B 2 54  ? 28.816  -25.469 -50.367 1.00 26.18 ?  54  PRO F N   1 
ATOM   2084 C CA  . PRO B 2 54  ? 30.279  -25.453 -50.458 1.00 26.39 ?  54  PRO F CA  1 
ATOM   2085 C C   . PRO B 2 54  ? 30.821  -26.862 -50.326 1.00 32.01 ?  54  PRO F C   1 
ATOM   2086 O O   . PRO B 2 54  ? 30.193  -27.742 -49.739 1.00 27.91 ?  54  PRO F O   1 
ATOM   2087 C CB  . PRO B 2 54  ? 30.715  -24.568 -49.283 1.00 28.68 ?  54  PRO F CB  1 
ATOM   2088 C CG  . PRO B 2 54  ? 29.483  -23.757 -48.893 1.00 24.32 ?  54  PRO F CG  1 
ATOM   2089 C CD  . PRO B 2 54  ? 28.311  -24.663 -49.238 1.00 25.03 ?  54  PRO F CD  1 
ATOM   2090 N N   . SER B 2 55  ? 31.984  -27.078 -50.921 1.00 32.62 ?  55  SER F N   1 
ATOM   2091 C CA  . SER B 2 55  ? 32.688  -28.332 -50.718 1.00 34.94 ?  55  SER F CA  1 
ATOM   2092 C C   . SER B 2 55  ? 32.912  -28.545 -49.227 1.00 32.49 ?  55  SER F C   1 
ATOM   2093 O O   . SER B 2 55  ? 33.189  -27.599 -48.484 1.00 39.15 ?  55  SER F O   1 
ATOM   2094 C CB  . SER B 2 55  ? 34.023  -28.300 -51.466 1.00 38.00 ?  55  SER F CB  1 
ATOM   2095 O OG  . SER B 2 55  ? 34.749  -29.478 -51.207 1.00 50.63 ?  55  SER F OG  1 
ATOM   2096 N N   . GLY B 2 56  ? 32.754  -29.781 -48.774 1.00 36.90 ?  56  GLY F N   1 
ATOM   2097 C CA  . GLY B 2 56  ? 32.925  -30.083 -47.369 1.00 35.24 ?  56  GLY F CA  1 
ATOM   2098 C C   . GLY B 2 56  ? 31.655  -30.057 -46.540 1.00 34.12 ?  56  GLY F C   1 
ATOM   2099 O O   . GLY B 2 56  ? 31.679  -30.503 -45.386 1.00 34.53 ?  56  GLY F O   1 
ATOM   2100 N N   . ILE B 2 57  ? 30.550  -29.559 -47.080 1.00 29.16 ?  57  ILE F N   1 
ATOM   2101 C CA  . ILE B 2 57  ? 29.290  -29.599 -46.343 1.00 28.46 ?  57  ILE F CA  1 
ATOM   2102 C C   . ILE B 2 57  ? 28.588  -30.904 -46.706 1.00 26.78 ?  57  ILE F C   1 
ATOM   2103 O O   . ILE B 2 57  ? 28.515  -31.242 -47.890 1.00 28.16 ?  57  ILE F O   1 
ATOM   2104 C CB  . ILE B 2 57  ? 28.416  -28.369 -46.652 1.00 28.54 ?  57  ILE F CB  1 
ATOM   2105 C CG1 . ILE B 2 57  ? 29.164  -27.077 -46.287 1.00 29.80 ?  57  ILE F CG1 1 
ATOM   2106 C CG2 . ILE B 2 57  ? 27.072  -28.462 -45.911 1.00 28.36 ?  57  ILE F CG2 1 
ATOM   2107 C CD1 . ILE B 2 57  ? 29.570  -26.993 -44.815 1.00 29.67 ?  57  ILE F CD1 1 
ATOM   2108 N N   . PRO B 2 58  ? 28.058  -31.650 -45.740 1.00 27.96 ?  58  PRO F N   1 
ATOM   2109 C CA  . PRO B 2 58  ? 27.432  -32.947 -46.058 1.00 30.86 ?  58  PRO F CA  1 
ATOM   2110 C C   . PRO B 2 58  ? 26.319  -32.829 -47.091 1.00 31.15 ?  58  PRO F C   1 
ATOM   2111 O O   . PRO B 2 58  ? 25.552  -31.868 -47.100 1.00 31.58 ?  58  PRO F O   1 
ATOM   2112 C CB  . PRO B 2 58  ? 26.892  -33.408 -44.702 1.00 33.06 ?  58  PRO F CB  1 
ATOM   2113 C CG  . PRO B 2 58  ? 27.873  -32.835 -43.729 1.00 35.79 ?  58  PRO F CG  1 
ATOM   2114 C CD  . PRO B 2 58  ? 28.151  -31.434 -44.284 1.00 29.87 ?  58  PRO F CD  1 
ATOM   2115 N N   . GLU B 2 59  ? 26.223  -33.837 -47.964 1.00 34.41 ?  59  GLU F N   1 
ATOM   2116 C CA  . GLU B 2 59  ? 25.144  -33.862 -48.948 1.00 34.50 ?  59  GLU F CA  1 
ATOM   2117 C C   . GLU B 2 59  ? 23.751  -33.939 -48.317 1.00 27.44 ?  59  GLU F C   1 
ATOM   2118 O O   . GLU B 2 59  ? 22.772  -33.688 -49.026 1.00 30.65 ?  59  GLU F O   1 
ATOM   2119 C CB  . GLU B 2 59  ? 25.345  -35.020 -49.941 1.00 39.90 ?  59  GLU F CB  1 
ATOM   2120 C CG  . GLU B 2 59  ? 26.348  -34.691 -51.057 1.00 45.70 ?  59  GLU F CG  1 
ATOM   2121 C CD  . GLU B 2 59  ? 26.710  -35.889 -51.931 1.00 58.17 ?  59  GLU F CD  1 
ATOM   2122 O OE1 . GLU B 2 59  ? 27.672  -36.619 -51.593 1.00 58.60 ?  59  GLU F OE1 1 
ATOM   2123 O OE2 . GLU B 2 59  ? 26.049  -36.084 -52.975 1.00 62.97 ?  59  GLU F OE2 1 
ATOM   2124 N N   . ARG B 2 60  ? 23.645  -34.248 -47.011 1.00 29.34 ?  60  ARG F N   1 
ATOM   2125 C CA  . ARG B 2 60  ? 22.371  -34.199 -46.289 1.00 28.44 ?  60  ARG F CA  1 
ATOM   2126 C C   . ARG B 2 60  ? 21.720  -32.820 -46.328 1.00 28.83 ?  60  ARG F C   1 
ATOM   2127 O O   . ARG B 2 60  ? 20.516  -32.714 -46.067 1.00 27.71 ?  60  ARG F O   1 
ATOM   2128 C CB  . ARG B 2 60  ? 22.535  -34.519 -44.794 1.00 29.95 ?  60  ARG F CB  1 
ATOM   2129 C CG  . ARG B 2 60  ? 23.413  -35.636 -44.386 1.00 44.29 ?  60  ARG F CG  1 
ATOM   2130 C CD  . ARG B 2 60  ? 23.198  -35.915 -42.891 1.00 40.93 ?  60  ARG F CD  1 
ATOM   2131 N NE  . ARG B 2 60  ? 23.792  -34.916 -41.996 1.00 33.27 ?  60  ARG F NE  1 
ATOM   2132 C CZ  . ARG B 2 60  ? 25.062  -34.969 -41.615 1.00 35.03 ?  60  ARG F CZ  1 
ATOM   2133 N NH1 . ARG B 2 60  ? 25.908  -35.826 -42.166 1.00 40.28 ?  60  ARG F NH1 1 
ATOM   2134 N NH2 . ARG B 2 60  ? 25.492  -34.159 -40.655 1.00 38.48 ?  60  ARG F NH2 1 
ATOM   2135 N N   . PHE B 2 61  ? 22.504  -31.762 -46.533 1.00 27.69 ?  61  PHE F N   1 
ATOM   2136 C CA  . PHE B 2 61  ? 22.000  -30.392 -46.520 1.00 26.70 ?  61  PHE F CA  1 
ATOM   2137 C C   . PHE B 2 61  ? 21.589  -29.990 -47.927 1.00 27.60 ?  61  PHE F C   1 
ATOM   2138 O O   . PHE B 2 61  ? 22.401  -30.059 -48.856 1.00 29.37 ?  61  PHE F O   1 
ATOM   2139 C CB  . PHE B 2 61  ? 23.066  -29.427 -45.982 1.00 26.12 ?  61  PHE F CB  1 
ATOM   2140 C CG  . PHE B 2 61  ? 23.357  -29.604 -44.527 1.00 25.76 ?  61  PHE F CG  1 
ATOM   2141 C CD1 . PHE B 2 61  ? 24.267  -30.561 -44.100 1.00 29.15 ?  61  PHE F CD1 1 
ATOM   2142 C CD2 . PHE B 2 61  ? 22.716  -28.821 -43.580 1.00 31.27 ?  61  PHE F CD2 1 
ATOM   2143 C CE1 . PHE B 2 61  ? 24.523  -30.746 -42.760 1.00 29.21 ?  61  PHE F CE1 1 
ATOM   2144 C CE2 . PHE B 2 61  ? 22.976  -28.994 -42.218 1.00 30.79 ?  61  PHE F CE2 1 
ATOM   2145 C CZ  . PHE B 2 61  ? 23.886  -29.957 -41.813 1.00 29.77 ?  61  PHE F CZ  1 
ATOM   2146 N N   . SER B 2 62  ? 20.340  -29.553 -48.089 1.00 23.68 ?  62  SER F N   1 
ATOM   2147 C CA  . SER B 2 62  ? 19.908  -29.034 -49.380 1.00 26.98 ?  62  SER F CA  1 
ATOM   2148 C C   . SER B 2 62  ? 18.914  -27.908 -49.151 1.00 27.83 ?  62  SER F C   1 
ATOM   2149 O O   . SER B 2 62  ? 18.335  -27.776 -48.069 1.00 28.43 ?  62  SER F O   1 
ATOM   2150 C CB  . SER B 2 62  ? 19.299  -30.136 -50.259 1.00 30.12 ?  62  SER F CB  1 
ATOM   2151 O OG  . SER B 2 62  ? 18.056  -30.563 -49.743 1.00 35.29 ?  62  SER F OG  1 
ATOM   2152 N N   . ASP B 2 63  ? 18.716  -27.097 -50.187 1.00 24.01 ?  63  ASP F N   1 
ATOM   2153 C CA  . ASP B 2 63  ? 17.880  -25.903 -50.089 1.00 26.28 ?  63  ASP F CA  1 
ATOM   2154 C C   . ASP B 2 63  ? 16.974  -25.841 -51.309 1.00 34.17 ?  63  ASP F C   1 
ATOM   2155 O O   . ASP B 2 63  ? 17.444  -26.008 -52.440 1.00 37.51 ?  63  ASP F O   1 
ATOM   2156 C CB  . ASP B 2 63  ? 18.795  -24.662 -49.979 1.00 27.22 ?  63  ASP F CB  1 
ATOM   2157 C CG  . ASP B 2 63  ? 18.096  -23.453 -49.432 1.00 31.47 ?  63  ASP F CG  1 
ATOM   2158 O OD1 . ASP B 2 63  ? 17.482  -23.581 -48.343 1.00 31.17 ?  63  ASP F OD1 1 
ATOM   2159 O OD2 . ASP B 2 63  ? 18.289  -22.337 -49.986 1.00 29.75 ?  63  ASP F OD2 1 
ATOM   2160 N N   . SER B 2 64  ? 15.679  -25.626 -51.084 1.00 29.82 ?  64  SER F N   1 
ATOM   2161 C CA  . SER B 2 64  ? 14.737  -25.481 -52.184 1.00 32.80 ?  64  SER F CA  1 
ATOM   2162 C C   . SER B 2 64  ? 13.943  -24.198 -51.987 1.00 35.83 ?  64  SER F C   1 
ATOM   2163 O O   . SER B 2 64  ? 13.913  -23.635 -50.889 1.00 29.63 ?  64  SER F O   1 
ATOM   2164 C CB  . SER B 2 64  ? 13.784  -26.670 -52.274 1.00 32.28 ?  64  SER F CB  1 
ATOM   2165 O OG  . SER B 2 64  ? 13.127  -26.886 -51.035 1.00 35.66 ?  64  SER F OG  1 
ATOM   2166 N N   . SER B 2 65  ? 13.307  -23.742 -53.071 1.00 36.48 ?  65  SER F N   1 
ATOM   2167 C CA  . SER B 2 65  ? 12.501  -22.523 -53.076 1.00 36.83 ?  65  SER F CA  1 
ATOM   2168 C C   . SER B 2 65  ? 11.083  -22.832 -53.518 1.00 45.11 ?  65  SER F C   1 
ATOM   2169 O O   . SER B 2 65  ? 10.831  -23.804 -54.239 1.00 44.83 ?  65  SER F O   1 
ATOM   2170 C CB  . SER B 2 65  ? 13.075  -21.466 -54.007 1.00 42.51 ?  65  SER F CB  1 
ATOM   2171 O OG  . SER B 2 65  ? 14.385  -21.125 -53.624 1.00 46.70 ?  65  SER F OG  1 
ATOM   2172 N N   . SER B 2 66  ? 10.159  -21.980 -53.088 1.00 42.77 ?  66  SER F N   1 
ATOM   2173 C CA  . SER B 2 66  ? 8.743   -22.160 -53.359 1.00 43.60 ?  66  SER F CA  1 
ATOM   2174 C C   . SER B 2 66  ? 8.061   -20.849 -53.002 1.00 46.26 ?  66  SER F C   1 
ATOM   2175 O O   . SER B 2 66  ? 7.763   -20.597 -51.829 1.00 42.74 ?  66  SER F O   1 
ATOM   2176 C CB  . SER B 2 66  ? 8.192   -23.346 -52.553 1.00 48.47 ?  66  SER F CB  1 
ATOM   2177 O OG  . SER B 2 66  ? 6.770   -23.363 -52.482 1.00 53.08 ?  66  SER F OG  1 
ATOM   2178 N N   . GLY B 2 67  ? 7.882   -19.982 -53.996 1.00 48.54 ?  67  GLY F N   1 
ATOM   2179 C CA  . GLY B 2 67  ? 7.256   -18.697 -53.772 1.00 46.59 ?  67  GLY F CA  1 
ATOM   2180 C C   . GLY B 2 67  ? 8.204   -17.702 -53.141 1.00 42.35 ?  67  GLY F C   1 
ATOM   2181 O O   . GLY B 2 67  ? 9.255   -17.373 -53.707 1.00 47.70 ?  67  GLY F O   1 
ATOM   2182 N N   . THR B 2 68  ? 7.847   -17.207 -51.958 1.00 40.85 ?  68  THR F N   1 
ATOM   2183 C CA  . THR B 2 68  ? 8.728   -16.327 -51.202 1.00 34.47 ?  68  THR F CA  1 
ATOM   2184 C C   . THR B 2 68  ? 9.407   -17.058 -50.055 1.00 32.12 ?  68  THR F C   1 
ATOM   2185 O O   . THR B 2 68  ? 9.882   -16.421 -49.112 1.00 30.57 ?  68  THR F O   1 
ATOM   2186 C CB  . THR B 2 68  ? 7.949   -15.134 -50.671 1.00 38.63 ?  68  THR F CB  1 
ATOM   2187 O OG1 . THR B 2 68  ? 6.881   -15.602 -49.839 1.00 34.77 ?  68  THR F OG1 1 
ATOM   2188 C CG2 . THR B 2 68  ? 7.386   -14.323 -51.842 1.00 36.04 ?  68  THR F CG2 1 
ATOM   2189 N N   . THR B 2 69  ? 9.442   -18.384 -50.108 1.00 32.74 ?  69  THR F N   1 
ATOM   2190 C CA  . THR B 2 69  ? 9.927   -19.203 -49.012 1.00 30.15 ?  69  THR F CA  1 
ATOM   2191 C C   . THR B 2 69  ? 11.060  -20.077 -49.524 1.00 33.42 ?  69  THR F C   1 
ATOM   2192 O O   . THR B 2 69  ? 10.985  -20.644 -50.620 1.00 32.85 ?  69  THR F O   1 
ATOM   2193 C CB  . THR B 2 69  ? 8.796   -20.074 -48.422 1.00 32.85 ?  69  THR F CB  1 
ATOM   2194 O OG1 . THR B 2 69  ? 7.783   -19.237 -47.836 1.00 34.05 ?  69  THR F OG1 1 
ATOM   2195 C CG2 . THR B 2 69  ? 9.328   -21.037 -47.363 1.00 32.64 ?  69  THR F CG2 1 
ATOM   2196 N N   . VAL B 2 70  ? 12.122  -20.156 -48.741 1.00 25.98 ?  70  VAL F N   1 
ATOM   2197 C CA  . VAL B 2 70  ? 13.222  -21.063 -49.006 1.00 28.72 ?  70  VAL F CA  1 
ATOM   2198 C C   . VAL B 2 70  ? 13.266  -22.058 -47.854 1.00 28.14 ?  70  VAL F C   1 
ATOM   2199 O O   . VAL B 2 70  ? 13.030  -21.682 -46.700 1.00 27.78 ?  70  VAL F O   1 
ATOM   2200 C CB  . VAL B 2 70  ? 14.533  -20.267 -49.137 1.00 29.61 ?  70  VAL F CB  1 
ATOM   2201 C CG1 . VAL B 2 70  ? 15.670  -21.165 -49.051 1.00 31.58 ?  70  VAL F CG1 1 
ATOM   2202 C CG2 . VAL B 2 70  ? 14.550  -19.472 -50.458 1.00 29.13 ?  70  VAL F CG2 1 
ATOM   2203 N N   . THR B 2 71  ? 13.534  -23.331 -48.155 1.00 26.13 ?  71  THR F N   1 
ATOM   2204 C CA  . THR B 2 71  ? 13.529  -24.358 -47.124 1.00 23.18 ?  71  THR F CA  1 
ATOM   2205 C C   . THR B 2 71  ? 14.889  -25.033 -47.106 1.00 25.78 ?  71  THR F C   1 
ATOM   2206 O O   . THR B 2 71  ? 15.316  -25.604 -48.118 1.00 23.54 ?  71  THR F O   1 
ATOM   2207 C CB  . THR B 2 71  ? 12.426  -25.395 -47.365 1.00 23.88 ?  71  THR F CB  1 
ATOM   2208 O OG1 . THR B 2 71  ? 11.145  -24.743 -47.312 1.00 25.78 ?  71  THR F OG1 1 
ATOM   2209 C CG2 . THR B 2 71  ? 12.489  -26.486 -46.285 1.00 25.25 ?  71  THR F CG2 1 
ATOM   2210 N N   . LEU B 2 72  ? 15.567  -24.944 -45.970 1.00 22.22 ?  72  LEU F N   1 
ATOM   2211 C CA  . LEU B 2 72  ? 16.785  -25.712 -45.751 1.00 25.19 ?  72  LEU F CA  1 
ATOM   2212 C C   . LEU B 2 72  ? 16.363  -27.069 -45.199 1.00 24.30 ?  72  LEU F C   1 
ATOM   2213 O O   . LEU B 2 72  ? 15.704  -27.145 -44.156 1.00 22.53 ?  72  LEU F O   1 
ATOM   2214 C CB  . LEU B 2 72  ? 17.725  -24.986 -44.793 1.00 21.25 ?  72  LEU F CB  1 
ATOM   2215 C CG  . LEU B 2 72  ? 18.928  -25.831 -44.354 1.00 23.18 ?  72  LEU F CG  1 
ATOM   2216 C CD1 . LEU B 2 72  ? 19.904  -26.045 -45.515 1.00 24.29 ?  72  LEU F CD1 1 
ATOM   2217 C CD2 . LEU B 2 72  ? 19.622  -25.201 -43.146 1.00 22.93 ?  72  LEU F CD2 1 
ATOM   2218 N N   . THR B 2 73  ? 16.706  -28.131 -45.908 1.00 24.69 ?  73  THR F N   1 
ATOM   2219 C CA  . THR B 2 73  ? 16.319  -29.473 -45.497 1.00 23.26 ?  73  THR F CA  1 
ATOM   2220 C C   . THR B 2 73  ? 17.562  -30.214 -45.026 1.00 26.74 ?  73  THR F C   1 
ATOM   2221 O O   . THR B 2 73  ? 18.588  -30.214 -45.718 1.00 25.02 ?  73  THR F O   1 
ATOM   2222 C CB  . THR B 2 73  ? 15.616  -30.218 -46.635 1.00 24.34 ?  73  THR F CB  1 
ATOM   2223 O OG1 . THR B 2 73  ? 14.392  -29.540 -46.970 1.00 25.75 ?  73  THR F OG1 1 
ATOM   2224 C CG2 . THR B 2 73  ? 15.273  -31.643 -46.202 1.00 28.67 ?  73  THR F CG2 1 
ATOM   2225 N N   . ILE B 2 74  ? 17.488  -30.787 -43.826 1.00 22.70 ?  74  ILE F N   1 
ATOM   2226 C CA  . ILE B 2 74  ? 18.563  -31.603 -43.277 1.00 25.08 ?  74  ILE F CA  1 
ATOM   2227 C C   . ILE B 2 74  ? 18.023  -33.025 -43.234 1.00 25.11 ?  74  ILE F C   1 
ATOM   2228 O O   . ILE B 2 74  ? 17.240  -33.371 -42.347 1.00 25.27 ?  74  ILE F O   1 
ATOM   2229 C CB  . ILE B 2 74  ? 19.000  -31.142 -41.886 1.00 24.14 ?  74  ILE F CB  1 
ATOM   2230 C CG1 . ILE B 2 74  ? 19.377  -29.659 -41.901 1.00 27.50 ?  74  ILE F CG1 1 
ATOM   2231 C CG2 . ILE B 2 74  ? 20.180  -31.997 -41.410 1.00 25.54 ?  74  ILE F CG2 1 
ATOM   2232 C CD1 . ILE B 2 74  ? 19.683  -29.119 -40.522 1.00 27.50 ?  74  ILE F CD1 1 
ATOM   2233 N N   . SER B 2 75  ? 18.394  -33.820 -44.221 1.00 23.71 ?  75  SER F N   1 
ATOM   2234 C CA  . SER B 2 75  ? 17.973  -35.216 -44.280 1.00 26.10 ?  75  SER F CA  1 
ATOM   2235 C C   . SER B 2 75  ? 18.771  -36.046 -43.283 1.00 27.82 ?  75  SER F C   1 
ATOM   2236 O O   . SER B 2 75  ? 19.925  -35.733 -42.981 1.00 28.91 ?  75  SER F O   1 
ATOM   2237 C CB  . SER B 2 75  ? 18.175  -35.746 -45.695 1.00 27.37 ?  75  SER F CB  1 
ATOM   2238 O OG  . SER B 2 75  ? 17.174  -35.194 -46.542 1.00 36.29 ?  75  SER F OG  1 
ATOM   2239 N N   . ALA B 2 76  ? 18.143  -37.113 -42.777 1.00 23.34 ?  76  ALA F N   1 
ATOM   2240 C CA  . ALA B 2 76  ? 18.793  -38.077 -41.883 1.00 24.61 ?  76  ALA F CA  1 
ATOM   2241 C C   . ALA B 2 76  ? 19.652  -37.372 -40.832 1.00 25.37 ?  76  ALA F C   1 
ATOM   2242 O O   . ALA B 2 76  ? 20.868  -37.558 -40.760 1.00 28.22 ?  76  ALA F O   1 
ATOM   2243 C CB  . ALA B 2 76  ? 19.636  -39.076 -42.678 1.00 25.97 ?  76  ALA F CB  1 
ATOM   2244 N N   . ALA B 2 77  ? 18.986  -36.569 -40.003 1.00 27.90 ?  77  ALA F N   1 
ATOM   2245 C CA  . ALA B 2 77  ? 19.678  -35.643 -39.113 1.00 25.34 ?  77  ALA F CA  1 
ATOM   2246 C C   . ALA B 2 77  ? 20.589  -36.383 -38.141 1.00 29.45 ?  77  ALA F C   1 
ATOM   2247 O O   . ALA B 2 77  ? 20.213  -37.406 -37.564 1.00 28.15 ?  77  ALA F O   1 
ATOM   2248 C CB  . ALA B 2 77  ? 18.657  -34.805 -38.350 1.00 26.40 ?  77  ALA F CB  1 
ATOM   2249 N N   . GLN B 2 78  ? 21.790  -35.838 -37.973 1.00 27.94 ?  78  GLN F N   1 
ATOM   2250 C CA  . GLN B 2 78  ? 22.804  -36.439 -37.081 1.00 28.41 ?  78  GLN F CA  1 
ATOM   2251 C C   . GLN B 2 78  ? 22.962  -35.555 -35.840 1.00 30.86 ?  78  GLN F C   1 
ATOM   2252 O O   . GLN B 2 78  ? 22.709  -34.360 -35.929 1.00 27.54 ?  78  GLN F O   1 
ATOM   2253 C CB  . GLN B 2 78  ? 24.126  -36.529 -37.837 1.00 28.10 ?  78  GLN F CB  1 
ATOM   2254 C CG  . GLN B 2 78  ? 24.047  -37.318 -39.129 1.00 30.91 ?  78  GLN F CG  1 
ATOM   2255 C CD  . GLN B 2 78  ? 23.944  -38.792 -38.836 1.00 33.77 ?  78  GLN F CD  1 
ATOM   2256 O OE1 . GLN B 2 78  ? 24.830  -39.382 -38.227 1.00 35.47 ?  78  GLN F OE1 1 
ATOM   2257 N NE2 . GLN B 2 78  ? 22.845  -39.392 -39.257 1.00 32.89 ?  78  GLN F NE2 1 
ATOM   2258 N N   . ALA B 2 79  ? 23.368  -36.158 -34.726 1.00 28.16 ?  79  ALA F N   1 
ATOM   2259 C CA  . ALA B 2 79  ? 23.540  -35.375 -33.502 1.00 30.77 ?  79  ALA F CA  1 
ATOM   2260 C C   . ALA B 2 79  ? 24.429  -34.155 -33.735 1.00 30.87 ?  79  ALA F C   1 
ATOM   2261 O O   . ALA B 2 79  ? 24.198  -33.088 -33.151 1.00 30.58 ?  79  ALA F O   1 
ATOM   2262 C CB  . ALA B 2 79  ? 24.131  -36.245 -32.392 1.00 34.34 ?  79  ALA F CB  1 
ATOM   2263 N N   . GLU B 2 80  ? 25.428  -34.280 -34.604 1.00 28.44 ?  80  GLU F N   1 
ATOM   2264 C CA  . GLU B 2 80  ? 26.323  -33.159 -34.862 1.00 31.66 ?  80  GLU F CA  1 
ATOM   2265 C C   . GLU B 2 80  ? 25.654  -32.030 -35.638 1.00 32.49 ?  80  GLU F C   1 
ATOM   2266 O O   . GLU B 2 80  ? 26.233  -30.942 -35.733 1.00 30.37 ?  80  GLU F O   1 
ATOM   2267 C CB  . GLU B 2 80  ? 27.589  -33.661 -35.583 1.00 32.89 ?  80  GLU F CB  1 
ATOM   2268 C CG  . GLU B 2 80  ? 27.347  -34.576 -36.775 1.00 39.49 ?  80  GLU F CG  1 
ATOM   2269 C CD  . GLU B 2 80  ? 27.347  -36.097 -36.436 1.00 43.46 ?  80  GLU F CD  1 
ATOM   2270 O OE1 . GLU B 2 80  ? 26.752  -36.543 -35.412 1.00 38.28 ?  80  GLU F OE1 1 
ATOM   2271 O OE2 . GLU B 2 80  ? 27.941  -36.864 -37.232 1.00 51.96 ?  80  GLU F OE2 1 
ATOM   2272 N N   . ASP B 2 81  ? 24.437  -32.239 -36.152 1.00 27.79 ?  81  ASP F N   1 
ATOM   2273 C CA  . ASP B 2 81  ? 23.711  -31.196 -36.861 1.00 25.87 ?  81  ASP F CA  1 
ATOM   2274 C C   . ASP B 2 81  ? 22.991  -30.247 -35.916 1.00 24.64 ?  81  ASP F C   1 
ATOM   2275 O O   . ASP B 2 81  ? 22.476  -29.208 -36.368 1.00 28.14 ?  81  ASP F O   1 
ATOM   2276 C CB  . ASP B 2 81  ? 22.695  -31.831 -37.822 1.00 26.37 ?  81  ASP F CB  1 
ATOM   2277 C CG  . ASP B 2 81  ? 23.358  -32.643 -38.922 1.00 30.53 ?  81  ASP F CG  1 
ATOM   2278 O OD1 . ASP B 2 81  ? 24.531  -32.363 -39.263 1.00 28.16 ?  81  ASP F OD1 1 
ATOM   2279 O OD2 . ASP B 2 81  ? 22.702  -33.571 -39.467 1.00 31.30 ?  81  ASP F OD2 1 
ATOM   2280 N N   . GLU B 2 82  ? 22.917  -30.579 -34.622 1.00 25.56 ?  82  GLU F N   1 
ATOM   2281 C CA  . GLU B 2 82  ? 22.317  -29.683 -33.641 1.00 28.91 ?  82  GLU F CA  1 
ATOM   2282 C C   . GLU B 2 82  ? 23.118  -28.382 -33.597 1.00 30.20 ?  82  GLU F C   1 
ATOM   2283 O O   . GLU B 2 82  ? 24.337  -28.404 -33.388 1.00 28.79 ?  82  GLU F O   1 
ATOM   2284 C CB  . GLU B 2 82  ? 22.277  -30.358 -32.264 1.00 29.88 ?  82  GLU F CB  1 
ATOM   2285 C CG  . GLU B 2 82  ? 21.685  -29.479 -31.166 1.00 30.08 ?  82  GLU F CG  1 
ATOM   2286 C CD  . GLU B 2 82  ? 21.054  -30.251 -30.005 1.00 40.27 ?  82  GLU F CD  1 
ATOM   2287 O OE1 . GLU B 2 82  ? 20.367  -31.283 -30.216 1.00 33.58 ?  82  GLU F OE1 1 
ATOM   2288 O OE2 . GLU B 2 82  ? 21.267  -29.810 -28.856 1.00 44.38 ?  82  GLU F OE2 1 
ATOM   2289 N N   . ALA B 2 83  ? 22.441  -27.262 -33.823 1.00 23.92 ?  83  ALA F N   1 
ATOM   2290 C CA  . ALA B 2 83  ? 23.095  -25.977 -34.035 1.00 23.01 ?  83  ALA F CA  1 
ATOM   2291 C C   . ALA B 2 83  ? 22.018  -24.931 -34.263 1.00 27.43 ?  83  ALA F C   1 
ATOM   2292 O O   . ALA B 2 83  ? 20.833  -25.249 -34.428 1.00 23.77 ?  83  ALA F O   1 
ATOM   2293 C CB  . ALA B 2 83  ? 24.039  -26.007 -35.240 1.00 23.30 ?  83  ALA F CB  1 
ATOM   2294 N N   . ASP B 2 84  ? 22.454  -23.665 -34.285 1.00 24.52 ?  84  ASP F N   1 
ATOM   2295 C CA  . ASP B 2 84  ? 21.602  -22.584 -34.729 1.00 25.43 ?  84  ASP F CA  1 
ATOM   2296 C C   . ASP B 2 84  ? 21.866  -22.350 -36.206 1.00 24.21 ?  84  ASP F C   1 
ATOM   2297 O O   . ASP B 2 84  ? 23.010  -22.410 -36.656 1.00 25.03 ?  84  ASP F O   1 
ATOM   2298 C CB  . ASP B 2 84  ? 21.866  -21.307 -33.930 1.00 24.28 ?  84  ASP F CB  1 
ATOM   2299 C CG  . ASP B 2 84  ? 21.582  -21.477 -32.450 1.00 29.74 ?  84  ASP F CG  1 
ATOM   2300 O OD1 . ASP B 2 84  ? 20.524  -22.017 -32.104 1.00 32.19 ?  84  ASP F OD1 1 
ATOM   2301 O OD2 . ASP B 2 84  ? 22.379  -21.012 -31.615 1.00 34.59 ?  84  ASP F OD2 1 
ATOM   2302 N N   . TYR B 2 85  ? 20.799  -22.147 -36.970 1.00 21.65 ?  85  TYR F N   1 
ATOM   2303 C CA  . TYR B 2 85  ? 20.883  -21.941 -38.415 1.00 21.23 ?  85  TYR F CA  1 
ATOM   2304 C C   . TYR B 2 85  ? 20.308  -20.565 -38.718 1.00 22.27 ?  85  TYR F C   1 
ATOM   2305 O O   . TYR B 2 85  ? 19.156  -20.288 -38.379 1.00 21.94 ?  85  TYR F O   1 
ATOM   2306 C CB  . TYR B 2 85  ? 20.134  -23.039 -39.184 1.00 21.33 ?  85  TYR F CB  1 
ATOM   2307 C CG  . TYR B 2 85  ? 20.806  -24.391 -39.061 1.00 19.69 ?  85  TYR F CG  1 
ATOM   2308 C CD1 . TYR B 2 85  ? 20.616  -25.189 -37.933 1.00 20.91 ?  85  TYR F CD1 1 
ATOM   2309 C CD2 . TYR B 2 85  ? 21.669  -24.836 -40.034 1.00 20.45 ?  85  TYR F CD2 1 
ATOM   2310 C CE1 . TYR B 2 85  ? 21.249  -26.405 -37.796 1.00 24.07 ?  85  TYR F CE1 1 
ATOM   2311 C CE2 . TYR B 2 85  ? 22.314  -26.066 -39.907 1.00 19.39 ?  85  TYR F CE2 1 
ATOM   2312 C CZ  . TYR B 2 85  ? 22.108  -26.831 -38.779 1.00 20.99 ?  85  TYR F CZ  1 
ATOM   2313 O OH  . TYR B 2 85  ? 22.737  -28.039 -38.648 1.00 22.52 ?  85  TYR F OH  1 
ATOM   2314 N N   . TYR B 2 86  ? 21.110  -19.705 -39.339 1.00 21.02 ?  86  TYR F N   1 
ATOM   2315 C CA  . TYR B 2 86  ? 20.696  -18.347 -39.686 1.00 20.97 ?  86  TYR F CA  1 
ATOM   2316 C C   . TYR B 2 86  ? 20.501  -18.236 -41.190 1.00 20.02 ?  86  TYR F C   1 
ATOM   2317 O O   . TYR B 2 86  ? 21.402  -18.585 -41.952 1.00 22.87 ?  86  TYR F O   1 
ATOM   2318 C CB  . TYR B 2 86  ? 21.740  -17.315 -39.216 1.00 21.92 ?  86  TYR F CB  1 
ATOM   2319 C CG  . TYR B 2 86  ? 21.863  -17.267 -37.705 1.00 20.76 ?  86  TYR F CG  1 
ATOM   2320 C CD1 . TYR B 2 86  ? 22.732  -18.118 -37.046 1.00 22.61 ?  86  TYR F CD1 1 
ATOM   2321 C CD2 . TYR B 2 86  ? 21.067  -16.398 -36.942 1.00 24.00 ?  86  TYR F CD2 1 
ATOM   2322 C CE1 . TYR B 2 86  ? 22.843  -18.112 -35.673 1.00 23.34 ?  86  TYR F CE1 1 
ATOM   2323 C CE2 . TYR B 2 86  ? 21.169  -16.388 -35.557 1.00 25.50 ?  86  TYR F CE2 1 
ATOM   2324 C CZ  . TYR B 2 86  ? 22.064  -17.251 -34.941 1.00 22.46 ?  86  TYR F CZ  1 
ATOM   2325 O OH  . TYR B 2 86  ? 22.211  -17.287 -33.574 1.00 26.20 ?  86  TYR F OH  1 
ATOM   2326 N N   . CYS B 2 87  ? 19.327  -17.762 -41.632 1.00 21.19 ?  87  CYS F N   1 
ATOM   2327 C CA  . CYS B 2 87  ? 19.285  -17.381 -43.039 1.00 21.23 ?  87  CYS F CA  1 
ATOM   2328 C C   . CYS B 2 87  ? 19.640  -15.908 -43.188 1.00 23.07 ?  87  CYS F C   1 
ATOM   2329 O O   . CYS B 2 87  ? 19.588  -15.124 -42.237 1.00 23.74 ?  87  CYS F O   1 
ATOM   2330 C CB  . CYS B 2 87  ? 17.927  -17.671 -43.683 1.00 25.49 ?  87  CYS F CB  1 
ATOM   2331 S SG  . CYS B 2 87  ? 16.526  -16.811 -43.004 1.00 27.55 ?  87  CYS F SG  1 
ATOM   2332 N N   . GLN B 2 88  ? 20.039  -15.544 -44.397 1.00 20.69 ?  88  GLN F N   1 
ATOM   2333 C CA  . GLN B 2 88  ? 20.604  -14.220 -44.626 1.00 19.78 ?  88  GLN F CA  1 
ATOM   2334 C C   . GLN B 2 88  ? 20.371  -13.839 -46.079 1.00 19.33 ?  88  GLN F C   1 
ATOM   2335 O O   . GLN B 2 88  ? 20.485  -14.686 -46.976 1.00 22.04 ?  88  GLN F O   1 
ATOM   2336 C CB  . GLN B 2 88  ? 22.113  -14.212 -44.305 1.00 19.83 ?  88  GLN F CB  1 
ATOM   2337 C CG  . GLN B 2 88  ? 22.821  -12.871 -44.573 1.00 21.95 ?  88  GLN F CG  1 
ATOM   2338 C CD  . GLN B 2 88  ? 23.657  -12.897 -45.846 1.00 21.66 ?  88  GLN F CD  1 
ATOM   2339 O OE1 . GLN B 2 88  ? 24.542  -13.758 -46.035 1.00 22.32 ?  88  GLN F OE1 1 
ATOM   2340 N NE2 . GLN B 2 88  ? 23.379  -11.960 -46.733 1.00 22.88 ?  88  GLN F NE2 1 
ATOM   2341 N N   . SER B 2 89  ? 20.103  -12.556 -46.318 1.00 19.84 ?  89  SER F N   1 
ATOM   2342 C CA  . SER B 2 89  ? 19.996  -12.053 -47.677 1.00 19.95 ?  89  SER F CA  1 
ATOM   2343 C C   . SER B 2 89  ? 20.493  -10.606 -47.688 1.00 19.90 ?  89  SER F C   1 
ATOM   2344 O O   . SER B 2 89  ? 20.990  -10.089 -46.685 1.00 20.13 ?  89  SER F O   1 
ATOM   2345 C CB  . SER B 2 89  ? 18.549  -12.183 -48.205 1.00 21.18 ?  89  SER F CB  1 
ATOM   2346 O OG  . SER B 2 89  ? 18.511  -12.020 -49.619 1.00 23.13 ?  89  SER F OG  1 
ATOM   2347 N N   . VAL B 2 90  ? 20.372  -9.960  -48.840 1.00 22.38 ?  90  VAL F N   1 
ATOM   2348 C CA  . VAL B 2 90  ? 20.877  -8.601  -49.024 1.00 20.33 ?  90  VAL F CA  1 
ATOM   2349 C C   . VAL B 2 90  ? 19.961  -7.928  -50.038 1.00 27.21 ?  90  VAL F C   1 
ATOM   2350 O O   . VAL B 2 90  ? 19.321  -8.592  -50.856 1.00 32.63 ?  90  VAL F O   1 
ATOM   2351 C CB  . VAL B 2 90  ? 22.368  -8.624  -49.467 1.00 25.61 ?  90  VAL F CB  1 
ATOM   2352 C CG1 . VAL B 2 90  ? 22.520  -9.390  -50.779 1.00 34.36 ?  90  VAL F CG1 1 
ATOM   2353 C CG2 . VAL B 2 90  ? 22.989  -7.221  -49.539 1.00 28.37 ?  90  VAL F CG2 1 
ATOM   2354 N N   . ASP B 2 91  ? 19.858  -6.612  -49.973 1.00 24.33 ?  91  ASP F N   1 
ATOM   2355 C CA  . ASP B 2 91  ? 19.134  -5.946  -51.035 1.00 26.45 ?  91  ASP F CA  1 
ATOM   2356 C C   . ASP B 2 91  ? 20.141  -5.423  -52.055 1.00 29.04 ?  91  ASP F C   1 
ATOM   2357 O O   . ASP B 2 91  ? 21.355  -5.607  -51.921 1.00 24.72 ?  91  ASP F O   1 
ATOM   2358 C CB  . ASP B 2 91  ? 18.187  -4.885  -50.461 1.00 25.69 ?  91  ASP F CB  1 
ATOM   2359 C CG  . ASP B 2 91  ? 18.903  -3.738  -49.787 1.00 28.36 ?  91  ASP F CG  1 
ATOM   2360 O OD1 . ASP B 2 91  ? 20.136  -3.551  -49.999 1.00 26.32 ?  91  ASP F OD1 1 
ATOM   2361 O OD2 . ASP B 2 91  ? 18.205  -2.997  -49.038 1.00 27.32 ?  91  ASP F OD2 1 
ATOM   2362 N N   . SER B 2 92  ? 19.628  -4.822  -53.124 1.00 28.18 ?  92  SER F N   1 
ATOM   2363 C CA  . SER B 2 92  ? 20.531  -4.406  -54.187 1.00 29.42 ?  92  SER F CA  1 
ATOM   2364 C C   . SER B 2 92  ? 21.423  -3.226  -53.784 1.00 28.94 ?  92  SER F C   1 
ATOM   2365 O O   . SER B 2 92  ? 22.464  -3.014  -54.418 1.00 31.16 ?  92  SER F O   1 
ATOM   2366 C CB  . SER B 2 92  ? 19.704  -4.120  -55.443 1.00 35.52 ?  92  SER F CB  1 
ATOM   2367 O OG  . SER B 2 92  ? 19.056  -2.880  -55.336 1.00 43.02 ?  92  SER F OG  1 
ATOM   2368 N N   . SER B 2 93  ? 21.089  -2.507  -52.711 1.00 25.54 ?  93  SER F N   1 
ATOM   2369 C CA  . SER B 2 93  ? 21.933  -1.429  -52.199 1.00 25.84 ?  93  SER F CA  1 
ATOM   2370 C C   . SER B 2 93  ? 23.004  -1.902  -51.220 1.00 27.09 ?  93  SER F C   1 
ATOM   2371 O O   . SER B 2 93  ? 23.837  -1.090  -50.806 1.00 26.69 ?  93  SER F O   1 
ATOM   2372 C CB  . SER B 2 93  ? 21.084  -0.362  -51.500 1.00 30.08 ?  93  SER F CB  1 
ATOM   2373 O OG  . SER B 2 93  ? 20.197  0.270   -52.416 1.00 29.33 ?  93  SER F OG  1 
ATOM   2374 N N   . GLY B 2 94  ? 23.011  -3.173  -50.829 1.00 25.46 ?  94  GLY F N   1 
ATOM   2375 C CA  . GLY B 2 94  ? 24.038  -3.670  -49.929 1.00 24.61 ?  94  GLY F CA  1 
ATOM   2376 C C   . GLY B 2 94  ? 23.649  -3.787  -48.468 1.00 22.60 ?  94  GLY F C   1 
ATOM   2377 O O   . GLY B 2 94  ? 24.525  -4.027  -47.629 1.00 23.24 ?  94  GLY F O   1 
ATOM   2378 N N   . THR B 2 95  ? 22.387  -3.573  -48.116 1.00 20.35 ?  95  THR F N   1 
ATOM   2379 C CA  . THR B 2 95  ? 21.981  -3.826  -46.745 1.00 18.25 ?  95  THR F CA  1 
ATOM   2380 C C   . THR B 2 95  ? 21.849  -5.330  -46.545 1.00 20.65 ?  95  THR F C   1 
ATOM   2381 O O   . THR B 2 95  ? 21.157  -5.996  -47.318 1.00 24.87 ?  95  THR F O   1 
ATOM   2382 C CB  . THR B 2 95  ? 20.663  -3.127  -46.438 1.00 22.59 ?  95  THR F CB  1 
ATOM   2383 O OG1 . THR B 2 95  ? 20.892  -1.707  -46.554 1.00 22.25 ?  95  THR F OG1 1 
ATOM   2384 C CG2 . THR B 2 95  ? 20.185  -3.469  -45.047 1.00 23.05 ?  95  THR F CG2 1 
ATOM   2385 N N   . TYR B 2 96  ? 22.480  -5.837  -45.498 1.00 19.38 ?  96  TYR F N   1 
ATOM   2386 C CA  . TYR B 2 96  ? 22.458  -7.256  -45.140 1.00 19.91 ?  96  TYR F CA  1 
ATOM   2387 C C   . TYR B 2 96  ? 21.390  -7.478  -44.082 1.00 22.69 ?  96  TYR F C   1 
ATOM   2388 O O   . TYR B 2 96  ? 21.224  -6.649  -43.180 1.00 22.21 ?  96  TYR F O   1 
ATOM   2389 C CB  . TYR B 2 96  ? 23.833  -7.710  -44.598 1.00 20.33 ?  96  TYR F CB  1 
ATOM   2390 C CG  . TYR B 2 96  ? 24.825  -8.019  -45.697 1.00 22.89 ?  96  TYR F CG  1 
ATOM   2391 C CD1 . TYR B 2 96  ? 25.297  -7.014  -46.533 1.00 20.87 ?  96  TYR F CD1 1 
ATOM   2392 C CD2 . TYR B 2 96  ? 25.245  -9.325  -45.940 1.00 22.21 ?  96  TYR F CD2 1 
ATOM   2393 C CE1 . TYR B 2 96  ? 26.178  -7.293  -47.564 1.00 19.92 ?  96  TYR F CE1 1 
ATOM   2394 C CE2 . TYR B 2 96  ? 26.120  -9.621  -46.977 1.00 19.12 ?  96  TYR F CE2 1 
ATOM   2395 C CZ  . TYR B 2 96  ? 26.575  -8.600  -47.788 1.00 23.60 ?  96  TYR F CZ  1 
ATOM   2396 O OH  . TYR B 2 96  ? 27.439  -8.864  -48.825 1.00 21.18 ?  96  TYR F OH  1 
ATOM   2397 N N   . VAL B 2 97  ? 20.649  -8.587  -44.205 1.00 19.10 ?  97  VAL F N   1 
ATOM   2398 C CA  . VAL B 2 97  ? 19.600  -8.925  -43.252 1.00 20.74 ?  97  VAL F CA  1 
ATOM   2399 C C   . VAL B 2 97  ? 19.762  -10.377 -42.834 1.00 19.42 ?  97  VAL F C   1 
ATOM   2400 O O   . VAL B 2 97  ? 19.883  -11.255 -43.693 1.00 22.06 ?  97  VAL F O   1 
ATOM   2401 C CB  . VAL B 2 97  ? 18.201  -8.700  -43.851 1.00 24.12 ?  97  VAL F CB  1 
ATOM   2402 C CG1 . VAL B 2 97  ? 17.119  -9.211  -42.911 1.00 22.36 ?  97  VAL F CG1 1 
ATOM   2403 C CG2 . VAL B 2 97  ? 17.976  -7.204  -44.156 1.00 25.75 ?  97  VAL F CG2 1 
ATOM   2404 N N   . PHE B 2 98  ? 19.714  -10.624 -41.522 1.00 22.61 ?  98  PHE F N   1 
ATOM   2405 C CA  . PHE B 2 98  ? 19.723  -11.967 -40.945 1.00 22.45 ?  98  PHE F CA  1 
ATOM   2406 C C   . PHE B 2 98  ? 18.336  -12.268 -40.382 1.00 24.67 ?  98  PHE F C   1 
ATOM   2407 O O   . PHE B 2 98  ? 17.680  -11.381 -39.819 1.00 24.48 ?  98  PHE F O   1 
ATOM   2408 C CB  . PHE B 2 98  ? 20.727  -12.064 -39.787 1.00 24.60 ?  98  PHE F CB  1 
ATOM   2409 C CG  . PHE B 2 98  ? 22.168  -12.107 -40.217 1.00 24.00 ?  98  PHE F CG  1 
ATOM   2410 C CD1 . PHE B 2 98  ? 22.783  -13.292 -40.592 1.00 22.24 ?  98  PHE F CD1 1 
ATOM   2411 C CD2 . PHE B 2 98  ? 22.917  -10.939 -40.196 1.00 25.71 ?  98  PHE F CD2 1 
ATOM   2412 C CE1 . PHE B 2 98  ? 24.121  -13.307 -40.973 1.00 23.49 ?  98  PHE F CE1 1 
ATOM   2413 C CE2 . PHE B 2 98  ? 24.277  -10.942 -40.578 1.00 28.52 ?  98  PHE F CE2 1 
ATOM   2414 C CZ  . PHE B 2 98  ? 24.868  -12.130 -40.972 1.00 26.26 ?  98  PHE F CZ  1 
ATOM   2415 N N   . GLY B 2 99  ? 17.900  -13.523 -40.504 1.00 23.99 ?  99  GLY F N   1 
ATOM   2416 C CA  . GLY B 2 99  ? 16.745  -13.966 -39.744 1.00 24.74 ?  99  GLY F CA  1 
ATOM   2417 C C   . GLY B 2 99  ? 17.123  -14.096 -38.279 1.00 26.75 ?  99  GLY F C   1 
ATOM   2418 O O   . GLY B 2 99  ? 18.288  -13.956 -37.905 1.00 23.81 ?  99  GLY F O   1 
ATOM   2419 N N   . ILE B 2 100 ? 16.126  -14.390 -37.433 1.00 22.51 ?  100 ILE F N   1 
ATOM   2420 C CA  . ILE B 2 100 ? 16.389  -14.509 -35.996 1.00 24.69 ?  100 ILE F CA  1 
ATOM   2421 C C   . ILE B 2 100 ? 17.272  -15.708 -35.638 1.00 27.56 ?  100 ILE F C   1 
ATOM   2422 O O   . ILE B 2 100 ? 17.809  -15.768 -34.520 1.00 28.11 ?  100 ILE F O   1 
ATOM   2423 C CB  . ILE B 2 100 ? 15.069  -14.609 -35.200 1.00 26.20 ?  100 ILE F CB  1 
ATOM   2424 C CG1 . ILE B 2 100 ? 14.296  -15.876 -35.642 1.00 28.63 ?  100 ILE F CG1 1 
ATOM   2425 C CG2 . ILE B 2 100 ? 14.299  -13.298 -35.316 1.00 30.68 ?  100 ILE F CG2 1 
ATOM   2426 C CD1 . ILE B 2 100 ? 13.102  -16.265 -34.757 1.00 33.30 ?  100 ILE F CD1 1 
ATOM   2427 N N   . GLY B 2 101 ? 17.440  -16.666 -36.540 1.00 23.11 ?  101 GLY F N   1 
ATOM   2428 C CA  . GLY B 2 101 ? 18.158  -17.882 -36.213 1.00 21.16 ?  101 GLY F CA  1 
ATOM   2429 C C   . GLY B 2 101 ? 17.201  -18.948 -35.700 1.00 24.03 ?  101 GLY F C   1 
ATOM   2430 O O   . GLY B 2 101 ? 16.343  -18.668 -34.857 1.00 25.12 ?  101 GLY F O   1 
ATOM   2431 N N   . THR B 2 102 ? 17.319  -20.162 -36.226 1.00 24.87 ?  102 THR F N   1 
ATOM   2432 C CA  . THR B 2 102 ? 16.506  -21.295 -35.788 1.00 25.48 ?  102 THR F CA  1 
ATOM   2433 C C   . THR B 2 102 ? 17.382  -22.235 -34.976 1.00 23.71 ?  102 THR F C   1 
ATOM   2434 O O   . THR B 2 102 ? 18.374  -22.758 -35.496 1.00 22.38 ?  102 THR F O   1 
ATOM   2435 C CB  . THR B 2 102 ? 15.905  -22.048 -36.978 1.00 22.24 ?  102 THR F CB  1 
ATOM   2436 O OG1 . THR B 2 102 ? 15.068  -21.169 -37.752 1.00 24.24 ?  102 THR F OG1 1 
ATOM   2437 C CG2 . THR B 2 102 ? 15.080  -23.254 -36.485 1.00 22.76 ?  102 THR F CG2 1 
ATOM   2438 N N   . LYS B 2 103 ? 17.024  -22.452 -33.711 1.00 21.89 ?  103 LYS F N   1 
ATOM   2439 C CA  . LYS B 2 103 ? 17.710  -23.474 -32.923 1.00 26.72 ?  103 LYS F CA  1 
ATOM   2440 C C   . LYS B 2 103 ? 17.184  -24.835 -33.341 1.00 27.78 ?  103 LYS F C   1 
ATOM   2441 O O   . LYS B 2 103 ? 16.014  -25.165 -33.092 1.00 23.51 ?  103 LYS F O   1 
ATOM   2442 C CB  . LYS B 2 103 ? 17.539  -23.252 -31.420 1.00 27.97 ?  103 LYS F CB  1 
ATOM   2443 C CG  . LYS B 2 103 ? 18.231  -24.350 -30.576 1.00 32.70 ?  103 LYS F CG  1 
ATOM   2444 C CD  . LYS B 2 103 ? 19.589  -24.813 -31.156 1.00 36.97 ?  103 LYS F CD  1 
ATOM   2445 C CE  . LYS B 2 103 ? 20.445  -25.665 -30.187 1.00 39.98 ?  103 LYS F CE  1 
ATOM   2446 N NZ  . LYS B 2 103 ? 21.911  -25.345 -30.276 1.00 44.27 ?  103 LYS F NZ  1 
ATOM   2447 N N   . VAL B 2 104 ? 18.030  -25.615 -33.995 1.00 23.95 ?  104 VAL F N   1 
ATOM   2448 C CA  . VAL B 2 104 ? 17.661  -26.969 -34.389 1.00 24.97 ?  104 VAL F CA  1 
ATOM   2449 C C   . VAL B 2 104 ? 18.187  -27.931 -33.336 1.00 29.16 ?  104 VAL F C   1 
ATOM   2450 O O   . VAL B 2 104 ? 19.400  -28.142 -33.208 1.00 27.83 ?  104 VAL F O   1 
ATOM   2451 C CB  . VAL B 2 104 ? 18.174  -27.329 -35.786 1.00 25.31 ?  104 VAL F CB  1 
ATOM   2452 C CG1 . VAL B 2 104 ? 17.947  -28.824 -36.029 1.00 28.25 ?  104 VAL F CG1 1 
ATOM   2453 C CG2 . VAL B 2 104 ? 17.426  -26.528 -36.829 1.00 26.23 ?  104 VAL F CG2 1 
ATOM   2454 N N   . THR B 2 105 ? 17.263  -28.522 -32.589 1.00 25.33 ?  105 THR F N   1 
ATOM   2455 C CA  . THR B 2 105 ? 17.577  -29.551 -31.607 1.00 25.08 ?  105 THR F CA  1 
ATOM   2456 C C   . THR B 2 105 ? 17.383  -30.907 -32.266 1.00 26.17 ?  105 THR F C   1 
ATOM   2457 O O   . THR B 2 105 ? 16.328  -31.172 -32.856 1.00 25.95 ?  105 THR F O   1 
ATOM   2458 C CB  . THR B 2 105 ? 16.687  -29.444 -30.368 1.00 29.97 ?  105 THR F CB  1 
ATOM   2459 O OG1 . THR B 2 105 ? 16.930  -28.193 -29.708 1.00 30.27 ?  105 THR F OG1 1 
ATOM   2460 C CG2 . THR B 2 105 ? 16.950  -30.606 -29.400 1.00 27.65 ?  105 THR F CG2 1 
ATOM   2461 N N   . VAL B 2 106 ? 18.413  -31.744 -32.204 1.00 27.14 ?  106 VAL F N   1 
ATOM   2462 C CA  . VAL B 2 106 ? 18.286  -33.141 -32.596 1.00 28.55 ?  106 VAL F CA  1 
ATOM   2463 C C   . VAL B 2 106 ? 17.885  -33.873 -31.319 1.00 29.89 ?  106 VAL F C   1 
ATOM   2464 O O   . VAL B 2 106 ? 18.727  -34.183 -30.466 1.00 27.86 ?  106 VAL F O   1 
ATOM   2465 C CB  . VAL B 2 106 ? 19.571  -33.680 -33.218 1.00 28.11 ?  106 VAL F CB  1 
ATOM   2466 C CG1 . VAL B 2 106 ? 19.406  -35.133 -33.607 1.00 29.31 ?  106 VAL F CG1 1 
ATOM   2467 C CG2 . VAL B 2 106 ? 19.931  -32.848 -34.441 1.00 27.75 ?  106 VAL F CG2 1 
ATOM   2468 N N   . LEU B 2 107 ? 16.580  -34.084 -31.170 1.00 28.47 ?  107 LEU F N   1 
ATOM   2469 C CA  . LEU B 2 107 ? 15.974  -34.435 -29.888 1.00 28.73 ?  107 LEU F CA  1 
ATOM   2470 C C   . LEU B 2 107 ? 15.986  -35.950 -29.751 1.00 29.50 ?  107 LEU F C   1 
ATOM   2471 O O   . LEU B 2 107 ? 15.173  -36.650 -30.369 1.00 28.93 ?  107 LEU F O   1 
ATOM   2472 C CB  . LEU B 2 107 ? 14.564  -33.867 -29.787 1.00 27.50 ?  107 LEU F CB  1 
ATOM   2473 C CG  . LEU B 2 107 ? 13.845  -34.197 -28.474 1.00 28.94 ?  107 LEU F CG  1 
ATOM   2474 C CD1 . LEU B 2 107 ? 14.501  -33.438 -27.314 1.00 28.99 ?  107 LEU F CD1 1 
ATOM   2475 C CD2 . LEU B 2 107 ? 12.380  -33.840 -28.573 1.00 30.29 ?  107 LEU F CD2 1 
ATOM   2476 N N   . GLY B 2 108 ? 16.934  -36.460 -28.962 1.00 29.06 ?  108 GLY F N   1 
ATOM   2477 C CA  . GLY B 2 108 ? 17.027  -37.896 -28.758 1.00 28.59 ?  108 GLY F CA  1 
ATOM   2478 C C   . GLY B 2 108 ? 15.747  -38.474 -28.186 1.00 24.15 ?  108 GLY F C   1 
ATOM   2479 O O   . GLY B 2 108 ? 14.931  -37.781 -27.577 1.00 26.93 ?  108 GLY F O   1 
ATOM   2480 N N   . ARG B 2 109 ? 15.567  -39.781 -28.392 1.00 26.56 ?  109 ARG F N   1 
ATOM   2481 C CA  . ARG B 2 109 ? 14.384  -40.465 -27.882 1.00 27.98 ?  109 ARG F CA  1 
ATOM   2482 C C   . ARG B 2 109 ? 14.527  -40.863 -26.426 1.00 28.92 ?  109 ARG F C   1 
ATOM   2483 O O   . ARG B 2 109 ? 13.513  -41.071 -25.743 1.00 28.12 ?  109 ARG F O   1 
ATOM   2484 C CB  . ARG B 2 109 ? 14.092  -41.712 -28.720 1.00 28.02 ?  109 ARG F CB  1 
ATOM   2485 C CG  . ARG B 2 109 ? 13.628  -41.366 -30.119 1.00 36.71 ?  109 ARG F CG  1 
ATOM   2486 C CD  . ARG B 2 109 ? 13.605  -42.583 -31.004 1.00 38.24 ?  109 ARG F CD  1 
ATOM   2487 N NE  . ARG B 2 109 ? 12.996  -42.286 -32.292 1.00 39.89 ?  109 ARG F NE  1 
ATOM   2488 C CZ  . ARG B 2 109 ? 13.659  -41.875 -33.362 1.00 42.76 ?  109 ARG F CZ  1 
ATOM   2489 N NH1 . ARG B 2 109 ? 14.982  -41.725 -33.345 1.00 35.87 ?  109 ARG F NH1 1 
ATOM   2490 N NH2 . ARG B 2 109 ? 12.980  -41.613 -34.482 1.00 42.61 ?  109 ARG F NH2 1 
ATOM   2491 N N   . THR B 2 110 ? 15.756  -40.977 -25.943 1.00 23.92 ?  110 THR F N   1 
ATOM   2492 C CA  . THR B 2 110 ? 15.981  -41.388 -24.568 1.00 26.55 ?  110 THR F CA  1 
ATOM   2493 C C   . THR B 2 110 ? 15.640  -40.267 -23.610 1.00 29.05 ?  110 THR F C   1 
ATOM   2494 O O   . THR B 2 110 ? 16.075  -39.128 -23.798 1.00 31.40 ?  110 THR F O   1 
ATOM   2495 C CB  . THR B 2 110 ? 17.432  -41.805 -24.383 1.00 29.11 ?  110 THR F CB  1 
ATOM   2496 O OG1 . THR B 2 110 ? 17.677  -42.975 -25.176 1.00 32.16 ?  110 THR F OG1 1 
ATOM   2497 C CG2 . THR B 2 110 ? 17.694  -42.113 -22.911 1.00 29.44 ?  110 THR F CG2 1 
ATOM   2498 N N   . VAL B 2 111 ? 14.854  -40.590 -22.587 1.00 25.19 ?  111 VAL F N   1 
ATOM   2499 C CA  . VAL B 2 111 ? 14.528  -39.660 -21.512 1.00 27.48 ?  111 VAL F CA  1 
ATOM   2500 C C   . VAL B 2 111 ? 15.282  -40.126 -20.276 1.00 31.39 ?  111 VAL F C   1 
ATOM   2501 O O   . VAL B 2 111 ? 14.995  -41.204 -19.739 1.00 29.03 ?  111 VAL F O   1 
ATOM   2502 C CB  . VAL B 2 111 ? 13.018  -39.594 -21.252 1.00 30.12 ?  111 VAL F CB  1 
ATOM   2503 C CG1 . VAL B 2 111 ? 12.715  -38.548 -20.192 1.00 33.12 ?  111 VAL F CG1 1 
ATOM   2504 C CG2 . VAL B 2 111 ? 12.269  -39.281 -22.554 1.00 30.72 ?  111 VAL F CG2 1 
ATOM   2505 N N   . ALA B 2 112 ? 16.245  -39.325 -19.822 1.00 27.90 ?  112 ALA F N   1 
ATOM   2506 C CA  . ALA B 2 112 ? 17.055  -39.639 -18.650 1.00 28.68 ?  112 ALA F CA  1 
ATOM   2507 C C   . ALA B 2 112 ? 16.661  -38.706 -17.510 1.00 28.17 ?  112 ALA F C   1 
ATOM   2508 O O   . ALA B 2 112 ? 16.778  -37.485 -17.640 1.00 26.53 ?  112 ALA F O   1 
ATOM   2509 C CB  . ALA B 2 112 ? 18.543  -39.500 -18.966 1.00 27.83 ?  112 ALA F CB  1 
ATOM   2510 N N   . ALA B 2 113 ? 16.162  -39.278 -16.415 1.00 28.35 ?  113 ALA F N   1 
ATOM   2511 C CA  . ALA B 2 113 ? 15.796  -38.470 -15.263 1.00 28.24 ?  113 ALA F CA  1 
ATOM   2512 C C   . ALA B 2 113 ? 17.051  -37.991 -14.532 1.00 27.03 ?  113 ALA F C   1 
ATOM   2513 O O   . ALA B 2 113 ? 18.062  -38.693 -14.501 1.00 27.75 ?  113 ALA F O   1 
ATOM   2514 C CB  . ALA B 2 113 ? 14.923  -39.269 -14.297 1.00 29.12 ?  113 ALA F CB  1 
ATOM   2515 N N   . PRO B 2 114 ? 17.005  -36.811 -13.920 1.00 24.49 ?  114 PRO F N   1 
ATOM   2516 C CA  . PRO B 2 114 ? 18.172  -36.317 -13.182 1.00 27.06 ?  114 PRO F CA  1 
ATOM   2517 C C   . PRO B 2 114 ? 18.371  -37.030 -11.857 1.00 30.54 ?  114 PRO F C   1 
ATOM   2518 O O   . PRO B 2 114 ? 17.410  -37.405 -11.177 1.00 27.69 ?  114 PRO F O   1 
ATOM   2519 C CB  . PRO B 2 114 ? 17.840  -34.833 -12.955 1.00 27.25 ?  114 PRO F CB  1 
ATOM   2520 C CG  . PRO B 2 114 ? 16.346  -34.813 -12.879 1.00 28.96 ?  114 PRO F CG  1 
ATOM   2521 C CD  . PRO B 2 114 ? 15.903  -35.832 -13.930 1.00 27.92 ?  114 PRO F CD  1 
ATOM   2522 N N   . SER B 2 115 ? 19.645  -37.233 -11.516 1.00 29.75 ?  115 SER F N   1 
ATOM   2523 C CA  . SER B 2 115 ? 20.067  -37.446 -10.139 1.00 29.53 ?  115 SER F CA  1 
ATOM   2524 C C   . SER B 2 115 ? 20.080  -36.090 -9.444  1.00 33.24 ?  115 SER F C   1 
ATOM   2525 O O   . SER B 2 115 ? 20.458  -35.088 -10.049 1.00 34.29 ?  115 SER F O   1 
ATOM   2526 C CB  . SER B 2 115 ? 21.467  -38.061 -10.093 1.00 35.26 ?  115 SER F CB  1 
ATOM   2527 O OG  . SER B 2 115 ? 21.420  -39.441 -10.400 1.00 46.61 ?  115 SER F OG  1 
ATOM   2528 N N   . VAL B 2 116 ? 19.638  -36.042 -8.189  1.00 29.84 ?  116 VAL F N   1 
ATOM   2529 C CA  . VAL B 2 116 ? 19.505  -34.776 -7.476  1.00 29.53 ?  116 VAL F CA  1 
ATOM   2530 C C   . VAL B 2 116 ? 20.343  -34.829 -6.210  1.00 30.95 ?  116 VAL F C   1 
ATOM   2531 O O   . VAL B 2 116 ? 20.282  -35.810 -5.464  1.00 31.02 ?  116 VAL F O   1 
ATOM   2532 C CB  . VAL B 2 116 ? 18.034  -34.457 -7.151  1.00 32.05 ?  116 VAL F CB  1 
ATOM   2533 C CG1 . VAL B 2 116 ? 17.925  -33.043 -6.642  1.00 31.32 ?  116 VAL F CG1 1 
ATOM   2534 C CG2 . VAL B 2 116 ? 17.168  -34.632 -8.404  1.00 32.43 ?  116 VAL F CG2 1 
ATOM   2535 N N   . PHE B 2 117 ? 21.121  -33.770 -5.974  1.00 29.35 ?  117 PHE F N   1 
ATOM   2536 C CA  . PHE B 2 117 ? 21.982  -33.637 -4.809  1.00 28.82 ?  117 PHE F CA  1 
ATOM   2537 C C   . PHE B 2 117 ? 21.809  -32.235 -4.242  1.00 31.00 ?  117 PHE F C   1 
ATOM   2538 O O   . PHE B 2 117 ? 21.572  -31.285 -4.990  1.00 31.93 ?  117 PHE F O   1 
ATOM   2539 C CB  . PHE B 2 117 ? 23.459  -33.843 -5.175  1.00 30.52 ?  117 PHE F CB  1 
ATOM   2540 C CG  . PHE B 2 117 ? 23.740  -35.127 -5.909  1.00 33.24 ?  117 PHE F CG  1 
ATOM   2541 C CD1 . PHE B 2 117 ? 23.638  -35.182 -7.288  1.00 34.97 ?  117 PHE F CD1 1 
ATOM   2542 C CD2 . PHE B 2 117 ? 24.130  -36.268 -5.221  1.00 35.69 ?  117 PHE F CD2 1 
ATOM   2543 C CE1 . PHE B 2 117 ? 23.914  -36.368 -7.975  1.00 36.92 ?  117 PHE F CE1 1 
ATOM   2544 C CE2 . PHE B 2 117 ? 24.414  -37.453 -5.898  1.00 37.32 ?  117 PHE F CE2 1 
ATOM   2545 C CZ  . PHE B 2 117 ? 24.301  -37.502 -7.274  1.00 36.36 ?  117 PHE F CZ  1 
ATOM   2546 N N   . ILE B 2 118 ? 21.936  -32.092 -2.923  1.00 30.38 ?  118 ILE F N   1 
ATOM   2547 C CA  . ILE B 2 118 ? 21.810  -30.776 -2.295  1.00 31.44 ?  118 ILE F CA  1 
ATOM   2548 C C   . ILE B 2 118 ? 22.985  -30.556 -1.348  1.00 33.78 ?  118 ILE F C   1 
ATOM   2549 O O   . ILE B 2 118 ? 23.442  -31.488 -0.676  1.00 33.34 ?  118 ILE F O   1 
ATOM   2550 C CB  . ILE B 2 118 ? 20.437  -30.604 -1.590  1.00 30.57 ?  118 ILE F CB  1 
ATOM   2551 C CG1 . ILE B 2 118 ? 20.231  -29.143 -1.158  1.00 33.18 ?  118 ILE F CG1 1 
ATOM   2552 C CG2 . ILE B 2 118 ? 20.238  -31.609 -0.449  1.00 32.88 ?  118 ILE F CG2 1 
ATOM   2553 C CD1 . ILE B 2 118 ? 18.802  -28.830 -0.719  1.00 32.06 ?  118 ILE F CD1 1 
ATOM   2554 N N   . PHE B 2 119 ? 23.522  -29.337 -1.351  1.00 30.88 ?  119 PHE F N   1 
ATOM   2555 C CA  . PHE B 2 119 ? 24.708  -29.003 -0.566  1.00 33.70 ?  119 PHE F CA  1 
ATOM   2556 C C   . PHE B 2 119 ? 24.412  -27.865 0.403   1.00 34.27 ?  119 PHE F C   1 
ATOM   2557 O O   . PHE B 2 119 ? 24.060  -26.758 -0.042  1.00 32.96 ?  119 PHE F O   1 
ATOM   2558 C CB  . PHE B 2 119 ? 25.877  -28.605 -1.479  1.00 34.79 ?  119 PHE F CB  1 
ATOM   2559 C CG  . PHE B 2 119 ? 26.286  -29.669 -2.453  1.00 34.13 ?  119 PHE F CG  1 
ATOM   2560 C CD1 . PHE B 2 119 ? 27.136  -30.696 -2.064  1.00 37.76 ?  119 PHE F CD1 1 
ATOM   2561 C CD2 . PHE B 2 119 ? 25.827  -29.638 -3.760  1.00 36.44 ?  119 PHE F CD2 1 
ATOM   2562 C CE1 . PHE B 2 119 ? 27.516  -31.670 -2.958  1.00 35.43 ?  119 PHE F CE1 1 
ATOM   2563 C CE2 . PHE B 2 119 ? 26.208  -30.617 -4.664  1.00 35.51 ?  119 PHE F CE2 1 
ATOM   2564 C CZ  . PHE B 2 119 ? 27.046  -31.630 -4.261  1.00 35.25 ?  119 PHE F CZ  1 
ATOM   2565 N N   . PRO B 2 120 ? 24.554  -28.066 1.710   1.00 35.35 ?  120 PRO F N   1 
ATOM   2566 C CA  . PRO B 2 120 ? 24.446  -26.948 2.656   1.00 34.14 ?  120 PRO F CA  1 
ATOM   2567 C C   . PRO B 2 120 ? 25.603  -25.982 2.478   1.00 34.50 ?  120 PRO F C   1 
ATOM   2568 O O   . PRO B 2 120 ? 26.630  -26.341 1.879   1.00 36.33 ?  120 PRO F O   1 
ATOM   2569 C CB  . PRO B 2 120 ? 24.510  -27.643 4.027   1.00 35.36 ?  120 PRO F CB  1 
ATOM   2570 C CG  . PRO B 2 120 ? 24.143  -29.079 3.748   1.00 39.45 ?  120 PRO F CG  1 
ATOM   2571 C CD  . PRO B 2 120 ? 24.761  -29.344 2.406   1.00 36.64 ?  120 PRO F CD  1 
ATOM   2572 N N   . PRO B 2 121 ? 25.490  -24.758 2.984   1.00 36.65 ?  121 PRO F N   1 
ATOM   2573 C CA  . PRO B 2 121 ? 26.626  -23.833 2.914   1.00 37.55 ?  121 PRO F CA  1 
ATOM   2574 C C   . PRO B 2 121 ? 27.787  -24.357 3.747   1.00 38.15 ?  121 PRO F C   1 
ATOM   2575 O O   . PRO B 2 121 ? 27.600  -25.083 4.723   1.00 39.96 ?  121 PRO F O   1 
ATOM   2576 C CB  . PRO B 2 121 ? 26.063  -22.525 3.501   1.00 37.40 ?  121 PRO F CB  1 
ATOM   2577 C CG  . PRO B 2 121 ? 24.577  -22.672 3.397   1.00 39.89 ?  121 PRO F CG  1 
ATOM   2578 C CD  . PRO B 2 121 ? 24.334  -24.133 3.654   1.00 35.68 ?  121 PRO F CD  1 
ATOM   2579 N N   . SER B 2 122 ? 28.999  -24.001 3.337   1.00 35.93 ?  122 SER F N   1 
ATOM   2580 C CA  . SER B 2 122 ? 30.173  -24.361 4.114   1.00 41.38 ?  122 SER F CA  1 
ATOM   2581 C C   . SER B 2 122 ? 30.284  -23.452 5.334   1.00 45.98 ?  122 SER F C   1 
ATOM   2582 O O   . SER B 2 122 ? 29.871  -22.288 5.303   1.00 44.10 ?  122 SER F O   1 
ATOM   2583 C CB  . SER B 2 122 ? 31.437  -24.243 3.268   1.00 39.36 ?  122 SER F CB  1 
ATOM   2584 O OG  . SER B 2 122 ? 31.608  -22.914 2.815   1.00 42.64 ?  122 SER F OG  1 
ATOM   2585 N N   . ASP B 2 123 ? 30.838  -23.993 6.423   1.00 47.57 ?  123 ASP F N   1 
ATOM   2586 C CA  . ASP B 2 123 ? 31.059  -23.163 7.606   1.00 51.31 ?  123 ASP F CA  1 
ATOM   2587 C C   . ASP B 2 123 ? 31.988  -21.997 7.287   1.00 49.60 ?  123 ASP F C   1 
ATOM   2588 O O   . ASP B 2 123 ? 31.882  -20.927 7.893   1.00 50.57 ?  123 ASP F O   1 
ATOM   2589 C CB  . ASP B 2 123 ? 31.635  -24.004 8.748   1.00 54.46 ?  123 ASP F CB  1 
ATOM   2590 C CG  . ASP B 2 123 ? 30.698  -25.132 9.179   1.00 62.79 ?  123 ASP F CG  1 
ATOM   2591 O OD1 . ASP B 2 123 ? 29.697  -24.843 9.887   1.00 60.21 ?  123 ASP F OD1 1 
ATOM   2592 O OD2 . ASP B 2 123 ? 30.965  -26.299 8.830   1.00 65.93 ?  123 ASP F OD2 1 
ATOM   2593 N N   . GLU B 2 124 ? 32.863  -22.179 6.302   1.00 49.16 ?  124 GLU F N   1 
ATOM   2594 C CA  . GLU B 2 124 ? 33.804  -21.148 5.882   1.00 47.38 ?  124 GLU F CA  1 
ATOM   2595 C C   . GLU B 2 124 ? 33.085  -19.972 5.235   1.00 46.48 ?  124 GLU F C   1 
ATOM   2596 O O   . GLU B 2 124 ? 33.407  -18.807 5.502   1.00 46.72 ?  124 GLU F O   1 
ATOM   2597 C CB  . GLU B 2 124 ? 34.782  -21.793 4.914   1.00 48.85 ?  124 GLU F CB  1 
ATOM   2598 C CG  . GLU B 2 124 ? 35.568  -22.905 5.575   1.00 55.47 ?  124 GLU F CG  1 
ATOM   2599 C CD  . GLU B 2 124 ? 35.550  -24.172 4.737   1.00 56.60 ?  124 GLU F CD  1 
ATOM   2600 O OE1 . GLU B 2 124 ? 34.497  -24.859 4.763   1.00 54.45 ?  124 GLU F OE1 1 
ATOM   2601 O OE2 . GLU B 2 124 ? 36.566  -24.483 4.075   1.00 56.06 ?  124 GLU F OE2 1 
ATOM   2602 N N   . GLN B 2 125 ? 32.123  -20.254 4.352   1.00 42.98 ?  125 GLN F N   1 
ATOM   2603 C CA  . GLN B 2 125 ? 31.347  -19.165 3.777   1.00 42.85 ?  125 GLN F CA  1 
ATOM   2604 C C   . GLN B 2 125 ? 30.478  -18.514 4.833   1.00 43.39 ?  125 GLN F C   1 
ATOM   2605 O O   . GLN B 2 125 ? 30.262  -17.300 4.802   1.00 45.24 ?  125 GLN F O   1 
ATOM   2606 C CB  . GLN B 2 125 ? 30.483  -19.659 2.619   1.00 39.40 ?  125 GLN F CB  1 
ATOM   2607 C CG  . GLN B 2 125 ? 29.894  -18.515 1.796   1.00 39.60 ?  125 GLN F CG  1 
ATOM   2608 C CD  . GLN B 2 125 ? 28.809  -18.965 0.847   1.00 39.46 ?  125 GLN F CD  1 
ATOM   2609 O OE1 . GLN B 2 125 ? 28.348  -20.105 0.910   1.00 39.05 ?  125 GLN F OE1 1 
ATOM   2610 N NE2 . GLN B 2 125 ? 28.413  -18.077 -0.061  1.00 36.99 ?  125 GLN F NE2 1 
ATOM   2611 N N   . LEU B 2 126 ? 29.948  -19.314 5.761   1.00 44.72 ?  126 LEU F N   1 
ATOM   2612 C CA  . LEU B 2 126 ? 29.076  -18.762 6.791   1.00 45.90 ?  126 LEU F CA  1 
ATOM   2613 C C   . LEU B 2 126 ? 29.815  -17.715 7.622   1.00 49.04 ?  126 LEU F C   1 
ATOM   2614 O O   . LEU B 2 126 ? 29.239  -16.686 7.993   1.00 48.71 ?  126 LEU F O   1 
ATOM   2615 C CB  . LEU B 2 126 ? 28.536  -19.896 7.664   1.00 46.18 ?  126 LEU F CB  1 
ATOM   2616 C CG  . LEU B 2 126 ? 27.427  -20.724 6.998   1.00 44.93 ?  126 LEU F CG  1 
ATOM   2617 C CD1 . LEU B 2 126 ? 27.007  -21.912 7.852   1.00 45.43 ?  126 LEU F CD1 1 
ATOM   2618 C CD2 . LEU B 2 126 ? 26.229  -19.842 6.684   1.00 44.88 ?  126 LEU F CD2 1 
ATOM   2619 N N   . LYS B 2 127 ? 31.108  -17.942 7.878   1.00 48.55 ?  127 LYS F N   1 
ATOM   2620 C CA  . LYS B 2 127 ? 31.911  -16.975 8.621   1.00 50.51 ?  127 LYS F CA  1 
ATOM   2621 C C   . LYS B 2 127 ? 32.012  -15.640 7.893   1.00 53.70 ?  127 LYS F C   1 
ATOM   2622 O O   . LYS B 2 127 ? 32.225  -14.601 8.530   1.00 57.45 ?  127 LYS F O   1 
ATOM   2623 C CB  . LYS B 2 127 ? 33.311  -17.541 8.879   1.00 50.16 ?  127 LYS F CB  1 
ATOM   2624 C CG  . LYS B 2 127 ? 33.342  -18.750 9.810   1.00 53.69 ?  127 LYS F CG  1 
ATOM   2625 C CD  . LYS B 2 127 ? 34.775  -19.066 10.241  1.00 58.64 ?  127 LYS F CD  1 
ATOM   2626 C CE  . LYS B 2 127 ? 34.968  -20.549 10.566  1.00 60.10 ?  127 LYS F CE  1 
ATOM   2627 N NZ  . LYS B 2 127 ? 36.132  -20.782 11.475  1.00 62.14 ?  127 LYS F NZ  1 
ATOM   2628 N N   . SER B 2 128 ? 31.862  -15.639 6.573   1.00 52.27 ?  128 SER F N   1 
ATOM   2629 C CA  . SER B 2 128 ? 31.957  -14.420 5.784   1.00 49.07 ?  128 SER F CA  1 
ATOM   2630 C C   . SER B 2 128 ? 30.633  -13.673 5.669   1.00 50.97 ?  128 SER F C   1 
ATOM   2631 O O   . SER B 2 128 ? 30.596  -12.609 5.043   1.00 51.83 ?  128 SER F O   1 
ATOM   2632 C CB  . SER B 2 128 ? 32.501  -14.746 4.387   1.00 51.88 ?  128 SER F CB  1 
ATOM   2633 O OG  . SER B 2 128 ? 31.462  -15.142 3.506   1.00 53.37 ?  128 SER F OG  1 
ATOM   2634 N N   . GLY B 2 129 ? 29.555  -14.191 6.252   1.00 48.13 ?  129 GLY F N   1 
ATOM   2635 C CA  . GLY B 2 129 ? 28.295  -13.482 6.289   1.00 46.67 ?  129 GLY F CA  1 
ATOM   2636 C C   . GLY B 2 129 ? 27.291  -13.849 5.217   1.00 48.43 ?  129 GLY F C   1 
ATOM   2637 O O   . GLY B 2 129 ? 26.270  -13.155 5.086   1.00 46.77 ?  129 GLY F O   1 
ATOM   2638 N N   . THR B 2 130 ? 27.532  -14.917 4.461   1.00 47.18 ?  130 THR F N   1 
ATOM   2639 C CA  . THR B 2 130 ? 26.662  -15.291 3.355   1.00 43.72 ?  130 THR F CA  1 
ATOM   2640 C C   . THR B 2 130 ? 26.483  -16.801 3.369   1.00 41.93 ?  130 THR F C   1 
ATOM   2641 O O   . THR B 2 130 ? 27.360  -17.541 3.822   1.00 42.80 ?  130 THR F O   1 
ATOM   2642 C CB  . THR B 2 130 ? 27.243  -14.808 2.008   1.00 45.77 ?  130 THR F CB  1 
ATOM   2643 O OG1 . THR B 2 130 ? 27.409  -13.385 2.055   1.00 50.77 ?  130 THR F OG1 1 
ATOM   2644 C CG2 . THR B 2 130 ? 26.311  -15.130 0.850   1.00 43.57 ?  130 THR F CG2 1 
ATOM   2645 N N   . ALA B 2 131 ? 25.319  -17.249 2.897   1.00 37.84 ?  131 ALA F N   1 
ATOM   2646 C CA  . ALA B 2 131 ? 25.005  -18.669 2.783   1.00 40.82 ?  131 ALA F CA  1 
ATOM   2647 C C   . ALA B 2 131 ? 24.554  -18.959 1.359   1.00 38.15 ?  131 ALA F C   1 
ATOM   2648 O O   . ALA B 2 131 ? 23.541  -18.420 0.906   1.00 36.29 ?  131 ALA F O   1 
ATOM   2649 C CB  . ALA B 2 131 ? 23.920  -19.077 3.785   1.00 40.10 ?  131 ALA F CB  1 
ATOM   2650 N N   . SER B 2 132 ? 25.322  -19.783 0.648   1.00 37.89 ?  132 SER F N   1 
ATOM   2651 C CA  . SER B 2 132 ? 24.938  -20.279 -0.667  1.00 36.16 ?  132 SER F CA  1 
ATOM   2652 C C   . SER B 2 132 ? 24.546  -21.739 -0.506  1.00 32.95 ?  132 SER F C   1 
ATOM   2653 O O   . SER B 2 132 ? 25.348  -22.550 -0.024  1.00 34.55 ?  132 SER F O   1 
ATOM   2654 C CB  . SER B 2 132 ? 26.080  -20.143 -1.678  1.00 34.69 ?  132 SER F CB  1 
ATOM   2655 O OG  . SER B 2 132 ? 26.447  -18.789 -1.878  1.00 39.19 ?  132 SER F OG  1 
ATOM   2656 N N   . VAL B 2 133 ? 23.321  -22.070 -0.894  1.00 33.69 ?  133 VAL F N   1 
ATOM   2657 C CA  . VAL B 2 133 ? 22.830  -23.439 -0.852  1.00 33.75 ?  133 VAL F CA  1 
ATOM   2658 C C   . VAL B 2 133 ? 22.697  -23.900 -2.298  1.00 34.53 ?  133 VAL F C   1 
ATOM   2659 O O   . VAL B 2 133 ? 22.114  -23.188 -3.127  1.00 33.18 ?  133 VAL F O   1 
ATOM   2660 C CB  . VAL B 2 133 ? 21.483  -23.528 -0.116  1.00 33.01 ?  133 VAL F CB  1 
ATOM   2661 C CG1 . VAL B 2 133 ? 21.034  -24.974 0.027   1.00 33.96 ?  133 VAL F CG1 1 
ATOM   2662 C CG2 . VAL B 2 133 ? 21.541  -22.799 1.230   1.00 35.33 ?  133 VAL F CG2 1 
ATOM   2663 N N   . VAL B 2 134 ? 23.244  -25.075 -2.609  1.00 34.06 ?  134 VAL F N   1 
ATOM   2664 C CA  . VAL B 2 134 ? 23.410  -25.502 -3.995  1.00 32.23 ?  134 VAL F CA  1 
ATOM   2665 C C   . VAL B 2 134 ? 22.635  -26.789 -4.222  1.00 34.06 ?  134 VAL F C   1 
ATOM   2666 O O   . VAL B 2 134 ? 22.772  -27.751 -3.457  1.00 30.95 ?  134 VAL F O   1 
ATOM   2667 C CB  . VAL B 2 134 ? 24.891  -25.686 -4.359  1.00 34.21 ?  134 VAL F CB  1 
ATOM   2668 C CG1 . VAL B 2 134 ? 25.021  -26.330 -5.741  1.00 34.20 ?  134 VAL F CG1 1 
ATOM   2669 C CG2 . VAL B 2 134 ? 25.618  -24.335 -4.319  1.00 32.20 ?  134 VAL F CG2 1 
ATOM   2670 N N   . CYS B 2 135 ? 21.817  -26.792 -5.270  1.00 33.53 ?  135 CYS F N   1 
ATOM   2671 C CA  . CYS B 2 135 ? 21.093  -27.967 -5.729  1.00 32.06 ?  135 CYS F CA  1 
ATOM   2672 C C   . CYS B 2 135 ? 21.669  -28.387 -7.078  1.00 32.68 ?  135 CYS F C   1 
ATOM   2673 O O   . CYS B 2 135 ? 21.793  -27.554 -7.981  1.00 37.41 ?  135 CYS F O   1 
ATOM   2674 C CB  . CYS B 2 135 ? 19.599  -27.646 -5.840  1.00 34.89 ?  135 CYS F CB  1 
ATOM   2675 S SG  . CYS B 2 135 ? 18.543  -29.014 -6.374  1.00 40.16 ?  135 CYS F SG  1 
ATOM   2676 N N   . LEU B 2 136 ? 22.041  -29.659 -7.205  1.00 32.72 ?  136 LEU F N   1 
ATOM   2677 C CA  . LEU B 2 136 ? 22.658  -30.185 -8.419  1.00 33.01 ?  136 LEU F CA  1 
ATOM   2678 C C   . LEU B 2 136 ? 21.754  -31.235 -9.054  1.00 33.51 ?  136 LEU F C   1 
ATOM   2679 O O   . LEU B 2 136 ? 21.309  -32.171 -8.377  1.00 29.67 ?  136 LEU F O   1 
ATOM   2680 C CB  . LEU B 2 136 ? 24.030  -30.802 -8.136  1.00 31.34 ?  136 LEU F CB  1 
ATOM   2681 C CG  . LEU B 2 136 ? 24.594  -31.677 -9.267  1.00 32.99 ?  136 LEU F CG  1 
ATOM   2682 C CD1 . LEU B 2 136 ? 25.073  -30.825 -10.444 1.00 33.06 ?  136 LEU F CD1 1 
ATOM   2683 C CD2 . LEU B 2 136 ? 25.703  -32.621 -8.789  1.00 34.23 ?  136 LEU F CD2 1 
ATOM   2684 N N   . LEU B 2 137 ? 21.483  -31.066 -10.349 1.00 31.84 ?  137 LEU F N   1 
ATOM   2685 C CA  . LEU B 2 137 ? 20.824  -32.067 -11.181 1.00 28.82 ?  137 LEU F CA  1 
ATOM   2686 C C   . LEU B 2 137 ? 21.862  -32.647 -12.132 1.00 29.62 ?  137 LEU F C   1 
ATOM   2687 O O   . LEU B 2 137 ? 22.573  -31.895 -12.805 1.00 32.59 ?  137 LEU F O   1 
ATOM   2688 C CB  . LEU B 2 137 ? 19.675  -31.429 -11.974 1.00 29.02 ?  137 LEU F CB  1 
ATOM   2689 C CG  . LEU B 2 137 ? 18.347  -31.167 -11.282 1.00 30.91 ?  137 LEU F CG  1 
ATOM   2690 C CD1 . LEU B 2 137 ? 18.517  -30.210 -10.105 1.00 34.36 ?  137 LEU F CD1 1 
ATOM   2691 C CD2 . LEU B 2 137 ? 17.389  -30.555 -12.301 1.00 34.23 ?  137 LEU F CD2 1 
ATOM   2692 N N   . ASN B 2 138 ? 21.964  -33.969 -12.199 1.00 30.81 ?  138 ASN F N   1 
ATOM   2693 C CA  . ASN B 2 138 ? 23.020  -34.582 -12.994 1.00 29.06 ?  138 ASN F CA  1 
ATOM   2694 C C   . ASN B 2 138 ? 22.452  -35.605 -13.968 1.00 30.83 ?  138 ASN F C   1 
ATOM   2695 O O   . ASN B 2 138 ? 21.517  -36.331 -13.628 1.00 27.78 ?  138 ASN F O   1 
ATOM   2696 C CB  . ASN B 2 138 ? 24.057  -35.250 -12.085 1.00 32.32 ?  138 ASN F CB  1 
ATOM   2697 C CG  . ASN B 2 138 ? 25.282  -35.729 -12.845 1.00 38.02 ?  138 ASN F CG  1 
ATOM   2698 O OD1 . ASN B 2 138 ? 26.023  -34.930 -13.427 1.00 43.39 ?  138 ASN F OD1 1 
ATOM   2699 N ND2 . ASN B 2 138 ? 25.517  -37.038 -12.821 1.00 40.62 ?  138 ASN F ND2 1 
ATOM   2700 N N   . ASN B 2 139 ? 23.025  -35.649 -15.181 1.00 32.28 ?  139 ASN F N   1 
ATOM   2701 C CA  . ASN B 2 139 ? 22.817  -36.742 -16.148 1.00 32.52 ?  139 ASN F CA  1 
ATOM   2702 C C   . ASN B 2 139 ? 21.356  -36.822 -16.586 1.00 28.36 ?  139 ASN F C   1 
ATOM   2703 O O   . ASN B 2 139 ? 20.733  -37.876 -16.526 1.00 31.51 ?  139 ASN F O   1 
ATOM   2704 C CB  . ASN B 2 139 ? 23.309  -38.088 -15.575 1.00 32.53 ?  139 ASN F CB  1 
ATOM   2705 C CG  . ASN B 2 139 ? 23.175  -39.282 -16.567 1.00 34.99 ?  139 ASN F CG  1 
ATOM   2706 O OD1 . ASN B 2 139 ? 22.503  -40.276 -16.267 1.00 31.66 ?  139 ASN F OD1 1 
ATOM   2707 N ND2 . ASN B 2 139 ? 23.802  -39.177 -17.732 1.00 34.65 ?  139 ASN F ND2 1 
ATOM   2708 N N   . PHE B 2 140 ? 20.797  -35.688 -17.015 1.00 27.68 ?  140 PHE F N   1 
ATOM   2709 C CA  . PHE B 2 140 ? 19.405  -35.698 -17.450 1.00 26.88 ?  140 PHE F CA  1 
ATOM   2710 C C   . PHE B 2 140 ? 19.277  -35.274 -18.907 1.00 26.10 ?  140 PHE F C   1 
ATOM   2711 O O   . PHE B 2 140 ? 20.146  -34.601 -19.473 1.00 28.56 ?  140 PHE F O   1 
ATOM   2712 C CB  . PHE B 2 140 ? 18.505  -34.830 -16.536 1.00 25.76 ?  140 PHE F CB  1 
ATOM   2713 C CG  . PHE B 2 140 ? 18.805  -33.347 -16.573 1.00 26.54 ?  140 PHE F CG  1 
ATOM   2714 C CD1 . PHE B 2 140 ? 19.736  -32.792 -15.698 1.00 24.76 ?  140 PHE F CD1 1 
ATOM   2715 C CD2 . PHE B 2 140 ? 18.098  -32.502 -17.417 1.00 27.21 ?  140 PHE F CD2 1 
ATOM   2716 C CE1 . PHE B 2 140 ? 20.012  -31.441 -15.716 1.00 27.20 ?  140 PHE F CE1 1 
ATOM   2717 C CE2 . PHE B 2 140 ? 18.353  -31.134 -17.425 1.00 26.73 ?  140 PHE F CE2 1 
ATOM   2718 C CZ  . PHE B 2 140 ? 19.306  -30.600 -16.565 1.00 27.72 ?  140 PHE F CZ  1 
ATOM   2719 N N   . TYR B 2 141 ? 18.169  -35.709 -19.517 1.00 28.71 ?  141 TYR F N   1 
ATOM   2720 C CA  . TYR B 2 141 ? 17.868  -35.417 -20.905 1.00 27.38 ?  141 TYR F CA  1 
ATOM   2721 C C   . TYR B 2 141 ? 16.381  -35.665 -21.098 1.00 24.94 ?  141 TYR F C   1 
ATOM   2722 O O   . TYR B 2 141 ? 15.875  -36.674 -20.595 1.00 27.36 ?  141 TYR F O   1 
ATOM   2723 C CB  . TYR B 2 141 ? 18.686  -36.315 -21.848 1.00 25.09 ?  141 TYR F CB  1 
ATOM   2724 C CG  . TYR B 2 141 ? 18.564  -35.855 -23.271 1.00 27.99 ?  141 TYR F CG  1 
ATOM   2725 C CD1 . TYR B 2 141 ? 19.413  -34.866 -23.763 1.00 31.74 ?  141 TYR F CD1 1 
ATOM   2726 C CD2 . TYR B 2 141 ? 17.586  -36.379 -24.121 1.00 27.71 ?  141 TYR F CD2 1 
ATOM   2727 C CE1 . TYR B 2 141 ? 19.294  -34.409 -25.051 1.00 33.09 ?  141 TYR F CE1 1 
ATOM   2728 C CE2 . TYR B 2 141 ? 17.460  -35.934 -25.414 1.00 30.20 ?  141 TYR F CE2 1 
ATOM   2729 C CZ  . TYR B 2 141 ? 18.319  -34.943 -25.876 1.00 33.84 ?  141 TYR F CZ  1 
ATOM   2730 O OH  . TYR B 2 141 ? 18.223  -34.473 -27.165 1.00 31.63 ?  141 TYR F OH  1 
ATOM   2731 N N   . PRO B 2 142 ? 15.645  -34.775 -21.784 1.00 29.38 ?  142 PRO F N   1 
ATOM   2732 C CA  . PRO B 2 142 ? 16.080  -33.527 -22.429 1.00 27.71 ?  142 PRO F CA  1 
ATOM   2733 C C   . PRO B 2 142 ? 16.382  -32.409 -21.448 1.00 28.59 ?  142 PRO F C   1 
ATOM   2734 O O   . PRO B 2 142 ? 16.334  -32.567 -20.233 1.00 28.17 ?  142 PRO F O   1 
ATOM   2735 C CB  . PRO B 2 142 ? 14.886  -33.179 -23.334 1.00 29.04 ?  142 PRO F CB  1 
ATOM   2736 C CG  . PRO B 2 142 ? 13.712  -33.738 -22.598 1.00 32.78 ?  142 PRO F CG  1 
ATOM   2737 C CD  . PRO B 2 142 ? 14.212  -35.038 -22.022 1.00 31.42 ?  142 PRO F CD  1 
ATOM   2738 N N   . ARG B 2 143 ? 16.707  -31.243 -21.993 1.00 31.47 ?  143 ARG F N   1 
ATOM   2739 C CA  . ARG B 2 143 ? 17.285  -30.160 -21.209 1.00 32.04 ?  143 ARG F CA  1 
ATOM   2740 C C   . ARG B 2 143 ? 16.261  -29.456 -20.332 1.00 34.62 ?  143 ARG F C   1 
ATOM   2741 O O   . ARG B 2 143 ? 16.634  -28.867 -19.308 1.00 34.80 ?  143 ARG F O   1 
ATOM   2742 C CB  . ARG B 2 143 ? 17.965  -29.185 -22.179 1.00 34.47 ?  143 ARG F CB  1 
ATOM   2743 C CG  . ARG B 2 143 ? 18.615  -27.961 -21.584 1.00 39.39 ?  143 ARG F CG  1 
ATOM   2744 C CD  . ARG B 2 143 ? 19.108  -27.119 -22.749 1.00 40.71 ?  143 ARG F CD  1 
ATOM   2745 N NE  . ARG B 2 143 ? 19.965  -26.013 -22.357 1.00 47.84 ?  143 ARG F NE  1 
ATOM   2746 C CZ  . ARG B 2 143 ? 19.510  -24.864 -21.881 1.00 48.29 ?  143 ARG F CZ  1 
ATOM   2747 N NH1 . ARG B 2 143 ? 18.217  -24.657 -21.696 1.00 48.98 ?  143 ARG F NH1 1 
ATOM   2748 N NH2 . ARG B 2 143 ? 20.370  -23.892 -21.605 1.00 51.49 ?  143 ARG F NH2 1 
ATOM   2749 N N   . GLU B 2 144 ? 14.987  -29.520 -20.701 1.00 33.13 ?  144 GLU F N   1 
ATOM   2750 C CA  . GLU B 2 144 ? 13.925  -28.837 -19.969 1.00 36.07 ?  144 GLU F CA  1 
ATOM   2751 C C   . GLU B 2 144 ? 13.815  -29.394 -18.555 1.00 34.50 ?  144 GLU F C   1 
ATOM   2752 O O   . GLU B 2 144 ? 13.555  -30.588 -18.366 1.00 34.70 ?  144 GLU F O   1 
ATOM   2753 C CB  . GLU B 2 144 ? 12.603  -29.013 -20.720 1.00 37.20 ?  144 GLU F CB  1 
