data_8SSV
# 
_entry.id   8SSV 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.402 
_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   8SSV         pdb_00008ssv 10.2210/pdb8ssv/pdb 
WWPDB D_1000273596 ?            ?                   
# 
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 
1 'Structure model' 1 0 2024-11-06 
2 'Structure model' 1 1 2025-02-19 
# 
_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' 
# 
_pdbx_audit_revision_category.ordinal             1 
_pdbx_audit_revision_category.revision_ordinal    2 
_pdbx_audit_revision_category.data_content_type   'Structure model' 
_pdbx_audit_revision_category.category            citation 
# 
loop_
_pdbx_audit_revision_item.ordinal 
_pdbx_audit_revision_item.revision_ordinal 
_pdbx_audit_revision_item.data_content_type 
_pdbx_audit_revision_item.item 
1 2 'Structure model' '_citation.journal_volume' 
2 2 'Structure model' '_citation.page_first'     
3 2 'Structure model' '_citation.page_last'      
4 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                        8SSV 
_pdbx_database_status.recvd_initial_deposition_date   2023-05-09 
_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              gewirth@hwi.buffalo.edu 
_pdbx_contact_author.name_first         Daniel 
_pdbx_contact_author.name_last          Gewirth 
_pdbx_contact_author.name_mi            T 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0003-2702-3731 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Que, N.L.S.'   1 0000-0002-6955-7988 
'Gewirth, D.T.' 2 0000-0003-2702-3731 
# 
_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                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            Proteins 
_citation.journal_id_ASTM           PSFGEY 
_citation.journal_id_CSD            0867 
_citation.journal_id_ISSN           1097-0134 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            93 
_citation.language                  ? 
_citation.page_first                654 
_citation.page_last                 672 
_citation.title                     
'Selective Inhibition of hsp90 Paralogs: Uncovering the Role of Helix 1 in Grp94-Selective Ligand Binding.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1002/prot.26756 
_citation.pdbx_database_id_PubMed   39473058 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Que, N.L.S.'   1 ?                   
primary 'Seidler, P.M.' 2 ?                   
primary 'Aw, W.J.'      3 ?                   
primary 'Chiosis, G.'   4 ?                   
primary 'Gewirth, D.T.' 5 0000-0003-2702-3731 
# 
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 Endoplasmin                                                                           26514.012 2   ? 
'Mutated residues 287-327 into GGGG' ? ? 
2 non-polymer syn '8-[(6-IODO-1,3-BENZODIOXOL-5-YL)THIO]-9-[3-(ISOPROPYLAMINO)PROPYL]-9H-PURIN-6-AMINE' 512.368   2   ? ? ? ? 
3 non-polymer syn 'TETRAETHYLENE GLYCOL'                                                                194.226   4   ? ? ? ? 
4 non-polymer syn 'CALCIUM ION'                                                                         40.078    3   ? ? ? ? 
5 non-polymer syn 'ACETATE ION'                                                                         59.044    2   ? ? ? ? 
6 non-polymer syn 'DI(HYDROXYETHYL)ETHER'                                                               106.120   2   ? ? ? ? 
7 non-polymer syn 'MAGNESIUM ION'                                                                       24.305    1   ? ? ? ? 
8 water       nat water                                                                                 18.015    197 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        '94 kDa glucose-regulated protein,GRP-94,Heat shock protein 90 kDa beta member 1' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GSHMLREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTVKIKCDKEKNL
LHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWE
SDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTGGGGKTVWDWELMN
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSHMLREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTVKIKCDKEKNL
LHVTDTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWE
SDSNEFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTGGGGKTVWDWELMN
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 '8-[(6-IODO-1,3-BENZODIOXOL-5-YL)THIO]-9-[3-(ISOPROPYLAMINO)PROPYL]-9H-PURIN-6-AMINE' H71 
3 'TETRAETHYLENE GLYCOL'                                                                PG4 
4 'CALCIUM ION'                                                                         CA  
5 'ACETATE ION'                                                                         ACT 
6 'DI(HYDROXYETHYL)ETHER'                                                               PEG 
7 'MAGNESIUM ION'                                                                       MG  
8 water                                                                                 HOH 
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   HIS n 
1 4   MET n 
1 5   LEU n 
1 6   ARG n 
1 7   GLU n 
1 8   LYS n 
1 9   SER n 
1 10  GLU n 
1 11  LYS n 
1 12  PHE n 
1 13  ALA n 
1 14  PHE n 
1 15  GLN n 
1 16  ALA n 
1 17  GLU n 
1 18  VAL n 
1 19  ASN n 
1 20  ARG n 
1 21  MET n 
1 22  MET n 
1 23  LYS n 
1 24  LEU n 
1 25  ILE n 
1 26  ILE n 
1 27  ASN n 
1 28  SER n 
1 29  LEU n 
1 30  TYR n 
1 31  LYS n 
1 32  ASN n 
1 33  LYS n 
1 34  GLU n 
1 35  ILE n 
1 36  PHE n 
1 37  LEU n 
1 38  ARG n 
1 39  GLU n 
1 40  LEU n 
1 41  ILE n 
1 42  SER n 
1 43  ASN n 
1 44  ALA n 
1 45  SER n 
1 46  ASP n 
1 47  ALA n 
1 48  LEU n 
1 49  ASP n 
1 50  LYS n 
1 51  ILE n 
1 52  ARG n 
1 53  LEU n 
1 54  ILE n 
1 55  SER n 
1 56  LEU n 
1 57  THR n 
1 58  ASP n 
1 59  GLU n 
1 60  ASN n 
1 61  ALA n 
1 62  LEU n 
1 63  ALA n 
1 64  GLY n 
1 65  ASN n 
1 66  GLU n 
1 67  GLU n 
1 68  LEU n 
1 69  THR n 
1 70  VAL n 
1 71  LYS n 
1 72  ILE n 
1 73  LYS n 
1 74  CYS n 
1 75  ASP n 
1 76  LYS n 
1 77  GLU n 
1 78  LYS n 
1 79  ASN n 
1 80  LEU n 
1 81  LEU n 
1 82  HIS n 
1 83  VAL n 
1 84  THR n 
1 85  ASP n 
1 86  THR n 
1 87  GLY n 
1 88  VAL n 
1 89  GLY n 
1 90  MET n 
1 91  THR n 
1 92  ARG n 
1 93  GLU n 
1 94  GLU n 
1 95  LEU n 
1 96  VAL n 
1 97  LYS n 
1 98  ASN n 
1 99  LEU n 
1 100 GLY n 
1 101 THR n 
1 102 ILE n 
1 103 ALA n 
1 104 LYS n 
1 105 SER n 
1 106 GLY n 
1 107 THR n 
1 108 SER n 
1 109 GLU n 
1 110 PHE n 
1 111 LEU n 
1 112 ASN n 
1 113 LYS n 
1 114 MET n 
1 115 THR n 
1 116 GLU n 
1 117 ALA n 
1 118 GLN n 
1 119 GLU n 
1 120 ASP n 
1 121 GLY n 
1 122 GLN n 
1 123 SER n 
1 124 THR n 
1 125 SER n 
1 126 GLU n 
1 127 LEU n 
1 128 ILE n 
1 129 GLY n 
1 130 GLN n 
1 131 PHE n 
1 132 GLY n 
1 133 VAL n 
1 134 GLY n 
1 135 PHE n 
1 136 TYR n 
1 137 SER n 
1 138 ALA n 
1 139 PHE n 
1 140 LEU n 
1 141 VAL n 
1 142 ALA n 
1 143 ASP n 
1 144 LYS n 
1 145 VAL n 
1 146 ILE n 
1 147 VAL n 
1 148 THR n 
1 149 SER n 
1 150 LYS n 
1 151 HIS n 
1 152 ASN n 
1 153 ASN n 
1 154 ASP n 
1 155 THR n 
1 156 GLN n 
1 157 HIS n 
1 158 ILE n 
1 159 TRP n 
1 160 GLU n 
1 161 SER n 
1 162 ASP n 
1 163 SER n 
1 164 ASN n 
1 165 GLU n 
1 166 PHE n 
1 167 SER n 
1 168 VAL n 
1 169 ILE n 
1 170 ALA n 
1 171 ASP n 
1 172 PRO n 
1 173 ARG n 
1 174 GLY n 
1 175 ASN n 
1 176 THR n 
1 177 LEU n 
1 178 GLY n 
1 179 ARG n 
1 180 GLY n 
1 181 THR n 
1 182 THR n 
1 183 ILE n 
1 184 THR n 
1 185 LEU n 
1 186 VAL n 
1 187 LEU n 
1 188 LYS n 
1 189 GLU n 
1 190 GLU n 
1 191 ALA n 
1 192 SER n 
1 193 ASP n 
1 194 TYR n 
1 195 LEU n 
1 196 GLU n 
1 197 LEU n 
1 198 ASP n 
1 199 THR n 
1 200 ILE n 
1 201 LYS n 
1 202 ASN n 
1 203 LEU n 
1 204 VAL n 
1 205 LYS n 
1 206 LYS n 
1 207 TYR n 
1 208 SER n 
1 209 GLN n 
1 210 PHE n 
1 211 ILE n 
1 212 ASN n 
1 213 PHE n 
1 214 PRO n 
1 215 ILE n 
1 216 TYR n 
1 217 VAL n 
1 218 TRP n 
1 219 SER n 
1 220 SER n 
1 221 LYS n 
1 222 THR n 
1 223 GLY n 
1 224 GLY n 
1 225 GLY n 
1 226 GLY n 
1 227 LYS n 
1 228 THR n 
1 229 VAL n 
1 230 TRP n 
1 231 ASP n 
1 232 TRP n 
1 233 GLU n 
1 234 LEU n 
1 235 MET n 
1 236 ASN n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   236 
_entity_src_gen.gene_src_common_name               dog 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'HSP90B1, GRP94, TRA1' 
_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      'Canis lupus familiaris' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9615 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_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               'BL21 STAR (DE3)' 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ACT non-polymer         . 'ACETATE ION'                                                                         ? 'C2 H3 O2 -1' 
59.044  
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 
CA  non-polymer         . 'CALCIUM ION'                                                                         ? 'Ca 2' 40.078  
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  
H71 non-polymer         . '8-[(6-IODO-1,3-BENZODIOXOL-5-YL)THIO]-9-[3-(ISOPROPYLAMINO)PROPYL]-9H-PURIN-6-AMINE' ? 
'C18 H21 I N6 O2 S' 512.368 
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 
MG  non-polymer         . 'MAGNESIUM ION'                                                                       ? 'Mg 2' 24.305  
PEG non-polymer         . 'DI(HYDROXYETHYL)ETHER'                                                               ? 'C4 H10 O3' 
106.120 
PG4 non-polymer         . 'TETRAETHYLENE GLYCOL'                                                                ? 'C8 H18 O5' 
194.226 
PHE 'L-peptide linking' y PHENYLALANINE                                                                         ? 'C9 H11 N O2' 
165.189 
PRO 'L-peptide linking' y PROLINE                                                                               ? 'C5 H9 N O2' 
115.130 
SER 'L-peptide linking' y SERINE                                                                                ? 'C3 H7 N O3' 
105.093 
THR 'L-peptide linking' y THREONINE                                                                             ? 'C4 H9 N O3' 
119.119 
TRP 'L-peptide linking' y TRYPTOPHAN                                                                            ? 'C11 H12 N2 O2' 
204.225 
TYR 'L-peptide linking' y TYROSINE                                                                              ? 'C9 H11 N O3' 
181.189 
VAL 'L-peptide linking' y VALINE                                                                                ? 'C5 H11 N O2' 
117.146 
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   65  ?   ?   ?   A . n 
A 1 2   SER 2   66  ?   ?   ?   A . n 
A 1 3   HIS 3   67  ?   ?   ?   A . n 
A 1 4   MET 4   68  ?   ?   ?   A . n 
A 1 5   LEU 5   69  ?   ?   ?   A . n 
A 1 6   ARG 6   70  70  ARG ARG A . n 
A 1 7   GLU 7   71  71  GLU GLU A . n 
A 1 8   LYS 8   72  72  LYS LYS A . n 
A 1 9   SER 9   73  73  SER SER A . n 
A 1 10  GLU 10  74  74  GLU GLU A . n 
A 1 11  LYS 11  75  75  LYS LYS A . n 
A 1 12  PHE 12  76  76  PHE PHE A . n 
A 1 13  ALA 13  77  77  ALA ALA A . n 
A 1 14  PHE 14  78  78  PHE PHE A . n 
A 1 15  GLN 15  79  79  GLN GLN A . n 
A 1 16  ALA 16  80  80  ALA ALA A . n 
A 1 17  GLU 17  81  81  GLU GLU A . n 
A 1 18  VAL 18  82  82  VAL VAL A . n 
A 1 19  ASN 19  83  83  ASN ASN A . n 
A 1 20  ARG 20  84  84  ARG ARG A . n 
A 1 21  MET 21  85  85  MET MET A . n 
A 1 22  MET 22  86  86  MET MET A . n 
A 1 23  LYS 23  87  87  LYS LYS A . n 
A 1 24  LEU 24  88  88  LEU LEU A . n 
A 1 25  ILE 25  89  89  ILE ILE A . n 
A 1 26  ILE 26  90  90  ILE ILE A . n 
A 1 27  ASN 27  91  91  ASN ASN A . n 
A 1 28  SER 28  92  92  SER SER A . n 
A 1 29  LEU 29  93  93  LEU LEU A . n 
A 1 30  TYR 30  94  94  TYR TYR A . n 
A 1 31  LYS 31  95  95  LYS LYS A . n 
A 1 32  ASN 32  96  96  ASN ASN A . n 
A 1 33  LYS 33  97  97  LYS LYS A . n 
A 1 34  GLU 34  98  98  GLU GLU A . n 
A 1 35  ILE 35  99  99  ILE ILE A . n 
A 1 36  PHE 36  100 100 PHE PHE A . n 
A 1 37  LEU 37  101 101 LEU LEU A . n 
A 1 38  ARG 38  102 102 ARG ARG A . n 
A 1 39  GLU 39  103 103 GLU GLU A . n 
A 1 40  LEU 40  104 104 LEU LEU A . n 
A 1 41  ILE 41  105 105 ILE ILE A . n 
A 1 42  SER 42  106 106 SER SER A . n 
A 1 43  ASN 43  107 107 ASN ASN A . n 
A 1 44  ALA 44  108 108 ALA ALA A . n 
A 1 45  SER 45  109 109 SER SER A . n 
A 1 46  ASP 46  110 110 ASP ASP A . n 
A 1 47  ALA 47  111 111 ALA ALA A . n 
A 1 48  LEU 48  112 112 LEU LEU A . n 
A 1 49  ASP 49  113 113 ASP ASP A . n 
A 1 50  LYS 50  114 114 LYS LYS A . n 
A 1 51  ILE 51  115 115 ILE ILE A . n 
A 1 52  ARG 52  116 116 ARG ARG A . n 
A 1 53  LEU 53  117 117 LEU LEU A . n 
A 1 54  ILE 54  118 118 ILE ILE A . n 
A 1 55  SER 55  119 119 SER SER A . n 
A 1 56  LEU 56  120 120 LEU LEU A . n 
A 1 57  THR 57  121 121 THR THR A . n 
A 1 58  ASP 58  122 122 ASP ASP A . n 
A 1 59  GLU 59  123 123 GLU GLU A . n 
A 1 60  ASN 60  124 124 ASN ASN A . n 
A 1 61  ALA 61  125 125 ALA ALA A . n 
A 1 62  LEU 62  126 126 LEU LEU A . n 
A 1 63  ALA 63  127 127 ALA ALA A . n 
A 1 64  GLY 64  128 128 GLY GLY A . n 
A 1 65  ASN 65  129 129 ASN ASN A . n 
A 1 66  GLU 66  130 130 GLU GLU A . n 
A 1 67  GLU 67  131 131 GLU GLU A . n 
A 1 68  LEU 68  132 132 LEU LEU A . n 
A 1 69  THR 69  133 133 THR THR A . n 
A 1 70  VAL 70  134 134 VAL VAL A . n 
A 1 71  LYS 71  135 135 LYS LYS A . n 
A 1 72  ILE 72  136 136 ILE ILE A . n 
A 1 73  LYS 73  137 137 LYS LYS A . n 
A 1 74  CYS 74  138 138 CYS CYS A . n 
A 1 75  ASP 75  139 139 ASP ASP A . n 
A 1 76  LYS 76  140 140 LYS LYS A . n 
A 1 77  GLU 77  141 141 GLU GLU A . n 
A 1 78  LYS 78  142 142 LYS LYS A . n 
A 1 79  ASN 79  143 143 ASN ASN A . n 
A 1 80  LEU 80  144 144 LEU LEU A . n 
A 1 81  LEU 81  145 145 LEU LEU A . n 
A 1 82  HIS 82  146 146 HIS HIS A . n 
A 1 83  VAL 83  147 147 VAL VAL A . n 
A 1 84  THR 84  148 148 THR THR A . n 
A 1 85  ASP 85  149 149 ASP ASP A . n 
A 1 86  THR 86  150 150 THR THR A . n 
A 1 87  GLY 87  151 151 GLY GLY A . n 
A 1 88  VAL 88  152 152 VAL VAL A . n 
A 1 89  GLY 89  153 153 GLY GLY A . n 
A 1 90  MET 90  154 154 MET MET A . n 
A 1 91  THR 91  155 155 THR THR A . n 
A 1 92  ARG 92  156 156 ARG ARG A . n 
A 1 93  GLU 93  157 157 GLU GLU A . n 
A 1 94  GLU 94  158 158 GLU GLU A . n 
A 1 95  LEU 95  159 159 LEU LEU A . n 
A 1 96  VAL 96  160 160 VAL VAL A . n 
A 1 97  LYS 97  161 161 LYS LYS A . n 
A 1 98  ASN 98  162 162 ASN ASN A . n 
A 1 99  LEU 99  163 163 LEU LEU A . n 
A 1 100 GLY 100 164 ?   ?   ?   A . n 
A 1 101 THR 101 165 ?   ?   ?   A . n 
A 1 102 ILE 102 166 ?   ?   ?   A . n 
A 1 103 ALA 103 167 ?   ?   ?   A . n 
A 1 104 LYS 104 168 ?   ?   ?   A . n 
A 1 105 SER 105 169 ?   ?   ?   A . n 
A 1 106 GLY 106 170 ?   ?   ?   A . n 
A 1 107 THR 107 171 ?   ?   ?   A . n 
A 1 108 SER 108 172 ?   ?   ?   A . n 
A 1 109 GLU 109 173 ?   ?   ?   A . n 
A 1 110 PHE 110 174 ?   ?   ?   A . n 
A 1 111 LEU 111 175 ?   ?   ?   A . n 
A 1 112 ASN 112 176 ?   ?   ?   A . n 
A 1 113 LYS 113 177 ?   ?   ?   A . n 
A 1 114 MET 114 178 ?   ?   ?   A . n 
A 1 115 THR 115 179 ?   ?   ?   A . n 
A 1 116 GLU 116 180 ?   ?   ?   A . n 
A 1 117 ALA 117 181 ?   ?   ?   A . n 
A 1 118 GLN 118 182 ?   ?   ?   A . n 
A 1 119 GLU 119 183 ?   ?   ?   A . n 
A 1 120 ASP 120 184 ?   ?   ?   A . n 
A 1 121 GLY 121 185 ?   ?   ?   A . n 
A 1 122 GLN 122 186 ?   ?   ?   A . n 
A 1 123 SER 123 187 ?   ?   ?   A . n 
A 1 124 THR 124 188 188 THR THR A . n 
A 1 125 SER 125 189 189 SER SER A . n 
A 1 126 GLU 126 190 190 GLU GLU A . n 
A 1 127 LEU 127 191 191 LEU LEU A . n 
A 1 128 ILE 128 192 192 ILE ILE A . n 
A 1 129 GLY 129 193 193 GLY GLY A . n 
A 1 130 GLN 130 194 194 GLN GLN A . n 
A 1 131 PHE 131 195 195 PHE PHE A . n 
A 1 132 GLY 132 196 196 GLY GLY A . n 
A 1 133 VAL 133 197 197 VAL VAL A . n 
A 1 134 GLY 134 198 198 GLY GLY A . n 
A 1 135 PHE 135 199 199 PHE PHE A . n 
A 1 136 TYR 136 200 200 TYR TYR A . n 
A 1 137 SER 137 201 201 SER SER A . n 
A 1 138 ALA 138 202 202 ALA ALA A . n 
A 1 139 PHE 139 203 203 PHE PHE A . n 
A 1 140 LEU 140 204 204 LEU LEU A . n 
A 1 141 VAL 141 205 205 VAL VAL A . n 
A 1 142 ALA 142 206 206 ALA ALA A . n 
A 1 143 ASP 143 207 207 ASP ASP A . n 
A 1 144 LYS 144 208 208 LYS LYS A . n 
A 1 145 VAL 145 209 209 VAL VAL A . n 
A 1 146 ILE 146 210 210 ILE ILE A . n 
A 1 147 VAL 147 211 211 VAL VAL A . n 
A 1 148 THR 148 212 212 THR THR A . n 
A 1 149 SER 149 213 213 SER SER A . n 
A 1 150 LYS 150 214 214 LYS LYS A . n 
A 1 151 HIS 151 215 215 HIS HIS A . n 
A 1 152 ASN 152 216 216 ASN ASN A . n 
A 1 153 ASN 153 217 217 ASN ASN A . n 
A 1 154 ASP 154 218 218 ASP ASP A . n 
A 1 155 THR 155 219 219 THR THR A . n 
A 1 156 GLN 156 220 220 GLN GLN A . n 
A 1 157 HIS 157 221 221 HIS HIS A . n 
A 1 158 ILE 158 222 222 ILE ILE A . n 
A 1 159 TRP 159 223 223 TRP TRP A . n 
A 1 160 GLU 160 224 224 GLU GLU A . n 
A 1 161 SER 161 225 225 SER SER A . n 
A 1 162 ASP 162 226 226 ASP ASP A . n 
A 1 163 SER 163 227 227 SER SER A . n 
A 1 164 ASN 164 228 228 ASN ASN A . n 
A 1 165 GLU 165 229 229 GLU GLU A . n 
A 1 166 PHE 166 230 230 PHE PHE A . n 
A 1 167 SER 167 231 231 SER SER A . n 
A 1 168 VAL 168 232 232 VAL VAL A . n 
A 1 169 ILE 169 233 233 ILE ILE A . n 
A 1 170 ALA 170 234 234 ALA ALA A . n 
A 1 171 ASP 171 235 235 ASP ASP A . n 
A 1 172 PRO 172 236 236 PRO PRO A . n 
A 1 173 ARG 173 237 237 ARG ARG A . n 
A 1 174 GLY 174 238 238 GLY GLY A . n 
A 1 175 ASN 175 239 239 ASN ASN A . n 
A 1 176 THR 176 240 240 THR THR A . n 
A 1 177 LEU 177 241 241 LEU LEU A . n 
A 1 178 GLY 178 242 242 GLY GLY A . n 
A 1 179 ARG 179 243 243 ARG ARG A . n 
A 1 180 GLY 180 244 244 GLY GLY A . n 
A 1 181 THR 181 245 245 THR THR A . n 
A 1 182 THR 182 246 246 THR THR A . n 
A 1 183 ILE 183 247 247 ILE ILE A . n 
A 1 184 THR 184 248 248 THR THR A . n 
A 1 185 LEU 185 249 249 LEU LEU A . n 
A 1 186 VAL 186 250 250 VAL VAL A . n 
A 1 187 LEU 187 251 251 LEU LEU A . n 
A 1 188 LYS 188 252 252 LYS LYS A . n 
A 1 189 GLU 189 253 253 GLU GLU A . n 
A 1 190 GLU 190 254 254 GLU GLU A . n 
A 1 191 ALA 191 255 255 ALA ALA A . n 
A 1 192 SER 192 256 256 SER SER A . n 
A 1 193 ASP 193 257 257 ASP ASP A . n 
A 1 194 TYR 194 258 258 TYR TYR A . n 
A 1 195 LEU 195 259 259 LEU LEU A . n 
A 1 196 GLU 196 260 260 GLU GLU A . n 
A 1 197 LEU 197 261 261 LEU LEU A . n 
A 1 198 ASP 198 262 262 ASP ASP A . n 
A 1 199 THR 199 263 263 THR THR A . n 
A 1 200 ILE 200 264 264 ILE ILE A . n 
A 1 201 LYS 201 265 265 LYS LYS A . n 
A 1 202 ASN 202 266 266 ASN ASN A . n 
A 1 203 LEU 203 267 267 LEU LEU A . n 
A 1 204 VAL 204 268 268 VAL VAL A . n 
A 1 205 LYS 205 269 269 LYS LYS A . n 
A 1 206 LYS 206 270 270 LYS LYS A . n 
A 1 207 TYR 207 271 271 TYR TYR A . n 
A 1 208 SER 208 272 272 SER SER A . n 
A 1 209 GLN 209 273 273 GLN GLN A . n 
A 1 210 PHE 210 274 274 PHE PHE A . n 
A 1 211 ILE 211 275 275 ILE ILE A . n 
A 1 212 ASN 212 276 276 ASN ASN A . n 
A 1 213 PHE 213 277 277 PHE PHE A . n 
A 1 214 PRO 214 278 278 PRO PRO A . n 
A 1 215 ILE 215 279 279 ILE ILE A . n 
A 1 216 TYR 216 280 280 TYR TYR A . n 
A 1 217 VAL 217 281 281 VAL VAL A . n 
A 1 218 TRP 218 282 282 TRP TRP A . n 
A 1 219 SER 219 283 283 SER SER A . n 
A 1 220 SER 220 284 284 SER SER A . n 
A 1 221 LYS 221 285 285 LYS LYS A . n 
A 1 222 THR 222 323 ?   ?   ?   A . n 
A 1 223 GLY 223 324 ?   ?   ?   A . n 
A 1 224 GLY 224 325 ?   ?   ?   A . n 
A 1 225 GLY 225 326 ?   ?   ?   A . n 
A 1 226 GLY 226 327 327 GLY GLY A . n 
A 1 227 LYS 227 328 328 LYS LYS A . n 
A 1 228 THR 228 329 329 THR THR A . n 
A 1 229 VAL 229 330 330 VAL VAL A . n 
A 1 230 TRP 230 331 331 TRP TRP A . n 
A 1 231 ASP 231 332 332 ASP ASP A . n 
A 1 232 TRP 232 333 333 TRP TRP A . n 
A 1 233 GLU 233 334 334 GLU GLU A . n 
A 1 234 LEU 234 335 335 LEU LEU A . n 
A 1 235 MET 235 336 336 MET MET A . n 
A 1 236 ASN 236 337 337 ASN ASN A . n 
B 1 1   GLY 1   65  65  GLY GLY B . n 
B 1 2   SER 2   66  66  SER SER B . n 
B 1 3   HIS 3   67  67  HIS HIS B . n 
B 1 4   MET 4   68  68  MET MET B . n 
B 1 5   LEU 5   69  69  LEU LEU B . n 
B 1 6   ARG 6   70  70  ARG ARG B . n 
B 1 7   GLU 7   71  71  GLU GLU B . n 
B 1 8   LYS 8   72  72  LYS LYS B . n 
B 1 9   SER 9   73  73  SER SER B . n 
B 1 10  GLU 10  74  74  GLU GLU B . n 
B 1 11  LYS 11  75  75  LYS LYS B . n 
B 1 12  PHE 12  76  76  PHE PHE B . n 
B 1 13  ALA 13  77  77  ALA ALA B . n 
B 1 14  PHE 14  78  78  PHE PHE B . n 
B 1 15  GLN 15  79  79  GLN GLN B . n 
B 1 16  ALA 16  80  80  ALA ALA B . n 
B 1 17  GLU 17  81  81  GLU GLU B . n 
B 1 18  VAL 18  82  82  VAL VAL B . n 
B 1 19  ASN 19  83  83  ASN ASN B . n 
B 1 20  ARG 20  84  84  ARG ARG B . n 
B 1 21  MET 21  85  85  MET MET B . n 
B 1 22  MET 22  86  86  MET MET B . n 
B 1 23  LYS 23  87  87  LYS LYS B . n 
B 1 24  LEU 24  88  88  LEU LEU B . n 
B 1 25  ILE 25  89  89  ILE ILE B . n 
B 1 26  ILE 26  90  90  ILE ILE B . n 
B 1 27  ASN 27  91  91  ASN ASN B . n 
B 1 28  SER 28  92  92  SER SER B . n 
B 1 29  LEU 29  93  93  LEU LEU B . n 
B 1 30  TYR 30  94  94  TYR TYR B . n 
B 1 31  LYS 31  95  95  LYS LYS B . n 
B 1 32  ASN 32  96  96  ASN ASN B . n 
B 1 33  LYS 33  97  97  LYS LYS B . n 
B 1 34  GLU 34  98  98  GLU GLU B . n 
B 1 35  ILE 35  99  99  ILE ILE B . n 
B 1 36  PHE 36  100 100 PHE PHE B . n 
B 1 37  LEU 37  101 101 LEU LEU B . n 
B 1 38  ARG 38  102 102 ARG ARG B . n 
B 1 39  GLU 39  103 103 GLU GLU B . n 
B 1 40  LEU 40  104 104 LEU LEU B . n 
B 1 41  ILE 41  105 105 ILE ILE B . n 
B 1 42  SER 42  106 106 SER SER B . n 
B 1 43  ASN 43  107 107 ASN ASN B . n 
B 1 44  ALA 44  108 108 ALA ALA B . n 
B 1 45  SER 45  109 109 SER SER B . n 
B 1 46  ASP 46  110 110 ASP ASP B . n 
B 1 47  ALA 47  111 111 ALA ALA B . n 
B 1 48  LEU 48  112 112 LEU LEU B . n 
B 1 49  ASP 49  113 113 ASP ASP B . n 
B 1 50  LYS 50  114 114 LYS LYS B . n 
B 1 51  ILE 51  115 115 ILE ILE B . n 
B 1 52  ARG 52  116 116 ARG ARG B . n 
B 1 53  LEU 53  117 117 LEU LEU B . n 
B 1 54  ILE 54  118 118 ILE ILE B . n 
B 1 55  SER 55  119 119 SER SER B . n 
B 1 56  LEU 56  120 120 LEU LEU B . n 
B 1 57  THR 57  121 121 THR THR B . n 
B 1 58  ASP 58  122 122 ASP ASP B . n 
B 1 59  GLU 59  123 123 GLU GLU B . n 
B 1 60  ASN 60  124 124 ASN ASN B . n 
B 1 61  ALA 61  125 125 ALA ALA B . n 
B 1 62  LEU 62  126 126 LEU LEU B . n 
B 1 63  ALA 63  127 127 ALA ALA B . n 
B 1 64  GLY 64  128 128 GLY GLY B . n 
B 1 65  ASN 65  129 129 ASN ASN B . n 
B 1 66  GLU 66  130 130 GLU GLU B . n 
B 1 67  GLU 67  131 131 GLU GLU B . n 
B 1 68  LEU 68  132 132 LEU LEU B . n 
B 1 69  THR 69  133 133 THR THR B . n 
B 1 70  VAL 70  134 134 VAL VAL B . n 
B 1 71  LYS 71  135 135 LYS LYS B . n 
B 1 72  ILE 72  136 136 ILE ILE B . n 
B 1 73  LYS 73  137 137 LYS LYS B . n 
B 1 74  CYS 74  138 138 CYS CYS B . n 
B 1 75  ASP 75  139 139 ASP ASP B . n 
B 1 76  LYS 76  140 140 LYS LYS B . n 
B 1 77  GLU 77  141 141 GLU GLU B . n 
B 1 78  LYS 78  142 142 LYS LYS B . n 
B 1 79  ASN 79  143 143 ASN ASN B . n 
B 1 80  LEU 80  144 144 LEU LEU B . n 
B 1 81  LEU 81  145 145 LEU LEU B . n 
B 1 82  HIS 82  146 146 HIS HIS B . n 
B 1 83  VAL 83  147 147 VAL VAL B . n 
B 1 84  THR 84  148 148 THR THR B . n 
B 1 85  ASP 85  149 149 ASP ASP B . n 
B 1 86  THR 86  150 150 THR THR B . n 
B 1 87  GLY 87  151 151 GLY GLY B . n 
B 1 88  VAL 88  152 152 VAL VAL B . n 
B 1 89  GLY 89  153 153 GLY GLY B . n 
B 1 90  MET 90  154 154 MET MET B . n 
B 1 91  THR 91  155 155 THR THR B . n 
B 1 92  ARG 92  156 156 ARG ARG B . n 
B 1 93  GLU 93  157 157 GLU GLU B . n 
B 1 94  GLU 94  158 158 GLU GLU B . n 
B 1 95  LEU 95  159 159 LEU LEU B . n 
B 1 96  VAL 96  160 160 VAL VAL B . n 
B 1 97  LYS 97  161 161 LYS LYS B . n 
B 1 98  ASN 98  162 162 ASN ASN B . n 
B 1 99  LEU 99  163 163 LEU LEU B . n 
B 1 100 GLY 100 164 164 GLY GLY B . n 
B 1 101 THR 101 165 ?   ?   ?   B . n 
B 1 102 ILE 102 166 ?   ?   ?   B . n 
B 1 103 ALA 103 167 ?   ?   ?   B . n 
B 1 104 LYS 104 168 ?   ?   ?   B . n 
B 1 105 SER 105 169 ?   ?   ?   B . n 
B 1 106 GLY 106 170 ?   ?   ?   B . n 
B 1 107 THR 107 171 ?   ?   ?   B . n 
B 1 108 SER 108 172 ?   ?   ?   B . n 
B 1 109 GLU 109 173 ?   ?   ?   B . n 
B 1 110 PHE 110 174 ?   ?   ?   B . n 
B 1 111 LEU 111 175 ?   ?   ?   B . n 
B 1 112 ASN 112 176 ?   ?   ?   B . n 
B 1 113 LYS 113 177 ?   ?   ?   B . n 
B 1 114 MET 114 178 ?   ?   ?   B . n 
B 1 115 THR 115 179 ?   ?   ?   B . n 
B 1 116 GLU 116 180 ?   ?   ?   B . n 
B 1 117 ALA 117 181 ?   ?   ?   B . n 
B 1 118 GLN 118 182 ?   ?   ?   B . n 
B 1 119 GLU 119 183 ?   ?   ?   B . n 
B 1 120 ASP 120 184 ?   ?   ?   B . n 
B 1 121 GLY 121 185 ?   ?   ?   B . n 
B 1 122 GLN 122 186 ?   ?   ?   B . n 
B 1 123 SER 123 187 ?   ?   ?   B . n 
B 1 124 THR 124 188 188 THR THR B . n 
B 1 125 SER 125 189 189 SER SER B . n 
B 1 126 GLU 126 190 190 GLU GLU B . n 
B 1 127 LEU 127 191 191 LEU LEU B . n 
B 1 128 ILE 128 192 192 ILE ILE B . n 
B 1 129 GLY 129 193 193 GLY GLY B . n 
B 1 130 GLN 130 194 194 GLN GLN B . n 
B 1 131 PHE 131 195 195 PHE PHE B . n 
B 1 132 GLY 132 196 196 GLY GLY B . n 
B 1 133 VAL 133 197 197 VAL VAL B . n 
B 1 134 GLY 134 198 198 GLY GLY B . n 
B 1 135 PHE 135 199 199 PHE PHE B . n 
B 1 136 TYR 136 200 200 TYR TYR B . n 
B 1 137 SER 137 201 201 SER SER B . n 
B 1 138 ALA 138 202 202 ALA ALA B . n 
B 1 139 PHE 139 203 203 PHE PHE B . n 
B 1 140 LEU 140 204 204 LEU LEU B . n 
B 1 141 VAL 141 205 205 VAL VAL B . n 
B 1 142 ALA 142 206 206 ALA ALA B . n 
B 1 143 ASP 143 207 207 ASP ASP B . n 
B 1 144 LYS 144 208 208 LYS LYS B . n 
B 1 145 VAL 145 209 209 VAL VAL B . n 
B 1 146 ILE 146 210 210 ILE ILE B . n 
B 1 147 VAL 147 211 211 VAL VAL B . n 
B 1 148 THR 148 212 212 THR THR B . n 
B 1 149 SER 149 213 213 SER SER B . n 
B 1 150 LYS 150 214 214 LYS LYS B . n 
B 1 151 HIS 151 215 215 HIS HIS B . n 
B 1 152 ASN 152 216 216 ASN ASN B . n 
B 1 153 ASN 153 217 217 ASN ASN B . n 
B 1 154 ASP 154 218 218 ASP ASP B . n 
B 1 155 THR 155 219 219 THR THR B . n 
B 1 156 GLN 156 220 220 GLN GLN B . n 
B 1 157 HIS 157 221 221 HIS HIS B . n 
B 1 158 ILE 158 222 222 ILE ILE B . n 
B 1 159 TRP 159 223 223 TRP TRP B . n 
B 1 160 GLU 160 224 224 GLU GLU B . n 
B 1 161 SER 161 225 225 SER SER B . n 
B 1 162 ASP 162 226 226 ASP ASP B . n 
B 1 163 SER 163 227 227 SER SER B . n 
B 1 164 ASN 164 228 228 ASN ASN B . n 
B 1 165 GLU 165 229 229 GLU GLU B . n 
B 1 166 PHE 166 230 230 PHE PHE B . n 
B 1 167 SER 167 231 231 SER SER B . n 
B 1 168 VAL 168 232 232 VAL VAL B . n 
B 1 169 ILE 169 233 233 ILE ILE B . n 
B 1 170 ALA 170 234 234 ALA ALA B . n 
B 1 171 ASP 171 235 235 ASP ASP B . n 
B 1 172 PRO 172 236 236 PRO PRO B . n 
B 1 173 ARG 173 237 237 ARG ARG B . n 
B 1 174 GLY 174 238 238 GLY GLY B . n 
B 1 175 ASN 175 239 239 ASN ASN B . n 
B 1 176 THR 176 240 240 THR THR B . n 
B 1 177 LEU 177 241 241 LEU LEU B . n 
B 1 178 GLY 178 242 242 GLY GLY B . n 
B 1 179 ARG 179 243 243 ARG ARG B . n 
B 1 180 GLY 180 244 244 GLY GLY B . n 
B 1 181 THR 181 245 245 THR THR B . n 
B 1 182 THR 182 246 246 THR THR B . n 
B 1 183 ILE 183 247 247 ILE ILE B . n 
B 1 184 THR 184 248 248 THR THR B . n 
B 1 185 LEU 185 249 249 LEU LEU B . n 
B 1 186 VAL 186 250 250 VAL VAL B . n 
B 1 187 LEU 187 251 251 LEU LEU B . n 
B 1 188 LYS 188 252 252 LYS LYS B . n 
B 1 189 GLU 189 253 253 GLU GLU B . n 
B 1 190 GLU 190 254 254 GLU GLU B . n 
B 1 191 ALA 191 255 255 ALA ALA B . n 
B 1 192 SER 192 256 256 SER SER B . n 
B 1 193 ASP 193 257 257 ASP ASP B . n 
B 1 194 TYR 194 258 258 TYR TYR B . n 
B 1 195 LEU 195 259 259 LEU LEU B . n 
B 1 196 GLU 196 260 260 GLU GLU B . n 
B 1 197 LEU 197 261 261 LEU LEU B . n 
B 1 198 ASP 198 262 262 ASP ASP B . n 
B 1 199 THR 199 263 263 THR THR B . n 
B 1 200 ILE 200 264 264 ILE ILE B . n 
B 1 201 LYS 201 265 265 LYS LYS B . n 
B 1 202 ASN 202 266 266 ASN ASN B . n 
B 1 203 LEU 203 267 267 LEU LEU B . n 
B 1 204 VAL 204 268 268 VAL VAL B . n 
B 1 205 LYS 205 269 269 LYS LYS B . n 
B 1 206 LYS 206 270 270 LYS LYS B . n 
B 1 207 TYR 207 271 271 TYR TYR B . n 
B 1 208 SER 208 272 272 SER SER B . n 
B 1 209 GLN 209 273 273 GLN GLN B . n 
B 1 210 PHE 210 274 274 PHE PHE B . n 
B 1 211 ILE 211 275 275 ILE ILE B . n 
B 1 212 ASN 212 276 276 ASN ASN B . n 
B 1 213 PHE 213 277 277 PHE PHE B . n 
B 1 214 PRO 214 278 278 PRO PRO B . n 
B 1 215 ILE 215 279 279 ILE ILE B . n 
B 1 216 TYR 216 280 280 TYR TYR B . n 
B 1 217 VAL 217 281 281 VAL VAL B . n 
B 1 218 TRP 218 282 282 TRP TRP B . n 
B 1 219 SER 219 283 283 SER SER B . n 
B 1 220 SER 220 284 284 SER SER B . n 
B 1 221 LYS 221 285 285 LYS LYS B . n 
B 1 222 THR 222 323 ?   ?   ?   B . n 
B 1 223 GLY 223 324 ?   ?   ?   B . n 
B 1 224 GLY 224 325 ?   ?   ?   B . n 
B 1 225 GLY 225 326 ?   ?   ?   B . n 
B 1 226 GLY 226 327 327 GLY GLY B . n 
B 1 227 LYS 227 328 328 LYS LYS B . n 
B 1 228 THR 228 329 329 THR THR B . n 
B 1 229 VAL 229 330 330 VAL VAL B . n 
B 1 230 TRP 230 331 331 TRP TRP B . n 
B 1 231 ASP 231 332 332 ASP ASP B . n 
B 1 232 TRP 232 333 333 TRP TRP B . n 
B 1 233 GLU 233 334 334 GLU GLU B . n 
B 1 234 LEU 234 335 335 LEU LEU B . n 
B 1 235 MET 235 336 336 MET MET B . n 
B 1 236 ASN 236 337 337 ASN ASN B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        H71 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   H71 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 H71 1   401 401  H71 H71 A . 
D 3 PG4 1   402 501  PG4 PG4 A . 
E 3 PG4 1   403 601  PG4 PG4 A . 
F 3 PG4 1   404 701  PG4 PG4 A . 
G 4 CA  1   405 1    CA  CA  A . 
H 2 H71 1   401 401  H71 H71 B . 
I 4 CA  1   402 501  CA  CA  B . 
J 5 ACT 1   403 601  ACT ACT B . 
K 3 PG4 1   404 701  PG4 PG4 B . 
L 6 PEG 1   405 801  PEG PEG B . 
M 6 PEG 1   406 901  PEG PEG B . 
N 7 MG  1   407 1001 MG  MG  B . 
O 5 ACT 1   408 1101 ACT ACT B . 
P 4 CA  1   409 2    CA  CA  B . 
Q 8 HOH 1   501 233  HOH HOH A . 
Q 8 HOH 2   502 102  HOH HOH A . 
Q 8 HOH 3   503 231  HOH HOH A . 
Q 8 HOH 4   504 84   HOH HOH A . 
Q 8 HOH 5   505 128  HOH HOH A . 
Q 8 HOH 6   506 27   HOH HOH A . 
Q 8 HOH 7   507 217  HOH HOH A . 
Q 8 HOH 8   508 153  HOH HOH A . 
Q 8 HOH 9   509 57   HOH HOH A . 
Q 8 HOH 10  510 108  HOH HOH A . 
Q 8 HOH 11  511 82   HOH HOH A . 
Q 8 HOH 12  512 204  HOH HOH A . 
Q 8 HOH 13  513 10   HOH HOH A . 
Q 8 HOH 14  514 190  HOH HOH A . 
Q 8 HOH 15  515 189  HOH HOH A . 
Q 8 HOH 16  516 229  HOH HOH A . 
Q 8 HOH 17  517 37   HOH HOH A . 
Q 8 HOH 18  518 88   HOH HOH A . 
Q 8 HOH 19  519 225  HOH HOH A . 
Q 8 HOH 20  520 6    HOH HOH A . 
Q 8 HOH 21  521 20   HOH HOH A . 
Q 8 HOH 22  522 38   HOH HOH A . 
Q 8 HOH 23  523 83   HOH HOH A . 
Q 8 HOH 24  524 230  HOH HOH A . 
Q 8 HOH 25  525 54   HOH HOH A . 
Q 8 HOH 26  526 114  HOH HOH A . 
Q 8 HOH 27  527 64   HOH HOH A . 
Q 8 HOH 28  528 33   HOH HOH A . 
Q 8 HOH 29  529 18   HOH HOH A . 
Q 8 HOH 30  530 245  HOH HOH A . 
Q 8 HOH 31  531 117  HOH HOH A . 
Q 8 HOH 32  532 154  HOH HOH A . 
Q 8 HOH 33  533 69   HOH HOH A . 
Q 8 HOH 34  534 22   HOH HOH A . 
Q 8 HOH 35  535 36   HOH HOH A . 
Q 8 HOH 36  536 91   HOH HOH A . 
Q 8 HOH 37  537 221  HOH HOH A . 
Q 8 HOH 38  538 158  HOH HOH A . 
Q 8 HOH 39  539 243  HOH HOH A . 
Q 8 HOH 40  540 51   HOH HOH A . 
Q 8 HOH 41  541 74   HOH HOH A . 
Q 8 HOH 42  542 13   HOH HOH A . 
Q 8 HOH 43  543 17   HOH HOH A . 
Q 8 HOH 44  544 24   HOH HOH A . 
Q 8 HOH 45  545 16   HOH HOH A . 
Q 8 HOH 46  546 25   HOH HOH A . 
Q 8 HOH 47  547 144  HOH HOH A . 
Q 8 HOH 48  548 253  HOH HOH A . 
Q 8 HOH 49  549 119  HOH HOH A . 
Q 8 HOH 50  550 206  HOH HOH A . 
Q 8 HOH 51  551 168  HOH HOH A . 
Q 8 HOH 52  552 178  HOH HOH A . 
Q 8 HOH 53  553 61   HOH HOH A . 
Q 8 HOH 54  554 180  HOH HOH A . 
Q 8 HOH 55  555 181  HOH HOH A . 
Q 8 HOH 56  556 81   HOH HOH A . 
Q 8 HOH 57  557 166  HOH HOH A . 
Q 8 HOH 58  558 250  HOH HOH A . 
Q 8 HOH 59  559 207  HOH HOH A . 
Q 8 HOH 60  560 92   HOH HOH A . 
Q 8 HOH 61  561 151  HOH HOH A . 
Q 8 HOH 62  562 223  HOH HOH A . 
Q 8 HOH 63  563 32   HOH HOH A . 
Q 8 HOH 64  564 210  HOH HOH A . 
Q 8 HOH 65  565 127  HOH HOH A . 
Q 8 HOH 66  566 202  HOH HOH A . 
Q 8 HOH 67  567 58   HOH HOH A . 
Q 8 HOH 68  568 105  HOH HOH A . 
Q 8 HOH 69  569 234  HOH HOH A . 
Q 8 HOH 70  570 123  HOH HOH A . 
Q 8 HOH 71  571 89   HOH HOH A . 
Q 8 HOH 72  572 39   HOH HOH A . 
Q 8 HOH 73  573 242  HOH HOH A . 
Q 8 HOH 74  574 73   HOH HOH A . 
Q 8 HOH 75  575 126  HOH HOH A . 
Q 8 HOH 76  576 205  HOH HOH A . 
Q 8 HOH 77  577 196  HOH HOH A . 
Q 8 HOH 78  578 28   HOH HOH A . 
Q 8 HOH 79  579 244  HOH HOH A . 
Q 8 HOH 80  580 97   HOH HOH A . 
Q 8 HOH 81  581 41   HOH HOH A . 
Q 8 HOH 82  582 209  HOH HOH A . 
Q 8 HOH 83  583 149  HOH HOH A . 
Q 8 HOH 84  584 115  HOH HOH A . 
Q 8 HOH 85  585 201  HOH HOH A . 
Q 8 HOH 86  586 170  HOH HOH A . 
Q 8 HOH 87  587 203  HOH HOH A . 
Q 8 HOH 88  588 152  HOH HOH A . 
Q 8 HOH 89  589 236  HOH HOH A . 
Q 8 HOH 90  590 208  HOH HOH A . 
Q 8 HOH 91  591 197  HOH HOH A . 
Q 8 HOH 92  592 218  HOH HOH A . 
Q 8 HOH 93  593 76   HOH HOH A . 
Q 8 HOH 94  594 109  HOH HOH A . 
Q 8 HOH 95  595 132  HOH HOH A . 
R 8 HOH 1   501 182  HOH HOH B . 
R 8 HOH 2   502 174  HOH HOH B . 
R 8 HOH 3   503 224  HOH HOH B . 
R 8 HOH 4   504 106  HOH HOH B . 
R 8 HOH 5   505 252  HOH HOH B . 
R 8 HOH 6   506 163  HOH HOH B . 
R 8 HOH 7   507 66   HOH HOH B . 
R 8 HOH 8   508 235  HOH HOH B . 
R 8 HOH 9   509 80   HOH HOH B . 
R 8 HOH 10  510 14   HOH HOH B . 
R 8 HOH 11  511 15   HOH HOH B . 
R 8 HOH 12  512 26   HOH HOH B . 
R 8 HOH 13  513 216  HOH HOH B . 
R 8 HOH 14  514 35   HOH HOH B . 
R 8 HOH 15  515 34   HOH HOH B . 
R 8 HOH 16  516 104  HOH HOH B . 
R 8 HOH 17  517 78   HOH HOH B . 
R 8 HOH 18  518 11   HOH HOH B . 
R 8 HOH 19  519 53   HOH HOH B . 
R 8 HOH 20  520 65   HOH HOH B . 
R 8 HOH 21  521 188  HOH HOH B . 
R 8 HOH 22  522 184  HOH HOH B . 
R 8 HOH 23  523 215  HOH HOH B . 
R 8 HOH 24  524 8    HOH HOH B . 
R 8 HOH 25  525 23   HOH HOH B . 
R 8 HOH 26  526 40   HOH HOH B . 
R 8 HOH 27  527 5    HOH HOH B . 
R 8 HOH 28  528 85   HOH HOH B . 
R 8 HOH 29  529 86   HOH HOH B . 
R 8 HOH 30  530 99   HOH HOH B . 
R 8 HOH 31  531 55   HOH HOH B . 
R 8 HOH 32  532 7    HOH HOH B . 
R 8 HOH 33  533 96   HOH HOH B . 
R 8 HOH 34  534 118  HOH HOH B . 
R 8 HOH 35  535 240  HOH HOH B . 
R 8 HOH 36  536 141  HOH HOH B . 
R 8 HOH 37  537 103  HOH HOH B . 
R 8 HOH 38  538 2    HOH HOH B . 
R 8 HOH 39  539 247  HOH HOH B . 
R 8 HOH 40  540 12   HOH HOH B . 
R 8 HOH 41  541 59   HOH HOH B . 
R 8 HOH 42  542 239  HOH HOH B . 
R 8 HOH 43  543 200  HOH HOH B . 
R 8 HOH 44  544 98   HOH HOH B . 
R 8 HOH 45  545 19   HOH HOH B . 
R 8 HOH 46  546 29   HOH HOH B . 
R 8 HOH 47  547 4    HOH HOH B . 
R 8 HOH 48  548 198  HOH HOH B . 
R 8 HOH 49  549 147  HOH HOH B . 
R 8 HOH 50  550 212  HOH HOH B . 
R 8 HOH 51  551 113  HOH HOH B . 
R 8 HOH 52  552 169  HOH HOH B . 
R 8 HOH 53  553 192  HOH HOH B . 
R 8 HOH 54  554 186  HOH HOH B . 
R 8 HOH 55  555 171  HOH HOH B . 
R 8 HOH 56  556 220  HOH HOH B . 
R 8 HOH 57  557 90   HOH HOH B . 
R 8 HOH 58  558 124  HOH HOH B . 
R 8 HOH 59  559 121  HOH HOH B . 
R 8 HOH 60  560 111  HOH HOH B . 
R 8 HOH 61  561 173  HOH HOH B . 
R 8 HOH 62  562 219  HOH HOH B . 
R 8 HOH 63  563 101  HOH HOH B . 
R 8 HOH 64  564 187  HOH HOH B . 
R 8 HOH 65  565 60   HOH HOH B . 
R 8 HOH 66  566 9    HOH HOH B . 
R 8 HOH 67  567 21   HOH HOH B . 
R 8 HOH 68  568 227  HOH HOH B . 
R 8 HOH 69  569 237  HOH HOH B . 
R 8 HOH 70  570 107  HOH HOH B . 
R 8 HOH 71  571 142  HOH HOH B . 
R 8 HOH 72  572 254  HOH HOH B . 
R 8 HOH 73  573 164  HOH HOH B . 
R 8 HOH 74  574 155  HOH HOH B . 
R 8 HOH 75  575 63   HOH HOH B . 
R 8 HOH 76  576 56   HOH HOH B . 
R 8 HOH 77  577 112  HOH HOH B . 
R 8 HOH 78  578 116  HOH HOH B . 
R 8 HOH 79  579 257  HOH HOH B . 
R 8 HOH 80  580 87   HOH HOH B . 
R 8 HOH 81  581 100  HOH HOH B . 
R 8 HOH 82  582 191  HOH HOH B . 
R 8 HOH 83  583 259  HOH HOH B . 
R 8 HOH 84  584 72   HOH HOH B . 
R 8 HOH 85  585 30   HOH HOH B . 
R 8 HOH 86  586 241  HOH HOH B . 
R 8 HOH 87  587 161  HOH HOH B . 
R 8 HOH 88  588 249  HOH HOH B . 
R 8 HOH 89  589 251  HOH HOH B . 
R 8 HOH 90  590 143  HOH HOH B . 
R 8 HOH 91  591 213  HOH HOH B . 
R 8 HOH 92  592 211  HOH HOH B . 
R 8 HOH 93  593 255  HOH HOH B . 
R 8 HOH 94  594 162  HOH HOH B . 
R 8 HOH 95  595 129  HOH HOH B . 
R 8 HOH 96  596 238  HOH HOH B . 
R 8 HOH 97  597 222  HOH HOH B . 
R 8 HOH 98  598 258  HOH HOH B . 
R 8 HOH 99  599 256  HOH HOH B . 
R 8 HOH 100 600 177  HOH HOH B . 
R 8 HOH 101 601 120  HOH HOH B . 
R 8 HOH 102 602 125  HOH HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1   1 Y 1 A ARG 70  ? CG  ? A ARG 6   CG  
2   1 Y 1 A ARG 70  ? CD  ? A ARG 6   CD  
3   1 Y 1 A ARG 70  ? NE  ? A ARG 6   NE  
4   1 Y 1 A ARG 70  ? CZ  ? A ARG 6   CZ  
5   1 Y 1 A ARG 70  ? NH1 ? A ARG 6   NH1 
6   1 Y 1 A ARG 70  ? NH2 ? A ARG 6   NH2 
7   1 Y 1 A LYS 72  ? CG  ? A LYS 8   CG  
8   1 Y 1 A LYS 72  ? CD  ? A LYS 8   CD  
9   1 Y 1 A LYS 72  ? CE  ? A LYS 8   CE  
10  1 Y 1 A LYS 72  ? NZ  ? A LYS 8   NZ  
11  1 Y 1 A LYS 75  ? CG  ? A LYS 11  CG  
12  1 Y 1 A LYS 75  ? CD  ? A LYS 11  CD  
13  1 Y 1 A LYS 75  ? CE  ? A LYS 11  CE  
14  1 Y 1 A LYS 75  ? NZ  ? A LYS 11  NZ  
15  1 Y 1 A GLN 79  ? CG  ? A GLN 15  CG  
16  1 Y 1 A GLN 79  ? CD  ? A GLN 15  CD  
17  1 Y 1 A GLN 79  ? OE1 ? A GLN 15  OE1 
18  1 Y 1 A GLN 79  ? NE2 ? A GLN 15  NE2 
19  1 Y 1 A GLU 81  ? CG  ? A GLU 17  CG  
20  1 Y 1 A GLU 81  ? CD  ? A GLU 17  CD  
21  1 Y 1 A GLU 81  ? OE1 ? A GLU 17  OE1 
22  1 Y 1 A GLU 81  ? OE2 ? A GLU 17  OE2 
23  1 Y 1 A VAL 82  ? CG1 ? A VAL 18  CG1 
24  1 Y 1 A VAL 82  ? CG2 ? A VAL 18  CG2 
25  1 Y 1 A ASN 83  ? CG  ? A ASN 19  CG  
26  1 Y 1 A ASN 83  ? OD1 ? A ASN 19  OD1 
27  1 Y 1 A ASN 83  ? ND2 ? A ASN 19  ND2 
28  1 Y 1 A ARG 84  ? CG  ? A ARG 20  CG  
29  1 Y 1 A ARG 84  ? CD  ? A ARG 20  CD  
30  1 Y 1 A ARG 84  ? NE  ? A ARG 20  NE  
31  1 Y 1 A ARG 84  ? CZ  ? A ARG 20  CZ  
32  1 Y 1 A ARG 84  ? NH1 ? A ARG 20  NH1 
33  1 Y 1 A ARG 84  ? NH2 ? A ARG 20  NH2 
34  1 Y 1 A MET 85  ? CG  ? A MET 21  CG  
35  1 Y 1 A MET 85  ? SD  ? A MET 21  SD  
36  1 Y 1 A MET 85  ? CE  ? A MET 21  CE  
37  1 Y 1 A LYS 87  ? CG  ? A LYS 23  CG  
38  1 Y 1 A LYS 87  ? CD  ? A LYS 23  CD  
39  1 Y 1 A LYS 87  ? CE  ? A LYS 23  CE  
40  1 Y 1 A LYS 87  ? NZ  ? A LYS 23  NZ  
41  1 Y 1 A LEU 88  ? CG  ? A LEU 24  CG  
42  1 Y 1 A LEU 88  ? CD1 ? A LEU 24  CD1 
43  1 Y 1 A LEU 88  ? CD2 ? A LEU 24  CD2 
44  1 Y 1 A ILE 89  ? CG1 ? A ILE 25  CG1 
45  1 Y 1 A ILE 89  ? CG2 ? A ILE 25  CG2 
46  1 Y 1 A ILE 89  ? CD1 ? A ILE 25  CD1 
47  1 Y 1 A ILE 90  ? CG1 ? A ILE 26  CG1 
48  1 Y 1 A ILE 90  ? CG2 ? A ILE 26  CG2 
49  1 Y 1 A ILE 90  ? CD1 ? A ILE 26  CD1 
50  1 Y 1 A ASN 91  ? CG  ? A ASN 27  CG  
51  1 Y 1 A ASN 91  ? OD1 ? A ASN 27  OD1 
52  1 Y 1 A ASN 91  ? ND2 ? A ASN 27  ND2 
53  1 Y 1 A TYR 94  ? CG  ? A TYR 30  CG  
54  1 Y 1 A TYR 94  ? CD1 ? A TYR 30  CD1 
55  1 Y 1 A TYR 94  ? CD2 ? A TYR 30  CD2 
56  1 Y 1 A TYR 94  ? CE1 ? A TYR 30  CE1 
57  1 Y 1 A TYR 94  ? CE2 ? A TYR 30  CE2 
58  1 Y 1 A TYR 94  ? CZ  ? A TYR 30  CZ  
59  1 Y 1 A TYR 94  ? OH  ? A TYR 30  OH  
60  1 Y 1 A LYS 95  ? CG  ? A LYS 31  CG  
61  1 Y 1 A LYS 95  ? CD  ? A LYS 31  CD  
62  1 Y 1 A LYS 95  ? CE  ? A LYS 31  CE  
63  1 Y 1 A LYS 95  ? NZ  ? A LYS 31  NZ  
64  1 Y 0 A ILE 118 ? N   B A ILE 54  N   
65  1 Y 0 A ILE 118 ? CA  B A ILE 54  CA  
66  1 Y 0 A ILE 118 ? C   B A ILE 54  C   
67  1 Y 0 A ILE 118 ? O   B A ILE 54  O   
68  1 Y 0 A ILE 118 ? CB  B A ILE 54  CB  
69  1 Y 0 A ILE 118 ? CG1 B A ILE 54  CG1 
70  1 Y 0 A ILE 118 ? CG2 B A ILE 54  CG2 
71  1 Y 0 A ILE 118 ? CD1 B A ILE 54  CD1 
72  1 Y 1 A GLU 123 ? CG  ? A GLU 59  CG  
73  1 Y 1 A GLU 123 ? CD  ? A GLU 59  CD  
74  1 Y 1 A GLU 123 ? OE1 ? A GLU 59  OE1 
75  1 Y 1 A GLU 123 ? OE2 ? A GLU 59  OE2 
76  1 Y 1 A ASN 124 ? CG  ? A ASN 60  CG  
77  1 Y 1 A ASN 124 ? OD1 ? A ASN 60  OD1 
78  1 Y 1 A ASN 124 ? ND2 ? A ASN 60  ND2 
79  1 Y 1 A GLU 141 ? CG  ? A GLU 77  CG  
80  1 Y 1 A GLU 141 ? CD  ? A GLU 77  CD  
81  1 Y 1 A GLU 141 ? OE1 ? A GLU 77  OE1 
82  1 Y 1 A GLU 141 ? OE2 ? A GLU 77  OE2 
83  1 Y 1 A LYS 142 ? NZ  ? A LYS 78  NZ  
84  1 Y 1 A SER 189 ? OG  ? A SER 125 OG  
85  1 Y 1 A GLU 190 ? CG  ? A GLU 126 CG  
86  1 Y 1 A GLU 190 ? CD  ? A GLU 126 CD  
87  1 Y 1 A GLU 190 ? OE1 ? A GLU 126 OE1 
88  1 Y 1 A GLU 190 ? OE2 ? A GLU 126 OE2 
89  1 Y 1 A LEU 191 ? CG  ? A LEU 127 CG  
90  1 Y 1 A LEU 191 ? CD1 ? A LEU 127 CD1 
91  1 Y 1 A LEU 191 ? CD2 ? A LEU 127 CD2 
92  1 Y 1 A ILE 192 ? CG1 ? A ILE 128 CG1 
93  1 Y 1 A ILE 192 ? CG2 ? A ILE 128 CG2 
94  1 Y 1 A ILE 192 ? CD1 ? A ILE 128 CD1 
95  1 Y 1 A GLN 194 ? CG  ? A GLN 130 CG  
96  1 Y 1 A GLN 194 ? CD  ? A GLN 130 CD  
97  1 Y 1 A GLN 194 ? OE1 ? A GLN 130 OE1 
98  1 Y 1 A GLN 194 ? NE2 ? A GLN 130 NE2 
99  1 Y 1 A PHE 195 ? CG  ? A PHE 131 CG  
100 1 Y 1 A PHE 195 ? CD1 ? A PHE 131 CD1 
101 1 Y 1 A PHE 195 ? CD2 ? A PHE 131 CD2 
102 1 Y 1 A PHE 195 ? CE1 ? A PHE 131 CE1 
103 1 Y 1 A PHE 195 ? CE2 ? A PHE 131 CE2 
104 1 Y 1 A PHE 195 ? CZ  ? A PHE 131 CZ  
105 1 Y 1 A VAL 197 ? CG1 ? A VAL 133 CG1 
106 1 Y 1 A VAL 197 ? CG2 ? A VAL 133 CG2 
107 1 Y 1 A GLU 253 ? CG  ? A GLU 189 CG  
108 1 Y 1 A GLU 253 ? CD  ? A GLU 189 CD  
109 1 Y 1 A GLU 253 ? OE1 ? A GLU 189 OE1 
110 1 Y 1 A GLU 253 ? OE2 ? A GLU 189 OE2 
111 1 Y 1 A SER 256 ? OG  ? A SER 192 OG  
112 1 Y 1 A GLN 273 ? CG  ? A GLN 209 CG  
113 1 Y 1 A GLN 273 ? CD  ? A GLN 209 CD  
114 1 Y 1 A GLN 273 ? OE1 ? A GLN 209 OE1 
115 1 Y 1 A GLN 273 ? NE2 ? A GLN 209 NE2 
116 1 Y 1 A PHE 274 ? CG  ? A PHE 210 CG  
117 1 Y 1 A PHE 274 ? CD1 ? A PHE 210 CD1 
118 1 Y 1 A PHE 274 ? CD2 ? A PHE 210 CD2 
119 1 Y 1 A PHE 274 ? CE1 ? A PHE 210 CE1 
120 1 Y 1 A PHE 274 ? CE2 ? A PHE 210 CE2 
121 1 Y 1 A PHE 274 ? CZ  ? A PHE 210 CZ  
122 1 Y 1 A ILE 275 ? CG1 ? A ILE 211 CG1 
123 1 Y 1 A ILE 275 ? CG2 ? A ILE 211 CG2 
124 1 Y 1 A ILE 275 ? CD1 ? A ILE 211 CD1 
125 1 Y 1 A LYS 285 ? CG  ? A LYS 221 CG  
126 1 Y 1 A LYS 285 ? CD  ? A LYS 221 CD  
127 1 Y 1 A LYS 285 ? CE  ? A LYS 221 CE  
128 1 Y 1 A LYS 285 ? NZ  ? A LYS 221 NZ  
129 1 Y 1 A LYS 328 ? CG  ? A LYS 227 CG  
130 1 Y 1 A LYS 328 ? CD  ? A LYS 227 CD  
131 1 Y 1 A LYS 328 ? CE  ? A LYS 227 CE  
132 1 Y 1 A LYS 328 ? NZ  ? A LYS 227 NZ  
133 1 Y 1 A VAL 330 ? CG1 ? A VAL 229 CG1 
134 1 Y 1 A VAL 330 ? CG2 ? A VAL 229 CG2 
135 1 Y 1 B HIS 67  ? CG  ? B HIS 3   CG  
136 1 Y 1 B HIS 67  ? ND1 ? B HIS 3   ND1 
137 1 Y 1 B HIS 67  ? CD2 ? B HIS 3   CD2 
138 1 Y 1 B HIS 67  ? CE1 ? B HIS 3   CE1 
139 1 Y 1 B HIS 67  ? NE2 ? B HIS 3   NE2 
140 1 Y 1 B MET 68  ? CG  ? B MET 4   CG  
141 1 Y 1 B MET 68  ? SD  ? B MET 4   SD  
142 1 Y 1 B MET 68  ? CE  ? B MET 4   CE  
143 1 Y 1 B LEU 69  ? CG  ? B LEU 5   CG  
144 1 Y 1 B LEU 69  ? CD1 ? B LEU 5   CD1 
145 1 Y 1 B LEU 69  ? CD2 ? B LEU 5   CD2 
146 1 Y 1 B GLU 71  ? CG  ? B GLU 7   CG  
147 1 Y 1 B GLU 71  ? CD  ? B GLU 7   CD  
148 1 Y 1 B GLU 71  ? OE1 ? B GLU 7   OE1 
149 1 Y 1 B GLU 71  ? OE2 ? B GLU 7   OE2 
150 1 Y 1 B LYS 72  ? CG  ? B LYS 8   CG  
151 1 Y 1 B LYS 72  ? CD  ? B LYS 8   CD  
152 1 Y 1 B LYS 72  ? CE  ? B LYS 8   CE  
153 1 Y 1 B LYS 72  ? NZ  ? B LYS 8   NZ  
154 1 Y 1 B SER 73  ? OG  ? B SER 9   OG  
155 1 Y 1 B LYS 75  ? CG  ? B LYS 11  CG  
156 1 Y 1 B LYS 75  ? CD  ? B LYS 11  CD  
157 1 Y 1 B LYS 75  ? CE  ? B LYS 11  CE  
158 1 Y 1 B LYS 75  ? NZ  ? B LYS 11  NZ  
159 1 Y 1 B GLN 79  ? CG  ? B GLN 15  CG  
160 1 Y 1 B GLN 79  ? CD  ? B GLN 15  CD  
161 1 Y 1 B GLN 79  ? OE1 ? B GLN 15  OE1 
162 1 Y 1 B GLN 79  ? NE2 ? B GLN 15  NE2 
163 1 Y 1 B GLU 81  ? CG  ? B GLU 17  CG  
164 1 Y 1 B GLU 81  ? CD  ? B GLU 17  CD  
165 1 Y 1 B GLU 81  ? OE1 ? B GLU 17  OE1 
166 1 Y 1 B GLU 81  ? OE2 ? B GLU 17  OE2 
167 1 Y 1 B VAL 82  ? CG1 ? B VAL 18  CG1 
168 1 Y 1 B VAL 82  ? CG2 ? B VAL 18  CG2 
169 1 Y 1 B ARG 84  ? CG  ? B ARG 20  CG  
170 1 Y 1 B ARG 84  ? CD  ? B ARG 20  CD  
171 1 Y 1 B ARG 84  ? NE  ? B ARG 20  NE  
172 1 Y 1 B ARG 84  ? CZ  ? B ARG 20  CZ  
173 1 Y 1 B ARG 84  ? NH1 ? B ARG 20  NH1 
174 1 Y 1 B ARG 84  ? NH2 ? B ARG 20  NH2 
175 1 Y 1 B LYS 87  ? CG  ? B LYS 23  CG  
176 1 Y 1 B LYS 87  ? CD  ? B LYS 23  CD  
177 1 Y 1 B LYS 87  ? CE  ? B LYS 23  CE  
178 1 Y 1 B LYS 87  ? NZ  ? B LYS 23  NZ  
179 1 Y 1 B LEU 88  ? CG  ? B LEU 24  CG  
180 1 Y 1 B LEU 88  ? CD1 ? B LEU 24  CD1 
181 1 Y 1 B LEU 88  ? CD2 ? B LEU 24  CD2 
182 1 Y 1 B ILE 90  ? CG1 ? B ILE 26  CG1 
183 1 Y 1 B ILE 90  ? CG2 ? B ILE 26  CG2 
184 1 Y 1 B ILE 90  ? CD1 ? B ILE 26  CD1 
185 1 Y 1 B ASN 91  ? CG  ? B ASN 27  CG  
186 1 Y 1 B ASN 91  ? OD1 ? B ASN 27  OD1 
187 1 Y 1 B ASN 91  ? ND2 ? B ASN 27  ND2 
188 1 Y 1 B LYS 95  ? CG  ? B LYS 31  CG  
189 1 Y 1 B LYS 95  ? CD  ? B LYS 31  CD  
190 1 Y 1 B LYS 95  ? CE  ? B LYS 31  CE  
191 1 Y 1 B LYS 95  ? NZ  ? B LYS 31  NZ  
192 1 Y 1 B ILE 99  ? CG1 ? B ILE 35  CG1 
193 1 Y 1 B ILE 99  ? CG2 ? B ILE 35  CG2 
194 1 Y 1 B ILE 99  ? CD1 ? B ILE 35  CD1 
195 1 Y 1 B LYS 114 ? CD  ? B LYS 50  CD  
196 1 Y 1 B LYS 114 ? CE  ? B LYS 50  CE  
197 1 Y 1 B LYS 114 ? NZ  ? B LYS 50  NZ  
198 1 Y 0 B ILE 118 ? N   B B ILE 54  N   
199 1 Y 0 B ILE 118 ? CA  B B ILE 54  CA  
200 1 Y 0 B ILE 118 ? C   B B ILE 54  C   
201 1 Y 0 B ILE 118 ? O   B B ILE 54  O   
202 1 Y 0 B ILE 118 ? CB  B B ILE 54  CB  
203 1 Y 0 B ILE 118 ? CG1 B B ILE 54  CG1 
204 1 Y 0 B ILE 118 ? CG2 B B ILE 54  CG2 
205 1 Y 0 B ILE 118 ? CD1 B B ILE 54  CD1 
206 1 Y 1 B GLU 123 ? CG  ? B GLU 59  CG  
207 1 Y 1 B GLU 123 ? CD  ? B GLU 59  CD  
208 1 Y 1 B GLU 123 ? OE1 ? B GLU 59  OE1 
209 1 Y 1 B GLU 123 ? OE2 ? B GLU 59  OE2 
210 1 Y 1 B ASN 124 ? CG  ? B ASN 60  CG  
211 1 Y 1 B ASN 124 ? OD1 ? B ASN 60  OD1 
212 1 Y 1 B ASN 124 ? ND2 ? B ASN 60  ND2 
213 1 Y 1 B GLU 130 ? CG  ? B GLU 66  CG  
214 1 Y 1 B GLU 130 ? CD  ? B GLU 66  CD  
215 1 Y 1 B GLU 130 ? OE1 ? B GLU 66  OE1 
216 1 Y 1 B GLU 130 ? OE2 ? B GLU 66  OE2 
217 1 Y 1 B GLU 141 ? CG  ? B GLU 77  CG  
218 1 Y 1 B GLU 141 ? CD  ? B GLU 77  CD  
219 1 Y 1 B GLU 141 ? OE1 ? B GLU 77  OE1 
220 1 Y 1 B GLU 141 ? OE2 ? B GLU 77  OE2 
221 1 Y 1 B LEU 163 ? CG  ? B LEU 99  CG  
222 1 Y 1 B LEU 163 ? CD1 ? B LEU 99  CD1 
223 1 Y 1 B LEU 163 ? CD2 ? B LEU 99  CD2 
224 1 Y 1 B THR 188 ? OG1 ? B THR 124 OG1 
225 1 Y 1 B THR 188 ? CG2 ? B THR 124 CG2 
226 1 Y 1 B SER 189 ? OG  ? B SER 125 OG  
227 1 Y 1 B GLU 190 ? CG  ? B GLU 126 CG  
228 1 Y 1 B GLU 190 ? CD  ? B GLU 126 CD  
229 1 Y 1 B GLU 190 ? OE1 ? B GLU 126 OE1 
230 1 Y 1 B GLU 190 ? OE2 ? B GLU 126 OE2 
231 1 Y 1 B LEU 191 ? CG  ? B LEU 127 CG  
232 1 Y 1 B LEU 191 ? CD1 ? B LEU 127 CD1 
233 1 Y 1 B LEU 191 ? CD2 ? B LEU 127 CD2 
234 1 Y 1 B ILE 192 ? CG1 ? B ILE 128 CG1 
235 1 Y 1 B ILE 192 ? CG2 ? B ILE 128 CG2 
236 1 Y 1 B ILE 192 ? CD1 ? B ILE 128 CD1 
237 1 Y 1 B GLN 194 ? CG  ? B GLN 130 CG  
238 1 Y 1 B GLN 194 ? CD  ? B GLN 130 CD  
239 1 Y 1 B GLN 194 ? OE1 ? B GLN 130 OE1 
240 1 Y 1 B GLN 194 ? NE2 ? B GLN 130 NE2 
241 1 Y 1 B VAL 197 ? CG1 ? B VAL 133 CG1 
242 1 Y 1 B VAL 197 ? CG2 ? B VAL 133 CG2 
243 1 Y 1 B SER 227 ? OG  ? B SER 163 OG  
244 1 Y 1 B GLU 253 ? CG  ? B GLU 189 CG  
245 1 Y 1 B GLU 253 ? CD  ? B GLU 189 CD  
246 1 Y 1 B GLU 253 ? OE1 ? B GLU 189 OE1 
247 1 Y 1 B GLU 253 ? OE2 ? B GLU 189 OE2 
248 1 Y 1 B ASP 257 ? CG  ? B ASP 193 CG  
249 1 Y 1 B ASP 257 ? OD1 ? B ASP 193 OD1 
250 1 Y 1 B ASP 257 ? OD2 ? B ASP 193 OD2 
251 1 Y 1 B LYS 270 ? NZ  ? B LYS 206 NZ  
252 1 Y 1 B PHE 274 ? CG  ? B PHE 210 CG  
253 1 Y 1 B PHE 274 ? CD1 ? B PHE 210 CD1 
254 1 Y 1 B PHE 274 ? CD2 ? B PHE 210 CD2 
255 1 Y 1 B PHE 274 ? CE1 ? B PHE 210 CE1 
256 1 Y 1 B PHE 274 ? CE2 ? B PHE 210 CE2 
257 1 Y 1 B PHE 274 ? CZ  ? B PHE 210 CZ  
258 1 Y 1 B ILE 275 ? CG1 ? B ILE 211 CG1 
259 1 Y 1 B ILE 275 ? CG2 ? B ILE 211 CG2 
260 1 Y 1 B ILE 275 ? CD1 ? B ILE 211 CD1 
261 1 Y 1 B LYS 285 ? CG  ? B LYS 221 CG  
262 1 Y 1 B LYS 285 ? CD  ? B LYS 221 CD  
263 1 Y 1 B LYS 285 ? CE  ? B LYS 221 CE  
264 1 Y 1 B LYS 285 ? NZ  ? B LYS 221 NZ  
265 1 Y 1 B LYS 328 ? CG  ? B LYS 227 CG  
266 1 Y 1 B LYS 328 ? CD  ? B LYS 227 CD  
267 1 Y 1 B LYS 328 ? CE  ? B LYS 227 CE  
268 1 Y 1 B LYS 328 ? NZ  ? B LYS 227 NZ  
269 1 Y 1 B THR 329 ? OG1 ? B THR 228 OG1 
270 1 Y 1 B THR 329 ? CG2 ? B THR 228 CG2 
271 1 Y 1 B TRP 331 ? CG  ? B TRP 230 CG  
272 1 Y 1 B TRP 331 ? CD1 ? B TRP 230 CD1 
273 1 Y 1 B TRP 331 ? CD2 ? B TRP 230 CD2 
274 1 Y 1 B TRP 331 ? NE1 ? B TRP 230 NE1 
275 1 Y 1 B TRP 331 ? CE2 ? B TRP 230 CE2 
276 1 Y 1 B TRP 331 ? CE3 ? B TRP 230 CE3 
277 1 Y 1 B TRP 331 ? CZ2 ? B TRP 230 CZ2 
278 1 Y 1 B TRP 331 ? CZ3 ? B TRP 230 CZ3 
279 1 Y 1 B TRP 331 ? CH2 ? B TRP 230 CH2 
280 1 N 1 A PG4 402 ? C7  ? D PG4 1   C7  
281 1 N 1 A PG4 402 ? C8  ? D PG4 1   C8  
282 1 N 1 A PG4 402 ? O5  ? D PG4 1   O5  
283 1 N 1 A PG4 403 ? C5  ? E PG4 1   C5  
284 1 N 1 A PG4 403 ? C6  ? E PG4 1   C6  
285 1 N 1 A PG4 403 ? O4  ? E PG4 1   O4  
286 1 N 1 A PG4 403 ? C7  ? E PG4 1   C7  
287 1 N 1 A PG4 403 ? C8  ? E PG4 1   C8  
288 1 N 1 A PG4 403 ? O5  ? E PG4 1   O5  
289 1 N 1 A PG4 404 ? C5  ? F PG4 1   C5  
290 1 N 1 A PG4 404 ? C6  ? F PG4 1   C6  
291 1 N 1 A PG4 404 ? O4  ? F PG4 1   O4  
292 1 N 1 A PG4 404 ? C7  ? F PG4 1   C7  
293 1 N 1 A PG4 404 ? C8  ? F PG4 1   C8  
294 1 N 1 A PG4 404 ? O5  ? F PG4 1   O5  
295 1 N 1 B PG4 404 ? O1  ? K PG4 1   O1  
296 1 N 1 B PG4 404 ? C1  ? K PG4 1   C1  
297 1 N 1 B PG4 404 ? C2  ? K PG4 1   C2  
298 1 N 1 B PG4 404 ? C7  ? K PG4 1   C7  
299 1 N 1 B PG4 404 ? C8  ? K PG4 1   C8  
300 1 N 1 B PG4 404 ? O5  ? K PG4 1   O5  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? refinement       ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? 1.20.1_4487 1 
? 'data reduction' ? ? ? ? ? ? ? ? ? ? ? autoPROC  ? ? ? .           2 
? 'data scaling'   ? ? ? ? ? ? ? ? ? ? ? STARANISO ? ? ? .           3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? PHENIX    ? ? ? .           4 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   95.200 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8SSV 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     51.902 
_cell.length_a_esd                 ? 
_cell.length_b                     65.429 
_cell.length_b_esd                 ? 
_cell.length_c                     75.376 
_cell.length_c_esd                 ? 
_cell.volume                       254915.587 
_cell.volume_esd                   ? 
_cell.Z_PDB                        4 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8SSV 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                4 
_symmetry.space_group_name_Hall            'P 2yb' 
_symmetry.space_group_name_H-M             'P 1 21 1' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   8SSV 
_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             2.53 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          51.46 
_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              7.5 
_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    'PEG 400, Calcium acetate, HEPES' 
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            293 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     PIXEL 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'DECTRIS 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         2022-04-07 
_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   1.03317 
_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        1.03317 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   23-ID-B 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          21.27 
_reflns.entry_id                                       8SSV 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.72 
_reflns.d_resolution_low                               75.07 
_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                                     23864 
_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                           91.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                5.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          8.9 
_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                                0.051 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.997 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                0.106 
_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                                    1.72 
_reflns_shell.d_res_low                                     1.93 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           1.8 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1193 
_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                               5.2 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.655 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          66.6 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  0.821 
_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                               31.04 
_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                                 8SSV 
_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                            1.72 
_refine.ls_d_res_low                             75.07 
_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                     23857 
_refine.ls_number_reflns_R_free                  1192 
_refine.ls_number_reflns_R_work                  22665 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    44.37 
_refine.ls_percent_reflns_R_free                 5.00 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.2111 
_refine.ls_R_factor_R_free                       0.2516 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.2089 
_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       'GeoStd + Monomer Library + CDL v1.2' 
_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             1.1000 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_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                 38.9439 
_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                            0.2453 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.72 
_refine_hist.d_res_low                        75.07 
_refine_hist.number_atoms_solvent             197 
_refine_hist.number_atoms_total               3351 
_refine_hist.number_reflns_all                ? 
_refine_hist.number_reflns_obs                ? 
_refine_hist.number_reflns_R_free             ? 
_refine_hist.number_reflns_R_work             ? 
_refine_hist.R_factor_all                     ? 
_refine_hist.R_factor_obs                     ? 
_refine_hist.R_factor_R_free                  ? 
_refine_hist.R_factor_R_work                  ? 
_refine_hist.pdbx_number_residues_total       ? 
_refine_hist.pdbx_B_iso_mean_ligand           ? 
_refine_hist.pdbx_B_iso_mean_solvent          ? 
_refine_hist.pdbx_number_atoms_protein        3041 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         113 
_refine_hist.pdbx_number_atoms_lipid          ? 
_refine_hist.pdbx_number_atoms_carb           ? 
_refine_hist.pdbx_pseudo_atom_details         ? 
# 
loop_
_refine_ls_restr.pdbx_refine_id 
_refine_ls_restr.criterion 
_refine_ls_restr.dev_ideal 
_refine_ls_restr.dev_ideal_target 
_refine_ls_restr.number 
_refine_ls_restr.rejects 
_refine_ls_restr.type 
_refine_ls_restr.weight 
_refine_ls_restr.pdbx_restraint_function 
'X-RAY DIFFRACTION' ? 0.0064  ? 3254 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.9150  ? 4407 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.0535  ? 512  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.0050  ? 556  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 10.0564 ? 479  ? f_dihedral_angle_d ? ? 
# 
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' 1.72 1.79  . . 6   152  2.66  . . . . 0.3090 . . . . . . . . . . . 0.4200 
'X-RAY DIFFRACTION' 1.79 1.87  . . 23  459  8.15  . . . . 0.2720 . . . . . . . . . . . 0.3050 
'X-RAY DIFFRACTION' 1.87 1.97  . . 36  905  15.90 . . . . 0.2613 . . . . . . . . . . . 0.2836 
'X-RAY DIFFRACTION' 1.97 2.09  . . 98  1639 29.19 . . . . 0.2527 . . . . . . . . . . . 0.2827 
'X-RAY DIFFRACTION' 2.09 2.25  . . 112 2274 39.98 . . . . 0.2410 . . . . . . . . . . . 0.2257 
'X-RAY DIFFRACTION' 2.25 2.48  . . 160 2806 49.82 . . . . 0.2359 . . . . . . . . . . . 0.2894 
'X-RAY DIFFRACTION' 2.48 2.83  . . 180 3648 64.10 . . . . 0.2291 . . . . . . . . . . . 0.2872 
'X-RAY DIFFRACTION' 2.84 3.57  . . 277 5057 88.93 . . . . 0.2023 . . . . . . . . . . . 0.2643 
'X-RAY DIFFRACTION' 3.57 75.07 . . 300 5725 98.71 . . . . 0.1928 . . . . . . . . . . . 0.2256 
# 
_struct.entry_id                     8SSV 
_struct.title                        'Crystal structure of Grp94 N-terminal domain bound to the purine inhibitor PU-H71.' 
_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        8SSV 
_struct_keywords.text            'CHAPERONE, Inhibitor, GRP94' 
_struct_keywords.pdbx_keywords   CHAPERONE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 3 ? 
F N N 3 ? 
G N N 4 ? 
H N N 2 ? 
I N N 4 ? 
J N N 5 ? 
K N N 3 ? 
L N N 6 ? 
M N N 6 ? 
N N N 7 ? 
O N N 5 ? 
P N N 4 ? 
Q N N 8 ? 
R N N 8 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    ENPL_CANLF 
_struct_ref.pdbx_db_accession          P41148 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;LREKSEKFAFQAEVNRMMKLIINSLYKNKEIFLRELISNASDALDKIRLISLTDENALAGNEELTVKIKCDKEKNLLHVT
DTGVGMTREELVKNLGTIAKSGTSEFLNKMTEAQEDGQSTSELIGQFGVGFYSAFLVADKVIVTSKHNNDTQHIWESDSN
EFSVIADPRGNTLGRGTTITLVLKEEASDYLELDTIKNLVKKYSQFINFPIYVWSSKTETVEEPMEEEEAAKEEKEDSDD
EAAVEEEEEEKKPKTKKVEKTVWDWELMN
;
_struct_ref.pdbx_align_begin           69 
# 
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 8SSV A 5 ? 236 ? P41148 69 ? 337 ? 69 337 
2 1 8SSV B 5 ? 236 ? P41148 69 ? 337 ? 69 337 
# 
loop_
_struct_ref_seq_dif.align_id 
_struct_ref_seq_dif.pdbx_pdb_id_code 
_struct_ref_seq_dif.mon_id 
_struct_ref_seq_dif.pdbx_pdb_strand_id 
_struct_ref_seq_dif.seq_num 
_struct_ref_seq_dif.pdbx_pdb_ins_code 
_struct_ref_seq_dif.pdbx_seq_db_name 
_struct_ref_seq_dif.pdbx_seq_db_accession_code 
_struct_ref_seq_dif.db_mon_id 
_struct_ref_seq_dif.pdbx_seq_db_seq_num 
_struct_ref_seq_dif.details 
_struct_ref_seq_dif.pdbx_auth_seq_num 
_struct_ref_seq_dif.pdbx_ordinal 
1 8SSV GLY A 1   ? UNP P41148 ?   ?   'expression tag' 65  1  
1 8SSV SER A 2   ? UNP P41148 ?   ?   'expression tag' 66  2  
1 8SSV HIS A 3   ? UNP P41148 ?   ?   'expression tag' 67  3  
1 8SSV MET A 4   ? UNP P41148 ?   ?   'expression tag' 68  4  
1 8SSV ?   A ?   ? UNP P41148 GLU 287 deletion         ?   5  
1 8SSV ?   A ?   ? UNP P41148 THR 288 deletion         ?   6  
1 8SSV ?   A ?   ? UNP P41148 VAL 289 deletion         ?   7  
1 8SSV ?   A ?   ? UNP P41148 GLU 290 deletion         ?   8  
1 8SSV ?   A ?   ? UNP P41148 GLU 291 deletion         ?   9  
1 8SSV ?   A ?   ? UNP P41148 PRO 292 deletion         ?   10 
1 8SSV ?   A ?   ? UNP P41148 MET 293 deletion         ?   11 
1 8SSV ?   A ?   ? UNP P41148 GLU 294 deletion         ?   12 
1 8SSV ?   A ?   ? UNP P41148 GLU 295 deletion         ?   13 
1 8SSV ?   A ?   ? UNP P41148 GLU 296 deletion         ?   14 
1 8SSV ?   A ?   ? UNP P41148 GLU 297 deletion         ?   15 
1 8SSV ?   A ?   ? UNP P41148 ALA 298 deletion         ?   16 
1 8SSV ?   A ?   ? UNP P41148 ALA 299 deletion         ?   17 
1 8SSV ?   A ?   ? UNP P41148 LYS 300 deletion         ?   18 
1 8SSV ?   A ?   ? UNP P41148 GLU 301 deletion         ?   19 
1 8SSV ?   A ?   ? UNP P41148 GLU 302 deletion         ?   20 
1 8SSV ?   A ?   ? UNP P41148 LYS 303 deletion         ?   21 
1 8SSV ?   A ?   ? UNP P41148 GLU 304 deletion         ?   22 
1 8SSV ?   A ?   ? UNP P41148 ASP 305 deletion         ?   23 
1 8SSV ?   A ?   ? UNP P41148 SER 306 deletion         ?   24 
1 8SSV ?   A ?   ? UNP P41148 ASP 307 deletion         ?   25 
1 8SSV ?   A ?   ? UNP P41148 ASP 308 deletion         ?   26 
1 8SSV ?   A ?   ? UNP P41148 GLU 309 deletion         ?   27 
1 8SSV ?   A ?   ? UNP P41148 ALA 310 deletion         ?   28 
1 8SSV ?   A ?   ? UNP P41148 ALA 311 deletion         ?   29 
1 8SSV ?   A ?   ? UNP P41148 VAL 312 deletion         ?   30 
1 8SSV ?   A ?   ? UNP P41148 GLU 313 deletion         ?   31 
1 8SSV ?   A ?   ? UNP P41148 GLU 314 deletion         ?   32 
1 8SSV ?   A ?   ? UNP P41148 GLU 315 deletion         ?   33 
1 8SSV ?   A ?   ? UNP P41148 GLU 316 deletion         ?   34 
1 8SSV ?   A ?   ? UNP P41148 GLU 317 deletion         ?   35 
1 8SSV ?   A ?   ? UNP P41148 GLU 318 deletion         ?   36 
1 8SSV ?   A ?   ? UNP P41148 LYS 319 deletion         ?   37 
1 8SSV ?   A ?   ? UNP P41148 LYS 320 deletion         ?   38 
1 8SSV ?   A ?   ? UNP P41148 PRO 321 deletion         ?   39 
1 8SSV ?   A ?   ? UNP P41148 LYS 322 deletion         ?   40 
1 8SSV ?   A ?   ? UNP P41148 THR 323 deletion         ?   41 
1 8SSV GLY A 223 ? UNP P41148 LYS 324 conflict         324 42 
1 8SSV GLY A 224 ? UNP P41148 LYS 325 conflict         325 43 
1 8SSV GLY A 225 ? UNP P41148 VAL 326 conflict         326 44 
1 8SSV GLY A 226 ? UNP P41148 GLU 327 conflict         327 45 
2 8SSV GLY B 1   ? UNP P41148 ?   ?   'expression tag' 65  46 
2 8SSV SER B 2   ? UNP P41148 ?   ?   'expression tag' 66  47 
2 8SSV HIS B 3   ? UNP P41148 ?   ?   'expression tag' 67  48 
2 8SSV MET B 4   ? UNP P41148 ?   ?   'expression tag' 68  49 
2 8SSV ?   B ?   ? UNP P41148 GLU 287 deletion         ?   50 
2 8SSV ?   B ?   ? UNP P41148 THR 288 deletion         ?   51 
2 8SSV ?   B ?   ? UNP P41148 VAL 289 deletion         ?   52 
2 8SSV ?   B ?   ? UNP P41148 GLU 290 deletion         ?   53 
2 8SSV ?   B ?   ? UNP P41148 GLU 291 deletion         ?   54 
2 8SSV ?   B ?   ? UNP P41148 PRO 292 deletion         ?   55 
2 8SSV ?   B ?   ? UNP P41148 MET 293 deletion         ?   56 
2 8SSV ?   B ?   ? UNP P41148 GLU 294 deletion         ?   57 
2 8SSV ?   B ?   ? UNP P41148 GLU 295 deletion         ?   58 
2 8SSV ?   B ?   ? UNP P41148 GLU 296 deletion         ?   59 
2 8SSV ?   B ?   ? UNP P41148 GLU 297 deletion         ?   60 
2 8SSV ?   B ?   ? UNP P41148 ALA 298 deletion         ?   61 
2 8SSV ?   B ?   ? UNP P41148 ALA 299 deletion         ?   62 
2 8SSV ?   B ?   ? UNP P41148 LYS 300 deletion         ?   63 
2 8SSV ?   B ?   ? UNP P41148 GLU 301 deletion         ?   64 
2 8SSV ?   B ?   ? UNP P41148 GLU 302 deletion         ?   65 
2 8SSV ?   B ?   ? UNP P41148 LYS 303 deletion         ?   66 
2 8SSV ?   B ?   ? UNP P41148 GLU 304 deletion         ?   67 
2 8SSV ?   B ?   ? UNP P41148 ASP 305 deletion         ?   68 
2 8SSV ?   B ?   ? UNP P41148 SER 306 deletion         ?   69 
2 8SSV ?   B ?   ? UNP P41148 ASP 307 deletion         ?   70 
2 8SSV ?   B ?   ? UNP P41148 ASP 308 deletion         ?   71 
2 8SSV ?   B ?   ? UNP P41148 GLU 309 deletion         ?   72 
2 8SSV ?   B ?   ? UNP P41148 ALA 310 deletion         ?   73 
2 8SSV ?   B ?   ? UNP P41148 ALA 311 deletion         ?   74 
2 8SSV ?   B ?   ? UNP P41148 VAL 312 deletion         ?   75 
2 8SSV ?   B ?   ? UNP P41148 GLU 313 deletion         ?   76 
2 8SSV ?   B ?   ? UNP P41148 GLU 314 deletion         ?   77 
2 8SSV ?   B ?   ? UNP P41148 GLU 315 deletion         ?   78 
2 8SSV ?   B ?   ? UNP P41148 GLU 316 deletion         ?   79 
2 8SSV ?   B ?   ? UNP P41148 GLU 317 deletion         ?   80 
2 8SSV ?   B ?   ? UNP P41148 GLU 318 deletion         ?   81 
2 8SSV ?   B ?   ? UNP P41148 LYS 319 deletion         ?   82 
2 8SSV ?   B ?   ? UNP P41148 LYS 320 deletion         ?   83 
2 8SSV ?   B ?   ? UNP P41148 PRO 321 deletion         ?   84 
2 8SSV ?   B ?   ? UNP P41148 LYS 322 deletion         ?   85 
2 8SSV ?   B ?   ? UNP P41148 THR 323 deletion         ?   86 
2 8SSV GLY B 223 ? UNP P41148 LYS 324 conflict         324 87 
2 8SSV GLY B 224 ? UNP P41148 LYS 325 conflict         325 88 
2 8SSV GLY B 225 ? UNP P41148 VAL 326 conflict         326 89 
2 8SSV GLY B 226 ? UNP P41148 GLU 327 conflict         327 90 
# 
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 monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,E,F,G,Q         
2 1 B,H,I,J,K,L,M,N,O,P,R 
# 
_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 GLN A 15  ? LEU A 29  ? GLN A 79  LEU A 93  1 ? 15 
HELX_P HELX_P2  AA2 GLU A 34  ? ASP A 58  ? GLU A 98  ASP A 122 1 ? 25 
HELX_P HELX_P3  AA3 LYS A 76  ? LYS A 78  ? LYS A 140 LYS A 142 5 ? 3  
HELX_P HELX_P4  AA4 THR A 91  ? ASN A 98  ? THR A 155 ASN A 162 1 ? 8  
HELX_P HELX_P5  AA5 SER A 125 ? PHE A 131 ? SER A 189 PHE A 195 1 ? 7  
HELX_P HELX_P6  AA6 VAL A 133 ? LEU A 140 ? VAL A 197 LEU A 204 5 ? 8  
HELX_P HELX_P7  AA7 GLU A 189 ? LEU A 195 ? GLU A 253 LEU A 259 5 ? 7  
HELX_P HELX_P8  AA8 GLU A 196 ? TYR A 207 ? GLU A 260 TYR A 271 1 ? 12 
HELX_P HELX_P9  AA9 THR A 228 ? TRP A 230 ? THR A 329 TRP A 331 5 ? 3  
HELX_P HELX_P10 AB1 HIS B 3   ? GLU B 10  ? HIS B 67  GLU B 74  1 ? 8  
HELX_P HELX_P11 AB2 GLN B 15  ? LEU B 29  ? GLN B 79  LEU B 93  1 ? 15 
HELX_P HELX_P12 AB3 GLU B 34  ? ASP B 58  ? GLU B 98  ASP B 122 1 ? 25 
HELX_P HELX_P13 AB4 LYS B 76  ? LYS B 78  ? LYS B 140 LYS B 142 5 ? 3  
HELX_P HELX_P14 AB5 THR B 91  ? LYS B 97  ? THR B 155 LYS B 161 1 ? 7  
HELX_P HELX_P15 AB6 SER B 125 ? PHE B 131 ? SER B 189 PHE B 195 1 ? 7  
HELX_P HELX_P16 AB7 VAL B 133 ? LEU B 140 ? VAL B 197 LEU B 204 5 ? 8  
HELX_P HELX_P17 AB8 GLU B 189 ? LEU B 195 ? GLU B 253 LEU B 259 5 ? 7  
HELX_P HELX_P18 AB9 GLU B 196 ? TYR B 207 ? GLU B 260 TYR B 271 1 ? 12 
HELX_P HELX_P19 AC1 SER B 208 ? ILE B 211 ? SER B 272 ILE B 275 5 ? 4  
HELX_P HELX_P20 AC2 THR B 228 ? TRP B 230 ? THR B 329 TRP B 331 5 ? 3  
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1  metalc ? ? A ASN 152 O   ? ? ? 1_555 G CA  .   CA  ? ? A ASN 216 A CA  405 1_555 ? ? ? ? ? ? ? 2.643 ? ? 
metalc2  metalc ? ? A ASP 198 OD2 ? ? ? 1_555 P CA  .   CA  ? ? A ASP 262 B CA  409 2_555 ? ? ? ? ? ? ? 2.641 ? ? 
metalc3  metalc ? ? G CA  .   CA  ? ? ? 1_555 Q HOH .   O   ? ? A CA  405 A HOH 539 1_555 ? ? ? ? ? ? ? 2.492 ? ? 
metalc4  metalc ? ? G CA  .   CA  ? ? ? 2_546 B ASP 198 OD2 ? ? A CA  405 B ASP 262 1_555 ? ? ? ? ? ? ? 2.653 ? ? 
metalc5  metalc ? ? G CA  .   CA  ? ? ? 1_555 R HOH .   O   ? ? A CA  405 B HOH 573 2_556 ? ? ? ? ? ? ? 2.851 ? ? 
metalc6  metalc ? ? G CA  .   CA  ? ? ? 1_555 R HOH .   O   ? ? A CA  405 B HOH 586 2_556 ? ? ? ? ? ? ? 3.082 ? ? 
metalc7  metalc ? ? Q HOH .   O   ? ? ? 2_545 P CA  .   CA  ? ? A HOH 558 B CA  409 1_555 ? ? ? ? ? ? ? 2.501 ? ? 
metalc8  metalc ? ? B SER 45  O   ? ? ? 1_555 I CA  .   CA  ? ? B SER 109 B CA  402 1_555 ? ? ? ? ? ? ? 3.101 ? ? 
metalc9  metalc ? ? B SER 45  OG  ? ? ? 1_555 I CA  .   CA  ? ? B SER 109 B CA  402 1_555 ? ? ? ? ? ? ? 2.461 ? ? 
metalc10 metalc ? ? B ASP 49  OD2 ? ? ? 1_555 I CA  .   CA  ? ? B ASP 113 B CA  402 1_555 ? ? ? ? ? ? ? 2.939 ? ? 
metalc11 metalc ? ? B ASP 49  OD1 ? ? ? 1_555 N MG  .   MG  ? ? B ASP 113 B MG  407 1_555 ? ? ? ? ? ? ? 1.966 ? ? 
metalc12 metalc ? ? B ASN 152 O   ? ? ? 1_555 P CA  .   CA  ? ? B ASN 216 B CA  409 1_555 ? ? ? ? ? ? ? 2.495 ? ? 
metalc13 metalc ? ? I CA  .   CA  ? ? ? 1_555 R HOH .   O   ? ? B CA  402 B HOH 537 1_555 ? ? ? ? ? ? ? 3.008 ? ? 
metalc14 metalc ? ? N MG  .   MG  ? ? ? 1_555 R HOH .   O   ? ? B MG  407 B HOH 536 1_555 ? ? ? ? ? ? ? 2.474 ? ? 
metalc15 metalc ? ? O ACT .   O   ? ? ? 1_555 P CA  .   CA  ? ? B ACT 408 B CA  409 1_555 ? ? ? ? ? ? ? 2.707 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  O   ? A ASN 152 ? A ASN 216 ? 1_555 CA ? G CA . ? A CA 405 ? 1_555 O   ? Q HOH .   ? A HOH 539 ? 1_555 66.7  ? 
2  O   ? A ASN 152 ? A ASN 216 ? 1_555 CA ? G CA . ? A CA 405 ? 1_555 OD2 ? B ASP 198 ? B ASP 262 ? 1_555 55.6  ? 
3  O   ? Q HOH .   ? A HOH 539 ? 1_555 CA ? G CA . ? A CA 405 ? 1_555 OD2 ? B ASP 198 ? B ASP 262 ? 1_555 82.2  ? 
4  O   ? A ASN 152 ? A ASN 216 ? 1_555 CA ? G CA . ? A CA 405 ? 1_555 O   ? R HOH .   ? B HOH 573 ? 2_556 139.7 ? 
5  O   ? Q HOH .   ? A HOH 539 ? 1_555 CA ? G CA . ? A CA 405 ? 1_555 O   ? R HOH .   ? B HOH 573 ? 2_556 78.5  ? 
6  OD2 ? B ASP 198 ? B ASP 262 ? 1_555 CA ? G CA . ? A CA 405 ? 1_555 O   ? R HOH .   ? B HOH 573 ? 2_556 140.3 ? 
7  O   ? A ASN 152 ? A ASN 216 ? 1_555 CA ? G CA . ? A CA 405 ? 1_555 O   ? R HOH .   ? B HOH 586 ? 2_556 154.6 ? 
8  O   ? Q HOH .   ? A HOH 539 ? 1_555 CA ? G CA . ? A CA 405 ? 1_555 O   ? R HOH .   ? B HOH 586 ? 2_556 125.3 ? 
9  OD2 ? B ASP 198 ? B ASP 262 ? 1_555 CA ? G CA . ? A CA 405 ? 1_555 O   ? R HOH .   ? B HOH 586 ? 2_556 141.1 ? 
10 O   ? R HOH .   ? B HOH 573 ? 2_556 CA ? G CA . ? A CA 405 ? 1_555 O   ? R HOH .   ? B HOH 586 ? 2_556 47.0  ? 
11 OD2 ? A ASP 198 ? A ASP 262 ? 1_555 CA ? P CA . ? B CA 409 ? 2_555 O   ? Q HOH .   ? A HOH 558 ? 2_545 40.5  ? 
12 OD2 ? A ASP 198 ? A ASP 262 ? 1_555 CA ? P CA . ? B CA 409 ? 2_555 O   ? B ASN 152 ? B ASN 216 ? 1_555 37.8  ? 
13 O   ? Q HOH .   ? A HOH 558 ? 2_545 CA ? P CA . ? B CA 409 ? 2_555 O   ? B ASN 152 ? B ASN 216 ? 1_555 4.3   ? 
14 OD2 ? A ASP 198 ? A ASP 262 ? 1_555 CA ? P CA . ? B CA 409 ? 2_555 O   ? O ACT .   ? B ACT 408 ? 1_555 38.3  ? 
15 O   ? Q HOH .   ? A HOH 558 ? 2_545 CA ? P CA . ? B CA 409 ? 2_555 O   ? O ACT .   ? B ACT 408 ? 1_555 3.2   ? 
16 O   ? B ASN 152 ? B ASN 216 ? 1_555 CA ? P CA . ? B CA 409 ? 2_555 O   ? O ACT .   ? B ACT 408 ? 1_555 5.4   ? 
17 O   ? B SER 45  ? B SER 109 ? 1_555 CA ? I CA . ? B CA 402 ? 1_555 OG  ? B SER 45  ? B SER 109 ? 1_555 66.8  ? 
18 O   ? B SER 45  ? B SER 109 ? 1_555 CA ? I CA . ? B CA 402 ? 1_555 OD2 ? B ASP 49  ? B ASP 113 ? 1_555 76.1  ? 
19 OG  ? B SER 45  ? B SER 109 ? 1_555 CA ? I CA . ? B CA 402 ? 1_555 OD2 ? B ASP 49  ? B ASP 113 ? 1_555 116.4 ? 
20 O   ? B SER 45  ? B SER 109 ? 1_555 CA ? I CA . ? B CA 402 ? 1_555 O   ? R HOH .   ? B HOH 537 ? 1_555 103.8 ? 
21 OG  ? B SER 45  ? B SER 109 ? 1_555 CA ? I CA . ? B CA 402 ? 1_555 O   ? R HOH .   ? B HOH 537 ? 1_555 169.9 ? 
22 OD2 ? B ASP 49  ? B ASP 113 ? 1_555 CA ? I CA . ? B CA 402 ? 1_555 O   ? R HOH .   ? B HOH 537 ? 1_555 55.7  ? 
23 OD1 ? B ASP 49  ? B ASP 113 ? 1_555 MG ? N MG . ? B MG 407 ? 1_555 O   ? R HOH .   ? B HOH 536 ? 1_555 77.0  ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 9 ? 
AA2 ? 9 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA1 4 5 ? anti-parallel 
AA1 5 6 ? anti-parallel 
AA1 6 7 ? anti-parallel 
AA1 7 8 ? parallel      
AA1 8 9 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? anti-parallel 
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA2 7 8 ? parallel      
AA2 8 9 ? 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 LYS A 11  ? ALA A 13  ? LYS A 75  ALA A 77  
AA1 2 GLU A 165 ? ALA A 170 ? GLU A 229 ALA A 234 
AA1 3 HIS A 157 ? SER A 161 ? HIS A 221 SER A 225 
AA1 4 ALA A 142 ? LYS A 150 ? ALA A 206 LYS A 214 
AA1 5 GLY A 180 ? LEU A 187 ? GLY A 244 LEU A 251 
AA1 6 LEU A 80  ? ASP A 85  ? LEU A 144 ASP A 149 
AA1 7 VAL A 70  ? ASP A 75  ? VAL A 134 ASP A 139 
AA1 8 ILE A 215 ? TRP A 218 ? ILE A 279 TRP A 282 
AA1 9 TRP A 232 ? LEU A 234 ? TRP A 333 LEU A 335 
AA2 1 LYS B 11  ? ALA B 13  ? LYS B 75  ALA B 77  
AA2 2 GLU B 165 ? ALA B 170 ? GLU B 229 ALA B 234 
AA2 3 HIS B 157 ? SER B 161 ? HIS B 221 SER B 225 
AA2 4 ALA B 142 ? LYS B 150 ? ALA B 206 LYS B 214 
AA2 5 GLY B 180 ? LEU B 187 ? GLY B 244 LEU B 251 
AA2 6 LEU B 80  ? ASP B 85  ? LEU B 144 ASP B 149 
AA2 7 VAL B 70  ? ASP B 75  ? VAL B 134 ASP B 139 
AA2 8 ILE B 215 ? TRP B 218 ? ILE B 279 TRP B 282 
AA2 9 TRP B 232 ? LEU B 234 ? TRP B 333 LEU B 335 
# 
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 PHE A 12  ? N PHE A 76  O PHE A 166 ? O PHE A 230 
AA1 2 3 O ILE A 169 ? O ILE A 233 N ILE A 158 ? N ILE A 222 
AA1 3 4 O TRP A 159 ? O TRP A 223 N VAL A 147 ? N VAL A 211 
AA1 4 5 N ILE A 146 ? N ILE A 210 O THR A 184 ? O THR A 248 
AA1 5 6 O ILE A 183 ? O ILE A 247 N VAL A 83  ? N VAL A 147 
AA1 6 7 O LEU A 80  ? O LEU A 144 N ASP A 75  ? N ASP A 139 
AA1 7 8 N ILE A 72  ? N ILE A 136 O TYR A 216 ? O TYR A 280 
AA1 8 9 N VAL A 217 ? N VAL A 281 O GLU A 233 ? O GLU A 334 
AA2 1 2 N PHE B 12  ? N PHE B 76  O PHE B 166 ? O PHE B 230 
AA2 2 3 O ILE B 169 ? O ILE B 233 N ILE B 158 ? N ILE B 222 
AA2 3 4 O TRP B 159 ? O TRP B 223 N VAL B 147 ? N VAL B 211 
AA2 4 5 N ILE B 146 ? N ILE B 210 O THR B 184 ? O THR B 248 
AA2 5 6 O LEU B 185 ? O LEU B 249 N LEU B 81  ? N LEU B 145 
AA2 6 7 O LEU B 80  ? O LEU B 144 N ASP B 75  ? N ASP B 139 
AA2 7 8 N ILE B 72  ? N ILE B 136 O TYR B 216 ? O TYR B 280 
AA2 8 9 N VAL B 217 ? N VAL B 281 O GLU B 233 ? O GLU B 334 
# 
_pdbx_entry_details.entry_id                   8SSV 
_pdbx_entry_details.has_ligand_of_interest     Y 
_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   N 
# 
loop_
_pdbx_validate_close_contact.id 
_pdbx_validate_close_contact.PDB_model_num 
_pdbx_validate_close_contact.auth_atom_id_1 
_pdbx_validate_close_contact.auth_asym_id_1 
_pdbx_validate_close_contact.auth_comp_id_1 
_pdbx_validate_close_contact.auth_seq_id_1 
_pdbx_validate_close_contact.PDB_ins_code_1 
_pdbx_validate_close_contact.label_alt_id_1 
_pdbx_validate_close_contact.auth_atom_id_2 
_pdbx_validate_close_contact.auth_asym_id_2 
_pdbx_validate_close_contact.auth_comp_id_2 
_pdbx_validate_close_contact.auth_seq_id_2 
_pdbx_validate_close_contact.PDB_ins_code_2 
_pdbx_validate_close_contact.label_alt_id_2 
_pdbx_validate_close_contact.dist 
1 1 O B HOH 561 ? ? O B HOH 567 ? ? 2.15 
2 1 O B HOH 537 ? ? O B HOH 578 ? ? 2.16 
3 1 O B HOH 589 ? ? O B HOH 591 ? ? 2.18 
4 1 O A HOH 504 ? ? O A HOH 574 ? ? 2.18 
# 
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 ASN A 129 ? ? -164.60 114.23  
2  1 THR A 150 ? ? -94.70  50.11   
3  1 SER A 283 ? ? -101.60 62.97   
4  1 SER B 66  ? ? -114.73 -169.87 
5  1 ASN B 129 ? ? -161.59 114.65  
6  1 LYS B 161 ? ? -95.66  58.29   
7  1 ASN B 162 ? ? -92.71  32.99   
8  1 SER B 227 ? ? 81.31   -3.81   
9  1 ASN B 228 ? ? -93.50  -60.30  
10 1 SER B 272 ? ? -68.85  2.66    
# 
loop_
_space_group_symop.id 
_space_group_symop.operation_xyz 
1 x,y,z       
2 -x,y+1/2,-z 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 3.49350692489  -10.5602311252   34.4514185081  0.133277735688  ? 0.0546874967901   ? 
0.00693555456608  ? 0.00511818712699 ? 0.0330858411935   ? 0.0533003854733 ? 0.308940084853 ? -0.017126323054 ? -0.443437403645 ? 
1.38319462271  ? -0.313844105743 ? 1.25933294992   ? 0.010861007965   ? -0.151284851624  ? -0.145935735262  ? 0.226956432043   ? 
-0.0398941838762 ? -0.166444988458  ? 0.276180908363    ? 0.326201812331   ? 0.0436283153618    ? 
2  'X-RAY DIFFRACTION' ? refined 14.5082476653  -17.3362319819   35.381887483   0.147468987203  ? 0.0698033537723   ? 
-0.0221227566527  ? 0.402894527085   ? 0.0202498884663   ? 0.539833048731  ? 4.10726985687  ? 1.23571432868   ? 2.16897737581   ? 
3.42683677225  ? -0.306136336784 ? 3.01049359256   ? -0.327934125455  ? 0.261988853011   ? -0.495877142915  ? 0.0666497734631  ? 
-0.0866233299271 ? -0.416551469238  ? 0.135285927281    ? -0.0788465030691 ? -0.00961319656965  ? 
3  'X-RAY DIFFRACTION' ? refined 4.55717323304  -3.0244999848    35.5309617179  0.0675487905101 ? 0.0134640916475   ? 
-0.0215824598754  ? 0.128998430304   ? 0.0174730470719   ? 0.0901869345022 ? 0.788832664401 ? 0.066712624403  ? -0.105372008237 ? 
1.23457300911  ? 0.227378016052  ? 1.49579966962   ? -0.0616814204411 ? -0.169190115811  ? 0.207837255101   ? 0.213577037097   ? 
0.055371575422   ? -0.109047146663  ? 0.0333854914968   ? 0.322016886835   ? 0.0217204507506    ? 
4  'X-RAY DIFFRACTION' ? refined -1.86491059552 -9.74367027938   18.3785401294  0.0853269755227 ? 0.00140723831515  ? 
-0.0193782397931  ? 0.1301742346     ? -0.0243334053334  ? 0.0716022205053 ? 1.40523780554  ? 0.685717146474  ? -0.518304174314 ? 
3.39767657177  ? -0.496469766216 ? 2.81609713347   ? 0.162283222407   ? 0.192791152748   ? -0.202274309956  ? -0.112012356977  ? 
-0.0774210970936 ? 0.255433761933   ? -0.0819360107619  ? -0.211303757374  ? 0.0510790010972    ? 
5  'X-RAY DIFFRACTION' ? refined 13.0314073914  -46.8539470119   -11.8944146285 0.665568242699  ? 0.0327028148704   ? 
0.0121287185101   ? 0.674936950263   ? -0.0761359577526  ? 0.432678690483  ? 5.10494557271  ? 1.22423789226   ? 1.60738228529   ? 
1.07580518316  ? 0.0816797102177 ? 0.623860225116  ? 0.472068441715   ? -0.468108674401  ? -0.640365073196  ? 0.279959998491   ? 
-0.184729339477  ? 0.0874577928301  ? -0.00663666400884 ? 1.1132301989     ? -0.195187914287    ? 
6  'X-RAY DIFFRACTION' ? refined 23.5892516225  -34.7584669904   8.93747386921  0.277421649332  ? -0.250352471343   ? 
-0.043851105225   ? 0.789977601739   ? -0.0449874525814  ? 0.668207709092  ? 0.527072128081 ? -0.299274521221 ? -0.121613228872 ? 
1.47886999628  ? 0.319541785013  ? 0.0755526242326 ? 0.0396265527339  ? -0.0500791794728 ? -0.0371964151391 ? 0.00253005238146 ? 
0.174728830766   ? -0.941013886475  ? -0.233824814581   ? 0.80018686729    ? 0.177939289912     ? 
7  'X-RAY DIFFRACTION' ? refined 0.588887972436 -32.0619157283   6.82670378903  0.138311607812  ? 0.00344137105424  ? 
-0.00423237448765 ? 0.0685886787872  ? -0.0130981036977  ? 0.0737592489333 ? 0.963157874357 ? 0.122000620138  ? -0.344586433537 ? 
2.21831286303  ? -0.405967807729 ? 1.29714585473   ? -0.0256871847019 ? -0.128961062139  ? 0.0901295472154  ? 0.068902061677   ? 
0.0626916737175  ? -0.0377210695817 ? -0.0940818189561  ? 0.0136168254553  ? -0.0206774154189   ? 
8  'X-RAY DIFFRACTION' ? refined 13.8639302812  -30.6547101193   -1.04868366298 0.527303246025  ? -0.132683696354   ? 
-0.153980810257   ? 0.279302626769   ? -0.00504260076134 ? 0.27832374896   ? 0.61833317768  ? 0.458742233211  ? 0.818478586369  ? 
0.487104849472 ? 0.809590327933  ? 1.34974107457   ? -0.227240910466  ? -0.124737007687  ? 0.349917257462   ? 0.353806161606   ? 