ATOM   2754 C CG  . GLU B 2 144 ? 12.452  -28.069 -21.911 1.00 44.31 ?  144 GLU F CG  1 
ATOM   2755 C CD  . GLU B 2 144 ? 13.439  -28.373 -23.046 1.00 47.69 ?  144 GLU F CD  1 
ATOM   2756 O OE1 . GLU B 2 144 ? 13.651  -29.574 -23.374 1.00 43.52 ?  144 GLU F OE1 1 
ATOM   2757 O OE2 . GLU B 2 144 ? 14.023  -27.408 -23.599 1.00 50.31 ?  144 GLU F OE2 1 
ATOM   2758 N N   . ALA B 2 145 ? 14.013  -28.533 -17.555 1.00 36.38 ?  145 ALA F N   1 
ATOM   2759 C CA  . ALA B 2 145 ? 13.912  -28.956 -16.163 1.00 35.62 ?  145 ALA F CA  1 
ATOM   2760 C C   . ALA B 2 145 ? 13.501  -27.767 -15.306 1.00 40.91 ?  145 ALA F C   1 
ATOM   2761 O O   . ALA B 2 145 ? 13.925  -26.637 -15.562 1.00 39.77 ?  145 ALA F O   1 
ATOM   2762 C CB  . ALA B 2 145 ? 15.234  -29.555 -15.668 1.00 35.27 ?  145 ALA F CB  1 
ATOM   2763 N N   . LYS B 2 146 ? 12.665  -28.023 -14.300 1.00 38.85 ?  146 LYS F N   1 
ATOM   2764 C CA  . LYS B 2 146 ? 12.205  -26.990 -13.380 1.00 40.01 ?  146 LYS F CA  1 
ATOM   2765 C C   . LYS B 2 146 ? 12.742  -27.294 -11.989 1.00 40.24 ?  146 LYS F C   1 
ATOM   2766 O O   . LYS B 2 146 ? 12.593  -28.415 -11.493 1.00 35.50 ?  146 LYS F O   1 
ATOM   2767 C CB  . LYS B 2 146 ? 10.677  -26.911 -13.364 1.00 42.64 ?  146 LYS F CB  1 
ATOM   2768 C CG  . LYS B 2 146 ? 10.087  -25.640 -12.748 1.00 47.66 ?  146 LYS F CG  1 
ATOM   2769 C CD  . LYS B 2 146 ? 8.564   -25.770 -12.642 1.00 50.51 ?  146 LYS F CD  1 
ATOM   2770 C CE  . LYS B 2 146 ? 7.941   -24.623 -11.856 1.00 57.44 ?  146 LYS F CE  1 
ATOM   2771 N NZ  . LYS B 2 146 ? 8.709   -23.342 -11.990 1.00 57.47 ?  146 LYS F NZ  1 
ATOM   2772 N N   . VAL B 2 147 ? 13.388  -26.310 -11.374 1.00 37.34 ?  147 VAL F N   1 
ATOM   2773 C CA  . VAL B 2 147 ? 13.933  -26.446 -10.027 1.00 36.71 ?  147 VAL F CA  1 
ATOM   2774 C C   . VAL B 2 147 ? 13.347  -25.325 -9.182  1.00 41.76 ?  147 VAL F C   1 
ATOM   2775 O O   . VAL B 2 147 ? 13.493  -24.144 -9.524  1.00 39.02 ?  147 VAL F O   1 
ATOM   2776 C CB  . VAL B 2 147 ? 15.468  -26.388 -10.018 1.00 40.92 ?  147 VAL F CB  1 
ATOM   2777 C CG1 . VAL B 2 147 ? 15.995  -26.514 -8.593  1.00 41.54 ?  147 VAL F CG1 1 
ATOM   2778 C CG2 . VAL B 2 147 ? 16.033  -27.488 -10.897 1.00 40.23 ?  147 VAL F CG2 1 
ATOM   2779 N N   . GLN B 2 148 ? 12.678  -25.690 -8.094  1.00 38.94 ?  148 GLN F N   1 
ATOM   2780 C CA  . GLN B 2 148 ? 12.077  -24.720 -7.194  1.00 36.69 ?  148 GLN F CA  1 
ATOM   2781 C C   . GLN B 2 148 ? 12.689  -24.868 -5.811  1.00 37.30 ?  148 GLN F C   1 
ATOM   2782 O O   . GLN B 2 148 ? 12.870  -25.985 -5.319  1.00 37.30 ?  148 GLN F O   1 
ATOM   2783 C CB  . GLN B 2 148 ? 10.560  -24.900 -7.133  1.00 38.81 ?  148 GLN F CB  1 
ATOM   2784 C CG  . GLN B 2 148 ? 9.840   -24.383 -8.353  1.00 41.15 ?  148 GLN F CG  1 
ATOM   2785 C CD  . GLN B 2 148 ? 8.406   -24.845 -8.407  1.00 50.35 ?  148 GLN F CD  1 
ATOM   2786 O OE1 . GLN B 2 148 ? 8.124   -26.042 -8.293  1.00 53.02 ?  148 GLN F OE1 1 
ATOM   2787 N NE2 . GLN B 2 148 ? 7.485   -23.898 -8.551  1.00 51.77 ?  148 GLN F NE2 1 
ATOM   2788 N N   . TRP B 2 149 ? 13.026  -23.738 -5.197  1.00 33.28 ?  149 TRP F N   1 
ATOM   2789 C CA  . TRP B 2 149 ? 13.556  -23.719 -3.843  1.00 35.88 ?  149 TRP F CA  1 
ATOM   2790 C C   . TRP B 2 149 ? 12.428  -23.517 -2.844  1.00 38.24 ?  149 TRP F C   1 
ATOM   2791 O O   . TRP B 2 149 ? 11.575  -22.638 -3.024  1.00 36.35 ?  149 TRP F O   1 
ATOM   2792 C CB  . TRP B 2 149 ? 14.585  -22.601 -3.690  1.00 36.57 ?  149 TRP F CB  1 
ATOM   2793 C CG  . TRP B 2 149 ? 15.927  -22.966 -4.213  1.00 36.38 ?  149 TRP F CG  1 
ATOM   2794 C CD1 . TRP B 2 149 ? 16.478  -22.546 -5.383  1.00 36.12 ?  149 TRP F CD1 1 
ATOM   2795 C CD2 . TRP B 2 149 ? 16.905  -23.813 -3.586  1.00 33.84 ?  149 TRP F CD2 1 
ATOM   2796 N NE1 . TRP B 2 149 ? 17.729  -23.084 -5.536  1.00 35.55 ?  149 TRP F NE1 1 
ATOM   2797 C CE2 . TRP B 2 149 ? 18.017  -23.865 -4.446  1.00 36.42 ?  149 TRP F CE2 1 
ATOM   2798 C CE3 . TRP B 2 149 ? 16.940  -24.543 -2.390  1.00 33.87 ?  149 TRP F CE3 1 
ATOM   2799 C CZ2 . TRP B 2 149 ? 19.163  -24.610 -4.148  1.00 33.85 ?  149 TRP F CZ2 1 
ATOM   2800 C CZ3 . TRP B 2 149 ? 18.078  -25.284 -2.096  1.00 35.97 ?  149 TRP F CZ3 1 
ATOM   2801 C CH2 . TRP B 2 149 ? 19.173  -25.310 -2.973  1.00 34.33 ?  149 TRP F CH2 1 
ATOM   2802 N N   . LYS B 2 150 ? 12.431  -24.326 -1.788  1.00 36.75 ?  150 LYS F N   1 
ATOM   2803 C CA  . LYS B 2 150 ? 11.492  -24.173 -0.685  1.00 37.96 ?  150 LYS F CA  1 
ATOM   2804 C C   . LYS B 2 150 ? 12.288  -24.085 0.608   1.00 39.60 ?  150 LYS F C   1 
ATOM   2805 O O   . LYS B 2 150 ? 13.105  -24.963 0.904   1.00 39.00 ?  150 LYS F O   1 
ATOM   2806 C CB  . LYS B 2 150 ? 10.481  -25.320 -0.654  1.00 39.39 ?  150 LYS F CB  1 
ATOM   2807 C CG  . LYS B 2 150 ? 9.445   -25.206 -1.763  1.00 41.86 ?  150 LYS F CG  1 
ATOM   2808 C CD  . LYS B 2 150 ? 8.823   -26.541 -2.086  1.00 45.67 ?  150 LYS F CD  1 
ATOM   2809 C CE  . LYS B 2 150 ? 7.439   -26.382 -2.688  1.00 50.49 ?  150 LYS F CE  1 
ATOM   2810 N NZ  . LYS B 2 150 ? 6.743   -27.702 -2.737  1.00 52.32 ?  150 LYS F NZ  1 
ATOM   2811 N N   . VAL B 2 151 ? 12.078  -23.004 1.351   1.00 36.93 ?  151 VAL F N   1 
ATOM   2812 C CA  . VAL B 2 151 ? 12.730  -22.778 2.631   1.00 36.04 ?  151 VAL F CA  1 
ATOM   2813 C C   . VAL B 2 151 ? 11.628  -22.770 3.677   1.00 40.05 ?  151 VAL F C   1 
ATOM   2814 O O   . VAL B 2 151 ? 10.703  -21.952 3.599   1.00 35.37 ?  151 VAL F O   1 
ATOM   2815 C CB  . VAL B 2 151 ? 13.529  -21.466 2.630   1.00 36.96 ?  151 VAL F CB  1 
ATOM   2816 C CG1 . VAL B 2 151 ? 14.102  -21.172 4.003   1.00 37.52 ?  151 VAL F CG1 1 
ATOM   2817 C CG2 . VAL B 2 151 ? 14.647  -21.541 1.607   1.00 35.40 ?  151 VAL F CG2 1 
ATOM   2818 N N   . ASP B 2 152 ? 11.688  -23.713 4.620   1.00 36.95 ?  152 ASP F N   1 
ATOM   2819 C CA  . ASP B 2 152 ? 10.616  -23.883 5.600   1.00 37.99 ?  152 ASP F CA  1 
ATOM   2820 C C   . ASP B 2 152 ? 9.269   -23.993 4.892   1.00 41.16 ?  152 ASP F C   1 
ATOM   2821 O O   . ASP B 2 152 ? 8.293   -23.322 5.244   1.00 36.81 ?  152 ASP F O   1 
ATOM   2822 C CB  . ASP B 2 152 ? 10.616  -22.737 6.616   1.00 36.21 ?  152 ASP F CB  1 
ATOM   2823 C CG  . ASP B 2 152 ? 11.702  -22.888 7.664   1.00 40.09 ?  152 ASP F CG  1 
ATOM   2824 O OD1 . ASP B 2 152 ? 12.377  -23.943 7.686   1.00 38.22 ?  152 ASP F OD1 1 
ATOM   2825 O OD2 . ASP B 2 152 ? 11.903  -21.936 8.446   1.00 41.48 ?  152 ASP F OD2 1 
ATOM   2826 N N   . ASN B 2 153 ? 9.255   -24.812 3.837   1.00 36.81 ?  153 ASN F N   1 
ATOM   2827 C CA  . ASN B 2 153 ? 8.086   -25.151 3.030   1.00 38.46 ?  153 ASN F CA  1 
ATOM   2828 C C   . ASN B 2 153 ? 7.491   -23.957 2.291   1.00 41.12 ?  153 ASN F C   1 
ATOM   2829 O O   . ASN B 2 153 ? 6.366   -24.044 1.787   1.00 43.22 ?  153 ASN F O   1 
ATOM   2830 C CB  . ASN B 2 153 ? 7.018   -25.848 3.882   1.00 40.15 ?  153 ASN F CB  1 
ATOM   2831 C CG  . ASN B 2 153 ? 7.559   -27.095 4.557   1.00 41.00 ?  153 ASN F CG  1 
ATOM   2832 O OD1 . ASN B 2 153 ? 8.008   -28.024 3.889   1.00 45.28 ?  153 ASN F OD1 1 
ATOM   2833 N ND2 . ASN B 2 153 ? 7.531   -27.117 5.885   1.00 44.98 ?  153 ASN F ND2 1 
ATOM   2834 N N   . ALA B 2 154 ? 8.225   -22.856 2.176   1.00 39.71 ?  154 ALA F N   1 
ATOM   2835 C CA  . ALA B 2 154 ? 7.769   -21.676 1.451   1.00 41.58 ?  154 ALA F CA  1 
ATOM   2836 C C   . ALA B 2 154 ? 8.531   -21.563 0.134   1.00 43.46 ?  154 ALA F C   1 
ATOM   2837 O O   . ALA B 2 154 ? 9.771   -21.503 0.126   1.00 38.17 ?  154 ALA F O   1 
ATOM   2838 C CB  . ALA B 2 154 ? 7.968   -20.411 2.284   1.00 38.89 ?  154 ALA F CB  1 
ATOM   2839 N N   . LEU B 2 155 ? 7.784   -21.496 -0.967  1.00 43.14 ?  155 LEU F N   1 
ATOM   2840 C CA  . LEU B 2 155 ? 8.388   -21.331 -2.282  1.00 43.91 ?  155 LEU F CA  1 
ATOM   2841 C C   . LEU B 2 155 ? 9.140   -20.014 -2.368  1.00 44.93 ?  155 LEU F C   1 
ATOM   2842 O O   . LEU B 2 155 ? 8.625   -18.960 -1.980  1.00 47.88 ?  155 LEU F O   1 
ATOM   2843 C CB  . LEU B 2 155 ? 7.316   -21.396 -3.371  1.00 45.49 ?  155 LEU F CB  1 
ATOM   2844 C CG  . LEU B 2 155 ? 7.900   -21.347 -4.783  1.00 47.83 ?  155 LEU F CG  1 
ATOM   2845 C CD1 . LEU B 2 155 ? 8.623   -22.652 -5.103  1.00 46.95 ?  155 LEU F CD1 1 
ATOM   2846 C CD2 . LEU B 2 155 ? 6.830   -21.038 -5.815  1.00 44.99 ?  155 LEU F CD2 1 
ATOM   2847 N N   . GLN B 2 156 ? 10.360  -20.071 -2.884  1.00 42.85 ?  156 GLN F N   1 
ATOM   2848 C CA  . GLN B 2 156 ? 11.191  -18.889 -3.035  1.00 44.03 ?  156 GLN F CA  1 
ATOM   2849 C C   . GLN B 2 156 ? 11.093  -18.332 -4.451  1.00 47.83 ?  156 GLN F C   1 
ATOM   2850 O O   . GLN B 2 156 ? 10.704  -19.021 -5.399  1.00 48.75 ?  156 GLN F O   1 
ATOM   2851 C CB  . GLN B 2 156 ? 12.646  -19.206 -2.683  1.00 44.72 ?  156 GLN F CB  1 
ATOM   2852 C CG  . GLN B 2 156 ? 12.770  -19.931 -1.357  1.00 43.36 ?  156 GLN F CG  1 
ATOM   2853 C CD  . GLN B 2 156 ? 12.459  -19.007 -0.194  1.00 44.46 ?  156 GLN F CD  1 
ATOM   2854 O OE1 . GLN B 2 156 ? 13.123  -17.994 -0.007  1.00 46.93 ?  156 GLN F OE1 1 
ATOM   2855 N NE2 . GLN B 2 156 ? 11.414  -19.329 0.556   1.00 43.06 ?  156 GLN F NE2 1 
ATOM   2856 N N   . SER B 2 157 ? 11.434  -17.052 -4.570  1.00 46.31 ?  157 SER F N   1 
ATOM   2857 C CA  . SER B 2 157 ? 11.439  -16.364 -5.852  1.00 50.78 ?  157 SER F CA  1 
ATOM   2858 C C   . SER B 2 157 ? 12.389  -15.183 -5.742  1.00 51.54 ?  157 SER F C   1 
ATOM   2859 O O   . SER B 2 157 ? 12.364  -14.463 -4.740  1.00 51.12 ?  157 SER F O   1 
ATOM   2860 C CB  . SER B 2 157 ? 10.030  -15.896 -6.230  1.00 55.42 ?  157 SER F CB  1 
ATOM   2861 O OG  . SER B 2 157 ? 10.080  -14.843 -7.175  1.00 59.88 ?  157 SER F OG  1 
ATOM   2862 N N   . GLY B 2 158 ? 13.244  -15.007 -6.749  1.00 51.97 ?  158 GLY F N   1 
ATOM   2863 C CA  . GLY B 2 158 ? 14.087  -13.836 -6.845  1.00 51.61 ?  158 GLY F CA  1 
ATOM   2864 C C   . GLY B 2 158 ? 15.460  -13.961 -6.227  1.00 52.69 ?  158 GLY F C   1 
ATOM   2865 O O   . GLY B 2 158 ? 16.299  -13.073 -6.442  1.00 56.27 ?  158 GLY F O   1 
ATOM   2866 N N   . ASN B 2 159 ? 15.728  -15.034 -5.482  1.00 47.89 ?  159 ASN F N   1 
ATOM   2867 C CA  . ASN B 2 159 ? 16.984  -15.177 -4.753  1.00 45.66 ?  159 ASN F CA  1 
ATOM   2868 C C   . ASN B 2 159 ? 17.801  -16.387 -5.203  1.00 44.35 ?  159 ASN F C   1 
ATOM   2869 O O   . ASN B 2 159 ? 18.706  -16.814 -4.480  1.00 43.13 ?  159 ASN F O   1 
ATOM   2870 C CB  . ASN B 2 159 ? 16.714  -15.247 -3.244  1.00 48.77 ?  159 ASN F CB  1 
ATOM   2871 C CG  . ASN B 2 159 ? 15.591  -16.223 -2.885  1.00 51.30 ?  159 ASN F CG  1 
ATOM   2872 O OD1 . ASN B 2 159 ? 15.006  -16.875 -3.761  1.00 50.64 ?  159 ASN F OD1 1 
ATOM   2873 N ND2 . ASN B 2 159 ? 15.281  -16.325 -1.591  1.00 50.37 ?  159 ASN F ND2 1 
ATOM   2874 N N   . SER B 2 160 ? 17.531  -16.937 -6.386  1.00 44.13 ?  160 SER F N   1 
ATOM   2875 C CA  . SER B 2 160 ? 18.313  -18.062 -6.887  1.00 42.45 ?  160 SER F CA  1 
ATOM   2876 C C   . SER B 2 160 ? 18.743  -17.820 -8.329  1.00 43.33 ?  160 SER F C   1 
ATOM   2877 O O   . SER B 2 160 ? 18.114  -17.060 -9.070  1.00 42.44 ?  160 SER F O   1 
ATOM   2878 C CB  . SER B 2 160 ? 17.545  -19.395 -6.782  1.00 39.52 ?  160 SER F CB  1 
ATOM   2879 O OG  . SER B 2 160 ? 16.192  -19.273 -7.199  1.00 42.15 ?  160 SER F OG  1 
ATOM   2880 N N   . GLN B 2 161 ? 19.836  -18.491 -8.698  1.00 37.97 ?  161 GLN F N   1 
ATOM   2881 C CA  . GLN B 2 161 ? 20.365  -18.421 -10.084 1.00 40.49 ?  161 GLN F CA  1 
ATOM   2882 C C   . GLN B 2 161 ? 20.674  -19.846 -10.560 1.00 40.13 ?  161 GLN F C   1 
ATOM   2883 O O   . GLN B 2 161 ? 21.208  -20.631 -9.768  1.00 37.69 ?  161 GLN F O   1 
ATOM   2884 C CB  . GLN B 2 161 ? 21.592  -17.516 -10.153 1.00 42.83 ?  161 GLN F CB  1 
ATOM   2885 C CG  . GLN B 2 161 ? 21.233  -16.051 -10.349 1.00 45.67 ?  161 GLN F CG  1 
ATOM   2886 C CD  . GLN B 2 161 ? 22.423  -15.125 -10.344 1.00 51.51 ?  161 GLN F CD  1 
ATOM   2887 O OE1 . GLN B 2 161 ? 23.286  -15.193 -9.472  1.00 49.89 ?  161 GLN F OE1 1 
ATOM   2888 N NE2 . GLN B 2 161 ? 22.469  -14.234 -11.320 1.00 48.93 ?  161 GLN F NE2 1 
ATOM   2889 N N   . GLU B 2 162 ? 20.331  -20.155 -11.802 1.00 38.12 ?  162 GLU F N   1 
ATOM   2890 C CA  . GLU B 2 162 ? 20.520  -21.479 -12.380 1.00 39.68 ?  162 GLU F CA  1 
ATOM   2891 C C   . GLU B 2 162 ? 21.599  -21.435 -13.455 1.00 38.47 ?  162 GLU F C   1 
ATOM   2892 O O   . GLU B 2 162 ? 21.803  -20.415 -14.118 1.00 37.75 ?  162 GLU F O   1 
ATOM   2893 C CB  . GLU B 2 162 ? 19.228  -22.010 -13.013 1.00 37.87 ?  162 GLU F CB  1 
ATOM   2894 C CG  . GLU B 2 162 ? 18.218  -22.661 -12.072 1.00 42.50 ?  162 GLU F CG  1 
ATOM   2895 C CD  . GLU B 2 162 ? 16.993  -23.178 -12.833 1.00 46.99 ?  162 GLU F CD  1 
ATOM   2896 O OE1 . GLU B 2 162 ? 17.014  -23.136 -14.084 1.00 49.18 ?  162 GLU F OE1 1 
ATOM   2897 O OE2 . GLU B 2 162 ? 16.003  -23.613 -12.202 1.00 49.18 ?  162 GLU F OE2 1 
ATOM   2898 N N   . SER B 2 163 ? 22.272  -22.562 -13.631 1.00 33.80 ?  163 SER F N   1 
ATOM   2899 C CA  . SER B 2 163 ? 23.240  -22.730 -14.703 1.00 34.66 ?  163 SER F CA  1 
ATOM   2900 C C   . SER B 2 163 ? 23.159  -24.156 -15.224 1.00 33.64 ?  163 SER F C   1 
ATOM   2901 O O   . SER B 2 163 ? 23.111  -25.108 -14.441 1.00 33.83 ?  163 SER F O   1 
ATOM   2902 C CB  . SER B 2 163 ? 24.660  -22.430 -14.216 1.00 36.00 ?  163 SER F CB  1 
ATOM   2903 O OG  . SER B 2 163 ? 25.578  -22.546 -15.281 1.00 37.78 ?  163 SER F OG  1 
ATOM   2904 N N   . VAL B 2 164 ? 23.177  -24.306 -16.540 1.00 30.64 ?  164 VAL F N   1 
ATOM   2905 C CA  . VAL B 2 164 ? 23.125  -25.619 -17.161 1.00 33.33 ?  164 VAL F CA  1 
ATOM   2906 C C   . VAL B 2 164 ? 24.348  -25.780 -18.054 1.00 39.35 ?  164 VAL F C   1 
ATOM   2907 O O   . VAL B 2 164 ? 24.789  -24.828 -18.707 1.00 38.99 ?  164 VAL F O   1 
ATOM   2908 C CB  . VAL B 2 164 ? 21.807  -25.798 -17.946 1.00 40.27 ?  164 VAL F CB  1 
ATOM   2909 C CG1 . VAL B 2 164 ? 21.709  -24.760 -19.017 1.00 43.96 ?  164 VAL F CG1 1 
ATOM   2910 C CG2 . VAL B 2 164 ? 21.713  -27.167 -18.531 1.00 36.62 ?  164 VAL F CG2 1 
ATOM   2911 N N   . THR B 2 165 ? 24.930  -26.969 -18.042 1.00 36.94 ?  165 THR F N   1 
ATOM   2912 C CA  . THR B 2 165 ? 26.026  -27.212 -18.956 1.00 42.60 ?  165 THR F CA  1 
ATOM   2913 C C   . THR B 2 165 ? 25.524  -27.201 -20.400 1.00 44.27 ?  165 THR F C   1 
ATOM   2914 O O   . THR B 2 165 ? 24.322  -27.276 -20.673 1.00 44.53 ?  165 THR F O   1 
ATOM   2915 C CB  . THR B 2 165 ? 26.684  -28.548 -18.636 1.00 39.78 ?  165 THR F CB  1 
ATOM   2916 O OG1 . THR B 2 165 ? 25.714  -29.610 -18.813 1.00 33.82 ?  165 THR F OG1 1 
ATOM   2917 C CG2 . THR B 2 165 ? 27.247  -28.538 -17.214 1.00 35.03 ?  165 THR F CG2 1 
ATOM   2918 N N   . GLU B 2 166 ? 26.459  -27.092 -21.340 1.00 44.85 ?  166 GLU F N   1 
ATOM   2919 C CA  . GLU B 2 166 ? 26.155  -27.680 -22.634 1.00 47.96 ?  166 GLU F CA  1 
ATOM   2920 C C   . GLU B 2 166 ? 26.096  -29.203 -22.466 1.00 45.24 ?  166 GLU F C   1 
ATOM   2921 O O   . GLU B 2 166 ? 26.461  -29.741 -21.415 1.00 39.74 ?  166 GLU F O   1 
ATOM   2922 C CB  . GLU B 2 166 ? 27.183  -27.240 -23.676 1.00 49.34 ?  166 GLU F CB  1 
ATOM   2923 C CG  . GLU B 2 166 ? 27.283  -25.719 -23.791 1.00 55.06 ?  166 GLU F CG  1 
ATOM   2924 C CD  . GLU B 2 166 ? 26.235  -25.122 -24.737 1.00 58.64 ?  166 GLU F CD  1 
ATOM   2925 O OE1 . GLU B 2 166 ? 25.277  -25.840 -25.104 1.00 60.68 ?  166 GLU F OE1 1 
ATOM   2926 O OE2 . GLU B 2 166 ? 26.350  -23.926 -25.090 1.00 62.49 ?  166 GLU F OE2 1 
ATOM   2927 N N   . GLN B 2 167 ? 25.593  -29.891 -23.481 1.00 44.38 ?  167 GLN F N   1 
ATOM   2928 C CA  . GLN B 2 167 ? 25.421  -31.362 -23.376 1.00 44.23 ?  167 GLN F CA  1 
ATOM   2929 C C   . GLN B 2 167 ? 26.775  -32.015 -23.060 1.00 44.84 ?  167 GLN F C   1 
ATOM   2930 O O   . GLN B 2 167 ? 27.733  -31.720 -23.791 1.00 47.94 ?  167 GLN F O   1 
ATOM   2931 C CB  . GLN B 2 167 ? 24.786  -31.872 -24.671 1.00 45.97 ?  167 GLN F CB  1 
ATOM   2932 C CG  . GLN B 2 167 ? 23.543  -32.713 -24.462 1.00 44.86 ?  167 GLN F CG  1 
ATOM   2933 C CD  . GLN B 2 167 ? 22.833  -32.957 -25.769 1.00 43.27 ?  167 GLN F CD  1 
ATOM   2934 O OE1 . GLN B 2 167 ? 22.513  -32.032 -26.508 1.00 51.30 ?  167 GLN F OE1 1 
ATOM   2935 N NE2 . GLN B 2 167 ? 22.574  -34.218 -26.063 1.00 45.00 ?  167 GLN F NE2 1 
ATOM   2936 N N   . ASP B 2 168 ? 26.857  -32.825 -21.992 1.00 45.62 ?  168 ASP F N   1 
ATOM   2937 C CA  . ASP B 2 168 ? 28.085  -33.521 -21.641 1.00 42.27 ?  168 ASP F CA  1 
ATOM   2938 C C   . ASP B 2 168 ? 28.622  -34.221 -22.876 1.00 43.82 ?  168 ASP F C   1 
ATOM   2939 O O   . ASP B 2 168 ? 27.864  -34.766 -23.683 1.00 37.20 ?  168 ASP F O   1 
ATOM   2940 C CB  . ASP B 2 168 ? 27.857  -34.553 -20.536 1.00 43.67 ?  168 ASP F CB  1 
ATOM   2941 C CG  . ASP B 2 168 ? 29.154  -35.235 -20.114 1.00 47.10 ?  168 ASP F CG  1 
ATOM   2942 O OD1 . ASP B 2 168 ? 30.133  -34.501 -19.859 1.00 51.85 ?  168 ASP F OD1 1 
ATOM   2943 O OD2 . ASP B 2 168 ? 29.215  -36.491 -20.078 1.00 48.42 ?  168 ASP F OD2 1 
ATOM   2944 N N   . SER B 2 169 ? 29.940  -34.182 -23.036 1.00 41.72 ?  169 SER F N   1 
ATOM   2945 C CA  . SER B 2 169 ? 30.508  -34.693 -24.272 1.00 40.36 ?  169 SER F CA  1 
ATOM   2946 C C   . SER B 2 169 ? 30.345  -36.206 -24.359 1.00 34.65 ?  169 SER F C   1 
ATOM   2947 O O   . SER B 2 169 ? 30.007  -36.731 -25.425 1.00 36.91 ?  169 SER F O   1 
ATOM   2948 C CB  . SER B 2 169 ? 31.973  -34.278 -24.381 1.00 39.11 ?  169 SER F CB  1 
ATOM   2949 O OG  . SER B 2 169 ? 32.084  -32.927 -24.822 1.00 45.43 ?  169 SER F OG  1 
ATOM   2950 N N   . LYS B 2 170 ? 30.545  -36.923 -23.250 1.00 34.99 ?  170 LYS F N   1 
ATOM   2951 C CA  . LYS B 2 170 ? 30.506  -38.382 -23.333 1.00 37.50 ?  170 LYS F CA  1 
ATOM   2952 C C   . LYS B 2 170 ? 29.069  -38.906 -23.296 1.00 36.13 ?  170 LYS F C   1 
ATOM   2953 O O   . LYS B 2 170 ? 28.648  -39.635 -24.198 1.00 36.36 ?  170 LYS F O   1 
ATOM   2954 C CB  . LYS B 2 170 ? 31.336  -39.026 -22.221 1.00 38.20 ?  170 LYS F CB  1 
ATOM   2955 C CG  . LYS B 2 170 ? 31.223  -40.546 -22.233 1.00 37.32 ?  170 LYS F CG  1 
ATOM   2956 C CD  . LYS B 2 170 ? 31.653  -41.057 -23.622 1.00 40.02 ?  170 LYS F CD  1 
ATOM   2957 C CE  . LYS B 2 170 ? 31.497  -42.584 -23.817 1.00 44.92 ?  170 LYS F CE  1 
ATOM   2958 N NZ  . LYS B 2 170 ? 31.676  -42.940 -25.283 1.00 37.52 ?  170 LYS F NZ  1 
ATOM   2959 N N   . ASP B 2 171 ? 28.302  -38.533 -22.261 1.00 34.83 ?  171 ASP F N   1 
ATOM   2960 C CA  . ASP B 2 171 ? 26.950  -39.061 -22.075 1.00 34.67 ?  171 ASP F CA  1 
ATOM   2961 C C   . ASP B 2 171 ? 25.904  -38.344 -22.922 1.00 31.19 ?  171 ASP F C   1 
ATOM   2962 O O   . ASP B 2 171 ? 24.783  -38.849 -23.063 1.00 29.27 ?  171 ASP F O   1 
ATOM   2963 C CB  . ASP B 2 171 ? 26.539  -38.968 -20.602 1.00 37.16 ?  171 ASP F CB  1 
ATOM   2964 C CG  . ASP B 2 171 ? 27.149  -40.065 -19.744 1.00 43.08 ?  171 ASP F CG  1 
ATOM   2965 O OD1 . ASP B 2 171 ? 28.013  -40.820 -20.249 1.00 42.65 ?  171 ASP F OD1 1 
ATOM   2966 O OD2 . ASP B 2 171 ? 26.753  -40.182 -18.557 1.00 45.98 ?  171 ASP F OD2 1 
ATOM   2967 N N   . SER B 2 172 ? 26.228  -37.184 -23.477 1.00 31.54 ?  172 SER F N   1 
ATOM   2968 C CA  . SER B 2 172 ? 25.271  -36.386 -24.241 1.00 31.53 ?  172 SER F CA  1 
ATOM   2969 C C   . SER B 2 172 ? 24.037  -36.048 -23.399 1.00 34.22 ?  172 SER F C   1 
ATOM   2970 O O   . SER B 2 172 ? 22.913  -36.017 -23.902 1.00 36.85 ?  172 SER F O   1 
ATOM   2971 C CB  . SER B 2 172 ? 24.879  -37.094 -25.543 1.00 33.04 ?  172 SER F CB  1 
ATOM   2972 O OG  . SER B 2 172 ? 24.041  -36.283 -26.333 1.00 36.82 ?  172 SER F OG  1 
ATOM   2973 N N   . THR B 2 173 ? 24.237  -35.820 -22.105 1.00 31.90 ?  173 THR F N   1 
ATOM   2974 C CA  . THR B 2 173 ? 23.195  -35.374 -21.185 1.00 28.45 ?  173 THR F CA  1 
ATOM   2975 C C   . THR B 2 173 ? 23.576  -34.003 -20.632 1.00 31.21 ?  173 THR F C   1 
ATOM   2976 O O   . THR B 2 173 ? 24.636  -33.445 -20.945 1.00 30.90 ?  173 THR F O   1 
ATOM   2977 C CB  . THR B 2 173 ? 22.999  -36.369 -20.034 1.00 30.84 ?  173 THR F CB  1 
ATOM   2978 O OG1 . THR B 2 173 ? 24.269  -36.645 -19.441 1.00 32.16 ?  173 THR F OG1 1 
ATOM   2979 C CG2 . THR B 2 173 ? 22.371  -37.685 -20.509 1.00 28.02 ?  173 THR F CG2 1 
ATOM   2980 N N   . TYR B 2 174 ? 22.699  -33.463 -19.795 1.00 27.40 ?  174 TYR F N   1 
ATOM   2981 C CA  . TYR B 2 174 ? 22.912  -32.173 -19.160 1.00 28.24 ?  174 TYR F CA  1 
ATOM   2982 C C   . TYR B 2 174 ? 23.067  -32.337 -17.658 1.00 27.30 ?  174 TYR F C   1 
ATOM   2983 O O   . TYR B 2 174 ? 22.596  -33.307 -17.061 1.00 26.57 ?  174 TYR F O   1 
ATOM   2984 C CB  . TYR B 2 174 ? 21.745  -31.228 -19.422 1.00 29.83 ?  174 TYR F CB  1 
ATOM   2985 C CG  . TYR B 2 174 ? 21.574  -30.850 -20.863 1.00 32.52 ?  174 TYR F CG  1 
ATOM   2986 C CD1 . TYR B 2 174 ? 22.241  -29.752 -21.389 1.00 37.12 ?  174 TYR F CD1 1 
ATOM   2987 C CD2 . TYR B 2 174 ? 20.742  -31.595 -21.705 1.00 30.60 ?  174 TYR F CD2 1 
ATOM   2988 C CE1 . TYR B 2 174 ? 22.081  -29.392 -22.703 1.00 37.50 ?  174 TYR F CE1 1 
ATOM   2989 C CE2 . TYR B 2 174 ? 20.586  -31.250 -23.025 1.00 34.35 ?  174 TYR F CE2 1 
ATOM   2990 C CZ  . TYR B 2 174 ? 21.247  -30.133 -23.516 1.00 37.73 ?  174 TYR F CZ  1 
ATOM   2991 O OH  . TYR B 2 174 ? 21.108  -29.763 -24.833 1.00 37.64 ?  174 TYR F OH  1 
ATOM   2992 N N   . SER B 2 175 ? 23.741  -31.363 -17.062 1.00 27.96 ?  175 SER F N   1 
ATOM   2993 C CA  . SER B 2 175 ? 23.712  -31.132 -15.629 1.00 30.52 ?  175 SER F CA  1 
ATOM   2994 C C   . SER B 2 175 ? 23.266  -29.698 -15.384 1.00 29.15 ?  175 SER F C   1 
ATOM   2995 O O   . SER B 2 175 ? 23.380  -28.835 -16.260 1.00 30.08 ?  175 SER F O   1 
ATOM   2996 C CB  . SER B 2 175 ? 25.080  -31.389 -14.991 1.00 29.94 ?  175 SER F CB  1 
ATOM   2997 O OG  . SER B 2 175 ? 25.416  -32.763 -15.109 1.00 32.25 ?  175 SER F OG  1 
ATOM   2998 N N   . LEU B 2 176 ? 22.742  -29.451 -14.185 1.00 27.33 ?  176 LEU F N   1 
ATOM   2999 C CA  . LEU B 2 176 ? 22.199  -28.143 -13.832 1.00 28.64 ?  176 LEU F CA  1 
ATOM   3000 C C   . LEU B 2 176 ? 22.517  -27.858 -12.377 1.00 32.77 ?  176 LEU F C   1 
ATOM   3001 O O   . LEU B 2 176 ? 22.343  -28.728 -11.519 1.00 31.72 ?  176 LEU F O   1 
ATOM   3002 C CB  . LEU B 2 176 ? 20.683  -28.076 -14.048 1.00 31.32 ?  176 LEU F CB  1 
ATOM   3003 C CG  . LEU B 2 176 ? 19.971  -26.743 -13.766 1.00 34.25 ?  176 LEU F CG  1 
ATOM   3004 C CD1 . LEU B 2 176 ? 18.788  -26.571 -14.713 1.00 35.44 ?  176 LEU F CD1 1 
ATOM   3005 C CD2 . LEU B 2 176 ? 19.504  -26.638 -12.305 1.00 32.81 ?  176 LEU F CD2 1 
ATOM   3006 N N   . SER B 2 177 ? 22.986  -26.647 -12.100 1.00 31.36 ?  177 SER F N   1 
ATOM   3007 C CA  . SER B 2 177 ? 23.143  -26.187 -10.730 1.00 34.07 ?  177 SER F CA  1 
ATOM   3008 C C   . SER B 2 177 ? 22.161  -25.050 -10.488 1.00 39.07 ?  177 SER F C   1 
ATOM   3009 O O   . SER B 2 177 ? 21.933  -24.210 -11.368 1.00 37.57 ?  177 SER F O   1 
ATOM   3010 C CB  . SER B 2 177 ? 24.577  -25.721 -10.449 1.00 38.79 ?  177 SER F CB  1 
ATOM   3011 O OG  . SER B 2 177 ? 24.762  -24.411 -10.949 1.00 41.47 ?  177 SER F OG  1 
ATOM   3012 N N   . SER B 2 178 ? 21.538  -25.059 -9.317  1.00 35.02 ?  178 SER F N   1 
ATOM   3013 C CA  . SER B 2 178 ? 20.736  -23.944 -8.836  1.00 37.63 ?  178 SER F CA  1 
ATOM   3014 C C   . SER B 2 178 ? 21.318  -23.505 -7.506  1.00 38.60 ?  178 SER F C   1 
ATOM   3015 O O   . SER B 2 178 ? 21.559  -24.344 -6.633  1.00 37.90 ?  178 SER F O   1 
ATOM   3016 C CB  . SER B 2 178 ? 19.267  -24.335 -8.679  1.00 37.46 ?  178 SER F CB  1 
ATOM   3017 O OG  . SER B 2 178 ? 18.482  -23.206 -8.338  1.00 40.37 ?  178 SER F OG  1 
ATOM   3018 N N   . THR B 2 179 ? 21.578  -22.208 -7.360  1.00 35.75 ?  179 THR F N   1 
ATOM   3019 C CA  . THR B 2 179 ? 22.196  -21.685 -6.149  1.00 36.07 ?  179 THR F CA  1 
ATOM   3020 C C   . THR B 2 179 ? 21.249  -20.689 -5.508  1.00 34.70 ?  179 THR F C   1 
ATOM   3021 O O   . THR B 2 179 ? 20.806  -19.740 -6.161  1.00 34.68 ?  179 THR F O   1 
ATOM   3022 C CB  . THR B 2 179 ? 23.547  -21.035 -6.431  1.00 36.18 ?  179 THR F CB  1 
ATOM   3023 O OG1 . THR B 2 179 ? 24.379  -21.967 -7.125  1.00 37.34 ?  179 THR F OG1 1 
ATOM   3024 C CG2 . THR B 2 179 ? 24.229  -20.660 -5.123  1.00 35.85 ?  179 THR F CG2 1 
ATOM   3025 N N   . LEU B 2 180 ? 20.921  -20.932 -4.245  1.00 34.27 ?  180 LEU F N   1 
ATOM   3026 C CA  . LEU B 2 180 ? 20.141  -20.012 -3.428  1.00 34.00 ?  180 LEU F CA  1 
ATOM   3027 C C   . LEU B 2 180 ? 21.105  -19.266 -2.522  1.00 35.85 ?  180 LEU F C   1 
ATOM   3028 O O   . LEU B 2 180 ? 21.856  -19.892 -1.770  1.00 34.28 ?  180 LEU F O   1 
ATOM   3029 C CB  . LEU B 2 180 ? 19.115  -20.776 -2.597  1.00 35.00 ?  180 LEU F CB  1 
ATOM   3030 C CG  . LEU B 2 180 ? 18.262  -19.959 -1.637  1.00 39.17 ?  180 LEU F CG  1 
ATOM   3031 C CD1 . LEU B 2 180 ? 17.209  -19.155 -2.392  1.00 39.31 ?  180 LEU F CD1 1 
ATOM   3032 C CD2 . LEU B 2 180 ? 17.615  -20.928 -0.657  1.00 38.70 ?  180 LEU F CD2 1 
ATOM   3033 N N   . THR B 2 181 ? 21.092  -17.943 -2.596  1.00 37.57 ?  181 THR F N   1 
ATOM   3034 C CA  . THR B 2 181 ? 22.002  -17.116 -1.814  1.00 39.62 ?  181 THR F CA  1 
ATOM   3035 C C   . THR B 2 181 ? 21.214  -16.342 -0.773  1.00 36.89 ?  181 THR F C   1 
ATOM   3036 O O   . THR B 2 181 ? 20.283  -15.607 -1.115  1.00 41.22 ?  181 THR F O   1 
ATOM   3037 C CB  . THR B 2 181 ? 22.786  -16.153 -2.704  1.00 42.42 ?  181 THR F CB  1 
ATOM   3038 O OG1 . THR B 2 181 ? 23.242  -16.853 -3.871  1.00 48.54 ?  181 THR F OG1 1 
ATOM   3039 C CG2 . THR B 2 181 ? 23.972  -15.569 -1.932  1.00 41.53 ?  181 THR F CG2 1 
ATOM   3040 N N   . LEU B 2 182 ? 21.576  -16.526 0.493   1.00 36.48 ?  182 LEU F N   1 
ATOM   3041 C CA  . LEU B 2 182 ? 20.993  -15.768 1.585   1.00 40.73 ?  182 LEU F CA  1 
ATOM   3042 C C   . LEU B 2 182 ? 22.108  -15.189 2.442   1.00 37.58 ?  182 LEU F C   1 
ATOM   3043 O O   . LEU B 2 182 ? 23.266  -15.606 2.368   1.00 39.40 ?  182 LEU F O   1 
ATOM   3044 C CB  . LEU B 2 182 ? 20.051  -16.627 2.454   1.00 40.23 ?  182 LEU F CB  1 
ATOM   3045 C CG  . LEU B 2 182 ? 18.894  -17.339 1.749   1.00 43.31 ?  182 LEU F CG  1 
ATOM   3046 C CD1 . LEU B 2 182 ? 18.250  -18.402 2.640   1.00 43.10 ?  182 LEU F CD1 1 
ATOM   3047 C CD2 . LEU B 2 182 ? 17.860  -16.328 1.280   1.00 45.53 ?  182 LEU F CD2 1 
ATOM   3048 N N   . SER B 2 183 ? 21.747  -14.187 3.236   1.00 41.32 ?  183 SER F N   1 
ATOM   3049 C CA  . SER B 2 183 ? 22.621  -13.764 4.315   1.00 41.04 ?  183 SER F CA  1 
ATOM   3050 C C   . SER B 2 183 ? 22.678  -14.859 5.368   1.00 41.06 ?  183 SER F C   1 
ATOM   3051 O O   . SER B 2 183 ? 21.758  -15.673 5.495   1.00 41.91 ?  183 SER F O   1 
ATOM   3052 C CB  . SER B 2 183 ? 22.114  -12.459 4.926   1.00 42.10 ?  183 SER F CB  1 
ATOM   3053 O OG  . SER B 2 183 ? 20.871  -12.674 5.566   1.00 40.14 ?  183 SER F OG  1 
ATOM   3054 N N   . LYS B 2 184 ? 23.792  -14.900 6.103   1.00 40.99 ?  184 LYS F N   1 
ATOM   3055 C CA  . LYS B 2 184 ? 23.885  -15.785 7.258   1.00 41.24 ?  184 LYS F CA  1 
ATOM   3056 C C   . LYS B 2 184 ? 22.731  -15.558 8.222   1.00 43.29 ?  184 LYS F C   1 
ATOM   3057 O O   . LYS B 2 184 ? 22.197  -16.512 8.800   1.00 42.35 ?  184 LYS F O   1 
ATOM   3058 C CB  . LYS B 2 184 ? 25.221  -15.579 7.971   1.00 46.38 ?  184 LYS F CB  1 
ATOM   3059 C CG  . LYS B 2 184 ? 25.457  -16.492 9.171   1.00 46.29 ?  184 LYS F CG  1 
ATOM   3060 C CD  . LYS B 2 184 ? 26.681  -16.027 9.953   1.00 51.50 ?  184 LYS F CD  1 
ATOM   3061 C CE  . LYS B 2 184 ? 26.443  -16.023 11.459  1.00 56.97 ?  184 LYS F CE  1 
ATOM   3062 N NZ  . LYS B 2 184 ? 26.420  -17.391 12.041  1.00 58.37 ?  184 LYS F NZ  1 
ATOM   3063 N N   . ALA B 2 185 ? 22.327  -14.297 8.405   1.00 42.96 ?  185 ALA F N   1 
ATOM   3064 C CA  . ALA B 2 185 ? 21.238  -13.993 9.328   1.00 42.43 ?  185 ALA F CA  1 
ATOM   3065 C C   . ALA B 2 185 ? 19.935  -14.643 8.875   1.00 41.52 ?  185 ALA F C   1 
ATOM   3066 O O   . ALA B 2 185 ? 19.231  -15.272 9.673   1.00 44.32 ?  185 ALA F O   1 
ATOM   3067 C CB  . ALA B 2 185 ? 21.076  -12.479 9.461   1.00 41.64 ?  185 ALA F CB  1 
ATOM   3068 N N   . ASP B 2 186 ? 19.597  -14.507 7.590   1.00 41.85 ?  186 ASP F N   1 
ATOM   3069 C CA  . ASP B 2 186 ? 18.380  -15.140 7.087   1.00 42.87 ?  186 ASP F CA  1 
ATOM   3070 C C   . ASP B 2 186 ? 18.509  -16.657 7.071   1.00 40.03 ?  186 ASP F C   1 
ATOM   3071 O O   . ASP B 2 186 ? 17.547  -17.366 7.382   1.00 43.07 ?  186 ASP F O   1 
ATOM   3072 C CB  . ASP B 2 186 ? 18.048  -14.625 5.690   1.00 43.92 ?  186 ASP F CB  1 
ATOM   3073 C CG  . ASP B 2 186 ? 17.381  -13.273 5.718   1.00 50.10 ?  186 ASP F CG  1 
ATOM   3074 O OD1 . ASP B 2 186 ? 16.595  -13.031 6.653   1.00 53.20 ?  186 ASP F OD1 1 
ATOM   3075 O OD2 . ASP B 2 186 ? 17.643  -12.455 4.808   1.00 49.17 ?  186 ASP F OD2 1 
ATOM   3076 N N   . TYR B 2 187 ? 19.685  -17.171 6.701   1.00 39.61 ?  187 TYR F N   1 
ATOM   3077 C CA  . TYR B 2 187 ? 19.889  -18.616 6.708   1.00 39.91 ?  187 TYR F CA  1 
ATOM   3078 C C   . TYR B 2 187 ? 19.603  -19.213 8.083   1.00 41.40 ?  187 TYR F C   1 
ATOM   3079 O O   . TYR B 2 187 ? 18.941  -20.254 8.193   1.00 39.39 ?  187 TYR F O   1 
ATOM   3080 C CB  . TYR B 2 187 ? 21.317  -18.951 6.261   1.00 39.69 ?  187 TYR F CB  1 
ATOM   3081 C CG  . TYR B 2 187 ? 21.643  -20.432 6.293   1.00 38.80 ?  187 TYR F CG  1 
ATOM   3082 C CD1 . TYR B 2 187 ? 21.062  -21.308 5.383   1.00 37.61 ?  187 TYR F CD1 1 
ATOM   3083 C CD2 . TYR B 2 187 ? 22.533  -20.950 7.224   1.00 39.39 ?  187 TYR F CD2 1 
ATOM   3084 C CE1 . TYR B 2 187 ? 21.346  -22.663 5.408   1.00 36.99 ?  187 TYR F CE1 1 
ATOM   3085 C CE2 . TYR B 2 187 ? 22.831  -22.309 7.255   1.00 38.91 ?  187 TYR F CE2 1 
ATOM   3086 C CZ  . TYR B 2 187 ? 22.234  -23.159 6.343   1.00 38.22 ?  187 TYR F CZ  1 
ATOM   3087 O OH  . TYR B 2 187 ? 22.522  -24.510 6.363   1.00 38.16 ?  187 TYR F OH  1 
ATOM   3088 N N   . GLU B 2 188 ? 20.085  -18.566 9.150   1.00 41.49 ?  188 GLU F N   1 
ATOM   3089 C CA  . GLU B 2 188 ? 19.890  -19.101 10.495  1.00 43.98 ?  188 GLU F CA  1 
ATOM   3090 C C   . GLU B 2 188 ? 18.454  -18.967 11.002  1.00 44.32 ?  188 GLU F C   1 
ATOM   3091 O O   . GLU B 2 188 ? 18.127  -19.558 12.038  1.00 45.52 ?  188 GLU F O   1 
ATOM   3092 C CB  . GLU B 2 188 ? 20.857  -18.425 11.468  1.00 44.17 ?  188 GLU F CB  1 
ATOM   3093 C CG  . GLU B 2 188 ? 22.308  -18.816 11.235  1.00 45.23 ?  188 GLU F CG  1 
ATOM   3094 C CD  . GLU B 2 188 ? 23.281  -18.023 12.089  1.00 56.50 ?  188 GLU F CD  1 
ATOM   3095 O OE1 . GLU B 2 188 ? 22.919  -16.917 12.552  1.00 59.08 ?  188 GLU F OE1 1 
ATOM   3096 O OE2 . GLU B 2 188 ? 24.413  -18.513 12.296  1.00 60.38 ?  188 GLU F OE2 1 
ATOM   3097 N N   . LYS B 2 189 ? 17.590  -18.238 10.299  1.00 38.76 ?  189 LYS F N   1 
ATOM   3098 C CA  . LYS B 2 189 ? 16.207  -18.069 10.724  1.00 42.81 ?  189 LYS F CA  1 
ATOM   3099 C C   . LYS B 2 189 ? 15.312  -19.211 10.272  1.00 44.88 ?  189 LYS F C   1 
ATOM   3100 O O   . LYS B 2 189 ? 14.110  -19.197 10.573  1.00 44.78 ?  189 LYS F O   1 
ATOM   3101 C CB  . LYS B 2 189 ? 15.659  -16.743 10.189  1.00 45.71 ?  189 LYS F CB  1 
ATOM   3102 C CG  . LYS B 2 189 ? 16.144  -15.516 10.959  1.00 49.50 ?  189 LYS F CG  1 
ATOM   3103 C CD  . LYS B 2 189 ? 15.725  -14.219 10.270  1.00 51.80 ?  189 LYS F CD  1 
ATOM   3104 C CE  . LYS B 2 189 ? 16.149  -12.992 11.074  1.00 55.86 ?  189 LYS F CE  1 
ATOM   3105 N NZ  . LYS B 2 189 ? 16.161  -13.265 12.546  1.00 59.32 ?  189 LYS F NZ  1 
ATOM   3106 N N   . HIS B 2 190 ? 15.893  -20.160 9.542   1.00 41.48 ?  190 HIS F N   1 
ATOM   3107 C CA  . HIS B 2 190 ? 15.063  -21.240 8.960   1.00 40.05 ?  190 HIS F CA  1 
ATOM   3108 C C   . HIS B 2 190 ? 15.691  -22.607 9.217   1.00 41.88 ?  190 HIS F C   1 
ATOM   3109 O O   . HIS B 2 190 ? 16.880  -22.701 9.518   1.00 41.96 ?  190 HIS F O   1 
ATOM   3110 C CB  . HIS B 2 190 ? 14.845  -20.978 7.471   1.00 39.16 ?  190 HIS F CB  1 
ATOM   3111 C CG  . HIS B 2 190 ? 14.218  -19.661 7.187   1.00 41.66 ?  190 HIS F CG  1 
ATOM   3112 N ND1 . HIS B 2 190 ? 12.892  -19.395 7.441   1.00 43.48 ?  190 HIS F ND1 1 
ATOM   3113 C CD2 . HIS B 2 190 ? 14.730  -18.539 6.686   1.00 40.15 ?  190 HIS F CD2 1 
ATOM   3114 C CE1 . HIS B 2 190 ? 12.627  -18.148 7.095   1.00 38.57 ?  190 HIS F CE1 1 
ATOM   3115 N NE2 . HIS B 2 190 ? 13.730  -17.612 6.635   1.00 43.80 ?  190 HIS F NE2 1 
ATOM   3116 N N   . LYS B 2 191 ? 14.886  -23.645 9.066   1.00 36.95 ?  191 LYS F N   1 
ATOM   3117 C CA  . LYS B 2 191 ? 15.352  -24.982 9.381   1.00 40.36 ?  191 LYS F CA  1 
ATOM   3118 C C   . LYS B 2 191 ? 15.474  -25.882 8.160   1.00 39.22 ?  191 LYS F C   1 
ATOM   3119 O O   . LYS B 2 191 ? 16.521  -26.509 7.962   1.00 38.48 ?  191 LYS F O   1 
ATOM   3120 C CB  . LYS B 2 191 ? 14.423  -25.623 10.421  1.00 38.30 ?  191 LYS F CB  1 
ATOM   3121 C CG  . LYS B 2 191 ? 14.748  -27.080 10.729  1.00 44.64 ?  191 LYS F CG  1 
ATOM   3122 C CD  . LYS B 2 191 ? 16.042  -27.200 11.539  1.00 45.72 ?  191 LYS F CD  1 
ATOM   3123 C CE  . LYS B 2 191 ? 16.110  -26.175 12.674  1.00 51.08 ?  191 LYS F CE  1 
ATOM   3124 N NZ  . LYS B 2 191 ? 17.016  -26.609 13.789  1.00 56.57 ?  191 LYS F NZ  1 
ATOM   3125 N N   . VAL B 2 192 ? 14.442  -25.963 7.327   1.00 35.60 ?  192 VAL F N   1 
ATOM   3126 C CA  . VAL B 2 192 ? 14.380  -26.950 6.255   1.00 34.60 ?  192 VAL F CA  1 
ATOM   3127 C C   . VAL B 2 192 ? 14.724  -26.271 4.940   1.00 35.50 ?  192 VAL F C   1 
ATOM   3128 O O   . VAL B 2 192 ? 14.086  -25.283 4.557   1.00 33.51 ?  192 VAL F O   1 
ATOM   3129 C CB  . VAL B 2 192 ? 12.991  -27.602 6.170   1.00 38.70 ?  192 VAL F CB  1 
ATOM   3130 C CG1 . VAL B 2 192 ? 12.979  -28.654 5.080   1.00 37.29 ?  192 VAL F CG1 1 
ATOM   3131 C CG2 . VAL B 2 192 ? 12.572  -28.188 7.511   1.00 37.75 ?  192 VAL F CG2 1 
ATOM   3132 N N   . TYR B 2 193 ? 15.706  -26.818 4.233   1.00 31.69 ?  193 TYR F N   1 
ATOM   3133 C CA  . TYR B 2 193 ? 16.121  -26.306 2.934   1.00 35.03 ?  193 TYR F CA  1 
ATOM   3134 C C   . TYR B 2 193 ? 15.902  -27.405 1.907   1.00 33.10 ?  193 TYR F C   1 
ATOM   3135 O O   . TYR B 2 193 ? 16.417  -28.511 2.071   1.00 33.70 ?  193 TYR F O   1 
ATOM   3136 C CB  . TYR B 2 193 ? 17.583  -25.852 2.982   1.00 33.42 ?  193 TYR F CB  1 
ATOM   3137 C CG  . TYR B 2 193 ? 17.719  -24.546 3.734   1.00 34.35 ?  193 TYR F CG  1 
ATOM   3138 C CD1 . TYR B 2 193 ? 17.838  -24.529 5.118   1.00 34.86 ?  193 TYR F CD1 1 
ATOM   3139 C CD2 . TYR B 2 193 ? 17.676  -23.334 3.064   1.00 34.81 ?  193 TYR F CD2 1 
ATOM   3140 C CE1 . TYR B 2 193 ? 17.937  -23.341 5.815   1.00 35.16 ?  193 TYR F CE1 1 
ATOM   3141 C CE2 . TYR B 2 193 ? 17.775  -22.135 3.750   1.00 35.97 ?  193 TYR F CE2 1 
ATOM   3142 C CZ  . TYR B 2 193 ? 17.901  -22.146 5.128   1.00 37.00 ?  193 TYR F CZ  1 
ATOM   3143 O OH  . TYR B 2 193 ? 17.990  -20.951 5.816   1.00 37.87 ?  193 TYR F OH  1 
ATOM   3144 N N   . ALA B 2 194 ? 15.139  -27.106 0.855   1.00 31.53 ?  194 ALA F N   1 
ATOM   3145 C CA  . ALA B 2 194 ? 14.740  -28.136 -0.092  1.00 33.08 ?  194 ALA F CA  1 
ATOM   3146 C C   . ALA B 2 194 ? 14.732  -27.586 -1.508  1.00 35.06 ?  194 ALA F C   1 
ATOM   3147 O O   . ALA B 2 194 ? 14.382  -26.424 -1.726  1.00 34.14 ?  194 ALA F O   1 
ATOM   3148 C CB  . ALA B 2 194 ? 13.356  -28.690 0.258   1.00 34.44 ?  194 ALA F CB  1 
ATOM   3149 N N   . CYS B 2 195 ? 15.116  -28.418 -2.479  1.00 34.33 ?  195 CYS F N   1 
ATOM   3150 C CA  . CYS B 2 195 ? 14.888  -28.079 -3.877  1.00 35.69 ?  195 CYS F CA  1 
ATOM   3151 C C   . CYS B 2 195 ? 14.015  -29.162 -4.482  1.00 35.57 ?  195 CYS F C   1 
ATOM   3152 O O   . CYS B 2 195 ? 14.258  -30.359 -4.271  1.00 36.81 ?  195 CYS F O   1 
ATOM   3153 C CB  . CYS B 2 195 ? 16.194  -27.900 -4.676  1.00 39.93 ?  195 CYS F CB  1 
ATOM   3154 S SG  . CYS B 2 195 ? 17.223  -29.357 -4.824  1.00 43.28 ?  195 CYS F SG  1 
ATOM   3155 N N   . GLU B 2 196 ? 12.976  -28.744 -5.187  1.00 31.49 ?  196 GLU F N   1 
ATOM   3156 C CA  . GLU B 2 196 ? 12.021  -29.663 -5.777  1.00 35.84 ?  196 GLU F CA  1 
ATOM   3157 C C   . GLU B 2 196 ? 12.197  -29.621 -7.289  1.00 35.42 ?  196 GLU F C   1 
ATOM   3158 O O   . GLU B 2 196 ? 12.263  -28.537 -7.886  1.00 35.66 ?  196 GLU F O   1 
ATOM   3159 C CB  . GLU B 2 196 ? 10.591  -29.303 -5.358  1.00 38.07 ?  196 GLU F CB  1 
ATOM   3160 C CG  . GLU B 2 196 ? 9.515   -30.048 -6.112  1.00 40.75 ?  196 GLU F CG  1 
ATOM   3161 C CD  . GLU B 2 196 ? 8.120   -29.681 -5.629  1.00 48.73 ?  196 GLU F CD  1 
ATOM   3162 O OE1 . GLU B 2 196 ? 7.997   -28.781 -4.772  1.00 50.35 ?  196 GLU F OE1 1 
ATOM   3163 O OE2 . GLU B 2 196 ? 7.153   -30.317 -6.092  1.00 49.04 ?  196 GLU F OE2 1 
ATOM   3164 N N   . VAL B 2 197 ? 12.282  -30.797 -7.906  1.00 33.01 ?  197 VAL F N   1 
ATOM   3165 C CA  . VAL B 2 197 ? 12.717  -30.920 -9.290  1.00 32.73 ?  197 VAL F CA  1 
ATOM   3166 C C   . VAL B 2 197 ? 11.607  -31.568 -10.102 1.00 33.81 ?  197 VAL F C   1 
ATOM   3167 O O   . VAL B 2 197 ? 11.069  -32.606 -9.702  1.00 31.02 ?  197 VAL F O   1 
ATOM   3168 C CB  . VAL B 2 197 ? 14.014  -31.744 -9.376  1.00 31.87 ?  197 VAL F CB  1 
ATOM   3169 C CG1 . VAL B 2 197 ? 14.378  -32.026 -10.831 1.00 31.91 ?  197 VAL F CG1 1 
ATOM   3170 C CG2 . VAL B 2 197 ? 15.137  -31.001 -8.640  1.00 33.49 ?  197 VAL F CG2 1 
ATOM   3171 N N   . THR B 2 198 ? 11.270  -30.959 -11.236 1.00 30.84 ?  198 THR F N   1 
ATOM   3172 C CA  . THR B 2 198 ? 10.360  -31.562 -12.204 1.00 33.41 ?  198 THR F CA  1 
ATOM   3173 C C   . THR B 2 198 ? 11.074  -31.741 -13.537 1.00 32.75 ?  198 THR F C   1 
ATOM   3174 O O   . THR B 2 198 ? 11.811  -30.856 -13.995 1.00 32.58 ?  198 THR F O   1 
ATOM   3175 C CB  . THR B 2 198 ? 9.070   -30.743 -12.388 1.00 39.34 ?  198 THR F CB  1 
ATOM   3176 O OG1 . THR B 2 198 ? 9.336   -29.600 -13.201 1.00 48.40 ?  198 THR F OG1 1 
ATOM   3177 C CG2 . THR B 2 198 ? 8.484   -30.305 -11.059 1.00 34.65 ?  198 THR F CG2 1 
ATOM   3178 N N   . HIS B 2 199 ? 10.882  -32.920 -14.114 1.00 29.50 ?  199 HIS F N   1 
ATOM   3179 C CA  . HIS B 2 199 ? 11.537  -33.268 -15.394 1.00 31.38 ?  199 HIS F CA  1 
ATOM   3180 C C   . HIS B 2 199 ? 10.712  -34.383 -16.032 1.00 31.14 ?  199 HIS F C   1 
ATOM   3181 O O   . HIS B 2 199 ? 10.070  -35.159 -15.324 1.00 30.41 ?  199 HIS F O   1 
ATOM   3182 C CB  . HIS B 2 199 ? 12.987  -33.691 -15.170 1.00 30.27 ?  199 HIS F CB  1 
ATOM   3183 C CG  . HIS B 2 199 ? 13.696  -34.167 -16.389 1.00 28.87 ?  199 HIS F CG  1 
ATOM   3184 N ND1 . HIS B 2 199 ? 14.318  -33.317 -17.275 1.00 31.88 ?  199 HIS F ND1 1 
ATOM   3185 C CD2 . HIS B 2 199 ? 13.884  -35.396 -16.867 1.00 29.31 ?  199 HIS F CD2 1 
ATOM   3186 C CE1 . HIS B 2 199 ? 14.850  -34.028 -18.252 1.00 29.32 ?  199 HIS F CE1 1 
ATOM   3187 N NE2 . HIS B 2 199 ? 14.594  -35.291 -18.025 1.00 30.91 ?  199 HIS F NE2 1 
ATOM   3188 N N   . GLN B 2 200 ? 10.747  -34.444 -17.353 1.00 35.44 ?  200 GLN F N   1 
ATOM   3189 C CA  . GLN B 2 200 ? 9.962   -35.445 -18.079 1.00 35.89 ?  200 GLN F CA  1 
ATOM   3190 C C   . GLN B 2 200 ? 10.258  -36.866 -17.613 1.00 36.85 ?  200 GLN F C   1 
ATOM   3191 O O   . GLN B 2 200 ? 9.381   -37.740 -17.663 1.00 35.66 ?  200 GLN F O   1 
ATOM   3192 C CB  . GLN B 2 200 ? 10.231  -35.309 -19.576 1.00 35.41 ?  200 GLN F CB  1 
ATOM   3193 C CG  . GLN B 2 200 ? 9.277   -36.087 -20.452 1.00 40.83 ?  200 GLN F CG  1 
ATOM   3194 C CD  . GLN B 2 200 ? 9.690   -36.063 -21.910 1.00 40.01 ?  200 GLN F CD  1 
ATOM   3195 O OE1 . GLN B 2 200 ? 10.445  -35.189 -22.337 1.00 40.14 ?  200 GLN F OE1 1 
ATOM   3196 N NE2 . GLN B 2 200 ? 9.185   -37.015 -22.684 1.00 44.65 ?  200 GLN F NE2 1 
ATOM   3197 N N   . GLY B 2 201 ? 11.481  -37.125 -17.164 1.00 33.44 ?  201 GLY F N   1 
ATOM   3198 C CA  . GLY B 2 201 ? 11.826  -38.450 -16.706 1.00 31.99 ?  201 GLY F CA  1 
ATOM   3199 C C   . GLY B 2 201 ? 11.327  -38.803 -15.326 1.00 34.56 ?  201 GLY F C   1 
ATOM   3200 O O   . GLY B 2 201 ? 11.501  -39.941 -14.894 1.00 36.14 ?  201 GLY F O   1 
ATOM   3201 N N   . LEU B 2 202 ? 10.716  -37.858 -14.616 1.00 34.37 ?  202 LEU F N   1 
ATOM   3202 C CA  . LEU B 2 202 ? 10.221  -38.078 -13.262 1.00 37.45 ?  202 LEU F CA  1 
ATOM   3203 C C   . LEU B 2 202 ? 8.702   -38.160 -13.314 1.00 37.36 ?  202 LEU F C   1 
ATOM   3204 O O   . LEU B 2 202 ? 8.043   -37.242 -13.821 1.00 40.26 ?  202 LEU F O   1 
ATOM   3205 C CB  . LEU B 2 202 ? 10.670  -36.960 -12.310 1.00 34.88 ?  202 LEU F CB  1 
ATOM   3206 C CG  . LEU B 2 202 ? 12.184  -36.757 -12.146 1.00 32.60 ?  202 LEU F CG  1 
ATOM   3207 C CD1 . LEU B 2 202 ? 12.482  -35.440 -11.437 1.00 32.80 ?  202 LEU F CD1 1 
ATOM   3208 C CD2 . LEU B 2 202 ? 12.829  -37.912 -11.398 1.00 32.61 ?  202 LEU F CD2 1 
ATOM   3209 N N   . SER B 2 203 ? 8.156   -39.258 -12.796 1.00 40.25 ?  203 SER F N   1 
ATOM   3210 C CA  . SER B 2 203 ? 6.706   -39.415 -12.753 1.00 45.00 ?  203 SER F CA  1 
ATOM   3211 C C   . SER B 2 203 ? 6.057   -38.259 -12.007 1.00 41.87 ?  203 SER F C   1 
ATOM   3212 O O   . SER B 2 203 ? 5.068   -37.678 -12.472 1.00 49.37 ?  203 SER F O   1 
ATOM   3213 C CB  . SER B 2 203 ? 6.356   -40.743 -12.091 1.00 43.63 ?  203 SER F CB  1 
ATOM   3214 O OG  . SER B 2 203 ? 6.863   -41.820 -12.857 1.00 51.75 ?  203 SER F OG  1 
ATOM   3215 N N   . SER B 2 204 ? 6.616   -37.896 -10.861 1.00 40.70 ?  204 SER F N   1 
ATOM   3216 C CA  . SER B 2 204 ? 6.134   -36.819 -10.015 1.00 41.10 ?  204 SER F CA  1 
ATOM   3217 C C   . SER B 2 204 ? 7.340   -36.045 -9.512  1.00 40.39 ?  204 SER F C   1 
ATOM   3218 O O   . SER B 2 204 ? 8.448   -36.592 -9.449  1.00 37.06 ?  204 SER F O   1 
ATOM   3219 C CB  . SER B 2 204 ? 5.324   -37.372 -8.836  1.00 44.25 ?  204 SER F CB  1 
ATOM   3220 O OG  . SER B 2 204 ? 4.591   -38.523 -9.229  1.00 50.33 ?  204 SER F OG  1 
ATOM   3221 N N   . PRO B 2 205 ? 7.160   -34.775 -9.139  1.00 36.32 ?  205 PRO F N   1 
ATOM   3222 C CA  . PRO B 2 205 ? 8.305   -33.972 -8.686  1.00 36.44 ?  205 PRO F CA  1 
ATOM   3223 C C   . PRO B 2 205 ? 8.989   -34.608 -7.487  1.00 39.26 ?  205 PRO F C   1 
ATOM   3224 O O   . PRO B 2 205 ? 8.339   -35.188 -6.616  1.00 40.99 ?  205 PRO F O   1 
ATOM   3225 C CB  . PRO B 2 205 ? 7.669   -32.626 -8.324  1.00 37.71 ?  205 PRO F CB  1 
ATOM   3226 C CG  . PRO B 2 205 ? 6.466   -32.557 -9.218  1.00 38.19 ?  205 PRO F CG  1 
ATOM   3227 C CD  . PRO B 2 205 ? 5.934   -33.966 -9.220  1.00 37.80 ?  205 PRO F CD  1 
ATOM   3228 N N   . VAL B 2 206 ? 10.318  -34.523 -7.464  1.00 34.97 ?  206 VAL F N   1 
ATOM   3229 C CA  . VAL B 2 206 ? 11.108  -35.088 -6.378  1.00 35.80 ?  206 VAL F CA  1 
ATOM   3230 C C   . VAL B 2 206 ? 11.745  -33.943 -5.606  1.00 36.74 ?  206 VAL F C   1 
ATOM   3231 O O   . VAL B 2 206 ? 12.065  -32.890 -6.170  1.00 36.03 ?  206 VAL F O   1 
ATOM   3232 C CB  . VAL B 2 206 ? 12.188  -36.071 -6.875  1.00 38.67 ?  206 VAL F CB  1 
ATOM   3233 C CG1 . VAL B 2 206 ? 11.538  -37.268 -7.579  1.00 40.46 ?  206 VAL F CG1 1 
ATOM   3234 C CG2 . VAL B 2 206 ? 13.198  -35.372 -7.758  1.00 35.51 ?  206 VAL F CG2 1 
ATOM   3235 N N   . THR B 2 207 ? 11.942  -34.160 -4.308  1.00 33.37 ?  207 THR F N   1 
ATOM   3236 C CA  . THR B 2 207 ? 12.488  -33.139 -3.420  1.00 33.66 ?  207 THR F CA  1 
ATOM   3237 C C   . THR B 2 207 ? 13.702  -33.698 -2.688  1.00 35.46 ?  207 THR F C   1 
ATOM   3238 O O   . THR B 2 207 ? 13.628  -34.777 -2.090  1.00 36.95 ?  207 THR F O   1 
ATOM   3239 C CB  . THR B 2 207 ? 11.425  -32.680 -2.412  1.00 38.57 ?  207 THR F CB  1 
ATOM   3240 O OG1 . THR B 2 207 ? 10.285  -32.160 -3.113  1.00 37.49 ?  207 THR F OG1 1 
ATOM   3241 C CG2 . THR B 2 207 ? 11.986  -31.618 -1.481  1.00 35.35 ?  207 THR F CG2 1 
ATOM   3242 N N   . LYS B 2 208 ? 14.816  -32.980 -2.751  1.00 33.37 ?  208 LYS F N   1 
ATOM   3243 C CA  . LYS B 2 208 ? 15.950  -33.206 -1.868  1.00 34.28 ?  208 LYS F CA  1 
ATOM   3244 C C   . LYS B 2 208 ? 15.997  -32.096 -0.834  1.00 34.02 ?  208 LYS F C   1 
ATOM   3245 O O   . LYS B 2 208 ? 15.810  -30.922 -1.166  1.00 33.88 ?  208 LYS F O   1 
ATOM   3246 C CB  . LYS B 2 208 ? 17.288  -33.244 -2.616  1.00 35.52 ?  208 LYS F CB  1 
ATOM   3247 C CG  . LYS B 2 208 ? 17.508  -34.474 -3.449  1.00 38.73 ?  208 LYS F CG  1 
ATOM   3248 C CD  . LYS B 2 208 ? 17.581  -35.700 -2.563  1.00 41.46 ?  208 LYS F CD  1 
ATOM   3249 C CE  . LYS B 2 208 ? 18.738  -35.614 -1.595  1.00 40.73 ?  208 LYS F CE  1 
ATOM   3250 N NZ  . LYS B 2 208 ? 19.111  -36.985 -1.152  1.00 51.33 ?  208 LYS F NZ  1 
ATOM   3251 N N   . SER B 2 209 ? 16.270  -32.461 0.415   1.00 34.63 ?  209 SER F N   1 
ATOM   3252 C CA  . SER B 2 209 ? 16.274  -31.459 1.467   1.00 35.13 ?  209 SER F CA  1 
ATOM   3253 C C   . SER B 2 209 ? 17.299  -31.804 2.538   1.00 35.58 ?  209 SER F C   1 
ATOM   3254 O O   . SER B 2 209 ? 17.795  -32.934 2.619   1.00 34.24 ?  209 SER F O   1 
ATOM   3255 C CB  . SER B 2 209 ? 14.878  -31.311 2.078   1.00 33.53 ?  209 SER F CB  1 
ATOM   3256 O OG  . SER B 2 209 ? 14.507  -32.510 2.723   1.00 35.67 ?  209 SER F OG  1 
ATOM   3257 N N   . PHE B 2 210 ? 17.621  -30.798 3.352   1.00 32.28 ?  210 PHE F N   1 
ATOM   3258 C CA  . PHE B 2 210 ? 18.367  -30.991 4.590   1.00 35.95 ?  210 PHE F CA  1 
ATOM   3259 C C   . PHE B 2 210 ? 17.807  -30.055 5.655   1.00 36.25 ?  210 PHE F C   1 
ATOM   3260 O O   . PHE B 2 210 ? 17.132  -29.069 5.349   1.00 33.39 ?  210 PHE F O   1 
ATOM   3261 C CB  . PHE B 2 210 ? 19.879  -30.758 4.391   1.00 33.66 ?  210 PHE F CB  1 
ATOM   3262 C CG  . PHE B 2 210 ? 20.247  -29.331 4.100   1.00 35.13 ?  210 PHE F CG  1 
ATOM   3263 C CD1 . PHE B 2 210 ? 20.523  -28.434 5.129   1.00 34.39 ?  210 PHE F CD1 1 
ATOM   3264 C CD2 . PHE B 2 210 ? 20.355  -28.890 2.788   1.00 33.73 ?  210 PHE F CD2 1 
ATOM   3265 C CE1 . PHE B 2 210 ? 20.861  -27.114 4.855   1.00 35.44 ?  210 PHE F CE1 1 
ATOM   3266 C CE2 . PHE B 2 210 ? 20.705  -27.576 2.507   1.00 31.75 ?  210 PHE F CE2 1 
ATOM   3267 C CZ  . PHE B 2 210 ? 20.955  -26.687 3.542   1.00 32.79 ?  210 PHE F CZ  1 
ATOM   3268 N N   . ASN B 2 211 ? 18.079  -30.390 6.916   1.00 38.00 ?  211 ASN F N   1 
ATOM   3269 C CA  . ASN B 2 211 ? 17.734  -29.535 8.046   1.00 41.01 ?  211 ASN F CA  1 
ATOM   3270 C C   . ASN B 2 211 ? 19.000  -28.863 8.555   1.00 41.34 ?  211 ASN F C   1 
ATOM   3271 O O   . ASN B 2 211 ? 19.999  -29.540 8.824   1.00 43.20 ?  211 ASN F O   1 
ATOM   3272 C CB  . ASN B 2 211 ? 17.088  -30.330 9.182   1.00 40.64 ?  211 ASN F CB  1 
ATOM   3273 C CG  . ASN B 2 211 ? 15.680  -30.783 8.863   1.00 43.51 ?  211 ASN F CG  1 
ATOM   3274 O OD1 . ASN B 2 211 ? 15.094  -30.394 7.852   1.00 45.38 ?  211 ASN F OD1 1 
ATOM   3275 N ND2 . ASN B 2 211 ? 15.124  -31.610 9.738   1.00 53.21 ?  211 ASN F ND2 1 
ATOM   3276 N N   . ARG B 2 212 ? 18.960  -27.538 8.678   1.00 38.49 ?  212 ARG F N   1 
ATOM   3277 C CA  . ARG B 2 212 ? 20.099  -26.798 9.211   1.00 41.95 ?  212 ARG F CA  1 
ATOM   3278 C C   . ARG B 2 212 ? 20.421  -27.281 10.619  1.00 46.47 ?  212 ARG F C   1 
ATOM   3279 O O   . ARG B 2 212 ? 19.545  -27.335 11.486  1.00 48.10 ?  212 ARG F O   1 
ATOM   3280 C CB  . ARG B 2 212 ? 19.814  -25.295 9.213   1.00 42.62 ?  212 ARG F CB  1 
ATOM   3281 C CG  . ARG B 2 212 ? 21.023  -24.446 9.590   1.00 42.12 ?  212 ARG F CG  1 
ATOM   3282 C CD  . ARG B 2 212 ? 20.681  -22.965 9.748   1.00 41.92 ?  212 ARG F CD  1 
ATOM   3283 N NE  . ARG B 2 212 ? 19.419  -22.742 10.435  1.00 45.93 ?  212 ARG F NE  1 
ATOM   3284 C CZ  . ARG B 2 212 ? 19.253  -22.827 11.748  1.00 47.70 ?  212 ARG F CZ  1 
ATOM   3285 N NH1 . ARG B 2 212 ? 20.277  -23.024 12.563  1.00 49.52 ?  212 ARG F NH1 1 
ATOM   3286 N NH2 . ARG B 2 212 ? 18.030  -22.697 12.256  1.00 50.43 ?  212 ARG F NH2 1 
ATOM   3287 N N   . GLY B 2 213 ? 21.679  -27.650 10.836  1.00 48.87 ?  213 GLY F N   1 
ATOM   3288 C CA  . GLY B 2 213 ? 22.081  -28.321 12.057  1.00 47.17 ?  213 GLY F CA  1 
ATOM   3289 C C   . GLY B 2 213 ? 21.714  -29.795 12.022  1.00 52.13 ?  213 GLY F C   1 
ATOM   3290 O O   . GLY B 2 213 ? 22.576  -30.667 12.142  1.00 59.31 ?  213 GLY F O   1 
ATOM   3291 N N   . GLN C 1 1   ? -4.962  20.635  -47.517 1.00 44.73 ?  1   GLN D N   1 
ATOM   3292 C CA  . GLN C 1 1   ? -6.003  19.668  -47.914 1.00 31.59 ?  1   GLN D CA  1 
ATOM   3293 C C   . GLN C 1 1   ? -5.547  18.240  -47.589 1.00 27.29 ?  1   GLN D C   1 
ATOM   3294 O O   . GLN C 1 1   ? -6.400  17.393  -47.514 1.00 26.71 ?  1   GLN D O   1 
ATOM   3295 C CB  . GLN C 1 1   ? -6.412  19.920  -49.358 1.00 32.73 ?  1   GLN D CB  1 
ATOM   3296 C CG  . GLN C 1 1   ? -7.545  20.929  -49.456 1.00 49.97 ?  1   GLN D CG  1 
ATOM   3297 C CD  . GLN C 1 1   ? -7.695  21.461  -50.856 1.00 41.38 ?  1   GLN D CD  1 
ATOM   3298 O OE1 . GLN C 1 1   ? -7.571  20.724  -51.828 1.00 41.34 ?  1   GLN D OE1 1 
ATOM   3299 N NE2 . GLN C 1 1   ? -7.958  22.753  -50.968 1.00 47.51 ?  1   GLN D NE2 1 
ATOM   3300 N N   . VAL C 1 2   ? -4.249  18.005  -47.404 1.00 26.28 ?  2   VAL D N   1 
ATOM   3301 C CA  . VAL C 1 2   ? -3.806  16.656  -46.942 1.00 25.22 ?  2   VAL D CA  1 
ATOM   3302 C C   . VAL C 1 2   ? -3.655  16.682  -45.424 1.00 24.18 ?  2   VAL D C   1 
ATOM   3303 O O   . VAL C 1 2   ? -3.001  17.594  -44.929 1.00 26.60 ?  2   VAL D O   1 
ATOM   3304 C CB  . VAL C 1 2   ? -2.514  16.162  -47.618 1.00 26.55 ?  2   VAL D CB  1 
ATOM   3305 C CG1 . VAL C 1 2   ? -2.002  14.890  -46.963 1.00 26.94 ?  2   VAL D CG1 1 
ATOM   3306 C CG2 . VAL C 1 2   ? -2.705  15.951  -49.109 1.00 27.91 ?  2   VAL D CG2 1 
ATOM   3307 N N   . HIS C 1 3   ? -4.265  15.719  -44.734 1.00 22.58 ?  3   HIS D N   1 
ATOM   3308 C CA  . HIS C 1 3   ? -4.131  15.603  -43.289 1.00 22.02 ?  3   HIS D CA  1 
ATOM   3309 C C   . HIS C 1 3   ? -3.842  14.153  -42.907 1.00 23.91 ?  3   HIS D C   1 
ATOM   3310 O O   . HIS C 1 3   ? -4.413  13.211  -43.478 1.00 24.47 ?  3   HIS D O   1 
ATOM   3311 C CB  . HIS C 1 3   ? -5.376  16.091  -42.556 1.00 21.12 ?  3   HIS D CB  1 
ATOM   3312 C CG  . HIS C 1 3   ? -5.596  17.573  -42.673 1.00 26.20 ?  3   HIS D CG  1 
ATOM   3313 N ND1 . HIS C 1 3   ? -5.096  18.472  -41.757 1.00 29.85 ?  3   HIS D ND1 1 
ATOM   3314 C CD2 . HIS C 1 3   ? -6.273  18.306  -43.592 1.00 26.44 ?  3   HIS D CD2 1 
ATOM   3315 C CE1 . HIS C 1 3   ? -5.450  19.700  -42.110 1.00 33.20 ?  3   HIS D CE1 1 
ATOM   3316 N NE2 . HIS C 1 3   ? -6.170  19.628  -43.217 1.00 26.10 ?  3   HIS D NE2 1 
ATOM   3317 N N   . LEU C 1 4   ? -2.935  13.989  -41.942 1.00 20.44 ?  4   LEU D N   1 
ATOM   3318 C CA  . LEU C 1 4   ? -2.688  12.708  -41.285 1.00 22.91 ?  4   LEU D CA  1 
ATOM   3319 C C   . LEU C 1 4   ? -2.984  12.898  -39.807 1.00 22.46 ?  4   LEU D C   1 
ATOM   3320 O O   . LEU C 1 4   ? -2.400  13.785  -39.172 1.00 24.10 ?  4   LEU D O   1 
ATOM   3321 C CB  . LEU C 1 4   ? -1.234  12.260  -41.491 1.00 19.25 ?  4   LEU D CB  1 
ATOM   3322 C CG  . LEU C 1 4   ? -0.843  11.950  -42.928 1.00 22.27 ?  4   LEU D CG  1 
ATOM   3323 C CD1 . LEU C 1 4   ? 0.659   11.590  -42.973 1.00 24.44 ?  4   LEU D CD1 1 
ATOM   3324 C CD2 . LEU C 1 4   ? -1.671  10.798  -43.439 1.00 24.94 ?  4   LEU D CD2 1 
ATOM   3325 N N   . VAL C 1 5   ? -3.908  12.098  -39.261 1.00 23.37 ?  5   VAL D N   1 
ATOM   3326 C CA  . VAL C 1 5   ? -4.372  12.263  -37.881 1.00 23.22 ?  5   VAL D CA  1 
ATOM   3327 C C   . VAL C 1 5   ? -4.098  10.974  -37.126 1.00 24.54 ?  5   VAL D C   1 
ATOM   3328 O O   . VAL C 1 5   ? -4.589  9.911   -37.521 1.00 23.06 ?  5   VAL D O   1 
ATOM   3329 C CB  . VAL C 1 5   ? -5.873  12.608  -37.807 1.00 26.62 ?  5   VAL D CB  1 
ATOM   3330 C CG1 . VAL C 1 5   ? -6.326  12.639  -36.338 1.00 25.96 ?  5   VAL D CG1 1 
ATOM   3331 C CG2 . VAL C 1 5   ? -6.158  13.962  -38.489 1.00 25.05 ?  5   VAL D CG2 1 
ATOM   3332 N N   . GLN C 1 6   ? -3.315  11.068  -36.046 1.00 22.97 ?  6   GLN D N   1 
ATOM   3333 C CA  . GLN C 1 6   ? -2.886  9.910   -35.272 1.00 22.30 ?  6   GLN D CA  1 
ATOM   3334 C C   . GLN C 1 6   ? -3.708  9.718   -34.005 1.00 22.73 ?  6   GLN D C   1 
ATOM   3335 O O   . GLN C 1 6   ? -4.374  10.638  -33.508 1.00 22.37 ?  6   GLN D O   1 
ATOM   3336 C CB  . GLN C 1 6   ? -1.403  10.044  -34.905 1.00 22.68 ?  6   GLN D CB  1 
ATOM   3337 C CG  . GLN C 1 6   ? -0.522  10.142  -36.121 1.00 21.71 ?  6   GLN D CG  1 
ATOM   3338 C CD  . GLN C 1 6   ? 0.948   10.224  -35.770 1.00 22.69 ?  6   GLN D CD  1 
ATOM   3339 O OE1 . GLN C 1 6   ? 1.681   11.002  -36.361 1.00 21.55 ?  6   GLN D OE1 1 
ATOM   3340 N NE2 . GLN C 1 6   ? 1.386   9.400   -34.811 1.00 24.99 ?  6   GLN D NE2 1 
ATOM   3341 N N   . SER C 1 7   ? -3.667  8.484   -33.496 1.00 21.86 ?  7   SER D N   1 
ATOM   3342 C CA  . SER C 1 7   ? -4.360  8.132   -32.267 1.00 24.13 ?  7   SER D CA  1 
ATOM   3343 C C   . SER C 1 7   ? -3.646  8.737   -31.059 1.00 25.83 ?  7   SER D C   1 
ATOM   3344 O O   . SER C 1 7   ? -2.535  9.275   -31.157 1.00 24.76 ?  7   SER D O   1 
ATOM   3345 C CB  . SER C 1 7   ? -4.463  6.606   -32.135 1.00 26.22 ?  7   SER D CB  1 
ATOM   3346 O OG  . SER C 1 7   ? -3.203  6.005   -32.423 1.00 26.22 ?  7   SER D OG  1 
ATOM   3347 N N   . GLY C 1 8   ? -4.291  8.612   -29.894 1.00 27.31 ?  8   GLY D N   1 
ATOM   3348 C CA  . GLY C 1 8   ? -3.879  9.313   -28.697 1.00 28.24 ?  8   GLY D CA  1 
ATOM   3349 C C   . GLY C 1 8   ? -2.763  8.646   -27.903 1.00 29.79 ?  8   GLY D C   1 
ATOM   3350 O O   . GLY C 1 8   ? -2.267  7.564   -28.222 1.00 26.43 ?  8   GLY D O   1 
ATOM   3351 N N   . VAL C 1 9   ? -2.377  9.337   -26.822 1.00 28.69 ?  9   VAL D N   1 
ATOM   3352 C CA  . VAL C 1 9   ? -1.247  8.935   -25.990 1.00 28.89 ?  9   VAL D CA  1 
ATOM   3353 C C   . VAL C 1 9   ? -1.440  7.515   -25.471 1.00 30.33 ?  9   VAL D C   1 
ATOM   3354 O O   . VAL C 1 9   ? -2.557  7.090   -25.165 1.00 29.93 ?  9   VAL D O   1 
ATOM   3355 C CB  . VAL C 1 9   ? -1.065  9.938   -24.834 1.00 31.41 ?  9   VAL D CB  1 
ATOM   3356 C CG1 . VAL C 1 9   ? -2.287  9.942   -23.921 1.00 33.17 ?  9   VAL D CG1 1 
ATOM   3357 C CG2 . VAL C 1 9   ? 0.184   9.624   -24.038 1.00 33.60 ?  9   VAL D CG2 1 
ATOM   3358 N N   . GLU C 1 10  ? -0.338  6.777   -25.377 1.00 27.40 ?  10  GLU D N   1 
ATOM   3359 C CA  . GLU C 1 10  ? -0.339  5.390   -24.925 1.00 31.34 ?  10  GLU D CA  1 
ATOM   3360 C C   . GLU C 1 10  ? 0.612   5.260   -23.748 1.00 33.77 ?  10  GLU D C   1 
ATOM   3361 O O   . GLU C 1 10  ? 1.739   5.758   -23.804 1.00 33.00 ?  10  GLU D O   1 
ATOM   3362 C CB  . GLU C 1 10  ? 0.109   4.453   -26.043 1.00 29.48 ?  10  GLU D CB  1 
ATOM   3363 C CG  . GLU C 1 10  ? -0.786  4.476   -27.267 1.00 27.51 ?  10  GLU D CG  1 
ATOM   3364 C CD  . GLU C 1 10  ? -2.019  3.582   -27.131 1.00 37.11 ?  10  GLU D CD  1 
ATOM   3365 O OE1 . GLU C 1 10  ? -2.227  2.978   -26.050 1.00 32.61 ?  10  GLU D OE1 1 
ATOM   3366 O OE2 . GLU C 1 10  ? -2.766  3.479   -28.131 1.00 35.95 ?  10  GLU D OE2 1 
ATOM   3367 N N   . VAL C 1 11  ? 0.169   4.589   -22.689 1.00 30.59 ?  11  VAL D N   1 
ATOM   3368 C CA  . VAL C 1 11  ? 1.029   4.299   -21.548 1.00 33.38 ?  11  VAL D CA  1 
ATOM   3369 C C   . VAL C 1 11  ? 1.018   2.788   -21.352 1.00 33.73 ?  11  VAL D C   1 
ATOM   3370 O O   . VAL C 1 11  ? -0.050  2.197   -21.131 1.00 32.23 ?  11  VAL D O   1 
ATOM   3371 C CB  . VAL C 1 11  ? 0.561   5.029   -20.276 1.00 33.71 ?  11  VAL D CB  1 
ATOM   3372 C CG1 . VAL C 1 11  ? 1.503   4.706   -19.124 1.00 35.06 ?  11  VAL D CG1 1 
ATOM   3373 C CG2 . VAL C 1 11  ? 0.481   6.537   -20.504 1.00 35.05 ?  11  VAL D CG2 1 
ATOM   3374 N N   . LYS C 1 12  ? 2.195   2.163   -21.446 1.00 32.09 ?  12  LYS D N   1 
ATOM   3375 C CA  . LYS C 1 12  ? 2.299   0.709   -21.490 1.00 35.96 ?  12  LYS D CA  1 
ATOM   3376 C C   . LYS C 1 12  ? 3.352   0.211   -20.514 1.00 35.90 ?  12  LYS D C   1 
ATOM   3377 O O   . LYS C 1 12  ? 4.285   0.933   -20.158 1.00 36.34 ?  12  LYS D O   1 
ATOM   3378 C CB  . LYS C 1 12  ? 2.659   0.216   -22.892 1.00 33.85 ?  12  LYS D CB  1 
ATOM   3379 C CG  . LYS C 1 12  ? 1.594   0.476   -23.940 1.00 34.18 ?  12  LYS D CG  1 
ATOM   3380 C CD  . LYS C 1 12  ? 0.403   -0.447  -23.785 1.00 38.17 ?  12  LYS D CD  1 
ATOM   3381 C CE  . LYS C 1 12  ? -0.698  -0.043  -24.747 1.00 40.42 ?  12  LYS D CE  1 
ATOM   3382 N NZ  . LYS C 1 12  ? -1.818  -1.017  -24.713 1.00 44.14 ?  12  LYS D NZ  1 
ATOM   3383 N N   . LYS C 1 13  ? 3.192   -1.073  -20.077 1.00 35.53 ?  13  LYS D N   1 
ATOM   3384 C CA  . LYS C 1 13  ? 4.143   -1.840  -19.278 1.00 37.90 ?  13  LYS D CA  1 
ATOM   3385 C C   . LYS C 1 13  ? 5.159   -2.536  -20.184 1.00 36.73 ?  13  LYS D C   1 
ATOM   3386 O O   . LYS C 1 13  ? 4.835   -2.911  -21.317 1.00 34.07 ?  13  LYS D O   1 
ATOM   3387 C CB  . LYS C 1 13  ? 3.411   -2.895  -18.447 1.00 38.23 ?  13  LYS D CB  1 
ATOM   3388 C CG  . LYS C 1 13  ? 2.443   -2.367  -17.366 1.00 39.74 ?  13  LYS D CG  1 
ATOM   3389 C CD  . LYS C 1 13  ? 3.179   -1.622  -16.266 1.00 45.34 ?  13  LYS D CD  1 
ATOM   3390 C CE  . LYS C 1 13  ? 2.335   -1.516  -14.990 1.00 44.51 ?  13  LYS D CE  1 
ATOM   3391 N NZ  . LYS C 1 13  ? 1.031   -0.861  -15.213 1.00 51.21 ?  13  LYS D NZ  1 
ATOM   3392 N N   . PRO C 1 14  ? 6.396   -2.744  -19.718 1.00 37.79 ?  14  PRO D N   1 
ATOM   3393 C CA  . PRO C 1 14  ? 7.350   -3.535  -20.506 1.00 36.50 ?  14  PRO D CA  1 
ATOM   3394 C C   . PRO C 1 14  ? 6.766   -4.900  -20.838 1.00 38.26 ?  14  PRO D C   1 
ATOM   3395 O O   . PRO C 1 14  ? 6.021   -5.482  -20.046 1.00 37.50 ?  14  PRO D O   1 
ATOM   3396 C CB  . PRO C 1 14  ? 8.565   -3.656  -19.575 1.00 38.21 ?  14  PRO D CB  1 
ATOM   3397 C CG  . PRO C 1 14  ? 8.451   -2.512  -18.649 1.00 36.58 ?  14  PRO D CG  1 
ATOM   3398 C CD  . PRO C 1 14  ? 6.977   -2.296  -18.440 1.00 38.48 ?  14  PRO D CD  1 
ATOM   3399 N N   . GLY C 1 15  ? 7.089   -5.401  -22.035 1.00 35.61 ?  15  GLY D N   1 
ATOM   3400 C CA  . GLY C 1 15  ? 6.537   -6.645  -22.526 1.00 37.27 ?  15  GLY D CA  1 
ATOM   3401 C C   . GLY C 1 15  ? 5.193   -6.539  -23.225 1.00 37.37 ?  15  GLY D C   1 
ATOM   3402 O O   . GLY C 1 15  ? 4.812   -7.467  -23.952 1.00 39.17 ?  15  GLY D O   1 
ATOM   3403 N N   . ALA C 1 16  ? 4.451   -5.456  -23.024 1.00 36.76 ?  16  ALA D N   1 
ATOM   3404 C CA  . ALA C 1 16  ? 3.168   -5.298  -23.695 1.00 35.35 ?  16  ALA D CA  1 
ATOM   3405 C C   . ALA C 1 16  ? 3.386   -4.859  -25.144 1.00 37.78 ?  16  ALA D C   1 
ATOM   3406 O O   . ALA C 1 16  ? 4.519   -4.770  -25.636 1.00 35.83 ?  16  ALA D O   1 
ATOM   3407 C CB  . ALA C 1 16  ? 2.285   -4.314  -22.934 1.00 35.84 ?  16  ALA D CB  1 
ATOM   3408 N N   . SER C 1 17  ? 2.290   -4.619  -25.858 1.00 33.43 ?  17  SER D N   1 
ATOM   3409 C CA  . SER C 1 17  ? 2.371   -4.124  -27.220 1.00 34.72 ?  17  SER D CA  1 
ATOM   3410 C C   . SER C 1 17  ? 1.492   -2.885  -27.352 1.00 34.58 ?  17  SER D C   1 
ATOM   3411 O O   . SER C 1 17  ? 0.627   -2.611  -26.514 1.00 34.57 ?  17  SER D O   1 
ATOM   3412 C CB  . SER C 1 17  ? 1.969   -5.197  -28.248 1.00 36.14 ?  17  SER D CB  1 
ATOM   3413 O OG  . SER C 1 17  ? 0.629   -5.616  -28.071 1.00 44.19 ?  17  SER D OG  1 
ATOM   3414 N N   . VAL C 1 18  ? 1.738   -2.111  -28.404 1.00 31.26 ?  18  VAL D N   1 
ATOM   3415 C CA  . VAL C 1 18  ? 0.958   -0.908  -28.658 1.00 31.95 ?  18  VAL D CA  1 
ATOM   3416 C C   . VAL C 1 18  ? 0.629   -0.863  -30.143 1.00 30.28 ?  18  VAL D C   1 
ATOM   3417 O O   . VAL C 1 18  ? 1.413   -1.306  -30.984 1.00 31.78 ?  18  VAL D O   1 
ATOM   3418 C CB  . VAL C 1 18  ? 1.706   0.372   -28.204 1.00 30.38 ?  18  VAL D CB  1 
ATOM   3419 C CG1 . VAL C 1 18  ? 3.028   0.517   -28.939 1.00 31.52 ?  18  VAL D CG1 1 
ATOM   3420 C CG2 . VAL C 1 18  ? 0.840   1.610   -28.400 1.00 30.17 ?  18  VAL D CG2 1 
ATOM   3421 N N   . ARG C 1 19  ? -0.559  -0.364  -30.465 1.00 26.82 ?  19  ARG D N   1 
ATOM   3422 C CA  . ARG C 1 19  ? -0.932  -0.085  -31.841 1.00 29.09 ?  19  ARG D CA  1 
ATOM   3423 C C   . ARG C 1 19  ? -1.253  1.395   -31.980 1.00 27.67 ?  19  ARG D C   1 
ATOM   3424 O O   . ARG C 1 19  ? -2.052  1.941   -31.208 1.00 28.15 ?  19  ARG D O   1 
ATOM   3425 C CB  . ARG C 1 19  ? -2.120  -0.941  -32.283 1.00 31.60 ?  19  ARG D CB  1 
ATOM   3426 C CG  . ARG C 1 19  ? -2.475  -0.803  -33.753 1.00 32.69 ?  19  ARG D CG  1 
ATOM   3427 C CD  . ARG C 1 19  ? -3.840  -1.419  -34.077 1.00 33.35 ?  19  ARG D CD  1 
ATOM   3428 N NE  . ARG C 1 19  ? -4.906  -0.864  -33.248 1.00 38.67 ?  19  ARG D NE  1 
ATOM   3429 C CZ  . ARG C 1 19  ? -5.536  -1.525  -32.283 1.00 45.98 ?  19  ARG D CZ  1 
ATOM   3430 N NH1 . ARG C 1 19  ? -5.258  -2.795  -32.014 1.00 48.14 ?  19  ARG D NH1 1 
ATOM   3431 N NH2 . ARG C 1 19  ? -6.468  -0.899  -31.569 1.00 47.58 ?  19  ARG D NH2 1 
ATOM   3432 N N   . VAL C 1 20  ? -0.637  2.036   -32.966 1.00 26.20 ?  20  VAL D N   1 
ATOM   3433 C CA  . VAL C 1 20  ? -0.868  3.447   -33.259 1.00 25.26 ?  20  VAL D CA  1 
ATOM   3434 C C   . VAL C 1 20  ? -1.488  3.540   -34.643 1.00 24.30 ?  20  VAL D C   1 
ATOM   3435 O O   . VAL C 1 20  ? -1.051  2.853   -35.569 1.00 22.08 ?  20  VAL D O   1 
ATOM   3436 C CB  . VAL C 1 20  ? 0.450   4.248   -33.200 1.00 27.00 ?  20  VAL D CB  1 
ATOM   3437 C CG1 . VAL C 1 20  ? 0.203   5.728   -33.503 1.00 24.64 ?  20  VAL D CG1 1 
ATOM   3438 C CG2 . VAL C 1 20  ? 1.126   4.050   -31.858 1.00 25.37 ?  20  VAL D CG2 1 
ATOM   3439 N N   . SER C 1 21  ? -2.498  4.395   -34.797 1.00 21.92 ?  21  SER D N   1 
ATOM   3440 C CA  . SER C 1 21  ? -3.151  4.535   -36.085 1.00 21.66 ?  21  SER D CA  1 
ATOM   3441 C C   . SER C 1 21  ? -2.850  5.904   -36.682 1.00 24.00 ?  21  SER D C   1 
ATOM   3442 O O   . SER C 1 21  ? -2.477  6.854   -35.988 1.00 22.54 ?  21  SER D O   1 
ATOM   3443 C CB  . SER C 1 21  ? -4.668  4.328   -35.965 1.00 24.02 ?  21  SER D CB  1 
ATOM   3444 O OG  . SER C 1 21  ? -5.258  5.432   -35.285 1.00 25.50 ?  21  SER D OG  1 
ATOM   3445 N N   . CYS C 1 22  ? -3.032  5.985   -37.994 1.00 23.63 ?  22  CYS D N   1 
ATOM   3446 C CA  . CYS C 1 22  ? -2.711  7.168   -38.779 1.00 20.63 ?  22  CYS D CA  1 
ATOM   3447 C C   . CYS C 1 22  ? -3.774  7.265   -39.861 1.00 21.49 ?  22  CYS D C   1 
ATOM   3448 O O   . CYS C 1 22  ? -3.750  6.475   -40.811 1.00 21.59 ?  22  CYS D O   1 
ATOM   3449 C CB  . CYS C 1 22  ? -1.311  7.029   -39.389 1.00 21.03 ?  22  CYS D CB  1 
ATOM   3450 S SG  . CYS C 1 22  ? -0.833  8.374   -40.487 1.00 27.93 ?  22  CYS D SG  1 
ATOM   3451 N N   . LYS C 1 23  ? -4.717  8.210   -39.705 1.00 23.80 ?  23  LYS D N   1 
ATOM   3452 C CA  . LYS C 1 23  ? -5.867  8.340   -40.602 1.00 22.07 ?  23  LYS D CA  1 
ATOM   3453 C C   . LYS C 1 23  ? -5.623  9.424   -41.643 1.00 23.00 ?  23  LYS D C   1 
ATOM   3454 O O   . LYS C 1 23  ? -5.456  10.602  -41.298 1.00 24.11 ?  23  LYS D O   1 
ATOM   3455 C CB  . LYS C 1 23  ? -7.143  8.635   -39.811 1.00 23.73 ?  23  LYS D CB  1 
ATOM   3456 C CG  . LYS C 1 23  ? -7.585  7.461   -38.903 1.00 24.54 ?  23  LYS D CG  1 
ATOM   3457 C CD  . LYS C 1 23  ? -8.647  7.891   -37.896 1.00 23.64 ?  23  LYS D CD  1 
ATOM   3458 C CE  . LYS C 1 23  ? -8.987  6.739   -36.958 1.00 30.01 ?  23  LYS D CE  1 
ATOM   3459 N NZ  . LYS C 1 23  ? -10.094 7.062   -35.993 1.00 31.21 ?  23  LYS D NZ  1 
ATOM   3460 N N   . ALA C 1 24  ? -5.685  9.042   -42.914 1.00 22.70 ?  24  ALA D N   1 
ATOM   3461 C CA  . ALA C 1 24  ? -5.364  9.935   -44.021 1.00 22.14 ?  24  ALA D CA  1 
ATOM   3462 C C   . ALA C 1 24  ? -6.616  10.599  -44.580 1.00 23.81 ?  24  ALA D C   1 
ATOM   3463 O O   . ALA C 1 24  ? -7.698  10.000  -44.607 1.00 21.44 ?  24  ALA D O   1 
ATOM   3464 C CB  . ALA C 1 24  ? -4.655  9.157   -45.137 1.00 24.98 ?  24  ALA D CB  1 
ATOM   3465 N N   . SER C 1 25  ? -6.460  11.849  -45.029 1.00 20.06 ?  25  SER D N   1 
ATOM   3466 C CA  . SER C 1 25  ? -7.512  12.504  -45.788 1.00 22.00 ?  25  SER D CA  1 
ATOM   3467 C C   . SER C 1 25  ? -6.858  13.397  -46.829 1.00 22.92 ?  25  SER D C   1 
ATOM   3468 O O   . SER C 1 25  ? -5.724  13.850  -46.639 1.00 22.80 ?  25  SER D O   1 
ATOM   3469 C CB  . SER C 1 25  ? -8.447  13.318  -44.876 1.00 25.05 ?  25  SER D CB  1 
ATOM   3470 O OG  . SER C 1 25  ? -7.783  14.455  -44.355 1.00 25.41 ?  25  SER D OG  1 
ATOM   3471 N N   . GLY C 1 26  ? -7.573  13.625  -47.941 1.00 21.32 ?  26  GLY D N   1 
ATOM   3472 C CA  . GLY C 1 26  ? -7.176  14.649  -48.895 1.00 22.07 ?  26  GLY D CA  1 
ATOM   3473 C C   . GLY C 1 26  ? -6.310  14.192  -50.042 1.00 26.25 ?  26  GLY D C   1 
ATOM   3474 O O   . GLY C 1 26  ? -5.780  15.043  -50.774 1.00 24.83 ?  26  GLY D O   1 
ATOM   3475 N N   . TYR C 1 27  ? -6.108  12.886  -50.201 1.00 22.27 ?  27  TYR D N   1 
ATOM   3476 C CA  . TYR C 1 27  ? -5.308  12.375  -51.306 1.00 22.40 ?  27  TYR D CA  1 
ATOM   3477 C C   . TYR C 1 27  ? -5.691  10.920  -51.537 1.00 23.71 ?  27  TYR D C   1 
ATOM   3478 O O   . TYR C 1 27  ? -6.380  10.305  -50.720 1.00 24.28 ?  27  TYR D O   1 
ATOM   3479 C CB  . TYR C 1 27  ? -3.801  12.507  -51.027 1.00 21.22 ?  27  TYR D CB  1 
ATOM   3480 C CG  . TYR C 1 27  ? -3.251  11.627  -49.915 1.00 22.03 ?  27  TYR D CG  1 
ATOM   3481 C CD1 . TYR C 1 27  ? -3.350  12.010  -48.581 1.00 22.39 ?  27  TYR D CD1 1 
ATOM   3482 C CD2 . TYR C 1 27  ? -2.605  10.433  -50.206 1.00 23.11 ?  27  TYR D CD2 1 
ATOM   3483 C CE1 . TYR C 1 27  ? -2.811  11.235  -47.562 1.00 20.61 ?  27  TYR D CE1 1 
ATOM   3484 C CE2 . TYR C 1 27  ? -2.083  9.632   -49.190 1.00 22.81 ?  27  TYR D CE2 1 
ATOM   3485 C CZ  . TYR C 1 27  ? -2.192  10.037  -47.882 1.00 22.10 ?  27  TYR D CZ  1 
ATOM   3486 O OH  . TYR C 1 27  ? -1.673  9.266   -46.878 1.00 24.39 ?  27  TYR D OH  1 
ATOM   3487 N N   . THR C 1 28  ? -5.255  10.386  -52.675 1.00 23.15 ?  28  THR D N   1 
ATOM   3488 C CA  . THR C 1 28  ? -5.512  8.985   -53.018 1.00 25.18 ?  28  THR D CA  1 
ATOM   3489 C C   . THR C 1 28  ? -4.536  8.119   -52.225 1.00 25.53 ?  28  THR D C   1 
ATOM   3490 O O   . THR C 1 28  ? -3.390  7.905   -52.631 1.00 23.14 ?  28  THR D O   1 
ATOM   3491 C CB  . THR C 1 28  ? -5.389  8.752   -54.520 1.00 29.09 ?  28  THR D CB  1 
ATOM   3492 O OG1 . THR C 1 28  ? -6.292  9.637   -55.210 1.00 28.75 ?  28  THR D OG1 1 
ATOM   3493 C CG2 . THR C 1 28  ? -5.747  7.298   -54.868 1.00 25.22 ?  28  THR D CG2 1 
ATOM   3494 N N   . PHE C 1 29  ? -5.031  7.618   -51.092 1.00 26.07 ?  29  PHE D N   1 
ATOM   3495 C CA  . PHE C 1 29  ? -4.228  6.912   -50.096 1.00 25.94 ?  29  PHE D CA  1 
ATOM   3496 C C   . PHE C 1 29  ? -3.419  5.759   -50.685 1.00 25.50 ?  29  PHE D C   1 
ATOM   3497 O O   . PHE C 1 29  ? -2.260  5.543   -50.302 1.00 25.20 ?  29  PHE D O   1 
ATOM   3498 C CB  . PHE C 1 29  ? -5.184  6.403   -49.016 1.00 27.65 ?  29  PHE D CB  1 
ATOM   3499 C CG  . PHE C 1 29  ? -4.531  5.601   -47.923 1.00 28.30 ?  29  PHE D CG  1 
ATOM   3500 C CD1 . PHE C 1 29  ? -3.750  6.222   -46.964 1.00 27.60 ?  29  PHE D CD1 1 
ATOM   3501 C CD2 . PHE C 1 29  ? -4.754  4.228   -47.825 1.00 29.59 ?  29  PHE D CD2 1 
ATOM   3502 C CE1 . PHE C 1 29  ? -3.182  5.491   -45.935 1.00 28.28 ?  29  PHE D CE1 1 
ATOM   3503 C CE2 . PHE C 1 29  ? -4.182  3.495   -46.794 1.00 29.64 ?  29  PHE D CE2 1 
ATOM   3504 C CZ  . PHE C 1 29  ? -3.386  4.142   -45.852 1.00 28.18 ?  29  PHE D CZ  1 
ATOM   3505 N N   . ALA C 1 30  ? -4.007  5.012   -51.617 1.00 25.58 ?  30  ALA D N   1 
ATOM   3506 C CA  . ALA C 1 30  ? -3.378  3.793   -52.122 1.00 26.77 ?  30  ALA D CA  1 
ATOM   3507 C C   . ALA C 1 30  ? -2.242  4.046   -53.105 1.00 25.25 ?  30  ALA D C   1 
ATOM   3508 O O   . ALA C 1 30  ? -1.599  3.072   -53.519 1.00 28.47 ?  30  ALA D O   1 
ATOM   3509 C CB  . ALA C 1 30  ? -4.441  2.888   -52.776 1.00 25.98 ?  30  ALA D CB  1 
ATOM   3510 N N   . THR C 1 31  ? -1.943  5.305   -53.485 1.00 23.32 ?  31  THR D N   1 
ATOM   3511 C CA  . THR C 1 31  ? -0.809  5.540   -54.373 1.00 23.97 ?  31  THR D CA  1 
ATOM   3512 C C   . THR C 1 31  ? 0.446   6.023   -53.649 1.00 23.66 ?  31  THR D C   1 
ATOM   3513 O O   . THR C 1 31  ? 1.506   6.104   -54.288 1.00 25.14 ?  31  THR D O   1 
ATOM   3514 C CB  . THR C 1 31  ? -1.148  6.554   -55.487 1.00 25.32 ?  31  THR D CB  1 
ATOM   3515 O OG1 . THR C 1 31  ? -1.433  7.859   -54.944 1.00 27.10 ?  31  THR D OG1 1 
ATOM   3516 C CG2 . THR C 1 31  ? -2.362  6.058   -56.313 1.00 24.79 ?  31  THR D CG2 1 
ATOM   3517 N N   . TYR C 1 32  ? 0.359   6.331   -52.355 1.00 21.65 ?  32  TYR D N   1 
ATOM   3518 C CA  . TYR C 1 32  ? 1.489   6.793   -51.554 1.00 24.11 ?  32  TYR D CA  1 
ATOM   3519 C C   . TYR C 1 32  ? 1.818   5.732   -50.507 1.00 25.45 ?  32  TYR D C   1 
ATOM   3520 O O   . TYR C 1 32  ? 1.033   4.811   -50.261 1.00 27.01 ?  32  TYR D O   1 
ATOM   3521 C CB  . TYR C 1 32  ? 1.173   8.138   -50.862 1.00 21.33 ?  32  TYR D CB  1 
ATOM   3522 C CG  . TYR C 1 32  ? 1.182   9.296   -51.827 1.00 23.33 ?  32  TYR D CG  1 
ATOM   3523 C CD1 . TYR C 1 32  ? 0.078   9.571   -52.624 1.00 24.15 ?  32  TYR D CD1 1 
ATOM   3524 C CD2 . TYR C 1 32  ? 2.301   10.121  -51.934 1.00 22.40 ?  32  TYR D CD2 1 
ATOM   3525 C CE1 . TYR C 1 32  ? 0.109   10.647  -53.521 1.00 23.53 ?  32  TYR D CE1 1 
ATOM   3526 C CE2 . TYR C 1 32  ? 2.359   11.157  -52.827 1.00 20.79 ?  32  TYR D CE2 1 
ATOM   3527 C CZ  . TYR C 1 32  ? 1.248   11.431  -53.611 1.00 25.98 ?  32  TYR D CZ  1 
ATOM   3528 O OH  . TYR C 1 32  ? 1.293   12.496  -54.488 1.00 24.31 ?  32  TYR D OH  1 
ATOM   3529 N N   . GLY C 1 33  ? 2.983   5.865   -49.896 1.00 23.25 ?  33  GLY D N   1 
ATOM   3530 C CA  . GLY C 1 33  ? 3.350   5.049   -48.762 1.00 21.34 ?  33  GLY D CA  1 
ATOM   3531 C C   . GLY C 1 33  ? 3.091   5.800   -47.470 1.00 24.42 ?  33  GLY D C   1 
ATOM   3532 O O   . GLY C 1 33  ? 2.834   7.003   -47.457 1.00 25.36 ?  33  GLY D O   1 
ATOM   3533 N N   . ILE C 1 34  ? 3.151   5.068   -46.367 1.00 22.10 ?  34  ILE D N   1 
ATOM   3534 C CA  . ILE C 1 34  ? 3.159   5.676   -45.046 1.00 22.57 ?  34  ILE D CA  1 
ATOM   3535 C C   . ILE C 1 34  ? 4.454   5.269   -44.360 1.00 22.38 ?  34  ILE D C   1 
ATOM   3536 O O   . ILE C 1 34  ? 4.789   4.077   -44.301 1.00 21.89 ?  34  ILE D O   1 
ATOM   3537 C CB  . ILE C 1 34  ? 1.943   5.270   -44.199 1.00 22.53 ?  34  ILE D CB  1 
ATOM   3538 C CG1 . ILE C 1 34  ? 0.643   5.883   -44.774 1.00 22.08 ?  34  ILE D CG1 1 
ATOM   3539 C CG2 . ILE C 1 34  ? 2.151   5.714   -42.738 1.00 23.11 ?  34  ILE D CG2 1 
ATOM   3540 C CD1 . ILE C 1 34  ? 0.534   7.380   -44.628 1.00 24.86 ?  34  ILE D CD1 1 
ATOM   3541 N N   . THR C 1 35  ? 5.176   6.259   -43.858 1.00 21.57 ?  35  THR D N   1 
ATOM   3542 C CA  . THR C 1 35  ? 6.430   6.072   -43.142 1.00 20.99 ?  35  THR D CA  1 
ATOM   3543 C C   . THR C 1 35  ? 6.187   6.342   -41.668 1.00 22.11 ?  35  THR D C   1 
ATOM   3544 O O   . THR C 1 35  ? 5.382   7.209   -41.315 1.00 22.21 ?  35  THR D O   1 
ATOM   3545 C CB  . THR C 1 35  ? 7.483   7.042   -43.689 1.00 22.48 ?  35  THR D CB  1 
ATOM   3546 O OG1 . THR C 1 35  ? 7.706   6.745   -45.071 1.00 22.69 ?  35  THR D OG1 1 
ATOM   3547 C CG2 . THR C 1 35  ? 8.809   6.953   -42.922 1.00 24.20 ?  35  THR D CG2 1 
ATOM   3548 N N   . TRP C 1 36  ? 6.886   5.615   -40.802 1.00 20.96 ?  36  TRP D N   1 
ATOM   3549 C CA  . TRP C 1 36  ? 6.858   5.912   -39.379 1.00 20.23 ?  36  TRP D CA  1 
ATOM   3550 C C   . TRP C 1 36  ? 8.251   6.327   -38.936 1.00 20.29 ?  36  TRP D C   1 
ATOM   3551 O O   . TRP C 1 36  ? 9.249   5.748   -39.372 1.00 18.74 ?  36  TRP D O   1 
ATOM   3552 C CB  . TRP C 1 36  ? 6.371   4.705   -38.572 1.00 21.28 ?  36  TRP D CB  1 
ATOM   3553 C CG  . TRP C 1 36  ? 4.896   4.417   -38.839 1.00 21.39 ?  36  TRP D CG  1 
ATOM   3554 C CD1 . TRP C 1 36  ? 4.392   3.645   -39.852 1.00 23.38 ?  36  TRP D CD1 1 
ATOM   3555 C CD2 . TRP C 1 36  ? 3.766   4.908   -38.110 1.00 21.51 ?  36  TRP D CD2 1 
ATOM   3556 N NE1 . TRP C 1 36  ? 3.023   3.602   -39.777 1.00 23.57 ?  36  TRP D NE1 1 
ATOM   3557 C CE2 . TRP C 1 36  ? 2.612   4.373   -38.722 1.00 24.23 ?  36  TRP D CE2 1 
ATOM   3558 C CE3 . TRP C 1 36  ? 3.614   5.732   -36.988 1.00 22.48 ?  36  TRP D CE3 1 
ATOM   3559 C CZ2 . TRP C 1 36  ? 1.326   4.639   -38.256 1.00 24.15 ?  36  TRP D CZ2 1 
ATOM   3560 C CZ3 . TRP C 1 36  ? 2.330   5.984   -36.521 1.00 24.61 ?  36  TRP D CZ3 1 
ATOM   3561 C CH2 . TRP C 1 36  ? 1.206   5.437   -37.160 1.00 23.14 ?  36  TRP D CH2 1 
ATOM   3562 N N   . VAL C 1 37  ? 8.303   7.349   -38.092 1.00 21.17 ?  37  VAL D N   1 
ATOM   3563 C CA  . VAL C 1 37  ? 9.535   7.915   -37.556 1.00 21.82 ?  37  VAL D CA  1 
ATOM   3564 C C   . VAL C 1 37  ? 9.314   8.065   -36.064 1.00 22.73 ?  37  VAL D C   1 
ATOM   3565 O O   . VAL C 1 37  ? 8.228   8.473   -35.640 1.00 24.57 ?  37  VAL D O   1 
ATOM   3566 C CB  . VAL C 1 37  ? 9.827   9.298   -38.201 1.00 21.80 ?  37  VAL D CB  1 
ATOM   3567 C CG1 . VAL C 1 37  ? 11.068  9.938   -37.592 1.00 24.02 ?  37  VAL D CG1 1 
ATOM   3568 C CG2 . VAL C 1 37  ? 10.001  9.151   -39.721 1.00 21.83 ?  37  VAL D CG2 1 
ATOM   3569 N N   . ARG C 1 38  ? 10.326  7.763   -35.255 1.00 24.10 ?  38  ARG D N   1 
ATOM   3570 C CA  . ARG C 1 38  ? 10.155  7.994   -33.831 1.00 21.55 ?  38  ARG D CA  1 
ATOM   3571 C C   . ARG C 1 38  ? 11.245  8.908   -33.288 1.00 23.69 ?  38  ARG D C   1 
ATOM   3572 O O   . ARG C 1 38  ? 12.271  9.156   -33.933 1.00 25.07 ?  38  ARG D O   1 
ATOM   3573 C CB  . ARG C 1 38  ? 10.099  6.667   -33.074 1.00 26.22 ?  38  ARG D CB  1 
ATOM   3574 C CG  . ARG C 1 38  ? 11.451  6.058   -32.831 1.00 24.90 ?  38  ARG D CG  1 
ATOM   3575 C CD  . ARG C 1 38  ? 11.300  4.972   -31.773 1.00 33.68 ?  38  ARG D CD  1 
ATOM   3576 N NE  . ARG C 1 38  ? 12.560  4.281   -31.559 1.00 32.89 ?  38  ARG D NE  1 
ATOM   3577 C CZ  . ARG C 1 38  ? 12.692  3.171   -30.848 1.00 35.31 ?  38  ARG D CZ  1 
ATOM   3578 N NH1 . ARG C 1 38  ? 11.649  2.596   -30.264 1.00 32.06 ?  38  ARG D NH1 1 
ATOM   3579 N NH2 . ARG C 1 38  ? 13.902  2.635   -30.712 1.00 36.63 ?  38  ARG D NH2 1 
ATOM   3580 N N   . GLN C 1 39  ? 10.985  9.456   -32.107 1.00 25.23 ?  39  GLN D N   1 
ATOM   3581 C CA  . GLN C 1 39  ? 11.869  10.475  -31.544 1.00 23.49 ?  39  GLN D CA  1 
ATOM   3582 C C   . GLN C 1 39  ? 11.833  10.344  -30.029 1.00 26.20 ?  39  GLN D C   1 
ATOM   3583 O O   . GLN C 1 39  ? 10.827  10.684  -29.407 1.00 25.79 ?  39  GLN D O   1 
ATOM   3584 C CB  . GLN C 1 39  ? 11.425  11.869  -31.973 1.00 22.18 ?  39  GLN D CB  1 
ATOM   3585 C CG  . GLN C 1 39  ? 12.300  12.964  -31.395 1.00 26.34 ?  39  GLN D CG  1 
ATOM   3586 C CD  . GLN C 1 39  ? 12.033  14.282  -32.092 1.00 25.24 ?  39  GLN D CD  1 
ATOM   3587 O OE1 . GLN C 1 39  ? 10.873  14.689  -32.236 1.00 25.72 ?  39  GLN D OE1 1 
ATOM   3588 N NE2 . GLN C 1 39  ? 13.097  14.944  -32.548 1.00 25.32 ?  39  GLN D NE2 1 
ATOM   3589 N N   . ALA C 1 40  ? 12.904  9.828   -29.437 1.00 28.35 ?  40  ALA D N   1 
ATOM   3590 C CA  . ALA C 1 40  ? 12.954  9.737   -27.986 1.00 30.68 ?  40  ALA D CA  1 
ATOM   3591 C C   . ALA C 1 40  ? 13.114  11.135  -27.384 1.00 36.00 ?  40  ALA D C   1 
ATOM   3592 O O   . ALA C 1 40  ? 13.549  12.061  -28.068 1.00 32.53 ?  40  ALA D O   1 
ATOM   3593 C CB  . ALA C 1 40  ? 14.099  8.817   -27.552 1.00 31.70 ?  40  ALA D CB  1 
ATOM   3594 N N   . PRO C 1 41  ? 12.741  11.318  -26.112 1.00 35.72 ?  41  PRO D N   1 
ATOM   3595 C CA  . PRO C 1 41  ? 12.824  12.651  -25.502 1.00 37.29 ?  41  PRO D CA  1 
ATOM   3596 C C   . PRO C 1 41  ? 14.230  13.221  -25.614 1.00 35.16 ?  41  PRO D C   1 
ATOM   3597 O O   . PRO C 1 41  ? 15.204  12.584  -25.213 1.00 38.63 ?  41  PRO D O   1 
ATOM   3598 C CB  . PRO C 1 41  ? 12.441  12.390  -24.040 1.00 38.11 ?  41  PRO D CB  1 
ATOM   3599 C CG  . PRO C 1 41  ? 11.574  11.189  -24.094 1.00 37.39 ?  41  PRO D CG  1 
ATOM   3600 C CD  . PRO C 1 41  ? 12.188  10.328  -25.163 1.00 36.09 ?  41  PRO D CD  1 
ATOM   3601 N N   . GLY C 1 42  ? 14.327  14.418  -26.190 1.00 39.27 ?  42  GLY D N   1 
ATOM   3602 C CA  . GLY C 1 42  ? 15.606  15.092  -26.333 1.00 39.17 ?  42  GLY D CA  1 
ATOM   3603 C C   . GLY C 1 42  ? 16.535  14.539  -27.392 1.00 40.67 ?  42  GLY D C   1 
ATOM   3604 O O   . GLY C 1 42  ? 17.685  14.991  -27.480 1.00 40.71 ?  42  GLY D O   1 
ATOM   3605 N N   . ARG C 1 43  ? 16.081  13.579  -28.199 1.00 34.96 ?  43  ARG D N   1 
ATOM   3606 C CA  . ARG C 1 43  ? 16.913  12.935  -29.205 1.00 30.01 ?  43  ARG D CA  1 
ATOM   3607 C C   . ARG C 1 43  ? 16.380  13.243  -30.609 1.00 28.65 ?  43  ARG D C   1 
ATOM   3608 O O   . ARG C 1 43  ? 15.432  14.014  -30.797 1.00 29.00 ?  43  ARG D O   1 
ATOM   3609 C CB  . ARG C 1 43  ? 16.984  11.432  -28.935 1.00 33.16 ?  43  ARG D CB  1 
ATOM   3610 C CG  . ARG C 1 43  ? 17.614  11.092  -27.587 1.00 41.69 ?  43  ARG D CG  1 
ATOM   3611 C CD  . ARG C 1 43  ? 19.124  10.994  -27.716 1.00 50.89 ?  43  ARG D CD  1 
ATOM   3612 N NE  . ARG C 1 43  ? 19.510  9.932   -28.642 1.00 56.21 ?  43  ARG D NE  1 
ATOM   3613 C CZ  . ARG C 1 43  ? 20.531  9.105   -28.459 1.00 59.28 ?  43  ARG D CZ  1 
ATOM   3614 N NH1 . ARG C 1 43  ? 21.329  9.216   -27.409 1.00 63.32 ?  43  ARG D NH1 1 
ATOM   3615 N NH2 . ARG C 1 43  ? 20.754  8.143   -29.350 1.00 62.58 ?  43  ARG D NH2 1 
ATOM   3616 N N   . GLY C 1 44  ? 17.011  12.623  -31.611 1.00 27.28 ?  44  GLY D N   1 
ATOM   3617 C CA  . GLY C 1 44  ? 16.751  12.960  -32.992 1.00 26.19 ?  44  GLY D CA  1 
ATOM   3618 C C   . GLY C 1 44  ? 15.704  12.054  -33.621 1.00 26.18 ?  44  GLY D C   1 
ATOM   3619 O O   . GLY C 1 44  ? 15.104  11.206  -32.970 1.00 27.18 ?  44  GLY D O   1 
ATOM   3620 N N   . LEU C 1 45  ? 15.497  12.248  -34.921 1.00 24.24 ?  45  LEU D N   1 
ATOM   3621 C CA  . LEU C 1 45  ? 14.519  11.462  -35.663 1.00 24.39 ?  45  LEU D CA  1 
ATOM   3622 C C   . LEU C 1 45  ? 15.126  10.131  -36.074 1.00 27.75 ?  45  LEU D C   1 
ATOM   3623 O O   . LEU C 1 45  ? 16.216  10.078  -36.643 1.00 25.56 ?  45  LEU D O   1 
ATOM   3624 C CB  . LEU C 1 45  ? 14.055  12.205  -36.911 1.00 23.51 ?  45  LEU D CB  1 
ATOM   3625 C CG  . LEU C 1 45  ? 13.430  13.576  -36.707 1.00 24.88 ?  45  LEU D CG  1 
ATOM   3626 C CD1 . LEU C 1 45  ? 13.074  14.178  -38.072 1.00 25.00 ?  45  LEU D CD1 1 
ATOM   3627 C CD2 . LEU C 1 45  ? 12.188  13.475  -35.806 1.00 23.09 ?  45  LEU D CD2 1 
ATOM   3628 N N   . GLU C 1 46  ? 14.392  9.060   -35.830 1.00 23.23 ?  46  GLU D N   1 
ATOM   3629 C CA  . GLU C 1 46  ? 14.849  7.718   -36.149 1.00 27.50 ?  46  GLU D CA  1 
ATOM   3630 C C   . GLU C 1 46  ? 13.820  7.078   -37.072 1.00 25.41 ?  46  GLU D C   1 
ATOM   3631 O O   . GLU C 1 46  ? 12.639  6.998   -36.722 1.00 24.34 ?  46  GLU D O   1 
ATOM   3632 C CB  . GLU C 1 46  ? 15.031  6.898   -34.872 1.00 26.62 ?  46  GLU D CB  1 
ATOM   3633 C CG  . GLU C 1 46  ? 15.333  5.427   -35.101 1.00 34.45 ?  46  GLU D CG  1 
ATOM   3634 C CD  . GLU C 1 46  ? 15.602  4.688   -33.787 1.00 41.68 ?  46  GLU D CD  1 
ATOM   3635 O OE1 . GLU C 1 46  ? 14.923  4.993   -32.778 1.00 42.44 ?  46  GLU D OE1 1 
ATOM   3636 O OE2 . GLU C 1 46  ? 16.512  3.831   -33.757 1.00 50.03 ?  46  GLU D OE2 1 
ATOM   3637 N N   . TRP C 1 47  ? 14.270  6.633   -38.240 1.00 24.80 ?  47  TRP D N   1 
ATOM   3638 C CA  . TRP C 1 47  ? 13.392  5.964   -39.186 1.00 22.95 ?  47  TRP D CA  1 
ATOM   3639 C C   . TRP C 1 47  ? 12.974  4.595   -38.646 1.00 24.92 ?  47  TRP D C   1 
ATOM   3640 O O   . TRP C 1 47  ? 13.826  3.786   -38.256 1.00 24.50 ?  47  TRP D O   1 
ATOM   3641 C CB  . TRP C 1 47  ? 14.103  5.810   -40.529 1.00 21.63 ?  47  TRP D CB  1 
ATOM   3642 C CG  . TRP C 1 47  ? 13.305  5.076   -41.616 1.00 22.75 ?  47  TRP D CG  1 
ATOM   3643 C CD1 . TRP C 1 47  ? 12.132  5.479   -42.209 1.00 22.31 ?  47  TRP D CD1 1 
ATOM   3644 C CD2 . TRP C 1 47  ? 13.661  3.839   -42.239 1.00 21.83 ?  47  TRP D CD2 1 
ATOM   3645 N NE1 . TRP C 1 47  ? 11.720  4.541   -43.138 1.00 21.26 ?  47  TRP D NE1 1 
ATOM   3646 C CE2 . TRP C 1 47  ? 12.666  3.541   -43.192 1.00 21.34 ?  47  TRP D CE2 1 
ATOM   3647 C CE3 . TRP C 1 47  ? 14.743  2.962   -42.097 1.00 22.57 ?  47  TRP D CE3 1 
ATOM   3648 C CZ2 . TRP C 1 47  ? 12.715  2.382   -43.992 1.00 21.95 ?  47  TRP D CZ2 1 
ATOM   3649 C CZ3 . TRP C 1 47  ? 14.789  1.809   -42.889 1.00 20.09 ?  47  TRP D CZ3 1 
ATOM   3650 C CH2 . TRP C 1 47  ? 13.789  1.531   -43.822 1.00 22.43 ?  47  TRP D CH2 1 
ATOM   3651 N N   . VAL C 1 48  ? 11.667  4.335   -38.632 1.00 22.13 ?  48  VAL D N   1 
ATOM   3652 C CA  . VAL C 1 48  ? 11.150  3.025   -38.214 1.00 23.85 ?  48  VAL D CA  1 
ATOM   3653 C C   . VAL C 1 48  ? 10.917  2.126   -39.421 1.00 22.89 ?  48  VAL D C   1 
ATOM   3654 O O   . VAL C 1 48  ? 11.372  0.979   -39.456 1.00 23.66 ?  48  VAL D O   1 
ATOM   3655 C CB  . VAL C 1 48  ? 9.859   3.172   -37.365 1.00 22.02 ?  48  VAL D CB  1 
ATOM   3656 C CG1 . VAL C 1 48  ? 9.295   1.747   -36.991 1.00 21.97 ?  48  VAL D CG1 1 
ATOM   3657 C CG2 . VAL C 1 48  ? 10.128  3.937   -36.095 1.00 19.98 ?  48  VAL D CG2 1 
ATOM   3658 N N   . GLY C 1 49  ? 10.233  2.639   -40.438 1.00 20.54 ?  49  GLY D N   1 
ATOM   3659 C CA  . GLY C 1 49  ? 9.976   1.858   -41.636 1.00 21.96 ?  49  GLY D CA  1 
ATOM   3660 C C   . GLY C 1 49  ? 8.902   2.523   -42.481 1.00 20.91 ?  49  GLY D C   1 
ATOM   3661 O O   . GLY C 1 49  ? 8.430   3.628   -42.169 1.00 20.34 ?  49  GLY D O   1 
ATOM   3662 N N   . TRP C 1 50  ? 8.545   1.848   -43.580 1.00 19.18 ?  50  TRP D N   1 
ATOM   3663 C CA  . TRP C 1 50  ? 7.420   2.290   -44.414 1.00 19.73 ?  50  TRP D CA  1 
ATOM   3664 C C   . TRP C 1 50  ? 6.644   1.090   -44.929 1.00 22.09 ?  50  TRP D C   1 
ATOM   3665 O O   . TRP C 1 50  ? 7.141   -0.045  -44.955 1.00 22.29 ?  50  TRP D O   1 
ATOM   3666 C CB  . TRP C 1 50  ? 7.836   3.162   -45.627 1.00 22.47 ?  50  TRP D CB  1 
ATOM   3667 C CG  . TRP C 1 50  ? 8.933   2.603   -46.513 1.00 21.00 ?  50  TRP D CG  1 
ATOM   3668 C CD1 . TRP C 1 50  ? 10.246  3.053   -46.577 1.00 21.02 ?  50  TRP D CD1 1 
ATOM   3669 C CD2 . TRP C 1 50  ? 8.840   1.511   -47.462 1.00 23.88 ?  50  TRP D CD2 1 
ATOM   3670 N NE1 . TRP C 1 50  ? 10.961  2.291   -47.482 1.00 21.00 ?  50  TRP D NE1 1 
ATOM   3671 C CE2 . TRP C 1 50  ? 10.127  1.354   -48.050 1.00 23.90 ?  50  TRP D CE2 1 
ATOM   3672 C CE3 . TRP C 1 50  ? 7.805   0.662   -47.876 1.00 23.47 ?  50  TRP D CE3 1 
ATOM   3673 C CZ2 . TRP C 1 50  ? 10.395  0.381   -49.023 1.00 24.93 ?  50  TRP D CZ2 1 
ATOM   3674 C CZ3 . TRP C 1 50  ? 8.073   -0.301  -48.848 1.00 23.86 ?  50  TRP D CZ3 1 
ATOM   3675 C CH2 . TRP C 1 50  ? 9.360   -0.441  -49.401 1.00 25.54 ?  50  TRP D CH2 1 
ATOM   3676 N N   . ILE C 1 51  ? 5.395   1.357   -45.321 1.00 21.97 ?  51  ILE D N   1 
ATOM   3677 C CA  . ILE C 1 51  ? 4.553   0.365   -45.977 1.00 21.44 ?  51  ILE D CA  1 
ATOM   3678 C C   . ILE C 1 51  ? 3.943   0.993   -47.221 1.00 23.82 ?  51  ILE D C   1 
ATOM   3679 O O   . ILE C 1 51  ? 3.508   2.148   -47.186 1.00 24.39 ?  51  ILE D O   1 
ATOM   3680 C CB  . ILE C 1 51  ? 3.461   -0.163  -45.019 1.00 22.80 ?  51  ILE D CB  1 
ATOM   3681 C CG1 . ILE C 1 51  ? 2.588   -1.202  -45.734 1.00 26.96 ?  51  ILE D CG1 1 
ATOM   3682 C CG2 . ILE C 1 51  ? 2.639   0.997   -44.405 1.00 23.51 ?  51  ILE D CG2 1 
ATOM   3683 C CD1 . ILE C 1 51  ? 1.765   -2.047  -44.759 1.00 26.59 ?  51  ILE D CD1 1 
ATOM   3684 N N   . THR C 1 52  ? 3.938   0.254   -48.334 1.00 22.33 ?  52  THR D N   1 
ATOM   3685 C CA  . THR C 1 52  ? 3.255   0.717   -49.545 1.00 23.80 ?  52  THR D CA  1 
ATOM   3686 C C   . THR C 1 52  ? 2.015   -0.137  -49.776 1.00 27.46 ?  52  THR D C   1 
ATOM   3687 O O   . THR C 1 52  ? 2.128   -1.371  -49.869 1.00 26.64 ?  52  THR D O   1 
ATOM   3688 C CB  . THR C 1 52  ? 4.169   0.677   -50.776 1.00 25.85 ?  52  THR D CB  1 
ATOM   3689 O OG1 . THR C 1 52  ? 4.933   -0.543  -50.785 1.00 25.91 ?  52  THR D OG1 1 
ATOM   3690 C CG2 . THR C 1 52  ? 5.141   1.886   -50.770 1.00 24.45 ?  52  THR D CG2 1 
ATOM   3691 N N   . PRO C 1 53  ? 0.826   0.469   -49.852 1.00 26.45 ?  53  PRO D N   1 
ATOM   3692 C CA  . PRO C 1 53  ? -0.413  -0.339  -49.888 1.00 28.87 ?  53  PRO D CA  1 
ATOM   3693 C C   . PRO C 1 53  ? -0.650  -1.051  -51.202 1.00 31.03 ?  53  PRO D C   1 
ATOM   3694 O O   . PRO C 1 53  ? -1.368  -2.062  -51.216 1.00 36.04 ?  53  PRO D O   1 
ATOM   3695 C CB  . PRO C 1 53  ? -1.523  0.692   -49.604 1.00 29.13 ?  53  PRO D CB  1 
ATOM   3696 C CG  . PRO C 1 53  ? -0.940  2.021   -49.908 1.00 30.71 ?  53  PRO D CG  1 
ATOM   3697 C CD  . PRO C 1 53  ? 0.556   1.894   -49.594 1.00 27.55 ?  53  PRO D CD  1 
ATOM   3698 N N   . TYR C 1 54  ? -0.098  -0.563  -52.310 1.00 28.25 ?  54  TYR D N   1 
ATOM   3699 C CA  . TYR C 1 54  ? -0.421  -1.171  -53.594 1.00 31.57 ?  54  TYR D CA  1 
ATOM   3700 C C   . TYR C 1 54  ? 0.312   -2.485  -53.818 1.00 34.60 ?  54  TYR D C   1 
ATOM   3701 O O   . TYR C 1 54  ? -0.034  -3.218  -54.752 1.00 37.85 ?  54  TYR D O   1 
ATOM   3702 C CB  . TYR C 1 54  ? -0.116  -0.193  -54.731 1.00 29.80 ?  54  TYR D CB  1 
ATOM   3703 C CG  . TYR C 1 54  ? 1.222   0.519   -54.601 1.00 31.96 ?  54  TYR D CG  1 
ATOM   3704 C CD1 . TYR C 1 54  ? 2.409   -0.097  -55.027 1.00 28.81 ?  54  TYR D CD1 1 
ATOM   3705 C CD2 . TYR C 1 54  ? 1.309   1.773   -54.008 1.00 26.54 ?  54  TYR D CD2 1 
ATOM   3706 C CE1 . TYR C 1 54  ? 3.628   0.537   -54.906 1.00 26.63 ?  54  TYR D CE1 1 
ATOM   3707 C CE2 . TYR C 1 54  ? 2.550   2.424   -53.876 1.00 28.20 ?  54  TYR D CE2 1 
ATOM   3708 C CZ  . TYR C 1 54  ? 3.694   1.803   -54.326 1.00 28.87 ?  54  TYR D CZ  1 
ATOM   3709 O OH  . TYR C 1 54  ? 4.901   2.449   -54.178 1.00 25.28 ?  54  TYR D OH  1 
ATOM   3710 N N   . ASN C 1 55  ? 1.307   -2.805  -53.000 1.00 33.16 ?  55  ASN D N   1 
ATOM   3711 C CA  . ASN C 1 55  ? 1.945   -4.108  -53.107 1.00 34.06 ?  55  ASN D CA  1 
ATOM   3712 C C   . ASN C 1 55  ? 2.138   -4.765  -51.742 1.00 33.34 ?  55  ASN D C   1 
ATOM   3713 O O   . ASN C 1 55  ? 2.773   -5.820  -51.670 1.00 38.70 ?  55  ASN D O   1 
ATOM   3714 C CB  . ASN C 1 55  ? 3.265   -3.959  -53.863 1.00 33.80 ?  55  ASN D CB  1 
ATOM   3715 C CG  . ASN C 1 55  ? 4.190   -2.974  -53.209 1.00 32.09 ?  55  ASN D CG  1 
ATOM   3716 O OD1 . ASN C 1 55  ? 3.956   -2.553  -52.078 1.00 33.44 ?  55  ASN D OD1 1 
ATOM   3717 N ND2 . ASN C 1 55  ? 5.273   -2.627  -53.898 1.00 30.91 ?  55  ASN D ND2 1 
ATOM   3718 N N   . ASP C 1 56  ? 1.593   -4.172  -50.677 1.00 34.73 ?  56  ASP D N   1 
ATOM   3719 C CA  . ASP C 1 56  ? 1.761   -4.619  -49.290 1.00 36.55 ?  56  ASP D CA  1 
ATOM   3720 C C   . ASP C 1 56  ? 3.211   -4.954  -48.957 1.00 40.43 ?  56  ASP D C   1 
ATOM   3721 O O   . ASP C 1 56  ? 3.502   -5.882  -48.198 1.00 39.45 ?  56  ASP D O   1 
ATOM   3722 C CB  . ASP C 1 56  ? 0.833   -5.792  -48.984 1.00 44.03 ?  56  ASP D CB  1 
ATOM   3723 C CG  . ASP C 1 56  ? -0.605  -5.458  -49.278 1.00 46.77 ?  56  ASP D CG  1 
ATOM   3724 O OD1 . ASP C 1 56  ? -1.229  -4.726  -48.469 1.00 52.01 ?  56  ASP D OD1 1 
ATOM   3725 O OD2 . ASP C 1 56  ? -1.100  -5.882  -50.341 1.00 55.64 ?  56  ASP D OD2 1 
ATOM   3726 N N   . ARG C 1 57  ? 4.138   -4.187  -49.514 1.00 29.62 ?  57  ARG D N   1 
ATOM   3727 C CA  . ARG C 1 57  ? 5.526   -4.326  -49.101 1.00 28.68 ?  57  ARG D CA  1 
ATOM   3728 C C   . ARG C 1 57  ? 5.828   -3.401  -47.933 1.00 29.10 ?  57  ARG D C   1 
ATOM   3729 O O   . ARG C 1 57  ? 5.284   -2.292  -47.814 1.00 24.66 ?  57  ARG D O   1 
ATOM   3730 C CB  . ARG C 1 57  ? 6.489   -4.058  -50.259 1.00 30.36 ?  57  ARG D CB  1 
ATOM   3731 C CG  . ARG C 1 57  ? 6.094   -4.827  -51.501 1.00 38.00 ?  57  ARG D CG  1 
ATOM   3732 C CD  . ARG C 1 57  ? 6.659   -6.231  -51.519 1.00 41.15 ?  57  ARG D CD  1 
ATOM   3733 N NE  . ARG C 1 57  ? 8.055   -6.252  -51.116 1.00 41.00 ?  57  ARG D NE  1 
ATOM   3734 C CZ  . ARG C 1 57  ? 9.037   -6.673  -51.901 1.00 46.36 ?  57  ARG D CZ  1 
ATOM   3735 N NH1 . ARG C 1 57  ? 8.800   -7.100  -53.130 1.00 48.70 ?  57  ARG D NH1 1 
ATOM   3736 N NH2 . ARG C 1 57  ? 10.289  -6.649  -51.446 1.00 47.99 ?  57  ARG D NH2 1 
ATOM   3737 N N   . THR C 1 58  ? 6.689   -3.889  -47.049 1.00 26.27 ?  58  THR D N   1 
ATOM   3738 C CA  . THR C 1 58  ? 7.150   -3.122  -45.910 1.00 24.50 ?  58  THR D CA  1 
ATOM   3739 C C   . THR C 1 58  ? 8.666   -3.120  -45.904 1.00 28.60 ?  58  THR D C   1 
ATOM   3740 O O   . THR C 1 58  ? 9.320   -3.998  -46.476 1.00 29.44 ?  58  THR D O   1 
ATOM   3741 C CB  . THR C 1 58  ? 6.638   -3.693  -44.592 1.00 27.76 ?  58  THR D CB  1 
ATOM   3742 O OG1 . THR C 1 58  ? 6.977   -5.092  -44.527 1.00 30.42 ?  58  THR D OG1 1 
ATOM   3743 C CG2 . THR C 1 58  ? 5.115   -3.523  -44.493 1.00 27.62 ?  58  THR D CG2 1 
ATOM   3744 N N   . SER C 1 59  ? 9.222   -2.119  -45.247 1.00 23.08 ?  59  SER D N   1 
ATOM   3745 C CA  . SER C 1 59  ? 10.649  -2.129  -44.978 1.00 25.00 ?  59  SER D CA  1 
ATOM   3746 C C   . SER C 1 59  ? 10.817  -1.517  -43.606 1.00 24.35 ?  59  SER D C   1 
ATOM   3747 O O   . SER C 1 59  ? 10.254  -0.454  -43.343 1.00 22.66 ?  59  SER D O   1 
ATOM   3748 C CB  . SER C 1 59  ? 11.436  -1.353  -46.038 1.00 26.46 ?  59  SER D CB  1 
ATOM   3749 O OG  . SER C 1 59  ? 12.813  -1.245  -45.669 1.00 26.07 ?  59  SER D OG  1 
ATOM   3750 N N   . TYR C 1 60  ? 11.559  -2.206  -42.737 1.00 21.10 ?  60  TYR D N   1 
ATOM   3751 C CA  . TYR C 1 60  ? 11.763  -1.818  -41.346 1.00 23.91 ?  60  TYR D CA  1 
ATOM   3752 C C   . TYR C 1 60  ? 13.248  -1.668  -41.040 1.00 25.80 ?  60  TYR D C   1 
ATOM   3753 O O   . TYR C 1 60  ? 14.068  -2.452  -41.528 1.00 25.54 ?  60  TYR D O   1 
ATOM   3754 C CB  . TYR C 1 60  ? 11.213  -2.860  -40.388 1.00 27.84 ?  60  TYR D CB  1 
ATOM   3755 C CG  . TYR C 1 60  ? 9.769   -3.262  -40.607 1.00 27.23 ?  60  TYR D CG  1 
ATOM   3756 C CD1 . TYR C 1 60  ? 8.773   -2.310  -40.845 1.00 26.75 ?  60  TYR D CD1 1 
ATOM   3757 C CD2 . TYR C 1 60  ? 9.405   -4.591  -40.564 1.00 29.28 ?  60  TYR D CD2 1 
ATOM   3758 C CE1 . TYR C 1 60  ? 7.440   -2.695  -41.034 1.00 27.36 ?  60  TYR D CE1 1 
ATOM   3759 C CE2 . TYR C 1 60  ? 8.091   -4.988  -40.745 1.00 33.24 ?  60  TYR D CE2 1 
ATOM   3760 C CZ  . TYR C 1 60  ? 7.118   -4.051  -40.982 1.00 28.92 ?  60  TYR D CZ  1 
ATOM   3761 O OH  . TYR C 1 60  ? 5.818   -4.504  -41.153 1.00 28.76 ?  60  TYR D OH  1 
ATOM   3762 N N   . ALA C 1 61  ? 13.582  -0.693  -40.191 1.00 22.21 ?  61  ALA D N   1 
ATOM   3763 C CA  . ALA C 1 61  ? 14.946  -0.592  -39.684 1.00 23.61 ?  61  ALA D CA  1 
ATOM   3764 C C   . ALA C 1 61  ? 15.305  -1.861  -38.912 1.00 25.78 ?  61  ALA D C   1 
ATOM   3765 O O   . ALA C 1 61  ? 14.468  -2.448  -38.230 1.00 25.30 ?  61  ALA D O   1 
ATOM   3766 C CB  . ALA C 1 61  ? 15.106  0.629   -38.776 1.00 25.94 ?  61  ALA D CB  1 
ATOM   3767 N N   . GLN C 1 62  ? 16.584  -2.238  -38.988 1.00 26.20 ?  62  GLN D N   1 
ATOM   3768 C CA  . GLN C 1 62  ? 17.024  -3.549  -38.506 1.00 29.00 ?  62  GLN D CA  1 
ATOM   3769 C C   . GLN C 1 62  ? 16.600  -3.786  -37.064 1.00 23.90 ?  62  GLN D C   1 
ATOM   3770 O O   . GLN C 1 62  ? 16.129  -4.878  -36.718 1.00 28.41 ?  62  GLN D O   1 
ATOM   3771 C CB  . GLN C 1 62  ? 18.554  -3.641  -38.619 1.00 31.89 ?  62  GLN D CB  1 
ATOM   3772 C CG  . GLN C 1 62  ? 19.209  -4.660  -37.684 1.00 31.79 ?  62  GLN D CG  1 
ATOM   3773 C CD  . GLN C 1 62  ? 20.737  -4.758  -37.890 1.00 35.06 ?  62  GLN D CD  1 
ATOM   3774 O OE1 . GLN C 1 62  ? 21.215  -4.934  -39.004 1.00 31.71 ?  62  GLN D OE1 1 
ATOM   3775 N NE2 . GLN C 1 62  ? 21.483  -4.699  -36.803 1.00 34.54 ?  62  GLN D NE2 1 
ATOM   3776 N N   . ILE C 1 63  ? 16.777  -2.782  -36.199 1.00 27.12 ?  63  ILE D N   1 
ATOM   3777 C CA  . ILE C 1 63  ? 16.476  -2.982  -34.787 1.00 31.62 ?  63  ILE D CA  1 
ATOM   3778 C C   . ILE C 1 63  ? 15.015  -3.265  -34.520 1.00 31.97 ?  63  ILE D C   1 
ATOM   3779 O O   . ILE C 1 63  ? 14.680  -3.692  -33.414 1.00 35.58 ?  63  ILE D O   1 
ATOM   3780 C CB  . ILE C 1 63  ? 16.904  -1.772  -33.939 1.00 34.52 ?  63  ILE D CB  1 
ATOM   3781 C CG1 . ILE C 1 63  ? 16.123  -0.525  -34.378 1.00 32.90 ?  63  ILE D CG1 1 
ATOM   3782 C CG2 . ILE C 1 63  ? 18.400  -1.630  -33.946 1.00 37.64 ?  63  ILE D CG2 1 
ATOM   3783 C CD1 . ILE C 1 63  ? 16.100  0.581   -33.343 1.00 42.31 ?  63  ILE D CD1 1 
ATOM   3784 N N   . PHE C 1 64  ? 14.136  -3.054  -35.498 1.00 30.18 ?  64  PHE D N   1 
ATOM   3785 C CA  . PHE C 1 64  ? 12.719  -3.314  -35.305 1.00 31.00 ?  64  PHE D CA  1 
ATOM   3786 C C   . PHE C 1 64  ? 12.262  -4.637  -35.894 1.00 33.01 ?  64  PHE D C   1 
ATOM   3787 O O   . PHE C 1 64  ? 11.108  -5.016  -35.700 1.00 30.99 ?  64  PHE D O   1 
ATOM   3788 C CB  . PHE C 1 64  ? 11.894  -2.165  -35.896 1.00 30.82 ?  64  PHE D CB  1 
ATOM   3789 C CG  . PHE C 1 64  ? 12.101  -0.876  -35.189 1.00 28.13 ?  64  PHE D CG  1 
ATOM   3790 C CD1 . PHE C 1 64  ? 11.643  -0.706  -33.901 1.00 30.40 ?  64  PHE D CD1 1 
ATOM   3791 C CD2 . PHE C 1 64  ? 12.794  0.165   -35.803 1.00 28.37 ?  64  PHE D CD2 1 
ATOM   3792 C CE1 . PHE C 1 64  ? 11.846  0.489   -33.241 1.00 34.72 ?  64  PHE D CE1 1 
ATOM   3793 C CE2 . PHE C 1 64  ? 13.008  1.356   -35.144 1.00 30.67 ?  64  PHE D CE2 1 
ATOM   3794 C CZ  . PHE C 1 64  ? 12.531  1.515   -33.861 1.00 33.34 ?  64  PHE D CZ  1 
ATOM   3795 N N   . HIS C 1 65  ? 13.129  -5.353  -36.596 1.00 30.97 ?  65  HIS D N   1 
ATOM   3796 C CA  . HIS C 1 65  ? 12.721  -6.636  -37.163 1.00 31.87 ?  65  HIS D CA  1 
ATOM   3797 C C   . HIS C 1 65  ? 12.200  -7.580  -36.084 1.00 33.16 ?  65  HIS D C   1 
ATOM   3798 O O   . HIS C 1 65  ? 12.804  -7.735  -35.016 1.00 33.31 ?  65  HIS D O   1 
ATOM   3799 C CB  . HIS C 1 65  ? 13.895  -7.286  -37.895 1.00 33.10 ?  65  HIS D CB  1 
ATOM   3800 C CG  . HIS C 1 65  ? 14.204  -6.649  -39.208 1.00 30.89 ?  65  HIS D CG  1 
ATOM   3801 N ND1 . HIS C 1 65  ? 14.737  -7.350  -40.270 1.00 29.78 ?  65  HIS D ND1 1 
ATOM   3802 C CD2 . HIS C 1 65  ? 14.074  -5.367  -39.628 1.00 27.36 ?  65  HIS D CD2 1 
ATOM   3803 C CE1 . HIS C 1 65  ? 14.910  -6.527  -41.292 1.00 31.71 ?  65  HIS D CE1 1 
ATOM   3804 N NE2 . HIS C 1 65  ? 14.530  -5.315  -40.923 1.00 27.43 ?  65  HIS D NE2 1 
ATOM   3805 N N   . GLY C 1 66  ? 11.085  -8.247  -36.390 1.00 32.76 ?  66  GLY D N   1 
ATOM   3806 C CA  . GLY C 1 66  ? 10.455  -9.163  -35.465 1.00 34.57 ?  66  GLY D CA  1 
ATOM   3807 C C   . GLY C 1 66  ? 9.638   -8.508  -34.380 1.00 39.49 ?  66  GLY D C   1 
ATOM   3808 O O   . GLY C 1 66  ? 8.895   -9.210  -33.674 1.00 42.50 ?  66  GLY D O   1 
ATOM   3809 N N   . ARG C 1 67  ? 9.730   -7.186  -34.227 1.00 31.24 ?  67  ARG D N   1 
ATOM   3810 C CA  . ARG C 1 67  ? 9.026   -6.477  -33.173 1.00 34.85 ?  67  ARG D CA  1 
ATOM   3811 C C   . ARG C 1 67  ? 7.941   -5.543  -33.692 1.00 32.22 ?  67  ARG D C   1 
ATOM   3812 O O   . ARG C 1 67  ? 6.944   -5.342  -33.002 1.00 36.14 ?  67  ARG D O   1 
ATOM   3813 C CB  . ARG C 1 67  ? 10.010  -5.657  -32.335 1.00 36.16 ?  67  ARG D CB  1 
ATOM   3814 C CG  . ARG C 1 67  ? 11.094  -6.481  -31.691 1.00 41.70 ?  67  ARG D CG  1 
ATOM   3815 C CD  . ARG C 1 67  ? 11.900  -5.638  -30.714 1.00 45.47 ?  67  ARG D CD  1 
ATOM   3816 N NE  . ARG C 1 67  ? 11.013  -4.968  -29.775 1.00 43.26 ?  67  ARG D NE  1 
ATOM   3817 C CZ  . ARG C 1 67  ? 11.091  -3.686  -29.449 1.00 41.66 ?  67  ARG D CZ  1 
ATOM   3818 N NH1 . ARG C 1 67  ? 12.057  -2.907  -29.916 1.00 43.71 ?  67  ARG D NH1 1 
ATOM   3819 N NH2 . ARG C 1 67  ? 10.176  -3.172  -28.631 1.00 38.03 ?  67  ARG D NH2 1 
ATOM   3820 N N   . VAL C 1 68  ? 8.110   -4.970  -34.885 1.00 31.61 ?  68  VAL D N   1 
ATOM   3821 C CA  . VAL C 1 68  ? 7.151   -4.010  -35.437 1.00 29.04 ?  68  VAL D CA  1 
ATOM   3822 C C   . VAL C 1 68  ? 6.397   -4.679  -36.569 1.00 30.54 ?  68  VAL D C   1 
ATOM   3823 O O   . VAL C 1 68  ? 6.939   -5.531  -37.288 1.00 30.02 ?  68  VAL D O   1 
ATOM   3824 C CB  . VAL C 1 68  ? 7.839   -2.719  -35.934 1.00 31.25 ?  68  VAL D CB  1 
ATOM   3825 C CG1 . VAL C 1 68  ? 8.589   -2.983  -37.241 1.00 33.36 ?  68  VAL D CG1 1 
ATOM   3826 C CG2 . VAL C 1 68  ? 6.812   -1.614  -36.143 1.00 28.41 ?  68  VAL D CG2 1 
ATOM   3827 N N   . THR C 1 69  ? 5.126   -4.305  -36.722 1.00 26.12 ?  69  THR D N   1 
ATOM   3828 C CA  . THR C 1 69  ? 4.356   -4.704  -37.887 1.00 27.77 ?  69  THR D CA  1 
ATOM   3829 C C   . THR C 1 69  ? 3.631   -3.476  -38.401 1.00 25.64 ?  69  THR D C   1 
ATOM   3830 O O   . THR C 1 69  ? 2.933   -2.807  -37.631 1.00 28.03 ?  69  THR D O   1 
ATOM   3831 C CB  . THR C 1 69  ? 3.320   -5.790  -37.556 1.00 32.13 ?  69  THR D CB  1 
ATOM   3832 O OG1 . THR C 1 69  ? 3.982   -6.956  -37.079 1.00 35.92 ?  69  THR D OG1 1 
ATOM   3833 C CG2 . THR C 1 69  ? 2.565   -6.166  -38.822 1.00 31.96 ?  69  THR D CG2 1 
ATOM   3834 N N   . MET C 1 70  ? 3.755   -3.179  -39.687 1.00 22.98 ?  70  MET D N   1 
ATOM   3835 C CA  . MET C 1 70  ? 2.940   -2.101  -40.243 1.00 22.85 ?  70  MET D CA  1 
ATOM   3836 C C   . MET C 1 70  ? 1.857   -2.702  -41.113 1.00 25.27 ?  70  MET D C   1 
ATOM   3837 O O   . MET C 1 70  ? 2.081   -3.714  -41.791 1.00 26.04 ?  70  MET D O   1 
ATOM   3838 C CB  . MET C 1 70  ? 3.741   -1.099  -41.079 1.00 21.72 ?  70  MET D CB  1 
ATOM   3839 C CG  . MET C 1 70  ? 4.726   -0.355  -40.230 1.00 24.66 ?  70  MET D CG  1 
ATOM   3840 S SD  . MET C 1 70  ? 6.021   0.536   -41.141 1.00 25.08 ?  70  MET D SD  1 
ATOM   3841 C CE  . MET C 1 70  ? 6.870   1.126   -39.710 1.00 21.38 ?  70  MET D CE  1 
ATOM   3842 N N   . THR C 1 71  ? 0.684   -2.098  -41.069 1.00 25.17 ?  71  THR D N   1 
ATOM   3843 C CA  . THR C 1 71  ? -0.383  -2.523  -41.955 1.00 24.84 ?  71  THR D CA  1 
ATOM   3844 C C   . THR C 1 71  ? -1.080  -1.286  -42.490 1.00 25.36 ?  71  THR D C   1 
ATOM   3845 O O   . THR C 1 71  ? -0.946  -0.190  -41.946 1.00 23.76 ?  71  THR D O   1 
ATOM   3846 C CB  . THR C 1 71  ? -1.397  -3.418  -41.246 1.00 27.85 ?  71  THR D CB  1 
ATOM   3847 O OG1 . THR C 1 71  ? -1.869  -2.754  -40.087 1.00 27.38 ?  71  THR D OG1 1 
ATOM   3848 C CG2 . THR C 1 71  ? -0.748  -4.716  -40.815 1.00 26.48 ?  71  THR D CG2 1 
ATOM   3849 N N   . THR C 1 72  ? -1.820  -1.471  -43.580 1.00 24.79 ?  72  THR D N   1 
ATOM   3850 C CA  . THR C 1 72  ? -2.646  -0.415  -44.133 1.00 27.19 ?  72  THR D CA  1 
ATOM   3851 C C   . THR C 1 72  ? -4.003  -1.030  -44.392 1.00 28.77 ?  72  THR D C   1 
ATOM   3852 O O   . THR C 1 72  ? -4.090  -2.165  -44.860 1.00 30.57 ?  72  THR D O   1 
ATOM   3853 C CB  . THR C 1 72  ? -2.086  0.178   -45.435 1.00 31.06 ?  72  THR D CB  1 
ATOM   3854 O OG1 . THR C 1 72  ? -1.582  -0.873  -46.270 1.00 35.34 ?  72  THR D OG1 1 
ATOM   3855 C CG2 . THR C 1 72  ? -0.937  1.087   -45.126 1.00 30.62 ?  72  THR D CG2 1 
ATOM   3856 N N   . ASP C 1 73  ? -5.050  -0.299  -44.045 1.00 25.58 ?  73  ASP D N   1 
ATOM   3857 C CA  . ASP C 1 73  ? -6.420  -0.743  -44.265 1.00 24.82 ?  73  ASP D CA  1 
ATOM   3858 C C   . ASP C 1 73  ? -7.020  0.201   -45.302 1.00 27.12 ?  73  ASP D C   1 
ATOM   3859 O O   . ASP C 1 73  ? -7.381  1.343   -44.991 1.00 26.41 ?  73  ASP D O   1 
ATOM   3860 C CB  . ASP C 1 73  ? -7.183  -0.750  -42.941 1.00 25.05 ?  73  ASP D CB  1 
ATOM   3861 C CG  . ASP C 1 73  ? -8.588  -1.305  -43.070 1.00 31.78 ?  73  ASP D CG  1 
ATOM   3862 O OD1 . ASP C 1 73  ? -9.048  -1.554  -44.204 1.00 32.77 ?  73  ASP D OD1 1 
ATOM   3863 O OD2 . ASP C 1 73  ? -9.214  -1.543  -42.015 1.00 35.81 ?  73  ASP D OD2 1 
ATOM   3864 N N   . THR C 1 74  ? -7.094  -0.267  -46.549 1.00 25.86 ?  74  THR D N   1 
ATOM   3865 C CA  . THR C 1 74  ? -7.696  0.558   -47.590 1.00 30.54 ?  74  THR D CA  1 
ATOM   3866 C C   . THR C 1 74  ? -9.200  0.700   -47.418 1.00 31.34 ?  74  THR D C   1 
ATOM   3867 O O   . THR C 1 74  ? -9.796  1.588   -48.028 1.00 35.08 ?  74  THR D O   1 
ATOM   3868 C CB  . THR C 1 74  ? -7.376  -0.004  -48.974 1.00 36.10 ?  74  THR D CB  1 
ATOM   3869 O OG1 . THR C 1 74  ? -7.639  -1.418  -48.992 1.00 34.39 ?  74  THR D OG1 1 
ATOM   3870 C CG2 . THR C 1 74  ? -5.921  0.265   -49.325 1.00 33.44 ?  74  THR D CG2 1 
ATOM   3871 N N   . SER C 1 75  ? -9.835  -0.148  -46.605 1.00 30.33 ?  75  SER D N   1 
ATOM   3872 C CA  . SER C 1 75  ? -11.266 0.026   -46.397 1.00 28.01 ?  75  SER D CA  1 
ATOM   3873 C C   . SER C 1 75  ? -11.551 1.275   -45.568 1.00 31.06 ?  75  SER D C   1 
ATOM   3874 O O   . SER C 1 75  ? -12.618 1.880   -45.718 1.00 28.48 ?  75  SER D O   1 
ATOM   3875 C CB  . SER C 1 75  ? -11.861 -1.229  -45.764 1.00 30.27 ?  75  SER D CB  1 
ATOM   3876 O OG  . SER C 1 75  ? -11.606 -1.335  -44.370 1.00 31.07 ?  75  SER D OG  1 
ATOM   3877 N N   . THR C 1 76  ? -10.601 1.699   -44.720 1.00 26.28 ?  76  THR D N   1 
ATOM   3878 C CA  . THR C 1 76  ? -10.787 2.897   -43.910 1.00 27.47 ?  76  THR D CA  1 
ATOM   3879 C C   . THR C 1 76  ? -9.721  3.954   -44.167 1.00 24.93 ?  76  THR D C   1 
ATOM   3880 O O   . THR C 1 76  ? -9.744  5.014   -43.518 1.00 29.48 ?  76  THR D O   1 
ATOM   3881 C CB  . THR C 1 76  ? -10.806 2.547   -42.418 1.00 29.83 ?  76  THR D CB  1 
ATOM   3882 O OG1 . THR C 1 76  ? -9.547  1.968   -42.057 1.00 29.78 ?  76  THR D OG1 1 
ATOM   3883 C CG2 . THR C 1 76  ? -11.901 1.534   -42.113 1.00 32.48 ?  76  THR D CG2 1 
ATOM   3884 N N   . ASN C 1 77  ? -8.815  3.720   -45.113 1.00 26.92 ?  77  ASN D N   1 
ATOM   3885 C CA  . ASN C 1 77  ? -7.740  4.656   -45.440 1.00 24.70 ?  77  ASN D CA  1 
ATOM   3886 C C   . ASN C 1 77  ? -6.942  5.027   -44.190 1.00 28.39 ?  77  ASN D C   1 
ATOM   3887 O O   . ASN C 1 77  ? -6.684  6.206   -43.898 1.00 26.95 ?  77  ASN D O   1 
ATOM   3888 C CB  . ASN C 1 77  ? -8.290  5.909   -46.129 1.00 30.94 ?  77  ASN D CB  1 
ATOM   3889 C CG  . ASN C 1 77  ? -8.249  5.811   -47.648 1.00 35.76 ?  77  ASN D CG  1 
ATOM   3890 O OD1 . ASN C 1 77  ? -8.033  4.744   -48.208 1.00 30.11 ?  77  ASN D OD1 1 
ATOM   3891 N ND2 . ASN C 1 77  ? -8.435  6.949   -48.321 1.00 37.45 ?  77  ASN D ND2 1 
ATOM   3892 N N   . THR C 1 78  ? -6.524  3.994   -43.461 1.00 25.48 ?  78  THR D N   1 
ATOM   3893 C CA  . THR C 1 78  ? -5.847  4.144   -42.183 1.00 20.66 ?  78  THR D CA  1 
ATOM   3894 C C   . THR C 1 78  ? -4.619  3.250   -42.203 1.00 22.12 ?  78  THR D C   1 
ATOM   3895 O O   . THR C 1 78  ? -4.707  2.098   -42.644 1.00 23.29 ?  78  THR D O   1 
ATOM   3896 C CB  . THR C 1 78  ? -6.767  3.745   -41.029 1.00 22.86 ?  78  THR D CB  1 
ATOM   3897 O OG1 . THR C 1 78  ? -8.001  4.482   -41.109 1.00 26.38 ?  78  THR D OG1 1 
ATOM   3898 C CG2 . THR C 1 78  ? -6.122  4.009   -39.687 1.00 24.39 ?  78  THR D CG2 1 
ATOM   3899 N N   . ALA C 1 79  ? -3.485  3.782   -41.749 1.00 23.46 ?  79  ALA D N   1 
ATOM   3900 C CA  . ALA C 1 79  ? -2.285  2.978   -41.554 1.00 22.54 ?  79  ALA D CA  1 
ATOM   3901 C C   . ALA C 1 79  ? -2.071  2.725   -40.067 1.00 23.89 ?  79  ALA D C   1 
ATOM   3902 O O   . ALA C 1 79  ? -2.470  3.530   -39.222 1.00 24.49 ?  79  ALA D O   1 
ATOM   3903 C CB  . ALA C 1 79  ? -1.058  3.667   -42.161 1.00 23.06 ?  79  ALA D CB  1 
ATOM   3904 N N   . TYR C 1 80  ? -1.463  1.571   -39.751 1.00 23.15 ?  80  TYR D N   1 
ATOM   3905 C CA  . TYR C 1 80  ? -1.200  1.157   -38.377 1.00 22.41 ?  80  TYR D CA  1 
ATOM   3906 C C   . TYR C 1 80  ? 0.256   0.740   -38.191 1.00 22.79 ?  80  TYR D C   1 
ATOM   3907 O O   . TYR C 1 80  ? 0.874   0.134   -39.081 1.00 24.12 ?  80  TYR D O   1 
ATOM   3908 C CB  . TYR C 1 80  ? -2.081  -0.024  -37.948 1.00 24.66 ?  80  TYR D CB  1 
ATOM   3909 C CG  . TYR C 1 80  ? -3.551  0.279   -38.020 1.00 23.87 ?  80  TYR D CG  1 
ATOM   3910 C CD1 . TYR C 1 80  ? -4.217  0.818   -36.938 1.00 23.28 ?  80  TYR D CD1 1 
ATOM   3911 C CD2 . TYR C 1 80  ? -4.266  0.029   -39.181 1.00 26.74 ?  80  TYR D CD2 1 
ATOM   3912 C CE1 . TYR C 1 80  ? -5.600  1.094   -37.009 1.00 25.76 ?  80  TYR D CE1 1 
ATOM   3913 C CE2 . TYR C 1 80  ? -5.607  0.305   -39.267 1.00 26.48 ?  80  TYR D CE2 1 
ATOM   3914 C CZ  . TYR C 1 80  ? -6.271  0.829   -38.181 1.00 25.61 ?  80  TYR D CZ  1 
ATOM   3915 O OH  . TYR C 1 80  ? -7.619  1.083   -38.296 1.00 28.61 ?  80  TYR D OH  1 
ATOM   3916 N N   . MET C 1 81  ? 0.785   1.076   -37.014 1.00 23.45 ?  81  MET D N   1 
ATOM   3917 C CA  . MET C 1 81  ? 2.064   0.583   -36.528 1.00 24.52 ?  81  MET D CA  1 
ATOM   3918 C C   . MET C 1 81  ? 1.814   -0.158  -35.234 1.00 24.59 ?  81  MET D C   1 
ATOM   3919 O O   . MET C 1 81  ? 1.300   0.432   -34.279 1.00 26.29 ?  81  MET D O   1 
ATOM   3920 C CB  . MET C 1 81  ? 3.036   1.708   -36.234 1.00 23.54 ?  81  MET D CB  1 
ATOM   3921 C CG  . MET C 1 81  ? 4.415   1.132   -35.893 1.00 28.57 ?  81  MET D CG  1 
ATOM   3922 S SD  . MET C 1 81  ? 5.460   2.452   -35.333 1.00 40.53 ?  81  MET D SD  1 
ATOM   3923 C CE  . MET C 1 81  ? 4.817   2.512   -33.658 1.00 37.54 ?  81  MET D CE  1 
ATOM   3924 N N   . GLU C 1 82  ? 2.221   -1.413  -35.183 1.00 27.26 ?  82  GLU D N   1 
ATOM   3925 C CA  . GLU C 1 82  ? 2.176   -2.187  -33.955 1.00 25.59 ?  82  GLU D CA  1 
ATOM   3926 C C   . GLU C 1 82  ? 3.586   -2.521  -33.505 1.00 26.99 ?  82  GLU D C   1 
ATOM   3927 O O   . GLU C 1 82  ? 4.388   -3.023  -34.290 1.00 29.62 ?  82  GLU D O   1 
ATOM   3928 C CB  . GLU C 1 82  ? 1.397   -3.478  -34.154 1.00 28.83 ?  82  GLU D CB  1 
ATOM   3929 C CG  . GLU C 1 82  ? 1.289   -4.258  -32.871 1.00 35.24 ?  82  GLU D CG  1 
ATOM   3930 C CD  . GLU C 1 82  ? 0.584   -5.570  -33.092 1.00 42.28 ?  82  GLU D CD  1 
ATOM   3931 O OE1 . GLU C 1 82  ? -0.660  -5.597  -33.027 1.00 45.37 ?  82  GLU D OE1 1 
ATOM   3932 O OE2 . GLU C 1 82  ? 1.297   -6.564  -33.361 1.00 45.22 ?  82  GLU D OE2 1 
ATOM   3933 N N   . LEU C 1 83  ? 3.887   -2.233  -32.251 1.00 26.11 ?  83  LEU D N   1 
ATOM   3934 C CA  . LEU C 1 83  ? 5.202   -2.514  -31.687 1.00 31.56 ?  83  LEU D CA  1 
ATOM   3935 C C   . LEU C 1 83  ? 4.995   -3.446  -30.505 1.00 32.31 ?  83  LEU D C   1 
ATOM   3936 O O   . LEU C 1 83  ? 4.227   -3.126  -29.591 1.00 33.67 ?  83  LEU D O   1 
ATOM   3937 C CB  . LEU C 1 83  ? 5.906   -1.219  -31.264 1.00 30.50 ?  83  LEU D CB  1 
ATOM   3938 C CG  . LEU C 1 83  ? 7.381   -1.320  -30.873 1.00 34.80 ?  83  LEU D CG  1 
ATOM   3939 C CD1 . LEU C 1 83  ? 8.246   -1.978  -31.976 1.00 33.40 ?  83  LEU D CD1 1 
ATOM   3940 C CD2 . LEU C 1 83  ? 7.933   0.051   -30.434 1.00 34.30 ?  83  LEU D CD2 1 
ATOM   3941 N N   . ARG C 1 84  ? 5.660   -4.599  -30.539 1.00 33.29 ?  84  ARG D N   1 
ATOM   3942 C CA  . ARG C 1 84  ? 5.497   -5.655  -29.550 1.00 34.32 ?  84  ARG D CA  1 
ATOM   3943 C C   . ARG C 1 84  ? 6.716   -5.715  -28.644 1.00 38.74 ?  84  ARG D C   1 
ATOM   3944 O O   . ARG C 1 84  ? 7.757   -5.100  -28.916 1.00 34.61 ?  84  ARG D O   1 
ATOM   3945 C CB  . ARG C 1 84  ? 5.289   -7.002  -30.244 1.00 39.36 ?  84  ARG D CB  1 
ATOM   3946 C CG  . ARG C 1 84  ? 4.258   -6.953  -31.341 1.00 42.97 ?  84  ARG D CG  1 
ATOM   3947 C CD  . ARG C 1 84  ? 4.044   -8.326  -31.939 1.00 45.42 ?  84  ARG D CD  1 
ATOM   3948 N NE  . ARG C 1 84  ? 5.109   -8.661  -32.880 1.00 46.13 ?  84  ARG D NE  1 
ATOM   3949 C CZ  . ARG C 1 84  ? 5.165   -8.202  -34.123 1.00 44.70 ?  84  ARG D CZ  1 
ATOM   3950 N NH1 . ARG C 1 84  ? 4.253   -7.360  -34.589 1.00 45.34 ?  84  ARG D NH1 1 
ATOM   3951 N NH2 . ARG C 1 84  ? 6.160   -8.591  -34.916 1.00 41.95 ?  84  ARG D NH2 1 
ATOM   3952 N N   . SER C 1 85  ? 6.605   -6.513  -27.576 1.00 36.22 ?  85  SER D N   1 
ATOM   3953 C CA  . SER C 1 85  ? 7.738   -6.677  -26.626 1.00 37.41 ?  85  SER D CA  1 
ATOM   3954 C C   . SER C 1 85  ? 8.288   -5.296  -26.267 1.00 37.01 ?  85  SER D C   1 
ATOM   3955 O O   . SER C 1 85  ? 9.510   -5.097  -26.389 1.00 36.52 ?  85  SER D O   1 
ATOM   3956 C CB  . SER C 1 85  ? 8.802   -7.570  -27.204 1.00 38.09 ?  85  SER D CB  1 
ATOM   3957 O OG  . SER C 1 85  ? 8.245   -8.807  -27.623 1.00 44.46 ?  85  SER D OG  1 
ATOM   3958 N N   . LEU C 1 86  ? 7.411   -4.389  -25.833 1.00 34.60 ?  86  LEU D N   1 
ATOM   3959 C CA  . LEU C 1 86  ? 7.836   -2.992  -25.549 1.00 34.79 ?  86  LEU D CA  1 
ATOM   3960 C C   . LEU C 1 86  ? 8.912   -2.961  -24.463 1.00 38.13 ?  86  LEU D C   1 
ATOM   3961 O O   . LEU C 1 86  ? 8.807   -3.742  -23.501 1.00 37.93 ?  86  LEU D O   1 
ATOM   3962 C CB  . LEU C 1 86  ? 6.612   -2.179  -25.121 1.00 34.17 ?  86  LEU D CB  1 
ATOM   3963 C CG  . LEU C 1 86  ? 5.624   -1.856  -26.239 1.00 33.64 ?  86  LEU D CG  1 
ATOM   3964 C CD1 . LEU C 1 86  ? 4.484   -0.998  -25.719 1.00 31.16 ?  86  LEU D CD1 1 
ATOM   3965 C CD2 . LEU C 1 86  ? 6.329   -1.160  -27.390 1.00 32.52 ?  86  LEU D CD2 1 
ATOM   3966 N N   . ARG C 1 87  ? 9.908   -2.088  -24.626 1.00 39.80 ?  87  ARG D N   1 
ATOM   3967 C CA  . ARG C 1 87  ? 10.955  -1.912  -23.586 1.00 41.23 ?  87  ARG D CA  1 
ATOM   3968 C C   . ARG C 1 87  ? 10.997  -0.426  -23.218 1.00 43.17 ?  87  ARG D C   1 
ATOM   3969 O O   . ARG C 1 87  ? 10.553  0.390   -24.043 1.00 37.38 ?  87  ARG D O   1 
ATOM   3970 C CB  . ARG C 1 87  ? 12.304  -2.441  -24.084 1.00 30.00 ?  87  ARG D CB  1 
ATOM   3971 C CG  . ARG C 1 87  ? 12.338  -2.762  -25.571 1.00 30.00 ?  87  ARG D CG  1 
ATOM   3972 C CD  . ARG C 1 87  ? 13.615  -3.476  -25.968 1.00 30.00 ?  87  ARG D CD  1 
ATOM   3973 N NE  . ARG C 1 87  ? 14.798  -2.761  -25.515 1.00 30.00 ?  87  ARG D NE  1 
ATOM   3974 C CZ  . ARG C 1 87  ? 16.044  -3.183  -25.692 1.00 30.00 ?  87  ARG D CZ  1 
ATOM   3975 N NH1 . ARG C 1 87  ? 17.054  -2.480  -25.211 1.00 30.00 ?  87  ARG D NH1 1 
ATOM   3976 N NH2 . ARG C 1 87  ? 16.276  -4.308  -26.346 1.00 30.00 ?  87  ARG D NH2 1 
ATOM   3977 N N   . SER C 1 88  ? 11.495  -0.091  -22.027 1.00 40.29 ?  88  SER D N   1 
ATOM   3978 C CA  . SER C 1 88  ? 11.477  1.319   -21.559 1.00 39.29 ?  88  SER D CA  1 
ATOM   3979 C C   . SER C 1 88  ? 12.091  2.239   -22.619 1.00 40.59 ?  88  SER D C   1 
ATOM   3980 O O   . SER C 1 88  ? 11.642  3.395   -22.718 1.00 39.70 ?  88  SER D O   1 
ATOM   3981 C CB  . SER C 1 88  ? 12.193  1.452   -20.240 1.00 45.16 ?  88  SER D CB  1 
ATOM   3982 O OG  . SER C 1 88  ? 13.520  0.958   -20.339 1.00 48.31 ?  88  SER D OG  1 
ATOM   3983 N N   . ASP C 1 89  ? 13.071  1.745   -23.379 1.00 39.61 ?  89  ASP D N   1 
ATOM   3984 C CA  . ASP C 1 89  ? 13.776  2.597   -24.375 1.00 38.06 ?  89  ASP D CA  1 
ATOM   3985 C C   . ASP C 1 89  ? 12.877  2.860   -25.590 1.00 39.03 ?  89  ASP D C   1 
ATOM   3986 O O   . ASP C 1 89  ? 13.270  3.689   -26.430 1.00 35.46 ?  89  ASP D O   1 
ATOM   3987 C CB  . ASP C 1 89  ? 15.123  1.985   -24.770 1.00 42.82 ?  89  ASP D CB  1 
ATOM   3988 C CG  . ASP C 1 89  ? 15.022  0.573   -25.320 1.00 48.84 ?  89  ASP D CG  1 
ATOM   3989 O OD1 . ASP C 1 89  ? 13.894  0.053   -25.398 1.00 49.83 ?  89  ASP D OD1 1 
ATOM   3990 O OD2 . ASP C 1 89  ? 16.077  0.005   -25.662 1.00 54.35 ?  89  ASP D OD2 1 
ATOM   3991 N N   . ASP C 1 90  ? 11.731  2.180   -25.689 1.00 34.21 ?  90  ASP D N   1 
ATOM   3992 C CA  . ASP C 1 90  ? 10.808  2.461   -26.785 1.00 35.87 ?  90  ASP D CA  1 
ATOM   3993 C C   . ASP C 1 90  ? 9.967   3.700   -26.520 1.00 33.83 ?  90  ASP D C   1 
ATOM   3994 O O   . ASP C 1 90  ? 9.183   4.106   -27.393 1.00 31.96 ?  90  ASP D O   1 
ATOM   3995 C CB  . ASP C 1 90  ? 9.857   1.278   -27.037 1.00 33.59 ?  90  ASP D CB  1 
ATOM   3996 C CG  . ASP C 1 90  ? 10.558  0.058   -27.612 1.00 38.80 ?  90  ASP D CG  1 
ATOM   3997 O OD1 . ASP C 1 90  ? 11.396  0.230   -28.521 1.00 34.93 ?  90  ASP D OD1 1 
ATOM   3998 O OD2 . ASP C 1 90  ? 10.228  -1.080  -27.188 1.00 36.36 ?  90  ASP D OD2 1 
ATOM   3999 N N   . THR C 1 91  ? 10.074  4.270   -25.324 1.00 29.85 ?  91  THR D N   1 
ATOM   4000 C CA  . THR C 1 91  ? 9.425   5.529   -25.006 1.00 32.57 ?  91  THR D CA  1 
ATOM   4001 C C   . THR C 1 91  ? 9.852   6.596   -26.009 1.00 33.26 ?  91  THR D C   1 
ATOM   4002 O O   . THR C 1 91  ? 11.046  6.879   -26.153 1.00 33.06 ?  91  THR D O   1 
ATOM   4003 C CB  . THR C 1 91  ? 9.778   5.939   -23.576 1.00 34.76 ?  91  THR D CB  1 
ATOM   4004 O OG1 . THR C 1 91  ? 9.226   4.981   -22.653 1.00 31.56 ?  91  THR D OG1 1 
ATOM   4005 C CG2 . THR C 1 91  ? 9.229   7.312   -23.260 1.00 33.97 ?  91  THR D CG2 1 
ATOM   4006 N N   . ALA C 1 92  ? 8.876   7.164   -26.717 1.00 29.64 ?  92  ALA D N   1 
ATOM   4007 C CA  . ALA C 1 92  ? 9.152   8.099   -27.799 1.00 28.10 ?  92  ALA D CA  1 
ATOM   4008 C C   . ALA C 1 92  ? 7.849   8.665   -28.337 1.00 30.30 ?  92  ALA D C   1 
ATOM   4009 O O   . ALA C 1 92  ? 6.764   8.111   -28.121 1.00 27.70 ?  92  ALA D O   1 
ATOM   4010 C CB  . ALA C 1 92  ? 9.922   7.431   -28.938 1.00 24.55 ?  92  ALA D CB  1 
ATOM   4011 N N   . MET C 1 93  ? 7.986   9.782   -29.044 1.00 26.30 ?  93  MET D N   1 
ATOM   4012 C CA  . MET C 1 93  ? 6.967   10.256  -29.966 1.00 26.69 ?  93  MET D CA  1 
ATOM   4013 C C   . MET C 1 93  ? 7.071   9.489   -31.279 1.00 26.54 ?  93  MET D C   1 
ATOM   4014 O O   . MET C 1 93  ? 8.139   9.444   -31.894 1.00 25.89 ?  93  MET D O   1 
ATOM   4015 C CB  . MET C 1 93  ? 7.147   11.750  -30.235 1.00 27.50 ?  93  MET D CB  1 
ATOM   4016 C CG  . MET C 1 93  ? 5.974   12.363  -30.972 1.00 30.00 ?  93  MET D CG  1 
ATOM   4017 S SD  . MET C 1 93  ? 4.532   12.614  -29.920 1.00 32.77 ?  93  MET D SD  1 
ATOM   4018 C CE  . MET C 1 93  ? 5.032   13.977  -28.886 1.00 32.67 ?  93  MET D CE  1 
ATOM   4019 N N   . TYR C 1 94  ? 5.961   8.921   -31.729 1.00 24.19 ?  94  TYR D N   1 
ATOM   4020 C CA  . TYR C 1 94  ? 5.916   8.187   -32.987 1.00 23.11 ?  94  TYR D CA  1 
ATOM   4021 C C   . TYR C 1 94  ? 5.122   9.022   -33.982 1.00 23.53 ?  94  TYR D C   1 
ATOM   4022 O O   . TYR C 1 94  ? 3.972   9.393   -33.698 1.00 24.74 ?  94  TYR D O   1 
ATOM   4023 C CB  . TYR C 1 94  ? 5.286   6.806   -32.799 1.00 24.28 ?  94  TYR D CB  1 
ATOM   4024 C CG  . TYR C 1 94  ? 6.188   5.877   -32.019 1.00 25.95 ?  94  TYR D CG  1 
ATOM   4025 C CD1 . TYR C 1 94  ? 6.310   5.999   -30.634 1.00 25.21 ?  94  TYR D CD1 1 
ATOM   4026 C CD2 . TYR C 1 94  ? 6.960   4.929   -32.671 1.00 24.40 ?  94  TYR D CD2 1 
ATOM   4027 C CE1 . TYR C 1 94  ? 7.176   5.164   -29.914 1.00 29.98 ?  94  TYR D CE1 1 
ATOM   4028 C CE2 . TYR C 1 94  ? 7.829   4.085   -31.959 1.00 29.13 ?  94  TYR D CE2 1 
ATOM   4029 C CZ  . TYR C 1 94  ? 7.922   4.213   -30.582 1.00 29.11 ?  94  TYR D CZ  1 
ATOM   4030 O OH  . TYR C 1 94  ? 8.771   3.393   -29.869 1.00 30.32 ?  94  TYR D OH  1 
ATOM   4031 N N   . TYR C 1 95  ? 5.735   9.336   -35.129 1.00 21.59 ?  95  TYR D N   1 
ATOM   4032 C CA  . TYR C 1 95  ? 5.070   10.077  -36.203 1.00 23.20 ?  95  TYR D CA  1 
ATOM   4033 C C   . TYR C 1 95  ? 4.788   9.164   -37.387 1.00 20.60 ?  95  TYR D C   1 
ATOM   4034 O O   . TYR C 1 95  ? 5.631   8.344   -37.753 1.00 21.00 ?  95  TYR D O   1 
ATOM   4035 C CB  . TYR C 1 95  ? 5.920   11.236  -36.718 1.00 21.26 ?  95  TYR D CB  1 
ATOM   4036 C CG  . TYR C 1 95  ? 6.201   12.337  -35.731 1.00 21.53 ?  95  TYR D CG  1 
ATOM   4037 C CD1 . TYR C 1 95  ? 5.272   13.338  -35.514 1.00 22.39 ?  95  TYR D CD1 1 
ATOM   4038 C CD2 . TYR C 1 95  ? 7.418   12.393  -35.043 1.00 26.09 ?  95  TYR D CD2 1 
ATOM   4039 C CE1 . TYR C 1 95  ? 5.525   14.397  -34.623 1.00 20.73 ?  95  TYR D CE1 1 
ATOM   4040 C CE2 . TYR C 1 95  ? 7.681   13.442  -34.138 1.00 24.62 ?  95  TYR D CE2 1 
ATOM   4041 C CZ  . TYR C 1 95  ? 6.729   14.424  -33.937 1.00 24.87 ?  95  TYR D CZ  1 
ATOM   4042 O OH  . TYR C 1 95  ? 6.971   15.448  -33.062 1.00 26.32 ?  95  TYR D OH  1 
ATOM   4043 N N   . CYS C 1 96  ? 3.627   9.342   -38.016 1.00 19.28 ?  96  CYS D N   1 
ATOM   4044 C CA  . CYS C 1 96  ? 3.446   8.823   -39.362 1.00 19.19 ?  96  CYS D CA  1 
ATOM   4045 C C   . CYS C 1 96  ? 3.651   9.973   -40.335 1.00 21.83 ?  96  CYS D C   1 
ATOM   4046 O O   . CYS C 1 96  ? 3.496   11.143  -39.972 1.00 21.21 ?  96  CYS D O   1 
ATOM   4047 C CB  . CYS C 1 96  ? 2.067   8.170   -39.551 1.00 21.18 ?  96  CYS D CB  1 
ATOM   4048 S SG  . CYS C 1 96  ? 0.691   9.322   -39.434 1.00 26.48 ?  96  CYS D SG  1 
ATOM   4049 N N   . ALA C 1 97  ? 4.054   9.644   -41.558 1.00 19.22 ?  97  ALA D N   1 
ATOM   4050 C CA  . ALA C 1 97  ? 4.305   10.669  -42.562 1.00 19.18 ?  97  ALA D CA  1 
ATOM   4051 C C   . ALA C 1 97  ? 4.114   10.039  -43.928 1.00 23.75 ?  97  ALA D C   1 
ATOM   4052 O O   . ALA C 1 97  ? 4.178   8.821   -44.075 1.00 23.05 ?  97  ALA D O   1 
ATOM   4053 C CB  . ALA C 1 97  ? 5.723   11.269  -42.447 1.00 22.36 ?  97  ALA D CB  1 
ATOM   4054 N N   . ARG C 1 98  ? 3.891   10.866  -44.937 1.00 21.45 ?  98  ARG D N   1 
ATOM   4055 C CA  . ARG C 1 98  ? 3.588   10.354  -46.266 1.00 21.79 ?  98  ARG D CA  1 
ATOM   4056 C C   . ARG C 1 98  ? 4.834   10.357  -47.151 1.00 24.19 ?  98  ARG D C   1 
ATOM   4057 O O   . ARG C 1 98  ? 5.433   11.409  -47.372 1.00 21.73 ?  98  ARG D O   1 
ATOM   4058 C CB  . ARG C 1 98  ? 2.489   11.186  -46.910 1.00 21.27 ?  98  ARG D CB  1 
ATOM   4059 C CG  . ARG C 1 98  ? 1.977   10.581  -48.200 1.00 19.80 ?  98  ARG D CG  1 
ATOM   4060 C CD  . ARG C 1 98  ? 0.921   11.467  -48.832 1.00 20.87 ?  98  ARG D CD  1 
ATOM   4061 N NE  . ARG C 1 98  ? 1.510   12.591  -49.563 1.00 22.11 ?  98  ARG D NE  1 
ATOM   4062 C CZ  . ARG C 1 98  ? 0.863   13.275  -50.491 1.00 23.39 ?  98  ARG D CZ  1 
ATOM   4063 N NH1 . ARG C 1 98  ? -0.403  12.990  -50.797 1.00 24.06 ?  98  ARG D NH1 1 
ATOM   4064 N NH2 . ARG C 1 98  ? 1.496   14.257  -51.135 1.00 24.29 ?  98  ARG D NH2 1 
ATOM   4065 N N   . ASN C 1 99  ? 5.182   9.200   -47.706 1.00 21.53 ?  99  ASN D N   1 
ATOM   4066 C CA  . ASN C 1 99  ? 6.214   9.106   -48.738 1.00 20.37 ?  99  ASN D CA  1 
ATOM   4067 C C   . ASN C 1 99  ? 5.631   8.418   -49.969 1.00 21.86 ?  99  ASN D C   1 
ATOM   4068 O O   . ASN C 1 99  ? 4.442   8.048   -50.012 1.00 23.27 ?  99  ASN D O   1 
ATOM   4069 C CB  . ASN C 1 99  ? 7.467   8.365   -48.216 1.00 20.89 ?  99  ASN D CB  1 
ATOM   4070 C CG  . ASN C 1 99  ? 7.253   6.848   -48.048 1.00 21.69 ?  99  ASN D CG  1 
ATOM   4071 O OD1 . ASN C 1 99  ? 6.158   6.381   -47.653 1.00 22.04 ?  99  ASN D OD1 1 
ATOM   4072 N ND2 . ASN C 1 99  ? 8.320   6.066   -48.294 1.00 22.64 ?  99  ASN D ND2 1 
ATOM   4073 N N   . HIS C 1 100 ? 6.466   8.271   -50.992 1.00 20.93 ?  100 HIS D N   1 
ATOM   4074 C CA  . HIS C 1 100 ? 6.070   7.576   -52.209 1.00 21.85 ?  100 HIS D CA  1 
ATOM   4075 C C   . HIS C 1 100 ? 7.339   7.181   -52.941 1.00 25.56 ?  100 HIS D C   1 
ATOM   4076 O O   . HIS C 1 100 ? 8.434   7.663   -52.623 1.00 23.09 ?  100 HIS D O   1 
ATOM   4077 C CB  . HIS C 1 100 ? 5.159   8.449   -53.098 1.00 25.12 ?  100 HIS D CB  1 
ATOM   4078 C CG  . HIS C 1 100 ? 5.804   9.710   -53.593 1.00 21.65 ?  100 HIS D CG  1 
ATOM   4079 N ND1 . HIS C 1 100 ? 5.890   10.863  -52.830 1.00 21.20 ?  100 HIS D ND1 1 
ATOM   4080 C CD2 . HIS C 1 100 ? 6.370   10.012  -54.788 1.00 23.93 ?  100 HIS D CD2 1 
ATOM   4081 C CE1 . HIS C 1 100 ? 6.473   11.816  -53.536 1.00 22.38 ?  100 HIS D CE1 1 
ATOM   4082 N NE2 . HIS C 1 100 ? 6.793   11.320  -54.719 1.00 26.16 ?  100 HIS D NE2 1 
ATOM   4083 N N   . CYS C 1 101 ? 7.146   6.341   -53.961 1.00 26.30 ?  101 CYS D N   1 
ATOM   4084 C CA  . CYS C 1 101 ? 8.265   5.998   -54.869 1.00 24.79 ?  101 CYS D CA  1 
ATOM   4085 C C   . CYS C 1 101 ? 7.898   6.595   -56.228 1.00 28.07 ?  101 CYS D C   1 
ATOM   4086 O O   . CYS C 1 101 ? 6.802   6.286   -56.722 1.00 29.31 ?  101 CYS D O   1 
ATOM   4087 C CB  . CYS C 1 101 ? 8.451   4.493   -55.010 1.00 31.36 ?  101 CYS D CB  1 
ATOM   4088 S SG  . CYS C 1 101 ? 9.906   4.054   -55.998 1.00 42.10 ?  101 CYS D SG  1 
ATOM   4089 N N   . ASN C 1 102 ? 8.746   7.462   -56.774 1.00 27.80 ?  102 ASN D N   1 
ATOM   4090 C CA  . ASN C 1 102 ? 8.512   8.096   -58.065 1.00 29.87 ?  102 ASN D CA  1 
ATOM   4091 C C   . ASN C 1 102 ? 8.941   7.093   -59.123 1.00 31.35 ?  102 ASN D C   1 
ATOM   4092 O O   . ASN C 1 102 ? 10.131  6.779   -59.239 1.00 31.03 ?  102 ASN D O   1 
ATOM   4093 C CB  . ASN C 1 102 ? 9.282   9.411   -58.169 1.00 25.68 ?  102 ASN D CB  1 
ATOM   4094 C CG  . ASN C 1 102 ? 9.040   10.116  -59.481 1.00 31.51 ?  102 ASN D CG  1 
ATOM   4095 O OD1 . ASN C 1 102 ? 9.318   9.576   -60.547 1.00 33.34 ?  102 ASN D OD1 1 
ATOM   4096 N ND2 . ASN C 1 102 ? 8.466   11.323  -59.410 1.00 30.73 ?  102 ASN D ND2 1 