-0.151007381193  ? -0.401429640526  ? -0.594906431129   ? 0.662423979905   ? -0.0697657599958   ? 
9  'X-RAY DIFFRACTION' ? refined 7.43628817235  -41.3446069112   3.30016329718  0.0663890501954 ? -0.00662091207353 ? 
0.0153276655052   ? 0.0967483881956  ? -0.00209165450924 ? 0.089445426797  ? 0.988301713119 ? 0.103840020527  ? -0.283279064208 ? 
1.22144671775  ? 0.248781098453  ? 2.08728144822   ? -0.0369536495444 ? -0.0577124692596 ? -0.121821054492  ? 0.0844125993534  ? 
0.0685038648655  ? -0.140803888568  ? -0.0537492723488  ? 0.246062489027   ? 0.0329041372905    ? 
10 'X-RAY DIFFRACTION' ? refined 4.24212158354  -31.0564840776   19.9060117406  0.281401225996  ? -0.0175762652974  ? 
0.0683782474265   ? 0.200094330053   ? -0.0102622391834  ? 0.143696112773  ? 2.15747660694  ? -1.03566024698  ? 1.1354443745    ? 
2.7021232636   ? -1.16501927455  ? 0.774063008374  ? 0.269548702374   ? -0.130048145422  ? 0.416878218883   ? 0.247281304769   ? 
-0.211029471777  ? -0.330074169311  ? -0.138472297915   ? 0.253445933532   ? -0.000703150530206 ? 
11 'X-RAY DIFFRACTION' ? refined -6.31395494119 -37.17242511     18.216043634   0.199166793133  ? -0.0432898239491  ? 
-0.0136202011105  ? 0.181504930818   ? 0.0101402711917   ? 0.107581494037  ? 1.20802900594  ? -1.72594602963  ? 0.294280955958  ? 
3.3105430375   ? -0.3146269382   ? 2.64482152365   ? 0.118550194745   ? -0.0575900826094 ? -0.0352494490724 ? -0.316010172943  ? 
-0.0346072181713 ? -0.0715504833296 ? 0.547848710872    ? -0.60211921007   ? -0.109141248639    ? 
12 'X-RAY DIFFRACTION' ? refined -4.78307691613 -0.0998729469685 29.3767740313  0.195555590478  ? 0.0628476249583   ? 
-0.105850374012   ? 0.423152688494   ? -0.0346945168896  ? 0.127527036446  ? 4.4803100745   ? -2.7617081129   ? 5.28512408126   ? 
2.49642990163  ? -3.74531612846  ? 6.53200708001   ? 0.427658903769   ? 0.700623089773   ? -0.724060203615  ? -0.782466127443  ? 
0.0410663177259  ? 0.569749229565   ? 0.553987408023    ? -0.26485838819   ? -0.590172672095    ? 
13 'X-RAY DIFFRACTION' ? refined -4.33531519658 -42.5371468692   8.69074007557  0.19215726203   ? -0.130658675166   ? 
-0.147785192162   ? 0.451643722248   ? -0.0130485869752  ? 0.15653605548   ? 1.1197919275   ? 1.26075320511   ? 0.23722297166   ? 
1.63596717826  ? 0.299992466468  ? 0.196810166673  ? -0.0237148982893 ? -0.14017538268   ? 0.401727953579   ? -0.0378995095381 ? 
-0.187453046082  ? 0.330902924806   ? -0.0483651397336  ? -0.182874542317  ? -0.0296678559456   ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  A 1   A 70  ? A 92  A 161 ? ? 
;chain 'A' and (resid 70 through 161 )
;
2  'X-RAY DIFFRACTION' 2  A 93  A 162 ? A 104 A 197 ? ? 
;chain 'A' and (resid 162 through 197 )
;
3  'X-RAY DIFFRACTION' 3  A 105 A 198 ? A 167 A 260 ? ? 
;chain 'A' and (resid 198 through 260 )
;
4  'X-RAY DIFFRACTION' 4  A 168 A 261 ? A 203 A 337 ? ? 
;chain 'A' and (resid 261 through 337 )
;
5  'X-RAY DIFFRACTION' 5  F 1   B 65  ? F 15  B 79  ? ? 
;chain 'B' and (resid 65 through 79 )
;
6  'X-RAY DIFFRACTION' 6  F 16  B 80  ? F 33  B 97  ? ? 
;chain 'B' and (resid 80 through 97 )
;
7  'X-RAY DIFFRACTION' 7  F 34  B 98  ? F 91  B 155 ? ? 
;chain 'B' and (resid 98 through 155 )
;
8  'X-RAY DIFFRACTION' 8  F 92  B 156 ? F 110 B 197 ? ? 
;chain 'B' and (resid 156 through 197 )
;
9  'X-RAY DIFFRACTION' 9  F 111 B 198 ? F 173 B 260 ? ? 
;chain 'B' and (resid 198 through 260 )
;
10 'X-RAY DIFFRACTION' 10 F 174 B 261 ? F 190 B 277 ? ? 
;chain 'B' and (resid 261 through 277 )
;
11 'X-RAY DIFFRACTION' 11 F 191 B 278 ? F 209 B 337 ? ? 
;chain 'B' and (resid 278 through 337 )
;
12 'X-RAY DIFFRACTION' 12 C ?   A 501 ? E ?   A 701 ? ? 
;chain 'A' and (resid 501 through 801)
;
13 'X-RAY DIFFRACTION' 13 I ?   B 601 ? L ?   B 901 ? ? 
;chain 'B' and (resid 601 through 901)
;
# 
_pdbx_distant_solvent_atoms.id                                1 
_pdbx_distant_solvent_atoms.PDB_model_num                     1 
_pdbx_distant_solvent_atoms.auth_atom_id                      O 
_pdbx_distant_solvent_atoms.label_alt_id                      ? 
_pdbx_distant_solvent_atoms.auth_asym_id                      A 
_pdbx_distant_solvent_atoms.auth_comp_id                      HOH 
_pdbx_distant_solvent_atoms.auth_seq_id                       595 
_pdbx_distant_solvent_atoms.PDB_ins_code                      ? 
_pdbx_distant_solvent_atoms.neighbor_macromolecule_distance   6.72 
_pdbx_distant_solvent_atoms.neighbor_ligand_distance          . 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 65  ? A GLY 1   
2  1 Y 1 A SER 66  ? A SER 2   
3  1 Y 1 A HIS 67  ? A HIS 3   
4  1 Y 1 A MET 68  ? A MET 4   
5  1 Y 1 A LEU 69  ? A LEU 5   
6  1 Y 1 A GLY 164 ? A GLY 100 
7  1 Y 1 A THR 165 ? A THR 101 
8  1 Y 1 A ILE 166 ? A ILE 102 
9  1 Y 1 A ALA 167 ? A ALA 103 
10 1 Y 1 A LYS 168 ? A LYS 104 
11 1 Y 1 A SER 169 ? A SER 105 
12 1 Y 1 A GLY 170 ? A GLY 106 
13 1 Y 1 A THR 171 ? A THR 107 
14 1 Y 1 A SER 172 ? A SER 108 
15 1 Y 1 A GLU 173 ? A GLU 109 
16 1 Y 1 A PHE 174 ? A PHE 110 
17 1 Y 1 A LEU 175 ? A LEU 111 
18 1 Y 1 A ASN 176 ? A ASN 112 
19 1 Y 1 A LYS 177 ? A LYS 113 
20 1 Y 1 A MET 178 ? A MET 114 
21 1 Y 1 A THR 179 ? A THR 115 
22 1 Y 1 A GLU 180 ? A GLU 116 
23 1 Y 1 A ALA 181 ? A ALA 117 
24 1 Y 1 A GLN 182 ? A GLN 118 
25 1 Y 1 A GLU 183 ? A GLU 119 
26 1 Y 1 A ASP 184 ? A ASP 120 
27 1 Y 1 A GLY 185 ? A GLY 121 
28 1 Y 1 A GLN 186 ? A GLN 122 
29 1 Y 1 A SER 187 ? A SER 123 
30 1 Y 1 A THR 323 ? A THR 222 
31 1 Y 1 A GLY 324 ? A GLY 223 
32 1 Y 1 A GLY 325 ? A GLY 224 
33 1 Y 1 A GLY 326 ? A GLY 225 
34 1 Y 1 B THR 165 ? B THR 101 
35 1 Y 1 B ILE 166 ? B ILE 102 
36 1 Y 1 B ALA 167 ? B ALA 103 
37 1 Y 1 B LYS 168 ? B LYS 104 
38 1 Y 1 B SER 169 ? B SER 105 
39 1 Y 1 B GLY 170 ? B GLY 106 
40 1 Y 1 B THR 171 ? B THR 107 
41 1 Y 1 B SER 172 ? B SER 108 
42 1 Y 1 B GLU 173 ? B GLU 109 
43 1 Y 1 B PHE 174 ? B PHE 110 
44 1 Y 1 B LEU 175 ? B LEU 111 
45 1 Y 1 B ASN 176 ? B ASN 112 
46 1 Y 1 B LYS 177 ? B LYS 113 
47 1 Y 1 B MET 178 ? B MET 114 
48 1 Y 1 B THR 179 ? B THR 115 
49 1 Y 1 B GLU 180 ? B GLU 116 
50 1 Y 1 B ALA 181 ? B ALA 117 
51 1 Y 1 B GLN 182 ? B GLN 118 
52 1 Y 1 B GLU 183 ? B GLU 119 
53 1 Y 1 B ASP 184 ? B ASP 120 
54 1 Y 1 B GLY 185 ? B GLY 121 
55 1 Y 1 B GLN 186 ? B GLN 122 
56 1 Y 1 B SER 187 ? B SER 123 
57 1 Y 1 B THR 323 ? B THR 222 
58 1 Y 1 B GLY 324 ? B GLY 223 
59 1 Y 1 B GLY 325 ? B GLY 224 
60 1 Y 1 B GLY 326 ? B GLY 225 
# 
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 
ACT C      C  N N 1   
ACT O      O  N N 2   
ACT OXT    O  N N 3   
ACT CH3    C  N N 4   
ACT H1     H  N N 5   
ACT H2     H  N N 6   
ACT H3     H  N N 7   
ALA N      N  N N 8   
ALA CA     C  N S 9   
ALA C      C  N N 10  
ALA O      O  N N 11  
ALA CB     C  N N 12  
ALA OXT    O  N N 13  
ALA H      H  N N 14  
ALA H2     H  N N 15  
ALA HA     H  N N 16  
ALA HB1    H  N N 17  
ALA HB2    H  N N 18  
ALA HB3    H  N N 19  
ALA HXT    H  N N 20  
ARG N      N  N N 21  
ARG CA     C  N S 22  
ARG C      C  N N 23  
ARG O      O  N N 24  
ARG CB     C  N N 25  
ARG CG     C  N N 26  
ARG CD     C  N N 27  
ARG NE     N  N N 28  
ARG CZ     C  N N 29  
ARG NH1    N  N N 30  
ARG NH2    N  N N 31  
ARG OXT    O  N N 32  
ARG H      H  N N 33  
ARG H2     H  N N 34  
ARG HA     H  N N 35  
ARG HB2    H  N N 36  
ARG HB3    H  N N 37  
ARG HG2    H  N N 38  
ARG HG3    H  N N 39  
ARG HD2    H  N N 40  
ARG HD3    H  N N 41  
ARG HE     H  N N 42  
ARG HH11   H  N N 43  
ARG HH12   H  N N 44  
ARG HH21   H  N N 45  
ARG HH22   H  N N 46  
ARG HXT    H  N N 47  
ASN N      N  N N 48  
ASN CA     C  N S 49  
ASN C      C  N N 50  
ASN O      O  N N 51  
ASN CB     C  N N 52  
ASN CG     C  N N 53  
ASN OD1    O  N N 54  
ASN ND2    N  N N 55  
ASN OXT    O  N N 56  
ASN H      H  N N 57  
ASN H2     H  N N 58  
ASN HA     H  N N 59  
ASN HB2    H  N N 60  
ASN HB3    H  N N 61  
ASN HD21   H  N N 62  
ASN HD22   H  N N 63  
ASN HXT    H  N N 64  
ASP N      N  N N 65  
ASP CA     C  N S 66  
ASP C      C  N N 67  
ASP O      O  N N 68  
ASP CB     C  N N 69  
ASP CG     C  N N 70  
ASP OD1    O  N N 71  
ASP OD2    O  N N 72  
ASP OXT    O  N N 73  
ASP H      H  N N 74  
ASP H2     H  N N 75  
ASP HA     H  N N 76  
ASP HB2    H  N N 77  
ASP HB3    H  N N 78  
ASP HD2    H  N N 79  
ASP HXT    H  N N 80  
CA  CA     CA N N 81  
CYS N      N  N N 82  
CYS CA     C  N R 83  
CYS C      C  N N 84  
CYS O      O  N N 85  
CYS CB     C  N N 86  
CYS SG     S  N N 87  
CYS OXT    O  N N 88  
CYS H      H  N N 89  
CYS H2     H  N N 90  
CYS HA     H  N N 91  
CYS HB2    H  N N 92  
CYS HB3    H  N N 93  
CYS HG     H  N N 94  
CYS HXT    H  N N 95  
GLN N      N  N N 96  
GLN CA     C  N S 97  
GLN C      C  N N 98  
GLN O      O  N N 99  
GLN CB     C  N N 100 
GLN CG     C  N N 101 
GLN CD     C  N N 102 
GLN OE1    O  N N 103 
GLN NE2    N  N N 104 
GLN OXT    O  N N 105 
GLN H      H  N N 106 
GLN H2     H  N N 107 
GLN HA     H  N N 108 
GLN HB2    H  N N 109 
GLN HB3    H  N N 110 
GLN HG2    H  N N 111 
GLN HG3    H  N N 112 
GLN HE21   H  N N 113 
GLN HE22   H  N N 114 
GLN HXT    H  N N 115 
GLU N      N  N N 116 
GLU CA     C  N S 117 
GLU C      C  N N 118 
GLU O      O  N N 119 
GLU CB     C  N N 120 
GLU CG     C  N N 121 
GLU CD     C  N N 122 
GLU OE1    O  N N 123 
GLU OE2    O  N N 124 
GLU OXT    O  N N 125 
GLU H      H  N N 126 
GLU H2     H  N N 127 
GLU HA     H  N N 128 
GLU HB2    H  N N 129 
GLU HB3    H  N N 130 
GLU HG2    H  N N 131 
GLU HG3    H  N N 132 
GLU HE2    H  N N 133 
GLU HXT    H  N N 134 
GLY N      N  N N 135 
GLY CA     C  N N 136 
GLY C      C  N N 137 
GLY O      O  N N 138 
GLY OXT    O  N N 139 
GLY H      H  N N 140 
GLY H2     H  N N 141 
GLY HA2    H  N N 142 
GLY HA3    H  N N 143 
GLY HXT    H  N N 144 
H71 C96    C  N N 145 
H71 C95    C  N N 146 
H71 C97    C  N N 147 
H71 N94    N  N N 148 
H71 C93    C  N N 149 
H71 C92    C  N N 150 
H71 C91    C  N N 151 
H71 N9     N  Y N 152 
H71 C4     C  Y N 153 
H71 N3     N  Y N 154 
H71 C2     C  Y N 155 
H71 N1     N  Y N 156 
H71 C6     C  Y N 157 
H71 N6     N  N N 158 
H71 C5     C  Y N 159 
H71 N7     N  Y N 160 
H71 C8     C  Y N 161 
H71 S      S  N N 162 
H71 "C1'"  C  Y N 163 
H71 "C6'"  C  Y N 164 
H71 "C5'"  C  Y N 165 
H71 "O3'"  O  N N 166 
H71 "C'2"  C  N N 167 
H71 "O1'"  O  N N 168 
H71 "C4'"  C  Y N 169 
H71 "C3'"  C  Y N 170 
H71 "C2'"  C  Y N 171 
H71 I      I  N N 172 
H71 H961   H  N N 173 
H71 H962   H  N N 174 
H71 H963   H  N N 175 
H71 H95    H  N N 176 
H71 H971   H  N N 177 
H71 H972   H  N N 178 
H71 H973   H  N N 179 
H71 HN94   H  N N 180 
H71 H931   H  N N 181 
H71 H932   H  N N 182 
H71 H921   H  N N 183 
H71 H922   H  N N 184 
H71 H911   H  N N 185 
H71 H912   H  N N 186 
H71 H2     H  N N 187 
H71 HN61   H  N N 188 
H71 HN62   H  N N 189 
H71 "H6'"  H  N N 190 
H71 "H'21" H  N N 191 
H71 "H'22" H  N N 192 
H71 "H3'"  H  N N 193 
HIS N      N  N N 194 
HIS CA     C  N S 195 
HIS C      C  N N 196 
HIS O      O  N N 197 
HIS CB     C  N N 198 
HIS CG     C  Y N 199 
HIS ND1    N  Y N 200 
HIS CD2    C  Y N 201 
HIS CE1    C  Y N 202 
HIS NE2    N  Y N 203 
HIS OXT    O  N N 204 
HIS H      H  N N 205 
HIS H2     H  N N 206 
HIS HA     H  N N 207 
HIS HB2    H  N N 208 
HIS HB3    H  N N 209 
HIS HD1    H  N N 210 
HIS HD2    H  N N 211 
HIS HE1    H  N N 212 
HIS HE2    H  N N 213 
HIS HXT    H  N N 214 
HOH O      O  N N 215 
HOH H1     H  N N 216 
HOH H2     H  N N 217 
ILE N      N  N N 218 
ILE CA     C  N S 219 
ILE C      C  N N 220 
ILE O      O  N N 221 
ILE CB     C  N S 222 
ILE CG1    C  N N 223 
ILE CG2    C  N N 224 
ILE CD1    C  N N 225 
ILE OXT    O  N N 226 
ILE H      H  N N 227 
ILE H2     H  N N 228 
ILE HA     H  N N 229 
ILE HB     H  N N 230 
ILE HG12   H  N N 231 
ILE HG13   H  N N 232 
ILE HG21   H  N N 233 
ILE HG22   H  N N 234 
ILE HG23   H  N N 235 
ILE HD11   H  N N 236 
ILE HD12   H  N N 237 
ILE HD13   H  N N 238 
ILE HXT    H  N N 239 
LEU N      N  N N 240 
LEU CA     C  N S 241 
LEU C      C  N N 242 
LEU O      O  N N 243 
LEU CB     C  N N 244 
LEU CG     C  N N 245 
LEU CD1    C  N N 246 
LEU CD2    C  N N 247 
LEU OXT    O  N N 248 
LEU H      H  N N 249 
LEU H2     H  N N 250 
LEU HA     H  N N 251 
LEU HB2    H  N N 252 
LEU HB3    H  N N 253 
LEU HG     H  N N 254 
LEU HD11   H  N N 255 
LEU HD12   H  N N 256 
LEU HD13   H  N N 257 
LEU HD21   H  N N 258 
LEU HD22   H  N N 259 
LEU HD23   H  N N 260 
LEU HXT    H  N N 261 
LYS N      N  N N 262 
LYS CA     C  N S 263 
LYS C      C  N N 264 
LYS O      O  N N 265 
LYS CB     C  N N 266 
LYS CG     C  N N 267 
LYS CD     C  N N 268 
LYS CE     C  N N 269 
LYS NZ     N  N N 270 
LYS OXT    O  N N 271 
LYS H      H  N N 272 
LYS H2     H  N N 273 
LYS HA     H  N N 274 
LYS HB2    H  N N 275 
LYS HB3    H  N N 276 
LYS HG2    H  N N 277 
LYS HG3    H  N N 278 
LYS HD2    H  N N 279 
LYS HD3    H  N N 280 
LYS HE2    H  N N 281 
LYS HE3    H  N N 282 
LYS HZ1    H  N N 283 
LYS HZ2    H  N N 284 
LYS HZ3    H  N N 285 
LYS HXT    H  N N 286 
MET N      N  N N 287 
MET CA     C  N S 288 
MET C      C  N N 289 
MET O      O  N N 290 
MET CB     C  N N 291 
MET CG     C  N N 292 
MET SD     S  N N 293 
MET CE     C  N N 294 
MET OXT    O  N N 295 
MET H      H  N N 296 
MET H2     H  N N 297 
MET HA     H  N N 298 
MET HB2    H  N N 299 
MET HB3    H  N N 300 
MET HG2    H  N N 301 
MET HG3    H  N N 302 
MET HE1    H  N N 303 
MET HE2    H  N N 304 
MET HE3    H  N N 305 
MET HXT    H  N N 306 
MG  MG     MG N N 307 
PEG C1     C  N N 308 
PEG O1     O  N N 309 
PEG C2     C  N N 310 
PEG O2     O  N N 311 
PEG C3     C  N N 312 
PEG C4     C  N N 313 
PEG O4     O  N N 314 
PEG H11    H  N N 315 
PEG H12    H  N N 316 
PEG HO1    H  N N 317 
PEG H21    H  N N 318 
PEG H22    H  N N 319 
PEG H31    H  N N 320 
PEG H32    H  N N 321 
PEG H41    H  N N 322 
PEG H42    H  N N 323 
PEG HO4    H  N N 324 
PG4 O1     O  N N 325 
PG4 C1     C  N N 326 
PG4 C2     C  N N 327 
PG4 O2     O  N N 328 
PG4 C3     C  N N 329 
PG4 C4     C  N N 330 
PG4 O3     O  N N 331 
PG4 C5     C  N N 332 
PG4 C6     C  N N 333 
PG4 O4     O  N N 334 
PG4 C7     C  N N 335 
PG4 C8     C  N N 336 
PG4 O5     O  N N 337 
PG4 HO1    H  N N 338 
PG4 H11    H  N N 339 
PG4 H12    H  N N 340 
PG4 H21    H  N N 341 
PG4 H22    H  N N 342 
PG4 H31    H  N N 343 
PG4 H32    H  N N 344 
PG4 H41    H  N N 345 
PG4 H42    H  N N 346 
PG4 H51    H  N N 347 
PG4 H52    H  N N 348 
PG4 H61    H  N N 349 
PG4 H62    H  N N 350 
PG4 H71    H  N N 351 
PG4 H72    H  N N 352 
PG4 H81    H  N N 353 
PG4 H82    H  N N 354 
PG4 HO5    H  N N 355 
PHE N      N  N N 356 
PHE CA     C  N S 357 
PHE C      C  N N 358 
PHE O      O  N N 359 
PHE CB     C  N N 360 
PHE CG     C  Y N 361 
PHE CD1    C  Y N 362 
PHE CD2    C  Y N 363 
PHE CE1    C  Y N 364 
PHE CE2    C  Y N 365 
PHE CZ     C  Y N 366 
PHE OXT    O  N N 367 
PHE H      H  N N 368 
PHE H2     H  N N 369 
PHE HA     H  N N 370 
PHE HB2    H  N N 371 
PHE HB3    H  N N 372 
PHE HD1    H  N N 373 
PHE HD2    H  N N 374 
PHE HE1    H  N N 375 
PHE HE2    H  N N 376 
PHE HZ     H  N N 377 
PHE HXT    H  N N 378 
PRO N      N  N N 379 
PRO CA     C  N S 380 
PRO C      C  N N 381 
PRO O      O  N N 382 
PRO CB     C  N N 383 
PRO CG     C  N N 384 
PRO CD     C  N N 385 
PRO OXT    O  N N 386 
PRO H      H  N N 387 
PRO HA     H  N N 388 
PRO HB2    H  N N 389 
PRO HB3    H  N N 390 
PRO HG2    H  N N 391 
PRO HG3    H  N N 392 
PRO HD2    H  N N 393 
PRO HD3    H  N N 394 
PRO HXT    H  N N 395 
SER N      N  N N 396 
SER CA     C  N S 397 
SER C      C  N N 398 
SER O      O  N N 399 
SER CB     C  N N 400 
SER OG     O  N N 401 
SER OXT    O  N N 402 
SER H      H  N N 403 
SER H2     H  N N 404 
SER HA     H  N N 405 
SER HB2    H  N N 406 
SER HB3    H  N N 407 
SER HG     H  N N 408 
SER HXT    H  N N 409 
THR N      N  N N 410 
THR CA     C  N S 411 
THR C      C  N N 412 
THR O      O  N N 413 
THR CB     C  N R 414 
THR OG1    O  N N 415 
THR CG2    C  N N 416 
THR OXT    O  N N 417 
THR H      H  N N 418 
THR H2     H  N N 419 
THR HA     H  N N 420 
THR HB     H  N N 421 
THR HG1    H  N N 422 
THR HG21   H  N N 423 
THR HG22   H  N N 424 
THR HG23   H  N N 425 
THR HXT    H  N N 426 
TRP N      N  N N 427 
TRP CA     C  N S 428 
TRP C      C  N N 429 
TRP O      O  N N 430 
TRP CB     C  N N 431 
TRP CG     C  Y N 432 
TRP CD1    C  Y N 433 
TRP CD2    C  Y N 434 
TRP NE1    N  Y N 435 
TRP CE2    C  Y N 436 
TRP CE3    C  Y N 437 
TRP CZ2    C  Y N 438 
TRP CZ3    C  Y N 439 
TRP CH2    C  Y N 440 
TRP OXT    O  N N 441 
TRP H      H  N N 442 
TRP H2     H  N N 443 
TRP HA     H  N N 444 
TRP HB2    H  N N 445 
TRP HB3    H  N N 446 
TRP HD1    H  N N 447 
TRP HE1    H  N N 448 
TRP HE3    H  N N 449 
TRP HZ2    H  N N 450 
TRP HZ3    H  N N 451 
TRP HH2    H  N N 452 
TRP HXT    H  N N 453 
TYR N      N  N N 454 
TYR CA     C  N S 455 
TYR C      C  N N 456 
TYR O      O  N N 457 
TYR CB     C  N N 458 
TYR CG     C  Y N 459 
TYR CD1    C  Y N 460 
TYR CD2    C  Y N 461 
TYR CE1    C  Y N 462 
TYR CE2    C  Y N 463 
TYR CZ     C  Y N 464 
TYR OH     O  N N 465 
TYR OXT    O  N N 466 
TYR H      H  N N 467 
TYR H2     H  N N 468 
TYR HA     H  N N 469 
TYR HB2    H  N N 470 
TYR HB3    H  N N 471 
TYR HD1    H  N N 472 
TYR HD2    H  N N 473 
TYR HE1    H  N N 474 
TYR HE2    H  N N 475 
TYR HH     H  N N 476 
TYR HXT    H  N N 477 
VAL N      N  N N 478 
VAL CA     C  N S 479 
VAL C      C  N N 480 
VAL O      O  N N 481 
VAL CB     C  N N 482 
VAL CG1    C  N N 483 
VAL CG2    C  N N 484 
VAL OXT    O  N N 485 
VAL H      H  N N 486 
VAL H2     H  N N 487 
VAL HA     H  N N 488 
VAL HB     H  N N 489 
VAL HG11   H  N N 490 
VAL HG12   H  N N 491 
VAL HG13   H  N N 492 
VAL HG21   H  N N 493 
VAL HG22   H  N N 494 
VAL HG23   H  N N 495 
VAL HXT    H  N N 496 
# 
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 
ACT C     O      doub N N 1   
ACT C     OXT    sing N N 2   
ACT C     CH3    sing N N 3   
ACT CH3   H1     sing N N 4   
ACT CH3   H2     sing N N 5   
ACT CH3   H3     sing N N 6   
ALA N     CA     sing N N 7   
ALA N     H      sing N N 8   
ALA N     H2     sing N N 9   
ALA CA    C      sing N N 10  
ALA CA    CB     sing N N 11  
ALA CA    HA     sing N N 12  
ALA C     O      doub N N 13  
ALA C     OXT    sing N N 14  
ALA CB    HB1    sing N N 15  
ALA CB    HB2    sing N N 16  
ALA CB    HB3    sing N N 17  
ALA OXT   HXT    sing N N 18  
ARG N     CA     sing N N 19  
ARG N     H      sing N N 20  
ARG N     H2     sing N N 21  
ARG CA    C      sing N N 22  
ARG CA    CB     sing N N 23  
ARG CA    HA     sing N N 24  
ARG C     O      doub N N 25  
ARG C     OXT    sing N N 26  
ARG CB    CG     sing N N 27  
ARG CB    HB2    sing N N 28  
ARG CB    HB3    sing N N 29  
ARG CG    CD     sing N N 30  
ARG CG    HG2    sing N N 31  
ARG CG    HG3    sing N N 32  
ARG CD    NE     sing N N 33  
ARG CD    HD2    sing N N 34  
ARG CD    HD3    sing N N 35  
ARG NE    CZ     sing N N 36  
ARG NE    HE     sing N N 37  
ARG CZ    NH1    sing N N 38  
ARG CZ    NH2    doub N N 39  
ARG NH1   HH11   sing N N 40  
ARG NH1   HH12   sing N N 41  
ARG NH2   HH21   sing N N 42  
ARG NH2   HH22   sing N N 43  
ARG OXT   HXT    sing N N 44  
ASN N     CA     sing N N 45  
ASN N     H      sing N N 46  
ASN N     H2     sing N N 47  
ASN CA    C      sing N N 48  
ASN CA    CB     sing N N 49  
ASN CA    HA     sing N N 50  
ASN C     O      doub N N 51  
ASN C     OXT    sing N N 52  
ASN CB    CG     sing N N 53  
ASN CB    HB2    sing N N 54  
ASN CB    HB3    sing N N 55  
ASN CG    OD1    doub N N 56  
ASN CG    ND2    sing N N 57  
ASN ND2   HD21   sing N N 58  
ASN ND2   HD22   sing N N 59  
ASN OXT   HXT    sing N N 60  
ASP N     CA     sing N N 61  
ASP N     H      sing N N 62  
ASP N     H2     sing N N 63  
ASP CA    C      sing N N 64  
ASP CA    CB     sing N N 65  
ASP CA    HA     sing N N 66  
ASP C     O      doub N N 67  
ASP C     OXT    sing N N 68  
ASP CB    CG     sing N N 69  
ASP CB    HB2    sing N N 70  
ASP CB    HB3    sing N N 71  
ASP CG    OD1    doub N N 72  
ASP CG    OD2    sing N N 73  
ASP OD2   HD2    sing N N 74  
ASP OXT   HXT    sing N N 75  
CYS N     CA     sing N N 76  
CYS N     H      sing N N 77  
CYS N     H2     sing N N 78  
CYS CA    C      sing N N 79  
CYS CA    CB     sing N N 80  
CYS CA    HA     sing N N 81  
CYS C     O      doub N N 82  
CYS C     OXT    sing N N 83  
CYS CB    SG     sing N N 84  
CYS CB    HB2    sing N N 85  
CYS CB    HB3    sing N N 86  
CYS SG    HG     sing N N 87  
CYS OXT   HXT    sing N N 88  
GLN N     CA     sing N N 89  
GLN N     H      sing N N 90  
GLN N     H2     sing N N 91  
GLN CA    C      sing N N 92  
GLN CA    CB     sing N N 93  
GLN CA    HA     sing N N 94  
GLN C     O      doub N N 95  
GLN C     OXT    sing N N 96  
GLN CB    CG     sing N N 97  
GLN CB    HB2    sing N N 98  
GLN CB    HB3    sing N N 99  
GLN CG    CD     sing N N 100 
GLN CG    HG2    sing N N 101 
GLN CG    HG3    sing N N 102 
GLN CD    OE1    doub N N 103 
GLN CD    NE2    sing N N 104 
GLN NE2   HE21   sing N N 105 
GLN NE2   HE22   sing N N 106 
GLN OXT   HXT    sing N N 107 
GLU N     CA     sing N N 108 
GLU N     H      sing N N 109 
GLU N     H2     sing N N 110 
GLU CA    C      sing N N 111 
GLU CA    CB     sing N N 112 
GLU CA    HA     sing N N 113 
GLU C     O      doub N N 114 
GLU C     OXT    sing N N 115 
GLU CB    CG     sing N N 116 
GLU CB    HB2    sing N N 117 
GLU CB    HB3    sing N N 118 
GLU CG    CD     sing N N 119 
GLU CG    HG2    sing N N 120 
GLU CG    HG3    sing N N 121 
GLU CD    OE1    doub N N 122 
GLU CD    OE2    sing N N 123 
GLU OE2   HE2    sing N N 124 
GLU OXT   HXT    sing N N 125 
GLY N     CA     sing N N 126 
GLY N     H      sing N N 127 
GLY N     H2     sing N N 128 
GLY CA    C      sing N N 129 
GLY CA    HA2    sing N N 130 
GLY CA    HA3    sing N N 131 
GLY C     O      doub N N 132 
GLY C     OXT    sing N N 133 
GLY OXT   HXT    sing N N 134 
H71 C96   C95    sing N N 135 
H71 C96   H961   sing N N 136 
H71 C96   H962   sing N N 137 
H71 C96   H963   sing N N 138 
H71 C95   C97    sing N N 139 
H71 C95   N94    sing N N 140 
H71 C95   H95    sing N N 141 
H71 C97   H971   sing N N 142 
H71 C97   H972   sing N N 143 
H71 C97   H973   sing N N 144 
H71 N94   C93    sing N N 145 
H71 N94   HN94   sing N N 146 
H71 C93   C92    sing N N 147 
H71 C93   H931   sing N N 148 
H71 C93   H932   sing N N 149 
H71 C92   C91    sing N N 150 
H71 C92   H921   sing N N 151 
H71 C92   H922   sing N N 152 
H71 C91   N9     sing N N 153 
H71 C91   H911   sing N N 154 
H71 C91   H912   sing N N 155 
H71 N9    C4     sing Y N 156 
H71 N9    C8     sing Y N 157 
H71 C4    N3     doub Y N 158 
H71 C4    C5     sing Y N 159 
H71 N3    C2     sing Y N 160 
H71 C2    N1     doub Y N 161 
H71 C2    H2     sing N N 162 
H71 N1    C6     sing Y N 163 
H71 C6    N6     sing N N 164 
H71 C6    C5     doub Y N 165 
H71 N6    HN61   sing N N 166 
H71 N6    HN62   sing N N 167 
H71 C5    N7     sing Y N 168 
H71 N7    C8     doub Y N 169 
H71 C8    S      sing N N 170 
H71 S     "C1'"  sing N N 171 
H71 "C1'" "C6'"  sing Y N 172 
H71 "C1'" "C2'"  doub Y N 173 
H71 "C6'" "C5'"  doub Y N 174 
H71 "C6'" "H6'"  sing N N 175 
H71 "C5'" "O3'"  sing N N 176 
H71 "C5'" "C4'"  sing Y N 177 
H71 "O3'" "C'2"  sing N N 178 
H71 "C'2" "O1'"  sing N N 179 
H71 "C'2" "H'21" sing N N 180 
H71 "C'2" "H'22" sing N N 181 
H71 "O1'" "C4'"  sing N N 182 
H71 "C4'" "C3'"  doub Y N 183 
H71 "C3'" "C2'"  sing Y N 184 
H71 "C3'" "H3'"  sing N N 185 
H71 "C2'" I      sing N N 186 
HIS N     CA     sing N N 187 
HIS N     H      sing N N 188 
HIS N     H2     sing N N 189 
HIS CA    C      sing N N 190 
HIS CA    CB     sing N N 191 
HIS CA    HA     sing N N 192 
HIS C     O      doub N N 193 
HIS C     OXT    sing N N 194 
HIS CB    CG     sing N N 195 
HIS CB    HB2    sing N N 196 
HIS CB    HB3    sing N N 197 
HIS CG    ND1    sing Y N 198 
HIS CG    CD2    doub Y N 199 
HIS ND1   CE1    doub Y N 200 
HIS ND1   HD1    sing N N 201 
HIS CD2   NE2    sing Y N 202 
HIS CD2   HD2    sing N N 203 
HIS CE1   NE2    sing Y N 204 
HIS CE1   HE1    sing N N 205 
HIS NE2   HE2    sing N N 206 
HIS OXT   HXT    sing N N 207 
HOH O     H1     sing N N 208 
HOH O     H2     sing N N 209 
ILE N     CA     sing N N 210 
ILE N     H      sing N N 211 
ILE N     H2     sing N N 212 
ILE CA    C      sing N N 213 
ILE CA    CB     sing N N 214 
ILE CA    HA     sing N N 215 
ILE C     O      doub N N 216 
ILE C     OXT    sing N N 217 
ILE CB    CG1    sing N N 218 
ILE CB    CG2    sing N N 219 
ILE CB    HB     sing N N 220 
ILE CG1   CD1    sing N N 221 
ILE CG1   HG12   sing N N 222 
ILE CG1   HG13   sing N N 223 
ILE CG2   HG21   sing N N 224 
ILE CG2   HG22   sing N N 225 
ILE CG2   HG23   sing N N 226 
ILE CD1   HD11   sing N N 227 
ILE CD1   HD12   sing N N 228 
ILE CD1   HD13   sing N N 229 
ILE OXT   HXT    sing N N 230 
LEU N     CA     sing N N 231 
LEU N     H      sing N N 232 
LEU N     H2     sing N N 233 
LEU CA    C      sing N N 234 
LEU CA    CB     sing N N 235 
LEU CA    HA     sing N N 236 
LEU C     O      doub N N 237 
LEU C     OXT    sing N N 238 
LEU CB    CG     sing N N 239 
LEU CB    HB2    sing N N 240 
LEU CB    HB3    sing N N 241 
LEU CG    CD1    sing N N 242 
LEU CG    CD2    sing N N 243 
LEU CG    HG     sing N N 244 
LEU CD1   HD11   sing N N 245 
LEU CD1   HD12   sing N N 246 
LEU CD1   HD13   sing N N 247 
LEU CD2   HD21   sing N N 248 
LEU CD2   HD22   sing N N 249 
LEU CD2   HD23   sing N N 250 
LEU OXT   HXT    sing N N 251 
LYS N     CA     sing N N 252 
LYS N     H      sing N N 253 
LYS N     H2     sing N N 254 
LYS CA    C      sing N N 255 
LYS CA    CB     sing N N 256 
LYS CA    HA     sing N N 257 
LYS C     O      doub N N 258 
LYS C     OXT    sing N N 259 
LYS CB    CG     sing N N 260 
LYS CB    HB2    sing N N 261 
LYS CB    HB3    sing N N 262 
LYS CG    CD     sing N N 263 
LYS CG    HG2    sing N N 264 
LYS CG    HG3    sing N N 265 
LYS CD    CE     sing N N 266 
LYS CD    HD2    sing N N 267 
LYS CD    HD3    sing N N 268 
LYS CE    NZ     sing N N 269 
LYS CE    HE2    sing N N 270 
LYS CE    HE3    sing N N 271 
LYS NZ    HZ1    sing N N 272 
LYS NZ    HZ2    sing N N 273 
LYS NZ    HZ3    sing N N 274 
LYS OXT   HXT    sing N N 275 
MET N     CA     sing N N 276 
MET N     H      sing N N 277 
MET N     H2     sing N N 278 
MET CA    C      sing N N 279 
MET CA    CB     sing N N 280 
MET CA    HA     sing N N 281 
MET C     O      doub N N 282 
MET C     OXT    sing N N 283 
MET CB    CG     sing N N 284 
MET CB    HB2    sing N N 285 
MET CB    HB3    sing N N 286 
MET CG    SD     sing N N 287 
MET CG    HG2    sing N N 288 
MET CG    HG3    sing N N 289 
MET SD    CE     sing N N 290 
MET CE    HE1    sing N N 291 
MET CE    HE2    sing N N 292 
MET CE    HE3    sing N N 293 
MET OXT   HXT    sing N N 294 
PEG C1    O1     sing N N 295 
PEG C1    C2     sing N N 296 
PEG C1    H11    sing N N 297 
PEG C1    H12    sing N N 298 
PEG O1    HO1    sing N N 299 
PEG C2    O2     sing N N 300 
PEG C2    H21    sing N N 301 
PEG C2    H22    sing N N 302 
PEG O2    C3     sing N N 303 
PEG C3    C4     sing N N 304 
PEG C3    H31    sing N N 305 
PEG C3    H32    sing N N 306 
PEG C4    O4     sing N N 307 
PEG C4    H41    sing N N 308 
PEG C4    H42    sing N N 309 
PEG O4    HO4    sing N N 310 
PG4 O1    C1     sing N N 311 
PG4 O1    HO1    sing N N 312 
PG4 C1    C2     sing N N 313 
PG4 C1    H11    sing N N 314 
PG4 C1    H12    sing N N 315 
PG4 C2    O2     sing N N 316 
PG4 C2    H21    sing N N 317 
PG4 C2    H22    sing N N 318 
PG4 O2    C3     sing N N 319 
PG4 C3    C4     sing N N 320 
PG4 C3    H31    sing N N 321 
PG4 C3    H32    sing N N 322 
PG4 C4    O3     sing N N 323 
PG4 C4    H41    sing N N 324 
PG4 C4    H42    sing N N 325 
PG4 O3    C5     sing N N 326 
PG4 C5    C6     sing N N 327 
PG4 C5    H51    sing N N 328 
PG4 C5    H52    sing N N 329 
PG4 C6    O4     sing N N 330 
PG4 C6    H61    sing N N 331 
PG4 C6    H62    sing N N 332 
PG4 O4    C7     sing N N 333 
PG4 C7    C8     sing N N 334 
PG4 C7    H71    sing N N 335 
PG4 C7    H72    sing N N 336 
PG4 C8    O5     sing N N 337 
PG4 C8    H81    sing N N 338 
PG4 C8    H82    sing N N 339 
PG4 O5    HO5    sing N N 340 
PHE N     CA     sing N N 341 
PHE N     H      sing N N 342 
PHE N     H2     sing N N 343 
PHE CA    C      sing N N 344 
PHE CA    CB     sing N N 345 
PHE CA    HA     sing N N 346 
PHE C     O      doub N N 347 
PHE C     OXT    sing N N 348 
PHE CB    CG     sing N N 349 
PHE CB    HB2    sing N N 350 
PHE CB    HB3    sing N N 351 
PHE CG    CD1    doub Y N 352 
PHE CG    CD2    sing Y N 353 
PHE CD1   CE1    sing Y N 354 
PHE CD1   HD1    sing N N 355 
PHE CD2   CE2    doub Y N 356 
PHE CD2   HD2    sing N N 357 
PHE CE1   CZ     doub Y N 358 
PHE CE1   HE1    sing N N 359 
PHE CE2   CZ     sing Y N 360 
PHE CE2   HE2    sing N N 361 
PHE CZ    HZ     sing N N 362 
PHE OXT   HXT    sing N N 363 
PRO N     CA     sing N N 364 
PRO N     CD     sing N N 365 
PRO N     H      sing N N 366 
PRO CA    C      sing N N 367 
PRO CA    CB     sing N N 368 
PRO CA    HA     sing N N 369 
PRO C     O      doub N N 370 
PRO C     OXT    sing N N 371 
PRO CB    CG     sing N N 372 
PRO CB    HB2    sing N N 373 
PRO CB    HB3    sing N N 374 
PRO CG    CD     sing N N 375 
PRO CG    HG2    sing N N 376 
PRO CG    HG3    sing N N 377 
PRO CD    HD2    sing N N 378 
PRO CD    HD3    sing N N 379 
PRO OXT   HXT    sing N N 380 
SER N     CA     sing N N 381 
SER N     H      sing N N 382 
SER N     H2     sing N N 383 
SER CA    C      sing N N 384 
SER CA    CB     sing N N 385 
SER CA    HA     sing N N 386 
SER C     O      doub N N 387 
SER C     OXT    sing N N 388 
SER CB    OG     sing N N 389 
SER CB    HB2    sing N N 390 
SER CB    HB3    sing N N 391 
SER OG    HG     sing N N 392 
SER OXT   HXT    sing N N 393 
THR N     CA     sing N N 394 
THR N     H      sing N N 395 
THR N     H2     sing N N 396 
THR CA    C      sing N N 397 
THR CA    CB     sing N N 398 
THR CA    HA     sing N N 399 
THR C     O      doub N N 400 
THR C     OXT    sing N N 401 
THR CB    OG1    sing N N 402 
THR CB    CG2    sing N N 403 
THR CB    HB     sing N N 404 
THR OG1   HG1    sing N N 405 
THR CG2   HG21   sing N N 406 
THR CG2   HG22   sing N N 407 
THR CG2   HG23   sing N N 408 
THR OXT   HXT    sing N N 409 
TRP N     CA     sing N N 410 
TRP N     H      sing N N 411 
TRP N     H2     sing N N 412 
TRP CA    C      sing N N 413 
TRP CA    CB     sing N N 414 
TRP CA    HA     sing N N 415 
TRP C     O      doub N N 416 
TRP C     OXT    sing N N 417 
TRP CB    CG     sing N N 418 
TRP CB    HB2    sing N N 419 
TRP CB    HB3    sing N N 420 
TRP CG    CD1    doub Y N 421 
TRP CG    CD2    sing Y N 422 
TRP CD1   NE1    sing Y N 423 
TRP CD1   HD1    sing N N 424 
TRP CD2   CE2    doub Y N 425 
TRP CD2   CE3    sing Y N 426 
TRP NE1   CE2    sing Y N 427 
TRP NE1   HE1    sing N N 428 
TRP CE2   CZ2    sing Y N 429 
TRP CE3   CZ3    doub Y N 430 
TRP CE3   HE3    sing N N 431 
TRP CZ2   CH2    doub Y N 432 
TRP CZ2   HZ2    sing N N 433 
TRP CZ3   CH2    sing Y N 434 
TRP CZ3   HZ3    sing N N 435 
TRP CH2   HH2    sing N N 436 
TRP OXT   HXT    sing N N 437 
TYR N     CA     sing N N 438 
TYR N     H      sing N N 439 
TYR N     H2     sing N N 440 
TYR CA    C      sing N N 441 
TYR CA    CB     sing N N 442 
TYR CA    HA     sing N N 443 
TYR C     O      doub N N 444 
TYR C     OXT    sing N N 445 
TYR CB    CG     sing N N 446 
TYR CB    HB2    sing N N 447 
TYR CB    HB3    sing N N 448 
TYR CG    CD1    doub Y N 449 
TYR CG    CD2    sing Y N 450 
TYR CD1   CE1    sing Y N 451 
TYR CD1   HD1    sing N N 452 
TYR CD2   CE2    doub Y N 453 
TYR CD2   HD2    sing N N 454 
TYR CE1   CZ     doub Y N 455 
TYR CE1   HE1    sing N N 456 
TYR CE2   CZ     sing Y N 457 
TYR CE2   HE2    sing N N 458 
TYR CZ    OH     sing N N 459 
TYR OH    HH     sing N N 460 
TYR OXT   HXT    sing N N 461 
VAL N     CA     sing N N 462 
VAL N     H      sing N N 463 
VAL N     H2     sing N N 464 
VAL CA    C      sing N N 465 
VAL CA    CB     sing N N 466 
VAL CA    HA     sing N N 467 
VAL C     O      doub N N 468 
VAL C     OXT    sing N N 469 
VAL CB    CG1    sing N N 470 
VAL CB    CG2    sing N N 471 
VAL CB    HB     sing N N 472 
VAL CG1   HG11   sing N N 473 
VAL CG1   HG12   sing N N 474 
VAL CG1   HG13   sing N N 475 
VAL CG2   HG21   sing N N 476 
VAL CG2   HG22   sing N N 477 
VAL CG2   HG23   sing N N 478 
VAL OXT   HXT    sing N N 479 
# 
loop_
_pdbx_audit_support.funding_organization 
_pdbx_audit_support.country 
_pdbx_audit_support.grant_number 
_pdbx_audit_support.ordinal 
'National Institutes of Health/National Cancer Institute (NIH/NCI)' 'United States' P01-CA186866 1 
'National Institutes of Health/National Cancer Institute (NIH/NCI)' 'United States' R01-CA095130 2 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   1TC0 
_pdbx_initial_refinement_model.details          ? 
# 
_space_group.name_H-M_alt     'P 1 21 1' 
_space_group.name_Hall        'P 2yb' 
_space_group.IT_number        4 
_space_group.crystal_system   monoclinic 
_space_group.id               1 
# 
_atom_sites.entry_id                    8SSV 
_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.fract_transf_matrix[1][1]   0.019267 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.001753 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.015284 
_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]   0.013322 
_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 
_atom_type.scat_dispersion_real 
_atom_type.scat_dispersion_imag 
_atom_type.scat_Cromer_Mann_a1 
_atom_type.scat_Cromer_Mann_a2 
_atom_type.scat_Cromer_Mann_a3 
_atom_type.scat_Cromer_Mann_a4 
_atom_type.scat_Cromer_Mann_b1 
_atom_type.scat_Cromer_Mann_b2 
_atom_type.scat_Cromer_Mann_b3 
_atom_type.scat_Cromer_Mann_b4 
_atom_type.scat_Cromer_Mann_c 
_atom_type.scat_source 
_atom_type.scat_dispersion_source 
C  ? ? 3.54356  2.42580  ? ? 25.62398 1.50364  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
CA ? ? 16.26893 3.65395  ? ? 3.58509  77.28589 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
I  ? ? 40.26819 12.56501 ? ? 1.42647  27.02115 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
MG ? ? 9.41153  2.53737  ? ? 2.59044  63.03566 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
N  ? ? 4.01032  2.96436  ? ? 19.97189 1.75589  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
O  ? ? 4.49882  3.47563  ? ? 15.80542 1.70748  ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
S  ? ? 9.55732  6.39887  ? ? 1.23737  29.19336 ? ? 0.0 
;2-Gaussian fit: Grosse-Kunstleve RW, Sauter NK, Adams PD: Newsletter of the IUCr Commission on Crystallographic Computing 2004, 3, 22-31.
;
? 
# 
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     . ARG A 1 6   ? 3.53788   6.69110   54.73864  1.000 60.98622  ? 70  ARG A N     1 
ATOM   2    C  CA    . ARG A 1 6   ? 3.06840   6.01021   53.53432  1.000 59.60912  ? 70  ARG A CA    1 
ATOM   3    C  C     . ARG A 1 6   ? 4.22183   5.67909   52.59976  1.000 59.34604  ? 70  ARG A C     1 
ATOM   4    O  O     . ARG A 1 6   ? 4.02978   5.55186   51.39806  1.000 58.16466  ? 70  ARG A O     1 
ATOM   5    C  CB    . ARG A 1 6   ? 2.03190   6.86539   52.79641  1.000 59.19291  ? 70  ARG A CB    1 
ATOM   6    N  N     . GLU A 1 7   ? 5.42558   5.56717   53.15677  1.000 57.01139  ? 71  GLU A N     1 
ATOM   7    C  CA    . GLU A 1 7   ? 6.62919   5.26144   52.39097  1.000 57.20930  ? 71  GLU A CA    1 
ATOM   8    C  C     . GLU A 1 7   ? 7.31714   3.99544   52.87527  1.000 58.29351  ? 71  GLU A C     1 
ATOM   9    O  O     . GLU A 1 7   ? 7.64560   3.12399   52.06193  1.000 57.89062  ? 71  GLU A O     1 
ATOM   10   C  CB    . GLU A 1 7   ? 7.59912   6.45303   52.45536  1.000 57.95613  ? 71  GLU A CB    1 
ATOM   11   C  CG    . GLU A 1 7   ? 8.69600   6.45918   51.40497  1.000 57.87292  ? 71  GLU A CG    1 
ATOM   12   C  CD    . GLU A 1 7   ? 9.50759   7.74646   51.43984  1.000 58.56462  ? 71  GLU A CD    1 
ATOM   13   O  OE1   . GLU A 1 7   ? 10.44658  7.84184   52.26295  1.000 60.18233  ? 71  GLU A OE1   1 
ATOM   14   O  OE2   . GLU A 1 7   ? 9.19908   8.66620   50.64956  1.000 57.56952  ? 71  GLU A OE2   1 
ATOM   15   N  N     . LYS A 1 8   ? 7.53131   3.86078   54.18895  1.000 52.84567  ? 72  LYS A N     1 
ATOM   16   C  CA    . LYS A 1 8   ? 8.16490   2.66327   54.72822  1.000 54.01348  ? 72  LYS A CA    1 
ATOM   17   C  C     . LYS A 1 8   ? 7.34921   1.41330   54.43878  1.000 53.23656  ? 72  LYS A C     1 
ATOM   18   O  O     . LYS A 1 8   ? 7.88393   0.30064   54.52041  1.000 53.92931  ? 72  LYS A O     1 
ATOM   19   C  CB    . LYS A 1 8   ? 8.37702   2.80790   56.23703  1.000 55.69230  ? 72  LYS A CB    1 
ATOM   20   N  N     . SER A 1 9   ? 6.06768   1.57240   54.11176  1.000 50.16862  ? 73  SER A N     1 
ATOM   21   C  CA    . SER A 1 9   ? 5.21795   0.46557   53.70184  1.000 49.35115  ? 73  SER A CA    1 
ATOM   22   C  C     . SER A 1 9   ? 5.03502   0.38150   52.19185  1.000 64.75138  ? 73  SER A C     1 
ATOM   23   O  O     . SER A 1 9   ? 4.32738   -0.51601  51.71982  1.000 64.04166  ? 73  SER A O     1 
ATOM   24   C  CB    . SER A 1 9   ? 3.85413   0.57428   54.38669  1.000 49.02994  ? 73  SER A CB    1 
ATOM   25   O  OG    . SER A 1 9   ? 4.00532   0.61840   55.79609  1.000 50.44641  ? 73  SER A OG    1 
ATOM   26   N  N     . GLU A 1 10  ? 5.65109   1.28569   51.42152  1.000 48.38088  ? 74  GLU A N     1 
ATOM   27   C  CA    . GLU A 1 10  ? 5.57337   1.22163   49.96448  1.000 47.08444  ? 74  GLU A CA    1 
ATOM   28   C  C     . GLU A 1 10  ? 6.92216   1.08550   49.27802  1.000 47.49037  ? 74  GLU A C     1 
ATOM   29   O  O     . GLU A 1 10  ? 7.01307   0.39587   48.26543  1.000 46.84162  ? 74  GLU A O     1 
ATOM   30   C  CB    . GLU A 1 10  ? 4.84302   2.45007   49.39889  1.000 45.92967  ? 74  GLU A CB    1 
ATOM   31   C  CG    . GLU A 1 10  ? 3.46147   2.67730   49.98429  1.000 45.53741  ? 74  GLU A CG    1 
ATOM   32   C  CD    . GLU A 1 10  ? 2.78081   3.90481   49.39866  1.000 44.63935  ? 74  GLU A CD    1 
ATOM   33   O  OE1   . GLU A 1 10  ? 3.47279   4.71056   48.73350  1.000 44.34058  ? 74  GLU A OE1   1 
ATOM   34   O  OE2   . GLU A 1 10  ? 1.55655   4.06665   49.61010  1.000 44.32064  ? 74  GLU A OE2   1 
ATOM   35   N  N     . LYS A 1 11  ? 7.97287   1.72206   49.78547  1.000 44.56685  ? 75  LYS A N     1 
ATOM   36   C  CA    . LYS A 1 11  ? 9.28523   1.65180   49.15246  1.000 47.89225  ? 75  LYS A CA    1 
ATOM   37   C  C     . LYS A 1 11  ? 10.08412  0.48121   49.71738  1.000 46.66200  ? 75  LYS A C     1 
ATOM   38   O  O     . LYS A 1 11  ? 10.25040  0.36460   50.93473  1.000 48.54774  ? 75  LYS A O     1 
ATOM   39   C  CB    . LYS A 1 11  ? 10.05073  2.96121   49.35259  1.000 43.60525  ? 75  LYS A CB    1 
ATOM   40   N  N     . PHE A 1 12  ? 10.57181  -0.38682  48.83328  1.000 45.02220  ? 76  PHE A N     1 
ATOM   41   C  CA    . PHE A 1 12  ? 11.44565  -1.48250  49.22782  1.000 42.17978  ? 76  PHE A CA    1 
ATOM   42   C  C     . PHE A 1 12  ? 12.64581  -1.52483  48.28952  1.000 43.39196  ? 76  PHE A C     1 
ATOM   43   O  O     . PHE A 1 12  ? 12.68817  -0.84038  47.26191  1.000 43.95094  ? 76  PHE A O     1 
ATOM   44   C  CB    . PHE A 1 12  ? 10.73902  -2.85546  49.22020  1.000 43.35021  ? 76  PHE A CB    1 
ATOM   45   C  CG    . PHE A 1 12  ? 9.29078   -2.83222  49.65868  1.000 42.75262  ? 76  PHE A CG    1 
ATOM   46   C  CD1   . PHE A 1 12  ? 8.28798   -2.36518  48.81515  1.000 42.54481  ? 76  PHE A CD1   1 
ATOM   47   C  CD2   . PHE A 1 12  ? 8.93358   -3.27404  50.92326  1.000 42.55900  ? 76  PHE A CD2   1 
ATOM   48   C  CE1   . PHE A 1 12  ? 6.95165   -2.35623  49.22046  1.000 42.30269  ? 76  PHE A CE1   1 
ATOM   49   C  CE2   . PHE A 1 12  ? 7.59608   -3.26228  51.33442  1.000 36.73427  ? 76  PHE A CE2   1 
ATOM   50   C  CZ    . PHE A 1 12  ? 6.60636   -2.79765  50.47330  1.000 35.11857  ? 76  PHE A CZ    1 
ATOM   51   N  N     . ALA A 1 13  ? 13.63343  -2.34335  48.65795  1.000 57.88435  ? 77  ALA A N     1 
ATOM   52   C  CA    . ALA A 1 13  ? 14.79996  -2.59589  47.82281  1.000 60.54519  ? 77  ALA A CA    1 
ATOM   53   C  C     . ALA A 1 13  ? 15.00502  -4.09813  47.67340  1.000 60.21699  ? 77  ALA A C     1 
ATOM   54   O  O     . ALA A 1 13  ? 14.60032  -4.88571  48.53494  1.000 59.47963  ? 77  ALA A O     1 
ATOM   55   C  CB    . ALA A 1 13  ? 16.06540  -1.94591  48.39682  1.000 63.51328  ? 77  ALA A CB    1 
ATOM   56   N  N     . PHE A 1 14  ? 15.63708  -4.48226  46.56306  1.000 48.87502  ? 78  PHE A N     1 
ATOM   57   C  CA    . PHE A 1 14  ? 15.80687  -5.88753  46.21320  1.000 47.72621  ? 78  PHE A CA    1 
ATOM   58   C  C     . PHE A 1 14  ? 16.85099  -6.55558  47.10292  1.000 53.62241  ? 78  PHE A C     1 
ATOM   59   O  O     . PHE A 1 14  ? 17.78488  -5.91558  47.59599  1.000 51.60307  ? 78  PHE A O     1 
ATOM   60   C  CB    . PHE A 1 14  ? 16.23814  -6.02412  44.75201  1.000 49.17877  ? 78  PHE A CB    1 
ATOM   61   C  CG    . PHE A 1 14  ? 15.16839  -5.66059  43.75771  1.000 46.33831  ? 78  PHE A CG    1 
ATOM   62   C  CD1   . PHE A 1 14  ? 14.21284  -6.58553  43.37380  1.000 44.08508  ? 78  PHE A CD1   1 
ATOM   63   C  CD2   . PHE A 1 14  ? 15.13567  -4.39569  43.19018  1.000 41.69575  ? 78  PHE A CD2   1 
ATOM   64   C  CE1   . PHE A 1 14  ? 13.23449  -6.25046  42.45236  1.000 38.72836  ? 78  PHE A CE1   1 
ATOM   65   C  CE2   . PHE A 1 14  ? 14.16104  -4.05761  42.26593  1.000 34.08052  ? 78  PHE A CE2   1 
ATOM   66   C  CZ    . PHE A 1 14  ? 13.21138  -4.98497  41.89856  1.000 34.32083  ? 78  PHE A CZ    1 
ATOM   67   N  N     . GLN A 1 15  ? 16.70052  -7.86696  47.28089  1.000 72.78440  ? 79  GLN A N     1 
ATOM   68   C  CA    . GLN A 1 15  ? 17.69363  -8.63926  48.01184  1.000 72.56375  ? 79  GLN A CA    1 
ATOM   69   C  C     . GLN A 1 15  ? 19.03210  -8.61499  47.27472  1.000 78.15836  ? 79  GLN A C     1 
ATOM   70   O  O     . GLN A 1 15  ? 19.10388  -8.37132  46.06597  1.000 76.56707  ? 79  GLN A O     1 
ATOM   71   C  CB    . GLN A 1 15  ? 17.22005  -10.08054 48.19803  1.000 68.18526  ? 79  GLN A CB    1 
ATOM   72   N  N     . ALA A 1 16  ? 20.10802  -8.86350  48.02847  1.000 68.89311  ? 80  ALA A N     1 
ATOM   73   C  CA    . ALA A 1 16  ? 21.44431  -8.84811  47.43982  1.000 64.19868  ? 80  ALA A CA    1 
ATOM   74   C  C     . ALA A 1 16  ? 21.57342  -9.89639  46.34319  1.000 70.32897  ? 80  ALA A C     1 
ATOM   75   O  O     . ALA A 1 16  ? 22.14932  -9.62873  45.28080  1.000 72.47088  ? 80  ALA A O     1 
ATOM   76   C  CB    . ALA A 1 16  ? 22.49819  -9.07046  48.52406  1.000 71.57285  ? 80  ALA A CB    1 
ATOM   77   N  N     . GLU A 1 17  ? 21.04637  -11.09978 46.58601  1.000 77.26203  ? 81  GLU A N     1 
ATOM   78   C  CA    . GLU A 1 17  ? 20.97174  -12.10244 45.52912  1.000 71.01684  ? 81  GLU A CA    1 
ATOM   79   C  C     . GLU A 1 17  ? 20.03726  -11.65118 44.41598  1.000 69.88939  ? 81  GLU A C     1 
ATOM   80   O  O     . GLU A 1 17  ? 20.31129  -11.88283 43.23286  1.000 72.56289  ? 81  GLU A O     1 
ATOM   81   C  CB    . GLU A 1 17  ? 20.51191  -13.44191 46.10428  1.000 69.73089  ? 81  GLU A CB    1 
ATOM   82   N  N     . VAL A 1 18  ? 18.92651  -11.00381 44.77843  1.000 97.36069  ? 82  VAL A N     1 
ATOM   83   C  CA    . VAL A 1 18  ? 17.96081  -10.54755 43.78067  1.000 91.45598  ? 82  VAL A CA    1 
ATOM   84   C  C     . VAL A 1 18  ? 18.59970  -9.52361  42.85150  1.000 89.75985  ? 82  VAL A C     1 
ATOM   85   O  O     . VAL A 1 18  ? 18.45201  -9.59412  41.62571  1.000 92.84242  ? 82  VAL A O     1 
ATOM   86   C  CB    . VAL A 1 18  ? 16.70710  -9.97768  44.46868  1.000 87.81399  ? 82  VAL A CB    1 
ATOM   87   N  N     . ASN A 1 19  ? 19.32241  -8.55574  43.42205  1.000 54.82828  ? 83  ASN A N     1 
ATOM   88   C  CA    . ASN A 1 19  ? 20.00336  -7.56305  42.59649  1.000 56.10479  ? 83  ASN A CA    1 
ATOM   89   C  C     . ASN A 1 19  ? 21.10378  -8.20491  41.75920  1.000 56.29765  ? 83  ASN A C     1 
ATOM   90   O  O     . ASN A 1 19  ? 21.31896  -7.81853  40.60469  1.000 58.12190  ? 83  ASN A O     1 
ATOM   91   C  CB    . ASN A 1 19  ? 20.56827  -6.44799  43.47492  1.000 50.83678  ? 83  ASN A CB    1 
ATOM   92   N  N     . ARG A 1 20  ? 21.80639  -9.19127  42.32177  1.000 64.98049  ? 84  ARG A N     1 
ATOM   93   C  CA    . ARG A 1 20  ? 22.85899  -9.87261  41.57446  1.000 68.24638  ? 84  ARG A CA    1 
ATOM   94   C  C     . ARG A 1 20  ? 22.29899  -10.62723 40.37482  1.000 67.01888  ? 84  ARG A C     1 
ATOM   95   O  O     . ARG A 1 20  ? 22.96558  -10.72965 39.33787  1.000 62.37578  ? 84  ARG A O     1 
ATOM   96   C  CB    . ARG A 1 20  ? 23.61922  -10.82679 42.49819  1.000 70.44534  ? 84  ARG A CB    1 
ATOM   97   N  N     . MET A 1 21  ? 21.08011  -11.15901 40.49673  1.000 57.74480  ? 85  MET A N     1 
ATOM   98   C  CA    . MET A 1 21  ? 20.46493  -11.87477 39.38496  1.000 54.69515  ? 85  MET A CA    1 
ATOM   99   C  C     . MET A 1 21  ? 20.28880  -10.97941 38.16270  1.000 53.20690  ? 85  MET A C     1 
ATOM   100  O  O     . MET A 1 21  ? 20.33400  -11.46797 37.02883  1.000 53.40727  ? 85  MET A O     1 
ATOM   101  C  CB    . MET A 1 21  ? 19.11780  -12.45674 39.81915  1.000 45.09944  ? 85  MET A CB    1 
ATOM   102  N  N     . MET A 1 22  ? 20.08053  -9.67485  38.36345  1.000 65.13107  ? 86  MET A N     1 
ATOM   103  C  CA    . MET A 1 22  ? 20.01277  -8.76841  37.22057  1.000 61.64504  ? 86  MET A CA    1 
ATOM   104  C  C     . MET A 1 22  ? 21.33406  -8.74039  36.46696  1.000 66.10520  ? 86  MET A C     1 
ATOM   105  O  O     . MET A 1 22  ? 21.35292  -8.75776  35.23088  1.000 67.14473  ? 86  MET A O     1 
ATOM   106  C  CB    . MET A 1 22  ? 19.63731  -7.35266  37.66664  1.000 64.33210  ? 86  MET A CB    1 
ATOM   107  C  CG    . MET A 1 22  ? 18.13516  -7.04939  37.74934  1.000 64.93200  ? 86  MET A CG    1 
ATOM   108  S  SD    . MET A 1 22  ? 17.20829  -8.07502  38.91561  1.000 67.65394  ? 86  MET A SD    1 
ATOM   109  C  CE    . MET A 1 22  ? 16.96219  -6.90659  40.25376  1.000 56.71046  ? 86  MET A CE    1 
ATOM   110  N  N     . LYS A 1 23  ? 22.45185  -8.70000  37.19707  1.000 78.43074  ? 87  LYS A N     1 
ATOM   111  C  CA    . LYS A 1 23  ? 23.76040  -8.67341  36.55186  1.000 79.39981  ? 87  LYS A CA    1 
ATOM   112  C  C     . LYS A 1 23  ? 23.95216  -9.86359  35.62207  1.000 79.00495  ? 87  LYS A C     1 
ATOM   113  O  O     . LYS A 1 23  ? 24.66246  -9.75830  34.61682  1.000 82.64218  ? 87  LYS A O     1 
ATOM   114  C  CB    . LYS A 1 23  ? 24.86406  -8.64341  37.60918  1.000 85.19463  ? 87  LYS A CB    1 
ATOM   115  N  N     . LEU A 1 24  ? 23.32637  -10.99758 35.93371  1.000 74.01891  ? 88  LEU A N     1 
ATOM   116  C  CA    . LEU A 1 24  ? 23.39160  -12.14697 35.04110  1.000 74.37129  ? 88  LEU A CA    1 
ATOM   117  C  C     . LEU A 1 24  ? 22.49484  -11.95930 33.82053  1.000 75.54282  ? 88  LEU A C     1 
ATOM   118  O  O     . LEU A 1 24  ? 22.93878  -12.14941 32.68410  1.000 74.45608  ? 88  LEU A O     1 
ATOM   119  C  CB    . LEU A 1 24  ? 23.00907  -13.41784 35.79884  1.000 78.06583  ? 88  LEU A CB    1 
ATOM   120  N  N     . ILE A 1 25  ? 21.23229  -11.57826 34.03462  1.000 76.15326  ? 89  ILE A N     1 
ATOM   121  C  CA    . ILE A 1 25  ? 20.27443  -11.51391 32.93039  1.000 71.16152  ? 89  ILE A CA    1 
ATOM   122  C  C     . ILE A 1 25  ? 20.67967  -10.44316 31.92301  1.000 69.65046  ? 89  ILE A C     1 
ATOM   123  O  O     . ILE A 1 25  ? 20.75941  -10.69975 30.71547  1.000 70.20459  ? 89  ILE A O     1 
ATOM   124  C  CB    . ILE A 1 25  ? 18.85171  -11.27002 33.46614  1.000 68.55245  ? 89  ILE A CB    1 
ATOM   125  N  N     . ILE A 1 26  ? 20.94885  -9.22862  32.40396  1.000 79.63589  ? 90  ILE A N     1 
ATOM   126  C  CA    . ILE A 1 26  ? 21.23881  -8.11820  31.49902  1.000 82.90543  ? 90  ILE A CA    1 
ATOM   127  C  C     . ILE A 1 26  ? 22.53579  -8.36660  30.73862  1.000 83.72393  ? 90  ILE A C     1 
ATOM   128  O  O     . ILE A 1 26  ? 22.60934  -8.16510  29.52066  1.000 82.97849  ? 90  ILE A O     1 
ATOM   129  C  CB    . ILE A 1 26  ? 21.28964  -6.79001  32.27459  1.000 81.71164  ? 90  ILE A CB    1 
ATOM   130  N  N     . ASN A 1 27  ? 23.57979  -8.80250  31.44462  1.000 89.64397  ? 91  ASN A N     1 
ATOM   131  C  CA    . ASN A 1 27  ? 24.87086  -8.99459  30.79453  1.000 93.24799  ? 91  ASN A CA    1 
ATOM   132  C  C     . ASN A 1 27  ? 24.83654  -10.16340 29.81607  1.000 89.88258  ? 91  ASN A C     1 
ATOM   133  O  O     . ASN A 1 27  ? 25.45817  -10.10100 28.74940  1.000 97.34562  ? 91  ASN A O     1 
ATOM   134  C  CB    . ASN A 1 27  ? 25.96316  -9.19900  31.84356  1.000 99.37360  ? 91  ASN A CB    1 
ATOM   135  N  N     . SER A 1 28  ? 24.11869  -11.23730 30.15554  1.000 54.85227  ? 92  SER A N     1 
ATOM   136  C  CA    . SER A 1 28  ? 24.15055  -12.43255 29.31647  1.000 53.37519  ? 92  SER A CA    1 
ATOM   137  C  C     . SER A 1 28  ? 23.34765  -12.25454 28.03307  1.000 50.20023  ? 92  SER A C     1 
ATOM   138  O  O     . SER A 1 28  ? 23.80763  -12.64100 26.95241  1.000 56.28858  ? 92  SER A O     1 
ATOM   139  C  CB    . SER A 1 28  ? 23.63931  -13.64203 30.09905  1.000 51.28874  ? 92  SER A CB    1 
ATOM   140  O  OG    . SER A 1 28  ? 22.44481  -13.32452 30.79236  1.000 56.34984  ? 92  SER A OG    1 
ATOM   141  N  N     . LEU A 1 29  ? 22.15814  -11.66141 28.12211  1.000 46.66283  ? 93  LEU A N     1 
ATOM   142  C  CA    . LEU A 1 29  ? 21.24444  -11.57320 26.99014  1.000 42.75076  ? 93  LEU A CA    1 
ATOM   143  C  C     . LEU A 1 29  ? 21.37328  -10.25471 26.23698  1.000 41.61634  ? 93  LEU A C     1 
ATOM   144  O  O     . LEU A 1 29  ? 20.42484  -9.82689  25.57189  1.000 41.08261  ? 93  LEU A O     1 
ATOM   145  C  CB    . LEU A 1 29  ? 19.80771  -11.77350 27.46533  1.000 40.04009  ? 93  LEU A CB    1 
ATOM   146  C  CG    . LEU A 1 29  ? 19.54804  -13.04943 28.26474  1.000 39.57205  ? 93  LEU A CG    1 
ATOM   147  C  CD1   . LEU A 1 29  ? 18.72804  -12.74703 29.49817  1.000 38.93944  ? 93  LEU A CD1   1 
ATOM   148  C  CD2   . LEU A 1 29  ? 18.85584  -14.09811 27.40840  1.000 38.86351  ? 93  LEU A CD2   1 
ATOM   149  N  N     . TYR A 1 30  ? 22.53877  -9.60655  26.31387  1.000 63.05021  ? 94  TYR A N     1 
ATOM   150  C  CA    . TYR A 1 30  ? 22.71000  -8.29600  25.69390  1.000 60.89549  ? 94  TYR A CA    1 
ATOM   151  C  C     . TYR A 1 30  ? 22.56256  -8.33511  24.17662  1.000 62.32839  ? 94  TYR A C     1 
ATOM   152  O  O     . TYR A 1 30  ? 22.30535  -7.29187  23.56682  1.000 60.59720  ? 94  TYR A O     1 
ATOM   153  C  CB    . TYR A 1 30  ? 24.07472  -7.71316  26.06685  1.000 66.96662  ? 94  TYR A CB    1 
ATOM   154  N  N     . LYS A 1 31  ? 22.72652  -9.50212  23.55165  1.000 48.90371  ? 95  LYS A N     1 
ATOM   155  C  CA    . LYS A 1 31  ? 22.55640  -9.63665  22.11083  1.000 47.07063  ? 95  LYS A CA    1 
ATOM   156  C  C     . LYS A 1 31  ? 21.16777  -10.12347 21.72040  1.000 43.09647  ? 95  LYS A C     1 
ATOM   157  O  O     . LYS A 1 31  ? 20.79698  -10.02399 20.54458  1.000 45.27923  ? 95  LYS A O     1 
ATOM   158  C  CB    . LYS A 1 31  ? 23.60907  -10.59492 21.54029  1.000 48.32816  ? 95  LYS A CB    1 
ATOM   159  N  N     . ASN A 1 32  ? 20.39071  -10.62203 22.67663  1.000 60.94484  ? 96  ASN A N     1 
ATOM   160  C  CA    . ASN A 1 32  ? 19.09238  -11.21565 22.39174  1.000 58.50374  ? 96  ASN A CA    1 
ATOM   161  C  C     . ASN A 1 32  ? 17.99429  -10.46098 23.13804  1.000 53.54004  ? 96  ASN A C     1 
ATOM   162  O  O     . ASN A 1 32  ? 17.15238  -11.07036 23.80288  1.000 48.79557  ? 96  ASN A O     1 
ATOM   163  C  CB    . ASN A 1 32  ? 19.10846  -12.69904 22.76854  1.000 59.54495  ? 96  ASN A CB    1 
ATOM   164  C  CG    . ASN A 1 32  ? 18.07585  -13.50581 22.00991  1.000 62.61021  ? 96  ASN A CG    1 
ATOM   165  O  OD1   . ASN A 1 32  ? 17.60179  -13.08705 20.95280  1.000 59.57163  ? 96  ASN A OD1   1 
ATOM   166  N  ND2   . ASN A 1 32  ? 17.73266  -14.68110 22.53800  1.000 63.11521  ? 96  ASN A ND2   1 
ATOM   167  N  N     . LYS A 1 33  ? 18.00997  -9.12699  23.03582  1.000 35.07034  ? 97  LYS A N     1 
ATOM   168  C  CA    . LYS A 1 33  ? 17.12250  -8.28710  23.83669  1.000 29.60059  ? 97  LYS A CA    1 
ATOM   169  C  C     . LYS A 1 33  ? 15.64890  -8.57520  23.56759  1.000 30.39474  ? 97  LYS A C     1 
ATOM   170  O  O     . LYS A 1 33  ? 14.81119  -8.42244  24.46917  1.000 26.20333  ? 97  LYS A O     1 
ATOM   171  C  CB    . LYS A 1 33  ? 17.41125  -6.81551  23.55688  1.000 26.66675  ? 97  LYS A CB    1 
ATOM   172  C  CG    . LYS A 1 33  ? 18.70439  -6.29732  24.13514  1.000 30.07122  ? 97  LYS A CG    1 
ATOM   173  C  CD    . LYS A 1 33  ? 18.98801  -4.89304  23.62819  1.000 31.68756  ? 97  LYS A CD    1 
ATOM   174  C  CE    . LYS A 1 33  ? 20.17317  -4.27471  24.35838  1.000 38.65865  ? 97  LYS A CE    1 
ATOM   175  N  NZ    . LYS A 1 33  ? 20.82934  -3.18480  23.56971  1.000 41.39626  ? 97  LYS A NZ    1 
ATOM   176  N  N     A GLU A 1 34  ? 15.31057  -8.99348  22.34714  0.573 28.94102  ? 98  GLU A N     1 
ATOM   177  N  N     B GLU A 1 34  ? 15.31401  -8.98741  22.34101  0.427 28.94127  ? 98  GLU A N     1 
ATOM   178  C  CA    A GLU A 1 34  ? 13.91808  -9.22242  21.98035  0.573 26.99297  ? 98  GLU A CA    1 
ATOM   179  C  CA    B GLU A 1 34  ? 13.92565  -9.18908  21.94275  0.427 26.99357  ? 98  GLU A CA    1 
ATOM   180  C  C     A GLU A 1 34  ? 13.34800  -10.49716 22.57553  0.573 27.07636  ? 98  GLU A C     1 
ATOM   181  C  C     B GLU A 1 34  ? 13.28301  -10.38252 22.62960  0.427 26.94442  ? 98  GLU A C     1 
ATOM   182  O  O     A GLU A 1 34  ? 12.19142  -10.82340 22.28855  0.573 27.63902  ? 98  GLU A O     1 
ATOM   183  O  O     B GLU A 1 34  ? 12.06327  -10.54976 22.52544  0.427 27.24164  ? 98  GLU A O     1 
ATOM   184  C  CB    A GLU A 1 34  ? 13.77037  -9.23844  20.45578  0.573 27.97757  ? 98  GLU A CB    1 
ATOM   185  C  CB    B GLU A 1 34  ? 13.83416  -9.35078  20.42177  0.427 28.07488  ? 98  GLU A CB    1 
ATOM   186  C  CG    A GLU A 1 34  ? 14.50161  -10.36363 19.73853  0.573 29.47251  ? 98  GLU A CG    1 
ATOM   187  C  CG    B GLU A 1 34  ? 14.09222  -10.76023 19.91328  0.427 29.53072  ? 98  GLU A CG    1 
ATOM   188  C  CD    A GLU A 1 34  ? 15.98793  -10.08594 19.56398  0.573 31.10456  ? 98  GLU A CD    1 
ATOM   189  C  CD    B GLU A 1 34  ? 14.37698  -10.79884 18.42054  0.427 30.35250  ? 98  GLU A CD    1 
ATOM   190  O  OE1   A GLU A 1 34  ? 16.39462  -8.90489  19.62786  0.573 32.16927  ? 98  GLU A OE1   1 
ATOM   191  O  OE1   B GLU A 1 34  ? 14.77555  -9.75797  17.85900  0.427 28.47771  ? 98  GLU A OE1   1 
ATOM   192  O  OE2   A GLU A 1 34  ? 16.74776  -11.04982 19.33849  0.573 32.68355  ? 98  GLU A OE2   1 
ATOM   193  O  OE2   B GLU A 1 34  ? 14.19421  -11.86877 17.80408  0.427 33.75836  ? 98  GLU A OE2   1 
ATOM   194  N  N     A ILE A 1 35  ? 14.12160  -11.21756 23.39286  0.573 32.75821  ? 99  ILE A N     1 
ATOM   195  N  N     B ILE A 1 35  ? 14.06752  -11.20547 23.32866  0.427 32.69445  ? 99  ILE A N     1 
ATOM   196  C  CA    A ILE A 1 35  ? 13.60391  -12.36651 24.12635  0.573 32.20486  ? 99  ILE A CA    1 
ATOM   197  C  CA    B ILE A 1 35  ? 13.54821  -12.34637 24.06797  0.427 32.12559  ? 99  ILE A CA    1 
ATOM   198  C  C     A ILE A 1 35  ? 12.57815  -11.94821 25.17518  0.573 29.85072  ? 99  ILE A C     1 
ATOM   199  C  C     B ILE A 1 35  ? 12.57976  -11.94467 25.17273  0.427 29.84587  ? 99  ILE A C     1 
ATOM   200  O  O     A ILE A 1 35  ? 11.81752  -12.79454 25.66407  0.573 28.58340  ? 99  ILE A O     1 
ATOM   201  O  O     B ILE A 1 35  ? 11.87075  -12.80536 25.70702  0.427 28.63077  ? 99  ILE A O     1 
ATOM   202  C  CB    A ILE A 1 35  ? 14.77237  -13.13582 24.77737  0.573 34.38916  ? 99  ILE A CB    1 
ATOM   203  C  CB    B ILE A 1 35  ? 14.72541  -13.16309 24.64863  0.427 34.36730  ? 99  ILE A CB    1 
ATOM   204  C  CG1   A ILE A 1 35  ? 14.35028  -14.54159 25.19801  0.573 36.39797  ? 99  ILE A CG1   1 
ATOM   205  C  CG1   B ILE A 1 35  ? 14.42914  -14.65643 24.56286  0.427 37.34435  ? 99  ILE A CG1   1 
ATOM   206  C  CG2   A ILE A 1 35  ? 15.31076  -12.38432 25.98914  0.573 31.32933  ? 99  ILE A CG2   1 
ATOM   207  C  CG2   B ILE A 1 35  ? 15.05256  -12.73113 26.07762  0.427 32.30855  ? 99  ILE A CG2   1 
ATOM   208  C  CD1   A ILE A 1 35  ? 15.51878  -15.39663 25.66867  0.573 38.27046  ? 99  ILE A CD1   1 
ATOM   209  C  CD1   B ILE A 1 35  ? 14.54999  -15.20321 23.17170  0.427 36.98475  ? 99  ILE A CD1   1 
ATOM   210  N  N     . PHE A 1 36  ? 12.52518  -10.65365 25.51572  1.000 24.97024  ? 100 PHE A N     1 
ATOM   211  C  CA    . PHE A 1 36  ? 11.67793  -10.19292 26.61345  1.000 21.81087  ? 100 PHE A CA    1 
ATOM   212  C  C     . PHE A 1 36  ? 10.20710  -10.48160 26.34849  1.000 21.11561  ? 100 PHE A C     1 
ATOM   213  O  O     . PHE A 1 36  ? 9.47909   -10.89503 27.25934  1.000 19.58636  ? 100 PHE A O     1 
ATOM   214  C  CB    . PHE A 1 36  ? 11.89120  -8.69404  26.84431  1.000 21.79668  ? 100 PHE A CB    1 
ATOM   215  C  CG    . PHE A 1 36  ? 11.11755  -7.82026  25.89627  1.000 22.63663  ? 100 PHE A CG    1 
ATOM   216  C  CD1   . PHE A 1 36  ? 11.60409  -7.55051  24.62855  1.000 20.88841  ? 100 PHE A CD1   1 
ATOM   217  C  CD2   . PHE A 1 36  ? 9.89144   -7.28141  26.26699  1.000 19.41135  ? 100 PHE A CD2   1 
ATOM   218  C  CE1   . PHE A 1 36  ? 10.88570  -6.76365  23.74510  1.000 19.77021  ? 100 PHE A CE1   1 
ATOM   219  C  CE2   . PHE A 1 36  ? 9.16998   -6.49273  25.38387  1.000 20.42542  ? 100 PHE A CE2   1 
ATOM   220  C  CZ    . PHE A 1 36  ? 9.67191   -6.22498  24.12147  1.000 16.67066  ? 100 PHE A CZ    1 
ATOM   221  N  N     . LEU A 1 37  ? 9.74604   -10.25648 25.11405  1.000 21.83133  ? 101 LEU A N     1 
ATOM   222  C  CA    . LEU A 1 37  ? 8.34001   -10.49101 24.80245  1.000 21.23821  ? 101 LEU A CA    1 
ATOM   223  C  C     . LEU A 1 37  ? 7.97616   -11.95327 25.00365  1.000 21.99354  ? 101 LEU A C     1 
ATOM   224  O  O     . LEU A 1 37  ? 6.93302   -12.26842 25.59179  1.000 21.94262  ? 101 LEU A O     1 
ATOM   225  C  CB    . LEU A 1 37  ? 8.03506   -10.05776 23.37101  1.000 21.43601  ? 101 LEU A CB    1 
ATOM   226  C  CG    . LEU A 1 37  ? 6.55629   -9.83842  23.03831  1.000 15.19975  ? 101 LEU A CG    1 
ATOM   227  C  CD1   . LEU A 1 37  ? 5.84464   -9.04391  24.12813  1.000 21.40686  ? 101 LEU A CD1   1 
ATOM   228  C  CD2   . LEU A 1 37  ? 6.42039   -9.16753  21.70301  1.000 17.85816  ? 101 LEU A CD2   1 
ATOM   229  N  N     . ARG A 1 38  ? 8.83789   -12.86219 24.54609  1.000 21.32902  ? 102 ARG A N     1 
ATOM   230  C  CA    . ARG A 1 38  ? 8.62240   -14.28236 24.80196  1.000 25.16316  ? 102 ARG A CA    1 
ATOM   231  C  C     . ARG A 1 38  ? 8.46256   -14.55602 26.28835  1.000 23.68519  ? 102 ARG A C     1 
ATOM   232  O  O     . ARG A 1 38  ? 7.52287   -15.24383 26.70683  1.000 25.80655  ? 102 ARG A O     1 
ATOM   233  C  CB    . ARG A 1 38  ? 9.78186   -15.09931 24.23648  1.000 26.49433  ? 102 ARG A CB    1 
ATOM   234  C  CG    . ARG A 1 38  ? 9.52529   -16.59613 24.19186  1.000 28.52335  ? 102 ARG A CG    1 
ATOM   235  C  CD    . ARG A 1 38  ? 10.77960  -17.31047 23.73447  1.000 30.32013  ? 102 ARG A CD    1 
ATOM   236  N  NE    . ARG A 1 38  ? 11.70866  -17.49233 24.84445  1.000 36.00600  ? 102 ARG A NE    1 
ATOM   237  C  CZ    . ARG A 1 38  ? 12.96361  -17.89756 24.71336  1.000 42.94152  ? 102 ARG A CZ    1 
ATOM   238  N  NH1   . ARG A 1 38  ? 13.47753  -18.18793 23.52704  1.000 43.67106  ? 102 ARG A NH1   1 
ATOM   239  N  NH2   . ARG A 1 38  ? 13.71995  -18.02190 25.79861  1.000 45.92037  ? 102 ARG A NH2   1 
ATOM   240  N  N     . GLU A 1 39  ? 9.37252   -14.01890 27.10738  1.000 19.70332  ? 103 GLU A N     1 
ATOM   241  C  CA    . GLU A 1 39  ? 9.31540   -14.29030 28.53957  1.000 20.60206  ? 103 GLU A CA    1 
ATOM   242  C  C     . GLU A 1 39  ? 8.02122   -13.76817 29.15002  1.000 18.69900  ? 103 GLU A C     1 
ATOM   243  O  O     . GLU A 1 39  ? 7.39709   -14.44987 29.97397  1.000 22.02108  ? 103 GLU A O     1 
ATOM   244  C  CB    . GLU A 1 39  ? 10.51858  -13.66234 29.25227  1.000 22.88768  ? 103 GLU A CB    1 
ATOM   245  C  CG    . GLU A 1 39  ? 11.87414  -14.28768 28.91543  1.000 23.48602  ? 103 GLU A CG    1 
ATOM   246  C  CD    . GLU A 1 39  ? 11.87392  -15.80520 29.00488  1.000 28.04755  ? 103 GLU A CD    1 
ATOM   247  O  OE1   . GLU A 1 39  ? 11.29885  -16.34984 29.96988  1.000 24.54558  ? 103 GLU A OE1   1 
ATOM   248  O  OE2   . GLU A 1 39  ? 12.46696  -16.45229 28.11809  1.000 28.50555  ? 103 GLU A OE2   1 
ATOM   249  N  N     . LEU A 1 40  ? 7.61351   -12.55458 28.77832  1.000 16.90773  ? 104 LEU A N     1 
ATOM   250  C  CA    . LEU A 1 40  ? 6.39017   -11.99014 29.34335  1.000 16.27565  ? 104 LEU A CA    1 
ATOM   251  C  C     . LEU A 1 40  ? 5.17647   -12.79316 28.90527  1.000 15.97168  ? 104 LEU A C     1 
ATOM   252  O  O     . LEU A 1 40  ? 4.24582   -13.01367 29.69119  1.000 16.02925  ? 104 LEU A O     1 
ATOM   253  C  CB    . LEU A 1 40  ? 6.23270   -10.52942 28.92851  1.000 10.36359  ? 104 LEU A CB    1 
ATOM   254  C  CG    . LEU A 1 40  ? 7.28345   -9.53010  29.40236  1.000 10.84001  ? 104 LEU A CG    1 
ATOM   255  C  CD1   . LEU A 1 40  ? 6.87528   -8.10171  29.01285  1.000 13.75135  ? 104 LEU A CD1   1 
ATOM   256  C  CD2   . LEU A 1 40  ? 7.48414   -9.67300  30.90788  1.000 12.40131  ? 104 LEU A CD2   1 
ATOM   257  N  N     . ILE A 1 41  ? 5.17996   -13.23973 27.65519  1.000 16.74799  ? 105 ILE A N     1 
ATOM   258  C  CA    . ILE A 1 41  ? 4.06589   -14.00866 27.11596  1.000 15.96418  ? 105 ILE A CA    1 
ATOM   259  C  C     . ILE A 1 41  ? 3.98269   -15.38111 27.78269  1.000 17.02457  ? 105 ILE A C     1 
ATOM   260  O  O     . ILE A 1 41  ? 2.88424   -15.90299 28.02716  1.000 15.31203  ? 105 ILE A O     1 
ATOM   261  C  CB    . ILE A 1 41  ? 4.21489   -14.09342 25.58528  1.000 22.25297  ? 105 ILE A CB    1 
ATOM   262  C  CG1   . ILE A 1 41  ? 3.58253   -12.84983 24.92538  1.000 13.77887  ? 105 ILE A CG1   1 
ATOM   263  C  CG2   . ILE A 1 41  ? 3.60663   -15.36457 25.06267  1.000 25.74802  ? 105 ILE A CG2   1 
ATOM   264  C  CD1   . ILE A 1 41  ? 3.54832   -12.88285 23.40147  1.000 18.90703  ? 105 ILE A CD1   1 
ATOM   265  N  N     . SER A 1 42  ? 5.12996   -15.99190 28.10304  1.000 21.51376  ? 106 SER A N     1 
ATOM   266  C  CA    . SER A 1 42  ? 5.09216   -17.25671 28.83498  1.000 21.37009  ? 106 SER A CA    1 
ATOM   267  C  C     . SER A 1 42  ? 4.43145   -17.08196 30.19743  1.000 19.26171  ? 106 SER A C     1 
ATOM   268  O  O     . SER A 1 42  ? 3.53851   -17.85113 30.57153  1.000 16.03041  ? 106 SER A O     1 
ATOM   269  C  CB    . SER A 1 42  ? 6.50052   -17.82806 29.00568  1.000 23.61537  ? 106 SER A CB    1 
ATOM   270  O  OG    . SER A 1 42  ? 7.07364   -18.17500 27.76213  1.000 29.15118  ? 106 SER A OG    1 
ATOM   271  N  N     . ASN A 1 43  ? 4.84643   -16.05432 30.94258  1.000 17.35799  ? 107 ASN A N     1 
ATOM   272  C  CA    . ASN A 1 43  ? 4.26785   -15.80319 32.25714  1.000 15.84975  ? 107 ASN A CA    1 
ATOM   273  C  C     . ASN A 1 43  ? 2.76068   -15.63009 32.15781  1.000 13.33650  ? 107 ASN A C     1 
ATOM   274  O  O     . ASN A 1 43  ? 2.00260   -16.22561 32.93222  1.000 16.83224  ? 107 ASN A O     1 
ATOM   275  C  CB    . ASN A 1 43  ? 4.92415   -14.56856 32.87467  1.000 13.93626  ? 107 ASN A CB    1 
ATOM   276  C  CG    . ASN A 1 43  ? 6.39909   -14.78285 33.15267  1.000 18.46581  ? 107 ASN A CG    1 
ATOM   277  O  OD1   . ASN A 1 43  ? 6.87627   -15.90851 33.14699  1.000 18.44644  ? 107 ASN A OD1   1 
ATOM   278  N  ND2   . ASN A 1 43  ? 7.13310   -13.70351 33.34281  1.000 18.69894  ? 107 ASN A ND2   1 
ATOM   279  N  N     . ALA A 1 44  ? 2.31201   -14.82658 31.19415  1.000 18.77044  ? 108 ALA A N     1 
ATOM   280  C  CA    . ALA A 1 44  ? 0.88371   -14.66907 30.94145  1.000 15.03897  ? 108 ALA A CA    1 
ATOM   281  C  C     . ALA A 1 44  ? 0.20882   -16.02169 30.75443  1.000 15.78780  ? 108 ALA A C     1 
ATOM   282  O  O     . ALA A 1 44  ? -0.83669  -16.29510 31.35230  1.000 16.56767  ? 108 ALA A O     1 
ATOM   283  C  CB    . ALA A 1 44  ? 0.67781   -13.77837 29.71302  1.000 14.18775  ? 108 ALA A CB    1 
ATOM   284  N  N     . SER A 1 45  ? 0.81272   -16.90170 29.94576  1.000 16.06773  ? 109 SER A N     1 
ATOM   285  C  CA    . SER A 1 45  ? 0.22020   -18.21252 29.72309  1.000 11.53739  ? 109 SER A CA    1 
ATOM   286  C  C     . SER A 1 45  ? 0.20653   -19.03527 31.00130  1.000 14.31596  ? 109 SER A C     1 
ATOM   287  O  O     . SER A 1 45  ? -0.78223  -19.72092 31.28784  1.000 16.86706  ? 109 SER A O     1 
ATOM   288  C  CB    . SER A 1 45  ? 0.96333   -18.95409 28.60992  1.000 15.03055  ? 109 SER A CB    1 
ATOM   289  O  OG    . SER A 1 45  ? 0.40191   -20.23489 28.40693  1.000 16.27828  ? 109 SER A OG    1 
ATOM   290  N  N     . ASP A 1 46  ? 1.29629   -18.98392 31.78871  1.000 17.70413  ? 110 ASP A N     1 
ATOM   291  C  CA    . ASP A 1 46  ? 1.32527   -19.69982 33.06545  1.000 18.48658  ? 110 ASP A CA    1 
ATOM   292  C  C     . ASP A 1 46  ? 0.23103   -19.20022 33.99328  1.000 19.64895  ? 110 ASP A C     1 
ATOM   293  O  O     . ASP A 1 46  ? -0.43307  -19.99357 34.67371  1.000 19.32350  ? 110 ASP A O     1 
ATOM   294  C  CB    . ASP A 1 46  ? 2.68369   -19.52735 33.75346  1.000 17.15561  ? 110 ASP A CB    1 
ATOM   295  C  CG    . ASP A 1 46  ? 3.78717   -20.28843 33.05853  1.000 21.03198  ? 110 ASP A CG    1 
ATOM   296  O  OD1   . ASP A 1 46  ? 3.47771   -21.01589 32.09404  1.000 22.72073  ? 110 ASP A OD1   1 
ATOM   297  O  OD2   . ASP A 1 46  ? 4.96321   -20.13148 33.45861  1.000 24.07480  ? 110 ASP A OD2   1 
ATOM   298  N  N     . ALA A 1 47  ? 0.05827   -17.88292 34.06292  1.000 15.84002  ? 111 ALA A N     1 
ATOM   299  C  CA    . ALA A 1 47  ? -0.97760  -17.31469 34.91261  1.000 16.64842  ? 111 ALA A CA    1 
ATOM   300  C  C     . ALA A 1 47  ? -2.36831  -17.65815 34.39703  1.000 17.63590  ? 111 ALA A C     1 
ATOM   301  O  O     . ALA A 1 47  ? -3.30856  -17.77869 35.18639  1.000 17.54264  ? 111 ALA A O     1 
ATOM   302  C  CB    . ALA A 1 47  ? -0.80055  -15.80390 34.99325  1.000 17.49021  ? 111 ALA A CB    1 
ATOM   303  N  N     . LEU A 1 48  ? -2.52000  -17.81165 33.08155  1.000 16.26840  ? 112 LEU A N     1 
ATOM   304  C  CA    . LEU A 1 48  ? -3.78748  -18.28797 32.53669  1.000 17.54895  ? 112 LEU A CA    1 
ATOM   305  C  C     . LEU A 1 48  ? -4.02441  -19.75711 32.87065  1.000 17.91560  ? 112 LEU A C     1 
ATOM   306  O  O     . LEU A 1 48  ? -5.14740  -20.15300 33.20313  1.000 18.28250  ? 112 LEU A O     1 
ATOM   307  C  CB    . LEU A 1 48  ? -3.80876  -18.05351 31.03137  1.000 15.59947  ? 112 LEU A CB    1 
ATOM   308  C  CG    . LEU A 1 48  ? -3.99055  -16.56224 30.76555  1.000 16.52150  ? 112 LEU A CG    1 
ATOM   309  C  CD1   . LEU A 1 48  ? -3.55976  -16.17666 29.37132  1.000 14.33228  ? 112 LEU A CD1   1 
ATOM   310  C  CD2   . LEU A 1 48  ? -5.43668  -16.17475 30.99342  1.000 18.10145  ? 112 LEU A CD2   1 
ATOM   311  N  N     . ASP A 1 49  ? -2.98005  -20.58103 32.79223  1.000 20.05713  ? 113 ASP A N     1 
ATOM   312  C  CA    . ASP A 1 49  ? -3.10707  -21.96263 33.24381  1.000 18.57413  ? 113 ASP A CA    1 
ATOM   313  C  C     . ASP A 1 49  ? -3.56871  -22.02679 34.69707  1.000 18.78531  ? 113 ASP A C     1 
ATOM   314  O  O     . ASP A 1 49  ? -4.45768  -22.81733 35.03745  1.000 24.88083  ? 113 ASP A O     1 
ATOM   315  C  CB    . ASP A 1 49  ? -1.77850  -22.69269 33.06163  1.000 19.47427  ? 113 ASP A CB    1 
ATOM   316  C  CG    . ASP A 1 49  ? -1.58118  -23.22156 31.64023  1.000 21.79688  ? 113 ASP A CG    1 
ATOM   317  O  OD1   . ASP A 1 49  ? -2.57998  -23.58049 30.96462  1.000 18.95632  ? 113 ASP A OD1   1 
ATOM   318  O  OD2   . ASP A 1 49  ? -0.41088  -23.30351 31.20072  1.000 19.97437  ? 113 ASP A OD2   1 
ATOM   319  N  N     . LYS A 1 50  ? -2.98971  -21.19835 35.57031  1.000 21.71094  ? 114 LYS A N     1 
ATOM   320  C  CA    . LYS A 1 50  ? -3.33044  -21.26419 36.99117  1.000 20.33785  ? 114 LYS A CA    1 
ATOM   321  C  C     . LYS A 1 50  ? -4.80889  -20.99270 37.22626  1.000 22.83435  ? 114 LYS A C     1 
ATOM   322  O  O     . LYS A 1 50  ? -5.52043  -21.83075 37.78947  1.000 24.16428  ? 114 LYS A O     1 
ATOM   323  C  CB    . LYS A 1 50  ? -2.48002  -20.28525 37.79673  1.000 21.78720  ? 114 LYS A CB    1 
ATOM   324  C  CG    . LYS A 1 50  ? -1.03476  -20.72431 37.94737  1.000 32.24577  ? 114 LYS A CG    1 
ATOM   325  C  CD    . LYS A 1 50  ? -0.51039  -20.49634 39.36713  1.000 38.83070  ? 114 LYS A CD    1 
ATOM   326  C  CE    . LYS A 1 50  ? 0.96024   -20.92759 39.48152  1.000 41.60590  ? 114 LYS A CE    1 
ATOM   327  N  NZ    . LYS A 1 50  ? 1.88564   -19.97151 38.78119  1.000 38.61320  ? 114 LYS A NZ    1 
ATOM   328  N  N     . ILE A 1 51  ? -5.30423  -19.84473 36.76229  1.000 20.48224  ? 115 ILE A N     1 
ATOM   329  C  CA    . ILE A 1 51  ? -6.69926  -19.50819 37.03915  1.000 21.94744  ? 115 ILE A CA    1 
ATOM   330  C  C     . ILE A 1 51  ? -7.62997  -20.50551 36.37038  1.000 19.27110  ? 115 ILE A C     1 
ATOM   331  O  O     . ILE A 1 51  ? -8.72332  -20.78201 36.87806  1.000 21.63962  ? 115 ILE A O     1 
ATOM   332  C  CB    . ILE A 1 51  ? -7.01167  -18.05703 36.62407  1.000 22.26047  ? 115 ILE A CB    1 
ATOM   333  C  CG1   . ILE A 1 51  ? -8.33293  -17.60706 37.25885  1.000 18.08785  ? 115 ILE A CG1   1 
ATOM   334  C  CG2   . ILE A 1 51  ? -7.01493  -17.88452 35.08621  1.000 18.14810  ? 115 ILE A CG2   1 
ATOM   335  C  CD1   . ILE A 1 51  ? -8.26796  -17.49057 38.76154  1.000 17.38597  ? 115 ILE A CD1   1 
ATOM   336  N  N     . ARG A 1 52  ? -7.21160  -21.07286 35.23573  1.000 19.26376  ? 116 ARG A N     1 
ATOM   337  C  CA    . ARG A 1 52  ? -7.98743  -22.13433 34.60394  1.000 19.73136  ? 116 ARG A CA    1 
ATOM   338  C  C     . ARG A 1 52  ? -8.02749  -23.38525 35.46453  1.000 21.60386  ? 116 ARG A C     1 
ATOM   339  O  O     . ARG A 1 52  ? -9.07979  -24.02733 35.58363  1.000 25.94091  ? 116 ARG A O     1 
ATOM   340  C  CB    . ARG A 1 52  ? -7.41196  -22.45608 33.23165  1.000 24.07631  ? 116 ARG A CB    1 
ATOM   341  C  CG    . ARG A 1 52  ? -8.38860  -23.15812 32.30419  1.000 25.47062  ? 116 ARG A CG    1 
ATOM   342  C  CD    . ARG A 1 52  ? -7.62334  -23.89946 31.22393  1.000 31.44267  ? 116 ARG A CD    1 
ATOM   343  N  NE    . ARG A 1 52  ? -8.49235  -24.65724 30.33369  1.000 40.96361  ? 116 ARG A NE    1 
ATOM   344  C  CZ    . ARG A 1 52  ? -8.06066  -25.55258 29.45678  1.000 38.43128  ? 116 ARG A CZ    1 
ATOM   345  N  NH1   . ARG A 1 52  ? -6.77346  -25.85439 29.35446  1.000 35.87008  ? 116 ARG A NH1   1 
ATOM   346  N  NH2   . ARG A 1 52  ? -8.93836  -26.14427 28.64724  1.000 36.73582  ? 116 ARG A NH2   1 
ATOM   347  N  N     . LEU A 1 53  ? -6.88646  -23.77536 36.05376  1.000 12.54001  ? 117 LEU A N     1 
ATOM   348  C  CA    . LEU A 1 53  ? -6.90642  -24.89634 36.98818  1.000 17.02312  ? 117 LEU A CA    1 
ATOM   349  C  C     . LEU A 1 53  ? -7.71726  -24.58073 38.23218  1.000 19.30862  ? 117 LEU A C     1 
ATOM   350  O  O     . LEU A 1 53  ? -8.42910  -25.45084 38.74871  1.000 18.42734  ? 117 LEU A O     1 
ATOM   351  C  CB    . LEU A 1 53  ? -5.49532  -25.32514 37.39245  1.000 17.61264  ? 117 LEU A CB    1 
ATOM   352  C  CG    . LEU A 1 53  ? -4.62747  -26.05010 36.35723  1.000 18.69449  ? 117 LEU A CG    1 
ATOM   353  C  CD1   . LEU A 1 53  ? -3.14840  -25.86841 36.70398  1.000 22.52204  ? 117 LEU A CD1   1 
ATOM   354  C  CD2   . LEU A 1 53  ? -4.97499  -27.51941 36.30059  1.000 21.20279  ? 117 LEU A CD2   1 
ATOM   355  N  N     A ILE A 1 54  ? -7.60010  -23.35418 38.73864  1.000 20.57105  ? 118 ILE A N     1 
ATOM   356  N  N     B ILE A 1 54  ? -7.59972  -23.35798 38.75316  0.000 20.52921  ? 118 ILE A N     1 
ATOM   357  C  CA    A ILE A 1 54  ? -8.34521  -22.94889 39.92731  1.000 21.31667  ? 118 ILE A CA    1 
ATOM   358  C  CA    B ILE A 1 54  ? -8.36066  -22.99041 39.94406  0.000 21.34269  ? 118 ILE A CA    1 
ATOM   359  C  C     A ILE A 1 54  ? -9.83998  -22.98460 39.64272  1.000 21.06879  ? 118 ILE A C     1 
ATOM   360  C  C     B ILE A 1 54  ? -9.85258  -23.00598 39.64062  0.000 21.13519  ? 118 ILE A C     1 
ATOM   361  O  O     A ILE A 1 54  ? -10.64506 -23.38747 40.49580  1.000 22.70570  ? 118 ILE A O     1 
ATOM   362  O  O     B ILE A 1 54  ? -10.67042 -23.40273 40.48009  0.000 22.60459  ? 118 ILE A O     1 
ATOM   363  C  CB    A ILE A 1 54  ? -7.87533  -21.55467 40.39143  1.000 18.56009  ? 118 ILE A CB    1 
ATOM   364  C  CB    B ILE A 1 54  ? -7.89776  -21.62055 40.47547  0.000 18.78289  ? 118 ILE A CB    1 
ATOM   365  C  CG1   A ILE A 1 54  ? -6.55761  -21.66334 41.17266  1.000 18.95268  ? 118 ILE A CG1   1 
ATOM   366  C  CG1   B ILE A 1 54  ? -6.44055  -21.69422 40.93573  0.000 19.09083  ? 118 ILE A CG1   1 
ATOM   367  C  CG2   A ILE A 1 54  ? -8.95035  -20.84451 41.21228  1.000 20.32241  ? 118 ILE A CG2   1 
ATOM   368  C  CG2   B ILE A 1 54  ? -8.78981  -21.15414 41.61798  0.000 21.04278  ? 118 ILE A CG2   1 
ATOM   369  C  CD1   A ILE A 1 54  ? -5.80674  -20.33147 41.29536  1.000 17.37909  ? 118 ILE A CD1   1 
ATOM   370  C  CD1   B ILE A 1 54  ? -6.23579  -22.52326 42.18718  0.000 22.25355  ? 118 ILE A CD1   1 
ATOM   371  N  N     . SER A 1 55  ? -10.22804 -22.59646 38.42699  1.000 20.88211  ? 119 SER A N     1 
ATOM   372  C  CA    . SER A 1 55  ? -11.63141 -22.57625 38.03841  1.000 22.48479  ? 119 SER A CA    1 
ATOM   373  C  C     . SER A 1 55  ? -12.23767 -23.97607 37.94785  1.000 26.01384  ? 119 SER A C     1 
ATOM   374  O  O     . SER A 1 55  ? -13.46790 -24.10102 37.96308  1.000 24.75126  ? 119 SER A O     1 
ATOM   375  C  CB    . SER A 1 55  ? -11.78166 -21.83344 36.70481  1.000 19.56861  ? 119 SER A CB    1 
ATOM   376  O  OG    . SER A 1 55  ? -11.60389 -22.70743 35.60506  1.000 29.99449  ? 119 SER A OG    1 
ATOM   377  N  N     . LEU A 1 56  ? -11.41592 -25.03105 37.86342  1.000 21.60266  ? 120 LEU A N     1 
ATOM   378  C  CA    . LEU A 1 56  ? -11.95793 -26.38564 37.94411  1.000 24.70846  ? 120 LEU A CA    1 
ATOM   379  C  C     . LEU A 1 56  ? -12.54131 -26.67021 39.31467  1.000 27.73298  ? 120 LEU A C     1 
ATOM   380  O  O     . LEU A 1 56  ? -13.51649 -27.41574 39.42008  1.000 29.00374  ? 120 LEU A O     1 
ATOM   381  C  CB    . LEU A 1 56  ? -10.89119 -27.43711 37.64400  1.000 23.38432  ? 120 LEU A CB    1 
ATOM   382  C  CG    . LEU A 1 56  ? -10.26168 -27.50665 36.25491  1.000 21.21698  ? 120 LEU A CG    1 
ATOM   383  C  CD1   . LEU A 1 56  ? -9.04182  -28.40090 36.32985  1.000 23.22856  ? 120 LEU A CD1   1 
ATOM   384  C  CD2   . LEU A 1 56  ? -11.23865 -28.03269 35.22561  1.000 25.45024  ? 120 LEU A CD2   1 
ATOM   385  N  N     . THR A 1 57  ? -11.94459 -26.11619 40.37396  1.000 28.18446  ? 121 THR A N     1 
ATOM   386  C  CA    . THR A 1 57  ? -12.37111 -26.36631 41.74322  1.000 26.98585  ? 121 THR A CA    1 
ATOM   387  C  C     . THR A 1 57  ? -13.11651 -25.20406 42.36905  1.000 27.57666  ? 121 THR A C     1 
ATOM   388  O  O     . THR A 1 57  ? -13.61647 -25.34761 43.48666  1.000 30.12944  ? 121 THR A O     1 
ATOM   389  C  CB    . THR A 1 57  ? -11.16283 -26.69134 42.63539  1.000 29.05310  ? 121 THR A CB    1 
ATOM   390  O  OG1   . THR A 1 57  ? -10.11045 -25.75341 42.37901  1.000 30.03984  ? 121 THR A OG1   1 
ATOM   391  C  CG2   . THR A 1 57  ? -10.65845 -28.11242 42.38782  1.000 30.52618  ? 121 THR A CG2   1 
ATOM   392  N  N     . ASP A 1 58  ? -13.18952 -24.05690 41.69722  1.000 28.53175  ? 122 ASP A N     1 
ATOM   393  C  CA    . ASP A 1 58  ? -13.72615 -22.82521 42.27092  1.000 28.23109  ? 122 ASP A CA    1 
ATOM   394  C  C     . ASP A 1 58  ? -14.66809 -22.22491 41.23077  1.000 33.65708  ? 122 ASP A C     1 
ATOM   395  O  O     . ASP A 1 58  ? -14.21476 -21.62346 40.25351  1.000 30.22641  ? 122 ASP A O     1 
ATOM   396  C  CB    . ASP A 1 58  ? -12.58722 -21.87484 42.63163  1.000 26.71216  ? 122 ASP A CB    1 
ATOM   397  C  CG    . ASP A 1 58  ? -13.05365 -20.59821 43.32603  1.000 33.33572  ? 122 ASP A CG    1 
ATOM   398  O  OD1   . ASP A 1 58  ? -14.28002 -20.32400 43.40209  1.000 29.32389  ? 122 ASP A OD1   1 
ATOM   399  O  OD2   . ASP A 1 58  ? -12.15387 -19.84504 43.76684  1.000 27.99475  ? 122 ASP A OD2   1 
ATOM   400  N  N     . GLU A 1 59  ? -15.97786 -22.39485 41.43456  1.000 53.93800  ? 123 GLU A N     1 
ATOM   401  C  CA    . GLU A 1 59  ? -16.96172 -21.91831 40.46672  1.000 53.29835  ? 123 GLU A CA    1 
ATOM   402  C  C     . GLU A 1 59  ? -17.05679 -20.39738 40.41141  1.000 46.74013  ? 123 GLU A C     1 
ATOM   403  O  O     . GLU A 1 59  ? -17.69322 -19.86899 39.49425  1.000 54.85021  ? 123 GLU A O     1 
ATOM   404  C  CB    . GLU A 1 59  ? -18.33708 -22.51093 40.78154  1.000 54.51841  ? 123 GLU A CB    1 
ATOM   405  N  N     . ASN A 1 60  ? -16.45462 -19.68687 41.36324  1.000 28.34532  ? 124 ASN A N     1 
ATOM   406  C  CA    . ASN A 1 60  ? -16.42405 -18.22969 41.35848  1.000 30.82601  ? 124 ASN A CA    1 
ATOM   407  C  C     . ASN A 1 60  ? -15.09007 -17.67557 40.86199  1.000 29.44679  ? 124 ASN A C     1 
ATOM   408  O  O     . ASN A 1 60  ? -14.87786 -16.45657 40.90290  1.000 27.80715  ? 124 ASN A O     1 
ATOM   409  C  CB    . ASN A 1 60  ? -16.72902 -17.69693 42.76150  1.000 28.75890  ? 124 ASN A CB    1 
ATOM   410  N  N     . ALA A 1 61  ? -14.19782 -18.54157 40.37288  1.000 32.16465  ? 125 ALA A N     1 
ATOM   411  C  CA    . ALA A 1 61  ? -12.83987 -18.11818 40.05482  1.000 29.39429  ? 125 ALA A CA    1 
ATOM   412  C  C     . ALA A 1 61  ? -12.80345 -17.10746 38.91795  1.000 28.63363  ? 125 ALA A C     1 
ATOM   413  O  O     . ALA A 1 61  ? -11.94254 -16.22292 38.91115  1.000 24.84802  ? 125 ALA A O     1 