ATOM   4097 N N   . PHE C 1 103 ? 7.973   6.580   -59.884 1.00 31.04 ?  103 PHE D N   1 
ATOM   4098 C CA  . PHE C 1 103 ? 8.237   5.491   -60.815 1.00 33.08 ?  103 PHE D CA  1 
ATOM   4099 C C   . PHE C 1 103 ? 8.768   5.985   -62.150 1.00 34.72 ?  103 PHE D C   1 
ATOM   4100 O O   . PHE C 1 103 ? 9.381   5.201   -62.876 1.00 41.95 ?  103 PHE D O   1 
ATOM   4101 C CB  . PHE C 1 103 ? 6.965   4.678   -61.054 1.00 29.87 ?  103 PHE D CB  1 
ATOM   4102 C CG  . PHE C 1 103 ? 6.615   3.760   -59.926 1.00 29.09 ?  103 PHE D CG  1 
ATOM   4103 C CD1 . PHE C 1 103 ? 5.836   4.214   -58.878 1.00 29.89 ?  103 PHE D CD1 1 
ATOM   4104 C CD2 . PHE C 1 103 ? 7.046   2.442   -59.919 1.00 31.65 ?  103 PHE D CD2 1 
ATOM   4105 C CE1 . PHE C 1 103 ? 5.509   3.382   -57.835 1.00 31.30 ?  103 PHE D CE1 1 
ATOM   4106 C CE2 . PHE C 1 103 ? 6.713   1.594   -58.878 1.00 34.26 ?  103 PHE D CE2 1 
ATOM   4107 C CZ  . PHE C 1 103 ? 5.940   2.064   -57.832 1.00 34.35 ?  103 PHE D CZ  1 
ATOM   4108 N N   . TYR C 1 104 ? 8.531   7.251   -62.492 1.00 34.04 ?  104 TYR D N   1 
ATOM   4109 C CA  . TYR C 1 104 ? 9.144   7.836   -63.684 1.00 39.16 ?  104 TYR D CA  1 
ATOM   4110 C C   . TYR C 1 104 ? 10.665  7.889   -63.554 1.00 41.45 ?  104 TYR D C   1 
ATOM   4111 O O   . TYR C 1 104 ? 11.398  7.505   -64.474 1.00 40.54 ?  104 TYR D O   1 
ATOM   4112 C CB  . TYR C 1 104 ? 8.584   9.240   -63.917 1.00 41.55 ?  104 TYR D CB  1 
ATOM   4113 C CG  . TYR C 1 104 ? 7.179   9.275   -64.476 1.00 47.30 ?  104 TYR D CG  1 
ATOM   4114 C CD1 . TYR C 1 104 ? 6.859   8.589   -65.642 1.00 52.19 ?  104 TYR D CD1 1 
ATOM   4115 C CD2 . TYR C 1 104 ? 6.181   10.021  -63.862 1.00 48.11 ?  104 TYR D CD2 1 
ATOM   4116 C CE1 . TYR C 1 104 ? 5.574   8.623   -66.168 1.00 52.87 ?  104 TYR D CE1 1 
ATOM   4117 C CE2 . TYR C 1 104 ? 4.887   10.060  -64.381 1.00 47.31 ?  104 TYR D CE2 1 
ATOM   4118 C CZ  . TYR C 1 104 ? 4.593   9.361   -65.535 1.00 53.60 ?  104 TYR D CZ  1 
ATOM   4119 O OH  . TYR C 1 104 ? 3.316   9.393   -66.058 1.00 54.65 ?  104 TYR D OH  1 
ATOM   4120 N N   . HIS C 1 105 ? 11.155  8.367   -62.412 1.00 37.91 ?  105 HIS D N   1 
ATOM   4121 C CA  . HIS C 1 105 ? 12.571  8.623   -62.196 1.00 40.14 ?  105 HIS D CA  1 
ATOM   4122 C C   . HIS C 1 105 ? 13.216  7.652   -61.224 1.00 37.36 ?  105 HIS D C   1 
ATOM   4123 O O   . HIS C 1 105 ? 14.426  7.749   -60.988 1.00 41.71 ?  105 HIS D O   1 
ATOM   4124 C CB  . HIS C 1 105 ? 12.760  10.059  -61.699 1.00 39.38 ?  105 HIS D CB  1 
ATOM   4125 C CG  . HIS C 1 105 ? 12.217  11.090  -62.633 1.00 42.78 ?  105 HIS D CG  1 
ATOM   4126 N ND1 . HIS C 1 105 ? 12.651  11.209  -63.936 1.00 48.29 ?  105 HIS D ND1 1 
ATOM   4127 C CD2 . HIS C 1 105 ? 11.263  12.036  -62.464 1.00 43.85 ?  105 HIS D CD2 1 
ATOM   4128 C CE1 . HIS C 1 105 ? 12.007  12.203  -64.523 1.00 48.86 ?  105 HIS D CE1 1 
ATOM   4129 N NE2 . HIS C 1 105 ? 11.158  12.720  -63.652 1.00 51.20 ?  105 HIS D NE2 1 
ATOM   4130 N N   . ASP C 1 106 ? 12.440  6.736   -60.646 1.00 32.76 ?  106 ASP D N   1 
ATOM   4131 C CA  . ASP C 1 106 ? 12.958  5.646   -59.829 1.00 36.24 ?  106 ASP D CA  1 
ATOM   4132 C C   . ASP C 1 106 ? 13.722  6.174   -58.612 1.00 36.61 ?  106 ASP D C   1 
ATOM   4133 O O   . ASP C 1 106 ? 14.900  5.871   -58.397 1.00 35.91 ?  106 ASP D O   1 
ATOM   4134 C CB  . ASP C 1 106 ? 13.831  4.716   -60.680 1.00 39.52 ?  106 ASP D CB  1 
ATOM   4135 C CG  . ASP C 1 106 ? 13.945  3.330   -60.094 1.00 49.19 ?  106 ASP D CG  1 
ATOM   4136 O OD1 . ASP C 1 106 ? 12.915  2.775   -59.656 1.00 55.61 ?  106 ASP D OD1 1 
ATOM   4137 O OD2 . ASP C 1 106 ? 15.070  2.788   -60.075 1.00 57.64 ?  106 ASP D OD2 1 
ATOM   4138 N N   . PHE C 1 107 ? 13.031  6.979   -57.806 1.00 29.66 ?  107 PHE D N   1 
ATOM   4139 C CA  . PHE C 1 107 ? 13.591  7.399   -56.532 1.00 29.52 ?  107 PHE D CA  1 
ATOM   4140 C C   . PHE C 1 107 ? 12.510  7.393   -55.461 1.00 28.41 ?  107 PHE D C   1 
ATOM   4141 O O   . PHE C 1 107 ? 11.322  7.593   -55.742 1.00 27.47 ?  107 PHE D O   1 
ATOM   4142 C CB  . PHE C 1 107 ? 14.269  8.781   -56.621 1.00 28.64 ?  107 PHE D CB  1 
ATOM   4143 C CG  . PHE C 1 107 ? 13.322  9.927   -56.864 1.00 28.36 ?  107 PHE D CG  1 
ATOM   4144 C CD1 . PHE C 1 107 ? 12.655  10.535  -55.802 1.00 27.68 ?  107 PHE D CD1 1 
ATOM   4145 C CD2 . PHE C 1 107 ? 13.119  10.424  -58.148 1.00 31.85 ?  107 PHE D CD2 1 
ATOM   4146 C CE1 . PHE C 1 107 ? 11.781  11.602  -56.009 1.00 29.45 ?  107 PHE D CE1 1 
ATOM   4147 C CE2 . PHE C 1 107 ? 12.243  11.505  -58.366 1.00 32.84 ?  107 PHE D CE2 1 
ATOM   4148 C CZ  . PHE C 1 107 ? 11.571  12.089  -57.289 1.00 28.94 ?  107 PHE D CZ  1 
ATOM   4149 N N   . TRP C 1 108 ? 12.951  7.176   -54.227 1.00 24.11 ?  108 TRP D N   1 
ATOM   4150 C CA  . TRP C 1 108 ? 12.088  7.260   -53.061 1.00 24.89 ?  108 TRP D CA  1 
ATOM   4151 C C   . TRP C 1 108 ? 12.033  8.697   -52.577 1.00 26.73 ?  108 TRP D C   1 
ATOM   4152 O O   . TRP C 1 108 ? 13.052  9.388   -52.544 1.00 26.52 ?  108 TRP D O   1 
ATOM   4153 C CB  . TRP C 1 108 ? 12.620  6.352   -51.956 1.00 24.26 ?  108 TRP D CB  1 
ATOM   4154 C CG  . TRP C 1 108 ? 12.306  4.932   -52.231 1.00 24.26 ?  108 TRP D CG  1 
ATOM   4155 C CD1 . TRP C 1 108 ? 13.089  4.012   -52.884 1.00 26.37 ?  108 TRP D CD1 1 
ATOM   4156 C CD2 . TRP C 1 108 ? 11.083  4.277   -51.918 1.00 24.30 ?  108 TRP D CD2 1 
ATOM   4157 N NE1 . TRP C 1 108 ? 12.422  2.798   -52.966 1.00 26.48 ?  108 TRP D NE1 1 
ATOM   4158 C CE2 . TRP C 1 108 ? 11.189  2.942   -52.377 1.00 26.10 ?  108 TRP D CE2 1 
ATOM   4159 C CE3 . TRP C 1 108 ? 9.906   4.684   -51.275 1.00 26.37 ?  108 TRP D CE3 1 
ATOM   4160 C CZ2 . TRP C 1 108 ? 10.166  2.022   -52.222 1.00 27.93 ?  108 TRP D CZ2 1 
ATOM   4161 C CZ3 . TRP C 1 108 ? 8.882   3.752   -51.115 1.00 25.39 ?  108 TRP D CZ3 1 
ATOM   4162 C CH2 . TRP C 1 108 ? 9.025   2.438   -51.587 1.00 27.73 ?  108 TRP D CH2 1 
ATOM   4163 N N   . SER C 1 109 ? 10.849  9.132   -52.160 1.00 21.10 ?  109 SER D N   1 
ATOM   4164 C CA  . SER C 1 109 ? 10.610  10.545  -51.901 1.00 22.78 ?  109 SER D CA  1 
ATOM   4165 C C   . SER C 1 109 ? 10.987  10.952  -50.472 1.00 22.32 ?  109 SER D C   1 
ATOM   4166 O O   . SER C 1 109 ? 11.284  10.124  -49.607 1.00 22.40 ?  109 SER D O   1 
ATOM   4167 C CB  . SER C 1 109 ? 9.140   10.848  -52.136 1.00 22.57 ?  109 SER D CB  1 
ATOM   4168 O OG  . SER C 1 109 ? 8.413   10.409  -51.008 1.00 21.94 ?  109 SER D OG  1 
ATOM   4169 N N   . GLY C 1 110 ? 10.907  12.255  -50.213 1.00 21.87 ?  110 GLY D N   1 
ATOM   4170 C CA  . GLY C 1 110 ? 10.912  12.750  -48.856 1.00 21.00 ?  110 GLY D CA  1 
ATOM   4171 C C   . GLY C 1 110 ? 9.517   12.662  -48.266 1.00 20.33 ?  110 GLY D C   1 
ATOM   4172 O O   . GLY C 1 110 ? 8.569   12.195  -48.898 1.00 22.09 ?  110 GLY D O   1 
ATOM   4173 N N   . LEU C 1 111 ? 9.387   13.176  -47.045 1.00 20.18 ?  111 LEU D N   1 
ATOM   4174 C CA  . LEU C 1 111 ? 8.190   13.016  -46.231 1.00 19.86 ?  111 LEU D CA  1 
ATOM   4175 C C   . LEU C 1 111 ? 7.449   14.348  -46.232 1.00 21.56 ?  111 LEU D C   1 
ATOM   4176 O O   . LEU C 1 111 ? 7.830   15.264  -45.500 1.00 21.31 ?  111 LEU D O   1 
ATOM   4177 C CB  . LEU C 1 111 ? 8.566   12.574  -44.819 1.00 19.16 ?  111 LEU D CB  1 
ATOM   4178 C CG  . LEU C 1 111 ? 9.470   11.317  -44.771 1.00 25.16 ?  111 LEU D CG  1 
ATOM   4179 C CD1 . LEU C 1 111 ? 9.766   10.929  -43.335 1.00 26.50 ?  111 LEU D CD1 1 
ATOM   4180 C CD2 . LEU C 1 111 ? 8.830   10.170  -45.482 1.00 24.18 ?  111 LEU D CD2 1 
ATOM   4181 N N   . ASP C 1 112 ? 6.415   14.467  -47.077 1.00 19.19 ?  112 ASP D N   1 
ATOM   4182 C CA  . ASP C 1 112 ? 5.865   15.799  -47.295 1.00 21.57 ?  112 ASP D CA  1 
ATOM   4183 C C   . ASP C 1 112 ? 4.808   16.185  -46.268 1.00 22.44 ?  112 ASP D C   1 
ATOM   4184 O O   . ASP C 1 112 ? 4.787   17.336  -45.823 1.00 26.06 ?  112 ASP D O   1 
ATOM   4185 C CB  . ASP C 1 112 ? 5.325   15.990  -48.734 1.00 21.67 ?  112 ASP D CB  1 
ATOM   4186 C CG  . ASP C 1 112 ? 4.438   14.841  -49.244 1.00 23.55 ?  112 ASP D CG  1 
ATOM   4187 O OD1 . ASP C 1 112 ? 3.974   14.018  -48.460 1.00 20.76 ?  112 ASP D OD1 1 
ATOM   4188 O OD2 . ASP C 1 112 ? 4.185   14.792  -50.469 1.00 22.88 ?  112 ASP D OD2 1 
ATOM   4189 N N   . TYR C 1 113 ? 3.939   15.275  -45.859 1.00 23.93 ?  113 TYR D N   1 
ATOM   4190 C CA  . TYR C 1 113 ? 2.951   15.583  -44.834 1.00 21.60 ?  113 TYR D CA  1 
ATOM   4191 C C   . TYR C 1 113 ? 3.173   14.665  -43.644 1.00 20.57 ?  113 TYR D C   1 
ATOM   4192 O O   . TYR C 1 113 ? 3.471   13.485  -43.821 1.00 21.75 ?  113 TYR D O   1 
ATOM   4193 C CB  . TYR C 1 113 ? 1.525   15.409  -45.363 1.00 22.22 ?  113 TYR D CB  1 
ATOM   4194 C CG  . TYR C 1 113 ? 1.187   16.379  -46.469 1.00 23.01 ?  113 TYR D CG  1 
ATOM   4195 C CD1 . TYR C 1 113 ? 0.965   17.728  -46.195 1.00 27.12 ?  113 TYR D CD1 1 
ATOM   4196 C CD2 . TYR C 1 113 ? 1.148   15.959  -47.789 1.00 25.28 ?  113 TYR D CD2 1 
ATOM   4197 C CE1 . TYR C 1 113 ? 0.670   18.634  -47.227 1.00 26.99 ?  113 TYR D CE1 1 
ATOM   4198 C CE2 . TYR C 1 113 ? 0.846   16.858  -48.818 1.00 26.86 ?  113 TYR D CE2 1 
ATOM   4199 C CZ  . TYR C 1 113 ? 0.618   18.184  -48.537 1.00 27.71 ?  113 TYR D CZ  1 
ATOM   4200 O OH  . TYR C 1 113 ? 0.323   19.063  -49.567 1.00 29.71 ?  113 TYR D OH  1 
ATOM   4201 N N   . TRP C 1 114 ? 3.001   15.211  -42.443 1.00 20.10 ?  114 TRP D N   1 
ATOM   4202 C CA  . TRP C 1 114 ? 3.291   14.503  -41.204 1.00 21.08 ?  114 TRP D CA  1 
ATOM   4203 C C   . TRP C 1 114 ? 2.075   14.506  -40.293 1.00 22.06 ?  114 TRP D C   1 
ATOM   4204 O O   . TRP C 1 114 ? 1.363   15.518  -40.201 1.00 20.73 ?  114 TRP D O   1 
ATOM   4205 C CB  . TRP C 1 114 ? 4.436   15.161  -40.448 1.00 21.17 ?  114 TRP D CB  1 
ATOM   4206 C CG  . TRP C 1 114 ? 5.748   15.049  -41.093 1.00 21.46 ?  114 TRP D CG  1 
ATOM   4207 C CD1 . TRP C 1 114 ? 6.144   15.602  -42.281 1.00 21.58 ?  114 TRP D CD1 1 
ATOM   4208 C CD2 . TRP C 1 114 ? 6.880   14.344  -40.573 1.00 21.16 ?  114 TRP D CD2 1 
ATOM   4209 N NE1 . TRP C 1 114 ? 7.470   15.263  -42.538 1.00 22.38 ?  114 TRP D NE1 1 
ATOM   4210 C CE2 . TRP C 1 114 ? 7.933   14.493  -41.503 1.00 23.42 ?  114 TRP D CE2 1 
ATOM   4211 C CE3 . TRP C 1 114 ? 7.097   13.590  -39.416 1.00 21.90 ?  114 TRP D CE3 1 
ATOM   4212 C CZ2 . TRP C 1 114 ? 9.189   13.927  -41.303 1.00 23.79 ?  114 TRP D CZ2 1 
ATOM   4213 C CZ3 . TRP C 1 114 ? 8.340   13.024  -39.220 1.00 22.22 ?  114 TRP D CZ3 1 
ATOM   4214 C CH2 . TRP C 1 114 ? 9.373   13.191  -40.156 1.00 22.76 ?  114 TRP D CH2 1 
ATOM   4215 N N   . GLY C 1 115 ? 1.849   13.373  -39.607 1.00 19.48 ?  115 GLY D N   1 
ATOM   4216 C CA  . GLY C 1 115 ? 0.900   13.333  -38.507 1.00 19.67 ?  115 GLY D CA  1 
ATOM   4217 C C   . GLY C 1 115 ? 1.355   14.197  -37.334 1.00 26.39 ?  115 GLY D C   1 
ATOM   4218 O O   . GLY C 1 115 ? 2.470   14.724  -37.304 1.00 24.08 ?  115 GLY D O   1 
ATOM   4219 N N   . GLN C 1 116 ? 0.470   14.353  -36.340 1.00 22.27 ?  116 GLN D N   1 
ATOM   4220 C CA  . GLN C 1 116 ? 0.810   15.214  -35.204 1.00 22.03 ?  116 GLN D CA  1 
ATOM   4221 C C   . GLN C 1 116 ? 1.683   14.512  -34.163 1.00 25.53 ?  116 GLN D C   1 
ATOM   4222 O O   . GLN C 1 116 ? 2.140   15.158  -33.217 1.00 26.53 ?  116 GLN D O   1 
ATOM   4223 C CB  . GLN C 1 116 ? -0.475  15.735  -34.535 1.00 25.81 ?  116 GLN D CB  1 
ATOM   4224 C CG  . GLN C 1 116 ? -1.098  14.769  -33.511 1.00 26.97 ?  116 GLN D CG  1 
ATOM   4225 C CD  . GLN C 1 116 ? -2.093  13.776  -34.137 1.00 27.00 ?  116 GLN D CD  1 
ATOM   4226 O OE1 . GLN C 1 116 ? -2.040  13.490  -35.339 1.00 23.86 ?  116 GLN D OE1 1 
ATOM   4227 N NE2 . GLN C 1 116 ? -3.005  13.260  -33.318 1.00 25.74 ?  116 GLN D NE2 1 
ATOM   4228 N N   . GLY C 1 117 ? 1.923   13.215  -34.308 1.00 24.05 ?  117 GLY D N   1 
ATOM   4229 C CA  . GLY C 1 117 ? 2.688   12.474  -33.322 1.00 22.43 ?  117 GLY D CA  1 
ATOM   4230 C C   . GLY C 1 117 ? 1.837   11.787  -32.276 1.00 26.57 ?  117 GLY D C   1 
ATOM   4231 O O   . GLY C 1 117 ? 0.796   12.310  -31.870 1.00 26.35 ?  117 GLY D O   1 
ATOM   4232 N N   . THR C 1 118 ? 2.280   10.610  -31.832 1.00 26.22 ?  118 THR D N   1 
ATOM   4233 C CA  . THR C 1 118 ? 1.647   9.872   -30.745 1.00 26.48 ?  118 THR D CA  1 
ATOM   4234 C C   . THR C 1 118 ? 2.721   9.569   -29.712 1.00 26.66 ?  118 THR D C   1 
ATOM   4235 O O   . THR C 1 118 ? 3.711   8.904   -30.030 1.00 25.15 ?  118 THR D O   1 
ATOM   4236 C CB  . THR C 1 118 ? 1.040   8.562   -31.250 1.00 26.52 ?  118 THR D CB  1 
ATOM   4237 O OG1 . THR C 1 118 ? 0.003   8.837   -32.200 1.00 25.95 ?  118 THR D OG1 1 
ATOM   4238 C CG2 . THR C 1 118 ? 0.476   7.742   -30.079 1.00 26.71 ?  118 THR D CG2 1 
ATOM   4239 N N   . LEU C 1 119 ? 2.539   10.056  -28.491 1.00 27.32 ?  119 LEU D N   1 
ATOM   4240 C CA  . LEU C 1 119 ? 3.484   9.730   -27.433 1.00 29.25 ?  119 LEU D CA  1 
ATOM   4241 C C   . LEU C 1 119 ? 3.194   8.332   -26.892 1.00 30.89 ?  119 LEU D C   1 
ATOM   4242 O O   . LEU C 1 119 ? 2.055   8.023   -26.510 1.00 29.47 ?  119 LEU D O   1 
ATOM   4243 C CB  . LEU C 1 119 ? 3.406   10.760  -26.311 1.00 27.72 ?  119 LEU D CB  1 
ATOM   4244 C CG  . LEU C 1 119 ? 4.371   10.445  -25.171 1.00 33.57 ?  119 LEU D CG  1 
ATOM   4245 C CD1 . LEU C 1 119 ? 5.830   10.552  -25.639 1.00 35.14 ?  119 LEU D CD1 1 
ATOM   4246 C CD2 . LEU C 1 119 ? 4.107   11.374  -23.989 1.00 37.64 ?  119 LEU D CD2 1 
ATOM   4247 N N   . VAL C 1 120 ? 4.221   7.485   -26.875 1.00 30.94 ?  120 VAL D N   1 
ATOM   4248 C CA  . VAL C 1 120 ? 4.143   6.157   -26.274 1.00 30.50 ?  120 VAL D CA  1 
ATOM   4249 C C   . VAL C 1 120 ? 5.146   6.116   -25.131 1.00 34.28 ?  120 VAL D C   1 
ATOM   4250 O O   . VAL C 1 120 ? 6.354   6.262   -25.355 1.00 31.82 ?  120 VAL D O   1 
ATOM   4251 C CB  . VAL C 1 120 ? 4.436   5.032   -27.279 1.00 28.59 ?  120 VAL D CB  1 
ATOM   4252 C CG1 . VAL C 1 120 ? 4.432   3.691   -26.547 1.00 31.40 ?  120 VAL D CG1 1 
ATOM   4253 C CG2 . VAL C 1 120 ? 3.417   5.026   -28.422 1.00 29.75 ?  120 VAL D CG2 1 
ATOM   4254 N N   . SER C 1 121 ? 4.650   5.916   -23.916 1.00 33.67 ?  121 SER D N   1 
ATOM   4255 C CA  . SER C 1 121 ? 5.480   5.818   -22.720 1.00 34.66 ?  121 SER D CA  1 
ATOM   4256 C C   . SER C 1 121 ? 5.462   4.376   -22.226 1.00 35.28 ?  121 SER D C   1 
ATOM   4257 O O   . SER C 1 121 ? 4.385   3.805   -22.025 1.00 35.29 ?  121 SER D O   1 
ATOM   4258 C CB  . SER C 1 121 ? 4.962   6.771   -21.641 1.00 39.09 ?  121 SER D CB  1 
ATOM   4259 O OG  . SER C 1 121 ? 5.561   6.506   -20.388 1.00 50.77 ?  121 SER D OG  1 
ATOM   4260 N N   . VAL C 1 122 ? 6.646   3.788   -22.047 1.00 36.38 ?  122 VAL D N   1 
ATOM   4261 C CA  . VAL C 1 122 ? 6.800   2.422   -21.550 1.00 34.88 ?  122 VAL D CA  1 
ATOM   4262 C C   . VAL C 1 122 ? 7.452   2.493   -20.180 1.00 38.23 ?  122 VAL D C   1 
ATOM   4263 O O   . VAL C 1 122 ? 8.542   3.059   -20.033 1.00 35.21 ?  122 VAL D O   1 
ATOM   4264 C CB  . VAL C 1 122 ? 7.631   1.551   -22.503 1.00 35.45 ?  122 VAL D CB  1 
ATOM   4265 C CG1 . VAL C 1 122 ? 7.687   0.108   -22.000 1.00 38.10 ?  122 VAL D CG1 1 
ATOM   4266 C CG2 . VAL C 1 122 ? 7.057   1.599   -23.919 1.00 34.48 ?  122 VAL D CG2 1 
ATOM   4267 N N   . SER C 1 123 ? 6.789   1.913   -19.181 1.00 37.21 ?  123 SER D N   1 
ATOM   4268 C CA  . SER C 1 123 ? 7.254   2.012   -17.804 1.00 41.89 ?  123 SER D CA  1 
ATOM   4269 C C   . SER C 1 123 ? 6.613   0.903   -16.984 1.00 40.62 ?  123 SER D C   1 
ATOM   4270 O O   . SER C 1 123 ? 5.462   0.543   -17.223 1.00 37.88 ?  123 SER D O   1 
ATOM   4271 C CB  . SER C 1 123 ? 6.904   3.379   -17.204 1.00 42.57 ?  123 SER D CB  1 
ATOM   4272 O OG  . SER C 1 123 ? 7.264   3.462   -15.835 1.00 44.99 ?  123 SER D OG  1 
ATOM   4273 N N   . SER C 1 124 ? 7.359   0.371   -16.018 1.00 42.01 ?  124 SER D N   1 
ATOM   4274 C CA  . SER C 1 124 ? 6.772   -0.586  -15.089 1.00 43.79 ?  124 SER D CA  1 
ATOM   4275 C C   . SER C 1 124 ? 6.040   0.097   -13.942 1.00 45.90 ?  124 SER D C   1 
ATOM   4276 O O   . SER C 1 124 ? 5.379   -0.589  -13.158 1.00 44.78 ?  124 SER D O   1 
ATOM   4277 C CB  . SER C 1 124 ? 7.847   -1.535  -14.544 1.00 41.62 ?  124 SER D CB  1 
ATOM   4278 O OG  . SER C 1 124 ? 9.007   -0.825  -14.141 1.00 48.58 ?  124 SER D OG  1 
ATOM   4279 N N   . ALA C 1 125 ? 6.105   1.427   -13.855 1.00 43.01 ?  125 ALA D N   1 
ATOM   4280 C CA  . ALA C 1 125 ? 5.438   2.163   -12.791 1.00 42.72 ?  125 ALA D CA  1 
ATOM   4281 C C   . ALA C 1 125 ? 3.923   2.138   -12.955 1.00 43.06 ?  125 ALA D C   1 
ATOM   4282 O O   . ALA C 1 125 ? 3.385   1.974   -14.051 1.00 45.74 ?  125 ALA D O   1 
ATOM   4283 C CB  . ALA C 1 125 ? 5.915   3.614   -12.758 1.00 46.48 ?  125 ALA D CB  1 
ATOM   4284 N N   . SER C 1 126 ? 3.236   2.328   -11.835 1.00 44.83 ?  126 SER D N   1 
ATOM   4285 C CA  . SER C 1 126 ? 1.786   2.378   -11.781 1.00 46.60 ?  126 SER D CA  1 
ATOM   4286 C C   . SER C 1 126 ? 1.335   3.810   -11.539 1.00 44.98 ?  126 SER D C   1 
ATOM   4287 O O   . SER C 1 126 ? 2.098   4.649   -11.056 1.00 47.48 ?  126 SER D O   1 
ATOM   4288 C CB  . SER C 1 126 ? 1.241   1.467   -10.671 1.00 50.21 ?  126 SER D CB  1 
ATOM   4289 O OG  . SER C 1 126 ? 1.641   0.120   -10.873 1.00 51.01 ?  126 SER D OG  1 
ATOM   4290 N N   . THR C 1 127 ? 0.075   4.073   -11.879 1.00 43.34 ?  127 THR D N   1 
ATOM   4291 C CA  . THR C 1 127 ? -0.513  5.390   -11.684 1.00 43.59 ?  127 THR D CA  1 
ATOM   4292 C C   . THR C 1 127 ? -0.387  5.833   -10.232 1.00 48.19 ?  127 THR D C   1 
ATOM   4293 O O   . THR C 1 127 ? -0.677  5.068   -9.309  1.00 44.54 ?  127 THR D O   1 
ATOM   4294 C CB  . THR C 1 127 ? -1.980  5.360   -12.115 1.00 42.67 ?  127 THR D CB  1 
ATOM   4295 O OG1 . THR C 1 127 ? -2.056  4.881   -13.461 1.00 45.90 ?  127 THR D OG1 1 
ATOM   4296 C CG2 . THR C 1 127 ? -2.610  6.746   -12.039 1.00 43.49 ?  127 THR D CG2 1 
ATOM   4297 N N   . LYS C 1 128 ? 0.051   7.075   -10.033 1.00 44.87 ?  128 LYS D N   1 
ATOM   4298 C CA  . LYS C 1 128 ? 0.310   7.584   -8.691  1.00 43.35 ?  128 LYS D CA  1 
ATOM   4299 C C   . LYS C 1 128 ? 0.233   9.105   -8.706  1.00 44.96 ?  128 LYS D C   1 
ATOM   4300 O O   . LYS C 1 128 ? 0.900   9.750   -9.524  1.00 43.67 ?  128 LYS D O   1 
ATOM   4301 C CB  . LYS C 1 128 ? 1.683   7.125   -8.192  1.00 43.84 ?  128 LYS D CB  1 
ATOM   4302 C CG  . LYS C 1 128 ? 1.969   7.556   -6.770  1.00 45.25 ?  128 LYS D CG  1 
ATOM   4303 C CD  . LYS C 1 128 ? 3.332   7.098   -6.295  1.00 49.61 ?  128 LYS D CD  1 
ATOM   4304 C CE  . LYS C 1 128 ? 3.799   7.940   -5.111  1.00 49.55 ?  128 LYS D CE  1 
ATOM   4305 N NZ  . LYS C 1 128 ? 2.952   7.711   -3.899  1.00 56.04 ?  128 LYS D NZ  1 
ATOM   4306 N N   . GLY C 1 129 ? -0.578  9.668   -7.812  1.00 39.76 ?  129 GLY D N   1 
ATOM   4307 C CA  . GLY C 1 129 ? -0.680  11.099  -7.655  1.00 42.37 ?  129 GLY D CA  1 
ATOM   4308 C C   . GLY C 1 129 ? 0.538   11.686  -6.964  1.00 41.39 ?  129 GLY D C   1 
ATOM   4309 O O   . GLY C 1 129 ? 1.217   11.023  -6.175  1.00 39.61 ?  129 GLY D O   1 
ATOM   4310 N N   . PRO C 1 130 ? 0.835   12.950  -7.244  1.00 42.75 ?  130 PRO D N   1 
ATOM   4311 C CA  . PRO C 1 130 ? 2.048   13.563  -6.693  1.00 41.57 ?  130 PRO D CA  1 
ATOM   4312 C C   . PRO C 1 130 ? 1.891   13.949  -5.232  1.00 41.04 ?  130 PRO D C   1 
ATOM   4313 O O   . PRO C 1 130 ? 0.787   14.196  -4.736  1.00 40.65 ?  130 PRO D O   1 
ATOM   4314 C CB  . PRO C 1 130 ? 2.225   14.814  -7.559  1.00 41.84 ?  130 PRO D CB  1 
ATOM   4315 C CG  . PRO C 1 130 ? 0.814   15.212  -7.868  1.00 41.03 ?  130 PRO D CG  1 
ATOM   4316 C CD  . PRO C 1 130 ? 0.080   13.886  -8.091  1.00 40.48 ?  130 PRO D CD  1 
ATOM   4317 N N   . SER C 1 131 ? 3.025   13.994  -4.538  1.00 38.31 ?  131 SER D N   1 
ATOM   4318 C CA  . SER C 1 131 ? 3.109   14.717  -3.279  1.00 42.30 ?  131 SER D CA  1 
ATOM   4319 C C   . SER C 1 131 ? 3.635   16.111  -3.578  1.00 43.88 ?  131 SER D C   1 
ATOM   4320 O O   . SER C 1 131 ? 4.575   16.270  -4.366  1.00 41.97 ?  131 SER D O   1 
ATOM   4321 C CB  . SER C 1 131 ? 4.024   14.000  -2.287  1.00 44.00 ?  131 SER D CB  1 
ATOM   4322 O OG  . SER C 1 131 ? 3.564   12.679  -2.047  1.00 51.42 ?  131 SER D OG  1 
ATOM   4323 N N   . VAL C 1 132 ? 3.009   17.122  -2.980  1.00 39.95 ?  132 VAL D N   1 
ATOM   4324 C CA  . VAL C 1 132 ? 3.340   18.516  -3.259  1.00 42.77 ?  132 VAL D CA  1 
ATOM   4325 C C   . VAL C 1 132 ? 3.975   19.115  -2.012  1.00 43.60 ?  132 VAL D C   1 
ATOM   4326 O O   . VAL C 1 132 ? 3.354   19.141  -0.939  1.00 41.11 ?  132 VAL D O   1 
ATOM   4327 C CB  . VAL C 1 132 ? 2.103   19.316  -3.696  1.00 40.58 ?  132 VAL D CB  1 
ATOM   4328 C CG1 . VAL C 1 132 ? 2.483   20.763  -4.000  1.00 40.61 ?  132 VAL D CG1 1 
ATOM   4329 C CG2 . VAL C 1 132 ? 1.437   18.645  -4.907  1.00 41.06 ?  132 VAL D CG2 1 
ATOM   4330 N N   . PHE C 1 133 ? 5.215   19.594  -2.155  1.00 38.64 ?  133 PHE D N   1 
ATOM   4331 C CA  . PHE C 1 133 ? 5.964   20.203  -1.071  1.00 39.19 ?  133 PHE D CA  1 
ATOM   4332 C C   . PHE C 1 133 ? 6.237   21.676  -1.358  1.00 41.74 ?  133 PHE D C   1 
ATOM   4333 O O   . PHE C 1 133 ? 6.440   22.056  -2.519  1.00 39.04 ?  133 PHE D O   1 
ATOM   4334 C CB  . PHE C 1 133 ? 7.294   19.476  -0.858  1.00 40.79 ?  133 PHE D CB  1 
ATOM   4335 C CG  . PHE C 1 133 ? 7.138   18.021  -0.576  1.00 42.97 ?  133 PHE D CG  1 
ATOM   4336 C CD1 . PHE C 1 133 ? 6.433   17.594  0.536   1.00 45.20 ?  133 PHE D CD1 1 
ATOM   4337 C CD2 . PHE C 1 133 ? 7.658   17.074  -1.441  1.00 43.53 ?  133 PHE D CD2 1 
ATOM   4338 C CE1 . PHE C 1 133 ? 6.283   16.250  0.794   1.00 43.93 ?  133 PHE D CE1 1 
ATOM   4339 C CE2 . PHE C 1 133 ? 7.506   15.725  -1.188  1.00 44.14 ?  133 PHE D CE2 1 
ATOM   4340 C CZ  . PHE C 1 133 ? 6.818   15.313  -0.070  1.00 45.13 ?  133 PHE D CZ  1 
ATOM   4341 N N   . PRO C 1 134 ? 6.252   22.524  -0.331  1.00 40.49 ?  134 PRO D N   1 
ATOM   4342 C CA  . PRO C 1 134 ? 6.534   23.942  -0.554  1.00 41.31 ?  134 PRO D CA  1 
ATOM   4343 C C   . PRO C 1 134 ? 8.025   24.196  -0.723  1.00 40.71 ?  134 PRO D C   1 
ATOM   4344 O O   . PRO C 1 134 ? 8.866   23.538  -0.104  1.00 40.43 ?  134 PRO D O   1 
ATOM   4345 C CB  . PRO C 1 134 ? 5.992   24.609  0.716   1.00 42.34 ?  134 PRO D CB  1 
ATOM   4346 C CG  . PRO C 1 134 ? 6.196   23.573  1.766   1.00 44.45 ?  134 PRO D CG  1 
ATOM   4347 C CD  . PRO C 1 134 ? 5.933   22.244  1.081   1.00 44.43 ?  134 PRO D CD  1 
ATOM   4348 N N   . LEU C 1 135 ? 8.341   25.137  -1.607  1.00 38.70 ?  135 LEU D N   1 
ATOM   4349 C CA  . LEU C 1 135 ? 9.688   25.676  -1.784  1.00 39.42 ?  135 LEU D CA  1 
ATOM   4350 C C   . LEU C 1 135 ? 9.608   27.082  -1.192  1.00 41.68 ?  135 LEU D C   1 
ATOM   4351 O O   . LEU C 1 135 ? 9.200   28.035  -1.863  1.00 42.17 ?  135 LEU D O   1 
ATOM   4352 C CB  . LEU C 1 135 ? 10.103  25.674  -3.260  1.00 37.81 ?  135 LEU D CB  1 
ATOM   4353 C CG  . LEU C 1 135 ? 10.200  24.298  -3.935  1.00 38.76 ?  135 LEU D CG  1 
ATOM   4354 C CD1 . LEU C 1 135 ? 10.418  24.440  -5.428  1.00 37.85 ?  135 LEU D CD1 1 
ATOM   4355 C CD2 . LEU C 1 135 ? 11.303  23.461  -3.318  1.00 38.41 ?  135 LEU D CD2 1 
ATOM   4356 N N   . ALA C 1 136 ? 9.982   27.201  0.121   1.00 43.73 ?  136 ALA D N   1 
ATOM   4357 C CA  . ALA C 1 136 ? 9.573   28.421  0.804   1.00 46.72 ?  136 ALA D CA  1 
ATOM   4358 C C   . ALA C 1 136 ? 10.631  29.513  0.677   1.00 44.81 ?  136 ALA D C   1 
ATOM   4359 O O   . ALA C 1 136 ? 11.830  29.224  0.633   1.00 48.40 ?  136 ALA D O   1 
ATOM   4360 C CB  . ALA C 1 136 ? 9.314   28.143  2.283   1.00 46.61 ?  136 ALA D CB  1 
ATOM   4361 N N   . PRO C 1 137 ? 10.194  30.784  0.640   1.00 51.16 ?  137 PRO D N   1 
ATOM   4362 C CA  . PRO C 1 137 ? 11.102  31.935  0.662   1.00 50.80 ?  137 PRO D CA  1 
ATOM   4363 C C   . PRO C 1 137 ? 11.819  32.063  2.006   1.00 55.71 ?  137 PRO D C   1 
ATOM   4364 O O   . PRO C 1 137 ? 12.921  32.618  2.050   1.00 55.78 ?  137 PRO D O   1 
ATOM   4365 C CB  . PRO C 1 137 ? 10.171  33.136  0.433   1.00 52.60 ?  137 PRO D CB  1 
ATOM   4366 C CG  . PRO C 1 137 ? 8.824   32.556  0.098   1.00 51.00 ?  137 PRO D CG  1 
ATOM   4367 C CD  . PRO C 1 137 ? 8.784   31.202  0.706   1.00 49.91 ?  137 PRO D CD  1 
ATOM   4368 N N   . GLY C 1 145 ? 15.710  42.718  -4.396  1.00 30.00 ?  145 GLY D N   1 
ATOM   4369 C CA  . GLY C 1 145 ? 14.409  42.764  -3.705  1.00 30.00 ?  145 GLY D CA  1 
ATOM   4370 C C   . GLY C 1 145 ? 13.472  41.724  -4.279  1.00 30.00 ?  145 GLY D C   1 
ATOM   4371 O O   . GLY C 1 145 ? 12.258  41.859  -4.098  1.00 30.00 ?  145 GLY D O   1 
ATOM   4372 N N   . THR C 1 146 ? 14.033  40.734  -4.959  1.00 44.00 ?  146 THR D N   1 
ATOM   4373 C CA  . THR C 1 146 ? 13.221  39.658  -5.564  1.00 40.60 ?  146 THR D CA  1 
ATOM   4374 C C   . THR C 1 146 ? 13.294  38.409  -4.694  1.00 38.12 ?  146 THR D C   1 
ATOM   4375 O O   . THR C 1 146 ? 14.399  38.023  -4.318  1.00 41.17 ?  146 THR D O   1 
ATOM   4376 C CB  . THR C 1 146 ? 13.709  39.331  -6.976  1.00 41.85 ?  146 THR D CB  1 
ATOM   4377 O OG1 . THR C 1 146 ? 13.394  40.432  -7.825  1.00 43.29 ?  146 THR D OG1 1 
ATOM   4378 C CG2 . THR C 1 146 ? 13.087  38.072  -7.538  1.00 40.77 ?  146 THR D CG2 1 
ATOM   4379 N N   . ALA C 1 147 ? 12.147  37.820  -4.399  1.00 37.55 ?  147 ALA D N   1 
ATOM   4380 C CA  . ALA C 1 147 ? 12.149  36.531  -3.688  1.00 40.11 ?  147 ALA D CA  1 
ATOM   4381 C C   . ALA C 1 147 ? 11.610  35.444  -4.617  1.00 38.10 ?  147 ALA D C   1 
ATOM   4382 O O   . ALA C 1 147 ? 10.830  35.764  -5.508  1.00 38.90 ?  147 ALA D O   1 
ATOM   4383 C CB  . ALA C 1 147 ? 11.300  36.616  -2.463  1.00 43.37 ?  147 ALA D CB  1 
ATOM   4384 N N   . ALA C 1 148 ? 12.047  34.214  -4.417  1.00 34.41 ?  148 ALA D N   1 
ATOM   4385 C CA  . ALA C 1 148 ? 11.488  33.099  -5.164  1.00 35.17 ?  148 ALA D CA  1 
ATOM   4386 C C   . ALA C 1 148 ? 10.766  32.158  -4.210  1.00 37.00 ?  148 ALA D C   1 
ATOM   4387 O O   . ALA C 1 148 ? 11.161  31.986  -3.055  1.00 36.09 ?  148 ALA D O   1 
ATOM   4388 C CB  . ALA C 1 148 ? 12.557  32.334  -5.931  1.00 35.84 ?  148 ALA D CB  1 
ATOM   4389 N N   . LEU C 1 149 ? 9.680   31.569  -4.693  1.00 34.84 ?  149 LEU D N   1 
ATOM   4390 C CA  . LEU C 1 149 ? 9.005   30.533  -3.936  1.00 37.98 ?  149 LEU D CA  1 
ATOM   4391 C C   . LEU C 1 149 ? 8.382   29.602  -4.956  1.00 35.32 ?  149 LEU D C   1 
ATOM   4392 O O   . LEU C 1 149 ? 8.318   29.926  -6.143  1.00 35.81 ?  149 LEU D O   1 
ATOM   4393 C CB  . LEU C 1 149 ? 7.997   31.137  -2.943  1.00 39.92 ?  149 LEU D CB  1 
ATOM   4394 C CG  . LEU C 1 149 ? 6.885   32.119  -3.336  1.00 45.10 ?  149 LEU D CG  1 
ATOM   4395 C CD1 . LEU C 1 149 ? 5.863   31.463  -4.232  1.00 45.58 ?  149 LEU D CD1 1 
ATOM   4396 C CD2 . LEU C 1 149 ? 6.203   32.734  -2.127  1.00 48.70 ?  149 LEU D CD2 1 
ATOM   4397 N N   . GLY C 1 150 ? 7.957   28.431  -4.511  1.00 35.45 ?  150 GLY D N   1 
ATOM   4398 C CA  . GLY C 1 150 ? 7.378   27.510  -5.465  1.00 34.23 ?  150 GLY D CA  1 
ATOM   4399 C C   . GLY C 1 150 ? 6.823   26.275  -4.794  1.00 35.74 ?  150 GLY D C   1 
ATOM   4400 O O   . GLY C 1 150 ? 6.699   26.207  -3.571  1.00 36.60 ?  150 GLY D O   1 
ATOM   4401 N N   . CYS C 1 151 ? 6.495   25.294  -5.631  1.00 35.05 ?  151 CYS D N   1 
ATOM   4402 C CA  . CYS C 1 151 ? 6.041   23.988  -5.180  1.00 34.73 ?  151 CYS D CA  1 
ATOM   4403 C C   . CYS C 1 151 ? 6.841   22.906  -5.879  1.00 38.99 ?  151 CYS D C   1 
ATOM   4404 O O   . CYS C 1 151 ? 7.081   22.979  -7.088  1.00 36.59 ?  151 CYS D O   1 
ATOM   4405 C CB  . CYS C 1 151 ? 4.552   23.786  -5.469  1.00 37.41 ?  151 CYS D CB  1 
ATOM   4406 S SG  . CYS C 1 151 ? 3.505   24.781  -4.396  1.00 48.23 ?  151 CYS D SG  1 
ATOM   4407 N N   . LEU C 1 152 ? 7.257   21.906  -5.109  1.00 34.16 ?  152 LEU D N   1 
ATOM   4408 C CA  . LEU C 1 152 ? 7.860   20.704  -5.660  1.00 37.54 ?  152 LEU D CA  1 
ATOM   4409 C C   . LEU C 1 152 ? 6.765   19.654  -5.821  1.00 39.01 ?  152 LEU D C   1 
ATOM   4410 O O   . LEU C 1 152 ? 6.089   19.306  -4.847  1.00 38.07 ?  152 LEU D O   1 
ATOM   4411 C CB  . LEU C 1 152 ? 8.984   20.202  -4.757  1.00 35.96 ?  152 LEU D CB  1 
ATOM   4412 C CG  . LEU C 1 152 ? 9.662   18.892  -5.148  1.00 38.15 ?  152 LEU D CG  1 
ATOM   4413 C CD1 . LEU C 1 152 ? 10.510  19.076  -6.388  1.00 40.22 ?  152 LEU D CD1 1 
ATOM   4414 C CD2 . LEU C 1 152 ? 10.511  18.402  -3.990  1.00 40.55 ?  152 LEU D CD2 1 
ATOM   4415 N N   . VAL C 1 153 ? 6.580   19.174  -7.044  1.00 34.82 ?  153 VAL D N   1 
ATOM   4416 C CA  . VAL C 1 153 ? 5.505   18.245  -7.393  1.00 35.81 ?  153 VAL D CA  1 
ATOM   4417 C C   . VAL C 1 153 ? 6.179   16.913  -7.686  1.00 39.10 ?  153 VAL D C   1 
ATOM   4418 O O   . VAL C 1 153 ? 6.658   16.682  -8.803  1.00 38.35 ?  153 VAL D O   1 
ATOM   4419 C CB  . VAL C 1 153 ? 4.690   18.751  -8.591  1.00 38.71 ?  153 VAL D CB  1 
ATOM   4420 C CG1 . VAL C 1 153 ? 3.587   17.758  -8.981  1.00 37.29 ?  153 VAL D CG1 1 
ATOM   4421 C CG2 . VAL C 1 153 ? 4.094   20.125  -8.287  1.00 37.88 ?  153 VAL D CG2 1 
ATOM   4422 N N   . LYS C 1 154 ? 6.252   16.024  -6.700  1.00 40.61 ?  154 LYS D N   1 
ATOM   4423 C CA  . LYS C 1 154 ? 7.224   14.944  -6.773  1.00 39.80 ?  154 LYS D CA  1 
ATOM   4424 C C   . LYS C 1 154 ? 6.547   13.572  -6.724  1.00 43.51 ?  154 LYS D C   1 
ATOM   4425 O O   . LYS C 1 154 ? 5.504   13.392  -6.081  1.00 42.39 ?  154 LYS D O   1 
ATOM   4426 C CB  . LYS C 1 154 ? 8.268   15.114  -5.653  1.00 45.50 ?  154 LYS D CB  1 
ATOM   4427 C CG  . LYS C 1 154 ? 9.030   13.880  -5.212  1.00 49.61 ?  154 LYS D CG  1 
ATOM   4428 C CD  . LYS C 1 154 ? 10.519  14.262  -5.122  1.00 48.21 ?  154 LYS D CD  1 
ATOM   4429 C CE  . LYS C 1 154 ? 11.319  13.403  -4.151  1.00 53.54 ?  154 LYS D CE  1 
ATOM   4430 N NZ  . LYS C 1 154 ? 11.177  11.939  -4.414  1.00 55.17 ?  154 LYS D NZ  1 
ATOM   4431 N N   . ASP C 1 155 ? 7.127   12.628  -7.469  1.00 42.52 ?  155 ASP D N   1 
ATOM   4432 C CA  . ASP C 1 155 ? 6.766   11.205  -7.463  1.00 43.27 ?  155 ASP D CA  1 
ATOM   4433 C C   . ASP C 1 155 ? 5.329   10.973  -7.934  1.00 44.50 ?  155 ASP D C   1 
ATOM   4434 O O   . ASP C 1 155 ? 4.483   10.451  -7.207  1.00 46.57 ?  155 ASP D O   1 
ATOM   4435 C CB  . ASP C 1 155 ? 7.010   10.584  -6.082  1.00 42.57 ?  155 ASP D CB  1 
ATOM   4436 C CG  . ASP C 1 155 ? 8.488   10.538  -5.716  1.00 45.79 ?  155 ASP D CG  1 
ATOM   4437 O OD1 . ASP C 1 155 ? 9.330   10.540  -6.637  1.00 45.95 ?  155 ASP D OD1 1 
ATOM   4438 O OD2 . ASP C 1 155 ? 8.816   10.488  -4.513  1.00 50.07 ?  155 ASP D OD2 1 
ATOM   4439 N N   . TYR C 1 156 ? 5.070   11.343  -9.189  1.00 40.55 ?  156 TYR D N   1 
ATOM   4440 C CA  . TYR C 1 156 ? 3.785   11.051  -9.809  1.00 41.10 ?  156 TYR D CA  1 
ATOM   4441 C C   . TYR C 1 156 ? 3.988   10.279  -11.107 1.00 40.46 ?  156 TYR D C   1 
ATOM   4442 O O   . TYR C 1 156 ? 5.094   10.219  -11.652 1.00 38.27 ?  156 TYR D O   1 
ATOM   4443 C CB  . TYR C 1 156 ? 2.973   12.322  -10.073 1.00 40.25 ?  156 TYR D CB  1 
ATOM   4444 C CG  . TYR C 1 156 ? 3.547   13.226  -11.145 1.00 41.40 ?  156 TYR D CG  1 
ATOM   4445 C CD1 . TYR C 1 156 ? 4.480   14.213  -10.830 1.00 40.58 ?  156 TYR D CD1 1 
ATOM   4446 C CD2 . TYR C 1 156 ? 3.163   13.087  -12.473 1.00 40.68 ?  156 TYR D CD2 1 
ATOM   4447 C CE1 . TYR C 1 156 ? 5.004   15.044  -11.819 1.00 41.10 ?  156 TYR D CE1 1 
ATOM   4448 C CE2 . TYR C 1 156 ? 3.682   13.896  -13.462 1.00 41.19 ?  156 TYR D CE2 1 
ATOM   4449 C CZ  . TYR C 1 156 ? 4.597   14.877  -13.136 1.00 43.17 ?  156 TYR D CZ  1 
ATOM   4450 O OH  . TYR C 1 156 ? 5.101   15.682  -14.138 1.00 38.80 ?  156 TYR D OH  1 
ATOM   4451 N N   . PHE C 1 157 ? 2.896   9.677   -11.593 1.00 38.84 ?  157 PHE D N   1 
ATOM   4452 C CA  . PHE C 1 157 ? 2.912   8.898   -12.824 1.00 40.15 ?  157 PHE D CA  1 
ATOM   4453 C C   . PHE C 1 157 ? 1.481   8.705   -13.290 1.00 40.45 ?  157 PHE D C   1 
ATOM   4454 O O   . PHE C 1 157 ? 0.595   8.511   -12.448 1.00 40.75 ?  157 PHE D O   1 
ATOM   4455 C CB  . PHE C 1 157 ? 3.585   7.532   -12.639 1.00 39.51 ?  157 PHE D CB  1 
ATOM   4456 C CG  . PHE C 1 157 ? 3.741   6.764   -13.924 1.00 41.31 ?  157 PHE D CG  1 
ATOM   4457 C CD1 . PHE C 1 157 ? 4.831   6.981   -14.750 1.00 39.46 ?  157 PHE D CD1 1 
ATOM   4458 C CD2 . PHE C 1 157 ? 2.766   5.857   -14.329 1.00 42.63 ?  157 PHE D CD2 1 
ATOM   4459 C CE1 . PHE C 1 157 ? 4.969   6.289   -15.946 1.00 40.26 ?  157 PHE D CE1 1 
ATOM   4460 C CE2 . PHE C 1 157 ? 2.897   5.162   -15.520 1.00 41.58 ?  157 PHE D CE2 1 
ATOM   4461 C CZ  . PHE C 1 157 ? 4.003   5.381   -16.331 1.00 42.00 ?  157 PHE D CZ  1 
ATOM   4462 N N   . PRO C 1 158 ? 1.207   8.796   -14.595 1.00 42.31 ?  158 PRO D N   1 
ATOM   4463 C CA  . PRO C 1 158 ? 2.112   9.230   -15.662 1.00 40.78 ?  158 PRO D CA  1 
ATOM   4464 C C   . PRO C 1 158 ? 2.017   10.741  -15.850 1.00 40.48 ?  158 PRO D C   1 
ATOM   4465 O O   . PRO C 1 158 ? 1.307   11.431  -15.111 1.00 38.38 ?  158 PRO D O   1 
ATOM   4466 C CB  . PRO C 1 158 ? 1.578   8.462   -16.878 1.00 37.68 ?  158 PRO D CB  1 
ATOM   4467 C CG  . PRO C 1 158 ? 0.081   8.474   -16.651 1.00 38.22 ?  158 PRO D CG  1 
ATOM   4468 C CD  . PRO C 1 158 ? -0.110  8.409   -15.139 1.00 39.18 ?  158 PRO D CD  1 
ATOM   4469 N N   . GLU C 1 159 ? 2.738   11.278  -16.834 1.00 41.99 ?  159 GLU D N   1 
ATOM   4470 C CA  . GLU C 1 159 ? 2.466   12.623  -17.306 1.00 41.92 ?  159 GLU D CA  1 
ATOM   4471 C C   . GLU C 1 159 ? 1.013   12.703  -17.772 1.00 42.84 ?  159 GLU D C   1 
ATOM   4472 O O   . GLU C 1 159 ? 0.432   11.694  -18.181 1.00 43.78 ?  159 GLU D O   1 
ATOM   4473 C CB  . GLU C 1 159 ? 3.391   12.974  -18.470 1.00 40.77 ?  159 GLU D CB  1 
ATOM   4474 C CG  . GLU C 1 159 ? 4.855   13.278  -18.177 1.00 43.75 ?  159 GLU D CG  1 
ATOM   4475 C CD  . GLU C 1 159 ? 5.105   14.631  -17.514 1.00 47.35 ?  159 GLU D CD  1 
ATOM   4476 O OE1 . GLU C 1 159 ? 4.203   15.219  -16.871 1.00 43.65 ?  159 GLU D OE1 1 
ATOM   4477 O OE2 . GLU C 1 159 ? 6.197   15.171  -17.771 1.00 43.80 ?  159 GLU D OE2 1 
ATOM   4478 N N   . PRO C 1 160 ? 0.411   13.892  -17.763 1.00 43.54 ?  160 PRO D N   1 
ATOM   4479 C CA  . PRO C 1 160 ? 0.966   15.177  -17.345 1.00 42.75 ?  160 PRO D CA  1 
ATOM   4480 C C   . PRO C 1 160 ? 0.340   15.697  -16.059 1.00 42.47 ?  160 PRO D C   1 
ATOM   4481 O O   . PRO C 1 160 ? -0.675  15.183  -15.589 1.00 39.41 ?  160 PRO D O   1 
ATOM   4482 C CB  . PRO C 1 160 ? 0.615   16.076  -18.534 1.00 42.57 ?  160 PRO D CB  1 
ATOM   4483 C CG  . PRO C 1 160 ? -0.769  15.556  -18.960 1.00 43.33 ?  160 PRO D CG  1 
ATOM   4484 C CD  . PRO C 1 160 ? -0.850  14.096  -18.494 1.00 43.18 ?  160 PRO D CD  1 
ATOM   4485 N N   . VAL C 1 161 ? 0.954   16.716  -15.467 1.00 35.80 ?  161 VAL D N   1 
ATOM   4486 C CA  . VAL C 1 161 ? 0.318   17.529  -14.442 1.00 41.05 ?  161 VAL D CA  1 
ATOM   4487 C C   . VAL C 1 161 ? 0.200   18.942  -14.995 1.00 41.49 ?  161 VAL D C   1 
ATOM   4488 O O   . VAL C 1 161 ? 1.025   19.383  -15.801 1.00 40.90 ?  161 VAL D O   1 
ATOM   4489 C CB  . VAL C 1 161 ? 1.114   17.543  -13.118 1.00 42.52 ?  161 VAL D CB  1 
ATOM   4490 C CG1 . VAL C 1 161 ? 1.116   16.172  -12.459 1.00 39.99 ?  161 VAL D CG1 1 
ATOM   4491 C CG2 . VAL C 1 161 ? 2.523   18.038  -13.348 1.00 40.08 ?  161 VAL D CG2 1 
ATOM   4492 N N   . THR C 1 162 ? -0.824  19.655  -14.555 1.00 39.77 ?  162 THR D N   1 
ATOM   4493 C CA  . THR C 1 162 ? -0.915  21.080  -14.811 1.00 40.74 ?  162 THR D CA  1 
ATOM   4494 C C   . THR C 1 162 ? -0.783  21.829  -13.495 1.00 43.02 ?  162 THR D C   1 
ATOM   4495 O O   . THR C 1 162 ? -1.212  21.354  -12.437 1.00 40.45 ?  162 THR D O   1 
ATOM   4496 C CB  . THR C 1 162 ? -2.233  21.460  -15.492 1.00 40.84 ?  162 THR D CB  1 
ATOM   4497 O OG1 . THR C 1 162 ? -3.322  20.961  -14.713 1.00 46.65 ?  162 THR D OG1 1 
ATOM   4498 C CG2 . THR C 1 162 ? -2.304  20.865  -16.890 1.00 43.55 ?  162 THR D CG2 1 
ATOM   4499 N N   . VAL C 1 163 ? -0.176  23.006  -13.573 1.00 39.51 ?  163 VAL D N   1 
ATOM   4500 C CA  . VAL C 1 163 ? 0.044   23.854  -12.411 1.00 38.67 ?  163 VAL D CA  1 
ATOM   4501 C C   . VAL C 1 163 ? -0.428  25.262  -12.737 1.00 38.39 ?  163 VAL D C   1 
ATOM   4502 O O   . VAL C 1 163 ? -0.183  25.777  -13.833 1.00 39.43 ?  163 VAL D O   1 
ATOM   4503 C CB  . VAL C 1 163 ? 1.528   23.848  -11.982 1.00 39.35 ?  163 VAL D CB  1 
ATOM   4504 C CG1 . VAL C 1 163 ? 1.712   24.660  -10.709 1.00 38.71 ?  163 VAL D CG1 1 
ATOM   4505 C CG2 . VAL C 1 163 ? 2.008   22.414  -11.766 1.00 38.99 ?  163 VAL D CG2 1 
ATOM   4506 N N   . SER C 1 164 ? -1.125  25.873  -11.789 1.00 38.90 ?  164 SER D N   1 
ATOM   4507 C CA  . SER C 1 164 ? -1.450  27.289  -11.821 1.00 39.47 ?  164 SER D CA  1 
ATOM   4508 C C   . SER C 1 164 ? -1.137  27.869  -10.450 1.00 39.95 ?  164 SER D C   1 
ATOM   4509 O O   . SER C 1 164 ? -0.796  27.147  -9.509  1.00 39.57 ?  164 SER D O   1 
ATOM   4510 C CB  . SER C 1 164 ? -2.916  27.526  -12.221 1.00 41.71 ?  164 SER D CB  1 
ATOM   4511 O OG  . SER C 1 164 ? -3.810  27.296  -11.140 1.00 43.09 ?  164 SER D OG  1 
ATOM   4512 N N   . TRP C 1 165 ? -1.210  29.189  -10.341 1.00 40.94 ?  165 TRP D N   1 
ATOM   4513 C CA  . TRP C 1 165 ? -0.946  29.853  -9.079  1.00 38.26 ?  165 TRP D CA  1 
ATOM   4514 C C   . TRP C 1 165 ? -2.104  30.786  -8.783  1.00 42.00 ?  165 TRP D C   1 
ATOM   4515 O O   . TRP C 1 165 ? -2.577  31.500  -9.675  1.00 43.60 ?  165 TRP D O   1 
ATOM   4516 C CB  . TRP C 1 165 ? 0.384   30.627  -9.105  1.00 39.58 ?  165 TRP D CB  1 
ATOM   4517 C CG  . TRP C 1 165 ? 1.578   29.741  -8.918  1.00 38.64 ?  165 TRP D CG  1 
ATOM   4518 C CD1 . TRP C 1 165 ? 2.226   29.040  -9.890  1.00 39.91 ?  165 TRP D CD1 1 
ATOM   4519 C CD2 . TRP C 1 165 ? 2.266   29.458  -7.692  1.00 39.95 ?  165 TRP D CD2 1 
ATOM   4520 N NE1 . TRP C 1 165 ? 3.273   28.337  -9.350  1.00 37.50 ?  165 TRP D NE1 1 
ATOM   4521 C CE2 . TRP C 1 165 ? 3.320   28.579  -8.001  1.00 38.33 ?  165 TRP D CE2 1 
ATOM   4522 C CE3 . TRP C 1 165 ? 2.093   29.863  -6.364  1.00 42.18 ?  165 TRP D CE3 1 
ATOM   4523 C CZ2 . TRP C 1 165 ? 4.200   28.094  -7.030  1.00 38.50 ?  165 TRP D CZ2 1 
ATOM   4524 C CZ3 . TRP C 1 165 ? 2.966   29.378  -5.402  1.00 41.04 ?  165 TRP D CZ3 1 
ATOM   4525 C CH2 . TRP C 1 165 ? 4.003   28.506  -5.738  1.00 42.12 ?  165 TRP D CH2 1 
ATOM   4526 N N   . ASN C 1 166 ? -2.564  30.756  -7.533  1.00 44.31 ?  166 ASN D N   1 
ATOM   4527 C CA  . ASN C 1 166 ? -3.703  31.552  -7.071  1.00 45.93 ?  166 ASN D CA  1 
ATOM   4528 C C   . ASN C 1 166 ? -4.880  31.431  -8.037  1.00 46.34 ?  166 ASN D C   1 
ATOM   4529 O O   . ASN C 1 166 ? -5.464  32.423  -8.482  1.00 49.14 ?  166 ASN D O   1 
ATOM   4530 C CB  . ASN C 1 166 ? -3.297  33.008  -6.857  1.00 41.44 ?  166 ASN D CB  1 
ATOM   4531 C CG  . ASN C 1 166 ? -2.342  33.169  -5.685  1.00 45.49 ?  166 ASN D CG  1 
ATOM   4532 O OD1 . ASN C 1 166 ? -2.066  32.207  -4.964  1.00 48.34 ?  166 ASN D OD1 1 
ATOM   4533 N ND2 . ASN C 1 166 ? -1.819  34.370  -5.500  1.00 46.52 ?  166 ASN D ND2 1 
ATOM   4534 N N   . SER C 1 167 ? -5.200  30.182  -8.383  1.00 46.09 ?  167 SER D N   1 
ATOM   4535 C CA  . SER C 1 167 ? -6.333  29.846  -9.243  1.00 48.08 ?  167 SER D CA  1 
ATOM   4536 C C   . SER C 1 167 ? -6.227  30.505  -10.614 1.00 47.89 ?  167 SER D C   1 
ATOM   4537 O O   . SER C 1 167 ? -7.234  30.723  -11.288 1.00 49.54 ?  167 SER D O   1 
ATOM   4538 C CB  . SER C 1 167 ? -7.656  30.210  -8.563  1.00 48.72 ?  167 SER D CB  1 
ATOM   4539 O OG  . SER C 1 167 ? -7.690  29.654  -7.260  1.00 50.81 ?  167 SER D OG  1 
ATOM   4540 N N   . GLY C 1 168 ? -5.007  30.808  -11.051 1.00 46.46 ?  168 GLY D N   1 
ATOM   4541 C CA  . GLY C 1 168 ? -4.790  31.442  -12.329 1.00 46.67 ?  168 GLY D CA  1 
ATOM   4542 C C   . GLY C 1 168 ? -4.697  32.949  -12.283 1.00 46.97 ?  168 GLY D C   1 
ATOM   4543 O O   . GLY C 1 168 ? -4.432  33.569  -13.322 1.00 49.25 ?  168 GLY D O   1 
ATOM   4544 N N   . ALA C 1 169 ? -4.902  33.564  -11.115 1.00 45.22 ?  169 ALA D N   1 
ATOM   4545 C CA  . ALA C 1 169 ? -4.765  35.012  -11.017 1.00 49.43 ?  169 ALA D CA  1 
ATOM   4546 C C   . ALA C 1 169 ? -3.308  35.443  -11.090 1.00 47.54 ?  169 ALA D C   1 
ATOM   4547 O O   . ALA C 1 169 ? -3.021  36.580  -11.482 1.00 49.50 ?  169 ALA D O   1 
ATOM   4548 C CB  . ALA C 1 169 ? -5.405  35.521  -9.724  1.00 49.25 ?  169 ALA D CB  1 
ATOM   4549 N N   . LEU C 1 170 ? -2.378  34.561  -10.722 1.00 45.22 ?  170 LEU D N   1 
ATOM   4550 C CA  . LEU C 1 170 ? -0.949  34.860  -10.752 1.00 43.19 ?  170 LEU D CA  1 
ATOM   4551 C C   . LEU C 1 170 ? -0.331  34.165  -11.957 1.00 44.35 ?  170 LEU D C   1 
ATOM   4552 O O   . LEU C 1 170 ? -0.265  32.929  -12.003 1.00 42.02 ?  170 LEU D O   1 
ATOM   4553 C CB  . LEU C 1 170 ? -0.274  34.415  -9.459  1.00 43.18 ?  170 LEU D CB  1 
ATOM   4554 C CG  . LEU C 1 170 ? 1.221   34.699  -9.306  1.00 41.18 ?  170 LEU D CG  1 
ATOM   4555 C CD1 . LEU C 1 170 ? 1.577   36.123  -9.731  1.00 42.65 ?  170 LEU D CD1 1 
ATOM   4556 C CD2 . LEU C 1 170 ? 1.662   34.424  -7.877  1.00 41.17 ?  170 LEU D CD2 1 
ATOM   4557 N N   . THR C 1 171 ? 0.127   34.958  -12.927 1.00 44.42 ?  171 THR D N   1 
ATOM   4558 C CA  . THR C 1 171 ? 0.737   34.401  -14.130 1.00 42.38 ?  171 THR D CA  1 
ATOM   4559 C C   . THR C 1 171 ? 2.104   35.014  -14.429 1.00 41.75 ?  171 THR D C   1 
ATOM   4560 O O   . THR C 1 171 ? 2.987   34.329  -14.949 1.00 42.02 ?  171 THR D O   1 
ATOM   4561 C CB  . THR C 1 171 ? -0.205  34.571  -15.328 1.00 45.52 ?  171 THR D CB  1 
ATOM   4562 O OG1 . THR C 1 171 ? -0.317  35.960  -15.661 1.00 45.69 ?  171 THR D OG1 1 
ATOM   4563 C CG2 . THR C 1 171 ? -1.593  34.000  -15.021 1.00 45.76 ?  171 THR D CG2 1 
ATOM   4564 N N   . SER C 1 172 ? 2.300   36.288  -14.110 1.00 45.08 ?  172 SER D N   1 
ATOM   4565 C CA  . SER C 1 172 ? 3.586   36.923  -14.377 1.00 48.23 ?  172 SER D CA  1 
ATOM   4566 C C   . SER C 1 172 ? 4.641   36.406  -13.408 1.00 42.78 ?  172 SER D C   1 
ATOM   4567 O O   . SER C 1 172 ? 4.429   36.402  -12.192 1.00 45.03 ?  172 SER D O   1 
ATOM   4568 C CB  . SER C 1 172 ? 3.470   38.442  -14.257 1.00 49.90 ?  172 SER D CB  1 
ATOM   4569 O OG  . SER C 1 172 ? 2.478   38.941  -15.135 1.00 56.56 ?  172 SER D OG  1 
ATOM   4570 N N   . GLY C 1 173 ? 5.780   35.976  -13.943 1.00 41.73 ?  173 GLY D N   1 
ATOM   4571 C CA  . GLY C 1 173 ? 6.850   35.464  -13.108 1.00 39.14 ?  173 GLY D CA  1 
ATOM   4572 C C   . GLY C 1 173 ? 6.747   33.998  -12.750 1.00 39.73 ?  173 GLY D C   1 
ATOM   4573 O O   . GLY C 1 173 ? 7.591   33.498  -11.995 1.00 39.07 ?  173 GLY D O   1 
ATOM   4574 N N   . VAL C 1 174 ? 5.758   33.287  -13.275 1.00 35.76 ?  174 VAL D N   1 
ATOM   4575 C CA  . VAL C 1 174 ? 5.596   31.862  -13.007 1.00 32.24 ?  174 VAL D CA  1 
ATOM   4576 C C   . VAL C 1 174 ? 6.428   31.059  -13.996 1.00 35.11 ?  174 VAL D C   1 
ATOM   4577 O O   . VAL C 1 174 ? 6.381   31.304  -15.206 1.00 37.40 ?  174 VAL D O   1 
ATOM   4578 C CB  . VAL C 1 174 ? 4.117   31.453  -13.088 1.00 33.31 ?  174 VAL D CB  1 
ATOM   4579 C CG1 . VAL C 1 174 ? 3.999   29.953  -12.904 1.00 32.40 ?  174 VAL D CG1 1 
ATOM   4580 C CG2 . VAL C 1 174 ? 3.313   32.187  -12.040 1.00 33.04 ?  174 VAL D CG2 1 
ATOM   4581 N N   . HIS C 1 175 ? 7.161   30.087  -13.464 1.00 33.23 ?  175 HIS D N   1 
ATOM   4582 C CA  . HIS C 1 175 ? 7.948   29.161  -14.309 1.00 37.15 ?  175 HIS D CA  1 
ATOM   4583 C C   . HIS C 1 175 ? 7.674   27.721  -13.860 1.00 34.41 ?  175 HIS D C   1 
ATOM   4584 O O   . HIS C 1 175 ? 8.113   27.350  -12.767 1.00 35.74 ?  175 HIS D O   1 
ATOM   4585 C CB  . HIS C 1 175 ? 9.437   29.526  -14.252 1.00 37.04 ?  175 HIS D CB  1 
ATOM   4586 C CG  . HIS C 1 175 ? 9.717   30.978  -14.434 1.00 39.85 ?  175 HIS D CG  1 
ATOM   4587 N ND1 . HIS C 1 175 ? 9.913   31.546  -15.673 1.00 44.29 ?  175 HIS D ND1 1 
ATOM   4588 C CD2 . HIS C 1 175 ? 9.833   31.972  -13.550 1.00 41.79 ?  175 HIS D CD2 1 
ATOM   4589 C CE1 . HIS C 1 175 ? 10.134  32.843  -15.526 1.00 43.24 ?  175 HIS D CE1 1 
ATOM   4590 N NE2 . HIS C 1 175 ? 10.085  33.123  -14.245 1.00 44.97 ?  175 HIS D NE2 1 
ATOM   4591 N N   . THR C 1 176 ? 6.947   26.951  -14.665 1.00 36.15 ?  176 THR D N   1 
ATOM   4592 C CA  . THR C 1 176 ? 6.734   25.535  -14.393 1.00 37.25 ?  176 THR D CA  1 
ATOM   4593 C C   . THR C 1 176 ? 7.684   24.722  -15.263 1.00 37.36 ?  176 THR D C   1 
ATOM   4594 O O   . THR C 1 176 ? 7.709   24.894  -16.484 1.00 41.52 ?  176 THR D O   1 
ATOM   4595 C CB  . THR C 1 176 ? 5.275   25.148  -14.656 1.00 37.88 ?  176 THR D CB  1 
ATOM   4596 O OG1 . THR C 1 176 ? 4.410   26.030  -13.921 1.00 37.28 ?  176 THR D OG1 1 
ATOM   4597 C CG2 . THR C 1 176 ? 5.016   23.708  -14.241 1.00 38.36 ?  176 THR D CG2 1 
ATOM   4598 N N   . PHE C 1 177 ? 8.464   23.849  -14.635 1.00 35.48 ?  177 PHE D N   1 
ATOM   4599 C CA  . PHE C 1 177 ? 9.553   23.183  -15.335 1.00 34.64 ?  177 PHE D CA  1 
ATOM   4600 C C   . PHE C 1 177 ? 9.096   21.873  -15.962 1.00 36.02 ?  177 PHE D C   1 
ATOM   4601 O O   . PHE C 1 177 ? 8.161   21.232  -15.470 1.00 38.76 ?  177 PHE D O   1 
ATOM   4602 C CB  . PHE C 1 177 ? 10.713  22.909  -14.383 1.00 36.04 ?  177 PHE D CB  1 
ATOM   4603 C CG  . PHE C 1 177 ? 11.493  24.141  -14.034 1.00 37.07 ?  177 PHE D CG  1 
ATOM   4604 C CD1 . PHE C 1 177 ? 11.098  24.952  -12.977 1.00 36.20 ?  177 PHE D CD1 1 
ATOM   4605 C CD2 . PHE C 1 177 ? 12.601  24.509  -14.786 1.00 36.19 ?  177 PHE D CD2 1 
ATOM   4606 C CE1 . PHE C 1 177 ? 11.800  26.106  -12.665 1.00 38.58 ?  177 PHE D CE1 1 
ATOM   4607 C CE2 . PHE C 1 177 ? 13.325  25.651  -14.472 1.00 36.13 ?  177 PHE D CE2 1 
ATOM   4608 C CZ  . PHE C 1 177 ? 12.920  26.456  -13.417 1.00 36.81 ?  177 PHE D CZ  1 
ATOM   4609 N N   . PRO C 1 178 ? 9.734   21.471  -17.058 1.00 38.67 ?  178 PRO D N   1 
ATOM   4610 C CA  . PRO C 1 178 ? 9.476   20.139  -17.605 1.00 37.50 ?  178 PRO D CA  1 
ATOM   4611 C C   . PRO C 1 178 ? 9.784   19.086  -16.559 1.00 38.76 ?  178 PRO D C   1 
ATOM   4612 O O   . PRO C 1 178 ? 10.756  19.194  -15.811 1.00 37.18 ?  178 PRO D O   1 
ATOM   4613 C CB  . PRO C 1 178 ? 10.444  20.052  -18.787 1.00 39.18 ?  178 PRO D CB  1 
ATOM   4614 C CG  . PRO C 1 178 ? 10.622  21.467  -19.214 1.00 38.23 ?  178 PRO D CG  1 
ATOM   4615 C CD  . PRO C 1 178 ? 10.588  22.276  -17.946 1.00 39.38 ?  178 PRO D CD  1 
ATOM   4616 N N   . ALA C 1 179 ? 8.945   18.062  -16.504 1.00 37.48 ?  179 ALA D N   1 
ATOM   4617 C CA  . ALA C 1 179 ? 9.154   17.009  -15.528 1.00 41.21 ?  179 ALA D CA  1 
ATOM   4618 C C   . ALA C 1 179 ? 10.424  16.228  -15.837 1.00 41.15 ?  179 ALA D C   1 
ATOM   4619 O O   . ALA C 1 179 ? 10.787  16.012  -16.997 1.00 42.73 ?  179 ALA D O   1 
ATOM   4620 C CB  . ALA C 1 179 ? 7.958   16.061  -15.503 1.00 39.18 ?  179 ALA D CB  1 
ATOM   4621 N N   . VAL C 1 180 ? 11.102  15.805  -14.790 1.00 38.44 ?  180 VAL D N   1 
ATOM   4622 C CA  . VAL C 1 180 ? 12.234  14.901  -14.928 1.00 39.34 ?  180 VAL D CA  1 
ATOM   4623 C C   . VAL C 1 180 ? 11.775  13.506  -14.540 1.00 43.46 ?  180 VAL D C   1 
ATOM   4624 O O   . VAL C 1 180 ? 10.903  13.323  -13.679 1.00 41.17 ?  180 VAL D O   1 
ATOM   4625 C CB  . VAL C 1 180 ? 13.444  15.348  -14.080 1.00 43.94 ?  180 VAL D CB  1 
ATOM   4626 C CG1 . VAL C 1 180 ? 13.165  15.164  -12.589 1.00 43.10 ?  180 VAL D CG1 1 
ATOM   4627 C CG2 . VAL C 1 180 ? 14.693  14.586  -14.498 1.00 47.84 ?  180 VAL D CG2 1 
ATOM   4628 N N   . LEU C 1 181 ? 12.351  12.512  -15.203 1.00 43.71 ?  181 LEU D N   1 
ATOM   4629 C CA  . LEU C 1 181 ? 12.089  11.114  -14.895 1.00 48.84 ?  181 LEU D CA  1 
ATOM   4630 C C   . LEU C 1 181 ? 13.132  10.648  -13.887 1.00 48.18 ?  181 LEU D C   1 
ATOM   4631 O O   . LEU C 1 181 ? 14.338  10.716  -14.153 1.00 48.34 ?  181 LEU D O   1 
ATOM   4632 C CB  . LEU C 1 181 ? 12.137  10.262  -16.159 1.00 46.69 ?  181 LEU D CB  1 
ATOM   4633 C CG  . LEU C 1 181 ? 11.656  8.822   -16.009 1.00 48.51 ?  181 LEU D CG  1 
ATOM   4634 C CD1 . LEU C 1 181 ? 10.197  8.790   -15.588 1.00 46.54 ?  181 LEU D CD1 1 
ATOM   4635 C CD2 . LEU C 1 181 ? 11.897  8.038   -17.297 1.00 50.29 ?  181 LEU D CD2 1 
ATOM   4636 N N   . GLN C 1 182 ? 12.673  10.199  -12.733 1.00 45.85 ?  182 GLN D N   1 
ATOM   4637 C CA  . GLN C 1 182 ? 13.566  9.808   -11.660 1.00 49.14 ?  182 GLN D CA  1 
ATOM   4638 C C   . GLN C 1 182 ? 13.981  8.354   -11.832 1.00 52.18 ?  182 GLN D C   1 
ATOM   4639 O O   . GLN C 1 182 ? 13.383  7.598   -12.603 1.00 51.67 ?  182 GLN D O   1 
ATOM   4640 C CB  . GLN C 1 182 ? 12.883  10.019  -10.313 1.00 51.00 ?  182 GLN D CB  1 
ATOM   4641 C CG  . GLN C 1 182 ? 12.734  11.482  -9.940  1.00 48.64 ?  182 GLN D CG  1 
ATOM   4642 C CD  . GLN C 1 182 ? 11.884  11.663  -8.712  1.00 49.91 ?  182 GLN D CD  1 
ATOM   4643 O OE1 . GLN C 1 182 ? 12.247  12.378  -7.780  1.00 54.44 ?  182 GLN D OE1 1 
ATOM   4644 N NE2 . GLN C 1 182 ? 10.729  11.021  -8.707  1.00 48.63 ?  182 GLN D NE2 1 
ATOM   4645 N N   . SER C 1 183 ? 15.037  7.974   -11.105 1.00 56.68 ?  183 SER D N   1 
ATOM   4646 C CA  . SER C 1 183 ? 15.514  6.595   -11.144 1.00 56.88 ?  183 SER D CA  1 
ATOM   4647 C C   . SER C 1 183 ? 14.399  5.619   -10.795 1.00 57.51 ?  183 SER D C   1 
ATOM   4648 O O   . SER C 1 183 ? 14.313  4.528   -11.370 1.00 59.29 ?  183 SER D O   1 
ATOM   4649 C CB  . SER C 1 183 ? 16.705  6.429   -10.195 1.00 58.25 ?  183 SER D CB  1 
ATOM   4650 O OG  . SER C 1 183 ? 16.333  6.702   -8.853  1.00 63.08 ?  183 SER D OG  1 
ATOM   4651 N N   . SER C 1 184 ? 13.512  6.015   -9.876  1.00 57.86 ?  184 SER D N   1 
ATOM   4652 C CA  . SER C 1 184 ? 12.371  5.200   -9.473  1.00 55.61 ?  184 SER D CA  1 
ATOM   4653 C C   . SER C 1 184 ? 11.381  4.940   -10.600 1.00 53.40 ?  184 SER D C   1 
ATOM   4654 O O   . SER C 1 184 ? 10.483  4.108   -10.430 1.00 52.22 ?  184 SER D O   1 
ATOM   4655 C CB  . SER C 1 184 ? 11.628  5.887   -8.330  1.00 54.76 ?  184 SER D CB  1 
ATOM   4656 O OG  . SER C 1 184 ? 10.687  6.821   -8.843  1.00 54.59 ?  184 SER D OG  1 
ATOM   4657 N N   . GLY C 1 185 ? 11.501  5.641   -11.729 1.00 53.90 ?  185 GLY D N   1 
ATOM   4658 C CA  . GLY C 1 185 ? 10.501  5.583   -12.774 1.00 45.83 ?  185 GLY D CA  1 
ATOM   4659 C C   . GLY C 1 185 ? 9.337   6.532   -12.599 1.00 46.58 ?  185 GLY D C   1 
ATOM   4660 O O   . GLY C 1 185 ? 8.409   6.510   -13.418 1.00 44.74 ?  185 GLY D O   1 
ATOM   4661 N N   . LEU C 1 186 ? 9.337   7.350   -11.553 1.00 44.67 ?  186 LEU D N   1 
ATOM   4662 C CA  . LEU C 1 186 ? 8.285   8.330   -11.334 1.00 44.53 ?  186 LEU D CA  1 
ATOM   4663 C C   . LEU C 1 186 ? 8.766   9.704   -11.788 1.00 41.52 ?  186 LEU D C   1 
ATOM   4664 O O   . LEU C 1 186 ? 9.966   9.963   -11.890 1.00 44.61 ?  186 LEU D O   1 
ATOM   4665 C CB  . LEU C 1 186 ? 7.878   8.374   -9.860  1.00 42.78 ?  186 LEU D CB  1 
ATOM   4666 C CG  . LEU C 1 186 ? 7.295   7.094   -9.237  1.00 43.97 ?  186 LEU D CG  1 
ATOM   4667 C CD1 . LEU C 1 186 ? 7.064   7.303   -7.747  1.00 44.30 ?  186 LEU D CD1 1 
ATOM   4668 C CD2 . LEU C 1 186 ? 6.015   6.638   -9.924  1.00 43.54 ?  186 LEU D CD2 1 
ATOM   4669 N N   . TYR C 1 187 ? 7.812   10.580  -12.080 1.00 39.84 ?  187 TYR D N   1 
ATOM   4670 C CA  . TYR C 1 187 ? 8.126   11.933  -12.526 1.00 40.23 ?  187 TYR D CA  1 
ATOM   4671 C C   . TYR C 1 187 ? 8.143   12.911  -11.364 1.00 41.81 ?  187 TYR D C   1 
ATOM   4672 O O   . TYR C 1 187 ? 7.470   12.722  -10.349 1.00 41.46 ?  187 TYR D O   1 
ATOM   4673 C CB  . TYR C 1 187 ? 7.114   12.428  -13.561 1.00 39.44 ?  187 TYR D CB  1 
ATOM   4674 C CG  . TYR C 1 187 ? 7.201   11.711  -14.885 1.00 44.68 ?  187 TYR D CG  1 
ATOM   4675 C CD1 . TYR C 1 187 ? 8.218   12.004  -15.789 1.00 43.33 ?  187 TYR D CD1 1 
ATOM   4676 C CD2 . TYR C 1 187 ? 6.274   10.728  -15.226 1.00 42.98 ?  187 TYR D CD2 1 
ATOM   4677 C CE1 . TYR C 1 187 ? 8.302   11.348  -17.006 1.00 46.61 ?  187 TYR D CE1 1 
ATOM   4678 C CE2 . TYR C 1 187 ? 6.354   10.067  -16.436 1.00 45.47 ?  187 TYR D CE2 1 
ATOM   4679 C CZ  . TYR C 1 187 ? 7.369   10.375  -17.319 1.00 47.90 ?  187 TYR D CZ  1 
ATOM   4680 O OH  . TYR C 1 187 ? 7.444   9.709   -18.523 1.00 49.12 ?  187 TYR D OH  1 
ATOM   4681 N N   . SER C 1 188 ? 8.892   13.991  -11.540 1.00 38.69 ?  188 SER D N   1 
ATOM   4682 C CA  . SER C 1 188 ? 8.888   15.059  -10.559 1.00 37.86 ?  188 SER D CA  1 
ATOM   4683 C C   . SER C 1 188 ? 9.175   16.360  -11.296 1.00 40.14 ?  188 SER D C   1 
ATOM   4684 O O   . SER C 1 188 ? 9.906   16.366  -12.297 1.00 36.98 ?  188 SER D O   1 
ATOM   4685 C CB  . SER C 1 188 ? 9.913   14.767  -9.453  1.00 44.34 ?  188 SER D CB  1 
ATOM   4686 O OG  . SER C 1 188 ? 10.196  15.907  -8.662  1.00 48.56 ?  188 SER D OG  1 
ATOM   4687 N N   . LEU C 1 189 ? 8.554   17.442  -10.835 1.00 34.58 ?  189 LEU D N   1 
ATOM   4688 C CA  . LEU C 1 189 ? 8.821   18.763  -11.379 1.00 39.73 ?  189 LEU D CA  1 
ATOM   4689 C C   . LEU C 1 189 ? 8.732   19.799  -10.270 1.00 40.28 ?  189 LEU D C   1 
ATOM   4690 O O   . LEU C 1 189 ? 8.314   19.507  -9.144  1.00 39.85 ?  189 LEU D O   1 
ATOM   4691 C CB  . LEU C 1 189 ? 7.854   19.137  -12.514 1.00 36.32 ?  189 LEU D CB  1 
ATOM   4692 C CG  . LEU C 1 189 ? 6.337   19.239  -12.355 1.00 39.57 ?  189 LEU D CG  1 
ATOM   4693 C CD1 . LEU C 1 189 ? 5.892   20.523  -11.663 1.00 39.72 ?  189 LEU D CD1 1 
ATOM   4694 C CD2 . LEU C 1 189 ? 5.738   19.185  -13.740 1.00 38.96 ?  189 LEU D CD2 1 
ATOM   4695 N N   . SER C 1 190 ? 9.129   21.023  -10.614 1.00 37.15 ?  190 SER D N   1 
ATOM   4696 C CA  . SER C 1 190 ? 8.959   22.194  -9.773  1.00 36.01 ?  190 SER D CA  1 
ATOM   4697 C C   . SER C 1 190 ? 8.190   23.249  -10.548 1.00 34.63 ?  190 SER D C   1 
ATOM   4698 O O   . SER C 1 190 ? 8.272   23.322  -11.775 1.00 36.27 ?  190 SER D O   1 
ATOM   4699 C CB  . SER C 1 190 ? 10.308  22.792  -9.329  1.00 39.68 ?  190 SER D CB  1 
ATOM   4700 O OG  . SER C 1 190 ? 10.965  21.946  -8.401  1.00 44.83 ?  190 SER D OG  1 
ATOM   4701 N N   . SER C 1 191 ? 7.445   24.067  -9.819  1.00 32.08 ?  191 SER D N   1 
ATOM   4702 C CA  . SER C 1 191 ? 6.872   25.294  -10.343 1.00 32.05 ?  191 SER D CA  1 
ATOM   4703 C C   . SER C 1 191 ? 7.241   26.412  -9.385  1.00 35.99 ?  191 SER D C   1 
ATOM   4704 O O   . SER C 1 191 ? 7.042   26.277  -8.175  1.00 35.50 ?  191 SER D O   1 
ATOM   4705 C CB  . SER C 1 191 ? 5.348   25.192  -10.496 1.00 32.99 ?  191 SER D CB  1 
ATOM   4706 O OG  . SER C 1 191 ? 4.818   26.398  -11.013 1.00 32.60 ?  191 SER D OG  1 
ATOM   4707 N N   . VAL C 1 192 ? 7.810   27.501  -9.911  1.00 32.13 ?  192 VAL D N   1 
ATOM   4708 C CA  . VAL C 1 192 ? 8.309   28.575  -9.066  1.00 32.12 ?  192 VAL D CA  1 
ATOM   4709 C C   . VAL C 1 192 ? 7.731   29.882  -9.575  1.00 34.14 ?  192 VAL D C   1 
ATOM   4710 O O   . VAL C 1 192 ? 7.307   29.993  -10.727 1.00 33.80 ?  192 VAL D O   1 
ATOM   4711 C CB  . VAL C 1 192 ? 9.851   28.651  -9.051  1.00 33.00 ?  192 VAL D CB  1 
ATOM   4712 C CG1 . VAL C 1 192 ? 10.460  27.327  -8.594  1.00 33.14 ?  192 VAL D CG1 1 
ATOM   4713 C CG2 . VAL C 1 192 ? 10.371  29.071  -10.422 1.00 35.44 ?  192 VAL D CG2 1 
ATOM   4714 N N   . VAL C 1 193 ? 7.719   30.882  -8.703  1.00 32.13 ?  193 VAL D N   1 
ATOM   4715 C CA  . VAL C 1 193 ? 7.355   32.232  -9.102  1.00 32.84 ?  193 VAL D CA  1 
ATOM   4716 C C   . VAL C 1 193 ? 8.276   33.207  -8.382  1.00 35.32 ?  193 VAL D C   1 
ATOM   4717 O O   . VAL C 1 193 ? 8.648   32.984  -7.225  1.00 32.70 ?  193 VAL D O   1 
ATOM   4718 C CB  . VAL C 1 193 ? 5.862   32.517  -8.830  1.00 36.73 ?  193 VAL D CB  1 
ATOM   4719 C CG1 . VAL C 1 193 ? 5.558   32.315  -7.406  1.00 36.83 ?  193 VAL D CG1 1 
ATOM   4720 C CG2 . VAL C 1 193 ? 5.497   33.933  -9.234  1.00 35.62 ?  193 VAL D CG2 1 
ATOM   4721 N N   . THR C 1 194 ? 8.702   34.248  -9.098  1.00 31.93 ?  194 THR D N   1 
ATOM   4722 C CA  . THR C 1 194 ? 9.506   35.322  -8.534  1.00 33.85 ?  194 THR D CA  1 
ATOM   4723 C C   . THR C 1 194 ? 8.586   36.482  -8.182  1.00 36.06 ?  194 THR D C   1 
ATOM   4724 O O   . THR C 1 194 ? 7.772   36.904  -9.008  1.00 36.97 ?  194 THR D O   1 
ATOM   4725 C CB  . THR C 1 194 ? 10.578  35.782  -9.525  1.00 37.89 ?  194 THR D CB  1 
ATOM   4726 O OG1 . THR C 1 194 ? 9.962   36.080  -10.782 1.00 37.16 ?  194 THR D OG1 1 
ATOM   4727 C CG2 . THR C 1 194 ? 11.606  34.694  -9.736  1.00 35.04 ?  194 THR D CG2 1 
ATOM   4728 N N   . VAL C 1 195 ? 8.716   36.990  -6.961  1.00 36.53 ?  195 VAL D N   1 
ATOM   4729 C CA  . VAL C 1 195 ? 7.833   38.038  -6.451  1.00 39.97 ?  195 VAL D CA  1 
ATOM   4730 C C   . VAL C 1 195 ? 8.687   39.086  -5.751  1.00 40.84 ?  195 VAL D C   1 
ATOM   4731 O O   . VAL C 1 195 ? 9.846   38.820  -5.395  1.00 40.71 ?  195 VAL D O   1 
ATOM   4732 C CB  . VAL C 1 195 ? 6.775   37.466  -5.478  1.00 40.90 ?  195 VAL D CB  1 
ATOM   4733 C CG1 . VAL C 1 195 ? 5.909   36.418  -6.167  1.00 41.52 ?  195 VAL D CG1 1 
ATOM   4734 C CG2 . VAL C 1 195 ? 7.463   36.881  -4.260  1.00 42.88 ?  195 VAL D CG2 1 
ATOM   4735 N N   . PRO C 1 196 ? 8.147   40.284  -5.532  1.00 44.06 ?  196 PRO D N   1 
ATOM   4736 C CA  . PRO C 1 196 ? 8.844   41.242  -4.664  1.00 44.05 ?  196 PRO D CA  1 
ATOM   4737 C C   . PRO C 1 196 ? 8.930   40.685  -3.251  1.00 46.81 ?  196 PRO D C   1 
ATOM   4738 O O   . PRO C 1 196 ? 7.928   40.252  -2.673  1.00 48.25 ?  196 PRO D O   1 
ATOM   4739 C CB  . PRO C 1 196 ? 7.957   42.495  -4.722  1.00 44.24 ?  196 PRO D CB  1 
ATOM   4740 C CG  . PRO C 1 196 ? 7.117   42.330  -5.942  1.00 44.32 ?  196 PRO D CG  1 
ATOM   4741 C CD  . PRO C 1 196 ? 6.890   40.841  -6.060  1.00 40.74 ?  196 PRO D CD  1 
ATOM   4742 N N   . SER C 1 197 ? 10.144  40.675  -2.703  1.00 45.64 ?  197 SER D N   1 
ATOM   4743 C CA  . SER C 1 197 ? 10.310  40.247  -1.322  1.00 48.06 ?  197 SER D CA  1 
ATOM   4744 C C   . SER C 1 197 ? 9.535   41.131  -0.358  1.00 51.95 ?  197 SER D C   1 
ATOM   4745 O O   . SER C 1 197 ? 9.220   40.693  0.753   1.00 53.19 ?  197 SER D O   1 
ATOM   4746 C CB  . SER C 1 197 ? 11.794  40.224  -0.958  1.00 47.00 ?  197 SER D CB  1 
ATOM   4747 O OG  . SER C 1 197 ? 12.406  41.455  -1.277  1.00 55.74 ?  197 SER D OG  1 
ATOM   4748 N N   . SER C 1 198 ? 9.190   42.354  -0.770  1.00 51.00 ?  198 SER D N   1 
ATOM   4749 C CA  . SER C 1 198 ? 8.387   43.228  0.069   1.00 51.58 ?  198 SER D CA  1 
ATOM   4750 C C   . SER C 1 198 ? 6.950   42.745  0.213   1.00 55.49 ?  198 SER D C   1 
ATOM   4751 O O   . SER C 1 198 ? 6.237   43.230  1.098   1.00 60.94 ?  198 SER D O   1 
ATOM   4752 C CB  . SER C 1 198 ? 8.404   44.653  -0.495  1.00 54.03 ?  198 SER D CB  1 
ATOM   4753 O OG  . SER C 1 198 ? 7.621   44.756  -1.676  1.00 55.84 ?  198 SER D OG  1 
ATOM   4754 N N   . SER C 1 199 ? 6.501   41.808  -0.623  1.00 54.94 ?  199 SER D N   1 
ATOM   4755 C CA  . SER C 1 199 ? 5.109   41.377  -0.611  1.00 55.86 ?  199 SER D CA  1 
ATOM   4756 C C   . SER C 1 199 ? 4.894   40.071  0.144   1.00 55.74 ?  199 SER D C   1 
ATOM   4757 O O   . SER C 1 199 ? 3.774   39.549  0.146   1.00 59.65 ?  199 SER D O   1 
ATOM   4758 C CB  . SER C 1 199 ? 4.582   41.232  -2.042  1.00 54.45 ?  199 SER D CB  1 
ATOM   4759 O OG  . SER C 1 199 ? 5.028   40.020  -2.631  1.00 53.69 ?  199 SER D OG  1 
ATOM   4760 N N   . LEU C 1 200 ? 5.926   39.538  0.793   1.00 55.87 ?  200 LEU D N   1 
ATOM   4761 C CA  . LEU C 1 200 ? 5.836   38.227  1.426   1.00 55.80 ?  200 LEU D CA  1 
ATOM   4762 C C   . LEU C 1 200 ? 5.008   38.224  2.706   1.00 59.40 ?  200 LEU D C   1 
ATOM   4763 O O   . LEU C 1 200 ? 4.776   37.149  3.269   1.00 59.47 ?  200 LEU D O   1 
ATOM   4764 C CB  . LEU C 1 200 ? 7.236   37.688  1.722   1.00 53.94 ?  200 LEU D CB  1 
ATOM   4765 C CG  . LEU C 1 200 ? 8.096   37.353  0.501   1.00 54.89 ?  200 LEU D CG  1 
ATOM   4766 C CD1 . LEU C 1 200 ? 9.341   36.581  0.912   1.00 54.41 ?  200 LEU D CD1 1 
ATOM   4767 C CD2 . LEU C 1 200 ? 7.294   36.579  -0.531  1.00 55.09 ?  200 LEU D CD2 1 
ATOM   4768 N N   . GLY C 1 201 ? 4.564   39.380  3.186   1.00 59.61 ?  201 GLY D N   1 
ATOM   4769 C CA  . GLY C 1 201 ? 3.676   39.407  4.329   1.00 60.42 ?  201 GLY D CA  1 
ATOM   4770 C C   . GLY C 1 201 ? 2.251   39.717  3.924   1.00 64.40 ?  201 GLY D C   1 
ATOM   4771 O O   . GLY C 1 201 ? 1.298   39.192  4.507   1.00 68.08 ?  201 GLY D O   1 
ATOM   4772 N N   . THR C 1 202 ? 2.094   40.563  2.909   1.00 63.20 ?  202 THR D N   1 
ATOM   4773 C CA  . THR C 1 202 ? 0.763   41.020  2.530   1.00 63.03 ?  202 THR D CA  1 
ATOM   4774 C C   . THR C 1 202 ? 0.057   40.062  1.578   1.00 64.31 ?  202 THR D C   1 
ATOM   4775 O O   . THR C 1 202 ? -1.178  40.037  1.545   1.00 66.37 ?  202 THR D O   1 
ATOM   4776 C CB  . THR C 1 202 ? 0.851   42.409  1.896   1.00 64.56 ?  202 THR D CB  1 
ATOM   4777 O OG1 . THR C 1 202 ? -0.469  42.908  1.650   1.00 69.65 ?  202 THR D OG1 1 
ATOM   4778 C CG2 . THR C 1 202 ? 1.638   42.361  0.583   1.00 63.47 ?  202 THR D CG2 1 
ATOM   4779 N N   . GLN C 1 203 ? 0.800   39.273  0.805   1.00 61.13 ?  203 GLN D N   1 
ATOM   4780 C CA  . GLN C 1 203 ? 0.224   38.488  -0.278  1.00 59.46 ?  203 GLN D CA  1 
ATOM   4781 C C   . GLN C 1 203 ? 0.323   36.995  0.002   1.00 54.52 ?  203 GLN D C   1 
ATOM   4782 O O   . GLN C 1 203 ? 1.332   36.511  0.524   1.00 56.37 ?  203 GLN D O   1 
ATOM   4783 C CB  . GLN C 1 203 ? 0.895   38.818  -1.618  1.00 56.93 ?  203 GLN D CB  1 
ATOM   4784 C CG  . GLN C 1 203 ? 0.309   38.047  -2.807  1.00 57.20 ?  203 GLN D CG  1 
ATOM   4785 C CD  . GLN C 1 203 ? -1.150  38.373  -3.072  1.00 58.17 ?  203 GLN D CD  1 
ATOM   4786 O OE1 . GLN C 1 203 ? -1.501  39.513  -3.376  1.00 63.15 ?  203 GLN D OE1 1 
ATOM   4787 N NE2 . GLN C 1 203 ? -2.012  37.369  -2.945  1.00 55.53 ?  203 GLN D NE2 1 
ATOM   4788 N N   . THR C 1 204 ? -0.743  36.279  -0.348  1.00 53.14 ?  204 THR D N   1 
ATOM   4789 C CA  . THR C 1 204 ? -0.822  34.832  -0.227  1.00 53.75 ?  204 THR D CA  1 
ATOM   4790 C C   . THR C 1 204 ? -0.545  34.189  -1.580  1.00 48.74 ?  204 THR D C   1 
ATOM   4791 O O   . THR C 1 204 ? -1.070  34.629  -2.607  1.00 47.65 ?  204 THR D O   1 
ATOM   4792 C CB  . THR C 1 204 ? -2.202  34.411  0.281   1.00 56.44 ?  204 THR D CB  1 
ATOM   4793 O OG1 . THR C 1 204 ? -2.292  34.683  1.685   1.00 62.29 ?  204 THR D OG1 1 
ATOM   4794 C CG2 . THR C 1 204 ? -2.451  32.927  0.038   1.00 50.29 ?  204 THR D CG2 1 
ATOM   4795 N N   . TYR C 1 205 ? 0.278   33.142  -1.568  1.00 49.16 ?  205 TYR D N   1 
ATOM   4796 C CA  . TYR C 1 205 ? 0.685   32.433  -2.773  1.00 46.72 ?  205 TYR D CA  1 
ATOM   4797 C C   . TYR C 1 205 ? 0.326   30.963  -2.634  1.00 42.58 ?  205 TYR D C   1 
ATOM   4798 O O   . TYR C 1 205 ? 0.845   30.274  -1.748  1.00 45.35 ?  205 TYR D O   1 
ATOM   4799 C CB  . TYR C 1 205 ? 2.186   32.597  -3.021  1.00 44.93 ?  205 TYR D CB  1 
ATOM   4800 C CG  . TYR C 1 205 ? 2.590   34.025  -3.243  1.00 45.86 ?  205 TYR D CG  1 
ATOM   4801 C CD1 . TYR C 1 205 ? 2.288   34.664  -4.437  1.00 44.73 ?  205 TYR D CD1 1 
ATOM   4802 C CD2 . TYR C 1 205 ? 3.263   34.742  -2.262  1.00 46.38 ?  205 TYR D CD2 1 
ATOM   4803 C CE1 . TYR C 1 205 ? 2.642   35.972  -4.655  1.00 45.56 ?  205 TYR D CE1 1 
ATOM   4804 C CE2 . TYR C 1 205 ? 3.629   36.061  -2.471  1.00 47.94 ?  205 TYR D CE2 1 
ATOM   4805 C CZ  . TYR C 1 205 ? 3.315   36.668  -3.675  1.00 47.71 ?  205 TYR D CZ  1 
ATOM   4806 O OH  . TYR C 1 205 ? 3.669   37.973  -3.907  1.00 51.59 ?  205 TYR D OH  1 
ATOM   4807 N N   . ILE C 1 206 ? -0.532  30.480  -3.527  1.00 41.80 ?  206 ILE D N   1 
ATOM   4808 C CA  . ILE C 1 206 ? -1.020  29.109  -3.488  1.00 41.10 ?  206 ILE D CA  1 
ATOM   4809 C C   . ILE C 1 206 ? -0.783  28.484  -4.851  1.00 40.15 ?  206 ILE D C   1 
ATOM   4810 O O   . ILE C 1 206 ? -1.189  29.050  -5.871  1.00 43.30 ?  206 ILE D O   1 
ATOM   4811 C CB  . ILE C 1 206 ? -2.518  29.061  -3.120  1.00 44.47 ?  206 ILE D CB  1 
ATOM   4812 C CG1 . ILE C 1 206 ? -2.705  29.461  -1.662  1.00 43.15 ?  206 ILE D CG1 1 
ATOM   4813 C CG2 . ILE C 1 206 ? -3.095  27.664  -3.350  1.00 42.21 ?  206 ILE D CG2 1 
ATOM   4814 C CD1 . ILE C 1 206 ? -4.112  29.874  -1.342  1.00 46.06 ?  206 ILE D CD1 1 
ATOM   4815 N N   . CYS C 1 207 ? -0.132  27.321  -4.875  1.00 41.31 ?  207 CYS D N   1 
ATOM   4816 C CA  . CYS C 1 207 ? 0.017   26.582  -6.119  1.00 40.56 ?  207 CYS D CA  1 
ATOM   4817 C C   . CYS C 1 207 ? -1.082  25.532  -6.237  1.00 42.87 ?  207 CYS D C   1 
ATOM   4818 O O   . CYS C 1 207 ? -1.426  24.853  -5.263  1.00 42.19 ?  207 CYS D O   1 
ATOM   4819 C CB  . CYS C 1 207 ? 1.394   25.926  -6.227  1.00 42.05 ?  207 CYS D CB  1 
ATOM   4820 S SG  . CYS C 1 207 ? 1.650   24.509  -5.180  1.00 45.77 ?  207 CYS D SG  1 
ATOM   4821 N N   . ASN C 1 208 ? -1.629  25.416  -7.441  1.00 42.12 ?  208 ASN D N   1 
ATOM   4822 C CA  . ASN C 1 208 ? -2.735  24.518  -7.749  1.00 43.16 ?  208 ASN D CA  1 
ATOM   4823 C C   . ASN C 1 208 ? -2.187  23.450  -8.684  1.00 40.49 ?  208 ASN D C   1 
ATOM   4824 O O   . ASN C 1 208 ? -1.815  23.751  -9.822  1.00 39.74 ?  208 ASN D O   1 
ATOM   4825 C CB  . ASN C 1 208 ? -3.875  25.283  -8.414  1.00 40.02 ?  208 ASN D CB  1 
ATOM   4826 C CG  . ASN C 1 208 ? -4.062  26.655  -7.819  1.00 42.87 ?  208 ASN D CG  1 
ATOM   4827 O OD1 . ASN C 1 208 ? -3.995  27.657  -8.525  1.00 44.74 ?  208 ASN D OD1 1 
ATOM   4828 N ND2 . ASN C 1 208 ? -4.267  26.714  -6.510  1.00 46.99 ?  208 ASN D ND2 1 
ATOM   4829 N N   . VAL C 1 209 ? -2.119  22.216  -8.202  1.00 39.53 ?  209 VAL D N   1 
ATOM   4830 C CA  . VAL C 1 209 ? -1.564  21.097  -8.955  1.00 38.13 ?  209 VAL D CA  1 
ATOM   4831 C C   . VAL C 1 209 ? -2.716  20.166  -9.319  1.00 44.36 ?  209 VAL D C   1 
ATOM   4832 O O   . VAL C 1 209 ? -3.458  19.716  -8.439  1.00 45.80 ?  209 VAL D O   1 
ATOM   4833 C CB  . VAL C 1 209 ? -0.476  20.366  -8.151  1.00 42.07 ?  209 VAL D CB  1 
ATOM   4834 C CG1 . VAL C 1 209 ? 0.207   19.282  -8.993  1.00 36.75 ?  209 VAL D CG1 1 
ATOM   4835 C CG2 . VAL C 1 209 ? 0.556   21.361  -7.629  1.00 41.08 ?  209 VAL D CG2 1 
ATOM   4836 N N   . ASN C 1 210 ? -2.881  19.899  -10.618 1.00 42.79 ?  210 ASN D N   1 
ATOM   4837 C CA  . ASN C 1 210 ? -3.881  18.966  -11.131 1.00 43.43 ?  210 ASN D CA  1 
ATOM   4838 C C   . ASN C 1 210 ? -3.205  17.787  -11.813 1.00 42.48 ?  210 ASN D C   1 
ATOM   4839 O O   . ASN C 1 210 ? -2.382  17.973  -12.714 1.00 43.69 ?  210 ASN D O   1 
ATOM   4840 C CB  . ASN C 1 210 ? -4.830  19.641  -12.120 1.00 42.44 ?  210 ASN D CB  1 
ATOM   4841 C CG  . ASN C 1 210 ? -6.157  18.899  -12.260 1.00 48.43 ?  210 ASN D CG  1 
ATOM   4842 O OD1 . ASN C 1 210 ? -6.749  18.447  -11.278 1.00 48.55 ?  210 ASN D OD1 1 
ATOM   4843 N ND2 . ASN C 1 210 ? -6.617  18.759  -13.497 1.00 50.56 ?  210 ASN D ND2 1 
ATOM   4844 N N   . HIS C 1 211 ? -3.575  16.576  -11.405 1.00 44.76 ?  211 HIS D N   1 
ATOM   4845 C CA  . HIS C 1 211 ? -3.073  15.349  -12.023 1.00 42.96 ?  211 HIS D CA  1 
ATOM   4846 C C   . HIS C 1 211 ? -4.286  14.483  -12.356 1.00 47.56 ?  211 HIS D C   1 
ATOM   4847 O O   . HIS C 1 211 ? -4.687  13.628  -11.559 1.00 46.45 ?  211 HIS D O   1 
ATOM   4848 C CB  . HIS C 1 211 ? -2.087  14.627  -11.115 1.00 41.94 ?  211 HIS D CB  1 
ATOM   4849 C CG  . HIS C 1 211 ? -1.481  13.407  -11.733 1.00 41.95 ?  211 HIS D CG  1 
ATOM   4850 N ND1 . HIS C 1 211 ? -1.536  12.165  -11.139 1.00 43.18 ?  211 HIS D ND1 1 
ATOM   4851 C CD2 . HIS C 1 211 ? -0.796  13.240  -12.890 1.00 41.49 ?  211 HIS D CD2 1 
ATOM   4852 C CE1 . HIS C 1 211 ? -0.908  11.286  -11.900 1.00 42.79 ?  211 HIS D CE1 1 
ATOM   4853 N NE2 . HIS C 1 211 ? -0.448  11.912  -12.970 1.00 43.46 ?  211 HIS D NE2 1 
ATOM   4854 N N   . LYS C 1 212 ? -4.864  14.710  -13.539 1.00 47.27 ?  212 LYS D N   1 
ATOM   4855 C CA  . LYS C 1 212 ? -6.080  13.993  -13.916 1.00 48.39 ?  212 LYS D CA  1 
ATOM   4856 C C   . LYS C 1 212 ? -5.907  12.477  -13.994 1.00 49.55 ?  212 LYS D C   1 
ATOM   4857 O O   . LYS C 1 212 ? -6.855  11.763  -13.620 1.00 50.66 ?  212 LYS D O   1 
ATOM   4858 C CB  . LYS C 1 212 ? -6.623  14.549  -15.240 1.00 49.56 ?  212 LYS D CB  1 
ATOM   4859 C CG  . LYS C 1 212 ? -7.861  13.805  -15.755 1.00 54.68 ?  212 LYS D CG  1 
ATOM   4860 C CD  . LYS C 1 212 ? -8.581  14.569  -16.861 1.00 54.83 ?  212 LYS D CD  1 
ATOM   4861 C CE  . LYS C 1 212 ? -10.071 14.234  -16.873 1.00 56.20 ?  212 LYS D CE  1 
ATOM   4862 N NZ  . LYS C 1 212 ? -10.870 15.193  -16.048 1.00 54.32 ?  212 LYS D NZ  1 
ATOM   4863 N N   . PRO C 1 213 ? -4.775  11.915  -14.449 1.00 48.91 ?  213 PRO D N   1 
ATOM   4864 C CA  . PRO C 1 213 ? -4.655  10.444  -14.461 1.00 47.48 ?  213 PRO D CA  1 
ATOM   4865 C C   . PRO C 1 213 ? -4.954  9.773   -13.127 1.00 50.21 ?  213 PRO D C   1 
ATOM   4866 O O   . PRO C 1 213 ? -5.392  8.617   -13.114 1.00 48.75 ?  213 PRO D O   1 
ATOM   4867 C CB  . PRO C 1 213 ? -3.201  10.226  -14.893 1.00 45.31 ?  213 PRO D CB  1 
ATOM   4868 C CG  . PRO C 1 213 ? -2.928  11.371  -15.799 1.00 44.97 ?  213 PRO D CG  1 
ATOM   4869 C CD  . PRO C 1 213 ? -3.644  12.543  -15.163 1.00 45.60 ?  213 PRO D CD  1 
ATOM   4870 N N   . SER C 1 214 ? -4.753  10.456  -12.003 1.00 49.65 ?  214 SER D N   1 
ATOM   4871 C CA  . SER C 1 214 ? -5.024  9.883   -10.693 1.00 48.59 ?  214 SER D CA  1 
ATOM   4872 C C   . SER C 1 214 ? -6.199  10.551  -9.992  1.00 50.29 ?  214 SER D C   1 
ATOM   4873 O O   . SER C 1 214 ? -6.475  10.227  -8.834  1.00 53.42 ?  214 SER D O   1 
ATOM   4874 C CB  . SER C 1 214 ? -3.775  9.972   -9.813  1.00 47.65 ?  214 SER D CB  1 
ATOM   4875 O OG  . SER C 1 214 ? -3.499  11.320  -9.468  1.00 45.64 ?  214 SER D OG  1 
ATOM   4876 N N   . ASN C 1 215 ? -6.889  11.474  -10.666 1.00 50.92 ?  215 ASN D N   1 
ATOM   4877 C CA  . ASN C 1 215 ? -7.987  12.254  -10.083 1.00 52.87 ?  215 ASN D CA  1 
ATOM   4878 C C   . ASN C 1 215 ? -7.538  13.000  -8.831  1.00 55.62 ?  215 ASN D C   1 
ATOM   4879 O O   . ASN C 1 215 ? -8.328  13.238  -7.912  1.00 57.43 ?  215 ASN D O   1 
ATOM   4880 C CB  . ASN C 1 215 ? -9.206  11.378  -9.780  1.00 55.27 ?  215 ASN D CB  1 
ATOM   4881 C CG  . ASN C 1 215 ? -10.128 11.241  -10.972 1.00 56.15 ?  215 ASN D CG  1 
ATOM   4882 O OD1 . ASN C 1 215 ? -10.168 12.113  -11.842 1.00 58.33 ?  215 ASN D OD1 1 
ATOM   4883 N ND2 . ASN C 1 215 ? -10.883 10.151  -11.014 1.00 61.04 ?  215 ASN D ND2 1 
ATOM   4884 N N   . THR C 1 216 ? -6.261  13.370  -8.806  1.00 51.19 ?  216 THR D N   1 
ATOM   4885 C CA  . THR C 1 216 ? -5.649  14.113  -7.717  1.00 50.49 ?  216 THR D CA  1 
ATOM   4886 C C   . THR C 1 216 ? -5.637  15.594  -8.058  1.00 50.00 ?  216 THR D C   1 
ATOM   4887 O O   . THR C 1 216 ? -5.372  15.974  -9.203  1.00 49.62 ?  216 THR D O   1 
ATOM   4888 C CB  . THR C 1 216 ? -4.212  13.638  -7.476  1.00 48.57 ?  216 THR D CB  1 
ATOM   4889 O OG1 . THR C 1 216 ? -4.194  12.217  -7.282  1.00 55.25 ?  216 THR D OG1 1 
ATOM   4890 C CG2 . THR C 1 216 ? -3.578  14.340  -6.274  1.00 47.06 ?  216 THR D CG2 1 
ATOM   4891 N N   . LYS C 1 217 ? -5.913  16.428  -7.065  1.00 46.27 ?  217 LYS D N   1 
ATOM   4892 C CA  . LYS C 1 217 ? -5.788  17.863  -7.264  1.00 45.61 ?  217 LYS D CA  1 
ATOM   4893 C C   . LYS C 1 217 ? -5.389  18.467  -5.926  1.00 47.49 ?  217 LYS D C   1 
ATOM   4894 O O   . LYS C 1 217 ? -6.034  18.200  -4.908  1.00 45.92 ?  217 LYS D O   1 
ATOM   4895 C CB  . LYS C 1 217 ? -7.098  18.451  -7.792  1.00 47.17 ?  217 LYS D CB  1 
ATOM   4896 C CG  . LYS C 1 217 ? -7.314  19.919  -7.537  1.00 47.01 ?  217 LYS D CG  1 
ATOM   4897 C CD  . LYS C 1 217 ? -6.719  20.776  -8.624  1.00 47.81 ?  217 LYS D CD  1 
ATOM   4898 C CE  . LYS C 1 217 ? -7.603  22.000  -8.850  1.00 50.85 ?  217 LYS D CE  1 
ATOM   4899 N NZ  . LYS C 1 217 ? -7.501  22.995  -7.738  1.00 49.03 ?  217 LYS D NZ  1 
ATOM   4900 N N   . VAL C 1 218 ? -4.306  19.242  -5.918  1.00 42.50 ?  218 VAL D N   1 
ATOM   4901 C CA  . VAL C 1 218 ? -3.688  19.700  -4.679  1.00 44.97 ?  218 VAL D CA  1 
ATOM   4902 C C   . VAL C 1 218 ? -3.521  21.209  -4.728  1.00 48.56 ?  218 VAL D C   1 
ATOM   4903 O O   . VAL C 1 218 ? -2.933  21.744  -5.677  1.00 48.88 ?  218 VAL D O   1 
ATOM   4904 C CB  . VAL C 1 218 ? -2.326  19.021  -4.428  1.00 46.87 ?  218 VAL D CB  1 
ATOM   4905 C CG1 . VAL C 1 218 ? -1.786  19.413  -3.067  1.00 46.54 ?  218 VAL D CG1 1 
ATOM   4906 C CG2 . VAL C 1 218 ? -2.445  17.507  -4.528  1.00 47.81 ?  218 VAL D CG2 1 
ATOM   4907 N N   . ASP C 1 219 ? -4.039  21.889  -3.710  1.00 45.57 ?  219 ASP D N   1 
ATOM   4908 C CA  . ASP C 1 219 ? -3.749  23.290  -3.454  1.00 46.77 ?  219 ASP D CA  1 
ATOM   4909 C C   . ASP C 1 219 ? -2.800  23.376  -2.267  1.00 50.08 ?  219 ASP D C   1 
ATOM   4910 O O   . ASP C 1 219 ? -3.005  22.710  -1.248  1.00 48.30 ?  219 ASP D O   1 
ATOM   4911 C CB  . ASP C 1 219 ? -5.024  24.079  -3.166  1.00 45.49 ?  219 ASP D CB  1 
ATOM   4912 C CG  . ASP C 1 219 ? -5.857  24.308  -4.410  1.00 49.59 ?  219 ASP D CG  1 
ATOM   4913 O OD1 . ASP C 1 219 ? -5.337  24.078  -5.524  1.00 49.14 ?  219 ASP D OD1 1 
ATOM   4914 O OD2 . ASP C 1 219 ? -7.037  24.703  -4.268  1.00 49.78 ?  219 ASP D OD2 1 
ATOM   4915 N N   . LYS C 1 220 ? -1.752  24.188  -2.403  1.00 45.99 ?  220 LYS D N   1 
ATOM   4916 C CA  . LYS C 1 220 ? -0.692  24.241  -1.403  1.00 43.51 ?  220 LYS D CA  1 
ATOM   4917 C C   . LYS C 1 220 ? -0.292  25.694  -1.199  1.00 45.83 ?  220 LYS D C   1 
ATOM   4918 O O   . LYS C 1 220 ? 0.275   26.319  -2.102  1.00 44.40 ?  220 LYS D O   1 
ATOM   4919 C CB  . LYS C 1 220 ? 0.503   23.403  -1.845  1.00 46.32 ?  220 LYS D CB  1 
ATOM   4920 C CG  . LYS C 1 220 ? 1.678   23.460  -0.915  1.00 45.44 ?  220 LYS D CG  1 
ATOM   4921 C CD  . LYS C 1 220 ? 1.251   23.088  0.484   1.00 48.70 ?  220 LYS D CD  1 
ATOM   4922 C CE  . LYS C 1 220 ? 2.123   21.977  1.029   1.00 50.94 ?  220 LYS D CE  1 
ATOM   4923 N NZ  . LYS C 1 220 ? 2.193   22.034  2.520   1.00 54.22 ?  220 LYS D NZ  1 
ATOM   4924 N N   . LYS C 1 221 ? -0.585  26.238  -0.025  1.00 45.69 ?  221 LYS D N   1 
ATOM   4925 C CA  . LYS C 1 221 ? -0.175  27.596  0.283   1.00 44.96 ?  221 LYS D CA  1 
ATOM   4926 C C   . LYS C 1 221 ? 1.297   27.568  0.679   1.00 46.96 ?  221 LYS D C   1 
ATOM   4927 O O   . LYS C 1 221 ? 1.728   26.694  1.437   1.00 43.83 ?  221 LYS D O   1 
ATOM   4928 C CB  . LYS C 1 221 ? -1.044  28.169  1.399   1.00 50.77 ?  221 LYS D CB  1 
ATOM   4929 C CG  . LYS C 1 221 ? -0.435  29.290  2.212   1.00 53.17 ?  221 LYS D CG  1 
ATOM   4930 C CD  . LYS C 1 221 ? -1.311  29.565  3.424   1.00 55.58 ?  221 LYS D CD  1 
ATOM   4931 C CE  . LYS C 1 221 ? -1.750  31.029  3.483   1.00 57.34 ?  221 LYS D CE  1 
ATOM   4932 N NZ  . LYS C 1 221 ? -0.637  31.992  3.732   1.00 60.85 ?  221 LYS D NZ  1 
ATOM   4933 N N   . VAL C 1 222 ? 2.080   28.491  0.128   1.00 46.88 ?  222 VAL D N   1 
ATOM   4934 C CA  . VAL C 1 222 ? 3.523   28.525  0.353   1.00 45.33 ?  222 VAL D CA  1 
ATOM   4935 C C   . VAL C 1 222 ? 3.838   29.742  1.205   1.00 47.85 ?  222 VAL D C   1 
ATOM   4936 O O   . VAL C 1 222 ? 3.561   30.879  0.806   1.00 47.53 ?  222 VAL D O   1 
ATOM   4937 C CB  . VAL C 1 222 ? 4.303   28.540  -0.969  1.00 43.00 ?  222 VAL D CB  1 
ATOM   4938 C CG1 . VAL C 1 222 ? 5.795   28.582  -0.703  1.00 40.53 ?  222 VAL D CG1 1 
ATOM   4939 C CG2 . VAL C 1 222 ? 3.962   27.288  -1.776  1.00 42.35 ?  222 VAL D CG2 1 
ATOM   4940 N N   . GLU C 1 223 ? 4.419   29.502  2.381   1.00 51.46 ?  223 GLU D N   1 
ATOM   4941 C CA  . GLU C 1 223 ? 4.660   30.550  3.364   1.00 54.02 ?  223 GLU D CA  1 
ATOM   4942 C C   . GLU C 1 223 ? 6.147   30.723  3.641   1.00 54.15 ?  223 GLU D C   1 
ATOM   4943 O O   . GLU C 1 223 ? 6.904   29.747  3.622   1.00 51.54 ?  223 GLU D O   1 
ATOM   4944 C CB  . GLU C 1 223 ? 3.935   30.244  4.683   1.00 55.98 ?  223 GLU D CB  1 
ATOM   4945 C CG  . GLU C 1 223 ? 2.533   29.688  4.512   1.00 57.23 ?  223 GLU D CG  1 
ATOM   4946 C CD  . GLU C 1 223 ? 1.590   30.220  5.565   1.00 62.93 ?  223 GLU D CD  1 
ATOM   4947 O OE1 . GLU C 1 223 ? 1.656   29.741  6.718   1.00 64.56 ?  223 GLU D OE1 1 
ATOM   4948 O OE2 . GLU C 1 223 ? 0.818   31.150  5.255   1.00 63.97 ?  223 GLU D OE2 1 
ATOM   4949 N N   . PRO C 1 224 ? 6.598   31.957  3.888   1.00 56.80 ?  224 PRO D N   1 
ATOM   4950 C CA  . PRO C 1 224 ? 7.966   32.273  4.311   1.00 58.06 ?  224 PRO D CA  1 
ATOM   4951 C C   . PRO C 1 224 ? 8.380   31.513  5.570   1.00 56.92 ?  224 PRO D C   1 
ATOM   4952 O O   . PRO C 1 224 ? 7.521   31.287  6.420   1.00 59.23 ?  224 PRO D O   1 
ATOM   4953 C CB  . PRO C 1 224 ? 7.917   33.778  4.586   1.00 56.21 ?  224 PRO D CB  1 
ATOM   4954 C CG  . PRO C 1 224 ? 6.717   34.294  3.872   1.00 57.30 ?  224 PRO D CG  1 
ATOM   4955 C CD  . PRO C 1 224 ? 5.848   33.150  3.458   1.00 58.97 ?  224 PRO D CD  1 
ATOM   4956 N N   . SER D 2 1   ? 23.369  0.987   -43.778 1.00 21.70 ?  1   SER G N   1 
ATOM   4957 C CA  . SER D 2 1   ? 22.985  2.125   -44.615 1.00 24.39 ?  1   SER G CA  1 
ATOM   4958 C C   . SER D 2 1   ? 24.133  3.107   -44.654 1.00 24.55 ?  1   SER G C   1 
ATOM   4959 O O   . SER D 2 1   ? 24.986  3.105   -43.769 1.00 23.89 ?  1   SER G O   1 
ATOM   4960 C CB  . SER D 2 1   ? 21.752  2.843   -44.067 1.00 26.06 ?  1   SER G CB  1 
ATOM   4961 O OG  . SER D 2 1   ? 21.809  2.974   -42.659 1.00 29.48 ?  1   SER G OG  1 
ATOM   4962 N N   . PHE D 2 2   ? 24.163  3.958   -45.665 1.00 26.35 ?  2   PHE G N   1 
ATOM   4963 C CA  . PHE D 2 2   ? 25.192  4.982   -45.707 1.00 28.50 ?  2   PHE G CA  1 
ATOM   4964 C C   . PHE D 2 2   ? 24.884  6.031   -44.645 1.00 31.01 ?  2   PHE G C   1 
ATOM   4965 O O   . PHE D 2 2   ? 23.726  6.252   -44.288 1.00 29.80 ?  2   PHE G O   1 
ATOM   4966 C CB  . PHE D 2 2   ? 25.236  5.593   -47.102 1.00 34.55 ?  2   PHE G CB  1 
ATOM   4967 C CG  . PHE D 2 2   ? 25.740  4.627   -48.149 1.00 38.45 ?  2   PHE G CG  1 
ATOM   4968 C CD1 . PHE D 2 2   ? 26.770  3.740   -47.859 1.00 35.73 ?  2   PHE G CD1 1 
ATOM   4969 C CD2 . PHE D 2 2   ? 25.103  4.522   -49.379 1.00 43.62 ?  2   PHE G CD2 1 
ATOM   4970 C CE1 . PHE D 2 2   ? 27.204  2.817   -48.804 1.00 34.79 ?  2   PHE G CE1 1 
ATOM   4971 C CE2 . PHE D 2 2   ? 25.531  3.604   -50.331 1.00 45.97 ?  2   PHE G CE2 1 
ATOM   4972 C CZ  . PHE D 2 2   ? 26.590  2.750   -50.040 1.00 43.25 ?  2   PHE G CZ  1 
ATOM   4973 N N   . GLU D 2 3   ? 25.935  6.636   -44.092 1.00 27.81 ?  3   GLU G N   1 
ATOM   4974 C CA  . GLU D 2 3   ? 25.786  7.662   -43.064 1.00 28.32 ?  3   GLU G CA  1 
ATOM   4975 C C   . GLU D 2 3   ? 25.578  9.048   -43.663 1.00 24.53 ?  3   GLU G C   1 
ATOM   4976 O O   . GLU D 2 3   ? 26.046  9.347   -44.765 1.00 26.01 ?  3   GLU G O   1 
ATOM   4977 C CB  . GLU D 2 3   ? 27.011  7.721   -42.139 1.00 31.17 ?  3   GLU G CB  1 
ATOM   4978 C CG  . GLU D 2 3   ? 27.056  6.620   -41.119 1.00 33.64 ?  3   GLU G CG  1 
ATOM   4979 C CD  . GLU D 2 3   ? 28.246  6.736   -40.193 1.00 38.20 ?  3   GLU G CD  1 
ATOM   4980 O OE1 . GLU D 2 3   ? 29.347  7.125   -40.663 1.00 43.26 ?  3   GLU G OE1 1 
ATOM   4981 O OE2 . GLU D 2 3   ? 28.067  6.465   -38.981 1.00 44.13 ?  3   GLU G OE2 1 
ATOM   4982 N N   . LEU D 2 4   ? 24.889  9.898   -42.907 1.00 20.28 ?  4   LEU G N   1 
ATOM   4983 C CA  . LEU D 2 4   ? 24.787  11.330  -43.202 1.00 19.98 ?  4   LEU G CA  1 
ATOM   4984 C C   . LEU D 2 4   ? 25.385  12.072  -42.026 1.00 23.12 ?  4   LEU G C   1 
ATOM   4985 O O   . LEU D 2 4   ? 24.993  11.820  -40.882 1.00 25.65 ?  4   LEU G O   1 
ATOM   4986 C CB  . LEU D 2 4   ? 23.325  11.752  -43.409 1.00 23.72 ?  4   LEU G CB  1 
ATOM   4987 C CG  . LEU D 2 4   ? 22.592  11.186  -44.611 1.00 23.78 ?  4   LEU G CG  1 
ATOM   4988 C CD1 . LEU D 2 4   ? 21.122  11.652  -44.582 1.00 23.48 ?  4   LEU G CD1 1 
ATOM   4989 C CD2 . LEU D 2 4   ? 23.234  11.577  -45.898 1.00 25.55 ?  4   LEU G CD2 1 
ATOM   4990 N N   . THR D 2 5   ? 26.346  12.972  -42.298 1.00 23.12 ?  5   THR G N   1 
ATOM   4991 C CA  . THR D 2 5   ? 27.055  13.710  -41.258 1.00 23.90 ?  5   THR G CA  1 
ATOM   4992 C C   . THR D 2 5   ? 26.669  15.175  -41.324 1.00 22.18 ?  5   THR G C   1 
ATOM   4993 O O   . THR D 2 5   ? 26.897  15.834  -42.341 1.00 22.82 ?  5   THR G O   1 
ATOM   4994 C CB  . THR D 2 5   ? 28.574  13.553  -41.398 1.00 23.59 ?  5   THR G CB  1 
ATOM   4995 O OG1 . THR D 2 5   ? 28.910  12.164  -41.309 1.00 25.69 ?  5   THR G OG1 1 
ATOM   4996 C CG2 . THR D 2 5   ? 29.279  14.296  -40.288 1.00 23.97 ?  5   THR G CG2 1 
ATOM   4997 N N   . GLN D 2 6   ? 26.082  15.667  -40.245 1.00 20.51 ?  6   GLN G N   1 
ATOM   4998 C CA  . GLN D 2 6   ? 25.749  17.073  -40.091 1.00 22.48 ?  6   GLN G CA  1 
ATOM   4999 C C   . GLN D 2 6   ? 26.186  17.478  -38.692 1.00 24.42 ?  6   GLN G C   1 
ATOM   5000 O O   . GLN D 2 6   ? 26.233  16.631  -37.791 1.00 26.14 ?  6   GLN G O   1 
ATOM   5001 C CB  . GLN D 2 6   ? 24.238  17.320  -40.326 1.00 23.24 ?  6   GLN G CB  1 
ATOM   5002 C CG  . GLN D 2 6   ? 23.267  16.683  -39.311 1.00 20.85 ?  6   GLN G CG  1 
ATOM   5003 C CD  . GLN D 2 6   ? 21.814  17.004  -39.626 1.00 23.15 ?  6   GLN G CD  1 
ATOM   5004 O OE1 . GLN D 2 6   ? 20.985  16.103  -39.793 1.00 23.68 ?  6   GLN G OE1 1 
ATOM   5005 N NE2 . GLN D 2 6   ? 21.505  18.291  -39.728 1.00 21.00 ?  6   GLN G NE2 1 
ATOM   5006 N N   . PRO D 2 7   ? 26.552  18.747  -38.488 1.00 25.08 ?  7   PRO G N   1 
ATOM   5007 C CA  . PRO D 2 7   ? 27.029  19.153  -37.163 1.00 25.07 ?  7   PRO G CA  1 
ATOM   5008 C C   . PRO D 2 7   ? 25.921  19.093  -36.131 1.00 26.75 ?  7   PRO G C   1 
ATOM   5009 O O   . PRO D 2 7   ? 24.731  19.260  -36.454 1.00 21.96 ?  7   PRO G O   1 
ATOM   5010 C CB  . PRO D 2 7   ? 27.522  20.599  -37.389 1.00 26.26 ?  7   PRO G CB  1 
ATOM   5011 C CG  . PRO D 2 7   ? 26.845  21.070  -38.622 1.00 28.35 ?  7   PRO G CG  1 
ATOM   5012 C CD  . PRO D 2 7   ? 26.602  19.838  -39.478 1.00 23.74 ?  7   PRO G CD  1 
ATOM   5013 N N   . PRO D 2 8   ? 26.256  18.841  -34.865 1.00 26.53 ?  8   PRO G N   1 
ATOM   5014 C CA  . PRO D 2 8   ? 25.212  18.815  -33.836 1.00 25.33 ?  8   PRO G CA  1 
ATOM   5015 C C   . PRO D 2 8   ? 24.632  20.180  -33.532 1.00 27.86 ?  8   PRO G C   1 
ATOM   5016 O O   . PRO D 2 8   ? 23.507  20.260  -33.032 1.00 25.55 ?  8   PRO G O   1 
ATOM   5017 C CB  . PRO D 2 8   ? 25.940  18.229  -32.616 1.00 30.35 ?  8   PRO G CB  1 
ATOM   5018 C CG  . PRO D 2 8   ? 27.377  18.485  -32.868 1.00 30.88 ?  8   PRO G CG  1 
ATOM   5019 C CD  . PRO D 2 8   ? 27.570  18.417  -34.340 1.00 29.80 ?  8   PRO G CD  1 
ATOM   5020 N N   . SER D 2 9   ? 25.355  21.250  -33.832 1.00 27.56 ?  9   SER G N   1 
ATOM   5021 C CA  . SER D 2 9   ? 24.940  22.570  -33.395 1.00 28.13 ?  9   SER G CA  1 
ATOM   5022 C C   . SER D 2 9   ? 25.579  23.626  -34.279 1.00 27.06 ?  9   SER G C   1 
ATOM   5023 O O   . SER D 2 9   ? 26.757  23.513  -34.650 1.00 26.22 ?  9   SER G O   1 
ATOM   5024 C CB  . SER D 2 9   ? 25.300  22.771  -31.919 1.00 32.65 ?  9   SER G CB  1 
ATOM   5025 O OG  . SER D 2 9   ? 26.643  23.168  -31.802 1.00 40.05 ?  9   SER G OG  1 
ATOM   5026 N N   . VAL D 2 10  ? 24.774  24.632  -34.637 1.00 23.26 ?  10  VAL G N   1 
ATOM   5027 C CA  . VAL D 2 10  ? 25.214  25.810  -35.376 1.00 25.45 ?  10  VAL G CA  1 
ATOM   5028 C C   . VAL D 2 10  ? 24.608  27.025  -34.690 1.00 27.29 ?  10  VAL G C   1 
ATOM   5029 O O   . VAL D 2 10  ? 23.407  27.037  -34.400 1.00 25.77 ?  10  VAL G O   1 
ATOM   5030 C CB  . VAL D 2 10  ? 24.789  25.752  -36.859 1.00 26.78 ?  10  VAL G CB  1 
ATOM   5031 C CG1 . VAL D 2 10  ? 24.870  27.100  -37.507 1.00 25.82 ?  10  VAL G CG1 1 
ATOM   5032 C CG2 . VAL D 2 10  ? 25.645  24.787  -37.632 1.00 25.80 ?  10  VAL G CG2 1 
ATOM   5033 N N   . SER D 2 11  ? 25.436  28.025  -34.386 1.00 25.62 ?  11  SER G N   1 
ATOM   5034 C CA  . SER D 2 11  ? 24.946  29.302  -33.871 1.00 25.53 ?  11  SER G CA  1 
ATOM   5035 C C   . SER D 2 11  ? 25.026  30.361  -34.956 1.00 28.48 ?  11  SER G C   1 
ATOM   5036 O O   . SER D 2 11  ? 26.025  30.437  -35.685 1.00 27.40 ?  11  SER G O   1 
ATOM   5037 C CB  . SER D 2 11  ? 25.749  29.801  -32.659 1.00 30.75 ?  11  SER G CB  1 
ATOM   5038 O OG  . SER D 2 11  ? 25.468  29.031  -31.507 1.00 39.05 ?  11  SER G OG  1 
ATOM   5039 N N   . VAL D 2 12  ? 23.988  31.198  -35.027 1.00 26.87 ?  12  VAL G N   1 
ATOM   5040 C CA  . VAL D 2 12  ? 23.931  32.314  -35.967 1.00 23.87 ?  12  VAL G CA  1 
ATOM   5041 C C   . VAL D 2 12  ? 23.309  33.518  -35.265 1.00 28.72 ?  12  VAL G C   1 
ATOM   5042 O O   . VAL D 2 12  ? 22.384  33.369  -34.462 1.00 26.79 ?  12  VAL G O   1 
ATOM   5043 C CB  . VAL D 2 12  ? 23.138  31.915  -37.229 1.00 26.15 ?  12  VAL G CB  1 
ATOM   5044 C CG1 . VAL D 2 12  ? 21.661  31.580  -36.892 1.00 25.38 ?  12  VAL G CG1 1 
ATOM   5045 C CG2 . VAL D 2 12  ? 23.278  32.966  -38.319 1.00 26.51 ?  12  VAL G CG2 1 
ATOM   5046 N N   . SER D 2 13  ? 23.836  34.727  -35.555 1.00 27.49 ?  13  SER G N   1 
ATOM   5047 C CA  . SER D 2 13  ? 23.214  35.940  -35.027 1.00 26.23 ?  13  SER G CA  1 
ATOM   5048 C C   . SER D 2 13  ? 22.031  36.345  -35.909 1.00 24.99 ?  13  SER G C   1 
ATOM   5049 O O   . SER D 2 13  ? 22.042  36.100  -37.116 1.00 25.30 ?  13  SER G O   1 
ATOM   5050 C CB  . SER D 2 13  ? 24.227  37.090  -34.989 1.00 28.55 ?  13  SER G CB  1 
ATOM   5051 O OG  . SER D 2 13  ? 25.385  36.740  -34.236 1.00 28.69 ?  13  SER G OG  1 
ATOM   5052 N N   . PRO D 2 14  ? 21.008  37.000  -35.350 1.00 28.22 ?  14  PRO G N   1 
ATOM   5053 C CA  . PRO D 2 14  ? 19.901  37.464  -36.192 1.00 25.48 ?  14  PRO G CA  1 
ATOM   5054 C C   . PRO D 2 14  ? 20.415  38.341  -37.330 1.00 26.14 ?  14  PRO G C   1 
ATOM   5055 O O   . PRO D 2 14  ? 21.286  39.194  -37.136 1.00 26.86 ?  14  PRO G O   1 
ATOM   5056 C CB  . PRO D 2 14  ? 19.021  38.260  -35.219 1.00 29.12 ?  14  PRO G CB  1 
ATOM   5057 C CG  . PRO D 2 14  ? 19.356  37.736  -33.872 1.00 30.08 ?  14  PRO G CG  1 
ATOM   5058 C CD  . PRO D 2 14  ? 20.800  37.331  -33.926 1.00 28.40 ?  14  PRO G CD  1 
ATOM   5059 N N   . GLY D 2 15  ? 19.892  38.106  -38.533 1.00 25.42 ?  15  GLY G N   1 
ATOM   5060 C CA  . GLY D 2 15  ? 20.327  38.843  -39.705 1.00 25.04 ?  15  GLY G CA  1 
ATOM   5061 C C   . GLY D 2 15  ? 21.604  38.354  -40.348 1.00 26.77 ?  15  GLY G C   1 
ATOM   5062 O O   . GLY D 2 15  ? 22.019  38.923  -41.369 1.00 25.89 ?  15  GLY G O   1 
ATOM   5063 N N   . GLN D 2 16  ? 22.223  37.310  -39.813 1.00 25.02 ?  16  GLN G N   1 
ATOM   5064 C CA  . GLN D 2 16  ? 23.455  36.762  -40.357 1.00 22.88 ?  16  GLN G CA  1 
ATOM   5065 C C   . GLN D 2 16  ? 23.161  35.436  -41.047 1.00 25.46 ?  16  GLN G C   1 
ATOM   5066 O O   . GLN D 2 16  ? 22.069  34.862  -40.921 1.00 25.14 ?  16  GLN G O   1 
ATOM   5067 C CB  . GLN D 2 16  ? 24.480  36.601  -39.232 1.00 28.23 ?  16  GLN G CB  1 
ATOM   5068 C CG  . GLN D 2 16  ? 24.823  37.965  -38.626 1.00 29.85 ?  16  GLN G CG  1 
ATOM   5069 C CD  . GLN D 2 16  ? 26.144  37.991  -37.871 1.00 35.58 ?  16  GLN G CD  1 
ATOM   5070 O OE1 . GLN D 2 16  ? 26.710  36.942  -37.539 1.00 37.76 ?  16  GLN G OE1 1 
ATOM   5071 N NE2 . GLN D 2 16  ? 26.612  39.195  -37.549 1.00 34.84 ?  16  GLN G NE2 1 
ATOM   5072 N N   . THR D 2 17  ? 24.140  34.955  -41.806 1.00 23.22 ?  17  THR G N   1 
ATOM   5073 C CA  . THR D 2 17  ? 23.954  33.748  -42.614 1.00 25.23 ?  17  THR G CA  1 
ATOM   5074 C C   . THR D 2 17  ? 24.355  32.500  -41.833 1.00 25.51 ?  17  THR G C   1 
ATOM   5075 O O   . THR D 2 17  ? 25.481  32.421  -41.323 1.00 26.63 ?  17  THR G O   1 
ATOM   5076 C CB  . THR D 2 17  ? 24.783  33.858  -43.894 1.00 26.83 ?  17  THR G CB  1 
ATOM   5077 O OG1 . THR D 2 17  ? 24.361  35.021  -44.628 1.00 27.58 ?  17  THR G OG1 1 
ATOM   5078 C CG2 . THR D 2 17  ? 24.626  32.614  -44.758 1.00 24.48 ?  17  THR G CG2 1 
ATOM   5079 N N   . ALA D 2 18  ? 23.443  31.523  -41.755 1.00 24.25 ?  18  ALA G N   1 
ATOM   5080 C CA  . ALA D 2 18  ? 23.730  30.214  -41.183 1.00 22.44 ?  18  ALA G CA  1 
ATOM   5081 C C   . ALA D 2 18  ? 24.017  29.229  -42.310 1.00 22.42 ?  18  ALA G C   1 
ATOM   5082 O O   . ALA D 2 18  ? 23.352  29.251  -43.344 1.00 23.99 ?  18  ALA G O   1 
ATOM   5083 C CB  . ALA D 2 18  ? 22.544  29.701  -40.352 1.00 22.98 ?  18  ALA G CB  1 
ATOM   5084 N N   . ARG D 2 19  ? 24.977  28.338  -42.099 1.00 20.78 ?  19  ARG G N   1 
ATOM   5085 C CA  . ARG D 2 19  ? 25.262  27.292  -43.071 1.00 19.32 ?  19  ARG G CA  1 
ATOM   5086 C C   . ARG D 2 19  ? 25.291  25.954  -42.344 1.00 22.51 ?  19  ARG G C   1 
ATOM   5087 O O   . ARG D 2 19  ? 26.087  25.768  -41.417 1.00 22.38 ?  19  ARG G O   1 
ATOM   5088 C CB  . ARG D 2 19  ? 26.596  27.556  -43.779 1.00 21.24 ?  19  ARG G CB  1 
ATOM   5089 C CG  . ARG D 2 19  ? 26.535  28.735  -44.761 1.00 23.01 ?  19  ARG G CG  1 
ATOM   5090 C CD  . ARG D 2 19  ? 27.834  28.879  -45.583 1.00 23.13 ?  19  ARG G CD  1 
ATOM   5091 N NE  . ARG D 2 19  ? 27.760  30.113  -46.360 1.00 24.01 ?  19  ARG G NE  1 
ATOM   5092 C CZ  . ARG D 2 19  ? 28.333  31.254  -46.008 1.00 25.52 ?  19  ARG G CZ  1 
ATOM   5093 N NH1 . ARG D 2 19  ? 29.102  31.332  -44.944 1.00 24.23 ?  19  ARG G NH1 1 
ATOM   5094 N NH2 . ARG D 2 19  ? 28.133  32.342  -46.754 1.00 25.18 ?  19  ARG G NH2 1 
ATOM   5095 N N   . ILE D 2 20  ? 24.437  25.023  -42.767 1.00 21.76 ?  20  ILE G N   1 
ATOM   5096 C CA  . ILE D 2 20  ? 24.361  23.708  -42.156 1.00 21.01 ?  20  ILE G CA  1 
ATOM   5097 C C   . ILE D 2 20  ? 24.733  22.695  -43.224 1.00 24.98 ?  20  ILE G C   1 
ATOM   5098 O O   . ILE D 2 20  ? 23.999  22.523  -44.205 1.00 22.74 ?  20  ILE G O   1 
ATOM   5099 C CB  . ILE D 2 20  ? 22.975  23.399  -41.568 1.00 23.24 ?  20  ILE G CB  1 
ATOM   5100 C CG1 . ILE D 2 20  ? 22.517  24.506  -40.602 1.00 24.31 ?  20  ILE G CG1 1 
ATOM   5101 C CG2 . ILE D 2 20  ? 23.023  22.095  -40.812 1.00 24.91 ?  20  ILE G CG2 1 
ATOM   5102 C CD1 . ILE D 2 20  ? 21.685  25.594  -41.245 1.00 31.99 ?  20  ILE G CD1 1 
ATOM   5103 N N   . THR D 2 21  ? 25.853  22.008  -43.032 1.00 22.95 ?  21  THR G N   1 
ATOM   5104 C CA  . THR D 2 21  ? 26.245  21.014  -44.016 1.00 18.88 ?  21  THR G CA  1 
ATOM   5105 C C   . THR D 2 21  ? 25.703  19.629  -43.680 1.00 22.59 ?  21  THR G C   1 
ATOM   5106 O O   . THR D 2 21  ? 25.410  19.292  -42.527 1.00 21.97 ?  21  THR G O   1 
ATOM   5107 C CB  . THR D 2 21  ? 27.766  20.947  -44.149 1.00 20.94 ?  21  THR G CB  1 
ATOM   5108 O OG1 . THR D 2 21  ? 28.347  20.763  -42.846 1.00 22.39 ?  21  THR G OG1 1 
ATOM   5109 C CG2 . THR D 2 21  ? 28.266  22.267  -44.765 1.00 22.68 ?  21  THR G CG2 1 
ATOM   5110 N N   . CYS D 2 22  ? 25.592  18.824  -44.729 1.00 20.36 ?  22  CYS G N   1 
ATOM   5111 C CA  . CYS D 2 22  ? 25.191  17.429  -44.627 1.00 19.43 ?  22  CYS G CA  1 
ATOM   5112 C C   . CYS D 2 22  ? 25.997  16.664  -45.662 1.00 23.04 ?  22  CYS G C   1 
ATOM   5113 O O   . CYS D 2 22  ? 25.862  16.929  -46.860 1.00 23.94 ?  22  CYS G O   1 
ATOM   5114 C CB  . CYS D 2 22  ? 23.686  17.276  -44.875 1.00 21.24 ?  22  CYS G CB  1 
ATOM   5115 S SG  . CYS D 2 22  ? 23.158  15.560  -44.712 1.00 25.88 ?  22  CYS G SG  1 
ATOM   5116 N N   . SER D 2 23  ? 26.814  15.707  -45.215 1.00 22.08 ?  23  SER G N   1 
ATOM   5117 C CA  . SER D 2 23  ? 27.725  14.988  -46.102 1.00 21.87 ?  23  SER G CA  1 
ATOM   5118 C C   . SER D 2 23  ? 27.514  13.490  -46.032 1.00 24.16 ?  23  SER G C   1 
ATOM   5119 O O   . SER D 2 23  ? 27.247  12.943  -44.960 1.00 25.72 ?  23  SER G O   1 
ATOM   5120 C CB  . SER D 2 23  ? 29.216  15.256  -45.749 1.00 24.12 ?  23  SER G CB  1 
ATOM   5121 O OG  . SER D 2 23  ? 29.543  16.620  -45.902 1.00 33.39 ?  23  SER G OG  1 
ATOM   5122 N N   . GLY D 2 24  ? 27.725  12.835  -47.168 1.00 26.16 ?  24  GLY G N   1 
ATOM   5123 C CA  . GLY D 2 24  ? 27.693  11.383  -47.251 1.00 31.21 ?  24  GLY G CA  1 
ATOM   5124 C C   . GLY D 2 24  ? 28.029  10.961  -48.667 1.00 36.92 ?  24  GLY G C   1 
ATOM   5125 O O   . GLY D 2 24  ? 27.766  11.700  -49.613 1.00 35.91 ?  24  GLY G O   1 
ATOM   5126 N N   . ASP D 2 25  ? 28.629  9.797   -48.858 1.00 46.93 ?  25  ASP G N   1 
ATOM   5127 C CA  . ASP D 2 25  ? 29.071  9.465   -50.207 1.00 45.24 ?  25  ASP G CA  1 
ATOM   5128 C C   . ASP D 2 25  ? 27.982  8.810   -51.035 1.00 45.97 ?  25  ASP G C   1 
ATOM   5129 O O   . ASP D 2 25  ? 28.245  8.403   -52.169 1.00 56.10 ?  25  ASP G O   1 
ATOM   5130 C CB  . ASP D 2 25  ? 30.332  8.603   -50.160 1.00 47.53 ?  25  ASP G CB  1 
ATOM   5131 C CG  . ASP D 2 25  ? 30.236  7.514   -49.148 1.00 48.78 ?  25  ASP G CG  1 
ATOM   5132 O OD1 . ASP D 2 25  ? 29.200  6.807   -49.145 1.00 52.55 ?  25  ASP G OD1 1 
ATOM   5133 O OD2 . ASP D 2 25  ? 31.181  7.381   -48.343 1.00 53.41 ?  25  ASP G OD2 1 
ATOM   5134 N N   . ALA D 2 26  ? 26.762  8.722   -50.507 1.00 39.69 ?  26  ALA G N   1 
ATOM   5135 C CA  . ALA D 2 26  ? 25.601  8.471   -51.342 1.00 45.34 ?  26  ALA G CA  1 
ATOM   5136 C C   . ALA D 2 26  ? 25.052  9.744   -51.972 1.00 39.97 ?  26  ALA G C   1 
ATOM   5137 O O   . ALA D 2 26  ? 24.233  9.665   -52.894 1.00 40.02 ?  26  ALA G O   1 
ATOM   5138 C CB  . ALA D 2 26  ? 24.491  7.808   -50.525 1.00 46.73 ?  26  ALA G CB  1 
ATOM   5139 N N   . LEU D 2 27  ? 25.458  10.915  -51.488 1.00 35.03 ?  27  LEU G N   1 
ATOM   5140 C CA  . LEU D 2 27  ? 24.765  12.118  -51.934 1.00 35.60 ?  27  LEU G CA  1 
ATOM   5141 C C   . LEU D 2 27  ? 24.981  12.454  -53.405 1.00 35.59 ?  27  LEU G C   1 
ATOM   5142 O O   . LEU D 2 27  ? 24.065  13.007  -54.030 1.00 34.54 ?  27  LEU G O   1 
ATOM   5143 C CB  . LEU D 2 27  ? 25.135  13.325  -51.061 1.00 36.10 ?  27  LEU G CB  1 
ATOM   5144 C CG  . LEU D 2 27  ? 24.662  13.124  -49.610 1.00 34.95 ?  27  LEU G CG  1 
ATOM   5145 C CD1 . LEU D 2 27  ? 24.779  14.411  -48.804 1.00 31.70 ?  27  LEU G CD1 1 
ATOM   5146 C CD2 . LEU D 2 27  ? 23.260  12.549  -49.528 1.00 34.06 ?  27  LEU G CD2 1 
ATOM   5147 N N   . PRO D 2 28  ? 26.150  12.181  -54.038 1.00 35.65 ?  28  PRO G N   1 
ATOM   5148 C CA  . PRO D 2 28  ? 26.270  12.449  -55.462 1.00 36.16 ?  28  PRO G CA  1 
ATOM   5149 C C   . PRO D 2 28  ? 25.205  11.723  -56.296 1.00 39.45 ?  28  PRO G C   1 
ATOM   5150 O O   . PRO D 2 28  ? 24.942  12.163  -57.376 1.00 41.97 ?  28  PRO G O   1 
ATOM   5151 C CB  . PRO D 2 28  ? 27.666  11.932  -55.836 1.00 38.67 ?  28  PRO G CB  1 
ATOM   5152 C CG  . PRO D 2 28  ? 28.096  11.092  -54.667 1.00 41.04 ?  28  PRO G CG  1 
ATOM   5153 C CD  . PRO D 2 28  ? 27.457  11.776  -53.485 1.00 37.95 ?  28  PRO G CD  1 
ATOM   5154 N N   . LYS D 2 29  ? 24.607  10.656  -55.761 1.00 33.13 ?  29  LYS G N   1 
ATOM   5155 C CA  . LYS D 2 29  ? 23.646  9.850   -56.554 1.00 36.90 ?  29  LYS G CA  1 
ATOM   5156 C C   . LYS D 2 29  ? 22.227  9.921   -55.977 1.00 37.92 ?  29  LYS G C   1 
ATOM   5157 O O   . LYS D 2 29  ? 21.320  9.441   -56.648 1.00 41.03 ?  29  LYS G O   1 
ATOM   5158 C CB  . LYS D 2 29  ? 24.111  8.393   -56.603 1.00 37.75 ?  29  LYS G CB  1 
ATOM   5159 C CG  . LYS D 2 29  ? 25.345  8.151   -57.460 1.00 47.13 ?  29  LYS G CG  1 
ATOM   5160 C CD  . LYS D 2 29  ? 25.311  8.917   -58.764 1.00 50.20 ?  29  LYS G CD  1 
ATOM   5161 C CE  . LYS D 2 29  ? 26.458  8.575   -59.693 1.00 48.56 ?  29  LYS G CE  1 
ATOM   5162 N NZ  . LYS D 2 29  ? 27.476  9.651   -59.721 1.00 55.52 ?  29  LYS G NZ  1 
ATOM   5163 N N   . GLN D 2 30  ? 22.052  10.497  -54.793 1.00 30.89 ?  30  GLN G N   1 
ATOM   5164 C CA  . GLN D 2 30  ? 20.705  10.491  -54.170 1.00 29.14 ?  30  GLN G CA  1 
ATOM   5165 C C   . GLN D 2 30  ? 20.282  11.911  -53.790 1.00 29.05 ?  30  GLN G C   1 
ATOM   5166 O O   . GLN D 2 30  ? 21.158  12.737  -53.584 1.00 27.65 ?  30  GLN G O   1 
ATOM   5167 C CB  . GLN D 2 30  ? 20.701  9.567   -52.956 1.00 33.05 ?  30  GLN G CB  1 
ATOM   5168 C CG  . GLN D 2 30  ? 20.876  8.094   -53.301 1.00 35.17 ?  30  GLN G CG  1 
ATOM   5169 C CD  . GLN D 2 30  ? 19.761  7.464   -54.106 1.00 37.33 ?  30  GLN G CD  1 
ATOM   5170 O OE1 . GLN D 2 30  ? 18.612  7.897   -54.088 1.00 37.25 ?  30  GLN G OE1 1 
ATOM   5171 N NE2 . GLN D 2 30  ? 20.095  6.404   -54.821 1.00 37.08 ?  30  GLN G NE2 1 
ATOM   5172 N N   . TYR D 2 31  ? 18.973  12.152  -53.712 1.00 27.46 ?  31  TYR G N   1 
ATOM   5173 C CA  . TYR D 2 31  ? 18.479  13.461  -53.271 1.00 26.37 ?  31  TYR G CA  1 
ATOM   5174 C C   . TYR D 2 31  ? 18.636  13.625  -51.763 1.00 24.54 ?  31  TYR G C   1 
ATOM   5175 O O   . TYR D 2 31  ? 18.622  12.650  -51.005 1.00 24.59 ?  31  TYR G O   1 
ATOM   5176 C CB  . TYR D 2 31  ? 16.998  13.599  -53.627 1.00 26.11 ?  31  TYR G CB  1 
ATOM   5177 C CG  . TYR D 2 31  ? 16.747  13.845  -55.085 1.00 28.19 ?  31  TYR G CG  1 
ATOM   5178 C CD1 . TYR D 2 31  ? 17.401  14.885  -55.761 1.00 29.61 ?  31  TYR G CD1 1 
ATOM   5179 C CD2 . TYR D 2 31  ? 15.868  13.043  -55.801 1.00 30.58 ?  31  TYR G CD2 1 
ATOM   5180 C CE1 . TYR D 2 31  ? 17.164  15.123  -57.095 1.00 30.43 ?  31  TYR G CE1 1 
ATOM   5181 C CE2 . TYR D 2 31  ? 15.625  13.276  -57.136 1.00 32.06 ?  31  TYR G CE2 1 
ATOM   5182 C CZ  . TYR D 2 31  ? 16.273  14.315  -57.779 1.00 32.26 ?  31  TYR G CZ  1 
ATOM   5183 O OH  . TYR D 2 31  ? 16.035  14.540  -59.110 1.00 37.81 ?  31  TYR G OH  1 
ATOM   5184 N N   . VAL D 2 32  ? 18.720  14.876  -51.315 1.00 22.57 ?  32  VAL G N   1 
ATOM   5185 C CA  . VAL D 2 32  ? 18.719  15.213  -49.890 1.00 21.54 ?  32  VAL G CA  1 
ATOM   5186 C C   . VAL D 2 32  ? 17.436  15.969  -49.584 1.00 22.56 ?  32  VAL G C   1 
ATOM   5187 O O   . VAL D 2 32  ? 16.981  16.793  -50.387 1.00 23.55 ?  32  VAL G O   1 
ATOM   5188 C CB  . VAL D 2 32  ? 19.936  16.063  -49.468 1.00 26.96 ?  32  VAL G CB  1 
ATOM   5189 C CG1 . VAL D 2 32  ? 19.867  16.400  -47.988 1.00 25.98 ?  32  VAL G CG1 1 
ATOM   5190 C CG2 . VAL D 2 32  ? 21.215  15.296  -49.702 1.00 28.74 ?  32  VAL G CG2 1 
ATOM   5191 N N   . TYR D 2 33  ? 16.885  15.722  -48.406 1.00 20.53 ?  33  TYR G N   1 
ATOM   5192 C CA  . TYR D 2 33  ? 15.702  16.401  -47.901 1.00 20.34 ?  33  TYR G CA  1 
ATOM   5193 C C   . TYR D 2 33  ? 16.041  17.042  -46.567 1.00 21.75 ?  33  TYR G C   1 
ATOM   5194 O O   . TYR D 2 33  ? 16.836  16.489  -45.804 1.00 21.65 ?  33  TYR G O   1 
ATOM   5195 C CB  . TYR D 2 33  ? 14.537  15.387  -47.759 1.00 18.66 ?  33  TYR G CB  1 
ATOM   5196 C CG  . TYR D 2 33  ? 14.257  14.689  -49.079 1.00 20.25 ?  33  TYR G CG  1 
ATOM   5197 C CD1 . TYR D 2 33  ? 15.019  13.586  -49.497 1.00 20.48 ?  33  TYR G CD1 1 
ATOM   5198 C CD2 . TYR D 2 33  ? 13.272  15.178  -49.932 1.00 22.18 ?  33  TYR G CD2 1 
ATOM   5199 C CE1 . TYR D 2 33  ? 14.773  12.963  -50.717 1.00 23.64 ?  33  TYR G CE1 1 
ATOM   5200 C CE2 . TYR D 2 33  ? 13.013  14.567  -51.157 1.00 22.20 ?  33  TYR G CE2 1 
ATOM   5201 C CZ  . TYR D 2 33  ? 13.779  13.473  -51.546 1.00 23.02 ?  33  TYR G CZ  1 
ATOM   5202 O OH  . TYR D 2 33  ? 13.534  12.874  -52.744 1.00 24.01 ?  33  TYR G OH  1 
ATOM   5203 N N   . TRP D 2 34  ? 15.497  18.244  -46.304 1.00 20.13 ?  34  TRP G N   1 
ATOM   5204 C CA  . TRP D 2 34  ? 15.741  18.951  -45.048 1.00 19.59 ?  34  TRP G CA  1 
ATOM   5205 C C   . TRP D 2 34  ? 14.419  19.164  -44.326 1.00 21.91 ?  34  TRP G C   1 
ATOM   5206 O O   . TRP D 2 34  ? 13.437  19.591  -44.942 1.00 22.73 ?  34  TRP G O   1 
ATOM   5207 C CB  . TRP D 2 34  ? 16.418  20.324  -45.264 1.00 19.17 ?  34  TRP G CB  1 
ATOM   5208 C CG  . TRP D 2 34  ? 17.874  20.266  -45.610 1.00 20.63 ?  34  TRP G CG  1 
ATOM   5209 C CD1 . TRP D 2 34  ? 18.424  20.351  -46.859 1.00 21.71 ?  34  TRP G CD1 1 
ATOM   5210 C CD2 . TRP D 2 34  ? 18.977  20.175  -44.691 1.00 18.33 ?  34  TRP G CD2 1 
ATOM   5211 N NE1 . TRP D 2 34  ? 19.803  20.284  -46.782 1.00 19.28 ?  34  TRP G NE1 1 
ATOM   5212 C CE2 . TRP D 2 34  ? 20.161  20.150  -45.465 1.00 18.14 ?  34  TRP G CE2 1 
ATOM   5213 C CE3 . TRP D 2 34  ? 19.071  20.044  -43.301 1.00 18.40 ?  34  TRP G CE3 1 
ATOM   5214 C CZ2 . TRP D 2 34  ? 21.431  20.070  -44.894 1.00 20.68 ?  34  TRP G CZ2 1 
ATOM   5215 C CZ3 . TRP D 2 34  ? 20.364  19.969  -42.726 1.00 19.50 ?  34  TRP G CZ3 1 
ATOM   5216 C CH2 . TRP D 2 34  ? 21.508  19.980  -43.529 1.00 20.74 ?  34  TRP G CH2 1 
ATOM   5217 N N   . TYR D 2 35  ? 14.394  18.859  -43.026 1.00 20.87 ?  35  TYR G N   1 
ATOM   5218 C CA  . TYR D 2 35  ? 13.232  19.071  -42.171 1.00 19.38 ?  35  TYR G CA  1 
ATOM   5219 C C   . TYR D 2 35  ? 13.597  20.053  -41.079 1.00 23.27 ?  35  TYR G C   1 
ATOM   5220 O O   . TYR D 2 35  ? 14.698  19.999  -40.521 1.00 23.44 ?  35  TYR G O   1 
ATOM   5221 C CB  . TYR D 2 35  ? 12.737  17.765  -41.526 1.00 21.16 ?  35  TYR G CB  1 
ATOM   5222 C CG  . TYR D 2 35  ? 12.441  16.753  -42.584 1.00 22.62 ?  35  TYR G CG  1 
ATOM   5223 C CD1 . TYR D 2 35  ? 11.179  16.684  -43.182 1.00 19.55 ?  35  TYR G CD1 1 
ATOM   5224 C CD2 . TYR D 2 35  ? 13.443  15.890  -43.026 1.00 22.78 ?  35  TYR G CD2 1 
ATOM   5225 C CE1 . TYR D 2 35  ? 10.923  15.766  -44.186 1.00 20.37 ?  35  TYR G CE1 1 
ATOM   5226 C CE2 . TYR D 2 35  ? 13.199  14.959  -44.020 1.00 23.44 ?  35  TYR G CE2 1 
ATOM   5227 C CZ  . TYR D 2 35  ? 11.942  14.910  -44.593 1.00 20.77 ?  35  TYR G CZ  1 
ATOM   5228 O OH  . TYR D 2 35  ? 11.712  14.020  -45.603 1.00 20.65 ?  35  TYR G OH  1 
ATOM   5229 N N   . GLN D 2 36  ? 12.661  20.928  -40.769 1.00 19.80 ?  36  GLN G N   1 
ATOM   5230 C CA  . GLN D 2 36  ? 12.793  21.866  -39.668 1.00 20.53 ?  36  GLN G CA  1 
ATOM   5231 C C   . GLN D 2 36  ? 11.856  21.404  -38.567 1.00 23.02 ?  36  GLN G C   1 
ATOM   5232 O O   . GLN D 2 36  ? 10.684  21.145  -38.835 1.00 22.67 ?  36  GLN G O   1 
ATOM   5233 C CB  . GLN D 2 36  ? 12.413  23.281  -40.123 1.00 22.56 ?  36  GLN G CB  1 
ATOM   5234 C CG  . GLN D 2 36  ? 12.404  24.318  -39.010 1.00 23.87 ?  36  GLN G CG  1 
ATOM   5235 C CD  . GLN D 2 36  ? 11.780  25.621  -39.464 1.00 26.41 ?  36  GLN G CD  1 
ATOM   5236 O OE1 . GLN D 2 36  ? 12.472  26.646  -39.620 1.00 28.56 ?  36  GLN G OE1 1 
ATOM   5237 N NE2 . GLN D 2 36  ? 10.475  25.592  -39.701 1.00 25.31 ?  36  GLN G NE2 1 
ATOM   5238 N N   . GLN D 2 37  ? 12.352  21.307  -37.338 1.00 20.65 ?  37  GLN G N   1 
ATOM   5239 C CA  . GLN D 2 37  ? 11.483  20.937  -36.225 1.00 23.63 ?  37  GLN G CA  1 
ATOM   5240 C C   . GLN D 2 37  ? 11.632  21.962  -35.112 1.00 27.52 ?  37  GLN G C   1 
ATOM   5241 O O   . GLN D 2 37  ? 12.696  22.073  -34.497 1.00 25.74 ?  37  GLN G O   1 
ATOM   5242 C CB  . GLN D 2 37  ? 11.795  19.531  -35.707 1.00 24.64 ?  37  GLN G CB  1 
ATOM   5243 C CG  . GLN D 2 37  ? 10.838  19.120  -34.599 1.00 23.74 ?  37  GLN G CG  1 
ATOM   5244 C CD  . GLN D 2 37  ? 11.078  17.709  -34.113 1.00 26.00 ?  37  GLN G CD  1 
ATOM   5245 O OE1 . GLN D 2 37  ? 12.221  17.280  -34.003 1.00 26.32 ?  37  GLN G OE1 1 
ATOM   5246 N NE2 . GLN D 2 37  ? 10.011  17.011  -33.739 1.00 25.24 ?  37  GLN G NE2 1 
ATOM   5247 N N   . LYS D 2 38  ? 10.580  22.701  -34.859 1.00 31.33 ?  38  LYS G N   1 
ATOM   5248 C CA  . LYS D 2 38  ? 10.550  23.611  -33.725 1.00 34.15 ?  38  LYS G CA  1 
ATOM   5249 C C   . LYS D 2 38  ? 10.046  22.882  -32.482 1.00 36.22 ?  38  LYS G C   1 
ATOM   5250 O O   . LYS D 2 38  ? 9.420   21.825  -32.578 1.00 35.90 ?  38  LYS G O   1 
ATOM   5251 C CB  . LYS D 2 38  ? 9.667   24.807  -34.059 1.00 33.86 ?  38  LYS G CB  1 
ATOM   5252 C CG  . LYS D 2 38  ? 10.200  25.573  -35.243 1.00 35.19 ?  38  LYS G CG  1 
ATOM   5253 C CD  . LYS D 2 38  ? 9.203   26.556  -35.789 1.00 41.48 ?  38  LYS G CD  1 
ATOM   5254 C CE  . LYS D 2 38  ? 9.907   27.760  -36.343 1.00 37.32 ?  38  LYS G CE  1 
ATOM   5255 N NZ  . LYS D 2 38  ? 9.060   28.587  -37.258 1.00 42.03 ?  38  LYS G NZ  1 
ATOM   5256 N N   . PRO D 2 39  ? 10.324  23.406  -31.288 1.00 41.73 ?  39  PRO G N   1 
ATOM   5257 C CA  . PRO D 2 39  ? 10.032  22.640  -30.066 1.00 42.60 ?  39  PRO G CA  1 
ATOM   5258 C C   . PRO D 2 39  ? 8.549   22.350  -29.893 1.00 46.06 ?  39  PRO G C   1 
ATOM   5259 O O   . PRO D 2 39  ? 7.700   23.237  -30.011 1.00 43.95 ?  39  PRO G O   1 
ATOM   5260 C CB  . PRO D 2 39  ? 10.569  23.551  -28.951 1.00 48.53 ?  39  PRO G CB  1 
ATOM   5261 C CG  . PRO D 2 39  ? 10.714  24.898  -29.593 1.00 45.16 ?  39  PRO G CG  1 
ATOM   5262 C CD  . PRO D 2 39  ? 11.142  24.588  -30.983 1.00 41.65 ?  39  PRO G CD  1 
ATOM   5263 N N   . GLY D 2 40  ? 8.246   21.084  -29.612 1.00 45.31 ?  40  GLY G N   1 
ATOM   5264 C CA  . GLY D 2 40  ? 6.871   20.673  -29.451 1.00 43.04 ?  40  GLY G CA  1 
ATOM   5265 C C   . GLY D 2 40  ? 6.049   20.708  -30.715 1.00 42.17 ?  40  GLY G C   1 
ATOM   5266 O O   . GLY D 2 40  ? 4.821   20.686  -30.639 1.00 45.04 ?  40  GLY G O   1 
ATOM   5267 N N   . GLN D 2 41  ? 6.688   20.761  -31.885 1.00 39.66 ?  41  GLN G N   1 
ATOM   5268 C CA  . GLN D 2 41  ? 5.985   20.671  -33.154 1.00 34.28 ?  41  GLN G CA  1 
ATOM   5269 C C   . GLN D 2 41  ? 6.498   19.467  -33.937 1.00 32.02 ?  41  GLN G C   1 
ATOM   5270 O O   . GLN D 2 41  ? 7.578   18.936  -33.660 1.00 29.48 ?  41  GLN G O   1 
ATOM   5271 C CB  . GLN D 2 41  ? 6.152   21.945  -33.990 1.00 34.80 ?  41  GLN G CB  1 
ATOM   5272 C CG  . GLN D 2 41  ? 5.506   23.181  -33.374 1.00 36.81 ?  41  GLN G CG  1 
ATOM   5273 C CD  . GLN D 2 41  ? 5.687   24.410  -34.229 1.00 38.25 ?  41  GLN G CD  1 
ATOM   5274 O OE1 . GLN D 2 41  ? 6.295   24.351  -35.295 1.00 42.74 ?  41  GLN G OE1 1 
ATOM   5275 N NE2 . GLN D 2 41  ? 5.184   25.544  -33.756 1.00 48.20 ?  41  GLN G NE2 1 
ATOM   5276 N N   . ALA D 2 42  ? 5.699   19.025  -34.907 1.00 29.05 ?  42  ALA G N   1 
ATOM   5277 C CA  . ALA D 2 42  ? 6.135   17.969  -35.811 1.00 25.90 ?  42  ALA G CA  1 
ATOM   5278 C C   . ALA D 2 42  ? 7.135   18.527  -36.820 1.00 24.89 ?  42  ALA G C   1 
ATOM   5279 O O   . ALA D 2 42  ? 7.136   19.734  -37.108 1.00 24.29 ?  42  ALA G O   1 
ATOM   5280 C CB  . ALA D 2 42  ? 4.939   17.376  -36.549 1.00 28.22 ?  42  ALA G CB  1 
ATOM   5281 N N   . PRO D 2 43  ? 7.997   17.674  -37.381 1.00 25.03 ?  43  PRO G N   1 
ATOM   5282 C CA  . PRO D 2 43  ? 8.929   18.157  -38.413 1.00 23.06 ?  43  PRO G CA  1 
ATOM   5283 C C   . PRO D 2 43  ? 8.191   18.668  -39.643 1.00 23.11 ?  43  PRO G C   1 
ATOM   5284 O O   . PRO D 2 43  ? 7.075   18.246  -39.964 1.00 24.77 ?  43  PRO G O   1 
ATOM   5285 C CB  . PRO D 2 43  ? 9.769   16.921  -38.751 1.00 21.75 ?  43  PRO G CB  1 
ATOM   5286 C CG  . PRO D 2 43  ? 9.634   16.016  -37.534 1.00 25.51 ?  43  PRO G CG  1 
ATOM   5287 C CD  . PRO D 2 43  ? 8.212   16.247  -37.059 1.00 23.35 ?  43  PRO G CD  1 
ATOM   5288 N N   . VAL D 2 44  ? 8.859   19.560  -40.372 1.00 23.92 ?  44  VAL G N   1 
ATOM   5289 C CA  . VAL D 2 44  ? 8.298   20.170  -41.569 1.00 22.12 ?  44  VAL G CA  1 
ATOM   5290 C C   . VAL D 2 44  ? 9.336   20.082  -42.679 1.00 21.21 ?  44  VAL G C   1 
ATOM   5291 O O   . VAL D 2 44  ? 10.491  20.470  -42.480 1.00 20.62 ?  44  VAL G O   1 
ATOM   5292 C CB  . VAL D 2 44  ? 7.908   21.643  -41.323 1.00 22.34 ?  44  VAL G CB  1 
ATOM   5293 C CG1 . VAL D 2 44  ? 7.458   22.290  -42.617 1.00 26.97 ?  44  VAL G CG1 1 
ATOM   5294 C CG2 . VAL D 2 44  ? 6.843   21.745  -40.247 1.00 27.15 ?  44  VAL G CG2 1 
ATOM   5295 N N   . LEU D 2 45  ? 8.917   19.628  -43.855 1.00 21.33 ?  45  LEU G N   1 
ATOM   5296 C CA  . LEU D 2 45  ? 9.826   19.533  -44.995 1.00 21.96 ?  45  LEU G CA  1 
ATOM   5297 C C   . LEU D 2 45  ? 10.074  20.934  -45.548 1.00 24.39 ?  45  LEU G C   1 
ATOM   5298 O O   . LEU D 2 45  ? 9.118   21.639  -45.909 1.00 25.18 ?  45  LEU G O   1 
ATOM   5299 C CB  . LEU D 2 45  ? 9.228   18.600  -46.061 1.00 24.02 ?  45  LEU G CB  1 
ATOM   5300 C CG  . LEU D 2 45  ? 10.021  18.366  -47.355 1.00 23.79 ?  45  LEU G CG  1 
ATOM   5301 C CD1 . LEU D 2 45  ? 11.348  17.666  -47.086 1.00 21.24 ?  45  LEU G CD1 1 
ATOM   5302 C CD2 . LEU D 2 45  ? 9.211   17.527  -48.358 1.00 22.34 ?  45  LEU G CD2 1 
ATOM   5303 N N   . VAL D 2 46  ? 11.338  21.356  -45.581 1.00 23.53 ?  46  VAL G N   1 
ATOM   5304 C CA  . VAL D 2 46  ? 11.669  22.713  -46.018 1.00 23.76 ?  46  VAL G CA  1 
ATOM   5305 C C   . VAL D 2 46  ? 12.510  22.753  -47.282 1.00 23.55 ?  46  VAL G C   1 
ATOM   5306 O O   . VAL D 2 46  ? 12.530  23.799  -47.960 1.00 23.32 ?  46  VAL G O   1 
ATOM   5307 C CB  . VAL D 2 46  ? 12.356  23.528  -44.898 1.00 28.01 ?  46  VAL G CB  1 
ATOM   5308 C CG1 . VAL D 2 46  ? 11.411  23.710  -43.722 1.00 26.52 ?  46  VAL G CG1 1 
ATOM   5309 C CG2 . VAL D 2 46  ? 13.699  22.918  -44.478 1.00 22.86 ?  46  VAL G CG2 1 
ATOM   5310 N N   . ILE D 2 47  ? 13.203  21.674  -47.629 1.00 22.38 ?  47  ILE G N   1 
ATOM   5311 C CA  . ILE D 2 47  ? 13.886  21.527  -48.903 1.00 21.22 ?  47  ILE G CA  1 
ATOM   5312 C C   . ILE D 2 47  ? 13.671  20.096  -49.357 1.00 23.83 ?  47  ILE G C   1 
ATOM   5313 O O   . ILE D 2 47  ? 13.819  19.163  -48.562 1.00 22.68 ?  47  ILE G O   1 
ATOM   5314 C CB  . ILE D 2 47  ? 15.393  21.828  -48.811 1.00 22.65 ?  47  ILE G CB  1 
ATOM   5315 C CG1 . ILE D 2 47  ? 15.642  23.299  -48.455 1.00 26.96 ?  47  ILE G CG1 1 
ATOM   5316 C CG2 . ILE D 2 47  ? 16.088  21.469  -50.128 1.00 23.65 ?  47  ILE G CG2 1 
ATOM   5317 C CD1 . ILE D 2 47  ? 15.365  24.238  -49.607 1.00 25.68 ?  47  ILE G CD1 1 
ATOM   5318 N N   . TYR D 2 48  ? 13.345  19.908  -50.631 1.00 22.71 ?  48  TYR G N   1 
ATOM   5319 C CA  . TYR D 2 48  ? 13.236  18.544  -51.125 1.00 23.54 ?  48  TYR G CA  1 
ATOM   5320 C C   . TYR D 2 48  ? 13.939  18.416  -52.464 1.00 24.35 ?  48  TYR G C   1 
ATOM   5321 O O   . TYR D 2 48  ? 14.169  19.406  -53.165 1.00 25.56 ?  48  TYR G O   1 
ATOM   5322 C CB  . TYR D 2 48  ? 11.772  18.087  -51.205 1.00 20.61 ?  48  TYR G CB  1 
ATOM   5323 C CG  . TYR D 2 48  ? 10.895  18.808  -52.211 1.00 22.35 ?  48  TYR G CG  1 
ATOM   5324 C CD1 . TYR D 2 48  ? 10.458  20.109  -51.971 1.00 24.72 ?  48  TYR G CD1 1 
ATOM   5325 C CD2 . TYR D 2 48  ? 10.474  18.173  -53.385 1.00 25.58 ?  48  TYR G CD2 1 
ATOM   5326 C CE1 . TYR D 2 48  ? 9.644   20.762  -52.879 1.00 26.95 ?  48  TYR G CE1 1 
ATOM   5327 C CE2 . TYR D 2 48  ? 9.647   18.831  -54.300 1.00 28.76 ?  48  TYR G CE2 1 
ATOM   5328 C CZ  . TYR D 2 48  ? 9.242   20.128  -54.033 1.00 31.09 ?  48  TYR G CZ  1 
ATOM   5329 O OH  . TYR D 2 48  ? 8.419   20.823  -54.906 1.00 32.44 ?  48  TYR G OH  1 
ATOM   5330 N N   . LYS D 2 49  ? 14.296  17.164  -52.790 1.00 24.04 ?  49  LYS G N   1 
ATOM   5331 C CA  . LYS D 2 49  ? 15.071  16.839  -53.992 1.00 25.11 ?  49  LYS G CA  1 
ATOM   5332 C C   . LYS D 2 49  ? 16.290  17.749  -54.137 1.00 25.01 ?  49  LYS G C   1 
ATOM   5333 O O   . LYS D 2 49  ? 16.604  18.225  -55.233 1.00 25.71 ?  49  LYS G O   1 
ATOM   5334 C CB  . LYS D 2 49  ? 14.200  16.897  -55.244 1.00 26.37 ?  49  LYS G CB  1 
ATOM   5335 C CG  . LYS D 2 49  ? 13.129  15.804  -55.277 1.00 28.33 ?  49  LYS G CG  1 
ATOM   5336 C CD  . LYS D 2 49  ? 12.116  16.045  -56.374 1.00 31.31 ?  49  LYS G CD  1 
ATOM   5337 C CE  . LYS D 2 49  ? 12.701  15.751  -57.750 1.00 32.72 ?  49  LYS G CE  1 
ATOM   5338 N NZ  . LYS D 2 49  ? 11.606  15.845  -58.770 1.00 38.06 ?  49  LYS G NZ  1 
ATOM   5339 N N   . THR D 2 50  ? 16.966  17.997  -53.007 1.00 22.38 ?  50  THR G N   1 
ATOM   5340 C CA  . THR D 2 50  ? 18.203  18.758  -52.876 1.00 23.62 ?  50  THR G CA  1 
ATOM   5341 C C   . THR D 2 50  ? 18.037  20.257  -53.096 1.00 24.75 ?  50  THR G C   1 
ATOM   5342 O O   . THR D 2 50  ? 18.608  21.030  -52.329 1.00 29.45 ?  50  THR G O   1 
ATOM   5343 C CB  . THR D 2 50  ? 19.293  18.191  -53.796 1.00 25.04 ?  50  THR G CB  1 
ATOM   5344 O OG1 . THR D 2 50  ? 19.499  16.815  -53.438 1.00 24.92 ?  50  THR G OG1 1 
ATOM   5345 C CG2 . THR D 2 50  ? 20.623  18.934  -53.601 1.00 26.22 ?  50  THR G CG2 1 
ATOM   5346 N N   . THR D 2 51  ? 17.291  20.699  -54.102 1.00 23.14 ?  51  THR G N   1 
ATOM   5347 C CA  . THR D 2 51  ? 17.265  22.131  -54.401 1.00 31.98 ?  51  THR G CA  1 
ATOM   5348 C C   . THR D 2 51  ? 15.893  22.781  -54.306 1.00 30.63 ?  51  THR G C   1 
ATOM   5349 O O   . THR D 2 51  ? 15.821  24.019  -54.342 1.00 34.47 ?  51  THR G O   1 
ATOM   5350 C CB  . THR D 2 51  ? 17.821  22.413  -55.806 1.00 31.49 ?  51  THR G CB  1 
ATOM   5351 O OG1 . THR D 2 51  ? 17.137  21.599  -56.759 1.00 36.42 ?  51  THR G OG1 1 
ATOM   5352 C CG2 . THR D 2 51  ? 19.304  22.112  -55.863 1.00 32.20 ?  51  THR G CG2 1 
ATOM   5353 N N   . GLU D 2 52  ? 14.817  22.018  -54.169 1.00 27.72 ?  52  GLU G N   1 
ATOM   5354 C CA  . GLU D 2 52  ? 13.483  22.587  -54.325 1.00 26.15 ?  52  GLU G CA  1 
ATOM   5355 C C   . GLU D 2 52  ? 12.937  23.069  -52.993 1.00 28.22 ?  52  GLU G C   1 
ATOM   5356 O O   . GLU D 2 52  ? 13.080  22.410  -51.965 1.00 26.97 ?  52  GLU G O   1 
ATOM   5357 C CB  . GLU D 2 52  ? 12.516  21.571  -54.940 1.00 27.67 ?  52  GLU G CB  1 
ATOM   5358 C CG  . GLU D 2 52  ? 13.027  20.948  -56.236 1.00 32.72 ?  52  GLU G CG  1 
ATOM   5359 C CD  . GLU D 2 52  ? 13.303  22.014  -57.276 1.00 41.78 ?  52  GLU G CD  1 
ATOM   5360 O OE1 . GLU D 2 52  ? 12.317  22.563  -57.813 1.00 42.68 ?  52  GLU G OE1 1 
ATOM   5361 O OE2 . GLU D 2 52  ? 14.497  22.306  -57.544 1.00 43.53 ?  52  GLU G OE2 1 
ATOM   5362 N N   . ARG D 2 53  ? 12.309  24.240  -53.018 1.00 27.64 ?  53  ARG G N   1 
ATOM   5363 C CA  . ARG D 2 53  ? 11.705  24.779  -51.828 1.00 25.38 ?  53  ARG G CA  1 
ATOM   5364 C C   . ARG D 2 53  ? 10.194  24.720  -51.952 1.00 26.67 ?  53  ARG G C   1 
ATOM   5365 O O   . ARG D 2 53  ? 9.650   25.186  -52.960 1.00 29.48 ?  53  ARG G O   1 
ATOM   5366 C CB  . ARG D 2 53  ? 12.185  26.225  -51.625 1.00 31.25 ?  53  ARG G CB  1 
ATOM   5367 C CG  . ARG D 2 53  ? 11.848  26.861  -50.311 1.00 31.22 ?  53  ARG G CG  1 
ATOM   5368 C CD  . ARG D 2 53  ? 12.560  28.211  -50.247 1.00 34.26 ?  53  ARG G CD  1 
ATOM   5369 N NE  . ARG D 2 53  ? 12.292  29.020  -51.428 1.00 36.24 ?  53  ARG G NE  1 
ATOM   5370 C CZ  . ARG D 2 53  ? 13.238  29.423  -52.269 1.00 42.20 ?  53  ARG G CZ  1 
ATOM   5371 N NH1 . ARG D 2 53  ? 14.512  29.101  -52.086 1.00 41.69 ?  53  ARG G NH1 1 
ATOM   5372 N NH2 . ARG D 2 53  ? 12.898  30.149  -53.330 1.00 47.60 ?  53  ARG G NH2 1 
ATOM   5373 N N   . PRO D 2 54  ? 9.488   24.132  -50.983 1.00 25.90 ?  54  PRO G N   1 
ATOM   5374 C CA  . PRO D 2 54  ? 8.024   24.111  -51.044 1.00 26.86 ?  54  PRO G CA  1 
ATOM   5375 C C   . PRO D 2 54  ? 7.485   25.527  -50.987 1.00 32.14 ?  54  PRO G C   1 
ATOM   5376 O O   . PRO D 2 54  ? 8.095   26.422  -50.402 1.00 27.47 ?  54  PRO G O   1 
ATOM   5377 C CB  . PRO D 2 54  ? 7.624   23.327  -49.790 1.00 29.48 ?  54  PRO G CB  1 
ATOM   5378 C CG  . PRO D 2 54  ? 8.825   22.518  -49.448 1.00 27.26 ?  54  PRO G CG  1 
ATOM   5379 C CD  . PRO D 2 54  ? 10.000  23.356  -49.840 1.00 26.59 ?  54  PRO G CD  1 
ATOM   5380 N N   . SER D 2 55  ? 6.338   25.734  -51.617 1.00 32.25 ?  55  SER G N   1 
ATOM   5381 C CA  . SER D 2 55  ? 5.628   26.987  -51.433 1.00 31.21 ?  55  SER G CA  1 
ATOM   5382 C C   . SER D 2 55  ? 5.354   27.206  -49.948 1.00 32.44 ?  55  SER G C   1 
ATOM   5383 O O   . SER D 2 55  ? 5.026   26.269  -49.222 1.00 39.18 ?  55  SER G O   1 
ATOM   5384 C CB  . SER D 2 55  ? 4.321   26.960  -52.223 1.00 34.78 ?  55  SER G CB  1 
ATOM   5385 O OG  . SER D 2 55  ? 3.349   27.708  -51.530 1.00 49.99 ?  55  SER G OG  1 
ATOM   5386 N N   . GLY D 2 56  ? 5.524   28.440  -49.482 1.00 31.61 ?  56  GLY G N   1 
ATOM   5387 C CA  . GLY D 2 56  ? 5.327   28.728  -48.074 1.00 35.24 ?  56  GLY G CA  1 
ATOM   5388 C C   . GLY D 2 56  ? 6.585   28.702  -47.234 1.00 37.70 ?  56  GLY G C   1 
ATOM   5389 O O   . GLY D 2 56  ? 6.561   29.151  -46.077 1.00 37.43 ?  56  GLY G O   1 
ATOM   5390 N N   . ILE D 2 57  ? 7.683   28.190  -47.769 1.00 28.51 ?  57  ILE G N   1 
ATOM   5391 C CA  . ILE D 2 57  ? 8.952   28.240  -47.054 1.00 30.60 ?  57  ILE G CA  1 
ATOM   5392 C C   . ILE D 2 57  ? 9.626   29.537  -47.475 1.00 27.90 ?  57  ILE G C   1 
ATOM   5393 O O   . ILE D 2 57  ? 9.734   29.797  -48.682 1.00 29.43 ?  57  ILE G O   1 
ATOM   5394 C CB  . ILE D 2 57  ? 9.822   27.017  -47.371 1.00 27.22 ?  57  ILE G CB  1 
ATOM   5395 C CG1 . ILE D 2 57  ? 9.075   25.735  -47.000 1.00 30.48 ?  57  ILE G CG1 1 
ATOM   5396 C CG2 . ILE D 2 57  ? 11.200  27.107  -46.652 1.00 27.74 ?  57  ILE G CG2 1 
ATOM   5397 C CD1 . ILE D 2 57  ? 8.753   25.638  -45.533 1.00 31.13 ?  57  ILE G CD1 1 
ATOM   5398 N N   . PRO D 2 58  ? 10.111  30.354  -46.538 1.00 28.17 ?  58  PRO G N   1 
ATOM   5399 C CA  . PRO D 2 58  ? 10.757  31.621  -46.912 1.00 30.44 ?  58  PRO G CA  1 
ATOM   5400 C C   . PRO D 2 58  ? 11.908  31.451  -47.895 1.00 31.41 ?  58  PRO G C   1 
ATOM   5401 O O   . PRO D 2 58  ? 12.677  30.491  -47.841 1.00 29.32 ?  58  PRO G O   1 
ATOM   5402 C CB  . PRO D 2 58  ? 11.258  32.165  -45.569 1.00 28.92 ?  58  PRO G CB  1 
ATOM   5403 C CG  . PRO D 2 58  ? 10.351  31.597  -44.578 1.00 30.07 ?  58  PRO G CG  1 
ATOM   5404 C CD  . PRO D 2 58  ? 10.038  30.198  -45.077 1.00 33.41 ?  58  PRO G CD  1 
ATOM   5405 N N   . GLU D 2 59  ? 12.052  32.440  -48.776 1.00 31.38 ?  59  GLU G N   1 
ATOM   5406 C CA  . GLU D 2 59  ? 13.102  32.417  -49.788 1.00 32.22 ?  59  GLU G CA  1 
ATOM   5407 C C   . GLU D 2 59  ? 14.505  32.492  -49.198 1.00 29.92 ?  59  GLU G C   1 
ATOM   5408 O O   . GLU D 2 59  ? 15.474  32.234  -49.919 1.00 31.84 ?  59  GLU G O   1 
ATOM   5409 C CB  . GLU D 2 59  ? 12.905  33.577  -50.767 1.00 44.84 ?  59  GLU G CB  1 
ATOM   5410 C CG  . GLU D 2 59  ? 11.946  33.251  -51.905 1.00 48.43 ?  59  GLU G CG  1 
ATOM   5411 C CD  . GLU D 2 59  ? 12.166  34.130  -53.119 1.00 57.55 ?  59  GLU G CD  1 
ATOM   5412 O OE1 . GLU D 2 59  ? 12.702  35.252  -52.957 1.00 59.64 ?  59  GLU G OE1 1 
ATOM   5413 O OE2 . GLU D 2 59  ? 11.816  33.679  -54.236 1.00 61.47 ?  59  GLU G OE2 1 
ATOM   5414 N N   . ARG D 2 60  ? 14.644  32.824  -47.918 1.00 23.22 ?  60  ARG G N   1 
ATOM   5415 C CA  . ARG D 2 60  ? 15.982  32.867  -47.339 1.00 28.14 ?  60  ARG G CA  1 
ATOM   5416 C C   . ARG D 2 60  ? 16.565  31.477  -47.094 1.00 27.20 ?  60  ARG G C   1 
ATOM   5417 O O   . ARG D 2 60  ? 17.740  31.374  -46.718 1.00 26.22 ?  60  ARG G O   1 
ATOM   5418 C CB  . ARG D 2 60  ? 15.960  33.665  -46.043 1.00 27.42 ?  60  ARG G CB  1 
ATOM   5419 C CG  . ARG D 2 60  ? 15.025  33.148  -44.977 1.00 30.42 ?  60  ARG G CG  1 
ATOM   5420 C CD  . ARG D 2 60  ? 15.065  34.058  -43.738 1.00 32.57 ?  60  ARG G CD  1 
ATOM   5421 N NE  . ARG D 2 60  ? 14.204  33.545  -42.679 1.00 31.87 ?  60  ARG G NE  1 
ATOM   5422 C CZ  . ARG D 2 60  ? 12.919  33.847  -42.561 1.00 33.90 ?  60  ARG G CZ  1 
ATOM   5423 N NH1 . ARG D 2 60  ? 12.335  34.709  -43.378 1.00 37.07 ?  60  ARG G NH1 1 
ATOM   5424 N NH2 . ARG D 2 60  ? 12.201  33.272  -41.601 1.00 33.28 ?  60  ARG G NH2 1 
ATOM   5425 N N   . PHE D 2 61  ? 15.772  30.422  -47.279 1.00 27.37 ?  61  PHE G N   1 
ATOM   5426 C CA  . PHE D 2 61  ? 16.251  29.043  -47.179 1.00 24.47 ?  61  PHE G CA  1 
ATOM   5427 C C   . PHE D 2 61  ? 16.665  28.583  -48.569 1.00 26.59 ?  61  PHE G C   1 
ATOM   5428 O O   . PHE D 2 61  ? 15.841  28.568  -49.488 1.00 28.99 ?  61  PHE G O   1 
ATOM   5429 C CB  . PHE D 2 61  ? 15.150  28.119  -46.644 1.00 21.94 ?  61  PHE G CB  1 
ATOM   5430 C CG  . PHE D 2 61  ? 14.857  28.295  -45.178 1.00 25.51 ?  61  PHE G CG  1 
ATOM   5431 C CD1 . PHE D 2 61  ? 13.908  29.227  -44.768 1.00 29.45 ?  61  PHE G CD1 1 
ATOM   5432 C CD2 . PHE D 2 61  ? 15.492  27.532  -44.218 1.00 25.12 ?  61  PHE G CD2 1 
ATOM   5433 C CE1 . PHE D 2 61  ? 13.615  29.418  -43.423 1.00 26.83 ?  61  PHE G CE1 1 
ATOM   5434 C CE2 . PHE D 2 61  ? 15.204  27.720  -42.859 1.00 26.97 ?  61  PHE G CE2 1 
ATOM   5435 C CZ  . PHE D 2 61  ? 14.265  28.661  -42.469 1.00 28.71 ?  61  PHE G CZ  1 
ATOM   5436 N N   . SER D 2 62  ? 17.921  28.181  -48.724 1.00 25.74 ?  62  SER G N   1 
ATOM   5437 C CA  . SER D 2 62  ? 18.372  27.630  -49.991 1.00 24.96 ?  62  SER G CA  1 
ATOM   5438 C C   . SER D 2 62  ? 19.363  26.515  -49.715 1.00 26.77 ?  62  SER G C   1 