ATOM   414  C  CB    . ALA A 1 61  ? -11.97605 -19.32732 39.70608  1.000 25.42118  ? 125 ALA A CB    1 
ATOM   415  N  N     . LEU A 1 62  ? -13.72200 -17.20631 37.95861  1.000 25.21334  ? 126 LEU A N     1 
ATOM   416  C  CA    . LEU A 1 62  ? -13.66269 -16.38590 36.75782  1.000 29.32014  ? 126 LEU A CA    1 
ATOM   417  C  C     . LEU A 1 62  ? -14.60233 -15.18806 36.82125  1.000 32.36040  ? 126 LEU A C     1 
ATOM   418  O  O     . LEU A 1 62  ? -14.80105 -14.51763 35.80179  1.000 35.18022  ? 126 LEU A O     1 
ATOM   419  C  CB    . LEU A 1 62  ? -13.98468 -17.23714 35.52633  1.000 26.54867  ? 126 LEU A CB    1 
ATOM   420  C  CG    . LEU A 1 62  ? -12.86603 -18.13360 34.96029  1.000 28.41509  ? 126 LEU A CG    1 
ATOM   421  C  CD1   . LEU A 1 62  ? -13.08766 -18.41307 33.47875  1.000 30.42175  ? 126 LEU A CD1   1 
ATOM   422  C  CD2   . LEU A 1 62  ? -11.46108 -17.59122 35.20290  1.000 21.42441  ? 126 LEU A CD2   1 
ATOM   423  N  N     . ALA A 1 63  ? -15.16566 -14.89260 37.99933  1.000 33.60304  ? 127 ALA A N     1 
ATOM   424  C  CA    . ALA A 1 63  ? -16.24887 -13.91509 38.10111  1.000 31.71534  ? 127 ALA A CA    1 
ATOM   425  C  C     . ALA A 1 63  ? -15.80585 -12.51096 37.69858  1.000 30.98932  ? 127 ALA A C     1 
ATOM   426  O  O     . ALA A 1 63  ? -16.56184 -11.77922 37.04772  1.000 35.36033  ? 127 ALA A O     1 
ATOM   427  C  CB    . ALA A 1 63  ? -16.80234 -13.90785 39.52275  1.000 29.48751  ? 127 ALA A CB    1 
ATOM   428  N  N     . GLY A 1 64  ? -14.60038 -12.10146 38.09590  1.000 42.94286  ? 128 GLY A N     1 
ATOM   429  C  CA    . GLY A 1 64  ? -14.14235 -10.74676 37.81398  1.000 38.14554  ? 128 GLY A CA    1 
ATOM   430  C  C     . GLY A 1 64  ? -13.69247 -10.48434 36.38435  1.000 41.20680  ? 128 GLY A C     1 
ATOM   431  O  O     . GLY A 1 64  ? -13.49058 -9.31916  36.01927  1.000 38.18616  ? 128 GLY A O     1 
ATOM   432  N  N     . ASN A 1 65  ? -13.48565 -11.54335 35.59095  1.000 39.59663  ? 129 ASN A N     1 
ATOM   433  C  CA    . ASN A 1 65  ? -13.20305 -11.48103 34.15645  1.000 35.35882  ? 129 ASN A CA    1 
ATOM   434  C  C     . ASN A 1 65  ? -13.40715 -12.86707 33.53609  1.000 40.92451  ? 129 ASN A C     1 
ATOM   435  O  O     . ASN A 1 65  ? -12.66984 -13.80589 33.85956  1.000 40.77062  ? 129 ASN A O     1 
ATOM   436  C  CB    . ASN A 1 65  ? -11.77989 -10.95589 33.92724  1.000 34.20902  ? 129 ASN A CB    1 
ATOM   437  C  CG    . ASN A 1 65  ? -11.63885 -10.18804 32.63166  1.000 34.46171  ? 129 ASN A CG    1 
ATOM   438  O  OD1   . ASN A 1 65  ? -12.30424 -10.49972 31.64152  1.000 40.26553  ? 129 ASN A OD1   1 
ATOM   439  N  ND2   . ASN A 1 65  ? -10.81260 -9.14380  32.64249  1.000 31.35269  ? 129 ASN A ND2   1 
ATOM   440  N  N     . GLU A 1 66  ? -14.39711 -13.03158 32.65390  1.000 47.03080  ? 130 GLU A N     1 
ATOM   441  C  CA    . GLU A 1 66  ? -14.70602 -14.38191 32.18404  1.000 51.25352  ? 130 GLU A CA    1 
ATOM   442  C  C     . GLU A 1 66  ? -13.80895 -14.83626 31.03677  1.000 51.85485  ? 130 GLU A C     1 
ATOM   443  O  O     . GLU A 1 66  ? -13.87728 -16.00583 30.64124  1.000 48.21771  ? 130 GLU A O     1 
ATOM   444  C  CB    . GLU A 1 66  ? -16.18035 -14.47806 31.77632  1.000 49.45081  ? 130 GLU A CB    1 
ATOM   445  C  CG    . GLU A 1 66  ? -17.06622 -13.47142 32.49071  1.000 52.07962  ? 130 GLU A CG    1 
ATOM   446  C  CD    . GLU A 1 66  ? -17.42780 -13.90134 33.90874  1.000 64.18885  ? 130 GLU A CD    1 
ATOM   447  O  OE1   . GLU A 1 66  ? -18.03494 -13.09017 34.64581  1.000 66.42792  ? 130 GLU A OE1   1 
ATOM   448  O  OE2   . GLU A 1 66  ? -17.13895 -15.06112 34.27581  1.000 71.51036  ? 130 GLU A OE2   1 
ATOM   449  N  N     . GLU A 1 67  ? -12.95312 -13.95355 30.53569  1.000 31.07908  ? 131 GLU A N     1 
ATOM   450  C  CA    . GLU A 1 67  ? -12.07332 -14.19600 29.40454  1.000 29.63755  ? 131 GLU A CA    1 
ATOM   451  C  C     . GLU A 1 67  ? -10.69107 -14.67248 29.85080  1.000 31.38863  ? 131 GLU A C     1 
ATOM   452  O  O     . GLU A 1 67  ? -10.20477 -14.32673 30.93277  1.000 28.17359  ? 131 GLU A O     1 
ATOM   453  C  CB    . GLU A 1 67  ? -11.98529 -12.90609 28.58850  1.000 32.03622  ? 131 GLU A CB    1 
ATOM   454  C  CG    . GLU A 1 67  ? -10.79011 -12.02622 28.87719  1.000 30.53703  ? 131 GLU A CG    1 
ATOM   455  C  CD    . GLU A 1 67  ? -10.49259 -11.03605 27.75425  1.000 30.82506  ? 131 GLU A CD    1 
ATOM   456  O  OE1   . GLU A 1 67  ? -11.28200 -10.08323 27.57278  1.000 27.19877  ? 131 GLU A OE1   1 
ATOM   457  O  OE2   . GLU A 1 67  ? -9.44235  -11.15201 27.10707  1.000 32.05199  ? 131 GLU A OE2   1 
ATOM   458  N  N     . LEU A 1 68  ? -10.06633 -15.49849 28.99961  1.000 22.46973  ? 132 LEU A N     1 
ATOM   459  C  CA    . LEU A 1 68  ? -8.74463  -16.09748 29.24826  1.000 26.07485  ? 132 LEU A CA    1 
ATOM   460  C  C     . LEU A 1 68  ? -7.84824  -15.74446 28.05887  1.000 20.88794  ? 132 LEU A C     1 
ATOM   461  O  O     . LEU A 1 68  ? -7.69009  -16.53364 27.12723  1.000 20.95082  ? 132 LEU A O     1 
ATOM   462  C  CB    . LEU A 1 68  ? -8.85774  -17.62217 29.42977  1.000 21.54985  ? 132 LEU A CB    1 
ATOM   463  C  CG    . LEU A 1 68  ? -9.48250  -18.10990 30.73230  1.000 21.40735  ? 132 LEU A CG    1 
ATOM   464  C  CD1   . LEU A 1 68  ? -9.44149  -19.63536 30.85597  1.000 20.56200  ? 132 LEU A CD1   1 
ATOM   465  C  CD2   . LEU A 1 68  ? -8.78189  -17.45379 31.89824  1.000 20.98439  ? 132 LEU A CD2   1 
ATOM   466  N  N     . THR A 1 69  ? -7.25168  -14.55527 28.08468  1.000 22.02700  ? 133 THR A N     1 
ATOM   467  C  CA    . THR A 1 69  ? -6.49320  -14.08550 26.93522  1.000 21.34016  ? 133 THR A CA    1 
ATOM   468  C  C     . THR A 1 69  ? -5.28438  -13.28122 27.37640  1.000 21.28490  ? 133 THR A C     1 
ATOM   469  O  O     . THR A 1 69  ? -5.14426  -12.89458 28.54172  1.000 19.21310  ? 133 THR A O     1 
ATOM   470  C  CB    . THR A 1 69  ? -7.31005  -13.17225 26.02443  1.000 22.16477  ? 133 THR A CB    1 
ATOM   471  O  OG1   . THR A 1 69  ? -7.37251  -11.88175 26.63642  1.000 21.76418  ? 133 THR A OG1   1 
ATOM   472  C  CG2   . THR A 1 69  ? -8.71587  -13.70725 25.78014  1.000 24.40114  ? 133 THR A CG2   1 
ATOM   473  N  N     . VAL A 1 70  ? -4.43599  -13.01193 26.39089  1.000 10.17857  ? 134 VAL A N     1 
ATOM   474  C  CA    . VAL A 1 70  ? -3.34776  -12.04920 26.44695  1.000 12.07781  ? 134 VAL A CA    1 
ATOM   475  C  C     . VAL A 1 70  ? -3.62643  -10.98339 25.39912  1.000 15.54896  ? 134 VAL A C     1 
ATOM   476  O  O     . VAL A 1 70  ? -4.01401  -11.31171 24.27072  1.000 14.41941  ? 134 VAL A O     1 
ATOM   477  C  CB    . VAL A 1 70  ? -1.98688  -12.71759 26.17005  1.000 12.07212  ? 134 VAL A CB    1 
ATOM   478  C  CG1   . VAL A 1 70  ? -0.83794  -11.73046 26.40298  1.000 12.58965  ? 134 VAL A CG1   1 
ATOM   479  C  CG2   . VAL A 1 70  ? -1.83586  -13.92905 27.02309  1.000 13.72635  ? 134 VAL A CG2   1 
ATOM   480  N  N     . LYS A 1 71  ? -3.42700  -9.71386  25.76737  1.000 18.78721  ? 135 LYS A N     1 
ATOM   481  C  CA    . LYS A 1 71  ? -3.67296  -8.58092  24.87868  1.000 18.35717  ? 135 LYS A CA    1 
ATOM   482  C  C     . LYS A 1 71  ? -2.49591  -7.62146  24.95717  1.000 19.79863  ? 135 LYS A C     1 
ATOM   483  O  O     . LYS A 1 71  ? -2.20211  -7.08410  26.02593  1.000 20.48456  ? 135 LYS A O     1 
ATOM   484  C  CB    . LYS A 1 71  ? -4.97340  -7.85897  25.24766  1.000 18.23675  ? 135 LYS A CB    1 
ATOM   485  C  CG    . LYS A 1 71  ? -6.18861  -8.77942  25.27369  1.000 24.26060  ? 135 LYS A CG    1 
ATOM   486  C  CD    . LYS A 1 71  ? -7.49407  -8.01243  25.31285  1.000 19.93913  ? 135 LYS A CD    1 
ATOM   487  C  CE    . LYS A 1 71  ? -8.53916  -8.65249  24.40798  1.000 24.92556  ? 135 LYS A CE    1 
ATOM   488  N  NZ    . LYS A 1 71  ? -9.88988  -8.58340  25.07196  1.000 29.39452  ? 135 LYS A NZ    1 
ATOM   489  N  N     . ILE A 1 72  ? -1.84369  -7.38837  23.82407  1.000 16.41074  ? 136 ILE A N     1 
ATOM   490  C  CA    . ILE A 1 72  ? -0.62440  -6.59600  23.75190  1.000 12.60144  ? 136 ILE A CA    1 
ATOM   491  C  C     . ILE A 1 72  ? -0.95428  -5.30171  23.03938  1.000 16.29259  ? 136 ILE A C     1 
ATOM   492  O  O     . ILE A 1 72  ? -1.58968  -5.31828  21.97987  1.000 17.07929  ? 136 ILE A O     1 
ATOM   493  C  CB    . ILE A 1 72  ? 0.48910   -7.33652  22.99755  1.000 16.06839  ? 136 ILE A CB    1 
ATOM   494  C  CG1   . ILE A 1 72  ? 0.85771   -8.61133  23.74611  1.000 14.33970  ? 136 ILE A CG1   1 
ATOM   495  C  CG2   . ILE A 1 72  ? 1.67859   -6.38802  22.76198  1.000 13.60695  ? 136 ILE A CG2   1 
ATOM   496  C  CD1   . ILE A 1 72  ? 1.51839   -9.66972  22.87301  1.000 15.98213  ? 136 ILE A CD1   1 
ATOM   497  N  N     . LYS A 1 73  ? -0.52961  -4.18493  23.60552  1.000 17.23033  ? 137 LYS A N     1 
ATOM   498  C  CA    . LYS A 1 73  ? -0.81354  -2.94666  22.90685  1.000 18.99376  ? 137 LYS A CA    1 
ATOM   499  C  C     . LYS A 1 73  ? 0.30159   -1.93212  23.10175  1.000 19.47787  ? 137 LYS A C     1 
ATOM   500  O  O     . LYS A 1 73  ? 0.74766   -1.68907  24.22630  1.000 17.63209  ? 137 LYS A O     1 
ATOM   501  C  CB    . LYS A 1 73  ? -2.19260  -2.40955  23.31418  1.000 19.07369  ? 137 LYS A CB    1 
ATOM   502  C  CG    . LYS A 1 73  ? -2.37601  -1.66127  24.57382  1.000 24.81386  ? 137 LYS A CG    1 
ATOM   503  C  CD    . LYS A 1 73  ? -3.67552  -0.86276  24.37654  1.000 24.26300  ? 137 LYS A CD    1 
ATOM   504  C  CE    . LYS A 1 73  ? -4.14949  -0.15871  25.63623  1.000 30.65516  ? 137 LYS A CE    1 
ATOM   505  N  NZ    . LYS A 1 73  ? -5.41743  -0.78834  26.14103  1.000 26.69870  ? 137 LYS A NZ    1 
ATOM   506  N  N     . CYS A 1 74  ? 0.77446   -1.38723  21.97447  1.000 17.38057  ? 138 CYS A N     1 
ATOM   507  C  CA    . CYS A 1 74  ? 1.79126   -0.34456  21.95670  1.000 20.14253  ? 138 CYS A CA    1 
ATOM   508  C  C     . CYS A 1 74  ? 1.11903   1.00422   22.10494  1.000 21.17806  ? 138 CYS A C     1 
ATOM   509  O  O     . CYS A 1 74  ? 0.16433   1.31043   21.38243  1.000 22.47915  ? 138 CYS A O     1 
ATOM   510  C  CB    . CYS A 1 74  ? 2.58706   -0.33786  20.65176  1.000 16.01990  ? 138 CYS A CB    1 
ATOM   511  S  SG    . CYS A 1 74  ? 2.87371   -1.94083  19.92834  1.000 20.80690  ? 138 CYS A SG    1 
ATOM   512  N  N     . ASP A 1 75  ? 1.63609   1.82243   23.00778  1.000 15.02341  ? 139 ASP A N     1 
ATOM   513  C  CA    . ASP A 1 75  ? 1.20744   3.20865   23.09100  1.000 17.39073  ? 139 ASP A CA    1 
ATOM   514  C  C     . ASP A 1 75  ? 2.40842   4.07849   22.72528  1.000 17.18007  ? 139 ASP A C     1 
ATOM   515  O  O     . ASP A 1 75  ? 3.09977   4.62032   23.59029  1.000 20.86526  ? 139 ASP A O     1 
ATOM   516  C  CB    . ASP A 1 75  ? 0.67469   3.53421   24.45121  1.000 19.13690  ? 139 ASP A CB    1 
ATOM   517  C  CG    . ASP A 1 75  ? -0.05445  4.84454   24.46225  1.000 22.51465  ? 139 ASP A CG    1 
ATOM   518  O  OD1   . ASP A 1 75  ? 0.21064   5.64220   23.55039  1.000 25.06941  ? 139 ASP A OD1   1 
ATOM   519  O  OD2   . ASP A 1 75  ? -0.87087  5.09605   25.36880  1.000 21.85437  ? 139 ASP A OD2   1 
ATOM   520  N  N     . LYS A 1 76  ? 2.61347   4.24952   21.41415  1.000 17.29988  ? 140 LYS A N     1 
ATOM   521  C  CA    . LYS A 1 76  ? 3.78211   4.95769   20.89880  1.000 15.79769  ? 140 LYS A CA    1 
ATOM   522  C  C     . LYS A 1 76  ? 3.81977   6.41348   21.34976  1.000 17.18061  ? 140 LYS A C     1 
ATOM   523  O  O     . LYS A 1 76  ? 4.90698   6.96041   21.59005  1.000 20.29923  ? 140 LYS A O     1 
ATOM   524  C  CB    . LYS A 1 76  ? 3.79888   4.86995   19.37053  1.000 24.79063  ? 140 LYS A CB    1 
ATOM   525  C  CG    . LYS A 1 76  ? 4.93860   5.63839   18.70909  1.000 25.05612  ? 140 LYS A CG    1 
ATOM   526  C  CD    . LYS A 1 76  ? 4.84936   5.59670   17.18694  1.000 25.23352  ? 140 LYS A CD    1 
ATOM   527  C  CE    . LYS A 1 76  ? 5.97064   6.41143   16.56306  1.000 25.56008  ? 140 LYS A CE    1 
ATOM   528  N  NZ    . LYS A 1 76  ? 5.99844   6.29360   15.06926  1.000 25.79880  ? 140 LYS A NZ    1 
ATOM   529  N  N     . GLU A 1 77  ? 2.65642   7.06206   21.46552  1.000 19.53227  ? 141 GLU A N     1 
ATOM   530  C  CA    . GLU A 1 77  ? 2.63075   8.44239   21.94517  1.000 24.71813  ? 141 GLU A CA    1 
ATOM   531  C  C     . GLU A 1 77  ? 3.20638   8.55392   23.35462  1.000 29.62030  ? 141 GLU A C     1 
ATOM   532  O  O     . GLU A 1 77  ? 3.89416   9.53079   23.67856  1.000 28.31473  ? 141 GLU A O     1 
ATOM   533  C  CB    . GLU A 1 77  ? 1.20040   8.98754   21.91515  1.000 28.89721  ? 141 GLU A CB    1 
ATOM   534  N  N     . LYS A 1 78  ? 2.92300   7.57367   24.21250  1.000 20.05422  ? 142 LYS A N     1 
ATOM   535  C  CA    . LYS A 1 78  ? 3.39072   7.58871   25.59066  1.000 16.85631  ? 142 LYS A CA    1 
ATOM   536  C  C     . LYS A 1 78  ? 4.67207   6.79728   25.78154  1.000 16.43597  ? 142 LYS A C     1 
ATOM   537  O  O     . LYS A 1 78  ? 5.14865   6.68156   26.91486  1.000 15.45737  ? 142 LYS A O     1 
ATOM   538  C  CB    . LYS A 1 78  ? 2.30263   7.03682   26.52246  1.000 18.25474  ? 142 LYS A CB    1 
ATOM   539  C  CG    . LYS A 1 78  ? 0.94097   7.70433   26.34050  1.000 23.99233  ? 142 LYS A CG    1 
ATOM   540  C  CD    . LYS A 1 78  ? 0.36207   8.16075   27.66816  1.000 22.87062  ? 142 LYS A CD    1 
ATOM   541  C  CE    . LYS A 1 78  ? -0.41233  9.46598   27.47695  1.000 29.93581  ? 142 LYS A CE    1 
ATOM   542  N  N     . ASN A 1 79  ? 5.22491   6.24060   24.70734  1.000 23.08307  ? 143 ASN A N     1 
ATOM   543  C  CA    . ASN A 1 79  ? 6.42919   5.41532   24.77240  1.000 19.00259  ? 143 ASN A CA    1 
ATOM   544  C  C     . ASN A 1 79  ? 6.21117   4.19157   25.66954  1.000 18.10673  ? 143 ASN A C     1 
ATOM   545  O  O     . ASN A 1 79  ? 7.07438   3.80365   26.46284  1.000 16.67339  ? 143 ASN A O     1 
ATOM   546  C  CB    . ASN A 1 79  ? 7.62960   6.26119   25.22459  1.000 16.67389  ? 143 ASN A CB    1 
ATOM   547  C  CG    . ASN A 1 79  ? 8.91436   5.46042   25.30324  1.000 21.79207  ? 143 ASN A CG    1 
ATOM   548  O  OD1   . ASN A 1 79  ? 9.27813   4.74909   24.36048  1.000 22.69612  ? 143 ASN A OD1   1 
ATOM   549  N  ND2   . ASN A 1 79  ? 9.59306   5.54414   26.44881  1.000 20.87398  ? 143 ASN A ND2   1 
ATOM   550  N  N     . LEU A 1 80  ? 5.05395   3.53979   25.52788  1.000 11.90637  ? 144 LEU A N     1 
ATOM   551  C  CA    . LEU A 1 80  ? 4.71297   2.42222   26.39907  1.000 12.27325  ? 144 LEU A CA    1 
ATOM   552  C  C     . LEU A 1 80  ? 4.32705   1.19284   25.59251  1.000 12.64435  ? 144 LEU A C     1 
ATOM   553  O  O     . LEU A 1 80  ? 3.74926   1.28943   24.50469  1.000 16.22973  ? 144 LEU A O     1 
ATOM   554  C  CB    . LEU A 1 80  ? 3.56282   2.78571   27.37477  1.000 13.01460  ? 144 LEU A CB    1 
ATOM   555  C  CG    . LEU A 1 80  ? 3.72980   3.98486   28.30890  1.000 13.96455  ? 144 LEU A CG    1 
ATOM   556  C  CD1   . LEU A 1 80  ? 2.43145   4.25569   29.08549  1.000 10.24321  ? 144 LEU A CD1   1 
ATOM   557  C  CD2   . LEU A 1 80  ? 4.90342   3.77743   29.27611  1.000 12.07827  ? 144 LEU A CD2   1 
ATOM   558  N  N     . LEU A 1 81  ? 4.67144   0.02673   26.13554  1.000 12.45262  ? 145 LEU A N     1 
ATOM   559  C  CA    . LEU A 1 81  ? 4.25645   -1.26573  25.61811  1.000 12.35640  ? 145 LEU A CA    1 
ATOM   560  C  C     . LEU A 1 81  ? 3.58203   -2.01377  26.76169  1.000 13.94327  ? 145 LEU A C     1 
ATOM   561  O  O     . LEU A 1 81  ? 4.17059   -2.15308  27.84013  1.000 11.69840  ? 145 LEU A O     1 
ATOM   562  C  CB    . LEU A 1 81  ? 5.46120   -2.05174  25.10025  1.000 9.17452   ? 145 LEU A CB    1 
ATOM   563  C  CG    . LEU A 1 81  ? 5.19288   -3.48549  24.68654  1.000 10.17536  ? 145 LEU A CG    1 
ATOM   564  C  CD1   . LEU A 1 81  ? 4.32068   -3.48891  23.44813  1.000 11.84379  ? 145 LEU A CD1   1 
ATOM   565  C  CD2   . LEU A 1 81  ? 6.49196   -4.19894  24.42759  1.000 18.27872  ? 145 LEU A CD2   1 
ATOM   566  N  N     . HIS A 1 82  ? 2.34795   -2.47109  26.54429  1.000 10.71108  ? 146 HIS A N     1 
ATOM   567  C  CA    . HIS A 1 82  ? 1.54468   -3.09618  27.59143  1.000 9.15463   ? 146 HIS A CA    1 
ATOM   568  C  C     . HIS A 1 82  ? 1.29575   -4.55005  27.22863  1.000 13.87283  ? 146 HIS A C     1 
ATOM   569  O  O     . HIS A 1 82  ? 0.93933   -4.85304  26.08571  1.000 13.53027  ? 146 HIS A O     1 
ATOM   570  C  CB    . HIS A 1 82  ? 0.19381   -2.39168  27.75827  1.000 11.19472  ? 146 HIS A CB    1 
ATOM   571  C  CG    . HIS A 1 82  ? 0.27711   -0.93472  28.10837  1.000 12.25215  ? 146 HIS A CG    1 
ATOM   572  N  ND1   . HIS A 1 82  ? 0.48942   -0.48276  29.39499  1.000 16.21235  ? 146 HIS A ND1   1 
ATOM   573  C  CD2   . HIS A 1 82  ? 0.13803   0.17374   27.34125  1.000 11.05232  ? 146 HIS A CD2   1 
ATOM   574  C  CE1   . HIS A 1 82  ? 0.48694   0.83967   29.40274  1.000 17.98158  ? 146 HIS A CE1   1 
ATOM   575  N  NE2   . HIS A 1 82  ? 0.27604   1.26304   28.16945  1.000 11.93584  ? 146 HIS A NE2   1 
ATOM   576  N  N     . VAL A 1 83  ? 1.45904   -5.45025  28.19320  1.000 9.05797   ? 147 VAL A N     1 
ATOM   577  C  CA    . VAL A 1 83  ? 1.15364   -6.86266  27.99118  1.000 9.62483   ? 147 VAL A CA    1 
ATOM   578  C  C     . VAL A 1 83  ? 0.18110   -7.25509  29.09594  1.000 8.85934   ? 147 VAL A C     1 
ATOM   579  O  O     . VAL A 1 83  ? 0.54555   -7.24932  30.27683  1.000 8.57996   ? 147 VAL A O     1 
ATOM   580  C  CB    . VAL A 1 83  ? 2.41222   -7.74115  28.00956  1.000 11.58374  ? 147 VAL A CB    1 
ATOM   581  C  CG1   . VAL A 1 83  ? 2.06429   -9.19394  27.74132  1.000 13.59317  ? 147 VAL A CG1   1 
ATOM   582  C  CG2   . VAL A 1 83  ? 3.40446   -7.22697  26.97171  1.000 10.62098  ? 147 VAL A CG2   1 
ATOM   583  N  N     . THR A 1 84  ? -1.05875  -7.57463  28.72145  1.000 12.08654  ? 148 THR A N     1 
ATOM   584  C  CA    . THR A 1 84  ? -2.14147  -7.73604  29.68609  1.000 12.73622  ? 148 THR A CA    1 
ATOM   585  C  C     . THR A 1 84  ? -2.76153  -9.11637  29.54144  1.000 14.26730  ? 148 THR A C     1 
ATOM   586  O  O     . THR A 1 84  ? -3.22304  -9.49183  28.45662  1.000 13.50675  ? 148 THR A O     1 
ATOM   587  C  CB    . THR A 1 84  ? -3.20212  -6.65190  29.50129  1.000 13.90752  ? 148 THR A CB    1 
ATOM   588  O  OG1   . THR A 1 84  ? -2.60956  -5.35750  29.69321  1.000 16.36970  ? 148 THR A OG1   1 
ATOM   589  C  CG2   . THR A 1 84  ? -4.31940  -6.82651  30.51185  1.000 9.99400   ? 148 THR A CG2   1 
ATOM   590  N  N     . ASP A 1 85  ? -2.76033  -9.86906  30.63171  1.000 15.56454  ? 149 ASP A N     1 
ATOM   591  C  CA    . ASP A 1 85  ? -3.33583  -11.19477 30.67762  1.000 16.83423  ? 149 ASP A CA    1 
ATOM   592  C  C     . ASP A 1 85  ? -4.49161  -11.18845 31.66211  1.000 17.17700  ? 149 ASP A C     1 
ATOM   593  O  O     . ASP A 1 85  ? -4.49530  -10.42450 32.62726  1.000 17.35056  ? 149 ASP A O     1 
ATOM   594  C  CB    . ASP A 1 85  ? -2.26962  -12.21305 31.05774  1.000 15.19528  ? 149 ASP A CB    1 
ATOM   595  C  CG    . ASP A 1 85  ? -1.83187  -12.09376 32.50298  1.000 15.53200  ? 149 ASP A CG    1 
ATOM   596  O  OD1   . ASP A 1 85  ? -2.64696  -12.32988 33.42200  1.000 18.30746  ? 149 ASP A OD1   1 
ATOM   597  O  OD2   . ASP A 1 85  ? -0.65008  -11.72673 32.71282  1.000 17.53482  ? 149 ASP A OD2   1 
ATOM   598  N  N     . THR A 1 86  ? -5.51277  -11.97947 31.37564  1.000 12.94018  ? 150 THR A N     1 
ATOM   599  C  CA    . THR A 1 86  ? -6.56430  -12.19829 32.36710  1.000 13.09743  ? 150 THR A CA    1 
ATOM   600  C  C     . THR A 1 86  ? -6.27922  -13.46608 33.16780  1.000 13.19233  ? 150 THR A C     1 
ATOM   601  O  O     . THR A 1 86  ? -7.12775  -14.33520 33.35287  1.000 15.28724  ? 150 THR A O     1 
ATOM   602  C  CB    . THR A 1 86  ? -7.92102  -12.25303 31.67473  1.000 17.33201  ? 150 THR A CB    1 
ATOM   603  O  OG1   . THR A 1 86  ? -7.86155  -13.17371 30.58083  1.000 15.22316  ? 150 THR A OG1   1 
ATOM   604  C  CG2   . THR A 1 86  ? -8.27142  -10.86433 31.10173  1.000 17.82523  ? 150 THR A CG2   1 
ATOM   605  N  N     . GLY A 1 87  ? -5.06125  -13.58006 33.68260  1.000 13.45210  ? 151 GLY A N     1 
ATOM   606  C  CA    . GLY A 1 87  ? -4.63916  -14.75490 34.41620  1.000 17.94796  ? 151 GLY A CA    1 
ATOM   607  C  C     . GLY A 1 87  ? -4.99973  -14.66380 35.88646  1.000 18.24190  ? 151 GLY A C     1 
ATOM   608  O  O     . GLY A 1 87  ? -5.91284  -13.93913 36.28950  1.000 16.47444  ? 151 GLY A O     1 
ATOM   609  N  N     . VAL A 1 88  ? -4.24575  -15.40675 36.70232  1.000 16.87989  ? 152 VAL A N     1 
ATOM   610  C  CA    . VAL A 1 88  ? -4.49961  -15.46665 38.13958  1.000 19.43056  ? 152 VAL A CA    1 
ATOM   611  C  C     . VAL A 1 88  ? -4.23315  -14.14319 38.84854  1.000 15.01430  ? 152 VAL A C     1 
ATOM   612  O  O     . VAL A 1 88  ? -4.81772  -13.89176 39.90617  1.000 16.70942  ? 152 VAL A O     1 
ATOM   613  C  CB    . VAL A 1 88  ? -3.66873  -16.60420 38.75849  1.000 19.83481  ? 152 VAL A CB    1 
ATOM   614  C  CG1   . VAL A 1 88  ? -2.18339  -16.25850 38.72451  1.000 23.36213  ? 152 VAL A CG1   1 
ATOM   615  C  CG2   . VAL A 1 88  ? -4.13485  -16.91322 40.18385  1.000 18.91579  ? 152 VAL A CG2   1 
ATOM   616  N  N     . GLY A 1 89  ? -3.37771  -13.28106 38.30363  1.000 15.61351  ? 153 GLY A N     1 
ATOM   617  C  CA    . GLY A 1 89  ? -3.02786  -12.04350 38.98685  1.000 15.94092  ? 153 GLY A CA    1 
ATOM   618  C  C     . GLY A 1 89  ? -2.08302  -12.30886 40.15132  1.000 16.32434  ? 153 GLY A C     1 
ATOM   619  O  O     . GLY A 1 89  ? -1.74212  -13.44875 40.46710  1.000 18.48949  ? 153 GLY A O     1 
ATOM   620  N  N     . MET A 1 90  ? -1.64314  -11.21956 40.79163  1.000 17.16887  ? 154 MET A N     1 
ATOM   621  C  CA    . MET A 1 90  ? -0.87556  -11.29148 42.03332  1.000 17.59472  ? 154 MET A CA    1 
ATOM   622  C  C     . MET A 1 90  ? -1.44526  -10.39458 43.12060  1.000 19.23196  ? 154 MET A C     1 
ATOM   623  O  O     . MET A 1 90  ? -1.85826  -9.26065  42.86695  1.000 19.69994  ? 154 MET A O     1 
ATOM   624  C  CB    . MET A 1 90  ? 0.62479   -10.96269 41.83624  1.000 15.37217  ? 154 MET A CB    1 
ATOM   625  C  CG    . MET A 1 90  ? 1.31422   -11.84721 40.78130  1.000 22.86951  ? 154 MET A CG    1 
ATOM   626  S  SD    . MET A 1 90  ? 2.78473   -11.10541 40.05990  1.000 21.28363  ? 154 MET A SD    1 
ATOM   627  C  CE    . MET A 1 90  ? 2.01320   -10.12251 38.79263  1.000 15.63579  ? 154 MET A CE    1 
ATOM   628  N  N     . THR A 1 91  ? -1.45553  -10.92675 44.34155  1.000 16.07565  ? 155 THR A N     1 
ATOM   629  C  CA    . THR A 1 91  ? -1.78153  -10.15090 45.52244  1.000 16.58461  ? 155 THR A CA    1 
ATOM   630  C  C     . THR A 1 91  ? -0.65584  -9.16700  45.81531  1.000 17.21689  ? 155 THR A C     1 
ATOM   631  O  O     . THR A 1 91  ? 0.41094   -9.20516  45.19147  1.000 16.24533  ? 155 THR A O     1 
ATOM   632  C  CB    . THR A 1 91  ? -2.00209  -11.07306 46.70969  1.000 17.25238  ? 155 THR A CB    1 
ATOM   633  O  OG1   . THR A 1 91  ? -0.74565  -11.65551 47.08396  1.000 19.35947  ? 155 THR A OG1   1 
ATOM   634  C  CG2   . THR A 1 91  ? -2.96049  -12.19603 46.34122  1.000 15.65777  ? 155 THR A CG2   1 
ATOM   635  N  N     . ARG A 1 92  ? -0.90987  -8.25275  46.75433  1.000 18.77531  ? 156 ARG A N     1 
ATOM   636  C  CA    . ARG A 1 92  ? 0.14232   -7.33109  47.17592  1.000 20.25943  ? 156 ARG A CA    1 
ATOM   637  C  C     . ARG A 1 92  ? 1.32880   -8.09471  47.74102  1.000 20.13499  ? 156 ARG A C     1 
ATOM   638  O  O     . ARG A 1 92  ? 2.48384   -7.80208  47.41689  1.000 22.31649  ? 156 ARG A O     1 
ATOM   639  C  CB    . ARG A 1 92  ? -0.37628  -6.35244  48.22635  1.000 20.00264  ? 156 ARG A CB    1 
ATOM   640  C  CG    . ARG A 1 92  ? 0.72649   -5.44905  48.78665  1.000 21.81395  ? 156 ARG A CG    1 
ATOM   641  C  CD    . ARG A 1 92  ? 0.30532   -4.79784  50.07929  1.000 22.71314  ? 156 ARG A CD    1 
ATOM   642  N  NE    . ARG A 1 92  ? 1.33124   -3.91894  50.63628  1.000 30.03383  ? 156 ARG A NE    1 
ATOM   643  C  CZ    . ARG A 1 92  ? 2.29386   -4.29287  51.47202  1.000 29.72387  ? 156 ARG A CZ    1 
ATOM   644  N  NH1   . ARG A 1 92  ? 2.38179   -5.53215  51.91866  1.000 25.95629  ? 156 ARG A NH1   1 
ATOM   645  N  NH2   . ARG A 1 92  ? 3.17025   -3.38516  51.90039  1.000 30.53645  ? 156 ARG A NH2   1 
ATOM   646  N  N     . GLU A 1 93  ? 1.05801   -9.07826  48.59835  1.000 20.52496  ? 157 GLU A N     1 
ATOM   647  C  CA    . GLU A 1 93  ? 2.13457   -9.86002  49.19220  1.000 22.56676  ? 157 GLU A CA    1 
ATOM   648  C  C     . GLU A 1 93  ? 3.00255   -10.49747 48.11264  1.000 22.37965  ? 157 GLU A C     1 
ATOM   649  O  O     . GLU A 1 93  ? 4.23646   -10.51334 48.22330  1.000 20.88084  ? 157 GLU A O     1 
ATOM   650  C  CB    . GLU A 1 93  ? 1.54451   -10.91502 50.12168  1.000 20.93664  ? 157 GLU A CB    1 
ATOM   651  C  CG    . GLU A 1 93  ? 2.55270   -11.90596 50.66284  1.000 25.19750  ? 157 GLU A CG    1 
ATOM   652  C  CD    . GLU A 1 93  ? 1.92690   -12.93854 51.58510  1.000 28.34999  ? 157 GLU A CD    1 
ATOM   653  O  OE1   . GLU A 1 93  ? 0.74305   -13.29732 51.37984  1.000 26.04162  ? 157 GLU A OE1   1 
ATOM   654  O  OE2   . GLU A 1 93  ? 2.62537   -13.40256 52.51588  1.000 30.95006  ? 157 GLU A OE2   1 
ATOM   655  N  N     . GLU A 1 94  ? 2.37938   -11.00463 47.04768  1.000 22.75410  ? 158 GLU A N     1 
ATOM   656  C  CA    . GLU A 1 94  ? 3.16083   -11.58354 45.96159  1.000 28.70883  ? 158 GLU A CA    1 
ATOM   657  C  C     . GLU A 1 94  ? 3.99633   -10.52149 45.25353  1.000 28.68615  ? 158 GLU A C     1 
ATOM   658  O  O     . GLU A 1 94  ? 5.17252   -10.75673 44.95096  1.000 25.45143  ? 158 GLU A O     1 
ATOM   659  C  CB    . GLU A 1 94  ? 2.24103   -12.32734 44.99299  1.000 25.57360  ? 158 GLU A CB    1 
ATOM   660  C  CG    . GLU A 1 94  ? 1.62626   -13.58548 45.64535  1.000 27.29213  ? 158 GLU A CG    1 
ATOM   661  C  CD    . GLU A 1 94  ? 0.56182   -14.28562 44.81318  1.000 26.89966  ? 158 GLU A CD    1 
ATOM   662  O  OE1   . GLU A 1 94  ? -0.30224  -13.61654 44.22512  1.000 26.13095  ? 158 GLU A OE1   1 
ATOM   663  O  OE2   . GLU A 1 94  ? 0.55359   -15.53390 44.79104  1.000 37.01733  ? 158 GLU A OE2   1 
ATOM   664  N  N     . LEU A 1 95  ? 3.42448   -9.33535  45.00783  1.000 25.47767  ? 159 LEU A N     1 
ATOM   665  C  CA    . LEU A 1 95  ? 4.19520   -8.27991  44.35135  1.000 22.61332  ? 159 LEU A CA    1 
ATOM   666  C  C     . LEU A 1 95  ? 5.35539   -7.81799  45.21801  1.000 26.66141  ? 159 LEU A C     1 
ATOM   667  O  O     . LEU A 1 95  ? 6.38068   -7.37095  44.69290  1.000 25.52925  ? 159 LEU A O     1 
ATOM   668  C  CB    . LEU A 1 95  ? 3.30427   -7.08855  43.99783  1.000 18.51433  ? 159 LEU A CB    1 
ATOM   669  C  CG    . LEU A 1 95  ? 2.21635   -7.32569  42.95247  1.000 21.00718  ? 159 LEU A CG    1 
ATOM   670  C  CD1   . LEU A 1 95  ? 1.18070   -6.19877  43.00157  1.000 16.16883  ? 159 LEU A CD1   1 
ATOM   671  C  CD2   . LEU A 1 95  ? 2.84824   -7.42758  41.57214  1.000 17.83172  ? 159 LEU A CD2   1 
ATOM   672  N  N     . VAL A 1 96  ? 5.21469   -7.91332  46.54046  1.000 24.96205  ? 160 VAL A N     1 
ATOM   673  C  CA    . VAL A 1 96  ? 6.26116   -7.43740  47.43892  1.000 27.74596  ? 160 VAL A CA    1 
ATOM   674  C  C     . VAL A 1 96  ? 7.34658   -8.49015  47.62392  1.000 29.78748  ? 160 VAL A C     1 
ATOM   675  O  O     . VAL A 1 96  ? 8.54040   -8.17052  47.59070  1.000 31.30201  ? 160 VAL A O     1 
ATOM   676  C  CB    . VAL A 1 96  ? 5.65027   -7.01664  48.78709  1.000 26.63876  ? 160 VAL A CB    1 
ATOM   677  C  CG1   . VAL A 1 96  ? 6.72599   -6.95976  49.85461  1.000 28.66256  ? 160 VAL A CG1   1 
ATOM   678  C  CG2   . VAL A 1 96  ? 4.95246   -5.67765  48.65850  1.000 24.29549  ? 160 VAL A CG2   1 
ATOM   679  N  N     . LYS A 1 97  ? 6.96043   -9.75403  47.82853  1.000 37.01539  ? 161 LYS A N     1 
ATOM   680  C  CA    . LYS A 1 97  ? 7.92721   -10.78719 48.17926  1.000 38.78392  ? 161 LYS A CA    1 
ATOM   681  C  C     . LYS A 1 97  ? 8.49452   -11.54438 46.98461  1.000 41.00143  ? 161 LYS A C     1 
ATOM   682  O  O     . LYS A 1 97  ? 9.51445   -12.22919 47.14015  1.000 44.95305  ? 161 LYS A O     1 
ATOM   683  C  CB    . LYS A 1 97  ? 7.30985   -11.81447 49.13396  1.000 46.37289  ? 161 LYS A CB    1 
ATOM   684  C  CG    . LYS A 1 97  ? 6.61519   -11.24191 50.35692  1.000 46.64852  ? 161 LYS A CG    1 
ATOM   685  C  CD    . LYS A 1 97  ? 6.10482   -12.37028 51.24477  1.000 47.39014  ? 161 LYS A CD    1 
ATOM   686  C  CE    . LYS A 1 97  ? 5.98459   -11.94119 52.69294  1.000 48.37205  ? 161 LYS A CE    1 
ATOM   687  N  NZ    . LYS A 1 97  ? 4.68197   -12.34887 53.27730  1.000 48.19609  ? 161 LYS A NZ    1 
ATOM   688  N  N     . ASN A 1 98  ? 7.87021   -11.47675 45.81259  1.000 65.82009  ? 162 ASN A N     1 
ATOM   689  C  CA    . ASN A 1 98  ? 8.35680   -12.27529 44.68996  1.000 65.51857  ? 162 ASN A CA    1 
ATOM   690  C  C     . ASN A 1 98  ? 9.55748   -11.51138 44.14664  1.000 63.50699  ? 162 ASN A C     1 
ATOM   691  O  O     . ASN A 1 98  ? 9.41273   -10.53153 43.41021  1.000 61.85726  ? 162 ASN A O     1 
ATOM   692  C  CB    . ASN A 1 98  ? 7.25627   -12.48629 43.65005  1.000 59.91926  ? 162 ASN A CB    1 
ATOM   693  C  CG    . ASN A 1 98  ? 7.77616   -12.85980 42.25214  1.000 60.46342  ? 162 ASN A CG    1 
ATOM   694  O  OD1   . ASN A 1 98  ? 8.97518   -12.87076 41.97271  1.000 60.45685  ? 162 ASN A OD1   1 
ATOM   695  N  ND2   . ASN A 1 98  ? 6.84000   -13.16166 41.35906  1.000 60.89785  ? 162 ASN A ND2   1 
ATOM   696  N  N     . LEU A 1 99  ? 10.74805  -11.95202 44.52543  1.000 68.07025  ? 163 LEU A N     1 
ATOM   697  C  CA    . LEU A 1 99  ? 11.98050  -11.33767 44.06316  1.000 67.19783  ? 163 LEU A CA    1 
ATOM   698  C  C     . LEU A 1 99  ? 13.11540  -12.34171 44.22282  1.000 67.60173  ? 163 LEU A C     1 
ATOM   699  O  O     . LEU A 1 99  ? 12.86982  -13.53945 44.38029  1.000 68.98718  ? 163 LEU A O     1 
ATOM   700  C  CB    . LEU A 1 99  ? 12.25949  -10.03017 44.82736  1.000 66.91126  ? 163 LEU A CB    1 
ATOM   701  C  CG    . LEU A 1 99  ? 12.46220  -10.02147 46.35137  1.000 68.60713  ? 163 LEU A CG    1 
ATOM   702  C  CD1   . LEU A 1 99  ? 13.87723  -10.43326 46.76362  1.000 68.48602  ? 163 LEU A CD1   1 
ATOM   703  C  CD2   . LEU A 1 99  ? 12.10662  -8.66232  46.94377  1.000 70.12681  ? 163 LEU A CD2   1 
ATOM   704  N  N     . THR A 1 124 ? 21.60433  -18.75739 27.85480  1.000 75.38332  ? 188 THR A N     1 
ATOM   705  C  CA    . THR A 1 124 ? 20.72933  -18.70784 29.02215  1.000 83.53662  ? 188 THR A CA    1 
ATOM   706  C  C     . THR A 1 124 ? 19.29907  -18.33052 28.62678  1.000 75.80060  ? 188 THR A C     1 
ATOM   707  O  O     . THR A 1 124 ? 18.50571  -17.88454 29.46068  1.000 69.26559  ? 188 THR A O     1 
ATOM   708  C  CB    . THR A 1 124 ? 21.25546  -17.71282 30.08500  1.000 74.51462  ? 188 THR A CB    1 
ATOM   709  O  OG1   . THR A 1 124 ? 21.37629  -16.40304 29.51406  1.000 74.38637  ? 188 THR A OG1   1 
ATOM   710  C  CG2   . THR A 1 124 ? 22.61172  -18.15599 30.60067  1.000 75.22501  ? 188 THR A CG2   1 
ATOM   711  N  N     . SER A 1 125 ? 18.97639  -18.51062 27.34265  1.000 76.08673  ? 189 SER A N     1 
ATOM   712  C  CA    . SER A 1 125 ? 17.59531  -18.34521 26.90302  1.000 79.37056  ? 189 SER A CA    1 
ATOM   713  C  C     . SER A 1 125 ? 16.67841  -19.36614 27.56420  1.000 79.78459  ? 189 SER A C     1 
ATOM   714  O  O     . SER A 1 125 ? 15.48834  -19.09755 27.76323  1.000 80.50922  ? 189 SER A O     1 
ATOM   715  C  CB    . SER A 1 125 ? 17.51025  -18.46046 25.38048  1.000 79.90815  ? 189 SER A CB    1 
ATOM   716  N  N     . GLU A 1 126 ? 17.20997  -20.53968 27.90581  1.000 90.53785  ? 190 GLU A N     1 
ATOM   717  C  CA    . GLU A 1 126 ? 16.44438  -21.57096 28.59450  1.000 90.92686  ? 190 GLU A CA    1 
ATOM   718  C  C     . GLU A 1 126 ? 16.61197  -21.49640 30.10655  1.000 87.31720  ? 190 GLU A C     1 
ATOM   719  O  O     . GLU A 1 126 ? 15.65070  -21.73074 30.84713  1.000 88.15876  ? 190 GLU A O     1 
ATOM   720  C  CB    . GLU A 1 126 ? 16.85796  -22.95830 28.09383  1.000 91.98907  ? 190 GLU A CB    1 
ATOM   721  N  N     . LEU A 1 127 ? 17.82042  -21.17608 30.57819  1.000 74.82573  ? 191 LEU A N     1 
ATOM   722  C  CA    . LEU A 1 127 ? 18.05527  -21.08746 32.01549  1.000 71.92560  ? 191 LEU A CA    1 
ATOM   723  C  C     . LEU A 1 127 ? 17.22012  -19.98361 32.65452  1.000 70.34311  ? 191 LEU A C     1 
ATOM   724  O  O     . LEU A 1 127 ? 16.81367  -20.10972 33.81557  1.000 71.59806  ? 191 LEU A O     1 
ATOM   725  C  CB    . LEU A 1 127 ? 19.54402  -20.86615 32.29121  1.000 70.64608  ? 191 LEU A CB    1 
ATOM   726  N  N     . ILE A 1 128 ? 16.95227  -18.90013 31.91947  1.000 55.85356  ? 192 ILE A N     1 
ATOM   727  C  CA    . ILE A 1 128 ? 16.06669  -17.85660 32.43099  1.000 48.69066  ? 192 ILE A CA    1 
ATOM   728  C  C     . ILE A 1 128 ? 14.67364  -18.42563 32.67113  1.000 48.50739  ? 192 ILE A C     1 
ATOM   729  O  O     . ILE A 1 128 ? 14.05906  -18.20189 33.72166  1.000 47.56609  ? 192 ILE A O     1 
ATOM   730  C  CB    . ILE A 1 128 ? 16.02997  -16.65819 31.46503  1.000 47.51713  ? 192 ILE A CB    1 
ATOM   731  N  N     . GLY A 1 129 ? 14.16095  -19.18839 31.70535  1.000 42.12344  ? 193 GLY A N     1 
ATOM   732  C  CA    . GLY A 1 129 ? 12.90108  -19.87403 31.91583  1.000 41.46298  ? 193 GLY A CA    1 
ATOM   733  C  C     . GLY A 1 129 ? 12.97920  -20.99334 32.93137  1.000 47.03453  ? 193 GLY A C     1 
ATOM   734  O  O     . GLY A 1 129 ? 11.94038  -21.44054 33.42807  1.000 47.00537  ? 193 GLY A O     1 
ATOM   735  N  N     . GLN A 1 130 ? 14.18836  -21.45711 33.25176  1.000 67.18963  ? 194 GLN A N     1 
ATOM   736  C  CA    . GLN A 1 130 ? 14.33685  -22.51724 34.24321  1.000 67.99568  ? 194 GLN A CA    1 
ATOM   737  C  C     . GLN A 1 130 ? 14.07035  -21.99102 35.64979  1.000 59.51612  ? 194 GLN A C     1 
ATOM   738  O  O     . GLN A 1 130 ? 13.17105  -22.47433 36.34746  1.000 60.61007  ? 194 GLN A O     1 
ATOM   739  C  CB    . GLN A 1 130 ? 15.73450  -23.13492 34.14596  1.000 69.20125  ? 194 GLN A CB    1 
ATOM   740  N  N     . PHE A 1 131 ? 14.83154  -20.98347 36.07571  1.000 46.59649  ? 195 PHE A N     1 
ATOM   741  C  CA    . PHE A 1 131 ? 14.74461  -20.45167 37.42997  1.000 46.98947  ? 195 PHE A CA    1 
ATOM   742  C  C     . PHE A 1 131 ? 13.66125  -19.38599 37.59231  1.000 43.49858  ? 195 PHE A C     1 
ATOM   743  O  O     . PHE A 1 131 ? 13.58171  -18.76098 38.65537  1.000 42.16446  ? 195 PHE A O     1 
ATOM   744  C  CB    . PHE A 1 131 ? 16.10150  -19.88778 37.86144  1.000 52.80058  ? 195 PHE A CB    1 
ATOM   745  N  N     . GLY A 1 132 ? 12.84059  -19.15434 36.56927  1.000 49.20902  ? 196 GLY A N     1 
ATOM   746  C  CA    . GLY A 1 132 ? 11.67696  -18.29931 36.71664  1.000 46.60393  ? 196 GLY A CA    1 
ATOM   747  C  C     . GLY A 1 132 ? 11.94303  -16.81149 36.75539  1.000 45.27354  ? 196 GLY A C     1 
ATOM   748  O  O     . GLY A 1 132 ? 11.05230  -16.04587 37.13839  1.000 48.29098  ? 196 GLY A O     1 
ATOM   749  N  N     . VAL A 1 133 ? 13.13534  -16.37139 36.36723  1.000 31.37370  ? 197 VAL A N     1 
ATOM   750  C  CA    . VAL A 1 133 ? 13.49398  -14.96229 36.41972  1.000 29.70401  ? 197 VAL A CA    1 
ATOM   751  C  C     . VAL A 1 133 ? 13.37152  -14.29907 35.04295  1.000 27.32000  ? 197 VAL A C     1 
ATOM   752  O  O     . VAL A 1 133 ? 13.94374  -13.23983 34.81786  1.000 27.29039  ? 197 VAL A O     1 
ATOM   753  C  CB    . VAL A 1 133 ? 14.89953  -14.76678 37.01329  1.000 27.77168  ? 197 VAL A CB    1 
ATOM   754  N  N     . GLY A 1 134 ? 12.62966  -14.91198 34.11590  1.000 28.94769  ? 198 GLY A N     1 
ATOM   755  C  CA    . GLY A 1 134 ? 12.49860  -14.34090 32.78440  1.000 26.74546  ? 198 GLY A CA    1 
ATOM   756  C  C     . GLY A 1 134 ? 11.85717  -12.96595 32.78223  1.000 24.87409  ? 198 GLY A C     1 
ATOM   757  O  O     . GLY A 1 134 ? 12.10312  -12.16317 31.87798  1.000 24.81052  ? 198 GLY A O     1 
ATOM   758  N  N     . PHE A 1 135 ? 11.03750  -12.67287 33.79327  1.000 23.45704  ? 199 PHE A N     1 
ATOM   759  C  CA    . PHE A 1 135 ? 10.38288  -11.37288 33.87692  1.000 22.90341  ? 199 PHE A CA    1 
ATOM   760  C  C     . PHE A 1 135 ? 11.37918  -10.22774 33.75333  1.000 26.73653  ? 199 PHE A C     1 
ATOM   761  O  O     . PHE A 1 135 ? 11.12264  -9.25115  33.04257  1.000 23.45266  ? 199 PHE A O     1 
ATOM   762  C  CB    . PHE A 1 135 ? 9.62179   -11.26194 35.19687  1.000 22.12677  ? 199 PHE A CB    1 
ATOM   763  C  CG    . PHE A 1 135 ? 9.30447   -9.84809  35.59850  1.000 22.00660  ? 199 PHE A CG    1 
ATOM   764  C  CD1   . PHE A 1 135 ? 8.23966   -9.17377  35.02701  1.000 22.28127  ? 199 PHE A CD1   1 
ATOM   765  C  CD2   . PHE A 1 135 ? 10.05627  -9.19925  36.55678  1.000 23.61760  ? 199 PHE A CD2   1 
ATOM   766  C  CE1   . PHE A 1 135 ? 7.93318   -7.87159  35.40861  1.000 20.48753  ? 199 PHE A CE1   1 
ATOM   767  C  CE2   . PHE A 1 135 ? 9.76493   -7.89890  36.93429  1.000 23.92081  ? 199 PHE A CE2   1 
ATOM   768  C  CZ    . PHE A 1 135 ? 8.70240   -7.23441  36.36448  1.000 24.36586  ? 199 PHE A CZ    1 
ATOM   769  N  N     . TYR A 1 136 ? 12.52305  -10.32516 34.43502  1.000 24.00135  ? 200 TYR A N     1 
ATOM   770  C  CA    . TYR A 1 136 ? 13.46897  -9.21627  34.43278  1.000 25.04069  ? 200 TYR A CA    1 
ATOM   771  C  C     . TYR A 1 136 ? 14.25835  -9.08288  33.13790  1.000 26.79900  ? 200 TYR A C     1 
ATOM   772  O  O     . TYR A 1 136 ? 15.10961  -8.19019  33.04779  1.000 30.32495  ? 200 TYR A O     1 
ATOM   773  C  CB    . TYR A 1 136 ? 14.42173  -9.30442  35.63031  1.000 28.43500  ? 200 TYR A CB    1 
ATOM   774  C  CG    . TYR A 1 136 ? 13.72883  -9.63475  36.93235  1.000 28.73459  ? 200 TYR A CG    1 
ATOM   775  C  CD1   . TYR A 1 136 ? 13.48019  -10.94954 37.30581  1.000 26.69427  ? 200 TYR A CD1   1 
ATOM   776  C  CD2   . TYR A 1 136 ? 13.28898  -8.62153  37.76769  1.000 27.75535  ? 200 TYR A CD2   1 
ATOM   777  C  CE1   . TYR A 1 136 ? 12.84558  -11.24639 38.47754  1.000 30.78809  ? 200 TYR A CE1   1 
ATOM   778  C  CE2   . TYR A 1 136 ? 12.64451  -8.90998  38.94809  1.000 30.03845  ? 200 TYR A CE2   1 
ATOM   779  C  CZ    . TYR A 1 136 ? 12.42519  -10.22805 39.29691  1.000 31.39673  ? 200 TYR A CZ    1 
ATOM   780  O  OH    . TYR A 1 136 ? 11.78052  -10.52746 40.47605  1.000 38.64387  ? 200 TYR A OH    1 
ATOM   781  N  N     . SER A 1 137 ? 13.97885  -9.90333  32.12363  1.000 30.52845  ? 201 SER A N     1 
ATOM   782  C  CA    . SER A 1 137 ? 14.47406  -9.59249  30.79050  1.000 28.78344  ? 201 SER A CA    1 
ATOM   783  C  C     . SER A 1 137 ? 13.75015  -8.39931  30.18582  1.000 25.14808  ? 201 SER A C     1 
ATOM   784  O  O     . SER A 1 137 ? 14.13682  -7.94305  29.10578  1.000 26.82864  ? 201 SER A O     1 
ATOM   785  C  CB    . SER A 1 137 ? 14.33559  -10.79531 29.85941  1.000 28.75324  ? 201 SER A CB    1 
ATOM   786  O  OG    . SER A 1 137 ? 12.97674  -11.05727 29.55997  1.000 25.80524  ? 201 SER A OG    1 
ATOM   787  N  N     . ALA A 1 138 ? 12.70087  -7.89847  30.84594  1.000 20.71483  ? 202 ALA A N     1 
ATOM   788  C  CA    . ALA A 1 138 ? 12.06069  -6.66409  30.39956  1.000 17.36428  ? 202 ALA A CA    1 
ATOM   789  C  C     . ALA A 1 138 ? 13.00029  -5.47129  30.51335  1.000 19.44204  ? 202 ALA A C     1 
ATOM   790  O  O     . ALA A 1 138 ? 12.86891  -4.50539  29.75733  1.000 20.51950  ? 202 ALA A O     1 
ATOM   791  C  CB    . ALA A 1 138 ? 10.79241  -6.41451  31.21620  1.000 19.55708  ? 202 ALA A CB    1 
ATOM   792  N  N     . PHE A 1 139 ? 13.95804  -5.52286  31.43632  1.000 16.27171  ? 203 PHE A N     1 
ATOM   793  C  CA    . PHE A 1 139 ? 14.86727  -4.40691  31.64472  1.000 21.58767  ? 203 PHE A CA    1 
ATOM   794  C  C     . PHE A 1 139 ? 15.97853  -4.34226  30.60431  1.000 21.37643  ? 203 PHE A C     1 
ATOM   795  O  O     . PHE A 1 139 ? 16.82437  -3.44200  30.68262  1.000 24.99190  ? 203 PHE A O     1 
ATOM   796  C  CB    . PHE A 1 139 ? 15.46659  -4.47712  33.04538  1.000 20.28029  ? 203 PHE A CB    1 
ATOM   797  C  CG    . PHE A 1 139 ? 14.50050  -4.09990  34.13018  1.000 19.64429  ? 203 PHE A CG    1 
ATOM   798  C  CD1   . PHE A 1 139 ? 14.13413  -2.78023  34.32556  1.000 17.26589  ? 203 PHE A CD1   1 
ATOM   799  C  CD2   . PHE A 1 139 ? 13.95318  -5.07524  34.94868  1.000 17.74640  ? 203 PHE A CD2   1 
ATOM   800  C  CE1   . PHE A 1 139 ? 13.24886  -2.43654  35.32963  1.000 22.49250  ? 203 PHE A CE1   1 
ATOM   801  C  CE2   . PHE A 1 139 ? 13.06032  -4.74309  35.95071  1.000 21.79760  ? 203 PHE A CE2   1 
ATOM   802  C  CZ    . PHE A 1 139 ? 12.71186  -3.42535  36.14833  1.000 16.75970  ? 203 PHE A CZ    1 
ATOM   803  N  N     . LEU A 1 140 ? 16.01116  -5.27396  29.65019  1.000 22.48242  ? 204 LEU A N     1 
ATOM   804  C  CA    . LEU A 1 140 ? 16.91827  -5.12306  28.51993  1.000 24.99445  ? 204 LEU A CA    1 
ATOM   805  C  C     . LEU A 1 140 ? 16.46322  -4.00465  27.59629  1.000 23.55023  ? 204 LEU A C     1 
ATOM   806  O  O     . LEU A 1 140 ? 17.29643  -3.34444  26.96460  1.000 27.42662  ? 204 LEU A O     1 
ATOM   807  C  CB    . LEU A 1 140 ? 17.03217  -6.43467  27.73931  1.000 24.86411  ? 204 LEU A CB    1 
ATOM   808  C  CG    . LEU A 1 140 ? 17.71762  -7.62531  28.41800  1.000 29.17248  ? 204 LEU A CG    1 
ATOM   809  C  CD1   . LEU A 1 140 ? 17.25904  -8.94622  27.78966  1.000 23.88701  ? 204 LEU A CD1   1 
ATOM   810  C  CD2   . LEU A 1 140 ? 19.23863  -7.49013  28.37682  1.000 34.23888  ? 204 LEU A CD2   1 
ATOM   811  N  N     . VAL A 1 141 ? 15.15246  -3.77521  27.51127  1.000 28.82887  ? 205 VAL A N     1 
ATOM   812  C  CA    . VAL A 1 141 ? 14.57133  -2.78100  26.61982  1.000 22.19562  ? 205 VAL A CA    1 
ATOM   813  C  C     . VAL A 1 141 ? 13.86591  -1.65780  27.36452  1.000 22.79282  ? 205 VAL A C     1 
ATOM   814  O  O     . VAL A 1 141 ? 13.37035  -0.72926  26.72163  1.000 25.47307  ? 205 VAL A O     1 
ATOM   815  C  CB    . VAL A 1 141 ? 13.58950  -3.43355  25.62945  1.000 24.68803  ? 205 VAL A CB    1 
ATOM   816  C  CG1   . VAL A 1 141 ? 14.31822  -4.36831  24.67592  1.000 23.03461  ? 205 VAL A CG1   1 
ATOM   817  C  CG2   . VAL A 1 141 ? 12.50650  -4.17187  26.40548  1.000 22.51538  ? 205 VAL A CG2   1 
ATOM   818  N  N     . ALA A 1 142 ? 13.77234  -1.71791  28.68938  1.000 26.21815  ? 206 ALA A N     1 
ATOM   819  C  CA    . ALA A 1 142 ? 12.97430  -0.75171  29.43267  1.000 26.70242  ? 206 ALA A CA    1 
ATOM   820  C  C     . ALA A 1 142 ? 13.80305  -0.06740  30.51012  1.000 27.26713  ? 206 ALA A C     1 
ATOM   821  O  O     . ALA A 1 142 ? 14.58215  -0.71318  31.22319  1.000 26.97702  ? 206 ALA A O     1 
ATOM   822  C  CB    . ALA A 1 142 ? 11.74370  -1.41784  30.07980  1.000 23.02242  ? 206 ALA A CB    1 
ATOM   823  N  N     . ASP A 1 143 ? 13.62358  1.24873   30.62502  1.000 23.32329  ? 207 ASP A N     1 
ATOM   824  C  CA    . ASP A 1 143 ? 14.17597  1.97296   31.76157  1.000 28.27678  ? 207 ASP A CA    1 
ATOM   825  C  C     . ASP A 1 143 ? 13.38053  1.72382   33.03144  1.000 28.48775  ? 207 ASP A C     1 
ATOM   826  O  O     . ASP A 1 143 ? 13.90808  1.90781   34.13712  1.000 28.64717  ? 207 ASP A O     1 
ATOM   827  C  CB    . ASP A 1 143 ? 14.20058  3.47677   31.48570  1.000 31.03599  ? 207 ASP A CB    1 
ATOM   828  C  CG    . ASP A 1 143 ? 15.21165  3.85697   30.43236  1.000 32.05517  ? 207 ASP A CG    1 
ATOM   829  O  OD1   . ASP A 1 143 ? 16.40708  3.54887   30.61952  1.000 37.98289  ? 207 ASP A OD1   1 
ATOM   830  O  OD2   . ASP A 1 143 ? 14.81838  4.50355   29.43873  1.000 31.04673  ? 207 ASP A OD2   1 
ATOM   831  N  N     . LYS A 1 144 ? 12.12334  1.31702   32.89521  1.000 22.99605  ? 208 LYS A N     1 
ATOM   832  C  CA    . LYS A 1 144 ? 11.25372  1.16421   34.04565  1.000 15.89372  ? 208 LYS A CA    1 
ATOM   833  C  C     . LYS A 1 144 ? 10.14834  0.19727   33.67475  1.000 15.53009  ? 208 LYS A C     1 
ATOM   834  O  O     . LYS A 1 144 ? 9.63178   0.23925   32.55636  1.000 17.16717  ? 208 LYS A O     1 
ATOM   835  C  CB    . LYS A 1 144 ? 10.67704  2.51352   34.47013  1.000 21.97665  ? 208 LYS A CB    1 
ATOM   836  C  CG    . LYS A 1 144 ? 9.57942   2.42648   35.48781  1.000 17.46715  ? 208 LYS A CG    1 
ATOM   837  C  CD    . LYS A 1 144 ? 9.21103   3.82203   35.90883  1.000 26.37745  ? 208 LYS A CD    1 
ATOM   838  C  CE    . LYS A 1 144 ? 10.04578  4.29944   37.07467  1.000 26.35355  ? 208 LYS A CE    1 
ATOM   839  N  NZ    . LYS A 1 144 ? 9.17349   4.78646   38.17629  1.000 29.97337  ? 208 LYS A NZ    1 
ATOM   840  N  N     . VAL A 1 145 ? 9.80491   -0.68264  34.60452  1.000 16.92699  ? 209 VAL A N     1 
ATOM   841  C  CA    . VAL A 1 145 ? 8.75762   -1.67042  34.40019  1.000 15.84121  ? 209 VAL A CA    1 
ATOM   842  C  C     . VAL A 1 145 ? 7.69891   -1.43698  35.46001  1.000 16.93351  ? 209 VAL A C     1 
ATOM   843  O  O     . VAL A 1 145 ? 8.02733   -1.28672  36.64257  1.000 18.23584  ? 209 VAL A O     1 
ATOM   844  C  CB    . VAL A 1 145 ? 9.31258   -3.10538  34.46187  1.000 14.74908  ? 209 VAL A CB    1 
ATOM   845  C  CG1   . VAL A 1 145 ? 8.17346   -4.15095  34.40288  1.000 14.03518  ? 209 VAL A CG1   1 
ATOM   846  C  CG2   . VAL A 1 145 ? 10.27585  -3.33025  33.30953  1.000 15.24809  ? 209 VAL A CG2   1 
ATOM   847  N  N     A ILE A 1 146 ? 6.43074   -1.41938  35.04470  0.341 14.35777  ? 210 ILE A N     1 
ATOM   848  N  N     B ILE A 1 146 ? 6.44758   -1.32623  35.02379  0.659 14.30498  ? 210 ILE A N     1 
ATOM   849  C  CA    A ILE A 1 146 ? 5.30423   -1.17933  35.94514  0.341 15.00789  ? 210 ILE A CA    1 
ATOM   850  C  CA    B ILE A 1 146 ? 5.30530   -1.20933  35.91862  0.659 14.96541  ? 210 ILE A CA    1 
ATOM   851  C  C     A ILE A 1 146 ? 4.31163   -2.32662  35.80505  0.341 13.60307  ? 210 ILE A C     1 
ATOM   852  C  C     B ILE A 1 146 ? 4.49446   -2.48845  35.78964  0.659 13.73393  ? 210 ILE A C     1 
ATOM   853  O  O     A ILE A 1 146 ? 3.80864   -2.58342  34.70577  0.341 12.09506  ? 210 ILE A O     1 
ATOM   854  O  O     B ILE A 1 146 ? 4.35827   -3.04145  34.69291  0.659 10.80736  ? 210 ILE A O     1 
ATOM   855  C  CB    A ILE A 1 146 ? 4.61978   0.16389   35.65162  0.341 14.03126  ? 210 ILE A CB    1 
ATOM   856  C  CB    B ILE A 1 146 ? 4.45117   0.03460   35.60394  0.659 13.83928  ? 210 ILE A CB    1 
ATOM   857  C  CG1   A ILE A 1 146 ? 5.62967   1.30113   35.79844  0.341 16.67452  ? 210 ILE A CG1   1 
ATOM   858  C  CG1   B ILE A 1 146 ? 5.23638   1.31424   35.91638  0.659 16.56154  ? 210 ILE A CG1   1 
ATOM   859  C  CG2   A ILE A 1 146 ? 3.42411   0.37534   36.57861  0.341 12.85058  ? 210 ILE A CG2   1 
ATOM   860  C  CG2   B ILE A 1 146 ? 3.15963   0.02462   36.42319  0.659 12.21743  ? 210 ILE A CG2   1 
ATOM   861  C  CD1   A ILE A 1 146 ? 5.11507   2.61624   35.32164  0.341 15.47324  ? 210 ILE A CD1   1 
ATOM   862  C  CD1   B ILE A 1 146 ? 5.58754   2.13708   34.69327  0.659 15.40056  ? 210 ILE A CD1   1 
ATOM   863  N  N     . VAL A 1 147 ? 4.01083   -2.99601  36.91628  1.000 16.61389  ? 211 VAL A N     1 
ATOM   864  C  CA    . VAL A 1 147 ? 3.16157   -4.17819  36.93312  1.000 13.18496  ? 211 VAL A CA    1 
ATOM   865  C  C     . VAL A 1 147 ? 1.88548   -3.81135  37.67928  1.000 20.01369  ? 211 VAL A C     1 
ATOM   866  O  O     . VAL A 1 147 ? 1.92156   -3.51517  38.88332  1.000 16.89592  ? 211 VAL A O     1 
ATOM   867  C  CB    . VAL A 1 147 ? 3.85887   -5.37298  37.59350  1.000 15.77556  ? 211 VAL A CB    1 
ATOM   868  C  CG1   . VAL A 1 147 ? 2.87499   -6.50141  37.79460  1.000 15.57900  ? 211 VAL A CG1   1 
ATOM   869  C  CG2   . VAL A 1 147 ? 5.01345   -5.84713  36.72543  1.000 17.32658  ? 211 VAL A CG2   1 
ATOM   870  N  N     . THR A 1 148 ? 0.75963   -3.81343  36.97124  1.000 15.10791  ? 212 THR A N     1 
ATOM   871  C  CA    . THR A 1 148 ? -0.54227  -3.60321  37.59431  1.000 13.77009  ? 212 THR A CA    1 
ATOM   872  C  C     . THR A 1 148 ? -1.21387  -4.97135  37.67353  1.000 13.80916  ? 212 THR A C     1 
ATOM   873  O  O     . THR A 1 148 ? -1.37560  -5.63185  36.65250  1.000 12.17483  ? 212 THR A O     1 
ATOM   874  C  CB    . THR A 1 148 ? -1.38353  -2.60745  36.78813  1.000 12.02342  ? 212 THR A CB    1 
ATOM   875  O  OG1   . THR A 1 148 ? -0.67293  -1.35995  36.64234  1.000 10.35910  ? 212 THR A OG1   1 
ATOM   876  C  CG2   . THR A 1 148 ? -2.67460  -2.31679  37.52220  1.000 14.57028  ? 212 THR A CG2   1 
ATOM   877  N  N     . SER A 1 149 ? -1.56086  -5.42778  38.87609  1.000 14.75753  ? 213 SER A N     1 
ATOM   878  C  CA    . SER A 1 149 ? -2.14114  -6.75862  38.97979  1.000 17.89262  ? 213 SER A CA    1 
ATOM   879  C  C     . SER A 1 149 ? -3.34330  -6.75410  39.90943  1.000 17.99502  ? 213 SER A C     1 
ATOM   880  O  O     . SER A 1 149 ? -3.41891  -5.97086  40.85928  1.000 19.90486  ? 213 SER A O     1 
ATOM   881  C  CB    . SER A 1 149 ? -1.13175  -7.80902  39.46269  1.000 18.12922  ? 213 SER A CB    1 
ATOM   882  O  OG    . SER A 1 149 ? -1.59865  -9.11477  39.16440  1.000 18.19669  ? 213 SER A OG    1 
ATOM   883  N  N     . LYS A 1 150 ? -4.28048  -7.65027  39.60305  1.000 15.62129  ? 214 LYS A N     1 
ATOM   884  C  CA    . LYS A 1 150 ? -5.49048  -7.86395  40.37917  1.000 14.05014  ? 214 LYS A CA    1 
ATOM   885  C  C     . LYS A 1 150 ? -5.65942  -9.36417  40.57560  1.000 15.15380  ? 214 LYS A C     1 
ATOM   886  O  O     . LYS A 1 150 ? -5.78214  -10.12007 39.60201  1.000 16.91442  ? 214 LYS A O     1 
ATOM   887  C  CB    . LYS A 1 150 ? -6.71725  -7.28227  39.68155  1.000 13.55909  ? 214 LYS A CB    1 
ATOM   888  C  CG    . LYS A 1 150 ? -8.00591  -7.63466  40.39773  1.000 14.51298  ? 214 LYS A CG    1 
ATOM   889  C  CD    . LYS A 1 150 ? -8.10411  -6.86901  41.69160  1.000 15.65317  ? 214 LYS A CD    1 
ATOM   890  C  CE    . LYS A 1 150 ? -9.49182  -6.95594  42.31188  1.000 15.79785  ? 214 LYS A CE    1 
ATOM   891  N  NZ    . LYS A 1 150 ? -9.81318  -8.32885  42.78361  1.000 20.13219  ? 214 LYS A NZ    1 
ATOM   892  N  N     . HIS A 1 151 ? -5.65272  -9.78583  41.82723  1.000 15.41063  ? 215 HIS A N     1 
ATOM   893  C  CA    . HIS A 1 151 ? -5.89659  -11.15873 42.22211  1.000 15.95072  ? 215 HIS A CA    1 
ATOM   894  C  C     . HIS A 1 151 ? -7.27870  -11.23865 42.85904  1.000 18.75188  ? 215 HIS A C     1 
ATOM   895  O  O     . HIS A 1 151 ? -7.77198  -10.25268 43.41865  1.000 18.88367  ? 215 HIS A O     1 
ATOM   896  C  CB    . HIS A 1 151 ? -4.81312  -11.62055 43.19880  1.000 14.38218  ? 215 HIS A CB    1 
ATOM   897  C  CG    . HIS A 1 151 ? -4.83598  -13.08730 43.49091  1.000 14.63328  ? 215 HIS A CG    1 
ATOM   898  N  ND1   . HIS A 1 151 ? -5.69097  -13.64333 44.41635  1.000 17.00973  ? 215 HIS A ND1   1 
ATOM   899  C  CD2   . HIS A 1 151 ? -4.09934  -14.11279 42.99638  1.000 16.22157  ? 215 HIS A CD2   1 
ATOM   900  C  CE1   . HIS A 1 151 ? -5.48059  -14.94685 44.48229  1.000 14.47127  ? 215 HIS A CE1   1 
ATOM   901  N  NE2   . HIS A 1 151 ? -4.52431  -15.25990 43.62642  1.000 15.72533  ? 215 HIS A NE2   1 
ATOM   902  N  N     . ASN A 1 152 ? -7.91509  -12.41179 42.76132  1.000 19.43796  ? 216 ASN A N     1 
ATOM   903  C  CA    . ASN A 1 152 ? -9.28486  -12.53680 43.26040  1.000 20.50643  ? 216 ASN A CA    1 
ATOM   904  C  C     . ASN A 1 152 ? -9.38253  -12.19410 44.74697  1.000 19.51624  ? 216 ASN A C     1 
ATOM   905  O  O     . ASN A 1 152 ? -10.38228 -11.61186 45.18917  1.000 20.23821  ? 216 ASN A O     1 
ATOM   906  C  CB    . ASN A 1 152 ? -9.82638  -13.94879 42.99448  1.000 19.79231  ? 216 ASN A CB    1 
ATOM   907  C  CG    . ASN A 1 152 ? -10.29844 -14.13417 41.55438  1.000 22.72127  ? 216 ASN A CG    1 
ATOM   908  O  OD1   . ASN A 1 152 ? -10.46454 -13.16637 40.82230  1.000 22.64160  ? 216 ASN A OD1   1 
ATOM   909  N  ND2   . ASN A 1 152 ? -10.51611 -15.37994 41.14811  1.000 19.53010  ? 216 ASN A ND2   1 
ATOM   910  N  N     . ASN A 1 153 ? -8.36031  -12.53442 45.54368  1.000 14.15142  ? 217 ASN A N     1 
ATOM   911  C  CA    . ASN A 1 153 ? -8.42355  -12.29902 46.98569  1.000 16.87974  ? 217 ASN A CA    1 
ATOM   912  C  C     . ASN A 1 153 ? -7.73398  -11.00975 47.42938  1.000 20.97354  ? 217 ASN A C     1 
ATOM   913  O  O     . ASN A 1 153 ? -7.27167  -10.93471 48.57449  1.000 22.36117  ? 217 ASN A O     1 
ATOM   914  C  CB    . ASN A 1 153 ? -7.82020  -13.45444 47.79323  1.000 19.58184  ? 217 ASN A CB    1 
ATOM   915  C  CG    . ASN A 1 153 ? -8.14128  -14.82033 47.24905  1.000 21.47225  ? 217 ASN A CG    1 
ATOM   916  O  OD1   . ASN A 1 153 ? -9.24540  -15.08233 46.76277  1.000 25.44070  ? 217 ASN A OD1   1 
ATOM   917  N  ND2   . ASN A 1 153 ? -7.20642  -15.74907 47.44832  1.000 18.78185  ? 217 ASN A ND2   1 
ATOM   918  N  N     . ASP A 1 154 ? -7.66153  -9.98634  46.58544  1.000 19.25129  ? 218 ASP A N     1 
ATOM   919  C  CA    . ASP A 1 154 ? -6.94584  -8.78632  47.00850  1.000 14.90531  ? 218 ASP A CA    1 
ATOM   920  C  C     . ASP A 1 154 ? -7.34127  -7.63593  46.10016  1.000 15.01574  ? 218 ASP A C     1 
ATOM   921  O  O     . ASP A 1 154 ? -7.88497  -7.83736  45.00960  1.000 16.94808  ? 218 ASP A O     1 
ATOM   922  C  CB    . ASP A 1 154 ? -5.42836  -9.01427  46.96559  1.000 17.20976  ? 218 ASP A CB    1 
ATOM   923  C  CG    . ASP A 1 154 ? -4.64144  -8.01245  47.79690  1.000 22.12477  ? 218 ASP A CG    1 
ATOM   924  O  OD1   . ASP A 1 154 ? -5.23367  -7.07346  48.39678  1.000 24.48975  ? 218 ASP A OD1   1 
ATOM   925  O  OD2   . ASP A 1 154 ? -3.40121  -8.18437  47.85829  1.000 19.42511  ? 218 ASP A OD2   1 
ATOM   926  N  N     . THR A 1 155 ? -7.05704  -6.42412  46.55193  1.000 14.06621  ? 219 THR A N     1 
ATOM   927  C  CA    . THR A 1 155 ? -7.34529  -5.29103  45.69334  1.000 10.79471  ? 219 THR A CA    1 
ATOM   928  C  C     . THR A 1 155 ? -6.26172  -5.15838  44.63610  1.000 11.42137  ? 219 THR A C     1 
ATOM   929  O  O     . THR A 1 155 ? -5.23445  -5.84464  44.66966  1.000 12.94785  ? 219 THR A O     1 
ATOM   930  C  CB    . THR A 1 155 ? -7.45822  -4.00707  46.50194  1.000 13.48138  ? 219 THR A CB    1 
ATOM   931  O  OG1   . THR A 1 155 ? -6.24016  -3.80176  47.24112  1.000 15.84418  ? 219 THR A OG1   1 
ATOM   932  C  CG2   . THR A 1 155 ? -8.65529  -4.10093  47.46971  1.000 12.50260  ? 219 THR A CG2   1 
ATOM   933  N  N     . GLN A 1 156 ? -6.51676  -4.28438  43.66548  1.000 15.61246  ? 220 GLN A N     1 
ATOM   934  C  CA    . GLN A 1 156 ? -5.57842  -4.06122  42.58397  1.000 13.98100  ? 220 GLN A CA    1 
ATOM   935  C  C     . GLN A 1 156 ? -4.42092  -3.20317  43.07515  1.000 16.86506  ? 220 GLN A C     1 
ATOM   936  O  O     . GLN A 1 156 ? -4.61419  -2.24991  43.83437  1.000 18.25760  ? 220 GLN A O     1 
ATOM   937  C  CB    . GLN A 1 156 ? -6.27875  -3.38620  41.40891  1.000 14.74085  ? 220 GLN A CB    1 
ATOM   938  C  CG    . GLN A 1 156 ? -5.37957  -3.10287  40.20816  1.000 9.97993   ? 220 GLN A CG    1 
ATOM   939  C  CD    . GLN A 1 156 ? -6.18720  -2.71125  38.97724  1.000 16.17980  ? 220 GLN A CD    1 
ATOM   940  O  OE1   . GLN A 1 156 ? -7.17392  -3.36963  38.64158  1.000 12.97385  ? 220 GLN A OE1   1 
ATOM   941  N  NE2   . GLN A 1 156 ? -5.76394  -1.65065  38.29400  1.000 14.77580  ? 220 GLN A NE2   1 
ATOM   942  N  N     . HIS A 1 157 ? -3.20898  -3.55110  42.64192  1.000 12.09182  ? 221 HIS A N     1 
ATOM   943  C  CA    . HIS A 1 157 ? -2.00388  -2.88027  43.09463  1.000 15.43969  ? 221 HIS A CA    1 
ATOM   944  C  C     . HIS A 1 157 ? -1.09429  -2.58866  41.90863  1.000 15.71528  ? 221 HIS A C     1 
ATOM   945  O  O     . HIS A 1 157 ? -1.19042  -3.21131  40.85280  1.000 14.01623  ? 221 HIS A O     1 
ATOM   946  C  CB    . HIS A 1 157 ? -1.25257  -3.71701  44.13756  1.000 11.97142  ? 221 HIS A CB    1 
ATOM   947  C  CG    . HIS A 1 157 ? -1.94532  -3.79472  45.46865  1.000 15.80989  ? 221 HIS A CG    1 
ATOM   948  N  ND1   . HIS A 1 157 ? -2.93879  -4.71614  45.74171  1.000 14.88783  ? 221 HIS A ND1   1 
ATOM   949  C  CD2   . HIS A 1 157 ? -1.77993  -3.07541  46.60427  1.000 14.41179  ? 221 HIS A CD2   1 
ATOM   950  C  CE1   . HIS A 1 157 ? -3.36583  -4.54451  46.98205  1.000 17.18172  ? 221 HIS A CE1   1 
ATOM   951  N  NE2   . HIS A 1 157 ? -2.67882  -3.55774  47.52589  1.000 15.47414  ? 221 HIS A NE2   1 
ATOM   952  N  N     . ILE A 1 158 ? -0.19801  -1.62885  42.11072  1.000 15.85752  ? 222 ILE A N     1 
ATOM   953  C  CA    . ILE A 1 158 ? 0.81526   -1.25474  41.13628  1.000 15.97225  ? 222 ILE A CA    1 
ATOM   954  C  C     . ILE A 1 158 ? 2.19258   -1.48021  41.75353  1.000 18.80521  ? 222 ILE A C     1 
ATOM   955  O  O     . ILE A 1 158 ? 2.46824   -1.00587  42.85840  1.000 16.39088  ? 222 ILE A O     1 
ATOM   956  C  CB    . ILE A 1 158 ? 0.65278   0.21052   40.70313  1.000 14.90831  ? 222 ILE A CB    1 
ATOM   957  C  CG1   . ILE A 1 158 ? -0.66558  0.38320   39.92315  1.000 15.98422  ? 222 ILE A CG1   1 
ATOM   958  C  CG2   . ILE A 1 158 ? 1.86563   0.64276   39.86698  1.000 14.66880  ? 222 ILE A CG2   1 
ATOM   959  C  CD1   . ILE A 1 158 ? -1.17000  1.83255   39.86576  1.000 12.67970  ? 222 ILE A CD1   1 
ATOM   960  N  N     . TRP A 1 159 ? 3.04830   -2.19958  41.03690  1.000 15.72028  ? 223 TRP A N     1 
ATOM   961  C  CA    . TRP A 1 159 ? 4.45524   -2.37816  41.37053  1.000 15.12607  ? 223 TRP A CA    1 
ATOM   962  C  C     . TRP A 1 159 ? 5.26612   -1.63162  40.32060  1.000 17.85410  ? 223 TRP A C     1 
ATOM   963  O  O     . TRP A 1 159 ? 4.90291   -1.63865  39.14328  1.000 16.99661  ? 223 TRP A O     1 
ATOM   964  C  CB    . TRP A 1 159 ? 4.77862   -3.87341  41.37205  1.000 12.86694  ? 223 TRP A CB    1 
ATOM   965  C  CG    . TRP A 1 159 ? 6.18929   -4.32398  41.52599  1.000 16.85936  ? 223 TRP A CG    1 
ATOM   966  C  CD1   . TRP A 1 159 ? 6.74404   -4.89304  42.63785  1.000 20.92339  ? 223 TRP A CD1   1 
ATOM   967  C  CD2   . TRP A 1 159 ? 7.20851   -4.33652  40.51851  1.000 20.66544  ? 223 TRP A CD2   1 
ATOM   968  N  NE1   . TRP A 1 159 ? 8.05064   -5.23629  42.39349  1.000 21.04321  ? 223 TRP A NE1   1 
ATOM   969  C  CE2   . TRP A 1 159 ? 8.36510   -4.90003  41.10267  1.000 21.13425  ? 223 TRP A CE2   1 
ATOM   970  C  CE3   . TRP A 1 159 ? 7.26806   -3.90177  39.19065  1.000 17.15426  ? 223 TRP A CE3   1 
ATOM   971  C  CZ2   . TRP A 1 159 ? 9.56615   -5.04212  40.40098  1.000 23.75417  ? 223 TRP A CZ2   1 
ATOM   972  C  CZ3   . TRP A 1 159 ? 8.46284   -4.05659  38.49118  1.000 19.79050  ? 223 TRP A CZ3   1 
ATOM   973  C  CH2   . TRP A 1 159 ? 9.59197   -4.61765  39.10020  1.000 21.26091  ? 223 TRP A CH2   1 
ATOM   974  N  N     . GLU A 1 160 ? 6.33102   -0.94584  40.72747  1.000 17.33099  ? 224 GLU A N     1 
ATOM   975  C  CA    . GLU A 1 160 ? 7.12321   -0.24123  39.72930  1.000 18.06994  ? 224 GLU A CA    1 
ATOM   976  C  C     . GLU A 1 160 ? 8.57584   -0.29862  40.16019  1.000 22.90380  ? 224 GLU A C     1 
ATOM   977  O  O     . GLU A 1 160 ? 8.87687   -0.28315  41.35211  1.000 25.24895  ? 224 GLU A O     1 
ATOM   978  C  CB    . GLU A 1 160 ? 6.66807   1.22126   39.54321  1.000 19.09087  ? 224 GLU A CB    1 
ATOM   979  C  CG    . GLU A 1 160 ? 6.57951   2.05580   40.82164  1.000 24.99976  ? 224 GLU A CG    1 
ATOM   980  C  CD    . GLU A 1 160 ? 7.92914   2.64850   41.26111  1.000 34.16224  ? 224 GLU A CD    1 
ATOM   981  O  OE1   . GLU A 1 160 ? 8.92934   2.49610   40.52607  1.000 35.46104  ? 224 GLU A OE1   1 
ATOM   982  O  OE2   . GLU A 1 160 ? 8.00645   3.24093   42.36281  1.000 34.17334  ? 224 GLU A OE2   1 
ATOM   983  N  N     . SER A 1 161 ? 9.47828   -0.35406  39.18556  1.000 28.39548  ? 225 SER A N     1 
ATOM   984  C  CA    . SER A 1 161 ? 10.89157  -0.43423  39.51994  1.000 27.94507  ? 225 SER A CA    1 
ATOM   985  C  C     . SER A 1 161 ? 11.71969  0.02941   38.33750  1.000 27.25681  ? 225 SER A C     1 
ATOM   986  O  O     . SER A 1 161 ? 11.29322  -0.07484  37.18971  1.000 24.17224  ? 225 SER A O     1 
ATOM   987  C  CB    . SER A 1 161 ? 11.29828  -1.85814  39.89827  1.000 27.39340  ? 225 SER A CB    1 
ATOM   988  O  OG    . SER A 1 161 ? 12.70502  -1.97002  40.02094  1.000 31.93709  ? 225 SER A OG    1 
ATOM   989  N  N     . ASP A 1 162 ? 12.90688  0.54311   38.63987  1.000 44.08734  ? 226 ASP A N     1 
ATOM   990  C  CA    . ASP A 1 162 ? 13.95584  0.78426   37.66128  1.000 43.92499  ? 226 ASP A CA    1 
ATOM   991  C  C     . ASP A 1 162 ? 15.05983  -0.26529  37.73461  1.000 42.82823  ? 226 ASP A C     1 
ATOM   992  O  O     . ASP A 1 162 ? 16.13417  -0.06266  37.16029  1.000 47.05305  ? 226 ASP A O     1 
ATOM   993  C  CB    . ASP A 1 162 ? 14.53273  2.19133   37.85294  1.000 46.25329  ? 226 ASP A CB    1 
ATOM   994  C  CG    . ASP A 1 162 ? 15.42706  2.30547   39.08832  1.000 50.61228  ? 226 ASP A CG    1 
ATOM   995  O  OD1   . ASP A 1 162 ? 16.16848  3.30783   39.19633  1.000 51.59687  ? 226 ASP A OD1   1 
ATOM   996  O  OD2   . ASP A 1 162 ? 15.36324  1.42054   39.97090  1.000 53.15262  ? 226 ASP A OD2   1 
ATOM   997  N  N     . SER A 1 163 ? 14.81137  -1.37122  38.44164  1.000 38.13986  ? 227 SER A N     1 
ATOM   998  C  CA    . SER A 1 163 ? 15.74117  -2.45789  38.75314  1.000 38.79733  ? 227 SER A CA    1 
ATOM   999  C  C     . SER A 1 163 ? 16.78620  -2.07083  39.79629  1.000 42.83072  ? 227 SER A C     1 
ATOM   1000 O  O     . SER A 1 163 ? 17.73827  -2.83166  40.01527  1.000 48.02316  ? 227 SER A O     1 
ATOM   1001 C  CB    . SER A 1 163 ? 16.42662  -3.02232  37.49794  1.000 36.01006  ? 227 SER A CB    1 
ATOM   1002 O  OG    . SER A 1 163 ? 17.38572  -2.12396  36.97304  1.000 40.60423  ? 227 SER A OG    1 
ATOM   1003 N  N     . ASN A 1 164 ? 16.63075  -0.92637  40.46829  1.000 35.66770  ? 228 ASN A N     1 
ATOM   1004 C  CA    . ASN A 1 164 ? 17.45258  -0.58292  41.62681  1.000 36.24820  ? 228 ASN A CA    1 
ATOM   1005 C  C     . ASN A 1 164 ? 16.67231  -0.71330  42.92954  1.000 38.05073  ? 228 ASN A C     1 
ATOM   1006 O  O     . ASN A 1 164 ? 17.08736  -1.43676  43.83996  1.000 41.41839  ? 228 ASN A O     1 
ATOM   1007 C  CB    . ASN A 1 164 ? 18.01759  0.84183   41.48856  1.000 40.93442  ? 228 ASN A CB    1 
ATOM   1008 C  CG    . ASN A 1 164 ? 19.25419  0.89962   40.60548  1.000 47.53344  ? 228 ASN A CG    1 
ATOM   1009 O  OD1   . ASN A 1 164 ? 19.34968  1.72672   39.69419  1.000 48.34701  ? 228 ASN A OD1   1 
ATOM   1010 N  ND2   . ASN A 1 164 ? 20.21022  0.01596   40.87330  1.000 46.58785  ? 228 ASN A ND2   1 
ATOM   1011 N  N     . GLU A 1 165 ? 15.55528  -0.01011  43.05121  1.000 50.79313  ? 229 GLU A N     1 
ATOM   1012 C  CA    . GLU A 1 165 ? 14.56304  -0.24814  44.08975  1.000 49.02181  ? 229 GLU A CA    1 
ATOM   1013 C  C     . GLU A 1 165 ? 13.22410  -0.54935  43.42112  1.000 46.66058  ? 229 GLU A C     1 
ATOM   1014 O  O     . GLU A 1 165 ? 13.09933  -0.54459  42.19500  1.000 44.67902  ? 229 GLU A O     1 
ATOM   1015 C  CB    . GLU A 1 165 ? 14.45140  0.94139   45.05602  1.000 47.78510  ? 229 GLU A CB    1 
ATOM   1016 C  CG    . GLU A 1 165 ? 15.72438  1.26284   45.83788  1.000 59.61771  ? 229 GLU A CG    1 
ATOM   1017 C  CD    . GLU A 1 165 ? 15.77867  2.70164   46.35734  1.000 71.89714  ? 229 GLU A CD    1 
ATOM   1018 O  OE1   . GLU A 1 165 ? 14.72268  3.23148   46.77188  1.000 66.75719  ? 229 GLU A OE1   1 
ATOM   1019 O  OE2   . GLU A 1 165 ? 16.88597  3.29172   46.37874  1.000 69.08336  ? 229 GLU A OE2   1 
ATOM   1020 N  N     . PHE A 1 166 ? 12.22036  -0.83975  44.24022  1.000 30.62923  ? 230 PHE A N     1 
ATOM   1021 C  CA    . PHE A 1 166 ? 10.86466  -0.99712  43.74223  1.000 21.29904  ? 230 PHE A CA    1 
ATOM   1022 C  C     . PHE A 1 166 ? 9.89648   -0.52157  44.81007  1.000 25.41550  ? 230 PHE A C     1 
ATOM   1023 O  O     . PHE A 1 166 ? 10.24171  -0.41973  45.98853  1.000 24.92387  ? 230 PHE A O     1 
ATOM   1024 C  CB    . PHE A 1 166 ? 10.56931  -2.44489  43.32329  1.000 23.51233  ? 230 PHE A CB    1 
ATOM   1025 C  CG    . PHE A 1 166 ? 10.52865  -3.43345  44.45333  1.000 22.48520  ? 230 PHE A CG    1 
ATOM   1026 C  CD1   . PHE A 1 166 ? 11.67769  -4.08391  44.85886  1.000 28.05942  ? 230 PHE A CD1   1 
ATOM   1027 C  CD2   . PHE A 1 166 ? 9.33098   -3.76428  45.06715  1.000 23.79112  ? 230 PHE A CD2   1 
ATOM   1028 C  CE1   . PHE A 1 166 ? 11.64494  -5.01579  45.88658  1.000 29.85794  ? 230 PHE A CE1   1 
ATOM   1029 C  CE2   . PHE A 1 166 ? 9.28970   -4.70018  46.09039  1.000 24.39421  ? 230 PHE A CE2   1 
ATOM   1030 C  CZ    . PHE A 1 166 ? 10.45146  -5.32518  46.50290  1.000 25.43288  ? 230 PHE A CZ    1 
ATOM   1031 N  N     . SER A 1 167 ? 8.68427   -0.20003  44.37716  1.000 28.06626  ? 231 SER A N     1 
ATOM   1032 C  CA    . SER A 1 167 ? 7.62520   0.17137   45.29601  1.000 25.23706  ? 231 SER A CA    1 
ATOM   1033 C  C     . SER A 1 167 ? 6.35586   -0.54704  44.87638  1.000 22.06962  ? 231 SER A C     1 
ATOM   1034 O  O     . SER A 1 167 ? 6.21287   -0.97497  43.73029  1.000 19.30919  ? 231 SER A O     1 
ATOM   1035 C  CB    . SER A 1 167 ? 7.41402   1.69121   45.34677  1.000 30.05968  ? 231 SER A CB    1 
ATOM   1036 O  OG    . SER A 1 167 ? 6.82813   2.17025   44.15401  1.000 29.24462  ? 231 SER A OG    1 
ATOM   1037 N  N     . VAL A 1 168 ? 5.45266   -0.72106  45.83382  1.000 20.98006  ? 232 VAL A N     1 
ATOM   1038 C  CA    . VAL A 1 168 ? 4.15165   -1.33171  45.58946  1.000 19.19198  ? 232 VAL A CA    1 
ATOM   1039 C  C     . VAL A 1 168 ? 3.10317   -0.46217  46.26754  1.000 21.26033  ? 232 VAL A C     1 
ATOM   1040 O  O     . VAL A 1 168 ? 3.19488   -0.20712  47.47442  1.000 19.17454  ? 232 VAL A O     1 
ATOM   1041 C  CB    . VAL A 1 168 ? 4.07297   -2.77495  46.13180  1.000 18.37714  ? 232 VAL A CB    1 
ATOM   1042 C  CG1   . VAL A 1 168 ? 2.68776   -3.34102  45.91740  1.000 14.77519  ? 232 VAL A CG1   1 
ATOM   1043 C  CG2   . VAL A 1 168 ? 5.11574   -3.67359  45.48369  1.000 21.40639  ? 232 VAL A CG2   1 
ATOM   1044 N  N     . ILE A 1 169 ? 2.10385   -0.01667  45.50405  1.000 13.96243  ? 233 ILE A N     1 
ATOM   1045 C  CA    . ILE A 1 169 ? 1.06573   0.85001   46.05233  1.000 14.89721  ? 233 ILE A CA    1 
ATOM   1046 C  C     . ILE A 1 169 ? -0.30274  0.30237   45.67348  1.000 15.09583  ? 233 ILE A C     1 
ATOM   1047 O  O     . ILE A 1 169 ? -0.46221  -0.39380  44.66897  1.000 12.15786  ? 233 ILE A O     1 
ATOM   1048 C  CB    . ILE A 1 169 ? 1.20499   2.32247   45.57259  1.000 17.51390  ? 233 ILE A CB    1 
ATOM   1049 C  CG1   . ILE A 1 169 ? 0.96069   2.43163   44.05998  1.000 15.40195  ? 233 ILE A CG1   1 
ATOM   1050 C  CG2   . ILE A 1 169 ? 2.56061   2.88754   45.97124  1.000 14.97781  ? 233 ILE A CG2   1 
ATOM   1051 C  CD1   . ILE A 1 169 ? 0.77206   3.88358   43.53806  1.000 17.23717  ? 233 ILE A CD1   1 
ATOM   1052 N  N     . ALA A 1 170 ? -1.29600  0.61120   46.49868  1.000 18.12436  ? 234 ALA A N     1 
ATOM   1053 C  CA    . ALA A 1 170 ? -2.67322  0.40641   46.08497  1.000 19.95161  ? 234 ALA A CA    1 
ATOM   1054 C  C     . ALA A 1 170 ? -2.94214  1.20005   44.81647  1.000 19.04059  ? 234 ALA A C     1 
ATOM   1055 O  O     . ALA A 1 170 ? -2.54769  2.36359   44.70312  1.000 17.71773  ? 234 ALA A O     1 
ATOM   1056 C  CB    . ALA A 1 170 ? -3.62431  0.85165   47.19486  1.000 21.70367  ? 234 ALA A CB    1 
ATOM   1057 N  N     . ASP A 1 171 ? -3.61071  0.57921   43.85478  1.000 17.25706  ? 235 ASP A N     1 
ATOM   1058 C  CA    . ASP A 1 171 ? -3.92940  1.30443   42.62145  1.000 17.21789  ? 235 ASP A CA    1 
ATOM   1059 C  C     . ASP A 1 171 ? -5.02549  2.33507   42.87421  1.000 19.29878  ? 235 ASP A C     1 
ATOM   1060 O  O     . ASP A 1 171 ? -6.16926  1.94752   43.16265  1.000 16.78646  ? 235 ASP A O     1 
ATOM   1061 C  CB    . ASP A 1 171 ? -4.37145  0.31850   41.54513  1.000 17.59070  ? 235 ASP A CB    1 
ATOM   1062 C  CG    . ASP A 1 171 ? -4.40949  0.93373   40.15337  1.000 18.48714  ? 235 ASP A CG    1 
ATOM   1063 O  OD1   . ASP A 1 171 ? -4.58156  2.16685   40.02356  1.000 18.90156  ? 235 ASP A OD1   1 
ATOM   1064 O  OD2   . ASP A 1 171 ? -4.27633  0.15559   39.18225  1.000 19.14785  ? 235 ASP A OD2   1 
ATOM   1065 N  N     . PRO A 1 172 ? -4.75256  3.63881   42.71899  1.000 17.81251  ? 236 PRO A N     1 
ATOM   1066 C  CA    . PRO A 1 172 ? -5.81305  4.64441   42.92176  1.000 13.75633  ? 236 PRO A CA    1 
ATOM   1067 C  C     . PRO A 1 172 ? -6.95302  4.55639   41.90440  1.000 19.49776  ? 236 PRO A C     1 
ATOM   1068 O  O     . PRO A 1 172 ? -8.01396  5.15832   42.12252  1.000 15.69885  ? 236 PRO A O     1 
ATOM   1069 C  CB    . PRO A 1 172 ? -5.05522  5.97800   42.81410  1.000 17.04221  ? 236 PRO A CB    1 
ATOM   1070 C  CG    . PRO A 1 172 ? -3.89904  5.65944   41.92489  1.000 17.40883  ? 236 PRO A CG    1 
ATOM   1071 C  CD    . PRO A 1 172 ? -3.48827  4.25698   42.28034  1.000 14.73154  ? 236 PRO A CD    1 
ATOM   1072 N  N     . ARG A 1 173 ? -6.78709  3.81777   40.81334  1.000 18.59629  ? 237 ARG A N     1 
ATOM   1073 C  CA    . ARG A 1 173 ? -7.86910  3.67255   39.84781  1.000 15.15945  ? 237 ARG A CA    1 
ATOM   1074 C  C     . ARG A 1 173 ? -8.85260  2.57968   40.23559  1.000 18.12646  ? 237 ARG A C     1 
ATOM   1075 O  O     . ARG A 1 173 ? -9.85004  2.38568   39.53038  1.000 21.10963  ? 237 ARG A O     1 
ATOM   1076 C  CB    . ARG A 1 173 ? -7.28514  3.38713   38.46583  1.000 14.00838  ? 237 ARG A CB    1 
ATOM   1077 C  CG    . ARG A 1 173 ? -6.33829  4.46766   37.99571  1.000 14.34934  ? 237 ARG A CG    1 
ATOM   1078 C  CD    . ARG A 1 173 ? -5.42037  3.99162   36.85715  1.000 15.63965  ? 237 ARG A CD    1 
ATOM   1079 N  NE    . ARG A 1 173 ? -4.67367  2.78319   37.20978  1.000 13.26037  ? 237 ARG A NE    1 
ATOM   1080 C  CZ    . ARG A 1 173 ? -3.73471  2.24182   36.44406  1.000 12.92263  ? 237 ARG A CZ    1 
ATOM   1081 N  NH1   . ARG A 1 173 ? -3.39959  2.77340   35.27790  1.000 17.18220  ? 237 ARG A NH1   1 
ATOM   1082 N  NH2   . ARG A 1 173 ? -3.10564  1.15246   36.86156  1.000 12.47265  ? 237 ARG A NH2   1 
ATOM   1083 N  N     . GLY A 1 174 ? -8.59464  1.85803   41.32381  1.000 17.35480  ? 238 GLY A N     1 
ATOM   1084 C  CA    . GLY A 1 174 ? -9.47448  0.78753   41.73619  1.000 16.74488  ? 238 GLY A CA    1 
ATOM   1085 C  C     . GLY A 1 174 ? -9.28366  -0.45104  40.88369  1.000 16.80310  ? 238 GLY A C     1 
ATOM   1086 O  O     . GLY A 1 174 ? -8.22632  -0.67361  40.27742  1.000 18.01439  ? 238 GLY A O     1 
ATOM   1087 N  N     . ASN A 1 175 ? -10.33408 -1.26510  40.82386  1.000 21.33528  ? 239 ASN A N     1 
ATOM   1088 C  CA    . ASN A 1 175 ? -10.27348 -2.53437  40.10141  1.000 19.95928  ? 239 ASN A CA    1 
ATOM   1089 C  C     . ASN A 1 175 ? -10.66834 -2.28618  38.64713  1.000 23.79454  ? 239 ASN A C     1 
ATOM   1090 O  O     . ASN A 1 175 ? -11.83904 -2.37139  38.27064  1.000 22.41474  ? 239 ASN A O     1 
ATOM   1091 C  CB    . ASN A 1 175 ? -11.16783 -3.57299  40.77003  1.000 19.75527  ? 239 ASN A CB    1 
ATOM   1092 C  CG    . ASN A 1 175 ? -11.26412 -4.86266  39.98738  1.000 17.15302  ? 239 ASN A CG    1 
ATOM   1093 O  OD1   . ASN A 1 175 ? -10.47695 -5.12395  39.06459  1.000 17.37996  ? 239 ASN A OD1   1 
ATOM   1094 N  ND2   . ASN A 1 175 ? -12.22732 -5.69219  40.35618  1.000 18.58698  ? 239 ASN A ND2   1 
ATOM   1095 N  N     . THR A 1 176 ? -9.67313  -1.98412  37.81471  1.000 16.23373  ? 240 THR A N     1 
ATOM   1096 C  CA    . THR A 1 176 ? -9.89674  -1.78828  36.38775  1.000 12.82352  ? 240 THR A CA    1 
ATOM   1097 C  C     . THR A 1 176 ? -9.60629  -3.03459  35.57212  1.000 12.68390  ? 240 THR A C     1 
ATOM   1098 O  O     . THR A 1 176 ? -10.21940 -3.23682  34.51664  1.000 15.58480  ? 240 THR A O     1 
ATOM   1099 C  CB    . THR A 1 176 ? -9.03131  -0.63463  35.86507  1.000 14.28064  ? 240 THR A CB    1 
ATOM   1100 O  OG1   . THR A 1 176 ? -7.65104  -1.02438  35.92962  1.000 12.05088  ? 240 THR A OG1   1 
ATOM   1101 C  CG2   . THR A 1 176 ? -9.25396  0.64901   36.67691  1.000 14.87399  ? 240 THR A CG2   1 
ATOM   1102 N  N     . LEU A 1 177 ? -8.69825  -3.88839  36.03692  1.000 15.02576  ? 241 LEU A N     1 
ATOM   1103 C  CA    . LEU A 1 177 ? -8.39221  -5.12288  35.33195  1.000 14.16099  ? 241 LEU A CA    1 
ATOM   1104 C  C     . LEU A 1 177 ? -9.45428  -6.18961  35.52642  1.000 15.89414  ? 241 LEU A C     1 
ATOM   1105 O  O     . LEU A 1 177 ? -9.55468  -7.09592  34.69600  1.000 13.74398  ? 241 LEU A O     1 
ATOM   1106 C  CB    . LEU A 1 177 ? -7.04603  -5.68715  35.80217  1.000 12.17664  ? 241 LEU A CB    1 
ATOM   1107 C  CG    . LEU A 1 177 ? -5.75820  -4.89698  35.54302  1.000 12.68401  ? 241 LEU A CG    1 
ATOM   1108 C  CD1   . LEU A 1 177 ? -4.60429  -5.59267  36.24423  1.000 13.64959  ? 241 LEU A CD1   1 
ATOM   1109 C  CD2   . LEU A 1 177 ? -5.48162  -4.74706  34.04010  1.000 12.35146  ? 241 LEU A CD2   1 
ATOM   1110 N  N     . GLY A 1 178 ? -10.21411 -6.13674  36.61054  1.000 11.66684  ? 242 GLY A N     1 
ATOM   1111 C  CA    . GLY A 1 178 ? -11.11845 -7.25480  36.92075  1.000 11.41942  ? 242 GLY A CA    1 
ATOM   1112 C  C     . GLY A 1 178 ? -10.43514 -8.48845  37.48305  1.000 11.22696  ? 242 GLY A C     1 
ATOM   1113 O  O     . GLY A 1 178 ? -10.82379 -8.98841  38.54355  1.000 13.48947  ? 242 GLY A O     1 
ATOM   1114 N  N     . ARG A 1 179 ? -9.42799  -9.00142  36.77522  1.000 11.36173  ? 243 ARG A N     1 
ATOM   1115 C  CA    . ARG A 1 179 ? -8.52816  -10.05696 37.21833  1.000 13.13602  ? 243 ARG A CA    1 
ATOM   1116 C  C     . ARG A 1 179 ? -7.40729  -10.12450 36.20096  1.000 10.59999  ? 243 ARG A C     1 
ATOM   1117 O  O     . ARG A 1 179 ? -7.64842  -9.91655  35.01651  1.000 12.43128  ? 243 ARG A O     1 
ATOM   1118 C  CB    . ARG A 1 179 ? -9.24441  -11.41416 37.33471  1.000 10.57427  ? 243 ARG A CB    1 
ATOM   1119 C  CG    . ARG A 1 179 ? -8.39882  -12.53986 37.91958  1.000 9.66155   ? 243 ARG A CG    1 
ATOM   1120 C  CD    . ARG A 1 179 ? -8.95934  -13.89628 37.55300  1.000 10.71734  ? 243 ARG A CD    1 
ATOM   1121 N  NE    . ARG A 1 179 ? -8.91234  -14.14338 36.11540  1.000 11.47372  ? 243 ARG A NE    1 
ATOM   1122 C  CZ    . ARG A 1 179 ? -9.98395  -14.18195 35.33184  1.000 13.15003  ? 243 ARG A CZ    1 
ATOM   1123 N  NH1   . ARG A 1 179 ? -11.20609 -14.00686 35.81981  1.000 16.55731  ? 243 ARG A NH1   1 
ATOM   1124 N  NH2   . ARG A 1 179 ? -9.82730  -14.38500 34.02688  1.000 14.83879  ? 243 ARG A NH2   1 
ATOM   1125 N  N     . GLY A 1 180 ? -6.18784  -10.38817 36.66312  1.000 11.20661  ? 244 GLY A N     1 
ATOM   1126 C  CA    . GLY A 1 180 ? -5.06158  -10.50708 35.75051  1.000 7.15721   ? 244 GLY A CA    1 
ATOM   1127 C  C     . GLY A 1 180 ? -3.95858  -9.50100  35.99768  1.000 7.88914   ? 244 GLY A C     1 
ATOM   1128 O  O     . GLY A 1 180 ? -3.87657  -8.90978  37.07853  1.000 11.15172  ? 244 GLY A O     1 
ATOM   1129 N  N     . THR A 1 181 ? -3.12727  -9.24876  34.99078  1.000 9.63019   ? 245 THR A N     1 
ATOM   1130 C  CA    . THR A 1 181 ? -1.89018  -8.51055  35.20941  1.000 9.84102   ? 245 THR A CA    1 
ATOM   1131 C  C     . THR A 1 181 ? -1.46612  -7.79872  33.94359  1.000 10.43995  ? 245 THR A C     1 
ATOM   1132 O  O     . THR A 1 181 ? -1.32850  -8.43799  32.90054  1.000 10.51448  ? 245 THR A O     1 
ATOM   1133 C  CB    . THR A 1 181 ? -0.76876  -9.45345  35.63420  1.000 10.23669  ? 245 THR A CB    1 
ATOM   1134 O  OG1   . THR A 1 181 ? -1.15393  -10.11352 36.83856  1.000 9.47348   ? 245 THR A OG1   1 
ATOM   1135 C  CG2   . THR A 1 181 ? 0.52671   -8.66179  35.85653  1.000 9.17069   ? 245 THR A CG2   1 
ATOM   1136 N  N     . THR A 1 182 ? -1.19374  -6.50830  34.05056  1.000 11.18779  ? 246 THR A N     1 
ATOM   1137 C  CA    . THR A 1 182 ? -0.61853  -5.74437  32.94875  1.000 13.10175  ? 246 THR A CA    1 
ATOM   1138 C  C     . THR A 1 182 ? 0.85493   -5.48781  33.23882  1.000 13.53903  ? 246 THR A C     1 
ATOM   1139 O  O     . THR A 1 182 ? 1.19602   -5.00254  34.32481  1.000 11.76316  ? 246 THR A O     1 
ATOM   1140 C  CB    . THR A 1 182 ? -1.35982  -4.42672  32.75943  1.000 9.65080   ? 246 THR A CB    1 
ATOM   1141 O  OG1   . THR A 1 182 ? -2.71486  -4.71319  32.41528  1.000 12.66907  ? 246 THR A OG1   1 
ATOM   1142 C  CG2   . THR A 1 182 ? -0.73546  -3.60869  31.64507  1.000 9.42099   ? 246 THR A CG2   1 
ATOM   1143 N  N     . ILE A 1 183 ? 1.72378   -5.86739  32.29802  1.000 10.94216  ? 247 ILE A N     1 
ATOM   1144 C  CA    . ILE A 1 183 ? 3.13797   -5.50873  32.34285  1.000 13.85307  ? 247 ILE A CA    1 
ATOM   1145 C  C     . ILE A 1 183 ? 3.33292   -4.30027  31.43548  1.000 13.60453  ? 247 ILE A C     1 
ATOM   1146 O  O     . ILE A 1 183 ? 3.14745   -4.39493  30.21418  1.000 15.78993  ? 247 ILE A O     1 
ATOM   1147 C  CB    . ILE A 1 183 ? 4.03992   -6.66892  31.88756  1.000 15.36283  ? 247 ILE A CB    1 
ATOM   1148 C  CG1   . ILE A 1 183 ? 3.61877   -8.01626  32.49371  1.000 14.39154  ? 247 ILE A CG1   1 
ATOM   1149 C  CG2   . ILE A 1 183 ? 5.51196   -6.35800  32.21916  1.000 15.21467  ? 247 ILE A CG2   1 
ATOM   1150 C  CD1   . ILE A 1 183 ? 3.74649   -8.10366  33.98174  1.000 16.18313  ? 247 ILE A CD1   1 
ATOM   1151 N  N     . THR A 1 184 ? 3.71116   -3.16086  32.01115  1.000 11.30174  ? 248 THR A N     1 
ATOM   1152 C  CA    . THR A 1 184 ? 3.91079   -1.94176  31.24821  1.000 9.60641   ? 248 THR A CA    1 
ATOM   1153 C  C     . THR A 1 184 ? 5.39632   -1.61980  31.16943  1.000 12.94081  ? 248 THR A C     1 
ATOM   1154 O  O     . THR A 1 184 ? 6.07476   -1.54340  32.19544  1.000 13.72479  ? 248 THR A O     1 
ATOM   1155 C  CB    . THR A 1 184 ? 3.13719   -0.78158  31.86746  1.000 10.70313  ? 248 THR A CB    1 
ATOM   1156 O  OG1   . THR A 1 184 ? 1.74455   -0.98269  31.59964  1.000 11.77302  ? 248 THR A OG1   1 
ATOM   1157 C  CG2   . THR A 1 184 ? 3.56123   0.54589   31.24387  1.000 10.58540  ? 248 THR A CG2   1 
ATOM   1158 N  N     . LEU A 1 185 ? 5.89336   -1.41972  29.95188  1.000 15.11009  ? 249 LEU A N     1 
ATOM   1159 C  CA    . LEU A 1 185 ? 7.30470   -1.16023  29.72043  1.000 13.50844  ? 249 LEU A CA    1 
ATOM   1160 C  C     . LEU A 1 185 ? 7.47531   0.27636   29.26620  1.000 14.23752  ? 249 LEU A C     1 
ATOM   1161 O  O     . LEU A 1 185 ? 6.91418   0.67707   28.24560  1.000 17.19015  ? 249 LEU A O     1 
ATOM   1162 C  CB    . LEU A 1 185 ? 7.88009   -2.10316  28.66425  1.000 15.16795  ? 249 LEU A CB    1 
ATOM   1163 C  CG    . LEU A 1 185 ? 8.27202   -3.53258  29.05088  1.000 20.53691  ? 249 LEU A CG    1 