ATOM   5439 O O   . SER D 2 62  ? 19.919  26.409  -48.620 1.00 29.87 ?  62  SER G O   1 
ATOM   5440 C CB  . SER D 2 62  ? 18.970  28.718  -50.894 1.00 29.90 ?  62  SER G CB  1 
ATOM   5441 O OG  . SER D 2 62  ? 20.205  29.173  -50.380 1.00 34.09 ?  62  SER G OG  1 
ATOM   5442 N N   . ASP D 2 63  ? 19.571  25.675  -50.721 1.00 22.53 ?  63  ASP G N   1 
ATOM   5443 C CA  . ASP D 2 63  ? 20.413  24.492  -50.588 1.00 26.21 ?  63  ASP G CA  1 
ATOM   5444 C C   . ASP D 2 63  ? 21.326  24.411  -51.802 1.00 31.12 ?  63  ASP G C   1 
ATOM   5445 O O   . ASP D 2 63  ? 20.894  24.671  -52.924 1.00 34.46 ?  63  ASP G O   1 
ATOM   5446 C CB  . ASP D 2 63  ? 19.523  23.234  -50.477 1.00 25.87 ?  63  ASP G CB  1 
ATOM   5447 C CG  . ASP D 2 63  ? 20.180  22.085  -49.740 1.00 29.72 ?  63  ASP G CG  1 
ATOM   5448 O OD1 . ASP D 2 63  ? 20.885  22.297  -48.737 1.00 30.55 ?  63  ASP G OD1 1 
ATOM   5449 O OD2 . ASP D 2 63  ? 19.966  20.929  -50.163 1.00 30.69 ?  63  ASP G OD2 1 
ATOM   5450 N N   . SER D 2 64  ? 22.597  24.096  -51.574 1.00 30.62 ?  64  SER G N   1 
ATOM   5451 C CA  . SER D 2 64  ? 23.549  23.936  -52.663 1.00 32.90 ?  64  SER G CA  1 
ATOM   5452 C C   . SER D 2 64  ? 24.343  22.671  -52.391 1.00 35.13 ?  64  SER G C   1 
ATOM   5453 O O   . SER D 2 64  ? 24.413  22.199  -51.254 1.00 30.31 ?  64  SER G O   1 
ATOM   5454 C CB  . SER D 2 64  ? 24.506  25.124  -52.800 1.00 37.05 ?  64  SER G CB  1 
ATOM   5455 O OG  . SER D 2 64  ? 25.196  25.393  -51.582 1.00 39.13 ?  64  SER G OG  1 
ATOM   5456 N N   . SER D 2 65  ? 24.947  22.127  -53.438 1.00 38.49 ?  65  SER G N   1 
ATOM   5457 C CA  . SER D 2 65  ? 25.560  20.815  -53.317 1.00 35.76 ?  65  SER G CA  1 
ATOM   5458 C C   . SER D 2 65  ? 26.833  20.769  -54.129 1.00 43.42 ?  65  SER G C   1 
ATOM   5459 O O   . SER D 2 65  ? 26.884  21.270  -55.255 1.00 45.08 ?  65  SER G O   1 
ATOM   5460 C CB  . SER D 2 65  ? 24.630  19.704  -53.789 1.00 37.96 ?  65  SER G CB  1 
ATOM   5461 O OG  . SER D 2 65  ? 24.541  19.702  -55.201 1.00 49.58 ?  65  SER G OG  1 
ATOM   5462 N N   . SER D 2 66  ? 27.849  20.151  -53.542 1.00 38.80 ?  66  SER G N   1 
ATOM   5463 C CA  . SER D 2 66  ? 29.155  20.047  -54.166 1.00 45.48 ?  66  SER G CA  1 
ATOM   5464 C C   . SER D 2 66  ? 29.779  18.760  -53.674 1.00 45.59 ?  66  SER G C   1 
ATOM   5465 O O   . SER D 2 66  ? 30.031  18.619  -52.471 1.00 45.37 ?  66  SER G O   1 
ATOM   5466 C CB  . SER D 2 66  ? 30.038  21.234  -53.805 1.00 46.14 ?  66  SER G CB  1 
ATOM   5467 O OG  . SER D 2 66  ? 31.228  21.200  -54.562 1.00 58.83 ?  66  SER G OG  1 
ATOM   5468 N N   . GLY D 2 67  ? 30.019  17.838  -54.596 1.00 48.13 ?  67  GLY G N   1 
ATOM   5469 C CA  . GLY D 2 67  ? 30.654  16.589  -54.245 1.00 42.54 ?  67  GLY G CA  1 
ATOM   5470 C C   . GLY D 2 67  ? 29.741  15.750  -53.388 1.00 41.85 ?  67  GLY G C   1 
ATOM   5471 O O   . GLY D 2 67  ? 28.614  15.428  -53.786 1.00 47.10 ?  67  GLY G O   1 
ATOM   5472 N N   . THR D 2 68  ? 30.211  15.403  -52.196 1.00 37.38 ?  68  THR G N   1 
ATOM   5473 C CA  . THR D 2 68  ? 29.433  14.623  -51.249 1.00 35.03 ?  68  THR G CA  1 
ATOM   5474 C C   . THR D 2 68  ? 28.783  15.478  -50.169 1.00 31.19 ?  68  THR G C   1 
ATOM   5475 O O   . THR D 2 68  ? 28.286  14.925  -49.182 1.00 28.15 ?  68  THR G O   1 
ATOM   5476 C CB  . THR D 2 68  ? 30.316  13.552  -50.613 1.00 36.22 ?  68  THR G CB  1 
ATOM   5477 O OG1 . THR D 2 68  ? 31.365  14.183  -49.871 1.00 38.37 ?  68  THR G OG1 1 
ATOM   5478 C CG2 . THR D 2 68  ? 30.895  12.641  -51.684 1.00 38.51 ?  68  THR G CG2 1 
ATOM   5479 N N   . THR D 2 69  ? 28.744  16.802  -50.342 1.00 32.00 ?  69  THR G N   1 
ATOM   5480 C CA  . THR D 2 69  ? 28.248  17.711  -49.317 1.00 27.50 ?  69  THR G CA  1 
ATOM   5481 C C   . THR D 2 69  ? 27.155  18.604  -49.887 1.00 32.06 ?  69  THR G C   1 
ATOM   5482 O O   . THR D 2 69  ? 27.307  19.175  -50.972 1.00 33.72 ?  69  THR G O   1 
ATOM   5483 C CB  . THR D 2 69  ? 29.379  18.580  -48.742 1.00 29.34 ?  69  THR G CB  1 
ATOM   5484 O OG1 . THR D 2 69  ? 30.374  17.740  -48.139 1.00 30.29 ?  69  THR G OG1 1 
ATOM   5485 C CG2 . THR D 2 69  ? 28.841  19.561  -47.679 1.00 29.90 ?  69  THR G CG2 1 
ATOM   5486 N N   . VAL D 2 70  ? 26.058  18.726  -49.153 1.00 23.24 ?  70  VAL G N   1 
ATOM   5487 C CA  . VAL D 2 70  ? 25.055  19.735  -49.461 1.00 25.20 ?  70  VAL G CA  1 
ATOM   5488 C C   . VAL D 2 70  ? 25.075  20.732  -48.316 1.00 26.98 ?  70  VAL G C   1 
ATOM   5489 O O   . VAL D 2 70  ? 25.342  20.374  -47.164 1.00 25.55 ?  70  VAL G O   1 
ATOM   5490 C CB  . VAL D 2 70  ? 23.644  19.149  -49.666 1.00 29.92 ?  70  VAL G CB  1 
ATOM   5491 C CG1 . VAL D 2 70  ? 23.688  17.982  -50.646 1.00 29.19 ?  70  VAL G CG1 1 
ATOM   5492 C CG2 . VAL D 2 70  ? 23.085  18.700  -48.350 1.00 33.90 ?  70  VAL G CG2 1 
ATOM   5493 N N   . THR D 2 71  ? 24.784  21.993  -48.625 1.00 23.17 ?  71  THR G N   1 
ATOM   5494 C CA  . THR D 2 71  ? 24.769  23.025  -47.601 1.00 25.73 ?  71  THR G CA  1 
ATOM   5495 C C   . THR D 2 71  ? 23.415  23.707  -47.618 1.00 23.92 ?  71  THR G C   1 
ATOM   5496 O O   . THR D 2 71  ? 23.012  24.248  -48.649 1.00 25.60 ?  71  THR G O   1 
ATOM   5497 C CB  . THR D 2 71  ? 25.860  24.066  -47.832 1.00 27.89 ?  71  THR G CB  1 
ATOM   5498 O OG1 . THR D 2 71  ? 27.145  23.428  -47.767 1.00 28.41 ?  71  THR G OG1 1 
ATOM   5499 C CG2 . THR D 2 71  ? 25.762  25.145  -46.757 1.00 22.60 ?  71  THR G CG2 1 
ATOM   5500 N N   . LEU D 2 72  ? 22.720  23.653  -46.492 1.00 21.31 ?  72  LEU G N   1 
ATOM   5501 C CA  . LEU D 2 72  ? 21.501  24.429  -46.298 1.00 22.40 ?  72  LEU G CA  1 
ATOM   5502 C C   . LEU D 2 72  ? 21.931  25.793  -45.776 1.00 24.10 ?  72  LEU G C   1 
ATOM   5503 O O   . LEU D 2 72  ? 22.647  25.868  -44.770 1.00 23.03 ?  72  LEU G O   1 
ATOM   5504 C CB  . LEU D 2 72  ? 20.556  23.739  -45.320 1.00 22.41 ?  72  LEU G CB  1 
ATOM   5505 C CG  . LEU D 2 72  ? 19.334  24.592  -44.895 1.00 24.28 ?  72  LEU G CG  1 
ATOM   5506 C CD1 . LEU D 2 72  ? 18.335  24.715  -46.035 1.00 24.69 ?  72  LEU G CD1 1 
ATOM   5507 C CD2 . LEU D 2 72  ? 18.627  24.002  -43.663 1.00 24.87 ?  72  LEU G CD2 1 
ATOM   5508 N N   . THR D 2 73  ? 21.564  26.849  -46.500 1.00 23.50 ?  73  THR G N   1 
ATOM   5509 C CA  . THR D 2 73  ? 21.955  28.213  -46.153 1.00 21.77 ?  73  THR G CA  1 
ATOM   5510 C C   . THR D 2 73  ? 20.684  28.941  -45.758 1.00 23.87 ?  73  THR G C   1 
ATOM   5511 O O   . THR D 2 73  ? 19.688  28.886  -46.486 1.00 25.94 ?  73  THR G O   1 
ATOM   5512 C CB  . THR D 2 73  ? 22.645  28.936  -47.321 1.00 26.02 ?  73  THR G CB  1 
ATOM   5513 O OG1 . THR D 2 73  ? 23.862  28.262  -47.663 1.00 25.99 ?  73  THR G OG1 1 
ATOM   5514 C CG2 . THR D 2 73  ? 22.999  30.393  -46.953 1.00 25.13 ?  73  THR G CG2 1 
ATOM   5515 N N   . ILE D 2 74  ? 20.692  29.521  -44.570 1.00 22.85 ?  74  ILE G N   1 
ATOM   5516 C CA  . ILE D 2 74  ? 19.622  30.374  -44.092 1.00 21.04 ?  74  ILE G CA  1 
ATOM   5517 C C   . ILE D 2 74  ? 20.198  31.784  -44.104 1.00 24.90 ?  74  ILE G C   1 
ATOM   5518 O O   . ILE D 2 74  ? 20.990  32.136  -43.232 1.00 24.91 ?  74  ILE G O   1 
ATOM   5519 C CB  . ILE D 2 74  ? 19.138  29.971  -42.694 1.00 24.26 ?  74  ILE G CB  1 
ATOM   5520 C CG1 . ILE D 2 74  ? 18.778  28.471  -42.669 1.00 28.39 ?  74  ILE G CG1 1 
ATOM   5521 C CG2 . ILE D 2 74  ? 17.970  30.859  -42.244 1.00 25.42 ?  74  ILE G CG2 1 
ATOM   5522 C CD1 . ILE D 2 74  ? 18.445  27.915  -41.267 1.00 26.26 ?  74  ILE G CD1 1 
ATOM   5523 N N   . SER D 2 75  ? 19.852  32.566  -45.116 1.00 22.07 ?  75  SER G N   1 
ATOM   5524 C CA  . SER D 2 75  ? 20.318  33.945  -45.199 1.00 25.55 ?  75  SER G CA  1 
ATOM   5525 C C   . SER D 2 75  ? 19.508  34.817  -44.262 1.00 26.16 ?  75  SER G C   1 
ATOM   5526 O O   . SER D 2 75  ? 18.330  34.548  -44.021 1.00 26.46 ?  75  SER G O   1 
ATOM   5527 C CB  . SER D 2 75  ? 20.175  34.473  -46.622 1.00 31.21 ?  75  SER G CB  1 
ATOM   5528 O OG  . SER D 2 75  ? 20.979  33.696  -47.500 1.00 33.71 ?  75  SER G OG  1 
ATOM   5529 N N   . ALA D 2 76  ? 20.147  35.868  -43.743 1.00 22.81 ?  76  ALA G N   1 
ATOM   5530 C CA  . ALA D 2 76  ? 19.505  36.832  -42.843 1.00 26.37 ?  76  ALA G CA  1 
ATOM   5531 C C   . ALA D 2 76  ? 18.575  36.130  -41.848 1.00 25.04 ?  76  ALA G C   1 
ATOM   5532 O O   . ALA D 2 76  ? 17.358  36.333  -41.824 1.00 25.43 ?  76  ALA G O   1 
ATOM   5533 C CB  . ALA D 2 76  ? 18.757  37.891  -43.641 1.00 26.35 ?  76  ALA G CB  1 
ATOM   5534 N N   . ALA D 2 77  ? 19.184  35.268  -41.029 1.00 23.85 ?  77  ALA G N   1 
ATOM   5535 C CA  . ALA D 2 77  ? 18.428  34.407  -40.124 1.00 24.48 ?  77  ALA G CA  1 
ATOM   5536 C C   . ALA D 2 77  ? 17.528  35.223  -39.202 1.00 29.29 ?  77  ALA G C   1 
ATOM   5537 O O   . ALA D 2 77  ? 17.913  36.277  -38.689 1.00 26.78 ?  77  ALA G O   1 
ATOM   5538 C CB  . ALA D 2 77  ? 19.382  33.547  -39.287 1.00 25.43 ?  77  ALA G CB  1 
ATOM   5539 N N   . GLN D 2 78  ? 16.313  34.729  -39.002 1.00 25.93 ?  78  GLN G N   1 
ATOM   5540 C CA  . GLN D 2 78  ? 15.333  35.364  -38.135 1.00 28.28 ?  78  GLN G CA  1 
ATOM   5541 C C   . GLN D 2 78  ? 15.200  34.556  -36.854 1.00 30.67 ?  78  GLN G C   1 
ATOM   5542 O O   . GLN D 2 78  ? 15.476  33.354  -36.833 1.00 25.33 ?  78  GLN G O   1 
ATOM   5543 C CB  . GLN D 2 78  ? 13.976  35.449  -38.836 1.00 26.35 ?  78  GLN G CB  1 
ATOM   5544 C CG  . GLN D 2 78  ? 14.071  36.180  -40.152 1.00 26.90 ?  78  GLN G CG  1 
ATOM   5545 C CD  . GLN D 2 78  ? 14.448  37.641  -39.932 1.00 29.19 ?  78  GLN G CD  1 
ATOM   5546 O OE1 . GLN D 2 78  ? 13.800  38.353  -39.156 1.00 27.43 ?  78  GLN G OE1 1 
ATOM   5547 N NE2 . GLN D 2 78  ? 15.505  38.082  -40.592 1.00 25.14 ?  78  GLN G NE2 1 
ATOM   5548 N N   . ALA D 2 79  ? 14.744  35.211  -35.782 1.00 28.77 ?  79  ALA G N   1 
ATOM   5549 C CA  . ALA D 2 79  ? 14.544  34.482  -34.528 1.00 30.15 ?  79  ALA G CA  1 
ATOM   5550 C C   . ALA D 2 79  ? 13.640  33.266  -34.727 1.00 28.68 ?  79  ALA G C   1 
ATOM   5551 O O   . ALA D 2 79  ? 13.825  32.232  -34.080 1.00 28.92 ?  79  ALA G O   1 
ATOM   5552 C CB  . ALA D 2 79  ? 13.944  35.403  -33.465 1.00 35.80 ?  79  ALA G CB  1 
ATOM   5553 N N   . GLU D 2 80  ? 12.656  33.382  -35.615 1.00 24.82 ?  80  GLU G N   1 
ATOM   5554 C CA  . GLU D 2 80  ? 11.716  32.312  -35.932 1.00 28.85 ?  80  GLU G CA  1 
ATOM   5555 C C   . GLU D 2 80  ? 12.392  31.108  -36.577 1.00 31.80 ?  80  GLU G C   1 
ATOM   5556 O O   . GLU D 2 80  ? 11.788  30.037  -36.637 1.00 29.14 ?  80  GLU G O   1 
ATOM   5557 C CB  . GLU D 2 80  ? 10.625  32.897  -36.855 1.00 35.08 ?  80  GLU G CB  1 
ATOM   5558 C CG  . GLU D 2 80  ? 10.830  32.499  -38.318 1.00 41.72 ?  80  GLU G CG  1 
ATOM   5559 C CD  . GLU D 2 80  ? 9.748   33.063  -39.251 1.00 48.21 ?  80  GLU G CD  1 
ATOM   5560 O OE1 . GLU D 2 80  ? 9.780   34.293  -39.532 1.00 50.03 ?  80  GLU G OE1 1 
ATOM   5561 O OE2 . GLU D 2 80  ? 8.892   32.268  -39.719 1.00 53.10 ?  80  GLU G OE2 1 
ATOM   5562 N N   . ASP D 2 81  ? 13.635  31.240  -37.058 1.00 27.95 ?  81  ASP G N   1 
ATOM   5563 C CA  . ASP D 2 81  ? 14.310  30.109  -37.690 1.00 23.66 ?  81  ASP G CA  1 
ATOM   5564 C C   . ASP D 2 81  ? 15.020  29.200  -36.693 1.00 23.20 ?  81  ASP G C   1 
ATOM   5565 O O   . ASP D 2 81  ? 15.570  28.165  -37.094 1.00 24.66 ?  81  ASP G O   1 
ATOM   5566 C CB  . ASP D 2 81  ? 15.319  30.606  -38.735 1.00 22.33 ?  81  ASP G CB  1 
ATOM   5567 C CG  . ASP D 2 81  ? 14.678  31.476  -39.793 1.00 27.40 ?  81  ASP G CG  1 
ATOM   5568 O OD1 . ASP D 2 81  ? 13.495  31.252  -40.125 1.00 26.32 ?  81  ASP G OD1 1 
ATOM   5569 O OD2 . ASP D 2 81  ? 15.351  32.402  -40.304 1.00 27.92 ?  81  ASP G OD2 1 
ATOM   5570 N N   . GLU D 2 82  ? 15.040  29.551  -35.418 1.00 23.22 ?  82  GLU G N   1 
ATOM   5571 C CA  . GLU D 2 82  ? 15.675  28.702  -34.420 1.00 25.92 ?  82  GLU G CA  1 
ATOM   5572 C C   . GLU D 2 82  ? 14.892  27.395  -34.302 1.00 27.34 ?  82  GLU G C   1 
ATOM   5573 O O   . GLU D 2 82  ? 13.674  27.402  -34.076 1.00 25.51 ?  82  GLU G O   1 
ATOM   5574 C CB  . GLU D 2 82  ? 15.756  29.442  -33.086 1.00 29.40 ?  82  GLU G CB  1 
ATOM   5575 C CG  . GLU D 2 82  ? 16.166  28.591  -31.897 1.00 27.99 ?  82  GLU G CG  1 
ATOM   5576 C CD  . GLU D 2 82  ? 16.757  29.411  -30.756 1.00 34.56 ?  82  GLU G CD  1 
ATOM   5577 O OE1 . GLU D 2 82  ? 17.464  30.415  -31.015 1.00 33.28 ?  82  GLU G OE1 1 
ATOM   5578 O OE2 . GLU D 2 82  ? 16.574  29.007  -29.589 1.00 44.02 ?  82  GLU G OE2 1 
ATOM   5579 N N   . ALA D 2 83  ? 15.590  26.280  -34.476 1.00 24.55 ?  83  ALA G N   1 
ATOM   5580 C CA  . ALA D 2 83  ? 14.957  24.980  -34.681 1.00 22.34 ?  83  ALA G CA  1 
ATOM   5581 C C   . ALA D 2 83  ? 16.063  23.942  -34.831 1.00 25.88 ?  83  ALA G C   1 
ATOM   5582 O O   . ALA D 2 83  ? 17.248  24.273  -34.959 1.00 22.50 ?  83  ALA G O   1 
ATOM   5583 C CB  . ALA D 2 83  ? 14.068  24.983  -35.929 1.00 21.12 ?  83  ALA G CB  1 
ATOM   5584 N N   . ASP D 2 84  ? 15.653  22.674  -34.793 1.00 25.13 ?  84  ASP G N   1 
ATOM   5585 C CA  . ASP D 2 84  ? 16.491  21.558  -35.199 1.00 24.89 ?  84  ASP G CA  1 
ATOM   5586 C C   . ASP D 2 84  ? 16.261  21.312  -36.683 1.00 24.37 ?  84  ASP G C   1 
ATOM   5587 O O   . ASP D 2 84  ? 15.118  21.320  -37.143 1.00 23.46 ?  84  ASP G O   1 
ATOM   5588 C CB  . ASP D 2 84  ? 16.150  20.308  -34.388 1.00 26.49 ?  84  ASP G CB  1 
ATOM   5589 C CG  . ASP D 2 84  ? 16.453  20.478  -32.919 1.00 32.13 ?  84  ASP G CG  1 
ATOM   5590 O OD1 . ASP D 2 84  ? 17.479  21.104  -32.613 1.00 33.98 ?  84  ASP G OD1 1 
ATOM   5591 O OD2 . ASP D 2 84  ? 15.679  20.010  -32.071 1.00 35.80 ?  84  ASP G OD2 1 
ATOM   5592 N N   . TYR D 2 85  ? 17.343  21.134  -37.433 1.00 21.60 ?  85  TYR G N   1 
ATOM   5593 C CA  . TYR D 2 85  ? 17.275  20.881  -38.865 1.00 20.51 ?  85  TYR G CA  1 
ATOM   5594 C C   . TYR D 2 85  ? 17.853  19.501  -39.121 1.00 21.77 ?  85  TYR G C   1 
ATOM   5595 O O   . TYR D 2 85  ? 18.995  19.224  -38.739 1.00 23.81 ?  85  TYR G O   1 
ATOM   5596 C CB  . TYR D 2 85  ? 18.042  21.947  -39.663 1.00 20.79 ?  85  TYR G CB  1 
ATOM   5597 C CG  . TYR D 2 85  ? 17.356  23.285  -39.589 1.00 20.20 ?  85  TYR G CG  1 
ATOM   5598 C CD1 . TYR D 2 85  ? 17.522  24.119  -38.487 1.00 20.34 ?  85  TYR G CD1 1 
ATOM   5599 C CD2 . TYR D 2 85  ? 16.485  23.678  -40.583 1.00 21.05 ?  85  TYR G CD2 1 
ATOM   5600 C CE1 . TYR D 2 85  ? 16.875  25.339  -38.409 1.00 22.16 ?  85  TYR G CE1 1 
ATOM   5601 C CE2 . TYR D 2 85  ? 15.803  24.905  -40.500 1.00 20.87 ?  85  TYR G CE2 1 
ATOM   5602 C CZ  . TYR D 2 85  ? 16.003  25.714  -39.412 1.00 21.55 ?  85  TYR G CZ  1 
ATOM   5603 O OH  . TYR D 2 85  ? 15.361  26.922  -39.342 1.00 21.91 ?  85  TYR G OH  1 
ATOM   5604 N N   . TYR D 2 86  ? 17.060  18.629  -39.736 1.00 19.99 ?  86  TYR G N   1 
ATOM   5605 C CA  . TYR D 2 86  ? 17.485  17.255  -40.005 1.00 20.33 ?  86  TYR G CA  1 
ATOM   5606 C C   . TYR D 2 86  ? 17.721  17.078  -41.496 1.00 20.63 ?  86  TYR G C   1 
ATOM   5607 O O   . TYR D 2 86  ? 16.834  17.380  -42.296 1.00 22.64 ?  86  TYR G O   1 
ATOM   5608 C CB  . TYR D 2 86  ? 16.435  16.257  -39.516 1.00 22.65 ?  86  TYR G CB  1 
ATOM   5609 C CG  . TYR D 2 86  ? 16.291  16.222  -38.024 1.00 20.88 ?  86  TYR G CG  1 
ATOM   5610 C CD1 . TYR D 2 86  ? 17.076  15.360  -37.245 1.00 22.95 ?  86  TYR G CD1 1 
ATOM   5611 C CD2 . TYR D 2 86  ? 15.358  17.026  -37.387 1.00 23.92 ?  86  TYR G CD2 1 
ATOM   5612 C CE1 . TYR D 2 86  ? 16.956  15.346  -35.869 1.00 22.82 ?  86  TYR G CE1 1 
ATOM   5613 C CE2 . TYR D 2 86  ? 15.225  17.012  -36.015 1.00 23.05 ?  86  TYR G CE2 1 
ATOM   5614 C CZ  . TYR D 2 86  ? 16.021  16.158  -35.262 1.00 25.08 ?  86  TYR G CZ  1 
ATOM   5615 O OH  . TYR D 2 86  ? 15.871  16.160  -33.894 1.00 28.76 ?  86  TYR G OH  1 
ATOM   5616 N N   . CYS D 2 87  ? 18.906  16.592  -41.888 1.00 19.24 ?  87  CYS G N   1 
ATOM   5617 C CA  . CYS D 2 87  ? 18.955  16.184  -43.282 1.00 19.58 ?  87  CYS G CA  1 
ATOM   5618 C C   . CYS D 2 87  ? 18.583  14.711  -43.405 1.00 21.18 ?  87  CYS G C   1 
ATOM   5619 O O   . CYS D 2 87  ? 18.608  13.954  -42.433 1.00 23.16 ?  87  CYS G O   1 
ATOM   5620 C CB  . CYS D 2 87  ? 20.319  16.456  -43.927 1.00 22.76 ?  87  CYS G CB  1 
ATOM   5621 S SG  . CYS D 2 87  ? 21.711  15.616  -43.208 1.00 27.64 ?  87  CYS G SG  1 
ATOM   5622 N N   . GLN D 2 88  ? 18.221  14.316  -44.618 1.00 19.31 ?  88  GLN G N   1 
ATOM   5623 C CA  . GLN D 2 88  ? 17.656  12.981  -44.823 1.00 19.58 ?  88  GLN G CA  1 
ATOM   5624 C C   . GLN D 2 88  ? 17.900  12.558  -46.264 1.00 19.88 ?  88  GLN G C   1 
ATOM   5625 O O   . GLN D 2 88  ? 17.759  13.364  -47.190 1.00 22.55 ?  88  GLN G O   1 
ATOM   5626 C CB  . GLN D 2 88  ? 16.149  12.962  -44.515 1.00 19.67 ?  88  GLN G CB  1 
ATOM   5627 C CG  . GLN D 2 88  ? 15.451  11.601  -44.784 1.00 20.31 ?  88  GLN G CG  1 
ATOM   5628 C CD  . GLN D 2 88  ? 14.666  11.599  -46.095 1.00 21.09 ?  88  GLN G CD  1 
ATOM   5629 O OE1 . GLN D 2 88  ? 13.730  12.396  -46.283 1.00 22.40 ?  88  GLN G OE1 1 
ATOM   5630 N NE2 . GLN D 2 88  ? 15.040  10.691  -47.010 1.00 23.38 ?  88  GLN G NE2 1 
ATOM   5631 N N   . SER D 2 89  ? 18.203  11.278  -46.461 1.00 20.63 ?  89  SER G N   1 
ATOM   5632 C CA  . SER D 2 89  ? 18.325  10.761  -47.812 1.00 20.15 ?  89  SER G CA  1 
ATOM   5633 C C   . SER D 2 89  ? 17.818  9.319   -47.814 1.00 19.63 ?  89  SER G C   1 
ATOM   5634 O O   . SER D 2 89  ? 17.268  8.828   -46.821 1.00 20.45 ?  89  SER G O   1 
ATOM   5635 C CB  . SER D 2 89  ? 19.782  10.909  -48.290 1.00 20.89 ?  89  SER G CB  1 
ATOM   5636 O OG  . SER D 2 89  ? 19.899  10.645  -49.689 1.00 22.75 ?  89  SER G OG  1 
ATOM   5637 N N   . VAL D 2 90  ? 17.980  8.633   -48.941 1.00 21.77 ?  90  VAL G N   1 
ATOM   5638 C CA  . VAL D 2 90  ? 17.448  7.281   -49.102 1.00 22.26 ?  90  VAL G CA  1 
ATOM   5639 C C   . VAL D 2 90  ? 18.336  6.584   -50.119 1.00 27.09 ?  90  VAL G C   1 
ATOM   5640 O O   . VAL D 2 90  ? 18.991  7.238   -50.927 1.00 32.96 ?  90  VAL G O   1 
ATOM   5641 C CB  . VAL D 2 90  ? 15.943  7.332   -49.516 1.00 28.13 ?  90  VAL G CB  1 
ATOM   5642 C CG1 . VAL D 2 90  ? 15.762  8.131   -50.786 1.00 31.14 ?  90  VAL G CG1 1 
ATOM   5643 C CG2 . VAL D 2 90  ? 15.350  5.933   -49.699 1.00 26.54 ?  90  VAL G CG2 1 
ATOM   5644 N N   . ASP D 2 91  ? 18.413  5.260   -50.060 1.00 23.88 ?  91  ASP G N   1 
ATOM   5645 C CA  . ASP D 2 91  ? 19.105  4.573   -51.133 1.00 26.42 ?  91  ASP G CA  1 
ATOM   5646 C C   . ASP D 2 91  ? 18.088  4.042   -52.140 1.00 27.91 ?  91  ASP G C   1 
ATOM   5647 O O   . ASP D 2 91  ? 16.874  4.184   -51.978 1.00 26.57 ?  91  ASP G O   1 
ATOM   5648 C CB  . ASP D 2 91  ? 20.035  3.484   -50.587 1.00 27.90 ?  91  ASP G CB  1 
ATOM   5649 C CG  . ASP D 2 91  ? 19.306  2.366   -49.882 1.00 25.76 ?  91  ASP G CG  1 
ATOM   5650 O OD1 . ASP D 2 91  ? 18.064  2.182   -50.061 1.00 24.80 ?  91  ASP G OD1 1 
ATOM   5651 O OD2 . ASP D 2 91  ? 20.010  1.636   -49.133 1.00 27.36 ?  91  ASP G OD2 1 
ATOM   5652 N N   . SER D 2 92  ? 18.598  3.452   -53.218 1.00 28.03 ?  92  SER G N   1 
ATOM   5653 C CA  . SER D 2 92  ? 17.708  2.992   -54.271 1.00 29.39 ?  92  SER G CA  1 
ATOM   5654 C C   . SER D 2 92  ? 16.814  1.831   -53.821 1.00 28.36 ?  92  SER G C   1 
ATOM   5655 O O   . SER D 2 92  ? 15.801  1.553   -54.480 1.00 30.52 ?  92  SER G O   1 
ATOM   5656 C CB  . SER D 2 92  ? 18.548  2.628   -55.489 1.00 31.19 ?  92  SER G CB  1 
ATOM   5657 O OG  . SER D 2 92  ? 19.138  1.359   -55.291 1.00 42.00 ?  92  SER G OG  1 
ATOM   5658 N N   . SER D 2 93  ? 17.130  1.177   -52.698 1.00 25.76 ?  93  SER G N   1 
ATOM   5659 C CA  . SER D 2 93  ? 16.284  0.099   -52.178 1.00 26.95 ?  93  SER G CA  1 
ATOM   5660 C C   . SER D 2 93  ? 15.206  0.583   -51.222 1.00 28.60 ?  93  SER G C   1 
ATOM   5661 O O   . SER D 2 93  ? 14.383  -0.228  -50.773 1.00 27.80 ?  93  SER G O   1 
ATOM   5662 C CB  . SER D 2 93  ? 17.124  -0.956  -51.455 1.00 28.77 ?  93  SER G CB  1 
ATOM   5663 O OG  . SER D 2 93  ? 17.979  -1.625  -52.370 1.00 30.02 ?  93  SER G OG  1 
ATOM   5664 N N   . GLY D 2 94  ? 15.190  1.866   -50.884 1.00 25.53 ?  94  GLY G N   1 
ATOM   5665 C CA  . GLY D 2 94  ? 14.153  2.393   -50.026 1.00 24.29 ?  94  GLY G CA  1 
ATOM   5666 C C   . GLY D 2 94  ? 14.527  2.537   -48.571 1.00 23.94 ?  94  GLY G C   1 
ATOM   5667 O O   . GLY D 2 94  ? 13.646  2.836   -47.750 1.00 22.59 ?  94  GLY G O   1 
ATOM   5668 N N   . THR D 2 95  ? 15.801  2.364   -48.217 1.00 22.97 ?  95  THR G N   1 
ATOM   5669 C CA  . THR D 2 95  ? 16.205  2.587   -46.839 1.00 19.78 ?  95  THR G CA  1 
ATOM   5670 C C   . THR D 2 95  ? 16.391  4.080   -46.605 1.00 21.65 ?  95  THR G C   1 
ATOM   5671 O O   . THR D 2 95  ? 17.150  4.735   -47.323 1.00 23.92 ?  95  THR G O   1 
ATOM   5672 C CB  . THR D 2 95  ? 17.499  1.837   -46.516 1.00 21.01 ?  95  THR G CB  1 
ATOM   5673 O OG1 . THR D 2 95  ? 17.241  0.420   -46.518 1.00 20.81 ?  95  THR G OG1 1 
ATOM   5674 C CG2 . THR D 2 95  ? 18.001  2.224   -45.139 1.00 20.89 ?  95  THR G CG2 1 
ATOM   5675 N N   . TYR D 2 96  ? 15.748  4.599   -45.571 1.00 20.15 ?  96  TYR G N   1 
ATOM   5676 C CA  . TYR D 2 96  ? 15.807  6.017   -45.239 1.00 20.23 ?  96  TYR G CA  1 
ATOM   5677 C C   . TYR D 2 96  ? 16.814  6.233   -44.131 1.00 21.02 ?  96  TYR G C   1 
ATOM   5678 O O   . TYR D 2 96  ? 16.908  5.424   -43.202 1.00 21.81 ?  96  TYR G O   1 
ATOM   5679 C CB  . TYR D 2 96  ? 14.433  6.535   -44.780 1.00 17.52 ?  96  TYR G CB  1 
ATOM   5680 C CG  . TYR D 2 96  ? 13.472  6.803   -45.901 1.00 19.30 ?  96  TYR G CG  1 
ATOM   5681 C CD1 . TYR D 2 96  ? 13.015  5.772   -46.703 1.00 19.37 ?  96  TYR G CD1 1 
ATOM   5682 C CD2 . TYR D 2 96  ? 13.039  8.096   -46.171 1.00 20.38 ?  96  TYR G CD2 1 
ATOM   5683 C CE1 . TYR D 2 96  ? 12.151  5.997   -47.745 1.00 21.36 ?  96  TYR G CE1 1 
ATOM   5684 C CE2 . TYR D 2 96  ? 12.159  8.346   -47.211 1.00 19.50 ?  96  TYR G CE2 1 
ATOM   5685 C CZ  . TYR D 2 96  ? 11.724  7.307   -47.994 1.00 21.90 ?  96  TYR G CZ  1 
ATOM   5686 O OH  . TYR D 2 96  ? 10.867  7.540   -49.037 1.00 21.39 ?  96  TYR G OH  1 
ATOM   5687 N N   . VAL D 2 97  ? 17.572  7.323   -44.226 1.00 18.79 ?  97  VAL G N   1 
ATOM   5688 C CA  . VAL D 2 97  ? 18.535  7.699   -43.196 1.00 20.42 ?  97  VAL G CA  1 
ATOM   5689 C C   . VAL D 2 97  ? 18.360  9.170   -42.860 1.00 19.88 ?  97  VAL G C   1 
ATOM   5690 O O   . VAL D 2 97  ? 18.249  9.999   -43.767 1.00 19.74 ?  97  VAL G O   1 
ATOM   5691 C CB  . VAL D 2 97  ? 19.991  7.462   -43.643 1.00 22.04 ?  97  VAL G CB  1 
ATOM   5692 C CG1 . VAL D 2 97  ? 20.923  7.981   -42.568 1.00 21.57 ?  97  VAL G CG1 1 
ATOM   5693 C CG2 . VAL D 2 97  ? 20.267  5.970   -43.900 1.00 23.11 ?  97  VAL G CG2 1 
ATOM   5694 N N   . PHE D 2 98  ? 18.353  9.483   -41.566 1.00 20.16 ?  98  PHE G N   1 
ATOM   5695 C CA  . PHE D 2 98  ? 18.375  10.856  -41.058 1.00 21.46 ?  98  PHE G CA  1 
ATOM   5696 C C   . PHE D 2 98  ? 19.759  11.154  -40.480 1.00 24.30 ?  98  PHE G C   1 
ATOM   5697 O O   . PHE D 2 98  ? 20.400  10.276  -39.899 1.00 24.38 ?  98  PHE G O   1 
ATOM   5698 C CB  . PHE D 2 98  ? 17.337  11.051  -39.946 1.00 21.79 ?  98  PHE G CB  1 
ATOM   5699 C CG  . PHE D 2 98  ? 15.898  11.039  -40.415 1.00 22.98 ?  98  PHE G CG  1 
ATOM   5700 C CD1 . PHE D 2 98  ? 15.286  12.200  -40.872 1.00 22.99 ?  98  PHE G CD1 1 
ATOM   5701 C CD2 . PHE D 2 98  ? 15.156  9.871   -40.379 1.00 25.97 ?  98  PHE G CD2 1 
ATOM   5702 C CE1 . PHE D 2 98  ? 13.940  12.193  -41.280 1.00 26.22 ?  98  PHE G CE1 1 
ATOM   5703 C CE2 . PHE D 2 98  ? 13.785  9.863   -40.787 1.00 24.24 ?  98  PHE G CE2 1 
ATOM   5704 C CZ  . PHE D 2 98  ? 13.200  11.012  -41.252 1.00 24.78 ?  98  PHE G CZ  1 
ATOM   5705 N N   . GLY D 2 99  ? 20.227  12.399  -40.622 1.00 23.61 ?  99  GLY G N   1 
ATOM   5706 C CA  . GLY D 2 99  ? 21.389  12.826  -39.859 1.00 25.07 ?  99  GLY G CA  1 
ATOM   5707 C C   . GLY D 2 99  ? 20.975  13.011  -38.405 1.00 23.64 ?  99  GLY G C   1 
ATOM   5708 O O   . GLY D 2 99  ? 19.812  12.875  -38.043 1.00 23.32 ?  99  GLY G O   1 
ATOM   5709 N N   . ILE D 2 100 ? 21.944  13.362  -37.554 1.00 24.14 ?  100 ILE G N   1 
ATOM   5710 C CA  . ILE D 2 100 ? 21.640  13.498  -36.124 1.00 25.24 ?  100 ILE G CA  1 
ATOM   5711 C C   . ILE D 2 100 ? 20.784  14.710  -35.774 1.00 28.52 ?  100 ILE G C   1 
ATOM   5712 O O   . ILE D 2 100 ? 20.238  14.766  -34.656 1.00 28.27 ?  100 ILE G O   1 
ATOM   5713 C CB  . ILE D 2 100 ? 22.947  13.555  -35.304 1.00 27.83 ?  100 ILE G CB  1 
ATOM   5714 C CG1 . ILE D 2 100 ? 23.808  14.730  -35.798 1.00 29.68 ?  100 ILE G CG1 1 
ATOM   5715 C CG2 . ILE D 2 100 ? 23.674  12.233  -35.400 1.00 32.97 ?  100 ILE G CG2 1 
ATOM   5716 C CD1 . ILE D 2 100 ? 24.909  15.167  -34.822 1.00 32.87 ?  100 ILE G CD1 1 
ATOM   5717 N N   . GLY D 2 101 ? 20.630  15.671  -36.690 1.00 24.08 ?  101 GLY G N   1 
ATOM   5718 C CA  . GLY D 2 101 ? 19.944  16.917  -36.399 1.00 22.37 ?  101 GLY G CA  1 
ATOM   5719 C C   . GLY D 2 101 ? 20.936  17.986  -35.976 1.00 23.44 ?  101 GLY G C   1 
ATOM   5720 O O   . GLY D 2 101 ? 21.812  17.713  -35.149 1.00 26.45 ?  101 GLY G O   1 
ATOM   5721 N N   . THR D 2 102 ? 20.861  19.174  -36.579 1.00 20.42 ?  102 THR G N   1 
ATOM   5722 C CA  . THR D 2 102 ? 21.647  20.335  -36.173 1.00 25.18 ?  102 THR G CA  1 
ATOM   5723 C C   . THR D 2 102 ? 20.743  21.282  -35.395 1.00 24.58 ?  102 THR G C   1 
ATOM   5724 O O   . THR D 2 102 ? 19.745  21.773  -35.939 1.00 23.72 ?  102 THR G O   1 
ATOM   5725 C CB  . THR D 2 102 ? 22.223  21.060  -37.392 1.00 22.60 ?  102 THR G CB  1 
ATOM   5726 O OG1 . THR D 2 102 ? 23.062  20.156  -38.127 1.00 20.90 ?  102 THR G OG1 1 
ATOM   5727 C CG2 . THR D 2 102 ? 23.039  22.304  -36.981 1.00 22.49 ?  102 THR G CG2 1 
ATOM   5728 N N   . LYS D 2 103 ? 21.075  21.518  -34.129 1.00 23.93 ?  103 LYS G N   1 
ATOM   5729 C CA  . LYS D 2 103 ? 20.378  22.526  -33.333 1.00 25.52 ?  103 LYS G CA  1 
ATOM   5730 C C   . LYS D 2 103 ? 20.889  23.880  -33.795 1.00 26.96 ?  103 LYS G C   1 
ATOM   5731 O O   . LYS D 2 103 ? 22.060  24.215  -33.567 1.00 25.42 ?  103 LYS G O   1 
ATOM   5732 C CB  . LYS D 2 103 ? 20.629  22.332  -31.837 1.00 27.60 ?  103 LYS G CB  1 
ATOM   5733 C CG  . LYS D 2 103 ? 19.959  23.386  -30.927 1.00 35.69 ?  103 LYS G CG  1 
ATOM   5734 C CD  . LYS D 2 103 ? 18.454  23.523  -31.232 1.00 38.45 ?  103 LYS G CD  1 
ATOM   5735 C CE  . LYS D 2 103 ? 17.818  24.837  -30.752 1.00 38.33 ?  103 LYS G CE  1 
ATOM   5736 N NZ  . LYS D 2 103 ? 16.317  24.732  -30.724 1.00 42.12 ?  103 LYS G NZ  1 
ATOM   5737 N N   . VAL D 2 104 ? 20.046  24.628  -34.491 1.00 22.84 ?  104 VAL G N   1 
ATOM   5738 C CA  . VAL D 2 104 ? 20.407  25.952  -34.970 1.00 23.67 ?  104 VAL G CA  1 
ATOM   5739 C C   . VAL D 2 104 ? 19.869  26.959  -33.965 1.00 27.22 ?  104 VAL G C   1 
ATOM   5740 O O   . VAL D 2 104 ? 18.654  27.147  -33.849 1.00 25.90 ?  104 VAL G O   1 
ATOM   5741 C CB  . VAL D 2 104 ? 19.868  26.228  -36.374 1.00 24.99 ?  104 VAL G CB  1 
ATOM   5742 C CG1 . VAL D 2 104 ? 20.174  27.692  -36.759 1.00 25.35 ?  104 VAL G CG1 1 
ATOM   5743 C CG2 . VAL D 2 104 ? 20.509  25.293  -37.382 1.00 23.63 ?  104 VAL G CG2 1 
ATOM   5744 N N   . THR D 2 105 ? 20.772  27.579  -33.210 1.00 24.80 ?  105 THR G N   1 
ATOM   5745 C CA  . THR D 2 105 ? 20.421  28.631  -32.264 1.00 25.08 ?  105 THR G CA  1 
ATOM   5746 C C   . THR D 2 105 ? 20.582  29.974  -32.959 1.00 25.40 ?  105 THR G C   1 
ATOM   5747 O O   . THR D 2 105 ? 21.640  30.247  -33.533 1.00 25.44 ?  105 THR G O   1 
ATOM   5748 C CB  . THR D 2 105 ? 21.334  28.584  -31.036 1.00 28.36 ?  105 THR G CB  1 
ATOM   5749 O OG1 . THR D 2 105 ? 21.128  27.359  -30.324 1.00 31.06 ?  105 THR G OG1 1 
ATOM   5750 C CG2 . THR D 2 105 ? 21.039  29.750  -30.101 1.00 30.45 ?  105 THR G CG2 1 
ATOM   5751 N N   . VAL D 2 106 ? 19.533  30.797  -32.933 1.00 26.94 ?  106 VAL G N   1 
ATOM   5752 C CA  . VAL D 2 106 ? 19.642  32.173  -33.397 1.00 25.21 ?  106 VAL G CA  1 
ATOM   5753 C C   . VAL D 2 106 ? 19.992  32.983  -32.159 1.00 28.38 ?  106 VAL G C   1 
ATOM   5754 O O   . VAL D 2 106 ? 19.123  33.367  -31.374 1.00 29.38 ?  106 VAL G O   1 
ATOM   5755 C CB  . VAL D 2 106 ? 18.367  32.666  -34.072 1.00 26.91 ?  106 VAL G CB  1 
ATOM   5756 C CG1 . VAL D 2 106 ? 18.576  34.086  -34.568 1.00 28.37 ?  106 VAL G CG1 1 
ATOM   5757 C CG2 . VAL D 2 106 ? 18.044  31.774  -35.243 1.00 27.69 ?  106 VAL G CG2 1 
ATOM   5758 N N   . LEU D 2 107 ? 21.279  33.212  -31.980 1.00 25.69 ?  107 LEU G N   1 
ATOM   5759 C CA  . LEU D 2 107 ? 21.823  33.653  -30.707 1.00 24.97 ?  107 LEU G CA  1 
ATOM   5760 C C   . LEU D 2 107 ? 21.721  35.169  -30.587 1.00 25.81 ?  107 LEU G C   1 
ATOM   5761 O O   . LEU D 2 107 ? 22.368  35.913  -31.342 1.00 26.92 ?  107 LEU G O   1 
ATOM   5762 C CB  . LEU D 2 107 ? 23.274  33.181  -30.592 1.00 25.33 ?  107 LEU G CB  1 
ATOM   5763 C CG  . LEU D 2 107 ? 24.042  33.540  -29.321 1.00 28.91 ?  107 LEU G CG  1 
ATOM   5764 C CD1 . LEU D 2 107 ? 23.467  32.776  -28.150 1.00 31.59 ?  107 LEU G CD1 1 
ATOM   5765 C CD2 . LEU D 2 107 ? 25.512  33.179  -29.514 1.00 33.27 ?  107 LEU G CD2 1 
ATOM   5766 N N   . GLY D 2 108 ? 20.919  35.623  -29.638 1.00 24.09 ?  108 GLY G N   1 
ATOM   5767 C CA  . GLY D 2 108 ? 20.831  37.043  -29.373 1.00 27.64 ?  108 GLY G CA  1 
ATOM   5768 C C   . GLY D 2 108 ? 22.122  37.589  -28.795 1.00 27.49 ?  108 GLY G C   1 
ATOM   5769 O O   . GLY D 2 108 ? 22.974  36.869  -28.272 1.00 27.53 ?  108 GLY G O   1 
ATOM   5770 N N   . ARG D 2 109 ? 22.260  38.907  -28.899 1.00 26.76 ?  109 ARG G N   1 
ATOM   5771 C CA  . ARG D 2 109 ? 23.485  39.566  -28.448 1.00 25.85 ?  109 ARG G CA  1 
ATOM   5772 C C   . ARG D 2 109 ? 23.472  39.810  -26.941 1.00 26.66 ?  109 ARG G C   1 
ATOM   5773 O O   . ARG D 2 109 ? 24.534  39.820  -26.307 1.00 27.75 ?  109 ARG G O   1 
ATOM   5774 C CB  . ARG D 2 109 ? 23.644  40.882  -29.220 1.00 30.13 ?  109 ARG G CB  1 
ATOM   5775 C CG  . ARG D 2 109 ? 24.924  41.675  -28.985 1.00 28.11 ?  109 ARG G CG  1 
ATOM   5776 C CD  . ARG D 2 109 ? 26.197  40.820  -29.056 1.00 29.27 ?  109 ARG G CD  1 
ATOM   5777 N NE  . ARG D 2 109 ? 27.344  41.595  -28.577 1.00 32.22 ?  109 ARG G NE  1 
ATOM   5778 C CZ  . ARG D 2 109 ? 27.749  41.574  -27.312 1.00 34.28 ?  109 ARG G CZ  1 
ATOM   5779 N NH1 . ARG D 2 109 ? 27.111  40.864  -26.399 1.00 31.32 ?  109 ARG G NH1 1 
ATOM   5780 N NH2 . ARG D 2 109 ? 28.827  42.274  -26.954 1.00 37.62 ?  109 ARG G NH2 1 
ATOM   5781 N N   . THR D 2 110 ? 22.292  39.995  -26.349 1.00 24.78 ?  110 THR G N   1 
ATOM   5782 C CA  . THR D 2 110 ? 22.219  40.312  -24.931 1.00 25.07 ?  110 THR G CA  1 
ATOM   5783 C C   . THR D 2 110 ? 22.578  39.119  -24.071 1.00 28.54 ?  110 THR G C   1 
ATOM   5784 O O   . THR D 2 110 ? 22.134  37.996  -24.317 1.00 28.55 ?  110 THR G O   1 
ATOM   5785 C CB  . THR D 2 110 ? 20.815  40.799  -24.566 1.00 29.43 ?  110 THR G CB  1 
ATOM   5786 O OG1 . THR D 2 110 ? 20.476  41.924  -25.379 1.00 32.34 ?  110 THR G OG1 1 
ATOM   5787 C CG2 . THR D 2 110 ? 20.755  41.193  -23.104 1.00 28.17 ?  110 THR G CG2 1 
ATOM   5788 N N   . VAL D 2 111 ? 23.378  39.362  -23.038 1.00 25.89 ?  111 VAL G N   1 
ATOM   5789 C CA  . VAL D 2 111 ? 23.746  38.319  -22.088 1.00 26.65 ?  111 VAL G CA  1 
ATOM   5790 C C   . VAL D 2 111 ? 23.087  38.663  -20.764 1.00 29.71 ?  111 VAL G C   1 
ATOM   5791 O O   . VAL D 2 111 ? 23.418  39.679  -20.138 1.00 30.45 ?  111 VAL G O   1 
ATOM   5792 C CB  . VAL D 2 111 ? 25.264  38.182  -21.924 1.00 30.26 ?  111 VAL G CB  1 
ATOM   5793 C CG1 . VAL D 2 111 ? 25.564  36.954  -21.064 1.00 32.27 ?  111 VAL G CG1 1 
ATOM   5794 C CG2 . VAL D 2 111 ? 25.944  38.077  -23.283 1.00 28.79 ?  111 VAL G CG2 1 
ATOM   5795 N N   . ALA D 2 112 ? 22.149  37.826  -20.341 1.00 27.07 ?  112 ALA G N   1 
ATOM   5796 C CA  . ALA D 2 112 ? 21.413  38.030  -19.098 1.00 30.49 ?  112 ALA G CA  1 
ATOM   5797 C C   . ALA D 2 112 ? 21.924  37.023  -18.079 1.00 29.81 ?  112 ALA G C   1 
ATOM   5798 O O   . ALA D 2 112 ? 21.847  35.812  -18.312 1.00 27.57 ?  112 ALA G O   1 
ATOM   5799 C CB  . ALA D 2 112 ? 19.907  37.877  -19.319 1.00 26.99 ?  112 ALA G CB  1 
ATOM   5800 N N   . ALA D 2 113 ? 22.505  37.526  -16.990 1.00 27.57 ?  113 ALA G N   1 
ATOM   5801 C CA  . ALA D 2 113 ? 22.995  36.659  -15.930 1.00 27.43 ?  113 ALA G CA  1 
ATOM   5802 C C   . ALA D 2 113 ? 21.813  36.110  -15.131 1.00 27.77 ?  113 ALA G C   1 
ATOM   5803 O O   . ALA D 2 113 ? 20.795  36.792  -14.979 1.00 26.97 ?  113 ALA G O   1 
ATOM   5804 C CB  . ALA D 2 113 ? 23.928  37.429  -14.996 1.00 31.91 ?  113 ALA G CB  1 
ATOM   5805 N N   . PRO D 2 114 ? 21.916  34.879  -14.640 1.00 25.89 ?  114 PRO G N   1 
ATOM   5806 C CA  . PRO D 2 114 ? 20.834  34.321  -13.824 1.00 27.23 ?  114 PRO G CA  1 
ATOM   5807 C C   . PRO D 2 114 ? 20.805  34.938  -12.441 1.00 30.61 ?  114 PRO G C   1 
ATOM   5808 O O   . PRO D 2 114 ? 21.836  35.272  -11.858 1.00 30.51 ?  114 PRO G O   1 
ATOM   5809 C CB  . PRO D 2 114 ? 21.175  32.825  -13.753 1.00 28.92 ?  114 PRO G CB  1 
ATOM   5810 C CG  . PRO D 2 114 ? 22.695  32.781  -13.903 1.00 30.76 ?  114 PRO G CG  1 
ATOM   5811 C CD  . PRO D 2 114 ? 22.997  33.905  -14.886 1.00 26.40 ?  114 PRO G CD  1 
ATOM   5812 N N   . SER D 2 115 ? 19.601  35.107  -11.909 1.00 28.88 ?  115 SER G N   1 
ATOM   5813 C CA  . SER D 2 115 ? 19.504  35.247  -10.468 1.00 29.39 ?  115 SER G CA  1 
ATOM   5814 C C   . SER D 2 115 ? 19.380  33.840  -9.897  1.00 30.36 ?  115 SER G C   1 
ATOM   5815 O O   . SER D 2 115 ? 18.839  32.940  -10.544 1.00 32.68 ?  115 SER G O   1 
ATOM   5816 C CB  . SER D 2 115 ? 18.323  36.131  -10.064 1.00 33.53 ?  115 SER G CB  1 
ATOM   5817 O OG  . SER D 2 115 ? 17.175  35.763  -10.786 1.00 39.84 ?  115 SER G OG  1 
ATOM   5818 N N   . VAL D 2 116 ? 19.951  33.628  -8.717  1.00 30.05 ?  116 VAL G N   1 
ATOM   5819 C CA  . VAL D 2 116 ? 20.104  32.285  -8.162  1.00 31.67 ?  116 VAL G CA  1 
ATOM   5820 C C   . VAL D 2 116 ? 19.435  32.239  -6.799  1.00 30.97 ?  116 VAL G C   1 
ATOM   5821 O O   . VAL D 2 116 ? 19.640  33.135  -5.973  1.00 31.52 ?  116 VAL G O   1 
ATOM   5822 C CB  . VAL D 2 116 ? 21.585  31.876  -8.058  1.00 30.60 ?  116 VAL G CB  1 
ATOM   5823 C CG1 . VAL D 2 116 ? 21.696  30.417  -7.583  1.00 30.82 ?  116 VAL G CG1 1 
ATOM   5824 C CG2 . VAL D 2 116 ? 22.258  32.043  -9.416  1.00 29.19 ?  116 VAL G CG2 1 
ATOM   5825 N N   . PHE D 2 117 ? 18.643  31.187  -6.575  1.00 29.37 ?  117 PHE G N   1 
ATOM   5826 C CA  . PHE D 2 117 ? 17.880  30.967  -5.353  1.00 30.96 ?  117 PHE G CA  1 
ATOM   5827 C C   . PHE D 2 117 ? 18.079  29.524  -4.920  1.00 32.06 ?  117 PHE G C   1 
ATOM   5828 O O   . PHE D 2 117 ? 18.196  28.634  -5.760  1.00 31.63 ?  117 PHE G O   1 
ATOM   5829 C CB  . PHE D 2 117 ? 16.379  31.209  -5.571  1.00 31.32 ?  117 PHE G CB  1 
ATOM   5830 C CG  . PHE D 2 117 ? 16.053  32.530  -6.206  1.00 30.22 ?  117 PHE G CG  1 
ATOM   5831 C CD1 . PHE D 2 117 ? 15.986  32.663  -7.590  1.00 31.91 ?  117 PHE G CD1 1 
ATOM   5832 C CD2 . PHE D 2 117 ? 15.766  33.630  -5.419  1.00 32.61 ?  117 PHE G CD2 1 
ATOM   5833 C CE1 . PHE D 2 117 ? 15.658  33.895  -8.178  1.00 31.64 ?  117 PHE G CE1 1 
ATOM   5834 C CE2 . PHE D 2 117 ? 15.434  34.850  -5.988  1.00 31.25 ?  117 PHE G CE2 1 
ATOM   5835 C CZ  . PHE D 2 117 ? 15.387  34.984  -7.373  1.00 32.01 ?  117 PHE G CZ  1 
ATOM   5836 N N   . ILE D 2 118 ? 18.109  29.279  -3.610  1.00 31.12 ?  118 ILE G N   1 
ATOM   5837 C CA  . ILE D 2 118 ? 18.258  27.918  -3.104  1.00 30.52 ?  118 ILE G CA  1 
ATOM   5838 C C   . ILE D 2 118 ? 17.158  27.660  -2.086  1.00 32.14 ?  118 ILE G C   1 
ATOM   5839 O O   . ILE D 2 118 ? 16.787  28.554  -1.316  1.00 33.75 ?  118 ILE G O   1 
ATOM   5840 C CB  . ILE D 2 118 ? 19.672  27.662  -2.510  1.00 30.50 ?  118 ILE G CB  1 
ATOM   5841 C CG1 . ILE D 2 118 ? 19.876  26.173  -2.225  1.00 31.42 ?  118 ILE G CG1 1 
ATOM   5842 C CG2 . ILE D 2 118 ? 19.921  28.491  -1.266  1.00 33.13 ?  118 ILE G CG2 1 
ATOM   5843 C CD1 . ILE D 2 118 ? 21.332  25.800  -1.919  1.00 35.58 ?  118 ILE G CD1 1 
ATOM   5844 N N   . PHE D 2 119 ? 16.601  26.453  -2.120  1.00 31.89 ?  119 PHE G N   1 
ATOM   5845 C CA  . PHE D 2 119 ? 15.491  26.077  -1.255  1.00 34.98 ?  119 PHE G CA  1 
ATOM   5846 C C   . PHE D 2 119 ? 15.872  24.861  -0.417  1.00 36.01 ?  119 PHE G C   1 
ATOM   5847 O O   . PHE D 2 119 ? 16.188  23.802  -0.982  1.00 35.97 ?  119 PHE G O   1 
ATOM   5848 C CB  . PHE D 2 119 ? 14.251  25.767  -2.082  1.00 35.61 ?  119 PHE G CB  1 
ATOM   5849 C CG  . PHE D 2 119 ? 13.730  26.936  -2.861  1.00 33.60 ?  119 PHE G CG  1 
ATOM   5850 C CD1 . PHE D 2 119 ? 12.979  27.925  -2.241  1.00 34.66 ?  119 PHE G CD1 1 
ATOM   5851 C CD2 . PHE D 2 119 ? 13.990  27.041  -4.219  1.00 35.69 ?  119 PHE G CD2 1 
ATOM   5852 C CE1 . PHE D 2 119 ? 12.480  29.005  -2.973  1.00 40.15 ?  119 PHE G CE1 1 
ATOM   5853 C CE2 . PHE D 2 119 ? 13.501  28.121  -4.955  1.00 34.07 ?  119 PHE G CE2 1 
ATOM   5854 C CZ  . PHE D 2 119 ? 12.754  29.102  -4.328  1.00 35.73 ?  119 PHE G CZ  1 
ATOM   5855 N N   . PRO D 2 120 ? 15.880  24.959  0.907   1.00 37.58 ?  120 PRO G N   1 
ATOM   5856 C CA  . PRO D 2 120 ? 16.085  23.765  1.744   1.00 38.46 ?  120 PRO G CA  1 
ATOM   5857 C C   . PRO D 2 120 ? 14.908  22.817  1.606   1.00 39.10 ?  120 PRO G C   1 
ATOM   5858 O O   . PRO D 2 120 ? 13.824  23.229  1.173   1.00 36.91 ?  120 PRO G O   1 
ATOM   5859 C CB  . PRO D 2 120 ? 16.165  24.334  3.168   1.00 39.59 ?  120 PRO G CB  1 
ATOM   5860 C CG  . PRO D 2 120 ? 16.514  25.787  3.011   1.00 42.33 ?  120 PRO G CG  1 
ATOM   5861 C CD  . PRO D 2 120 ? 16.081  26.224  1.637   1.00 38.57 ?  120 PRO G CD  1 
ATOM   5862 N N   . PRO D 2 121 ? 15.072  21.538  1.949   1.00 39.10 ?  121 PRO G N   1 
ATOM   5863 C CA  . PRO D 2 121 ? 13.918  20.632  1.937   1.00 40.67 ?  121 PRO G CA  1 
ATOM   5864 C C   . PRO D 2 121 ? 12.903  21.064  2.985   1.00 44.74 ?  121 PRO G C   1 
ATOM   5865 O O   . PRO D 2 121 ? 13.250  21.654  4.012   1.00 45.21 ?  121 PRO G O   1 
ATOM   5866 C CB  . PRO D 2 121 ? 14.537  19.267  2.261   1.00 44.11 ?  121 PRO G CB  1 
ATOM   5867 C CG  . PRO D 2 121 ? 15.768  19.613  3.032   1.00 42.57 ?  121 PRO G CG  1 
ATOM   5868 C CD  . PRO D 2 121 ? 16.305  20.830  2.323   1.00 39.33 ?  121 PRO G CD  1 
ATOM   5869 N N   . SER D 2 122 ? 11.630  20.818  2.692   1.00 43.70 ?  122 SER G N   1 
ATOM   5870 C CA  . SER D 2 122 ? 10.575  21.156  3.633   1.00 45.05 ?  122 SER G CA  1 
ATOM   5871 C C   . SER D 2 122 ? 10.522  20.123  4.750   1.00 49.11 ?  122 SER G C   1 
ATOM   5872 O O   . SER D 2 122 ? 10.909  18.962  4.570   1.00 48.52 ?  122 SER G O   1 
ATOM   5873 C CB  . SER D 2 122 ? 9.217   21.220  2.935   1.00 46.35 ?  122 SER G CB  1 
ATOM   5874 O OG  . SER D 2 122 ? 8.909   19.967  2.347   1.00 47.52 ?  122 SER G OG  1 
ATOM   5875 N N   . ASP D 2 123 ? 10.039  20.557  5.917   1.00 51.03 ?  123 ASP G N   1 
ATOM   5876 C CA  . ASP D 2 123 ? 9.816   19.614  7.008   1.00 53.26 ?  123 ASP G CA  1 
ATOM   5877 C C   . ASP D 2 123 ? 8.803   18.545  6.617   1.00 52.48 ?  123 ASP G C   1 
ATOM   5878 O O   . ASP D 2 123 ? 8.923   17.390  7.038   1.00 57.08 ?  123 ASP G O   1 
ATOM   5879 C CB  . ASP D 2 123 ? 9.359   20.347  8.268   1.00 55.11 ?  123 ASP G CB  1 
ATOM   5880 C CG  . ASP D 2 123 ? 10.428  21.250  8.832   1.00 59.28 ?  123 ASP G CG  1 
ATOM   5881 O OD1 . ASP D 2 123 ? 11.623  20.913  8.691   1.00 60.06 ?  123 ASP G OD1 1 
ATOM   5882 O OD2 . ASP D 2 123 ? 10.074  22.289  9.431   1.00 66.93 ?  123 ASP G OD2 1 
ATOM   5883 N N   . GLU D 2 124 ? 7.802   18.909  5.807   1.00 51.91 ?  124 GLU G N   1 
ATOM   5884 C CA  . GLU D 2 124 ? 6.848   17.913  5.320   1.00 52.03 ?  124 GLU G CA  1 
ATOM   5885 C C   . GLU D 2 124 ? 7.567   16.763  4.627   1.00 53.41 ?  124 GLU G C   1 
ATOM   5886 O O   . GLU D 2 124 ? 7.300   15.587  4.905   1.00 54.39 ?  124 GLU G O   1 
ATOM   5887 C CB  . GLU D 2 124 ? 5.836   18.550  4.362   1.00 51.47 ?  124 GLU G CB  1 
ATOM   5888 C CG  . GLU D 2 124 ? 4.912   19.592  4.972   1.00 53.58 ?  124 GLU G CG  1 
ATOM   5889 C CD  . GLU D 2 124 ? 5.332   21.030  4.672   1.00 59.19 ?  124 GLU G CD  1 
ATOM   5890 O OE1 . GLU D 2 124 ? 6.397   21.479  5.165   1.00 58.05 ?  124 GLU G OE1 1 
ATOM   5891 O OE2 . GLU D 2 124 ? 4.570   21.716  3.951   1.00 57.18 ?  124 GLU G OE2 1 
ATOM   5892 N N   . GLN D 2 125 ? 8.502   17.085  3.727   1.00 52.27 ?  125 GLN G N   1 
ATOM   5893 C CA  . GLN D 2 125 ? 9.225   16.041  3.008   1.00 49.23 ?  125 GLN G CA  1 
ATOM   5894 C C   . GLN D 2 125 ? 10.172  15.278  3.926   1.00 51.20 ?  125 GLN G C   1 
ATOM   5895 O O   . GLN D 2 125 ? 10.335  14.060  3.783   1.00 54.90 ?  125 GLN G O   1 
ATOM   5896 C CB  . GLN D 2 125 ? 10.002  16.638  1.832   1.00 47.34 ?  125 GLN G CB  1 
ATOM   5897 C CG  . GLN D 2 125 ? 10.450  15.585  0.831   1.00 49.17 ?  125 GLN G CG  1 
ATOM   5898 C CD  . GLN D 2 125 ? 11.549  16.056  -0.108  1.00 47.84 ?  125 GLN G CD  1 
ATOM   5899 O OE1 . GLN D 2 125 ? 12.115  17.137  0.055   1.00 43.93 ?  125 GLN G OE1 1 
ATOM   5900 N NE2 . GLN D 2 125 ? 11.863  15.225  -1.100  1.00 47.02 ?  125 GLN G NE2 1 
ATOM   5901 N N   . LEU D 2 126 ? 10.821  15.971  4.864   1.00 51.49 ?  126 LEU G N   1 
ATOM   5902 C CA  . LEU D 2 126 ? 11.762  15.294  5.751   1.00 53.77 ?  126 LEU G CA  1 
ATOM   5903 C C   . LEU D 2 126 ? 11.075  14.241  6.617   1.00 57.34 ?  126 LEU G C   1 
ATOM   5904 O O   . LEU D 2 126 ? 11.745  13.319  7.099   1.00 58.38 ?  126 LEU G O   1 
ATOM   5905 C CB  . LEU D 2 126 ? 12.498  16.320  6.618   1.00 52.48 ?  126 LEU G CB  1 
ATOM   5906 C CG  . LEU D 2 126 ? 13.610  17.113  5.918   1.00 48.49 ?  126 LEU G CG  1 
ATOM   5907 C CD1 . LEU D 2 126 ? 14.066  18.279  6.772   1.00 50.26 ?  126 LEU G CD1 1 
ATOM   5908 C CD2 . LEU D 2 126 ? 14.797  16.232  5.554   1.00 46.11 ?  126 LEU G CD2 1 
ATOM   5909 N N   . LYS D 2 127 ? 9.755   14.349  6.809   1.00 56.83 ?  127 LYS G N   1 
ATOM   5910 C CA  . LYS D 2 127 ? 8.996   13.291  7.474   1.00 57.22 ?  127 LYS G CA  1 
ATOM   5911 C C   . LYS D 2 127 ? 9.097   11.980  6.704   1.00 59.78 ?  127 LYS G C   1 
ATOM   5912 O O   . LYS D 2 127 ? 9.351   10.918  7.286   1.00 62.02 ?  127 LYS G O   1 
ATOM   5913 C CB  . LYS D 2 127 ? 7.531   13.706  7.613   1.00 58.05 ?  127 LYS G CB  1 
ATOM   5914 C CG  . LYS D 2 127 ? 7.287   14.944  8.465   1.00 59.92 ?  127 LYS G CG  1 
ATOM   5915 C CD  . LYS D 2 127 ? 7.562   14.682  9.938   1.00 66.55 ?  127 LYS G CD  1 
ATOM   5916 C CE  . LYS D 2 127 ? 7.166   15.877  10.802  1.00 67.98 ?  127 LYS G CE  1 
ATOM   5917 N NZ  . LYS D 2 127 ? 7.432   15.634  12.251  1.00 73.04 ?  127 LYS G NZ  1 
ATOM   5918 N N   . SER D 2 128 ? 8.894   12.037  5.395   1.00 57.87 ?  128 SER G N   1 
ATOM   5919 C CA  . SER D 2 128 ? 8.905   10.868  4.523   1.00 55.25 ?  128 SER G CA  1 
ATOM   5920 C C   . SER D 2 128 ? 10.290  10.282  4.309   1.00 57.02 ?  128 SER G C   1 
ATOM   5921 O O   . SER D 2 128 ? 10.404  9.366   3.479   1.00 58.68 ?  128 SER G O   1 
ATOM   5922 C CB  . SER D 2 128 ? 8.286   11.235  3.173   1.00 60.19 ?  128 SER G CB  1 
ATOM   5923 O OG  . SER D 2 128 ? 9.115   12.151  2.470   1.00 60.42 ?  128 SER G OG  1 
ATOM   5924 N N   . GLY D 2 129 ? 11.348  10.739  4.970   1.00 53.28 ?  129 GLY G N   1 
ATOM   5925 C CA  . GLY D 2 129 ? 12.633  10.089  4.837   1.00 53.80 ?  129 GLY G CA  1 
ATOM   5926 C C   . GLY D 2 129 ? 13.471  10.512  3.653   1.00 53.80 ?  129 GLY G C   1 
ATOM   5927 O O   . GLY D 2 129 ? 14.545  9.937   3.447   1.00 53.40 ?  129 GLY G O   1 
ATOM   5928 N N   . THR D 2 130 ? 13.029  11.500  2.872   1.00 56.13 ?  130 THR G N   1 
ATOM   5929 C CA  . THR D 2 130 ? 13.816  12.030  1.766   1.00 54.19 ?  130 THR G CA  1 
ATOM   5930 C C   . THR D 2 130 ? 13.984  13.538  1.912   1.00 51.37 ?  130 THR G C   1 
ATOM   5931 O O   . THR D 2 130 ? 13.119  14.230  2.462   1.00 50.48 ?  130 THR G O   1 
ATOM   5932 C CB  . THR D 2 130 ? 13.175  11.716  0.406   1.00 55.77 ?  130 THR G CB  1 
ATOM   5933 O OG1 . THR D 2 130 ? 11.828  12.210  0.384   1.00 60.56 ?  130 THR G OG1 1 
ATOM   5934 C CG2 . THR D 2 130 ? 13.159  10.215  0.160   1.00 53.42 ?  130 THR G CG2 1 
ATOM   5935 N N   . ALA D 2 131 ? 15.118  14.039  1.416   1.00 48.30 ?  131 ALA G N   1 
ATOM   5936 C CA  . ALA D 2 131 ? 15.427  15.467  1.410   1.00 46.96 ?  131 ALA G CA  1 
ATOM   5937 C C   . ALA D 2 131 ? 15.736  15.907  -0.015  1.00 45.58 ?  131 ALA G C   1 
ATOM   5938 O O   . ALA D 2 131 ? 16.713  15.445  -0.613  1.00 44.33 ?  131 ALA G O   1 
ATOM   5939 C CB  . ALA D 2 131 ? 16.609  15.786  2.333   1.00 44.70 ?  131 ALA G CB  1 
ATOM   5940 N N   . SER D 2 132 ? 14.914  16.806  -0.551  1.00 44.66 ?  132 SER G N   1 
ATOM   5941 C CA  . SER D 2 132 ? 15.151  17.409  -1.855  1.00 39.75 ?  132 SER G CA  1 
ATOM   5942 C C   . SER D 2 132 ? 15.635  18.837  -1.649  1.00 39.52 ?  132 SER G C   1 
ATOM   5943 O O   . SER D 2 132 ? 14.975  19.627  -0.963  1.00 40.81 ?  132 SER G O   1 
ATOM   5944 C CB  . SER D 2 132 ? 13.876  17.402  -2.704  1.00 40.76 ?  132 SER G CB  1 
ATOM   5945 O OG  . SER D 2 132 ? 13.544  16.095  -3.137  1.00 42.05 ?  132 SER G OG  1 
ATOM   5946 N N   . VAL D 2 133 ? 16.780  19.172  -2.235  1.00 37.52 ?  133 VAL G N   1 
ATOM   5947 C CA  . VAL D 2 133 ? 17.298  20.532  -2.191  1.00 38.65 ?  133 VAL G CA  1 
ATOM   5948 C C   . VAL D 2 133 ? 17.262  21.088  -3.608  1.00 37.68 ?  133 VAL G C   1 
ATOM   5949 O O   . VAL D 2 133 ? 17.787  20.461  -4.536  1.00 37.41 ?  133 VAL G O   1 
ATOM   5950 C CB  . VAL D 2 133 ? 18.724  20.586  -1.621  1.00 37.57 ?  133 VAL G CB  1 
ATOM   5951 C CG1 . VAL D 2 133 ? 19.075  22.026  -1.280  1.00 37.81 ?  133 VAL G CG1 1 
ATOM   5952 C CG2 . VAL D 2 133 ? 18.866  19.672  -0.413  1.00 38.61 ?  133 VAL G CG2 1 
ATOM   5953 N N   . VAL D 2 134 ? 16.658  22.265  -3.778  1.00 35.57 ?  134 VAL G N   1 
ATOM   5954 C CA  . VAL D 2 134 ? 16.406  22.827  -5.104  1.00 36.67 ?  134 VAL G CA  1 
ATOM   5955 C C   . VAL D 2 134 ? 17.214  24.105  -5.277  1.00 34.43 ?  134 VAL G C   1 
ATOM   5956 O O   . VAL D 2 134 ? 17.248  24.961  -4.386  1.00 32.22 ?  134 VAL G O   1 
ATOM   5957 C CB  . VAL D 2 134 ? 14.909  23.096  -5.334  1.00 37.32 ?  134 VAL G CB  1 
ATOM   5958 C CG1 . VAL D 2 134 ? 14.681  23.655  -6.739  1.00 35.55 ?  134 VAL G CG1 1 
ATOM   5959 C CG2 . VAL D 2 134 ? 14.109  21.823  -5.138  1.00 35.91 ?  134 VAL G CG2 1 
ATOM   5960 N N   . CYS D 2 135 ? 17.884  24.209  -6.420  1.00 34.73 ?  135 CYS G N   1 
ATOM   5961 C CA  . CYS D 2 135 ? 18.583  25.404  -6.855  1.00 36.16 ?  135 CYS G CA  1 
ATOM   5962 C C   . CYS D 2 135 ? 17.866  25.944  -8.085  1.00 35.75 ?  135 CYS G C   1 
ATOM   5963 O O   . CYS D 2 135 ? 17.585  25.187  -9.020  1.00 33.92 ?  135 CYS G O   1 
ATOM   5964 C CB  . CYS D 2 135 ? 20.047  25.080  -7.166  1.00 36.00 ?  135 CYS G CB  1 
ATOM   5965 S SG  . CYS D 2 135 ? 21.071  26.498  -7.615  1.00 42.78 ?  135 CYS G SG  1 
ATOM   5966 N N   . LEU D 2 136 ? 17.554  27.244  -8.070  1.00 33.37 ?  136 LEU G N   1 
ATOM   5967 C CA  . LEU D 2 136 ? 16.817  27.893  -9.143  1.00 32.20 ?  136 LEU G CA  1 
ATOM   5968 C C   . LEU D 2 136 ? 17.697  28.949  -9.799  1.00 31.20 ?  136 LEU G C   1 
ATOM   5969 O O   . LEU D 2 136 ? 18.251  29.804  -9.106  1.00 31.76 ?  136 LEU G O   1 
ATOM   5970 C CB  . LEU D 2 136 ? 15.538  28.553  -8.610  1.00 30.68 ?  136 LEU G CB  1 
ATOM   5971 C CG  . LEU D 2 136 ? 14.779  29.413  -9.629  1.00 31.64 ?  136 LEU G CG  1 
ATOM   5972 C CD1 . LEU D 2 136 ? 14.374  28.582  -10.849 1.00 31.36 ?  136 LEU G CD1 1 
ATOM   5973 C CD2 . LEU D 2 136 ? 13.564  30.087  -9.003  1.00 32.53 ?  136 LEU G CD2 1 
ATOM   5974 N N   . LEU D 2 137 ? 17.811  28.887  -11.129 1.00 30.31 ?  137 LEU G N   1 
ATOM   5975 C CA  . LEU D 2 137 ? 18.433  29.922  -11.951 1.00 31.15 ?  137 LEU G CA  1 
ATOM   5976 C C   . LEU D 2 137 ? 17.342  30.571  -12.789 1.00 31.37 ?  137 LEU G C   1 
ATOM   5977 O O   . LEU D 2 137 ? 16.622  29.874  -13.505 1.00 28.94 ?  137 LEU G O   1 
ATOM   5978 C CB  . LEU D 2 137 ? 19.492  29.323  -12.881 1.00 29.94 ?  137 LEU G CB  1 
ATOM   5979 C CG  . LEU D 2 137 ? 20.888  29.013  -12.364 1.00 32.18 ?  137 LEU G CG  1 
ATOM   5980 C CD1 . LEU D 2 137 ? 20.823  27.976  -11.265 1.00 32.64 ?  137 LEU G CD1 1 
ATOM   5981 C CD2 . LEU D 2 137 ? 21.707  28.489  -13.526 1.00 32.26 ?  137 LEU G CD2 1 
ATOM   5982 N N   . ASN D 2 138 ? 17.221  31.895  -12.726 1.00 30.90 ?  138 ASN G N   1 
ATOM   5983 C CA  . ASN D 2 138 ? 16.068  32.543  -13.348 1.00 28.66 ?  138 ASN G CA  1 
ATOM   5984 C C   . ASN D 2 138 ? 16.508  33.648  -14.294 1.00 30.24 ?  138 ASN G C   1 
ATOM   5985 O O   . ASN D 2 138 ? 17.468  34.369  -14.002 1.00 28.48 ?  138 ASN G O   1 
ATOM   5986 C CB  . ASN D 2 138 ? 15.134  33.131  -12.300 1.00 31.24 ?  138 ASN G CB  1 
ATOM   5987 C CG  . ASN D 2 138 ? 13.819  33.601  -12.904 1.00 33.94 ?  138 ASN G CG  1 
ATOM   5988 O OD1 . ASN D 2 138 ? 13.131  32.825  -13.571 1.00 36.01 ?  138 ASN G OD1 1 
ATOM   5989 N ND2 . ASN D 2 138 ? 13.469  34.859  -12.682 1.00 35.58 ?  138 ASN G ND2 1 
ATOM   5990 N N   . ASN D 2 139 ? 15.790  33.788  -15.420 1.00 30.42 ?  139 ASN G N   1 
ATOM   5991 C CA  . ASN D 2 139 ? 15.936  34.957  -16.308 1.00 29.71 ?  139 ASN G CA  1 
ATOM   5992 C C   . ASN D 2 139 ? 17.359  35.068  -16.856 1.00 28.54 ?  139 ASN G C   1 
ATOM   5993 O O   . ASN D 2 139 ? 18.000  36.109  -16.738 1.00 31.25 ?  139 ASN G O   1 
ATOM   5994 C CB  . ASN D 2 139 ? 15.544  36.254  -15.585 1.00 34.18 ?  139 ASN G CB  1 
ATOM   5995 C CG  . ASN D 2 139 ? 15.528  37.490  -16.509 1.00 33.95 ?  139 ASN G CG  1 
ATOM   5996 O OD1 . ASN D 2 139 ? 16.157  38.517  -16.203 1.00 32.31 ?  139 ASN G OD1 1 
ATOM   5997 N ND2 . ASN D 2 139 ? 14.859  37.380  -17.652 1.00 33.52 ?  139 ASN G ND2 1 
ATOM   5998 N N   . PHE D 2 140 ? 17.863  33.992  -17.455 1.00 24.85 ?  140 PHE G N   1 
ATOM   5999 C CA  . PHE D 2 140 ? 19.220  34.036  -17.991 1.00 26.20 ?  140 PHE G CA  1 
ATOM   6000 C C   . PHE D 2 140 ? 19.254  33.699  -19.475 1.00 25.74 ?  140 PHE G C   1 
ATOM   6001 O O   . PHE D 2 140 ? 18.378  33.019  -20.006 1.00 27.04 ?  140 PHE G O   1 
ATOM   6002 C CB  . PHE D 2 140 ? 20.188  33.108  -17.205 1.00 26.61 ?  140 PHE G CB  1 
ATOM   6003 C CG  . PHE D 2 140 ? 19.929  31.629  -17.363 1.00 27.02 ?  140 PHE G CG  1 
ATOM   6004 C CD1 . PHE D 2 140 ? 19.063  30.962  -16.497 1.00 24.29 ?  140 PHE G CD1 1 
ATOM   6005 C CD2 . PHE D 2 140 ? 20.581  30.896  -18.350 1.00 28.32 ?  140 PHE G CD2 1 
ATOM   6006 C CE1 . PHE D 2 140 ? 18.843  29.597  -16.615 1.00 27.81 ?  140 PHE G CE1 1 
ATOM   6007 C CE2 . PHE D 2 140 ? 20.363  29.519  -18.486 1.00 27.48 ?  140 PHE G CE2 1 
ATOM   6008 C CZ  . PHE D 2 140 ? 19.499  28.871  -17.609 1.00 27.97 ?  140 PHE G CZ  1 
ATOM   6009 N N   . TYR D 2 141 ? 20.293  34.200  -20.142 1.00 24.53 ?  141 TYR G N   1 
ATOM   6010 C CA  . TYR D 2 141 ? 20.510  33.983  -21.563 1.00 25.19 ?  141 TYR G CA  1 
ATOM   6011 C C   . TYR D 2 141 ? 21.975  34.271  -21.852 1.00 25.71 ?  141 TYR G C   1 
ATOM   6012 O O   . TYR D 2 141 ? 22.476  35.309  -21.419 1.00 25.73 ?  141 TYR G O   1 
ATOM   6013 C CB  . TYR D 2 141 ? 19.629  34.910  -22.403 1.00 25.77 ?  141 TYR G CB  1 
ATOM   6014 C CG  . TYR D 2 141 ? 19.630  34.563  -23.876 1.00 28.24 ?  141 TYR G CG  1 
ATOM   6015 C CD1 . TYR D 2 141 ? 18.722  33.640  -24.403 1.00 28.11 ?  141 TYR G CD1 1 
ATOM   6016 C CD2 . TYR D 2 141 ? 20.569  35.130  -24.732 1.00 29.45 ?  141 TYR G CD2 1 
ATOM   6017 C CE1 . TYR D 2 141 ? 18.737  33.320  -25.744 1.00 31.22 ?  141 TYR G CE1 1 
ATOM   6018 C CE2 . TYR D 2 141 ? 20.592  34.816  -26.074 1.00 30.27 ?  141 TYR G CE2 1 
ATOM   6019 C CZ  . TYR D 2 141 ? 19.685  33.910  -26.576 1.00 28.68 ?  141 TYR G CZ  1 
ATOM   6020 O OH  . TYR D 2 141 ? 19.708  33.607  -27.914 1.00 29.93 ?  141 TYR G OH  1 
ATOM   6021 N N   . PRO D 2 142 ? 22.681  33.419  -22.609 1.00 26.71 ?  142 PRO G N   1 
ATOM   6022 C CA  . PRO D 2 142 ? 22.224  32.223  -23.324 1.00 29.21 ?  142 PRO G CA  1 
ATOM   6023 C C   . PRO D 2 142 ? 21.942  31.046  -22.409 1.00 29.38 ?  142 PRO G C   1 
ATOM   6024 O O   . PRO D 2 142 ? 22.133  31.106  -21.198 1.00 29.88 ?  142 PRO G O   1 
ATOM   6025 C CB  . PRO D 2 142 ? 23.406  31.895  -24.268 1.00 32.79 ?  142 PRO G CB  1 
ATOM   6026 C CG  . PRO D 2 142 ? 24.286  33.109  -24.248 1.00 35.23 ?  142 PRO G CG  1 
ATOM   6027 C CD  . PRO D 2 142 ? 24.106  33.671  -22.875 1.00 31.06 ?  142 PRO G CD  1 
ATOM   6028 N N   . ARG D 2 143 ? 21.497  29.957  -23.035 1.00 32.03 ?  143 ARG G N   1 
ATOM   6029 C CA  . ARG D 2 143 ? 21.037  28.772  -22.313 1.00 33.72 ?  143 ARG G CA  1 
ATOM   6030 C C   . ARG D 2 143 ? 22.167  28.060  -21.579 1.00 34.94 ?  143 ARG G C   1 
ATOM   6031 O O   . ARG D 2 143 ? 21.920  27.401  -20.563 1.00 37.69 ?  143 ARG G O   1 
ATOM   6032 C CB  . ARG D 2 143 ? 20.364  27.824  -23.304 1.00 35.40 ?  143 ARG G CB  1 
ATOM   6033 C CG  . ARG D 2 143 ? 19.536  26.718  -22.691 1.00 38.84 ?  143 ARG G CG  1 
ATOM   6034 C CD  . ARG D 2 143 ? 19.044  25.813  -23.802 1.00 42.45 ?  143 ARG G CD  1 
ATOM   6035 N NE  . ARG D 2 143 ? 18.180  24.749  -23.310 1.00 49.35 ?  143 ARG G NE  1 
ATOM   6036 C CZ  . ARG D 2 143 ? 18.586  23.501  -23.124 1.00 52.11 ?  143 ARG G CZ  1 
ATOM   6037 N NH1 . ARG D 2 143 ? 19.845  23.145  -23.335 1.00 53.60 ?  143 ARG G NH1 1 
ATOM   6038 N NH2 . ARG D 2 143 ? 17.711  22.590  -22.710 1.00 55.56 ?  143 ARG G NH2 1 
ATOM   6039 N N   . GLU D 2 144 ? 23.394  28.163  -22.067 1.00 35.56 ?  144 GLU G N   1 
ATOM   6040 C CA  . GLU D 2 144 ? 24.500  27.398  -21.488 1.00 39.60 ?  144 GLU G CA  1 
ATOM   6041 C C   . GLU D 2 144 ? 24.779  27.880  -20.071 1.00 36.12 ?  144 GLU G C   1 
ATOM   6042 O O   . GLU D 2 144 ? 25.175  29.031  -19.856 1.00 34.71 ?  144 GLU G O   1 
ATOM   6043 C CB  . GLU D 2 144 ? 25.741  27.516  -22.364 1.00 42.26 ?  144 GLU G CB  1 
ATOM   6044 C CG  . GLU D 2 144 ? 25.709  26.602  -23.576 1.00 43.45 ?  144 GLU G CG  1 
ATOM   6045 C CD  . GLU D 2 144 ? 24.638  27.011  -24.565 1.00 45.88 ?  144 GLU G CD  1 
ATOM   6046 O OE1 . GLU D 2 144 ? 24.475  28.239  -24.776 1.00 46.70 ?  144 GLU G OE1 1 
ATOM   6047 O OE2 . GLU D 2 144 ? 23.972  26.113  -25.139 1.00 47.12 ?  144 GLU G OE2 1 
ATOM   6048 N N   . ALA D 2 145 ? 24.564  26.999  -19.100 1.00 37.24 ?  145 ALA G N   1 
ATOM   6049 C CA  . ALA D 2 145 ? 24.860  27.292  -17.710 1.00 36.54 ?  145 ALA G CA  1 
ATOM   6050 C C   . ALA D 2 145 ? 25.447  26.041  -17.077 1.00 38.19 ?  145 ALA G C   1 
ATOM   6051 O O   . ALA D 2 145 ? 25.208  24.920  -17.529 1.00 41.75 ?  145 ALA G O   1 
ATOM   6052 C CB  . ALA D 2 145 ? 23.612  27.759  -16.949 1.00 36.44 ?  145 ALA G CB  1 
ATOM   6053 N N   . LYS D 2 146 ? 26.240  26.247  -16.039 1.00 36.45 ?  146 LYS G N   1 
ATOM   6054 C CA  . LYS D 2 146 ? 26.857  25.160  -15.290 1.00 37.29 ?  146 LYS G CA  1 
ATOM   6055 C C   . LYS D 2 146 ? 26.405  25.287  -13.845 1.00 38.74 ?  146 LYS G C   1 
ATOM   6056 O O   . LYS D 2 146 ? 26.617  26.330  -13.213 1.00 36.72 ?  146 LYS G O   1 
ATOM   6057 C CB  . LYS D 2 146 ? 28.385  25.217  -15.391 1.00 40.53 ?  146 LYS G CB  1 
ATOM   6058 C CG  . LYS D 2 146 ? 29.093  23.891  -15.133 1.00 45.49 ?  146 LYS G CG  1 
ATOM   6059 C CD  . LYS D 2 146 ? 30.531  24.164  -14.703 1.00 50.55 ?  146 LYS G CD  1 
ATOM   6060 C CE  . LYS D 2 146 ? 31.494  23.068  -15.109 1.00 55.82 ?  146 LYS G CE  1 
ATOM   6061 N NZ  . LYS D 2 146 ? 32.874  23.455  -14.691 1.00 52.81 ?  146 LYS G NZ  1 
ATOM   6062 N N   . VAL D 2 147 ? 25.778  24.238  -13.324 1.00 38.11 ?  147 VAL G N   1 
ATOM   6063 C CA  . VAL D 2 147 ? 25.277  24.233  -11.959 1.00 37.81 ?  147 VAL G CA  1 
ATOM   6064 C C   . VAL D 2 147 ? 25.913  23.052  -11.242 1.00 38.69 ?  147 VAL G C   1 
ATOM   6065 O O   . VAL D 2 147 ? 25.720  21.897  -11.643 1.00 37.89 ?  147 VAL G O   1 
ATOM   6066 C CB  . VAL D 2 147 ? 23.746  24.152  -11.919 1.00 38.89 ?  147 VAL G CB  1 
ATOM   6067 C CG1 . VAL D 2 147 ? 23.250  24.191  -10.480 1.00 41.60 ?  147 VAL G CG1 1 
ATOM   6068 C CG2 . VAL D 2 147 ? 23.145  25.291  -12.742 1.00 40.04 ?  147 VAL G CG2 1 
ATOM   6069 N N   . GLN D 2 148 ? 26.663  23.338  -10.186 1.00 38.36 ?  148 GLN G N   1 
ATOM   6070 C CA  . GLN D 2 148 ? 27.414  22.326  -9.458  1.00 38.84 ?  148 GLN G CA  1 
ATOM   6071 C C   . GLN D 2 148 ? 26.969  22.313  -8.007  1.00 39.85 ?  148 GLN G C   1 
ATOM   6072 O O   . GLN D 2 148 ? 26.977  23.355  -7.340  1.00 37.80 ?  148 GLN G O   1 
ATOM   6073 C CB  . GLN D 2 148 ? 28.906  22.609  -9.552  1.00 40.08 ?  148 GLN G CB  1 
ATOM   6074 C CG  . GLN D 2 148 ? 29.468  22.341  -10.919 1.00 45.09 ?  148 GLN G CG  1 
ATOM   6075 C CD  . GLN D 2 148 ? 30.923  22.721  -11.001 1.00 51.37 ?  148 GLN G CD  1 
ATOM   6076 O OE1 . GLN D 2 148 ? 31.269  23.901  -10.862 1.00 50.37 ?  148 GLN G OE1 1 
ATOM   6077 N NE2 . GLN D 2 148 ? 31.791  21.736  -11.210 1.00 50.58 ?  148 GLN G NE2 1 
ATOM   6078 N N   . TRP D 2 149 ? 26.581  21.136  -7.525  1.00 39.24 ?  149 TRP G N   1 
ATOM   6079 C CA  . TRP D 2 149 ? 26.193  20.960  -6.134  1.00 39.46 ?  149 TRP G CA  1 
ATOM   6080 C C   . TRP D 2 149 ? 27.443  20.703  -5.302  1.00 43.88 ?  149 TRP G C   1 
ATOM   6081 O O   . TRP D 2 149 ? 28.283  19.874  -5.667  1.00 44.50 ?  149 TRP G O   1 
ATOM   6082 C CB  . TRP D 2 149 ? 25.204  19.800  -5.999  1.00 40.26 ?  149 TRP G CB  1 
ATOM   6083 C CG  . TRP D 2 149 ? 23.798  20.193  -6.318  1.00 38.63 ?  149 TRP G CG  1 
ATOM   6084 C CD1 . TRP D 2 149 ? 23.094  19.875  -7.442  1.00 38.74 ?  149 TRP G CD1 1 
ATOM   6085 C CD2 . TRP D 2 149 ? 22.920  20.975  -5.504  1.00 37.84 ?  149 TRP G CD2 1 
ATOM   6086 N NE1 . TRP D 2 149 ? 21.836  20.415  -7.383  1.00 38.51 ?  149 TRP G NE1 1 
ATOM   6087 C CE2 . TRP D 2 149 ? 21.705  21.099  -6.203  1.00 38.56 ?  149 TRP G CE2 1 
ATOM   6088 C CE3 . TRP D 2 149 ? 23.047  21.589  -4.255  1.00 39.22 ?  149 TRP G CE3 1 
ATOM   6089 C CZ2 . TRP D 2 149 ? 20.624  21.808  -5.693  1.00 37.94 ?  149 TRP G CZ2 1 
ATOM   6090 C CZ3 . TRP D 2 149 ? 21.975  22.299  -3.755  1.00 37.42 ?  149 TRP G CZ3 1 
ATOM   6091 C CH2 . TRP D 2 149 ? 20.779  22.406  -4.473  1.00 38.94 ?  149 TRP G CH2 1 
ATOM   6092 N N   . LYS D 2 150 ? 27.586  21.441  -4.207  1.00 39.64 ?  150 LYS G N   1 
ATOM   6093 C CA  . LYS D 2 150 ? 28.609  21.158  -3.209  1.00 42.23 ?  150 LYS G CA  1 
ATOM   6094 C C   . LYS D 2 150 ? 27.931  20.968  -1.865  1.00 45.96 ?  150 LYS G C   1 
ATOM   6095 O O   . LYS D 2 150 ? 27.159  21.828  -1.425  1.00 41.40 ?  150 LYS G O   1 
ATOM   6096 C CB  . LYS D 2 150 ? 29.681  22.251  -3.144  1.00 41.81 ?  150 LYS G CB  1 
ATOM   6097 C CG  . LYS D 2 150 ? 30.227  22.679  -4.500  1.00 41.98 ?  150 LYS G CG  1 
ATOM   6098 C CD  . LYS D 2 150 ? 31.468  23.541  -4.332  1.00 45.64 ?  150 LYS G CD  1 
ATOM   6099 C CE  . LYS D 2 150 ? 31.087  24.944  -3.890  1.00 52.25 ?  150 LYS G CE  1 
ATOM   6100 N NZ  . LYS D 2 150 ? 32.259  25.772  -3.475  1.00 56.58 ?  150 LYS G NZ  1 
ATOM   6101 N N   . VAL D 2 151 ? 28.186  19.822  -1.243  1.00 45.59 ?  151 VAL G N   1 
ATOM   6102 C CA  . VAL D 2 151 ? 27.684  19.519  0.086   1.00 42.26 ?  151 VAL G CA  1 
ATOM   6103 C C   . VAL D 2 151 ? 28.897  19.436  0.998   1.00 47.63 ?  151 VAL G C   1 
ATOM   6104 O O   . VAL D 2 151 ? 29.766  18.573  0.810   1.00 45.30 ?  151 VAL G O   1 
ATOM   6105 C CB  . VAL D 2 151 ? 26.870  18.220  0.106   1.00 44.08 ?  151 VAL G CB  1 
ATOM   6106 C CG1 . VAL D 2 151 ? 26.540  17.831  1.535   1.00 42.77 ?  151 VAL G CG1 1 
ATOM   6107 C CG2 . VAL D 2 151 ? 25.602  18.384  -0.728  1.00 45.31 ?  151 VAL G CG2 1 
ATOM   6108 N N   . ASP D 2 152 ? 28.972  20.362  1.953   1.00 45.16 ?  152 ASP G N   1 
ATOM   6109 C CA  . ASP D 2 152 ? 30.121  20.488  2.841   1.00 45.82 ?  152 ASP G CA  1 
ATOM   6110 C C   . ASP D 2 152 ? 31.372  20.778  2.014   1.00 48.86 ?  152 ASP G C   1 
ATOM   6111 O O   . ASP D 2 152 ? 32.427  20.162  2.189   1.00 49.98 ?  152 ASP G O   1 
ATOM   6112 C CB  . ASP D 2 152 ? 30.273  19.236  3.705   1.00 46.82 ?  152 ASP G CB  1 
ATOM   6113 C CG  . ASP D 2 152 ? 29.395  19.285  4.937   1.00 47.04 ?  152 ASP G CG  1 
ATOM   6114 O OD1 . ASP D 2 152 ? 28.888  20.382  5.255   1.00 47.50 ?  152 ASP G OD1 1 
ATOM   6115 O OD2 . ASP D 2 152 ? 29.179  18.235  5.569   1.00 48.64 ?  152 ASP G OD2 1 
ATOM   6116 N N   . ASN D 2 153 ? 31.212  21.717  1.077   1.00 44.88 ?  153 ASN G N   1 
ATOM   6117 C CA  . ASN D 2 153 ? 32.250  22.170  0.146   1.00 46.40 ?  153 ASN G CA  1 
ATOM   6118 C C   . ASN D 2 153 ? 32.861  21.016  -0.647  1.00 47.27 ?  153 ASN G C   1 
ATOM   6119 O O   . ASN D 2 153 ? 34.021  21.080  -1.053  1.00 53.32 ?  153 ASN G O   1 
ATOM   6120 C CB  . ASN D 2 153 ? 33.331  22.984  0.870   1.00 50.89 ?  153 ASN G CB  1 
ATOM   6121 C CG  . ASN D 2 153 ? 32.776  24.270  1.507   1.00 54.97 ?  153 ASN G CG  1 
ATOM   6122 O OD1 . ASN D 2 153 ? 32.212  24.249  2.604   1.00 52.03 ?  153 ASN G OD1 1 
ATOM   6123 N ND2 . ASN D 2 153 ? 32.917  25.388  0.802   1.00 53.54 ?  153 ASN G ND2 1 
ATOM   6124 N N   . ALA D 2 154 ? 32.073  19.970  -0.898  1.00 42.91 ?  154 ALA G N   1 
ATOM   6125 C CA  . ALA D 2 154 ? 32.497  18.811  -1.673  1.00 47.49 ?  154 ALA G CA  1 
ATOM   6126 C C   . ALA D 2 154 ? 31.583  18.645  -2.880  1.00 48.74 ?  154 ALA G C   1 
ATOM   6127 O O   . ALA D 2 154 ? 30.367  18.468  -2.725  1.00 46.33 ?  154 ALA G O   1 
ATOM   6128 C CB  . ALA D 2 154 ? 32.485  17.542  -0.816  1.00 45.75 ?  154 ALA G CB  1 
ATOM   6129 N N   . LEU D 2 155 ? 32.174  18.683  -4.075  1.00 46.58 ?  155 LEU G N   1 
ATOM   6130 C CA  . LEU D 2 155 ? 31.414  18.544  -5.311  1.00 47.34 ?  155 LEU G CA  1 
ATOM   6131 C C   . LEU D 2 155 ? 30.676  17.210  -5.350  1.00 49.48 ?  155 LEU G C   1 
ATOM   6132 O O   . LEU D 2 155 ? 31.237  16.164  -5.024  1.00 51.03 ?  155 LEU G O   1 
ATOM   6133 C CB  . LEU D 2 155 ? 32.354  18.669  -6.510  1.00 50.09 ?  155 LEU G CB  1 
ATOM   6134 C CG  . LEU D 2 155 ? 31.766  18.397  -7.895  1.00 53.28 ?  155 LEU G CG  1 
ATOM   6135 C CD1 . LEU D 2 155 ? 30.624  19.371  -8.189  1.00 51.48 ?  155 LEU G CD1 1 
ATOM   6136 C CD2 . LEU D 2 155 ? 32.851  18.504  -8.955  1.00 53.12 ?  155 LEU G CD2 1 
ATOM   6137 N N   . GLN D 2 156 ? 29.404  17.285  -5.736  1.00 46.85 ?  156 GLN G N   1 
ATOM   6138 C CA  . GLN D 2 156 ? 28.537  16.087  -5.764  1.00 48.89 ?  156 GLN G CA  1 
ATOM   6139 C C   . GLN D 2 156 ? 28.413  15.535  -7.185  1.00 51.80 ?  156 GLN G C   1 
ATOM   6140 O O   . GLN D 2 156 ? 28.620  16.297  -8.137  1.00 53.95 ?  156 GLN G O   1 
ATOM   6141 C CB  . GLN D 2 156 ? 27.167  16.429  -5.186  1.00 47.99 ?  156 GLN G CB  1 
ATOM   6142 C CG  . GLN D 2 156 ? 27.230  16.963  -3.768  1.00 48.14 ?  156 GLN G CG  1 
ATOM   6143 C CD  . GLN D 2 156 ? 27.754  15.906  -2.830  1.00 50.85 ?  156 GLN G CD  1 
ATOM   6144 O OE1 . GLN D 2 156 ? 27.144  14.855  -2.655  1.00 50.90 ?  156 GLN G OE1 1 
ATOM   6145 N NE2 . GLN D 2 156 ? 28.901  16.174  -2.228  1.00 50.08 ?  156 GLN G NE2 1 
ATOM   6146 N N   . SER D 2 157 ? 28.073  14.259  -7.303  1.00 53.99 ?  157 SER G N   1 
ATOM   6147 C CA  . SER D 2 157 ? 27.957  13.570  -8.581  1.00 54.60 ?  157 SER G CA  1 
ATOM   6148 C C   . SER D 2 157 ? 26.932  12.458  -8.452  1.00 55.90 ?  157 SER G C   1 
ATOM   6149 O O   . SER D 2 157 ? 26.891  11.756  -7.438  1.00 57.56 ?  157 SER G O   1 
ATOM   6150 C CB  . SER D 2 157 ? 29.299  12.979  -9.028  1.00 55.17 ?  157 SER G CB  1 
ATOM   6151 O OG  . SER D 2 157 ? 30.283  13.988  -9.146  1.00 58.95 ?  157 SER G OG  1 
ATOM   6152 N N   . GLY D 2 158 ? 26.104  12.306  -9.482  1.00 54.65 ?  158 GLY G N   1 
ATOM   6153 C CA  . GLY D 2 158 ? 25.192  11.186  -9.569  1.00 55.63 ?  158 GLY G CA  1 
ATOM   6154 C C   . GLY D 2 158 ? 23.957  11.262  -8.698  1.00 55.91 ?  158 GLY G C   1 
ATOM   6155 O O   . GLY D 2 158 ? 23.180  10.297  -8.679  1.00 57.30 ?  158 GLY G O   1 
ATOM   6156 N N   . ASN D 2 159 ? 23.732  12.370  -7.983  1.00 53.80 ?  159 ASN G N   1 
ATOM   6157 C CA  . ASN D 2 159 ? 22.543  12.485  -7.146  1.00 50.74 ?  159 ASN G CA  1 
ATOM   6158 C C   . ASN D 2 159 ? 21.786  13.791  -7.398  1.00 50.59 ?  159 ASN G C   1 
ATOM   6159 O O   . ASN D 2 159 ? 21.057  14.272  -6.522  1.00 50.55 ?  159 ASN G O   1 
ATOM   6160 C CB  . ASN D 2 159 ? 22.895  12.351  -5.661  1.00 49.56 ?  159 ASN G CB  1 
ATOM   6161 C CG  . ASN D 2 159 ? 23.983  13.315  -5.225  1.00 53.34 ?  159 ASN G CG  1 
ATOM   6162 O OD1 . ASN D 2 159 ? 24.472  14.127  -6.014  1.00 53.10 ?  159 ASN G OD1 1 
ATOM   6163 N ND2 . ASN D 2 159 ? 24.356  13.243  -3.949  1.00 52.19 ?  159 ASN G ND2 1 
ATOM   6164 N N   . SER D 2 160 ? 21.917  14.372  -8.587  1.00 49.69 ?  160 SER G N   1 
ATOM   6165 C CA  . SER D 2 160 ? 21.109  15.539  -8.918  1.00 46.59 ?  160 SER G CA  1 
ATOM   6166 C C   . SER D 2 160 ? 20.552  15.404  -10.327 1.00 45.76 ?  160 SER G C   1 
ATOM   6167 O O   . SER D 2 160 ? 21.048  14.633  -11.150 1.00 46.27 ?  160 SER G O   1 
ATOM   6168 C CB  . SER D 2 160 ? 21.896  16.848  -8.784  1.00 43.74 ?  160 SER G CB  1 
ATOM   6169 O OG  . SER D 2 160 ? 23.173  16.744  -9.380  1.00 49.14 ?  160 SER G OG  1 
ATOM   6170 N N   . GLN D 2 161 ? 19.494  16.172  -10.584 1.00 44.06 ?  161 GLN G N   1 
ATOM   6171 C CA  . GLN D 2 161 ? 18.826  16.219  -11.875 1.00 41.83 ?  161 GLN G CA  1 
ATOM   6172 C C   . GLN D 2 161 ? 18.500  17.667  -12.210 1.00 42.51 ?  161 GLN G C   1 
ATOM   6173 O O   . GLN D 2 161 ? 18.093  18.437  -11.332 1.00 40.51 ?  161 GLN G O   1 
ATOM   6174 C CB  . GLN D 2 161 ? 17.556  15.370  -11.847 1.00 41.83 ?  161 GLN G CB  1 
ATOM   6175 C CG  . GLN D 2 161 ? 17.862  13.884  -11.705 1.00 46.58 ?  161 GLN G CG  1 
ATOM   6176 C CD  . GLN D 2 161 ? 16.703  13.003  -12.114 1.00 46.41 ?  161 GLN G CD  1 
ATOM   6177 O OE1 . GLN D 2 161 ? 15.636  13.059  -11.504 1.00 46.88 ?  161 GLN G OE1 1 
ATOM   6178 N NE2 . GLN D 2 161 ? 16.904  12.184  -13.146 1.00 46.66 ?  161 GLN G NE2 1 
ATOM   6179 N N   . GLU D 2 162 ? 18.682  18.031  -13.477 1.00 38.31 ?  162 GLU G N   1 
ATOM   6180 C CA  . GLU D 2 162 ? 18.430  19.384  -13.955 1.00 38.99 ?  162 GLU G CA  1 
ATOM   6181 C C   . GLU D 2 162 ? 17.226  19.410  -14.883 1.00 39.54 ?  162 GLU G C   1 
ATOM   6182 O O   . GLU D 2 162 ? 16.947  18.441  -15.592 1.00 37.82 ?  162 GLU G O   1 
ATOM   6183 C CB  . GLU D 2 162 ? 19.631  19.946  -14.718 1.00 38.55 ?  162 GLU G CB  1 
ATOM   6184 C CG  . GLU D 2 162 ? 20.690  20.603  -13.867 1.00 46.10 ?  162 GLU G CG  1 
ATOM   6185 C CD  . GLU D 2 162 ? 21.790  21.233  -14.716 1.00 47.35 ?  162 GLU G CD  1 
ATOM   6186 O OE1 . GLU D 2 162 ? 21.691  21.176  -15.965 1.00 51.44 ?  162 GLU G OE1 1 
ATOM   6187 O OE2 . GLU D 2 162 ? 22.750  21.786  -14.140 1.00 48.98 ?  162 GLU G OE2 1 
ATOM   6188 N N   . SER D 2 163 ? 16.534  20.546  -14.890 1.00 35.68 ?  163 SER G N   1 
ATOM   6189 C CA  . SER D 2 163 ? 15.459  20.813  -15.832 1.00 35.12 ?  163 SER G CA  1 
ATOM   6190 C C   . SER D 2 163 ? 15.570  22.253  -16.307 1.00 36.66 ?  163 SER G C   1 
ATOM   6191 O O   . SER D 2 163 ? 15.706  23.169  -15.489 1.00 35.15 ?  163 SER G O   1 
ATOM   6192 C CB  . SER D 2 163 ? 14.090  20.586  -15.187 1.00 34.89 ?  163 SER G CB  1 
ATOM   6193 O OG  . SER D 2 163 ? 13.062  20.781  -16.125 1.00 38.95 ?  163 SER G OG  1 
ATOM   6194 N N   . VAL D 2 164 ? 15.473  22.455  -17.618 1.00 37.57 ?  164 VAL G N   1 
ATOM   6195 C CA  . VAL D 2 164 ? 15.536  23.777  -18.222 1.00 35.13 ?  164 VAL G CA  1 
ATOM   6196 C C   . VAL D 2 164 ? 14.205  24.053  -18.902 1.00 38.45 ?  164 VAL G C   1 
ATOM   6197 O O   . VAL D 2 164 ? 13.666  23.189  -19.600 1.00 36.90 ?  164 VAL G O   1 
ATOM   6198 C CB  . VAL D 2 164 ? 16.687  23.887  -19.242 1.00 39.14 ?  164 VAL G CB  1 
ATOM   6199 C CG1 . VAL D 2 164 ? 16.775  25.302  -19.778 1.00 40.27 ?  164 VAL G CG1 1 
ATOM   6200 C CG2 . VAL D 2 164 ? 17.995  23.450  -18.624 1.00 42.15 ?  164 VAL G CG2 1 
ATOM   6201 N N   . THR D 2 165 ? 13.674  25.250  -18.701 1.00 35.96 ?  165 THR G N   1 
ATOM   6202 C CA  . THR D 2 165 ? 12.477  25.612  -19.434 1.00 41.07 ?  165 THR G CA  1 
ATOM   6203 C C   . THR D 2 165 ? 12.778  25.705  -20.925 1.00 43.22 ?  165 THR G C   1 
ATOM   6204 O O   . THR D 2 165 ? 13.927  25.841  -21.354 1.00 40.50 ?  165 THR G O   1 
ATOM   6205 C CB  . THR D 2 165 ? 11.928  26.954  -18.965 1.00 38.39 ?  165 THR G CB  1 
ATOM   6206 O OG1 . THR D 2 165 ? 12.883  28.001  -19.254 1.00 36.88 ?  165 THR G OG1 1 
ATOM   6207 C CG2 . THR D 2 165 ? 11.619  26.904  -17.477 1.00 38.20 ?  165 THR G CG2 1 
ATOM   6208 N N   . GLU D 2 166 ? 11.721  25.624  -21.720 1.00 42.93 ?  166 GLU G N   1 
ATOM   6209 C CA  . GLU D 2 166 ? 11.780  26.241  -23.029 1.00 45.89 ?  166 GLU G CA  1 
ATOM   6210 C C   . GLU D 2 166 ? 12.064  27.739  -22.869 1.00 43.78 ?  166 GLU G C   1 
ATOM   6211 O O   . GLU D 2 166 ? 11.908  28.316  -21.786 1.00 40.98 ?  166 GLU G O   1 
ATOM   6212 C CB  . GLU D 2 166 ? 10.479  25.987  -23.793 1.00 46.85 ?  166 GLU G CB  1 
ATOM   6213 C CG  . GLU D 2 166 ? 9.240   26.609  -23.157 1.00 51.36 ?  166 GLU G CG  1 
ATOM   6214 C CD  . GLU D 2 166 ? 8.593   25.723  -22.080 1.00 59.49 ?  166 GLU G CD  1 
ATOM   6215 O OE1 . GLU D 2 166 ? 9.294   25.222  -21.162 1.00 53.15 ?  166 GLU G OE1 1 
ATOM   6216 O OE2 . GLU D 2 166 ? 7.357   25.530  -22.161 1.00 60.66 ?  166 GLU G OE2 1 
ATOM   6217 N N   . GLN D 2 167 ? 12.510  28.362  -23.958 1.00 41.72 ?  167 GLN G N   1 
ATOM   6218 C CA  . GLN D 2 167 ? 12.788  29.820  -23.931 1.00 41.91 ?  167 GLN G CA  1 
ATOM   6219 C C   . GLN D 2 167 ? 11.494  30.535  -23.556 1.00 43.43 ?  167 GLN G C   1 
ATOM   6220 O O   . GLN D 2 167 ? 10.488  30.328  -24.253 1.00 44.26 ?  167 GLN G O   1 
ATOM   6221 C CB  . GLN D 2 167 ? 13.344  30.319  -25.266 1.00 41.98 ?  167 GLN G CB  1 
ATOM   6222 C CG  . GLN D 2 167 ? 14.230  31.548  -25.144 1.00 39.31 ?  167 GLN G CG  1 
ATOM   6223 C CD  . GLN D 2 167 ? 14.906  31.881  -26.451 1.00 45.29 ?  167 GLN G CD  1 
ATOM   6224 O OE1 . GLN D 2 167 ? 15.384  31.008  -27.167 1.00 50.86 ?  167 GLN G OE1 1 
ATOM   6225 N NE2 . GLN D 2 167 ? 14.948  33.161  -26.776 1.00 44.86 ?  167 GLN G NE2 1 
ATOM   6226 N N   . ASP D 2 168 ? 11.538  31.329  -22.493 1.00 40.63 ?  168 ASP G N   1 
ATOM   6227 C CA  . ASP D 2 168 ? 10.350  32.033  -22.012 1.00 41.26 ?  168 ASP G CA  1 
ATOM   6228 C C   . ASP D 2 168 ? 9.776   32.892  -23.124 1.00 40.47 ?  168 ASP G C   1 
ATOM   6229 O O   . ASP D 2 168 ? 10.507  33.597  -23.823 1.00 40.12 ?  168 ASP G O   1 
ATOM   6230 C CB  . ASP D 2 168 ? 10.662  32.914  -20.802 1.00 38.38 ?  168 ASP G CB  1 
ATOM   6231 C CG  . ASP D 2 168 ? 9.409   33.596  -20.245 1.00 44.66 ?  168 ASP G CG  1 
ATOM   6232 O OD1 . ASP D 2 168 ? 8.535   32.872  -19.719 1.00 46.69 ?  168 ASP G OD1 1 
ATOM   6233 O OD2 . ASP D 2 168 ? 9.273   34.838  -20.347 1.00 43.73 ?  168 ASP G OD2 1 
ATOM   6234 N N   . SER D 2 169 ? 8.457   32.830  -23.285 1.00 39.97 ?  169 SER G N   1 
ATOM   6235 C CA  . SER D 2 169 ? 7.834   33.437  -24.453 1.00 39.07 ?  169 SER G CA  1 
ATOM   6236 C C   . SER D 2 169 ? 7.964   34.957  -24.420 1.00 37.43 ?  169 SER G C   1 
ATOM   6237 O O   . SER D 2 169 ? 8.240   35.585  -25.446 1.00 39.88 ?  169 SER G O   1 
ATOM   6238 C CB  . SER D 2 169 ? 6.367   33.009  -24.529 1.00 39.98 ?  169 SER G CB  1 
ATOM   6239 O OG  . SER D 2 169 ? 6.274   31.618  -24.801 1.00 44.37 ?  169 SER G OG  1 
ATOM   6240 N N   . LYS D 2 170 ? 7.786   35.561  -23.251 1.00 36.96 ?  170 LYS G N   1 
ATOM   6241 C CA  . LYS D 2 170 ? 7.779   37.015  -23.138 1.00 38.26 ?  170 LYS G CA  1 
ATOM   6242 C C   . LYS D 2 170 ? 9.175   37.608  -23.044 1.00 35.76 ?  170 LYS G C   1 
ATOM   6243 O O   . LYS D 2 170 ? 9.472   38.602  -23.714 1.00 34.65 ?  170 LYS G O   1 
ATOM   6244 C CB  . LYS D 2 170 ? 6.962   37.433  -21.920 1.00 39.75 ?  170 LYS G CB  1 
ATOM   6245 C CG  . LYS D 2 170 ? 6.834   38.937  -21.743 1.00 42.17 ?  170 LYS G CG  1 
ATOM   6246 C CD  . LYS D 2 170 ? 6.296   39.575  -23.001 1.00 42.65 ?  170 LYS G CD  1 
ATOM   6247 C CE  . LYS D 2 170 ? 6.573   41.085  -23.069 1.00 47.39 ?  170 LYS G CE  1 
ATOM   6248 N NZ  . LYS D 2 170 ? 6.180   41.647  -24.410 1.00 39.91 ?  170 LYS G NZ  1 
ATOM   6249 N N   . ASP D 2 171 ? 10.045  37.010  -22.231 1.00 33.39 ?  171 ASP G N   1 
ATOM   6250 C CA  . ASP D 2 171 ? 11.342  37.603  -21.943 1.00 29.96 ?  171 ASP G CA  1 
ATOM   6251 C C   . ASP D 2 171 ? 12.464  37.028  -22.799 1.00 30.80 ?  171 ASP G C   1 
ATOM   6252 O O   . ASP D 2 171 ? 13.566  37.582  -22.790 1.00 28.77 ?  171 ASP G O   1 
ATOM   6253 C CB  . ASP D 2 171 ? 11.666  37.405  -20.461 1.00 33.36 ?  171 ASP G CB  1 
ATOM   6254 C CG  . ASP D 2 171 ? 10.844  38.317  -19.558 1.00 43.72 ?  171 ASP G CG  1 
ATOM   6255 O OD1 . ASP D 2 171 ? 10.025  39.105  -20.084 1.00 45.80 ?  171 ASP G OD1 1 
ATOM   6256 O OD2 . ASP D 2 171 ? 10.979  38.208  -18.315 1.00 48.15 ?  171 ASP G OD2 1 
ATOM   6257 N N   . SER D 2 172 ? 12.211  35.937  -23.526 1.00 28.00 ?  172 SER G N   1 
ATOM   6258 C CA  . SER D 2 172 ? 13.219  35.246  -24.336 1.00 33.27 ?  172 SER G CA  1 
ATOM   6259 C C   . SER D 2 172 ? 14.447  34.887  -23.506 1.00 33.35 ?  172 SER G C   1 
ATOM   6260 O O   . SER D 2 172 ? 15.592  35.048  -23.942 1.00 36.58 ?  172 SER G O   1 
ATOM   6261 C CB  . SER D 2 172 ? 13.618  36.060  -25.567 1.00 33.51 ?  172 SER G CB  1 
ATOM   6262 O OG  . SER D 2 172 ? 12.556  36.070  -26.509 1.00 39.74 ?  172 SER G OG  1 
ATOM   6263 N N   . THR D 2 173 ? 14.204  34.427  -22.284 1.00 27.72 ?  173 THR G N   1 
ATOM   6264 C CA  . THR D 2 173 ? 15.258  33.930  -21.416 1.00 27.12 ?  173 THR G CA  1 
ATOM   6265 C C   . THR D 2 173 ? 14.886  32.530  -20.956 1.00 29.23 ?  173 THR G C   1 
ATOM   6266 O O   . THR D 2 173 ? 13.808  32.013  -21.261 1.00 30.19 ?  173 THR G O   1 
ATOM   6267 C CB  . THR D 2 173 ? 15.479  34.831  -20.200 1.00 27.08 ?  173 THR G CB  1 
ATOM   6268 O OG1 . THR D 2 173 ? 14.253  34.961  -19.480 1.00 32.14 ?  173 THR G OG1 1 
ATOM   6269 C CG2 . THR D 2 173 ? 15.996  36.207  -20.635 1.00 26.74 ?  173 THR G CG2 1 
ATOM   6270 N N   . TYR D 2 174 ? 15.790  31.940  -20.189 1.00 27.28 ?  174 TYR G N   1 
ATOM   6271 C CA  . TYR D 2 174 ? 15.644  30.596  -19.665 1.00 28.81 ?  174 TYR G CA  1 
ATOM   6272 C C   . TYR D 2 174 ? 15.582  30.638  -18.153 1.00 26.80 ?  174 TYR G C   1 
ATOM   6273 O O   . TYR D 2 174 ? 16.061  31.577  -17.513 1.00 27.55 ?  174 TYR G O   1 
ATOM   6274 C CB  . TYR D 2 174 ? 16.807  29.702  -20.085 1.00 29.62 ?  174 TYR G CB  1 
ATOM   6275 C CG  . TYR D 2 174 ? 16.846  29.451  -21.565 1.00 33.99 ?  174 TYR G CG  1 
ATOM   6276 C CD1 . TYR D 2 174 ? 16.076  28.437  -22.127 1.00 33.96 ?  174 TYR G CD1 1 
ATOM   6277 C CD2 . TYR D 2 174 ? 17.657  30.215  -22.403 1.00 31.80 ?  174 TYR G CD2 1 
ATOM   6278 C CE1 . TYR D 2 174 ? 16.105  28.184  -23.479 1.00 37.28 ?  174 TYR G CE1 1 
ATOM   6279 C CE2 . TYR D 2 174 ? 17.686  29.978  -23.768 1.00 34.65 ?  174 TYR G CE2 1 
ATOM   6280 C CZ  . TYR D 2 174 ? 16.910  28.957  -24.297 1.00 40.43 ?  174 TYR G CZ  1 
ATOM   6281 O OH  . TYR D 2 174 ? 16.931  28.707  -25.647 1.00 41.13 ?  174 TYR G OH  1 
ATOM   6282 N N   . SER D 2 175 ? 14.973  29.605  -17.592 1.00 29.41 ?  175 SER G N   1 
ATOM   6283 C CA  . SER D 2 175 ? 15.108  29.292  -16.178 1.00 30.09 ?  175 SER G CA  1 
ATOM   6284 C C   . SER D 2 175 ? 15.540  27.843  -16.071 1.00 30.01 ?  175 SER G C   1 
ATOM   6285 O O   . SER D 2 175 ? 15.318  27.050  -16.990 1.00 31.37 ?  175 SER G O   1 
ATOM   6286 C CB  . SER D 2 175 ? 13.808  29.550  -15.404 1.00 34.38 ?  175 SER G CB  1 
ATOM   6287 O OG  . SER D 2 175 ? 13.504  30.941  -15.428 1.00 32.78 ?  175 SER G OG  1 
ATOM   6288 N N   . LEU D 2 176 ? 16.193  27.512  -14.961 1.00 28.25 ?  176 LEU G N   1 
ATOM   6289 C CA  . LEU D 2 176 ? 16.755  26.183  -14.785 1.00 33.10 ?  176 LEU G CA  1 
ATOM   6290 C C   . LEU D 2 176 ? 16.559  25.753  -13.346 1.00 34.96 ?  176 LEU G C   1 
ATOM   6291 O O   . LEU D 2 176 ? 16.793  26.532  -12.419 1.00 33.92 ?  176 LEU G O   1 
ATOM   6292 C CB  . LEU D 2 176 ? 18.248  26.149  -15.127 1.00 35.05 ?  176 LEU G CB  1 
ATOM   6293 C CG  . LEU D 2 176 ? 18.982  24.807  -14.991 1.00 36.71 ?  176 LEU G CG  1 
ATOM   6294 C CD1 . LEU D 2 176 ? 20.095  24.753  -16.013 1.00 37.67 ?  176 LEU G CD1 1 
ATOM   6295 C CD2 . LEU D 2 176 ? 19.529  24.566  -13.585 1.00 33.91 ?  176 LEU G CD2 1 
ATOM   6296 N N   . SER D 2 177 ? 16.163  24.498  -13.177 1.00 34.52 ?  177 SER G N   1 
ATOM   6297 C CA  . SER D 2 177 ? 16.020  23.882  -11.873 1.00 38.97 ?  177 SER G CA  1 
ATOM   6298 C C   . SER D 2 177 ? 17.060  22.781  -11.727 1.00 39.35 ?  177 SER G C   1 
ATOM   6299 O O   . SER D 2 177 ? 17.303  22.012  -12.664 1.00 38.75 ?  177 SER G O   1 
ATOM   6300 C CB  . SER D 2 177 ? 14.611  23.302  -11.700 1.00 41.99 ?  177 SER G CB  1 
ATOM   6301 O OG  . SER D 2 177 ? 14.295  23.115  -10.336 1.00 47.06 ?  177 SER G OG  1 
ATOM   6302 N N   . SER D 2 178 ? 17.691  22.728  -10.563 1.00 36.35 ?  178 SER G N   1 
ATOM   6303 C CA  . SER D 2 178 ? 18.579  21.634  -10.201 1.00 38.65 ?  178 SER G CA  1 
ATOM   6304 C C   . SER D 2 178 ? 18.145  21.107  -8.845  1.00 41.21 ?  178 SER G C   1 
ATOM   6305 O O   . SER D 2 178 ? 18.016  21.877  -7.889  1.00 40.09 ?  178 SER G O   1 
ATOM   6306 C CB  . SER D 2 178 ? 20.041  22.070  -10.161 1.00 40.19 ?  178 SER G CB  1 
ATOM   6307 O OG  . SER D 2 178 ? 20.885  20.933  -10.225 1.00 41.44 ?  178 SER G OG  1 
ATOM   6308 N N   . THR D 2 179 ? 17.906  19.801  -8.766  1.00 39.39 ?  179 THR G N   1 
ATOM   6309 C CA  . THR D 2 179 ? 17.369  19.182  -7.563  1.00 40.84 ?  179 THR G CA  1 
ATOM   6310 C C   . THR D 2 179 ? 18.342  18.121  -7.085  1.00 40.88 ?  179 THR G C   1 
ATOM   6311 O O   . THR D 2 179 ? 18.670  17.194  -7.833  1.00 38.81 ?  179 THR G O   1 
ATOM   6312 C CB  . THR D 2 179 ? 15.993  18.573  -7.822  1.00 40.97 ?  179 THR G CB  1 
ATOM   6313 O OG1 . THR D 2 179 ? 15.101  19.602  -8.265  1.00 41.56 ?  179 THR G OG1 1 
ATOM   6314 C CG2 . THR D 2 179 ? 15.452  17.949  -6.548  1.00 39.94 ?  179 THR G CG2 1 
ATOM   6315 N N   . LEU D 2 180 ? 18.828  18.285  -5.861  1.00 38.78 ?  180 LEU G N   1 
ATOM   6316 C CA  . LEU D 2 180 ? 19.688  17.309  -5.213  1.00 41.40 ?  180 LEU G CA  1 
ATOM   6317 C C   . LEU D 2 180 ? 18.820  16.502  -4.256  1.00 42.59 ?  180 LEU G C   1 
ATOM   6318 O O   . LEU D 2 180 ? 18.142  17.080  -3.400  1.00 41.29 ?  180 LEU G O   1 
ATOM   6319 C CB  . LEU D 2 180 ? 20.832  18.002  -4.475  1.00 41.06 ?  180 LEU G CB  1 
ATOM   6320 C CG  . LEU D 2 180 ? 21.809  17.084  -3.751  1.00 41.88 ?  180 LEU G CG  1 
ATOM   6321 C CD1 . LEU D 2 180 ? 22.854  16.621  -4.738  1.00 41.92 ?  180 LEU G CD1 1 
ATOM   6322 C CD2 . LEU D 2 180 ? 22.444  17.850  -2.614  1.00 41.84 ?  180 LEU G CD2 1 
ATOM   6323 N N   . THR D 2 181 ? 18.818  15.181  -4.421  1.00 43.76 ?  181 THR G N   1 
ATOM   6324 C CA  . THR D 2 181 ? 17.981  14.289  -3.625  1.00 47.09 ?  181 THR G CA  1 
ATOM   6325 C C   . THR D 2 181 ? 18.876  13.417  -2.753  1.00 48.01 ?  181 THR G C   1 
ATOM   6326 O O   . THR D 2 181 ? 19.727  12.686  -3.267  1.00 47.39 ?  181 THR G O   1 
ATOM   6327 C CB  . THR D 2 181 ? 17.094  13.410  -4.514  1.00 50.57 ?  181 THR G CB  1 
ATOM   6328 O OG1 . THR D 2 181 ? 16.541  14.194  -5.582  1.00 53.04 ?  181 THR G OG1 1 
ATOM   6329 C CG2 . THR D 2 181 ? 15.947  12.823  -3.697  1.00 48.63 ?  181 THR G CG2 1 
ATOM   6330 N N   . LEU D 2 182 ? 18.702  13.517  -1.440  1.00 47.99 ?  182 LEU G N   1 
ATOM   6331 C CA  . LEU D 2 182 ? 19.443  12.709  -0.487  1.00 46.19 ?  182 LEU G CA  1 
ATOM   6332 C C   . LEU D 2 182 ? 18.459  12.041  0.460   1.00 47.45 ?  182 LEU G C   1 
ATOM   6333 O O   . LEU D 2 182 ? 17.367  12.555  0.718   1.00 49.30 ?  182 LEU G O   1 
ATOM   6334 C CB  . LEU D 2 182 ? 20.439  13.539  0.335   1.00 47.58 ?  182 LEU G CB  1 
ATOM   6335 C CG  . LEU D 2 182 ? 21.553  14.352  -0.334  1.00 49.86 ?  182 LEU G CG  1 
ATOM   6336 C CD1 . LEU D 2 182 ? 22.317  15.145  0.714   1.00 50.83 ?  182 LEU G CD1 1 
ATOM   6337 C CD2 . LEU D 2 182 ? 22.506  13.473  -1.111  1.00 48.43 ?  182 LEU G CD2 1 
ATOM   6338 N N   . SER D 2 183 ? 18.851  10.881  0.976   1.00 51.39 ?  183 SER G N   1 
ATOM   6339 C CA  . SER D 2 183 ? 18.113  10.319  2.093   1.00 51.50 ?  183 SER G CA  1 
ATOM   6340 C C   . SER D 2 183 ? 18.149  11.299  3.257   1.00 51.21 ?  183 SER G C   1 
ATOM   6341 O O   . SER D 2 183 ? 19.149  11.988  3.480   1.00 50.16 ?  183 SER G O   1 
ATOM   6342 C CB  . SER D 2 183 ? 18.713  8.975   2.505   1.00 52.16 ?  183 SER G CB  1 
ATOM   6343 O OG  . SER D 2 183 ? 19.778  9.172   3.421   1.00 53.47 ?  183 SER G OG  1 
ATOM   6344 N N   . LYS D 2 184 ? 17.041  11.372  3.990   1.00 49.88 ?  184 LYS G N   1 
ATOM   6345 C CA  . LYS D 2 184 ? 16.993  12.177  5.202   1.00 51.90 ?  184 LYS G CA  1 
ATOM   6346 C C   . LYS D 2 184 ? 18.160  11.869  6.136   1.00 54.52 ?  184 LYS G C   1 
ATOM   6347 O O   . LYS D 2 184 ? 18.545  12.730  6.940   1.00 54.61 ?  184 LYS G O   1 
ATOM   6348 C CB  . LYS D 2 184 ? 15.628  11.944  5.862   1.00 53.39 ?  184 LYS G CB  1 
ATOM   6349 C CG  . LYS D 2 184 ? 15.238  12.848  7.011   1.00 55.86 ?  184 LYS G CG  1 
ATOM   6350 C CD  . LYS D 2 184 ? 15.498  12.173  8.340   1.00 58.82 ?  184 LYS G CD  1 
ATOM   6351 C CE  . LYS D 2 184 ? 14.532  12.687  9.394   1.00 60.76 ?  184 LYS G CE  1 
ATOM   6352 N NZ  . LYS D 2 184 ? 14.937  12.289  10.766  1.00 61.88 ?  184 LYS G NZ  1 
ATOM   6353 N N   . ALA D 2 185 ? 18.762  10.679  6.003   1.00 53.47 ?  185 ALA G N   1 
ATOM   6354 C CA  . ALA D 2 185 ? 19.926  10.308  6.803   1.00 54.90 ?  185 ALA G CA  1 
ATOM   6355 C C   . ALA D 2 185 ? 21.174  11.078  6.378   1.00 53.85 ?  185 ALA G C   1 
ATOM   6356 O O   . ALA D 2 185 ? 21.812  11.740  7.206   1.00 57.23 ?  185 ALA G O   1 
ATOM   6357 C CB  . ALA D 2 185 ? 20.167  8.798   6.718   1.00 54.04 ?  185 ALA G CB  1 
ATOM   6358 N N   . ASP D 2 186 ? 21.564  10.994  5.098   1.00 52.72 ?  186 ASP G N   1 
ATOM   6359 C CA  . ASP D 2 186 ? 22.740  11.766  4.697   1.00 55.55 ?  186 ASP G CA  1 
ATOM   6360 C C   . ASP D 2 186 ? 22.507  13.262  4.791   1.00 53.14 ?  186 ASP G C   1 
ATOM   6361 O O   . ASP D 2 186 ? 23.463  14.012  5.015   1.00 53.88 ?  186 ASP G O   1 
ATOM   6362 C CB  . ASP D 2 186 ? 23.233  11.421  3.289   1.00 56.69 ?  186 ASP G CB  1 
ATOM   6363 C CG  . ASP D 2 186 ? 23.425  9.942   3.077   1.00 64.00 ?  186 ASP G CG  1 
ATOM   6364 O OD1 . ASP D 2 186 ? 22.425  9.202   2.935   1.00 61.39 ?  186 ASP G OD1 1 
ATOM   6365 O OD2 . ASP D 2 186 ? 24.603  9.530   3.025   1.00 66.56 ?  186 ASP G OD2 1 
ATOM   6366 N N   . TYR D 2 187 ? 21.265  13.721  4.620   1.00 51.96 ?  187 TYR G N   1 
ATOM   6367 C CA  . TYR D 2 187 ? 21.000  15.150  4.745   1.00 48.64 ?  187 TYR G CA  1 
ATOM   6368 C C   . TYR D 2 187 ? 21.418  15.656  6.118   1.00 50.98 ?  187 TYR G C   1 
ATOM   6369 O O   . TYR D 2 187 ? 22.203  16.607  6.236   1.00 49.70 ?  187 TYR G O   1 
ATOM   6370 C CB  . TYR D 2 187 ? 19.523  15.452  4.490   1.00 48.25 ?  187 TYR G CB  1 
ATOM   6371 C CG  . TYR D 2 187 ? 19.180  16.921  4.637   1.00 45.62 ?  187 TYR G CG  1 
ATOM   6372 C CD1 . TYR D 2 187 ? 19.751  17.871  3.797   1.00 45.67 ?  187 TYR G CD1 1 
ATOM   6373 C CD2 . TYR D 2 187 ? 18.292  17.356  5.609   1.00 47.37 ?  187 TYR G CD2 1 
ATOM   6374 C CE1 . TYR D 2 187 ? 19.448  19.219  3.922   1.00 42.60 ?  187 TYR G CE1 1 
ATOM   6375 C CE2 . TYR D 2 187 ? 17.980  18.700  5.740   1.00 48.91 ?  187 TYR G CE2 1 
ATOM   6376 C CZ  . TYR D 2 187 ? 18.567  19.627  4.895   1.00 43.77 ?  187 TYR G CZ  1 
ATOM   6377 O OH  . TYR D 2 187 ? 18.258  20.961  5.019   1.00 47.16 ?  187 TYR G OH  1 
ATOM   6378 N N   . GLU D 2 188 ? 20.925  15.008  7.173   1.00 54.30 ?  188 GLU G N   1 
ATOM   6379 C CA  . GLU D 2 188 ? 21.265  15.412  8.530   1.00 54.38 ?  188 GLU G CA  1 
ATOM   6380 C C   . GLU D 2 188 ? 22.697  15.048  8.922   1.00 52.69 ?  188 GLU G C   1 
ATOM   6381 O O   . GLU D 2 188 ? 23.122  15.392  10.031  1.00 54.14 ?  188 GLU G O   1 
ATOM   6382 C CB  . GLU D 2 188 ? 20.249  14.805  9.498   1.00 55.68 ?  188 GLU G CB  1 
ATOM   6383 C CG  . GLU D 2 188 ? 19.042  15.722  9.688   1.00 58.83 ?  188 GLU G CG  1 
ATOM   6384 C CD  . GLU D 2 188 ? 17.751  14.976  9.950   1.00 62.10 ?  188 GLU G CD  1 
ATOM   6385 O OE1 . GLU D 2 188 ? 17.812  13.815  10.411  1.00 62.10 ?  188 GLU G OE1 1 
ATOM   6386 O OE2 . GLU D 2 188 ? 16.671  15.552  9.675   1.00 65.15 ?  188 GLU G OE2 1 
ATOM   6387 N N   . LYS D 2 189 ? 23.457  14.398  8.039   1.00 52.51 ?  189 LYS G N   1 
ATOM   6388 C CA  . LYS D 2 189 ? 24.869  14.123  8.278   1.00 51.06 ?  189 LYS G CA  1 
ATOM   6389 C C   . LYS D 2 189 ? 25.791  15.263  7.859   1.00 53.24 ?  189 LYS G C   1 
ATOM   6390 O O   . LYS D 2 189 ? 26.994  15.194  8.136   1.00 50.88 ?  189 LYS G O   1 
ATOM   6391 C CB  . LYS D 2 189 ? 25.304  12.856  7.532   1.00 55.34 ?  189 LYS G CB  1 
ATOM   6392 C CG  . LYS D 2 189 ? 24.912  11.539  8.188   1.00 55.03 ?  189 LYS G CG  1 
ATOM   6393 C CD  . LYS D 2 189 ? 25.487  10.365  7.396   1.00 59.79 ?  189 LYS G CD  1 
ATOM   6394 C CE  . LYS D 2 189 ? 27.020  10.434  7.368   1.00 58.05 ?  189 LYS G CE  1 
ATOM   6395 N NZ  . LYS D 2 189 ? 27.653  9.585   6.310   1.00 59.59 ?  189 LYS G NZ  1 
ATOM   6396 N N   . HIS D 2 190 ? 25.236  16.251  7.142   1.00 51.15 ?  190 HIS G N   1 
ATOM   6397 C CA  . HIS D 2 190 ? 26.070  17.355  6.596   1.00 48.24 ?  190 HIS G CA  1 
ATOM   6398 C C   . HIS D 2 190 ? 25.496  18.708  7.010   1.00 44.86 ?  190 HIS G C   1 
ATOM   6399 O O   . HIS D 2 190 ? 24.352  18.760  7.458   1.00 46.48 ?  190 HIS G O   1 
ATOM   6400 C CB  . HIS D 2 190 ? 26.212  17.209  5.080   1.00 47.99 ?  190 HIS G CB  1 
ATOM   6401 C CG  . HIS D 2 190 ? 26.804  15.915  4.642   1.00 48.75 ?  190 HIS G CG  1 
ATOM   6402 N ND1 . HIS D 2 190 ? 28.159  15.670  4.645   1.00 53.37 ?  190 HIS G ND1 1 
ATOM   6403 C CD2 . HIS D 2 190 ? 26.232  14.801  4.182   1.00 50.56 ?  190 HIS G CD2 1 
ATOM   6404 C CE1 . HIS D 2 190 ? 28.381  14.444  4.203   1.00 51.35 ?  190 HIS G CE1 1 
ATOM   6405 N NE2 . HIS D 2 190 ? 27.224  13.897  3.918   1.00 51.14 ?  190 HIS G NE2 1 
ATOM   6406 N N   . LYS D 2 191 ? 26.280  19.766  6.829   1.00 43.57 ?  191 LYS G N   1 
ATOM   6407 C CA  . LYS D 2 191 ? 25.870  21.083  7.303   1.00 46.10 ?  191 LYS G CA  1 
ATOM   6408 C C   . LYS D 2 191 ? 25.682  22.110  6.195   1.00 45.55 ?  191 LYS G C   1 
ATOM   6409 O O   . LYS D 2 191 ? 24.700  22.855  6.225   1.00 46.82 ?  191 LYS G O   1 
ATOM   6410 C CB  . LYS D 2 191 ? 26.884  21.625  8.326   1.00 47.00 ?  191 LYS G CB  1 
ATOM   6411 C CG  . LYS D 2 191 ? 26.583  23.032  8.828   1.00 49.80 ?  191 LYS G CG  1 
ATOM   6412 C CD  . LYS D 2 191 ? 27.857  23.749  9.286   1.00 55.40 ?  191 LYS G CD  1 
ATOM   6413 C CE  . LYS D 2 191 ? 27.575  24.799  10.365  1.00 55.67 ?  191 LYS G CE  1 
ATOM   6414 N NZ  . LYS D 2 191 ? 28.816  25.199  11.087  1.00 56.97 ?  191 LYS G NZ  1 
ATOM   6415 N N   . VAL D 2 192 ? 26.583  22.187  5.220   1.00 44.46 ?  192 VAL G N   1 
ATOM   6416 C CA  . VAL D 2 192 ? 26.572  23.272  4.243   1.00 43.33 ?  192 VAL G CA  1 
ATOM   6417 C C   . VAL D 2 192 ? 26.099  22.733  2.902   1.00 43.79 ?  192 VAL G C   1 
ATOM   6418 O O   . VAL D 2 192 ? 26.700  21.810  2.340   1.00 42.60 ?  192 VAL G O   1 
ATOM   6419 C CB  . VAL D 2 192 ? 27.943  23.942  4.111   1.00 41.61 ?  192 VAL G CB  1 
ATOM   6420 C CG1 . VAL D 2 192 ? 27.806  25.196  3.262   1.00 44.55 ?  192 VAL G CG1 1 
ATOM   6421 C CG2 . VAL D 2 192 ? 28.494  24.285  5.491   1.00 45.51 ?  192 VAL G CG2 1 
ATOM   6422 N N   . TYR D 2 193 ? 25.032  23.333  2.381   1.00 39.51 ?  193 TYR G N   1 
ATOM   6423 C CA  . TYR D 2 193 ? 24.436  22.939  1.114   1.00 39.62 ?  193 TYR G CA  1 
ATOM   6424 C C   . TYR D 2 193 ? 24.513  24.124  0.170   1.00 37.44 ?  193 TYR G C   1 
ATOM   6425 O O   . TYR D 2 193 ? 24.017  25.203  0.498   1.00 35.58 ?  193 TYR G O   1 
ATOM   6426 C CB  . TYR D 2 193 ? 22.994  22.496  1.331   1.00 34.41 ?  193 TYR G CB  1 
ATOM   6427 C CG  . TYR D 2 193 ? 22.946  21.156  2.007   1.00 40.51 ?  193 TYR G CG  1 
ATOM   6428 C CD1 . TYR D 2 193 ? 23.011  21.053  3.393   1.00 42.21 ?  193 TYR G CD1 1 
ATOM   6429 C CD2 . TYR D 2 193 ? 22.852  19.991  1.260   1.00 40.01 ?  193 TYR G CD2 1 
ATOM   6430 C CE1 . TYR D 2 193 ? 22.980  19.815  4.014   1.00 41.19 ?  193 TYR G CE1 1 
ATOM   6431 C CE2 . TYR D 2 193 ? 22.819  18.755  1.870   1.00 38.86 ?  193 TYR G CE2 1 
ATOM   6432 C CZ  . TYR D 2 193 ? 22.892  18.678  3.246   1.00 41.77 ?  193 TYR G CZ  1 
ATOM   6433 O OH  . TYR D 2 193 ? 22.863  17.444  3.848   1.00 45.76 ?  193 TYR G OH  1 
ATOM   6434 N N   . ALA D 2 194 ? 25.129  23.925  -0.995  1.00 35.67 ?  194 ALA G N   1 
ATOM   6435 C CA  . ALA D 2 194 ? 25.379  25.038  -1.899  1.00 37.47 ?  194 ALA G CA  1 
ATOM   6436 C C   . ALA D 2 194 ? 25.261  24.589  -3.347  1.00 38.84 ?  194 ALA G C   1 
ATOM   6437 O O   . ALA D 2 194 ? 25.582  23.448  -3.689  1.00 36.95 ?  194 ALA G O   1 
ATOM   6438 C CB  . ALA D 2 194 ? 26.764  25.644  -1.652  1.00 33.29 ?  194 ALA G CB  1 
ATOM   6439 N N   . CYS D 2 195 ? 24.798  25.498  -4.206  1.00 37.04 ?  195 CYS G N   1 
ATOM   6440 C CA  . CYS D 2 195 ? 24.911  25.298  -5.644  1.00 38.85 ?  195 CYS G CA  1 
ATOM   6441 C C   . CYS D 2 195 ? 25.768  26.417  -6.211  1.00 38.05 ?  195 CYS G C   1 
ATOM   6442 O O   . CYS D 2 195 ? 25.587  27.589  -5.857  1.00 37.05 ?  195 CYS G O   1 
ATOM   6443 C CB  . CYS D 2 195 ? 23.542  25.220  -6.338  1.00 40.58 ?  195 CYS G CB  1 
ATOM   6444 S SG  . CYS D 2 195 ? 22.465  26.635  -6.112  1.00 46.83 ?  195 CYS G SG  1 
ATOM   6445 N N   . GLU D 2 196 ? 26.746  26.039  -7.031  1.00 36.42 ?  196 GLU G N   1 
ATOM   6446 C CA  . GLU D 2 196 ? 27.683  26.961  -7.654  1.00 38.61 ?  196 GLU G CA  1 
ATOM   6447 C C   . GLU D 2 196 ? 27.313  27.107  -9.119  1.00 35.18 ?  196 GLU G C   1 
ATOM   6448 O O   . GLU D 2 196 ? 27.163  26.103  -9.821  1.00 36.62 ?  196 GLU G O   1 
ATOM   6449 C CB  . GLU D 2 196 ? 29.126  26.459  -7.522  1.00 39.21 ?  196 GLU G CB  1 
ATOM   6450 C CG  . GLU D 2 196 ? 30.161  27.537  -7.792  1.00 42.99 ?  196 GLU G CG  1 
ATOM   6451 C CD  . GLU D 2 196 ? 31.586  27.023  -7.671  1.00 49.68 ?  196 GLU G CD  1 
ATOM   6452 O OE1 . GLU D 2 196 ? 31.807  26.047  -6.930  1.00 48.94 ?  196 GLU G OE1 1 
ATOM   6453 O OE2 . GLU D 2 196 ? 32.484  27.601  -8.319  1.00 55.17 ?  196 GLU G OE2 1 
ATOM   6454 N N   . VAL D 2 197 ? 27.168  28.349  -9.580  1.00 34.11 ?  197 VAL G N   1 
ATOM   6455 C CA  . VAL D 2 197 ? 26.644  28.624  -10.914 1.00 35.16 ?  197 VAL G CA  1 
ATOM   6456 C C   . VAL D 2 197 ? 27.698  29.357  -11.733 1.00 34.02 ?  197 VAL G C   1 
ATOM   6457 O O   . VAL D 2 197 ? 28.277  30.346  -11.280 1.00 33.62 ?  197 VAL G O   1 
ATOM   6458 C CB  . VAL D 2 197 ? 25.338  29.437  -10.858 1.00 35.72 ?  197 VAL G CB  1 
ATOM   6459 C CG1 . VAL D 2 197 ? 24.877  29.777  -12.272 1.00 33.15 ?  197 VAL G CG1 1 
ATOM   6460 C CG2 . VAL D 2 197 ? 24.251  28.660  -10.089 1.00 33.84 ?  197 VAL G CG2 1 
ATOM   6461 N N   . THR D 2 198 ? 27.948  28.859  -12.935 1.00 35.22 ?  198 THR G N   1 
ATOM   6462 C CA  . THR D 2 198 ? 28.805  29.511  -13.910 1.00 34.20 ?  198 THR G CA  1 
ATOM   6463 C C   . THR D 2 198 ? 27.944  29.867  -15.106 1.00 33.11 ?  198 THR G C   1 
ATOM   6464 O O   . THR D 2 198 ? 27.158  29.037  -15.576 1.00 33.56 ?  198 THR G O   1 
ATOM   6465 C CB  . THR D 2 198 ? 29.960  28.600  -14.335 1.00 37.87 ?  198 THR G CB  1 
ATOM   6466 O OG1 . THR D 2 198 ? 30.687  28.181  -13.169 1.00 38.95 ?  198 THR G OG1 1 
ATOM   6467 C CG2 . THR D 2 198 ? 30.903  29.341  -15.277 1.00 39.61 ?  198 THR G CG2 1 
ATOM   6468 N N   . HIS D 2 199 ? 28.061  31.113  -15.536 1.00 31.77 ?  199 HIS G N   1 
ATOM   6469 C CA  . HIS D 2 199 ? 27.290  31.574  -16.711 1.00 32.44 ?  199 HIS G CA  1 
ATOM   6470 C C   . HIS D 2 199 ? 28.053  32.738  -17.334 1.00 33.20 ?  199 HIS G C   1 
ATOM   6471 O O   . HIS D 2 199 ? 28.661  33.534  -16.613 1.00 33.88 ?  199 HIS G O   1 
ATOM   6472 C CB  . HIS D 2 199 ? 25.856  31.936  -16.324 1.00 29.49 ?  199 HIS G CB  1 
ATOM   6473 C CG  . HIS D 2 199 ? 25.049  32.466  -17.458 1.00 30.48 ?  199 HIS G CG  1 
ATOM   6474 N ND1 . HIS D 2 199 ? 24.363  31.657  -18.333 1.00 30.88 ?  199 HIS G ND1 1 
ATOM   6475 C CD2 . HIS D 2 199 ? 24.822  33.716  -17.863 1.00 28.56 ?  199 HIS G CD2 1 
ATOM   6476 C CE1 . HIS D 2 199 ? 23.755  32.411  -19.230 1.00 29.34 ?  199 HIS G CE1 1 
ATOM   6477 N NE2 . HIS D 2 199 ? 24.024  33.662  -18.966 1.00 31.42 ?  199 HIS G NE2 1 
ATOM   6478 N N   . GLN D 2 200 ? 27.992  32.822  -18.650 1.00 33.58 ?  200 GLN G N   1 
ATOM   6479 C CA  . GLN D 2 200 ? 28.683  33.882  -19.379 1.00 35.77 ?  200 GLN G CA  1 
ATOM   6480 C C   . GLN D 2 200 ? 28.361  35.278  -18.857 1.00 36.65 ?  200 GLN G C   1 
ATOM   6481 O O   . GLN D 2 200 ? 29.182  36.194  -18.990 1.00 36.06 ?  200 GLN G O   1 
ATOM   6482 C CB  . GLN D 2 200 ? 28.314  33.781  -20.857 1.00 39.41 ?  200 GLN G CB  1 
ATOM   6483 C CG  . GLN D 2 200 ? 29.216  34.542  -21.771 1.00 46.78 ?  200 GLN G CG  1 
ATOM   6484 C CD  . GLN D 2 200 ? 28.580  34.739  -23.110 1.00 42.42 ?  200 GLN G CD  1 
ATOM   6485 O OE1 . GLN D 2 200 ? 27.888  33.857  -23.609 1.00 46.13 ?  200 GLN G OE1 1 
ATOM   6486 N NE2 . GLN D 2 200 ? 28.822  35.884  -23.713 1.00 46.19 ?  200 GLN G NE2 1 
ATOM   6487 N N   . GLY D 2 201 ? 27.174  35.469  -18.281 1.00 34.22 ?  201 GLY G N   1 
ATOM   6488 C CA  . GLY D 2 201 ? 26.796  36.766  -17.748 1.00 35.59 ?  201 GLY G CA  1 
ATOM   6489 C C   . GLY D 2 201 ? 27.397  37.107  -16.408 1.00 35.28 ?  201 GLY G C   1 
ATOM   6490 O O   . GLY D 2 201 ? 27.297  38.257  -15.972 1.00 39.09 ?  201 GLY G O   1 
ATOM   6491 N N   . LEU D 2 202 ? 28.018  36.141  -15.749 1.00 33.03 ?  202 LEU G N   1 
ATOM   6492 C CA  . LEU D 2 202 ? 28.611  36.341  -14.438 1.00 40.18 ?  202 LEU G CA  1 
ATOM   6493 C C   . LEU D 2 202 ? 30.114  36.523  -14.596 1.00 43.07 ?  202 LEU G C   1 
ATOM   6494 O O   . LEU D 2 202 ? 30.785  35.673  -15.195 1.00 44.44 ?  202 LEU G O   1 
ATOM   6495 C CB  . LEU D 2 202 ? 28.317  35.149  -13.526 1.00 39.57 ?  202 LEU G CB  1 
ATOM   6496 C CG  . LEU D 2 202 ? 26.832  34.873  -13.265 1.00 35.12 ?  202 LEU G CG  1 
ATOM   6497 C CD1 . LEU D 2 202 ? 26.636  33.474  -12.694 1.00 35.57 ?  202 LEU G CD1 1 
ATOM   6498 C CD2 . LEU D 2 202 ? 26.212  35.946  -12.363 1.00 33.85 ?  202 LEU G CD2 1 
ATOM   6499 N N   . SER D 2 203 ? 30.643  37.622  -14.049 1.00 45.33 ?  203 SER G N   1 
ATOM   6500 C CA  . SER D 2 203 ? 32.085  37.852  -14.128 1.00 48.45 ?  203 SER G CA  1 
ATOM   6501 C C   . SER D 2 203 ? 32.886  36.739  -13.469 1.00 51.14 ?  203 SER G C   1 
ATOM   6502 O O   . SER D 2 203 ? 34.051  36.537  -13.829 1.00 55.91 ?  203 SER G O   1 
ATOM   6503 C CB  . SER D 2 203 ? 32.444  39.211  -13.517 1.00 49.04 ?  203 SER G CB  1 
ATOM   6504 O OG  . SER D 2 203 ? 32.045  39.308  -12.162 1.00 52.80 ?  203 SER G OG  1 
ATOM   6505 N N   . SER D 2 204 ? 32.291  36.003  -12.534 1.00 48.63 ?  204 SER G N   1 
ATOM   6506 C CA  . SER D 2 204 ? 32.920  34.834  -11.935 1.00 49.21 ?  204 SER G CA  1 
ATOM   6507 C C   . SER D 2 204 ? 31.828  33.966  -11.326 1.00 47.97 ?  204 SER G C   1 
ATOM   6508 O O   . SER D 2 204 ? 30.692  34.427  -11.156 1.00 43.87 ?  204 SER G O   1 
ATOM   6509 C CB  . SER D 2 204 ? 33.953  35.239  -10.869 1.00 52.28 ?  204 SER G CB  1 
ATOM   6510 O OG  . SER D 2 204 ? 33.307  35.815  -9.755  1.00 54.07 ?  204 SER G OG  1 
ATOM   6511 N N   . PRO D 2 205 ? 32.129  32.701  -11.018 1.00 48.18 ?  205 PRO G N   1 
ATOM   6512 C CA  . PRO D 2 205 ? 31.107  31.822  -10.432 1.00 45.46 ?  205 PRO G CA  1 
ATOM   6513 C C   . PRO D 2 205 ? 30.537  32.394  -9.141  1.00 47.11 ?  205 PRO G C   1 
ATOM   6514 O O   . PRO D 2 205 ? 31.226  33.076  -8.378  1.00 47.64 ?  205 PRO G O   1 
ATOM   6515 C CB  . PRO D 2 205 ? 31.871  30.522  -10.161 1.00 46.50 ?  205 PRO G CB  1 
ATOM   6516 C CG  . PRO D 2 205 ? 32.984  30.517  -11.148 1.00 44.49 ?  205 PRO G CG  1 
ATOM   6517 C CD  . PRO D 2 205 ? 33.277  31.943  -11.547 1.00 46.51 ?  205 PRO G CD  1 
ATOM   6518 N N   . VAL D 2 206 ? 29.255  32.112  -8.906  1.00 43.09 ?  206 VAL G N   1 
ATOM   6519 C CA  . VAL D 2 206 ? 28.557  32.580  -7.716  1.00 43.72 ?  206 VAL G CA  1 
ATOM   6520 C C   . VAL D 2 206 ? 27.953  31.379  -7.006  1.00 42.97 ?  206 VAL G C   1 
ATOM   6521 O O   . VAL D 2 206 ? 27.551  30.396  -7.637  1.00 43.37 ?  206 VAL G O   1 
ATOM   6522 C CB  . VAL D 2 206 ? 27.466  33.622  -8.045  1.00 41.96 ?  206 VAL G CB  1 
ATOM   6523 C CG1 . VAL D 2 206 ? 28.090  34.879  -8.648  1.00 45.16 ?  206 VAL G CG1 1 
ATOM   6524 C CG2 . VAL D 2 206 ? 26.425  33.035  -8.976  1.00 40.43 ?  206 VAL G CG2 1 
ATOM   6525 N N   . THR D 2 207 ? 27.895  31.458  -5.680  1.00 38.43 ?  207 THR G N   1 
ATOM   6526 C CA  . THR D 2 207 ? 27.433  30.350  -4.853  1.00 38.14 ?  207 THR G CA  1 
ATOM   6527 C C   . THR D 2 207 ? 26.331  30.846  -3.933  1.00 39.95 ?  207 THR G C   1 
ATOM   6528 O O   . THR D 2 207 ? 26.516  31.849  -3.236  1.00 44.57 ?  207 THR G O   1 
ATOM   6529 C CB  . THR D 2 207 ? 28.575  29.757  -4.027  1.00 41.60 ?  207 THR G CB  1 
ATOM   6530 O OG1 . THR D 2 207 ? 29.666  29.403  -4.888  1.00 45.23 ?  207 THR G OG1 1 
ATOM   6531 C CG2 . THR D 2 207 ? 28.095  28.524  -3.288  1.00 40.23 ?  207 THR G CG2 1 
ATOM   6532 N N   . LYS D 2 208 ? 25.187  30.159  -3.954  1.00 36.72 ?  208 LYS G N   1 
ATOM   6533 C CA  . LYS D 2 208 ? 24.117  30.327  -2.970  1.00 40.90 ?  208 LYS G CA  1 
ATOM   6534 C C   . LYS D 2 208 ? 24.130  29.110  -2.048  1.00 38.59 ?  208 LYS G C   1 
ATOM   6535 O O   . LYS D 2 208 ? 24.163  27.970  -2.524  1.00 37.91 ?  208 LYS G O   1 
ATOM   6536 C CB  . LYS D 2 208 ? 22.741  30.464  -3.647  1.00 38.74 ?  208 LYS G CB  1 
ATOM   6537 C CG  . LYS D 2 208 ? 22.167  31.896  -3.792  1.00 40.92 ?  208 LYS G CG  1 
ATOM   6538 C CD  . LYS D 2 208 ? 22.173  32.713  -2.502  1.00 42.20 ?  208 LYS G CD  1 
ATOM   6539 C CE  . LYS D 2 208 ? 21.187  33.896  -2.601  1.00 52.17 ?  208 LYS G CE  1 
ATOM   6540 N NZ  . LYS D 2 208 ? 20.994  34.666  -1.325  1.00 58.58 ?  208 LYS G NZ  1 
ATOM   6541 N N   . SER D 2 209 ? 24.098  29.346  -0.738  1.00 37.01 ?  209 SER G N   1 
ATOM   6542 C CA  . SER D 2 209 ? 24.185  28.253  0.216   1.00 37.52 ?  209 SER G CA  1 
ATOM   6543 C C   . SER D 2 209 ? 23.261  28.515  1.391   1.00 39.51 ?  209 SER G C   1 
ATOM   6544 O O   . SER D 2 209 ? 22.810  29.638  1.618   1.00 42.58 ?  209 SER G O   1 
ATOM   6545 C CB  . SER D 2 209 ? 25.614  28.064  0.748   1.00 37.50 ?  209 SER G CB  1 
ATOM   6546 O OG  . SER D 2 209 ? 26.149  29.307  1.156   1.00 42.18 ?  209 SER G OG  1 
ATOM   6547 N N   . PHE D 2 210 ? 22.997  27.450  2.144   1.00 40.35 ?  210 PHE G N   1 
ATOM   6548 C CA  . PHE D 2 210 ? 22.396  27.548  3.463   1.00 40.91 ?  210 PHE G CA  1 
ATOM   6549 C C   . PHE D 2 210 ? 23.043  26.495  4.352   1.00 42.36 ?  210 PHE G C   1 
ATOM   6550 O O   . PHE D 2 210 ? 23.560  25.484  3.868   1.00 39.95 ?  210 PHE G O   1 
ATOM   6551 C CB  . PHE D 2 210 ? 20.871  27.357  3.411   1.00 34.66 ?  210 PHE G CB  1 
ATOM   6552 C CG  . PHE D 2 210 ? 20.438  25.968  3.032   1.00 35.45 ?  210 PHE G CG  1 
ATOM   6553 C CD1 . PHE D 2 210 ? 20.277  24.988  4.002   1.00 38.08 ?  210 PHE G CD1 1 
ATOM   6554 C CD2 . PHE D 2 210 ? 20.179  25.645  1.714   1.00 34.65 ?  210 PHE G CD2 1 
ATOM   6555 C CE1 . PHE D 2 210 ? 19.880  23.712  3.664   1.00 39.03 ?  210 PHE G CE1 1 
ATOM   6556 C CE2 . PHE D 2 210 ? 19.775  24.376  1.363   1.00 36.46 ?  210 PHE G CE2 1 
ATOM   6557 C CZ  . PHE D 2 210 ? 19.623  23.400  2.339   1.00 38.11 ?  210 PHE G CZ  1 
ATOM   6558 N N   . ASN D 2 211 ? 23.027  26.743  5.657   1.00 44.18 ?  211 ASN G N   1 
ATOM   6559 C CA  . ASN D 2 211 ? 23.439  25.747  6.639   1.00 45.70 ?  211 ASN G CA  1 
ATOM   6560 C C   . ASN D 2 211 ? 22.202  25.106  7.247   1.00 44.87 ?  211 ASN G C   1 
ATOM   6561 O O   . ASN D 2 211 ? 21.277  25.811  7.666   1.00 45.39 ?  211 ASN G O   1 
ATOM   6562 C CB  . ASN D 2 211 ? 24.313  26.363  7.734   1.00 48.00 ?  211 ASN G CB  1 
ATOM   6563 C CG  . ASN D 2 211 ? 25.388  27.281  7.179   1.00 50.90 ?  211 ASN G CG  1 
ATOM   6564 O OD1 . ASN D 2 211 ? 26.141  26.897  6.284   1.00 46.71 ?  211 ASN G OD1 1 
ATOM   6565 N ND2 . ASN D 2 211 ? 25.461  28.503  7.703   1.00 55.89 ?  211 ASN G ND2 1 
ATOM   6566 N N   . ARG D 2 212 ? 22.181  23.776  7.275   1.00 46.15 ?  212 ARG G N   1 
ATOM   6567 C CA  . ARG D 2 212 ? 21.064  23.066  7.878   1.00 50.93 ?  212 ARG G CA  1 
ATOM   6568 C C   . ARG D 2 212 ? 20.884  23.530  9.318   1.00 52.79 ?  212 ARG G C   1 
ATOM   6569 O O   . ARG D 2 212 ? 21.842  23.566  10.097  1.00 53.66 ?  212 ARG G O   1 
ATOM   6570 C CB  . ARG D 2 212 ? 21.288  21.553  7.819   1.00 48.15 ?  212 ARG G CB  1 
ATOM   6571 C CG  . ARG D 2 212 ? 20.026  20.741  8.140   1.00 51.45 ?  212 ARG G CG  1 
ATOM   6572 C CD  . ARG D 2 212 ? 20.303  19.235  8.195   1.00 50.64 ?  212 ARG G CD  1 
ATOM   6573 N NE  . ARG D 2 212 ? 21.598  18.941  8.795   1.00 51.94 ?  212 ARG G NE  1 
ATOM   6574 C CZ  . ARG D 2 212 ? 21.788  18.728  10.090  1.00 52.43 ?  212 ARG G CZ  1 
ATOM   6575 N NH1 . ARG D 2 212 ? 20.778  18.734  10.945  1.00 53.92 ?  212 ARG G NH1 1 
ATOM   6576 N NH2 . ARG D 2 212 ? 23.021  18.510  10.540  1.00 54.50 ?  212 ARG G NH2 1 
ATOM   6577 N N   . GLY D 2 213 ? 19.658  23.913  9.660   1.00 53.96 ?  213 GLY G N   1 
ATOM   6578 C CA  . GLY D 2 213 ? 19.387  24.547  10.936  1.00 54.68 ?  213 GLY G CA  1 
ATOM   6579 C C   . GLY D 2 213 ? 19.764  26.018  10.939  1.00 57.48 ?  213 GLY G C   1 
ATOM   6580 O O   . GLY D 2 213 ? 18.904  26.889  10.797  1.00 69.11 ?  213 GLY G O   1 
ATOM   6581 N N   . ASN E 3 7   ? 31.445  -17.034 -63.157 1.00 49.81 ?  161 ASN A N   1 
ATOM   6582 C CA  . ASN E 3 7   ? 31.915  -15.741 -62.679 1.00 46.20 ?  161 ASN A CA  1 
ATOM   6583 C C   . ASN E 3 7   ? 31.443  -15.464 -61.253 1.00 40.87 ?  161 ASN A C   1 
ATOM   6584 O O   . ASN E 3 7   ? 30.879  -14.393 -60.976 1.00 38.08 ?  161 ASN A O   1 
ATOM   6585 C CB  . ASN E 3 7   ? 31.445  -14.628 -63.610 1.00 50.34 ?  161 ASN A CB  1 
ATOM   6586 C CG  . ASN E 3 7   ? 32.094  -14.707 -64.976 1.00 57.67 ?  161 ASN A CG  1 
ATOM   6587 O OD1 . ASN E 3 7   ? 31.409  -14.757 -66.002 1.00 60.21 ?  161 ASN A OD1 1 
ATOM   6588 N ND2 . ASN E 3 7   ? 33.427  -14.755 -64.996 1.00 60.68 ?  161 ASN A ND2 1 
ATOM   6589 N N   . ASP E 3 8   ? 31.677  -16.428 -60.358 1.00 34.16 ?  162 ASP A N   1 
ATOM   6590 C CA  . ASP E 3 8   ? 31.370  -16.290 -58.941 1.00 32.00 ?  162 ASP A CA  1 
ATOM   6591 C C   . ASP E 3 8   ? 32.653  -16.299 -58.124 1.00 32.05 ?  162 ASP A C   1 
ATOM   6592 O O   . ASP E 3 8   ? 33.581  -17.067 -58.414 1.00 29.15 ?  162 ASP A O   1 
ATOM   6593 C CB  . ASP E 3 8   ? 30.454  -17.397 -58.429 1.00 32.40 ?  162 ASP A CB  1 
ATOM   6594 C CG  . ASP E 3 8   ? 29.949  -17.108 -57.027 1.00 31.20 ?  162 ASP A CG  1 
ATOM   6595 O OD1 . ASP E 3 8   ? 29.055  -16.240 -56.873 1.00 31.50 ?  162 ASP A OD1 1 
ATOM   6596 O OD2 . ASP E 3 8   ? 30.493  -17.717 -56.078 1.00 28.20 ?  162 ASP A OD2 1 
ATOM   6597 N N   . PHE E 3 9   ? 32.683  -15.467 -57.079 1.00 27.37 ?  163 PHE A N   1 
ATOM   6598 C CA  . PHE E 3 9   ? 33.905  -15.240 -56.325 1.00 26.78 ?  163 PHE A CA  1 
ATOM   6599 C C   . PHE E 3 9   ? 33.792  -15.637 -54.860 1.00 27.97 ?  163 PHE A C   1 
ATOM   6600 O O   . PHE E 3 9   ? 34.721  -15.369 -54.088 1.00 26.53 ?  163 PHE A O   1 
ATOM   6601 C CB  . PHE E 3 9   ? 34.317  -13.772 -56.494 1.00 28.47 ?  163 PHE A CB  1 
ATOM   6602 C CG  . PHE E 3 9   ? 34.538  -13.414 -57.931 1.00 27.97 ?  163 PHE A CG  1 
ATOM   6603 C CD1 . PHE E 3 9   ? 35.740  -13.723 -58.546 1.00 32.79 ?  163 PHE A CD1 1 
ATOM   6604 C CD2 . PHE E 3 9   ? 33.514  -12.851 -58.689 1.00 32.45 ?  163 PHE A CD2 1 
ATOM   6605 C CE1 . PHE E 3 9   ? 35.943  -13.437 -59.879 1.00 37.12 ?  163 PHE A CE1 1 
ATOM   6606 C CE2 . PHE E 3 9   ? 33.708  -12.557 -60.033 1.00 34.02 ?  163 PHE A CE2 1 
ATOM   6607 C CZ  . PHE E 3 9   ? 34.929  -12.850 -60.625 1.00 37.67 ?  163 PHE A CZ  1 
ATOM   6608 N N   . HIS E 3 10  ? 32.732  -16.344 -54.512 1.00 23.29 ?  164 HIS A N   1 
ATOM   6609 C CA  . HIS E 3 10  ? 32.700  -16.923 -53.157 1.00 25.96 ?  164 HIS A CA  1 
ATOM   6610 C C   . HIS E 3 10  ? 33.837  -17.946 -53.078 1.00 25.35 ?  164 HIS A C   1 
ATOM   6611 O O   . HIS E 3 10  ? 34.015  -18.706 -54.037 1.00 25.46 ?  164 HIS A O   1 
ATOM   6612 C CB  . HIS E 3 10  ? 31.378  -17.629 -52.882 1.00 24.44 ?  164 HIS A CB  1 
ATOM   6613 C CG  . HIS E 3 10  ? 30.195  -16.750 -52.679 1.00 23.95 ?  164 HIS A CG  1 
ATOM   6614 N ND1 . HIS E 3 10  ? 29.352  -16.381 -53.702 1.00 26.02 ?  164 HIS A ND1 1 
ATOM   6615 C CD2 . HIS E 3 10  ? 29.697  -16.200 -51.573 1.00 21.65 ?  164 HIS A CD2 1 
ATOM   6616 C CE1 . HIS E 3 10  ? 28.391  -15.619 -53.217 1.00 22.60 ?  164 HIS A CE1 1 
ATOM   6617 N NE2 . HIS E 3 10  ? 28.581  -15.499 -51.927 1.00 26.64 ?  164 HIS A NE2 1 
ATOM   6618 N N   . PHE E 3 11  ? 34.562  -17.957 -51.976 1.00 23.84 ?  165 PHE A N   1 
ATOM   6619 C CA  . PHE E 3 11  ? 35.668  -18.878 -51.710 1.00 26.80 ?  165 PHE A CA  1 
ATOM   6620 C C   . PHE E 3 11  ? 36.827  -18.731 -52.700 1.00 26.88 ?  165 PHE A C   1 
ATOM   6621 O O   . PHE E 3 11  ? 37.670  -19.625 -52.801 1.00 31.35 ?  165 PHE A O   1 
ATOM   6622 C CB  . PHE E 3 11  ? 35.176  -20.333 -51.666 1.00 25.99 ?  165 PHE A CB  1 
ATOM   6623 C CG  . PHE E 3 11  ? 34.067  -20.555 -50.673 1.00 23.32 ?  165 PHE A CG  1 
ATOM   6624 C CD1 . PHE E 3 11  ? 34.346  -20.645 -49.314 1.00 26.22 ?  165 PHE A CD1 1 
ATOM   6625 C CD2 . PHE E 3 11  ? 32.749  -20.680 -51.093 1.00 24.61 ?  165 PHE A CD2 1 
ATOM   6626 C CE1 . PHE E 3 11  ? 33.326  -20.843 -48.387 1.00 25.58 ?  165 PHE A CE1 1 
ATOM   6627 C CE2 . PHE E 3 11  ? 31.735  -20.882 -50.174 1.00 25.28 ?  165 PHE A CE2 1 
ATOM   6628 C CZ  . PHE E 3 11  ? 32.022  -20.953 -48.820 1.00 26.50 ?  165 PHE A CZ  1 
ATOM   6629 N N   . GLU E 3 12  ? 36.896  -17.631 -53.436 1.00 25.79 ?  166 GLU A N   1 
ATOM   6630 C CA  . GLU E 3 12  ? 38.015  -17.394 -54.334 1.00 28.96 ?  166 GLU A CA  1 
ATOM   6631 C C   . GLU E 3 12  ? 38.978  -16.398 -53.689 1.00 26.88 ?  166 GLU A C   1 
ATOM   6632 O O   . GLU E 3 12  ? 38.752  -15.896 -52.584 1.00 27.14 ?  166 GLU A O   1 
ATOM   6633 C CB  . GLU E 3 12  ? 37.519  -16.910 -55.700 1.00 27.88 ?  166 GLU A CB  1 
ATOM   6634 C CG  . GLU E 3 12  ? 36.542  -17.865 -56.409 1.00 29.91 ?  166 GLU A CG  1 
ATOM   6635 C CD  . GLU E 3 12  ? 37.230  -19.070 -57.016 1.00 38.65 ?  166 GLU A CD  1 
ATOM   6636 O OE1 . GLU E 3 12  ? 38.478  -19.117 -56.994 1.00 38.42 ?  166 GLU A OE1 1 
ATOM   6637 O OE2 . GLU E 3 12  ? 36.523  -19.977 -57.501 1.00 39.90 ?  166 GLU A OE2 1 
ATOM   6638 N N   . VAL E 3 13  ? 40.069  -16.090 -54.391 1.00 26.79 ?  167 VAL A N   1 
ATOM   6639 C CA  . VAL E 3 13  ? 41.117  -15.247 -53.822 1.00 29.40 ?  167 VAL A CA  1 
ATOM   6640 C C   . VAL E 3 13  ? 41.165  -13.850 -54.425 1.00 26.89 ?  167 VAL A C   1 
ATOM   6641 O O   . VAL E 3 13  ? 41.867  -12.986 -53.872 1.00 27.42 ?  167 VAL A O   1 
ATOM   6642 C CB  . VAL E 3 13  ? 42.508  -15.902 -53.946 1.00 29.47 ?  167 VAL A CB  1 
ATOM   6643 C CG1 . VAL E 3 13  ? 42.553  -17.216 -53.181 1.00 31.79 ?  167 VAL A CG1 1 
ATOM   6644 C CG2 . VAL E 3 13  ? 42.883  -16.058 -55.403 1.00 30.31 ?  167 VAL A CG2 1 
ATOM   6645 N N   . PHE E 3 14  ? 40.454  -13.596 -55.524 1.00 25.70 ?  168 PHE A N   1 
ATOM   6646 C CA  . PHE E 3 14  ? 40.536  -12.320 -56.229 1.00 28.14 ?  168 PHE A CA  1 
ATOM   6647 C C   . PHE E 3 14  ? 39.176  -12.006 -56.843 1.00 30.33 ?  168 PHE A C   1 
ATOM   6648 O O   . PHE E 3 14  ? 38.708  -12.755 -57.703 1.00 30.17 ?  168 PHE A O   1 
ATOM   6649 C CB  . PHE E 3 14  ? 41.610  -12.383 -57.325 1.00 27.92 ?  168 PHE A CB  1 
ATOM   6650 C CG  . PHE E 3 14  ? 41.867  -11.061 -57.995 1.00 26.35 ?  168 PHE A CG  1 
ATOM   6651 C CD1 . PHE E 3 14  ? 41.095  -10.653 -59.076 1.00 31.67 ?  168 PHE A CD1 1 
ATOM   6652 C CD2 . PHE E 3 14  ? 42.874  -10.233 -57.549 1.00 27.65 ?  168 PHE A CD2 1 
ATOM   6653 C CE1 . PHE E 3 14  ? 41.327  -9.430  -59.686 1.00 32.30 ?  168 PHE A CE1 1 
ATOM   6654 C CE2 . PHE E 3 14  ? 43.110  -9.003  -58.164 1.00 30.45 ?  168 PHE A CE2 1 
ATOM   6655 C CZ  . PHE E 3 14  ? 42.339  -8.616  -59.231 1.00 30.83 ?  168 PHE A CZ  1 
ATOM   6656 N N   . ASN E 3 15  ? 38.553  -10.905 -56.427 1.00 29.19 ?  169 ASN A N   1 
ATOM   6657 C CA  . ASN E 3 15  ? 37.273  -10.488 -56.983 1.00 25.56 ?  169 ASN A CA  1 
ATOM   6658 C C   . ASN E 3 15  ? 37.480  -9.420  -58.054 1.00 27.89 ?  169 ASN A C   1 
ATOM   6659 O O   . ASN E 3 15  ? 38.363  -8.577  -57.938 1.00 29.00 ?  169 ASN A O   1 
ATOM   6660 C CB  . ASN E 3 15  ? 36.358  -9.949  -55.886 1.00 26.23 ?  169 ASN A CB  1 
ATOM   6661 C CG  . ASN E 3 15  ? 35.007  -9.482  -56.427 1.00 26.29 ?  169 ASN A CG  1 
ATOM   6662 O OD1 . ASN E 3 15  ? 34.380  -10.170 -57.223 1.00 28.79 ?  169 ASN A OD1 1 
ATOM   6663 N ND2 . ASN E 3 15  ? 34.555  -8.321  -55.970 1.00 25.72 ?  169 ASN A ND2 1 
ATOM   6664 N N   . PHE E 3 16  ? 36.664  -9.459  -59.098 1.00 29.07 ?  170 PHE A N   1 
ATOM   6665 C CA  . PHE E 3 16  ? 36.844  -8.547  -60.218 1.00 30.11 ?  170 PHE A CA  1 
ATOM   6666 C C   . PHE E 3 16  ? 36.153  -7.221  -59.925 1.00 31.92 ?  170 PHE A C   1 
ATOM   6667 O O   . PHE E 3 16  ? 34.931  -7.173  -59.743 1.00 31.30 ?  170 PHE A O   1 
ATOM   6668 C CB  . PHE E 3 16  ? 36.319  -9.184  -61.503 1.00 36.49 ?  170 PHE A CB  1 
ATOM   6669 C CG  . PHE E 3 16  ? 37.303  -10.140 -62.136 1.00 44.13 ?  170 PHE A CG  1 
ATOM   6670 C CD1 . PHE E 3 16  ? 37.813  -11.209 -61.410 1.00 41.37 ?  170 PHE A CD1 1 
ATOM   6671 C CD2 . PHE E 3 16  ? 37.711  -9.983  -63.454 1.00 49.62 ?  170 PHE A CD2 1 
ATOM   6672 C CE1 . PHE E 3 16  ? 38.726  -12.093 -61.972 1.00 44.26 ?  170 PHE A CE1 1 
ATOM   6673 C CE2 . PHE E 3 16  ? 38.619  -10.876 -64.023 1.00 50.40 ?  170 PHE A CE2 1 
ATOM   6674 C CZ  . PHE E 3 16  ? 39.122  -11.930 -63.276 1.00 45.88 ?  170 PHE A CZ  1 
ATOM   6675 N N   . VAL E 3 17  ? 36.942  -6.160  -59.844 1.00 29.14 ?  171 VAL A N   1 
ATOM   6676 C CA  . VAL E 3 17  ? 36.465  -4.801  -59.602 1.00 30.85 ?  171 VAL A CA  1 
ATOM   6677 C C   . VAL E 3 17  ? 36.700  -3.996  -60.874 1.00 33.34 ?  171 VAL A C   1 
ATOM   6678 O O   . VAL E 3 17  ? 37.854  -3.866  -61.308 1.00 32.30 ?  171 VAL A O   1 
ATOM   6679 C CB  . VAL E 3 17  ? 37.180  -4.154  -58.406 1.00 30.47 ?  171 VAL A CB  1 
ATOM   6680 C CG1 . VAL E 3 17  ? 36.637  -2.741  -58.144 1.00 31.03 ?  171 VAL A CG1 1 
ATOM   6681 C CG2 . VAL E 3 17  ? 37.053  -5.025  -57.165 1.00 27.37 ?  171 VAL A CG2 1 
ATOM   6682 N N   . PRO E 3 18  ? 35.659  -3.451  -61.506 1.00 33.38 ?  172 PRO A N   1 
ATOM   6683 C CA  . PRO E 3 18  ? 35.854  -2.759  -62.789 1.00 35.34 ?  172 PRO A CA  1 
ATOM   6684 C C   . PRO E 3 18  ? 36.531  -1.413  -62.607 1.00 34.95 ?  172 PRO A C   1 
ATOM   6685 O O   . PRO E 3 18  ? 36.240  -0.665  -61.668 1.00 36.17 ?  172 PRO A O   1 
ATOM   6686 C CB  . PRO E 3 18  ? 34.428  -2.591  -63.322 1.00 40.17 ?  172 PRO A CB  1 
ATOM   6687 C CG  . PRO E 3 18  ? 33.574  -2.563  -62.083 1.00 35.93 ?  172 PRO A CG  1 
ATOM   6688 C CD  . PRO E 3 18  ? 34.237  -3.504  -61.116 1.00 33.85 ?  172 PRO A CD  1 
ATOM   6689 N N   . CYS E 3 19  ? 37.431  -1.095  -63.540 1.00 38.95 ?  173 CYS A N   1 
ATOM   6690 C CA  . CYS E 3 19  ? 38.166  0.160   -63.443 1.00 36.69 ?  173 CYS A CA  1 
ATOM   6691 C C   . CYS E 3 19  ? 37.247  1.365   -63.619 1.00 37.53 ?  173 CYS A C   1 
ATOM   6692 O O   . CYS E 3 19  ? 37.609  2.469   -63.205 1.00 37.74 ?  173 CYS A O   1 
ATOM   6693 C CB  . CYS E 3 19  ? 39.294  0.182   -64.475 1.00 38.82 ?  173 CYS A CB  1 
ATOM   6694 S SG  . CYS E 3 19  ? 40.677  -0.992  -64.113 1.00 41.73 ?  173 CYS A SG  1 
ATOM   6695 N N   . SER E 3 20  ? 36.057  1.177   -64.195 1.00 39.42 ?  174 SER A N   1 
ATOM   6696 C CA  . SER E 3 20  ? 35.158  2.308   -64.414 1.00 39.78 ?  174 SER A CA  1 
ATOM   6697 C C   . SER E 3 20  ? 34.708  2.970   -63.114 1.00 42.11 ?  174 SER A C   1 
ATOM   6698 O O   . SER E 3 20  ? 34.278  4.130   -63.145 1.00 41.25 ?  174 SER A O   1 
ATOM   6699 C CB  . SER E 3 20  ? 33.937  1.865   -65.213 1.00 43.79 ?  174 SER A CB  1 
ATOM   6700 O OG  . SER E 3 20  ? 33.164  0.945   -64.470 1.00 47.29 ?  174 SER A OG  1 
ATOM   6701 N N   . ILE E 3 21  ? 34.802  2.277   -61.972 1.00 38.75 ?  175 ILE A N   1 
ATOM   6702 C CA  . ILE E 3 21  ? 34.364  2.833   -60.690 1.00 37.39 ?  175 ILE A CA  1 
ATOM   6703 C C   . ILE E 3 21  ? 35.494  3.442   -59.881 1.00 40.63 ?  175 ILE A C   1 
ATOM   6704 O O   . ILE E 3 21  ? 35.250  3.905   -58.757 1.00 40.64 ?  175 ILE A O   1 
ATOM   6705 C CB  . ILE E 3 21  ? 33.642  1.778   -59.822 1.00 38.96 ?  175 ILE A CB  1 
ATOM   6706 C CG1 . ILE E 3 21  ? 34.661  0.786   -59.226 1.00 35.13 ?  175 ILE A CG1 1 
ATOM   6707 C CG2 . ILE E 3 21  ? 32.501  1.114   -60.595 1.00 37.88 ?  175 ILE A CG2 1 
ATOM   6708 C CD1 . ILE E 3 21  ? 34.134  -0.020  -58.068 1.00 35.77 ?  175 ILE A CD1 1 
ATOM   6709 N N   . CYS E 3 22  ? 36.716  3.477   -60.409 1.00 37.97 ?  176 CYS A N   1 
ATOM   6710 C CA  . CYS E 3 22  ? 37.858  3.776   -59.554 1.00 39.13 ?  176 CYS A CA  1 
ATOM   6711 C C   . CYS E 3 22  ? 38.046  5.259   -59.279 1.00 43.83 ?  176 CYS A C   1 
ATOM   6712 O O   . CYS E 3 22  ? 38.685  5.598   -58.277 1.00 45.36 ?  176 CYS A O   1 
ATOM   6713 C CB  . CYS E 3 22  ? 39.126  3.200   -60.179 1.00 37.34 ?  176 CYS A CB  1 
ATOM   6714 S SG  . CYS E 3 22  ? 39.216  1.412   -59.924 1.00 38.39 ?  176 CYS A SG  1 
ATOM   6715 N N   . SER E 3 23  ? 37.514  6.142   -60.135 1.00 42.34 ?  177 SER A N   1 
ATOM   6716 C CA  . SER E 3 23  ? 37.596  7.577   -59.881 1.00 45.93 ?  177 SER A CA  1 
ATOM   6717 C C   . SER E 3 23  ? 39.042  7.993   -59.630 1.00 44.30 ?  177 SER A C   1 
ATOM   6718 O O   . SER E 3 23  ? 39.907  7.784   -60.487 1.00 43.34 ?  177 SER A O   1 
ATOM   6719 C CB  . SER E 3 23  ? 36.693  7.951   -58.700 1.00 49.24 ?  177 SER A CB  1 
ATOM   6720 O OG  . SER E 3 23  ? 37.232  9.017   -57.947 1.00 52.91 ?  177 SER A OG  1 
ATOM   6721 N N   . ASN E 3 24  ? 39.342  8.543   -58.457 1.00 43.18 ?  178 ASN A N   1 
ATOM   6722 C CA  . ASN E 3 24  ? 40.728  8.858   -58.152 1.00 47.46 ?  178 ASN A CA  1 
ATOM   6723 C C   . ASN E 3 24  ? 41.211  8.107   -56.913 1.00 45.93 ?  178 ASN A C   1 
ATOM   6724 O O   . ASN E 3 24  ? 42.146  8.544   -56.236 1.00 47.13 ?  178 ASN A O   1 
ATOM   6725 C CB  . ASN E 3 24  ? 40.944  10.366  -58.006 1.00 48.70 ?  178 ASN A CB  1 
ATOM   6726 C CG  . ASN E 3 24  ? 40.289  10.951  -56.770 1.00 55.71 ?  178 ASN A CG  1 
ATOM   6727 O OD1 . ASN E 3 24  ? 39.416  10.338  -56.144 1.00 57.42 ?  178 ASN A OD1 1 
ATOM   6728 N ND2 . ASN E 3 24  ? 40.733  12.151  -56.397 1.00 57.42 ?  178 ASN A ND2 1 
ATOM   6729 N N   . ASN E 3 25  ? 40.606  6.953   -56.632 1.00 43.59 ?  179 ASN A N   1 
ATOM   6730 C CA  . ASN E 3 25  ? 41.018  6.095   -55.529 1.00 38.56 ?  179 ASN A CA  1 
ATOM   6731 C C   . ASN E 3 25  ? 42.209  5.237   -55.953 1.00 37.60 ?  179 ASN A C   1 
ATOM   6732 O O   . ASN E 3 25  ? 42.060  4.370   -56.826 1.00 37.14 ?  179 ASN A O   1 
ATOM   6733 C CB  . ASN E 3 25  ? 39.848  5.212   -55.092 1.00 42.41 ?  179 ASN A CB  1 
ATOM   6734 C CG  . ASN E 3 25  ? 40.114  4.494   -53.796 1.00 40.81 ?  179 ASN A CG  1 
ATOM   6735 O OD1 . ASN E 3 25  ? 40.999  3.644   -53.719 1.00 40.16 ?  179 ASN A OD1 1 
ATOM   6736 N ND2 . ASN E 3 25  ? 39.334  4.812   -52.772 1.00 42.80 ?  179 ASN A ND2 1 
ATOM   6737 N N   . PRO E 3 26  ? 43.393  5.438   -55.367 1.00 37.21 ?  180 PRO A N   1 
ATOM   6738 C CA  . PRO E 3 26  ? 44.573  4.688   -55.832 1.00 37.15 ?  180 PRO A CA  1 
ATOM   6739 C C   . PRO E 3 26  ? 44.509  3.209   -55.517 1.00 36.55 ?  180 PRO A C   1 
ATOM   6740 O O   . PRO E 3 26  ? 45.095  2.409   -56.258 1.00 37.31 ?  180 PRO A O   1 
ATOM   6741 C CB  . PRO E 3 26  ? 45.755  5.363   -55.114 1.00 41.86 ?  180 PRO A CB  1 
ATOM   6742 C CG  . PRO E 3 26  ? 45.187  6.331   -54.153 1.00 45.42 ?  180 PRO A CG  1 
ATOM   6743 C CD  . PRO E 3 26  ? 43.698  6.389   -54.283 1.00 41.98 ?  180 PRO A CD  1 
ATOM   6744 N N   . THR E 3 27  ? 43.826  2.820   -54.441 1.00 34.84 ?  181 THR A N   1 
ATOM   6745 C CA  . THR E 3 27  ? 43.672  1.398   -54.142 1.00 32.04 ?  181 THR A CA  1 
ATOM   6746 C C   . THR E 3 27  ? 42.888  0.711   -55.250 1.00 34.11 ?  181 THR A C   1 
ATOM   6747 O O   . THR E 3 27  ? 43.266  -0.363  -55.745 1.00 31.90 ?  181 THR A O   1 
ATOM   6748 C CB  . THR E 3 27  ? 42.955  1.233   -52.806 1.00 36.36 ?  181 THR A CB  1 
ATOM   6749 O OG1 . THR E 3 27  ? 43.831  1.655   -51.759 1.00 36.75 ?  181 THR A OG1 1 
ATOM   6750 C CG2 . THR E 3 27  ? 42.592  -0.232  -52.575 1.00 35.01 ?  181 THR A CG2 1 
ATOM   6751 N N   . CYS E 3 28  ? 41.787  1.336   -55.662 1.00 33.51 ?  182 CYS A N   1 
ATOM   6752 C CA  . CYS E 3 28  ? 40.973  0.799   -56.739 1.00 31.14 ?  182 CYS A CA  1 
ATOM   6753 C C   . CYS E 3 28  ? 41.798  0.591   -58.008 1.00 31.28 ?  182 CYS A C   1 
ATOM   6754 O O   . CYS E 3 28  ? 41.773  -0.489  -58.612 1.00 30.81 ?  182 CYS A O   1 
ATOM   6755 C CB  . CYS E 3 28  ? 39.799  1.748   -56.988 1.00 32.22 ?  182 CYS A CB  1 
ATOM   6756 S SG  . CYS E 3 28  ? 38.513  1.050   -58.022 1.00 37.18 ?  182 CYS A SG  1 
ATOM   6757 N N   . TRP E 3 29  ? 42.538  1.624   -58.430 1.00 30.57 ?  183 TRP A N   1 
ATOM   6758 C CA  . TRP E 3 29  ? 43.335  1.507   -59.645 1.00 30.96 ?  183 TRP A CA  1 
ATOM   6759 C C   . TRP E 3 29  ? 44.384  0.413   -59.527 1.00 32.72 ?  183 TRP A C   1 
ATOM   6760 O O   . TRP E 3 29  ? 44.760  -0.196  -60.534 1.00 34.23 ?  183 TRP A O   1 
ATOM   6761 C CB  . TRP E 3 29  ? 44.009  2.842   -59.982 1.00 35.06 ?  183 TRP A CB  1 
ATOM   6762 C CG  . TRP E 3 29  ? 43.061  3.820   -60.621 1.00 34.92 ?  183 TRP A CG  1 
ATOM   6763 C CD1 . TRP E 3 29  ? 42.520  4.939   -60.054 1.00 36.81 ?  183 TRP A CD1 1 
ATOM   6764 C CD2 . TRP E 3 29  ? 42.471  3.702   -61.920 1.00 33.31 ?  183 TRP A CD2 1 
ATOM   6765 N NE1 . TRP E 3 29  ? 41.662  5.554   -60.944 1.00 37.80 ?  183 TRP A NE1 1 
ATOM   6766 C CE2 . TRP E 3 29  ? 41.612  4.808   -62.094 1.00 34.98 ?  183 TRP A CE2 1 
ATOM   6767 C CE3 . TRP E 3 29  ? 42.602  2.778   -62.962 1.00 33.37 ?  183 TRP A CE3 1 
ATOM   6768 C CZ2 . TRP E 3 29  ? 40.894  5.018   -63.266 1.00 35.65 ?  183 TRP A CZ2 1 
ATOM   6769 C CZ3 . TRP E 3 29  ? 41.891  2.982   -64.123 1.00 35.31 ?  183 TRP A CZ3 1 
ATOM   6770 C CH2 . TRP E 3 29  ? 41.047  4.097   -64.270 1.00 36.74 ?  183 TRP A CH2 1 
ATOM   6771 N N   . ALA E 3 30  ? 44.859  0.145   -58.311 1.00 32.95 ?  184 ALA A N   1 
ATOM   6772 C CA  . ALA E 3 30  ? 45.893  -0.871  -58.130 1.00 31.38 ?  184 ALA A CA  1 
ATOM   6773 C C   . ALA E 3 30  ? 45.377  -2.277  -58.428 1.00 31.52 ?  184 ALA A C   1 
ATOM   6774 O O   . ALA E 3 30  ? 46.145  -3.128  -58.892 1.00 31.43 ?  184 ALA A O   1 
ATOM   6775 C CB  . ALA E 3 30  ? 46.458  -0.782  -56.704 1.00 31.33 ?  184 ALA A CB  1 
ATOM   6776 N N   . ILE E 3 31  ? 44.089  -2.540  -58.205 1.00 27.97 ?  185 ILE A N   1 
ATOM   6777 C CA  . ILE E 3 31  ? 43.551  -3.895  -58.291 1.00 31.08 ?  185 ILE A CA  1 
ATOM   6778 C C   . ILE E 3 31  ? 42.479  -4.064  -59.360 1.00 32.04 ?  185 ILE A C   1 
ATOM   6779 O O   . ILE E 3 31  ? 42.026  -5.201  -59.579 1.00 30.80 ?  185 ILE A O   1 
ATOM   6780 C CB  . ILE E 3 31  ? 42.985  -4.363  -56.934 1.00 31.28 ?  185 ILE A CB  1 