ATOM   1164 C  CD1   . LEU A 1 185 ? 7.13061   -4.27340  29.70166  1.000 20.52169  ? 249 LEU A CD1   1 
ATOM   1165 C  CD2   . LEU A 1 185 ? 8.76775   -4.26518  27.84038  1.000 20.18447  ? 249 LEU A CD2   1 
ATOM   1166 N  N     . VAL A 1 186 ? 8.25075   1.04842   30.01748  1.000 15.16562  ? 250 VAL A N     1 
ATOM   1167 C  CA    . VAL A 1 186 ? 8.71184   2.34894   29.56220  1.000 16.92714  ? 250 VAL A CA    1 
ATOM   1168 C  C     . VAL A 1 186 ? 9.98719   2.07597   28.77847  1.000 17.63706  ? 250 VAL A C     1 
ATOM   1169 O  O     . VAL A 1 186 ? 11.04851  1.83647   29.36158  1.000 22.38598  ? 250 VAL A O     1 
ATOM   1170 C  CB    . VAL A 1 186 ? 8.94736   3.31514   30.72529  1.000 19.81828  ? 250 VAL A CB    1 
ATOM   1171 C  CG1   . VAL A 1 186 ? 9.24801   4.70745   30.19992  1.000 17.57405  ? 250 VAL A CG1   1 
ATOM   1172 C  CG2   . VAL A 1 186 ? 7.72727   3.32981   31.64362  1.000 19.29861  ? 250 VAL A CG2   1 
ATOM   1173 N  N     . LEU A 1 187 ? 9.88176   2.12080   27.45136  1.000 18.92977  ? 251 LEU A N     1 
ATOM   1174 C  CA    . LEU A 1 187 ? 10.96885  1.66639   26.59980  1.000 19.55886  ? 251 LEU A CA    1 
ATOM   1175 C  C     . LEU A 1 187 ? 12.13425  2.64676   26.60306  1.000 21.30005  ? 251 LEU A C     1 
ATOM   1176 O  O     . LEU A 1 187 ? 11.95951  3.86662   26.68539  1.000 21.34596  ? 251 LEU A O     1 
ATOM   1177 C  CB    . LEU A 1 187 ? 10.46749  1.45513   25.17424  1.000 19.23051  ? 251 LEU A CB    1 
ATOM   1178 C  CG    . LEU A 1 187 ? 9.57397   0.22951   25.00674  1.000 14.50147  ? 251 LEU A CG    1 
ATOM   1179 C  CD1   . LEU A 1 187 ? 9.04024   0.20675   23.61450  1.000 13.20894  ? 251 LEU A CD1   1 
ATOM   1180 C  CD2   . LEU A 1 187 ? 10.33982  -1.04775  25.29842  1.000 16.65117  ? 251 LEU A CD2   1 
ATOM   1181 N  N     . LYS A 1 188 ? 13.33435  2.09580   26.51159  1.000 21.68711  ? 252 LYS A N     1 
ATOM   1182 C  CA    . LYS A 1 188 ? 14.51507  2.90835   26.32007  1.000 22.82962  ? 252 LYS A CA    1 
ATOM   1183 C  C     . LYS A 1 188 ? 14.46945  3.57517   24.95477  1.000 22.48100  ? 252 LYS A C     1 
ATOM   1184 O  O     . LYS A 1 188 ? 13.78215  3.12018   24.03600  1.000 22.28249  ? 252 LYS A O     1 
ATOM   1185 C  CB    . LYS A 1 188 ? 15.76120  2.04321   26.43939  1.000 24.24391  ? 252 LYS A CB    1 
ATOM   1186 C  CG    . LYS A 1 188 ? 15.72947  1.22084   27.67734  1.000 21.77076  ? 252 LYS A CG    1 
ATOM   1187 C  CD    . LYS A 1 188 ? 17.09840  1.02893   28.26023  1.000 28.05516  ? 252 LYS A CD    1 
ATOM   1188 C  CE    . LYS A 1 188 ? 17.38136  -0.43877  28.43524  1.000 28.44039  ? 252 LYS A CE    1 
ATOM   1189 N  NZ    . LYS A 1 188 ? 18.01342  -0.62135  29.75315  1.000 34.02268  ? 252 LYS A NZ    1 
ATOM   1190 N  N     . GLU A 1 189 ? 15.24181  4.65817   24.82342  1.000 33.37332  ? 253 GLU A N     1 
ATOM   1191 C  CA    . GLU A 1 189 ? 15.29377  5.40025   23.56816  1.000 33.96051  ? 253 GLU A CA    1 
ATOM   1192 C  C     . GLU A 1 189 ? 15.65739  4.49721   22.39752  1.000 31.63252  ? 253 GLU A C     1 
ATOM   1193 O  O     . GLU A 1 189 ? 15.15077  4.67098   21.28392  1.000 36.24184  ? 253 GLU A O     1 
ATOM   1194 C  CB    . GLU A 1 189 ? 16.29926  6.54723   23.68656  1.000 34.22251  ? 253 GLU A CB    1 
ATOM   1195 N  N     . GLU A 1 190 ? 16.53653  3.52909   22.62715  1.000 30.83293  ? 254 GLU A N     1 
ATOM   1196 C  CA    . GLU A 1 190 ? 16.97674  2.64181   21.56142  1.000 28.91343  ? 254 GLU A CA    1 
ATOM   1197 C  C     . GLU A 1 190 ? 15.99240  1.51160   21.28510  1.000 27.15844  ? 254 GLU A C     1 
ATOM   1198 O  O     . GLU A 1 190 ? 16.14042  0.82407   20.27039  1.000 30.19473  ? 254 GLU A O     1 
ATOM   1199 C  CB    . GLU A 1 190 ? 18.33907  2.06130   21.92415  1.000 28.44830  ? 254 GLU A CB    1 
ATOM   1200 C  CG    . GLU A 1 190 ? 18.29540  1.30859   23.22987  1.000 36.30740  ? 254 GLU A CG    1 
ATOM   1201 C  CD    . GLU A 1 190 ? 19.14369  1.94864   24.30605  1.000 42.36779  ? 254 GLU A CD    1 
ATOM   1202 O  OE1   . GLU A 1 190 ? 18.92815  3.15105   24.59479  1.000 39.03411  ? 254 GLU A OE1   1 
ATOM   1203 O  OE2   . GLU A 1 190 ? 20.01217  1.24178   24.86644  1.000 38.97811  ? 254 GLU A OE2   1 
ATOM   1204 N  N     . ALA A 1 191 ? 15.00847  1.29429   22.16063  1.000 19.35146  ? 255 ALA A N     1 
ATOM   1205 C  CA    . ALA A 1 191 ? 13.98856  0.27042   21.97082  1.000 18.63366  ? 255 ALA A CA    1 
ATOM   1206 C  C     . ALA A 1 191 ? 12.70686  0.83908   21.36247  1.000 20.93890  ? 255 ALA A C     1 
ATOM   1207 O  O     . ALA A 1 191 ? 11.62505  0.25608   21.54230  1.000 16.75858  ? 255 ALA A O     1 
ATOM   1208 C  CB    . ALA A 1 191 ? 13.67570  -0.41627  23.29578  1.000 16.12804  ? 255 ALA A CB    1 
ATOM   1209 N  N     . SER A 1 192 ? 12.82045  1.95785   20.64404  1.000 18.08339  ? 256 SER A N     1 
ATOM   1210 C  CA    . SER A 1 192 ? 11.66568  2.61985   20.03894  1.000 19.49808  ? 256 SER A CA    1 
ATOM   1211 C  C     . SER A 1 192 ? 10.87741  1.68241   19.12921  1.000 17.05032  ? 256 SER A C     1 
ATOM   1212 O  O     . SER A 1 192 ? 9.66282   1.85273   18.97117  1.000 18.14265  ? 256 SER A O     1 
ATOM   1213 C  CB    . SER A 1 192 ? 12.13028  3.85333   19.24852  1.000 16.70537  ? 256 SER A CB    1 
ATOM   1214 N  N     . ASP A 1 193 ? 11.54836  0.70150   18.51875  1.000 34.79248  ? 257 ASP A N     1 
ATOM   1215 C  CA    . ASP A 1 193 ? 10.91833  -0.14358  17.50742  1.000 31.73302  ? 257 ASP A CA    1 
ATOM   1216 C  C     . ASP A 1 193 ? 9.79101   -0.98466  18.08702  1.000 30.08117  ? 257 ASP A C     1 
ATOM   1217 O  O     . ASP A 1 193 ? 8.87828   -1.38686  17.36374  1.000 31.18044  ? 257 ASP A O     1 
ATOM   1218 C  CB    . ASP A 1 193 ? 11.97115  -1.05282  16.88107  1.000 37.02704  ? 257 ASP A CB    1 
ATOM   1219 C  CG    . ASP A 1 193 ? 12.45124  -0.53757  15.55289  1.000 37.88374  ? 257 ASP A CG    1 
ATOM   1220 O  OD1   . ASP A 1 193 ? 13.68052  -0.34426  15.40543  1.000 38.88331  ? 257 ASP A OD1   1 
ATOM   1221 O  OD2   . ASP A 1 193 ? 11.59840  -0.30065  14.66717  1.000 37.64337  ? 257 ASP A OD2   1 
ATOM   1222 N  N     . TYR A 1 194 ? 9.83673   -1.26690  19.37988  1.000 18.89769  ? 258 TYR A N     1 
ATOM   1223 C  CA    . TYR A 1 194 ? 8.80949   -2.08846  19.99229  1.000 17.27398  ? 258 TYR A CA    1 
ATOM   1224 C  C     . TYR A 1 194 ? 7.49065   -1.34840  20.14140  1.000 16.03238  ? 258 TYR A C     1 
ATOM   1225 O  O     . TYR A 1 194 ? 6.49883   -1.95022  20.56320  1.000 17.02496  ? 258 TYR A O     1 
ATOM   1226 C  CB    . TYR A 1 194 ? 9.32633   -2.60124  21.33342  1.000 15.01648  ? 258 TYR A CB    1 
ATOM   1227 C  CG    . TYR A 1 194 ? 10.50916  -3.50870  21.13511  1.000 16.30386  ? 258 TYR A CG    1 
ATOM   1228 C  CD1   . TYR A 1 194 ? 10.38353  -4.68115  20.40384  1.000 18.36897  ? 258 TYR A CD1   1 
ATOM   1229 C  CD2   . TYR A 1 194 ? 11.76394  -3.17065  21.61941  1.000 21.75455  ? 258 TYR A CD2   1 
ATOM   1230 C  CE1   . TYR A 1 194 ? 11.46910  -5.51342  20.18647  1.000 24.75083  ? 258 TYR A CE1   1 
ATOM   1231 C  CE2   . TYR A 1 194 ? 12.86019  -4.00068  21.41429  1.000 22.43088  ? 258 TYR A CE2   1 
ATOM   1232 C  CZ    . TYR A 1 194 ? 12.70597  -5.16990  20.69451  1.000 27.68522  ? 258 TYR A CZ    1 
ATOM   1233 O  OH    . TYR A 1 194 ? 13.78620  -6.00492  20.48400  1.000 26.98681  ? 258 TYR A OH    1 
ATOM   1234 N  N     . LEU A 1 195 ? 7.45141   -0.06960  19.81339  1.000 16.23080  ? 259 LEU A N     1 
ATOM   1235 C  CA    . LEU A 1 195 ? 6.20300   0.66694   19.73963  1.000 16.20558  ? 259 LEU A CA    1 
ATOM   1236 C  C     . LEU A 1 195 ? 5.54093   0.52826   18.37258  1.000 16.13329  ? 259 LEU A C     1 
ATOM   1237 O  O     . LEU A 1 195 ? 4.43963   1.05298   18.16789  1.000 17.61276  ? 259 LEU A O     1 
ATOM   1238 C  CB    . LEU A 1 195 ? 6.46013   2.13476   20.05656  1.000 19.87047  ? 259 LEU A CB    1 
ATOM   1239 C  CG    . LEU A 1 195 ? 7.12009   2.44023   21.40564  1.000 16.91270  ? 259 LEU A CG    1 
ATOM   1240 C  CD1   . LEU A 1 195 ? 7.47234   3.92592   21.49124  1.000 17.98691  ? 259 LEU A CD1   1 
ATOM   1241 C  CD2   . LEU A 1 195 ? 6.19858   2.02501   22.54246  1.000 14.92795  ? 259 LEU A CD2   1 
ATOM   1242 N  N     . GLU A 1 196 ? 6.19381   -0.16349  17.44029  1.000 20.59778  ? 260 GLU A N     1 
ATOM   1243 C  CA    . GLU A 1 196 ? 5.72764   -0.28646  16.06780  1.000 20.45806  ? 260 GLU A CA    1 
ATOM   1244 C  C     . GLU A 1 196 ? 4.90483   -1.55311  15.91016  1.000 16.52535  ? 260 GLU A C     1 
ATOM   1245 O  O     . GLU A 1 196 ? 5.26867   -2.61354  16.43114  1.000 15.48503  ? 260 GLU A O     1 
ATOM   1246 C  CB    . GLU A 1 196 ? 6.90568   -0.29972  15.09535  1.000 19.24081  ? 260 GLU A CB    1 
ATOM   1247 C  CG    . GLU A 1 196 ? 7.74419   0.98864   15.11606  1.000 22.24313  ? 260 GLU A CG    1 
ATOM   1248 C  CD    . GLU A 1 196 ? 6.91580   2.23987   14.83174  1.000 24.74062  ? 260 GLU A CD    1 
ATOM   1249 O  OE1   . GLU A 1 196 ? 5.97972   2.16603   14.00133  1.000 24.13693  ? 260 GLU A OE1   1 
ATOM   1250 O  OE2   . GLU A 1 196 ? 7.18793   3.30148   15.44467  1.000 26.66970  ? 260 GLU A OE2   1 
ATOM   1251 N  N     . LEU A 1 197 ? 3.77789   -1.42127  15.19991  1.000 17.37520  ? 261 LEU A N     1 
ATOM   1252 C  CA    . LEU A 1 197 ? 2.82750   -2.52142  15.04201  1.000 18.46126  ? 261 LEU A CA    1 
ATOM   1253 C  C     . LEU A 1 197 ? 3.42847   -3.68997  14.26781  1.000 17.62163  ? 261 LEU A C     1 
ATOM   1254 O  O     . LEU A 1 197 ? 3.21397   -4.85192  14.62601  1.000 20.35251  ? 261 LEU A O     1 
ATOM   1255 C  CB    . LEU A 1 197 ? 1.58003   -2.01544  14.32198  1.000 24.73085  ? 261 LEU A CB    1 
ATOM   1256 C  CG    . LEU A 1 197 ? 0.18660   -2.40729  14.80268  1.000 27.78126  ? 261 LEU A CG    1 
ATOM   1257 C  CD1   . LEU A 1 197 ? 0.14609   -2.49898  16.31748  1.000 26.60381  ? 261 LEU A CD1   1 
ATOM   1258 C  CD2   . LEU A 1 197 ? -0.83466  -1.40008  14.26903  1.000 22.67289  ? 261 LEU A CD2   1 
ATOM   1259 N  N     . ASP A 1 198 ? 4.15649   -3.41844  13.18578  1.000 18.48264  ? 262 ASP A N     1 
ATOM   1260 C  CA    . ASP A 1 198 ? 4.75005   -4.52615  12.44487  1.000 15.26061  ? 262 ASP A CA    1 
ATOM   1261 C  C     . ASP A 1 198 ? 5.78716   -5.25538  13.28494  1.000 16.79405  ? 262 ASP A C     1 
ATOM   1262 O  O     . ASP A 1 198 ? 5.88439   -6.48958  13.22565  1.000 17.28333  ? 262 ASP A O     1 
ATOM   1263 C  CB    . ASP A 1 198 ? 5.36080   -4.06332  11.11832  1.000 26.01662  ? 262 ASP A CB    1 
ATOM   1264 C  CG    . ASP A 1 198 ? 6.23610   -2.83287  11.24819  1.000 26.31932  ? 262 ASP A CG    1 
ATOM   1265 O  OD1   . ASP A 1 198 ? 6.22580   -2.15380  12.29107  1.000 25.78479  ? 262 ASP A OD1   1 
ATOM   1266 O  OD2   . ASP A 1 198 ? 6.95957   -2.55207  10.27373  1.000 27.29815  ? 262 ASP A OD2   1 
ATOM   1267 N  N     . THR A 1 199 ? 6.56563   -4.52017  14.08036  1.000 16.39834  ? 263 THR A N     1 
ATOM   1268 C  CA    . THR A 1 199 ? 7.59860   -5.17093  14.88066  1.000 19.02682  ? 263 THR A CA    1 
ATOM   1269 C  C     . THR A 1 199 ? 6.98386   -6.08358  15.93528  1.000 18.47045  ? 263 THR A C     1 
ATOM   1270 O  O     . THR A 1 199 ? 7.35751   -7.25587  16.05261  1.000 20.82068  ? 263 THR A O     1 
ATOM   1271 C  CB    . THR A 1 199 ? 8.48484   -4.12124  15.53737  1.000 21.66261  ? 263 THR A CB    1 
ATOM   1272 O  OG1   . THR A 1 199 ? 9.34055   -3.54991  14.54385  1.000 27.57089  ? 263 THR A OG1   1 
ATOM   1273 C  CG2   . THR A 1 199 ? 9.35480   -4.75934  16.60583  1.000 22.96959  ? 263 THR A CG2   1 
ATOM   1274 N  N     . ILE A 1 200 ? 6.01932   -5.56996  16.69913  1.000 19.25029  ? 264 ILE A N     1 
ATOM   1275 C  CA    . ILE A 1 200 ? 5.43711   -6.35936  17.77885  1.000 16.33650  ? 264 ILE A CA    1 
ATOM   1276 C  C     . ILE A 1 200 ? 4.64550   -7.53173  17.21949  1.000 19.50616  ? 264 ILE A C     1 
ATOM   1277 O  O     . ILE A 1 200 ? 4.63984   -8.62732  17.79736  1.000 18.40726  ? 264 ILE A O     1 
ATOM   1278 C  CB    . ILE A 1 200 ? 4.57138   -5.46686  18.67900  1.000 18.84356  ? 264 ILE A CB    1 
ATOM   1279 C  CG1   . ILE A 1 200 ? 5.46201   -4.55022  19.51211  1.000 22.20876  ? 264 ILE A CG1   1 
ATOM   1280 C  CG2   . ILE A 1 200 ? 3.73491   -6.31321  19.63756  1.000 21.67976  ? 264 ILE A CG2   1 
ATOM   1281 C  CD1   . ILE A 1 200 ? 6.33386   -5.28299  20.53591  1.000 22.51879  ? 264 ILE A CD1   1 
ATOM   1282 N  N     . LYS A 1 201 ? 3.95757   -7.32556  16.09328  1.000 16.10187  ? 265 LYS A N     1 
ATOM   1283 C  CA    . LYS A 1 201 ? 3.19841   -8.41816  15.49335  1.000 18.77009  ? 265 LYS A CA    1 
ATOM   1284 C  C     . LYS A 1 201 ? 4.12311   -9.52447  14.98769  1.000 20.38967  ? 265 LYS A C     1 
ATOM   1285 O  O     . LYS A 1 201 ? 3.83359   -10.71150 15.16858  1.000 18.55710  ? 265 LYS A O     1 
ATOM   1286 C  CB    . LYS A 1 201 ? 2.31597   -7.89493  14.36192  1.000 19.91112  ? 265 LYS A CB    1 
ATOM   1287 C  CG    . LYS A 1 201 ? 0.87448   -7.53714  14.77126  1.000 19.92651  ? 265 LYS A CG    1 
ATOM   1288 C  CD    . LYS A 1 201 ? 0.18219   -6.74288  13.66183  1.000 18.27612  ? 265 LYS A CD    1 
ATOM   1289 C  CE    . LYS A 1 201 ? -1.01174  -5.94234  14.17122  1.000 19.59228  ? 265 LYS A CE    1 
ATOM   1290 N  NZ    . LYS A 1 201 ? -2.01541  -5.71209  13.06370  1.000 21.17243  ? 265 LYS A NZ    1 
ATOM   1291 N  N     . ASN A 1 202 ? 5.24077   -9.16174  14.35033  1.000 24.84765  ? 266 ASN A N     1 
ATOM   1292 C  CA    . ASN A 1 202 ? 6.18457   -10.18560 13.90636  1.000 21.94656  ? 266 ASN A CA    1 
ATOM   1293 C  C     . ASN A 1 202 ? 6.77766   -10.93536 15.09120  1.000 24.58182  ? 266 ASN A C     1 
ATOM   1294 O  O     . ASN A 1 202 ? 6.97301   -12.15367 15.02592  1.000 24.39195  ? 266 ASN A O     1 
ATOM   1295 C  CB    . ASN A 1 202 ? 7.30146   -9.56636  13.06219  1.000 23.92441  ? 266 ASN A CB    1 
ATOM   1296 C  CG    . ASN A 1 202 ? 6.85080   -9.19321  11.66859  1.000 24.35211  ? 266 ASN A CG    1 
ATOM   1297 O  OD1   . ASN A 1 202 ? 5.99954   -9.86010  11.06852  1.000 26.48228  ? 266 ASN A OD1   1 
ATOM   1298 N  ND2   . ASN A 1 202 ? 7.43373   -8.13000  11.13347  1.000 23.14147  ? 266 ASN A ND2   1 
ATOM   1299 N  N     . LEU A 1 203 ? 7.09675   -10.21910 16.17268  1.000 21.92941  ? 267 LEU A N     1 
ATOM   1300 C  CA    . LEU A 1 203 ? 7.65427   -10.85700 17.36311  1.000 19.75658  ? 267 LEU A CA    1 
ATOM   1301 C  C     . LEU A 1 203 ? 6.66146   -11.80727 18.02493  1.000 23.80463  ? 267 LEU A C     1 
ATOM   1302 O  O     . LEU A 1 203 ? 7.04153   -12.90057 18.46961  1.000 21.87584  ? 267 LEU A O     1 
ATOM   1303 C  CB    . LEU A 1 203 ? 8.08879   -9.79962  18.37032  1.000 20.87451  ? 267 LEU A CB    1 
ATOM   1304 C  CG    . LEU A 1 203 ? 9.55749   -9.40228  18.37629  1.000 28.72173  ? 267 LEU A CG    1 
ATOM   1305 C  CD1   . LEU A 1 203 ? 9.84351   -8.58316  19.62356  1.000 25.84598  ? 267 LEU A CD1   1 
ATOM   1306 C  CD2   . LEU A 1 203 ? 10.40143  -10.65283 18.35458  1.000 28.70501  ? 267 LEU A CD2   1 
ATOM   1307 N  N     . VAL A 1 204 ? 5.39420   -11.39425 18.13350  1.000 18.65703  ? 268 VAL A N     1 
ATOM   1308 C  CA    . VAL A 1 204 ? 4.40683   -12.22716 18.80974  1.000 20.10118  ? 268 VAL A CA    1 
ATOM   1309 C  C     . VAL A 1 204 ? 4.19279   -13.52771 18.05356  1.000 25.73752  ? 268 VAL A C     1 
ATOM   1310 O  O     . VAL A 1 204 ? 4.13264   -14.60905 18.65453  1.000 30.65948  ? 268 VAL A O     1 
ATOM   1311 C  CB    . VAL A 1 204 ? 3.09223   -11.45553 19.00906  1.000 20.73807  ? 268 VAL A CB    1 
ATOM   1312 C  CG1   . VAL A 1 204 ? 2.03636   -12.38261 19.56408  1.000 22.34478  ? 268 VAL A CG1   1 
ATOM   1313 C  CG2   . VAL A 1 204 ? 3.31521   -10.30692 19.98706  1.000 18.72699  ? 268 VAL A CG2   1 
ATOM   1314 N  N     . LYS A 1 205 ? 4.09500   -13.45390 16.72706  1.000 32.14734  ? 269 LYS A N     1 
ATOM   1315 C  CA    . LYS A 1 205 ? 3.92251   -14.67078 15.94475  1.000 31.96781  ? 269 LYS A CA    1 
ATOM   1316 C  C     . LYS A 1 205 ? 5.12192   -15.59107 16.11199  1.000 35.50662  ? 269 LYS A C     1 
ATOM   1317 O  O     . LYS A 1 205 ? 4.96935   -16.80924 16.25941  1.000 41.24717  ? 269 LYS A O     1 
ATOM   1318 C  CB    . LYS A 1 205 ? 3.71315   -14.31452 14.47321  1.000 36.21386  ? 269 LYS A CB    1 
ATOM   1319 C  CG    . LYS A 1 205 ? 2.87660   -15.30940 13.70099  1.000 40.02623  ? 269 LYS A CG    1 
ATOM   1320 C  CD    . LYS A 1 205 ? 1.78781   -14.57130 12.92725  1.000 40.47991  ? 269 LYS A CD    1 
ATOM   1321 C  CE    . LYS A 1 205 ? 0.66752   -15.50592 12.49075  1.000 41.76727  ? 269 LYS A CE    1 
ATOM   1322 N  NZ    . LYS A 1 205 ? -0.66650  -14.83403 12.59480  1.000 33.85169  ? 269 LYS A NZ    1 
ATOM   1323 N  N     . LYS A 1 206 ? 6.32572   -15.02064 16.10533  1.000 21.75916  ? 270 LYS A N     1 
ATOM   1324 C  CA    . LYS A 1 206 ? 7.53242   -15.82962 16.23455  1.000 30.21085  ? 270 LYS A CA    1 
ATOM   1325 C  C     . LYS A 1 206 ? 7.61992   -16.47954 17.61219  1.000 34.87969  ? 270 LYS A C     1 
ATOM   1326 O  O     . LYS A 1 206 ? 8.03678   -17.63681 17.73776  1.000 34.36057  ? 270 LYS A O     1 
ATOM   1327 C  CB    . LYS A 1 206 ? 8.76102   -14.96287 15.94863  1.000 29.33998  ? 270 LYS A CB    1 
ATOM   1328 C  CG    . LYS A 1 206 ? 9.93462   -15.14784 16.89273  1.000 27.61015  ? 270 LYS A CG    1 
ATOM   1329 C  CD    . LYS A 1 206 ? 11.22981  -14.74619 16.19689  1.000 30.22208  ? 270 LYS A CD    1 
ATOM   1330 C  CE    . LYS A 1 206 ? 12.29688  -14.32662 17.20780  1.000 41.57197  ? 270 LYS A CE    1 
ATOM   1331 N  NZ    . LYS A 1 206 ? 13.59224  -13.94886 16.56156  1.000 37.96317  ? 270 LYS A NZ    1 
ATOM   1332 N  N     . TYR A 1 207 ? 7.22201   -15.75855 18.65701  1.000 51.64702  ? 271 TYR A N     1 
ATOM   1333 C  CA    . TYR A 1 207 ? 7.30831   -16.26574 20.01727  1.000 49.27487  ? 271 TYR A CA    1 
ATOM   1334 C  C     . TYR A 1 207 ? 5.98050   -16.81538 20.51867  1.000 54.06150  ? 271 TYR A C     1 
ATOM   1335 O  O     . TYR A 1 207 ? 5.72674   -16.80479 21.72806  1.000 54.30893  ? 271 TYR A O     1 
ATOM   1336 C  CB    . TYR A 1 207 ? 7.83136   -15.17779 20.95339  1.000 51.60720  ? 271 TYR A CB    1 
ATOM   1337 C  CG    . TYR A 1 207 ? 9.32489   -14.95819 20.82262  1.000 55.21204  ? 271 TYR A CG    1 
ATOM   1338 C  CD1   . TYR A 1 207 ? 10.17847  -16.01774 20.52851  1.000 56.21482  ? 271 TYR A CD1   1 
ATOM   1339 C  CD2   . TYR A 1 207 ? 9.87929   -13.69240 20.97474  1.000 54.41714  ? 271 TYR A CD2   1 
ATOM   1340 C  CE1   . TYR A 1 207 ? 11.54107  -15.82604 20.40297  1.000 57.10767  ? 271 TYR A CE1   1 
ATOM   1341 C  CE2   . TYR A 1 207 ? 11.24121  -13.49015 20.84817  1.000 53.35981  ? 271 TYR A CE2   1 
ATOM   1342 C  CZ    . TYR A 1 207 ? 12.06799  -14.55984 20.56215  1.000 58.77438  ? 271 TYR A CZ    1 
ATOM   1343 O  OH    . TYR A 1 207 ? 13.42504  -14.35734 20.42960  1.000 62.16372  ? 271 TYR A OH    1 
ATOM   1344 N  N     . SER A 1 208 ? 5.13858   -17.33966 19.62419  1.000 43.24769  ? 272 SER A N     1 
ATOM   1345 C  CA    . SER A 1 208 ? 3.96254   -18.05473 20.10030  1.000 43.30522  ? 272 SER A CA    1 
ATOM   1346 C  C     . SER A 1 208 ? 4.40604   -19.44382 20.54888  1.000 44.43662  ? 272 SER A C     1 
ATOM   1347 O  O     . SER A 1 208 ? 3.82404   -20.46658 20.16441  1.000 45.19687  ? 272 SER A O     1 
ATOM   1348 C  CB    . SER A 1 208 ? 2.87949   -18.14414 19.02638  1.000 43.38086  ? 272 SER A CB    1 
ATOM   1349 O  OG    . SER A 1 208 ? 1.86421   -19.05928 19.41987  1.000 43.86948  ? 272 SER A OG    1 
ATOM   1350 N  N     . GLN A 1 209 ? 5.44555   -19.46391 21.38570  1.000 70.53725  ? 273 GLN A N     1 
ATOM   1351 C  CA    . GLN A 1 209 ? 5.92517   -20.68178 22.02130  1.000 71.78749  ? 273 GLN A CA    1 
ATOM   1352 C  C     . GLN A 1 209 ? 5.01733   -21.07411 23.17025  1.000 71.74739  ? 273 GLN A C     1 
ATOM   1353 O  O     . GLN A 1 209 ? 4.44939   -22.17082 23.18709  1.000 72.56225  ? 273 GLN A O     1 
ATOM   1354 C  CB    . GLN A 1 209 ? 7.35723   -20.47593 22.52475  1.000 72.41964  ? 273 GLN A CB    1 
ATOM   1355 N  N     . PHE A 1 210 ? 4.87139   -20.17528 24.13699  1.000 44.43488  ? 274 PHE A N     1 
ATOM   1356 C  CA    . PHE A 1 210 ? 4.03496   -20.42016 25.30200  1.000 44.53849  ? 274 PHE A CA    1 
ATOM   1357 C  C     . PHE A 1 210 ? 2.66792   -19.75890 25.13028  1.000 43.60726  ? 274 PHE A C     1 
ATOM   1358 O  O     . PHE A 1 210 ? 2.32854   -18.79988 25.81188  1.000 42.98718  ? 274 PHE A O     1 
ATOM   1359 C  CB    . PHE A 1 210 ? 4.73524   -19.92073 26.55935  1.000 44.72668  ? 274 PHE A CB    1 
ATOM   1360 N  N     . ILE A 1 211 ? 1.87540   -20.26509 24.18395  1.000 47.75270  ? 275 ILE A N     1 
ATOM   1361 C  CA    . ILE A 1 211 ? 0.47209   -19.86458 24.18860  1.000 45.96349  ? 275 ILE A CA    1 
ATOM   1362 C  C     . ILE A 1 211 ? -0.44758  -20.91770 23.58397  1.000 41.82786  ? 275 ILE A C     1 
ATOM   1363 O  O     . ILE A 1 211 ? -0.42905  -21.14858 22.36995  1.000 43.26444  ? 275 ILE A O     1 
ATOM   1364 C  CB    . ILE A 1 211 ? 0.29558   -18.52108 23.46334  1.000 36.02590  ? 275 ILE A CB    1 
ATOM   1365 N  N     . ASN A 1 212 ? -1.30312  -21.51257 24.41899  1.000 34.60335  ? 276 ASN A N     1 
ATOM   1366 C  CA    . ASN A 1 212 ? -2.53286  -22.15410 23.97026  1.000 29.18662  ? 276 ASN A CA    1 
ATOM   1367 C  C     . ASN A 1 212 ? -3.75071  -21.33860 24.38032  1.000 32.87650  ? 276 ASN A C     1 
ATOM   1368 O  O     . ASN A 1 212 ? -4.87976  -21.83726 24.32232  1.000 36.66252  ? 276 ASN A O     1 
ATOM   1369 C  CB    . ASN A 1 212 ? -2.64751  -23.58955 24.49768  1.000 38.42923  ? 276 ASN A CB    1 
ATOM   1370 C  CG    . ASN A 1 212 ? -1.95053  -24.61171 23.59708  1.000 39.72951  ? 276 ASN A CG    1 
ATOM   1371 O  OD1   . ASN A 1 212 ? -1.82030  -24.41466 22.38302  1.000 33.55186  ? 276 ASN A OD1   1 
ATOM   1372 N  ND2   . ASN A 1 212 ? -1.50524  -25.71425 24.19310  1.000 36.64417  ? 276 ASN A ND2   1 
ATOM   1373 N  N     . PHE A 1 213 ? -3.53703  -20.10423 24.82233  1.000 21.59358  ? 277 PHE A N     1 
ATOM   1374 C  CA    . PHE A 1 213 ? -4.55266  -19.08380 24.95996  1.000 20.62591  ? 277 PHE A CA    1 
ATOM   1375 C  C     . PHE A 1 213 ? -4.37482  -18.04808 23.85733  1.000 14.88225  ? 277 PHE A C     1 
ATOM   1376 O  O     . PHE A 1 213 ? -3.25376  -17.81427 23.38498  1.000 11.51768  ? 277 PHE A O     1 
ATOM   1377 C  CB    . PHE A 1 213 ? -4.49105  -18.39556 26.33328  1.000 15.09107  ? 277 PHE A CB    1 
ATOM   1378 C  CG    . PHE A 1 213 ? -4.49215  -19.35712 27.47480  1.000 12.95851  ? 277 PHE A CG    1 
ATOM   1379 C  CD1   . PHE A 1 213 ? -5.69014  -19.85491 27.97737  1.000 18.11921  ? 277 PHE A CD1   1 
ATOM   1380 C  CD2   . PHE A 1 213 ? -3.29873  -19.82032 28.00618  1.000 13.25916  ? 277 PHE A CD2   1 
ATOM   1381 C  CE1   . PHE A 1 213 ? -5.69931  -20.78299 29.02368  1.000 20.02775  ? 277 PHE A CE1   1 
ATOM   1382 C  CE2   . PHE A 1 213 ? -3.28826  -20.73408 29.04711  1.000 13.76425  ? 277 PHE A CE2   1 
ATOM   1383 C  CZ    . PHE A 1 213 ? -4.49314  -21.21803 29.56650  1.000 15.98093  ? 277 PHE A CZ    1 
ATOM   1384 N  N     . PRO A 1 214 ? -5.46212  -17.43022 23.40613  1.000 18.44628  ? 278 PRO A N     1 
ATOM   1385 C  CA    . PRO A 1 214 ? -5.34716  -16.43369 22.33918  1.000 18.04781  ? 278 PRO A CA    1 
ATOM   1386 C  C     . PRO A 1 214 ? -4.45588  -15.26074 22.72834  1.000 20.32722  ? 278 PRO A C     1 
ATOM   1387 O  O     . PRO A 1 214 ? -4.44687  -14.80162 23.87524  1.000 16.35448  ? 278 PRO A O     1 
ATOM   1388 C  CB    . PRO A 1 214 ? -6.80148  -15.99919 22.11786  1.000 22.26175  ? 278 PRO A CB    1 
ATOM   1389 C  CG    . PRO A 1 214 ? -7.51226  -16.39117 23.37605  1.000 18.51776  ? 278 PRO A CG    1 
ATOM   1390 C  CD    . PRO A 1 214 ? -6.86352  -17.66106 23.78955  1.000 19.65644  ? 278 PRO A CD    1 
ATOM   1391 N  N     . ILE A 1 215 ? -3.70476  -14.76871 21.75255  1.000 19.84961  ? 279 ILE A N     1 
ATOM   1392 C  CA    . ILE A 1 215 ? -2.89831  -13.56947 21.92057  1.000 18.01505  ? 279 ILE A CA    1 
ATOM   1393 C  C     . ILE A 1 215 ? -3.35072  -12.54122 20.89472  1.000 21.47386  ? 279 ILE A C     1 
ATOM   1394 O  O     . ILE A 1 215 ? -3.39709  -12.83293 19.69453  1.000 20.07716  ? 279 ILE A O     1 
ATOM   1395 C  CB    . ILE A 1 215 ? -1.39366  -13.86003 21.77742  1.000 17.57170  ? 279 ILE A CB    1 
ATOM   1396 C  CG1   . ILE A 1 215 ? -0.99535  -15.03965 22.67129  1.000 23.28862  ? 279 ILE A CG1   1 
ATOM   1397 C  CG2   . ILE A 1 215 ? -0.59338  -12.61100 22.10049  1.000 17.09118  ? 279 ILE A CG2   1 
ATOM   1398 C  CD1   . ILE A 1 215 ? 0.46378   -15.05172 23.05122  1.000 27.61243  ? 279 ILE A CD1   1 
ATOM   1399 N  N     . TYR A 1 216 ? -3.68256  -11.34702 21.37274  1.000 14.01100  ? 280 TYR A N     1 
ATOM   1400 C  CA    . TYR A 1 216 ? -4.15964  -10.24688 20.55061  1.000 13.47043  ? 280 TYR A CA    1 
ATOM   1401 C  C     . TYR A 1 216 ? -3.18668  -9.08033  20.60756  1.000 13.14632  ? 280 TYR A C     1 
ATOM   1402 O  O     . TYR A 1 216 ? -2.59074  -8.78689  21.65268  1.000 13.03657  ? 280 TYR A O     1 
ATOM   1403 C  CB    . TYR A 1 216 ? -5.52366  -9.74869  21.02325  1.000 15.35813  ? 280 TYR A CB    1 
ATOM   1404 C  CG    . TYR A 1 216 ? -6.59405  -10.79998 20.97199  1.000 15.54668  ? 280 TYR A CG    1 
ATOM   1405 C  CD1   . TYR A 1 216 ? -6.70867  -11.74215 21.98829  1.000 19.21704  ? 280 TYR A CD1   1 
ATOM   1406 C  CD2   . TYR A 1 216 ? -7.50096  -10.83823 19.92401  1.000 15.82862  ? 280 TYR A CD2   1 
ATOM   1407 C  CE1   . TYR A 1 216 ? -7.68446  -12.71177 21.95453  1.000 22.30380  ? 280 TYR A CE1   1 
ATOM   1408 C  CE2   . TYR A 1 216 ? -8.48557  -11.81076 19.87397  1.000 23.56363  ? 280 TYR A CE2   1 
ATOM   1409 C  CZ    . TYR A 1 216 ? -8.57735  -12.74454 20.89442  1.000 23.41523  ? 280 TYR A CZ    1 
ATOM   1410 O  OH    . TYR A 1 216 ? -9.55747  -13.71991 20.86218  1.000 22.78353  ? 280 TYR A OH    1 
ATOM   1411 N  N     . VAL A 1 217 ? -3.07334  -8.38721  19.48212  1.000 13.97871  ? 281 VAL A N     1 
ATOM   1412 C  CA    . VAL A 1 217 ? -2.35136  -7.13112  19.38851  1.000 14.34581  ? 281 VAL A CA    1 
ATOM   1413 C  C     . VAL A 1 217 ? -3.35844  -6.06265  19.00145  1.000 16.66226  ? 281 VAL A C     1 
ATOM   1414 O  O     . VAL A 1 217 ? -4.10032  -6.23215  18.02385  1.000 16.81027  ? 281 VAL A O     1 
ATOM   1415 C  CB    . VAL A 1 217 ? -1.19904  -7.21297  18.36962  1.000 15.21952  ? 281 VAL A CB    1 
ATOM   1416 C  CG1   . VAL A 1 217 ? -0.57381  -5.85015  18.15813  1.000 13.75816  ? 281 VAL A CG1   1 
ATOM   1417 C  CG2   . VAL A 1 217 ? -0.15119  -8.19892  18.85964  1.000 13.21550  ? 281 VAL A CG2   1 
ATOM   1418 N  N     . TRP A 1 218 ? -3.40696  -4.97857  19.78490  1.000 15.36816  ? 282 TRP A N     1 
ATOM   1419 C  CA    . TRP A 1 218 ? -4.23980  -3.83926  19.42624  1.000 14.54361  ? 282 TRP A CA    1 
ATOM   1420 C  C     . TRP A 1 218 ? -3.76356  -3.29277  18.09469  1.000 18.00232  ? 282 TRP A C     1 
ATOM   1421 O  O     . TRP A 1 218 ? -2.63053  -2.80848  17.97659  1.000 14.94774  ? 282 TRP A O     1 
ATOM   1422 C  CB    . TRP A 1 218 ? -4.18908  -2.74787  20.49215  1.000 15.78385  ? 282 TRP A CB    1 
ATOM   1423 C  CG    . TRP A 1 218 ? -5.11980  -1.63146  20.23309  1.000 18.78889  ? 282 TRP A CG    1 
ATOM   1424 C  CD1   . TRP A 1 218 ? -4.79052  -0.33807  19.94670  1.000 18.01861  ? 282 TRP A CD1   1 
ATOM   1425 C  CD2   . TRP A 1 218 ? -6.54986  -1.69197  20.23980  1.000 21.41772  ? 282 TRP A CD2   1 
ATOM   1426 N  NE1   . TRP A 1 218 ? -5.93070  0.40885   19.76704  1.000 19.61214  ? 282 TRP A NE1   1 
ATOM   1427 C  CE2   . TRP A 1 218 ? -7.02362  -0.39891  19.94814  1.000 26.32891  ? 282 TRP A CE2   1 
ATOM   1428 C  CE3   . TRP A 1 218 ? -7.47725  -2.71827  20.46072  1.000 24.91646  ? 282 TRP A CE3   1 
ATOM   1429 C  CZ2   . TRP A 1 218 ? -8.38683  -0.09892  19.87967  1.000 27.32884  ? 282 TRP A CZ2   1 
ATOM   1430 C  CZ3   . TRP A 1 218 ? -8.83213  -2.42020  20.38961  1.000 23.88409  ? 282 TRP A CZ3   1 
ATOM   1431 C  CH2   . TRP A 1 218 ? -9.27129  -1.11973  20.10719  1.000 26.82581  ? 282 TRP A CH2   1 
ATOM   1432 N  N     . SER A 1 219 ? -4.59757  -3.44151  17.07693  1.000 15.75405  ? 283 SER A N     1 
ATOM   1433 C  CA    . SER A 1 219 ? -4.24176  -3.09811  15.70745  1.000 15.63949  ? 283 SER A CA    1 
ATOM   1434 C  C     . SER A 1 219 ? -4.85392  -1.75907  15.33459  1.000 17.38877  ? 283 SER A C     1 
ATOM   1435 O  O     . SER A 1 219 ? -5.70398  -1.66130  14.44694  1.000 23.59869  ? 283 SER A O     1 
ATOM   1436 C  CB    . SER A 1 219 ? -4.69642  -4.19839  14.75774  1.000 15.72231  ? 283 SER A CB    1 
ATOM   1437 O  OG    . SER A 1 219 ? -3.97048  -4.14882  13.53700  1.000 21.28950  ? 283 SER A OG    1 
ATOM   1438 N  N     . SER A 1 220 ? -4.41917  -0.73067  16.05222  1.000 25.69003  ? 284 SER A N     1 
ATOM   1439 C  CA    . SER A 1 220 ? -4.93201  0.61345   15.85045  1.000 28.68236  ? 284 SER A CA    1 
ATOM   1440 C  C     . SER A 1 220 ? -4.05973  1.58436   16.62969  1.000 32.60475  ? 284 SER A C     1 
ATOM   1441 O  O     . SER A 1 220 ? -3.27828  1.18266   17.50199  1.000 36.65407  ? 284 SER A O     1 
ATOM   1442 C  CB    . SER A 1 220 ? -6.38980  0.73896   16.28414  1.000 26.87759  ? 284 SER A CB    1 
ATOM   1443 O  OG    . SER A 1 220 ? -6.92800  1.92916   15.75306  1.000 36.05657  ? 284 SER A OG    1 
ATOM   1444 N  N     . LYS A 1 221 ? -4.20394  2.86603   16.29968  1.000 53.99183  ? 285 LYS A N     1 
ATOM   1445 C  CA    . LYS A 1 221 ? -3.43980  3.93095   16.94362  1.000 53.95369  ? 285 LYS A CA    1 
ATOM   1446 C  C     . LYS A 1 221 ? -4.35872  4.90028   17.68009  1.000 55.42301  ? 285 LYS A C     1 
ATOM   1447 O  O     . LYS A 1 221 ? -5.11774  5.64037   17.05467  1.000 56.88125  ? 285 LYS A O     1 
ATOM   1448 C  CB    . LYS A 1 221 ? -2.60227  4.69002   15.90991  1.000 54.08220  ? 285 LYS A CB    1 
ATOM   1449 N  N     . GLY A 1 226 ? -8.55905  4.18142   17.13922  1.000 55.99986  ? 327 GLY A N     1 
ATOM   1450 C  CA    . GLY A 1 226 ? -9.44710  3.03465   17.05403  1.000 56.34492  ? 327 GLY A CA    1 
ATOM   1451 C  C     . GLY A 1 226 ? -10.50858 3.05230   18.13325  1.000 57.70354  ? 327 GLY A C     1 
ATOM   1452 O  O     . GLY A 1 226 ? -10.29603 3.60811   19.21220  1.000 57.70586  ? 327 GLY A O     1 
ATOM   1453 N  N     . LYS A 1 227 ? -11.65382 2.42697   17.84656  1.000 73.67556  ? 328 LYS A N     1 
ATOM   1454 C  CA    . LYS A 1 227 ? -12.82951 2.56399   18.69368  1.000 75.58994  ? 328 LYS A CA    1 
ATOM   1455 C  C     . LYS A 1 227 ? -13.56025 1.26626   19.01264  1.000 75.90980  ? 328 LYS A C     1 
ATOM   1456 O  O     . LYS A 1 227 ? -14.39043 1.27211   19.92692  1.000 77.30766  ? 328 LYS A O     1 
ATOM   1457 C  CB    . LYS A 1 227 ? -13.83275 3.53680   18.05112  1.000 78.19478  ? 328 LYS A CB    1 
ATOM   1458 N  N     . THR A 1 228 ? -13.28870 0.16586   18.31580  1.000 67.22433  ? 329 THR A N     1 
ATOM   1459 C  CA    . THR A 1 228 ? -14.12120 -1.02541  18.43107  1.000 68.01583  ? 329 THR A CA    1 
ATOM   1460 C  C     . THR A 1 228 ? -13.31949 -2.25033  18.86291  1.000 66.02675  ? 329 THR A C     1 
ATOM   1461 O  O     . THR A 1 228 ? -12.08506 -2.26605  18.85091  1.000 64.04001  ? 329 THR A O     1 
ATOM   1462 C  CB    . THR A 1 228 ? -14.83514 -1.33437  17.11092  1.000 69.46056  ? 329 THR A CB    1 
ATOM   1463 O  OG1   . THR A 1 228 ? -15.40576 -2.64406  17.18844  1.000 69.92741  ? 329 THR A OG1   1 
ATOM   1464 C  CG2   . THR A 1 228 ? -13.85635 -1.29687  15.95646  1.000 68.08402  ? 329 THR A CG2   1 
ATOM   1465 N  N     . VAL A 1 229 ? -14.06756 -3.29655  19.22925  1.000 42.50200  ? 330 VAL A N     1 
ATOM   1466 C  CA    . VAL A 1 229 ? -13.48033 -4.55675  19.67270  1.000 47.64174  ? 330 VAL A CA    1 
ATOM   1467 C  C     . VAL A 1 229 ? -12.93168 -5.37966  18.51503  1.000 44.36843  ? 330 VAL A C     1 
ATOM   1468 O  O     . VAL A 1 229 ? -12.13193 -6.29707  18.74076  1.000 40.38915  ? 330 VAL A O     1 
ATOM   1469 C  CB    . VAL A 1 229 ? -14.51191 -5.38693  20.45809  1.000 51.74099  ? 330 VAL A CB    1 
ATOM   1470 N  N     . TRP A 1 230 ? -13.33946 -5.08580  17.28197  1.000 96.66529  ? 331 TRP A N     1 
ATOM   1471 C  CA    . TRP A 1 230 ? -12.75271 -5.72542  16.11310  1.000 93.83710  ? 331 TRP A CA    1 
ATOM   1472 C  C     . TRP A 1 230 ? -11.40941 -5.12112  15.72657  1.000 91.34631  ? 331 TRP A C     1 
ATOM   1473 O  O     . TRP A 1 230 ? -10.89618 -5.42006  14.64401  1.000 91.99035  ? 331 TRP A O     1 
ATOM   1474 C  CB    . TRP A 1 230 ? -13.72233 -5.66029  14.93140  1.000 87.96358  ? 331 TRP A CB    1 
ATOM   1475 C  CG    . TRP A 1 230 ? -14.88612 -6.59922  15.07430  1.000 89.79677  ? 331 TRP A CG    1 
ATOM   1476 C  CD1   . TRP A 1 230 ? -14.98316 -7.86399  14.56562  1.000 90.10857  ? 331 TRP A CD1   1 
ATOM   1477 C  CD2   . TRP A 1 230 ? -16.12408 -6.34663  15.75150  1.000 91.82154  ? 331 TRP A CD2   1 
ATOM   1478 N  NE1   . TRP A 1 230 ? -16.19680 -8.41724  14.89328  1.000 92.14704  ? 331 TRP A NE1   1 
ATOM   1479 C  CE2   . TRP A 1 230 ? -16.91768 -7.50565  15.61878  1.000 93.24215  ? 331 TRP A CE2   1 
ATOM   1480 C  CE3   . TRP A 1 230 ? -16.63734 -5.25761  16.45966  1.000 92.74886  ? 331 TRP A CE3   1 
ATOM   1481 C  CZ2   . TRP A 1 230 ? -18.19673 -7.60305  16.16692  1.000 95.54687  ? 331 TRP A CZ2   1 
ATOM   1482 C  CZ3   . TRP A 1 230 ? -17.90779 -5.35648  17.00383  1.000 95.09184  ? 331 TRP A CZ3   1 
ATOM   1483 C  CH2   . TRP A 1 230 ? -18.67243 -6.52066  16.85393  1.000 96.45421  ? 331 TRP A CH2   1 
ATOM   1484 N  N     . ASP A 1 231 ? -10.83624 -4.28346  16.58702  1.000 34.83311  ? 332 ASP A N     1 
ATOM   1485 C  CA    . ASP A 1 231 ? -9.52018  -3.70438  16.37781  1.000 30.41102  ? 332 ASP A CA    1 
ATOM   1486 C  C     . ASP A 1 231 ? -8.41818  -4.53773  17.00926  1.000 25.20335  ? 332 ASP A C     1 
ATOM   1487 O  O     . ASP A 1 231 ? -7.26131  -4.10960  17.02186  1.000 25.78796  ? 332 ASP A O     1 
ATOM   1488 C  CB    . ASP A 1 231 ? -9.47617  -2.28884  16.93938  1.000 32.46663  ? 332 ASP A CB    1 
ATOM   1489 C  CG    . ASP A 1 231 ? -10.02946 -1.26155  15.97644  1.000 36.09285  ? 332 ASP A CG    1 
ATOM   1490 O  OD1   . ASP A 1 231 ? -9.70043  -1.31901  14.76646  1.000 37.99230  ? 332 ASP A OD1   1 
ATOM   1491 O  OD2   . ASP A 1 231 ? -10.81934 -0.40974  16.43214  1.000 33.44657  ? 332 ASP A OD2   1 
ATOM   1492 N  N     . TRP A 1 232 ? -8.75798  -5.69321  17.56212  1.000 27.87003  ? 333 TRP A N     1 
ATOM   1493 C  CA    . TRP A 1 232 ? -7.77290  -6.63049  18.06846  1.000 21.49246  ? 333 TRP A CA    1 
ATOM   1494 C  C     . TRP A 1 232 ? -7.47014  -7.64198  16.97808  1.000 25.81650  ? 333 TRP A C     1 
ATOM   1495 O  O     . TRP A 1 232 ? -8.39113  -8.23830  16.41327  1.000 29.95750  ? 333 TRP A O     1 
ATOM   1496 C  CB    . TRP A 1 232 ? -8.28992  -7.35773  19.30747  1.000 24.04461  ? 333 TRP A CB    1 
ATOM   1497 C  CG    . TRP A 1 232 ? -8.40370  -6.51181  20.53698  1.000 27.50456  ? 333 TRP A CG    1 
ATOM   1498 C  CD1   . TRP A 1 232 ? -9.54744  -6.00006  21.06809  1.000 30.24351  ? 333 TRP A CD1   1 
ATOM   1499 C  CD2   . TRP A 1 232 ? -7.33282  -6.07814  21.39354  1.000 22.73003  ? 333 TRP A CD2   1 
ATOM   1500 N  NE1   . TRP A 1 232 ? -9.26172  -5.28016  22.20159  1.000 31.06945  ? 333 TRP A NE1   1 
ATOM   1501 C  CE2   . TRP A 1 232 ? -7.91079  -5.30955  22.42281  1.000 25.27722  ? 333 TRP A CE2   1 
ATOM   1502 C  CE3   . TRP A 1 232 ? -5.94585  -6.26874  21.38795  1.000 17.58532  ? 333 TRP A CE3   1 
ATOM   1503 C  CZ2   . TRP A 1 232 ? -7.15458  -4.73019  23.43997  1.000 23.31897  ? 333 TRP A CZ2   1 
ATOM   1504 C  CZ3   . TRP A 1 232 ? -5.19721  -5.69531  22.38437  1.000 17.07307  ? 333 TRP A CZ3   1 
ATOM   1505 C  CH2   . TRP A 1 232 ? -5.80180  -4.93587  23.40596  1.000 25.40512  ? 333 TRP A CH2   1 
ATOM   1506 N  N     . GLU A 1 233 ? -6.19214  -7.83719  16.67589  1.000 21.80718  ? 334 GLU A N     1 
ATOM   1507 C  CA    . GLU A 1 233 ? -5.79361  -8.88511  15.75418  1.000 21.78762  ? 334 GLU A CA    1 
ATOM   1508 C  C     . GLU A 1 233 ? -5.34975  -10.11350 16.54308  1.000 21.45333  ? 334 GLU A C     1 
ATOM   1509 O  O     . GLU A 1 233 ? -4.40429  -10.03949 17.33568  1.000 17.51671  ? 334 GLU A O     1 
ATOM   1510 C  CB    . GLU A 1 233 ? -4.68595  -8.41256  14.81810  1.000 19.87706  ? 334 GLU A CB    1 
ATOM   1511 C  CG    . GLU A 1 233 ? -4.64874  -9.21926  13.54061  1.000 22.96180  ? 334 GLU A CG    1 
ATOM   1512 C  CD    . GLU A 1 233 ? -3.38409  -9.01294  12.73744  1.000 20.50511  ? 334 GLU A CD    1 
ATOM   1513 O  OE1   . GLU A 1 233 ? -2.94810  -7.84650  12.63991  1.000 21.73020  ? 334 GLU A OE1   1 
ATOM   1514 O  OE2   . GLU A 1 233 ? -2.84889  -10.00817 12.18725  1.000 22.26909  ? 334 GLU A OE2   1 
ATOM   1515 N  N     . LEU A 1 234 ? -6.01568  -11.24338 16.30282  1.000 14.37589  ? 335 LEU A N     1 
ATOM   1516 C  CA    . LEU A 1 234 ? -5.63204  -12.50391 16.92601  1.000 13.85503  ? 335 LEU A CA    1 
ATOM   1517 C  C     . LEU A 1 234 ? -4.33555  -12.99933 16.30345  1.000 13.45527  ? 335 LEU A C     1 
ATOM   1518 O  O     . LEU A 1 234 ? -4.26671  -13.19347 15.08637  1.000 18.68617  ? 335 LEU A O     1 
ATOM   1519 C  CB    . LEU A 1 234 ? -6.73551  -13.54214 16.74488  1.000 15.43220  ? 335 LEU A CB    1 
ATOM   1520 C  CG    . LEU A 1 234 ? -6.34100  -14.93442 17.23547  1.000 15.25771  ? 335 LEU A CG    1 
ATOM   1521 C  CD1   . LEU A 1 234 ? -6.22757  -14.91696 18.73689  1.000 20.16233  ? 335 LEU A CD1   1 
ATOM   1522 C  CD2   . LEU A 1 234 ? -7.35405  -15.97605 16.81096  1.000 24.88789  ? 335 LEU A CD2   1 
ATOM   1523 N  N     . MET A 1 235 ? -3.30931  -13.21493 17.12599  1.000 16.03733  ? 336 MET A N     1 
ATOM   1524 C  CA    . MET A 1 235 ? -1.97413  -13.49080 16.60267  1.000 14.30633  ? 336 MET A CA    1 
ATOM   1525 C  C     . MET A 1 235 ? -1.67089  -14.97862 16.43142  1.000 17.00833  ? 336 MET A C     1 
ATOM   1526 O  O     . MET A 1 235 ? -0.80580  -15.33326 15.61552  1.000 17.77001  ? 336 MET A O     1 
ATOM   1527 C  CB    . MET A 1 235 ? -0.91686  -12.86693 17.52296  1.000 16.17768  ? 336 MET A CB    1 
ATOM   1528 C  CG    . MET A 1 235 ? -0.74761  -11.34378 17.42998  1.000 14.48456  ? 336 MET A CG    1 
ATOM   1529 S  SD    . MET A 1 235 ? -1.20508  -10.56307 15.86606  1.000 17.13800  ? 336 MET A SD    1 
ATOM   1530 C  CE    . MET A 1 235 ? 0.18990   -11.06617 14.84923  1.000 13.48595  ? 336 MET A CE    1 
ATOM   1531 N  N     . ASN A 1 236 ? -2.35586  -15.86171 17.15783  1.000 16.91295  ? 337 ASN A N     1 
ATOM   1532 C  CA    . ASN A 1 236 ? -1.98954  -17.27547 17.15986  1.000 20.54318  ? 337 ASN A CA    1 
ATOM   1533 C  C     . ASN A 1 236 ? -3.19533  -18.19466 17.02193  1.000 24.40629  ? 337 ASN A C     1 
ATOM   1534 O  O     . ASN A 1 236 ? -3.19671  -19.29643 17.58432  1.000 23.38215  ? 337 ASN A O     1 
ATOM   1535 C  CB    . ASN A 1 236 ? -1.23158  -17.61290 18.44884  1.000 21.02955  ? 337 ASN A CB    1 
ATOM   1536 C  CG    . ASN A 1 236 ? -2.06248  -17.35878 19.69184  1.000 15.94118  ? 337 ASN A CG    1 
ATOM   1537 O  OD1   . ASN A 1 236 ? -3.06532  -16.64887 19.63986  1.000 16.72030  ? 337 ASN A OD1   1 
ATOM   1538 N  ND2   . ASN A 1 236 ? -1.67715  -17.97888 20.80660  1.000 19.90928  ? 337 ASN A ND2   1 
ATOM   1539 O  OXT   . ASN A 1 236 ? -4.19206  -17.85745 16.37050  1.000 19.64581  ? 337 ASN A OXT   1 
ATOM   1540 N  N     . GLY B 1 1   ? 7.26935   -51.23252 -19.94479 1.000 77.68488  ? 65  GLY B N     1 
ATOM   1541 C  CA    . GLY B 1 1   ? 6.17036   -51.90358 -20.61582 1.000 77.07302  ? 65  GLY B CA    1 
ATOM   1542 C  C     . GLY B 1 1   ? 5.95460   -53.27281 -20.03676 1.000 78.17790  ? 65  GLY B C     1 
ATOM   1543 O  O     . GLY B 1 1   ? 4.84420   -53.80652 -20.01769 1.000 77.53846  ? 65  GLY B O     1 
ATOM   1544 N  N     . SER B 1 2   ? 7.05330   -53.82782 -19.55603 1.000 80.04891  ? 66  SER B N     1 
ATOM   1545 C  CA    . SER B 1 2   ? 7.09701   -55.03063 -18.75233 1.000 81.58833  ? 66  SER B CA    1 
ATOM   1546 C  C     . SER B 1 2   ? 7.60547   -54.62306 -17.37711 1.000 81.98203  ? 66  SER B C     1 
ATOM   1547 O  O     . SER B 1 2   ? 7.68221   -53.43020 -17.05472 1.000 80.81779  ? 66  SER B O     1 
ATOM   1548 C  CB    . SER B 1 2   ? 7.98079   -56.09012 -19.41225 1.000 83.85927  ? 66  SER B CB    1 
ATOM   1549 O  OG    . SER B 1 2   ? 9.05397   -55.48934 -20.11707 1.000 84.33613  ? 66  SER B OG    1 
ATOM   1550 N  N     . HIS B 1 3   ? 7.91928   -55.61346 -16.54342 1.000 77.94307  ? 67  HIS B N     1 
ATOM   1551 C  CA    . HIS B 1 3   ? 8.55266   -55.29972 -15.26916 1.000 80.61722  ? 67  HIS B CA    1 
ATOM   1552 C  C     . HIS B 1 3   ? 9.89824   -54.61249 -15.47269 1.000 82.50108  ? 67  HIS B C     1 
ATOM   1553 O  O     . HIS B 1 3   ? 10.32655  -53.82426 -14.62065 1.000 83.72977  ? 67  HIS B O     1 
ATOM   1554 C  CB    . HIS B 1 3   ? 8.72025   -56.57104 -14.43666 1.000 83.63772  ? 67  HIS B CB    1 
ATOM   1555 N  N     . MET B 1 4   ? 10.55937  -54.87164 -16.60793 1.000 77.51111  ? 68  MET B N     1 
ATOM   1556 C  CA    . MET B 1 4   ? 11.94696  -54.45030 -16.79160 1.000 79.74923  ? 68  MET B CA    1 
ATOM   1557 C  C     . MET B 1 4   ? 12.08684  -52.93573 -16.92065 1.000 78.57665  ? 68  MET B C     1 
ATOM   1558 O  O     . MET B 1 4   ? 13.10049  -52.37150 -16.49099 1.000 80.40361  ? 68  MET B O     1 
ATOM   1559 C  CB    . MET B 1 4   ? 12.54354  -55.14723 -18.01791 1.000 80.31313  ? 68  MET B CB    1 
ATOM   1560 N  N     . LEU B 1 5   ? 11.09813  -52.26240 -17.50397 1.000 72.68345  ? 69  LEU B N     1 
ATOM   1561 C  CA    . LEU B 1 5   ? 11.16040  -50.81748 -17.68075 1.000 71.47372  ? 69  LEU B CA    1 
ATOM   1562 C  C     . LEU B 1 5   ? 10.65951  -50.04288 -16.46660 1.000 71.14411  ? 69  LEU B C     1 
ATOM   1563 O  O     . LEU B 1 5   ? 10.76260  -48.81091 -16.45223 1.000 70.44458  ? 69  LEU B O     1 
ATOM   1564 C  CB    . LEU B 1 5   ? 10.36081  -50.40397 -18.92441 1.000 66.39501  ? 69  LEU B CB    1 
ATOM   1565 N  N     . ARG B 1 6   ? 10.12645  -50.72625 -15.45108 1.000 64.34247  ? 70  ARG B N     1 
ATOM   1566 C  CA    . ARG B 1 6   ? 9.66777   -50.03408 -14.25075 1.000 64.38545  ? 70  ARG B CA    1 
ATOM   1567 C  C     . ARG B 1 6   ? 10.83849  -49.41900 -13.49202 1.000 67.17949  ? 70  ARG B C     1 
ATOM   1568 O  O     . ARG B 1 6   ? 10.89549  -48.19951 -13.29813 1.000 66.49046  ? 70  ARG B O     1 
ATOM   1569 C  CB    . ARG B 1 6   ? 8.89377   -50.99586 -13.34821 1.000 65.46405  ? 70  ARG B CB    1 
ATOM   1570 C  CG    . ARG B 1 6   ? 7.40856   -51.13653 -13.66171 1.000 62.14857  ? 70  ARG B CG    1 
ATOM   1571 C  CD    . ARG B 1 6   ? 6.87751   -52.44136 -13.06685 1.000 63.26991  ? 70  ARG B CD    1 
ATOM   1572 N  NE    . ARG B 1 6   ? 5.43876   -52.43334 -12.82492 1.000 60.88362  ? 70  ARG B NE    1 
ATOM   1573 C  CZ    . ARG B 1 6   ? 4.52466   -52.71987 -13.74230 1.000 57.93160  ? 70  ARG B CZ    1 
ATOM   1574 N  NH1   . ARG B 1 6   ? 4.86288   -52.98557 -14.99411 1.000 56.84678  ? 70  ARG B NH1   1 
ATOM   1575 N  NH2   . ARG B 1 6   ? 3.23904   -52.74232 -13.39517 1.000 56.14967  ? 70  ARG B NH2   1 
ATOM   1576 N  N     . GLU B 1 7   ? 11.79783  -50.25316 -13.07291 1.000 70.10279  ? 71  GLU B N     1 
ATOM   1577 C  CA    . GLU B 1 7   ? 12.88269  -49.78301 -12.21324 1.000 62.85369  ? 71  GLU B CA    1 
ATOM   1578 C  C     . GLU B 1 7   ? 13.70304  -48.67735 -12.87135 1.000 71.98270  ? 71  GLU B C     1 
ATOM   1579 O  O     . GLU B 1 7   ? 14.24646  -47.81293 -12.17320 1.000 72.61053  ? 71  GLU B O     1 
ATOM   1580 C  CB    . GLU B 1 7   ? 13.78499  -50.95341 -11.82061 1.000 65.78934  ? 71  GLU B CB    1 
ATOM   1581 N  N     . LYS B 1 8   ? 13.80269  -48.68030 -14.20389 1.000 72.86542  ? 72  LYS B N     1 
ATOM   1582 C  CA    . LYS B 1 8   ? 14.50776  -47.60213 -14.89126 1.000 55.91337  ? 72  LYS B CA    1 
ATOM   1583 C  C     . LYS B 1 8   ? 13.83102  -46.25919 -14.64407 1.000 71.40195  ? 72  LYS B C     1 
ATOM   1584 O  O     . LYS B 1 8   ? 14.50532  -45.23637 -14.47002 1.000 71.70376  ? 72  LYS B O     1 
ATOM   1585 C  CB    . LYS B 1 8   ? 14.58530  -47.89388 -16.39129 1.000 72.91065  ? 72  LYS B CB    1 
ATOM   1586 N  N     . SER B 1 9   ? 12.49912  -46.24095 -14.63024 1.000 70.67438  ? 73  SER B N     1 
ATOM   1587 C  CA    . SER B 1 9   ? 11.73277  -45.02555 -14.39180 1.000 52.16897  ? 73  SER B CA    1 
ATOM   1588 C  C     . SER B 1 9   ? 11.28041  -44.87445 -12.94365 1.000 69.04364  ? 73  SER B C     1 
ATOM   1589 O  O     . SER B 1 9   ? 10.71919  -43.83142 -12.59271 1.000 68.41473  ? 73  SER B O     1 
ATOM   1590 C  CB    . SER B 1 9   ? 10.51094  -44.98516 -15.32096 1.000 50.77659  ? 73  SER B CB    1 
ATOM   1591 N  N     . GLU B 1 10  ? 11.50947  -45.87770 -12.09413 1.000 54.78685  ? 74  GLU B N     1 
ATOM   1592 C  CA    . GLU B 1 10  ? 11.06609  -45.82033 -10.70481 1.000 55.53202  ? 74  GLU B CA    1 
ATOM   1593 C  C     . GLU B 1 10  ? 12.18982  -45.51233 -9.72481  1.000 52.16623  ? 74  GLU B C     1 
ATOM   1594 O  O     . GLU B 1 10  ? 11.98595  -44.73367 -8.79133  1.000 50.12424  ? 74  GLU B O     1 
ATOM   1595 C  CB    . GLU B 1 10  ? 10.38394  -47.13397 -10.30290 1.000 52.30890  ? 74  GLU B CB    1 
ATOM   1596 C  CG    . GLU B 1 10  ? 8.87434   -47.12199 -10.50694 1.000 48.11259  ? 74  GLU B CG    1 
ATOM   1597 C  CD    . GLU B 1 10  ? 8.23503   -48.49932 -10.36958 1.000 51.71504  ? 74  GLU B CD    1 
ATOM   1598 O  OE1   . GLU B 1 10  ? 8.80937   -49.36560 -9.67314  1.000 56.58040  ? 74  GLU B OE1   1 
ATOM   1599 O  OE2   . GLU B 1 10  ? 7.14369   -48.70838 -10.94401 1.000 53.98520  ? 74  GLU B OE2   1 
ATOM   1600 N  N     . LYS B 1 11  ? 13.36887  -46.09800 -9.91268  1.000 48.13654  ? 75  LYS B N     1 
ATOM   1601 C  CA    . LYS B 1 11  ? 14.49060  -45.87963 -9.01235  1.000 49.83130  ? 75  LYS B CA    1 
ATOM   1602 C  C     . LYS B 1 11  ? 15.29041  -44.65935 -9.45061  1.000 49.56918  ? 75  LYS B C     1 
ATOM   1603 O  O     . LYS B 1 11  ? 15.50826  -44.43997 -10.64467 1.000 48.71362  ? 75  LYS B O     1 
ATOM   1604 C  CB    . LYS B 1 11  ? 15.39330  -47.11481 -8.97356  1.000 51.42072  ? 75  LYS B CB    1 
ATOM   1605 N  N     . PHE B 1 12  ? 15.70625  -43.84715 -8.48035  1.000 52.87792  ? 76  PHE B N     1 
ATOM   1606 C  CA    . PHE B 1 12  ? 16.61340  -42.74589 -8.76634  1.000 50.67246  ? 76  PHE B CA    1 
ATOM   1607 C  C     . PHE B 1 12  ? 17.66162  -42.66804 -7.66385  1.000 53.26533  ? 76  PHE B C     1 
ATOM   1608 O  O     . PHE B 1 12  ? 17.60514  -43.38576 -6.66257  1.000 53.82707  ? 76  PHE B O     1 
ATOM   1609 C  CB    . PHE B 1 12  ? 15.90423  -41.38055 -8.92761  1.000 49.63303  ? 76  PHE B CB    1 
ATOM   1610 C  CG    . PHE B 1 12  ? 14.60339  -41.42191 -9.71187  1.000 47.87065  ? 76  PHE B CG    1 
ATOM   1611 C  CD1   . PHE B 1 12  ? 13.46452  -42.03998 -9.21270  1.000 48.27540  ? 76  PHE B CD1   1 
ATOM   1612 C  CD2   . PHE B 1 12  ? 14.55466  -40.89999 -10.99827 1.000 46.76278  ? 76  PHE B CD2   1 
ATOM   1613 C  CE1   . PHE B 1 12  ? 12.28957  -42.07206 -9.95409  1.000 45.88770  ? 76  PHE B CE1   1 
ATOM   1614 C  CE2   . PHE B 1 12  ? 13.38892  -40.94176 -11.74371 1.000 46.09816  ? 76  PHE B CE2   1 
ATOM   1615 C  CZ    . PHE B 1 12  ? 12.25742  -41.53000 -11.22213 1.000 47.83002  ? 76  PHE B CZ    1 
ATOM   1616 N  N     . ALA B 1 13  ? 18.64191  -41.79389 -7.86853  1.000 83.40093  ? 77  ALA B N     1 
ATOM   1617 C  CA    . ALA B 1 13  ? 19.73713  -41.62117 -6.92978  1.000 85.50325  ? 77  ALA B CA    1 
ATOM   1618 C  C     . ALA B 1 13  ? 19.90068  -40.14621 -6.60461  1.000 88.91569  ? 77  ALA B C     1 
ATOM   1619 O  O     . ALA B 1 13  ? 19.60077  -39.27303 -7.42425  1.000 88.03211  ? 77  ALA B O     1 
ATOM   1620 C  CB    . ALA B 1 13  ? 21.05166  -42.17987 -7.48605  1.000 89.50475  ? 77  ALA B CB    1 
ATOM   1621 N  N     . PHE B 1 14  ? 20.37269  -39.88191 -5.39157  1.000 70.83526  ? 78  PHE B N     1 
ATOM   1622 C  CA    . PHE B 1 14  ? 20.65897  -38.51822 -4.97433  1.000 71.90307  ? 78  PHE B CA    1 
ATOM   1623 C  C     . PHE B 1 14  ? 21.88338  -37.97941 -5.70218  1.000 75.95702  ? 78  PHE B C     1 
ATOM   1624 O  O     . PHE B 1 14  ? 22.82927  -38.71789 -5.99442  1.000 71.45093  ? 78  PHE B O     1 
ATOM   1625 C  CB    . PHE B 1 14  ? 20.87419  -38.47693 -3.46543  1.000 70.84194  ? 78  PHE B CB    1 
ATOM   1626 C  CG    . PHE B 1 14  ? 19.71915  -39.02017 -2.68278  1.000 69.45593  ? 78  PHE B CG    1 
ATOM   1627 C  CD1   . PHE B 1 14  ? 18.49391  -38.37291 -2.69322  1.000 68.28324  ? 78  PHE B CD1   1 
ATOM   1628 C  CD2   . PHE B 1 14  ? 19.83767  -40.20870 -1.98256  1.000 70.15920  ? 78  PHE B CD2   1 
ATOM   1629 C  CE1   . PHE B 1 14  ? 17.41986  -38.87435 -1.97300  1.000 62.89591  ? 78  PHE B CE1   1 
ATOM   1630 C  CE2   . PHE B 1 14  ? 18.76421  -40.72231 -1.26849  1.000 67.56649  ? 78  PHE B CE2   1 
ATOM   1631 C  CZ    . PHE B 1 14  ? 17.55321  -40.05507 -1.26574  1.000 61.45038  ? 78  PHE B CZ    1 
ATOM   1632 N  N     . GLN B 1 15  ? 21.85494  -36.68348 -6.00474  1.000 85.90848  ? 79  GLN B N     1 
ATOM   1633 C  CA    . GLN B 1 15  ? 23.00195  -36.03244 -6.61502  1.000 87.36510  ? 79  GLN B CA    1 
ATOM   1634 C  C     . GLN B 1 15  ? 24.17842  -36.02201 -5.64290  1.000 93.17172  ? 79  GLN B C     1 
ATOM   1635 O  O     . GLN B 1 15  ? 24.02249  -36.21260 -4.43350  1.000 92.08875  ? 79  GLN B O     1 
ATOM   1636 C  CB    . GLN B 1 15  ? 22.64966  -34.60597 -7.03867  1.000 85.16586  ? 79  GLN B CB    1 
ATOM   1637 N  N     . ALA B 1 16  ? 25.37486  -35.80486 -6.19349  1.000 90.43062  ? 80  ALA B N     1 
ATOM   1638 C  CA    . ALA B 1 16  ? 26.58217  -35.83674 -5.37316  1.000 89.96907  ? 80  ALA B CA    1 
ATOM   1639 C  C     . ALA B 1 16  ? 26.53892  -34.77483 -4.28208  1.000 92.55245  ? 80  ALA B C     1 
ATOM   1640 O  O     . ALA B 1 16  ? 26.87446  -35.04904 -3.12313  1.000 89.10256  ? 80  ALA B O     1 
ATOM   1641 C  CB    . ALA B 1 16  ? 27.81894  -35.65233 -6.25301  1.000 95.92962  ? 80  ALA B CB    1 
ATOM   1642 N  N     . GLU B 1 17  ? 26.11556  -33.55811 -4.63152  0.902 118.49996 ? 81  GLU B N     1 
ATOM   1643 C  CA    . GLU B 1 17  ? 26.04283  -32.48767 -3.64396  0.902 118.30460 ? 81  GLU B CA    1 
ATOM   1644 C  C     . GLU B 1 17  ? 25.01505  -32.78670 -2.55961  0.902 116.16794 ? 81  GLU B C     1 
ATOM   1645 O  O     . GLU B 1 17  ? 25.20034  -32.38299 -1.40645  0.902 116.21755 ? 81  GLU B O     1 
ATOM   1646 C  CB    . GLU B 1 17  ? 25.71953  -31.16180 -4.33336  0.902 118.41263 ? 81  GLU B CB    1 
ATOM   1647 N  N     . VAL B 1 18  ? 23.93537  -33.49166 -2.90134  1.000 98.97751  ? 82  VAL B N     1 
ATOM   1648 C  CA    . VAL B 1 18  ? 22.88905  -33.76532 -1.91977  1.000 94.88589  ? 82  VAL B CA    1 
ATOM   1649 C  C     . VAL B 1 18  ? 23.38543  -34.74603 -0.86423  1.000 91.70088  ? 82  VAL B C     1 
ATOM   1650 O  O     . VAL B 1 18  ? 23.29509  -34.48462 0.34081   1.000 88.77565  ? 82  VAL B O     1 
ATOM   1651 C  CB    . VAL B 1 18  ? 21.61999  -34.28860 -2.61743  1.000 88.98836  ? 82  VAL B CB    1 
ATOM   1652 N  N     . ASN B 1 19  ? 23.93487  -35.88130 -1.29976  1.000 71.18070  ? 83  ASN B N     1 
ATOM   1653 C  CA    . ASN B 1 19  ? 24.29131  -36.93687 -0.35973  1.000 69.69560  ? 83  ASN B CA    1 
ATOM   1654 C  C     . ASN B 1 19  ? 25.40168  -36.51288 0.59248   1.000 76.08017  ? 83  ASN B C     1 
ATOM   1655 O  O     . ASN B 1 19  ? 25.54130  -37.10669 1.66742   1.000 68.86776  ? 83  ASN B O     1 
ATOM   1656 C  CB    . ASN B 1 19  ? 24.69747  -38.19815 -1.12152  1.000 67.62451  ? 83  ASN B CB    1 
ATOM   1657 C  CG    . ASN B 1 19  ? 24.12687  -39.45811 -0.50424  1.000 68.85899  ? 83  ASN B CG    1 
ATOM   1658 O  OD1   . ASN B 1 19  ? 23.98354  -39.55605 0.71616   1.000 69.88508  ? 83  ASN B OD1   1 
ATOM   1659 N  ND2   . ASN B 1 19  ? 23.80008  -40.43426 -1.34507  1.000 67.42616  ? 83  ASN B ND2   1 
ATOM   1660 N  N     . ARG B 1 20  ? 26.19715  -35.50602 0.22245   1.000 73.33105  ? 84  ARG B N     1 
ATOM   1661 C  CA    . ARG B 1 20  ? 27.17203  -34.95594 1.15942   1.000 70.33820  ? 84  ARG B CA    1 
ATOM   1662 C  C     . ARG B 1 20  ? 26.48233  -34.17804 2.27375   1.000 65.21771  ? 84  ARG B C     1 
ATOM   1663 O  O     . ARG B 1 20  ? 26.87179  -34.27901 3.44256   1.000 65.97464  ? 84  ARG B O     1 
ATOM   1664 C  CB    . ARG B 1 20  ? 28.16795  -34.06417 0.41877   1.000 71.03796  ? 84  ARG B CB    1 
ATOM   1665 N  N     . MET B 1 21  ? 25.45541  -33.39588 1.92774   1.000 76.41620  ? 85  MET B N     1 
ATOM   1666 C  CA    . MET B 1 21  ? 24.68426  -32.67972 2.93879   1.000 73.26426  ? 85  MET B CA    1 
ATOM   1667 C  C     . MET B 1 21  ? 24.06554  -33.63358 3.94869   1.000 69.37889  ? 85  MET B C     1 
ATOM   1668 O  O     . MET B 1 21  ? 23.94615  -33.30010 5.13378   1.000 67.29453  ? 85  MET B O     1 
ATOM   1669 C  CB    . MET B 1 21  ? 23.58900  -31.84781 2.27168   1.000 69.35225  ? 85  MET B CB    1 
ATOM   1670 C  CG    . MET B 1 21  ? 22.51307  -31.37746 3.23558   1.000 68.30596  ? 85  MET B CG    1 
ATOM   1671 S  SD    . MET B 1 21  ? 20.84065  -31.67905 2.64376   1.000 67.56577  ? 85  MET B SD    1 
ATOM   1672 C  CE    . MET B 1 21  ? 20.79076  -33.46996 2.63280   1.000 59.71772  ? 85  MET B CE    1 
ATOM   1673 N  N     . MET B 1 22  ? 23.67386  -34.82296 3.50009   1.000 86.73158  ? 86  MET B N     1 
ATOM   1674 C  CA    . MET B 1 22  ? 23.02242  -35.77261 4.39005   1.000 87.41569  ? 86  MET B CA    1 
ATOM   1675 C  C     . MET B 1 22  ? 23.94490  -36.14873 5.54148   1.000 83.56786  ? 86  MET B C     1 
ATOM   1676 O  O     . MET B 1 22  ? 23.53351  -36.15540 6.70733   1.000 87.78907  ? 86  MET B O     1 
ATOM   1677 C  CB    . MET B 1 22  ? 22.60785  -37.00588 3.58972   1.000 93.22951  ? 86  MET B CB    1 
ATOM   1678 C  CG    . MET B 1 22  ? 21.16137  -37.42979 3.76703   1.000 80.06542  ? 86  MET B CG    1 
ATOM   1679 S  SD    . MET B 1 22  ? 20.61181  -38.30304 2.28362   1.000 92.44226  ? 86  MET B SD    1 
ATOM   1680 C  CE    . MET B 1 22  ? 20.25256  -36.93051 1.18655   1.000 74.95120  ? 86  MET B CE    1 
ATOM   1681 N  N     . LYS B 1 23  ? 25.21202  -36.43577 5.23157   1.000 68.97845  ? 87  LYS B N     1 
ATOM   1682 C  CA    . LYS B 1 23  ? 26.18060  -36.75688 6.27677   1.000 75.22311  ? 87  LYS B CA    1 
ATOM   1683 C  C     . LYS B 1 23  ? 26.42213  -35.56391 7.19431   1.000 73.87583  ? 87  LYS B C     1 
ATOM   1684 O  O     . LYS B 1 23  ? 26.59255  -35.73018 8.40833   1.000 76.87991  ? 87  LYS B O     1 
ATOM   1685 C  CB    . LYS B 1 23  ? 27.49353  -37.22665 5.65071   1.000 80.06405  ? 87  LYS B CB    1 
ATOM   1686 N  N     . LEU B 1 24  ? 26.45036  -34.35212 6.63123   1.000 64.00366  ? 88  LEU B N     1 
ATOM   1687 C  CA    . LEU B 1 24  ? 26.59356  -33.15828 7.45803   1.000 62.61327  ? 88  LEU B CA    1 
ATOM   1688 C  C     . LEU B 1 24  ? 25.43638  -33.03558 8.44050   1.000 60.63658  ? 88  LEU B C     1 
ATOM   1689 O  O     . LEU B 1 24  ? 25.63996  -32.68992 9.60807   1.000 60.33224  ? 88  LEU B O     1 
ATOM   1690 C  CB    . LEU B 1 24  ? 26.68742  -31.91430 6.57425   1.000 66.08777  ? 88  LEU B CB    1 
ATOM   1691 N  N     . ILE B 1 25  ? 24.21584  -33.33394 7.98837   1.000 66.70643  ? 89  ILE B N     1 
ATOM   1692 C  CA    . ILE B 1 25  ? 23.05998  -33.33820 8.88300   1.000 59.76393  ? 89  ILE B CA    1 
ATOM   1693 C  C     . ILE B 1 25  ? 23.27218  -34.32004 10.02885  1.000 59.74462  ? 89  ILE B C     1 
ATOM   1694 O  O     . ILE B 1 25  ? 23.07376  -33.98513 11.20264  1.000 60.53044  ? 89  ILE B O     1 
ATOM   1695 C  CB    . ILE B 1 25  ? 21.78005  -33.67238 8.09694   1.000 56.23428  ? 89  ILE B CB    1 
ATOM   1696 C  CG1   . ILE B 1 25  ? 21.45458  -32.55736 7.09821   1.000 55.50344  ? 89  ILE B CG1   1 
ATOM   1697 C  CG2   . ILE B 1 25  ? 20.62614  -33.96616 9.05325   1.000 57.40586  ? 89  ILE B CG2   1 
ATOM   1698 C  CD1   . ILE B 1 25  ? 19.98387  -32.43426 6.76725   1.000 52.88654  ? 89  ILE B CD1   1 
ATOM   1699 N  N     . ILE B 1 26  ? 23.68020  -35.54907 9.70301   1.000 67.49174  ? 90  ILE B N     1 
ATOM   1700 C  CA    . ILE B 1 26  ? 23.83668  -36.58198 10.72479  1.000 68.28232  ? 90  ILE B CA    1 
ATOM   1701 C  C     . ILE B 1 26  ? 24.93113  -36.19564 11.70770  1.000 69.96456  ? 90  ILE B C     1 
ATOM   1702 O  O     . ILE B 1 26  ? 24.73460  -36.22753 12.92776  1.000 73.42908  ? 90  ILE B O     1 
ATOM   1703 C  CB    . ILE B 1 26  ? 24.12680  -37.94630 10.07348  1.000 73.28588  ? 90  ILE B CB    1 
ATOM   1704 N  N     . ASN B 1 27  ? 26.10042  -35.81653 11.19048  1.000 123.12449 ? 91  ASN B N     1 
ATOM   1705 C  CA    . ASN B 1 27  ? 27.21920  -35.48857 12.06684  1.000 128.37048 ? 91  ASN B CA    1 
ATOM   1706 C  C     . ASN B 1 27  ? 26.90111  -34.28216 12.94070  1.000 122.56489 ? 91  ASN B C     1 
ATOM   1707 O  O     . ASN B 1 27  ? 27.26705  -34.24705 14.12076  1.000 123.01278 ? 91  ASN B O     1 
ATOM   1708 C  CB    . ASN B 1 27  ? 28.47847  -35.23679 11.23772  1.000 132.10361 ? 91  ASN B CB    1 
ATOM   1709 N  N     . SER B 1 28  ? 26.21352  -33.28751 12.38273  1.000 74.40316  ? 92  SER B N     1 
ATOM   1710 C  CA    . SER B 1 28  ? 25.95313  -32.04517 13.09628  1.000 72.49162  ? 92  SER B CA    1 
ATOM   1711 C  C     . SER B 1 28  ? 24.79271  -32.13183 14.07781  1.000 73.26408  ? 92  SER B C     1 
ATOM   1712 O  O     . SER B 1 28  ? 24.60136  -31.19864 14.86532  1.000 74.99040  ? 92  SER B O     1 
ATOM   1713 C  CB    . SER B 1 28  ? 25.67055  -30.92149 12.10033  1.000 72.87396  ? 92  SER B CB    1 
ATOM   1714 O  OG    . SER B 1 28  ? 24.31985  -30.97267 11.67444  1.000 78.64127  ? 92  SER B OG    1 
ATOM   1715 N  N     . LEU B 1 29  ? 24.00741  -33.20516 14.06184  1.000 54.59379  ? 93  LEU B N     1 
ATOM   1716 C  CA    . LEU B 1 29  ? 22.75676  -33.17948 14.80733  1.000 52.21675  ? 93  LEU B CA    1 
ATOM   1717 C  C     . LEU B 1 29  ? 22.54260  -34.43139 15.64992  1.000 49.91738  ? 93  LEU B C     1 
ATOM   1718 O  O     . LEU B 1 29  ? 21.40283  -34.71671 16.03486  1.000 48.77393  ? 93  LEU B O     1 
ATOM   1719 C  CB    . LEU B 1 29  ? 21.58458  -32.98424 13.84757  1.000 49.79616  ? 93  LEU B CB    1 
ATOM   1720 C  CG    . LEU B 1 29  ? 21.46909  -31.54727 13.33961  1.000 46.26767  ? 93  LEU B CG    1 
ATOM   1721 C  CD1   . LEU B 1 29  ? 20.44303  -31.46974 12.21699  1.000 44.91422  ? 93  LEU B CD1   1 
ATOM   1722 C  CD2   . LEU B 1 29  ? 21.16546  -30.56447 14.46718  1.000 47.32240  ? 93  LEU B CD2   1 
ATOM   1723 N  N     . TYR B 1 30  ? 23.60532  -35.18731 15.94725  1.000 52.58875  ? 94  TYR B N     1 
ATOM   1724 C  CA    . TYR B 1 30  ? 23.43246  -36.40903 16.72593  1.000 50.11215  ? 94  TYR B CA    1 
ATOM   1725 C  C     . TYR B 1 30  ? 23.08265  -36.11435 18.17604  1.000 49.17171  ? 94  TYR B C     1 
ATOM   1726 O  O     . TYR B 1 30  ? 22.48501  -36.96629 18.84389  1.000 51.01486  ? 94  TYR B O     1 
ATOM   1727 C  CB    . TYR B 1 30  ? 24.69054  -37.28411 16.64703  1.000 58.31922  ? 94  TYR B CB    1 
ATOM   1728 C  CG    . TYR B 1 30  ? 25.92164  -36.71951 17.33354  1.000 60.24894  ? 94  TYR B CG    1 
ATOM   1729 C  CD1   . TYR B 1 30  ? 26.10981  -36.85609 18.70620  1.000 64.24632  ? 94  TYR B CD1   1 
ATOM   1730 C  CD2   . TYR B 1 30  ? 26.89990  -36.05585 16.60567  1.000 62.26740  ? 94  TYR B CD2   1 
ATOM   1731 C  CE1   . TYR B 1 30  ? 27.23299  -36.34068 19.32908  1.000 62.10378  ? 94  TYR B CE1   1 
ATOM   1732 C  CE2   . TYR B 1 30  ? 28.02763  -35.53777 17.21974  1.000 67.05338  ? 94  TYR B CE2   1 
ATOM   1733 C  CZ    . TYR B 1 30  ? 28.19136  -35.68292 18.58116  1.000 65.42769  ? 94  TYR B CZ    1 
ATOM   1734 O  OH    . TYR B 1 30  ? 29.31761  -35.16822 19.19664  1.000 68.09950  ? 94  TYR B OH    1 
ATOM   1735 N  N     . LYS B 1 31  ? 23.44067  -34.93106 18.67714  1.000 56.31972  ? 95  LYS B N     1 
ATOM   1736 C  CA    . LYS B 1 31  ? 23.11968  -34.60091 20.05901  1.000 57.12463  ? 95  LYS B CA    1 
ATOM   1737 C  C     . LYS B 1 31  ? 21.64293  -34.27511 20.22830  1.000 50.96444  ? 95  LYS B C     1 
ATOM   1738 O  O     . LYS B 1 31  ? 21.07981  -34.49551 21.30490  1.000 56.25970  ? 95  LYS B O     1 
ATOM   1739 C  CB    . LYS B 1 31  ? 23.98103  -33.43384 20.53546  1.000 60.29556  ? 95  LYS B CB    1 
ATOM   1740 N  N     . ASN B 1 32  ? 20.99287  -33.77116 19.18452  1.000 79.20936  ? 96  ASN B N     1 
ATOM   1741 C  CA    . ASN B 1 32  ? 19.60054  -33.33780 19.27493  1.000 76.68945  ? 96  ASN B CA    1 
ATOM   1742 C  C     . ASN B 1 32  ? 18.83614  -34.02508 18.14695  1.000 73.48850  ? 96  ASN B C     1 
ATOM   1743 O  O     . ASN B 1 32  ? 18.63306  -33.44362 17.07873  1.000 73.16994  ? 96  ASN B O     1 
ATOM   1744 C  CB    . ASN B 1 32  ? 19.50724  -31.82180 19.18479  1.000 78.66003  ? 96  ASN B CB    1 
ATOM   1745 C  CG    . ASN B 1 32  ? 18.58516  -31.23723 20.22234  1.000 75.55505  ? 96  ASN B CG    1 
ATOM   1746 O  OD1   . ASN B 1 32  ? 18.41938  -31.80259 21.30444  1.000 77.62874  ? 96  ASN B OD1   1 
ATOM   1747 N  ND2   . ASN B 1 32  ? 17.96121  -30.11013 19.89580  1.000 75.77923  ? 96  ASN B ND2   1 
ATOM   1748 N  N     . LYS B 1 33  ? 18.39946  -35.26216 18.39834  1.000 39.49150  ? 97  LYS B N     1 
ATOM   1749 C  CA    . LYS B 1 33  ? 17.73957  -36.07274 17.38269  1.000 38.10205  ? 97  LYS B CA    1 
ATOM   1750 C  C     . LYS B 1 33  ? 16.23929  -35.83700 17.30363  1.000 35.93050  ? 97  LYS B C     1 
ATOM   1751 O  O     . LYS B 1 33  ? 15.64038  -36.09464 16.25253  1.000 34.75054  ? 97  LYS B O     1 
ATOM   1752 C  CB    . LYS B 1 33  ? 17.98643  -37.56264 17.64495  1.000 38.41516  ? 97  LYS B CB    1 
ATOM   1753 C  CG    . LYS B 1 33  ? 19.33753  -38.08015 17.18326  1.000 40.21854  ? 97  LYS B CG    1 
ATOM   1754 C  CD    . LYS B 1 33  ? 19.56283  -39.48346 17.72940  1.000 40.62816  ? 97  LYS B CD    1 
ATOM   1755 C  CE    . LYS B 1 33  ? 20.90864  -40.05457 17.30311  1.000 42.47103  ? 97  LYS B CE    1 
ATOM   1756 N  NZ    . LYS B 1 33  ? 21.53948  -40.88612 18.39121  1.000 43.77096  ? 97  LYS B NZ    1 
ATOM   1757 N  N     A GLU B 1 34  ? 15.61134  -35.35357 18.36947  0.647 37.97113  ? 98  GLU B N     1 
ATOM   1758 N  N     B GLU B 1 34  ? 15.62768  -35.35329 18.38780  0.353 38.02908  ? 98  GLU B N     1 
ATOM   1759 C  CA    A GLU B 1 34  ? 14.16208  -35.20290 18.35307  0.647 37.52331  ? 98  GLU B CA    1 
ATOM   1760 C  CA    B GLU B 1 34  ? 14.18650  -35.14373 18.44991  0.353 37.63271  ? 98  GLU B CA    1 
ATOM   1761 C  C     A GLU B 1 34  ? 13.70830  -33.95958 17.60075  0.647 35.54951  ? 98  GLU B C     1 
ATOM   1762 C  C     B GLU B 1 34  ? 13.71978  -33.97531 17.59471  0.353 35.53694  ? 98  GLU B C     1 
ATOM   1763 O  O     A GLU B 1 34  ? 12.49812  -33.74024 17.47107  0.647 33.34856  ? 98  GLU B O     1 
ATOM   1764 O  O     B GLU B 1 34  ? 12.50965  -33.82591 17.39101  0.353 33.29180  ? 98  GLU B O     1 
ATOM   1765 C  CB    A GLU B 1 34  ? 13.61105  -35.19392 19.78551  0.647 39.15288  ? 98  GLU B CB    1 
ATOM   1766 C  CB    B GLU B 1 34  ? 13.75404  -34.92322 19.90310  0.353 39.15709  ? 98  GLU B CB    1 
ATOM   1767 C  CG    A GLU B 1 34  ? 13.93833  -33.95846 20.59826  0.647 39.19881  ? 98  GLU B CG    1 
ATOM   1768 C  CG    B GLU B 1 34  ? 14.28893  -33.63853 20.52188  0.353 39.65120  ? 98  GLU B CG    1 
ATOM   1769 C  CD    A GLU B 1 34  ? 15.36656  -33.95037 21.09718  0.647 42.13050  ? 98  GLU B CD    1 
ATOM   1770 C  CD    B GLU B 1 34  ? 14.06254  -33.56981 22.02067  0.353 41.96067  ? 98  GLU B CD    1 
ATOM   1771 O  OE1   A GLU B 1 34  ? 15.93416  -35.04206 21.31413  0.647 46.91931  ? 98  GLU B OE1   1 
ATOM   1772 O  OE1   B GLU B 1 34  ? 13.59461  -34.57095 22.59926  0.353 39.96227  ? 98  GLU B OE1   1 
ATOM   1773 O  OE2   A GLU B 1 34  ? 15.91634  -32.84771 21.28290  0.647 42.68386  ? 98  GLU B OE2   1 
ATOM   1774 O  OE2   B GLU B 1 34  ? 14.34950  -32.51201 22.62047  0.353 43.93920  ? 98  GLU B OE2   1 
ATOM   1775 N  N     . ILE B 1 35  ? 14.64172  -33.15299 17.08663  1.000 32.58075  ? 99  ILE B N     1 
ATOM   1776 C  CA    . ILE B 1 35  ? 14.26572  -32.01176 16.26352  1.000 30.19155  ? 99  ILE B CA    1 
ATOM   1777 C  C     . ILE B 1 35  ? 13.56013  -32.45194 14.98969  1.000 30.19451  ? 99  ILE B C     1 
ATOM   1778 O  O     . ILE B 1 35  ? 12.89840  -31.63346 14.33931  1.000 24.93896  ? 99  ILE B O     1 
ATOM   1779 C  CB    . ILE B 1 35  ? 15.50448  -31.14962 15.93267  1.000 32.34617  ? 99  ILE B CB    1 
ATOM   1780 N  N     . PHE B 1 36  ? 13.67936  -33.73407 14.61831  1.000 22.96379  ? 100 PHE B N     1 
ATOM   1781 C  CA    . PHE B 1 36  ? 13.03869  -34.22297 13.40133  1.000 16.23340  ? 100 PHE B CA    1 
ATOM   1782 C  C     . PHE B 1 36  ? 11.54585  -33.92091 13.40800  1.000 21.60754  ? 100 PHE B C     1 
ATOM   1783 O  O     . PHE B 1 36  ? 10.98913  -33.50730 12.38373  1.000 17.22086  ? 100 PHE B O     1 
ATOM   1784 C  CB    . PHE B 1 36  ? 13.29547  -35.72619 13.22861  1.000 18.47895  ? 100 PHE B CB    1 
ATOM   1785 C  CG    . PHE B 1 36  ? 12.32318  -36.60753 13.97684  1.000 20.75040  ? 100 PHE B CG    1 
ATOM   1786 C  CD1   . PHE B 1 36  ? 12.54102  -36.92807 15.29882  1.000 19.32233  ? 100 PHE B CD1   1 
ATOM   1787 C  CD2   . PHE B 1 36  ? 11.18143  -37.10176 13.35513  1.000 19.76999  ? 100 PHE B CD2   1 
ATOM   1788 C  CE1   . PHE B 1 36  ? 11.64645  -37.72010 15.99163  1.000 21.14307  ? 100 PHE B CE1   1 
ATOM   1789 C  CE2   . PHE B 1 36  ? 10.28444  -37.89689 14.04716  1.000 18.40752  ? 100 PHE B CE2   1 
ATOM   1790 C  CZ    . PHE B 1 36  ? 10.52075  -38.20881 15.36553  1.000 20.34133  ? 100 PHE B CZ    1 
ATOM   1791 N  N     . LEU B 1 37  ? 10.87636  -34.11353 14.55205  1.000 22.71548  ? 101 LEU B N     1 
ATOM   1792 C  CA    . LEU B 1 37  ? 9.44066   -33.84826 14.60257  1.000 19.90792  ? 101 LEU B CA    1 
ATOM   1793 C  C     . LEU B 1 37  ? 9.15254   -32.37521 14.35830  1.000 25.04337  ? 101 LEU B C     1 
ATOM   1794 O  O     . LEU B 1 37  ? 8.15912   -32.03149 13.70043  1.000 22.05298  ? 101 LEU B O     1 
ATOM   1795 C  CB    . LEU B 1 37  ? 8.85314   -34.29762 15.94288  1.000 22.11607  ? 101 LEU B CB    1 
ATOM   1796 C  CG    . LEU B 1 37  ? 7.32101   -34.42388 15.99365  1.000 20.20172  ? 101 LEU B CG    1 
ATOM   1797 C  CD1   . LEU B 1 37  ? 6.75839   -35.12962 14.76216  1.000 22.68382  ? 101 LEU B CD1   1 
ATOM   1798 C  CD2   . LEU B 1 37  ? 6.88306   -35.14693 17.26170  1.000 23.02824  ? 101 LEU B CD2   1 
ATOM   1799 N  N     . ARG B 1 38  ? 10.01170  -31.48886 14.87538  1.000 27.84192  ? 102 ARG B N     1 
ATOM   1800 C  CA    . ARG B 1 38  ? 9.86944   -30.06124 14.58587  1.000 30.59198  ? 102 ARG B CA    1 
ATOM   1801 C  C     . ARG B 1 38  ? 9.86595   -29.80816 13.08927  1.000 29.01349  ? 102 ARG B C     1 
ATOM   1802 O  O     . ARG B 1 38  ? 8.95907   -29.15335 12.56131  1.000 29.00896  ? 102 ARG B O     1 
ATOM   1803 C  CB    . ARG B 1 38  ? 10.99575  -29.25984 15.24675  1.000 35.79223  ? 102 ARG B CB    1 
ATOM   1804 C  CG    . ARG B 1 38  ? 10.69646  -27.77094 15.39156  1.000 37.95541  ? 102 ARG B CG    1 
ATOM   1805 C  CD    . ARG B 1 38  ? 11.88687  -26.97632 15.92977  1.000 41.96303  ? 102 ARG B CD    1 
ATOM   1806 N  NE    . ARG B 1 38  ? 13.02553  -26.93982 15.01541  1.000 44.35927  ? 102 ARG B NE    1 
ATOM   1807 C  CZ    . ARG B 1 38  ? 14.23891  -27.39816 15.30037  1.000 46.99807  ? 102 ARG B CZ    1 
ATOM   1808 N  NH1   . ARG B 1 38  ? 14.50972  -27.96655 16.46552  1.000 53.51184  ? 102 ARG B NH1   1 
ATOM   1809 N  NH2   . ARG B 1 38  ? 15.20599  -27.28259 14.39410  1.000 47.91525  ? 102 ARG B NH2   1 
ATOM   1810 N  N     . GLU B 1 39  ? 10.86827  -30.34039 12.38267  1.000 18.91357  ? 103 GLU B N     1 
ATOM   1811 C  CA    . GLU B 1 39  ? 11.01536  -30.03448 10.95995  1.000 18.60228  ? 103 GLU B CA    1 
ATOM   1812 C  C     . GLU B 1 39  ? 9.82515   -30.54961 10.15971  1.000 18.17972  ? 103 GLU B C     1 
ATOM   1813 O  O     . GLU B 1 39  ? 9.29536   -29.84212 9.29062   1.000 18.80698  ? 103 GLU B O     1 
ATOM   1814 C  CB    . GLU B 1 39  ? 12.31691  -30.63845 10.43029  1.000 17.83069  ? 103 GLU B CB    1 
ATOM   1815 C  CG    . GLU B 1 39  ? 13.58546  -30.08162 11.08287  1.000 21.58783  ? 103 GLU B CG    1 
ATOM   1816 C  CD    . GLU B 1 39  ? 13.67151  -28.57041 11.01910  1.000 27.08885  ? 103 GLU B CD    1 
ATOM   1817 O  OE1   . GLU B 1 39  ? 13.36390  -28.00365 9.95743   1.000 28.64208  ? 103 GLU B OE1   1 
ATOM   1818 O  OE2   . GLU B 1 39  ? 14.05802  -27.94211 12.02484  1.000 26.85244  ? 103 GLU B OE2   1 
ATOM   1819 N  N     . LEU B 1 40  ? 9.38621   -31.77792 10.44565  1.000 17.97590  ? 104 LEU B N     1 
ATOM   1820 C  CA    . LEU B 1 40  ? 8.24159   -32.34012 9.73469   1.000 17.82110  ? 104 LEU B CA    1 
ATOM   1821 C  C     . LEU B 1 40  ? 6.98606   -31.52084 9.99604   1.000 15.59272  ? 104 LEU B C     1 
ATOM   1822 O  O     . LEU B 1 40  ? 6.21061   -31.24061 9.08001   1.000 17.55148  ? 104 LEU B O     1 
ATOM   1823 C  CB    . LEU B 1 40  ? 8.03562   -33.79306 10.15920  1.000 14.30725  ? 104 LEU B CB    1 
ATOM   1824 C  CG    . LEU B 1 40  ? 9.22259   -34.71934 9.89209   1.000 12.64435  ? 104 LEU B CG    1 
ATOM   1825 C  CD1   . LEU B 1 40  ? 8.89744   -36.15060 10.33242  1.000 12.71837  ? 104 LEU B CD1   1 
ATOM   1826 C  CD2   . LEU B 1 40  ? 9.59564   -34.65570 8.42076   1.000 13.77796  ? 104 LEU B CD2   1 
ATOM   1827 N  N     . ILE B 1 41  ? 6.78017   -31.11727 11.24099  1.000 19.07236  ? 105 ILE B N     1 
ATOM   1828 C  CA    . ILE B 1 41  ? 5.60880   -30.32824 11.59842  1.000 20.30543  ? 105 ILE B CA    1 
ATOM   1829 C  C     . ILE B 1 41  ? 5.66345   -28.96656 10.91759  1.000 19.54312  ? 105 ILE B C     1 
ATOM   1830 O  O     . ILE B 1 41  ? 4.63649   -28.41405 10.49908  1.000 17.54670  ? 105 ILE B O     1 
ATOM   1831 C  CB    . ILE B 1 41  ? 5.53847   -30.20305 13.13147  1.000 27.18461  ? 105 ILE B CB    1 
ATOM   1832 C  CG1   . ILE B 1 41  ? 4.74503   -31.37897 13.72860  1.000 20.33346  ? 105 ILE B CG1   1 
ATOM   1833 C  CG2   . ILE B 1 41  ? 4.95896   -28.85291 13.53651  1.000 27.60888  ? 105 ILE B CG2   1 
ATOM   1834 C  CD1   . ILE B 1 41  ? 4.91280   -31.52054 15.26075  1.000 28.58722  ? 105 ILE B CD1   1 
ATOM   1835 N  N     . SER B 1 42  ? 6.86122   -28.39850 10.79364  1.000 20.47634  ? 106 SER B N     1 
ATOM   1836 C  CA    . SER B 1 42  ? 6.97719   -27.10424 10.13465  1.000 20.60762  ? 106 SER B CA    1 
ATOM   1837 C  C     . SER B 1 42  ? 6.73965   -27.22236 8.62985   1.000 19.29137  ? 106 SER B C     1 
ATOM   1838 O  O     . SER B 1 42  ? 6.06215   -26.37435 8.04008   1.000 15.93274  ? 106 SER B O     1 
ATOM   1839 C  CB    . SER B 1 42  ? 8.33823   -26.47974 10.45726  1.000 22.28792  ? 106 SER B CB    1 
ATOM   1840 O  OG    . SER B 1 42  ? 9.31040   -26.86662 9.50279   1.000 28.26408  ? 106 SER B OG    1 
ATOM   1841 N  N     . ASN B 1 43  ? 7.25658   -28.27825 7.98981   1.000 14.48121  ? 107 ASN B N     1 
ATOM   1842 C  CA    . ASN B 1 43  ? 6.92706   -28.50267 6.58563   1.000 11.95043  ? 107 ASN B CA    1 
ATOM   1843 C  C     . ASN B 1 43  ? 5.42760   -28.68566 6.41561   1.000 12.25889  ? 107 ASN B C     1 
ATOM   1844 O  O     . ASN B 1 43  ? 4.81500   -28.11214 5.50800   1.000 13.93872  ? 107 ASN B O     1 
ATOM   1845 C  CB    . ASN B 1 43  ? 7.65890   -29.73515 6.05575   1.000 10.34751  ? 107 ASN B CB    1 
ATOM   1846 C  CG    . ASN B 1 43  ? 9.15274   -29.56754 6.08826   1.000 16.93966  ? 107 ASN B CG    1 
ATOM   1847 O  OD1   . ASN B 1 43  ? 9.65983   -28.48134 6.37771   1.000 18.98677  ? 107 ASN B OD1   1 
ATOM   1848 N  ND2   . ASN B 1 43  ? 9.87258   -30.63760 5.80612   1.000 17.93007  ? 107 ASN B ND2   1 
ATOM   1849 N  N     . ALA B 1 44  ? 4.82122   -29.49838 7.28106   1.000 17.20664  ? 108 ALA B N     1 
ATOM   1850 C  CA    . ALA B 1 44  ? 3.37796   -29.68986 7.22471   1.000 15.94905  ? 108 ALA B CA    1 
ATOM   1851 C  C     . ALA B 1 44  ? 2.65492   -28.35608 7.31471   1.000 18.99219  ? 108 ALA B C     1 
ATOM   1852 O  O     . ALA B 1 44  ? 1.69774   -28.10582 6.57122   1.000 17.33179  ? 108 ALA B O     1 
ATOM   1853 C  CB    . ALA B 1 44  ? 2.92818   -30.62980 8.34572   1.000 12.68979  ? 108 ALA B CB    1 
ATOM   1854 N  N     . SER B 1 45  ? 3.13163   -27.45937 8.17806   1.000 15.26245  ? 109 SER B N     1 
ATOM   1855 C  CA    . SER B 1 45  ? 2.46065   -26.18162 8.31275   1.000 11.71689  ? 109 SER B CA    1 
ATOM   1856 C  C     . SER B 1 45  ? 2.67944   -25.31850 7.07804   1.000 9.63753   ? 109 SER B C     1 
ATOM   1857 O  O     . SER B 1 45  ? 1.78645   -24.55447 6.69756   1.000 11.16805  ? 109 SER B O     1 
ATOM   1858 C  CB    . SER B 1 45  ? 2.93680   -25.46955 9.57937   1.000 18.83475  ? 109 SER B CB    1 
ATOM   1859 O  OG    . SER B 1 45  ? 2.28238   -24.22962 9.74829   1.000 17.95787  ? 109 SER B OG    1 
ATOM   1860 N  N     . ASP B 1 46  ? 3.84221   -25.43742 6.42205   1.000 15.01648  ? 110 ASP B N     1 
ATOM   1861 C  CA    . ASP B 1 46  ? 4.05964   -24.70857 5.16968   1.000 12.49994  ? 110 ASP B CA    1 
ATOM   1862 C  C     . ASP B 1 46  ? 3.10562   -25.18976 4.09296   1.000 16.68366  ? 110 ASP B C     1 
ATOM   1863 O  O     . ASP B 1 46  ? 2.59162   -24.38678 3.30085   1.000 16.22198  ? 110 ASP B O     1 
ATOM   1864 C  CB    . ASP B 1 46  ? 5.50009   -24.88438 4.67892   1.000 14.65774  ? 110 ASP B CB    1 
ATOM   1865 C  CG    . ASP B 1 46  ? 6.50099   -24.14218 5.53957   1.000 20.42557  ? 110 ASP B CG    1 
ATOM   1866 O  OD1   . ASP B 1 46  ? 6.05916   -23.36892 6.40717   1.000 19.49970  ? 110 ASP B OD1   1 
ATOM   1867 O  OD2   . ASP B 1 46  ? 7.72447   -24.33392 5.35203   1.000 22.80544  ? 110 ASP B OD2   1 
ATOM   1868 N  N     . ALA B 1 47  ? 2.89079   -26.50578 4.02961   1.000 16.25539  ? 111 ALA B N     1 
ATOM   1869 C  CA    . ALA B 1 47  ? 2.00857   -27.08672 3.02605   1.000 12.55406  ? 111 ALA B CA    1 
ATOM   1870 C  C     . ALA B 1 47  ? 0.56472   -26.66354 3.25022   1.000 12.58304  ? 111 ALA B C     1 
ATOM   1871 O  O     . ALA B 1 47  ? -0.19102  -26.49851 2.28998   1.000 15.47638  ? 111 ALA B O     1 
ATOM   1872 C  CB    . ALA B 1 47  ? 2.12202   -28.60587 3.06071   1.000 15.45361  ? 111 ALA B CB    1 
ATOM   1873 N  N     . LEU B 1 48  ? 0.15498   -26.51746 4.51372   1.000 15.26303  ? 112 LEU B N     1 
ATOM   1874 C  CA    . LEU B 1 48  ? -1.19140  -26.03013 4.81132   1.000 18.67894  ? 112 LEU B CA    1 
ATOM   1875 C  C     . LEU B 1 48  ? -1.34831  -24.55053 4.47370   1.000 16.85342  ? 112 LEU B C     1 
ATOM   1876 O  O     . LEU B 1 48  ? -2.39687  -24.13398 3.96242   1.000 18.09897  ? 112 LEU B O     1 
ATOM   1877 C  CB    . LEU B 1 48  ? -1.52432  -26.29091 6.27965   1.000 13.89872  ? 112 LEU B CB    1 
ATOM   1878 C  CG    . LEU B 1 48  ? -1.56087  -27.79671 6.50879   1.000 15.86868  ? 112 LEU B CG    1 
ATOM   1879 C  CD1   . LEU B 1 48  ? -1.14107  -28.16232 7.93801   1.000 13.86934  ? 112 LEU B CD1   1 
ATOM   1880 C  CD2   . LEU B 1 48  ? -2.94342  -28.35833 6.17775   1.000 16.08537  ? 112 LEU B CD2   1 
ATOM   1881 N  N     . ASP B 1 49  ? -0.34381  -23.72837 4.78070   1.000 14.84917  ? 113 ASP B N     1 
ATOM   1882 C  CA    . ASP B 1 49  ? -0.36126  -22.36289 4.26244   1.000 12.93228  ? 113 ASP B CA    1 
ATOM   1883 C  C     . ASP B 1 49  ? -0.57425  -22.33322 2.75099   1.000 17.66570  ? 113 ASP B C     1 
ATOM   1884 O  O     . ASP B 1 49  ? -1.39855  -21.56066 2.24954   1.000 19.81214  ? 113 ASP B O     1 
ATOM   1885 C  CB    . ASP B 1 49  ? 0.92234   -21.61822 4.65727   1.000 17.34706  ? 113 ASP B CB    1 
ATOM   1886 C  CG    . ASP B 1 49  ? 0.93988   -21.17680 6.12867   1.000 20.63034  ? 113 ASP B CG    1 
ATOM   1887 O  OD1   . ASP B 1 49  ? -0.12924  -21.13891 6.77468   1.000 19.95457  ? 113 ASP B OD1   1 
ATOM   1888 O  OD2   . ASP B 1 49  ? 2.01605   -20.83764 6.65630   1.000 17.39672  ? 113 ASP B OD2   1 
ATOM   1889 N  N     . LYS B 1 50  ? 0.14886   -23.16916 1.99917   1.000 19.46579  ? 114 LYS B N     1 
ATOM   1890 C  CA    . LYS B 1 50  ? 0.09837   -23.03813 0.54347   1.000 14.73373  ? 114 LYS B CA    1 
ATOM   1891 C  C     . LYS B 1 50  ? -1.28778  -23.35299 -0.00140  1.000 18.59380  ? 114 LYS B C     1 
ATOM   1892 O  O     . LYS B 1 50  ? -1.85704  -22.55419 -0.75347  1.000 21.38558  ? 114 LYS B O     1 
ATOM   1893 C  CB    . LYS B 1 50  ? 1.14622   -23.92102 -0.11852  1.000 20.66741  ? 114 LYS B CB    1 
ATOM   1894 C  CG    . LYS B 1 50  ? 2.55830   -23.56891 0.28435   1.000 27.61666  ? 114 LYS B CG    1 
ATOM   1895 N  N     . ILE B 1 51  ? -1.86972  -24.48286 0.40136   1.000 19.35015  ? 115 ILE B N     1 
ATOM   1896 C  CA    . ILE B 1 51  ? -3.19349  -24.82541 -0.11162  1.000 20.94381  ? 115 ILE B CA    1 
ATOM   1897 C  C     . ILE B 1 51  ? -4.22957  -23.82030 0.36461   1.000 20.44620  ? 115 ILE B C     1 
ATOM   1898 O  O     . ILE B 1 51  ? -5.20707  -23.54074 -0.33815  1.000 21.37429  ? 115 ILE B O     1 
ATOM   1899 C  CB    . ILE B 1 51  ? -3.57475  -26.26515 0.27137   1.000 20.79648  ? 115 ILE B CB    1 
ATOM   1900 C  CG1   . ILE B 1 51  ? -4.84743  -26.68767 -0.47013  1.000 17.65358  ? 115 ILE B CG1   1 
ATOM   1901 C  CG2   . ILE B 1 51  ? -3.74321  -26.41463 1.78753   1.000 17.88626  ? 115 ILE B CG2   1 
ATOM   1902 C  CD1   . ILE B 1 51  ? -4.70360  -26.73141 -1.97460  1.000 18.27545  ? 115 ILE B CD1   1 
ATOM   1903 N  N     . ARG B 1 52  ? -4.03750  -23.24604 1.54823   1.000 17.31157  ? 116 ARG B N     1 
ATOM   1904 C  CA    . ARG B 1 52  ? -4.99540  -22.25976 2.02725   1.000 15.64871  ? 116 ARG B CA    1 
ATOM   1905 C  C     . ARG B 1 52  ? -4.86922  -20.95375 1.26348   1.000 16.17443  ? 116 ARG B C     1 
ATOM   1906 O  O     . ARG B 1 52  ? -5.87445  -20.27061 1.03411   1.000 19.52777  ? 116 ARG B O     1 
ATOM   1907 C  CB    . ARG B 1 52  ? -4.82485  -22.08970 3.53947   1.000 16.79072  ? 116 ARG B CB    1 
ATOM   1908 C  CG    . ARG B 1 52  ? -5.60416  -20.98286 4.18169   1.000 22.46144  ? 116 ARG B CG    1 
ATOM   1909 C  CD    . ARG B 1 52  ? -4.79761  -20.36698 5.32409   1.000 24.76275  ? 116 ARG B CD    1 
ATOM   1910 N  NE    . ARG B 1 52  ? -5.65385  -19.63534 6.24546   1.000 29.11031  ? 116 ARG B NE    1 
ATOM   1911 C  CZ    . ARG B 1 52  ? -5.21320  -18.84582 7.21752   1.000 31.51390  ? 116 ARG B CZ    1 
ATOM   1912 N  NH1   . ARG B 1 52  ? -3.92129  -18.74970 7.50138   1.000 32.69111  ? 116 ARG B NH1   1 
ATOM   1913 N  NH2   . ARG B 1 52  ? -6.08989  -18.14647 7.93435   1.000 31.76092  ? 116 ARG B NH2   1 
ATOM   1914 N  N     . LEU B 1 53  ? -3.65732  -20.59457 0.83546   1.000 16.43154  ? 117 LEU B N     1 
ATOM   1915 C  CA    . LEU B 1 53  ? -3.51570  -19.47376 -0.08889  1.000 19.47965  ? 117 LEU B CA    1 
ATOM   1916 C  C     . LEU B 1 53  ? -4.12975  -19.78417 -1.44179  1.000 20.33440  ? 117 LEU B C     1 
ATOM   1917 O  O     . LEU B 1 53  ? -4.79786  -18.92747 -2.03194  1.000 21.92766  ? 117 LEU B O     1 
ATOM   1918 C  CB    . LEU B 1 53  ? -2.04713  -19.10926 -0.26058  1.000 18.52710  ? 117 LEU B CB    1 
ATOM   1919 C  CG    . LEU B 1 53  ? -1.42025  -18.39658 0.93515   1.000 22.29870  ? 117 LEU B CG    1 
ATOM   1920 C  CD1   . LEU B 1 53  ? 0.09301   -18.43175 0.76575   1.000 21.23366  ? 117 LEU B CD1   1 
ATOM   1921 C  CD2   . LEU B 1 53  ? -1.93115  -16.98529 1.05798   1.000 23.24811  ? 117 LEU B CD2   1 
ATOM   1922 N  N     A ILE B 1 54  ? -3.89424  -20.99443 -1.95676  1.000 18.99679  ? 118 ILE B N     1 
ATOM   1923 N  N     B ILE B 1 54  ? -3.90952  -20.99871 -1.95180  0.000 19.00213  ? 118 ILE B N     1 
ATOM   1924 C  CA    A ILE B 1 54  ? -4.45680  -21.40853 -3.24128  1.000 19.63239  ? 118 ILE B CA    1 
ATOM   1925 C  CA    B ILE B 1 54  ? -4.46766  -21.38210 -3.24585  0.000 19.66157  ? 118 ILE B CA    1 
ATOM   1926 C  C     A ILE B 1 54  ? -5.98100  -21.33725 -3.19786  1.000 21.74783  ? 118 ILE B C     1 
ATOM   1927 C  C     B ILE B 1 54  ? -5.98907  -21.33719 -3.20055  0.000 21.76965  ? 118 ILE B C     1 
ATOM   1928 O  O     A ILE B 1 54  ? -6.62856  -20.88288 -4.15257  1.000 22.48684  ? 118 ILE B O     1 
ATOM   1929 O  O     B ILE B 1 54  ? -6.64459  -20.92909 -4.16771  0.000 22.76535  ? 118 ILE B O     1 
ATOM   1930 C  CB    A ILE B 1 54  ? -3.94496  -22.82135 -3.59497  1.000 18.74629  ? 118 ILE B CB    1 
ATOM   1931 C  CB    B ILE B 1 54  ? -3.94831  -22.77333 -3.65678  0.000 18.83488  ? 118 ILE B CB    1 
ATOM   1932 C  CG1   A ILE B 1 54  ? -2.45516  -22.78416 -3.94941  1.000 17.36473  ? 118 ILE B CG1   1 
ATOM   1933 C  CG1   B ILE B 1 54  ? -2.44841  -22.71519 -3.95488  0.000 17.17333  ? 118 ILE B CG1   1 
ATOM   1934 C  CG2   A ILE B 1 54  ? -4.74355  -23.46410 -4.72727  1.000 18.34021  ? 118 ILE B CG2   1 
ATOM   1935 C  CG2   B ILE B 1 54  ? -4.71103  -23.30478 -4.86188  0.000 19.05529  ? 118 ILE B CG2   1 
ATOM   1936 C  CD1   A ILE B 1 54  ? -1.83927  -24.14561 -4.06807  1.000 15.25529  ? 118 ILE B CD1   1 
ATOM   1937 C  CD1   B ILE B 1 54  ? -2.10525  -21.96892 -5.22529  0.000 19.22115  ? 118 ILE B CD1   1 
ATOM   1938 N  N     . SER B 1 55  ? -6.57405  -21.73865 -2.07021  1.000 20.59309  ? 119 SER B N     1 
ATOM   1939 C  CA    . SER B 1 55  ? -8.02636  -21.70940 -1.92566  1.000 23.62893  ? 119 SER B CA    1 
ATOM   1940 C  C     . SER B 1 55  ? -8.60802  -20.29614 -1.95314  1.000 25.21003  ? 119 SER B C     1 
ATOM   1941 O  O     . SER B 1 55  ? -9.82396  -20.15755 -2.12843  1.000 26.80613  ? 119 SER B O     1 
ATOM   1942 C  CB    . SER B 1 55  ? -8.44182  -22.41512 -0.62364  1.000 21.34355  ? 119 SER B CB    1 
ATOM   1943 O  OG    . SER B 1 55  ? -8.27307  -21.55929 0.49494   1.000 26.03622  ? 119 SER B OG    1 
ATOM   1944 N  N     . LEU B 1 56  ? -7.79175  -19.24548 -1.77159  1.000 18.67444  ? 120 LEU B N     1 
ATOM   1945 C  CA    . LEU B 1 56  ? -8.31746  -17.88768 -1.87935  1.000 23.18326  ? 120 LEU B CA    1 
ATOM   1946 C  C     . LEU B 1 56  ? -8.79431  -17.60176 -3.29552  1.000 24.17037  ? 120 LEU B C     1 
ATOM   1947 O  O     . LEU B 1 56  ? -9.81506  -16.93171 -3.49469  1.000 26.83846  ? 120 LEU B O     1 
ATOM   1948 C  CB    . LEU B 1 56  ? -7.26147  -16.85322 -1.47023  1.000 22.79874  ? 120 LEU B CB    1 
ATOM   1949 C  CG    . LEU B 1 56  ? -6.75932  -16.86279 -0.02151  1.000 19.72289  ? 120 LEU B CG    1 
ATOM   1950 C  CD1   . LEU B 1 56  ? -5.62870  -15.86873 0.14425   1.000 20.36499  ? 120 LEU B CD1   1 
ATOM   1951 C  CD2   . LEU B 1 56  ? -7.88229  -16.58873 0.97462   1.000 20.02591  ? 120 LEU B CD2   1 
ATOM   1952 N  N     . THR B 1 57  ? -8.06118  -18.10045 -4.29012  1.000 28.09643  ? 121 THR B N     1 
ATOM   1953 C  CA    . THR B 1 57  ? -8.35999  -17.89469 -5.69828  1.000 30.29535  ? 121 THR B CA    1 
ATOM   1954 C  C     . THR B 1 57  ? -9.07705  -19.07284 -6.33405  1.000 35.01224  ? 121 THR B C     1 
ATOM   1955 O  O     . THR B 1 57  ? -9.93541  -18.87136 -7.19577  1.000 38.27119  ? 121 THR B O     1 
ATOM   1956 C  CB    . THR B 1 57  ? -7.06762  -17.63455 -6.47218  1.000 30.36722  ? 121 THR B CB    1 
ATOM   1957 O  OG1   . THR B 1 57  ? -6.24780  -18.80759 -6.43682  1.000 32.71853  ? 121 THR B OG1   1 
ATOM   1958 C  CG2   . THR B 1 57  ? -6.30613  -16.49892 -5.83918  1.000 32.17257  ? 121 THR B CG2   1 
ATOM   1959 N  N     . ASP B 1 58  ? -8.74540  -20.29793 -5.92507  1.000 26.50968  ? 122 ASP B N     1 
ATOM   1960 C  CA    . ASP B 1 58  ? -9.20248  -21.51343 -6.58960  1.000 26.76964  ? 122 ASP B CA    1 
ATOM   1961 C  C     . ASP B 1 58  ? -10.36298 -22.07523 -5.77458  1.000 30.52805  ? 122 ASP B C     1 
ATOM   1962 O  O     . ASP B 1 58  ? -10.16762 -22.54678 -4.64808  1.000 27.81379  ? 122 ASP B O     1 
ATOM   1963 C  CB    . ASP B 1 58  ? -8.05437  -22.51488 -6.67960  1.000 25.31141  ? 122 ASP B CB    1 
ATOM   1964 C  CG    . ASP B 1 58  ? -8.41946  -23.80000 -7.41914  1.000 34.59962  ? 122 ASP B CG    1 
ATOM   1965 O  OD1   . ASP B 1 58  ? -9.63096  -24.12219 -7.60924  1.000 26.42373  ? 122 ASP B OD1   1 
ATOM   1966 O  OD2   . ASP B 1 58  ? -7.45045  -24.53000 -7.74847  1.000 29.89882  ? 122 ASP B OD2   1 
ATOM   1967 N  N     . GLU B 1 59  ? -11.56671 -22.05386 -6.35485  1.000 43.81113  ? 123 GLU B N     1 
ATOM   1968 C  CA    . GLU B 1 59  ? -12.76026 -22.42213 -5.59485  1.000 45.90431  ? 123 GLU B CA    1 
ATOM   1969 C  C     . GLU B 1 59  ? -12.75485 -23.89065 -5.18755  1.000 40.20135  ? 123 GLU B C     1 
ATOM   1970 O  O     . GLU B 1 59  ? -13.36850 -24.25119 -4.17546  1.000 43.00640  ? 123 GLU B O     1 
ATOM   1971 C  CB    . GLU B 1 59  ? -14.01644 -22.11205 -6.40790  1.000 43.78518  ? 123 GLU B CB    1 
ATOM   1972 N  N     . ASN B 1 60  ? -12.07855 -24.74697 -5.95238  1.000 35.36878  ? 124 ASN B N     1 
ATOM   1973 C  CA    . ASN B 1 60  ? -12.09632 -26.18677 -5.72322  1.000 31.68796  ? 124 ASN B CA    1 
ATOM   1974 C  C     . ASN B 1 60  ? -10.80587 -26.70400 -5.09355  1.000 30.62011  ? 124 ASN B C     1 
ATOM   1975 O  O     . ASN B 1 60  ? -10.59814 -27.92180 -5.03645  1.000 28.52780  ? 124 ASN B O     1 
ATOM   1976 C  CB    . ASN B 1 60  ? -12.37702 -26.91922 -7.03949  1.000 30.97763  ? 124 ASN B CB    1 
ATOM   1977 N  N     . ALA B 1 61  ? -9.95012  -25.81161 -4.59217  1.000 26.36116  ? 125 ALA B N     1 
ATOM   1978 C  CA    . ALA B 1 61  ? -8.66130  -26.23864 -4.05105  1.000 28.45182  ? 125 ALA B CA    1 
ATOM   1979 C  C     . ALA B 1 61  ? -8.82135  -27.27698 -2.94606  1.000 21.18915  ? 125 ALA B C     1 
ATOM   1980 O  O     . ALA B 1 61  ? -8.02859  -28.22073 -2.85751  1.000 22.33579  ? 125 ALA B O     1 
ATOM   1981 C  CB    . ALA B 1 61  ? -7.88248  -25.03143 -3.53397  1.000 23.86117  ? 125 ALA B CB    1 
ATOM   1982 N  N     . LEU B 1 62  ? -9.84797  -27.13839 -2.10826  1.000 24.25506  ? 126 LEU B N     1 
ATOM   1983 C  CA    . LEU B 1 62  ? -10.05273 -28.01325 -0.96066  1.000 22.08094  ? 126 LEU B CA    1 
ATOM   1984 C  C     . LEU B 1 62  ? -11.02989 -29.14825 -1.22593  1.000 27.56438  ? 126 LEU B C     1 
ATOM   1985 O  O     . LEU B 1 62  ? -11.38253 -29.87304 -0.29014  1.000 29.32230  ? 126 LEU B O     1 
ATOM   1986 C  CB    . LEU B 1 62  ? -10.53595 -27.19233 0.23995   1.000 22.02702  ? 126 LEU B CB    1 
ATOM   1987 C  CG    . LEU B 1 62  ? -9.64653  -25.99466 0.56979   1.000 23.82542  ? 126 LEU B CG    1 
ATOM   1988 C  CD1   . LEU B 1 62  ? -10.17268 -25.23881 1.78024   1.000 26.05081  ? 126 LEU B CD1   1 
ATOM   1989 C  CD2   . LEU B 1 62  ? -8.22637  -26.49774 0.83506   1.000 21.33169  ? 126 LEU B CD2   1 
ATOM   1990 N  N     . ALA B 1 63  ? -11.45871 -29.33682 -2.47518  1.000 26.34320  ? 127 ALA B N     1 
ATOM   1991 C  CA    . ALA B 1 63  ? -12.50202 -30.31415 -2.76107  1.000 22.78037  ? 127 ALA B CA    1 
ATOM   1992 C  C     . ALA B 1 63  ? -12.08468 -31.73121 -2.37984  1.000 31.17065  ? 127 ALA B C     1 
ATOM   1993 O  O     . ALA B 1 63  ? -12.92849 -32.53583 -1.95947  1.000 28.92688  ? 127 ALA B O     1 
ATOM   1994 C  CB    . ALA B 1 63  ? -12.87432 -30.25188 -4.24006  1.000 28.83066  ? 127 ALA B CB    1 
ATOM   1995 N  N     . GLY B 1 64  ? -10.79891 -32.06104 -2.51887  1.000 53.03461  ? 128 GLY B N     1 
ATOM   1996 C  CA    . GLY B 1 64  ? -10.35731 -33.40963 -2.20416  1.000 51.11835  ? 128 GLY B CA    1 
ATOM   1997 C  C     . GLY B 1 64  ? -10.36513 -33.71613 -0.72120  1.000 54.78879  ? 128 GLY B C     1 
ATOM   1998 O  O     . GLY B 1 64  ? -10.49737 -34.87746 -0.32324  1.000 58.78133  ? 128 GLY B O     1 
ATOM   1999 N  N     . ASN B 1 65  ? -10.22684 -32.68912 0.11282   1.000 38.24907  ? 129 ASN B N     1 
ATOM   2000 C  CA    . ASN B 1 65  ? -10.18490 -32.86649 1.56253   1.000 35.98853  ? 129 ASN B CA    1 
ATOM   2001 C  C     . ASN B 1 65  ? -10.48740 -31.49709 2.15521   1.000 37.76933  ? 129 ASN B C     1 
ATOM   2002 O  O     . ASN B 1 65  ? -9.70423  -30.56042 1.96464   1.000 35.96445  ? 129 ASN B O     1 
ATOM   2003 C  CB    . ASN B 1 65  ? -8.81531  -33.38040 2.00123   1.000 31.69505  ? 129 ASN B CB    1 
ATOM   2004 C  CG    . ASN B 1 65  ? -8.85573  -34.11698 3.32225   1.000 33.33218  ? 129 ASN B CG    1 
ATOM   2005 O  OD1   . ASN B 1 65  ? -9.44591  -33.64373 4.29105   1.000 37.66963  ? 129 ASN B OD1   1 
ATOM   2006 N  ND2   . ASN B 1 65  ? -8.20549  -35.27607 3.37461   1.000 33.09600  ? 129 ASN B ND2   1 
ATOM   2007 N  N     . GLU B 1 66  ? -11.61728 -31.36949 2.84958   1.000 41.29506  ? 130 GLU B N     1 
ATOM   2008 C  CA    . GLU B 1 66  ? -12.06391 -30.04179 3.25652   1.000 43.80557  ? 130 GLU B CA    1 
ATOM   2009 C  C     . GLU B 1 66  ? -11.38015 -29.53162 4.52532   1.000 47.56558  ? 130 GLU B C     1 
ATOM   2010 O  O     . GLU B 1 66  ? -11.58201 -28.36667 4.89058   1.000 47.02183  ? 130 GLU B O     1 
ATOM   2011 C  CB    . GLU B 1 66  ? -13.58542 -30.03809 3.44037   1.000 42.50295  ? 130 GLU B CB    1 
ATOM   2012 N  N     . GLU B 1 67  ? -10.57131 -30.35084 5.19129   1.000 31.19076  ? 131 GLU B N     1 
ATOM   2013 C  CA    . GLU B 1 67  ? -9.94373  -29.97424 6.45019   1.000 32.86554  ? 131 GLU B CA    1 
ATOM   2014 C  C     . GLU B 1 67  ? -8.49113  -29.55063 6.24648   1.000 31.33905  ? 131 GLU B C     1 
ATOM   2015 O  O     . GLU B 1 67  ? -7.83586  -29.92608 5.27179   1.000 28.93629  ? 131 GLU B O     1 
ATOM   2016 C  CB    . GLU B 1 67  ? -10.01470 -31.13178 7.45291   1.000 36.88229  ? 131 GLU B CB    1 
ATOM   2017 C  CG    . GLU B 1 67  ? -8.78791  -32.02854 7.47540   1.000 30.95091  ? 131 GLU B CG    1 
ATOM   2018 C  CD    . GLU B 1 67  ? -8.93766  -33.22698 8.40712   1.000 34.04714  ? 131 GLU B CD    1 
ATOM   2019 O  OE1   . GLU B 1 67  ? -9.99092  -33.91183 8.36646   1.000 36.15770  ? 131 GLU B OE1   1 
ATOM   2020 O  OE2   . GLU B 1 67  ? -7.98439  -33.49494 9.17114   1.000 31.42393  ? 131 GLU B OE2   1 
ATOM   2021 N  N     . LEU B 1 68  ? -7.98974  -28.75885 7.20397   1.000 17.41088  ? 132 LEU B N     1 
ATOM   2022 C  CA    . LEU B 1 68  ? -6.62283  -28.22542 7.18887   1.000 18.77388  ? 132 LEU B CA    1 
ATOM   2023 C  C     . LEU B 1 68  ? -5.97017  -28.59754 8.52641   1.000 18.03199  ? 132 LEU B C     1 
ATOM   2024 O  O     . LEU B 1 68  ? -5.91768  -27.79738 9.46176   1.000 16.40160  ? 132 LEU B O     1 
ATOM   2025 C  CB    . LEU B 1 68  ? -6.64830  -26.69370 6.96419   1.000 19.26801  ? 132 LEU B CB    1 
ATOM   2026 C  CG    . LEU B 1 68  ? -7.06638  -26.18688 5.58439   1.000 20.09891  ? 132 LEU B CG    1 
ATOM   2027 C  CD1   . LEU B 1 68  ? -7.12942  -24.66738 5.54813   1.000 15.81616  ? 132 LEU B CD1   1 
ATOM   2028 C  CD2   . LEU B 1 68  ? -6.11997  -26.71481 4.52345   1.000 18.66748  ? 132 LEU B CD2   1 
ATOM   2029 N  N     . THR B 1 69  ? -5.44679  -29.81536 8.62070   1.000 14.98940  ? 133 THR B N     1 
ATOM   2030 C  CA    . THR B 1 69  ? -4.95193  -30.32081 9.89353   1.000 14.69532  ? 133 THR B CA    1 
ATOM   2031 C  C     . THR B 1 69  ? -3.63989  -31.05103 9.69621   1.000 14.57762  ? 133 THR B C     1 
ATOM   2032 O  O     . THR B 1 69  ? -3.21774  -31.33656 8.57266   1.000 13.35922  ? 133 THR B O     1 
ATOM   2033 C  CB    . THR B 1 69  ? -5.93002  -31.28830 10.55619  1.000 15.89704  ? 133 THR B CB    1 
ATOM   2034 O  OG1   . THR B 1 69  ? -5.99330  -32.48469 9.76883   1.000 15.76546  ? 133 THR B OG1   1 
ATOM   2035 C  CG2   . THR B 1 69  ? -7.31032  -30.67002 10.71840  1.000 18.51925  ? 133 THR B CG2   1 
ATOM   2036 N  N     . VAL B 1 70  ? -2.99349  -31.31777 10.81910  1.000 9.93722   ? 134 VAL B N     1 
ATOM   2037 C  CA    . VAL B 1 70  ? -1.88572  -32.25511 10.92795  1.000 11.98041  ? 134 VAL B CA    1 
ATOM   2038 C  C     . VAL B 1 70  ? -2.31512  -33.35379 11.88305  1.000 14.17676  ? 134 VAL B C     1 
ATOM   2039 O  O     . VAL B 1 70  ? -2.91764  -33.07594 12.92655  1.000 15.02703  ? 134 VAL B O     1 
ATOM   2040 C  CB    . VAL B 1 70  ? -0.59275  -31.58384 11.43861  1.000 11.12156  ? 134 VAL B CB    1 
ATOM   2041 C  CG1   . VAL B 1 70  ? 0.53919   -32.61703 11.49300  1.000 12.90650  ? 134 VAL B CG1   1 
ATOM   2042 C  CG2   . VAL B 1 70  ? -0.21855  -30.44183 10.54149  1.000 13.79900  ? 134 VAL B CG2   1 
ATOM   2043 N  N     . LYS B 1 71  ? -2.02030  -34.60046 11.52356  1.000 15.90387  ? 135 LYS B N     1 
ATOM   2044 C  CA    . LYS B 1 71  ? -2.41170  -35.74723 12.32614  1.000 18.38305  ? 135 LYS B CA    1 
ATOM   2045 C  C     . LYS B 1 71  ? -1.21574  -36.67091 12.46185  1.000 18.79083  ? 135 LYS B C     1 
ATOM   2046 O  O     . LYS B 1 71  ? -0.66974  -37.13880 11.45764  1.000 19.33629  ? 135 LYS B O     1 
ATOM   2047 C  CB    . LYS B 1 71  ? -3.61372  -36.47126 11.70601  1.000 19.91199  ? 135 LYS B CB    1 
ATOM   2048 C  CG    . LYS B 1 71  ? -4.92885  -35.78445 12.06006  1.000 18.94689  ? 135 LYS B CG    1 
ATOM   2049 C  CD    . LYS B 1 71  ? -6.10647  -36.33501 11.28002  1.000 17.53090  ? 135 LYS B CD    1 
ATOM   2050 C  CE    . LYS B 1 71  ? -7.40558  -35.68633 11.76950  1.000 21.89418  ? 135 LYS B CE    1 
ATOM   2051 N  NZ    . LYS B 1 71  ? -8.52696  -35.92864 10.81240  1.000 26.51211  ? 135 LYS B NZ    1 
ATOM   2052 N  N     . ILE B 1 72  ? -0.81160  -36.91429 13.70049  1.000 16.64168  ? 136 ILE B N     1 
ATOM   2053 C  CA    . ILE B 1 72  ? 0.34664   -37.72614 14.03522  1.000 14.09160  ? 136 ILE B CA    1 
ATOM   2054 C  C     . ILE B 1 72  ? -0.16745  -39.01068 14.65165  1.000 15.78503  ? 136 ILE B C     1 
ATOM   2055 O  O     . ILE B 1 72  ? -1.01505  -38.97100 15.55324  1.000 17.89132  ? 136 ILE B O     1 
ATOM   2056 C  CB    . ILE B 1 72  ? 1.28058   -36.98834 15.01243  1.000 14.57979  ? 136 ILE B CB    1 
ATOM   2057 C  CG1   . ILE B 1 72  ? 1.96711   -35.82613 14.29417  1.000 14.24783  ? 136 ILE B CG1   1 
ATOM   2058 C  CG2   . ILE B 1 72  ? 2.29945   -37.94211 15.59813  1.000 15.88334  ? 136 ILE B CG2   1 
ATOM   2059 C  CD1   . ILE B 1 72  ? 2.29650   -34.67445 15.18801  1.000 19.16857  ? 136 ILE B CD1   1 
ATOM   2060 N  N     . LYS B 1 73  ? 0.31845   -40.14499 14.17083  1.000 13.62218  ? 137 LYS B N     1 
ATOM   2061 C  CA    . LYS B 1 73  ? -0.03100  -41.37200 14.86855  1.000 17.01711  ? 137 LYS B CA    1 
ATOM   2062 C  C     . LYS B 1 73  ? 1.12208   -42.36243 14.88311  1.000 16.59453  ? 137 LYS B C     1 
ATOM   2063 O  O     . LYS B 1 73  ? 1.82412   -42.54714 13.88178  1.000 14.60136  ? 137 LYS B O     1 
ATOM   2064 C  CB    . LYS B 1 73  ? -1.31806  -41.98445 14.29719  1.000 40.09078  ? 137 LYS B CB    1 
ATOM   2065 C  CG    . LYS B 1 73  ? -1.27262  -42.69048 12.99982  1.000 39.61319  ? 137 LYS B CG    1 
ATOM   2066 C  CD    . LYS B 1 73  ? -2.72020  -43.05889 12.66472  1.000 39.60777  ? 137 LYS B CD    1 
ATOM   2067 C  CE    . LYS B 1 73  ? -2.83572  -44.26841 11.75251  1.000 39.54133  ? 137 LYS B CE    1 
ATOM   2068 N  NZ    . LYS B 1 73  ? -4.04715  -44.20453 10.87754  1.000 39.41495  ? 137 LYS B NZ    1 
ATOM   2069 N  N     . CYS B 1 74  ? 1.32679   -42.96162 16.05702  1.000 16.93592  ? 138 CYS B N     1 
ATOM   2070 C  CA    . CYS B 1 74  ? 2.30146   -44.02512 16.24713  1.000 19.78651  ? 138 CYS B CA    1 
ATOM   2071 C  C     . CYS B 1 74  ? 1.64576   -45.36329 15.96249  1.000 18.74594  ? 138 CYS B C     1 
ATOM   2072 O  O     . CYS B 1 74  ? 0.60559   -45.68980 16.54564  1.000 22.39043  ? 138 CYS B O     1 
ATOM   2073 C  CB    . CYS B 1 74  ? 2.85284   -44.05850 17.67539  1.000 19.06979  ? 138 CYS B CB    1 
ATOM   2074 S  SG    . CYS B 1 74  ? 2.98359   -42.48616 18.51951  1.000 25.28197  ? 138 CYS B SG    1 
ATOM   2075 N  N     . ASP B 1 75  ? 2.26446   -46.14767 15.10496  1.000 18.57769  ? 139 ASP B N     1 
ATOM   2076 C  CA    . ASP B 1 75  ? 1.89086   -47.54616 14.97682  1.000 22.30839  ? 139 ASP B CA    1 
ATOM   2077 C  C     . ASP B 1 75  ? 3.01752   -48.36205 15.60912  1.000 24.28731  ? 139 ASP B C     1 
ATOM   2078 O  O     . ASP B 1 75  ? 3.97080   -48.76979 14.93636  1.000 23.24305  ? 139 ASP B O     1 
ATOM   2079 C  CB    . ASP B 1 75  ? 1.62882   -47.93836 13.52923  1.000 21.70239  ? 139 ASP B CB    1 
ATOM   2080 C  CG    . ASP B 1 75  ? 1.03895   -49.33761 13.41375  1.000 23.51040  ? 139 ASP B CG    1 
ATOM   2081 O  OD1   . ASP B 1 75  ? 1.38570   -50.18752 14.24319  1.000 30.40440  ? 139 ASP B OD1   1 
ATOM   2082 O  OD2   . ASP B 1 75  ? 0.21194   -49.58464 12.51126  1.000 24.12561  ? 139 ASP B OD2   1 
ATOM   2083 N  N     . LYS B 1 76  ? 2.87564   -48.61156 16.91364  1.000 23.35327  ? 140 LYS B N     1 
ATOM   2084 C  CA    . LYS B 1 76  ? 3.87513   -49.36056 17.66082  1.000 23.93363  ? 140 LYS B CA    1 
ATOM   2085 C  C     . LYS B 1 76  ? 4.01664   -50.77956 17.13145  1.000 23.12359  ? 140 LYS B C     1 
ATOM   2086 O  O     . LYS B 1 76  ? 5.12739   -51.32191 17.08284  1.000 30.49383  ? 140 LYS B O     1 
ATOM   2087 C  CB    . LYS B 1 76  ? 3.49854   -49.39365 19.13877  1.000 30.61950  ? 140 LYS B CB    1 
ATOM   2088 C  CG    . LYS B 1 76  ? 4.68358   -49.43995 20.09215  1.000 31.75674  ? 140 LYS B CG    1 
ATOM   2089 C  CD    . LYS B 1 76  ? 4.22303   -49.53007 21.53259  1.000 32.77601  ? 140 LYS B CD    1 
ATOM   2090 C  CE    . LYS B 1 76  ? 5.08113   -50.52033 22.31220  1.000 34.16667  ? 140 LYS B CE    1 
ATOM   2091 N  NZ    . LYS B 1 76  ? 6.48498   -50.50161 21.80599  1.000 34.36787  ? 140 LYS B NZ    1 
ATOM   2092 N  N     . GLU B 1 77  ? 2.89871   -51.40702 16.75251  1.000 34.33215  ? 141 GLU B N     1 
ATOM   2093 C  CA    . GLU B 1 77  ? 2.94369   -52.80156 16.31772  1.000 35.40704  ? 141 GLU B CA    1 
ATOM   2094 C  C     . GLU B 1 77  ? 3.82729   -52.98418 15.08947  1.000 39.31761  ? 141 GLU B C     1 
ATOM   2095 O  O     . GLU B 1 77  ? 4.43979   -54.04240 14.91649  1.000 43.77001  ? 141 GLU B O     1 
ATOM   2096 C  CB    . GLU B 1 77  ? 1.52831   -53.30841 16.02942  1.000 32.75426  ? 141 GLU B CB    1 
ATOM   2097 N  N     . LYS B 1 78  ? 3.91204   -51.97007 14.23442  1.000 25.44563  ? 142 LYS B N     1 
ATOM   2098 C  CA    . LYS B 1 78  ? 4.66179   -52.04833 12.98950  1.000 22.28588  ? 142 LYS B CA    1 
ATOM   2099 C  C     . LYS B 1 78  ? 5.90415   -51.16995 12.99498  1.000 18.96529  ? 142 LYS B C     1 
ATOM   2100 O  O     . LYS B 1 78  ? 6.52341   -50.98278 11.94234  1.000 23.54056  ? 142 LYS B O     1 
ATOM   2101 C  CB    . LYS B 1 78  ? 3.75628   -51.66484 11.81938  1.000 24.13942  ? 142 LYS B CB    1 
ATOM   2102 C  CG    . LYS B 1 78  ? 2.38442   -52.32745 11.86528  1.000 32.56786  ? 142 LYS B CG    1 
ATOM   2103 C  CD    . LYS B 1 78  ? 2.30363   -53.48119 10.85999  1.000 28.72962  ? 142 LYS B CD    1 
ATOM   2104 C  CE    . LYS B 1 78  ? 0.94509   -53.52552 10.16327  1.000 35.84107  ? 142 LYS B CE    1 
ATOM   2105 N  NZ    . LYS B 1 78  ? -0.10629  -54.16083 11.01214  1.000 37.20335  ? 142 LYS B NZ    1 
ATOM   2106 N  N     . ASN B 1 79  ? 6.26705   -50.60655 14.14641  1.000 25.36999  ? 143 ASN B N     1 
ATOM   2107 C  CA    . ASN B 1 79  ? 7.44333   -49.74549 14.26864  1.000 23.97905  ? 143 ASN B CA    1 
ATOM   2108 C  C     . ASN B 1 79  ? 7.35567   -48.52461 13.34729  1.000 21.76511  ? 143 ASN B C     1 
ATOM   2109 O  O     . ASN B 1 79  ? 8.33671   -48.13426 12.70816  1.000 23.35575  ? 143 ASN B O     1 
ATOM   2110 C  CB    . ASN B 1 79  ? 8.72007   -50.55409 14.00124  1.000 27.75151  ? 143 ASN B CB    1 
ATOM   2111 C  CG    . ASN B 1 79  ? 9.98763   -49.79701 14.35507  1.000 27.93967  ? 143 ASN B CG    1 
ATOM   2112 O  OD1   . ASN B 1 79  ? 10.07295  -49.13253 15.39292  1.000 27.75537  ? 143 ASN B OD1   1 
ATOM   2113 N  ND2   . ASN B 1 79  ? 10.96932  -49.85594 13.45814  1.000 31.73169  ? 143 ASN B ND2   1 
ATOM   2114 N  N     . LEU B 1 80  ? 6.17980   -47.88873 13.27842  1.000 18.15403  ? 144 LEU B N     1 
ATOM   2115 C  CA    . LEU B 1 80  ? 5.98993   -46.76066 12.36769  1.000 17.28431  ? 144 LEU B CA    1 
ATOM   2116 C  C     . LEU B 1 80  ? 5.44321   -45.53486 13.09386  1.000 18.47038  ? 144 LEU B C     1 
ATOM   2117 O  O     . LEU B 1 80  ? 4.59510   -45.65245 13.98561  1.000 16.86828  ? 144 LEU B O     1 
ATOM   2118 C  CB    . LEU B 1 80  ? 5.04386   -47.13178 11.19880  1.000 15.33522  ? 144 LEU B CB    1 
ATOM   2119 C  CG    . LEU B 1 80  ? 5.41857   -48.34254 10.33283  1.000 16.68300  ? 144 LEU B CG    1 
ATOM   2120 C  CD1   . LEU B 1 80  ? 4.30497   -48.62836 9.31020   1.000 12.34844  ? 144 LEU B CD1   1 
ATOM   2121 C  CD2   . LEU B 1 80  ? 6.76104   -48.13488 9.62139   1.000 15.72466  ? 144 LEU B CD2   1 
ATOM   2122 N  N     . LEU B 1 81  ? 5.94484   -44.35542 12.70905  1.000 16.17613  ? 145 LEU B N     1 
ATOM   2123 C  CA    . LEU B 1 81  ? 5.40570   -43.06038 13.11331  1.000 13.95507  ? 145 LEU B CA    1 
ATOM   2124 C  C     . LEU B 1 81  ? 4.91239   -42.34087 11.86100  1.000 13.92510  ? 145 LEU B C     1 
ATOM   2125 O  O     . LEU B 1 81  ? 5.66286   -42.21061 10.88234  1.000 12.84703  ? 145 LEU B O     1 
ATOM   2126 C  CB    . LEU B 1 81  ? 6.47861   -42.22028 13.81557  1.000 14.43902  ? 145 LEU B CB    1 
ATOM   2127 C  CG    . LEU B 1 81  ? 6.12052   -40.78674 14.20420  1.000 13.61766  ? 145 LEU B CG    1 
ATOM   2128 C  CD1   . LEU B 1 81  ? 4.99319   -40.78184 15.22565  1.000 16.21564  ? 145 LEU B CD1   1 
ATOM   2129 C  CD2   . LEU B 1 81  ? 7.32135   -40.04493 14.74467  1.000 20.25719  ? 145 LEU B CD2   1 
ATOM   2130 N  N     . HIS B 1 82  ? 3.65973   -41.88744 11.86662  1.000 13.38729  ? 146 HIS B N     1 
ATOM   2131 C  CA    . HIS B 1 82  ? 3.08574   -41.21372 10.70090  1.000 11.90516  ? 146 HIS B CA    1 
ATOM   2132 C  C     . HIS B 1 82  ? 2.80855   -39.75314 11.01534  1.000 15.57287  ? 146 HIS B C     1 
ATOM   2133 O  O     . HIS B 1 82  ? 2.22662   -39.44113 12.05864  1.000 14.12530  ? 146 HIS B O     1 
ATOM   2134 C  CB    . HIS B 1 82  ? 1.78109   -41.87565 10.25251  1.000 9.94994   ? 146 HIS B CB    1 
ATOM   2135 C  CG    . HIS B 1 82  ? 1.89371   -43.33698 9.98071   1.000 13.59029  ? 146 HIS B CG    1 
ATOM   2136 N  ND1   . HIS B 1 82  ? 2.33547   -43.83455 8.77766   1.000 13.77739  ? 146 HIS B ND1   1 
ATOM   2137 C  CD2   . HIS B 1 82  ? 1.60767   -44.41418 10.75263  1.000 13.16843  ? 146 HIS B CD2   1 
ATOM   2138 C  CE1   . HIS B 1 82  ? 2.31593   -45.15539 8.81509   1.000 14.01273  ? 146 HIS B CE1   1 
ATOM   2139 N  NE2   . HIS B 1 82  ? 1.87831   -45.53452 9.99975   1.000 13.75173  ? 146 HIS B NE2   1 
ATOM   2140 N  N     . VAL B 1 83  ? 3.21302   -38.85356 10.11940  1.000 9.29447   ? 147 VAL B N     1 
ATOM   2141 C  CA    . VAL B 1 83  ? 2.88403   -37.43440 10.25075  1.000 9.52628   ? 147 VAL B CA    1 
ATOM   2142 C  C     . VAL B 1 83  ? 2.11143   -37.04344 9.00324   1.000 8.38671   ? 147 VAL B C     1 
ATOM   2143 O  O     . VAL B 1 83  ? 2.68581   -36.95940 7.90802   1.000 7.98455   ? 147 VAL B O     1 
ATOM   2144 C  CB    . VAL B 1 83  ? 4.12677   -36.55506 10.42916  1.000 9.57685   ? 147 VAL B CB    1 
ATOM   2145 C  CG1   . VAL B 1 83  ? 3.71290   -35.13758 10.75681  1.000 11.41740  ? 147 VAL B CG1   1 
ATOM   2146 C  CG2   . VAL B 1 83  ? 5.05032   -37.13657 11.53045  1.000 10.78943  ? 147 VAL B CG2   1 
ATOM   2147 N  N     . THR B 1 84  ? 0.80715   -36.81242 9.14948   1.000 10.52948  ? 148 THR B N     1 
ATOM   2148 C  CA    . THR B 1 84  ? -0.05496  -36.59529 7.99051   1.000 10.58507  ? 148 THR B CA    1 
ATOM   2149 C  C     . THR B 1 84  ? -0.64191  -35.19444 8.02899   1.000 13.06855  ? 148 THR B C     1 
ATOM   2150 O  O     . THR B 1 84  ? -1.09563  -34.72981 9.08500   1.000 13.88306  ? 148 THR B O     1 
ATOM   2151 C  CB    . THR B 1 84  ? -1.16536  -37.63680 7.93155   1.000 11.33464  ? 148 THR B CB    1 
ATOM   2152 O  OG1   . THR B 1 84  ? -0.59818  -38.93938 7.70520   1.000 16.26760  ? 148 THR B OG1   1 
ATOM   2153 C  CG2   . THR B 1 84  ? -2.12056  -37.32905 6.80314   1.000 11.15668  ? 148 THR B CG2   1 
ATOM   2154 N  N     . ASP B 1 85  ? -0.58646  -34.50848 6.88929   1.000 13.22891  ? 149 ASP B N     1 
ATOM   2155 C  CA    . ASP B 1 85  ? -1.14200  -33.18026 6.74529   1.000 16.96633  ? 149 ASP B CA    1 
ATOM   2156 C  C     . ASP B 1 85  ? -2.07845  -33.18936 5.55284   1.000 17.09477  ? 149 ASP B C     1 
ATOM   2157 O  O     . ASP B 1 85  ? -1.92384  -33.99060 4.63253   1.000 17.17558  ? 149 ASP B O     1 
ATOM   2158 C  CB    . ASP B 1 85  ? -0.03313  -32.12113 6.59610   1.000 14.19415  ? 149 ASP B CB    1 
ATOM   2159 C  CG    . ASP B 1 85  ? 0.66136   -32.17900 5.24101   1.000 17.67049  ? 149 ASP B CG    1 
ATOM   2160 O  OD1   . ASP B 1 85  ? 0.04166   -31.85701 4.19967   1.000 14.87390  ? 149 ASP B OD1   1 
ATOM   2161 O  OD2   . ASP B 1 85  ? 1.84158   -32.60139 5.22220   1.000 15.08198  ? 149 ASP B OD2   1 
ATOM   2162 N  N     . THR B 1 86  ? -3.08590  -32.32937 5.60459   1.000 12.38671  ? 150 THR B N     1 
ATOM   2163 C  CA    . THR B 1 86  ? -4.00800  -32.15897 4.48578   1.000 12.63257  ? 150 THR B CA    1 
ATOM   2164 C  C     . THR B 1 86  ? -3.67926  -30.89030 3.71436   1.000 13.85244  ? 150 THR B C     1 
ATOM   2165 O  O     . THR B 1 86  ? -4.56903  -30.13012 3.30437   1.000 16.34046  ? 150 THR B O     1 
ATOM   2166 C  CB    . THR B 1 86  ? -5.45669  -32.15369 4.97885   1.000 13.87835  ? 150 THR B CB    1 
ATOM   2167 O  OG1   . THR B 1 86  ? -5.64120  -31.12811 5.96991   1.000 14.90750  ? 150 THR B OG1   1 
ATOM   2168 C  CG2   . THR B 1 86  ? -5.78312  -33.47097 5.60181   1.000 15.72043  ? 150 THR B CG2   1 
ATOM   2169 N  N     . GLY B 1 87  ? -2.38849  -30.60262 3.54517   1.000 13.26307  ? 151 GLY B N     1 
ATOM   2170 C  CA    . GLY B 1 87  ? -1.94399  -29.44292 2.80075   1.000 14.72112  ? 151 GLY B CA    1 
ATOM   2171 C  C     . GLY B 1 87  ? -1.86638  -29.68970 1.30051   1.000 14.87747  ? 151 GLY B C     1 
ATOM   2172 O  O     . GLY B 1 87  ? -2.49572  -30.59921 0.75582   1.000 14.97193  ? 151 GLY B O     1 
ATOM   2173 N  N     . VAL B 1 88  ? -1.02603  -28.88842 0.63402   1.000 16.10176  ? 152 VAL B N     1 
ATOM   2174 C  CA    . VAL B 1 88  ? -1.01660  -28.82405 -0.82966  1.000 16.32391  ? 152 VAL B CA    1 
ATOM   2175 C  C     . VAL B 1 88  ? -0.61162  -30.15227 -1.46385  1.000 15.32464  ? 152 VAL B C     1 
ATOM   2176 O  O     . VAL B 1 88  ? -0.99517  -30.45006 -2.60290  1.000 18.60178  ? 152 VAL B O     1 
ATOM   2177 C  CB    . VAL B 1 88  ? -0.11894  -27.65470 -1.29111  1.000 17.36756  ? 152 VAL B CB    1 
ATOM   2178 C  CG1   . VAL B 1 88  ? 1.33322   -27.91970 -0.95065  1.000 20.33549  ? 152 VAL B CG1   1 
ATOM   2179 C  CG2   . VAL B 1 88  ? -0.27849  -27.41030 -2.78015  1.000 16.60560  ? 152 VAL B CG2   1 
ATOM   2180 N  N     . GLY B 1 89  ? 0.13058   -30.97245 -0.75822  1.000 14.47192  ? 153 GLY B N     1 
ATOM   2181 C  CA    . GLY B 1 89  ? 0.54628   -32.23294 -1.36588  1.000 14.14496  ? 153 GLY B CA    1 
ATOM   2182 C  C     . GLY B 1 89  ? 1.67243   -31.95693 -2.34980  1.000 13.86261  ? 153 GLY B C     1 
ATOM   2183 O  O     . GLY B 1 89  ? 2.15798   -30.82889 -2.48938  1.000 13.81854  ? 153 GLY B O     1 
ATOM   2184 N  N     . MET B 1 90  ? 2.05878   -33.01416 -3.05099  1.000 22.67556  ? 154 MET B N     1 
ATOM   2185 C  CA    . MET B 1 90  ? 3.27610   -33.02259 -3.85200  1.000 19.38960  ? 154 MET B CA    1 
ATOM   2186 C  C     . MET B 1 90  ? 3.04918   -33.90357 -5.07266  1.000 19.83118  ? 154 MET B C     1 
ATOM   2187 O  O     . MET B 1 90  ? 2.69990   -35.08262 -4.94146  1.000 21.70416  ? 154 MET B O     1 
ATOM   2188 C  CB    . MET B 1 90  ? 4.41883   -33.53296 -2.97760  1.000 18.83972  ? 154 MET B CB    1 
ATOM   2189 C  CG    . MET B 1 90  ? 5.31121   -32.42146 -2.39422  1.000 21.86054  ? 154 MET B CG    1 
ATOM   2190 S  SD    . MET B 1 90  ? 6.73006   -33.12019 -1.50290  1.000 20.53911  ? 154 MET B SD    1 
ATOM   2191 C  CE    . MET B 1 90  ? 5.86929   -34.31041 -0.51423  1.000 16.20527  ? 154 MET B CE    1 
ATOM   2192 N  N     . THR B 1 91  ? 3.22304   -33.32634 -6.26093  1.000 15.26881  ? 155 THR B N     1 
ATOM   2193 C  CA    . THR B 1 91  ? 3.08392   -34.08471 -7.48748  1.000 15.86219  ? 155 THR B CA    1 
ATOM   2194 C  C     . THR B 1 91  ? 4.21028   -35.10052 -7.61413  1.000 15.47794  ? 155 THR B C     1 
ATOM   2195 O  O     . THR B 1 91  ? 5.13415   -35.15325 -6.79875  1.000 14.61081  ? 155 THR B O     1 
ATOM   2196 C  CB    . THR B 1 91  ? 3.09644   -33.17083 -8.70418  1.000 17.65314  ? 155 THR B CB    1 
ATOM   2197 O  OG1   . THR B 1 91  ? 4.41223   -32.60909 -8.86387  1.000 16.68480  ? 155 THR B OG1   1 
ATOM   2198 C  CG2   . THR B 1 91  ? 2.04543   -32.05617 -8.58207  1.000 15.93190  ? 155 THR B CG2   1 
ATOM   2199 N  N     . ARG B 1 92  ? 4.11913   -35.92309 -8.65607  1.000 16.55383  ? 156 ARG B N     1 
ATOM   2200 C  CA    . ARG B 1 92  ? 5.16918   -36.90303 -8.90454  1.000 15.61438  ? 156 ARG B CA    1 
ATOM   2201 C  C     . ARG B 1 92  ? 6.49493   -36.21934 -9.21867  1.000 19.36972  ? 156 ARG B C     1 
ATOM   2202 O  O     . ARG B 1 92  ? 7.53596   -36.57406 -8.65234  1.000 22.35822  ? 156 ARG B O     1 
ATOM   2203 C  CB    . ARG B 1 92  ? 4.77005   -37.83275 -10.03966 1.000 14.60345  ? 156 ARG B CB    1 
ATOM   2204 C  CG    . ARG B 1 92  ? 5.71846   -38.99465 -10.19478 1.000 12.69417  ? 156 ARG B CG    1 
ATOM   2205 C  CD    . ARG B 1 92  ? 6.23370   -38.93754 -11.59981 1.000 16.11004  ? 156 ARG B CD    1 
ATOM   2206 N  NE    . ARG B 1 92  ? 7.03025   -40.09995 -11.93102 1.000 14.60009  ? 156 ARG B NE    1 
ATOM   2207 C  CZ    . ARG B 1 92  ? 8.09802   -40.06771 -12.71168 1.000 20.39496  ? 156 ARG B CZ    1 
ATOM   2208 N  NH1   . ARG B 1 92  ? 8.52060   -38.93892 -13.25255 1.000 15.89008  ? 156 ARG B NH1   1 
ATOM   2209 N  NH2   . ARG B 1 92  ? 8.74134   -41.20293 -12.97472 1.000 20.22338  ? 156 ARG B NH2   1 
ATOM   2210 N  N     . GLU B 1 93  ? 6.47197   -35.23333 -10.12082 1.000 18.54806  ? 157 GLU B N     1 
ATOM   2211 C  CA    . GLU B 1 93  ? 7.67583   -34.47467 -10.46068 1.000 22.59336  ? 157 GLU B CA    1 
ATOM   2212 C  C     . GLU B 1 93  ? 8.32800   -33.87284 -9.21680  1.000 25.22707  ? 157 GLU B C     1 
ATOM   2213 O  O     . GLU B 1 93  ? 9.55220   -33.94350 -9.04882  1.000 25.45079  ? 157 GLU B O     1 
ATOM   2214 C  CB    . GLU B 1 93  ? 7.32126   -33.38252 -11.47224 1.000 20.32122  ? 157 GLU B CB    1 
ATOM   2215 C  CG    . GLU B 1 93  ? 8.42117   -32.34301 -11.73452 1.000 25.91235  ? 157 GLU B CG    1 
ATOM   2216 C  CD    . GLU B 1 93  ? 8.05973   -31.33188 -12.82789 1.000 28.86125  ? 157 GLU B CD    1 
ATOM   2217 O  OE1   . GLU B 1 93  ? 6.91049   -30.83488 -12.83983 1.000 27.24937  ? 157 GLU B OE1   1 
ATOM   2218 O  OE2   . GLU B 1 93  ? 8.92414   -31.01369 -13.68095 1.000 31.02341  ? 157 GLU B OE2   1 
ATOM   2219 N  N     . GLU B 1 94  ? 7.52455   -33.30540 -8.31307  1.000 25.49611  ? 158 GLU B N     1 
ATOM   2220 C  CA    . GLU B 1 94  ? 8.08609   -32.71799 -7.10057  1.000 33.97437  ? 158 GLU B CA    1 
ATOM   2221 C  C     . GLU B 1 94  ? 8.76502   -33.77159 -6.22896  1.000 30.25690  ? 158 GLU B C     1 
ATOM   2222 O  O     . GLU B 1 94  ? 9.80662   -33.49986 -5.61989  1.000 31.62374  ? 158 GLU B O     1 
ATOM   2223 C  CB    . GLU B 1 94  ? 6.99736   -31.96513 -6.33334  1.000 29.97402  ? 158 GLU B CB    1 
ATOM   2224 C  CG    . GLU B 1 94  ? 6.49910   -30.72337 -7.10034  1.000 28.53371  ? 158 GLU B CG    1 
ATOM   2225 C  CD    . GLU B 1 94  ? 5.40543   -29.95323 -6.38577  1.000 34.09994  ? 158 GLU B CD    1 
ATOM   2226 O  OE1   . GLU B 1 94  ? 4.42615   -30.58087 -5.93735  1.000 27.37334  ? 158 GLU B OE1   1 
ATOM   2227 O  OE2   . GLU B 1 94  ? 5.51220   -28.71196 -6.28548  1.000 47.37263  ? 158 GLU B OE2   1 
ATOM   2228 N  N     . LEU B 1 95  ? 8.20408   -34.98390 -6.15986  1.000 25.13335  ? 159 LEU B N     1 
ATOM   2229 C  CA    . LEU B 1 95  ? 8.86075   -36.03868 -5.38996  1.000 23.44956  ? 159 LEU B CA    1 
ATOM   2230 C  C     . LEU B 1 95  ? 10.15793  -36.48651 -6.05453  1.000 29.29118  ? 159 LEU B C     1 
ATOM   2231 O  O     . LEU B 1 95  ? 11.14465  -36.78578 -5.36588  1.000 29.23176  ? 159 LEU B O     1 
ATOM   2232 C  CB    . LEU B 1 95  ? 7.92388   -37.23230 -5.20265  1.000 18.98467  ? 159 LEU B CB    1 
ATOM   2233 C  CG    . LEU B 1 95  ? 6.66176   -37.00439 -4.37409  1.000 18.90460  ? 159 LEU B CG    1 
ATOM   2234 C  CD1   . LEU B 1 95  ? 5.66369   -38.12033 -4.63953  1.000 17.28741  ? 159 LEU B CD1   1 
ATOM   2235 C  CD2   . LEU B 1 95  ? 7.00926   -36.92435 -2.89991  1.000 20.11102  ? 159 LEU B CD2   1 
ATOM   2236 N  N     . VAL B 1 96  ? 10.16330  -36.58143 -7.38745  1.000 24.27913  ? 160 VAL B N     1 
ATOM   2237 C  CA    . VAL B 1 96  ? 11.36708  -37.01278 -8.09249  1.000 25.58330  ? 160 VAL B CA    1 
ATOM   2238 C  C     . VAL B 1 96  ? 12.42640  -35.92022 -8.04423  1.000 32.45149  ? 160 VAL B C     1 
ATOM   2239 O  O     . VAL B 1 96  ? 13.60498  -36.18982 -7.77984  1.000 36.10886  ? 160 VAL B O     1 
ATOM   2240 C  CB    . VAL B 1 96  ? 11.02577  -37.41615 -9.53802  1.000 26.29919  ? 160 VAL B CB    1 
ATOM   2241 C  CG1   . VAL B 1 96  ? 12.29908  -37.62357 -10.34621 1.000 31.45229  ? 160 VAL B CG1   1 
ATOM   2242 C  CG2   . VAL B 1 96  ? 10.16649  -38.68442 -9.55391  1.000 20.28856  ? 160 VAL B CG2   1 
ATOM   2243 N  N     . LYS B 1 97  ? 12.02056  -34.67326 -8.28268  1.000 30.24498  ? 161 LYS B N     1 
ATOM   2244 C  CA    . LYS B 1 97  ? 12.91077  -33.51578 -8.24331  1.000 32.98150  ? 161 LYS B CA    1 
ATOM   2245 C  C     . LYS B 1 97  ? 12.83526  -32.84397 -6.87326  1.000 40.91707  ? 161 LYS B C     1 
ATOM   2246 O  O     . LYS B 1 97  ? 12.51702  -31.66244 -6.74502  1.000 45.90341  ? 161 LYS B O     1 
ATOM   2247 C  CB    . LYS B 1 97  ? 12.52948  -32.53542 -9.34747  1.000 39.80280  ? 161 LYS B CB    1 
ATOM   2248 C  CG    . LYS B 1 97  ? 12.55423  -33.13579 -10.73587 1.000 38.27084  ? 161 LYS B CG    1 
ATOM   2249 C  CD    . LYS B 1 97  ? 12.11177  -32.12754 -11.79131 1.000 32.93210  ? 161 LYS B CD    1 
ATOM   2250 C  CE    . LYS B 1 97  ? 12.08127  -32.78844 -13.15422 1.000 33.51089  ? 161 LYS B CE    1 
ATOM   2251 N  NZ    . LYS B 1 97  ? 11.46644  -31.94165 -14.21771 1.000 32.74554  ? 161 LYS B NZ    1 
ATOM   2252 N  N     . ASN B 1 98  ? 13.14622  -33.61840 -5.83332  1.000 56.81855  ? 162 ASN B N     1 
ATOM   2253 C  CA    . ASN B 1 98  ? 12.99624  -33.19025 -4.44494  1.000 49.07403  ? 162 ASN B CA    1 
ATOM   2254 C  C     . ASN B 1 98  ? 14.26275  -32.57436 -3.88597  1.000 57.78853  ? 162 ASN B C     1 
ATOM   2255 O  O     . ASN B 1 98  ? 14.51631  -32.68957 -2.67947  1.000 63.06409  ? 162 ASN B O     1 
ATOM   2256 C  CB    . ASN B 1 98  ? 12.55287  -34.37705 -3.58457  1.000 54.61894  ? 162 ASN B CB    1 
ATOM   2257 C  CG    . ASN B 1 98  ? 13.58046  -35.51148 -3.56374  1.000 54.80025  ? 162 ASN B CG    1 
ATOM   2258 O  OD1   . ASN B 1 98  ? 14.72065  -35.33100 -3.12928  1.000 56.33169  ? 162 ASN B OD1   1 
ATOM   2259 N  ND2   . ASN B 1 98  ? 13.18062  -36.68026 -4.05593  1.000 53.29459  ? 162 ASN B ND2   1 
ATOM   2260 N  N     . LEU B 1 99  ? 15.03842  -31.89005 -4.73084  1.000 71.64441  ? 163 LEU B N     1 
ATOM   2261 C  CA    . LEU B 1 99  ? 16.46935  -31.66150 -4.53012  1.000 73.47286  ? 163 LEU B CA    1 
ATOM   2262 C  C     . LEU B 1 99  ? 17.24651  -32.97213 -4.62296  1.000 73.21302  ? 163 LEU B C     1 
ATOM   2263 O  O     . LEU B 1 99  ? 18.23336  -33.17732 -3.91041  1.000 74.44304  ? 163 LEU B O     1 
ATOM   2264 C  CB    . LEU B 1 99  ? 16.77083  -30.94058 -3.20952  1.000 74.90531  ? 163 LEU B CB    1 
ATOM   2265 N  N     . GLY B 1 100 ? 16.79097  -33.86399 -5.50267  1.000 60.63791  ? 164 GLY B N     1 
ATOM   2266 C  CA    . GLY B 1 100 ? 17.44962  -35.13062 -5.75914  1.000 60.31842  ? 164 GLY B CA    1 
ATOM   2267 C  C     . GLY B 1 100 ? 16.97799  -35.77764 -7.05086  1.000 58.79951  ? 164 GLY B C     1 
ATOM   2268 O  O     . GLY B 1 100 ? 17.20560  -35.25730 -8.14495  1.000 59.09830  ? 164 GLY B O     1 
ATOM   2269 N  N     . THR B 1 124 ? 23.44671  -25.96700 13.31969  1.000 66.74641  ? 188 THR B N     1 
ATOM   2270 C  CA    . THR B 1 124 ? 22.70320  -26.59676 12.23101  1.000 64.94699  ? 188 THR B CA    1 
ATOM   2271 C  C     . THR B 1 124 ? 21.20016  -26.60403 12.50062  1.000 63.56366  ? 188 THR B C     1 
ATOM   2272 O  O     . THR B 1 124 ? 20.40474  -26.71267 11.56709  1.000 62.20618  ? 188 THR B O     1 
ATOM   2273 C  CB    . THR B 1 124 ? 23.16645  -28.04628 11.98877  1.000 64.24213  ? 188 THR B CB    1 
ATOM   2274 N  N     . SER B 1 125 ? 20.82544  -26.47841 13.77882  1.000 74.41421  ? 189 SER B N     1 
ATOM   2275 C  CA    . SER B 1 125 ? 19.42478  -26.59092 14.17774  1.000 73.24799  ? 189 SER B CA    1 
ATOM   2276 C  C     . SER B 1 125 ? 18.54930  -25.60154 13.41740  1.000 72.79507  ? 189 SER B C     1 
ATOM   2277 O  O     . SER B 1 125 ? 17.57724  -25.98646 12.75761  1.000 71.25184  ? 189 SER B O     1 
ATOM   2278 C  CB    . SER B 1 125 ? 19.29742  -26.37350 15.68641  1.000 74.19702  ? 189 SER B CB    1 
ATOM   2279 N  N     . GLU B 1 126 ? 18.89261  -24.31644 13.48268  1.000 53.38922  ? 190 GLU B N     1 
ATOM   2280 C  CA    . GLU B 1 126 ? 18.20897  -23.33193 12.65690  1.000 50.97005  ? 190 GLU B CA    1 
ATOM   2281 C  C     . GLU B 1 126 ? 18.69172  -23.35640 11.21473  1.000 58.67106  ? 190 GLU B C     1 
ATOM   2282 O  O     . GLU B 1 126 ? 17.94328  -22.95076 10.31550  1.000 53.46645  ? 190 GLU B O     1 
ATOM   2283 C  CB    . GLU B 1 126 ? 18.39061  -21.92779 13.23764  1.000 54.48344  ? 190 GLU B CB    1 
ATOM   2284 N  N     . LEU B 1 127 ? 19.91560  -23.83218 10.97329  1.000 72.43513  ? 191 LEU B N     1 
ATOM   2285 C  CA    . LEU B 1 127 ? 20.44822  -23.84080 9.61544   1.000 70.27368  ? 191 LEU B CA    1 
ATOM   2286 C  C     . LEU B 1 127 ? 19.61232  -24.72937 8.70130   1.000 74.09205  ? 191 LEU B C     1 
ATOM   2287 O  O     . LEU B 1 127 ? 19.16271  -24.29026 7.63830   1.000 71.71914  ? 191 LEU B O     1 
ATOM   2288 C  CB    . LEU B 1 127 ? 21.90800  -24.29419 9.62774   1.000 74.12134  ? 191 LEU B CB    1 
ATOM   2289 N  N     . ILE B 1 128 ? 19.37170  -25.97826 9.11350   1.000 70.47032  ? 192 ILE B N     1 
ATOM   2290 C  CA    . ILE B 1 128 ? 18.67085  -26.93207 8.25466   1.000 61.38721  ? 192 ILE B CA    1 
ATOM   2291 C  C     . ILE B 1 128 ? 17.23506  -26.48582 8.00610   1.000 60.78741  ? 192 ILE B C     1 
ATOM   2292 O  O     . ILE B 1 128 ? 16.70169  -26.65032 6.90062   1.000 58.23827  ? 192 ILE B O     1 
ATOM   2293 C  CB    . ILE B 1 128 ? 18.72323  -28.34468 8.86511   1.000 50.20649  ? 192 ILE B CB    1 
ATOM   2294 N  N     . GLY B 1 129 ? 16.58310  -25.92469 9.02741   1.000 65.04659  ? 193 GLY B N     1 
ATOM   2295 C  CA    . GLY B 1 129 ? 15.19734  -25.50677 8.86549   1.000 63.77178  ? 193 GLY B CA    1 
ATOM   2296 C  C     . GLY B 1 129 ? 15.02985  -24.41623 7.82424   1.000 63.64880  ? 193 GLY B C     1 
ATOM   2297 O  O     . GLY B 1 129 ? 14.14814  -24.48968 6.96501   1.000 62.95245  ? 193 GLY B O     1 
ATOM   2298 N  N     . GLN B 1 130 ? 15.87980  -23.38872 7.88529   1.000 56.19607  ? 194 GLN B N     1 
ATOM   2299 C  CA    . GLN B 1 130 ? 15.84583  -22.31145 6.90271   1.000 59.71607  ? 194 GLN B CA    1 
ATOM   2300 C  C     . GLN B 1 130 ? 16.46269  -22.71236 5.56807   1.000 55.59267  ? 194 GLN B C     1 
ATOM   2301 O  O     . GLN B 1 130 ? 16.16559  -22.08346 4.54508   1.000 49.52212  ? 194 GLN B O     1 
ATOM   2302 C  CB    . GLN B 1 130 ? 16.56681  -21.07571 7.45306   1.000 63.66170  ? 194 GLN B CB    1 
ATOM   2303 N  N     . PHE B 1 131 ? 17.29881  -23.74809 5.55282   1.000 84.48085  ? 195 PHE B N     1 
ATOM   2304 C  CA    . PHE B 1 131 ? 17.99171  -24.16183 4.34171   1.000 85.07876  ? 195 PHE B CA    1 
ATOM   2305 C  C     . PHE B 1 131 ? 17.08958  -24.95420 3.40370   1.000 79.96433  ? 195 PHE B C     1 
ATOM   2306 O  O     . PHE B 1 131 ? 17.45258  -25.16030 2.24183   1.000 81.36340  ? 195 PHE B O     1 
ATOM   2307 C  CB    . PHE B 1 131 ? 19.21389  -25.00345 4.72737   1.000 89.22574  ? 195 PHE B CB    1 
ATOM   2308 C  CG    . PHE B 1 131 ? 20.38338  -24.86865 3.79449   1.000 87.69546  ? 195 PHE B CG    1 
ATOM   2309 C  CD1   . PHE B 1 131 ? 20.24962  -24.26849 2.55411   1.000 94.82112  ? 195 PHE B CD1   1 
ATOM   2310 C  CD2   . PHE B 1 131 ? 21.63501  -25.31801 4.18414   1.000 87.16978  ? 195 PHE B CD2   1 
ATOM   2311 C  CE1   . PHE B 1 131 ? 21.33777  -24.14095 1.71045   1.000 94.77637  ? 195 PHE B CE1   1 
ATOM   2312 C  CE2   . PHE B 1 131 ? 22.72746  -25.19121 3.34879   1.000 94.94468  ? 195 PHE B CE2   1 
ATOM   2313 C  CZ    . PHE B 1 131 ? 22.57991  -24.60174 2.11022   1.000 100.76987 ? 195 PHE B CZ    1 
ATOM   2314 N  N     . GLY B 1 132 ? 15.92203  -25.38790 3.87392   1.000 46.84972  ? 196 GLY B N     1 
ATOM   2315 C  CA    . GLY B 1 132 ? 15.06742  -26.28965 3.13089   1.000 41.71024  ? 196 GLY B CA    1 
ATOM   2316 C  C     . GLY B 1 132 ? 15.42254  -27.75279 3.27108   1.000 42.18628  ? 196 GLY B C     1 
ATOM   2317 O  O     . GLY B 1 132 ? 14.78279  -28.59524 2.63228   1.000 40.83047  ? 196 GLY B O     1 
ATOM   2318 N  N     . VAL B 1 133 ? 16.41617  -28.08508 4.09223   1.000 42.30780  ? 197 VAL B N     1 
ATOM   2319 C  CA    . VAL B 1 133 ? 16.91966  -29.44498 4.20595   1.000 40.37565  ? 197 VAL B CA    1 
ATOM   2320 C  C     . VAL B 1 133 ? 16.36720  -30.15592 5.43661   1.000 34.51985  ? 197 VAL B C     1 
ATOM   2321 O  O     . VAL B 1 133 ? 16.78053  -31.27963 5.73374   1.000 35.11961  ? 197 VAL B O     1 
ATOM   2322 C  CB    . VAL B 1 133 ? 18.45818  -29.44756 4.22268   1.000 42.84910  ? 197 VAL B CB    1 
ATOM   2323 N  N     . GLY B 1 134 ? 15.43327  -29.52833 6.15606   1.000 37.42299  ? 198 GLY B N     1 
ATOM   2324 C  CA    . GLY B 1 134 ? 15.06106  -30.01771 7.47361   1.000 36.52202  ? 198 GLY B CA    1 
ATOM   2325 C  C     . GLY B 1 134 ? 14.34332  -31.35093 7.46653   1.000 33.89851  ? 198 GLY B C     1 
ATOM   2326 O  O     . GLY B 1 134 ? 14.42752  -32.10326 8.44048   1.000 36.21204  ? 198 GLY B O     1 
ATOM   2327 N  N     . PHE B 1 135 ? 13.63110  -31.66475 6.38112   1.000 25.11923  ? 199 PHE B N     1 
ATOM   2328 C  CA    . PHE B 1 135 ? 12.93296  -32.94392 6.29297   1.000 23.81452  ? 199 PHE B CA    1 
ATOM   2329 C  C     . PHE B 1 135 ? 13.89443  -34.11952 6.44263   1.000 22.51897  ? 199 PHE B C     1 
ATOM   2330 O  O     . PHE B 1 135 ? 13.54341  -35.14596 7.03533   1.000 22.13888  ? 199 PHE B O     1 
ATOM   2331 C  CB    . PHE B 1 135 ? 12.18043  -33.02733 4.96503   1.000 23.38117  ? 199 PHE B CB    1 
ATOM   2332 C  CG    . PHE B 1 135 ? 12.09475  -34.41321 4.39095   1.000 19.69709  ? 199 PHE B CG    1 
ATOM   2333 C  CD1   . PHE B 1 135 ? 11.08627  -35.27728 4.77268   1.000 19.43169  ? 199 PHE B CD1   1 
ATOM   2334 C  CD2   . PHE B 1 135 ? 13.02372  -34.84700 3.44991   1.000 17.73738  ? 199 PHE B CD2   1 
ATOM   2335 C  CE1   . PHE B 1 135 ? 11.00921  -36.55624 4.23212   1.000 21.92181  ? 199 PHE B CE1   1 
ATOM   2336 C  CE2   . PHE B 1 135 ? 12.95965  -36.10755 2.92094   1.000 20.90156  ? 199 PHE B CE2   1 
ATOM   2337 C  CZ    . PHE B 1 135 ? 11.95241  -36.97141 3.30963   1.000 22.10999  ? 199 PHE B CZ    1 
ATOM   2338 N  N     . TYR B 1 136 ? 15.11169  -33.99178 5.91300   1.000 19.54701  ? 200 TYR B N     1 
ATOM   2339 C  CA    . TYR B 1 136 ? 16.07326  -35.08899 5.95169   1.000 23.09124  ? 200 TYR B CA    1 
ATOM   2340 C  C     . TYR B 1 136 ? 16.65028  -35.33086 7.34971   1.000 24.34625  ? 200 TYR B C     1 
ATOM   2341 O  O     . TYR B 1 136 ? 17.42220  -36.28181 7.53278   1.000 26.98251  ? 200 TYR B O     1 
ATOM   2342 C  CB    . TYR B 1 136 ? 17.19711  -34.82164 4.94796   1.000 26.18434  ? 200 TYR B CB    1 
ATOM   2343 C  CG    . TYR B 1 136 ? 16.80582  -35.00010 3.48840   1.000 24.82086  ? 200 TYR B CG    1 
ATOM   2344 C  CD1   . TYR B 1 136 ? 16.82541  -36.25235 2.89537   1.000 26.58439  ? 200 TYR B CD1   1 
ATOM   2345 C  CD2   . TYR B 1 136 ? 16.42174  -33.90709 2.70343   1.000 25.80327  ? 200 TYR B CD2   1 
ATOM   2346 C  CE1   . TYR B 1 136 ? 16.47804  -36.42275 1.56201   1.000 31.25911  ? 200 TYR B CE1   1 
ATOM   2347 C  CE2   . TYR B 1 136 ? 16.06462  -34.07149 1.35521   1.000 26.12737  ? 200 TYR B CE2   1 
ATOM   2348 C  CZ    . TYR B 1 136 ? 16.09617  -35.33455 0.79608   1.000 33.39222  ? 200 TYR B CZ    1 
ATOM   2349 O  OH    . TYR B 1 136 ? 15.74968  -35.53254 -0.53208  1.000 36.48317  ? 200 TYR B OH    1 
ATOM   2350 N  N     . SER B 1 137 ? 16.29694  -34.51277 8.34253   1.000 34.88790  ? 201 SER B N     1 
ATOM   2351 C  CA    . SER B 1 137 ? 16.60107  -34.85294 9.72740   1.000 31.97157  ? 201 SER B CA    1 
ATOM   2352 C  C     . SER B 1 137 ? 15.77317  -36.02940 10.22445  1.000 31.32248  ? 201 SER B C     1 
ATOM   2353 O  O     . SER B 1 137 ? 16.02229  -36.51824 11.33182  1.000 34.71741  ? 201 SER B O     1 
ATOM   2354 C  CB    . SER B 1 137 ? 16.37047  -33.65337 10.65006  1.000 33.27719  ? 201 SER B CB    1 
ATOM   2355 O  OG    . SER B 1 137 ? 14.99147  -33.33499 10.75322  1.000 31.58501  ? 201 SER B OG    1 
ATOM   2356 N  N     . ALA B 1 138 ? 14.78066  -36.47297 9.44894   1.000 30.70340  ? 202 ALA B N     1 
ATOM   2357 C  CA    . ALA B 1 138 ? 14.01244  -37.65674 9.82456   1.000 27.17399  ? 202 ALA B CA    1 
ATOM   2358 C  C     . ALA B 1 138 ? 14.89155  -38.89652 9.87514   1.000 26.49638  ? 202 ALA B C     1 
ATOM   2359 O  O     . ALA B 1 138 ? 14.58093  -39.84610 10.60459  1.000 26.89058  ? 202 ALA B O     1 
ATOM   2360 C  CB    . ALA B 1 138 ? 12.85771  -37.86625 8.83999   1.000 26.37468  ? 202 ALA B CB    1 
ATOM   2361 N  N     . PHE B 1 139 ? 15.99495  -38.90401 9.12060   1.000 19.97167  ? 203 PHE B N     1 
ATOM   2362 C  CA    . PHE B 1 139 ? 16.90921  -40.04235 9.10601   1.000 24.97740  ? 203 PHE B CA    1 
ATOM   2363 C  C     . PHE B 1 139 ? 17.81124  -40.10636 10.33703  1.000 27.23304  ? 203 PHE B C     1 
ATOM   2364 O  O     . PHE B 1 139 ? 18.65393  -41.00697 10.42185  1.000 29.26893  ? 203 PHE B O     1 
ATOM   2365 C  CB    . PHE B 1 139 ? 17.76473  -40.01324 7.83773   1.000 23.83900  ? 203 PHE B CB    1 
ATOM   2366 C  CG    . PHE B 1 139 ? 17.00923  -40.38970 6.59813   1.000 24.70803  ? 203 PHE B CG    1 
ATOM   2367 C  CD1   . PHE B 1 139 ? 16.57915  -41.68846 6.40332   1.000 20.52558  ? 203 PHE B CD1   1 
ATOM   2368 C  CD2   . PHE B 1 139 ? 16.71794  -39.43409 5.63154   1.000 21.54456  ? 203 PHE B CD2   1 
ATOM   2369 C  CE1   . PHE B 1 139 ? 15.87995  -42.03447 5.26707   1.000 21.51774  ? 203 PHE B CE1   1 
ATOM   2370 C  CE2   . PHE B 1 139 ? 16.01653  -39.77156 4.49217   1.000 21.20690  ? 203 PHE B CE2   1 
ATOM   2371 C  CZ    . PHE B 1 139 ? 15.59569  -41.06963 4.30992   1.000 17.95349  ? 203 PHE B CZ    1 
ATOM   2372 N  N     . LEU B 1 140 ? 17.67413  -39.17753 11.28292  1.000 23.86482  ? 204 LEU B N     1 
ATOM   2373 C  CA    . LEU B 1 140 ? 18.35840  -39.33773 12.56055  1.000 25.69691  ? 204 LEU B CA    1 
ATOM   2374 C  C     . LEU B 1 140 ? 17.70184  -40.39697 13.43367  1.000 27.86906  ? 204 LEU B C     1 
ATOM   2375 O  O     . LEU B 1 140 ? 18.35593  -40.94481 14.32661  1.000 27.72962  ? 204 LEU B O     1 
ATOM   2376 C  CB    . LEU B 1 140 ? 18.39396  -38.01082 13.31659  1.000 28.33426  ? 204 LEU B CB    1 
ATOM   2377 C  CG    . LEU B 1 140 ? 19.12907  -36.85241 12.65262  1.000 29.82380  ? 204 LEU B CG    1 
ATOM   2378 C  CD1   . LEU B 1 140 ? 18.74682  -35.55745 13.34678  1.000 26.01229  ? 204 LEU B CD1   1 
ATOM   2379 C  CD2   . LEU B 1 140 ? 20.63952  -37.08191 12.69354  1.000 33.68787  ? 204 LEU B CD2   1 
ATOM   2380 N  N     . VAL B 1 141 ? 16.42410  -40.68610 13.20648  1.000 31.85949  ? 205 VAL B N     1 
ATOM   2381 C  CA    . VAL B 1 141 ? 15.70015  -41.67535 13.99525  1.000 28.77370  ? 205 VAL B CA    1 
ATOM   2382 C  C     . VAL B 1 141 ? 15.09689  -42.77954 13.14244  1.000 23.91756  ? 205 VAL B C     1 
ATOM   2383 O  O     . VAL B 1 141 ? 14.53911  -43.73171 13.70064  1.000 26.24345  ? 205 VAL B O     1 
ATOM   2384 C  CB    . VAL B 1 141 ? 14.59665  -41.00978 14.84703  1.000 28.18432  ? 205 VAL B CB    1 
ATOM   2385 C  CG1   . VAL B 1 141 ? 15.19553  -39.99236 15.79840  1.000 29.25463  ? 205 VAL B CG1   1 
ATOM   2386 C  CG2   . VAL B 1 141 ? 13.57526  -40.35121 13.94035  1.000 27.46325  ? 205 VAL B CG2   1 
ATOM   2387 N  N     . ALA B 1 142 ? 15.17634  -42.68927 11.81704  1.000 22.89044  ? 206 ALA B N     1 
ATOM   2388 C  CA    . ALA B 1 142 ? 14.49738  -43.62480 10.93274  1.000 25.81016  ? 206 ALA B CA    1 
ATOM   2389 C  C     . ALA B 1 142 ? 15.48712  -44.21221 9.94460   1.000 20.73478  ? 206 ALA B C     1 
ATOM   2390 O  O     . ALA B 1 142 ? 16.24315  -43.47519 9.30798   1.000 23.26336  ? 206 ALA B O     1 
ATOM   2391 C  CB    . ALA B 1 142 ? 13.34545  -42.94311 10.18634  1.000 18.03413  ? 206 ALA B CB    1 
ATOM   2392 N  N     . ASP B 1 143 ? 15.48059  -45.53881 9.82388   1.000 21.40273  ? 207 ASP B N     1 
ATOM   2393 C  CA    . ASP B 1 143 ? 16.27856  -46.21777 8.81250   1.000 22.72517  ? 207 ASP B CA    1 
ATOM   2394 C  C     . ASP B 1 143 ? 15.68298  -46.09645 7.41804   1.000 20.89424  ? 207 ASP B C     1 
ATOM   2395 O  O     . ASP B 1 143 ? 16.38157  -46.36427 6.42931   1.000 22.94666  ? 207 ASP B O     1 
ATOM   2396 C  CB    . ASP B 1 143 ? 16.42214  -47.70069 9.16464   1.000 27.18838  ? 207 ASP B CB    1 
ATOM   2397 C  CG    . ASP B 1 143 ? 17.45145  -47.94418 10.24231  1.000 26.71239  ? 207 ASP B CG    1 
ATOM   2398 O  OD1   . ASP B 1 143 ? 18.52438  -47.29328 10.20681  1.000 32.46311  ? 207 ASP B OD1   1 
ATOM   2399 O  OD2   . ASP B 1 143 ? 17.19345  -48.79446 11.11356  1.000 25.19110  ? 207 ASP B OD2   1 
ATOM   2400 N  N     . LYS B 1 144 ? 14.41060  -45.71511 7.32454   1.000 24.52026  ? 208 LYS B N     1 
ATOM   2401 C  CA    . LYS B 1 144 ? 13.67974  -45.61813 6.07098   1.000 19.52541  ? 208 LYS B CA    1 
ATOM   2402 C  C     . LYS B 1 144 ? 12.59993  -44.57414 6.26171   1.000 18.21710  ? 208 LYS B C     1 
ATOM   2403 O  O     . LYS B 1 144 ? 11.92296  -44.56271 7.29246   1.000 20.88100  ? 208 LYS B O     1 
ATOM   2404 C  CB    . LYS B 1 144 ? 13.02168  -46.95142 5.68321   1.000 21.84859  ? 208 LYS B CB    1 
ATOM   2405 C  CG    . LYS B 1 144 ? 12.89372  -47.21500 4.18829   1.000 22.06373  ? 208 LYS B CG    1 
ATOM   2406 C  CD    . LYS B 1 144 ? 13.02395  -48.72130 3.92736   1.000 25.76127  ? 208 LYS B CD    1 
ATOM   2407 C  CE    . LYS B 1 144 ? 12.84160  -49.06523 2.46507   1.000 22.78276  ? 208 LYS B CE    1 
ATOM   2408 N  NZ    . LYS B 1 144 ? 11.77619  -48.20687 1.87006   1.000 26.40341  ? 208 LYS B NZ    1 
ATOM   2409 N  N     . VAL B 1 145 ? 12.43844  -43.70200 5.27562   1.000 17.89357  ? 209 VAL B N     1 
ATOM   2410 C  CA    . VAL B 1 145 ? 11.37787  -42.70532 5.27908   1.000 14.65631  ? 209 VAL B CA    1 
ATOM   2411 C  C     . VAL B 1 145 ? 10.53032  -42.93311 4.04071   1.000 15.29308  ? 209 VAL B C     1 
ATOM   2412 O  O     . VAL B 1 145 ? 11.06776  -43.08689 2.93704   1.000 17.51685  ? 209 VAL B O     1 
ATOM   2413 C  CB    . VAL B 1 145 ? 11.94173  -41.27480 5.31378   1.000 15.85218  ? 209 VAL B CB    1 
ATOM   2414 C  CG1   . VAL B 1 145 ? 10.81129  -40.23513 5.28357   1.000 16.89778  ? 209 VAL B CG1   1 
ATOM   2415 C  CG2   . VAL B 1 145 ? 12.79748  -41.09745 6.53320   1.000 18.74962  ? 209 VAL B CG2   1 
ATOM   2416 N  N     A ILE B 1 146 ? 9.21022   -42.94676 4.21652   0.443 12.74794  ? 210 ILE B N     1 
ATOM   2417 N  N     B ILE B 1 146 ? 9.21800   -43.02728 4.23882   0.557 12.61166  ? 210 ILE B N     1 
ATOM   2418 C  CA    A ILE B 1 146 ? 8.26781   -43.15626 3.11920   0.443 13.65096  ? 210 ILE B CA    1 
ATOM   2419 C  CA    B ILE B 1 146 ? 8.24903   -43.13881 3.15452   0.557 13.64673  ? 210 ILE B CA    1 
ATOM   2420 C  C     A ILE B 1 146 ? 7.31155   -41.97205 3.07184   0.443 11.94248  ? 210 ILE B C     1 
ATOM   2421 C  C     B ILE B 1 146 ? 7.45020   -41.84602 3.12042   0.557 11.90920  ? 210 ILE B C     1 
ATOM   2422 O  O     A ILE B 1 146 ? 6.63282   -41.67409 4.06086   0.443 11.71289  ? 210 ILE B O     1 
ATOM   2423 O  O     B ILE B 1 146 ? 7.05697   -41.32441 4.17037   0.557 10.01692  ? 210 ILE B O     1 
ATOM   2424 C  CB    A ILE B 1 146 ? 7.50495   -44.48092 3.27424   0.443 14.13432  ? 210 ILE B CB    1 
ATOM   2425 C  CB    B ILE B 1 146 ? 7.32819   -44.36107 3.33297   0.557 14.12915  ? 210 ILE B CB    1 
ATOM   2426 C  CG1   A ILE B 1 146 ? 8.48494   -45.65389 3.26128   0.443 14.01842  ? 210 ILE B CG1   1 
ATOM   2427 C  CG1   B ILE B 1 146 ? 8.10418   -45.66552 3.11702   0.557 13.29086  ? 210 ILE B CG1   1 
ATOM   2428 C  CG2   A ILE B 1 146 ? 6.48929   -44.65399 2.15648   0.443 12.71619  ? 210 ILE B CG2   1 
ATOM   2429 C  CG2   B ILE B 1 146 ? 6.15870   -44.29924 2.36231   0.557 12.77552  ? 210 ILE B CG2   1 
ATOM   2430 C  CD1   A ILE B 1 146 ? 7.86377   -46.93976 3.66496   0.443 14.16309  ? 210 ILE B CD1   1 
ATOM   2431 C  CD1   B ILE B 1 146 ? 8.54110   -46.31834 4.40150   0.557 15.24360  ? 210 ILE B CD1   1 
ATOM   2432 N  N     . VAL B 1 147 ? 7.25576   -41.30024 1.92602   1.000 14.44759  ? 211 VAL B N     1 
ATOM   2433 C  CA    . VAL B 1 147 ? 6.41386   -40.12878 1.73080   1.000 11.55502  ? 211 VAL B CA    1 
ATOM   2434 C  C     . VAL B 1 147 ? 5.28094   -40.53575 0.78742   1.000 18.33114  ? 211 VAL B C     1 
ATOM   2435 O  O     . VAL B 1 147 ? 5.52278   -40.92928 -0.36543  1.000 14.96371  ? 211 VAL B O     1 
ATOM   2436 C  CB    . VAL B 1 147 ? 7.21704   -38.94293 1.17727   1.000 13.41781  ? 211 VAL B CB    1 
ATOM   2437 C  CG1   . VAL B 1 147 ? 6.32749   -37.73411 0.98146   1.000 10.50515  ? 211 VAL B CG1   1 
ATOM   2438 C  CG2   . VAL B 1 147 ? 8.35489   -38.59314 2.11117   1.000 13.08687  ? 211 VAL B CG2   1 
ATOM   2439 N  N     . THR B 1 148 ? 4.05071   -40.48484 1.29386   1.000 13.67061  ? 212 THR B N     1 
ATOM   2440 C  CA    . THR B 1 148 ? 2.84890   -40.73314 0.50905   1.000 14.63478  ? 212 THR B CA    1 
ATOM   2441 C  C     . THR B 1 148 ? 2.19483   -39.37409 0.29317   1.000 12.68392  ? 212 THR B C     1 
ATOM   2442 O  O     . THR B 1 148 ? 1.96592   -38.64579 1.25371   1.000 13.73522  ? 212 THR B O     1 
ATOM   2443 C  CB    . THR B 1 148 ? 1.91284   -41.70290 1.23738   1.000 12.82872  ? 212 THR B CB    1 
ATOM   2444 O  OG1   . THR B 1 148 ? 2.57091   -42.97952 1.43595   1.000 10.69071  ? 212 THR B OG1   1 
ATOM   2445 C  CG2   . THR B 1 148 ? 0.65664   -41.93754 0.41056   1.000 14.70359  ? 212 THR B CG2   1 
ATOM   2446 N  N     . SER B 1 149 ? 1.94514   -38.99685 -0.95813  1.000 16.68294  ? 213 SER B N     1 
ATOM   2447 C  CA    . SER B 1 149 ? 1.48376   -37.63462 -1.17014  1.000 17.97363  ? 213 SER B CA    1 
ATOM   2448 C  C     . SER B 1 149 ? 0.49783   -37.58818 -2.32119  1.000 15.86751  ? 213 SER B C     1 
ATOM   2449 O  O     . SER B 1 149 ? 0.66090   -38.29384 -3.32289  1.000 16.71994  ? 213 SER B O     1 
ATOM   2450 C  CB    . SER B 1 149 ? 2.64678   -36.66313 -1.43644  1.000 17.08660  ? 213 SER B CB    1 
ATOM   2451 O  OG    . SER B 1 149 ? 2.20375   -35.31089 -1.40478  1.000 16.64063  ? 213 SER B OG    1 
ATOM   2452 N  N     . LYS B 1 150 ? -0.51319  -36.73222 -2.16278  1.000 10.30697  ? 214 LYS B N     1 
ATOM   2453 C  CA    . LYS B 1 150 ? -1.52216  -36.49418 -3.18170  1.000 9.13051   ? 214 LYS B CA    1 
ATOM   2454 C  C     . LYS B 1 150 ? -1.69558  -34.99270 -3.36251  1.000 11.16446  ? 214 LYS B C     1 
ATOM   2455 O  O     . LYS B 1 150 ? -1.99756  -34.26533 -2.40362  1.000 13.20625  ? 214 LYS B O     1 
ATOM   2456 C  CB    . LYS B 1 150 ? -2.84922  -37.14264 -2.81262  1.000 8.53584   ? 214 LYS B CB    1 
ATOM   2457 C  CG    . LYS B 1 150 ? -3.97151  -36.67968 -3.71862  1.000 11.43434  ? 214 LYS B CG    1 
ATOM   2458 C  CD    . LYS B 1 150 ? -4.15520  -37.60306 -4.91148  1.000 12.39549  ? 214 LYS B CD    1 
ATOM   2459 C  CE    . LYS B 1 150 ? -5.33341  -37.15233 -5.78481  1.000 8.81455   ? 214 LYS B CE    1 
ATOM   2460 N  NZ    . LYS B 1 150 ? -5.13624  -35.81528 -6.40243  1.000 12.82513  ? 214 LYS B NZ    1 
ATOM   2461 N  N     . HIS B 1 151 ? -1.49471  -34.54018 -4.59046  1.000 15.01528  ? 215 HIS B N     1 
ATOM   2462 C  CA    . HIS B 1 151 ? -1.68670  -33.16769 -5.01114  1.000 16.39978  ? 215 HIS B CA    1 
ATOM   2463 C  C     . HIS B 1 151 ? -2.92943  -33.10413 -5.89328  1.000 19.28016  ? 215 HIS B C     1 
ATOM   2464 O  O     . HIS B 1 151 ? -3.29263  -34.09081 -6.53714  1.000 15.76315  ? 215 HIS B O     1 
ATOM   2465 C  CB    . HIS B 1 151 ? -0.45802  -32.68923 -5.78016  1.000 14.84812  ? 215 HIS B CB    1 
ATOM   2466 C  CG    . HIS B 1 151 ? -0.46967  -31.23151 -6.09958  1.000 16.64584  ? 215 HIS B CG    1 
ATOM   2467 N  ND1   . HIS B 1 151 ? -1.08270  -30.72382 -7.22188  1.000 16.23974  ? 215 HIS B ND1   1 
ATOM   2468 C  CD2   . HIS B 1 151 ? 0.09187   -30.17513 -5.46726  1.000 17.03828  ? 215 HIS B CD2   1 
ATOM   2469 C  CE1   . HIS B 1 151 ? -0.91042  -29.41671 -7.26138  1.000 12.20078  ? 215 HIS B CE1   1 
ATOM   2470 N  NE2   . HIS B 1 151 ? -0.21002  -29.05527 -6.20165  1.000 16.31850  ? 215 HIS B NE2   1 
ATOM   2471 N  N     . ASN B 1 152 ? -3.58433  -31.93845 -5.91747  1.000 17.31210  ? 216 ASN B N     1 
ATOM   2472 C  CA    . ASN B 1 152 ? -4.81347  -31.79089 -6.69689  1.000 15.42483  ? 216 ASN B CA    1 
ATOM   2473 C  C     . ASN B 1 152 ? -4.59305  -32.08692 -8.17677  1.000 16.93948  ? 216 ASN B C     1 
ATOM   2474 O  O     . ASN B 1 152 ? -5.52069  -32.53389 -8.86823  1.000 20.46082  ? 216 ASN B O     1 
ATOM   2475 C  CB    . ASN B 1 152 ? -5.37412  -30.37600 -6.51866  1.000 18.47727  ? 216 ASN B CB    1 
ATOM   2476 C  CG    . ASN B 1 152 ? -6.11401  -30.19790 -5.20111  1.000 19.64457  ? 216 ASN B CG    1 
ATOM   2477 O  OD1   . ASN B 1 152 ? -6.51659  -31.16753 -4.56815  1.000 17.46125  ? 216 ASN B OD1   1 
ATOM   2478 N  ND2   . ASN B 1 152 ? -6.29671  -28.95192 -4.78700  1.000 18.26107  ? 216 ASN B ND2   1 
ATOM   2479 N  N     . ASN B 1 153 ? -3.37299  -31.87808 -8.67964  1.000 14.92526  ? 217 ASN B N     1 
ATOM   2480 C  CA    . ASN B 1 153 ? -3.07165  -31.99436 -10.10163 1.000 15.35203  ? 217 ASN B CA    1 
ATOM   2481 C  C     . ASN B 1 153 ? -2.42940  -33.31836 -10.48722 1.000 17.58276  ? 217 ASN B C     1 
ATOM   2482 O  O     . ASN B 1 153 ? -1.84370  -33.40604 -11.57122 1.000 17.73039  ? 217 ASN B O     1 
ATOM   2483 C  CB    . ASN B 1 153 ? -2.13010  -30.87820 -10.54194 1.000 15.88199  ? 217 ASN B CB    1 
ATOM   2484 C  CG    . ASN B 1 153 ? -2.73663  -29.51474 -10.42446 1.000 20.41765  ? 217 ASN B CG    1 
ATOM   2485 O  OD1   . ASN B 1 153 ? -3.95346  -29.35759 -10.26769 1.000 23.60442  ? 217 ASN B OD1   1 
ATOM   2486 N  ND2   . ASN B 1 153 ? -1.89323  -28.49986 -10.56479 1.000 18.09223  ? 217 ASN B ND2   1 
ATOM   2487 N  N     . ASP B 1 154 ? -2.50374  -34.34271 -9.64327  1.000 12.14926  ? 218 ASP B N     1 
ATOM   2488 C  CA    . ASP B 1 154 ? -1.74463  -35.55159 -9.93116  1.000 10.47761  ? 218 ASP B CA    1 
ATOM   2489 C  C     . ASP B 1 154 ? -2.28047  -36.69009 -9.07700  1.000 11.48640  ? 218 ASP B C     1 
ATOM   2490 O  O     . ASP B 1 154 ? -2.98971  -36.48391 -8.08399  1.000 12.81296  ? 218 ASP B O     1 
ATOM   2491 C  CB    . ASP B 1 154 ? -0.24378  -35.32559 -9.66922  1.000 12.50732  ? 218 ASP B CB    1 
ATOM   2492 C  CG    . ASP B 1 154 ? 0.66670   -36.32020 -10.40638 1.000 17.14187  ? 218 ASP B CG    1 
ATOM   2493 O  OD1   . ASP B 1 154 ? 0.17985   -37.31528 -11.02137 1.000 16.08003  ? 218 ASP B OD1   1 
ATOM   2494 O  OD2   . ASP B 1 154 ? 1.90119   -36.09052 -10.37197 1.000 12.25932  ? 218 ASP B OD2   1 
ATOM   2495 N  N     . THR B 1 155 ? -1.91963  -37.89738 -9.46214  1.000 12.32184  ? 219 THR B N     1 
ATOM   2496 C  CA    . THR B 1 155 ? -2.33831  -39.04528 -8.68155  1.000 9.20603   ? 219 THR B CA    1 
ATOM   2497 C  C     . THR B 1 155 ? -1.47067  -39.19456 -7.44057  1.000 12.46263  ? 219 THR B C     1 
ATOM   2498 O  O     . THR B 1 155 ? -0.41415  -38.55819 -7.30121  1.000 13.61326  ? 219 THR B O     1 
ATOM   2499 C  CB    . THR B 1 155 ? -2.27724  -40.30674 -9.53306  1.000 14.63532  ? 219 THR B CB    1 
ATOM   2500 O  OG1   . THR B 1 155 ? -0.97482  -40.39444 -10.14271 1.000 11.71479  ? 219 THR B OG1   1 
ATOM   2501 C  CG2   . THR B 1 155 ? -3.37469  -40.25441 -10.61085 1.000 11.40624  ? 219 THR B CG2   1 
ATOM   2502 N  N     . GLN B 1 156 ? -1.96647  -40.00124 -6.50261  1.000 14.03639  ? 220 GLN B N     1 
ATOM   2503 C  CA    . GLN B 1 156 ? -1.21903  -40.30292 -5.29606  1.000 10.35944  ? 220 GLN B CA    1 
ATOM   2504 C  C     . GLN B 1 156 ? 0.02697   -41.10648 -5.61990  1.000 13.61120  ? 220 GLN B C     1 
ATOM   2505 O  O     . GLN B 1 156 ? -0.01479  -42.04859 -6.41740  1.000 14.03835  ? 220 GLN B O     1 
ATOM   2506 C  CB    . GLN B 1 156 ? -2.09936  -41.06339 -4.30462  1.000 12.84055  ? 220 GLN B CB    1 
ATOM   2507 C  CG    . GLN B 1 156 ? -1.59232  -41.02280 -2.86675  1.000 9.49431   ? 220 GLN B CG    1 
ATOM   2508 C  CD    . GLN B 1 156 ? -2.62230  -41.49162 -1.86391  1.000 15.38694  ? 220 GLN B CD    1 
ATOM   2509 O  OE1   . GLN B 1 156 ? -3.68398  -40.86395 -1.72081  1.000 15.39724  ? 220 GLN B OE1   1 
ATOM   2510 N  NE2   . GLN B 1 156 ? -2.30566  -42.56458 -1.12487  1.000 9.51255   ? 220 GLN B NE2   1 
ATOM   2511 N  N     . HIS B 1 157 ? 1.13664   -40.74373 -4.97316  1.000 14.10129  ? 221 HIS B N     1 
ATOM   2512 C  CA    . HIS B 1 157 ? 2.41914   -41.38628 -5.20734  1.000 16.01650  ? 221 HIS B CA    1 
ATOM   2513 C  C     . HIS B 1 157 ? 3.09208   -41.70147 -3.87949  1.000 16.95913  ? 221 HIS B C     1 
ATOM   2514 O  O     . HIS B 1 157 ? 2.79104   -41.10612 -2.84670  1.000 15.24811  ? 221 HIS B O     1 
ATOM   2515 C  CB    . HIS B 1 157 ? 3.35410   -40.51510 -6.05667  1.000 14.18338  ? 221 HIS B CB    1 
ATOM   2516 C  CG    . HIS B 1 157 ? 3.01300   -40.51992 -7.51310  1.000 13.54350  ? 221 HIS B CG    1 
ATOM   2517 N  ND1   . HIS B 1 157 ? 2.09971   -39.64437 -8.06108  1.000 14.90453  ? 221 HIS B ND1   1 
ATOM   2518 C  CD2   . HIS B 1 157 ? 3.41741   -41.32338 -8.52267  1.000 11.22998  ? 221 HIS B CD2   1 
ATOM   2519 C  CE1   . HIS B 1 157 ? 1.97149   -39.89844 -9.35092  1.000 16.10858  ? 221 HIS B CE1   1 
ATOM   2520 N  NE2   . HIS B 1 157 ? 2.76023   -40.91233 -9.65509  1.000 14.78377  ? 221 HIS B NE2   1 
ATOM   2521 N  N     . ILE B 1 158 ? 4.01200   -42.65986 -3.93120  1.000 13.08065  ? 222 ILE B N     1 
ATOM   2522 C  CA    . ILE B 1 158 ? 4.80048   -43.07373 -2.78561  1.000 12.38598  ? 222 ILE B CA    1 
ATOM   2523 C  C     . ILE B 1 158 ? 6.26865   -42.87461 -3.13110  1.000 16.90520  ? 222 ILE B C     1 
ATOM   2524 O  O     . ILE B 1 158 ? 6.74426   -43.39189 -4.14897  1.000 14.73867  ? 222 ILE B O     1 
ATOM   2525 C  CB    . ILE B 1 158 ? 4.52838   -44.54142 -2.41434  1.000 12.12805  ? 222 ILE B CB    1 
ATOM   2526 C  CG1   . ILE B 1 158 ? 3.04355   -44.74511 -2.04547  1.000 14.37080  ? 222 ILE B CG1   1 
ATOM   2527 C  CG2   . ILE B 1 158 ? 5.45373   -44.96529 -1.27181  1.000 11.83328  ? 222 ILE B CG2   1 
ATOM   2528 C  CD1   . ILE B 1 158 ? 2.62840   -46.21198 -1.87706  1.000 9.77101   ? 222 ILE B CD1   1 
ATOM   2529 N  N     . TRP B 1 159 ? 6.97738   -42.13024 -2.28191  1.000 15.64152  ? 223 TRP B N     1 
ATOM   2530 C  CA    . TRP B 1 159 ? 8.42554   -41.95620 -2.34545  1.000 14.77924  ? 223 TRP B CA    1 
ATOM   2531 C  C     . TRP B 1 159 ? 9.05578   -42.72806 -1.19102  1.000 16.31072  ? 223 TRP B C     1 
ATOM   2532 O  O     . TRP B 1 159 ? 8.57957   -42.64936 -0.05503  1.000 16.93591  ? 223 TRP B O     1 
ATOM   2533 C  CB    . TRP B 1 159 ? 8.74951   -40.45834 -2.27468  1.000 14.31606  ? 223 TRP B CB    1 
ATOM   2534 C  CG    . TRP B 1 159 ? 10.19041  -40.01260 -2.12955  1.000 18.02533  ? 223 TRP B CG    1 
ATOM   2535 C  CD1   . TRP B 1 159 ? 10.95936  -39.41134 -3.08677  1.000 19.83845  ? 223 TRP B CD1   1 
ATOM   2536 C  CD2   . TRP B 1 159 ? 10.98914  -40.03741 -0.93256  1.000 19.48080  ? 223 TRP B CD2   1 
ATOM   2537 N  NE1   . TRP B 1 159 ? 12.19566  -39.08923 -2.56783  1.000 18.93913  ? 223 TRP B NE1   1 
ATOM   2538 C  CE2   . TRP B 1 159 ? 12.24224  -39.47388 -1.25281  1.000 20.55759  ? 223 TRP B CE2   1 
ATOM   2539 C  CE3   . TRP B 1 159 ? 10.77669  -40.50950 0.36570   1.000 19.70381  ? 223 TRP B CE3   1 
ATOM   2540 C  CZ2   . TRP B 1 159 ? 13.27650  -39.36388 -0.31826  1.000 23.91413  ? 223 TRP B CZ2   1 
ATOM   2541 C  CZ3   . TRP B 1 159 ? 11.80629  -40.39510 1.29783   1.000 20.92408  ? 223 TRP B CZ3   1 
ATOM   2542 C  CH2   . TRP B 1 159 ? 13.03715  -39.82153 0.95058   1.000 19.23418  ? 223 TRP B CH2   1 
ATOM   2543 N  N     . GLU B 1 160 ? 10.09270  -43.50020 -1.47657  1.000 20.48272  ? 224 GLU B N     1 
ATOM   2544 C  CA    . GLU B 1 160 ? 10.77158  -44.28490 -0.45364  1.000 20.82503  ? 224 GLU B CA    1 
ATOM   2545 C  C     . GLU B 1 160 ? 12.27522  -44.08051 -0.54122  1.000 23.51985  ? 224 GLU B C     1 
ATOM   2546 O  O     . GLU B 1 160 ? 12.82347  -43.93302 -1.63740  1.000 25.73107  ? 224 GLU B O     1 
ATOM   2547 C  CB    . GLU B 1 160 ? 10.39070  -45.77936 -0.58362  1.000 24.27600  ? 224 GLU B CB    1 
ATOM   2548 C  CG    . GLU B 1 160 ? 11.10849  -46.58295 -1.69285  1.000 26.10924  ? 224 GLU B CG    1 
ATOM   2549 C  CD    . GLU B 1 160 ? 12.52745  -47.04508 -1.35806  1.000 32.85396  ? 224 GLU B CD    1 
ATOM   2550 O  OE1   . GLU B 1 160 ? 12.78675  -47.42350 -0.19798  1.000 32.07057  ? 224 GLU B OE1   1 
ATOM   2551 O  OE2   . GLU B 1 160 ? 13.38351  -47.04365 -2.28476  1.000 34.13346  ? 224 GLU B OE2   1 
ATOM   2552 N  N     . SER B 1 161 ? 12.93972  -44.05846 0.61545   1.000 29.86102  ? 225 SER B N     1 
ATOM   2553 C  CA    . SER B 1 161 ? 14.39094  -43.94078 0.62029   1.000 29.03629  ? 225 SER B CA    1 
ATOM   2554 C  C     . SER B 1 161 ? 14.96635  -44.37191 1.95874   1.000 30.32091  ? 225 SER B C     1 
ATOM   2555 O  O     . SER B 1 161 ? 14.30417  -44.29097 2.99575   1.000 30.14489  ? 225 SER B O     1 
ATOM   2556 C  CB    . SER B 1 161 ? 14.84255  -42.51791 0.32173   1.000 28.83367  ? 225 SER B CB    1 
ATOM   2557 O  OG    . SER B 1 161 ? 16.23499  -42.40095 0.52371   1.000 33.42353  ? 225 SER B OG    1 
ATOM   2558 N  N     . ASP B 1 162 ? 16.22485  -44.80825 1.91198   1.000 41.20190  ? 226 ASP B N     1 
ATOM   2559 C  CA    . ASP B 1 162 ? 17.03058  -45.09977 3.08970   1.000 42.01320  ? 226 ASP B CA    1 
ATOM   2560 C  C     . ASP B 1 162 ? 18.22590  -44.15979 3.22415   1.000 41.28895  ? 226 ASP B C     1 
ATOM   2561 O  O     . ASP B 1 162 ? 19.13542  -44.43724 4.01364   1.000 45.46856  ? 226 ASP B O     1 
ATOM   2562 C  CB    . ASP B 1 162 ? 17.48926  -46.56145 3.05841   1.000 39.21803  ? 226 ASP B CB    1 
ATOM   2563 C  CG    . ASP B 1 162 ? 18.53063  -46.84885 1.95983   1.000 40.01549  ? 226 ASP B CG    1 
ATOM   2564 O  OD1   . ASP B 1 162 ? 18.96144  -45.91848 1.23389   1.000 40.02231  ? 226 ASP B OD1   1 
ATOM   2565 O  OD2   . ASP B 1 162 ? 18.91766  -48.03661 1.82192   1.000 40.81039  ? 226 ASP B OD2   1 
ATOM   2566 N  N     . SER B 1 163 ? 18.22679  -43.05227 2.48118   1.000 39.47932  ? 227 SER B N     1 
ATOM   2567 C  CA    . SER B 1 163 ? 19.27376  -42.03529 2.32132   1.000 41.34529  ? 227 SER B CA    1 
ATOM   2568 C  C     . SER B 1 163 ? 20.36385  -42.43606 1.32436   1.000 46.90414  ? 227 SER B C     1 
ATOM   2569 O  O     . SER B 1 163 ? 21.23076  -41.59974 1.03688   1.000 48.38932  ? 227 SER B O     1 
ATOM   2570 C  CB    . SER B 1 163 ? 19.94836  -41.64453 3.64915   1.000 40.36883  ? 227 SER B CB    1 
ATOM   2571 N  N     . ASN B 1 164 ? 20.34028  -43.64534 0.75656   1.000 39.78840  ? 228 ASN B N     1 
ATOM   2572 C  CA    . ASN B 1 164 ? 21.33725  -44.02278 -0.24591  1.000 42.46382  ? 228 ASN B CA    1 
ATOM   2573 C  C     . ASN B 1 164 ? 20.82870  -43.74297 -1.65978  1.000 42.93254  ? 228 ASN B C     1 
ATOM   2574 O  O     . ASN B 1 164 ? 21.43333  -42.96697 -2.40723  1.000 47.84504  ? 228 ASN B O     1 
ATOM   2575 C  CB    . ASN B 1 164 ? 21.71764  -45.50333 -0.09613  1.000 47.01772  ? 228 ASN B CB    1 
ATOM   2576 C  CG    . ASN B 1 164 ? 22.48697  -45.79214 1.19278   1.000 50.47964  ? 228 ASN B CG    1 
ATOM   2577 O  OD1   . ASN B 1 164 ? 23.22736  -44.94394 1.69668   1.000 48.87231  ? 228 ASN B OD1   1 
ATOM   2578 N  ND2   . ASN B 1 164 ? 22.31617  -47.00193 1.72671   1.000 54.74841  ? 228 ASN B ND2   1 
ATOM   2579 N  N     . GLU B 1 165 ? 19.72505  -44.37537 -2.03506  1.000 45.04469  ? 229 GLU B N     1 
ATOM   2580 C  CA    . GLU B 1 165 ? 18.97709  -44.07580 -3.24620  1.000 44.82355  ? 229 GLU B CA    1 
ATOM   2581 C  C     . GLU B 1 165 ? 17.53048  -43.77752 -2.85014  1.000 42.10189  ? 229 GLU B C     1 
ATOM   2582 O  O     . GLU B 1 165 ? 17.19476  -43.70857 -1.66651  1.000 38.83122  ? 229 GLU B O     1 
ATOM   2583 C  CB    . GLU B 1 165 ? 19.08049  -45.22791 -4.25485  1.000 43.34193  ? 229 GLU B CB    1 
ATOM   2584 C  CG    . GLU B 1 165 ? 19.19888  -46.62493 -3.64673  1.000 49.22774  ? 229 GLU B CG    1 
ATOM   2585 C  CD    . GLU B 1 165 ? 19.83558  -47.63714 -4.60859  1.000 64.04416  ? 229 GLU B CD    1 
ATOM   2586 O  OE1   . GLU B 1 165 ? 21.07293  -47.82105 -4.56491  1.000 63.75966  ? 229 GLU B OE1   1 
ATOM   2587 O  OE2   . GLU B 1 165 ? 19.09787  -48.25792 -5.40849  1.000 65.66621  ? 229 GLU B OE2   1 
ATOM   2588 N  N     . PHE B 1 166 ? 16.67100  -43.58938 -3.84917  1.000 33.49554  ? 230 PHE B N     1 
ATOM   2589 C  CA    . PHE B 1 166 ? 15.24944  -43.41696 -3.59500  1.000 22.68707  ? 230 PHE B CA    1 
ATOM   2590 C  C     . PHE B 1 166 ? 14.46882  -43.84045 -4.82550  1.000 26.94535  ? 230 PHE B C     1 
ATOM   2591 O  O     . PHE B 1 166 ? 15.01211  -43.93627 -5.92832  1.000 26.12118  ? 230 PHE B O     1 
ATOM   2592 C  CB    . PHE B 1 166 ? 14.91424  -41.97495 -3.19546  1.000 27.40125  ? 230 PHE B CB    1 
ATOM   2593 C  CG    . PHE B 1 166 ? 14.99640  -40.97434 -4.32329  1.000 25.77278  ? 230 PHE B CG    1 
ATOM   2594 C  CD1   . PHE B 1 166 ? 16.18941  -40.33301 -4.60820  1.000 30.16146  ? 230 PHE B CD1   1 
ATOM   2595 C  CD2   . PHE B 1 166 ? 13.87654  -40.65253 -5.07650  1.000 25.04923  ? 230 PHE B CD2   1 
ATOM   2596 C  CE1   . PHE B 1 166 ? 16.27579  -39.40154 -5.63298  1.000 28.89919  ? 230 PHE B CE1   1 
ATOM   2597 C  CE2   . PHE B 1 166 ? 13.95614  -39.72085 -6.10762  1.000 24.53472  ? 230 PHE B CE2   1 
ATOM   2598 C  CZ    . PHE B 1 166 ? 15.15903  -39.09427 -6.38338  1.000 24.79956  ? 230 PHE B CZ    1 
ATOM   2599 N  N     . SER B 1 167 ? 13.18189  -44.10790 -4.62622  1.000 27.10828  ? 231 SER B N     1 
ATOM   2600 C  CA    . SER B 1 167 ? 12.30366  -44.40521 -5.74691  1.000 24.44620  ? 231 SER B CA    1 
ATOM   2601 C  C     . SER B 1 167 ? 10.96517  -43.71781 -5.53107  1.000 20.71975  ? 231 SER B C     1 
ATOM   2602 O  O     . SER B 1 167 ? 10.62867  -43.30334 -4.41867  1.000 20.66960  ? 231 SER B O     1 
ATOM   2603 C  CB    . SER B 1 167 ? 12.12689  -45.91625 -5.94346  1.000 27.41565  ? 231 SER B CB    1 
ATOM   2604 O  OG    . SER B 1 167 ? 11.49847  -46.50246 -4.82965  1.000 25.55146  ? 231 SER B OG    1 
ATOM   2605 N  N     . VAL B 1 168 ? 10.21998  -43.56257 -6.62450  1.000 17.56214  ? 232 VAL B N     1 
ATOM   2606 C  CA    . VAL B 1 168 ? 8.89376   -42.94915 -6.59962  1.000 15.90948  ? 232 VAL B CA    1 
ATOM   2607 C  C     . VAL B 1 168 ? 7.96663   -43.80941 -7.44826  1.000 17.07709  ? 232 VAL B C     1 
ATOM   2608 O  O     . VAL B 1 168 ? 8.24299   -44.03549 -8.63065  1.000 15.02265  ? 232 VAL B O     1 
ATOM   2609 C  CB    . VAL B 1 168 ? 8.90361   -41.50567 -7.13238  1.000 13.84764  ? 232 VAL B CB    1 
ATOM   2610 C  CG1   . VAL B 1 168 ? 7.47761   -40.98972 -7.26038  1.000 16.98680  ? 232 VAL B CG1   1 
ATOM   2611 C  CG2   . VAL B 1 168 ? 9.72061   -40.57597 -6.22837  1.000 12.68296  ? 232 VAL B CG2   1 
ATOM   2612 N  N     . ILE B 1 169 ? 6.85679   -44.26993 -6.86538  1.000 11.70259  ? 233 ILE B N     1 
ATOM   2613 C  CA    . ILE B 1 169 ? 5.92693   -45.13093 -7.58802  1.000 12.94518  ? 233 ILE B CA    1 
ATOM   2614 C  C     . ILE B 1 169 ? 4.51286   -44.57358 -7.48191  1.000 13.38069  ? 233 ILE B C     1 
ATOM   2615 O  O     . ILE B 1 169 ? 4.17759   -43.84147 -6.55582  1.000 13.99885  ? 233 ILE B O     1 
ATOM   2616 C  CB    . ILE B 1 169 ? 5.95389   -46.59174 -7.07137  1.000 18.41022  ? 233 ILE B CB    1 
ATOM   2617 C  CG1   . ILE B 1 169 ? 5.38945   -46.68020 -5.65011  1.000 11.64060  ? 233 ILE B CG1   1 
ATOM   2618 C  CG2   . ILE B 1 169 ? 7.36503   -47.18562 -7.16611  1.000 16.32241  ? 233 ILE B CG2   1 
ATOM   2619 C  CD1   . ILE B 1 169 ? 5.20659   -48.13619 -5.14019  1.000 16.28485  ? 233 ILE B CD1   1 
ATOM   2620 N  N     . ALA B 1 170 ? 3.66849   -44.94304 -8.44492  1.000 15.41162  ? 234 ALA B N     1 
ATOM   2621 C  CA    . ALA B 1 170 ? 2.24230   -44.68735 -8.28375  1.000 14.94354  ? 234 ALA B CA    1 
ATOM   2622 C  C     . ALA B 1 170 ? 1.72294   -45.49260 -7.10526  1.000 15.79332  ? 234 ALA B C     1 
ATOM   2623 O  O     . ALA B 1 170 ? 2.03301   -46.68211 -6.96411  1.000 15.61341  ? 234 ALA B O     1 
ATOM   2624 C  CB    . ALA B 1 170 ? 1.47668   -45.05382 -9.54910  1.000 18.67260  ? 234 ALA B CB    1 
ATOM   2625 N  N     . ASP B 1 171 ? 0.94342   -44.85139 -6.25161  1.000 13.54203  ? 235 ASP B N     1 
ATOM   2626 C  CA    . ASP B 1 171 ? 0.44716   -45.56395 -5.07884  1.000 13.07852  ? 235 ASP B CA    1 
ATOM   2627 C  C     . ASP B 1 171 ? -0.55617  -46.61219 -5.53161  1.000 14.36571  ? 235 ASP B C     1 
ATOM   2628 O  O     . ASP B 1 171 ? -1.63106  -46.24541 -6.03421  1.000 15.36010  ? 235 ASP B O     1 
ATOM   2629 C  CB    . ASP B 1 171 ? -0.19752  -44.59122 -4.09945  1.000 14.46530  ? 235 ASP B CB    1 
ATOM   2630 C  CG    . ASP B 1 171 ? -0.51878  -45.23011 -2.75881  1.000 18.05204  ? 235 ASP B CG    1 
ATOM   2631 O  OD1   . ASP B 1 171 ? -0.62025  -46.47146 -2.67677  1.000 13.08061  ? 235 ASP B OD1   1 
ATOM   2632 O  OD2   . ASP B 1 171 ? -0.64601  -44.46621 -1.77754  1.000 17.67229  ? 235 ASP B OD2   1 
ATOM   2633 N  N     . PRO B 1 172 ? -0.27548  -47.90917 -5.35460  1.000 14.14896  ? 236 PRO B N     1 
ATOM   2634 C  CA    . PRO B 1 172 ? -1.25380  -48.93429 -5.76213  1.000 11.74094  ? 236 PRO B CA    1 
ATOM   2635 C  C     . PRO B 1 172 ? -2.58055  -48.84433 -5.01973  1.000 13.38755  ? 236 PRO B C     1 
ATOM   2636 O  O     . PRO B 1 172 ? -3.57488  -49.41144 -5.48052  1.000 14.71812  ? 236 PRO B O     1 
ATOM   2637 C  CB    . PRO B 1 172 ? -0.52648  -50.25189 -5.45153  1.000 14.46201  ? 236 PRO B CB    1 
ATOM   2638 C  CG    . PRO B 1 172 ? 0.40455   -49.87786 -4.33680  1.000 13.78042  ? 236 PRO B CG    1 
ATOM   2639 C  CD    . PRO B 1 172 ? 0.88985   -48.50763 -4.67770  1.000 12.60859  ? 236 PRO B CD    1 
ATOM   2640 N  N     . ARG B 1 173 ? -2.64030  -48.14452 -3.89507  1.000 13.25968  ? 237 ARG B N     1 
ATOM   2641 C  CA    . ARG B 1 173 ? -3.90006  -48.00073 -3.17688  1.000 16.18443  ? 237 ARG B CA    1 
ATOM   2642 C  C     . ARG B 1 173 ? -4.78376  -46.90101 -3.74368  1.000 17.07336  ? 237 ARG B C     1 
ATOM   2643 O  O     . ARG B 1 173 ? -5.90182  -46.71572 -3.24974  1.000 18.42092  ? 237 ARG B O     1 
ATOM   2644 C  CB    . ARG B 1 173 ? -3.62597  -47.72118 -1.70386  1.000 12.71344  ? 237 ARG B CB    1 
ATOM   2645 C  CG    . ARG B 1 173 ? -2.68291  -48.72712 -1.09639  1.000 16.32348  ? 237 ARG B CG    1 
ATOM   2646 C  CD    . ARG B 1 173 ? -2.12173  -48.21787 0.21104   1.000 17.60459  ? 237 ARG B CD    1 
ATOM   2647 N  NE    . ARG B 1 173 ? -1.23066  -47.08819 -0.02266  1.000 13.83051  ? 237 ARG B NE    1 
ATOM   2648 C  CZ    . ARG B 1 173 ? -0.47454  -46.54132 0.91522   1.000 11.08579  ? 237 ARG B CZ    1 
ATOM   2649 N  NH1   . ARG B 1 173 ? -0.48162  -46.99636 2.15022   1.000 12.16686  ? 237 ARG B NH1   1 
ATOM   2650 N  NH2   . ARG B 1 173 ? 0.31746   -45.52039 0.60124   1.000 12.12430  ? 237 ARG B NH2   1 
ATOM   2651 N  N     . GLY B 1 174 ? -4.31989  -46.16514 -4.74902  1.000 18.07282  ? 238 GLY B N     1 
ATOM   2652 C  CA    . GLY B 1 174 ? -5.11949  -45.07956 -5.27407  1.000 18.08049  ? 238 GLY B CA    1 
ATOM   2653 C  C     . GLY B 1 174 ? -5.12176  -43.87624 -4.35122  1.000 16.20474  ? 238 GLY B C     1 
ATOM   2654 O  O     . GLY B 1 174 ? -4.22478  -43.67982 -3.52410  1.000 17.90292  ? 238 GLY B O     1 
ATOM   2655 N  N     . ASN B 1 175 ? -6.14894  -43.04577 -4.51394  1.000 19.21001  ? 239 ASN B N     1 
ATOM   2656 C  CA    . ASN B 1 175 ? -6.26524  -41.78676 -3.77871  1.000 14.54372  ? 239 ASN B CA    1 
ATOM   2657 C  C     . ASN B 1 175 ? -6.87851  -42.06341 -2.40731  1.000 15.88338  ? 239 ASN B C     1 
ATOM   2658 O  O     . ASN B 1 175 ? -8.09529  -41.97119 -2.21707  1.000 17.50612  ? 239 ASN B O     1 
ATOM   2659 C  CB    . ASN B 1 175 ? -7.10487  -40.79051 -4.56856  1.000 15.39769  ? 239 ASN B CB    1 
ATOM   2660 C  CG    . ASN B 1 175 ? -7.32202  -39.48277 -3.83180  1.000 14.04099  ? 239 ASN B CG    1 
ATOM   2661 O  OD1   . ASN B 1 175 ? -6.70722  -39.21914 -2.79743  1.000 14.51698  ? 239 ASN B OD1   1 
ATOM   2662 N  ND2   . ASN B 1 175 ? -8.20191  -38.64488 -4.37322  1.000 16.44438  ? 239 ASN B ND2   1 
ATOM   2663 N  N     . THR B 1 176 ? -6.03195  -42.40051 -1.43074  1.000 12.58040  ? 240 THR B N     1 