ATOM   6781 C CG1 . ILE E 3 31  ? 42.036  -3.284  -56.393 1.00 31.15 ?  185 ILE A CG1 1 
ATOM   6782 C CG2 . ILE E 3 31  ? 44.137  -4.665  -55.967 1.00 29.72 ?  185 ILE A CG2 1 
ATOM   6783 C CD1 . ILE E 3 31  ? 40.542  -3.528  -56.641 1.00 31.30 ?  185 ILE A CD1 1 
ATOM   6784 N N   . CYS E 3 32  ? 42.027  -2.993  -60.012 1.00 30.23 ?  186 CYS A N   1 
ATOM   6785 C CA  . CYS E 3 32  ? 40.861  -3.097  -60.879 1.00 30.68 ?  186 CYS A CA  1 
ATOM   6786 C C   . CYS E 3 32  ? 41.206  -3.785  -62.200 1.00 37.70 ?  186 CYS A C   1 
ATOM   6787 O O   . CYS E 3 32  ? 42.369  -3.876  -62.604 1.00 35.56 ?  186 CYS A O   1 
ATOM   6788 C CB  . CYS E 3 32  ? 40.256  -1.713  -61.158 1.00 32.93 ?  186 CYS A CB  1 
ATOM   6789 S SG  . CYS E 3 32  ? 41.307  -0.608  -62.210 1.00 33.34 ?  186 CYS A SG  1 
ATOM   6790 N N   . LYS E 3 33  ? 40.161  -4.272  -62.868 1.00 36.25 ?  187 LYS A N   1 
ATOM   6791 C CA  . LYS E 3 33  ? 40.238  -4.920  -64.171 1.00 38.58 ?  187 LYS A CA  1 
ATOM   6792 C C   . LYS E 3 33  ? 39.355  -4.173  -65.164 1.00 44.13 ?  187 LYS A C   1 
ATOM   6793 O O   . LYS E 3 33  ? 38.295  -3.657  -64.800 1.00 42.52 ?  187 LYS A O   1 
ATOM   6794 C CB  . LYS E 3 33  ? 39.775  -6.383  -64.107 1.00 44.11 ?  187 LYS A CB  1 
ATOM   6795 C CG  . LYS E 3 33  ? 40.438  -7.214  -63.024 1.00 44.22 ?  187 LYS A CG  1 
ATOM   6796 C CD  . LYS E 3 33  ? 41.687  -7.883  -63.541 1.00 46.66 ?  187 LYS A CD  1 
ATOM   6797 C CE  . LYS E 3 33  ? 41.356  -8.835  -64.672 1.00 50.14 ?  187 LYS A CE  1 
ATOM   6798 N NZ  . LYS E 3 33  ? 42.614  -9.359  -65.286 1.00 56.56 ?  187 LYS A NZ  1 
ATOM   6799 N N   . ARG E 3 34  ? 39.824  -4.090  -66.407 1.00 49.59 ?  188 ARG A N   1 
ATOM   6800 C CA  . ARG E 3 34  ? 39.035  -3.437  -67.479 1.00 53.62 ?  188 ARG A CA  1 
ATOM   6801 C C   . ARG E 3 34  ? 37.981  -4.434  -67.960 1.00 58.30 ?  188 ARG A C   1 
ATOM   6802 O O   . ARG E 3 34  ? 36.907  -3.953  -68.352 1.00 58.24 ?  188 ARG A O   1 
ATOM   6803 C CB  . ARG E 3 34  ? 39.937  -3.029  -68.648 1.00 56.61 ?  188 ARG A CB  1 
ATOM   6804 C CG  . ARG E 3 34  ? 41.214  -2.301  -68.262 1.00 57.14 ?  188 ARG A CG  1 
ATOM   6805 C CD  . ARG E 3 34  ? 42.124  -2.201  -69.472 1.00 59.82 ?  188 ARG A CD  1 
ATOM   6806 N NE  . ARG E 3 34  ? 43.388  -1.531  -69.208 1.00 63.24 ?  188 ARG A NE  1 
ATOM   6807 C CZ  . ARG E 3 34  ? 44.577  -2.113  -69.302 1.00 61.96 ?  188 ARG A CZ  1 
ATOM   6808 N NH1 . ARG E 3 34  ? 44.660  -3.427  -69.383 1.00 59.29 ?  188 ARG A NH1 1 
ATOM   6809 N NH2 . ARG E 3 34  ? 45.675  -1.378  -69.312 1.00 60.58 ?  188 ARG A NH2 1 
ATOM   6810 N N   . ASN F 3 7   ? 6.818   15.954  -63.430 1.00 53.80 ?  161 ASN B N   1 
ATOM   6811 C CA  . ASN F 3 7   ? 6.507   14.546  -63.090 1.00 47.94 ?  161 ASN B CA  1 
ATOM   6812 C C   . ASN F 3 7   ? 6.913   14.274  -61.639 1.00 40.53 ?  161 ASN B C   1 
ATOM   6813 O O   . ASN F 3 7   ? 7.430   13.183  -61.376 1.00 42.22 ?  161 ASN B O   1 
ATOM   6814 C CB  . ASN F 3 7   ? 7.198   13.568  -64.034 1.00 50.45 ?  161 ASN B CB  1 
ATOM   6815 C CG  . ASN F 3 7   ? 6.550   13.507  -65.399 1.00 56.80 ?  161 ASN B CG  1 
ATOM   6816 O OD1 . ASN F 3 7   ? 7.236   13.550  -66.418 1.00 56.15 ?  161 ASN B OD1 1 
ATOM   6817 N ND2 . ASN F 3 7   ? 5.232   13.408  -65.431 1.00 58.82 ?  161 ASN B ND2 1 
ATOM   6818 N N   . ASP F 3 8   ? 6.671   15.232  -60.752 1.00 35.28 ?  162 ASP B N   1 
ATOM   6819 C CA  . ASP F 3 8   ? 6.973   14.994  -59.348 1.00 31.25 ?  162 ASP B CA  1 
ATOM   6820 C C   . ASP F 3 8   ? 5.681   14.994  -58.536 1.00 29.93 ?  162 ASP B C   1 
ATOM   6821 O O   . ASP F 3 8   ? 4.729   15.723  -58.851 1.00 30.55 ?  162 ASP B O   1 
ATOM   6822 C CB  . ASP F 3 8   ? 7.947   16.064  -58.810 1.00 33.01 ?  162 ASP B CB  1 
ATOM   6823 C CG  . ASP F 3 8   ? 8.416   15.770  -57.395 1.00 30.53 ?  162 ASP B CG  1 
ATOM   6824 O OD1 . ASP F 3 8   ? 9.303   14.897  -57.231 1.00 31.40 ?  162 ASP B OD1 1 
ATOM   6825 O OD2 . ASP F 3 8   ? 7.883   16.408  -56.455 1.00 31.44 -1 162 ASP B OD2 1 
ATOM   6826 N N   . PHE F 3 9   ? 5.657   14.189  -57.470 1.00 26.68 ?  163 PHE B N   1 
ATOM   6827 C CA  . PHE F 3 9   ? 4.417   13.965  -56.734 1.00 26.26 ?  163 PHE B CA  1 
ATOM   6828 C C   . PHE F 3 9   ? 4.501   14.361  -55.261 1.00 25.55 ?  163 PHE B C   1 
ATOM   6829 O O   . PHE F 3 9   ? 3.552   14.104  -54.510 1.00 25.60 ?  163 PHE B O   1 
ATOM   6830 C CB  . PHE F 3 9   ? 3.995   12.505  -56.919 1.00 25.13 ?  163 PHE B CB  1 
ATOM   6831 C CG  . PHE F 3 9   ? 3.763   12.155  -58.368 1.00 28.36 ?  163 PHE B CG  1 
ATOM   6832 C CD1 . PHE F 3 9   ? 2.608   12.576  -59.025 1.00 33.01 ?  163 PHE B CD1 1 
ATOM   6833 C CD2 . PHE F 3 9   ? 4.752   11.507  -59.105 1.00 29.77 ?  163 PHE B CD2 1 
ATOM   6834 C CE1 . PHE F 3 9   ? 2.415   12.293  -60.374 1.00 33.65 ?  163 PHE B CE1 1 
ATOM   6835 C CE2 . PHE F 3 9   ? 4.572   11.228  -60.465 1.00 32.66 ?  163 PHE B CE2 1 
ATOM   6836 C CZ  . PHE F 3 9   ? 3.413   11.620  -61.096 1.00 32.29 ?  163 PHE B CZ  1 
ATOM   6837 N N   . HIS F 3 10  ? 5.586   15.010  -54.833 1.00 25.45 ?  164 HIS B N   1 
ATOM   6838 C CA  . HIS F 3 10  ? 5.576   15.673  -53.534 1.00 25.74 ?  164 HIS B CA  1 
ATOM   6839 C C   . HIS F 3 10  ? 4.457   16.706  -53.492 1.00 26.96 ?  164 HIS B C   1 
ATOM   6840 O O   . HIS F 3 10  ? 4.264   17.470  -54.446 1.00 26.16 ?  164 HIS B O   1 
ATOM   6841 C CB  . HIS F 3 10  ? 6.905   16.391  -53.272 1.00 25.57 ?  164 HIS B CB  1 
ATOM   6842 C CG  . HIS F 3 10  ? 8.074   15.473  -53.064 1.00 25.05 ?  164 HIS B CG  1 
ATOM   6843 N ND1 . HIS F 3 10  ? 8.910   15.104  -54.093 1.00 23.55 ?  164 HIS B ND1 1 
ATOM   6844 C CD2 . HIS F 3 10  ? 8.592   14.920  -51.941 1.00 23.09 ?  164 HIS B CD2 1 
ATOM   6845 C CE1 . HIS F 3 10  ? 9.869   14.321  -53.621 1.00 25.38 ?  164 HIS B CE1 1 
ATOM   6846 N NE2 . HIS F 3 10  ? 9.703   14.201  -52.316 1.00 22.76 ?  164 HIS B NE2 1 
ATOM   6847 N N   . PHE F 3 11  ? 3.730   16.732  -52.373 1.00 22.93 ?  165 PHE B N   1 
ATOM   6848 C CA  . PHE F 3 11  ? 2.615   17.651  -52.129 1.00 24.98 ?  165 PHE B CA  1 
ATOM   6849 C C   . PHE F 3 11  ? 1.484   17.520  -53.150 1.00 28.10 ?  165 PHE B C   1 
ATOM   6850 O O   . PHE F 3 11  ? 0.705   18.457  -53.326 1.00 30.26 ?  165 PHE B O   1 
ATOM   6851 C CB  . PHE F 3 11  ? 3.105   19.105  -52.076 1.00 25.23 ?  165 PHE B CB  1 
ATOM   6852 C CG  . PHE F 3 11  ? 4.196   19.322  -51.068 1.00 21.80 ?  165 PHE B CG  1 
ATOM   6853 C CD1 . PHE F 3 11  ? 3.904   19.367  -49.709 1.00 22.88 ?  165 PHE B CD1 1 
ATOM   6854 C CD2 . PHE F 3 11  ? 5.523   19.453  -51.479 1.00 25.90 ?  165 PHE B CD2 1 
ATOM   6855 C CE1 . PHE F 3 11  ? 4.933   19.568  -48.765 1.00 25.33 ?  165 PHE B CE1 1 
ATOM   6856 C CE2 . PHE F 3 11  ? 6.548   19.660  -50.547 1.00 27.35 ?  165 PHE B CE2 1 
ATOM   6857 C CZ  . PHE F 3 11  ? 6.243   19.710  -49.187 1.00 25.61 ?  165 PHE B CZ  1 
ATOM   6858 N N   . GLU F 3 12  ? 1.375   16.388  -53.832 1.00 27.58 ?  166 GLU B N   1 
ATOM   6859 C CA  . GLU F 3 12  ? 0.292   16.173  -54.778 1.00 27.61 ?  166 GLU B CA  1 
ATOM   6860 C C   . GLU F 3 12  ? -0.726  15.230  -54.128 1.00 26.86 ?  166 GLU B C   1 
ATOM   6861 O O   . GLU F 3 12  ? -0.541  14.769  -52.999 1.00 27.06 ?  166 GLU B O   1 
ATOM   6862 C CB  . GLU F 3 12  ? 0.815   15.596  -56.090 1.00 25.43 ?  166 GLU B CB  1 
ATOM   6863 C CG  . GLU F 3 12  ? 1.728   16.522  -56.934 1.00 30.95 ?  166 GLU B CG  1 
ATOM   6864 C CD  . GLU F 3 12  ? 1.087   17.853  -57.323 1.00 37.03 ?  166 GLU B CD  1 
ATOM   6865 O OE1 . GLU F 3 12  ? -0.154  17.935  -57.443 1.00 38.98 ?  166 GLU B OE1 1 
ATOM   6866 O OE2 . GLU F 3 12  ? 1.838   18.833  -57.457 1.00 41.49 -1 166 GLU B OE2 1 
ATOM   6867 N N   . VAL F 3 13  ? -1.817  14.928  -54.835 1.00 26.59 ?  167 VAL B N   1 
ATOM   6868 C CA  . VAL F 3 13  ? -2.855  14.070  -54.269 1.00 27.68 ?  167 VAL B CA  1 
ATOM   6869 C C   . VAL F 3 13  ? -2.893  12.684  -54.894 1.00 24.14 ?  167 VAL B C   1 
ATOM   6870 O O   . VAL F 3 13  ? -3.606  11.816  -54.370 1.00 27.69 ?  167 VAL B O   1 
ATOM   6871 C CB  . VAL F 3 13  ? -4.256  14.720  -54.366 1.00 28.50 ?  167 VAL B CB  1 
ATOM   6872 C CG1 . VAL F 3 13  ? -4.291  16.043  -53.617 1.00 32.22 ?  167 VAL B CG1 1 
ATOM   6873 C CG2 . VAL F 3 13  ? -4.666  14.869  -55.823 1.00 31.83 ?  167 VAL B CG2 1 
ATOM   6874 N N   . PHE F 3 14  ? -2.151  12.437  -55.978 1.00 26.47 ?  168 PHE B N   1 
ATOM   6875 C CA  . PHE F 3 14  ? -2.228  11.159  -56.684 1.00 25.40 ?  168 PHE B CA  1 
ATOM   6876 C C   . PHE F 3 14  ? -0.870  10.837  -57.296 1.00 29.72 ?  168 PHE B C   1 
ATOM   6877 O O   . PHE F 3 14  ? -0.394  11.580  -58.157 1.00 29.01 ?  168 PHE B O   1 
ATOM   6878 C CB  . PHE F 3 14  ? -3.310  11.221  -57.773 1.00 26.36 ?  168 PHE B CB  1 
ATOM   6879 C CG  . PHE F 3 14  ? -3.567  9.904   -58.465 1.00 28.49 ?  168 PHE B CG  1 
ATOM   6880 C CD1 . PHE F 3 14  ? -2.815  9.527   -59.573 1.00 30.47 ?  168 PHE B CD1 1 
ATOM   6881 C CD2 . PHE F 3 14  ? -4.577  9.068   -58.032 1.00 29.74 ?  168 PHE B CD2 1 
ATOM   6882 C CE1 . PHE F 3 14  ? -3.070  8.311   -60.219 1.00 31.34 ?  168 PHE B CE1 1 
ATOM   6883 C CE2 . PHE F 3 14  ? -4.833  7.865   -58.670 1.00 31.49 ?  168 PHE B CE2 1 
ATOM   6884 C CZ  . PHE F 3 14  ? -4.069  7.486   -59.755 1.00 30.33 ?  168 PHE B CZ  1 
ATOM   6885 N N   . ASN F 3 15  ? -0.242  9.747   -56.845 1.00 27.59 ?  169 ASN B N   1 
ATOM   6886 C CA  . ASN F 3 15  ? 1.047   9.304   -57.374 1.00 27.30 ?  169 ASN B CA  1 
ATOM   6887 C C   . ASN F 3 15  ? 0.826   8.274   -58.478 1.00 29.16 ?  169 ASN B C   1 
ATOM   6888 O O   . ASN F 3 15  ? -0.113  7.480   -58.419 1.00 28.36 ?  169 ASN B O   1 
ATOM   6889 C CB  . ASN F 3 15  ? 1.901   8.702   -56.250 1.00 24.49 ?  169 ASN B CB  1 
ATOM   6890 C CG  . ASN F 3 15  ? 3.289   8.270   -56.728 1.00 25.14 ?  169 ASN B CG  1 
ATOM   6891 O OD1 . ASN F 3 15  ? 3.926   8.975   -57.504 1.00 28.06 ?  169 ASN B OD1 1 
ATOM   6892 N ND2 . ASN F 3 15  ? 3.732   7.077   -56.299 1.00 25.15 ?  169 ASN B ND2 1 
ATOM   6893 N N   . PHE F 3 16  ? 1.685   8.288   -59.489 1.00 28.24 ?  170 PHE B N   1 
ATOM   6894 C CA  . PHE F 3 16  ? 1.502   7.398   -60.632 1.00 31.86 ?  170 PHE B CA  1 
ATOM   6895 C C   . PHE F 3 16  ? 2.179   6.054   -60.376 1.00 31.38 ?  170 PHE B C   1 
ATOM   6896 O O   . PHE F 3 16  ? 3.402   5.974   -60.201 1.00 29.60 ?  170 PHE B O   1 
ATOM   6897 C CB  . PHE F 3 16  ? 2.013   8.065   -61.908 1.00 37.48 ?  170 PHE B CB  1 
ATOM   6898 C CG  . PHE F 3 16  ? 1.031   9.066   -62.490 1.00 44.20 ?  170 PHE B CG  1 
ATOM   6899 C CD1 . PHE F 3 16  ? 0.367   9.973   -61.666 1.00 41.61 ?  170 PHE B CD1 1 
ATOM   6900 C CD2 . PHE F 3 16  ? 0.776   9.107   -63.854 1.00 49.13 ?  170 PHE B CD2 1 
ATOM   6901 C CE1 . PHE F 3 16  ? -0.534  10.893  -62.189 1.00 44.19 ?  170 PHE B CE1 1 
ATOM   6902 C CE2 . PHE F 3 16  ? -0.124  10.032  -64.381 1.00 51.32 ?  170 PHE B CE2 1 
ATOM   6903 C CZ  . PHE F 3 16  ? -0.777  10.922  -63.545 1.00 49.27 ?  170 PHE B CZ  1 
ATOM   6904 N N   . VAL F 3 17  ? 1.370   5.005   -60.311 1.00 29.35 ?  171 VAL B N   1 
ATOM   6905 C CA  . VAL F 3 17  ? 1.835   3.644   -60.084 1.00 32.24 ?  171 VAL B CA  1 
ATOM   6906 C C   . VAL F 3 17  ? 1.592   2.853   -61.368 1.00 33.61 ?  171 VAL B C   1 
ATOM   6907 O O   . VAL F 3 17  ? 0.442   2.740   -61.806 1.00 33.03 ?  171 VAL B O   1 
ATOM   6908 C CB  . VAL F 3 17  ? 1.115   3.006   -58.885 1.00 31.19 ?  171 VAL B CB  1 
ATOM   6909 C CG1 . VAL F 3 17  ? 1.635   1.588   -58.628 1.00 30.16 ?  171 VAL B CG1 1 
ATOM   6910 C CG2 . VAL F 3 17  ? 1.274   3.890   -57.636 1.00 26.80 ?  171 VAL B CG2 1 
ATOM   6911 N N   . PRO F 3 18  ? 2.624   2.306   -62.004 1.00 33.96 ?  172 PRO B N   1 
ATOM   6912 C CA  . PRO F 3 18  ? 2.418   1.651   -63.302 1.00 34.46 ?  172 PRO B CA  1 
ATOM   6913 C C   . PRO F 3 18  ? 1.712   0.318   -63.134 1.00 35.26 ?  172 PRO B C   1 
ATOM   6914 O O   . PRO F 3 18  ? 1.997   -0.443  -62.208 1.00 36.71 ?  172 PRO B O   1 
ATOM   6915 C CB  . PRO F 3 18  ? 3.846   1.460   -63.831 1.00 37.39 ?  172 PRO B CB  1 
ATOM   6916 C CG  . PRO F 3 18  ? 4.670   1.333   -62.597 1.00 36.19 ?  172 PRO B CG  1 
ATOM   6917 C CD  . PRO F 3 18  ? 4.033   2.241   -61.570 1.00 32.77 ?  172 PRO B CD  1 
ATOM   6918 N N   . CYS F 3 19  ? 0.776   0.036   -64.045 1.00 38.59 ?  173 CYS B N   1 
ATOM   6919 C CA  . CYS F 3 19  ? 0.030   -1.215  -63.951 1.00 35.91 ?  173 CYS B CA  1 
ATOM   6920 C C   . CYS F 3 19  ? 0.934   -2.431  -64.128 1.00 39.59 ?  173 CYS B C   1 
ATOM   6921 O O   . CYS F 3 19  ? 0.539   -3.544  -63.772 1.00 39.78 ?  173 CYS B O   1 
ATOM   6922 C CB  . CYS F 3 19  ? -1.087  -1.231  -64.993 1.00 37.59 ?  173 CYS B CB  1 
ATOM   6923 S SG  . CYS F 3 19  ? -2.469  -0.096  -64.602 1.00 38.86 ?  173 CYS B SG  1 
ATOM   6924 N N   . SER F 3 20  ? 2.153   -2.235  -64.636 1.00 40.80 ?  174 SER B N   1 
ATOM   6925 C CA  . SER F 3 20  ? 3.047   -3.353  -64.895 1.00 40.21 ?  174 SER B CA  1 
ATOM   6926 C C   . SER F 3 20  ? 3.531   -4.039  -63.623 1.00 42.35 ?  174 SER B C   1 
ATOM   6927 O O   . SER F 3 20  ? 3.939   -5.202  -63.688 1.00 46.51 ?  174 SER B O   1 
ATOM   6928 C CB  . SER F 3 20  ? 4.224   -2.864  -65.731 1.00 44.12 ?  174 SER B CB  1 
ATOM   6929 O OG  . SER F 3 20  ? 4.983   -1.910  -65.012 1.00 41.69 ?  174 SER B OG  1 
ATOM   6930 N N   . ILE F 3 21  ? 3.478   -3.369  -62.467 1.00 39.40 ?  175 ILE B N   1 
ATOM   6931 C CA  . ILE F 3 21  ? 3.939   -3.960  -61.210 1.00 38.93 ?  175 ILE B CA  1 
ATOM   6932 C C   . ILE F 3 21  ? 2.800   -4.622  -60.443 1.00 41.25 ?  175 ILE B C   1 
ATOM   6933 O O   . ILE F 3 21  ? 3.000   -5.108  -59.324 1.00 42.89 ?  175 ILE B O   1 
ATOM   6934 C CB  . ILE F 3 21  ? 4.624   -2.909  -60.310 1.00 42.06 ?  175 ILE B CB  1 
ATOM   6935 C CG1 . ILE F 3 21  ? 3.588   -1.907  -59.767 1.00 38.20 ?  175 ILE B CG1 1 
ATOM   6936 C CG2 . ILE F 3 21  ? 5.788   -2.236  -61.034 1.00 40.84 ?  175 ILE B CG2 1 
ATOM   6937 C CD1 . ILE F 3 21  ? 3.875   -1.407  -58.344 1.00 36.83 ?  175 ILE B CD1 1 
ATOM   6938 N N   . CYS F 3 22  ? 1.592   -4.648  -61.016 1.00 42.06 ?  176 CYS B N   1 
ATOM   6939 C CA  . CYS F 3 22  ? 0.439   -4.926  -60.167 1.00 40.59 ?  176 CYS B CA  1 
ATOM   6940 C C   . CYS F 3 22  ? 0.227   -6.407  -59.878 1.00 46.82 ?  176 CYS B C   1 
ATOM   6941 O O   . CYS F 3 22  ? -0.364  -6.730  -58.841 1.00 47.73 ?  176 CYS B O   1 
ATOM   6942 C CB  . CYS F 3 22  ? -0.829  -4.328  -60.774 1.00 40.77 ?  176 CYS B CB  1 
ATOM   6943 S SG  . CYS F 3 22  ? -0.923  -2.545  -60.485 1.00 39.18 ?  176 CYS B SG  1 
ATOM   6944 N N   . SER F 3 23  ? 0.656   -7.274  -60.786 1.00 46.20 ?  177 SER B N   1 
ATOM   6945 C CA  . SER F 3 23  ? 0.558   -8.731  -60.519 1.00 48.76 ?  177 SER B CA  1 
ATOM   6946 C C   . SER F 3 23  ? -0.875  -9.112  -60.149 1.00 46.96 ?  177 SER B C   1 
ATOM   6947 O O   . SER F 3 23  ? -1.753  -8.940  -60.986 1.00 50.15 ?  177 SER B O   1 
ATOM   6948 C CB  . SER F 3 23  ? 1.523   -9.145  -59.446 1.00 51.98 ?  177 SER B CB  1 
ATOM   6949 O OG  . SER F 3 23  ? 2.604   -9.875  -59.997 1.00 59.50 ?  177 SER B OG  1 
ATOM   6950 N N   . ASN F 3 24  ? -1.079  -9.661  -58.958 1.00 46.32 ?  178 ASN B N   1 
ATOM   6951 C CA  . ASN F 3 24  ? -2.415  -10.045 -58.514 1.00 47.72 ?  178 ASN B CA  1 
ATOM   6952 C C   . ASN F 3 24  ? -2.853  -9.264  -57.279 1.00 47.85 ?  178 ASN B C   1 
ATOM   6953 O O   . ASN F 3 24  ? -3.704  -9.725  -56.517 1.00 47.94 ?  178 ASN B O   1 
ATOM   6954 C CB  . ASN F 3 24  ? -2.501  -11.552 -58.254 1.00 52.97 ?  178 ASN B CB  1 
ATOM   6955 C CG  . ASN F 3 24  ? -2.278  -12.379 -59.515 1.00 56.30 ?  178 ASN B CG  1 
ATOM   6956 O OD1 . ASN F 3 24  ? -2.870  -12.106 -60.566 1.00 59.69 ?  178 ASN B OD1 1 
ATOM   6957 N ND2 . ASN F 3 24  ? -1.433  -13.397 -59.415 1.00 58.24 ?  178 ASN B ND2 1 
ATOM   6958 N N   . ASN F 3 25  ? -2.297  -8.063  -57.090 1.00 45.66 ?  179 ASN B N   1 
ATOM   6959 C CA  . ASN F 3 25  ? -2.697  -7.193  -55.988 1.00 41.26 ?  179 ASN B CA  1 
ATOM   6960 C C   . ASN F 3 25  ? -3.873  -6.323  -56.419 1.00 40.25 ?  179 ASN B C   1 
ATOM   6961 O O   . ASN F 3 25  ? -3.695  -5.440  -57.275 1.00 36.80 ?  179 ASN B O   1 
ATOM   6962 C CB  . ASN F 3 25  ? -1.528  -6.323  -55.549 1.00 42.86 ?  179 ASN B CB  1 
ATOM   6963 C CG  . ASN F 3 25  ? -1.766  -5.680  -54.207 1.00 42.22 ?  179 ASN B CG  1 
ATOM   6964 O OD1 . ASN F 3 25  ? -2.683  -4.869  -54.059 1.00 43.69 ?  179 ASN B OD1 1 
ATOM   6965 N ND2 . ASN F 3 25  ? -0.949  -6.032  -53.215 1.00 42.66 ?  179 ASN B ND2 1 
ATOM   6966 N N   . PRO F 3 26  ? -5.073  -6.521  -55.867 1.00 38.57 ?  180 PRO B N   1 
ATOM   6967 C CA  . PRO F 3 26  ? -6.222  -5.722  -56.326 1.00 39.06 ?  180 PRO B CA  1 
ATOM   6968 C C   . PRO F 3 26  ? -6.131  -4.248  -55.969 1.00 37.39 ?  180 PRO B C   1 
ATOM   6969 O O   . PRO F 3 26  ? -6.674  -3.420  -56.709 1.00 30.74 ?  180 PRO B O   1 
ATOM   6970 C CB  . PRO F 3 26  ? -7.423  -6.398  -55.641 1.00 43.93 ?  180 PRO B CB  1 
ATOM   6971 C CG  . PRO F 3 26  ? -6.848  -7.181  -54.510 1.00 44.61 ?  180 PRO B CG  1 
ATOM   6972 C CD  . PRO F 3 26  ? -5.475  -7.600  -54.947 1.00 44.29 ?  180 PRO B CD  1 
ATOM   6973 N N   . THR F 3 27  ? -5.480  -3.888  -54.860 1.00 36.78 ?  181 THR B N   1 
ATOM   6974 C CA  . THR F 3 27  ? -5.265  -2.472  -54.568 1.00 35.34 ?  181 THR B CA  1 
ATOM   6975 C C   . THR F 3 27  ? -4.507  -1.811  -55.706 1.00 33.53 ?  181 THR B C   1 
ATOM   6976 O O   . THR F 3 27  ? -4.920  -0.769  -56.223 1.00 33.22 ?  181 THR B O   1 
ATOM   6977 C CB  . THR F 3 27  ? -4.507  -2.304  -53.248 1.00 35.86 ?  181 THR B CB  1 
ATOM   6978 O OG1 . THR F 3 27  ? -5.240  -2.930  -52.192 1.00 38.94 ?  181 THR B OG1 1 
ATOM   6979 C CG2 . THR F 3 27  ? -4.313  -0.816  -52.912 1.00 32.50 ?  181 THR B CG2 1 
ATOM   6980 N N   . CYS F 3 28  ? -3.396  -2.426  -56.119 1.00 31.74 ?  182 CYS B N   1 
ATOM   6981 C CA  . CYS F 3 28  ? -2.613  -1.914  -57.232 1.00 29.71 ?  182 CYS B CA  1 
ATOM   6982 C C   . CYS F 3 28  ? -3.481  -1.729  -58.476 1.00 33.37 ?  182 CYS B C   1 
ATOM   6983 O O   . CYS F 3 28  ? -3.484  -0.653  -59.090 1.00 31.97 ?  182 CYS B O   1 
ATOM   6984 C CB  . CYS F 3 28  ? -1.438  -2.863  -57.505 1.00 34.34 ?  182 CYS B CB  1 
ATOM   6985 S SG  . CYS F 3 28  ? -0.165  -2.202  -58.596 1.00 38.92 ?  182 CYS B SG  1 
ATOM   6986 N N   . TRP F 3 29  ? -4.266  -2.753  -58.840 1.00 33.87 ?  183 TRP B N   1 
ATOM   6987 C CA  . TRP F 3 29  ? -5.075  -2.619  -60.052 1.00 35.10 ?  183 TRP B CA  1 
ATOM   6988 C C   . TRP F 3 29  ? -6.092  -1.493  -59.928 1.00 35.35 ?  183 TRP B C   1 
ATOM   6989 O O   . TRP F 3 29  ? -6.430  -0.854  -60.931 1.00 33.50 ?  183 TRP B O   1 
ATOM   6990 C CB  . TRP F 3 29  ? -5.778  -3.933  -60.385 1.00 37.26 ?  183 TRP B CB  1 
ATOM   6991 C CG  . TRP F 3 29  ? -4.844  -4.917  -61.008 1.00 38.26 ?  183 TRP B CG  1 
ATOM   6992 C CD1 . TRP F 3 29  ? -4.361  -6.073  -60.445 1.00 38.35 ?  183 TRP B CD1 1 
ATOM   6993 C CD2 . TRP F 3 29  ? -4.209  -4.797  -62.284 1.00 36.73 ?  183 TRP B CD2 1 
ATOM   6994 N NE1 . TRP F 3 29  ? -3.501  -6.695  -61.317 1.00 38.02 ?  183 TRP B NE1 1 
ATOM   6995 C CE2 . TRP F 3 29  ? -3.383  -5.931  -62.448 1.00 39.92 ?  183 TRP B CE2 1 
ATOM   6996 C CE3 . TRP F 3 29  ? -4.276  -3.855  -63.316 1.00 37.35 ?  183 TRP B CE3 1 
ATOM   6997 C CZ2 . TRP F 3 29  ? -2.632  -6.143  -63.603 1.00 41.67 ?  183 TRP B CZ2 1 
ATOM   6998 C CZ3 . TRP F 3 29  ? -3.523  -4.068  -64.460 1.00 37.23 ?  183 TRP B CZ3 1 
ATOM   6999 C CH2 . TRP F 3 29  ? -2.716  -5.202  -64.594 1.00 38.15 ?  183 TRP B CH2 1 
ATOM   7000 N N   . ALA F 3 30  ? -6.558  -1.207  -58.704 1.00 33.76 ?  184 ALA B N   1 
ATOM   7001 C CA  . ALA F 3 30  ? -7.577  -0.170  -58.527 1.00 36.27 ?  184 ALA B CA  1 
ATOM   7002 C C   . ALA F 3 30  ? -7.055  1.227   -58.847 1.00 36.56 ?  184 ALA B C   1 
ATOM   7003 O O   . ALA F 3 30  ? -7.833  2.076   -59.295 1.00 36.35 ?  184 ALA B O   1 
ATOM   7004 C CB  . ALA F 3 30  ? -8.127  -0.207  -57.102 1.00 33.68 ?  184 ALA B CB  1 
ATOM   7005 N N   . ILE F 3 31  ? -5.763  1.488   -58.641 1.00 32.04 ?  185 ILE B N   1 
ATOM   7006 C CA  . ILE F 3 31  ? -5.215  2.839   -58.765 1.00 33.41 ?  185 ILE B CA  1 
ATOM   7007 C C   . ILE F 3 31  ? -4.158  2.980   -59.848 1.00 32.49 ?  185 ILE B C   1 
ATOM   7008 O O   . ILE F 3 31  ? -3.671  4.101   -60.061 1.00 32.31 ?  185 ILE B O   1 
ATOM   7009 C CB  . ILE F 3 31  ? -4.628  3.340   -57.428 1.00 30.63 ?  185 ILE B CB  1 
ATOM   7010 C CG1 . ILE F 3 31  ? -3.743  2.250   -56.836 1.00 29.59 ?  185 ILE B CG1 1 
ATOM   7011 C CG2 . ILE F 3 31  ? -5.756  3.713   -56.483 1.00 30.82 ?  185 ILE B CG2 1 
ATOM   7012 C CD1 . ILE F 3 31  ? -2.237  2.383   -57.152 1.00 30.45 ?  185 ILE B CD1 1 
ATOM   7013 N N   . CYS F 3 32  ? -3.753  1.901   -60.515 1.00 31.89 ?  186 CYS B N   1 
ATOM   7014 C CA  . CYS F 3 32  ? -2.582  1.971   -61.379 1.00 35.18 ?  186 CYS B CA  1 
ATOM   7015 C C   . CYS F 3 32  ? -2.906  2.658   -62.704 1.00 37.06 ?  186 CYS B C   1 
ATOM   7016 O O   . CYS F 3 32  ? -4.063  2.749   -63.127 1.00 36.25 ?  186 CYS B O   1 
ATOM   7017 C CB  . CYS F 3 32  ? -2.010  0.573   -61.623 1.00 32.36 ?  186 CYS B CB  1 
ATOM   7018 S SG  . CYS F 3 32  ? -3.032  -0.514  -62.688 1.00 35.74 ?  186 CYS B SG  1 
ATOM   7019 N N   . LYS F 3 33  ? -1.854  3.173   -63.340 1.00 33.45 ?  187 LYS B N   1 
ATOM   7020 C CA  . LYS F 3 33  ? -1.910  3.877   -64.616 1.00 38.71 ?  187 LYS B CA  1 
ATOM   7021 C C   . LYS F 3 33  ? -1.098  3.098   -65.642 1.00 43.44 ?  187 LYS B C   1 
ATOM   7022 O O   . LYS F 3 33  ? -0.117  2.423   -65.300 1.00 39.84 ?  187 LYS B O   1 
ATOM   7023 C CB  . LYS F 3 33  ? -1.326  5.294   -64.505 1.00 40.67 ?  187 LYS B CB  1 
ATOM   7024 C CG  . LYS F 3 33  ? -2.030  6.230   -63.523 1.00 43.84 ?  187 LYS B CG  1 
ATOM   7025 C CD  . LYS F 3 33  ? -3.421  6.622   -63.929 1.00 45.42 ?  187 LYS B CD  1 
ATOM   7026 C CE  . LYS F 3 33  ? -3.383  7.505   -65.154 1.00 53.23 ?  187 LYS B CE  1 
ATOM   7027 N NZ  . LYS F 3 33  ? -4.733  8.048   -65.471 1.00 58.30 ?  187 LYS B NZ  1 
ATOM   7028 N N   . ARG F 3 34  ? -1.489  3.212   -66.904 1.00 45.84 ?  188 ARG B N   1 
ATOM   7029 C CA  . ARG F 3 34  ? -0.793  2.475   -67.948 1.00 49.11 ?  188 ARG B CA  1 
ATOM   7030 C C   . ARG F 3 34  ? 0.355   3.299   -68.517 1.00 52.40 ?  188 ARG B C   1 
ATOM   7031 O O   . ARG F 3 34  ? 1.345   2.742   -69.007 1.00 60.17 ?  188 ARG B O   1 
ATOM   7032 C CB  . ARG F 3 34  ? -1.763  2.078   -69.058 1.00 53.56 ?  188 ARG B CB  1 
ATOM   7033 C CG  . ARG F 3 34  ? -2.627  0.886   -68.687 1.00 54.71 ?  188 ARG B CG  1 
ATOM   7034 C CD  . ARG F 3 34  ? -3.452  0.398   -69.858 1.00 59.70 ?  188 ARG B CD  1 
ATOM   7035 N NE  . ARG F 3 34  ? -4.884  0.358   -69.583 1.00 61.46 ?  188 ARG B NE  1 
ATOM   7036 C CZ  . ARG F 3 34  ? -5.650  -0.707  -69.784 1.00 61.59 ?  188 ARG B CZ  1 
ATOM   7037 N NH1 . ARG F 3 34  ? -5.132  -1.881  -70.115 1.00 61.70 ?  188 ARG B NH1 1 
ATOM   7038 N NH2 . ARG F 3 34  ? -6.970  -0.595  -69.640 1.00 59.72 ?  188 ARG B NH2 1 
HETATM 7039 S S   . SO4 G 4 .   ? 19.075  -0.060  -41.191 1.00 30.00 ?  301 SO4 E S   1 
HETATM 7040 O O1  . SO4 G 4 .   ? 19.075  -1.173  -42.082 1.00 30.00 ?  301 SO4 E O1  1 
HETATM 7041 O O2  . SO4 G 4 .   ? 17.995  0.818   -41.519 1.00 30.00 ?  301 SO4 E O2  1 
HETATM 7042 O O3  . SO4 G 4 .   ? 18.923  -0.527  -39.847 1.00 30.00 ?  301 SO4 E O3  1 
HETATM 7043 O O4  . SO4 G 4 .   ? 20.315  0.646   -41.315 1.00 30.00 ?  301 SO4 E O4  1 
HETATM 7044 S S   . SO4 H 4 .   ? 18.872  39.934  -27.809 1.00 30.00 ?  301 SO4 G S   1 
HETATM 7045 O O1  . SO4 H 4 .   ? 19.996  40.699  -28.251 1.00 30.00 ?  301 SO4 G O1  1 
HETATM 7046 O O2  . SO4 H 4 .   ? 18.075  39.545  -28.934 1.00 30.00 ?  301 SO4 G O2  1 
HETATM 7047 O O3  . SO4 H 4 .   ? 19.340  38.769  -27.120 1.00 30.00 ?  301 SO4 G O3  1 
HETATM 7048 O O4  . SO4 H 4 .   ? 18.087  40.736  -26.920 1.00 30.00 ?  301 SO4 G O4  1 
HETATM 7049 S S   . SO4 I 4 .   ? 42.861  -5.799  -67.149 1.00 30.00 ?  301 SO4 A S   1 
HETATM 7050 O O1  . SO4 I 4 .   ? 43.383  -5.474  -68.444 1.00 30.00 ?  301 SO4 A O1  1 
HETATM 7051 O O2  . SO4 I 4 .   ? 41.487  -6.193  -67.274 1.00 30.00 ?  301 SO4 A O2  1 
HETATM 7052 O O3  . SO4 I 4 .   ? 43.618  -6.877  -66.590 1.00 30.00 ?  301 SO4 A O3  1 
HETATM 7053 O O4  . SO4 I 4 .   ? 42.958  -4.655  -66.294 1.00 30.00 ?  301 SO4 A O4  1 
HETATM 7054 S S   . SO4 J 4 .   ? -5.029  4.561   -67.555 1.00 30.00 ?  301 SO4 B S   1 
HETATM 7055 O O1  . SO4 J 4 .   ? -3.620  4.664   -67.776 1.00 30.00 ?  301 SO4 B O1  1 
HETATM 7056 O O2  . SO4 J 4 .   ? -5.632  3.841   -68.636 1.00 30.00 ?  301 SO4 B O2  1 
HETATM 7057 O O3  . SO4 J 4 .   ? -5.271  3.865   -66.326 1.00 30.00 ?  301 SO4 B O3  1 
HETATM 7058 O O4  . SO4 J 4 .   ? -5.595  5.874   -67.480 1.00 30.00 ?  301 SO4 B O4  1 
HETATM 7059 O O   . HOH K 5 .   ? 46.375  -17.691 -45.660 1.00 24.26 ?  401 HOH E O   1 
HETATM 7060 O O   . HOH K 5 .   ? 47.441  -1.214  -39.671 1.00 35.46 ?  402 HOH E O   1 
HETATM 7061 O O   . HOH K 5 .   ? 38.767  -5.973  -47.753 1.00 30.70 ?  403 HOH E O   1 
HETATM 7062 O O   . HOH K 5 .   ? 35.946  -22.721 -16.783 1.00 42.63 ?  404 HOH E O   1 
HETATM 7063 O O   . HOH K 5 .   ? 23.137  -12.080 -52.924 1.00 26.29 ?  405 HOH E O   1 
HETATM 7064 O O   . HOH K 5 .   ? 35.414  -30.081 2.910   1.00 53.20 ?  406 HOH E O   1 
HETATM 7065 O O   . HOH K 5 .   ? 45.688  -31.482 -6.638  1.00 41.21 ?  407 HOH E O   1 
HETATM 7066 O O   . HOH K 5 .   ? 36.792  -28.365 -15.278 1.00 38.73 ?  408 HOH E O   1 
HETATM 7067 O O   . HOH K 5 .   ? 38.937  -35.077 0.112   1.00 46.53 ?  409 HOH E O   1 
HETATM 7068 O O   . HOH K 5 .   ? 39.356  -13.042 -29.932 1.00 27.63 ?  410 HOH E O   1 
HETATM 7069 O O   . HOH K 5 .   ? 40.370  -6.827  -29.544 1.00 28.55 ?  411 HOH E O   1 
HETATM 7070 O O   . HOH K 5 .   ? 36.554  -2.727  -40.716 1.00 26.90 ?  412 HOH E O   1 
HETATM 7071 O O   . HOH K 5 .   ? 47.110  -3.916  -36.387 1.00 40.16 ?  413 HOH E O   1 
HETATM 7072 O O   . HOH K 5 .   ? 45.854  -4.349  -49.633 1.00 42.26 ?  414 HOH E O   1 
HETATM 7073 O O   . HOH K 5 .   ? 34.492  -39.613 -10.694 1.00 46.27 ?  415 HOH E O   1 
HETATM 7074 O O   . HOH K 5 .   ? 32.849  5.757   -41.353 1.00 37.01 ?  416 HOH E O   1 
HETATM 7075 O O   . HOH K 5 .   ? 45.348  -18.450 -50.816 1.00 38.60 ?  417 HOH E O   1 
HETATM 7076 O O   . HOH K 5 .   ? 29.454  -15.985 -30.489 1.00 33.41 ?  418 HOH E O   1 
HETATM 7077 O O   . HOH K 5 .   ? 30.091  -7.310  -14.792 1.00 39.77 ?  419 HOH E O   1 
HETATM 7078 O O   . HOH K 5 .   ? 38.303  -8.502  -47.491 1.00 27.03 ?  420 HOH E O   1 
HETATM 7079 O O   . HOH K 5 .   ? 24.851  -7.736  -24.312 1.00 37.12 ?  421 HOH E O   1 
HETATM 7080 O O   . HOH K 5 .   ? 47.175  -9.992  -54.052 1.00 37.83 ?  422 HOH E O   1 
HETATM 7081 O O   . HOH K 5 .   ? 35.766  4.863   -42.497 1.00 35.89 ?  423 HOH E O   1 
HETATM 7082 O O   . HOH K 5 .   ? 35.511  -19.054 -32.757 1.00 41.80 ?  424 HOH E O   1 
HETATM 7083 O O   . HOH K 5 .   ? 35.262  -3.740  -16.242 1.00 42.27 ?  425 HOH E O   1 
HETATM 7084 O O   . HOH K 5 .   ? 23.365  -0.359  -47.339 1.00 27.69 ?  426 HOH E O   1 
HETATM 7085 O O   . HOH K 5 .   ? 31.172  -2.178  -54.153 1.00 29.79 ?  427 HOH E O   1 
HETATM 7086 O O   . HOH K 5 .   ? 32.120  -20.360 -43.846 1.00 23.28 ?  428 HOH E O   1 
HETATM 7087 O O   . HOH K 5 .   ? 22.300  -11.128 -23.882 1.00 42.84 ?  429 HOH E O   1 
HETATM 7088 O O   . HOH K 5 .   ? 40.644  -17.526 -37.713 1.00 39.09 ?  430 HOH E O   1 
HETATM 7089 O O   . HOH K 5 .   ? 22.916  -10.322 -30.747 1.00 29.64 ?  431 HOH E O   1 
HETATM 7090 O O   . HOH K 5 .   ? 23.618  2.019   -30.667 1.00 42.90 ?  432 HOH E O   1 
HETATM 7091 O O   . HOH K 5 .   ? 43.994  -9.273  -35.481 1.00 24.97 ?  433 HOH E O   1 
HETATM 7092 O O   . HOH K 5 .   ? 28.335  -10.774 -5.367  1.00 48.84 ?  434 HOH E O   1 
HETATM 7093 O O   . HOH K 5 .   ? 45.089  -13.406 -55.057 1.00 42.41 ?  435 HOH E O   1 
HETATM 7094 O O   . HOH K 5 .   ? 48.713  -20.985 -4.827  1.00 41.01 ?  436 HOH E O   1 
HETATM 7095 O O   . HOH K 5 .   ? 19.769  -12.933 -35.684 1.00 30.08 ?  437 HOH E O   1 
HETATM 7096 O O   . HOH K 5 .   ? 23.475  8.841   -40.385 1.00 30.74 ?  438 HOH E O   1 
HETATM 7097 O O   . HOH K 5 .   ? 23.609  -17.302 -29.173 1.00 40.23 ?  439 HOH E O   1 
HETATM 7098 O O   . HOH K 5 .   ? 23.362  -0.798  -21.761 1.00 52.49 ?  440 HOH E O   1 
HETATM 7099 O O   . HOH K 5 .   ? 40.738  -21.514 -45.103 1.00 39.41 ?  441 HOH E O   1 
HETATM 7100 O O   . HOH K 5 .   ? 33.291  -17.961 -31.581 1.00 41.93 ?  442 HOH E O   1 
HETATM 7101 O O   . HOH K 5 .   ? 45.520  -23.012 -44.095 1.00 25.83 ?  443 HOH E O   1 
HETATM 7102 O O   . HOH K 5 .   ? 28.444  -37.573 -13.818 1.00 47.83 ?  444 HOH E O   1 
HETATM 7103 O O   . HOH K 5 .   ? 33.928  6.254   -26.126 1.00 42.62 ?  445 HOH E O   1 
HETATM 7104 O O   . HOH K 5 .   ? 48.341  -13.621 -47.941 1.00 24.91 ?  446 HOH E O   1 
HETATM 7105 O O   . HOH K 5 .   ? 40.717  -32.517 -13.591 1.00 40.26 ?  447 HOH E O   1 
HETATM 7106 O O   . HOH K 5 .   ? 31.090  -0.447  -52.161 1.00 28.57 ?  448 HOH E O   1 
HETATM 7107 O O   . HOH K 5 .   ? 39.172  -39.799 -14.001 1.00 45.86 ?  449 HOH E O   1 
HETATM 7108 O O   . HOH K 5 .   ? 45.127  -6.252  -51.496 1.00 29.87 ?  450 HOH E O   1 
HETATM 7109 O O   . HOH K 5 .   ? 45.936  -13.441 -40.742 1.00 31.11 ?  451 HOH E O   1 
HETATM 7110 O O   . HOH K 5 .   ? 43.912  -13.020 -30.898 1.00 41.18 ?  452 HOH E O   1 
HETATM 7111 O O   . HOH K 5 .   ? 35.650  -19.319 -41.973 1.00 30.55 ?  453 HOH E O   1 
HETATM 7112 O O   . HOH K 5 .   ? 33.093  -13.128 -49.909 1.00 25.68 ?  454 HOH E O   1 
HETATM 7113 O O   . HOH K 5 .   ? 36.004  -19.010 -38.307 1.00 35.18 ?  455 HOH E O   1 
HETATM 7114 O O   . HOH K 5 .   ? 33.946  -4.570  -8.772  1.00 48.73 ?  456 HOH E O   1 
HETATM 7115 O O   . HOH K 5 .   ? 45.094  -8.984  -29.383 1.00 34.68 ?  457 HOH E O   1 
HETATM 7116 O O   . HOH K 5 .   ? 39.553  3.031   -44.193 1.00 29.52 ?  458 HOH E O   1 
HETATM 7117 O O   . HOH K 5 .   ? 48.203  -5.269  -38.514 1.00 37.00 ?  459 HOH E O   1 
HETATM 7118 O O   . HOH K 5 .   ? 31.132  9.034   -30.760 1.00 49.75 ?  460 HOH E O   1 
HETATM 7119 O O   . HOH K 5 .   ? 28.999  -17.774 -18.706 1.00 40.76 ?  461 HOH E O   1 
HETATM 7120 O O   . HOH K 5 .   ? 33.887  -6.527  -53.365 1.00 26.37 ?  462 HOH E O   1 
HETATM 7121 O O   . HOH K 5 .   ? 25.205  -1.892  -54.625 1.00 30.00 ?  463 HOH E O   1 
HETATM 7122 O O   . HOH K 5 .   ? 22.562  -7.566  -53.771 1.00 27.99 ?  464 HOH E O   1 
HETATM 7123 O O   . HOH K 5 .   ? 37.999  -12.867 -27.535 1.00 30.89 ?  465 HOH E O   1 
HETATM 7124 O O   . HOH K 5 .   ? 41.614  -13.412 -26.331 1.00 35.49 ?  466 HOH E O   1 
HETATM 7125 O O   . HOH K 5 .   ? 25.695  -16.873 -27.441 1.00 43.63 ?  467 HOH E O   1 
HETATM 7126 O O   . HOH K 5 .   ? 21.083  -8.375  -38.677 1.00 28.47 ?  468 HOH E O   1 
HETATM 7127 O O   . HOH K 5 .   ? 38.856  -18.735 -0.766  1.00 46.32 ?  469 HOH E O   1 
HETATM 7128 O O   . HOH K 5 .   ? 38.120  1.793   -37.242 1.00 32.48 ?  470 HOH E O   1 
HETATM 7129 O O   . HOH K 5 .   ? 43.670  -33.924 -17.214 1.00 52.76 ?  471 HOH E O   1 
HETATM 7130 O O   . HOH K 5 .   ? 37.600  -25.345 -16.259 1.00 38.20 ?  472 HOH E O   1 
HETATM 7131 O O   . HOH K 5 .   ? 33.031  5.895   -45.431 1.00 39.82 ?  473 HOH E O   1 
HETATM 7132 O O   . HOH K 5 .   ? 32.868  -29.610 -17.421 1.00 40.72 ?  474 HOH E O   1 
HETATM 7133 O O   . HOH K 5 .   ? 45.952  -23.531 -2.113  1.00 46.62 ?  475 HOH E O   1 
HETATM 7134 O O   . HOH K 5 .   ? 44.319  1.963   -46.389 1.00 39.89 ?  476 HOH E O   1 
HETATM 7135 O O   . HOH K 5 .   ? 30.293  -15.400 -0.081  1.00 45.08 ?  477 HOH E O   1 
HETATM 7136 O O   . HOH K 5 .   ? 37.888  0.755   -19.901 1.00 35.93 ?  478 HOH E O   1 
HETATM 7137 O O   . HOH K 5 .   ? 40.627  -1.253  -27.689 1.00 42.61 ?  479 HOH E O   1 
HETATM 7138 O O   . HOH K 5 .   ? 23.670  -1.577  -28.488 1.00 42.98 ?  480 HOH E O   1 
HETATM 7139 O O   . HOH K 5 .   ? 46.349  -8.314  -50.469 1.00 31.90 ?  481 HOH E O   1 
HETATM 7140 O O   . HOH K 5 .   ? 25.675  0.604   -19.138 1.00 47.24 ?  482 HOH E O   1 
HETATM 7141 O O   . HOH K 5 .   ? 28.366  -3.007  -15.168 1.00 50.30 ?  483 HOH E O   1 
HETATM 7142 O O   . HOH K 5 .   ? 28.356  -14.567 -27.866 1.00 40.67 ?  484 HOH E O   1 
HETATM 7143 O O   . HOH K 5 .   ? 34.343  -11.088 -18.265 1.00 30.00 ?  485 HOH E O   1 
HETATM 7144 O O   . HOH K 5 .   ? 31.839  2.803   -56.015 1.00 48.70 ?  486 HOH E O   1 
HETATM 7145 O O   . HOH K 5 .   ? 38.731  -11.846 -2.946  1.00 49.95 ?  487 HOH E O   1 
HETATM 7146 O O   . HOH K 5 .   ? 40.990  -15.191 -29.818 1.00 37.66 ?  488 HOH E O   1 
HETATM 7147 O O   . HOH K 5 .   ? 43.699  -19.064 -38.206 1.00 46.69 ?  489 HOH E O   1 
HETATM 7148 O O   . HOH K 5 .   ? 46.071  -10.168 -33.779 1.00 32.70 ?  490 HOH E O   1 
HETATM 7149 O O   . HOH K 5 .   ? 39.407  3.505   -35.656 1.00 46.00 ?  491 HOH E O   1 
HETATM 7150 O O   . HOH K 5 .   ? 37.750  -2.587  -17.077 1.00 48.54 ?  492 HOH E O   1 
HETATM 7151 O O   . HOH K 5 .   ? 36.012  -11.947 -20.394 1.00 30.00 ?  493 HOH E O   1 
HETATM 7152 O O   . HOH K 5 .   ? 45.744  -18.131 -39.040 1.00 40.53 ?  494 HOH E O   1 
HETATM 7153 O O   . HOH K 5 .   ? 45.953  -11.271 -29.224 1.00 52.30 ?  495 HOH E O   1 
HETATM 7154 O O   . HOH K 5 .   ? 28.348  0.644   -52.497 1.00 39.96 ?  496 HOH E O   1 
HETATM 7155 O O   . HOH K 5 .   ? 27.931  -5.731  -14.949 1.00 48.52 ?  497 HOH E O   1 
HETATM 7156 O O   . HOH K 5 .   ? 43.864  -24.869 -44.992 1.00 44.22 ?  498 HOH E O   1 
HETATM 7157 O O   . HOH K 5 .   ? 46.198  -8.198  -31.682 1.00 40.54 ?  499 HOH E O   1 
HETATM 7158 O O   . HOH K 5 .   ? 29.381  -14.638 -25.485 1.00 47.20 ?  500 HOH E O   1 
HETATM 7159 O O   . HOH K 5 .   ? 38.171  -15.043 -26.130 1.00 47.63 ?  501 HOH E O   1 
HETATM 7160 O O   . HOH K 5 .   ? 29.474  -1.003  -55.883 1.00 30.00 ?  502 HOH E O   1 
HETATM 7161 O O   . HOH L 5 .   ? 18.133  -3.524  -41.928 1.00 35.55 ?  301 HOH F O   1 
HETATM 7162 O O   . HOH L 5 .   ? 13.850  -23.922 -13.116 1.00 44.26 ?  302 HOH F O   1 
HETATM 7163 O O   . HOH L 5 .   ? 14.459  -18.290 -5.854  1.00 49.09 ?  303 HOH F O   1 
HETATM 7164 O O   . HOH L 5 .   ? 16.030  -29.796 -50.896 1.00 33.06 ?  304 HOH F O   1 
HETATM 7165 O O   . HOH L 5 .   ? 11.402  -35.509 -36.616 1.00 34.50 ?  305 HOH F O   1 
HETATM 7166 O O   . HOH L 5 .   ? 23.007  -25.861 -22.239 1.00 48.89 ?  306 HOH F O   1 
HETATM 7167 O O   . HOH L 5 .   ? 23.571  -18.902 -32.196 1.00 29.31 ?  307 HOH F O   1 
HETATM 7168 O O   . HOH L 5 .   ? 24.460  -38.931 -11.501 1.00 44.38 ?  308 HOH F O   1 
HETATM 7169 O O   . HOH L 5 .   ? 19.855  -32.632 -27.818 1.00 38.48 ?  309 HOH F O   1 
HETATM 7170 O O   . HOH L 5 .   ? 26.989  -23.186 -10.605 1.00 39.87 ?  310 HOH F O   1 
HETATM 7171 O O   . HOH L 5 .   ? 14.648  -28.106 -49.086 1.00 30.74 ?  311 HOH F O   1 
HETATM 7172 O O   . HOH L 5 .   ? 18.800  -13.132 2.601   1.00 48.76 ?  312 HOH F O   1 
HETATM 7173 O O   . HOH L 5 .   ? 19.103  -0.685  -48.111 1.00 25.19 ?  313 HOH F O   1 
HETATM 7174 O O   . HOH L 5 .   ? 20.993  -11.410 -54.471 1.00 32.71 ?  314 HOH F O   1 
HETATM 7175 O O   . HOH L 5 .   ? 14.557  -42.505 -36.346 1.00 36.30 ?  315 HOH F O   1 
HETATM 7176 O O   . HOH L 5 .   ? 15.725  -3.433  -48.333 1.00 28.62 ?  316 HOH F O   1 
HETATM 7177 O O   . HOH L 5 .   ? 11.674  -32.274 -19.090 1.00 37.07 ?  317 HOH F O   1 
HETATM 7178 O O   . HOH L 5 .   ? 7.845   -6.679  -47.604 1.00 41.05 ?  318 HOH F O   1 
HETATM 7179 O O   . HOH L 5 .   ? 10.359  -23.685 -49.594 1.00 36.77 ?  319 HOH F O   1 
HETATM 7180 O O   . HOH L 5 .   ? 13.402  -14.436 -38.639 1.00 23.90 ?  320 HOH F O   1 
HETATM 7181 O O   . HOH L 5 .   ? 7.300   -18.592 -43.304 1.00 28.36 ?  321 HOH F O   1 
HETATM 7182 O O   . HOH L 5 .   ? 12.767  -27.406 -30.552 1.00 36.45 ?  322 HOH F O   1 
HETATM 7183 O O   . HOH L 5 .   ? 26.721  -24.732 -0.669  1.00 41.85 ?  323 HOH F O   1 
HETATM 7184 O O   . HOH L 5 .   ? 27.427  -19.693 -58.394 1.00 46.21 ?  324 HOH F O   1 
HETATM 7185 O O   . HOH L 5 .   ? 7.050   -13.471 -47.694 1.00 39.52 ?  325 HOH F O   1 
HETATM 7186 O O   . HOH L 5 .   ? 18.495  -32.653 -47.813 1.00 29.13 ?  326 HOH F O   1 
HETATM 7187 O O   . HOH L 5 .   ? 23.868  -22.166 -9.804  1.00 40.40 ?  327 HOH F O   1 
HETATM 7188 O O   . HOH L 5 .   ? 9.416   -12.076 -43.592 1.00 30.35 ?  328 HOH F O   1 
HETATM 7189 O O   . HOH L 5 .   ? 16.460  -16.866 -53.419 1.00 33.92 ?  329 HOH F O   1 
HETATM 7190 O O   . HOH L 5 .   ? 26.383  -29.970 -32.618 1.00 39.40 ?  330 HOH F O   1 
HETATM 7191 O O   . HOH L 5 .   ? 25.502  -35.008 -17.692 1.00 37.12 ?  331 HOH F O   1 
HETATM 7192 O O   . HOH L 5 .   ? 26.557  -30.577 -39.383 1.00 29.49 ?  332 HOH F O   1 
HETATM 7193 O O   . HOH L 5 .   ? 28.861  -27.789 1.385   1.00 42.96 ?  333 HOH F O   1 
HETATM 7194 O O   . HOH L 5 .   ? 31.788  -22.741 -45.631 1.00 28.07 ?  334 HOH F O   1 
HETATM 7195 O O   . HOH L 5 .   ? 11.308  -26.286 2.780   1.00 36.11 ?  335 HOH F O   1 
HETATM 7196 O O   . HOH L 5 .   ? 15.156  -26.349 -30.694 1.00 30.85 ?  336 HOH F O   1 
HETATM 7197 O O   . HOH L 5 .   ? 4.130   -24.115 -52.418 1.00 42.00 ?  337 HOH F O   1 
HETATM 7198 O O   . HOH L 5 .   ? 14.527  -35.946 -46.556 1.00 36.77 ?  338 HOH F O   1 
HETATM 7199 O O   . HOH L 5 .   ? 11.415  -31.982 -37.668 1.00 35.31 ?  339 HOH F O   1 
HETATM 7200 O O   . HOH L 5 .   ? 9.559   -19.296 -41.926 1.00 22.49 ?  340 HOH F O   1 
HETATM 7201 O O   . HOH L 5 .   ? 17.836  -24.478 15.367  1.00 58.95 ?  341 HOH F O   1 
HETATM 7202 O O   . HOH L 5 .   ? 9.972   -9.622  -46.325 1.00 39.66 ?  342 HOH F O   1 
HETATM 7203 O O   . HOH L 5 .   ? 14.101  -37.143 -24.999 1.00 31.46 ?  343 HOH F O   1 
HETATM 7204 O O   . HOH L 5 .   ? 5.063   -20.915 -0.693  1.00 46.52 ?  344 HOH F O   1 
HETATM 7205 O O   . HOH L 5 .   ? 10.219  -15.948 -36.194 1.00 39.62 ?  345 HOH F O   1 
HETATM 7206 O O   . HOH L 5 .   ? 8.585   -34.224 -3.965  1.00 41.27 ?  346 HOH F O   1 
HETATM 7207 O O   . HOH L 5 .   ? 9.548   -22.486 -33.460 1.00 38.38 ?  347 HOH F O   1 
HETATM 7208 O O   . HOH L 5 .   ? 28.632  -36.519 -42.361 1.00 45.99 ?  348 HOH F O   1 
HETATM 7209 O O   . HOH L 5 .   ? 18.744  -26.791 -54.828 1.00 46.91 ?  349 HOH F O   1 
HETATM 7210 O O   . HOH L 5 .   ? 10.100  -28.000 -9.637  1.00 42.23 ?  350 HOH F O   1 
HETATM 7211 O O   . HOH L 5 .   ? 10.065  -28.826 2.096   1.00 45.24 ?  351 HOH F O   1 
HETATM 7212 O O   . HOH L 5 .   ? 19.988  -33.981 -49.574 1.00 39.61 ?  352 HOH F O   1 
HETATM 7213 O O   . HOH L 5 .   ? 9.577   -7.084  -45.053 1.00 33.32 ?  353 HOH F O   1 
HETATM 7214 O O   . HOH L 5 .   ? 29.036  -26.511 -20.236 1.00 49.65 ?  354 HOH F O   1 
HETATM 7215 O O   . HOH L 5 .   ? 28.121  -35.996 -47.914 1.00 39.12 ?  355 HOH F O   1 
HETATM 7216 O O   . HOH L 5 .   ? 34.611  -21.872 -34.993 1.00 38.37 ?  356 HOH F O   1 
HETATM 7217 O O   . HOH L 5 .   ? 29.799  -23.629 -36.085 1.00 25.28 ?  357 HOH F O   1 
HETATM 7218 O O   . HOH L 5 .   ? 28.805  -28.647 -41.040 1.00 42.89 ?  358 HOH F O   1 
HETATM 7219 O O   . HOH L 5 .   ? 10.691  -24.525 -40.454 1.00 25.44 ?  359 HOH F O   1 
HETATM 7220 O O   . HOH L 5 .   ? 13.777  -14.709 6.511   1.00 52.97 ?  360 HOH F O   1 
HETATM 7221 O O   . HOH L 5 .   ? 27.328  -26.091 7.445   1.00 50.99 ?  361 HOH F O   1 
HETATM 7222 O O   . HOH L 5 .   ? 20.640  -27.396 -52.379 1.00 34.01 ?  362 HOH F O   1 
HETATM 7223 O O   . HOH L 5 .   ? 24.626  -25.110 8.322   1.00 48.84 ?  363 HOH F O   1 
HETATM 7224 O O   . HOH L 5 .   ? 16.933  -30.995 -24.931 1.00 35.93 ?  364 HOH F O   1 
HETATM 7225 O O   . HOH L 5 .   ? 19.067  -8.216  -39.930 1.00 33.18 ?  365 HOH F O   1 
HETATM 7226 O O   . HOH L 5 .   ? 15.567  -38.623 -43.182 1.00 31.88 ?  366 HOH F O   1 
HETATM 7227 O O   . HOH L 5 .   ? 5.343   -19.137 -49.517 1.00 48.40 ?  367 HOH F O   1 
HETATM 7228 O O   . HOH L 5 .   ? 37.280  -29.365 -52.753 1.00 58.86 ?  368 HOH F O   1 
HETATM 7229 O O   . HOH L 5 .   ? 19.384  -17.961 -13.565 1.00 49.61 ?  369 HOH F O   1 
HETATM 7230 O O   . HOH L 5 .   ? 19.522  -32.921 7.491   1.00 47.15 ?  370 HOH F O   1 
HETATM 7231 O O   . HOH L 5 .   ? 15.500  -9.025  -46.709 1.00 38.77 ?  371 HOH F O   1 
HETATM 7232 O O   . HOH L 5 .   ? 16.549  -26.090 -18.206 1.00 44.54 ?  372 HOH F O   1 
HETATM 7233 O O   . HOH L 5 .   ? 25.735  0.468   -52.564 1.00 46.21 ?  373 HOH F O   1 
HETATM 7234 O O   . HOH L 5 .   ? 8.309   -34.057 -12.978 1.00 39.93 ?  374 HOH F O   1 
HETATM 7235 O O   . HOH L 5 .   ? 10.281  -11.869 -38.801 1.00 41.69 ?  375 HOH F O   1 
HETATM 7236 O O   . HOH L 5 .   ? 8.604   -26.059 -46.249 1.00 33.65 ?  376 HOH F O   1 
HETATM 7237 O O   . HOH L 5 .   ? 12.759  -20.991 -6.512  1.00 42.42 ?  377 HOH F O   1 
HETATM 7238 O O   . HOH L 5 .   ? 25.640  -27.450 -54.851 1.00 40.07 ?  378 HOH F O   1 
HETATM 7239 O O   . HOH L 5 .   ? 16.182  -35.483 0.906   1.00 40.46 ?  379 HOH F O   1 
HETATM 7240 O O   . HOH L 5 .   ? 11.716  -31.439 -24.847 1.00 47.98 ?  380 HOH F O   1 
HETATM 7241 O O   . HOH L 5 .   ? 32.331  -29.649 -34.353 1.00 51.77 ?  381 HOH F O   1 
HETATM 7242 O O   . HOH L 5 .   ? 13.039  -29.388 -27.843 1.00 49.12 ?  382 HOH F O   1 
HETATM 7243 O O   . HOH L 5 .   ? 14.943  -22.425 12.373  1.00 47.07 ?  383 HOH F O   1 
HETATM 7244 O O   . HOH L 5 .   ? 10.133  -26.142 -51.365 1.00 46.93 ?  384 HOH F O   1 
HETATM 7245 O O   . HOH L 5 .   ? 10.979  -9.648  -54.732 1.00 48.56 ?  385 HOH F O   1 
HETATM 7246 O O   . HOH L 5 .   ? 9.620   -26.657 -53.653 1.00 50.60 ?  386 HOH F O   1 
HETATM 7247 O O   . HOH L 5 .   ? 10.639  -17.520 3.139   1.00 49.02 ?  387 HOH F O   1 
HETATM 7248 O O   . HOH L 5 .   ? 33.742  -22.299 -37.238 1.00 37.12 ?  388 HOH F O   1 
HETATM 7249 O O   . HOH L 5 .   ? 22.187  2.254   -54.116 1.00 40.24 ?  389 HOH F O   1 
HETATM 7250 O O   . HOH L 5 .   ? 26.640  -37.461 -16.546 1.00 47.09 ?  390 HOH F O   1 
HETATM 7251 O O   . HOH L 5 .   ? 32.838  -25.393 -45.833 1.00 44.64 ?  391 HOH F O   1 
HETATM 7252 O O   . HOH L 5 .   ? 11.792  -20.372 -8.623  1.00 54.48 ?  392 HOH F O   1 
HETATM 7253 O O   . HOH L 5 .   ? 7.431   -13.700 -45.185 1.00 40.62 ?  393 HOH F O   1 
HETATM 7254 O O   . HOH L 5 .   ? 28.365  -31.171 -32.708 1.00 44.37 ?  394 HOH F O   1 
HETATM 7255 O O   . HOH L 5 .   ? 16.558  -7.059  -47.911 1.00 42.39 ?  395 HOH F O   1 
HETATM 7256 O O   . HOH L 5 .   ? 15.153  -38.509 -47.418 1.00 43.06 ?  396 HOH F O   1 
HETATM 7257 O O   . HOH L 5 .   ? 11.301  -13.549 -36.903 1.00 39.63 ?  397 HOH F O   1 
HETATM 7258 O O   . HOH L 5 .   ? 24.246  -23.754 10.584  1.00 52.50 ?  398 HOH F O   1 
HETATM 7259 O O   . HOH M 5 .   ? 13.079  14.546  -7.693  1.00 47.66 ?  301 HOH D O   1 
HETATM 7260 O O   . HOH M 5 .   ? -8.212  16.499  -46.104 1.00 23.56 ?  302 HOH D O   1 
HETATM 7261 O O   . HOH M 5 .   ? -3.915  1.112   -25.937 1.00 43.63 ?  303 HOH D O   1 
HETATM 7262 O O   . HOH M 5 .   ? -6.389  17.486  -51.219 1.00 40.69 ?  304 HOH D O   1 
HETATM 7263 O O   . HOH M 5 .   ? 14.484  7.848   -7.501  1.00 58.59 ?  305 HOH D O   1 
HETATM 7264 O O   . HOH M 5 .   ? -9.326  0.106   -40.055 1.00 35.89 ?  306 HOH D O   1 
HETATM 7265 O O   . HOH M 5 .   ? 13.255  6.480   -24.899 1.00 38.61 ?  307 HOH D O   1 
HETATM 7266 O O   . HOH M 5 .   ? 5.487   -7.034  -41.559 1.00 35.81 ?  308 HOH D O   1 
HETATM 7267 O O   . HOH M 5 .   ? 8.712   14.617  -30.817 1.00 34.72 ?  309 HOH D O   1 
HETATM 7268 O O   . HOH M 5 .   ? -6.699  12.150  -55.678 1.00 38.23 ?  310 HOH D O   1 
HETATM 7269 O O   . HOH M 5 .   ? 15.230  10.675  -53.108 1.00 25.44 ?  311 HOH D O   1 
HETATM 7270 O O   . HOH M 5 .   ? 1.605   32.597  0.842   1.00 49.78 ?  312 HOH D O   1 
HETATM 7271 O O   . HOH M 5 .   ? 4.301   -7.738  -26.493 1.00 40.70 ?  313 HOH D O   1 
HETATM 7272 O O   . HOH M 5 .   ? 1.545   1.495   -41.216 1.00 27.45 ?  314 HOH D O   1 
HETATM 7273 O O   . HOH M 5 .   ? -2.329  5.466   -29.985 1.00 29.94 ?  315 HOH D O   1 
HETATM 7274 O O   . HOH M 5 .   ? 19.757  -5.475  -41.169 1.00 32.52 ?  316 HOH D O   1 
HETATM 7275 O O   . HOH M 5 .   ? 5.227   37.420  -9.856  1.00 44.45 ?  317 HOH D O   1 
HETATM 7276 O O   . HOH M 5 .   ? -1.419  30.616  -12.677 1.00 41.47 ?  318 HOH D O   1 
HETATM 7277 O O   . HOH M 5 .   ? -8.153  24.405  -1.858  1.00 46.91 ?  319 HOH D O   1 
HETATM 7278 O O   . HOH M 5 .   ? -5.899  7.942   -35.963 1.00 25.85 ?  320 HOH D O   1 
HETATM 7279 O O   . HOH M 5 .   ? -2.685  16.242  -38.087 1.00 36.72 ?  321 HOH D O   1 
HETATM 7280 O O   . HOH M 5 .   ? -1.437  11.633  -30.412 1.00 29.39 ?  322 HOH D O   1 
HETATM 7281 O O   . HOH M 5 .   ? -7.682  12.145  -41.201 1.00 33.73 ?  323 HOH D O   1 
HETATM 7282 O O   . HOH M 5 .   ? -8.083  7.278   -50.990 1.00 30.96 ?  324 HOH D O   1 
HETATM 7283 O O   . HOH M 5 .   ? 10.135  5.220   -19.644 1.00 50.96 ?  325 HOH D O   1 
HETATM 7284 O O   . HOH M 5 .   ? 14.254  16.132  -29.551 1.00 39.70 ?  326 HOH D O   1 
HETATM 7285 O O   . HOH M 5 .   ? -0.734  4.822   -48.161 1.00 31.95 ?  327 HOH D O   1 
HETATM 7286 O O   . HOH M 5 .   ? 14.745  -0.828  -47.563 1.00 28.12 ?  328 HOH D O   1 
HETATM 7287 O O   . HOH M 5 .   ? -0.075  7.255   -47.834 1.00 26.67 ?  329 HOH D O   1 
HETATM 7288 O O   . HOH M 5 .   ? 11.156  44.036  -2.849  1.00 39.12 ?  330 HOH D O   1 
HETATM 7289 O O   . HOH M 5 .   ? -1.159  -4.382  -29.748 1.00 46.49 ?  331 HOH D O   1 
HETATM 7290 O O   . HOH M 5 .   ? 6.105   19.244  -44.351 1.00 26.74 ?  332 HOH D O   1 
HETATM 7291 O O   . HOH M 5 .   ? 7.127   0.893   -54.640 1.00 30.00 ?  333 HOH D O   1 
HETATM 7292 O O   . HOH M 5 .   ? 2.623   17.877  -33.131 1.00 39.52 ?  334 HOH D O   1 
HETATM 7293 O O   . HOH M 5 .   ? -5.735  29.336  -5.326  1.00 45.84 ?  335 HOH D O   1 
HETATM 7294 O O   . HOH M 5 .   ? -10.070 12.481  -48.332 1.00 25.22 ?  336 HOH D O   1 
HETATM 7295 O O   . HOH M 5 .   ? 8.332   14.625  -19.473 1.00 53.81 ?  337 HOH D O   1 
HETATM 7296 O O   . HOH M 5 .   ? 5.117   11.835  -50.333 1.00 25.42 ?  338 HOH D O   1 
HETATM 7297 O O   . HOH M 5 .   ? -7.952  3.059   -50.430 1.00 37.75 ?  339 HOH D O   1 
HETATM 7298 O O   . HOH M 5 .   ? 2.500   17.964  -42.456 1.00 28.71 ?  340 HOH D O   1 
HETATM 7299 O O   . HOH M 5 .   ? 14.746  -10.143 -40.469 1.00 25.79 ?  341 HOH D O   1 
HETATM 7300 O O   . HOH M 5 .   ? 3.106   2.021   -16.875 1.00 43.75 ?  342 HOH D O   1 
HETATM 7301 O O   . HOH M 5 .   ? 12.403  19.752  -9.394  1.00 48.17 ?  343 HOH D O   1 
HETATM 7302 O O   . HOH M 5 .   ? 4.300   5.180   -53.714 1.00 25.94 ?  344 HOH D O   1 
HETATM 7303 O O   . HOH M 5 .   ? 15.217  9.194   -30.953 1.00 27.73 ?  345 HOH D O   1 
HETATM 7304 O O   . HOH M 5 .   ? 12.993  0.334   -54.291 1.00 39.86 ?  346 HOH D O   1 
HETATM 7305 O O   . HOH M 5 .   ? 0.795   1.238   -17.147 1.00 46.45 ?  347 HOH D O   1 
HETATM 7306 O O   . HOH M 5 .   ? 7.181   -0.694  -52.571 1.00 30.00 ?  348 HOH D O   1 
HETATM 7307 O O   . HOH M 5 .   ? 0.772   23.751  -16.187 1.00 44.20 ?  349 HOH D O   1 
HETATM 7308 O O   . HOH M 5 .   ? -6.988  7.599   -29.682 1.00 35.40 ?  350 HOH D O   1 
HETATM 7309 O O   . HOH M 5 .   ? -4.382  -3.982  -39.350 1.00 43.09 ?  351 HOH D O   1 
HETATM 7310 O O   . HOH M 5 .   ? 0.241   37.962  -12.947 1.00 46.03 ?  352 HOH D O   1 
HETATM 7311 O O   . HOH M 5 .   ? 0.142   11.581  -27.903 1.00 31.09 ?  353 HOH D O   1 
HETATM 7312 O O   . HOH M 5 .   ? 1.962   17.906  -38.656 1.00 36.42 ?  354 HOH D O   1 
HETATM 7313 O O   . HOH M 5 .   ? 3.634   34.892  1.251   1.00 56.08 ?  355 HOH D O   1 
HETATM 7314 O O   . HOH M 5 .   ? -10.046 4.086   -39.081 1.00 35.52 ?  356 HOH D O   1 
HETATM 7315 O O   . HOH M 5 .   ? -6.328  27.107  -12.602 1.00 47.25 ?  357 HOH D O   1 
HETATM 7316 O O   . HOH M 5 .   ? 1.062   16.549  -0.877  1.00 48.91 ?  358 HOH D O   1 
HETATM 7317 O O   . HOH M 5 .   ? -6.127  -3.159  -46.723 1.00 41.71 ?  359 HOH D O   1 
HETATM 7318 O O   . HOH M 5 .   ? 15.735  6.270   -53.980 1.00 27.31 ?  360 HOH D O   1 
HETATM 7319 O O   . HOH M 5 .   ? -2.473  3.351   -23.142 1.00 38.41 ?  361 HOH D O   1 
HETATM 7320 O O   . HOH M 5 .   ? -6.936  4.931   -52.040 1.00 28.21 ?  362 HOH D O   1 
HETATM 7321 O O   . HOH M 5 .   ? 10.656  21.354  -1.023  1.00 47.88 ?  363 HOH D O   1 
HETATM 7322 O O   . HOH M 5 .   ? 17.077  7.255   -39.042 1.00 27.56 ?  364 HOH D O   1 
HETATM 7323 O O   . HOH M 5 .   ? -0.215  -3.044  -37.615 1.00 33.40 ?  365 HOH D O   1 
HETATM 7324 O O   . HOH M 5 .   ? 14.377  0.272   -28.903 1.00 42.81 ?  366 HOH D O   1 
HETATM 7325 O O   . HOH M 5 .   ? 12.187  15.561  -27.987 1.00 45.04 ?  367 HOH D O   1 
HETATM 7326 O O   . HOH M 5 .   ? 0.433   -2.228  -20.513 1.00 38.23 ?  368 HOH D O   1 
HETATM 7327 O O   . HOH M 5 .   ? -3.129  13.960  -30.375 1.00 39.56 ?  369 HOH D O   1 
HETATM 7328 O O   . HOH M 5 .   ? -1.478  -4.275  -44.681 1.00 29.96 ?  370 HOH D O   1 
HETATM 7329 O O   . HOH M 5 .   ? -3.679  12.075  -26.624 1.00 37.55 ?  371 HOH D O   1 
HETATM 7330 O O   . HOH M 5 .   ? 15.035  -0.727  -22.375 1.00 51.08 ?  372 HOH D O   1 
HETATM 7331 O O   . HOH M 5 .   ? -2.428  0.143   -28.107 1.00 38.55 ?  373 HOH D O   1 
HETATM 7332 O O   . HOH M 5 .   ? 8.276   6.751   -18.648 1.00 49.20 ?  374 HOH D O   1 
HETATM 7333 O O   . HOH M 5 .   ? 18.834  8.471   -37.030 1.00 41.73 ?  375 HOH D O   1 
HETATM 7334 O O   . HOH M 5 .   ? 19.270  10.503  -31.732 1.00 45.46 ?  376 HOH D O   1 
HETATM 7335 O O   . HOH M 5 .   ? -1.586  24.614  2.434   1.00 52.78 ?  377 HOH D O   1 
HETATM 7336 O O   . HOH M 5 .   ? 1.889   10.448  -20.705 1.00 47.63 ?  378 HOH D O   1 
HETATM 7337 O O   . HOH M 5 .   ? 4.112   3.245   -8.929  1.00 52.04 ?  379 HOH D O   1 
HETATM 7338 O O   . HOH M 5 .   ? -1.561  -3.105  -22.297 1.00 49.53 ?  380 HOH D O   1 
HETATM 7339 O O   . HOH M 5 .   ? 4.075   9.267   -19.037 1.00 44.34 ?  381 HOH D O   1 
HETATM 7340 O O   . HOH M 5 .   ? -5.662  23.593  -45.203 1.00 43.93 ?  382 HOH D O   1 
HETATM 7341 O O   . HOH M 5 .   ? -7.574  16.836  -39.224 1.00 42.26 ?  383 HOH D O   1 
HETATM 7342 O O   . HOH M 5 .   ? 1.051   13.785  -21.894 1.00 52.90 ?  384 HOH D O   1 
HETATM 7343 O O   . HOH M 5 .   ? -11.778 -0.222  -38.546 1.00 47.75 ?  385 HOH D O   1 
HETATM 7344 O O   . HOH M 5 .   ? 9.856   -1.984  -52.649 1.00 35.05 ?  386 HOH D O   1 
HETATM 7345 O O   . HOH M 5 .   ? 8.774   -0.081  -56.174 1.00 30.00 ?  387 HOH D O   1 
HETATM 7346 O O   . HOH M 5 .   ? 0.935   16.678  -22.388 1.00 57.69 ?  388 HOH D O   1 
HETATM 7347 O O   . HOH N 5 .   ? 14.518  17.950  -32.565 1.00 29.24 ?  401 HOH G O   1 
HETATM 7348 O O   . HOH N 5 .   ? 18.624  29.660  -27.101 1.00 40.99 ?  402 HOH G O   1 
HETATM 7349 O O   . HOH N 5 .   ? 27.110  31.544  -23.213 1.00 46.80 ?  403 HOH G O   1 
HETATM 7350 O O   . HOH N 5 .   ? 23.851  26.677  -49.614 1.00 30.48 ?  404 HOH G O   1 
HETATM 7351 O O   . HOH N 5 .   ? 28.682  10.940  -43.502 1.00 30.26 ?  405 HOH G O   1 
HETATM 7352 O O   . HOH N 5 .   ? 17.145  -0.798  -44.308 1.00 26.21 ?  406 HOH G O   1 
HETATM 7353 O O   . HOH N 5 .   ? 9.089   27.188  -41.086 1.00 45.78 ?  407 HOH G O   1 
HETATM 7354 O O   . HOH N 5 .   ? 17.823  14.591  -7.727  1.00 47.35 ?  408 HOH G O   1 
HETATM 7355 O O   . HOH N 5 .   ? 6.581   21.572  -45.992 1.00 30.23 ?  409 HOH G O   1 
HETATM 7356 O O   . HOH N 5 .   ? 23.758  36.197  -25.930 1.00 29.28 ?  410 HOH G O   1 
HETATM 7357 O O   . HOH N 5 .   ? 21.269  41.312  -35.694 1.00 32.07 ?  411 HOH G O   1 
HETATM 7358 O O   . HOH N 5 .   ? 26.895  30.881  -20.335 1.00 37.23 ?  412 HOH G O   1 
HETATM 7359 O O   . HOH N 5 .   ? 13.243  33.393  -17.683 1.00 36.87 ?  413 HOH G O   1 
HETATM 7360 O O   . HOH N 5 .   ? 23.939  34.629  -47.173 1.00 38.00 ?  414 HOH G O   1 
HETATM 7361 O O   . HOH N 5 .   ? 9.451   29.364  -51.241 1.00 41.89 ?  415 HOH G O   1 
HETATM 7362 O O   . HOH N 5 .   ? 22.320  2.112   -47.994 1.00 28.14 ?  416 HOH G O   1 
HETATM 7363 O O   . HOH N 5 .   ? 26.451  34.331  -37.533 1.00 34.00 ?  417 HOH G O   1 
HETATM 7364 O O   . HOH N 5 .   ? 17.341  10.053  -54.880 1.00 34.54 ?  418 HOH G O   1 
HETATM 7365 O O   . HOH N 5 .   ? 22.442  28.098  -51.260 1.00 34.18 ?  419 HOH G O   1 
HETATM 7366 O O   . HOH N 5 .   ? 13.549  21.819  -1.296  1.00 43.89 ?  420 HOH G O   1 
HETATM 7367 O O   . HOH N 5 .   ? 24.697  13.412  -38.794 1.00 24.94 ?  421 HOH G O   1 
HETATM 7368 O O   . HOH N 5 .   ? 22.801  25.493  -31.164 1.00 32.51 ?  422 HOH G O   1 
HETATM 7369 O O   . HOH N 5 .   ? 21.709  15.410  -53.811 1.00 35.35 ?  423 HOH G O   1 
HETATM 7370 O O   . HOH N 5 .   ? 14.875  36.855  -11.527 1.00 40.14 ?  424 HOH G O   1 
HETATM 7371 O O   . HOH N 5 .   ? 27.968  15.045  -36.551 1.00 42.27 ?  425 HOH G O   1 
HETATM 7372 O O   . HOH N 5 .   ? 9.800   12.810  -1.249  1.00 51.09 ?  426 HOH G O   1 
HETATM 7373 O O   . HOH N 5 .   ? 17.805  31.905  -28.808 1.00 38.15 ?  427 HOH G O   1 
HETATM 7374 O O   . HOH N 5 .   ? 29.028  23.142  0.399   1.00 39.11 ?  428 HOH G O   1 
HETATM 7375 O O   . HOH N 5 .   ? 14.791  12.918  -60.868 1.00 43.57 ?  429 HOH G O   1 
HETATM 7376 O O   . HOH N 5 .   ? 28.552  21.630  -33.908 1.00 37.07 ?  430 HOH G O   1 
HETATM 7377 O O   . HOH N 5 .   ? 18.342  11.906  -35.984 1.00 28.60 ?  431 HOH G O   1 
HETATM 7378 O O   . HOH N 5 .   ? 10.643  19.423  0.337   1.00 45.27 ?  432 HOH G O   1 
HETATM 7379 O O   . HOH N 5 .   ? 22.705  37.114  -44.150 1.00 30.03 ?  433 HOH G O   1 
HETATM 7380 O O   . HOH N 5 .   ? 28.055  22.234  -50.025 1.00 38.78 ?  434 HOH G O   1 
HETATM 7381 O O   . HOH N 5 .   ? 11.473  29.442  -40.151 1.00 26.48 ?  435 HOH G O   1 
HETATM 7382 O O   . HOH N 5 .   ? 29.546  26.111  -11.835 1.00 38.83 ?  436 HOH G O   1 
HETATM 7383 O O   . HOH N 5 .   ? 25.263  21.962  -15.175 1.00 44.49 ?  437 HOH G O   1 
HETATM 7384 O O   . HOH N 5 .   ? 28.562  18.106  -42.224 1.00 22.95 ?  438 HOH G O   1 
HETATM 7385 O O   . HOH N 5 .   ? 21.975  5.041   -53.371 1.00 46.76 ?  439 HOH G O   1 
HETATM 7386 O O   . HOH N 5 .   ? 17.179  35.231  -30.851 1.00 41.74 ?  440 HOH G O   1 
HETATM 7387 O O   . HOH N 5 .   ? 27.484  23.455  -40.923 1.00 24.71 ?  441 HOH G O   1 
HETATM 7388 O O   . HOH N 5 .   ? 11.712  29.288  -33.678 1.00 38.19 ?  442 HOH G O   1 
HETATM 7389 O O   . HOH N 5 .   ? 19.541  16.225  -15.374 1.00 46.04 ?  443 HOH G O   1 
HETATM 7390 O O   . HOH N 5 .   ? 29.064  43.451  -29.672 1.00 40.07 ?  444 HOH G O   1 
HETATM 7391 O O   . HOH N 5 .   ? 15.190  24.358  -23.308 1.00 45.39 ?  445 HOH G O   1 
HETATM 7392 O O   . HOH N 5 .   ? 21.054  -0.525  -43.922 1.00 30.00 ?  446 HOH G O   1 
HETATM 7393 O O   . HOH N 5 .   ? 19.896  31.387  -48.588 1.00 31.58 ?  447 HOH G O   1 
HETATM 7394 O O   . HOH N 5 .   ? 8.552   24.050  -38.417 1.00 35.57 ?  448 HOH G O   1 
HETATM 7395 O O   . HOH N 5 .   ? 16.369  21.575  6.968   1.00 49.21 ?  449 HOH G O   1 
HETATM 7396 O O   . HOH N 5 .   ? 11.463  24.705  1.073   1.00 44.83 ?  450 HOH G O   1 
HETATM 7397 O O   . HOH N 5 .   ? 26.525  31.007  -38.373 1.00 33.94 ?  451 HOH G O   1 
HETATM 7398 O O   . HOH N 5 .   ? 18.334  4.182   -41.132 1.00 33.11 ?  452 HOH G O   1 
HETATM 7399 O O   . HOH N 5 .   ? 23.326  20.434  -11.618 1.00 48.10 ?  453 HOH G O   1 
HETATM 7400 O O   . HOH N 5 .   ? 23.734  28.734  -27.456 1.00 46.91 ?  454 HOH G O   1 
HETATM 7401 O O   . HOH N 5 .   ? 28.547  5.636   -44.602 1.00 35.08 ?  455 HOH G O   1 
HETATM 7402 O O   . HOH N 5 .   ? 9.599   35.514  -43.453 1.00 45.01 ?  456 HOH G O   1 
HETATM 7403 O O   . HOH N 5 .   ? 10.809  18.585  -58.844 1.00 44.48 ?  457 HOH G O   1 
HETATM 7404 O O   . HOH N 5 .   ? 8.204   22.322  -36.484 1.00 25.49 ?  458 HOH G O   1 
HETATM 7405 O O   . HOH N 5 .   ? 26.680  18.778  -9.172  1.00 44.89 ?  459 HOH G O   1 
HETATM 7406 O O   . HOH N 5 .   ? 12.595  -1.645  -52.551 1.00 44.23 ?  460 HOH G O   1 
HETATM 7407 O O   . HOH N 5 .   ? 13.038  21.531  -31.673 1.00 43.79 ?  461 HOH G O   1 
HETATM 7408 O O   . HOH N 5 .   ? 25.403  28.987  4.413   1.00 47.93 ?  462 HOH G O   1 
HETATM 7409 O O   . HOH N 5 .   ? 15.443  20.015  -19.187 1.00 43.69 ?  463 HOH G O   1 
HETATM 7410 O O   . HOH N 5 .   ? 17.661  25.819  -53.000 1.00 31.71 ?  464 HOH G O   1 
HETATM 7411 O O   . HOH N 5 .   ? 12.338  25.886  -55.417 1.00 41.00 ?  465 HOH G O   1 
HETATM 7412 O O   . HOH N 5 .   ? 16.336  18.424  -58.128 1.00 41.93 ?  466 HOH G O   1 
HETATM 7413 O O   . HOH N 5 .   ? 15.614  20.042  -11.108 1.00 42.52 ?  467 HOH G O   1 
HETATM 7414 O O   . HOH N 5 .   ? 21.048  29.841  -25.933 1.00 38.67 ?  468 HOH G O   1 
HETATM 7415 O O   . HOH N 5 .   ? 30.173  25.545  -0.284  1.00 49.26 ?  469 HOH G O   1 
HETATM 7416 O O   . HOH N 5 .   ? 29.709  24.615  -46.866 1.00 35.99 ?  470 HOH G O   1 
HETATM 7417 O O   . HOH N 5 .   ? 22.427  31.173  -50.708 1.00 42.71 ?  471 HOH G O   1 
HETATM 7418 O O   . HOH N 5 .   ? 16.347  -3.720  -53.825 1.00 37.06 ?  472 HOH G O   1 
HETATM 7419 O O   . HOH N 5 .   ? 12.924  14.390  -61.076 1.00 47.90 ?  473 HOH G O   1 
HETATM 7420 O O   . HOH N 5 .   ? 22.019  29.511  6.559   1.00 47.23 ?  474 HOH G O   1 
HETATM 7421 O O   . HOH N 5 .   ? 22.557  7.693   -46.760 1.00 34.66 ?  475 HOH G O   1 
HETATM 7422 O O   . HOH N 5 .   ? 25.229  24.000  -55.895 1.00 47.69 ?  476 HOH G O   1 
HETATM 7423 O O   . HOH N 5 .   ? 22.322  17.492  -32.075 1.00 37.17 ?  477 HOH G O   1 
HETATM 7424 O O   . HOH N 5 .   ? 8.175   30.428  -34.885 1.00 40.77 ?  478 HOH G O   1 
HETATM 7425 O O   . HOH N 5 .   ? 24.533  32.365  0.038   1.00 46.12 ?  479 HOH G O   1 
HETATM 7426 O O   . HOH N 5 .   ? 31.151  12.074  -47.535 1.00 39.05 ?  480 HOH G O   1 
HETATM 7427 O O   . HOH N 5 .   ? 27.899  10.691  -38.586 1.00 45.83 ?  481 HOH G O   1 
HETATM 7428 O O   . HOH N 5 .   ? 24.095  16.266  -54.257 1.00 43.37 ?  482 HOH G O   1 
HETATM 7429 O O   . HOH N 5 .   ? 12.561  35.339  -16.300 1.00 44.00 ?  483 HOH G O   1 
HETATM 7430 O O   . HOH N 5 .   ? 28.361  24.146  -51.731 1.00 50.24 ?  484 HOH G O   1 
HETATM 7431 O O   . HOH N 5 .   ? 26.496  35.509  -26.381 1.00 39.97 ?  485 HOH G O   1 
HETATM 7432 O O   . HOH N 5 .   ? 17.870  10.049  -57.381 1.00 42.39 ?  486 HOH G O   1 
HETATM 7433 O O   . HOH N 5 .   ? 30.844  12.538  -45.069 1.00 38.12 ?  487 HOH G O   1 
HETATM 7434 O O   . HOH N 5 .   ? 21.238  5.854   -47.712 1.00 39.69 ?  488 HOH G O   1 
HETATM 7435 O O   . HOH N 5 .   ? 5.319   24.273  -46.069 1.00 45.49 ?  489 HOH G O   1 
HETATM 7436 O O   . HOH N 5 .   ? 29.948  25.634  -34.270 1.00 40.52 ?  490 HOH G O   1 
HETATM 7437 O O   . HOH N 5 .   ? 26.766  12.643  -37.151 1.00 38.22 ?  491 HOH G O   1 
HETATM 7438 O O   . HOH N 5 .   ? 22.947  23.873  -28.854 1.00 42.85 ?  492 HOH G O   1 
HETATM 7439 O O   . HOH N 5 .   ? 19.985  10.423  -34.355 1.00 35.77 ?  493 HOH G O   1 
HETATM 7440 O O   . HOH O 5 .   ? 32.300  -19.614 -56.177 1.00 40.00 ?  401 HOH A O   1 
HETATM 7441 O O   . HOH O 5 .   ? 39.377  -15.164 -58.619 1.00 41.78 ?  402 HOH A O   1 
HETATM 7442 O O   . HOH O 5 .   ? 33.065  -9.042  -59.320 1.00 28.80 ?  403 HOH A O   1 
HETATM 7443 O O   . HOH O 5 .   ? 39.600  -6.580  -59.594 1.00 32.81 ?  404 HOH A O   1 
HETATM 7444 O O   . HOH O 5 .   ? 30.364  -13.852 -56.597 1.00 27.63 ?  405 HOH A O   1 
HETATM 7445 O O   . HOH O 5 .   ? 34.177  -17.591 -63.549 1.00 57.74 ?  406 HOH A O   1 
HETATM 7446 O O   . HOH P 5 .   ? 7.997   12.592  -56.920 1.00 28.15 ?  401 HOH B O   1 
HETATM 7447 O O   . HOH P 5 .   ? -1.252  5.496   -60.161 1.00 31.74 ?  402 HOH B O   1 
HETATM 7448 O O   . HOH P 5 .   ? 5.362   7.745   -59.638 1.00 27.00 ?  403 HOH B O   1 
HETATM 7449 O O   . HOH P 5 .   ? -1.101  14.083  -59.137 1.00 37.18 ?  404 HOH B O   1 
HETATM 7450 O O   . HOH P 5 .   ? 5.929   18.491  -56.535 1.00 40.84 ?  405 HOH B O   1 
HETATM 7451 O O   . HOH P 5 .   ? -9.033  -4.087  -58.208 1.00 40.14 ?  406 HOH B O   1 
# 