ATOM   2664 C  CA    . THR B 1 176 ? -6.51061  -42.55519 -0.05632  1.000 10.46674  ? 240 THR B CA    1 
ATOM   2665 C  C     . THR B 1 176 ? -6.36555  -41.27865 0.77169   1.000 10.78712  ? 240 THR B C     1 
ATOM   2666 O  O     . THR B 1 176 ? -7.09886  -41.09741 1.74985   1.000 15.63565  ? 240 THR B O     1 
ATOM   2667 C  CB    . THR B 1 176 ? -5.78743  -43.71102 0.64522   1.000 11.34560  ? 240 THR B CB    1 
ATOM   2668 O  OG1   . THR B 1 176 ? -4.41502  -43.36161 0.87095   1.000 13.77922  ? 240 THR B OG1   1 
ATOM   2669 C  CG2   . THR B 1 176 ? -5.87017  -45.00532 -0.16646  1.000 12.79421  ? 240 THR B CG2   1 
ATOM   2670 N  N     . LEU B 1 177 ? -5.45357  -40.38340 0.41396   1.000 12.80390  ? 241 LEU B N     1 
ATOM   2671 C  CA    . LEU B 1 177 ? -5.28578  -39.18368 1.22298   1.000 13.04073  ? 241 LEU B CA    1 
ATOM   2672 C  C     . LEU B 1 177 ? -6.29024  -38.10273 0.86659   1.000 14.08285  ? 241 LEU B C     1 
ATOM   2673 O  O     . LEU B 1 177 ? -6.59968  -37.25369 1.71192   1.000 12.16486  ? 241 LEU B O     1 
ATOM   2674 C  CB    . LEU B 1 177 ? -3.86531  -38.61761 1.07971   1.000 13.51369  ? 241 LEU B CB    1 
ATOM   2675 C  CG    . LEU B 1 177 ? -2.62331  -39.45418 1.40294   1.000 11.41084  ? 241 LEU B CG    1 
ATOM   2676 C  CD1   . LEU B 1 177 ? -1.41574  -38.72125 0.83912   1.000 12.30305  ? 241 LEU B CD1   1 
ATOM   2677 C  CD2   . LEU B 1 177 ? -2.49466  -39.65488 2.91045   1.000 14.22284  ? 241 LEU B CD2   1 
ATOM   2678 N  N     . GLY B 1 178 ? -6.77797  -38.08468 -0.36957  1.000 14.97578  ? 242 GLY B N     1 
ATOM   2679 C  CA    . GLY B 1 178 ? -7.64013  -37.00472 -0.82302  1.000 18.18681  ? 242 GLY B CA    1 
ATOM   2680 C  C     . GLY B 1 178 ? -6.85141  -35.79089 -1.28382  1.000 21.73841  ? 242 GLY B C     1 
ATOM   2681 O  O     . GLY B 1 178 ? -6.98510  -35.32979 -2.42751  1.000 17.35313  ? 242 GLY B O     1 
ATOM   2682 N  N     . ARG B 1 179 ? -6.02506  -35.26786 -0.37595  1.000 12.69952  ? 243 ARG B N     1 
ATOM   2683 C  CA    . ARG B 1 179 ? -5.02339  -34.25129 -0.65542  1.000 11.81010  ? 243 ARG B CA    1 
ATOM   2684 C  C     . ARG B 1 179 ? -4.12317  -34.18572 0.56597   1.000 10.85617  ? 243 ARG B C     1 
ATOM   2685 O  O     . ARG B 1 179 ? -4.60071  -34.34381 1.69167   1.000 12.17622  ? 243 ARG B O     1 
ATOM   2686 C  CB    . ARG B 1 179 ? -5.66569  -32.88447 -0.93137  1.000 11.18974  ? 243 ARG B CB    1 
ATOM   2687 C  CG    . ARG B 1 179 ? -4.67708  -31.73717 -1.17418  1.000 9.34028   ? 243 ARG B CG    1 
ATOM   2688 C  CD    . ARG B 1 179 ? -5.30872  -30.35923 -1.02358  1.000 10.00204  ? 243 ARG B CD    1 
ATOM   2689 N  NE    . ARG B 1 179 ? -5.63025  -30.04005 0.36577   1.000 9.32878   ? 243 ARG B NE    1 
ATOM   2690 C  CZ    . ARG B 1 179 ? -6.83768  -30.18120 0.90208   1.000 12.73569  ? 243 ARG B CZ    1 
ATOM   2691 N  NH1   . ARG B 1 179 ? -7.87389  -30.58059 0.17877   1.000 15.09011  ? 243 ARG B NH1   1 
ATOM   2692 N  NH2   . ARG B 1 179 ? -7.01102  -29.92136 2.19864   1.000 16.08288  ? 243 ARG B NH2   1 
ATOM   2693 N  N     . GLY B 1 180 ? -2.82527  -33.98115 0.33950   1.000 16.03563  ? 244 GLY B N     1 
ATOM   2694 C  CA    . GLY B 1 180 ? -1.88727  -33.84887 1.43870   1.000 11.64270  ? 244 GLY B CA    1 
ATOM   2695 C  C     . GLY B 1 180 ? -0.75986  -34.85447 1.38350   1.000 9.98756   ? 244 GLY B C     1 
ATOM   2696 O  O     . GLY B 1 180 ? -0.49664  -35.44931 0.34162   1.000 11.66935  ? 244 GLY B O     1 
ATOM   2697 N  N     . THR B 1 181 ? -0.10238  -35.07859 2.51351   1.000 14.06212  ? 245 THR B N     1 
ATOM   2698 C  CA    . THR B 1 181 ? 1.13319   -35.84749 2.53994   1.000 13.98261  ? 245 THR B CA    1 
ATOM   2699 C  C     . THR B 1 181 ? 1.20703   -36.60501 3.85005   1.000 12.36157  ? 245 THR B C     1 
ATOM   2700 O  O     . THR B 1 181 ? 0.89413   -36.04102 4.90153   1.000 13.22201  ? 245 THR B O     1 
ATOM   2701 C  CB    . THR B 1 181 ? 2.33938   -34.91409 2.43792   1.000 13.87184  ? 245 THR B CB    1 
ATOM   2702 O  OG1   . THR B 1 181 ? 2.27779   -34.21041 1.20107   1.000 11.43888  ? 245 THR B OG1   1 
ATOM   2703 C  CG2   . THR B 1 181 ? 3.62793   -35.69187 2.48689   1.000 10.91027  ? 245 THR B CG2   1 
ATOM   2704 N  N     . THR B 1 182 ? 1.64847   -37.85856 3.79760   1.000 11.28685  ? 246 THR B N     1 
ATOM   2705 C  CA    . THR B 1 182 ? 2.00374   -38.60765 5.00049   1.000 11.48837  ? 246 THR B CA    1 
ATOM   2706 C  C     . THR B 1 182 ? 3.49300   -38.89892 4.97280   1.000 13.09341  ? 246 THR B C     1 
ATOM   2707 O  O     . THR B 1 182 ? 3.99990   -39.41629 3.97659   1.000 14.04110  ? 246 THR B O     1 
ATOM   2708 C  CB    . THR B 1 182 ? 1.22757   -39.91537 5.11257   1.000 11.96483  ? 246 THR B CB    1 
ATOM   2709 O  OG1   . THR B 1 182 ? -0.16713  -39.63266 5.21776   1.000 15.14341  ? 246 THR B OG1   1 
ATOM   2710 C  CG2   . THR B 1 182 ? 1.66952   -40.69863 6.34927   1.000 11.95999  ? 246 THR B CG2   1 
ATOM   2711 N  N     . ILE B 1 183 ? 4.19301   -38.52712 6.04189   1.000 13.56066  ? 247 ILE B N     1 
ATOM   2712 C  CA    . ILE B 1 183 ? 5.59515   -38.88156 6.23676   1.000 12.88703  ? 247 ILE B CA    1 
ATOM   2713 C  C     . ILE B 1 183 ? 5.61939   -40.06352 7.19728   1.000 15.25339  ? 247 ILE B C     1 
ATOM   2714 O  O     . ILE B 1 183 ? 5.29250   -39.91219 8.38118   1.000 17.38301  ? 247 ILE B O     1 
ATOM   2715 C  CB    . ILE B 1 183 ? 6.40865   -37.71484 6.81322   1.000 13.47199  ? 247 ILE B CB    1 
ATOM   2716 C  CG1   . ILE B 1 183 ? 6.16127   -36.38274 6.06966   1.000 13.09999  ? 247 ILE B CG1   1 
ATOM   2717 C  CG2   . ILE B 1 183 ? 7.88940   -38.09659 6.89105   1.000 14.86372  ? 247 ILE B CG2   1 
ATOM   2718 C  CD1   . ILE B 1 183 ? 6.63084   -36.35041 4.61244   1.000 11.62650  ? 247 ILE B CD1   1 
ATOM   2719 N  N     . THR B 1 184 ? 6.00690   -41.24147 6.71444   1.000 11.32040  ? 248 THR B N     1 
ATOM   2720 C  CA    . THR B 1 184 ? 6.07609   -42.44061 7.53574   1.000 9.35499   ? 248 THR B CA    1 
ATOM   2721 C  C     . THR B 1 184 ? 7.53393   -42.75829 7.82588   1.000 13.12758  ? 248 THR B C     1 
ATOM   2722 O  O     . THR B 1 184 ? 8.34506   -42.85765 6.89658   1.000 13.42890  ? 248 THR B O     1 
ATOM   2723 C  CB    . THR B 1 184 ? 5.39749   -43.62028 6.84041   1.000 10.54290  ? 248 THR B CB    1 
ATOM   2724 O  OG1   . THR B 1 184 ? 4.01331   -43.30153 6.65267   1.000 11.62293  ? 248 THR B OG1   1 
ATOM   2725 C  CG2   . THR B 1 184 ? 5.51331   -44.89459 7.66433   1.000 9.77337   ? 248 THR B CG2   1 
ATOM   2726 N  N     . LEU B 1 185 ? 7.86096   -42.90722 9.11174   1.000 13.21725  ? 249 LEU B N     1 
ATOM   2727 C  CA    . LEU B 1 185 ? 9.21591   -43.19609 9.55809   1.000 12.83514  ? 249 LEU B CA    1 
ATOM   2728 C  C     . LEU B 1 185 ? 9.28046   -44.63548 10.04085  1.000 13.46409  ? 249 LEU B C     1 
ATOM   2729 O  O     . LEU B 1 185 ? 8.52595   -45.02512 10.94071  1.000 17.40831  ? 249 LEU B O     1 
ATOM   2730 C  CB    . LEU B 1 185 ? 9.65015   -42.24026 10.67419  1.000 18.24045  ? 249 LEU B CB    1 
ATOM   2731 C  CG    . LEU B 1 185 ? 9.84556   -40.75072 10.33440  1.000 21.54604  ? 249 LEU B CG    1 
ATOM   2732 C  CD1   . LEU B 1 185 ? 8.52643   -39.96838 10.30672  1.000 18.13902  ? 249 LEU B CD1   1 
ATOM   2733 C  CD2   . LEU B 1 185 ? 10.79849  -40.12187 11.32672  1.000 22.41575  ? 249 LEU B CD2   1 
ATOM   2734 N  N     . VAL B 1 186 ? 10.17594  -45.42503 9.44917   1.000 15.18427  ? 250 VAL B N     1 
ATOM   2735 C  CA    . VAL B 1 186 ? 10.53084  -46.73125 9.99530   1.000 19.67206  ? 250 VAL B CA    1 
ATOM   2736 C  C     . VAL B 1 186 ? 11.64197  -46.46520 11.00424  1.000 19.74842  ? 250 VAL B C     1 
ATOM   2737 O  O     . VAL B 1 186 ? 12.78937  -46.21480 10.63288  1.000 24.27714  ? 250 VAL B O     1 
ATOM   2738 C  CB    . VAL B 1 186 ? 10.96885  -47.72041 8.91014   1.000 21.58610  ? 250 VAL B CB    1 
ATOM   2739 C  CG1   . VAL B 1 186 ? 11.06951  -49.12292 9.48575   1.000 21.60325  ? 250 VAL B CG1   1 
ATOM   2740 C  CG2   . VAL B 1 186 ? 10.00451  -47.69630 7.73094   1.000 18.42861  ? 250 VAL B CG2   1 
ATOM   2741 N  N     . LEU B 1 187 ? 11.30083  -46.52110 12.28717  1.000 20.50328  ? 251 LEU B N     1 
ATOM   2742 C  CA    . LEU B 1 187 ? 12.21074  -46.05298 13.31726  1.000 22.32753  ? 251 LEU B CA    1 
ATOM   2743 C  C     . LEU B 1 187 ? 13.37012  -47.02335 13.51821  1.000 26.74912  ? 251 LEU B C     1 
ATOM   2744 O  O     . LEU B 1 187 ? 13.23311  -48.24242 13.37267  1.000 22.49326  ? 251 LEU B O     1 
ATOM   2745 C  CB    . LEU B 1 187 ? 11.45023  -45.84536 14.62090  1.000 21.21738  ? 251 LEU B CB    1 
ATOM   2746 C  CG    . LEU B 1 187 ? 10.46926  -44.67295 14.53497  1.000 21.82042  ? 251 LEU B CG    1 
ATOM   2747 C  CD1   . LEU B 1 187 ? 9.62154   -44.58047 15.78479  1.000 18.93079  ? 251 LEU B CD1   1 
ATOM   2748 C  CD2   . LEU B 1 187 ? 11.19216  -43.35544 14.27189  1.000 21.78141  ? 251 LEU B CD2   1 
ATOM   2749 N  N     . LYS B 1 188 ? 14.52968  -46.46417 13.84813  1.000 24.17599  ? 252 LYS B N     1 
ATOM   2750 C  CA    . LYS B 1 188 ? 15.64250  -47.29938 14.25238  1.000 22.77249  ? 252 LYS B CA    1 
ATOM   2751 C  C     . LYS B 1 188 ? 15.29928  -48.00549 15.55668  1.000 27.58252  ? 252 LYS B C     1 
ATOM   2752 O  O     . LYS B 1 188 ? 14.38790  -47.60655 16.28518  1.000 25.81729  ? 252 LYS B O     1 
ATOM   2753 C  CB    . LYS B 1 188 ? 16.90372  -46.45895 14.41788  1.000 24.36871  ? 252 LYS B CB    1 
ATOM   2754 C  CG    . LYS B 1 188 ? 17.33428  -45.78321 13.14310  1.000 23.83957  ? 252 LYS B CG    1 
ATOM   2755 C  CD    . LYS B 1 188 ? 18.18274  -44.55021 13.42776  1.000 30.76018  ? 252 LYS B CD    1 
ATOM   2756 C  CE    . LYS B 1 188 ? 19.50849  -44.62950 12.69919  1.000 32.80726  ? 252 LYS B CE    1 
ATOM   2757 N  NZ    . LYS B 1 188 ? 19.29318  -44.54760 11.22602  1.000 30.24079  ? 252 LYS B NZ    1 
ATOM   2758 N  N     . GLU B 1 189 ? 16.05340  -49.06787 15.85455  1.000 33.95625  ? 253 GLU B N     1 
ATOM   2759 C  CA    . GLU B 1 189 ? 15.79241  -49.84399 17.06064  1.000 33.15432  ? 253 GLU B CA    1 
ATOM   2760 C  C     . GLU B 1 189 ? 15.85917  -48.98504 18.31505  1.000 35.45605  ? 253 GLU B C     1 
ATOM   2761 O  O     . GLU B 1 189 ? 15.14840  -49.26083 19.29055  1.000 37.61656  ? 253 GLU B O     1 
ATOM   2762 C  CB    . GLU B 1 189 ? 16.78607  -51.00494 17.17575  1.000 37.03775  ? 253 GLU B CB    1 
ATOM   2763 N  N     . GLU B 1 190 ? 16.70973  -47.96050 18.32924  1.000 31.71995  ? 254 GLU B N     1 
ATOM   2764 C  CA    . GLU B 1 190 ? 16.86241  -47.15650 19.53514  1.000 37.23338  ? 254 GLU B CA    1 
ATOM   2765 C  C     . GLU B 1 190 ? 15.95435  -45.93180 19.54571  1.000 33.93108  ? 254 GLU B C     1 
ATOM   2766 O  O     . GLU B 1 190 ? 15.92496  -45.20388 20.54308  1.000 34.00733  ? 254 GLU B O     1 
ATOM   2767 C  CB    . GLU B 1 190 ? 18.32488  -46.72648 19.72643  1.000 36.20147  ? 254 GLU B CB    1 
ATOM   2768 C  CG    . GLU B 1 190 ? 18.81248  -45.63779 18.77560  1.000 39.28435  ? 254 GLU B CG    1 
ATOM   2769 C  CD    . GLU B 1 190 ? 19.18060  -46.15210 17.39480  1.000 42.07494  ? 254 GLU B CD    1 
ATOM   2770 O  OE1   . GLU B 1 190 ? 18.97762  -47.35978 17.12114  1.000 40.08056  ? 254 GLU B OE1   1 
ATOM   2771 O  OE2   . GLU B 1 190 ? 19.69307  -45.33754 16.58843  1.000 38.50555  ? 254 GLU B OE2   1 
ATOM   2772 N  N     . ALA B 1 191 ? 15.20159  -45.69555 18.47605  1.000 27.35341  ? 255 ALA B N     1 
ATOM   2773 C  CA    . ALA B 1 191 ? 14.22888  -44.61346 18.43018  1.000 27.07040  ? 255 ALA B CA    1 
ATOM   2774 C  C     . ALA B 1 191 ? 12.82118  -45.09474 18.75821  1.000 22.93178  ? 255 ALA B C     1 
ATOM   2775 O  O     . ALA B 1 191 ? 11.84568  -44.42151 18.39886  1.000 20.91930  ? 255 ALA B O     1 
ATOM   2776 C  CB    . ALA B 1 191 ? 14.24535  -43.94032 17.05935  1.000 19.22271  ? 255 ALA B CB    1 
ATOM   2777 N  N     . SER B 1 192 ? 12.70374  -46.24454 19.43399  1.000 25.06132  ? 256 SER B N     1 
ATOM   2778 C  CA    . SER B 1 192 ? 11.40382  -46.85119 19.68727  1.000 22.49850  ? 256 SER B CA    1 
ATOM   2779 C  C     . SER B 1 192 ? 10.55497  -46.02725 20.64361  1.000 22.57036  ? 256 SER B C     1 
ATOM   2780 O  O     . SER B 1 192 ? 9.32622   -46.15591 20.62972  1.000 24.57323  ? 256 SER B O     1 
ATOM   2781 C  CB    . SER B 1 192 ? 11.56807  -48.27011 20.23923  1.000 30.60326  ? 256 SER B CB    1 
ATOM   2782 O  OG    . SER B 1 192 ? 12.66690  -48.38009 21.14075  1.000 32.13752  ? 256 SER B OG    1 
ATOM   2783 N  N     . ASP B 1 193 ? 11.17287  -45.18475 21.46931  1.000 28.48549  ? 257 ASP B N     1 
ATOM   2784 C  CA    . ASP B 1 193 ? 10.39741  -44.32856 22.35730  1.000 28.17346  ? 257 ASP B CA    1 
ATOM   2785 C  C     . ASP B 1 193 ? 9.49202   -43.37973 21.58415  1.000 25.46461  ? 257 ASP B C     1 
ATOM   2786 O  O     . ASP B 1 193 ? 8.50504   -42.90050 22.14277  1.000 23.17538  ? 257 ASP B O     1 
ATOM   2787 C  CB    . ASP B 1 193 ? 11.33161  -43.53930 23.28618  1.000 28.33543  ? 257 ASP B CB    1 
ATOM   2788 N  N     . TYR B 1 194 ? 9.79105   -43.11028 20.31205  1.000 23.21941  ? 258 TYR B N     1 
ATOM   2789 C  CA    . TYR B 1 194 ? 8.91990   -42.28063 19.49091  1.000 22.63562  ? 258 TYR B CA    1 
ATOM   2790 C  C     . TYR B 1 194 ? 7.63995   -42.99207 19.06607  1.000 21.94464  ? 258 TYR B C     1 
ATOM   2791 O  O     . TYR B 1 194 ? 6.80264   -42.36295 18.41044  1.000 20.77382  ? 258 TYR B O     1 
ATOM   2792 C  CB    . TYR B 1 194 ? 9.67795   -41.78069 18.25517  1.000 23.61103  ? 258 TYR B CB    1 
ATOM   2793 C  CG    . TYR B 1 194 ? 10.81628  -40.87903 18.63335  1.000 21.23323  ? 258 TYR B CG    1 
ATOM   2794 C  CD1   . TYR B 1 194 ? 10.57320  -39.66563 19.26402  1.000 24.91419  ? 258 TYR B CD1   1 
ATOM   2795 C  CD2   . TYR B 1 194 ? 12.13811  -41.25476 18.41299  1.000 28.93789  ? 258 TYR B CD2   1 
ATOM   2796 C  CE1   . TYR B 1 194 ? 11.61571  -38.83750 19.64831  1.000 31.72857  ? 258 TYR B CE1   1 
ATOM   2797 C  CE2   . TYR B 1 194 ? 13.19334  -40.42573 18.79101  1.000 28.58380  ? 258 TYR B CE2   1 
ATOM   2798 C  CZ    . TYR B 1 194 ? 12.92122  -39.21884 19.40918  1.000 33.43618  ? 258 TYR B CZ    1 
ATOM   2799 O  OH    . TYR B 1 194 ? 13.94301  -38.38279 19.79474  1.000 34.16631  ? 258 TYR B OH    1 
ATOM   2800 N  N     . LEU B 1 195 ? 7.46212   -44.26672 19.39370  1.000 22.11467  ? 259 LEU B N     1 
ATOM   2801 C  CA    . LEU B 1 195 ? 6.17358   -44.91782 19.20782  1.000 20.08333  ? 259 LEU B CA    1 
ATOM   2802 C  C     . LEU B 1 195 ? 5.29724   -44.81724 20.44785  1.000 20.93479  ? 259 LEU B C     1 
ATOM   2803 O  O     . LEU B 1 195 ? 4.20884   -45.40112 20.47647  1.000 22.94816  ? 259 LEU B O     1 
ATOM   2804 C  CB    . LEU B 1 195 ? 6.35506   -46.38322 18.82696  1.000 24.48828  ? 259 LEU B CB    1 
ATOM   2805 C  CG    . LEU B 1 195 ? 7.31405   -46.59750 17.65453  1.000 25.74777  ? 259 LEU B CG    1 
ATOM   2806 C  CD1   . LEU B 1 195 ? 8.18319   -47.83132 17.88366  1.000 26.79619  ? 259 LEU B CD1   1 
ATOM   2807 C  CD2   . LEU B 1 195 ? 6.60376   -46.62018 16.30537  1.000 19.00227  ? 259 LEU B CD2   1 
ATOM   2808 N  N     . GLU B 1 196 ? 5.75323   -44.09569 21.46328  1.000 20.32438  ? 260 GLU B N     1 
ATOM   2809 C  CA    . GLU B 1 196 ? 5.08513   -43.99383 22.75500  1.000 23.93592  ? 260 GLU B CA    1 
ATOM   2810 C  C     . GLU B 1 196 ? 4.21957   -42.74605 22.76806  1.000 23.06678  ? 260 GLU B C     1 
ATOM   2811 O  O     . GLU B 1 196 ? 4.65792   -41.67812 22.32857  1.000 22.36819  ? 260 GLU B O     1 
ATOM   2812 C  CB    . GLU B 1 196 ? 6.10504   -43.92126 23.88998  1.000 26.28918  ? 260 GLU B CB    1 
ATOM   2813 C  CG    . GLU B 1 196 ? 6.76428   -45.25837 24.29734  1.000 28.22516  ? 260 GLU B CG    1 
ATOM   2814 C  CD    . GLU B 1 196 ? 5.82900   -46.45991 24.22543  1.000 31.21853  ? 260 GLU B CD    1 
ATOM   2815 O  OE1   . GLU B 1 196 ? 4.73804   -46.41346 24.84012  1.000 32.07866  ? 260 GLU B OE1   1 
ATOM   2816 O  OE2   . GLU B 1 196 ? 6.18885   -47.45921 23.55974  1.000 34.60612  ? 260 GLU B OE2   1 
ATOM   2817 N  N     . LEU B 1 197 ? 2.98926   -42.88560 23.26915  1.000 20.68254  ? 261 LEU B N     1 
ATOM   2818 C  CA    . LEU B 1 197 ? 2.05685   -41.76120 23.26098  1.000 24.60896  ? 261 LEU B CA    1 
ATOM   2819 C  C     . LEU B 1 197 ? 2.54684   -40.61160 24.13777  1.000 23.39805  ? 261 LEU B C     1 
ATOM   2820 O  O     . LEU B 1 197 ? 2.41030   -39.44179 23.76354  1.000 24.92095  ? 261 LEU B O     1 
ATOM   2821 C  CB    . LEU B 1 197 ? 0.67298   -42.22342 23.71211  1.000 28.84073  ? 261 LEU B CB    1 
ATOM   2822 C  CG    . LEU B 1 197 ? -0.53161  -41.70612 22.92196  1.000 27.21035  ? 261 LEU B CG    1 
ATOM   2823 C  CD1   . LEU B 1 197 ? -0.25978  -41.75493 21.43347  1.000 24.47028  ? 261 LEU B CD1   1 
ATOM   2824 C  CD2   . LEU B 1 197 ? -1.76470  -42.53020 23.27549  1.000 23.78477  ? 261 LEU B CD2   1 
ATOM   2825 N  N     . ASP B 1 198 ? 3.10903   -40.91196 25.31178  1.000 22.34043  ? 262 ASP B N     1 
ATOM   2826 C  CA    . ASP B 1 198 ? 3.60649   -39.82920 26.16013  1.000 23.07348  ? 262 ASP B CA    1 
ATOM   2827 C  C     . ASP B 1 198 ? 4.78835   -39.10836 25.51559  1.000 21.33481  ? 262 ASP B C     1 
ATOM   2828 O  O     . ASP B 1 198 ? 4.86066   -37.87358 25.56288  1.000 21.69720  ? 262 ASP B O     1 
ATOM   2829 C  CB    . ASP B 1 198 ? 3.96768   -40.32985 27.56300  1.000 28.85124  ? 262 ASP B CB    1 
ATOM   2830 C  CG    . ASP B 1 198 ? 4.95240   -41.48972 27.56016  1.000 28.86860  ? 262 ASP B CG    1 
ATOM   2831 O  OD1   . ASP B 1 198 ? 5.16987   -42.11267 26.50936  1.000 28.11250  ? 262 ASP B OD1   1 
ATOM   2832 O  OD2   . ASP B 1 198 ? 5.51361   -41.77802 28.63761  1.000 29.79460  ? 262 ASP B OD2   1 
ATOM   2833 N  N     . THR B 1 199 ? 5.70773   -39.84350 24.88291  1.000 18.23962  ? 263 THR B N     1 
ATOM   2834 C  CA    . THR B 1 199 ? 6.83113   -39.18437 24.21338  1.000 22.34973  ? 263 THR B CA    1 
ATOM   2835 C  C     . THR B 1 199 ? 6.35458   -38.25249 23.10309  1.000 24.17211  ? 263 THR B C     1 
ATOM   2836 O  O     . THR B 1 199 ? 6.74304   -37.08025 23.04922  1.000 24.30129  ? 263 THR B O     1 
ATOM   2837 C  CB    . THR B 1 199 ? 7.79662   -40.22225 23.64018  1.000 23.99479  ? 263 THR B CB    1 
ATOM   2838 O  OG1   . THR B 1 199 ? 8.50543   -40.87220 24.70230  1.000 25.57914  ? 263 THR B OG1   1 
ATOM   2839 C  CG2   . THR B 1 199 ? 8.78194   -39.57171 22.69403  1.000 26.34367  ? 263 THR B CG2   1 
ATOM   2840 N  N     . ILE B 1 200 ? 5.50952   -38.75652 22.20442  1.000 25.92422  ? 264 ILE B N     1 
ATOM   2841 C  CA    . ILE B 1 200 ? 5.12698   -37.96576 21.04258  1.000 22.58771  ? 264 ILE B CA    1 
ATOM   2842 C  C     . ILE B 1 200 ? 4.24390   -36.80126 21.45404  1.000 23.74571  ? 264 ILE B C     1 
ATOM   2843 O  O     . ILE B 1 200 ? 4.37119   -35.69233 20.92208  1.000 24.26964  ? 264 ILE B O     1 
ATOM   2844 C  CB    . ILE B 1 200 ? 4.44637   -38.85416 19.99261  1.000 21.15452  ? 264 ILE B CB    1 
ATOM   2845 C  CG1   . ILE B 1 200 ? 5.47953   -39.77590 19.35629  1.000 26.35884  ? 264 ILE B CG1   1 
ATOM   2846 C  CG2   . ILE B 1 200 ? 3.77348   -38.01063 18.92197  1.000 24.40486  ? 264 ILE B CG2   1 
ATOM   2847 C  CD1   . ILE B 1 200 ? 6.28216   -39.13623 18.23892  1.000 25.24140  ? 264 ILE B CD1   1 
ATOM   2848 N  N     . LYS B 1 201 ? 3.33338   -37.02661 22.40234  1.000 18.21895  ? 265 LYS B N     1 
ATOM   2849 C  CA    . LYS B 1 201 ? 2.44755   -35.94934 22.83085  1.000 18.23800  ? 265 LYS B CA    1 
ATOM   2850 C  C     . LYS B 1 201 ? 3.24347   -34.80713 23.45260  1.000 24.04934  ? 265 LYS B C     1 
ATOM   2851 O  O     . LYS B 1 201 ? 3.02141   -33.63043 23.13493  1.000 19.30367  ? 265 LYS B O     1 
ATOM   2852 C  CB    . LYS B 1 201 ? 1.41569   -36.49059 23.81288  1.000 20.65260  ? 265 LYS B CB    1 
ATOM   2853 C  CG    . LYS B 1 201 ? 0.04979   -36.76079 23.19465  1.000 21.89612  ? 265 LYS B CG    1 
ATOM   2854 C  CD    . LYS B 1 201 ? -0.80066  -37.59026 24.13534  1.000 19.60693  ? 265 LYS B CD    1 
ATOM   2855 C  CE    . LYS B 1 201 ? -1.95505  -38.24099 23.41172  1.000 14.13945  ? 265 LYS B CE    1 
ATOM   2856 N  NZ    . LYS B 1 201 ? -3.05650  -38.50613 24.39905  1.000 17.95767  ? 265 LYS B NZ    1 
ATOM   2857 N  N     . ASN B 1 202 ? 4.19857   -35.13987 24.32960  1.000 22.02966  ? 266 ASN B N     1 
ATOM   2858 C  CA    . ASN B 1 202 ? 5.04941   -34.11106 24.91763  1.000 20.20197  ? 266 ASN B CA    1 
ATOM   2859 C  C     . ASN B 1 202 ? 5.86721   -33.40208 23.84901  1.000 20.79549  ? 266 ASN B C     1 
ATOM   2860 O  O     . ASN B 1 202 ? 6.08023   -32.18814 23.92431  1.000 25.07497  ? 266 ASN B O     1 
ATOM   2861 C  CB    . ASN B 1 202 ? 5.97498   -34.72363 25.97437  1.000 22.71273  ? 266 ASN B CB    1 
ATOM   2862 C  CG    . ASN B 1 202 ? 5.27359   -34.98111 27.29054  1.000 23.37570  ? 266 ASN B CG    1 
ATOM   2863 O  OD1   . ASN B 1 202 ? 4.43666   -34.18780 27.72886  1.000 22.97439  ? 266 ASN B OD1   1 
ATOM   2864 N  ND2   . ASN B 1 202 ? 5.61103   -36.09173 27.93281  1.000 19.52071  ? 266 ASN B ND2   1 
ATOM   2865 N  N     . LEU B 1 203 ? 6.34748   -34.14853 22.85521  1.000 23.67177  ? 267 LEU B N     1 
ATOM   2866 C  CA    . LEU B 1 203 ? 7.18649   -33.57072 21.80861  1.000 22.75354  ? 267 LEU B CA    1 
ATOM   2867 C  C     . LEU B 1 203 ? 6.40651   -32.59763 20.92696  1.000 23.17377  ? 267 LEU B C     1 
ATOM   2868 O  O     . LEU B 1 203 ? 6.93204   -31.54664 20.53871  1.000 22.23123  ? 267 LEU B O     1 
ATOM   2869 C  CB    . LEU B 1 203 ? 7.77776   -34.68424 20.95384  1.000 25.14117  ? 267 LEU B CB    1 
ATOM   2870 C  CG    . LEU B 1 203 ? 9.28895   -34.87688 20.93118  1.000 29.33346  ? 267 LEU B CG    1 
ATOM   2871 C  CD1   . LEU B 1 203 ? 9.66796   -35.77107 19.74551  1.000 27.73107  ? 267 LEU B CD1   1 
ATOM   2872 C  CD2   . LEU B 1 203 ? 10.01020  -33.54296 20.88706  1.000 34.41611  ? 267 LEU B CD2   1 
ATOM   2873 N  N     . VAL B 1 204 ? 5.16334   -32.94548 20.57404  1.000 19.02854  ? 268 VAL B N     1 
ATOM   2874 C  CA    . VAL B 1 204 ? 4.35314   -32.06349 19.74077  1.000 21.64141  ? 268 VAL B CA    1 
ATOM   2875 C  C     . VAL B 1 204 ? 4.08995   -30.74399 20.45424  1.000 27.22402  ? 268 VAL B C     1 
ATOM   2876 O  O     . VAL B 1 204 ? 4.12846   -29.66958 19.83919  1.000 30.02780  ? 268 VAL B O     1 
ATOM   2877 C  CB    . VAL B 1 204 ? 3.04427   -32.75986 19.32908  1.000 19.57621  ? 268 VAL B CB    1 
ATOM   2878 C  CG1   . VAL B 1 204 ? 2.13988   -31.77534 18.57706  1.000 19.05611  ? 268 VAL B CG1   1 
ATOM   2879 C  CG2   . VAL B 1 204 ? 3.34855   -33.96836 18.46307  1.000 15.91215  ? 268 VAL B CG2   1 
ATOM   2880 N  N     . LYS B 1 205 ? 3.82573   -30.79783 21.76069  1.000 32.70274  ? 269 LYS B N     1 
ATOM   2881 C  CA    . LYS B 1 205 ? 3.62910   -29.56636 22.51535  1.000 31.04959  ? 269 LYS B CA    1 
ATOM   2882 C  C     . LYS B 1 205 ? 4.88180   -28.70462 22.47784  1.000 36.44179  ? 269 LYS B C     1 
ATOM   2883 O  O     . LYS B 1 205 ? 4.80944   -27.49106 22.24187  1.000 42.62802  ? 269 LYS B O     1 
ATOM   2884 C  CB    . LYS B 1 205 ? 3.25732   -29.89288 23.95923  1.000 34.98249  ? 269 LYS B CB    1 
ATOM   2885 C  CG    . LYS B 1 205 ? 1.80864   -30.30482 24.14955  1.000 41.26023  ? 269 LYS B CG    1 
ATOM   2886 C  CD    . LYS B 1 205 ? 1.07615   -29.39328 25.12497  1.000 40.60013  ? 269 LYS B CD    1 
ATOM   2887 C  CE    . LYS B 1 205 ? -0.28371  -29.99211 25.48130  1.000 44.34520  ? 269 LYS B CE    1 
ATOM   2888 N  NZ    . LYS B 1 205 ? -1.41013  -29.43573 24.67311  1.000 40.88701  ? 269 LYS B NZ    1 
ATOM   2889 N  N     . LYS B 1 206 ? 6.04694   -29.32456 22.67658  1.000 26.60047  ? 270 LYS B N     1 
ATOM   2890 C  CA    . LYS B 1 206 ? 7.29761   -28.57679 22.72488  1.000 30.40790  ? 270 LYS B CA    1 
ATOM   2891 C  C     . LYS B 1 206 ? 7.60201   -27.87577 21.40107  1.000 34.51075  ? 270 LYS B C     1 
ATOM   2892 O  O     . LYS B 1 206 ? 8.32728   -26.87400 21.39238  1.000 38.07470  ? 270 LYS B O     1 
ATOM   2893 C  CB    . LYS B 1 206 ? 8.43787   -29.52184 23.12711  1.000 28.93651  ? 270 LYS B CB    1 
ATOM   2894 C  CG    . LYS B 1 206 ? 9.79814   -28.85184 23.32821  1.000 38.92767  ? 270 LYS B CG    1 
ATOM   2895 C  CD    . LYS B 1 206 ? 10.93325  -29.68804 22.74174  1.000 37.39120  ? 270 LYS B CD    1 
ATOM   2896 C  CE    . LYS B 1 206 ? 12.08906  -29.83503 23.73446  1.000 45.73713  ? 270 LYS B CE    1 
ATOM   2897 N  N     . TYR B 1 207 ? 7.04306   -28.35383 20.28473  1.000 41.33257  ? 271 TYR B N     1 
ATOM   2898 C  CA    . TYR B 1 207 ? 7.28869   -27.74410 18.98289  1.000 43.60674  ? 271 TYR B CA    1 
ATOM   2899 C  C     . TYR B 1 207 ? 6.01164   -27.22601 18.32695  1.000 46.47237  ? 271 TYR B C     1 
ATOM   2900 O  O     . TYR B 1 207 ? 5.99550   -27.00941 17.11160  1.000 46.84941  ? 271 TYR B O     1 
ATOM   2901 C  CB    . TYR B 1 207 ? 8.00032   -28.72819 18.05302  1.000 43.89901  ? 271 TYR B CB    1 
ATOM   2902 C  CG    . TYR B 1 207 ? 9.39212   -29.09313 18.52601  1.000 51.09645  ? 271 TYR B CG    1 
ATOM   2903 C  CD1   . TYR B 1 207 ? 10.31546  -28.10369 18.83690  1.000 50.23678  ? 271 TYR B CD1   1 
ATOM   2904 C  CD2   . TYR B 1 207 ? 9.79066   -30.42265 18.64421  1.000 49.78807  ? 271 TYR B CD2   1 
ATOM   2905 C  CE1   . TYR B 1 207 ? 11.58892  -28.42008 19.26565  1.000 50.56857  ? 271 TYR B CE1   1 
ATOM   2906 C  CE2   . TYR B 1 207 ? 11.06972  -30.74856 19.07377  1.000 49.44882  ? 271 TYR B CE2   1 
ATOM   2907 C  CZ    . TYR B 1 207 ? 11.96186  -29.74171 19.38479  1.000 52.79071  ? 271 TYR B CZ    1 
ATOM   2908 O  OH    . TYR B 1 207 ? 13.23221  -30.05720 19.81484  1.000 55.88922  ? 271 TYR B OH    1 
ATOM   2909 N  N     . SER B 1 208 ? 4.94470   -26.98760 19.10108  1.000 51.05148  ? 272 SER B N     1 
ATOM   2910 C  CA    . SER B 1 208 ? 3.72445   -26.38978 18.55364  1.000 49.23824  ? 272 SER B CA    1 
ATOM   2911 C  C     . SER B 1 208 ? 4.00444   -24.93950 18.17496  1.000 57.41263  ? 272 SER B C     1 
ATOM   2912 O  O     . SER B 1 208 ? 3.10314   -24.18618 17.78332  1.000 53.93455  ? 272 SER B O     1 
ATOM   2913 C  CB    . SER B 1 208 ? 2.56943   -26.46299 19.55066  1.000 43.80407  ? 272 SER B CB    1 
ATOM   2914 O  OG    . SER B 1 208 ? 2.41299   -25.23320 20.24631  1.000 45.03103  ? 272 SER B OG    1 
ATOM   2915 N  N     . GLN B 1 209 ? 5.26900   -24.55446 18.36167  1.000 35.52126  ? 273 GLN B N     1 
ATOM   2916 C  CA    . GLN B 1 209 ? 5.78724   -23.26814 17.92471  1.000 39.03012  ? 273 GLN B CA    1 
ATOM   2917 C  C     . GLN B 1 209 ? 5.70746   -23.11222 16.41182  1.000 38.22240  ? 273 GLN B C     1 
ATOM   2918 O  O     . GLN B 1 209 ? 5.36413   -22.03993 15.90589  1.000 33.63112  ? 273 GLN B O     1 
ATOM   2919 C  CB    . GLN B 1 209 ? 7.24230   -23.15820 18.36272  1.000 40.39267  ? 273 GLN B CB    1 
ATOM   2920 C  CG    . GLN B 1 209 ? 7.47267   -22.28628 19.53305  1.000 47.26265  ? 273 GLN B CG    1 
ATOM   2921 C  CD    . GLN B 1 209 ? 8.90694   -22.31538 19.97285  1.000 45.96123  ? 273 GLN B CD    1 
ATOM   2922 O  OE1   . GLN B 1 209 ? 9.74540   -21.63491 19.39730  1.000 42.61076  ? 273 GLN B OE1   1 
ATOM   2923 N  NE2   . GLN B 1 209 ? 9.20860   -23.13383 20.97740  1.000 42.96848  ? 273 GLN B NE2   1 
ATOM   2924 N  N     . PHE B 1 210 ? 6.06424   -24.16009 15.67247  1.000 38.98882  ? 274 PHE B N     1 
ATOM   2925 C  CA    . PHE B 1 210 ? 6.16293   -24.08450 14.22381  1.000 40.99478  ? 274 PHE B CA    1 
ATOM   2926 C  C     . PHE B 1 210 ? 4.87047   -24.49472 13.52759  1.000 36.72626  ? 274 PHE B C     1 
ATOM   2927 O  O     . PHE B 1 210 ? 4.89435   -24.81456 12.33337  1.000 35.19207  ? 274 PHE B O     1 
ATOM   2928 C  CB    . PHE B 1 210 ? 7.33068   -24.94557 13.73557  1.000 38.74754  ? 274 PHE B CB    1 
ATOM   2929 N  N     . ILE B 1 211 ? 3.74977   -24.48614 14.24579  1.000 42.50636  ? 275 ILE B N     1 
ATOM   2930 C  CA    . ILE B 1 211 ? 2.47007   -24.97090 13.74638  1.000 37.91178  ? 275 ILE B CA    1 
ATOM   2931 C  C     . ILE B 1 211 ? 1.45110   -23.85236 13.86382  1.000 38.12010  ? 275 ILE B C     1 
ATOM   2932 O  O     . ILE B 1 211 ? 1.26123   -23.28211 14.94680  1.000 27.48136  ? 275 ILE B O     1 
ATOM   2933 C  CB    . ILE B 1 211 ? 1.98792   -26.20663 14.51955  1.000 29.47418  ? 275 ILE B CB    1 
ATOM   2934 N  N     . ASN B 1 212 ? 0.78982   -23.55826 12.75049  1.000 51.73333  ? 276 ASN B N     1 
ATOM   2935 C  CA    . ASN B 1 212 ? -0.25124  -22.54630 12.67174  1.000 50.39560  ? 276 ASN B CA    1 
ATOM   2936 C  C     . ASN B 1 212 ? -1.63180  -23.15328 12.87291  1.000 48.29556  ? 276 ASN B C     1 
ATOM   2937 O  O     . ASN B 1 212 ? -2.50993  -22.52792 13.46912  1.000 50.66658  ? 276 ASN B O     1 
ATOM   2938 C  CB    . ASN B 1 212 ? -0.18331  -21.86815 11.30373  1.000 52.67969  ? 276 ASN B CB    1 
ATOM   2939 C  CG    . ASN B 1 212 ? 0.91322   -20.82825 11.22025  1.000 53.80780  ? 276 ASN B CG    1 
ATOM   2940 O  OD1   . ASN B 1 212 ? 1.80685   -20.78039 12.06768  1.000 49.24855  ? 276 ASN B OD1   1 
ATOM   2941 N  ND2   . ASN B 1 212 ? 0.86778   -20.00208 10.17636  1.000 60.48169  ? 276 ASN B ND2   1 
ATOM   2942 N  N     . PHE B 1 213 ? -1.81411  -24.36923 12.38141  1.000 25.54225  ? 277 PHE B N     1 
ATOM   2943 C  CA    . PHE B 1 213 ? -3.00017  -25.18245 12.19587  1.000 23.17022  ? 277 PHE B CA    1 
ATOM   2944 C  C     . PHE B 1 213 ? -3.11303  -26.20121 13.31542  1.000 19.01046  ? 277 PHE B C     1 
ATOM   2945 O  O     . PHE B 1 213 ? -2.13570  -26.47692 14.01885  1.000 17.90607  ? 277 PHE B O     1 
ATOM   2946 C  CB    . PHE B 1 213 ? -2.92480  -25.89888 10.83149  1.000 18.67753  ? 277 PHE B CB    1 
ATOM   2947 C  CG    . PHE B 1 213 ? -2.79184  -24.96115 9.67417   1.000 19.11682  ? 277 PHE B CG    1 
ATOM   2948 C  CD1   . PHE B 1 213 ? -1.54845  -24.42261 9.33034   1.000 22.23544  ? 277 PHE B CD1   1 
ATOM   2949 C  CD2   . PHE B 1 213 ? -3.91007  -24.55484 8.96349   1.000 17.53546  ? 277 PHE B CD2   1 
ATOM   2950 C  CE1   . PHE B 1 213 ? -1.42187  -23.53084 8.27731   1.000 24.57870  ? 277 PHE B CE1   1 
ATOM   2951 C  CE2   . PHE B 1 213 ? -3.79569  -23.64234 7.90437   1.000 20.05686  ? 277 PHE B CE2   1 
ATOM   2952 C  CZ    . PHE B 1 213 ? -2.54976  -23.13295 7.55415   1.000 21.02349  ? 277 PHE B CZ    1 
ATOM   2953 N  N     . PRO B 1 214 ? -4.29911  -26.76990 13.53124  1.000 14.84412  ? 278 PRO B N     1 
ATOM   2954 C  CA    . PRO B 1 214 ? -4.45552  -27.75022 14.61320  1.000 15.50916  ? 278 PRO B CA    1 
ATOM   2955 C  C     . PRO B 1 214 ? -3.62606  -29.00880 14.38400  1.000 20.90006  ? 278 PRO B C     1 
ATOM   2956 O  O     . PRO B 1 214 ? -3.58778  -29.55823 13.28008  1.000 17.65202  ? 278 PRO B O     1 
ATOM   2957 C  CB    . PRO B 1 214 ? -5.95731  -28.06034 14.58823  1.000 19.64017  ? 278 PRO B CB    1 
ATOM   2958 C  CG    . PRO B 1 214 ? -6.42439  -27.64300 13.21822  1.000 16.01612  ? 278 PRO B CG    1 
ATOM   2959 C  CD    . PRO B 1 214 ? -5.58165  -26.45976 12.87000  1.000 16.70340  ? 278 PRO B CD    1 
ATOM   2960 N  N     . ILE B 1 215 ? -2.97114  -29.47983 15.44611  1.000 20.69375  ? 279 ILE B N     1 
ATOM   2961 C  CA    . ILE B 1 215 ? -2.23459  -30.74013 15.41779  1.000 22.55028  ? 279 ILE B CA    1 
ATOM   2962 C  C     . ILE B 1 215 ? -2.86808  -31.72456 16.38242  1.000 23.77482  ? 279 ILE B C     1 
ATOM   2963 O  O     . ILE B 1 215 ? -3.06478  -31.41049 17.56324  1.000 18.33024  ? 279 ILE B O     1 
ATOM   2964 C  CB    . ILE B 1 215 ? -0.74148  -30.58451 15.75058  1.000 17.92980  ? 279 ILE B CB    1 
ATOM   2965 C  CG1   . ILE B 1 215 ? -0.13885  -29.34859 15.10239  1.000 25.50625  ? 279 ILE B CG1   1 
ATOM   2966 C  CG2   . ILE B 1 215 ? 0.01045   -31.84307 15.39484  1.000 24.27021  ? 279 ILE B CG2   1 
ATOM   2967 C  CD1   . ILE B 1 215 ? 1.36630   -29.43795 15.10486  1.000 30.54513  ? 279 ILE B CD1   1 
ATOM   2968 N  N     . TYR B 1 216 ? -3.14570  -32.92166 15.87605  1.000 19.88320  ? 280 TYR B N     1 
ATOM   2969 C  CA    . TYR B 1 216 ? -3.75787  -34.00933 16.61650  1.000 17.08554  ? 280 TYR B CA    1 
ATOM   2970 C  C     . TYR B 1 216 ? -2.78228  -35.16521 16.74736  1.000 17.92486  ? 280 TYR B C     1 
ATOM   2971 O  O     . TYR B 1 216 ? -1.93738  -35.39153 15.87317  1.000 17.69541  ? 280 TYR B O     1 
ATOM   2972 C  CB    . TYR B 1 216 ? -5.01966  -34.51556 15.91600  1.000 20.95982  ? 280 TYR B CB    1 
ATOM   2973 C  CG    . TYR B 1 216 ? -6.08490  -33.46765 15.73382  1.000 21.69245  ? 280 TYR B CG    1 
ATOM   2974 C  CD1   . TYR B 1 216 ? -6.03457  -32.58212 14.66428  1.000 25.68591  ? 280 TYR B CD1   1 
ATOM   2975 C  CD2   . TYR B 1 216 ? -7.14183  -33.36680 16.62524  1.000 21.78973  ? 280 TYR B CD2   1 
ATOM   2976 C  CE1   . TYR B 1 216 ? -7.00979  -31.62452 14.47987  1.000 23.53026  ? 280 TYR B CE1   1 
ATOM   2977 C  CE2   . TYR B 1 216 ? -8.12283  -32.40219 16.45864  1.000 26.34542  ? 280 TYR B CE2   1 
ATOM   2978 C  CZ    . TYR B 1 216 ? -8.05281  -31.53414 15.38520  1.000 26.44388  ? 280 TYR B CZ    1 
ATOM   2979 O  OH    . TYR B 1 216 ? -9.02768  -30.56967 15.21403  1.000 20.42393  ? 280 TYR B OH    1 
ATOM   2980 N  N     . VAL B 1 217 ? -2.93016  -35.92117 17.83175  1.000 14.90696  ? 281 VAL B N     1 
ATOM   2981 C  CA    . VAL B 1 217 ? -2.22186  -37.18032 18.02262  1.000 14.96830  ? 281 VAL B CA    1 
ATOM   2982 C  C     . VAL B 1 217 ? -3.26190  -38.25628 18.27231  1.000 14.08509  ? 281 VAL B C     1 
ATOM   2983 O  O     . VAL B 1 217 ? -4.10432  -38.11103 19.16582  1.000 15.69535  ? 281 VAL B O     1 
ATOM   2984 C  CB    . VAL B 1 217 ? -1.21503  -37.10401 19.18772  1.000 13.45860  ? 281 VAL B CB    1 
ATOM   2985 C  CG1   . VAL B 1 217 ? -0.67973  -38.48537 19.53044  1.000 12.86747  ? 281 VAL B CG1   1 
ATOM   2986 C  CG2   . VAL B 1 217 ? -0.08326  -36.17177 18.83023  1.000 12.45806  ? 281 VAL B CG2   1 
ATOM   2987 N  N     . TRP B 1 218 ? -3.20542  -39.33396 17.48758  1.000 16.28148  ? 282 TRP B N     1 
ATOM   2988 C  CA    . TRP B 1 218 ? -4.12631  -40.44722 17.67525  1.000 14.08343  ? 282 TRP B CA    1 
ATOM   2989 C  C     . TRP B 1 218 ? -3.91937  -41.02171 19.06364  1.000 18.09083  ? 282 TRP B C     1 
ATOM   2990 O  O     . TRP B 1 218 ? -2.86607  -41.60478 19.34130  1.000 17.65336  ? 282 TRP B O     1 
ATOM   2991 C  CB    . TRP B 1 218 ? -3.89434  -41.53916 16.63071  1.000 17.58857  ? 282 TRP B CB    1 
ATOM   2992 C  CG    . TRP B 1 218 ? -4.84764  -42.69117 16.72752  1.000 21.18218  ? 282 TRP B CG    1 
ATOM   2993 C  CD1   . TRP B 1 218 ? -4.55084  -43.96955 17.09158  1.000 19.74966  ? 282 TRP B CD1   1 
ATOM   2994 C  CD2   . TRP B 1 218 ? -6.24728  -42.67611 16.41672  1.000 20.48403  ? 282 TRP B CD2   1 
ATOM   2995 N  NE1   . TRP B 1 218 ? -5.68106  -44.74860 17.04371  1.000 23.88977  ? 282 TRP B NE1   1 
ATOM   2996 C  CE2   . TRP B 1 218 ? -6.73532  -43.97611 16.62881  1.000 24.23070  ? 282 TRP B CE2   1 
ATOM   2997 C  CE3   . TRP B 1 218 ? -7.13400  -41.68407 15.97961  1.000 24.58714  ? 282 TRP B CE3   1 
ATOM   2998 C  CZ2   . TRP B 1 218 ? -8.07774  -44.31710 16.42538  1.000 27.07346  ? 282 TRP B CZ2   1 
ATOM   2999 C  CZ3   . TRP B 1 218 ? -8.46638  -42.02101 15.77738  1.000 27.78507  ? 282 TRP B CZ3   1 
ATOM   3000 C  CH2   . TRP B 1 218 ? -8.92256  -43.32810 15.99677  1.000 26.34025  ? 282 TRP B CH2   1 
ATOM   3001 N  N     . SER B 1 219 ? -4.89433  -40.84250 19.94574  1.000 18.02913  ? 283 SER B N     1 
ATOM   3002 C  CA    . SER B 1 219 ? -4.75657  -41.23526 21.34585  1.000 17.21391  ? 283 SER B CA    1 
ATOM   3003 C  C     . SER B 1 219 ? -5.41804  -42.58649 21.58570  1.000 17.55699  ? 283 SER B C     1 
ATOM   3004 O  O     . SER B 1 219 ? -6.37934  -42.70497 22.34284  1.000 22.11159  ? 283 SER B O     1 
ATOM   3005 C  CB    . SER B 1 219 ? -5.35489  -40.16184 22.24415  1.000 15.68132  ? 283 SER B CB    1 
ATOM   3006 O  OG    . SER B 1 219 ? -4.81551  -40.22327 23.55927  1.000 20.00004  ? 283 SER B OG    1 
ATOM   3007 N  N     . SER B 1 220 ? -4.89335  -43.61214 20.92466  1.000 33.54266  ? 284 SER B N     1 
ATOM   3008 C  CA    . SER B 1 220 ? -5.48709  -44.94468 20.96477  1.000 37.71870  ? 284 SER B CA    1 
ATOM   3009 C  C     . SER B 1 220 ? -4.51034  -45.92152 20.32129  1.000 42.22566  ? 284 SER B C     1 
ATOM   3010 O  O     . SER B 1 220 ? -3.44602  -45.53253 19.82266  1.000 33.95646  ? 284 SER B O     1 
ATOM   3011 C  CB    . SER B 1 220 ? -6.84323  -44.97609 20.25580  1.000 36.94432  ? 284 SER B CB    1 
ATOM   3012 O  OG    . SER B 1 220 ? -7.64329  -46.04048 20.73253  1.000 41.74892  ? 284 SER B OG    1 
ATOM   3013 N  N     . LYS B 1 221 ? -4.89256  -47.19777 20.32942  1.000 51.51008  ? 285 LYS B N     1 
ATOM   3014 C  CA    . LYS B 1 221 ? -4.13953  -48.25680 19.65990  1.000 52.35379  ? 285 LYS B CA    1 
ATOM   3015 C  C     . LYS B 1 221 ? -4.35454  -48.21602 18.15003  1.000 52.82358  ? 285 LYS B C     1 
ATOM   3016 O  O     . LYS B 1 221 ? -5.15111  -47.42164 17.64189  1.000 52.56837  ? 285 LYS B O     1 
ATOM   3017 C  CB    . LYS B 1 221 ? -4.54227  -49.62890 20.20270  1.000 54.15690  ? 285 LYS B CB    1 
ATOM   3018 N  N     . GLY B 1 226 ? -8.65201  -48.39206 18.73596  1.000 55.00981  ? 327 GLY B N     1 
ATOM   3019 C  CA    . GLY B 1 226 ? -10.07953 -48.14229 18.61958  1.000 56.26014  ? 327 GLY B CA    1 
ATOM   3020 C  C     . GLY B 1 226 ? -10.44200 -47.42566 17.33215  1.000 56.11769  ? 327 GLY B C     1 
ATOM   3021 O  O     . GLY B 1 226 ? -9.63288  -47.38210 16.40769  1.000 55.49555  ? 327 GLY B O     1 
ATOM   3022 N  N     . LYS B 1 227 ? -11.65868 -46.87565 17.25125  1.000 88.46106  ? 328 LYS B N     1 
ATOM   3023 C  CA    . LYS B 1 227 ? -12.06173 -46.12337 16.06042  1.000 88.45899  ? 328 LYS B CA    1 
ATOM   3024 C  C     . LYS B 1 227 ? -13.14687 -45.12476 16.46518  1.000 88.48379  ? 328 LYS B C     1 
ATOM   3025 O  O     . LYS B 1 227 ? -14.31307 -45.50106 16.60914  1.000 90.55084  ? 328 LYS B O     1 
ATOM   3026 C  CB    . LYS B 1 227 ? -12.54419 -47.05322 14.95643  1.000 90.78953  ? 328 LYS B CB    1 
ATOM   3027 N  N     . THR B 1 228 ? -12.75175 -43.86503 16.63152  1.000 71.89048  ? 329 THR B N     1 
ATOM   3028 C  CA    . THR B 1 228 ? -13.68696 -42.78500 16.91002  1.000 71.81932  ? 329 THR B CA    1 
ATOM   3029 C  C     . THR B 1 228 ? -13.00973 -41.47110 16.55464  1.000 69.74490  ? 329 THR B C     1 
ATOM   3030 O  O     . THR B 1 228 ? -11.80096 -41.32470 16.74189  1.000 68.34669  ? 329 THR B O     1 
ATOM   3031 C  CB    . THR B 1 228 ? -14.12777 -42.77528 18.37963  1.000 72.01194  ? 329 THR B CB    1 
ATOM   3032 N  N     . VAL B 1 229 ? -13.78806 -40.52168 16.03204  1.000 48.47300  ? 330 VAL B N     1 
ATOM   3033 C  CA    . VAL B 1 229 ? -13.21670 -39.21616 15.72959  1.000 51.06308  ? 330 VAL B CA    1 
ATOM   3034 C  C     . VAL B 1 229 ? -12.86810 -38.47549 17.01328  1.000 52.37256  ? 330 VAL B C     1 
ATOM   3035 O  O     . VAL B 1 229 ? -12.01222 -37.58361 17.00441  1.000 47.45164  ? 330 VAL B O     1 
ATOM   3036 C  CB    . VAL B 1 229 ? -14.17249 -38.40476 14.82880  1.000 48.64499  ? 330 VAL B CB    1 
ATOM   3037 C  CG1   . VAL B 1 229 ? -15.38032 -37.91697 15.61350  1.000 49.31971  ? 330 VAL B CG1   1 
ATOM   3038 C  CG2   . VAL B 1 229 ? -13.43802 -37.24583 14.17078  1.000 47.44691  ? 330 VAL B CG2   1 
ATOM   3039 N  N     . TRP B 1 230 ? -13.49875 -38.84364 18.13026  1.000 54.92529  ? 331 TRP B N     1 
ATOM   3040 C  CA    . TRP B 1 230 ? -13.12309 -38.31279 19.43111  1.000 50.22472  ? 331 TRP B CA    1 
ATOM   3041 C  C     . TRP B 1 230 ? -11.78579 -38.85236 19.91770  1.000 48.91164  ? 331 TRP B C     1 
ATOM   3042 O  O     . TRP B 1 230 ? -11.28131 -38.36758 20.93527  1.000 50.10309  ? 331 TRP B O     1 
ATOM   3043 C  CB    . TRP B 1 230 ? -14.21176 -38.63188 20.45670  1.000 53.45769  ? 331 TRP B CB    1 
ATOM   3044 N  N     . ASP B 1 231 ? -11.21213 -39.84568 19.23127  1.000 37.86904  ? 332 ASP B N     1 
ATOM   3045 C  CA    . ASP B 1 231 ? -9.94589  -40.44912 19.63273  1.000 33.95623  ? 332 ASP B CA    1 
ATOM   3046 C  C     . ASP B 1 231 ? -8.73626  -39.61366 19.25258  1.000 31.29660  ? 332 ASP B C     1 
ATOM   3047 O  O     . ASP B 1 231 ? -7.61011  -40.01383 19.56142  1.000 33.23055  ? 332 ASP B O     1 
ATOM   3048 C  CB    . ASP B 1 231 ? -9.79823  -41.83809 19.02043  1.000 37.63960  ? 332 ASP B CB    1 
ATOM   3049 C  CG    . ASP B 1 231 ? -10.48410 -42.90633 19.83419  1.000 42.05424  ? 332 ASP B CG    1 
ATOM   3050 O  OD1   . ASP B 1 231 ? -10.46193 -42.80861 21.08131  1.000 42.49593  ? 332 ASP B OD1   1 
ATOM   3051 O  OD2   . ASP B 1 231 ? -11.06148 -43.83024 19.22590  1.000 40.48740  ? 332 ASP B OD2   1 
ATOM   3052 N  N     . TRP B 1 232 ? -8.92757  -38.49837 18.56170  1.000 29.89044  ? 333 TRP B N     1 
ATOM   3053 C  CA    . TRP B 1 232 ? -7.84785  -37.55537 18.32549  1.000 25.07672  ? 333 TRP B CA    1 
ATOM   3054 C  C     . TRP B 1 232 ? -7.78964  -36.59468 19.50515  1.000 26.41709  ? 333 TRP B C     1 
ATOM   3055 O  O     . TRP B 1 232 ? -8.80998  -36.00578 19.87793  1.000 29.17054  ? 333 TRP B O     1 
ATOM   3056 C  CB    . TRP B 1 232 ? -8.06002  -36.78431 17.01697  1.000 25.02986  ? 333 TRP B CB    1 
ATOM   3057 C  CG    . TRP B 1 232 ? -7.98561  -37.63669 15.76882  1.000 29.19535  ? 333 TRP B CG    1 
ATOM   3058 C  CD1   . TRP B 1 232 ? -9.03962  -38.09394 15.02415  1.000 27.08378  ? 333 TRP B CD1   1 
ATOM   3059 C  CD2   . TRP B 1 232 ? -6.79868  -38.13583 15.12365  1.000 26.38929  ? 333 TRP B CD2   1 
ATOM   3060 N  NE1   . TRP B 1 232 ? -8.58338  -38.83721 13.96224  1.000 29.37301  ? 333 TRP B NE1   1 
ATOM   3061 C  CE2   . TRP B 1 232 ? -7.21435  -38.87943 14.00176  1.000 28.08531  ? 333 TRP B CE2   1 
ATOM   3062 C  CE3   . TRP B 1 232 ? -5.42776  -38.01674 15.38159  1.000 19.54354  ? 333 TRP B CE3   1 
ATOM   3063 C  CZ2   . TRP B 1 232 ? -6.30740  -39.51156 13.14575  1.000 30.53912  ? 333 TRP B CZ2   1 
ATOM   3064 C  CZ3   . TRP B 1 232 ? -4.53202  -38.64525 14.53604  1.000 19.72846  ? 333 TRP B CZ3   1 
ATOM   3065 C  CH2   . TRP B 1 232 ? -4.97249  -39.37893 13.43191  1.000 24.26718  ? 333 TRP B CH2   1 
ATOM   3066 N  N     . GLU B 1 233 ? -6.60793  -36.46073 20.11205  1.000 22.71866  ? 334 GLU B N     1 
ATOM   3067 C  CA    . GLU B 1 233 ? -6.35324  -35.38775 21.06137  1.000 19.75191  ? 334 GLU B CA    1 
ATOM   3068 C  C     . GLU B 1 233 ? -5.74427  -34.20879 20.31678  1.000 21.30412  ? 334 GLU B C     1 
ATOM   3069 O  O     . GLU B 1 233 ? -4.71726  -34.36211 19.64655  1.000 15.65365  ? 334 GLU B O     1 
ATOM   3070 C  CB    . GLU B 1 233 ? -5.42017  -35.82989 22.18498  1.000 19.33057  ? 334 GLU B CB    1 
ATOM   3071 C  CG    . GLU B 1 233 ? -5.43432  -34.87730 23.37344  1.000 19.43523  ? 334 GLU B CG    1 
ATOM   3072 C  CD    . GLU B 1 233 ? -4.41269  -35.23872 24.44490  1.000 22.00827  ? 334 GLU B CD    1 
ATOM   3073 O  OE1   . GLU B 1 233 ? -4.09991  -36.43300 24.58245  1.000 20.70373  ? 334 GLU B OE1   1 
ATOM   3074 O  OE2   . GLU B 1 233 ? -3.93814  -34.33556 25.16081  1.000 24.57699  ? 334 GLU B OE2   1 
ATOM   3075 N  N     . LEU B 1 234 ? -6.37474  -33.03722 20.43817  1.000 15.66548  ? 335 LEU B N     1 
ATOM   3076 C  CA    . LEU B 1 234 ? -5.80746  -31.80423 19.90755  1.000 11.82888  ? 335 LEU B CA    1 
ATOM   3077 C  C     . LEU B 1 234 ? -4.67082  -31.34604 20.80971  1.000 16.96162  ? 335 LEU B C     1 
ATOM   3078 O  O     . LEU B 1 234 ? -4.84808  -31.23479 22.02994  1.000 16.72729  ? 335 LEU B O     1 
ATOM   3079 C  CB    . LEU B 1 234 ? -6.88098  -30.72615 19.82229  1.000 14.65769  ? 335 LEU B CB    1 
ATOM   3080 C  CG    . LEU B 1 234 ? -6.39624  -29.32930 19.43281  1.000 15.81185  ? 335 LEU B CG    1 
ATOM   3081 C  CD1   . LEU B 1 234 ? -5.76430  -29.33611 18.05332  1.000 15.67954  ? 335 LEU B CD1   1 
ATOM   3082 C  CD2   . LEU B 1 234 ? -7.52673  -28.30712 19.49101  1.000 19.28547  ? 335 LEU B CD2   1 
ATOM   3083 N  N     . MET B 1 235 ? -3.49736  -31.08618 20.22320  1.000 15.13933  ? 336 MET B N     1 
ATOM   3084 C  CA    . MET B 1 235 ? -2.33800  -30.73156 21.04083  1.000 14.92379  ? 336 MET B CA    1 
ATOM   3085 C  C     . MET B 1 235 ? -2.02650  -29.24465 21.10761  1.000 16.49725  ? 336 MET B C     1 
ATOM   3086 O  O     . MET B 1 235 ? -1.26627  -28.83913 21.99288  1.000 17.38723  ? 336 MET B O     1 
ATOM   3087 C  CB    . MET B 1 235 ? -1.09184  -31.49491 20.57845  1.000 19.72543  ? 336 MET B CB    1 
ATOM   3088 C  CG    . MET B 1 235 ? -1.41338  -32.90750 20.22436  1.000 17.76575  ? 336 MET B CG    1 
ATOM   3089 S  SD    . MET B 1 235 ? -1.57659  -33.80629 21.78275  1.000 19.30321  ? 336 MET B SD    1 
ATOM   3090 C  CE    . MET B 1 235 ? -0.39657  -33.02288 22.87593  1.000 16.93573  ? 336 MET B CE    1 
ATOM   3091 N  N     . ASN B 1 236 ? -2.59599  -28.42014 20.23934  1.000 15.29269  ? 337 ASN B N     1 
ATOM   3092 C  CA    . ASN B 1 236 ? -2.22941  -27.01185 20.25136  1.000 19.58095  ? 337 ASN B CA    1 
ATOM   3093 C  C     . ASN B 1 236 ? -3.46823  -26.15179 20.21755  1.000 23.59207  ? 337 ASN B C     1 
ATOM   3094 O  O     . ASN B 1 236 ? -3.43498  -25.03813 19.68920  1.000 21.27018  ? 337 ASN B O     1 
ATOM   3095 C  CB    . ASN B 1 236 ? -1.30416  -26.67170 19.07574  1.000 18.91195  ? 337 ASN B CB    1 
ATOM   3096 C  CG    . ASN B 1 236 ? -1.95007  -26.90554 17.73025  1.000 16.15193  ? 337 ASN B CG    1 
ATOM   3097 O  OD1   . ASN B 1 236 ? -2.90375  -27.66761 17.61467  1.000 17.68124  ? 337 ASN B OD1   1 
ATOM   3098 N  ND2   . ASN B 1 236 ? -1.46491  -26.19121 16.70283  1.000 21.80455  ? 337 ASN B ND2   1 
ATOM   3099 O  OXT   . ASN B 1 236 ? -4.51933  -26.57890 20.70820  1.000 19.66774  ? 337 ASN B OXT   1 
HETATM 3100 C  C96   . H71 C 2 .   ? 5.25749   -16.97866 43.52511  1.000 54.53539  ? 401 H71 A C96   1 
HETATM 3101 C  C95   . H71 C 2 .   ? 4.54807   -16.36461 42.28757  1.000 52.62914  ? 401 H71 A C95   1 
HETATM 3102 C  C97   . H71 C 2 .   ? 3.90244   -14.98189 42.63515  1.000 52.27576  ? 401 H71 A C97   1 
HETATM 3103 N  N94   . H71 C 2 .   ? 5.52426   -16.28026 41.11979  1.000 43.52628  ? 401 H71 A N94   1 
HETATM 3104 C  C93   . H71 C 2 .   ? 4.92107   -16.67887 39.82756  1.000 31.04860  ? 401 H71 A C93   1 
HETATM 3105 C  C92   . H71 C 2 .   ? 5.24486   -15.67025 38.72169  1.000 21.49928  ? 401 H71 A C92   1 
HETATM 3106 C  C91   . H71 C 2 .   ? 4.82438   -14.22265 39.04355  1.000 19.86928  ? 401 H71 A C91   1 
HETATM 3107 N  N9    . H71 C 2 .   ? 4.29270   -13.62089 37.76562  1.000 25.58928  ? 401 H71 A N9    1 
HETATM 3108 C  C4    . H71 C 2 .   ? 3.01323   -13.55606 37.42376  1.000 16.39928  ? 401 H71 A C4    1 
HETATM 3109 N  N3    . H71 C 2 .   ? 1.88281   -13.95234 38.09451  1.000 18.05928  ? 401 H71 A N3    1 
HETATM 3110 C  C2    . H71 C 2 .   ? 0.72881   -13.70641 37.40146  1.000 18.73928  ? 401 H71 A C2    1 
HETATM 3111 N  N1    . H71 C 2 .   ? 0.60356   -13.12532 36.18199  1.000 11.17928  ? 401 H71 A N1    1 
HETATM 3112 C  C6    . H71 C 2 .   ? 1.73980   -12.74388 35.52791  1.000 16.07928  ? 401 H71 A C6    1 
HETATM 3113 N  N6    . H71 C 2 .   ? 1.60315   -12.14695 34.25262  1.000 16.43928  ? 401 H71 A N6    1 
HETATM 3114 C  C5    . H71 C 2 .   ? 2.97962   -12.94786 36.13814  1.000 16.63928  ? 401 H71 A C5    1 
HETATM 3115 N  N7    . H71 C 2 .   ? 4.30543   -12.66393 35.75919  1.000 23.16928  ? 401 H71 A N7    1 
HETATM 3116 C  C8    . H71 C 2 .   ? 5.07976   -13.11302 36.77328  1.000 17.65928  ? 401 H71 A C8    1 
HETATM 3117 S  S     . H71 C 2 .   ? 6.84371   -12.96803 36.77235  1.000 18.85928  ? 401 H71 A S     1 
HETATM 3118 C  "C1'" . H71 C 2 .   ? 7.31080   -11.70941 37.94140  1.000 27.09928  ? 401 H71 A "C1'" 1 
HETATM 3119 C  "C6'" . H71 C 2 .   ? 6.42933   -10.58252 38.05098  1.000 25.59928  ? 401 H71 A "C6'" 1 
HETATM 3120 C  "C5'" . H71 C 2 .   ? 6.73083   -9.60776  38.93466  1.000 26.75928  ? 401 H71 A "C5'" 1 
HETATM 3121 O  "O3'" . H71 C 2 .   ? 5.99849   -8.41554  39.19455  1.000 24.62928  ? 401 H71 A "O3'" 1 
HETATM 3122 C  "C'2" . H71 C 2 .   ? 6.91748   -7.61576  39.94566  1.000 20.36928  ? 401 H71 A "C'2" 1 
HETATM 3123 O  "O1'" . H71 C 2 .   ? 7.89304   -8.45277  40.54443  1.000 28.26928  ? 401 H71 A "O1'" 1 
HETATM 3124 C  "C4'" . H71 C 2 .   ? 7.85412   -9.64935  39.72467  1.000 27.00928  ? 401 H71 A "C4'" 1 
HETATM 3125 C  "C3'" . H71 C 2 .   ? 8.74195   -10.68541 39.66347  1.000 29.81928  ? 401 H71 A "C3'" 1 
HETATM 3126 C  "C2'" . H71 C 2 .   ? 8.45121   -11.74153 38.75173  1.000 37.14362  ? 401 H71 A "C2'" 1 
HETATM 3127 I  I     . H71 C 2 .   ? 9.77361   -13.35363 38.64688  1.000 55.91592  ? 401 H71 A I     1 
HETATM 3128 O  O1    . PG4 D 3 .   ? -7.84414  -4.00930  30.74992  1.000 45.10835  ? 402 PG4 A O1    1 
HETATM 3129 C  C1    . PG4 D 3 .   ? -7.18273  -2.77789  30.49936  1.000 53.32085  ? 402 PG4 A C1    1 
HETATM 3130 C  C2    . PG4 D 3 .   ? -5.69008  -2.91717  30.59293  1.000 40.43080  ? 402 PG4 A C2    1 
HETATM 3131 O  O2    . PG4 D 3 .   ? -5.07145  -1.77570  30.01451  1.000 61.91723  ? 402 PG4 A O2    1 
HETATM 3132 C  C3    . PG4 D 3 .   ? -3.85889  -2.06990  29.33414  1.000 50.29339  ? 402 PG4 A C3    1 
HETATM 3133 C  C4    . PG4 D 3 .   ? -3.08317  -0.81094  29.11540  1.000 37.65287  ? 402 PG4 A C4    1 
HETATM 3134 O  O3    . PG4 D 3 .   ? -3.96666  0.23228   28.73796  1.000 57.13357  ? 402 PG4 A O3    1 
HETATM 3135 C  C5    . PG4 D 3 .   ? -3.22222  1.44164   28.71002  1.000 28.86826  ? 402 PG4 A C5    1 
HETATM 3136 C  C6    . PG4 D 3 .   ? -4.10069  2.53591   28.19313  1.000 45.13307  ? 402 PG4 A C6    1 
HETATM 3137 O  O4    . PG4 D 3 .   ? -3.85861  2.78651   26.81555  1.000 43.31976  ? 402 PG4 A O4    1 
HETATM 3138 O  O1    . PG4 E 3 .   ? -4.33804  -0.06948  33.24968  1.000 30.66430  ? 403 PG4 A O1    1 
HETATM 3139 C  C1    . PG4 E 3 .   ? -3.13647  -0.67816  33.68502  1.000 27.45949  ? 403 PG4 A C1    1 
HETATM 3140 C  C2    . PG4 E 3 .   ? -1.93308  0.05868   33.17071  1.000 26.25589  ? 403 PG4 A C2    1 
HETATM 3141 O  O2    . PG4 E 3 .   ? -1.46193  0.96262   34.16127  1.000 42.43810  ? 403 PG4 A O2    1 
HETATM 3142 C  C3    . PG4 E 3 .   ? -0.10092  1.32263   33.99200  1.000 10.72545  ? 403 PG4 A C3    1 
HETATM 3143 C  C4    . PG4 E 3 .   ? 0.21804   2.51615   34.83837  1.000 27.89849  ? 403 PG4 A C4    1 
HETATM 3144 O  O3    . PG4 E 3 .   ? -0.42421  3.68851   34.33750  1.000 35.01120  ? 403 PG4 A O3    1 
HETATM 3145 O  O1    . PG4 F 3 .   ? -6.74325  1.82525   23.23202  1.000 33.38248  ? 404 PG4 A O1    1 
HETATM 3146 C  C1    . PG4 F 3 .   ? -7.25300  0.92346   24.20193  1.000 37.77614  ? 404 PG4 A C1    1 
HETATM 3147 C  C2    . PG4 F 3 .   ? -8.20317  -0.06428  23.58990  1.000 33.60821  ? 404 PG4 A C2    1 
HETATM 3148 O  O2    . PG4 F 3 .   ? -8.21292  -1.25673  24.36170  1.000 51.87622  ? 404 PG4 A O2    1 
HETATM 3149 C  C3    . PG4 F 3 .   ? -8.89157  -1.11956  25.60200  1.000 41.83809  ? 404 PG4 A C3    1 
HETATM 3150 C  C4    . PG4 F 3 .   ? -8.40963  -2.15671  26.56584  1.000 42.94866  ? 404 PG4 A C4    1 
HETATM 3151 O  O3    . PG4 F 3 .   ? -7.49775  -1.58248  27.49511  1.000 58.36231  ? 404 PG4 A O3    1 
HETATM 3152 CA CA    . CA  G 4 .   ? -12.98244 -11.51884 45.65221  1.000 40.50928  ? 405 CA  A CA    1 
HETATM 3153 C  C96   . H71 H 2 .   ? 7.68445   -28.41809 -4.04796  1.000 53.30583  ? 401 H71 B C96   1 
HETATM 3154 C  C95   . H71 H 2 .   ? 8.15555   -27.31791 -3.05554  1.000 52.64998  ? 401 H71 B C95   1 
HETATM 3155 C  C97   . H71 H 2 .   ? 8.78485   -26.11705 -3.79554  1.000 52.63212  ? 401 H71 B C97   1 
HETATM 3156 N  N94   . H71 H 2 .   ? 9.12634   -27.92704 -2.06351  1.000 43.93308  ? 401 H71 B N94   1 
HETATM 3157 C  C93   . H71 H 2 .   ? 8.78256   -27.63997 -0.66283  1.000 31.31419  ? 401 H71 B C93   1 
HETATM 3158 C  C92   . H71 H 2 .   ? 9.14571   -28.81212 0.23016   1.000 21.27928  ? 401 H71 B C92   1 
HETATM 3159 C  C91   . H71 H 2 .   ? 8.42127   -30.12834 -0.16905  1.000 19.91928  ? 401 H71 B C91   1 
HETATM 3160 N  N9    . H71 H 2 .   ? 7.59919   -30.67397 0.99890   1.000 12.27928  ? 401 H71 B N9    1 
HETATM 3161 C  C4    . H71 H 2 .   ? 6.27474   -30.69190 1.06037   1.000 12.27928  ? 401 H71 B C4    1 
HETATM 3162 N  N3    . H71 H 2 .   ? 5.35183   -30.28053 0.15319   1.000 18.27928  ? 401 H71 B N3    1 
HETATM 3163 C  C2    . H71 H 2 .   ? 4.06029   -30.46586 0.56257   1.000 19.04928  ? 401 H71 B C2    1 
HETATM 3164 N  N1    . H71 H 2 .   ? 3.63801   -31.00893 1.73175   1.000 11.47928  ? 401 H71 B N1    1 
HETATM 3165 C  C6    . H71 H 2 .   ? 4.56597   -31.40682 2.63556   1.000 16.37928  ? 401 H71 B C6    1 
HETATM 3166 N  N6    . H71 H 2 .   ? 4.07888   -31.95887 3.83850   1.000 16.77928  ? 401 H71 B N6    1 
HETATM 3167 C  C5    . H71 H 2 .   ? 5.92819   -31.27631 2.32488   1.000 16.27928  ? 401 H71 B C5    1 
HETATM 3168 N  N7    . H71 H 2 .   ? 7.13909   -31.59499 2.99231   1.000 23.27928  ? 401 H71 B N7    1 
HETATM 3169 C  C8    . H71 H 2 .   ? 8.13734   -31.19544 2.15339   1.000 17.87928  ? 401 H71 B C8    1 
HETATM 3170 S  S     . H71 H 2 .   ? 9.86144   -31.38928 2.53680   1.000 18.27928  ? 401 H71 B S     1 
HETATM 3171 C  "C1'" . H71 H 2 .   ? 10.60361  -32.66356 1.49556   1.000 27.40928  ? 401 H71 B "C1'" 1 
HETATM 3172 C  "C6'" . H71 H 2 .   ? 9.75738   -33.76986 1.21456   1.000 25.87928  ? 401 H71 B "C6'" 1 
HETATM 3173 C  "C5'" . H71 H 2 .   ? 10.22101  -34.75621 0.43425   1.000 26.27928  ? 401 H71 B "C5'" 1 
HETATM 3174 O  "O3'" . H71 H 2 .   ? 9.52792   -35.93383 0.04798   1.000 24.87928  ? 401 H71 B "O3'" 1 
HETATM 3175 C  "C'2" . H71 H 2 .   ? 10.58785  -36.76317 -0.44688  1.000 20.67928  ? 401 H71 B "C'2" 1 
HETATM 3176 O  "O1'" . H71 H 2 .   ? 11.68013  -35.94521 -0.88329  1.000 28.57928  ? 401 H71 B "O1'" 1 
HETATM 3177 C  "C4'" . H71 H 2 .   ? 11.49089  -34.74635 -0.10595  1.000 27.27928  ? 401 H71 B "C4'" 1 
HETATM 3178 C  "C3'" . H71 H 2 .   ? 12.36378  -33.73350 0.12170   1.000 30.12928  ? 401 H71 B "C3'" 1 
HETATM 3179 C  "C2'" . H71 H 2 .   ? 11.90441  -32.66438 0.94235   1.000 38.47718  ? 401 H71 B "C2'" 1 
HETATM 3180 I  I     . H71 H 2 .   ? 13.26267  -31.10887 1.27885   1.000 57.16860  ? 401 H71 B I     1 
HETATM 3181 CA CA    . CA  I 4 .   ? 3.57096   -22.64900 8.37056   1.000 90.50928  ? 402 CA  B CA    1 
HETATM 3182 C  C     . ACT J 5 .   ? -10.95777 -34.14393 13.47063  1.000 46.39783  ? 403 ACT B C     1 
HETATM 3183 O  O     . ACT J 5 .   ? -10.92352 -33.22942 12.59125  1.000 51.13093  ? 403 ACT B O     1 
HETATM 3184 O  OXT   . ACT J 5 .   ? -10.53367 -35.31934 13.38548  1.000 51.06365  ? 403 ACT B OXT   1 
HETATM 3185 C  CH3   . ACT J 5 .   ? -11.61597 -33.75125 14.84697  1.000 32.37661  ? 403 ACT B CH3   1 
HETATM 3186 O  O2    . PG4 K 3 .   ? 2.37538   -46.56468 3.52381   1.000 42.10659  ? 404 PG4 B O2    1 
HETATM 3187 C  C3    . PG4 K 3 .   ? 2.43273   -45.20056 3.91831   1.000 18.43638  ? 404 PG4 B C3    1 
HETATM 3188 C  C4    . PG4 K 3 .   ? 1.19629   -44.81566 4.66113   1.000 32.93062  ? 404 PG4 B C4    1 
HETATM 3189 O  O3    . PG4 K 3 .   ? 0.25822   -44.15078 3.82020   1.000 42.72136  ? 404 PG4 B O3    1 
HETATM 3190 C  C5    . PG4 K 3 .   ? -0.98752  -44.21954 4.49638   1.000 19.52199  ? 404 PG4 B C5    1 
HETATM 3191 C  C6    . PG4 K 3 .   ? -2.11772  -44.11057 3.53075   1.000 38.22210  ? 404 PG4 B C6    1 
HETATM 3192 O  O4    . PG4 K 3 .   ? -3.08162  -45.11071 3.83151   1.000 51.05977  ? 404 PG4 B O4    1 
HETATM 3193 C  C1    . PEG L 6 .   ? -6.81898  -44.18983 12.95319  1.000 32.60197  ? 405 PEG B C1    1 
HETATM 3194 O  O1    . PEG L 6 .   ? -5.94495  -45.31301 12.95930  1.000 44.21974  ? 405 PEG B O1    1 
HETATM 3195 C  C2    . PEG L 6 .   ? -7.61007  -44.10982 11.68156  1.000 36.54409  ? 405 PEG B C2    1 
HETATM 3196 O  O2    . PEG L 6 .   ? -7.76328  -42.75078 11.29773  1.000 60.41562  ? 405 PEG B O2    1 
HETATM 3197 C  C3    . PEG L 6 .   ? -6.64300  -42.24285 10.58263  1.000 55.35939  ? 405 PEG B C3    1 
HETATM 3198 C  C4    . PEG L 6 .   ? -6.78070  -42.54992 9.12048   1.000 53.86646  ? 405 PEG B C4    1 
HETATM 3199 O  O4    . PEG L 6 .   ? -6.01082  -43.68147 8.73936   1.000 49.08505  ? 405 PEG B O4    1 
HETATM 3200 C  C1    . PEG M 6 .   ? -3.33580  -42.67462 7.32739   1.000 53.21434  ? 406 PEG B C1    1 
HETATM 3201 O  O1    . PEG M 6 .   ? -3.71853  -41.43162 6.75599   1.000 40.96986  ? 406 PEG B O1    1 
HETATM 3202 C  C2    . PEG M 6 .   ? -2.00598  -42.59195 8.02199   1.000 20.13149  ? 406 PEG B C2    1 
HETATM 3203 O  O2    . PEG M 6 .   ? -1.83393  -43.72313 8.86944   1.000 37.13630  ? 406 PEG B O2    1 
HETATM 3204 C  C3    . PEG M 6 .   ? -1.55842  -44.92139 8.15790   1.000 22.47364  ? 406 PEG B C3    1 
HETATM 3205 C  C4    . PEG M 6 .   ? -1.28308  -46.04965 9.10584   1.000 39.19229  ? 406 PEG B C4    1 
HETATM 3206 O  O4    . PEG M 6 .   ? -2.46997  -46.59502 9.67035   1.000 52.69397  ? 406 PEG B O4    1 
HETATM 3207 MG MG    . MG  N 7 .   ? -1.82498  -20.17194 6.54259   1.000 30.27928  ? 407 MG  B MG    1 
HETATM 3208 C  C     . ACT O 5 .   ? -9.42788  -30.12721 -7.49670  1.000 42.07644  ? 408 ACT B C     1 
HETATM 3209 O  O     . ACT O 5 .   ? -8.75513  -30.72523 -8.38399  0.605 44.18988  ? 408 ACT B O     1 
HETATM 3210 O  OXT   . ACT O 5 .   ? -9.98366  -29.00316 -7.56352  0.853 41.88118  ? 408 ACT B OXT   1 
HETATM 3211 C  CH3   . ACT O 5 .   ? -9.60585  -30.86319 -6.13071  1.000 39.42792  ? 408 ACT B CH3   1 
HETATM 3212 CA CA    . CA  P 4 .   ? -7.80516  -32.80350 -9.83456  1.000 50.27928  ? 409 CA  B CA    1 
HETATM 3213 O  O     . HOH Q 8 .   ? -1.12263  5.87577   33.98677  1.000 30.48928  ? 501 HOH A O     1 
HETATM 3214 O  O     . HOH Q 8 .   ? -0.66158  3.84041   27.32608  1.000 18.93928  ? 502 HOH A O     1 
HETATM 3215 O  O     . HOH Q 8 .   ? -4.85470  -24.82233 30.22248  1.000 30.48928  ? 503 HOH A O     1 
HETATM 3216 O  O     . HOH Q 8 .   ? -0.81546  -22.01906 26.67424  1.000 22.16928  ? 504 HOH A O     1 
HETATM 3217 O  O     . HOH Q 8 .   ? -10.40914 3.84208   37.75022  1.000 26.68928  ? 505 HOH A O     1 
HETATM 3218 O  O     . HOH Q 8 .   ? 1.48159   -21.80817 29.92871  1.000 14.90928  ? 506 HOH A O     1 
HETATM 3219 O  O     . HOH Q 8 .   ? 5.402     7.756     29.092    1.000 30.48928  ? 507 HOH A O     1 
HETATM 3220 O  O     . HOH Q 8 .   ? -5.95510  -1.65890  48.55251  1.000 16.75928  ? 508 HOH A O     1 
HETATM 3221 O  O     . HOH Q 8 .   ? -0.99124  -1.74226  19.61480  1.000 15.51928  ? 509 HOH A O     1 
HETATM 3222 O  O     . HOH Q 8 .   ? 7.339     -3.996    8.201     1.000 21.42928  ? 510 HOH A O     1 
HETATM 3223 O  O     . HOH Q 8 .   ? -2.18657  -6.77170  43.37008  1.000 17.72928  ? 511 HOH A O     1 
HETATM 3224 O  O     . HOH Q 8 .   ? -2.39790  7.16341   25.37457  1.000 30.41928  ? 512 HOH A O     1 
HETATM 3225 O  O     . HOH Q 8 .   ? 0.87055   -10.25977 31.23035  1.000 11.74928  ? 513 HOH A O     1 
HETATM 3226 O  O     . HOH Q 8 .   ? 9.86061   -14.37732 35.53772  1.000 29.99928  ? 514 HOH A O     1 
HETATM 3227 O  O     . HOH Q 8 .   ? -1.97392  -12.48513 36.11914  1.000 18.89928  ? 515 HOH A O     1 
HETATM 3228 O  O     . HOH Q 8 .   ? 14.33340  0.55146   18.38307  1.000 30.48928  ? 516 HOH A O     1 
HETATM 3229 O  O     . HOH Q 8 .   ? -0.55818  -15.49855 41.62260  1.000 21.10928  ? 517 HOH A O     1 
HETATM 3230 O  O     . HOH Q 8 .   ? -10.20756 -10.54216 40.76315  1.000 19.29928  ? 518 HOH A O     1 
HETATM 3231 O  O     . HOH Q 8 .   ? 6.68601   -18.62757 32.12595  1.000 30.48928  ? 519 HOH A O     1 
HETATM 3232 O  O     . HOH Q 8 .   ? -2.34435  -4.64950  27.15215  1.000 15.47928  ? 520 HOH A O     1 
HETATM 3233 O  O     . HOH Q 8 .   ? -7.10980  -14.57445 41.06860  1.000 15.35928  ? 521 HOH A O     1 
HETATM 3234 O  O     . HOH Q 8 .   ? 1.52242   -17.84330 37.22777  1.000 26.54928  ? 522 HOH A O     1 
HETATM 3235 O  O     . HOH Q 8 .   ? 9.34718   -16.19844 31.79595  1.000 26.07928  ? 523 HOH A O     1 
HETATM 3236 O  O     . HOH Q 8 .   ? 11.03507  -17.03052 33.74575  1.000 30.48928  ? 524 HOH A O     1 
HETATM 3237 O  O     . HOH Q 8 .   ? -4.60752  -8.37026  43.84636  1.000 18.57928  ? 525 HOH A O     1 
HETATM 3238 O  O     . HOH Q 8 .   ? 11.57375  4.34451   23.02838  1.000 25.83928  ? 526 HOH A O     1 
HETATM 3239 O  O     . HOH Q 8 .   ? -12.27079 -13.39172 38.46606  1.000 20.38928  ? 527 HOH A O     1 
HETATM 3240 O  O     . HOH Q 8 .   ? 8.94087   -7.92983  44.08367  1.000 29.58928  ? 528 HOH A O     1 
HETATM 3241 O  O     . HOH Q 8 .   ? -6.66678  -8.12073  33.25712  1.000 12.71928  ? 529 HOH A O     1 
HETATM 3242 O  O     . HOH Q 8 .   ? -11.90813 -7.39376  44.24400  1.000 30.50928  ? 530 HOH A O     1 
HETATM 3243 O  O     . HOH Q 8 .   ? 4.335     2.297     57.912    1.000 29.82928  ? 531 HOH A O     1 
HETATM 3244 O  O     . HOH Q 8 .   ? 9.06067   4.00823   17.37002  1.000 23.79928  ? 532 HOH A O     1 
HETATM 3245 O  O     . HOH Q 8 .   ? -9.10744  -3.36669  43.48994  1.000 18.02928  ? 533 HOH A O     1 
HETATM 3246 O  O     . HOH Q 8 .   ? -7.306    -3.469    13.122    1.000 20.35928  ? 534 HOH A O     1 
HETATM 3247 O  O     . HOH Q 8 .   ? 1.64723   -8.20922  51.93994  1.000 20.26928  ? 535 HOH A O     1 
HETATM 3248 O  O     . HOH Q 8 .   ? 5.40204   -10.69284 8.47495   1.000 19.32928  ? 536 HOH A O     1 
HETATM 3249 O  O     . HOH Q 8 .   ? -7.84027  -25.30939 43.96744  1.000 30.48928  ? 537 HOH A O     1 
HETATM 3250 O  O     . HOH Q 8 .   ? -9.83532  -21.01562 44.82923  1.000 31.91928  ? 538 HOH A O     1 
HETATM 3251 O  O     . HOH Q 8 .   ? -11.65654 -12.25852 47.62861  1.000 30.50928  ? 539 HOH A O     1 
HETATM 3252 O  O     . HOH Q 8 .   ? -2.72839  -12.77912 12.74602  1.000 12.50928  ? 540 HOH A O     1 
HETATM 3253 O  O     . HOH Q 8 .   ? 0.88584   -15.99211 39.80216  1.000 19.07928  ? 541 HOH A O     1 
HETATM 3254 O  O     . HOH Q 8 .   ? -6.17106  -9.83998  28.20871  1.000 15.26928  ? 542 HOH A O     1 
HETATM 3255 O  O     . HOH Q 8 .   ? 5.53969   -11.34450 33.44556  1.000 12.33928  ? 543 HOH A O     1 
HETATM 3256 O  O     . HOH Q 8 .   ? 0.99064   -2.10055  34.44793  1.000 13.38928  ? 544 HOH A O     1 
HETATM 3257 O  O     . HOH Q 8 .   ? -10.48361 -17.50164 43.05379  1.000 17.82928  ? 545 HOH A O     1 
HETATM 3258 O  O     . HOH Q 8 .   ? 2.80008   -16.48897 35.66545  1.000 14.04928  ? 546 HOH A O     1 
HETATM 3259 O  O     . HOH Q 8 .   ? -6.90991  -0.47912  44.53199  1.000 20.60928  ? 547 HOH A O     1 
HETATM 3260 O  O     . HOH Q 8 .   ? 9.36017   -19.03500 29.30792  1.000 30.27928  ? 548 HOH A O     1 
HETATM 3261 O  O     . HOH Q 8 .   ? 1.03984   -1.30828  49.42369  1.000 24.25928  ? 549 HOH A O     1 
HETATM 3262 O  O     . HOH Q 8 .   ? -12.26557 -0.62739  42.88364  1.000 30.41928  ? 550 HOH A O     1 
HETATM 3263 O  O     . HOH Q 8 .   ? 0.29807   3.51226   19.47048  1.000 25.32928  ? 551 HOH A O     1 
HETATM 3264 O  O     . HOH Q 8 .   ? -11.57765 -14.49222 22.82332  1.000 30.48928  ? 552 HOH A O     1 
HETATM 3265 O  O     . HOH Q 8 .   ? 3.33788   -11.33178 31.89823  1.000 9.04928   ? 553 HOH A O     1 
HETATM 3266 O  O     . HOH Q 8 .   ? -4.78604  -16.05785 14.14346  1.000 25.22928  ? 554 HOH A O     1 
HETATM 3267 O  O     . HOH Q 8 .   ? -7.73930  0.45134   29.59857  1.000 35.34928  ? 555 HOH A O     1 
HETATM 3268 O  O     . HOH Q 8 .   ? -7.68470  -6.81559  31.64634  1.000 23.37928  ? 556 HOH A O     1 
HETATM 3269 O  O     . HOH Q 8 .   ? 1.74783   1.53340   17.04780  1.000 24.98928  ? 557 HOH A O     1 
HETATM 3270 O  O     . HOH Q 8 .   ? 8.839     -0.791    12.001    1.000 30.27928  ? 558 HOH A O     1 
HETATM 3271 O  O     . HOH Q 8 .   ? 17.97485  1.09029   17.95097  1.000 30.41928  ? 559 HOH A O     1 
HETATM 3272 O  O     . HOH Q 8 .   ? 10.18818  -7.88645  15.19211  1.000 27.92928  ? 560 HOH A O     1 
HETATM 3273 O  O     . HOH Q 8 .   ? -15.73546 -10.27214 32.57144  1.000 41.40928  ? 561 HOH A O     1 
HETATM 3274 O  O     . HOH Q 8 .   ? -2.71996  -17.71731 43.23124  1.000 30.48928  ? 562 HOH A O     1 
HETATM 3275 O  O     . HOH Q 8 .   ? 6.855     -6.732    8.451     1.000 18.71928  ? 563 HOH A O     1 
HETATM 3276 O  O     . HOH Q 8 .   ? 3.49749   4.76828   14.08667  1.000 30.41928  ? 564 HOH A O     1 
HETATM 3277 O  O     . HOH Q 8 .   ? -14.39965 -13.97855 42.71497  1.000 38.87928  ? 565 HOH A O     1 
HETATM 3278 O  O     . HOH Q 8 .   ? -9.69757  -23.68899 44.66731  1.000 30.41928  ? 566 HOH A O     1 
HETATM 3279 O  O     . HOH Q 8 .   ? -4.99178  -18.33297 44.09707  1.000 14.72928  ? 567 HOH A O     1 
HETATM 3280 O  O     . HOH Q 8 .   ? -4.44851  5.23954   33.62350  1.000 24.14928  ? 568 HOH A O     1 
HETATM 3281 O  O     . HOH Q 8 .   ? -7.16810  -5.31712  27.89311  1.000 30.48928  ? 569 HOH A O     1 
HETATM 3282 O  O     . HOH Q 8 .   ? 8.71191   -16.81812 41.61944  1.000 35.40928  ? 570 HOH A O     1 
HETATM 3283 O  O     . HOH Q 8 .   ? 5.07163   -17.74410 35.70590  1.000 24.16928  ? 571 HOH A O     1 
HETATM 3284 O  O     . HOH Q 8 .   ? -2.267    -12.188   50.555    1.000 17.25928  ? 572 HOH A O     1 
HETATM 3285 O  O     . HOH Q 8 .   ? -13.13231 -11.24882 41.24750  1.000 30.50928  ? 573 HOH A O     1 
HETATM 3286 O  O     . HOH Q 8 .   ? 0.39865   -23.76935 26.20904  1.000 21.51928  ? 574 HOH A O     1 
HETATM 3287 O  O     . HOH Q 8 .   ? -16.29954 -26.09798 41.56494  1.000 31.04928  ? 575 HOH A O     1 
HETATM 3288 O  O     . HOH Q 8 .   ? 8.28128   7.55895   21.55937  1.000 30.41928  ? 576 HOH A O     1 
HETATM 3289 O  O     . HOH Q 8 .   ? -11.29669 -9.72089  22.02696  1.000 30.29928  ? 577 HOH A O     1 
HETATM 3290 O  O     . HOH Q 8 .   ? -7.30762  -17.25439 42.71128  1.000 14.04928  ? 578 HOH A O     1 
HETATM 3291 O  O     . HOH Q 8 .   ? -13.64609 -8.22865  42.40129  1.000 30.50928  ? 579 HOH A O     1 
HETATM 3292 O  O     . HOH Q 8 .   ? -5.00724  -4.24895  26.85812  1.000 19.09928  ? 580 HOH A O     1 
HETATM 3293 O  O     . HOH Q 8 .   ? 9.077     -8.086    7.960     1.000 29.80928  ? 581 HOH A O     1 
HETATM 3294 O  O     . HOH Q 8 .   ? 13.66913  -4.92681  17.07448  1.000 30.41928  ? 582 HOH A O     1 
HETATM 3295 O  O     . HOH Q 8 .   ? -14.22726 -4.46533  36.42339  1.000 35.75928  ? 583 HOH A O     1 
HETATM 3296 O  O     . HOH Q 8 .   ? -12.23361 -24.57880 27.96926  1.000 34.31928  ? 584 HOH A O     1 
HETATM 3297 O  O     . HOH Q 8 .   ? -16.80078 -10.24290 40.61978  1.000 30.41928  ? 585 HOH A O     1 
HETATM 3298 O  O     . HOH Q 8 .   ? -12.48728 -22.14299 46.82196  1.000 34.63928  ? 586 HOH A O     1 
HETATM 3299 O  O     . HOH Q 8 .   ? -2.76313  4.41598   21.44067  1.000 30.41928  ? 587 HOH A O     1 
HETATM 3300 O  O     . HOH Q 8 .   ? -1.15715  5.13703   29.20933  1.000 22.34928  ? 588 HOH A O     1 
HETATM 3301 O  O     . HOH Q 8 .   ? 0.970     -16.197   9.385     1.000 30.50928  ? 589 HOH A O     1 
HETATM 3302 O  O     . HOH Q 8 .   ? 15.27387  -2.46314  18.28852  1.000 30.41928  ? 590 HOH A O     1 
HETATM 3303 O  O     . HOH Q 8 .   ? -12.20661 -11.98364 24.18227  1.000 30.29928  ? 591 HOH A O     1 
HETATM 3304 O  O     . HOH Q 8 .   ? -7.04693  -7.47205  28.82089  1.000 30.48928  ? 592 HOH A O     1 
HETATM 3305 O  O     . HOH Q 8 .   ? 13.47028  5.91399   42.85046  1.000 42.79928  ? 593 HOH A O     1 
HETATM 3306 O  O     . HOH Q 8 .   ? 22.00379  2.47410   46.77540  1.000 43.43928  ? 594 HOH A O     1 
HETATM 3307 O  O     . HOH Q 8 .   ? -3.10858  9.94255   29.44309  1.000 36.95928  ? 595 HOH A O     1 
HETATM 3308 O  O     . HOH R 8 .   ? 7.70709   -48.41793 22.04980  1.000 26.10928  ? 501 HOH B O     1 
HETATM 3309 O  O     . HOH R 8 .   ? -1.17314  -51.48164 12.44197  1.000 34.55928  ? 502 HOH B O     1 
HETATM 3310 O  O     . HOH R 8 .   ? 8.99158   -25.64446 6.84548   1.000 30.48928  ? 503 HOH B O     1 
HETATM 3311 O  O     . HOH R 8 .   ? -4.35800  -31.45766 24.34592  1.000 16.89928  ? 504 HOH B O     1 
HETATM 3312 O  O     . HOH R 8 .   ? 0.63868   -48.15926 10.64922  1.000 30.27928  ? 505 HOH B O     1 
HETATM 3313 O  O     . HOH R 8 .   ? -6.74256  -48.14282 -1.46598  1.000 29.83928  ? 506 HOH B O     1 
HETATM 3314 O  O     . HOH R 8 .   ? 11.18809  -27.88016 8.21617   1.000 27.90928  ? 507 HOH B O     1 
HETATM 3315 O  O     . HOH R 8 .   ? 4.21981   -20.81151 11.48168  1.000 30.50928  ? 508 HOH B O     1 
HETATM 3316 O  O     . HOH R 8 .   ? 12.02542  -48.76252 16.90237  1.000 26.93928  ? 509 HOH B O     1 
HETATM 3317 O  O     . HOH R 8 .   ? 2.98227   -33.99878 6.97845   1.000 11.04928  ? 510 HOH B O     1 
HETATM 3318 O  O     . HOH R 8 .   ? -4.80092  -42.12149 25.24215  1.000 13.64928  ? 511 HOH B O     1 
HETATM 3319 O  O     . HOH R 8 .   ? -8.07589  -30.94785 -2.33674  1.000 18.06928  ? 512 HOH B O     1 
HETATM 3320 O  O     . HOH R 8 .   ? 4.74805   -24.94476 22.01180  1.000 30.41928  ? 513 HOH B O     1 
HETATM 3321 O  O     . HOH R 8 .   ? 2.28744   -37.55457 -5.45951  1.000 14.99928  ? 514 HOH B O     1 
HETATM 3322 O  O     . HOH R 8 .   ? 3.59152   -28.94170 -3.49781  1.000 17.39928  ? 515 HOH B O     1 
HETATM 3323 O  O     . HOH R 8 .   ? -1.11688  -23.32998 15.97260  1.000 30.23928  ? 516 HOH B O     1 
HETATM 3324 O  O     . HOH R 8 .   ? 0.79844   -25.46663 22.26259  1.000 26.24928  ? 517 HOH B O     1 
HETATM 3325 O  O     . HOH R 8 .   ? -3.00233  -29.67776 -4.06663  1.000 15.33928  ? 518 HOH B O     1 
HETATM 3326 O  O     . HOH R 8 .   ? 1.16172   -31.80058 1.83122   1.000 10.49928  ? 519 HOH B O     1 
HETATM 3327 O  O     . HOH R 8 .   ? 4.08327   -42.20718 3.83611   1.000 12.97928  ? 520 HOH B O     1 
HETATM 3328 O  O     . HOH R 8 .   ? -5.32287  -20.43887 -8.26683  1.000 37.01928  ? 521 HOH B O     1 
HETATM 3329 O  O     . HOH R 8 .   ? 13.77902  -45.30064 22.06363  1.000 31.00928  ? 522 HOH B O     1 
HETATM 3330 O  O     . HOH R 8 .   ? 2.39232   -45.28649 24.42709  1.000 30.41928  ? 523 HOH B O     1 
HETATM 3331 O  O     . HOH R 8 .   ? 3.781     -34.783   -11.758   1.000 9.02928   ? 524 HOH B O     1 
HETATM 3332 O  O     . HOH R 8 .   ? -4.49372  -40.78397 -6.91786  1.000 16.19928  ? 525 HOH B O     1 
HETATM 3333 O  O     . HOH R 8 .   ? 5.31970   -28.45328 -1.80992  1.000 19.92928  ? 526 HOH B O     1 
HETATM 3334 O  O     . HOH R 8 .   ? -0.95539  -42.89204 17.95608  1.000 13.66928  ? 527 HOH B O     1 
HETATM 3335 O  O     . HOH R 8 .   ? -0.308    -42.722   -11.321   1.000 17.13928  ? 528 HOH B O     1 
HETATM 3336 O  O     . HOH R 8 .   ? -5.90168  -33.80378 -4.52353  1.000 20.93928  ? 529 HOH B O     1 
HETATM 3337 O  O     . HOH R 8 .   ? 12.72896  -30.03385 4.40760   1.000 28.22928  ? 530 HOH B O     1 
HETATM 3338 O  O     . HOH R 8 .   ? -0.21990  -35.92834 -6.54544  1.000 17.23928  ? 531 HOH B O     1 
HETATM 3339 O  O     . HOH R 8 .   ? 6.19183   -28.00478 3.13639   1.000 10.36928  ? 532 HOH B O     1 
HETATM 3340 O  O     . HOH R 8 .   ? 13.63871  -27.45157 6.07935   1.000 35.45928  ? 533 HOH B O     1 
HETATM 3341 O  O     . HOH R 8 .   ? 2.94605   -33.65942 29.97800  1.000 20.15928  ? 534 HOH B O     1 
HETATM 3342 O  O     . HOH R 8 .   ? -11.70278 -34.54894 5.58209   1.000 30.50928  ? 535 HOH B O     1 
HETATM 3343 O  O     . HOH R 8 .   ? -1.62099  -20.35571 9.00087   1.000 31.70928  ? 536 HOH B O     1 
HETATM 3344 O  O     . HOH R 8 .   ? 4.77614   -20.80816 6.31900   1.000 30.71928  ? 537 HOH B O     1 
HETATM 3345 O  O     . HOH R 8 .   ? -1.34272  -39.61067 10.37506  1.000 12.49928  ? 538 HOH B O     1 
HETATM 3346 O  O     . HOH R 8 .   ? 6.74733   -42.89891 -10.74221 1.000 30.50928  ? 539 HOH B O     1 
HETATM 3347 O  O     . HOH R 8 .   ? -3.87702  -36.19598 3.70227   1.000 11.94928  ? 540 HOH B O     1 
HETATM 3348 O  O     . HOH R 8 .   ? 8.31315   -32.98312 5.51795   1.000 12.72928  ? 541 HOH B O     1 
HETATM 3349 O  O     . HOH R 8 .   ? -13.38957 -48.84341 18.38792  1.000 30.50928  ? 542 HOH B O     1 
HETATM 3350 O  O     . HOH R 8 .   ? -8.191    -32.717   22.634    1.000 30.41928  ? 543 HOH B O     1 
HETATM 3351 O  O     . HOH R 8 .   ? -7.67480  -25.72211 10.41032  1.000 27.34928  ? 544 HOH B O     1 
HETATM 3352 O  O     . HOH R 8 .   ? -3.95841  -34.54771 8.60929   1.000 14.00928  ? 545 HOH B O     1 
HETATM 3353 O  O     . HOH R 8 .   ? 5.78366   -32.97416 6.78057   1.000 9.50928   ? 546 HOH B O     1 
HETATM 3354 O  O     . HOH R 8 .   ? -5.47103  -26.82959 -6.61132  1.000 17.34928  ? 547 HOH B O     1 
HETATM 3355 O  O     . HOH R 8 .   ? 6.84787   -23.38911 10.69883  1.000 30.41928  ? 548 HOH B O     1 
HETATM 3356 O  O     . HOH R 8 .   ? 12.37853  -27.75879 1.17419   1.000 35.11928  ? 549 HOH B O     1 
HETATM 3357 O  O     . HOH R 8 .   ? 8.02646   -51.60614 17.55890  1.000 30.41928  ? 550 HOH B O     1 
HETATM 3358 O  O     . HOH R 8 .   ? 4.477     -53.594   -10.271   1.000 21.97928  ? 551 HOH B O     1 
HETATM 3359 O  O     . HOH R 8 .   ? -10.28938 -29.24855 12.84626  1.000 35.79928  ? 552 HOH B O     1 
HETATM 3360 O  O     . HOH R 8 .   ? 11.98361  -28.04912 -1.13945  1.000 30.19928  ? 553 HOH B O     1 
HETATM 3361 O  O     . HOH R 8 .   ? -2.43766  -43.79216 -7.57902  1.000 20.79928  ? 554 HOH B O     1 
HETATM 3362 O  O     . HOH R 8 .   ? -9.59612  -35.94644 -3.79238  1.000 32.10928  ? 555 HOH B O     1 
HETATM 3363 O  O     . HOH R 8 .   ? 4.90025   -37.67608 30.39797  1.000 30.48928  ? 556 HOH B O     1 
HETATM 3364 O  O     . HOH R 8 .   ? -1.97209  -46.58684 15.24731  1.000 25.14928  ? 557 HOH B O     1 
HETATM 3365 O  O     . HOH R 8 .   ? 7.84274   -44.23057 -13.46884 1.000 23.50928  ? 558 HOH B O     1 
HETATM 3366 O  O     . HOH R 8 .   ? 11.12184  -24.77765 8.23670   1.000 32.20928  ? 559 HOH B O     1 
HETATM 3367 O  O     . HOH R 8 .   ? 9.20635   -36.29269 24.65068  1.000 21.17928  ? 560 HOH B O     1 
HETATM 3368 O  O     . HOH R 8 .   ? 1.48090   -26.59658 -5.51706  1.000 20.76928  ? 561 HOH B O     1 
HETATM 3369 O  O     . HOH R 8 .   ? 23.75691  -40.25178 3.70057   1.000 30.48928  ? 562 HOH B O     1 
HETATM 3370 O  O     . HOH R 8 .   ? -6.82841  -21.66075 8.26781   1.000 35.16928  ? 563 HOH B O     1 
HETATM 3371 O  O     . HOH R 8 .   ? 10.56086  -28.36925 -14.13630 1.000 38.57928  ? 564 HOH B O     1 
HETATM 3372 O  O     . HOH R 8 .   ? -2.64163  -27.13440 -5.66044  1.000 15.40928  ? 565 HOH B O     1 
HETATM 3373 O  O     . HOH R 8 .   ? 1.17087   -22.18021 19.27650  1.000 34.44928  ? 566 HOH B O     1 
HETATM 3374 O  O     . HOH R 8 .   ? -0.11507  -25.95283 -6.79897  1.000 14.12928  ? 567 HOH B O     1 
HETATM 3375 O  O     . HOH R 8 .   ? -4.80129  -22.95724 -8.49216  1.000 30.48928  ? 568 HOH B O     1 
HETATM 3376 O  O     . HOH R 8 .   ? -3.90074  -50.88697 -8.28013  1.000 30.50928  ? 569 HOH B O     1 
HETATM 3377 O  O     . HOH R 8 .   ? 7.96693   -26.64622 3.17134   1.000 22.07928  ? 570 HOH B O     1 
HETATM 3378 O  O     . HOH R 8 .   ? -1.75112  -47.43571 5.67813   1.000 21.92928  ? 571 HOH B O     1 
HETATM 3379 O  O     . HOH R 8 .   ? -9.06314  -39.11023 10.25835  1.000 30.27928  ? 572 HOH B O     1 
HETATM 3380 O  O     . HOH R 8 .   ? 7.962     -43.688   27.280    1.000 31.98928  ? 573 HOH B O     1 
HETATM 3381 O  O     . HOH R 8 .   ? -8.179    -43.303   -7.103    1.000 23.27928  ? 574 HOH B O     1 
HETATM 3382 O  O     . HOH R 8 .   ? -2.07019  -49.46162 3.66533   1.000 14.93928  ? 575 HOH B O     1 
HETATM 3383 O  O     . HOH R 8 .   ? 0.649     -52.591   -15.441   1.000 28.71928  ? 576 HOH B O     1 
HETATM 3384 O  O     . HOH R 8 .   ? 1.06025   -47.60071 6.39975   1.000 17.59928  ? 577 HOH B O     1 
HETATM 3385 O  O     . HOH R 8 .   ? 4.41400   -20.70692 4.18818   1.000 29.59928  ? 578 HOH B O     1 
HETATM 3386 O  O     . HOH R 8 .   ? 4.83884   -26.52841 1.17606   1.000 30.27928  ? 579 HOH B O     1 
HETATM 3387 O  O     . HOH R 8 .   ? -2.84034  -49.08280 15.66214  1.000 27.58928  ? 580 HOH B O     1 
HETATM 3388 O  O     . HOH R 8 .   ? -4.16358  -39.97687 9.94797   1.000 19.12928  ? 581 HOH B O     1 
HETATM 3389 O  O     . HOH R 8 .   ? 10.72753  -27.26300 3.20706   1.000 29.99928  ? 582 HOH B O     1 
HETATM 3390 O  O     . HOH R 8 .   ? 10.90578  -31.02487 -2.01551  1.000 30.27928  ? 583 HOH B O     1 
HETATM 3391 O  O     . HOH R 8 .   ? -5.22991  -37.54259 5.03188   1.000 21.55928  ? 584 HOH B O     1 
HETATM 3392 O  O     . HOH R 8 .   ? 3.307     -32.201   -12.295   1.000 19.13928  ? 585 HOH B O     1 
HETATM 3393 O  O     . HOH R 8 .   ? 8.912     -42.869   29.297    1.000 30.50928  ? 586 HOH B O     1 
HETATM 3394 O  O     . HOH R 8 .   ? 0.83187   -50.01581 3.74112   1.000 19.96928  ? 587 HOH B O     1 
HETATM 3395 O  O     . HOH R 8 .   ? 3.51253   -26.35461 -4.24800  1.000 30.27928  ? 588 HOH B O     1 
HETATM 3396 O  O     . HOH R 8 .   ? -9.04920  -35.87509 -6.74284  1.000 30.27928  ? 589 HOH B O     1 
HETATM 3397 O  O     . HOH R 8 .   ? 14.74181  -41.95225 22.23199  1.000 32.20928  ? 590 HOH B O     1 
HETATM 3398 O  O     . HOH R 8 .   ? -9.11401  -34.00058 -5.64137  1.000 30.41928  ? 591 HOH B O     1 
HETATM 3399 O  O     . HOH R 8 .   ? -12.88120 -34.16637 -5.74018  1.000 30.41928  ? 592 HOH B O     1 
HETATM 3400 O  O     . HOH R 8 .   ? -6.50984  -39.12842 9.17700   1.000 30.27928  ? 593 HOH B O     1 
HETATM 3401 O  O     . HOH R 8 .   ? 11.380    -56.893   -12.005   1.000 33.11928  ? 594 HOH B O     1 
HETATM 3402 O  O     . HOH R 8 .   ? 20.95652  -31.09876 24.73900  1.000 40.08928  ? 595 HOH B O     1 
HETATM 3403 O  O     . HOH R 8 .   ? -11.76704 -51.43934 18.56054  1.000 30.50928  ? 596 HOH B O     1 
HETATM 3404 O  O     . HOH R 8 .   ? 0.61409   -49.68798 8.06673   1.000 30.48928  ? 597 HOH B O     1 
HETATM 3405 O  O     . HOH R 8 .   ? 7.66439   -24.87671 0.89950   1.000 30.27928  ? 598 HOH B O     1 
HETATM 3406 O  O     . HOH R 8 .   ? -5.14534  -36.77328 7.87623   1.000 30.27928  ? 599 HOH B O     1 
HETATM 3407 O  O     . HOH R 8 .   ? -14.96327 -36.99606 0.19550   1.000 36.57928  ? 600 HOH B O     1 
HETATM 3408 O  O     . HOH R 8 .   ? 18.18568  -34.24614 25.79733  1.000 36.45928  ? 601 HOH B O     1 
HETATM 3409 O  O     . HOH R 8 .   ? -9.44445  -22.61956 8.57368   1.000 32.74928  ? 602 HOH B O     1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N     . ARG A 6   ? 0.94865 0.70434 0.66421 -0.07896 -0.01172 0.00351  70  ARG A N     
2    C CA    . ARG A 6   ? 0.91914 0.68877 0.65696 -0.07124 -0.00805 0.00282  70  ARG A CA    
3    C C     . ARG A 6   ? 0.89991 0.70026 0.65471 -0.06896 -0.01577 0.00486  70  ARG A C     
4    O O     . ARG A 6   ? 0.87455 0.68741 0.64803 -0.06546 -0.01238 0.00409  70  ARG A O     
5    C CB    . ARG A 6   ? 0.90954 0.67878 0.66074 -0.06994 0.00281  -0.00090 70  ARG A CB    
6    N N     . GLU A 7   ? 0.87012 0.67991 0.61613 -0.07166 -0.02676 0.00671  71  GLU A N     
7    C CA    . GLU A 7   ? 0.85975 0.69567 0.61827 -0.07052 -0.03594 0.00765  71  GLU A CA    
8    C C     . GLU A 7   ? 0.87111 0.71707 0.62671 -0.06380 -0.04679 0.01083  71  GLU A C     
9    O O     . GLU A 7   ? 0.85533 0.71847 0.62578 -0.05657 -0.04981 0.01251  71  GLU A O     
10   C CB    . GLU A 7   ? 0.86833 0.71076 0.62298 -0.08083 -0.04082 0.00586  71  GLU A CB    
11   C CG    . GLU A 7   ? 0.85224 0.72198 0.62469 -0.08096 -0.04751 0.00512  71  GLU A CG    
12   C CD    . GLU A 7   ? 0.86033 0.73486 0.63000 -0.09207 -0.05028 0.00254  71  GLU A CD    
13   O OE1   . GLU A 7   ? 0.88216 0.76177 0.64272 -0.09672 -0.06143 0.00232  71  GLU A OE1   
14   O OE2   . GLU A 7   ? 0.84584 0.71906 0.62248 -0.09611 -0.04127 0.00086  71  GLU A OE2   
15   N N     . LYS A 8   ? 0.81230 0.64708 0.54852 -0.06559 -0.05258 0.01209  72  LYS A N     
16   C CA    . LYS A 8   ? 0.82532 0.66893 0.55801 -0.05855 -0.06289 0.01582  72  LYS A CA    
17   C C     . LYS A 8   ? 0.81458 0.65458 0.55359 -0.04813 -0.05699 0.01833  72  LYS A C     
18   O O     . LYS A 8   ? 0.81869 0.66988 0.56049 -0.04048 -0.06416 0.02223  72  LYS A O     
19   C CB    . LYS A 8   ? 0.85972 0.68816 0.56817 -0.06263 -0.06882 0.01659  72  LYS A CB    
20   N N     . SER A 9   ? 0.77960 0.60478 0.52180 -0.04759 -0.04418 0.01618  73  SER A N     
21   C CA    . SER A 9   ? 0.76709 0.59003 0.51800 -0.03882 -0.03780 0.01738  73  SER A CA    
22   C C     . SER A 9   ? 0.94981 0.78738 0.72307 -0.03579 -0.03321 0.01626  73  SER A C     
23   O O     . SER A 9   ? 0.93799 0.77516 0.72014 -0.02908 -0.02790 0.01674  73  SER A O     
24   C CB    . SER A 9   ? 0.77445 0.57294 0.51552 -0.03932 -0.02745 0.01490  73  SER A CB    
25   O OG    . SER A 9   ? 0.80525 0.58783 0.52365 -0.04192 -0.03128 0.01603  73  SER A OG    
26   N N     . GLU A 10  ? 0.73534 0.58547 0.51744 -0.04087 -0.03503 0.01454  74  GLU A N     
27   C CA    . GLU A 10  ? 0.70773 0.57159 0.50967 -0.03804 -0.03128 0.01361  74  GLU A CA    
28   C C     . GLU A 10  ? 0.70187 0.58910 0.51345 -0.03704 -0.04095 0.01523  74  GLU A C     
29   O O     . GLU A 10  ? 0.68516 0.58398 0.51063 -0.03081 -0.04052 0.01655  74  GLU A O     
30   C CB    . GLU A 10  ? 0.69335 0.55065 0.50112 -0.04397 -0.02192 0.00938  74  GLU A CB    
31   C CG    . GLU A 10  ? 0.69769 0.53351 0.49901 -0.04439 -0.01274 0.00672  74  GLU A CG    
32   C CD    . GLU A 10  ? 0.68747 0.51506 0.49356 -0.04994 -0.00478 0.00247  74  GLU A CD    
33   O OE1   . GLU A 10  ? 0.67715 0.51676 0.49083 -0.05431 -0.00602 0.00255  74  GLU A OE1   
34   O OE2   . GLU A 10  ? 0.68747 0.50361 0.49290 -0.04764 0.00281  -0.00088 74  GLU A OE2   
35   N N     . LYS A 11  ? 0.66424 0.55924 0.46986 -0.04300 -0.04992 0.01481  75  LYS A N     
36   C CA    . LYS A 11  ? 0.69387 0.61378 0.51203 -0.04229 -0.05998 0.01542  75  LYS A CA    
37   C C     . LYS A 11  ? 0.67491 0.60590 0.49214 -0.03440 -0.07108 0.02020  75  LYS A C     
38   O O     . LYS A 11  ? 0.70632 0.62983 0.50844 -0.03547 -0.07632 0.02163  75  LYS A O     
39   C CB    . LYS A 11  ? 0.63841 0.56396 0.45444 -0.05322 -0.06432 0.01196  75  LYS A CB    
40   N N     . PHE A 12  ? 0.64303 0.59130 0.47631 -0.02599 -0.07433 0.02309  76  PHE A N     
41   C CA    . PHE A 12  ? 0.60130 0.56361 0.43773 -0.01712 -0.08457 0.02848  76  PHE A CA    
42   C C     . PHE A 12  ? 0.60013 0.59028 0.45829 -0.01405 -0.09247 0.02905  76  PHE A C     
43   O O     . PHE A 12  ? 0.60097 0.59769 0.47128 -0.01845 -0.08903 0.02548  76  PHE A O     
44   C CB    . PHE A 12  ? 0.61967 0.57266 0.45478 -0.00675 -0.07904 0.03341  76  PHE A CB    
45   C CG    . PHE A 12  ? 0.62549 0.55163 0.44728 -0.00931 -0.06748 0.03150  76  PHE A CG    
46   C CD1   . PHE A 12  ? 0.62407 0.54102 0.45142 -0.01226 -0.05624 0.02758  76  PHE A CD1   
47   C CD2   . PHE A 12  ? 0.63371 0.54468 0.43866 -0.00845 -0.06798 0.03348  76  PHE A CD2   
48   C CE1   . PHE A 12  ? 0.63095 0.52629 0.45006 -0.01384 -0.04594 0.02548  76  PHE A CE1   
49   C CE2   . PHE A 12  ? 0.57105 0.45847 0.36622 -0.01041 -0.05728 0.03122  76  PHE A CE2   
50   C CZ    . PHE A 12  ? 0.54996 0.43080 0.35359 -0.01297 -0.04640 0.02707  76  PHE A CZ    
51   N N     . ALA A 13  ? 0.77613 0.78301 0.64020 -0.00601 -0.10275 0.03378  77  ALA A N     
52   C CA    . ALA A 13  ? 0.79293 0.82688 0.68063 -0.00016 -0.10999 0.03509  77  ALA A CA    
53   C C     . ALA A 13  ? 0.78421 0.82509 0.67866 0.01518  -0.11042 0.04244  77  ALA A C     
54   O O     . ALA A 13  ? 0.78319 0.81307 0.66369 0.01939  -0.10934 0.04734  77  ALA A O     
55   C CB    . ALA A 13  ? 0.82266 0.87480 0.71575 -0.00574 -0.12297 0.03320  77  ALA A CB    
56   N N     . PHE A 14  ? 0.62757 0.68541 0.54404 0.02307  -0.11111 0.04333  78  PHE A N     
57   C CA    . PHE A 14  ? 0.60846 0.67142 0.53350 0.03758  -0.10806 0.05029  78  PHE A CA    
58   C C     . PHE A 14  ? 0.67890 0.75391 0.60460 0.04540  -0.11804 0.05445  78  PHE A C     
59   O O     . PHE A 14  ? 0.64873 0.73522 0.57673 0.04217  -0.13097 0.05091  78  PHE A O     
60   C CB    . PHE A 14  ? 0.61777 0.68575 0.56505 0.04343  -0.10594 0.04672  78  PHE A CB    
61   C CG    . PHE A 14  ? 0.58485 0.64291 0.53288 0.03864  -0.09400 0.04471  78  PHE A CG    
62   C CD1   . PHE A 14  ? 0.55896 0.60711 0.50896 0.03760  -0.08265 0.05373  78  PHE A CD1   
63   C CD2   . PHE A 14  ? 0.52284 0.58465 0.47676 0.02759  -0.09484 0.03899  78  PHE A CD2   
64   C CE1   . PHE A 14  ? 0.49607 0.53021 0.44521 0.03426  -0.07437 0.04992  78  PHE A CE1   
65   C CE2   . PHE A 14  ? 0.43000 0.48115 0.38375 0.02369  -0.08445 0.03688  78  PHE A CE2   
66   C CZ    . PHE A 14  ? 0.43886 0.47694 0.38824 0.02992  -0.07423 0.04119  78  PHE A CZ    
67   N N     . GLN A 15  ? 0.92028 0.99632 0.84887 0.05116  -0.11214 0.06588  79  GLN A N     
68   C CA    . GLN A 15  ? 0.91114 1.00211 0.84384 0.05827  -0.11970 0.07316  79  GLN A CA    
69   C C     . GLN A 15  ? 0.98539 1.05483 0.92944 0.06806  -0.14094 0.05780  79  GLN A C     
70   O O     . GLN A 15  ? 0.95632 1.03036 0.92252 0.06242  -0.13848 0.05856  79  GLN A O     
71   C CB    . GLN A 15  ? 0.86208 0.93082 0.79783 0.05306  -0.12048 0.08820  79  GLN A CB    
72   N N     . ALA A 16  ? 0.86258 0.94460 0.81045 0.07203  -0.15410 0.06092  80  ALA A N     
73   C CA    . ALA A 16  ? 0.78414 0.89118 0.76394 0.07240  -0.16404 0.06440  80  ALA A CA    
74   C C     . ALA A 16  ? 0.85490 0.96004 0.85723 0.07725  -0.15844 0.07218  80  ALA A C     
75   O O     . ALA A 16  ? 0.86670 0.99263 0.89423 0.07946  -0.15512 0.07072  80  ALA A O     
76   C CB    . ALA A 16  ? 0.87345 0.99408 0.85191 0.07746  -0.17862 0.06708  80  ALA A CB    
77   N N     . GLU A 17  ? 0.95156 1.03756 0.94649 0.07915  -0.15484 0.08148  81  GLU A N     
78   C CA    . GLU A 17  ? 0.86719 0.95350 0.87763 0.08772  -0.14449 0.08616  81  GLU A CA    
79   C C     . GLU A 17  ? 0.85461 0.93432 0.86656 0.08351  -0.13077 0.08070  81  GLU A C     
80   O O     . GLU A 17  ? 0.87985 0.96770 0.90951 0.08966  -0.12270 0.07878  81  GLU A O     
81   C CB    . GLU A 17  ? 0.86007 0.93047 0.85892 0.09242  -0.14142 0.09561  81  GLU A CB    
82   N N     . VAL A 18  ? 1.21350 1.27896 1.20680 0.07247  -0.12631 0.07822  82  VAL A N     
83   C CA    . VAL A 18  ? 1.14095 1.19966 1.13430 0.06848  -0.11376 0.07327  82  VAL A CA    
84   C C     . VAL A 18  ? 1.10750 1.18476 1.11820 0.06839  -0.11454 0.06549  82  VAL A C     
85   O O     . VAL A 18  ? 1.14117 1.22160 1.16481 0.07127  -0.10410 0.06326  82  VAL A O     
86   C CB    . VAL A 18  ? 1.10601 1.15253 1.07799 0.05670  -0.10805 0.07368  82  VAL A CB    
87   N N     . ASN A 19  ? 0.65970 0.75245 0.67107 0.06480  -0.12452 0.06092  83  ASN A N     
88   C CA    . ASN A 19  ? 0.66017 0.77857 0.69299 0.06173  -0.12323 0.05596  83  ASN A CA    
89   C C     . ASN A 19  ? 0.64700 0.78429 0.70776 0.07035  -0.12115 0.05941  83  ASN A C     
90   O O     . ASN A 19  ? 0.66025 0.80927 0.73885 0.06946  -0.11237 0.05673  83  ASN A O     
91   C CB    . ASN A 19  ? 0.58923 0.72368 0.61865 0.05340  -0.13327 0.05191  83  ASN A CB    
92   N N     . ARG A 20  ? 0.75528 0.89466 0.81902 0.07906  -0.12852 0.06534  84  ARG A N     
93   C CA    . ARG A 20  ? 0.78278 0.93899 0.87128 0.08859  -0.12574 0.06867  84  ARG A CA    
94   C C     . ARG A 20  ? 0.77084 0.91364 0.86194 0.09426  -0.11040 0.06881  84  ARG A C     
95   O O     . ARG A 20  ? 0.70101 0.85701 0.81197 0.09877  -0.10346 0.06805  84  ARG A O     
96   C CB    . ARG A 20  ? 0.80977 0.96864 0.89820 0.09720  -0.13667 0.07555  84  ARG A CB    
97   N N     . MET A 21  ? 0.66909 0.78535 0.73960 0.09349  -0.10456 0.06945  85  MET A N     
98   C CA    . MET A 21  ? 0.63532 0.73739 0.70546 0.09771  -0.09009 0.06825  85  MET A CA    
99   C C     . MET A 21  ? 0.61090 0.71962 0.69111 0.09297  -0.08087 0.06186  85  MET A C     
100  O O     . MET A 21  ? 0.61208 0.71766 0.69949 0.09764  -0.07040 0.06034  85  MET A O     
101  C CB    . MET A 21  ? 0.53076 0.60545 0.57736 0.09528  -0.08555 0.06930  85  MET A CB    
102  N N     . MET A 22  ? 0.75958 0.87628 0.83882 0.08331  -0.08432 0.05793  86  MET A N     
103  C CA    . MET A 22  ? 0.70898 0.83398 0.79927 0.07853  -0.07576 0.05246  86  MET A CA    
104  C C     . MET A 22  ? 0.74963 0.89706 0.86500 0.08287  -0.07422 0.05259  86  MET A C     
105  O O     . MET A 22  ? 0.76037 0.90687 0.88395 0.08457  -0.06343 0.04978  86  MET A O     
106  C CB    . MET A 22  ? 0.74282 0.87391 0.82760 0.06664  -0.08007 0.04856  86  MET A CB    
107  C CG    . MET A 22  ? 0.76492 0.87399 0.82821 0.06102  -0.07506 0.04614  86  MET A CG    
108  S SD    . MET A 22  ? 0.81694 0.89924 0.85436 0.06347  -0.07883 0.05070  86  MET A SD    
109  C CE    . MET A 22  ? 0.68428 0.76657 0.70389 0.05264  -0.08985 0.04850  86  MET A CE    
110  N N     . LYS A 23  ? 0.89529 1.06238 1.02234 0.08449  -0.08498 0.05572  87  LYS A N     
111  C CA    . LYS A 23  ? 0.89143 1.08154 1.04386 0.08855  -0.08377 0.05638  87  LYS A CA    
112  C C     . LYS A 23  ? 0.88792 1.06931 1.04460 0.09980  -0.07390 0.05849  87  LYS A C     
113  O O     . LYS A 23  ? 0.92449 1.11739 1.09815 0.10218  -0.06693 0.05709  87  LYS A O     
114  C CB    . LYS A 23  ? 0.95446 1.16540 1.11715 0.08962  -0.09799 0.06024  87  LYS A CB    
115  N N     . LEU A 24  ? 0.83734 0.99741 0.97763 0.10606  -0.07270 0.06162  88  LEU A N     
116  C CA    . LEU A 24  ? 0.84554 0.99419 0.98603 0.11527  -0.06260 0.06292  88  LEU A CA    
117  C C     . LEU A 24  ? 0.86840 1.00080 1.00108 0.11129  -0.04969 0.05707  88  LEU A C     
118  O O     . LEU A 24  ? 0.85091 0.98550 0.99258 0.11472  -0.04101 0.05540  88  LEU A O     
119  C CB    . LEU A 24  ? 0.90340 1.03439 1.02835 0.12193  -0.06525 0.06797  88  LEU A CB    
120  N N     . ILE A 25  ? 0.88745 1.00324 1.00279 0.10395  -0.04848 0.05398  89  ILE A N     
121  C CA    . ILE A 25  ? 0.83313 0.93161 0.93908 0.10028  -0.03716 0.04863  89  ILE A CA    
122  C C     . ILE A 25  ? 0.80512 0.91666 0.92462 0.09575  -0.03207 0.04396  89  ILE A C     
123  O O     . ILE A 25  ? 0.81344 0.91928 0.93474 0.09761  -0.02290 0.04122  89  ILE A O     
124  C CB    . ILE A 25  ? 0.81271 0.89301 0.89895 0.09331  -0.03756 0.04677  89  ILE A CB    
125  N N     . ILE A 26  ? 0.92308 1.05168 1.05104 0.08900  -0.03799 0.04288  90  ILE A N     
126  C CA    . ILE A 26  ? 0.95685 1.09668 1.09649 0.08307  -0.03259 0.03806  90  ILE A CA    
127  C C     . ILE A 26  ? 0.95577 1.11080 1.11455 0.08882  -0.02917 0.03883  90  ILE A C     
128  O O     . ILE A 26  ? 0.94644 1.09817 1.10819 0.08823  -0.01980 0.03495  90  ILE A O     
129  C CB    . ILE A 26  ? 0.93500 1.09046 1.07922 0.07330  -0.04006 0.03690  90  ILE A CB    
130  N N     . ASN A 27  ? 1.02099 1.19270 1.19238 0.09451  -0.03690 0.04395  91  ASN A N     
131  C CA    . ASN A 27  ? 1.05412 1.24304 1.24583 0.10024  -0.03387 0.04531  91  ASN A CA    
132  C C     . ASN A 27  ? 1.01894 1.19163 1.20456 0.10921  -0.02408 0.04612  91  ASN A C     
133  O O     . ASN A 27  ? 1.10841 1.28627 1.30402 0.11135  -0.01624 0.04451  91  ASN A O     
134  C CB    . ASN A 27  ? 1.11919 1.33055 1.32601 0.10428  -0.04540 0.05098  91  ASN A CB    
135  N N     . SER A 28  ? 0.58783 0.74020 0.75610 0.11389  -0.02418 0.04856  92  SER A N     
136  C CA    . SER A 28  ? 0.57626 0.71369 0.73806 0.12193  -0.01565 0.04983  92  SER A CA    
137  C C     . SER A 28  ? 0.54617 0.66545 0.69576 0.11710  -0.00512 0.04395  92  SER A C     
138  O O     . SER A 28  ? 0.62294 0.74073 0.77503 0.12194  0.00379  0.04489  92  SER A O     
139  C CB    . SER A 28  ? 0.56017 0.68160 0.70697 0.12740  -0.01884 0.05409  92  SER A CB    
140  O OG    . SER A 28  ? 0.63401 0.74231 0.76472 0.12004  -0.02271 0.05202  92  SER A OG    
141  N N     . LEU A 29  ? 0.51025 0.61671 0.64601 0.10827  -0.00540 0.03947  93  LEU A N     
142  C CA    . LEU A 29  ? 0.47147 0.56011 0.59276 0.10407  0.00390  0.03560  93  LEU A CA    
143  C C     . LEU A 29  ? 0.45175 0.54893 0.58055 0.09696  0.00715  0.03048  93  LEU A C     
144  O O     . LEU A 29  ? 0.45374 0.53735 0.56985 0.09080  0.01185  0.02660  93  LEU A O     
145  C CB    . LEU A 29  ? 0.45023 0.51940 0.55171 0.09895  0.00244  0.03405  93  LEU A CB    
146  C CG    . LEU A 29  ? 0.45107 0.50977 0.54272 0.10480  -0.00031 0.03867  93  LEU A CG    
147  C CD1   . LEU A 29  ? 0.44708 0.50133 0.53110 0.09936  -0.00810 0.03830  93  LEU A CD1   
148  C CD2   . LEU A 29  ? 0.45463 0.49270 0.52930 0.10707  0.00849  0.03889  93  LEU A CD2   
149  N N     . TYR A 30  ? 0.70883 0.82869 0.85810 0.09751  0.00482  0.03050  94  TYR A N     
150  C CA    . TYR A 30  ? 0.67596 0.80504 0.83275 0.09007  0.00793  0.02541  94  TYR A CA    
151  C C     . TYR A 30  ? 0.70058 0.81782 0.84979 0.09047  0.01894  0.02401  94  TYR A C     
152  O O     . TYR A 30  ? 0.67921 0.79621 0.82700 0.08339  0.02236  0.01950  94  TYR A O     
153  C CB    . TYR A 30  ? 0.73513 0.89275 0.91655 0.09075  0.00401  0.02690  94  TYR A CB    
154  N N     . LYS A 31  ? 0.53607 0.64271 0.67935 0.09846  0.02454  0.02806  95  LYS A N     
155  C CA    . LYS A 31  ? 0.52060 0.61352 0.65435 0.09888  0.03450  0.02759  95  LYS A CA    
156  C C     . LYS A 31  ? 0.48678 0.55419 0.59650 0.09571  0.03697  0.02655  95  LYS A C     
157  O O     . LYS A 31  ? 0.52209 0.57678 0.62153 0.09349  0.04373  0.02548  95  LYS A O     
158  C CB    . LYS A 31  ? 0.53292 0.62913 0.67420 0.10925  0.04038  0.03288  95  LYS A CB    
159  N N     . ASN A 32  ? 0.71824 0.77837 0.81902 0.09501  0.03143  0.02703  96  ASN A N     
160  C CA    . ASN A 32  ? 0.70186 0.73978 0.78124 0.09212  0.03358  0.02638  96  ASN A CA    
161  C C     . ASN A 32  ? 0.64215 0.67706 0.71507 0.08353  0.02797  0.02272  96  ASN A C     
162  O O     . ASN A 32  ? 0.58906 0.61384 0.65111 0.08283  0.02519  0.02340  96  ASN A O     
163  C CB    . ASN A 32  ? 0.72026 0.74953 0.79265 0.09983  0.03402  0.03082  96  ASN A CB    
164  C CG    . ASN A 32  ? 0.77348 0.78051 0.82491 0.09838  0.03946  0.03060  96  ASN A CG    
165  O OD1   . ASN A 32  ? 0.74026 0.73916 0.78403 0.09350  0.04393  0.02832  96  ASN A OD1   
166  N ND2   . ASN A 32  ? 0.78637 0.78355 0.82817 0.10256  0.03896  0.03314  96  ASN A ND2   
167  N N     . LYS A 33  ? 0.40319 0.44673 0.48259 0.07711  0.02691  0.01893  97  LYS A N     
168  C CA    . LYS A 33  ? 0.33537 0.37843 0.41089 0.06965  0.02184  0.01576  97  LYS A CA    
169  C C     . LYS A 33  ? 0.35830 0.38195 0.41461 0.06491  0.02352  0.01482  97  LYS A C     
170  O O     . LYS A 33  ? 0.30828 0.32832 0.35900 0.06119  0.01934  0.01397  97  LYS A O     
171  C CB    . LYS A 33  ? 0.29169 0.34582 0.37570 0.06372  0.02235  0.01173  97  LYS A CB    
172  C CG    . LYS A 33  ? 0.32033 0.39744 0.42481 0.06552  0.01886  0.01167  97  LYS A CG    
173  C CD    . LYS A 33  ? 0.33544 0.42216 0.44638 0.05899  0.02149  0.00728  97  LYS A CD    
174  C CE    . LYS A 33  ? 0.40840 0.52008 0.54038 0.05822  0.01710  0.00656  97  LYS A CE    
175  N NZ    . LYS A 33  ? 0.43648 0.55939 0.57699 0.05371  0.02210  0.00320  97  LYS A NZ    
176  N N     A GLU A 34  ? 0.34720 0.35884 0.39359 0.06479  0.02949  0.01528  98  GLU A N     
177  N N     B GLU A 34  ? 0.34717 0.35886 0.39360 0.06477  0.02951  0.01526  98  GLU A N     
178  C CA    A GLU A 34  ? 0.33327 0.32926 0.36308 0.05950  0.03075  0.01449  98  GLU A CA    
179  C CA    B GLU A 34  ? 0.33323 0.32928 0.36312 0.05939  0.03087  0.01443  98  GLU A CA    
180  C C     A GLU A 34  ? 0.34055 0.32729 0.36093 0.06234  0.02964  0.01650  98  GLU A C     
181  C C     B GLU A 34  ? 0.33871 0.32584 0.35922 0.06162  0.02926  0.01622  98  GLU A C     
182  O O     A GLU A 34  ? 0.35590 0.33103 0.36323 0.05821  0.03078  0.01584  98  GLU A O     
183  O O     B GLU A 34  ? 0.34998 0.32676 0.35832 0.05672  0.02951  0.01527  98  GLU A O     
184  C CB    A GLU A 34  ? 0.35113 0.33822 0.37367 0.05824  0.03680  0.01466  98  GLU A CB    
185  C CB    B GLU A 34  ? 0.35248 0.33927 0.37496 0.05895  0.03712  0.01494  98  GLU A CB    
186  C CG    A GLU A 34  ? 0.37215 0.35455 0.39312 0.06581  0.04191  0.01770  98  GLU A CG    
187  C CG    B GLU A 34  ? 0.37614 0.35399 0.39190 0.06561  0.04133  0.01796  98  GLU A CG    
188  C CD    A GLU A 34  ? 0.38326 0.37871 0.41986 0.07147  0.04395  0.01885  98  GLU A CD    
189  C CD    B GLU A 34  ? 0.39030 0.36134 0.40161 0.06656  0.04793  0.01881  98  GLU A CD    
190  O OE1   A GLU A 34  ? 0.38955 0.39620 0.43653 0.06820  0.04255  0.01660  98  GLU A OE1   
191  O OE1   B GLU A 34  ? 0.36254 0.33913 0.38036 0.06397  0.04931  0.01761  98  GLU A OE1   
192  O OE2   A GLU A 34  ? 0.40287 0.39760 0.44136 0.07924  0.04742  0.02206  98  GLU A OE2   
193  O OE2   B GLU A 34  ? 0.44106 0.40020 0.44140 0.06990  0.05202  0.02068  98  GLU A OE2   
194  N N     A ILE A 35  ? 0.40853 0.40069 0.43545 0.06925  0.02733  0.01911  99  ILE A N     
195  N N     B ILE A 35  ? 0.40817 0.39967 0.43440 0.06892  0.02759  0.01899  99  ILE A N     
196  C CA    A ILE A 35  ? 0.40753 0.39076 0.42536 0.07195  0.02588  0.02110  99  ILE A CA    
197  C CA    B ILE A 35  ? 0.40690 0.38959 0.42413 0.07157  0.02611  0.02094  99  ILE A CA    
198  C C     A ILE A 35  ? 0.37994 0.36115 0.39310 0.06601  0.02111  0.01943  99  ILE A C     
199  C C     B ILE A 35  ? 0.37986 0.36110 0.39305 0.06600  0.02111  0.01943  99  ILE A C     
200  O O     A ILE A 35  ? 0.37068 0.34199 0.37337 0.06604  0.02078  0.02022  99  ILE A O     
201  O O     B ILE A 35  ? 0.37097 0.34271 0.37416 0.06636  0.02060  0.02036  99  ILE A O     
202  C CB    A ILE A 35  ? 0.42967 0.42029 0.45667 0.08125  0.02403  0.02511  99  ILE A CB    
203  C CB    B ILE A 35  ? 0.43011 0.41960 0.45608 0.08107  0.02470  0.02498  99  ILE A CB    
204  C CG1   A ILE A 35  ? 0.46327 0.44134 0.47834 0.08551  0.02487  0.02771  99  ILE A CG1   
205  C CG1   B ILE A 35  ? 0.47669 0.45221 0.49001 0.08606  0.02805  0.02756  99  ILE A CG1   
206  C CG2   A ILE A 35  ? 0.38150 0.38708 0.42179 0.08113  0.01651  0.02546  99  ILE A CG2   
207  C CG2   B ILE A 35  ? 0.39700 0.39788 0.43270 0.08148  0.01683  0.02591  99  ILE A CG2   
208  C CD1   A ILE A 35  ? 0.48244 0.46640 0.50526 0.09572  0.02399  0.03250  99  ILE A CD1   
209  C CD1   B ILE A 35  ? 0.47748 0.44401 0.48376 0.08832  0.03565  0.02799  99  ILE A CD1   
210  N N     . PHE A 36  ? 0.31299 0.30272 0.33304 0.06091  0.01805  0.01709  100 PHE A N     
211  C CA    . PHE A 36  ? 0.27466 0.26298 0.29108 0.05611  0.01379  0.01608  100 PHE A CA    
212  C C     . PHE A 36  ? 0.27498 0.25047 0.27684 0.05064  0.01641  0.01469  100 PHE A C     
213  O O     . PHE A 36  ? 0.25971 0.22961 0.25488 0.04954  0.01446  0.01519  100 PHE A O     
214  C CB    . PHE A 36  ? 0.26802 0.26677 0.29339 0.05165  0.01132  0.01358  100 PHE A CB    
215  C CG    . PHE A 36  ? 0.28182 0.27645 0.30182 0.04482  0.01517  0.01057  100 PHE A CG    
216  C CD1   . PHE A 36  ? 0.25822 0.25448 0.28096 0.04495  0.01925  0.00987  100 PHE A CD1   
217  C CD2   . PHE A 36  ? 0.24563 0.23445 0.25746 0.03842  0.01474  0.00920  100 PHE A CD2   
218  C CE1   . PHE A 36  ? 0.24748 0.23910 0.26460 0.03876  0.02202  0.00828  100 PHE A CE1   
219  C CE2   . PHE A 36  ? 0.26103 0.24672 0.26832 0.03239  0.01775  0.00771  100 PHE A CE2   
220  C CZ    . PHE A 36  ? 0.21224 0.19907 0.22210 0.03249  0.02097  0.00746  100 PHE A CZ    
221  N N     . LEU A 37  ? 0.28695 0.25840 0.28414 0.04706  0.02056  0.01324  101 LEU A N     
222  C CA    . LEU A 37  ? 0.28641 0.24869 0.27186 0.04177  0.02229  0.01225  101 LEU A CA    
223  C C     . LEU A 37  ? 0.30219 0.25485 0.27861 0.04524  0.02337  0.01356  101 LEU A C     
224  O O     . LEU A 37  ? 0.30570 0.25305 0.27497 0.04226  0.02259  0.01295  101 LEU A O     
225  C CB    . LEU A 37  ? 0.29046 0.25078 0.27323 0.03828  0.02576  0.01148  101 LEU A CB    
226  C CG    . LEU A 37  ? 0.21575 0.17147 0.19030 0.03176  0.02637  0.01050  101 LEU A CG    
227  C CD1   . LEU A 37  ? 0.29260 0.25228 0.26849 0.02730  0.02372  0.00965  101 LEU A CD1   
228  C CD2   . LEU A 37  ? 0.24962 0.20527 0.22363 0.02868  0.02877  0.01040  101 LEU A CD2   
229  N N     . ARG A 38  ? 0.29460 0.24465 0.27115 0.05182  0.02562  0.01545  102 ARG A N     
230  C CA    . ARG A 38  ? 0.34959 0.28946 0.31704 0.05598  0.02699  0.01698  102 ARG A CA    
231  C C     . ARG A 38  ? 0.33092 0.27079 0.29822 0.05715  0.02311  0.01799  102 ARG A C     
232  O O     . ARG A 38  ? 0.36404 0.29493 0.32157 0.05543  0.02348  0.01760  102 ARG A O     
233  C CB    . ARG A 38  ? 0.36637 0.30478 0.33552 0.06411  0.03017  0.01957  102 ARG A CB    
234  C CG    . ARG A 38  ? 0.40055 0.32560 0.35760 0.06839  0.03319  0.02109  102 ARG A CG    
235  C CD    . ARG A 38  ? 0.42254 0.34718 0.38231 0.07738  0.03675  0.02427  102 ARG A CD    
236  N NE    . ARG A 38  ? 0.48877 0.42141 0.45788 0.08386  0.03331  0.02735  102 ARG A NE    
237  C CZ    . ARG A 38  ? 0.57245 0.51009 0.54904 0.09242  0.03498  0.03081  102 ARG A CZ    
238  N NH1   . ARG A 38  ? 0.58331 0.51759 0.55840 0.09581  0.04098  0.03161  102 ARG A NH1   
239  N NH2   . ARG A 38  ? 0.60426 0.55055 0.58996 0.09795  0.03049  0.03393  102 ARG A NH2   
240  N N     . GLU A 39  ? 0.27360 0.22342 0.25162 0.06002  0.01913  0.01944  103 GLU A N     
241  C CA    . GLU A 39  ? 0.28545 0.23469 0.26265 0.06168  0.01486  0.02126  103 GLU A CA    
242  C C     . GLU A 39  ? 0.26475 0.21020 0.23552 0.05426  0.01381  0.01890  103 GLU A C     
243  O O     . GLU A 39  ? 0.31219 0.24977 0.27474 0.05434  0.01330  0.01963  103 GLU A O     
244  C CB    . GLU A 39  ? 0.30553 0.26778 0.29632 0.06539  0.00954  0.02358  103 GLU A CB    
245  C CG    . GLU A 39  ? 0.30841 0.27654 0.30741 0.07411  0.00991  0.02683  103 GLU A CG    
246  C CD    . GLU A 39  ? 0.37297 0.33017 0.36254 0.08040  0.01257  0.02966  103 GLU A CD    
247  O OE1   . GLU A 39  ? 0.33390 0.28357 0.31515 0.08028  0.01058  0.03084  103 GLU A OE1   
248  O OE2   . GLU A 39  ? 0.37928 0.33470 0.36910 0.08569  0.01710  0.03086  103 GLU A OE2   
249  N N     . LEU A 40  ? 0.23913 0.18995 0.21335 0.04813  0.01391  0.01626  104 LEU A N     
250  C CA    . LEU A 40  ? 0.23378 0.18204 0.20258 0.04158  0.01356  0.01430  104 LEU A CA    
251  C C     . LEU A 40  ? 0.23651 0.17550 0.19484 0.03889  0.01703  0.01308  104 LEU A C     
252  O O     . LEU A 40  ? 0.24097 0.17498 0.19309 0.03642  0.01688  0.01257  104 LEU A O     
253  C CB    . LEU A 40  ? 0.15460 0.11031 0.12886 0.03621  0.01366  0.01216  104 LEU A CB    
254  C CG    . LEU A 40  ? 0.15399 0.11906 0.13882 0.03753  0.00998  0.01271  104 LEU A CG    
255  C CD1   . LEU A 40  ? 0.18864 0.15811 0.17574 0.03146  0.01117  0.01025  104 LEU A CD1   
256  C CD2   . LEU A 40  ? 0.17418 0.13852 0.15850 0.03956  0.00512  0.01512  104 LEU A CD2   
257  N N     . ILE A 41  ? 0.24788 0.18428 0.20419 0.03943  0.02008  0.01272  105 ILE A N     
258  C CA    . ILE A 41  ? 0.24390 0.17171 0.19096 0.03691  0.02270  0.01170  105 ILE A CA    
259  C C     . ILE A 41  ? 0.26341 0.18092 0.20252 0.04092  0.02321  0.01309  105 ILE A C     
260  O O     . ILE A 41  ? 0.24646 0.15698 0.17835 0.03799  0.02414  0.01219  105 ILE A O     
261  C CB    . ILE A 41  ? 0.32422 0.25090 0.27038 0.03685  0.02540  0.01129  105 ILE A CB    
262  C CG1   . ILE A 41  ? 0.21340 0.14693 0.16321 0.03069  0.02536  0.00973  105 ILE A CG1   
263  C CG2   . ILE A 41  ? 0.37591 0.29077 0.31162 0.03769  0.02780  0.01117  105 ILE A CG2   
264  C CD1   . ILE A 41  ? 0.27995 0.21113 0.22730 0.03002  0.02772  0.00945  105 ILE A CD1   
265  N N     . SER A 42  ? 0.32011 0.23659 0.26072 0.04792  0.02272  0.01559  106 SER A N     
266  C CA    . SER A 42  ? 0.32445 0.23068 0.25683 0.05223  0.02330  0.01746  106 SER A CA    
267  C C     . SER A 42  ? 0.29903 0.20389 0.22894 0.04966  0.02087  0.01743  106 SER A C     
268  O O     . SER A 42  ? 0.26444 0.15951 0.18513 0.04819  0.02250  0.01707  106 SER A O     
269  C CB    . SER A 42  ? 0.35129 0.25870 0.28728 0.06103  0.02283  0.02093  106 SER A CB    
270  O OG    . SER A 42  ? 0.42174 0.32795 0.35792 0.06416  0.02635  0.02121  106 SER A OG    
271  N N     . ASN A 43  ? 0.26936 0.18324 0.20692 0.04888  0.01718  0.01784  107 ASN A N     
272  C CA    . ASN A 43  ? 0.25211 0.16386 0.18624 0.04651  0.01508  0.01799  107 ASN A CA    
273  C C     . ASN A 43  ? 0.22333 0.13137 0.15202 0.03963  0.01774  0.01502  107 ASN A C     
274  O O     . ASN A 43  ? 0.27298 0.17275 0.19381 0.03876  0.01874  0.01518  107 ASN A O     
275  C CB    . ASN A 43  ? 0.22159 0.14345 0.16448 0.04584  0.01074  0.01868  107 ASN A CB    
276  C CG    . ASN A 43  ? 0.27483 0.20206 0.22474 0.05295  0.00688  0.02262  107 ASN A CG    
277  O OD1   . ASN A 43  ? 0.27728 0.19953 0.22407 0.05901  0.00757  0.02511  107 ASN A OD1   
278  N ND2   . ASN A 43  ? 0.27087 0.20886 0.23074 0.05242  0.00284  0.02345  107 ASN A ND2   
279  N N     . ALA A 44  ? 0.28853 0.20295 0.22171 0.03500  0.01898  0.01270  108 ALA A N     
280  C CA    . ALA A 44  ? 0.24274 0.15574 0.17293 0.02916  0.02123  0.01054  108 ALA A CA    
281  C C     . ALA A 44  ? 0.25879 0.16054 0.18053 0.02967  0.02358  0.01077  108 ALA A C     
282  O O     . ALA A 44  ? 0.27175 0.16860 0.18914 0.02683  0.02476  0.01025  108 ALA A O     
283  C CB    . ALA A 44  ? 0.22727 0.14842 0.16338 0.02562  0.02201  0.00896  108 ALA A CB    
284  N N     . SER A 45  ? 0.26498 0.16163 0.18388 0.03345  0.02466  0.01164  109 SER A N     
285  C CA    . SER A 45  ? 0.21492 0.09906 0.12440 0.03389  0.02713  0.01180  109 SER A CA    
286  C C     . SER A 45  ? 0.25551 0.13064 0.15780 0.03676  0.02745  0.01354  109 SER A C     
287  O O     . SER A 45  ? 0.29303 0.15930 0.18853 0.03420  0.02937  0.01313  109 SER A O     
288  C CB    . SER A 45  ? 0.26188 0.14104 0.16817 0.03798  0.02886  0.01244  109 SER A CB    
289  O OG    . SER A 45  ? 0.28589 0.15113 0.18148 0.03825  0.03147  0.01249  109 SER A OG    
290  N N     . ASP A 46  ? 0.29726 0.17431 0.20111 0.04216  0.02542  0.01578  110 ASP A N     
291  C CA    . ASP A 46  ? 0.31256 0.18092 0.20892 0.04533  0.02526  0.01789  110 ASP A CA    
292  C C     . ASP A 46  ? 0.32800 0.19594 0.22264 0.03992  0.02529  0.01663  110 ASP A C     
293  O O     . ASP A 46  ? 0.33038 0.18766 0.21617 0.03956  0.02742  0.01719  110 ASP A O     
294  C CB    . ASP A 46  ? 0.29282 0.16576 0.19325 0.05189  0.02172  0.02097  110 ASP A CB    
295  C CG    . ASP A 46  ? 0.34222 0.21369 0.24321 0.05905  0.02257  0.02320  110 ASP A CG    
296  O OD1   . ASP A 46  ? 0.36771 0.23217 0.26341 0.05886  0.02637  0.02215  110 ASP A OD1   
297  O OD2   . ASP A 46  ? 0.37670 0.25431 0.28372 0.06488  0.01936  0.02622  110 ASP A OD2   
298  N N     . ALA A 47  ? 0.27352 0.15231 0.17601 0.03599  0.02348  0.01506  111 ALA A N     
299  C CA    . ALA A 47  ? 0.28428 0.16301 0.18527 0.03127  0.02427  0.01382  111 ALA A CA    
300  C C     . ALA A 47  ? 0.29840 0.17382 0.19786 0.02629  0.02774  0.01212  111 ALA A C     
301  O O     . ALA A 47  ? 0.30019 0.17069 0.19566 0.02374  0.02979  0.01192  111 ALA A O     
302  C CB    . ALA A 47  ? 0.28833 0.17877 0.19745 0.02863  0.02212  0.01248  111 ALA A CB    
303  N N     . LEU A 48  ? 0.27917 0.15695 0.18200 0.02488  0.02831  0.01109  112 LEU A N     
304  C CA    . LEU A 48  ? 0.29719 0.17072 0.19887 0.02048  0.03062  0.00995  112 LEU A CA    
305  C C     . LEU A 48  ? 0.31033 0.16883 0.20155 0.02204  0.03294  0.01119  112 LEU A C     
306  O O     . LEU A 48  ? 0.31768 0.17045 0.20652 0.01838  0.03511  0.01090  112 LEU A O     
307  C CB    . LEU A 48  ? 0.26905 0.14782 0.17584 0.01882  0.02990  0.00864  112 LEU A CB    
308  C CG    . LEU A 48  ? 0.27286 0.16547 0.18941 0.01601  0.02861  0.00731  112 LEU A CG    
309  C CD1   . LEU A 48  ? 0.24179 0.14015 0.16262 0.01596  0.02756  0.00655  112 LEU A CD1   
310  C CD2   . LEU A 48  ? 0.29091 0.18575 0.21112 0.01120  0.02987  0.00629  112 LEU A CD2   
311  N N     . ASP A 49  ? 0.34181 0.19344 0.22683 0.02768  0.03292  0.01276  113 ASP A N     
312  C CA    . ASP A 49  ? 0.33209 0.16819 0.20546 0.03002  0.03565  0.01422  113 ASP A CA    
313  C C     . ASP A 49  ? 0.33797 0.16917 0.20662 0.02962  0.03674  0.01527  113 ASP A C     
314  O O     . ASP A 49  ? 0.42097 0.24152 0.28287 0.02721  0.03989  0.01541  113 ASP A O     
315  C CB    . ASP A 49  ? 0.34701 0.17778 0.21514 0.03763  0.03559  0.01625  113 ASP A CB    
316  C CG    . ASP A 49  ? 0.37816 0.20545 0.24456 0.03815  0.03692  0.01541  113 ASP A CG    
317  O OD1   . ASP A 49  ? 0.34478 0.16678 0.20869 0.03298  0.03844  0.01368  113 ASP A OD1   
318  O OD2   . ASP A 49  ? 0.35412 0.18336 0.22145 0.04392  0.03650  0.01664  113 ASP A OD2   
319  N N     . LYS A 50  ? 0.37180 0.20974 0.24338 0.03169  0.03430  0.01601  114 LYS A N     
320  C CA    . LYS A 50  ? 0.35870 0.19032 0.22372 0.03191  0.03534  0.01711  114 LYS A CA    
321  C C     . LYS A 50  ? 0.38991 0.22125 0.25644 0.02534  0.03843  0.01551  114 LYS A C     
322  O O     . LYS A 50  ? 0.41325 0.23304 0.27185 0.02430  0.04200  0.01624  114 LYS A O     
323  C CB    . LYS A 50  ? 0.37354 0.21259 0.24168 0.03448  0.03146  0.01791  114 LYS A CB    
324  C CG    . LYS A 50  ? 0.50714 0.34471 0.37334 0.04204  0.02830  0.02075  114 LYS A CG    
325  C CD    . LYS A 50  ? 0.59314 0.42786 0.45439 0.04532  0.02543  0.02314  114 LYS A CD    
326  C CE    . LYS A 50  ? 0.62789 0.46332 0.48962 0.05347  0.02145  0.02694  114 LYS A CE    
327  N NZ    . LYS A 50  ? 0.58049 0.43098 0.45565 0.05411  0.01728  0.02686  114 LYS A NZ    
328  N N     . ILE A 51  ? 0.35245 0.19626 0.22952 0.02108  0.03751  0.01353  115 ILE A N     
329  C CA    . ILE A 51  ? 0.36960 0.21439 0.24991 0.01572  0.04057  0.01245  115 ILE A CA    
330  C C     . ILE A 51  ? 0.33834 0.17593 0.21795 0.01242  0.04303  0.01236  115 ILE A C     
331  O O     . ILE A 51  ? 0.37034 0.20274 0.24912 0.00904  0.04642  0.01256  115 ILE A O     
332  C CB    . ILE A 51  ? 0.36480 0.22437 0.25662 0.01277  0.03926  0.01056  115 ILE A CB    
333  C CG1   . ILE A 51  ? 0.31085 0.17096 0.20545 0.00893  0.04291  0.00996  115 ILE A CG1   
334  C CG2   . ILE A 51  ? 0.30731 0.17474 0.20749 0.01110  0.03728  0.00939  115 ILE A CG2   
335  C CD1   . ILE A 51  ? 0.30718 0.16032 0.19309 0.01062  0.04496  0.01068  115 ILE A CD1   
336  N N     . ARG A 52  ? 0.33873 0.17492 0.21829 0.01323  0.04151  0.01209  116 ARG A N     
337  C CA    . ARG A 52  ? 0.34886 0.17541 0.22543 0.01006  0.04342  0.01192  116 ARG A CA    
338  C C     . ARG A 52  ? 0.38245 0.19242 0.24598 0.01190  0.04702  0.01361  116 ARG A C     
339  O O     . ARG A 52  ? 0.44072 0.24254 0.30237 0.00760  0.04998  0.01367  116 ARG A O     
340  C CB    . ARG A 52  ? 0.40376 0.23050 0.28052 0.01112  0.04130  0.01110  116 ARG A CB    
341  C CG    . ARG A 52  ? 0.42360 0.24374 0.30043 0.00598  0.04189  0.01009  116 ARG A CG    
342  C CD    . ARG A 52  ? 0.50394 0.31699 0.37375 0.00862  0.04131  0.00967  116 ARG A CD    
343  N NE    . ARG A 52  ? 0.62832 0.43243 0.49567 0.00350  0.04160  0.00852  116 ARG A NE    
344  C CZ    . ARG A 52  ? 0.60318 0.39616 0.46087 0.00487  0.04226  0.00802  116 ARG A CZ    
345  N NH1   . ARG A 52  ? 0.57436 0.36393 0.42461 0.01183  0.04324  0.00891  116 ARG A NH1   
346  N NH2   . ARG A 52  ? 0.58515 0.36996 0.44069 -0.00087 0.04193  0.00667  116 ARG A NH2   
347  N N     . LEU A 53  ? 0.27255 0.07684 0.12708 0.01838  0.04678  0.01520  117 LEU A N     
348  C CA    . LEU A 53  ? 0.33924 0.12727 0.18028 0.02090  0.05042  0.01707  117 LEU A CA    
349  C C     . LEU A 53  ? 0.36922 0.15541 0.20901 0.01845  0.05310  0.01753  117 LEU A C     
350  O O     . LEU A 53  ? 0.36497 0.13830 0.19688 0.01667  0.05749  0.01832  117 LEU A O     
351  C CB    . LEU A 53  ? 0.35122 0.13421 0.18377 0.02926  0.04909  0.01916  117 LEU A CB    
352  C CG    . LEU A 53  ? 0.36739 0.14631 0.19660 0.03352  0.04856  0.01954  117 LEU A CG    
353  C CD1   . LEU A 53  ? 0.41479 0.19749 0.24346 0.04179  0.04552  0.02169  117 LEU A CD1   
354  C CD2   . LEU A 53  ? 0.40995 0.16998 0.22569 0.03397  0.05324  0.02031  117 LEU A CD2   
355  N N     A ILE A 54  ? 0.37914 0.17686 0.22561 0.01842  0.05104  0.01701  118 ILE A N     
356  N N     B ILE A 54  ? 0.37868 0.17630 0.22504 0.01845  0.05107  0.01703  118 ILE A N     
357  C CA    A ILE A 54  ? 0.38992 0.18558 0.23443 0.01646  0.05409  0.01725  118 ILE A CA    
358  C CA    B ILE A 54  ? 0.39055 0.18567 0.23470 0.01646  0.05424  0.01730  118 ILE A CA    
359  C C     A ILE A 54  ? 0.38421 0.18049 0.23582 0.00969  0.05770  0.01636  118 ILE A C     
360  C C     B ILE A 54  ? 0.38515 0.18122 0.23667 0.00965  0.05777  0.01637  118 ILE A C     
361  O O     A ILE A 54  ? 0.40966 0.19687 0.25618 0.00783  0.06249  0.01718  118 ILE A O     
362  O O     B ILE A 54  ? 0.40837 0.19550 0.25500 0.00771  0.06255  0.01717  118 ILE A O     
363  C CB    A ILE A 54  ? 0.34929 0.15678 0.19913 0.01761  0.05103  0.01648  118 ILE A CB    
364  C CB    B ILE A 54  ? 0.35281 0.15916 0.20169 0.01771  0.05133  0.01660  118 ILE A CB    
365  C CG1   A ILE A 54  ? 0.35891 0.16168 0.19952 0.02412  0.04792  0.01821  118 ILE A CG1   
366  C CG1   B ILE A 54  ? 0.35983 0.16384 0.20169 0.02432  0.04733  0.01815  118 ILE A CG1   
367  C CG2   A ILE A 54  ? 0.37045 0.17930 0.22242 0.01395  0.05476  0.01574  118 ILE A CG2   
368  C CG2   B ILE A 54  ? 0.38324 0.18663 0.22966 0.01539  0.05537  0.01645  118 ILE A CG2   
369  C CD1   A ILE A 54  ? 0.33270 0.14779 0.17984 0.02516  0.04321  0.01738  118 ILE A CD1   
370  C CD1   B ILE A 54  ? 0.41011 0.19854 0.23688 0.02824  0.04943  0.02043  118 ILE A CD1   
371  N N     . SER A 55  ? 0.37446 0.18092 0.23805 0.00603  0.05539  0.01490  119 SER A N     
372  C CA    . SER A 55  ? 0.39094 0.19952 0.26386 -0.00039 0.05744  0.01441  119 SER A CA    
373  C C     . SER A 55  ? 0.44289 0.23647 0.30904 -0.00325 0.06063  0.01530  119 SER A C     
374  O O     . SER A 55  ? 0.42509 0.21765 0.29770 -0.00883 0.06311  0.01557  119 SER A O     
375  C CB    . SER A 55  ? 0.34497 0.16726 0.23128 -0.00295 0.05313  0.01284  119 SER A CB    
376  O OG    . SER A 55  ? 0.47957 0.29639 0.36370 -0.00395 0.05120  0.01245  119 SER A OG    
377  N N     . LEU A 56  ? 0.39530 0.17677 0.24873 0.00044  0.06085  0.01593  120 LEU A N     
378  C CA    . LEU A 56  ? 0.44331 0.20797 0.28753 -0.00201 0.06491  0.01674  120 LEU A CA    
379  C C     . LEU A 56  ? 0.48703 0.24229 0.32441 -0.00241 0.07057  0.01823  120 LEU A C     
380  O O     . LEU A 56  ? 0.50673 0.25241 0.34287 -0.00738 0.07459  0.01872  120 LEU A O     
381  C CB    . LEU A 56  ? 0.43533 0.18763 0.26554 0.00323  0.06483  0.01726  120 LEU A CB    
382  C CG    . LEU A 56  ? 0.40579 0.16193 0.23842 0.00416  0.06082  0.01593  120 LEU A CG    
383  C CD1   . LEU A 56  ? 0.44012 0.18440 0.25806 0.01164  0.06178  0.01718  120 LEU A CD1   
384  C CD2   . LEU A 56  ? 0.45956 0.21149 0.29594 -0.00307 0.06080  0.01455  120 LEU A CD2   
385  N N     . THR A 57  ? 0.49401 0.25072 0.32615 0.00256  0.07100  0.01898  121 THR A N     
386  C CA    . THR A 57  ? 0.48542 0.23157 0.30834 0.00317  0.07658  0.02035  121 THR A CA    
387  C C     . THR A 57  ? 0.48651 0.24260 0.31868 0.00074  0.07823  0.01988  121 THR A C     
388  O O     . THR A 57  ? 0.52416 0.27135 0.34928 0.00070  0.08368  0.02085  121 THR A O     
389  C CB    . THR A 57  ? 0.52001 0.25685 0.32702 0.01104  0.07613  0.02179  121 THR A CB    
390  O OG1   . THR A 57  ? 0.52653 0.27629 0.33855 0.01504  0.06995  0.02119  121 THR A OG1   
391  C CG2   . THR A 57  ? 0.54839 0.26932 0.34214 0.01410  0.07758  0.02300  121 THR A CG2   
392  N N     . ASP A 58  ? 0.48810 0.26128 0.33470 -0.00084 0.07423  0.01843  122 ASP A N     
393  C CA    . ASP A 58  ? 0.47850 0.26130 0.33286 -0.00182 0.07575  0.01781  122 ASP A CA    
394  C C     . ASP A 58  ? 0.53660 0.33281 0.40940 -0.00715 0.07415  0.01697  122 ASP A C     
395  O O     . ASP A 58  ? 0.48656 0.29449 0.36741 -0.00680 0.06881  0.01573  122 ASP A O     
396  C CB    . ASP A 58  ? 0.45819 0.24765 0.30910 0.00324  0.07180  0.01697  122 ASP A CB    
397  C CG    . ASP A 58  ? 0.53815 0.33471 0.39374 0.00276  0.07396  0.01597  122 ASP A CG    
398  O OD1   . ASP A 58  ? 0.48365 0.28267 0.34785 -0.00105 0.07841  0.01598  122 ASP A OD1   
399  O OD2   . ASP A 58  ? 0.47107 0.27061 0.32199 0.00630  0.07099  0.01522  122 ASP A OD2   
400  N N     . GLU A 59  ? 0.79188 0.58604 0.67149 -0.01201 0.07870  0.01793  123 GLU A N     
401  C CA    . GLU A 59  ? 0.77385 0.57976 0.67148 -0.01729 0.07663  0.01790  123 GLU A CA    
402  C C     . GLU A 59  ? 0.68217 0.50333 0.59041 -0.01581 0.07530  0.01683  123 GLU A C     
403  O O     . GLU A 59  ? 0.77632 0.60852 0.69922 -0.01906 0.07236  0.01685  123 GLU A O     
404  C CB    . GLU A 59  ? 0.78964 0.58923 0.69258 -0.02307 0.08181  0.01987  123 GLU A CB    
405  N N     . ASN A 60  ? 0.45187 0.27282 0.35231 -0.01112 0.07726  0.01595  124 ASN A N     
406  C CA    . ASN A 60  ? 0.47661 0.31002 0.38461 -0.00931 0.07645  0.01448  124 ASN A CA    
407  C C     . ASN A 60  ? 0.45789 0.29817 0.36278 -0.00576 0.07046  0.01269  124 ASN A C     
408  O O     . ASN A 60  ? 0.43284 0.28207 0.34164 -0.00400 0.06971  0.01114  124 ASN A O     
409  C CB    . ASN A 60  ? 0.45461 0.28218 0.35591 -0.00713 0.08299  0.01440  124 ASN A CB    
410  N N     . ALA A 61  ? 0.49606 0.33185 0.39420 -0.00465 0.06657  0.01292  125 ALA A N     
411  C CA    . ALA A 61  ? 0.46061 0.30133 0.35490 -0.00092 0.06149  0.01179  125 ALA A CA    
412  C C     . ALA A 61  ? 0.44163 0.29753 0.34878 -0.00185 0.05763  0.01026  125 ALA A C     
413  O O     . ALA A 61  ? 0.39165 0.25422 0.29824 0.00071  0.05507  0.00900  125 ALA A O     
414  C CB    . ALA A 61  ? 0.41616 0.24822 0.30150 0.00094  0.05893  0.01271  125 ALA A CB    
415  N N     . LEU A 62  ? 0.39290 0.25374 0.31134 -0.00566 0.05691  0.01046  126 LEU A N     
416  C CA    . LEU A 62  ? 0.43707 0.31065 0.36631 -0.00631 0.05281  0.00923  126 LEU A CA    
417  C C     . LEU A 62  ? 0.46875 0.35172 0.40907 -0.00731 0.05487  0.00877  126 LEU A C     
418  O O     . LEU A 62  ? 0.49790 0.39078 0.44800 -0.00814 0.05189  0.00810  126 LEU A O     
419  C CB    . LEU A 62  ? 0.40101 0.27312 0.33460 -0.00961 0.04944  0.00976  126 LEU A CB    
420  C CG    . LEU A 62  ? 0.42973 0.29560 0.35431 -0.00761 0.04649  0.00947  126 LEU A CG    
421  C CD1   . LEU A 62  ? 0.45237 0.32059 0.38293 -0.01038 0.04242  0.00895  126 LEU A CD1   
422  C CD2   . LEU A 62  ? 0.34198 0.21141 0.26064 -0.00265 0.04494  0.00867  126 LEU A CD2   
423  N N     . ALA A 63  ? 0.48649 0.36560 0.42468 -0.00675 0.06026  0.00914  127 ALA A N     
424  C CA    . ALA A 63  ? 0.45670 0.34253 0.40581 -0.00745 0.06344  0.00920  127 ALA A CA    
425  C C     . ALA A 63  ? 0.44246 0.33903 0.39596 -0.00470 0.06185  0.00696  127 ALA A C     
426  O O     . ALA A 63  ? 0.49104 0.39599 0.45650 -0.00535 0.06159  0.00708  127 ALA A O     
427  C CB    . ALA A 63  ? 0.43316 0.31051 0.37672 -0.00661 0.07044  0.00984  127 ALA A CB    
428  N N     . GLY A 64  ? 0.59730 0.49316 0.54117 -0.00173 0.06070  0.00512  128 GLY A N     
429  C CA    . GLY A 64  ? 0.53270 0.43721 0.47944 0.00052  0.05976  0.00278  128 GLY A CA    
430  C C     . GLY A 64  ? 0.56590 0.48021 0.51957 0.00016  0.05465  0.00216  128 GLY A C     
431  O O     . GLY A 64  ? 0.52313 0.44592 0.48185 0.00143  0.05299  0.00079  128 GLY A O     
432  N N     . ASN A 65  ? 0.54597 0.45877 0.49975 -0.00175 0.05089  0.00350  129 ASN A N     
433  C CA    . ASN A 65  ? 0.48803 0.40784 0.44760 -0.00253 0.04628  0.00320  129 ASN A CA    
434  C C     . ASN A 65  ? 0.56098 0.47434 0.51963 -0.00533 0.04353  0.00486  129 ASN A C     
435  O O     . ASN A 65  ? 0.56481 0.47017 0.51412 -0.00458 0.04305  0.00534  129 ASN A O     
436  C CB    . ASN A 65  ? 0.47389 0.39764 0.42827 -0.00003 0.04405  0.00172  129 ASN A CB    
437  C CG    . ASN A 65  ? 0.47143 0.40490 0.43306 0.00004  0.04156  0.00071  129 ASN A CG    
438  O OD1   . ASN A 65  ? 0.54231 0.47734 0.51025 -0.00197 0.03938  0.00143  129 ASN A OD1   
439  N ND2   . ASN A 65  ? 0.42822 0.37025 0.39279 0.00120  0.03734  0.00031  129 ASN A ND2   
440  N N     . GLU A 66  ? 0.63463 0.55010 0.60223 -0.00857 0.04148  0.00584  130 GLU A N     
441  C CA    . GLU A 66  ? 0.69154 0.59855 0.65731 -0.01201 0.03915  0.00722  130 GLU A CA    
442  C C     . GLU A 66  ? 0.70086 0.60674 0.66264 -0.01149 0.03481  0.00628  130 GLU A C     
443  O O     . GLU A 66  ? 0.65912 0.55604 0.61689 -0.01367 0.03330  0.00683  130 GLU A O     
444  C CB    . GLU A 66  ? 0.66480 0.57281 0.64130 -0.01687 0.03803  0.00920  130 GLU A CB    
445  C CG    . GLU A 66  ? 0.69346 0.60756 0.67778 -0.01631 0.04203  0.00996  130 GLU A CG    
446  C CD    . GLU A 66  ? 0.85075 0.75745 0.83068 -0.01617 0.04797  0.01093  130 GLU A CD    
447  O OE1   . GLU A 66  ? 0.87652 0.78644 0.86100 -0.01470 0.05253  0.01125  130 GLU A OE1   
448  O OE2   . GLU A 66  ? 0.94966 0.84626 0.92115 -0.01731 0.04853  0.01141  130 GLU A OE2   
449  N N     . GLU A 67  ? 0.43504 0.34878 0.39704 -0.00860 0.03352  0.00479  131 GLU A N     
450  C CA    . GLU A 67  ? 0.41791 0.33155 0.37663 -0.00765 0.03020  0.00394  131 GLU A CA    
451  C C     . GLU A 67  ? 0.44506 0.35409 0.39348 -0.00413 0.03109  0.00380  131 GLU A C     
452  O O     . GLU A 67  ? 0.40521 0.31500 0.35026 -0.00191 0.03335  0.00393  131 GLU A O     
453  C CB    . GLU A 67  ? 0.44233 0.36715 0.40775 -0.00676 0.02875  0.00287  131 GLU A CB    
454  C CG    . GLU A 67  ? 0.42225 0.35340 0.38462 -0.00318 0.03030  0.00183  131 GLU A CG    
455  C CD    . GLU A 67  ? 0.42162 0.36133 0.38826 -0.00256 0.02878  0.00087  131 GLU A CD    
456  O OE1   . GLU A 67  ? 0.37104 0.31733 0.34506 -0.00300 0.02938  0.00043  131 GLU A OE1   
457  O OE2   . GLU A 67  ? 0.43858 0.37822 0.40103 -0.00127 0.02755  0.00072  131 GLU A OE2   
458  N N     . LEU A 68  ? 0.33587 0.23901 0.27886 -0.00355 0.02913  0.00368  132 LEU A N     
459  C CA    . LEU A 68  ? 0.38648 0.28408 0.32017 0.00024  0.02959  0.00408  132 LEU A CA    
460  C C     . LEU A 68  ? 0.31924 0.22120 0.25321 0.00198  0.02759  0.00339  132 LEU A C     
461  O O     . LEU A 68  ? 0.32384 0.21889 0.25330 0.00195  0.02657  0.00313  132 LEU A O     
462  C CB    . LEU A 68  ? 0.33692 0.22010 0.26177 -0.00001 0.03057  0.00488  132 LEU A CB    
463  C CG    . LEU A 68  ? 0.33826 0.21495 0.26018 -0.00098 0.03340  0.00599  132 LEU A CG    
464  C CD1   . LEU A 68  ? 0.33621 0.19742 0.24762 -0.00080 0.03489  0.00681  132 LEU A CD1   
465  C CD2   . LEU A 68  ? 0.33221 0.21287 0.25224 0.00233  0.03470  0.00648  132 LEU A CD2   
466  N N     . THR A 69  ? 0.32871 0.24113 0.26708 0.00338  0.02746  0.00308  133 THR A N     
467  C CA    . THR A 69  ? 0.31802 0.23519 0.25762 0.00451  0.02612  0.00266  133 THR A CA    
468  C C     . THR A 69  ? 0.31481 0.23860 0.25532 0.00717  0.02652  0.00319  133 THR A C     
469  O O     . THR A 69  ? 0.28786 0.21360 0.22855 0.00778  0.02734  0.00349  133 THR A O     
470  C CB    . THR A 69  ? 0.32354 0.24826 0.27036 0.00192  0.02504  0.00165  133 THR A CB    
471  O OG1   . THR A 69  ? 0.31322 0.24802 0.26571 0.00196  0.02650  0.00141  133 THR A OG1   
472  C CG2   . THR A 69  ? 0.35262 0.27264 0.30186 -0.00149 0.02380  0.00134  133 THR A CG2   
473  N N     . VAL A 70  ? 0.17309 0.09958 0.11407 0.00848  0.02581  0.00331  134 VAL A N     
474  C CA    . VAL A 70  ? 0.19352 0.12761 0.13777 0.00996  0.02581  0.00390  134 VAL A CA    
475  C C     . VAL A 70  ? 0.23174 0.17512 0.18392 0.00760  0.02451  0.00322  134 VAL A C     
476  O O     . VAL A 70  ? 0.21993 0.15935 0.16859 0.00703  0.02501  0.00286  134 VAL A O     
477  C CB    . VAL A 70  ? 0.19612 0.12559 0.13698 0.01398  0.02537  0.00503  134 VAL A CB    
478  C CG1   . VAL A 70  ? 0.19844 0.13554 0.14437 0.01533  0.02483  0.00582  134 VAL A CG1   
479  C CG2   . VAL A 70  ? 0.22229 0.14228 0.15698 0.01665  0.02547  0.00575  134 VAL A CG2   
480  N N     . LYS A 71  ? 0.26548 0.22036 0.22798 0.00625  0.02196  0.00295  135 LYS A N     
481  C CA    . LYS A 71  ? 0.25400 0.21845 0.22504 0.00427  0.01943  0.00234  135 LYS A CA    
482  C C     . LYS A 71  ? 0.26822 0.23944 0.24460 0.00426  0.01734  0.00270  135 LYS A C     
483  O O     . LYS A 71  ? 0.27645 0.24543 0.25645 0.00480  0.01539  0.00260  135 LYS A O     
484  C CB    . LYS A 71  ? 0.24862 0.21900 0.22529 0.00246  0.01812  0.00143  135 LYS A CB    
485  C CG    . LYS A 71  ? 0.32951 0.29165 0.30062 0.00209  0.02121  0.00106  135 LYS A CG    
486  C CD    . LYS A 71  ? 0.27116 0.23832 0.24812 0.00084  0.02081  0.00032  135 LYS A CD    
487  C CE    . LYS A 71  ? 0.33848 0.29785 0.31073 -0.00028 0.02378  -0.00023 135 LYS A CE    
488  N NZ    . LYS A 71  ? 0.39464 0.35270 0.36951 -0.00125 0.02667  -0.00081 135 LYS A NZ    
489  N N     . ILE A 72  ? 0.22487 0.19673 0.20193 0.00446  0.01723  0.00305  136 ILE A N     
490  C CA    . ILE A 72  ? 0.17471 0.14935 0.15473 0.00514  0.01699  0.00294  136 ILE A CA    
491  C C     . ILE A 72  ? 0.21900 0.19682 0.20322 0.00372  0.01608  0.00232  136 ILE A C     
492  O O     . ILE A 72  ? 0.22939 0.20657 0.21297 0.00331  0.01615  0.00203  136 ILE A O     
493  C CB    . ILE A 72  ? 0.22258 0.19059 0.19735 0.00759  0.01969  0.00491  136 ILE A CB    
494  C CG1   . ILE A 72  ? 0.20649 0.16559 0.17277 0.01143  0.02260  0.00605  136 ILE A CG1   
495  C CG2   . ILE A 72  ? 0.18885 0.16023 0.16791 0.00761  0.01958  0.00553  136 ILE A CG2   
496  C CD1   . ILE A 72  ? 0.23339 0.18303 0.19083 0.01564  0.02614  0.00748  136 ILE A CD1   
497  N N     . LYS A 73  ? 0.22976 0.20664 0.21827 0.00344  0.01397  0.00230  137 LYS A N     
498  C CA    . LYS A 73  ? 0.25065 0.22956 0.24146 0.00238  0.01341  0.00170  137 LYS A CA    
499  C C     . LYS A 73  ? 0.25568 0.23599 0.24840 0.00216  0.01327  0.00164  137 LYS A C     
500  O O     . LYS A 73  ? 0.23105 0.21533 0.22356 0.00192  0.01417  0.00148  137 LYS A O     
501  C CB    . LYS A 73  ? 0.25108 0.23101 0.24263 0.00153  0.01282  0.00111  137 LYS A CB    
502  C CG    . LYS A 73  ? 0.32247 0.30636 0.31398 0.00103  0.01368  0.00076  137 LYS A CG    
503  C CD    . LYS A 73  ? 0.31590 0.29708 0.30891 0.00058  0.01250  0.00044  137 LYS A CD    
504  C CE    . LYS A 73  ? 0.39623 0.38015 0.38838 0.00026  0.01405  0.00020  137 LYS A CE    
505  N NZ    . LYS A 73  ? 0.34658 0.32959 0.33826 0.00032  0.01483  0.00024  137 LYS A NZ    
506  N N     . CYS A 74  ? 0.22892 0.20912 0.22234 0.00204  0.01375  0.00161  138 CYS A N     
507  C CA    . CYS A 74  ? 0.26304 0.24399 0.25830 0.00160  0.01403  0.00135  138 CYS A CA    
508  C C     . CYS A 74  ? 0.27465 0.25997 0.27006 0.00050  0.01471  0.00043  138 CYS A C     
509  O O     . CYS A 74  ? 0.29247 0.27399 0.28765 0.00041  0.01339  0.00035  138 CYS A O     
510  C CB    . CYS A 74  ? 0.21008 0.19358 0.20502 0.00187  0.01684  0.00161  138 CYS A CB    
511  S SG    . CYS A 74  ? 0.27256 0.25348 0.26453 0.00349  0.01839  0.00281  138 CYS A SG    
512  N N     . ASP A 75  ? 0.19624 0.18209 0.19250 -0.00008 0.01462  -0.00007 139 ASP A N     
513  C CA    . ASP A 75  ? 0.22747 0.20945 0.22385 -0.00096 0.01364  -0.00084 139 ASP A CA    
514  C C     . ASP A 75  ? 0.22335 0.20876 0.22066 -0.00155 0.01603  -0.00143 139 ASP A C     
515  O O     . ASP A 75  ? 0.26980 0.25541 0.26757 -0.00238 0.01635  -0.00222 139 ASP A O     
516  C CB    . ASP A 75  ? 0.24997 0.23177 0.24538 -0.00139 0.01335  -0.00117 139 ASP A CB    
517  C CG    . ASP A 75  ? 0.29242 0.27657 0.28646 -0.00188 0.01543  -0.00155 139 ASP A CG    
518  O OD1   . ASP A 75  ? 0.32595 0.30578 0.32080 -0.00236 0.01489  -0.00198 139 ASP A OD1   
519  O OD2   . ASP A 75  ? 0.28484 0.26800 0.27753 -0.00205 0.01570  -0.00163 139 ASP A OD2   
520  N N     . LYS A 76  ? 0.22499 0.20973 0.22260 -0.00138 0.01699  -0.00129 140 LYS A N     
521  C CA    . LYS A 76  ? 0.20714 0.18677 0.20633 -0.00222 0.01709  -0.00217 140 LYS A CA    
522  C C     . LYS A 76  ? 0.22351 0.20713 0.22214 -0.00336 0.01961  -0.00325 140 LYS A C     
523  O O     . LYS A 76  ? 0.26240 0.24628 0.26260 -0.00451 0.02085  -0.00453 140 LYS A O     
524  C CB    . LYS A 76  ? 0.32020 0.30298 0.31876 -0.00150 0.01994  -0.00145 140 LYS A CB    
525  C CG    . LYS A 76  ? 0.32340 0.30510 0.32352 -0.00218 0.02234  -0.00219 140 LYS A CG    
526  C CD    . LYS A 76  ? 0.32890 0.30231 0.32755 -0.00165 0.02200  -0.00160 140 LYS A CD    
527  C CE    . LYS A 76  ? 0.33107 0.30889 0.33120 -0.00225 0.02696  -0.00226 140 LYS A CE    
528  N NZ    . LYS A 76  ? 0.33587 0.31058 0.33379 -0.00138 0.02916  -0.00133 140 LYS A NZ    
529  N N     . GLU A 77  ? 0.25580 0.23370 0.25264 -0.00369 0.01778  -0.00337 141 GLU A N     
530  C CA    . GLU A 77  ? 0.32095 0.30206 0.31616 -0.00467 0.02097  -0.00417 141 GLU A CA    
531  C C     . GLU A 77  ? 0.38443 0.36113 0.37987 -0.00642 0.01900  -0.00570 141 GLU A C     
532  O O     . GLU A 77  ? 0.36686 0.34778 0.36119 -0.00771 0.02262  -0.00680 141 GLU A O     
533  C CB    . GLU A 77  ? 0.37507 0.35468 0.36821 -0.00420 0.02109  -0.00357 141 GLU A CB    
534  N N     . LYS A 78  ? 0.26276 0.24104 0.25817 -0.00566 0.01742  -0.00497 142 LYS A N     
535  C CA    . LYS A 78  ? 0.22116 0.20423 0.21507 -0.00636 0.01901  -0.00543 142 LYS A CA    
536  C C     . LYS A 78  ? 0.21418 0.19958 0.21073 -0.00650 0.01836  -0.00592 142 LYS A C     
537  O O     . LYS A 78  ? 0.20317 0.18495 0.19918 -0.00835 0.01626  -0.00739 142 LYS A O     
538  C CB    . LYS A 78  ? 0.24100 0.21900 0.23359 -0.00611 0.01635  -0.00488 142 LYS A CB    
539  C CG    . LYS A 78  ? 0.31491 0.29074 0.30595 -0.00574 0.01713  -0.00443 142 LYS A CG    
540  C CD    . LYS A 78  ? 0.30157 0.27916 0.28825 -0.00619 0.01979  -0.00445 142 LYS A CD    
541  C CE    . LYS A 78  ? 0.39400 0.36345 0.37998 -0.00733 0.02006  -0.00521 142 LYS A CE    
542  N N     . ASN A 79  ? 0.29852 0.28038 0.29815 -0.00599 0.01669  -0.00593 143 ASN A N     
543  C CA    . ASN A 79  ? 0.24513 0.22883 0.24805 -0.00573 0.01649  -0.00626 143 ASN A CA    
544  C C     . ASN A 79  ? 0.23400 0.21657 0.23741 -0.00545 0.02063  -0.00592 143 ASN A C     
545  O O     . ASN A 79  ? 0.21420 0.19993 0.21938 -0.00549 0.01685  -0.00578 143 ASN A O     
546  C CB    . ASN A 79  ? 0.21450 0.19991 0.21913 -0.00837 0.01737  -0.00956 143 ASN A CB    
547  C CG    . ASN A 79  ? 0.27557 0.26371 0.28873 -0.01000 0.02294  -0.01322 143 ASN A CG    
548  O OD1   . ASN A 79  ? 0.28518 0.27427 0.30290 -0.00702 0.02434  -0.01092 143 ASN A OD1   
549  N ND2   . ASN A 79  ? 0.25926 0.25987 0.27399 -0.01087 0.02289  -0.01451 143 ASN A ND2   
550  N N     . LEU A 80  ? 0.15615 0.13982 0.15642 -0.00286 0.01434  -0.00289 144 LEU A N     
551  C CA    . LEU A 80  ? 0.16121 0.14496 0.16016 -0.00165 0.01343  -0.00159 144 LEU A CA    
552  C C     . LEU A 80  ? 0.16489 0.15203 0.16351 0.00010  0.01459  0.00010  144 LEU A C     
553  O O     . LEU A 80  ? 0.21169 0.19481 0.21015 0.00015  0.01361  0.00014  144 LEU A O     
554  C CB    . LEU A 80  ? 0.17210 0.15463 0.16776 -0.00222 0.01299  -0.00188 144 LEU A CB    
555  C CG    . LEU A 80  ? 0.18418 0.16909 0.17731 -0.00404 0.01483  -0.00321 144 LEU A CG    
556  C CD1   . LEU A 80  ? 0.13910 0.12155 0.12854 -0.00424 0.01504  -0.00301 144 LEU A CD1   
557  C CD2   . LEU A 80  ? 0.16019 0.14576 0.15296 -0.00521 0.01461  -0.00408 144 LEU A CD2   
558  N N     . LEU A 81  ? 0.16271 0.14972 0.16072 0.00148  0.01456  0.00139  145 LEU A N     
559  C CA    . LEU A 81  ? 0.16356 0.14599 0.15994 0.00323  0.01369  0.00283  145 LEU A CA    
560  C C     . LEU A 81  ? 0.18412 0.16891 0.17675 0.00366  0.01440  0.00284  145 LEU A C     
561  O O     . LEU A 81  ? 0.15714 0.13945 0.14790 0.00448  0.01472  0.00433  145 LEU A O     
562  C CB    . LEU A 81  ? 0.12365 0.10484 0.12010 0.00561  0.01888  0.00582  145 LEU A CB    
563  C CG    . LEU A 81  ? 0.13906 0.11685 0.13071 0.00872  0.02096  0.00751  145 LEU A CG    
564  C CD1   . LEU A 81  ? 0.15991 0.13895 0.15114 0.00612  0.01891  0.00612  145 LEU A CD1   
565  C CD2   . LEU A 81  ? 0.24048 0.21862 0.23541 0.01481  0.02171  0.00754  145 LEU A CD2   
566  N N     . HIS A 82  ? 0.14503 0.12532 0.13663 0.00373  0.01301  0.00272  146 HIS A N     
567  C CA    . HIS A 82  ? 0.12615 0.10791 0.11378 0.00374  0.01409  0.00245  146 HIS A CA    
568  C C     . HIS A 82  ? 0.18766 0.16721 0.17224 0.00515  0.01495  0.00314  146 HIS A C     
569  O O     . HIS A 82  ? 0.18401 0.15977 0.17031 0.00543  0.01406  0.00339  146 HIS A O     
570  C CB    . HIS A 82  ? 0.15181 0.13365 0.13989 0.00234  0.01378  0.00154  146 HIS A CB    
571  C CG    . HIS A 82  ? 0.16447 0.14721 0.15385 0.00118  0.01343  0.00081  146 HIS A CG    
572  N ND1   . HIS A 82  ? 0.21653 0.19461 0.20485 0.00084  0.01232  0.00053  146 HIS A ND1   
573  C CD2   . HIS A 82  ? 0.14821 0.13218 0.13955 0.00039  0.01337  0.00028  146 HIS A CD2   
574  C CE1   . HIS A 82  ? 0.23863 0.21699 0.22760 -0.00046 0.01248  -0.00030 146 HIS A CE1   
575  N NE2   . HIS A 82  ? 0.15991 0.14317 0.15042 -0.00051 0.01361  -0.00036 146 HIS A NE2   
576  N N     . VAL A 83  ? 0.12998 0.10494 0.10924 0.00699  0.01587  0.00426  147 VAL A N     
577  C CA    . VAL A 83  ? 0.14176 0.10960 0.11435 0.00966  0.01824  0.00507  147 VAL A CA    
578  C C     . VAL A 83  ? 0.13422 0.09911 0.10329 0.00917  0.01812  0.00432  147 VAL A C     
579  O O     . VAL A 83  ? 0.13360 0.09441 0.09799 0.01084  0.01824  0.00455  147 VAL A O     
580  C CB    . VAL A 83  ? 0.17118 0.13190 0.13705 0.01561  0.02072  0.00724  147 VAL A CB    
581  C CG1   . VAL A 83  ? 0.20076 0.15438 0.16135 0.01806  0.02122  0.00742  147 VAL A CG1   
582  C CG2   . VAL A 83  ? 0.15564 0.12031 0.12760 0.01619  0.02077  0.00790  147 VAL A CG2   
583  N N     . THR A 84  ? 0.17438 0.14019 0.14467 0.00731  0.01813  0.00353  148 THR A N     
584  C CA    . THR A 84  ? 0.18383 0.14774 0.15235 0.00645  0.01855  0.00285  148 THR A CA    
585  C C     . THR A 84  ? 0.20889 0.16351 0.16969 0.00776  0.02136  0.00329  148 THR A C     
586  O O     . THR A 84  ? 0.19926 0.15347 0.16047 0.00714  0.02197  0.00316  148 THR A O     
587  C CB    . THR A 84  ? 0.19499 0.16111 0.17233 0.00427  0.01587  0.00220  148 THR A CB    
588  O OG1   . THR A 84  ? 0.22349 0.19675 0.20173 0.00340  0.01627  0.00182  148 THR A OG1   
589  C CG2   . THR A 84  ? 0.14629 0.11405 0.11939 0.00341  0.01866  0.00174  148 THR A CG2   
590  N N     . ASP A 85  ? 0.23120 0.17683 0.18334 0.00963  0.02309  0.00376  149 ASP A N     
591  C CA    . ASP A 85  ? 0.25405 0.18879 0.19678 0.01084  0.02595  0.00415  149 ASP A CA    
592  C C     . ASP A 85  ? 0.25961 0.19186 0.20118 0.00907  0.02754  0.00353  149 ASP A C     
593  O O     . ASP A 85  ? 0.26005 0.19532 0.20387 0.00850  0.02660  0.00318  149 ASP A O     
594  C CB    . ASP A 85  ? 0.23812 0.16471 0.17452 0.01498  0.02481  0.00568  149 ASP A CB    
595  C CG    . ASP A 85  ? 0.24463 0.16798 0.17754 0.01671  0.02358  0.00629  149 ASP A CG    
596  O OD1   . ASP A 85  ? 0.28307 0.20117 0.21136 0.01563  0.02505  0.00607  149 ASP A OD1   
597  O OD2   . ASP A 85  ? 0.26842 0.19428 0.20355 0.01920  0.02095  0.00713  149 ASP A OD2   
598  N N     . THR A 86  ? 0.20887 0.13534 0.14746 0.00792  0.02991  0.00336  150 THR A N     
599  C CA    . THR A 86  ? 0.21308 0.13486 0.14970 0.00664  0.03223  0.00321  150 THR A CA    
600  C C     . THR A 86  ? 0.22100 0.13115 0.14909 0.00840  0.03219  0.00473  150 THR A C     
601  O O     . THR A 86  ? 0.25073 0.15368 0.17644 0.00707  0.03383  0.00525  150 THR A O     
602  C CB    . THR A 86  ? 0.26414 0.18767 0.20673 0.00376  0.03336  0.00264  150 THR A CB    
603  O OG1   . THR A 86  ? 0.23892 0.15859 0.18090 0.00325  0.03137  0.00311  150 THR A OG1   
604  C CG2   . THR A 86  ? 0.26341 0.19870 0.21517 0.00282  0.03311  0.00138  150 THR A CG2   
605  N N     . GLY A 87  ? 0.22663 0.13434 0.15015 0.01161  0.03027  0.00564  151 GLY A N     
606  C CA    . GLY A 87  ? 0.29016 0.18667 0.20511 0.01447  0.03004  0.00736  151 GLY A CA    
607  C C     . GLY A 87  ? 0.29782 0.18852 0.20677 0.01447  0.03154  0.00770  151 GLY A C     
608  O O     . GLY A 87  ? 0.27380 0.16727 0.18489 0.01174  0.03394  0.00646  151 GLY A O     
609  N N     . VAL A 88  ? 0.28619 0.16809 0.18708 0.01816  0.03027  0.00954  152 VAL A N     
610  C CA    . VAL A 88  ? 0.32396 0.19771 0.21660 0.01865  0.03151  0.01021  152 VAL A CA    
611  C C     . VAL A 88  ? 0.26609 0.14469 0.15969 0.01785  0.03004  0.00907  152 VAL A C     
612  O O     . VAL A 88  ? 0.29148 0.16435 0.17905 0.01676  0.03232  0.00865  152 VAL A O     
613  C CB    . VAL A 88  ? 0.33576 0.19867 0.21920 0.02357  0.02997  0.01288  152 VAL A CB    
614  C CG1   . VAL A 88  ? 0.37787 0.24559 0.26419 0.02773  0.02475  0.01427  152 VAL A CG1   
615  C CG2   . VAL A 88  ? 0.33146 0.18312 0.20414 0.02389  0.03215  0.01381  152 VAL A CG2   
616  N N     . GLY A 89  ? 0.26837 0.15620 0.16867 0.01822  0.02666  0.00847  153 GLY A N     
617  C CA    . GLY A 89  ? 0.27163 0.16226 0.17179 0.01724  0.02488  0.00740  153 GLY A CA    
618  C C     . GLY A 89  ? 0.28167 0.16439 0.17420 0.02035  0.02085  0.00989  153 GLY A C     
619  O O     . GLY A 89  ? 0.31331 0.18871 0.20050 0.02388  0.01994  0.01248  153 GLY A O     
620  N N     . MET A 90  ? 0.29228 0.17614 0.18392 0.01906  0.01819  0.00941  154 MET A N     
621  C CA    . MET A 90  ? 0.30292 0.17918 0.18642 0.02103  0.01382  0.01233  154 MET A CA    
622  C C     . MET A 90  ? 0.32877 0.19820 0.20376 0.01759  0.01537  0.01035  154 MET A C     
623  O O     . MET A 90  ? 0.33209 0.20595 0.21047 0.01405  0.01735  0.00701  154 MET A O     
624  C CB    . MET A 90  ? 0.26997 0.15394 0.16016 0.02335  0.00685  0.01578  154 MET A CB    
625  C CG    . MET A 90  ? 0.36014 0.25019 0.25861 0.02774  0.00562  0.01779  154 MET A CG    
626  S SD    . MET A 90  ? 0.33094 0.23520 0.24254 0.02930  -0.00020 0.02050  154 MET A SD    
627  C CE    . MET A 90  ? 0.25454 0.16574 0.17381 0.02427  0.00476  0.01483  154 MET A CE    
628  N N     . THR A 91  ? 0.29684 0.15432 0.15964 0.01905  0.01476  0.01241  155 THR A N     
629  C CA    . THR A 91  ? 0.30992 0.15821 0.16202 0.01627  0.01546  0.01116  155 THR A CA    
630  C C     . THR A 91  ? 0.31625 0.16861 0.16930 0.01463  0.00862  0.01310  155 THR A C     
631  O O     . THR A 91  ? 0.29736 0.16038 0.15951 0.01645  0.00328  0.01627  155 THR A O     
632  C CB    . THR A 91  ? 0.32802 0.16178 0.16572 0.01863  0.01641  0.01339  155 THR A CB    
633  O OG1   . THR A 91  ? 0.35555 0.18921 0.19081 0.02264  0.00909  0.01881  155 THR A OG1   
634  C CG2   . THR A 91  ? 0.30890 0.13955 0.14648 0.02018  0.02268  0.01268  155 THR A CG2   
635  N N     . ARG A 92  ? 0.34194 0.18605 0.18539 0.01093  0.00915  0.01138  156 ARG A N     
636  C CA    . ARG A 92  ? 0.36028 0.20742 0.20207 0.00826  0.00245  0.01389  156 ARG A CA    
637  C C     . ARG A 92  ? 0.35920 0.20881 0.19703 0.01220  -0.00541 0.02082  156 ARG A C     
638  O O     . ARG A 92  ? 0.37998 0.24316 0.22479 0.01269  -0.01205 0.02468  156 ARG A O     
639  C CB    . ARG A 92  ? 0.36568 0.19990 0.19444 0.00346  0.00471  0.01090  156 ARG A CB    
640  C CG    . ARG A 92  ? 0.38933 0.22606 0.21344 -0.00031 -0.00256 0.01395  156 ARG A CG    
641  C CD    . ARG A 92  ? 0.41230 0.23177 0.21892 -0.00443 -0.00097 0.01205  156 ARG A CD    
642  N NE    . ARG A 92  ? 0.50620 0.32838 0.30656 -0.00900 -0.00800 0.01468  156 ARG A NE    
643  C CZ    . ARG A 92  ? 0.50477 0.32893 0.29567 -0.00776 -0.01603 0.01990  156 ARG A CZ    
644  N NH1   . ARG A 92  ? 0.45970 0.28086 0.24567 -0.00183 -0.01794 0.02358  156 ARG A NH1   
645  N NH2   . ARG A 92  ? 0.51519 0.34451 0.30054 -0.01264 -0.02235 0.02106  156 ARG A NH2   
646  N N     . GLU A 93  ? 0.37186 0.20975 0.19825 0.01548  -0.00467 0.02262  157 GLU A N     
647  C CA    . GLU A 93  ? 0.39854 0.23873 0.22016 0.02022  -0.01217 0.02934  157 GLU A CA    
648  C C     . GLU A 93  ? 0.38583 0.24176 0.22273 0.02509  -0.01575 0.03290  157 GLU A C     
649  O O     . GLU A 93  ? 0.36162 0.22988 0.20187 0.02761  -0.02384 0.03847  157 GLU A O     
650  C CB    . GLU A 93  ? 0.38830 0.21168 0.19552 0.02350  -0.00910 0.03001  157 GLU A CB    
651  C CG    . GLU A 93  ? 0.44340 0.26826 0.24573 0.02973  -0.01609 0.03694  157 GLU A CG    
652  C CD    . GLU A 93  ? 0.49479 0.30104 0.28135 0.03298  -0.01227 0.03739  157 GLU A CD    
653  O OE1   . GLU A 93  ? 0.46942 0.26585 0.25420 0.03201  -0.00340 0.03275  157 GLU A OE1   
654  O OE2   . GLU A 93  ? 0.53258 0.33508 0.30830 0.03660  -0.01823 0.04263  157 GLU A OE2   
655  N N     . GLU A 94  ? 0.38714 0.24402 0.23339 0.02637  -0.00988 0.02966  158 GLU A N     
656  C CA    . GLU A 94  ? 0.45376 0.32326 0.31378 0.03083  -0.01234 0.03231  158 GLU A CA    
657  C C     . GLU A 94  ? 0.44384 0.32995 0.31616 0.02849  -0.01655 0.03319  158 GLU A C     
658  O O     . GLU A 94  ? 0.39615 0.29473 0.27616 0.03248  -0.02270 0.03816  158 GLU A O     
659  C CB    . GLU A 94  ? 0.41371 0.27956 0.27841 0.03175  -0.00492 0.02810  158 GLU A CB    
660  C CG    . GLU A 94  ? 0.44428 0.29568 0.29701 0.03493  -0.00133 0.02859  158 GLU A CG    
661  C CD    . GLU A 94  ? 0.43973 0.28777 0.29456 0.03431  0.00624  0.02462  158 GLU A CD    
662  O OE1   . GLU A 94  ? 0.42711 0.27889 0.28685 0.02959  0.01067  0.02011  158 GLU A OE1   
663  O OE2   . GLU A 94  ? 0.57148 0.41302 0.42199 0.03852  0.00780  0.02642  158 GLU A OE2   
664  N N     . LEU A 95  ? 0.40268 0.28902 0.27634 0.02236  -0.01329 0.02847  159 LEU A N     
665  C CA    . LEU A 95  ? 0.35860 0.25902 0.24158 0.01988  -0.01670 0.02899  159 LEU A CA    
666  C C     . LEU A 95  ? 0.41134 0.31630 0.28537 0.01997  -0.02597 0.03335  159 LEU A C     
667  O O     . LEU A 95  ? 0.39025 0.30897 0.27077 0.02082  -0.03180 0.03535  159 LEU A O     
668  C CB    . LEU A 95  ? 0.30719 0.20479 0.19148 0.01338  -0.01101 0.02277  159 LEU A CB    
669  C CG    . LEU A 95  ? 0.33738 0.23249 0.22831 0.01344  -0.00347 0.01728  159 LEU A CG    
670  C CD1   . LEU A 95  ? 0.27888 0.16872 0.16674 0.00795  0.00190  0.01112  159 LEU A CD1   
671  C CD2   . LEU A 95  ? 0.28804 0.19607 0.19341 0.01580  -0.00435 0.01821  159 LEU A CD2   
672  N N     . VAL A 96  ? 0.39799 0.29306 0.25739 0.01890  -0.02794 0.03454  160 VAL A N     
673  C CA    . VAL A 96  ? 0.43459 0.33521 0.28443 0.01790  -0.03756 0.03791  160 VAL A CA    
674  C C     . VAL A 96  ? 0.45612 0.36695 0.30872 0.02576  -0.04556 0.04482  160 VAL A C     
675  O O     . VAL A 96  ? 0.46812 0.39603 0.32518 0.02693  -0.05471 0.04799  160 VAL A O     
676  C CB    . VAL A 96  ? 0.43192 0.31639 0.26384 0.01305  -0.03623 0.03596  160 VAL A CB    
677  C CG1   . VAL A 96  ? 0.45983 0.34903 0.28019 0.01355  -0.04703 0.04021  160 VAL A CG1   
678  C CG2   . VAL A 96  ? 0.40462 0.28324 0.23525 0.00486  -0.03070 0.02993  160 VAL A CG2   
679  N N     . LYS A 97  ? 0.55119 0.45299 0.40224 0.03115  -0.04238 0.04704  161 LYS A N     
680  C CA    . LYS A 97  ? 0.57103 0.47962 0.42296 0.03871  -0.04949 0.05399  161 LYS A CA    
681  C C     . LYS A 97  ? 0.58947 0.50913 0.45927 0.04498  -0.04939 0.05646  161 LYS A C     
682  O O     . LYS A 97  ? 0.63479 0.56400 0.50922 0.05129  -0.05638 0.06268  161 LYS A O     
683  C CB    . LYS A 97  ? 0.67745 0.56847 0.51605 0.04157  -0.04645 0.05532  161 LYS A CB    
684  C CG    . LYS A 97  ? 0.69219 0.56803 0.51221 0.03606  -0.04497 0.05263  161 LYS A CG    
685  C CD    . LYS A 97  ? 0.71132 0.57054 0.51875 0.04000  -0.04217 0.05447  161 LYS A CD    
686  C CE    . LYS A 97  ? 0.73462 0.58171 0.52159 0.03687  -0.04508 0.05474  161 LYS A CE    
687  N NZ    . LYS A 97  ? 0.74410 0.56841 0.51872 0.03565  -0.03588 0.05083  161 LYS A NZ    
688  N N     . ASN A 98  ? 0.68266 0.97594 0.84226 0.14768  -0.08994 -0.04487 162 ASN A N     
689  C CA    . ASN A 98  ? 0.67135 0.95687 0.86118 0.13385  -0.08474 -0.02739 162 ASN A CA    
690  C C     . ASN A 98  ? 0.65542 0.90654 0.85101 0.13835  -0.11078 -0.01754 162 ASN A C     
691  O O     . ASN A 98  ? 0.63493 0.87853 0.83683 0.14540  -0.12439 -0.02679 162 ASN A O     
692  C CB    . ASN A 98  ? 0.58120 0.89722 0.79823 0.13278  -0.07122 -0.04053 162 ASN A CB    
693  C CG    . ASN A 98  ? 0.58296 0.88759 0.82679 0.12350  -0.07282 -0.03028 162 ASN A CG    
694  O OD1   . ASN A 98  ? 0.59090 0.86853 0.83766 0.11980  -0.08320 -0.01471 162 ASN A OD1   
695  N ND2   . ASN A 98  ? 0.57371 0.90265 0.83748 0.11928  -0.06205 -0.04015 162 ASN A ND2   
696  N N     . LEU A 99  ? 0.72274 0.94901 0.91462 0.12967  -0.11684 0.00452  163 LEU A N     
697  C CA    . LEU A 99  ? 0.71794 0.91630 0.91897 0.13011  -0.13930 0.01805  163 LEU A CA    
698  C C     . LEU A 99  ? 0.72318 0.90775 0.93763 0.11790  -0.13586 0.04312  163 LEU A C     
699  O O     . LEU A 99  ? 0.73540 0.92917 0.95662 0.10823  -0.11553 0.04900  163 LEU A O     
700  C CB    . LEU A 99  ? 0.73441 0.90533 0.90258 0.13573  -0.15941 0.01319  163 LEU A CB    
701  C CG    . LEU A 99  ? 0.76821 0.93238 0.90617 0.14478  -0.17461 0.01240  163 LEU A CG    
702  C CD1   . LEU A 99  ? 0.77612 0.91263 0.91341 0.13089  -0.18346 0.04127  163 LEU A CD1   
703  C CD2   . LEU A 99  ? 0.80269 0.95159 0.91022 0.15772  -0.19136 -0.00913 163 LEU A CD2   
704  N N     . THR A 124 ? 0.64149 1.07127 1.15147 0.05181  0.09830  -0.02302 188 THR A N     
705  C CA    . THR A 124 ? 0.76332 1.15043 1.26025 0.05638  0.07555  -0.01373 188 THR A CA    
706  C C     . THR A 124 ? 0.67489 1.06104 1.14414 0.04594  0.07040  -0.02245 188 THR A C     
707  O O     . THR A 124 ? 0.60577 0.96785 1.05816 0.04671  0.04932  -0.01147 188 THR A O     
708  C CB    . THR A 124 ? 0.65498 1.02789 1.14835 0.05652  0.04809  0.01561  188 THR A CB    
709  O OG1   . THR A 124 ? 0.64718 1.04779 1.13138 0.04250  0.03756  0.03084  188 THR A OG1   
710  C CG2   . THR A 124 ? 0.65723 1.02483 1.17615 0.06545  0.04959  0.02283  188 THR A CG2   
711  N N     . SER A 125 ? 0.67939 1.08533 1.12623 0.03495  0.08697  -0.04255 189 SER A N     
712  C CA    . SER A 125 ? 0.73831 1.13344 1.14398 0.02388  0.07917  -0.05247 189 SER A CA    
713  C C     . SER A 125 ? 0.75291 1.11512 1.16342 0.03231  0.07987  -0.06642 189 SER A C     
714  O O     . SER A 125 ? 0.77433 1.12357 1.16108 0.02690  0.06591  -0.06582 189 SER A O     
715  C CB    . SER A 125 ? 0.74495 1.16695 1.12424 0.00889  0.09672  -0.07195 189 SER A CB    
716  N N     . GLU A 126 ? 0.88206 1.23178 1.32618 0.04489  0.09473  -0.07807 190 GLU A N     
717  C CA    . GLU A 126 ? 0.89535 1.21186 1.34759 0.05035  0.09330  -0.08690 190 GLU A CA    
718  C C     . GLU A 126 ? 0.85039 1.14543 1.32183 0.05991  0.07692  -0.06303 190 GLU A C     
719  O O     . GLU A 126 ? 0.87132 1.14575 1.33257 0.05787  0.06708  -0.05918 190 GLU A O     
720  C CB    . GLU A 126 ? 0.90322 1.21130 1.38065 0.05771  0.11463  -0.11390 190 GLU A CB    
721  N N     . LEU A 127 ? 0.68809 0.98314 1.17181 0.06721  0.07161  -0.04472 191 LEU A N     
722  C CA    . LEU A 127 ? 0.65932 0.92818 1.14535 0.07297  0.05314  -0.02164 191 LEU A CA    
723  C C     . LEU A 127 ? 0.64880 0.91688 1.10704 0.06805  0.03390  -0.00732 191 LEU A C     
724  O O     . LEU A 127 ? 0.67353 0.92032 1.12655 0.07028  0.02239  0.00340  191 LEU A O     
725  C CB    . LEU A 127 ? 0.63710 0.90846 1.13867 0.07895  0.04932  -0.00696 191 LEU A CB    
726  N N     . ILE A 128 ? 0.46243 0.75485 0.90490 0.06126  0.02946  -0.00724 192 ILE A N     
727  C CA    . ILE A 128 ? 0.38076 0.67073 0.79854 0.05881  0.00943  0.00195  192 ILE A CA    
728  C C     . ILE A 128 ? 0.38484 0.66626 0.79196 0.05667  0.01232  -0.01073 192 ILE A C     
729  O O     . ILE A 128 ? 0.37975 0.65018 0.77736 0.06005  0.00092  -0.00325 192 ILE A O     
730  C CB    . ILE A 128 ? 0.36382 0.67645 0.76517 0.04991  0.00062  0.00474  192 ILE A CB    
731  N N     . GLY A 129 ? 0.30310 0.58972 0.70769 0.04965  0.02792  -0.03068 193 GLY A N     
732  C CA    . GLY A 129 ? 0.30041 0.57799 0.69701 0.04495  0.03069  -0.04138 193 GLY A CA    
733  C C     . GLY A 129 ? 0.37183 0.62681 0.78846 0.04902  0.03497  -0.03695 193 GLY A C     
734  O O     . GLY A 129 ? 0.37562 0.62441 0.78595 0.04359  0.03392  -0.03845 193 GLY A O     
735  N N     . GLN A 130 ? 0.62191 0.86612 1.06487 0.05723  0.03839  -0.02967 194 GLN A N     
736  C CA    . GLN A 130 ? 0.63370 0.85251 1.09731 0.06005  0.03769  -0.02151 194 GLN A CA    
737  C C     . GLN A 130 ? 0.53301 0.74529 0.98304 0.06078  0.02191  0.00033  194 GLN A C     
738  O O     . GLN A 130 ? 0.55269 0.75671 0.99350 0.05383  0.02039  0.00384  194 GLN A O     
739  C CB    . GLN A 130 ? 0.63923 0.84960 1.14051 0.07034  0.04331  -0.02033 194 GLN A CB    
740  N N     . PHE A 131 ? 0.36872 0.58625 0.81549 0.06768  0.00986  0.01489  195 PHE A N     
741  C CA    . PHE A 131 ? 0.38178 0.59092 0.81269 0.06954  -0.00617 0.03348  195 PHE A CA    
742  C C     . PHE A 131 ? 0.34386 0.56772 0.74116 0.06804  -0.01333 0.02878  195 PHE A C     
743  O O     . PHE A 131 ? 0.33429 0.55401 0.71376 0.07140  -0.02643 0.03961  195 PHE A O     
744  C CB    . PHE A 131 ? 0.45954 0.65720 0.88944 0.07492  -0.01875 0.04921  195 PHE A CB    
745  N N     . GLY A 132 ? 0.41340 0.65403 0.80229 0.06381  -0.00647 0.01184  196 GLY A N     
746  C CA    . GLY A 132 ? 0.38335 0.63881 0.74857 0.06375  -0.01346 0.00537  196 GLY A CA    
747  C C     . GLY A 132 ? 0.36972 0.62962 0.72085 0.07158  -0.03203 0.00959  196 GLY A C     
748  O O     . GLY A 132 ? 0.41059 0.67913 0.74511 0.07581  -0.04109 0.00417  196 GLY A O     
749  N N     . VAL A 133 ? 0.19619 0.44767 0.54820 0.07262  -0.03811 0.01818  197 VAL A N     
750  C CA    . VAL A 133 ? 0.18552 0.43031 0.51278 0.07576  -0.05730 0.02405  197 VAL A CA    
751  C C     . VAL A 133 ? 0.15113 0.41088 0.47603 0.06984  -0.06061 0.01893  197 VAL A C     
752  O O     . VAL A 133 ? 0.15791 0.41081 0.46819 0.06858  -0.07546 0.02670  197 VAL A O     
753  C CB    . VAL A 133 ? 0.16880 0.39299 0.49341 0.07682  -0.06497 0.03938  197 VAL A CB    
754  N N     . GLY A 134 ? 0.35195 0.42637 0.32156 0.08478  -0.01581 0.02748  198 GLY A N     
755  C CA    . GLY A 134 ? 0.31868 0.39908 0.29845 0.07888  -0.01196 0.02840  198 GLY A CA    
756  C C     . GLY A 134 ? 0.29104 0.37463 0.27943 0.06917  -0.01316 0.02796  198 GLY A C     
757  O O     . GLY A 134 ? 0.28256 0.37696 0.28317 0.06406  -0.01228 0.02829  198 GLY A O     
758  N N     . PHE A 135 ? 0.27842 0.35259 0.26026 0.06673  -0.01505 0.02729  199 PHE A N     
759  C CA    . PHE A 135 ? 0.26836 0.34464 0.25723 0.05856  -0.01644 0.02671  199 PHE A CA    
760  C C     . PHE A 135 ? 0.30472 0.40117 0.30998 0.05519  -0.02111 0.02457  199 PHE A C     
761  O O     . PHE A 135 ? 0.25813 0.35934 0.27363 0.04798  -0.02006 0.02491  199 PHE A O     
762  C CB    . PHE A 135 ? 0.26526 0.33146 0.24400 0.05846  -0.01871 0.02570  199 PHE A CB    
763  C CG    . PHE A 135 ? 0.25916 0.33173 0.24526 0.05230  -0.02236 0.02397  199 PHE A CG    
764  C CD1   . PHE A 135 ? 0.26341 0.33041 0.25277 0.04591  -0.01923 0.02531  199 PHE A CD1   
765  C CD2   . PHE A 135 ? 0.27450 0.35866 0.26419 0.05295  -0.02924 0.02070  199 PHE A CD2   
766  C CE1   . PHE A 135 ? 0.23648 0.30933 0.23262 0.04089  -0.02270 0.02356  199 PHE A CE1   
767  C CE2   . PHE A 135 ? 0.27427 0.36421 0.27040 0.04698  -0.03281 0.01817  199 PHE A CE2   
768  C CZ    . PHE A 135 ? 0.28071 0.36499 0.28009 0.04121  -0.02946 0.01959  199 PHE A CZ    
769  N N     . TYR A 136 ? 0.26492 0.37345 0.27357 0.05974  -0.02636 0.02216  200 TYR A N     
770  C CA    . TYR A 136 ? 0.26597 0.39401 0.29145 0.05510  -0.03106 0.01908  200 TYR A CA    
771  C C     . TYR A 136 ? 0.27948 0.42026 0.31850 0.05302  -0.02792 0.01960  200 TYR A C     
772  O O     . TYR A 136 ? 0.31351 0.47078 0.36792 0.04813  -0.03088 0.01681  200 TYR A O     
773  C CB    . TYR A 136 ? 0.30561 0.44359 0.33120 0.05990  -0.03835 0.01598  200 TYR A CB    
774  C CG    . TYR A 136 ? 0.31936 0.44395 0.32847 0.06333  -0.04100 0.01585  200 TYR A CG    
775  C CD1   . TYR A 136 ? 0.30341 0.41429 0.29657 0.07145  -0.03884 0.01821  200 TYR A CD1   
776  C CD2   . TYR A 136 ? 0.30700 0.43178 0.31580 0.05801  -0.04515 0.01318  200 TYR A CD2   
777  C CE1   . TYR A 136 ? 0.36468 0.46270 0.34243 0.07389  -0.04047 0.01827  200 TYR A CE1   
778  C CE2   . TYR A 136 ? 0.34546 0.45795 0.33792 0.06108  -0.04700 0.01297  200 TYR A CE2   
779  C CZ    . TYR A 136 ? 0.37230 0.47130 0.34933 0.06884  -0.04440 0.01578  200 TYR A CZ    
780  O OH    . TYR A 136 ? 0.47409 0.55994 0.43426 0.07129  -0.04549 0.01580  200 TYR A OH    
781  N N     . SER A 137 ? 0.33099 0.46439 0.36456 0.05579  -0.02172 0.02286  201 SER A N     
782  C CA    . SER A 137 ? 0.30162 0.44532 0.34670 0.05208  -0.01776 0.02382  201 SER A CA    
783  C C     . SER A 137 ? 0.25391 0.39576 0.30584 0.04155  -0.01585 0.02480  201 SER A C     
784  O O     . SER A 137 ? 0.26920 0.41924 0.33092 0.03669  -0.01257 0.02567  201 SER A O     
785  C CB    . SER A 137 ? 0.30696 0.44283 0.34270 0.05810  -0.01178 0.02707  201 SER A CB    
786  O OG    . SER A 137 ? 0.27978 0.39702 0.30368 0.05603  -0.00776 0.03014  201 SER A OG    
787  N N     . ALA A 138 ? 0.20323 0.33404 0.24980 0.03809  -0.01754 0.02480  202 ALA A N     
788  C CA    . ALA A 138 ? 0.15868 0.28825 0.21283 0.02836  -0.01666 0.02537  202 ALA A CA    
789  C C     . ALA A 138 ? 0.17439 0.31952 0.24480 0.02138  -0.02006 0.02140  202 ALA A C     
790  O O     . ALA A 138 ? 0.18485 0.33107 0.26373 0.01276  -0.01779 0.02198  202 ALA A O     
791  C CB    . ALA A 138 ? 0.19385 0.30976 0.23947 0.02733  -0.01812 0.02560  202 ALA A CB    
792  N N     . PHE A 139 ? 0.12920 0.28542 0.20363 0.02449  -0.02538 0.01745  203 PHE A N     
793  C CA    . PHE A 139 ? 0.18647 0.35727 0.27649 0.01723  -0.02899 0.01315  203 PHE A CA    
794  C C     . PHE A 139 ? 0.17485 0.35969 0.27766 0.01481  -0.02557 0.01304  203 PHE A C     
795  O O     . PHE A 139 ? 0.21175 0.40918 0.32865 0.00806  -0.02772 0.00954  203 PHE A O     
796  C CB    . PHE A 139 ? 0.16773 0.34586 0.25698 0.02111  -0.03660 0.00916  203 PHE A CB    
797  C CG    . PHE A 139 ? 0.16647 0.33382 0.24610 0.02026  -0.04044 0.00781  203 PHE A CG    
798  C CD1   . PHE A 139 ? 0.13425 0.30103 0.22075 0.01056  -0.04227 0.00495  203 PHE A CD1   
799  C CD2   . PHE A 139 ? 0.15151 0.30833 0.21444 0.02901  -0.04169 0.00922  203 PHE A CD2   
800  C CE1   . PHE A 139 ? 0.20638 0.36442 0.28381 0.01007  -0.04568 0.00308  203 PHE A CE1   
801  C CE2   . PHE A 139 ? 0.20924 0.35664 0.26233 0.02840  -0.04461 0.00780  203 PHE A CE2   
802  C CZ    . PHE A 139 ? 0.14240 0.29150 0.20289 0.01925  -0.04683 0.00448  203 PHE A CZ    
803  N N     . LEU A 140 ? 0.19101 0.37409 0.28913 0.01989  -0.02015 0.01659  204 LEU A N     
804  C CA    . LEU A 140 ? 0.21491 0.41027 0.32449 0.01658  -0.01560 0.01674  204 LEU A CA    
805  C C     . LEU A 140 ? 0.19670 0.38693 0.31117 0.00523  -0.01135 0.01819  204 LEU A C     
806  O O     . LEU A 140 ? 0.23803 0.43900 0.36505 -0.00145 -0.00884 0.01673  204 LEU A O     
807  C CB    . LEU A 140 ? 0.21630 0.41033 0.31810 0.02535  -0.01085 0.01996  204 LEU A CB    
808  C CG    . LEU A 140 ? 0.27040 0.46998 0.36804 0.03722  -0.01387 0.01869  204 LEU A CG    
809  C CD1   . LEU A 140 ? 0.21202 0.40033 0.29525 0.04583  -0.00909 0.02255  204 LEU A CD1   
810  C CD2   . LEU A 140 ? 0.32150 0.54354 0.43588 0.03774  -0.01527 0.01510  204 LEU A CD2   
811  N N     . VAL A 141 ? 0.27249 0.44584 0.37704 0.00287  -0.01036 0.02121  205 VAL A N     
812  C CA    . VAL A 141 ? 0.19082 0.35561 0.29690 -0.00687 -0.00659 0.02352  205 VAL A CA    
813  C C     . VAL A 141 ? 0.20082 0.35713 0.30808 -0.01336 -0.01017 0.02146  205 VAL A C     
814  O O     . VAL A 141 ? 0.23762 0.38474 0.34550 -0.02130 -0.00759 0.02310  205 VAL A O     
815  C CB    . VAL A 141 ? 0.23092 0.38238 0.32474 -0.00450 -0.00189 0.02979  205 VAL A CB    
816  C CG1   . VAL A 141 ? 0.20748 0.36695 0.30078 0.00025  0.00271  0.03157  205 VAL A CG1   
817  C CG2   . VAL A 141 ? 0.21133 0.35113 0.29302 0.00232  -0.00429 0.03152  205 VAL A CG2   
818  N N     . ALA A 142 ? 0.24409 0.40183 0.35026 -0.00988 -0.01602 0.01799  206 ALA A N     
819  C CA    . ALA A 142 ? 0.25328 0.40222 0.35907 -0.01512 -0.01920 0.01593  206 ALA A CA    
820  C C     . ALA A 142 ? 0.25369 0.41349 0.36885 -0.01826 -0.02531 0.00954  206 ALA A C     
821  O O     . ALA A 142 ? 0.24611 0.41692 0.36197 -0.01214 -0.02944 0.00735  206 ALA A O     
822  C CB    . ALA A 142 ? 0.21495 0.35202 0.30778 -0.00862 -0.02055 0.01821  206 ALA A CB    
823  N N     . ASP A 143 ? 0.20316 0.35852 0.32450 -0.02788 -0.02607 0.00673  207 ASP A N     
824  C CA    . ASP A 143 ? 0.26134 0.42364 0.38941 -0.03177 -0.03269 0.00063  207 ASP A CA    
825  C C     . ASP A 143 ? 0.26925 0.42603 0.38713 -0.02709 -0.03811 -0.00123 207 ASP A C     
826  O O     . ASP A 143 ? 0.26856 0.43268 0.38723 -0.02712 -0.04478 -0.00592 207 ASP A O     
827  C CB    . ASP A 143 ? 0.29541 0.45186 0.43196 -0.04385 -0.03140 -0.00208 207 ASP A CB    
828  C CG    . ASP A 143 ? 0.30215 0.46620 0.44960 -0.04962 -0.02683 -0.00123 207 ASP A CG    
829  O OD1   . ASP A 143 ? 0.36871 0.54957 0.52489 -0.04842 -0.02926 -0.00292 207 ASP A OD1   
830  O OD2   . ASP A 143 ? 0.29324 0.44644 0.43995 -0.05557 -0.02086 0.00121  207 ASP A OD2   
831  N N     . LYS A 144 ? 0.20735 0.35152 0.31488 -0.02340 -0.03536 0.00251  208 LYS A N     
832  C CA    . LYS A 144 ? 0.12261 0.26101 0.22026 -0.01987 -0.03948 0.00080  208 LYS A CA    
833  C C     . LYS A 144 ? 0.12499 0.25332 0.21176 -0.01271 -0.03531 0.00703  208 LYS A C     
834  O O     . LYS A 144 ? 0.14800 0.26833 0.23594 -0.01494 -0.02968 0.01199  208 LYS A O     
835  C CB    . LYS A 144 ? 0.20116 0.33162 0.30223 -0.02952 -0.04124 -0.00345 208 LYS A CB    
836  C CG    . LYS A 144 ? 0.15051 0.27274 0.24043 -0.02681 -0.04376 -0.00534 208 LYS A CG    
837  C CD    . LYS A 144 ? 0.26662 0.37674 0.35887 -0.03601 -0.04467 -0.01121 208 LYS A CD    
838  C CE    . LYS A 144 ? 0.26282 0.38318 0.35532 -0.03949 -0.05212 -0.02037 208 LYS A CE    
839  N NZ    . LYS A 144 ? 0.31867 0.42162 0.39857 -0.03873 -0.05281 -0.02649 208 LYS A NZ    
840  N N     . VAL A 145 ? 0.14713 0.27432 0.22170 -0.00408 -0.03796 0.00688  209 VAL A N     
841  C CA    . VAL A 145 ? 0.14097 0.25714 0.20379 0.00308  -0.03398 0.01250  209 VAL A CA    
842  C C     . VAL A 145 ? 0.16330 0.26535 0.21475 0.00394  -0.03453 0.00953  209 VAL A C     
843  O O     . VAL A 145 ? 0.18068 0.28589 0.22631 0.00542  -0.03959 0.00392  209 VAL A O     
844  C CB    . VAL A 145 ? 0.13048 0.24687 0.18304 0.01329  -0.03311 0.01447  209 VAL A CB    
845  C CG1   . VAL A 145 ? 0.13157 0.23249 0.16921 0.01985  -0.02865 0.01931  209 VAL A CG1   
846  C CG2   . VAL A 145 ? 0.13143 0.25517 0.19276 0.01214  -0.03001 0.01616  209 VAL A CG2   
847  N N     A ILE A 146 ? 0.13760 0.22296 0.18496 0.00313  -0.02893 0.01272  210 ILE A N     
848  N N     B ILE A 146 ? 0.13656 0.22212 0.18485 0.00248  -0.02902 0.01252  210 ILE A N     
849  C CA    A ILE A 146 ? 0.15423 0.22439 0.19162 0.00374  -0.02724 0.00962  210 ILE A CA    
850  C CA    B ILE A 146 ? 0.15368 0.22390 0.19104 0.00387  -0.02716 0.00982  210 ILE A CA    
851  C C     A ILE A 146 ? 0.14417 0.20306 0.16963 0.01002  -0.02198 0.01458  210 ILE A C     
852  C C     B ILE A 146 ? 0.14535 0.20620 0.17027 0.01095  -0.02246 0.01497  210 ILE A C     
853  O O     A ILE A 146 ? 0.12504 0.17994 0.15458 0.00905  -0.01800 0.01988  210 ILE A O     
854  O O     B ILE A 146 ? 0.10749 0.16792 0.13523 0.01173  -0.01929 0.02073  210 ILE A O     
855  C CB    A ILE A 146 ? 0.14178 0.20289 0.18846 -0.00428 -0.02548 0.00747  210 ILE A CB    
856  C CB    B ILE A 146 ? 0.14029 0.19977 0.18577 -0.00350 -0.02467 0.00822  210 ILE A CB    
857  C CG1   A ILE A 146 ? 0.16859 0.23889 0.22608 -0.01181 -0.03038 0.00231  210 ILE A CG1   
858  C CG1   B ILE A 146 ? 0.16960 0.23500 0.22466 -0.01112 -0.02925 0.00216  210 ILE A CG1   
859  C CG2   A ILE A 146 ? 0.13475 0.18139 0.17212 -0.00263 -0.02276 0.00376  210 ILE A CG2   
860  C CG2   B ILE A 146 ? 0.12804 0.17280 0.16337 -0.00091 -0.02116 0.00575  210 ILE A CG2   
861  C CD1   A ILE A 146 ? 0.15368 0.21377 0.22046 -0.01975 -0.02870 0.00126  210 ILE A CD1   
862  C CD1   B ILE A 146 ? 0.14912 0.21706 0.21897 -0.01901 -0.02849 0.00516  210 ILE A CD1   
863  N N     . VAL A 147 ? 0.18945 0.24248 0.19932 0.01573  -0.02193 0.01279  211 VAL A N     
864  C CA    . VAL A 147 ? 0.15416 0.19607 0.15074 0.02114  -0.01682 0.01715  211 VAL A CA    
865  C C     . VAL A 147 ? 0.24706 0.27598 0.23739 0.01932  -0.01249 0.01402  211 VAL A C     
866  O O     . VAL A 147 ? 0.21121 0.23801 0.19275 0.02016  -0.01417 0.00871  211 VAL A O     
867  C CB    . VAL A 147 ? 0.19129 0.23533 0.17278 0.02969  -0.01938 0.01857  211 VAL A CB    
868  C CG1   . VAL A 147 ? 0.19930 0.22804 0.16459 0.03387  -0.01343 0.02240  211 VAL A CG1   
869  C CG2   . VAL A 147 ? 0.20398 0.26126 0.19309 0.03274  -0.02231 0.02193  211 VAL A CG2   
870  N N     . THR A 148 ? 0.18596 0.20707 0.18100 0.01688  -0.00697 0.01690  212 THR A N     
871  C CA    . THR A 148 ? 0.17396 0.18449 0.16475 0.01584  -0.00167 0.01424  212 THR A CA    
872  C C     . THR A 148 ? 0.18166 0.18411 0.15892 0.01949  0.00363  0.01848  212 THR A C     
873  O O     . THR A 148 ? 0.16022 0.16214 0.14023 0.01951  0.00522  0.02382  212 THR A O     
874  C CB    . THR A 148 ? 0.14709 0.15568 0.15407 0.01079  0.00033  0.01413  212 THR A CB    
875  O OG1   . THR A 148 ? 0.12050 0.13430 0.13880 0.00681  -0.00447 0.01083  212 THR A OG1   
876  C CG2   . THR A 148 ? 0.18289 0.18313 0.18759 0.01055  0.00585  0.01026  212 THR A CG2   
877  N N     . SER A 149 ? 0.20149 0.19666 0.16257 0.02215  0.00645  0.01613  213 SER A N     
878  C CA    . SER A 149 ? 0.24919 0.23486 0.19578 0.02477  0.01186  0.02044  213 SER A CA    
879  C C     . SER A 149 ? 0.25629 0.23282 0.19462 0.02308  0.01912  0.01732  213 SER A C     
880  O O     . SER A 149 ? 0.28131 0.25769 0.21730 0.02254  0.01907  0.01142  213 SER A O     
881  C CB    . SER A 149 ? 0.25857 0.24258 0.18767 0.03141  0.00847  0.02316  213 SER A CB    
882  O OG    . SER A 149 ? 0.26348 0.23931 0.18860 0.03085  0.01244  0.02585  213 SER A OG    
883  N N     . LYS A 150 ? 0.23017 0.19925 0.16412 0.02178  0.02577  0.02100  214 LYS A N     
884  C CA    . LYS A 150 ? 0.21546 0.17657 0.14181 0.01946  0.03435  0.01888  214 LYS A CA    
885  C C     . LYS A 150 ? 0.23489 0.18893 0.15195 0.01916  0.03480  0.02120  214 LYS A C     
886  O O     . LYS A 150 ? 0.25404 0.20935 0.17928 0.01731  0.03298  0.02350  214 LYS A O     
887  C CB    . LYS A 150 ? 0.20135 0.16654 0.14730 0.01441  0.03874  0.01759  214 LYS A CB    
888  C CG    . LYS A 150 ? 0.21733 0.17664 0.15746 0.01161  0.04869  0.01555  214 LYS A CG    
889  C CD    . LYS A 150 ? 0.23435 0.19233 0.16807 0.01269  0.05115  0.00876  214 LYS A CD    
890  C CE    . LYS A 150 ? 0.23705 0.19254 0.17066 0.00933  0.06174  0.00551  214 LYS A CE    
891  N NZ    . LYS A 150 ? 0.29783 0.24709 0.22001 0.00727  0.06152  0.00847  214 LYS A NZ    
892  N N     . HIS A 151 ? 0.24497 0.19277 0.14779 0.02030  0.03593  0.01927  215 HIS A N     
893  C CA    . HIS A 151 ? 0.25660 0.19723 0.15223 0.01950  0.03662  0.02070  215 HIS A CA    
894  C C     . HIS A 151 ? 0.29426 0.23033 0.18789 0.01478  0.04459  0.01870  215 HIS A C     
895  O O     . HIS A 151 ? 0.29534 0.23311 0.18904 0.01362  0.04904  0.01514  215 HIS A O     
896  C CB    . HIS A 151 ? 0.24278 0.17977 0.12391 0.02455  0.03196  0.02100  215 HIS A CB    
897  C CG    . HIS A 151 ? 0.25140 0.17987 0.12473 0.02507  0.03241  0.02322  215 HIS A CG    
898  N ND1   . HIS A 151 ? 0.28790 0.20743 0.15096 0.02251  0.03789  0.02295  215 HIS A ND1   
899  C CD2   . HIS A 151 ? 0.27205 0.19884 0.14546 0.02808  0.02872  0.02547  215 HIS A CD2   
900  C CE1   . HIS A 151 ? 0.26070 0.17227 0.11687 0.02400  0.03731  0.02535  215 HIS A CE1   
901  N NE2   . HIS A 151 ? 0.27320 0.18881 0.13548 0.02760  0.03194  0.02663  215 HIS A NE2   
902  N N     . ASN A 152 ? 0.30513 0.23591 0.19751 0.01198  0.04683  0.02029  216 ASN A N     
903  C CA    . ASN A 152 ? 0.31955 0.24771 0.21189 0.00688  0.05458  0.01854  216 ASN A CA    
904  C C     . ASN A 152 ? 0.31298 0.23671 0.19184 0.00758  0.05840  0.01605  216 ASN A C     
905  O O     . ASN A 152 ? 0.32022 0.24624 0.20250 0.00420  0.06518  0.01273  216 ASN A O     
906  C CB    . ASN A 152 ? 0.31335 0.23527 0.20340 0.00397  0.05597  0.02062  216 ASN A CB    
907  C CG    . ASN A 152 ? 0.34337 0.27144 0.24849 0.00090  0.05451  0.02132  216 ASN A CG    
908  O OD1   . ASN A 152 ? 0.33502 0.27197 0.25329 0.00017  0.05372  0.02046  216 ASN A OD1   
909  N ND2   . ASN A 152 ? 0.30561 0.22840 0.20804 -0.00084 0.05420  0.02279  216 ASN A ND2   
910  N N     . ASN A 153 ? 0.25178 0.17009 0.11581 0.01209  0.05410  0.01715  217 ASN A N     
911  C CA    . ASN A 153 ? 0.29283 0.20652 0.14200 0.01267  0.05699  0.01482  217 ASN A CA    
912  C C     . ASN A 153 ? 0.34365 0.26286 0.19038 0.01581  0.05396  0.01083  217 ASN A C     
913  O O     . ASN A 153 ? 0.36746 0.28301 0.19914 0.01808  0.05252  0.00928  217 ASN A O     
914  C CB    . ASN A 153 ? 0.33625 0.23963 0.16813 0.01559  0.05449  0.01801  217 ASN A CB    
915  C CG    . ASN A 153 ? 0.36235 0.25866 0.19484 0.01396  0.05561  0.02165  217 ASN A CG    
916  O OD1   . ASN A 153 ? 0.40981 0.30634 0.25048 0.00860  0.06103  0.02133  217 ASN A OD1   
917  N ND2   . ASN A 153 ? 0.33410 0.22327 0.15625 0.01866  0.05088  0.02466  217 ASN A ND2   
918  N N     . ASP A 154 ? 0.31470 0.24200 0.17477 0.01587  0.05299  0.00868  218 ASP A N     
919  C CA    . ASP A 154 ? 0.25960 0.19081 0.11592 0.01884  0.04975  0.00386  218 ASP A CA    
920  C C     . ASP A 154 ? 0.25323 0.19122 0.12607 0.01755  0.05253  0.00051  218 ASP A C     
921  O O     . ASP A 154 ? 0.27190 0.21291 0.15914 0.01524  0.05473  0.00356  218 ASP A O     
922  C CB    . ASP A 154 ? 0.29070 0.22328 0.13992 0.02416  0.03954  0.00627  218 ASP A CB    
923  C CG    . ASP A 154 ? 0.35521 0.29043 0.19501 0.02688  0.03479  0.00053  218 ASP A CG    
924  O OD1   . ASP A 154 ? 0.38581 0.32057 0.22411 0.02478  0.03959  -0.00616 218 ASP A OD1   
925  O OD2   . ASP A 154 ? 0.32157 0.26000 0.15649 0.03113  0.02576  0.00202  218 ASP A OD2   
926  N N     . THR A 155 ? 0.24117 0.18103 0.11225 0.01905  0.05215  -0.00638 219 THR A N     
927  C CA    . THR A 155 ? 0.19071 0.13721 0.08223 0.01800  0.05319  -0.01011 219 THR A CA    
928  C C     . THR A 155 ? 0.19196 0.14619 0.09580 0.01935  0.04235  -0.00617 219 THR A C     
929  O O     . THR A 155 ? 0.21563 0.16897 0.10736 0.02263  0.03617  -0.00212 219 THR A O     
930  C CB    . THR A 155 ? 0.22375 0.17104 0.11744 0.01779  0.05370  -0.01960 219 THR A CB    
931  O OG1   . THR A 155 ? 0.25930 0.20518 0.13753 0.02039  0.04527  -0.02219 219 THR A OG1   
932  C CG2   . THR A 155 ? 0.21563 0.15787 0.10154 0.01602  0.06506  -0.02362 219 THR A CG2   
933  N N     . GLN A 156 ? 0.23440 0.19627 0.16254 0.01710  0.04040  -0.00714 220 GLN A N     
934  C CA    . GLN A 156 ? 0.20696 0.17630 0.14796 0.01728  0.03150  -0.00352 220 GLN A CA    
935  C C     . GLN A 156 ? 0.24278 0.21587 0.18215 0.01811  0.02330  -0.00836 220 GLN A C     
936  O O     . GLN A 156 ? 0.26117 0.23226 0.20027 0.01708  0.02418  -0.01577 220 GLN A O     
937  C CB    . GLN A 156 ? 0.20680 0.18128 0.17200 0.01436  0.03224  -0.00254 220 GLN A CB    
938  C CG    . GLN A 156 ? 0.13990 0.12129 0.11800 0.01366  0.02417  0.00153  220 GLN A CG    
939  C CD    . GLN A 156 ? 0.21081 0.19523 0.20871 0.01118  0.02525  0.00435  220 GLN A CD    
940  O OE1   . GLN A 156 ? 0.17002 0.15323 0.16969 0.01039  0.03062  0.00711  220 GLN A OE1   
941  N NE2   . GLN A 156 ? 0.18704 0.17513 0.19924 0.00958  0.01988  0.00382  220 GLN A NE2   
942  N N     . HIS A 157 ? 0.18065 0.15959 0.11920 0.01983  0.01544  -0.00465 221 HIS A N     
943  C CA    . HIS A 157 ? 0.22145 0.20640 0.15879 0.02008  0.00693  -0.00899 221 HIS A CA    
944  C C     . HIS A 157 ? 0.21571 0.21128 0.17012 0.01846  0.00028  -0.00564 221 HIS A C     
945  O O     . HIS A 157 ? 0.19133 0.18880 0.15242 0.01889  0.00149  0.00094  221 HIS A O     
946  C CB    . HIS A 157 ? 0.18584 0.16891 0.10011 0.02494  0.00349  -0.00878 221 HIS A CB    
947  C CG    . HIS A 157 ? 0.24453 0.21697 0.13921 0.02579  0.00917  -0.01330 221 HIS A CG    
948  N ND1   . HIS A 157 ? 0.24043 0.20267 0.12257 0.02682  0.01834  -0.00986 221 HIS A ND1   
949  C CD2   . HIS A 157 ? 0.23103 0.20109 0.11546 0.02520  0.00743  -0.02120 221 HIS A CD2   
950  C CE1   . HIS A 157 ? 0.27774 0.23213 0.14295 0.02691  0.02264  -0.01519 221 HIS A CE1   
951  N NE2   . HIS A 157 ? 0.25455 0.21319 0.12021 0.02626  0.01598  -0.02224 221 HIS A NE2   
952  N N     . ILE A 158 ? 0.21323 0.21547 0.17381 0.01597  -0.00648 -0.01064 222 ILE A N     
953  C CA    . ILE A 158 ? 0.20582 0.21930 0.18175 0.01340  -0.01267 -0.00845 222 ILE A CA    
954  C C     . ILE A 158 ? 0.24071 0.26433 0.20947 0.01567  -0.02089 -0.01051 222 ILE A C     
955  O O     . ILE A 158 ? 0.21335 0.23623 0.17320 0.01517  -0.02424 -0.01731 222 ILE A O     
956  C CB    . ILE A 158 ? 0.18695 0.19984 0.17966 0.00685  -0.01332 -0.01258 222 ILE A CB    
957  C CG1   . ILE A 158 ? 0.20010 0.20513 0.20210 0.00589  -0.00645 -0.00943 222 ILE A CG1   
958  C CG2   . ILE A 158 ? 0.17541 0.20023 0.18171 0.00294  -0.01969 -0.01102 222 ILE A CG2   
959  C CD1   . ILE A 158 ? 0.15638 0.15536 0.17003 0.00158  -0.00565 -0.01463 222 ILE A CD1   
960  N N     . TRP A 159 ? 0.19696 0.23059 0.16974 0.01843  -0.02426 -0.00502 223 TRP A N     
961  C CA    . TRP A 159 ? 0.18509 0.23277 0.15686 0.02088  -0.03277 -0.00645 223 TRP A CA    
962  C C     . TRP A 159 ? 0.20800 0.26899 0.20138 0.01494  -0.03600 -0.00622 223 TRP A C     
963  O O     . TRP A 159 ? 0.19406 0.25359 0.19815 0.01270  -0.03166 -0.00122 223 TRP A O     
964  C CB    . TRP A 159 ? 0.16046 0.20882 0.11960 0.02994  -0.03309 -0.00018 223 TRP A CB    
965  C CG    . TRP A 159 ? 0.20571 0.26982 0.16505 0.03513  -0.04146 0.00012  223 TRP A CG    
966  C CD1   . TRP A 159 ? 0.26222 0.32773 0.20504 0.04195  -0.04717 -0.00135 223 TRP A CD1   
967  C CD2   . TRP A 159 ? 0.24252 0.32350 0.21917 0.03478  -0.04469 0.00245  223 TRP A CD2   
968  N NE1   . TRP A 159 ? 0.25599 0.33398 0.20958 0.04333  -0.05109 -0.00023 223 TRP A NE1   
969  C CE2   . TRP A 159 ? 0.24710 0.33545 0.22046 0.03940  -0.04973 0.00171  223 TRP A CE2   
970  C CE3   . TRP A 159 ? 0.18989 0.27649 0.18539 0.02905  -0.04155 0.00501  223 TRP A CE3   
971  C CZ2   . TRP A 159 ? 0.27072 0.37254 0.25930 0.03887  -0.05134 0.00283  223 TRP A CZ2   
972  C CZ3   . TRP A 159 ? 0.21384 0.31575 0.22236 0.02920  -0.04403 0.00635  223 TRP A CZ3   
973  C CH2   . TRP A 159 ? 0.23158 0.33945 0.23679 0.03369  -0.04805 0.00488  223 TRP A CH2   
974  N N     . GLU A 160 ? 0.19509 0.26873 0.19468 0.01149  -0.04340 -0.01178 224 GLU A N     
975  C CA    . GLU A 160 ? 0.19337 0.27979 0.21342 0.00465  -0.04551 -0.01145 224 GLU A CA    
976  C C     . GLU A 160 ? 0.24651 0.35314 0.27060 0.00540  -0.05435 -0.01493 224 GLU A C     
977  O O     . GLU A 160 ? 0.27924 0.38772 0.29239 0.00761  -0.06009 -0.02043 224 GLU A O     
978  C CB    . GLU A 160 ? 0.20556 0.28400 0.23581 -0.00534 -0.04377 -0.01594 224 GLU A CB    
979  C CG    . GLU A 160 ? 0.28494 0.35756 0.30737 -0.00847 -0.04716 -0.02531 224 GLU A CG    
980  C CD    . GLU A 160 ? 0.39329 0.48218 0.42254 -0.01384 -0.05604 -0.03177 224 GLU A CD    
981  O OE1   . GLU A 160 ? 0.39960 0.50555 0.44221 -0.01569 -0.05894 -0.02897 224 GLU A OE1   
982  O OE2   . GLU A 160 ? 0.39725 0.48283 0.41836 -0.01632 -0.06011 -0.04009 224 GLU A OE2   
983  N N     . SER A 161 ? 0.30541 0.42810 0.34539 0.00346  -0.05548 -0.01196 225 SER A N     
984  C CA    . SER A 161 ? 0.29256 0.43109 0.33814 0.00394  -0.06159 -0.01432 225 SER A CA    
985  C C     . SER A 161 ? 0.27428 0.42194 0.33942 -0.00288 -0.05912 -0.01213 225 SER A C     
986  O O     . SER A 161 ? 0.23464 0.37826 0.30554 -0.00411 -0.05293 -0.00694 225 SER A O     
987  C CB    . SER A 161 ? 0.29000 0.42775 0.32307 0.01570  -0.06196 -0.01006 225 SER A CB    
988  O OG    . SER A 161 ? 0.34021 0.49174 0.38152 0.01615  -0.06624 -0.01129 225 SER A OG    
989  N N     . ASP A 162 ? 0.48054 0.63987 0.55471 -0.00733 -0.06390 -0.01616 226 ASP A N     
990  C CA    . ASP A 162 ? 0.46929 0.63939 0.56027 -0.01183 -0.06192 -0.01444 226 ASP A CA    
991  C C     . ASP A 162 ? 0.45117 0.63343 0.54268 -0.00334 -0.06383 -0.01264 226 ASP A C     
992  O O     . ASP A 162 ? 0.49570 0.69068 0.60142 -0.00666 -0.06355 -0.01291 226 ASP A O     
993  C CB    . ASP A 162 ? 0.49332 0.66805 0.59605 -0.02404 -0.06530 -0.02021 226 ASP A CB    
994  C CG    . ASP A 162 ? 0.54583 0.73087 0.64634 -0.02370 -0.07387 -0.02604 226 ASP A CG    
995  O OD1   . ASP A 162 ? 0.55256 0.74403 0.66386 -0.03323 -0.07696 -0.03041 226 ASP A OD1   
996  O OD2   . ASP A 162 ? 0.58243 0.76772 0.66940 -0.01422 -0.07754 -0.02617 226 ASP A OD2   
997  N N     . SER A 163 ? 0.39841 0.57624 0.47449 0.00743  -0.06548 -0.01094 227 SER A N     
998  C CA    . SER A 163 ? 0.40494 0.59114 0.47804 0.01689  -0.06804 -0.00952 227 SER A CA    
999  C C     . SER A 163 ? 0.45034 0.64999 0.52704 0.01551  -0.07685 -0.01490 227 SER A C     
1000 O O     . SER A 163 ? 0.51217 0.72222 0.59028 0.02248  -0.07987 -0.01421 227 SER A O     
1001 C CB    . SER A 163 ? 0.36338 0.55730 0.44754 0.01907  -0.06273 -0.00571 227 SER A CB    
1002 O OG    . SER A 163 ? 0.41028 0.61900 0.51349 0.01041  -0.06339 -0.00842 227 SER A OG    
1003 N N     . ASN A 164 ? 0.35940 0.55875 0.43706 0.00682  -0.08132 -0.02054 228 ASN A N     
1004 C CA    . ASN A 164 ? 0.36370 0.57296 0.44060 0.00552  -0.09044 -0.02609 228 ASN A CA    
1005 C C     . ASN A 164 ? 0.39788 0.59462 0.45326 0.00932  -0.09447 -0.02872 228 ASN A C     
1006 O O     . ASN A 164 ? 0.44344 0.64231 0.48796 0.01718  -0.09973 -0.02866 228 ASN A O     
1007 C CB    . ASN A 164 ? 0.41481 0.63267 0.50785 -0.00814 -0.09297 -0.03158 228 ASN A CB    
1008 C CG    . ASN A 164 ? 0.48558 0.72121 0.59927 -0.01099 -0.09181 -0.03036 228 ASN A CG    
1009 O OD1   . ASN A 164 ? 0.49098 0.72763 0.61835 -0.02050 -0.08733 -0.03034 228 ASN A OD1   
1010 N ND2   . ASN A 164 ? 0.46839 0.71768 0.58406 -0.00259 -0.09560 -0.02934 228 ASN A ND2   
1011 N N     . GLU A 165 ? 0.56603 0.74934 0.61454 0.00385  -0.09202 -0.03128 229 GLU A N     
1012 C CA    . GLU A 165 ? 0.55606 0.72437 0.58218 0.00834  -0.09302 -0.03310 229 GLU A CA    
1013 C C     . GLU A 165 ? 0.53296 0.68682 0.55311 0.01067  -0.08478 -0.02898 229 GLU A C     
1014 O O     . GLU A 165 ? 0.50297 0.65859 0.53604 0.00851  -0.07911 -0.02477 229 GLU A O     
1015 C CB    . GLU A 165 ? 0.54295 0.70828 0.56439 -0.00040 -0.09842 -0.04217 229 GLU A CB    
1016 C CG    . GLU A 165 ? 0.68689 0.86590 0.71241 -0.00318 -0.10755 -0.04663 229 GLU A CG    
1017 C CD    . GLU A 165 ? 0.84219 1.01931 0.87026 -0.01569 -0.11159 -0.05575 229 GLU A CD    
1018 O OE1   . GLU A 165 ? 0.78652 0.94768 0.80227 -0.01869 -0.10927 -0.06029 229 GLU A OE1   
1019 O OE2   . GLU A 165 ? 0.79740 0.98820 0.83926 -0.02247 -0.11692 -0.05880 229 GLU A OE2   
1020 N N     . PHE A 166 ? 0.34168 0.48084 0.34126 0.01518  -0.08395 -0.03006 230 PHE A N     
1021 C CA    . PHE A 166 ? 0.23011 0.35574 0.22341 0.01668  -0.07684 -0.02744 230 PHE A CA    
1022 C C     . PHE A 166 ? 0.29294 0.40481 0.26793 0.01569  -0.07750 -0.03411 230 PHE A C     
1023 O O     . PHE A 166 ? 0.29144 0.40162 0.25394 0.01631  -0.08255 -0.03861 230 PHE A O     
1024 C CB    . PHE A 166 ? 0.26340 0.38187 0.24809 0.02701  -0.07134 -0.01830 230 PHE A CB    
1025 C CG    . PHE A 166 ? 0.26101 0.36960 0.22372 0.03565  -0.07255 -0.01658 230 PHE A CG    
1026 C CD1   . PHE A 166 ? 0.32880 0.44566 0.29167 0.04055  -0.07728 -0.01510 230 PHE A CD1   
1027 C CD2   . PHE A 166 ? 0.29053 0.38083 0.23259 0.03883  -0.06818 -0.01599 230 PHE A CD2   
1028 C CE1   . PHE A 166 ? 0.36151 0.46843 0.30452 0.04814  -0.07837 -0.01300 230 PHE A CE1   
1029 C CE2   . PHE A 166 ? 0.30850 0.38793 0.23044 0.04553  -0.06805 -0.01360 230 PHE A CE2   
1030 C CZ    . PHE A 166 ? 0.31873 0.40639 0.24122 0.05016  -0.07352 -0.01202 230 PHE A CZ    
1031 N N     . SER A 167 ? 0.33174 0.42848 0.30617 0.01289  -0.06931 -0.03331 231 SER A N     
1032 C CA    . SER A 167 ? 0.30787 0.38533 0.26570 0.01191  -0.06502 -0.03787 231 SER A CA    
1033 C C     . SER A 167 ? 0.27554 0.33672 0.22629 0.01630  -0.05436 -0.03087 231 SER A C     
1034 O O     . SER A 167 ? 0.23614 0.29929 0.19824 0.01715  -0.05019 -0.02380 231 SER A O     
1035 C CB    . SER A 167 ? 0.36720 0.43977 0.33516 0.00104  -0.06447 -0.04606 231 SER A CB    
1036 O OG    . SER A 167 ? 0.35315 0.42024 0.33778 -0.00376 -0.05739 -0.04219 231 SER A OG    
1037 N N     . VAL A 168 ? 0.27347 0.31912 0.20455 0.01887  -0.04994 -0.03311 232 VAL A N     
1038 C CA    . VAL A 168 ? 0.25822 0.28863 0.18236 0.02169  -0.03930 -0.02783 232 VAL A CA    
1039 C C     . VAL A 168 ? 0.29086 0.30745 0.20949 0.01754  -0.03325 -0.03475 232 VAL A C     
1040 O O     . VAL A 168 ? 0.27129 0.28368 0.17358 0.01788  -0.03579 -0.04143 232 VAL A O     
1041 C CB    . VAL A 168 ? 0.25716 0.28189 0.15920 0.03077  -0.03827 -0.02206 232 VAL A CB    
1042 C CG1   . VAL A 168 ? 0.21885 0.22802 0.11452 0.03167  -0.02673 -0.01753 232 VAL A CG1   
1043 C CG2   . VAL A 168 ? 0.28961 0.32713 0.19661 0.03652  -0.04407 -0.01554 232 VAL A CG2   
1044 N N     . ILE A 169 ? 0.19641 0.20604 0.12805 0.01419  -0.02540 -0.03337 233 ILE A N     
1045 C CA    . ILE A 169 ? 0.21306 0.21045 0.14251 0.01121  -0.01900 -0.04010 233 ILE A CA    
1046 C C     . ILE A 169 ? 0.21855 0.20679 0.14823 0.01343  -0.00826 -0.03521 233 ILE A C     
1047 O O     . ILE A 169 ? 0.17754 0.16885 0.11555 0.01479  -0.00634 -0.02717 233 ILE A O     
1048 C CB    . ILE A 169 ? 0.23966 0.23778 0.18801 0.00404  -0.02112 -0.04566 233 ILE A CB    
1049 C CG1   . ILE A 169 ? 0.20482 0.20592 0.17447 0.00197  -0.01881 -0.03857 233 ILE A CG1   
1050 C CG2   . ILE A 169 ? 0.20402 0.21205 0.15302 0.00014  -0.03163 -0.05130 233 ILE A CG2   
1051 C CD1   . ILE A 169 ? 0.22405 0.22040 0.21048 -0.00447 -0.01867 -0.04279 233 ILE A CD1   
1052 N N     . ALA A 170 ? 0.26356 0.24112 0.18396 0.01355  -0.00105 -0.04061 234 ALA A N     
1053 C CA    . ALA A 170 ? 0.28674 0.25801 0.21332 0.01412  0.00931  -0.03783 234 ALA A CA    
1054 C C     . ALA A 170 ? 0.26566 0.24010 0.21770 0.01092  0.00905  -0.03598 234 ALA A C     
1055 O O     . ALA A 170 ? 0.24548 0.22015 0.20756 0.00741  0.00484  -0.04109 234 ALA A O     
1056 C CB    . ALA A 170 ? 0.31596 0.27721 0.23147 0.01436  0.01721  -0.04570 234 ALA A CB    
1057 N N     . ASP A 171 ? 0.23949 0.21529 0.20091 0.01179  0.01330  -0.02863 235 ASP A N     
1058 C CA    . ASP A 171 ? 0.23081 0.20877 0.21462 0.00924  0.01273  -0.02617 235 ASP A CA    
1059 C C     . ASP A 171 ? 0.25671 0.22768 0.24887 0.00893  0.01843  -0.03238 235 ASP A C     
1060 O O     . ASP A 171 ? 0.22649 0.19459 0.21673 0.01109  0.02663  -0.03275 235 ASP A O     
1061 C CB    . ASP A 171 ? 0.23237 0.21369 0.22230 0.01026  0.01518  -0.01706 235 ASP A CB    
1062 C CG    . ASP A 171 ? 0.23589 0.22047 0.24607 0.00772  0.01235  -0.01297 235 ASP A CG    
1063 O OD1   . ASP A 171 ? 0.23850 0.21994 0.25974 0.00576  0.01127  -0.01703 235 ASP A OD1   
1064 O OD2   . ASP A 171 ? 0.24173 0.23061 0.25520 0.00783  0.01137  -0.00555 235 ASP A OD2   
1065 N N     . PRO A 172 ? 0.23543 0.20345 0.23791 0.00632  0.01480  -0.03719 236 PRO A N     
1066 C CA    . PRO A 172 ? 0.18388 0.14396 0.19484 0.00742  0.02026  -0.04318 236 PRO A CA    
1067 C C     . PRO A 172 ? 0.25053 0.21221 0.27809 0.00947  0.02457  -0.03765 236 PRO A C     
1068 O O     . PRO A 172 ? 0.20147 0.15868 0.23634 0.01213  0.03031  -0.04212 236 PRO A O     
1069 C CB    . PRO A 172 ? 0.22495 0.18012 0.24245 0.00354  0.01397  -0.04810 236 PRO A CB    
1070 C CG    . PRO A 172 ? 0.22537 0.18887 0.24722 -0.00011 0.00626  -0.04116 236 PRO A CG    
1071 C CD    . PRO A 172 ? 0.19341 0.16492 0.20140 0.00207  0.00599  -0.03714 236 PRO A CD    
1072 N N     . ARG A 173 ? 0.23483 0.20323 0.26851 0.00868  0.02193  -0.02850 237 ARG A N     
1073 C CA    . ARG A 173 ? 0.18560 0.15644 0.23394 0.01030  0.02501  -0.02338 237 ARG A CA    
1074 C C     . ARG A 173 ? 0.22386 0.19804 0.26682 0.01234  0.03286  -0.02232 237 ARG A C     
1075 O O     . ARG A 173 ? 0.25622 0.23420 0.31166 0.01334  0.03574  -0.01892 237 ARG A O     
1076 C CB    . ARG A 173 ? 0.16687 0.14251 0.22288 0.00793  0.01888  -0.01447 237 ARG A CB    
1077 C CG    . ARG A 173 ? 0.17026 0.14267 0.23228 0.00466  0.01207  -0.01485 237 ARG A CG    
1078 C CD    . ARG A 173 ? 0.18384 0.16239 0.24800 0.00157  0.00666  -0.00667 237 ARG A CD    
1079 N NE    . ARG A 173 ? 0.15580 0.14109 0.20694 0.00186  0.00614  -0.00470 237 ARG A NE    
1080 C CZ    . ARG A 173 ? 0.14955 0.14128 0.20017 0.00010  0.00215  0.00104  237 ARG A CZ    
1081 N NH1   . ARG A 173 ? 0.19965 0.19226 0.26093 -0.00307 -0.00122 0.00557  237 ARG A NH1   
1082 N NH2   . ARG A 173 ? 0.14622 0.14302 0.18467 0.00191  0.00178  0.00229  237 ARG A NH2   
1083 N N     . GLY A 174 ? 0.22078 0.19353 0.24510 0.01259  0.03617  -0.02496 238 GLY A N     
1084 C CA    . GLY A 174 ? 0.21506 0.18916 0.23201 0.01334  0.04438  -0.02365 238 GLY A CA    
1085 C C     . GLY A 174 ? 0.21514 0.19325 0.23005 0.01194  0.04266  -0.01463 238 GLY A C     
1086 O O     . GLY A 174 ? 0.23061 0.21029 0.24356 0.01117  0.03539  -0.01001 238 GLY A O     
1087 N N     . ASN A 175 ? 0.27161 0.25158 0.28746 0.01132  0.04988  -0.01253 239 ASN A N     
1088 C CA    . ASN A 175 ? 0.25508 0.23655 0.26673 0.00953  0.04946  -0.00477 239 ASN A CA    
1089 C C     . ASN A 175 ? 0.29485 0.28252 0.32671 0.00837  0.04549  -0.00019 239 ASN A C     
1090 O O     . ASN A 175 ? 0.27173 0.26403 0.31590 0.00739  0.04975  0.00003  239 ASN A O     
1091 C CB    . ASN A 175 ? 0.25686 0.23592 0.25783 0.00799  0.05925  -0.00483 239 ASN A CB    
1092 C CG    . ASN A 175 ? 0.22523 0.20395 0.22256 0.00541  0.05956  0.00255  239 ASN A CG    
1093 O OD1   . ASN A 175 ? 0.22751 0.20690 0.22595 0.00565  0.05238  0.00776  239 ASN A OD1   
1094 N ND2   . ASN A 175 ? 0.24556 0.22274 0.23793 0.00246  0.06849  0.00272  239 ASN A ND2   
1095 N N     . THR A 176 ? 0.19774 0.18622 0.23284 0.00830  0.03716  0.00352  240 THR A N     
1096 C CA    . THR A 176 ? 0.14797 0.14081 0.19845 0.00708  0.03269  0.00869  240 THR A CA    
1097 C C     . THR A 176 ? 0.14821 0.14174 0.19198 0.00525  0.03138  0.01557  240 THR A C     
1098 O O     . THR A 176 ? 0.18046 0.17745 0.23424 0.00356  0.03027  0.01946  240 THR A O     
1099 C CB    . THR A 176 ? 0.16405 0.15636 0.22219 0.00725  0.02526  0.00881  240 THR A CB    
1100 O OG1   . THR A 176 ? 0.13994 0.13174 0.18621 0.00668  0.02108  0.01074  240 THR A OG1   
1101 C CG2   . THR A 176 ? 0.17095 0.15981 0.23438 0.00897  0.02632  0.00138  240 THR A CG2   
1102 N N     . LEU A 177 ? 0.18487 0.17473 0.21131 0.00596  0.03122  0.01697  241 LEU A N     
1103 C CA    . LEU A 177 ? 0.17716 0.16553 0.19537 0.00509  0.03062  0.02295  241 LEU A CA    
1104 C C     . LEU A 177 ? 0.20206 0.18723 0.21462 0.00288  0.03778  0.02381  241 LEU A C     
1105 O O     . LEU A 177 ? 0.17595 0.16055 0.18570 0.00126  0.03535  0.02653  241 LEU A O     
1106 C CB    . LEU A 177 ? 0.15853 0.14384 0.16028 0.00795  0.02785  0.02408  241 LEU A CB    
1107 C CG    . LEU A 177 ? 0.16192 0.15210 0.16791 0.00919  0.02057  0.02380  241 LEU A CG    
1108 C CD1   . LEU A 177 ? 0.18006 0.16893 0.16963 0.01289  0.01852  0.02405  241 LEU A CD1   
1109 C CD2   . LEU A 177 ? 0.15256 0.14706 0.16968 0.00728  0.01644  0.02872  241 LEU A CD2   
1110 N N     . GLY A 178 ? 0.15015 0.13362 0.15951 0.00259  0.04454  0.01929  242 GLY A N     
1111 C CA    . GLY A 178 ? 0.15091 0.13073 0.15225 -0.00042 0.05076  0.01943  242 GLY A CA    
1112 C C     . GLY A 178 ? 0.15876 0.12963 0.13819 0.00078  0.04894  0.02051  242 GLY A C     
1113 O O     . GLY A 178 ? 0.19291 0.15852 0.16111 0.00015  0.05342  0.01818  242 GLY A O     
1114 N N     . ARG A 179 ? 0.16219 0.13221 0.13729 0.00261  0.04180  0.02353  243 ARG A N     
1115 C CA    . ARG A 179 ? 0.19198 0.15586 0.15126 0.00521  0.03857  0.02411  243 ARG A CA    
1116 C C     . ARG A 179 ? 0.15733 0.12528 0.12015 0.00723  0.03129  0.02614  243 ARG A C     
1117 O O     . ARG A 179 ? 0.17500 0.14825 0.14908 0.00483  0.02845  0.02683  243 ARG A O     
1118 C CB    . ARG A 179 ? 0.16309 0.12222 0.11647 0.00227  0.04002  0.02357  243 ARG A CB    
1119 C CG    . ARG A 179 ? 0.15872 0.11054 0.09784 0.00532  0.03783  0.02417  243 ARG A CG    
1120 C CD    . ARG A 179 ? 0.17428 0.12195 0.11097 0.00244  0.03835  0.02456  243 ARG A CD    
1121 N NE    . ARG A 179 ? 0.17947 0.13163 0.12485 0.00107  0.03463  0.02531  243 ARG A NE    
1122 C CZ    . ARG A 179 ? 0.19681 0.15246 0.15037 -0.00360 0.03574  0.02526  243 ARG A CZ    
1123 N NH1   . ARG A 179 ? 0.23834 0.19570 0.19506 -0.00768 0.04030  0.02439  243 ARG A NH1   
1124 N NH2   . ARG A 179 ? 0.21557 0.17386 0.17438 -0.00427 0.03229  0.02601  243 ARG A NH2   
1125 N N     . GLY A 180 ? 0.16870 0.13494 0.12216 0.01154  0.02813  0.02656  244 GLY A N     
1126 C CA    . GLY A 180 ? 0.11431 0.08566 0.07197 0.01322  0.02219  0.02762  244 GLY A CA    
1127 C C     . GLY A 180 ? 0.12174 0.09811 0.07990 0.01715  0.01933  0.02885  244 GLY A C     
1128 O O     . GLY A 180 ? 0.16639 0.14070 0.11662 0.01982  0.02110  0.02857  244 GLY A O     
1129 N N     . THR A 181 ? 0.13862 0.12199 0.10530 0.01720  0.01494  0.02986  245 THR A N     
1130 C CA    . THR A 181 ? 0.13866 0.12912 0.10614 0.02104  0.01090  0.03114  245 THR A CA    
1131 C C     . THR A 181 ? 0.13861 0.13742 0.12064 0.01842  0.00799  0.03269  245 THR A C     
1132 O O     . THR A 181 ? 0.13863 0.13752 0.12335 0.01636  0.00757  0.03157  245 THR A O     
1133 C CB    . THR A 181 ? 0.14649 0.13725 0.10521 0.02537  0.00812  0.02988  245 THR A CB    
1134 O OG1   . THR A 181 ? 0.14416 0.12633 0.08947 0.02734  0.01044  0.02854  245 THR A OG1   
1135 C CG2   . THR A 181 ? 0.12837 0.13020 0.08987 0.02913  0.00258  0.03028  245 THR A CG2   
1136 N N     . THR A 182 ? 0.14273 0.14827 0.13408 0.01792  0.00549  0.03405  246 THR A N     
1137 C CA    . THR A 182 ? 0.15943 0.17329 0.16509 0.01461  0.00218  0.03558  246 THR A CA    
1138 C C     . THR A 182 ? 0.16088 0.18549 0.16805 0.01661  -0.00275 0.03381  246 THR A C     
1139 O O     . THR A 182 ? 0.13829 0.16528 0.14339 0.01730  -0.00530 0.02908  246 THR A O     
1140 C CB    . THR A 182 ? 0.11149 0.12469 0.13051 0.00931  0.00196  0.03344  246 THR A CB    
1141 O OG1   . THR A 182 ? 0.15177 0.15800 0.17159 0.00796  0.00599  0.03513  246 THR A OG1   
1142 C CG2   . THR A 182 ? 0.10232 0.12181 0.13383 0.00536  -0.00123 0.03566  246 THR A CG2   
1143 N N     . ILE A 183 ? 0.12479 0.15597 0.13499 0.01720  -0.00372 0.03635  247 ILE A N     
1144 C CA    . ILE A 183 ? 0.15477 0.20023 0.17135 0.01823  -0.00831 0.03536  247 ILE A CA    
1145 C C     . ILE A 183 ? 0.14444 0.19570 0.17677 0.01068  -0.00933 0.03584  247 ILE A C     
1146 O O     . ILE A 183 ? 0.17164 0.22105 0.20725 0.00812  -0.00685 0.03981  247 ILE A O     
1147 C CB    . ILE A 183 ? 0.17571 0.22213 0.18588 0.02188  -0.00666 0.03455  247 ILE A CB    
1148 C CG1   . ILE A 183 ? 0.17264 0.20666 0.16752 0.02643  -0.00393 0.03296  247 ILE A CG1   
1149 C CG2   . ILE A 183 ? 0.16659 0.22854 0.18296 0.02374  -0.01141 0.03226  247 ILE A CG2   
1150 C CD1   . ILE A 183 ? 0.19863 0.23170 0.18456 0.03080  -0.00676 0.03094  247 ILE A CD1   
1151 N N     . THR A 184 ? 0.11104 0.16716 0.15121 0.00643  -0.01267 0.03126  248 THR A N     
1152 C CA    . THR A 184 ? 0.08420 0.14298 0.13782 -0.00146 -0.01345 0.03153  248 THR A CA    
1153 C C     . THR A 184 ? 0.11823 0.19326 0.18020 -0.00383 -0.01668 0.02974  248 THR A C     
1154 O O     . THR A 184 ? 0.12579 0.20872 0.18697 -0.00223 -0.02062 0.02475  248 THR A O     
1155 C CB    . THR A 184 ? 0.09995 0.14973 0.15700 -0.00565 -0.01416 0.02740  248 THR A CB    
1156 O OG1   . THR A 184 ? 0.11866 0.15617 0.17248 -0.00436 -0.01062 0.02990  248 THR A OG1   
1157 C CG2   . THR A 184 ? 0.09374 0.14510 0.16335 -0.01391 -0.01570 0.02714  248 THR A CG2   
1158 N N     . LEU A 185 ? 0.14294 0.22081 0.21036 -0.00779 -0.01447 0.03273  249 LEU A N     
1159 C CA    . LEU A 185 ? 0.11670 0.20680 0.18976 -0.01019 -0.01533 0.02984  249 LEU A CA    
1160 C C     . LEU A 185 ? 0.12420 0.21118 0.20557 -0.01964 -0.01518 0.02831  249 LEU A C     
1161 O O     . LEU A 185 ? 0.16585 0.24177 0.24553 -0.02272 -0.01223 0.03216  249 LEU A O     
1162 C CB    . LEU A 185 ? 0.13781 0.23135 0.20716 -0.00675 -0.01162 0.03332  249 LEU A CB    
1163 C CG    . LEU A 185 ? 0.20711 0.30508 0.26812 0.00285  -0.01151 0.03322  249 LEU A CG    
1164 C CD1   . LEU A 185 ? 0.21461 0.30085 0.26427 0.00836  -0.01124 0.03462  249 LEU A CD1   
1165 C CD2   . LEU A 185 ? 0.20249 0.30289 0.26153 0.00467  -0.00728 0.03671  249 LEU A CD2   
1166 N N     . VAL A 186 ? 0.13072 0.22615 0.21936 -0.02383 -0.01864 0.02241  250 VAL A N     
1167 C CA    . VAL A 186 ? 0.15133 0.24477 0.24705 -0.03291 -0.01777 0.02016  250 VAL A CA    
1168 C C     . VAL A 186 ? 0.15474 0.26043 0.25495 -0.03370 -0.01544 0.02012  250 VAL A C     
1169 O O     . VAL A 186 ? 0.20786 0.32860 0.31411 -0.03236 -0.01819 0.01572  250 VAL A O     
1170 C CB    . VAL A 186 ? 0.18513 0.28120 0.28668 -0.03812 -0.02241 0.01316  250 VAL A CB    
1171 C CG1   . VAL A 186 ? 0.15715 0.24670 0.26388 -0.04780 -0.02041 0.01124  250 VAL A CG1   
1172 C CG2   . VAL A 186 ? 0.18332 0.26939 0.28054 -0.03585 -0.02507 0.01284  250 VAL A CG2   
1173 N N     . LEU A 187 ? 0.17425 0.27337 0.27162 -0.03557 -0.01077 0.02495  251 LEU A N     
1174 C CA    . LEU A 187 ? 0.17738 0.28771 0.27806 -0.03543 -0.00766 0.02577  251 LEU A CA    
1175 C C     . LEU A 187 ? 0.19231 0.31225 0.30474 -0.04330 -0.00738 0.02090  251 LEU A C     
1176 O O     . LEU A 187 ? 0.19463 0.30665 0.30977 -0.05081 -0.00745 0.01887  251 LEU A O     
1177 C CB    . LEU A 187 ? 0.17926 0.27917 0.27224 -0.03550 -0.00316 0.03208  251 LEU A CB    
1178 C CG    . LEU A 187 ? 0.12472 0.21863 0.20764 -0.02750 -0.00294 0.03676  251 LEU A CG    
1179 C CD1   . LEU A 187 ? 0.11443 0.19739 0.19006 -0.02844 0.00011  0.04180  251 LEU A CD1   
1180 C CD2   . LEU A 187 ? 0.14721 0.25508 0.23038 -0.02036 -0.00275 0.03601  251 LEU A CD2   
1181 N N     . LYS A 188 ? 0.18918 0.32588 0.30895 -0.04137 -0.00688 0.01903  252 LYS A N     
1182 C CA    . LYS A 188 ? 0.19586 0.34298 0.32858 -0.04891 -0.00570 0.01533  252 LYS A CA    
1183 C C     . LYS A 188 ? 0.19508 0.33310 0.32599 -0.05589 0.00074  0.01898  252 LYS A C     
1184 O O     . LYS A 188 ? 0.19951 0.32749 0.31963 -0.05317 0.00395  0.02449  252 LYS A O     
1185 C CB    . LYS A 188 ? 0.20422 0.37164 0.34530 -0.04396 -0.00644 0.01353  252 LYS A CB    
1186 C CG    . LYS A 188 ? 0.17164 0.34530 0.31025 -0.03518 -0.01280 0.01122  252 LYS A CG    
1187 C CD    . LYS A 188 ? 0.24056 0.43416 0.39125 -0.03361 -0.01654 0.00712  252 LYS A CD    
1188 C CE    . LYS A 188 ? 0.24469 0.44602 0.38989 -0.02158 -0.01752 0.00852  252 LYS A CE    
1189 N NZ    . LYS A 188 ? 0.31048 0.52284 0.45939 -0.01745 -0.02531 0.00432  252 LYS A NZ    
1190 N N     . GLU A 189 ? 0.32843 0.46971 0.46990 -0.06498 0.00233  0.01601  253 GLU A N     
1191 C CA    . GLU A 189 ? 0.33960 0.47155 0.47920 -0.07222 0.00872  0.01935  253 GLU A CA    
1192 C C     . GLU A 189 ? 0.30940 0.44696 0.44553 -0.06883 0.01396  0.02364  253 GLU A C     
1193 O O     . GLU A 189 ? 0.37537 0.49996 0.50169 -0.07068 0.01830  0.02840  253 GLU A O     
1194 C CB    . GLU A 189 ? 0.33608 0.47400 0.49022 -0.08219 0.00984  0.01557  253 GLU A CB    
1195 N N     . GLU A 190 ? 0.29051 0.44698 0.43403 -0.06344 0.01342  0.02190  254 GLU A N     
1196 C CA    . GLU A 190 ? 0.26473 0.42796 0.40589 -0.06001 0.01887  0.02508  254 GLU A CA    
1197 C C     . GLU A 190 ? 0.25050 0.40493 0.37647 -0.05105 0.01824  0.02934  254 GLU A C     
1198 O O     . GLU A 190 ? 0.29022 0.44587 0.41118 -0.04860 0.02303  0.03242  254 GLU A O     
1199 C CB    . GLU A 190 ? 0.24594 0.43328 0.40169 -0.05701 0.01859  0.02136  254 GLU A CB    
1200 C CG    . GLU A 190 ? 0.34260 0.53771 0.49920 -0.04820 0.01118  0.01834  254 GLU A CG    
1201 C CD    . GLU A 190 ? 0.41006 0.61815 0.58157 -0.05179 0.00581  0.01287  254 GLU A CD    
1202 O OE1   . GLU A 190 ? 0.36947 0.56943 0.54422 -0.06044 0.00441  0.01128  254 GLU A OE1   
1203 O OE2   . GLU A 190 ? 0.35866 0.58439 0.53794 -0.04567 0.00263  0.01028  254 GLU A OE2   
1204 N N     . ALA A 191 ? 0.15686 0.30258 0.27583 -0.04634 0.01276  0.02955  255 ALA A N     
1205 C CA    . ALA A 191 ? 0.15543 0.29162 0.26095 -0.03847 0.01195  0.03400  255 ALA A CA    
1206 C C     . ALA A 191 ? 0.19553 0.31036 0.28969 -0.04133 0.01210  0.03830  255 ALA A C     
1207 O O     . ALA A 191 ? 0.14901 0.25384 0.23390 -0.03578 0.00959  0.04116  255 ALA A O     
1208 C CB    . ALA A 191 ? 0.12280 0.26248 0.22751 -0.03088 0.00639  0.03200  255 ALA A CB    
1209 N N     . SER A 192 ? 0.16149 0.26915 0.25645 -0.04948 0.01497  0.03870  256 SER A N     
1210 C CA    . SER A 192 ? 0.18967 0.27707 0.27410 -0.05145 0.01452  0.04225  256 SER A CA    
1211 C C     . SER A 192 ? 0.16545 0.24468 0.23770 -0.04565 0.01511  0.04672  256 SER A C     
1212 O O     . SER A 192 ? 0.18694 0.25150 0.25090 -0.04350 0.01227  0.04879  256 SER A O     
1213 C CB    . SER A 192 ? 0.15541 0.23747 0.24185 -0.06061 0.01877  0.04235  256 SER A CB    
1214 N N     . ASP A 193 ? 0.38706 0.47610 0.45880 -0.04293 0.01876  0.04751  257 ASP A N     
1215 C CA    . ASP A 193 ? 0.35492 0.43584 0.41495 -0.03872 0.02008  0.05079  257 ASP A CA    
1216 C C     . ASP A 193 ? 0.33814 0.41263 0.39218 -0.03126 0.01533  0.05177  257 ASP A C     
1217 O O     . ASP A 193 ? 0.35905 0.42229 0.40338 -0.02876 0.01466  0.05320  257 ASP A O     
1218 C CB    . ASP A 193 ? 0.41702 0.51109 0.47875 -0.03699 0.02557  0.05061  257 ASP A CB    
1219 C CG    . ASP A 193 ? 0.43000 0.52078 0.48862 -0.04323 0.03171  0.05169  257 ASP A CG    
1220 O OD1   . ASP A 193 ? 0.43492 0.53940 0.50307 -0.04700 0.03670  0.04982  257 ASP A OD1   
1221 O OD2   . ASP A 193 ? 0.43616 0.51088 0.48323 -0.04431 0.03163  0.05409  257 ASP A OD2   
1222 N N     . TYR A 194 ? 0.19227 0.27375 0.25200 -0.02790 0.01227  0.05033  258 TYR A N     
1223 C CA    . TYR A 194 ? 0.17547 0.25104 0.22983 -0.02129 0.00886  0.05145  258 TYR A CA    
1224 C C     . TYR A 194 ? 0.16586 0.22654 0.21675 -0.02237 0.00508  0.05137  258 TYR A C     
1225 O O     . TYR A 194 ? 0.18155 0.23663 0.22870 -0.01763 0.00264  0.05141  258 TYR A O     
1226 C CB    . TYR A 194 ? 0.14082 0.22850 0.20124 -0.01730 0.00745  0.04978  258 TYR A CB    
1227 C CG    . TYR A 194 ? 0.15108 0.25406 0.21433 -0.01339 0.01083  0.04904  258 TYR A CG    
1228 C CD1   . TYR A 194 ? 0.18033 0.28184 0.23577 -0.00775 0.01369  0.05159  258 TYR A CD1   
1229 C CD2   . TYR A 194 ? 0.21118 0.32995 0.28544 -0.01506 0.01114  0.04482  258 TYR A CD2   
1230 C CE1   . TYR A 194 ? 0.25587 0.37091 0.31364 -0.00294 0.01726  0.05049  258 TYR A CE1   
1231 C CE2   . TYR A 194 ? 0.21359 0.34713 0.29155 -0.01028 0.01399  0.04331  258 TYR A CE2   
1232 C CZ    . TYR A 194 ? 0.28371 0.41513 0.35307 -0.00387 0.01729  0.04632  258 TYR A CZ    
1233 O OH    . TYR A 194 ? 0.26914 0.41438 0.34186 0.00200  0.02041  0.04441  258 TYR A OH    
1234 N N     . LEU A 195 ? 0.16981 0.22457 0.22232 -0.02818 0.00500  0.05079  259 LEU A N     
1235 C CA    . LEU A 195 ? 0.17509 0.21654 0.22410 -0.02824 0.00202  0.05065  259 LEU A CA    
1236 C C     . LEU A 195 ? 0.17993 0.21279 0.22027 -0.02766 0.00281  0.05165  259 LEU A C     
1237 O O     . LEU A 195 ? 0.20217 0.22657 0.24046 -0.02706 0.00005  0.05193  259 LEU A O     
1238 C CB    . LEU A 195 ? 0.22085 0.25909 0.27505 -0.03436 0.00184  0.04964  259 LEU A CB    
1239 C CG    . LEU A 195 ? 0.17759 0.22410 0.24091 -0.03645 0.00090  0.04673  259 LEU A CG    
1240 C CD1   . LEU A 195 ? 0.19104 0.23337 0.25901 -0.04396 0.00156  0.04485  259 LEU A CD1   
1241 C CD2   . LEU A 195 ? 0.15328 0.19728 0.21664 -0.03132 -0.00262 0.04587  259 LEU A CD2   
1242 N N     . GLU A 196 ? 0.23668 0.27304 0.27291 -0.02794 0.00639  0.05259  260 GLU A N     
1243 C CA    . GLU A 196 ? 0.23995 0.26935 0.26801 -0.02855 0.00734  0.05437  260 GLU A CA    
1244 C C     . GLU A 196 ? 0.19218 0.22029 0.21543 -0.02324 0.00582  0.05343  260 GLU A C     
1245 O O     . GLU A 196 ? 0.17722 0.21051 0.20064 -0.01957 0.00710  0.05174  260 GLU A O     
1246 C CB    . GLU A 196 ? 0.22427 0.25706 0.24974 -0.03259 0.01323  0.05559  260 GLU A CB    
1247 C CG    . GLU A 196 ? 0.26014 0.29405 0.29095 -0.03949 0.01596  0.05601  260 GLU A CG    
1248 C CD    . GLU A 196 ? 0.29636 0.31862 0.32505 -0.04241 0.01310  0.05834  260 GLU A CD    
1249 O OE1   . GLU A 196 ? 0.29384 0.30808 0.31517 -0.04074 0.01096  0.06072  260 GLU A OE1   
1250 O OE2   . GLU A 196 ? 0.31925 0.34028 0.35380 -0.04643 0.01300  0.05751  260 GLU A OE2   
1251 N N     . LEU A 197 ? 0.25985 0.24770 0.15263 0.00078  0.01824  -0.00248 261 LEU A N     
1252 C CA    . LEU A 197 ? 0.27030 0.26408 0.16707 0.00288  0.01354  -0.00626 261 LEU A CA    
1253 C C     . LEU A 197 ? 0.25610 0.25757 0.15587 0.00080  0.01227  -0.01163 261 LEU A C     
1254 O O     . LEU A 197 ? 0.29016 0.28912 0.19403 0.00021  0.00939  -0.01471 261 LEU A O     
1255 C CB    . LEU A 197 ? 0.35774 0.33971 0.24221 0.01135  0.01112  -0.00425 261 LEU A CB    
1256 C CG    . LEU A 197 ? 0.39564 0.37811 0.28181 0.02050  0.00675  -0.00379 261 LEU A CG    
1257 C CD1   . LEU A 197 ? 0.37787 0.36074 0.27222 0.01579  0.01092  -0.00328 261 LEU A CD1   
1258 C CD2   . LEU A 197 ? 0.33896 0.31138 0.21112 0.03387  0.00572  0.00133  261 LEU A CD2   
1259 N N     . ASP A 198 ? 0.26886 0.27140 0.16199 0.00121  0.01533  -0.01256 262 ASP A N     
1260 C CA    . ASP A 198 ? 0.22709 0.23180 0.12094 0.00004  0.01675  -0.01846 262 ASP A CA    
1261 C C     . ASP A 198 ? 0.24752 0.24537 0.14521 0.00911  0.01923  -0.01639 262 ASP A C     
1262 O O     . ASP A 198 ? 0.25231 0.25178 0.15260 0.00454  0.02026  -0.02329 262 ASP A O     
1263 C CB    . ASP A 198 ? 0.36702 0.37236 0.24914 0.00215  0.02123  -0.01937 262 ASP A CB    
1264 C CG    . ASP A 198 ? 0.37293 0.37681 0.25027 0.00275  0.02689  -0.01314 262 ASP A CG    
1265 O OD1   . ASP A 198 ? 0.36611 0.36584 0.24776 0.00115  0.02644  -0.00813 262 ASP A OD1   
1266 O OD2   . ASP A 198 ? 0.38981 0.39040 0.25699 0.00275  0.03285  -0.01329 262 ASP A OD2   
1267 N N     . THR A 199 ? 0.23953 0.24332 0.14021 0.00263  0.02337  -0.01212 263 THR A N     
1268 C CA    . THR A 199 ? 0.26556 0.27898 0.17839 -0.00818 0.02679  -0.01289 263 THR A CA    
1269 C C     . THR A 199 ? 0.25215 0.27375 0.17589 -0.01052 0.01942  -0.01466 263 THR A C     
1270 O O     . THR A 199 ? 0.27109 0.30670 0.21330 -0.00953 0.01751  -0.01813 263 THR A O     
1271 C CB    . THR A 199 ? 0.29902 0.31186 0.21220 -0.01885 0.02996  -0.00685 263 THR A CB    
1272 O OG1   . THR A 199 ? 0.37584 0.38814 0.28359 -0.01945 0.03836  -0.00630 263 THR A OG1   
1273 C CG2   . THR A 199 ? 0.30387 0.33644 0.23243 -0.03167 0.02912  -0.00520 263 THR A CG2   
1274 N N     . ILE A 200 ? 0.26682 0.27757 0.18704 -0.00962 0.01451  -0.01086 264 ILE A N     
1275 C CA    . ILE A 200 ? 0.22514 0.24163 0.15394 -0.01317 0.00853  -0.01124 264 ILE A CA    
1276 C C     . ILE A 200 ? 0.26025 0.28376 0.19714 -0.00598 0.00359  -0.01817 264 ILE A C     
1277 O O     . ILE A 200 ? 0.23835 0.26769 0.19335 -0.00697 -0.00156 -0.01873 264 ILE A O     
1278 C CB    . ILE A 200 ? 0.26297 0.26623 0.18677 -0.01288 0.00838  -0.00656 264 ILE A CB    
1279 C CG1   . ILE A 200 ? 0.30860 0.30545 0.22979 -0.02235 0.01056  -0.00182 264 ILE A CG1   
1280 C CG2   . ILE A 200 ? 0.29602 0.30215 0.22555 -0.01572 0.00413  -0.00709 264 ILE A CG2   
1281 C CD1   . ILE A 200 ? 0.30771 0.31303 0.23487 -0.03529 0.00579  0.00089  264 ILE A CD1   
1282 N N     . LYS A 201 ? 0.22254 0.23900 0.15026 0.00117  0.00350  -0.02096 265 LYS A N     
1283 C CA    . LYS A 201 ? 0.25229 0.27439 0.18650 0.00602  -0.00288 -0.02812 265 LYS A CA    
1284 C C     . LYS A 201 ? 0.26841 0.29558 0.21073 0.00750  -0.00117 -0.03505 265 LYS A C     
1285 O O     . LYS A 201 ? 0.23998 0.26870 0.19640 0.00797  -0.00616 -0.03903 265 LYS A O     
1286 C CB    . LYS A 201 ? 0.27323 0.28758 0.19572 0.00993  -0.00491 -0.02764 265 LYS A CB    
1287 C CG    . LYS A 201 ? 0.27107 0.28957 0.19648 0.01306  -0.01078 -0.02535 265 LYS A CG    
1288 C CD    . LYS A 201 ? 0.25589 0.27012 0.16840 0.01827  -0.01344 -0.02328 265 LYS A CD    
1289 C CE    . LYS A 201 ? 0.27103 0.28956 0.18383 0.02535  -0.01622 -0.01882 265 LYS A CE    
1290 N NZ    . LYS A 201 ? 0.29167 0.31442 0.19837 0.03317  -0.02601 -0.01822 265 LYS A NZ    
1291 N N     . ASN A 202 ? 0.32714 0.35412 0.26284 0.00801  0.00763  -0.03551 266 ASN A N     
1292 C CA    . ASN A 202 ? 0.28488 0.31554 0.23345 0.01098  0.01275  -0.04066 266 ASN A CA    
1293 C C     . ASN A 202 ? 0.30575 0.34567 0.28257 0.00866  0.00973  -0.03576 266 ASN A C     
1294 O O     . ASN A 202 ? 0.29865 0.33805 0.29009 0.01304  0.00905  -0.03990 266 ASN A O     
1295 C CB    . ASN A 202 ? 0.31273 0.34425 0.25204 0.01142  0.02560  -0.04102 266 ASN A CB    
1296 C CG    . ASN A 202 ? 0.33344 0.34607 0.24576 0.01350  0.02788  -0.04315 266 ASN A CG    
1297 O OD1   . ASN A 202 ? 0.36589 0.36952 0.27079 0.01523  0.02172  -0.04829 266 ASN A OD1   
1298 N ND2   . ASN A 202 ? 0.32581 0.32961 0.22386 0.01149  0.03585  -0.03757 266 ASN A ND2   
1299 N N     . LEU A 203 ? 0.26860 0.31411 0.25051 0.00153  0.00762  -0.02664 267 LEU A N     
1300 C CA    . LEU A 203 ? 0.23086 0.28419 0.23561 -0.00190 0.00194  -0.02003 267 LEU A CA    
1301 C C     . LEU A 203 ? 0.28280 0.32912 0.29255 -0.00151 -0.00658 -0.02080 267 LEU A C     
1302 O O     . LEU A 203 ? 0.25175 0.29951 0.27993 0.00069  -0.01025 -0.01906 267 LEU A O     
1303 C CB    . LEU A 203 ? 0.24525 0.30182 0.24607 -0.01251 -0.00003 -0.01079 267 LEU A CB    
1304 C CG    . LEU A 203 ? 0.33515 0.40660 0.34955 -0.01700 0.00387  -0.00557 267 LEU A CG    
1305 C CD1   . LEU A 203 ? 0.30063 0.37195 0.30945 -0.03068 -0.00256 0.00346  267 LEU A CD1   
1306 C CD2   . LEU A 203 ? 0.31983 0.40514 0.36569 -0.00978 0.00270  -0.00463 267 LEU A CD2   
1307 N N     . VAL A 204 ? 0.22495 0.26382 0.22011 -0.00356 -0.00923 -0.02238 268 VAL A N     
1308 C CA    . VAL A 204 ? 0.24279 0.27679 0.24417 -0.00544 -0.01560 -0.02255 268 VAL A CA    
1309 C C     . VAL A 204 ? 0.31280 0.34285 0.32226 -0.00011 -0.01729 -0.03077 268 VAL A C     
1310 O O     . VAL A 204 ? 0.37267 0.39785 0.39439 -0.00129 -0.02125 -0.02954 268 VAL A O     
1311 C CB    . VAL A 204 ? 0.25592 0.28696 0.24508 -0.00774 -0.01597 -0.02234 268 VAL A CB    
1312 C CG1   . VAL A 204 ? 0.27374 0.30266 0.27260 -0.01053 -0.02063 -0.02330 268 VAL A CG1   
1313 C CG2   . VAL A 204 ? 0.23511 0.26291 0.21353 -0.01396 -0.01283 -0.01458 268 VAL A CG2   
1314 N N     . LYS A 205 ? 0.39812 0.42632 0.39701 0.00503  -0.01411 -0.03924 269 LYS A N     
1315 C CA    . LYS A 205 ? 0.39828 0.41764 0.39871 0.00860  -0.01494 -0.04876 269 LYS A CA    
1316 C C     . LYS A 205 ? 0.43852 0.45536 0.45521 0.01361  -0.01031 -0.04807 269 LYS A C     
1317 O O     . LYS A 205 ? 0.51205 0.51808 0.53708 0.01475  -0.01264 -0.05122 269 LYS A O     
1318 C CB    . LYS A 205 ? 0.46054 0.47557 0.43985 0.01207  -0.01217 -0.05769 269 LYS A CB    
1319 C CG    . LYS A 205 ? 0.51530 0.51883 0.48668 0.01098  -0.01770 -0.06840 269 LYS A CG    
1320 C CD    . LYS A 205 ? 0.52630 0.53242 0.47933 0.00885  -0.02470 -0.07033 269 LYS A CD    
1321 C CE    . LYS A 205 ? 0.54517 0.54467 0.49712 0.00272  -0.03359 -0.07487 269 LYS A CE    
1322 N NZ    . LYS A 205 ? 0.43949 0.45161 0.39511 -0.00108 -0.04234 -0.06802 269 LYS A NZ    
1323 N N     . LYS A 206 ? 0.25885 0.28580 0.28210 0.01666  -0.00355 -0.04323 270 LYS A N     
1324 C CA    . LYS A 206 ? 0.35762 0.38749 0.40277 0.02358  0.00126  -0.04101 270 LYS A CA    
1325 C C     . LYS A 206 ? 0.41042 0.44077 0.47408 0.02118  -0.00788 -0.03097 270 LYS A C     
1326 O O     . LYS A 206 ? 0.40110 0.42417 0.48028 0.02794  -0.00764 -0.03076 270 LYS A O     
1327 C CB    . LYS A 206 ? 0.33881 0.38498 0.39100 0.02537  0.01011  -0.03684 270 LYS A CB    
1328 C CG    . LYS A 206 ? 0.30139 0.36393 0.38374 0.02644  0.00783  -0.02527 270 LYS A CG    
1329 C CD    . LYS A 206 ? 0.32423 0.40337 0.42070 0.03116  0.02062  -0.02493 270 LYS A CD    
1330 C CE    . LYS A 206 ? 0.45097 0.55410 0.57448 0.02620  0.01473  -0.01091 270 LYS A CE    
1331 N NZ    . LYS A 206 ? 0.39122 0.51581 0.53540 0.02951  0.02789  -0.00965 270 LYS A NZ    
1332 N N     . TYR A 207 ? 0.62262 0.65792 0.68181 0.01182  -0.01531 -0.02241 271 TYR A N     
1333 C CA    . TYR A 207 ? 0.58970 0.62296 0.65955 0.00756  -0.02430 -0.01180 271 TYR A CA    
1334 C C     . TYR A 207 ? 0.65861 0.67679 0.71869 0.00164  -0.02926 -0.01354 271 TYR A C     
1335 O O     . TYR A 207 ? 0.66365 0.67830 0.72154 -0.00597 -0.03534 -0.00464 271 TYR A O     
1336 C CB    . TYR A 207 ? 0.61601 0.66103 0.68380 -0.00102 -0.02852 -0.00105 271 TYR A CB    
1337 C CG    . TYR A 207 ? 0.64892 0.71221 0.73667 0.00263  -0.02695 0.00461  271 TYR A CG    
1338 C CD1   . TYR A 207 ? 0.65143 0.71944 0.76504 0.01412  -0.02529 0.00563  271 TYR A CD1   
1339 C CD2   . TYR A 207 ? 0.63646 0.71224 0.71890 -0.00543 -0.02610 0.00896  271 TYR A CD2   
1340 C CE1   . TYR A 207 ? 0.64709 0.73699 0.78575 0.01827  -0.02287 0.01160  271 TYR A CE1   
1341 C CE2   . TYR A 207 ? 0.60863 0.70518 0.71362 -0.00407 -0.02470 0.01453  271 TYR A CE2   
1342 C CZ    . TYR A 207 ? 0.66378 0.77000 0.79937 0.00821  -0.02305 0.01617  271 TYR A CZ    
1343 O OH    . TYR A 207 ? 0.68848 0.82046 0.85301 0.01033  -0.02065 0.02249  271 TYR A OH    
1344 N N     . SER A 208 ? 0.52702 0.53567 0.58052 0.00365  -0.02675 -0.02472 272 SER A N     
1345 C CA    . SER A 208 ? 0.53286 0.52922 0.58332 -0.00311 -0.03130 -0.02597 272 SER A CA    
1346 C C     . SER A 208 ? 0.54837 0.52941 0.61061 0.00005  -0.03371 -0.02272 272 SER A C     
1347 O O     . SER A 208 ? 0.56386 0.52858 0.62483 -0.00059 -0.03368 -0.03000 272 SER A O     
1348 C CB    . SER A 208 ? 0.53814 0.53133 0.57881 -0.00457 -0.03060 -0.03826 272 SER A CB    
1349 O OG    . SER A 208 ? 0.54729 0.52933 0.59023 -0.01212 -0.03472 -0.03994 272 SER A OG    
1350 N N     . GLN A 209 ? 0.87387 0.85920 0.94702 0.00288  -0.03680 -0.01097 273 GLN A N     
1351 C CA    . GLN A 209 ? 0.89064 0.86143 0.97552 0.00701  -0.04101 -0.00368 273 GLN A CA    
1352 C C     . GLN A 209 ? 0.89818 0.85457 0.97332 -0.00459 -0.04685 0.00317  273 GLN A C     
1353 O O     . GLN A 209 ? 0.91585 0.85146 0.98973 -0.00624 -0.04686 0.00035  273 GLN A O     
1354 C CB    . GLN A 209 ? 0.88809 0.87317 0.99036 0.01385  -0.04487 0.00852  273 GLN A CB    
1355 N N     . PHE A 210 ? 0.55269 0.51732 0.61831 -0.01382 -0.05042 0.01179  274 PHE A N     
1356 C CA    . PHE A 210 ? 0.56297 0.51356 0.61573 -0.02585 -0.05323 0.01880  274 PHE A CA    
1357 C C     . PHE A 210 ? 0.55327 0.50832 0.59528 -0.03479 -0.04671 0.01083  274 PHE A C     
1358 O O     . PHE A 210 ? 0.54776 0.50802 0.57754 -0.04214 -0.04474 0.01487  274 PHE A O     
1359 C CB    . PHE A 210 ? 0.56738 0.51972 0.61231 -0.03117 -0.06067 0.03356  274 PHE A CB    
1360 N N     . ILE A 211 ? 0.60485 0.55775 0.65179 -0.03395 -0.04337 -0.00072 275 ILE A N     
1361 C CA    . ILE A 211 ? 0.58164 0.54021 0.62456 -0.04310 -0.03915 -0.00561 275 ILE A CA    
1362 C C     . ILE A 211 ? 0.53002 0.47979 0.57945 -0.04761 -0.03928 -0.01450 275 ILE A C     
1363 O O     . ILE A 211 ? 0.54652 0.49824 0.59910 -0.04236 -0.04040 -0.02522 275 ILE A O     
1364 C CB    . ILE A 211 ? 0.44987 0.42873 0.49022 -0.03907 -0.03601 -0.01110 275 ILE A CB    
1365 N N     . ASN A 212 ? 0.44220 0.38142 0.49115 -0.05931 -0.03761 -0.01045 276 ASN A N     
1366 C CA    . ASN A 212 ? 0.37131 0.31202 0.42563 -0.06706 -0.03489 -0.01845 276 ASN A CA    
1367 C C     . ASN A 212 ? 0.40992 0.37079 0.46844 -0.07408 -0.02820 -0.01765 276 ASN A C     
1368 O O     . ASN A 212 ? 0.45381 0.41948 0.51972 -0.08278 -0.02477 -0.02151 276 ASN A O     
1369 C CB    . ASN A 212 ? 0.49772 0.41371 0.54871 -0.07310 -0.03340 -0.01565 276 ASN A CB    
1370 C CG    . ASN A 212 ? 0.52099 0.41660 0.57195 -0.06683 -0.03813 -0.02247 276 ASN A CG    
1371 O OD1   . ASN A 212 ? 0.43994 0.34195 0.49293 -0.06135 -0.04076 -0.03335 276 ASN A OD1   
1372 N ND2   . ASN A 212 ? 0.49247 0.36108 0.53876 -0.06671 -0.03797 -0.01623 276 ASN A ND2   
1373 N N     . PHE A 213 ? 0.26474 0.23627 0.31945 -0.07110 -0.02578 -0.01249 277 PHE A N     
1374 C CA    . PHE A 213 ? 0.24366 0.23482 0.30521 -0.07401 -0.01961 -0.01262 277 PHE A CA    
1375 C C     . PHE A 213 ? 0.16434 0.17345 0.22767 -0.06344 -0.02322 -0.01834 277 PHE A C     
1376 O O     . PHE A 213 ? 0.12636 0.13101 0.18026 -0.05474 -0.02724 -0.01927 277 PHE A O     
1377 C CB    . PHE A 213 ? 0.18050 0.16492 0.22797 -0.07709 -0.01036 -0.00265 277 PHE A CB    
1378 C CG    . PHE A 213 ? 0.16291 0.12740 0.20205 -0.08271 -0.00670 0.00414  277 PHE A CG    
1379 C CD1   . PHE A 213 ? 0.22438 0.19038 0.27369 -0.09033 0.00100  0.00502  277 PHE A CD1   
1380 C CD2   . PHE A 213 ? 0.17819 0.12405 0.20154 -0.08030 -0.01238 0.01069  277 PHE A CD2   
1381 C CE1   . PHE A 213 ? 0.25824 0.20473 0.29799 -0.09565 0.00432  0.01161  277 PHE A CE1   
1382 C CE2   . PHE A 213 ? 0.19399 0.12127 0.20771 -0.08504 -0.01047 0.01775  277 PHE A CE2   
1383 C CZ    . PHE A 213 ? 0.22029 0.14654 0.24037 -0.09279 -0.00137 0.01774  277 PHE A CZ    
1384 N N     . PRO A 214 ? 0.19813 0.22837 0.27437 -0.06299 -0.02136 -0.02163 278 PRO A N     
1385 C CA    . PRO A 214 ? 0.18885 0.23349 0.26339 -0.05185 -0.02510 -0.02579 278 PRO A CA    
1386 C C     . PRO A 214 ? 0.22544 0.26478 0.28213 -0.04415 -0.01955 -0.02053 278 PRO A C     
1387 O O     . PRO A 214 ? 0.18021 0.21243 0.22876 -0.04753 -0.01079 -0.01373 278 PRO A O     
1388 C CB    . PRO A 214 ? 0.22735 0.29606 0.32243 -0.05317 -0.02361 -0.02657 278 PRO A CB    
1389 C CG    . PRO A 214 ? 0.17736 0.24421 0.28201 -0.06385 -0.01324 -0.02110 278 PRO A CG    
1390 C CD    . PRO A 214 ? 0.20270 0.24603 0.29813 -0.07240 -0.01623 -0.02092 278 PRO A CD    
1391 N N     . ILE A 215 ? 0.22185 0.26263 0.26971 -0.03530 -0.02414 -0.02408 279 ILE A N     
1392 C CA    . ILE A 215 ? 0.20527 0.24238 0.23684 -0.02936 -0.01944 -0.01999 279 ILE A CA    
1393 C C     . ILE A 215 ? 0.24568 0.29468 0.27555 -0.02052 -0.02013 -0.02276 279 ILE A C     
1394 O O     . ILE A 215 ? 0.22556 0.28020 0.25708 -0.01678 -0.02780 -0.02896 279 ILE A O     
1395 C CB    . ILE A 215 ? 0.20616 0.23310 0.22839 -0.02745 -0.02267 -0.01958 279 ILE A CB    
1396 C CG1   . ILE A 215 ? 0.28121 0.29614 0.30751 -0.03420 -0.02487 -0.01576 279 ILE A CG1   
1397 C CG2   . ILE A 215 ? 0.20636 0.23018 0.21285 -0.02535 -0.01795 -0.01463 279 ILE A CG2   
1398 C CD1   . ILE A 215 ? 0.34043 0.34827 0.36044 -0.03273 -0.02702 -0.01034 279 ILE A CD1   
1399 N N     . TYR A 216 ? 0.15322 0.20254 0.17659 -0.01722 -0.01190 -0.01796 280 TYR A N     
1400 C CA    . TYR A 216 ? 0.14467 0.20195 0.16520 -0.00730 -0.01156 -0.01802 280 TYR A CA    
1401 C C     . TYR A 216 ? 0.15326 0.19640 0.14985 -0.00366 -0.00560 -0.01491 280 TYR A C     
1402 O O     . TYR A 216 ? 0.16039 0.19009 0.14485 -0.00950 0.00129  -0.01111 280 TYR A O     
1403 C CB    . TYR A 216 ? 0.15969 0.22826 0.19559 -0.00445 -0.00475 -0.01453 280 TYR A CB    
1404 C CG    . TYR A 216 ? 0.14688 0.23342 0.21039 -0.00998 -0.01008 -0.01691 280 TYR A CG    
1405 C CD1   . TYR A 216 ? 0.19266 0.27422 0.26328 -0.02138 -0.00562 -0.01623 280 TYR A CD1   
1406 C CD2   . TYR A 216 ? 0.13748 0.24520 0.21873 -0.00524 -0.02031 -0.01909 280 TYR A CD2   
1407 C CE1   . TYR A 216 ? 0.21842 0.31498 0.31404 -0.02884 -0.00952 -0.01835 280 TYR A CE1   
1408 C CE2   . TYR A 216 ? 0.22048 0.34625 0.32858 -0.01323 -0.02636 -0.02143 280 TYR A CE2   
1409 C CZ    . TYR A 216 ? 0.21799 0.33787 0.33381 -0.02544 -0.01995 -0.02134 280 TYR A CZ    
1410 O OH    . TYR A 216 ? 0.19567 0.33203 0.33797 -0.03573 -0.02491 -0.02359 280 TYR A OH    
1411 N N     . VAL A 217 ? 0.16623 0.21106 0.15383 0.00464  -0.00874 -0.01616 281 VAL A N     
1412 C CA    . VAL A 217 ? 0.18318 0.21408 0.14782 0.00805  -0.00223 -0.01291 281 VAL A CA    
1413 C C     . VAL A 217 ? 0.21242 0.24506 0.17561 0.01893  0.00077  -0.00952 281 VAL A C     
1414 O O     . VAL A 217 ? 0.20626 0.25281 0.17964 0.02582  -0.00813 -0.01079 281 VAL A O     
1415 C CB    . VAL A 217 ? 0.19948 0.22710 0.15169 0.00838  -0.00644 -0.01613 281 VAL A CB    
1416 C CG1   . VAL A 217 ? 0.19359 0.20697 0.12219 0.01070  0.00071  -0.01241 281 VAL A CG1   
1417 C CG2   . VAL A 217 ? 0.17244 0.19924 0.13044 0.00008  -0.00794 -0.01778 281 VAL A CG2   
1418 N N     . TRP A 218 ? 0.20557 0.22284 0.15551 0.02046  0.01277  -0.00494 282 TRP A N     
1419 C CA    . TRP A 218 ? 0.19726 0.21139 0.14394 0.03339  0.01761  -0.00056 282 TRP A CA    
1420 C C     . TRP A 218 ? 0.24840 0.25767 0.17793 0.03980  0.01095  -0.00001 282 TRP A C     
1421 O O     . TRP A 218 ? 0.22350 0.21538 0.12906 0.03467  0.01474  -0.00013 282 TRP A O     
1422 C CB    . TRP A 218 ? 0.22722 0.21716 0.15533 0.03311  0.03404  0.00300  282 TRP A CB    
1423 C CG    . TRP A 218 ? 0.26723 0.25175 0.19491 0.04869  0.04129  0.00800  282 TRP A CG    
1424 C CD1   . TRP A 218 ? 0.27499 0.23414 0.17550 0.05517  0.04842  0.01160  282 TRP A CD1   
1425 C CD2   . TRP A 218 ? 0.28363 0.28858 0.24157 0.06060  0.04259  0.01098  282 TRP A CD2   
1426 N NE1   . TRP A 218 ? 0.29124 0.25167 0.20227 0.07249  0.05396  0.01706  282 TRP A NE1   
1427 C CE2   . TRP A 218 ? 0.35345 0.34462 0.30231 0.07643  0.05036  0.01699  282 TRP A CE2   
1428 C CE3   . TRP A 218 ? 0.30626 0.34048 0.29997 0.05901  0.03814  0.00967  282 TRP A CE3   
1429 C CZ2   . TRP A 218 ? 0.35039 0.35937 0.32861 0.09271  0.05352  0.02239  282 TRP A CZ2   
1430 C CZ3   . TRP A 218 ? 0.27670 0.33062 0.30017 0.07268  0.04132  0.01448  282 TRP A CZ3   
1431 C CH2   . TRP A 218 ? 0.31967 0.36250 0.33708 0.09032  0.04882  0.02107  282 TRP A CH2   
1432 N N     . SER A 219 ? 0.21047 0.23603 0.15208 0.04918  0.00014  0.00073  283 SER A N     
1433 C CA    . SER A 219 ? 0.21693 0.23783 0.13947 0.05439  -0.00818 0.00118  283 SER A CA    
1434 C C     . SER A 219 ? 0.24636 0.25658 0.15775 0.06886  -0.00517 0.00960  283 SER A C     
1435 O O     . SER A 219 ? 0.31840 0.34114 0.23711 0.07928  -0.01680 0.01336  283 SER A O     
1436 C CB    . SER A 219 ? 0.20631 0.24825 0.14281 0.05341  -0.02471 -0.00366 283 SER A CB    
1437 O OG    . SER A 219 ? 0.28871 0.32088 0.19932 0.05325  -0.03043 -0.00607 283 SER A OG    
1438 N N     . SER A 220 ? 0.36602 0.35133 0.25875 0.06906  0.00991  0.01295  284 SER A N     
1439 C CA    . SER A 220 ? 0.41436 0.38188 0.29356 0.08344  0.01628  0.02126  284 SER A CA    
1440 C C     . SER A 220 ? 0.48540 0.41836 0.33507 0.07688  0.03331  0.02183  284 SER A C     
1441 O O     . SER A 220 ? 0.53442 0.46619 0.39207 0.05891  0.03617  0.01572  284 SER A O     
1442 C CB    . SER A 220 ? 0.37550 0.35991 0.28581 0.09711  0.01778  0.02610  284 SER A CB    
1443 O OG    . SER A 220 ? 0.49975 0.47035 0.39989 0.11477  0.01966  0.03544  284 SER A OG    
1444 N N     . LYS A 221 ? 0.77104 0.67904 0.60137 0.08692  0.03962  0.02818  285 LYS A N     
1445 C CA    . LYS A 221 ? 0.78405 0.66181 0.60414 0.07541  0.05005  0.02564  285 LYS A CA    
1446 C C     . LYS A 221 ? 0.81422 0.66806 0.62355 0.09090  0.06606  0.03173  285 LYS A C     
1447 O O     . LYS A 221 ? 0.84067 0.68365 0.63690 0.11247  0.07003  0.04094  285 LYS A O     
1448 C CB    . LYS A 221 ? 0.79499 0.65888 0.60101 0.07050  0.04626  0.02535  285 LYS A CB    
1449 N N     . GLY A 226 ? 0.76074 0.69767 0.66933 0.14858  0.05459  0.04962  327 GLY A N     
1450 C CA    . GLY A 226 ? 0.73379 0.71823 0.68883 0.14882  0.04152  0.04831  327 GLY A CA    
1451 C C     . GLY A 226 ? 0.73541 0.73334 0.72371 0.15121  0.05587  0.04824  327 GLY A C     
1452 O O     . GLY A 226 ? 0.75064 0.72042 0.72150 0.14663  0.07665  0.04571  327 GLY A O     
1453 N N     . LYS A 227 ? 0.90842 0.94822 0.94270 0.15512  0.04390  0.05043  328 LYS A N     
1454 C CA    . LYS A 227 ? 0.91616 0.97065 0.98526 0.15945  0.05657  0.05159  328 LYS A CA    
1455 C C     . LYS A 227 ? 0.89155 0.98782 1.00486 0.15039  0.05014  0.04735  328 LYS A C     
1456 O O     . LYS A 227 ? 0.89835 1.00326 1.03573 0.15071  0.06466  0.04640  328 LYS A O     
1457 C CB    . LYS A 227 ? 0.94147 1.00202 1.02756 0.17728  0.05190  0.06074  328 LYS A CB    
1458 N N     . THR A 228 ? 0.77072 0.89073 0.89277 0.14101  0.02982  0.04429  329 THR A N     
1459 C CA    . THR A 228 ? 0.75315 0.91279 0.91835 0.13121  0.02065  0.04080  329 THR A CA    
1460 C C     . THR A 228 ? 0.72936 0.89193 0.88742 0.11348  0.02009  0.03304  329 THR A C     
1461 O O     . THR A 228 ? 0.72568 0.86210 0.84545 0.10731  0.02112  0.02916  329 THR A O     
1462 C CB    . THR A 228 ? 0.75422 0.94247 0.94250 0.13314  -0.00710 0.04386  329 THR A CB    
1463 O OG1   . THR A 228 ? 0.73841 0.95856 0.95996 0.11852  -0.01727 0.03800  329 THR A OG1   
1464 C CG2   . THR A 228 ? 0.75459 0.92700 0.90530 0.13157  -0.02428 0.04430  329 THR A CG2   
1465 N N     . VAL A 229 ? 0.40985 0.60136 0.60367 0.10216  0.01727  0.02944  330 VAL A N     
1466 C CA    . VAL A 229 ? 0.47388 0.67004 0.66625 0.08396  0.01628  0.02289  330 VAL A CA    
1467 C C     . VAL A 229 ? 0.43446 0.63613 0.61520 0.07432  -0.00958 0.01785  330 VAL A C     
1468 O O     . VAL A 229 ? 0.39433 0.58263 0.55764 0.05798  -0.01163 0.01009  330 VAL A O     
1469 C CB    . VAL A 229 ? 0.50572 0.72488 0.73532 0.07298  0.02304  0.02014  330 VAL A CB    
1470 N N     . TRP A 230 ? 1.09237 1.30393 1.27653 0.08156  -0.02881 0.02109  331 TRP A N     
1471 C CA    . TRP A 230 ? 1.06522 1.27240 1.22776 0.07259  -0.05048 0.01609  331 TRP A CA    
1472 C C     . TRP A 230 ? 1.05963 1.23638 1.17474 0.07768  -0.04863 0.01438  331 TRP A C     
1473 O O     . TRP A 230 ? 1.07837 1.24678 1.17006 0.07292  -0.06380 0.01067  331 TRP A O     
1474 C CB    . TRP A 230 ? 0.98058 1.20254 1.15909 0.07460  -0.07111 0.02108  331 TRP A CB    
1475 C CG    . TRP A 230 ? 0.98013 1.22962 1.20212 0.06374  -0.07888 0.01961  331 TRP A CG    
1476 C CD1   . TRP A 230 ? 0.98150 1.23619 1.20603 0.04529  -0.09384 0.01558  331 TRP A CD1   
1477 C CD2   . TRP A 230 ? 0.98316 1.25730 1.24835 0.07075  -0.07073 0.02023  331 TRP A CD2   
1478 N NE1   . TRP A 230 ? 0.98644 1.26373 1.25100 0.03990  -0.09556 0.01251  331 TRP A NE1   
1479 C CE2   . TRP A 230 ? 0.98566 1.28167 1.27545 0.05649  -0.08152 0.01226  331 TRP A CE2   
1480 C CE3   . TRP A 230 ? 0.98926 1.26723 1.26754 0.08753  -0.05255 0.02549  331 TRP A CE3   
1481 C CZ2   . TRP A 230 ? 0.99018 1.32262 1.31755 0.05897  -0.07458 0.00986  331 TRP A CZ2   
1482 C CZ3   . TRP A 230 ? 0.99550 1.30360 1.31395 0.08975  -0.04592 0.02440  331 TRP A CZ3   
1483 C CH2   . TRP A 230 ? 0.99406 1.33247 1.33829 0.07553  -0.05718 0.01721  331 TRP A CH2   
1484 N N     . ASP A 231 ? 0.35927 0.50928 0.45495 0.08233  -0.02791 0.01633  332 ASP A N     
1485 C CA    . ASP A 231 ? 0.33005 0.44478 0.38065 0.08141  -0.02284 0.01445  332 ASP A CA    
1486 C C     . ASP A 231 ? 0.27435 0.37394 0.30932 0.06435  -0.01718 0.00601  332 ASP A C     
1487 O O     . ASP A 231 ? 0.30114 0.37476 0.30393 0.06137  -0.01124 0.00454  332 ASP A O     
1488 C CB    . ASP A 231 ? 0.36899 0.46018 0.40442 0.09408  -0.00474 0.02126  332 ASP A CB    
1489 C CG    . ASP A 231 ? 0.41558 0.50748 0.44830 0.11287  -0.01218 0.03062  332 ASP A CG    
1490 O OD1   . ASP A 231 ? 0.44601 0.53675 0.46077 0.11322  -0.02892 0.03093  332 ASP A OD1   
1491 O OD2   . ASP A 231 ? 0.37681 0.46925 0.42476 0.12792  -0.00074 0.03810  332 ASP A OD2   
1492 N N     . TRP A 232 ? 0.29500 0.41047 0.35346 0.05310  -0.01872 0.00149  333 TRP A N     
1493 C CA    . TRP A 232 ? 0.22236 0.32520 0.26905 0.03827  -0.01667 -0.00521 333 TRP A CA    
1494 C C     . TRP A 232 ? 0.27570 0.38517 0.32003 0.03201  -0.03377 -0.01197 333 TRP A C     
1495 O O     . TRP A 232 ? 0.31363 0.44504 0.37958 0.03066  -0.04645 -0.01342 333 TRP A O     
1496 C CB    . TRP A 232 ? 0.24490 0.35514 0.31354 0.02903  -0.00765 -0.00572 333 TRP A CB    
1497 C CG    . TRP A 232 ? 0.29545 0.39152 0.35807 0.03183  0.01231  -0.00112 333 TRP A CG    
1498 C CD1   . TRP A 232 ? 0.31885 0.42672 0.40355 0.03964  0.02379  0.00360  333 TRP A CD1   
1499 C CD2   . TRP A 232 ? 0.25538 0.32163 0.28663 0.02617  0.02371  -0.00113 333 TRP A CD2   
1500 N NE1   . TRP A 232 ? 0.34443 0.42717 0.40889 0.03930  0.04343  0.00542  333 TRP A NE1   
1501 C CE2   . TRP A 232 ? 0.29114 0.34791 0.32137 0.02993  0.04217  0.00263  333 TRP A CE2   
1502 C CE3   . TRP A 232 ? 0.20495 0.25287 0.21034 0.01795  0.02000  -0.00377 333 TRP A CE3   
1503 C CZ2   . TRP A 232 ? 0.28715 0.31317 0.28569 0.02373  0.05546  0.00306  333 TRP A CZ2   
1504 C CZ3   . TRP A 232 ? 0.21516 0.23832 0.19522 0.01202  0.03126  -0.00206 333 TRP A CZ3   
1505 C CH2   . TRP A 232 ? 0.32696 0.33748 0.30084 0.01387  0.04812  0.00096  333 TRP A CH2   
1506 N N     . GLU A 233 ? 0.23981 0.33042 0.25834 0.02762  -0.03369 -0.01630 334 GLU A N     
1507 C CA    . GLU A 233 ? 0.24118 0.33232 0.25433 0.02142  -0.04557 -0.02421 334 GLU A CA    
1508 C C     . GLU A 233 ? 0.23539 0.32224 0.25750 0.00982  -0.04262 -0.02893 334 GLU A C     
1509 O O     . GLU A 233 ? 0.19326 0.26616 0.20614 0.00699  -0.03304 -0.02740 334 GLU A O     
1510 C CB    . GLU A 233 ? 0.23316 0.30726 0.21482 0.02505  -0.04556 -0.02613 334 GLU A CB    
1511 C CG    . GLU A 233 ? 0.27576 0.34803 0.24866 0.02148  -0.05648 -0.03282 334 GLU A CG    
1512 C CD    . GLU A 233 ? 0.26062 0.31203 0.20645 0.02139  -0.04967 -0.03441 334 GLU A CD    
1513 O OE1   . GLU A 233 ? 0.28414 0.32709 0.21441 0.02710  -0.04306 -0.02903 334 GLU A OE1   
1514 O OE2   . GLU A 233 ? 0.28740 0.33037 0.22836 0.01540  -0.04978 -0.04059 334 GLU A OE2   
1515 N N     . LEU A 234 ? 0.13656 0.23418 0.17547 0.00246  -0.05207 -0.03408 335 LEU A N     
1516 C CA    . LEU A 234 ? 0.13056 0.22006 0.17581 -0.00813 -0.05032 -0.03833 335 LEU A CA    
1517 C C     . LEU A 234 ? 0.13891 0.20936 0.16296 -0.00801 -0.05039 -0.04387 335 LEU A C     
1518 O O     . LEU A 234 ? 0.21168 0.27600 0.22230 -0.00657 -0.05542 -0.04733 335 LEU A O     
1519 C CB    . LEU A 234 ? 0.14118 0.23995 0.20522 -0.01717 -0.05786 -0.04017 335 LEU A CB    
1520 C CG    . LEU A 234 ? 0.14394 0.22722 0.20856 -0.02757 -0.05579 -0.04341 335 LEU A CG    
1521 C CD1   . LEU A 234 ? 0.20220 0.28546 0.27841 -0.03159 -0.04619 -0.03954 335 LEU A CD1   
1522 C CD2   . LEU A 234 ? 0.26120 0.34865 0.33577 -0.03775 -0.06337 -0.04513 335 LEU A CD2   
1523 N N     . MET A 235 ? 0.17666 0.23538 0.19730 -0.00968 -0.04258 -0.04221 336 MET A N     
1524 C CA    . MET A 235 ? 0.16403 0.20951 0.17004 -0.00692 -0.04033 -0.04607 336 MET A CA    
1525 C C     . MET A 235 ? 0.20026 0.23516 0.21081 -0.01150 -0.04326 -0.05312 336 MET A C     
1526 O O     . MET A 235 ? 0.21711 0.24185 0.21622 -0.00767 -0.04165 -0.05915 336 MET A O     
1527 C CB    . MET A 235 ? 0.19090 0.23100 0.19278 -0.00580 -0.03143 -0.03870 336 MET A CB    
1528 C CG    . MET A 235 ? 0.17364 0.21503 0.16167 -0.00086 -0.02624 -0.03361 336 MET A CG    
1529 S SD    . MET A 235 ? 0.21167 0.25590 0.18360 0.00702  -0.03049 -0.03712 336 MET A SD    
1530 C CE    . MET A 235 ? 0.17346 0.20721 0.13173 0.00830  -0.02725 -0.04332 336 MET A CE    
1531 N N     . ASN A 236 ? 0.19434 0.22855 0.21973 -0.01942 -0.04543 -0.05221 337 ASN A N     
1532 C CA    . ASN A 236 ? 0.24481 0.26305 0.27269 -0.02355 -0.04655 -0.05743 337 ASN A CA    
1533 C C     . ASN A 236 ? 0.29196 0.30927 0.32610 -0.03314 -0.05118 -0.05910 337 ASN A C     
1534 O O     . ASN A 236 ? 0.28136 0.28575 0.32130 -0.03960 -0.05053 -0.05962 337 ASN A O     
1535 C CB    . ASN A 236 ? 0.25137 0.26126 0.28639 -0.02446 -0.04140 -0.04955 337 ASN A CB    
1536 C CG    . ASN A 236 ? 0.18156 0.19812 0.22601 -0.03192 -0.03965 -0.04130 337 ASN A CG    
1537 O OD1   . ASN A 236 ? 0.18498 0.21640 0.23392 -0.03346 -0.03987 -0.04064 337 ASN A OD1   
1538 N ND2   . ASN A 236 ? 0.23485 0.23949 0.28213 -0.03621 -0.03742 -0.03459 337 ASN A ND2   
1539 O OXT   . ASN A 236 ? 0.22774 0.25702 0.26169 -0.03531 -0.05625 -0.05926 337 ASN A OXT   
1540 N N     . GLY B 1   ? 1.07284 0.84498 1.03385 0.20018  -0.04085 -0.14601 65  GLY B N     
1541 C CA    . GLY B 1   ? 1.06623 0.80560 1.05659 0.20954  -0.04576 -0.14337 65  GLY B CA    
1542 C C     . GLY B 1   ? 1.06633 0.80627 1.09780 0.21970  -0.05854 -0.12511 65  GLY B C     
1543 O O     . GLY B 1   ? 1.05859 0.77966 1.10786 0.20794  -0.05193 -0.10424 65  GLY B O     
1544 N N     . SER B 2   ? 1.07587 0.84342 1.12220 0.24149  -0.07563 -0.13316 66  SER B N     
1545 C CA    . SER B 2   ? 1.08194 0.85142 1.16662 0.25107  -0.09176 -0.11368 66  SER B CA    
1546 C C     . SER B 2   ? 1.09368 0.86200 1.15926 0.24951  -0.09507 -0.09946 66  SER B C     
1547 O O     . SER B 2   ? 1.09316 0.86686 1.11069 0.22094  -0.07346 -0.09647 66  SER B O     
1548 C CB    . SER B 2   ? 1.08281 0.89646 1.20700 0.26947  -0.10893 -0.12982 66  SER B CB    
1549 O OG    . SER B 2   ? 1.07959 0.93501 1.18978 0.28132  -0.10897 -0.16222 66  SER B OG    
1550 N N     . HIS B 3   ? 1.02759 0.80547 1.12842 0.26074  -0.11515 -0.08056 67  HIS B N     
1551 C CA    . HIS B 3   ? 1.05973 0.86570 1.13765 0.23890  -0.11139 -0.05749 67  HIS B CA    
1552 C C     . HIS B 3   ? 1.07363 0.93609 1.12494 0.22931  -0.10305 -0.07446 67  HIS B C     
1553 O O     . HIS B 3   ? 1.09526 0.97823 1.10786 0.20283  -0.08985 -0.06256 67  HIS B O     
1554 C CB    . HIS B 3   ? 1.07967 0.89109 1.20709 0.25314  -0.13905 -0.03172 67  HIS B CB    
1555 N N     . MET B 4   ? 0.99427 0.88516 1.06564 0.24954  -0.10996 -0.10375 68  MET B N     
1556 C CA    . MET B 4   ? 1.00703 0.95920 1.06387 0.24440  -0.10665 -0.11873 68  MET B CA    
1557 C C     . MET B 4   ? 1.00909 0.97117 1.00530 0.21317  -0.07966 -0.12391 68  MET B C     
1558 O O     . MET B 4   ? 1.02583 1.03070 0.99844 0.19719  -0.07371 -0.12230 68  MET B O     
1559 C CB    . MET B 4   ? 0.98996 0.97468 1.08689 0.27428  -0.12037 -0.15183 68  MET B CB    
1560 N N     . LEU B 5   ? 0.95460 0.87791 0.92913 0.20372  -0.06497 -0.12929 69  LEU B N     
1561 C CA    . LEU B 5   ? 0.95356 0.88245 0.87967 0.17386  -0.04260 -0.13316 69  LEU B CA    
1562 C C     . LEU B 5   ? 0.96844 0.87125 0.86346 0.14552  -0.02843 -0.11200 69  LEU B C     
1563 O O     . LEU B 5   ? 0.96959 0.87738 0.82960 0.11927  -0.01151 -0.11499 69  LEU B O     
1564 C CB    . LEU B 5   ? 0.89945 0.80216 0.82110 0.17503  -0.03539 -0.14826 69  LEU B CB    
1565 N N     . ARG B 6   ? 0.88543 0.76430 0.79500 0.14919  -0.03574 -0.09131 70  ARG B N     
1566 C CA    . ARG B 6   ? 0.90082 0.76440 0.78114 0.12166  -0.02167 -0.07421 70  ARG B CA    
1567 C C     . ARG B 6   ? 0.92854 0.84236 0.78161 0.10118  -0.01629 -0.07154 70  ARG B C     
1568 O O     . ARG B 6   ? 0.92992 0.84748 0.74893 0.07490  0.00150  -0.07753 70  ARG B O     
1569 C CB    . ARG B 6   ? 0.91567 0.75266 0.81901 0.12938  -0.03247 -0.05029 70  ARG B CB    
1570 C CG    . ARG B 6   ? 0.88968 0.66694 0.80474 0.13503  -0.02867 -0.04789 70  ARG B CG    
1571 C CD    . ARG B 6   ? 0.89704 0.65708 0.84984 0.15176  -0.04800 -0.02417 70  ARG B CD    
1572 N NE    . ARG B 6   ? 0.88307 0.59201 0.83822 0.14700  -0.04071 -0.01349 70  ARG B NE    
1573 C CZ    . ARG B 6   ? 0.85335 0.51793 0.82986 0.16379  -0.04359 -0.02199 70  ARG B CZ    
1574 N NH1   . ARG B 6   ? 0.83299 0.49948 0.82744 0.18515  -0.05233 -0.04330 70  ARG B NH1   
1575 N NH2   . ARG B 6   ? 0.84417 0.46498 0.82428 0.15834  -0.03742 -0.00968 70  ARG B NH2   
1576 N N     . GLU B 7   ? 0.94616 0.89921 0.81821 0.11308  -0.03323 -0.06300 71  GLU B N     
1577 C CA    . GLU B 7   ? 0.84641 0.84709 0.69465 0.09362  -0.03031 -0.05672 71  GLU B CA    
1578 C C     . GLU B 7   ? 0.96101 0.99184 0.78217 0.07998  -0.01759 -0.07699 71  GLU B C     
1579 O O     . GLU B 7   ? 0.97099 1.02651 0.76137 0.05471  -0.00721 -0.07474 71  GLU B O     
1580 C CB    . GLU B 7   ? 0.86022 0.89716 0.74231 0.11186  -0.05421 -0.04420 71  GLU B CB    
1581 N N     . LYS B 8   ? 0.96772 1.00029 0.80055 0.09487  -0.01888 -0.09634 72  LYS B N     
1582 C CA    . LYS B 8   ? 0.75106 0.81407 0.55932 0.07927  -0.00759 -0.11189 72  LYS B CA    
1583 C C     . LYS B 8   ? 0.96780 1.00145 0.74369 0.04881  0.01186  -0.11122 72  LYS B C     
1584 O O     . LYS B 8   ? 0.97071 1.03163 0.72208 0.02557  0.02090  -0.11460 72  LYS B O     
1585 C CB    . LYS B 8   ? 0.95693 1.02954 0.78381 0.09916  -0.01265 -0.13141 72  LYS B CB    
1586 N N     . SER B 9   ? 0.97571 0.95394 0.75565 0.04870  0.01738  -0.10778 73  SER B N     
1587 C CA    . SER B 9   ? 0.75912 0.70514 0.51792 0.02193  0.03443  -0.10955 73  SER B CA    
1588 C C     . SER B 9   ? 0.98120 0.91446 0.72768 0.00575  0.04194  -0.09876 73  SER B C     
1589 O O     . SER B 9   ? 0.98504 0.89746 0.71694 -0.01760 0.05646  -0.10416 73  SER B O     
1590 C CB    . SER B 9   ? 0.75411 0.64878 0.52639 0.02956  0.03694  -0.11447 73  SER B CB    
1591 N N     . GLU B 10  ? 0.79272 0.74141 0.54752 0.01638  0.03152  -0.08399 74  GLU B N     
1592 C CA    . GLU B 10  ? 0.80760 0.75279 0.54958 -0.00039 0.03790  -0.07164 74  GLU B CA    
1593 C C     . GLU B 10  ? 0.75455 0.75266 0.47486 -0.01830 0.03811  -0.06712 74  GLU B C     
1594 O O     . GLU B 10  ? 0.73459 0.73790 0.43200 -0.04397 0.05134  -0.06946 74  GLU B O     
1595 C CB    . GLU B 10  ? 0.76500 0.69054 0.53196 0.01880  0.02498  -0.05201 74  GLU B CB    
1596 C CG    . GLU B 10  ? 0.72774 0.59601 0.50432 0.02123  0.03275  -0.05245 74  GLU B CG    
1597 C CD    . GLU B 10  ? 0.76978 0.61691 0.57825 0.04397  0.01642  -0.03260 74  GLU B CD    
1598 O OE1   . GLU B 10  ? 0.81750 0.69513 0.63717 0.04971  0.00103  -0.01330 74  GLU B OE1   
1599 O OE2   . GLU B 10  ? 0.80877 0.60845 0.63397 0.05511  0.01753  -0.03468 74  GLU B OE2   
1600 N N     . LYS B 11  ? 0.68681 0.72629 0.41587 -0.00550 0.02359  -0.06273 75  LYS B N     
1601 C CA    . LYS B 11  ? 0.69710 0.78832 0.40794 -0.02132 0.02155  -0.05665 75  LYS B CA    
1602 C C     . LYS B 11  ? 0.69295 0.80788 0.38257 -0.03862 0.03186  -0.07478 75  LYS B C     
1603 O O     . LYS B 11  ? 0.68019 0.79255 0.37815 -0.02898 0.03134  -0.08709 75  LYS B O     
1604 C CB    . LYS B 11  ? 0.69728 0.82240 0.43407 0.00075  -0.00100 -0.04227 75  LYS B CB    
1605 N N     . PHE B 12  ? 0.73517 0.87572 0.39822 -0.06579 0.04073  -0.07613 76  PHE B N     
1606 C CA    . PHE B 12  ? 0.70325 0.87231 0.34977 -0.08326 0.04707  -0.09007 76  PHE B CA    
1607 C C     . PHE B 12  ? 0.72491 0.94543 0.35351 -0.09886 0.04353  -0.08262 76  PHE B C     
1608 O O     . PHE B 12  ? 0.72823 0.96165 0.35530 -0.09893 0.03716  -0.06623 76  PHE B O     
1609 C CB    . PHE B 12  ? 0.70398 0.84234 0.33951 -0.10609 0.06415  -0.10742 76  PHE B CB    
1610 C CG    . PHE B 12  ? 0.69512 0.77659 0.34717 -0.09555 0.06884  -0.11198 76  PHE B CG    
1611 C CD1   . PHE B 12  ? 0.70943 0.75609 0.36872 -0.08835 0.07105  -0.10490 76  PHE B CD1   
1612 C CD2   . PHE B 12  ? 0.68282 0.74951 0.34444 -0.09281 0.06938  -0.12090 76  PHE B CD2   
1613 C CE1   . PHE B 12  ? 0.69114 0.68557 0.36682 -0.07859 0.07474  -0.10891 76  PHE B CE1   
1614 C CE2   . PHE B 12  ? 0.68600 0.70228 0.36324 -0.08391 0.07223  -0.12373 76  PHE B CE2   
1615 C CZ    . PHE B 12  ? 0.71807 0.69652 0.40273 -0.07600 0.07503  -0.11853 76  PHE B CZ    
1616 N N     . ALA B 13  ? 1.10005 1.35261 0.71620 -0.11331 0.04629  -0.09267 77  ALA B N     
1617 C CA    . ALA B 13  ? 1.11534 1.41896 0.71444 -0.12897 0.04254  -0.08733 77  ALA B CA    
1618 C C     . ALA B 13  ? 1.16330 1.47373 0.74136 -0.15997 0.05598  -0.10436 77  ALA B C     
1619 O O     . ALA B 13  ? 1.15836 1.44535 0.74111 -0.16619 0.06345  -0.11831 77  ALA B O     
1620 C CB    . ALA B 13  ? 1.14732 1.49455 0.75890 -0.11298 0.02795  -0.08152 77  ALA B CB    
1621 N N     . PHE B 14  ? 0.92936 1.27163 0.49043 -0.17928 0.05695  -0.10190 78  PHE B N     
1622 C CA    . PHE B 14  ? 0.94084 1.28453 0.50662 -0.20202 0.06452  -0.11548 78  PHE B CA    
1623 C C     . PHE B 14  ? 0.98011 1.34898 0.55692 -0.20224 0.05804  -0.11636 78  PHE B C     
1624 O O     . PHE B 14  ? 0.91123 1.31270 0.49088 -0.18815 0.04674  -0.10442 78  PHE B O     
1625 C CB    . PHE B 14  ? 0.92130 1.29182 0.47854 -0.21789 0.06476  -0.11107 78  PHE B CB    
1626 C CG    . PHE B 14  ? 0.91242 1.26762 0.45897 -0.22018 0.07090  -0.10768 78  PHE B CG    
1627 C CD1   . PHE B 14  ? 0.90977 1.22597 0.45871 -0.22877 0.08536  -0.12603 78  PHE B CD1   
1628 C CD2   . PHE B 14  ? 0.91596 1.29786 0.45190 -0.21449 0.06117  -0.08454 78  PHE B CD2   
1629 C CE1   . PHE B 14  ? 0.84804 1.15346 0.38825 -0.23155 0.09205  -0.12300 78  PHE B CE1   
1630 C CE2   . PHE B 14  ? 0.88960 1.26205 0.41557 -0.21885 0.06624  -0.07770 78  PHE B CE2   
1631 C CZ    . PHE B 14  ? 0.82430 1.15864 0.35189 -0.22696 0.08273  -0.09776 78  PHE B CZ    
1632 N N     . GLN B 15  ? 1.10756 1.46451 0.69206 -0.21965 0.06464  -0.13087 79  GLN B N     
1633 C CA    . GLN B 15  ? 1.11351 1.49818 0.70778 -0.22533 0.05896  -0.13035 79  GLN B CA    
1634 C C     . GLN B 15  ? 1.17310 1.60163 0.76537 -0.23320 0.05268  -0.12358 79  GLN B C     
1635 O O     . GLN B 15  ? 1.15991 1.59567 0.74336 -0.24049 0.05421  -0.12252 79  GLN B O     
1636 C CB    . GLN B 15  ? 1.08971 1.45480 0.69141 -0.24766 0.06591  -0.14624 79  GLN B CB    
1637 N N     . ALA B 16  ? 0.89400 1.32143 1.22053 -0.22994 0.18663  -0.05382 80  ALA B N     
1638 C CA    . ALA B 16  ? 0.86297 1.32168 1.23377 -0.23243 0.17834  -0.05747 80  ALA B CA    
1639 C C     . ALA B 16  ? 0.89849 1.35144 1.26664 -0.24266 0.16521  -0.05501 80  ALA B C     
1640 O O     . ALA B 16  ? 0.83982 1.31215 1.23352 -0.24063 0.14728  -0.05616 80  ALA B O     
1641 C CB    . ALA B 16  ? 0.92689 1.39870 1.31930 -0.23653 0.19693  -0.06167 80  ALA B CB    
1642 N N     . GLU B 17  ? 1.24713 1.67207 1.58326 -0.25279 0.17323  -0.05155 81  GLU B N     
1643 C CA    . GLU B 17  ? 1.24880 1.66593 1.58031 -0.26211 0.16155  -0.04934 81  GLU B CA    
1644 C C     . GLU B 17  ? 1.22916 1.63828 1.54641 -0.25729 0.14089  -0.04588 81  GLU B C     
1645 O O     . GLU B 17  ? 1.22382 1.63954 1.55238 -0.26093 0.12558  -0.04586 81  GLU B O     
1646 C CB    . GLU B 17  ? 1.27174 1.65797 1.56943 -0.27198 0.17469  -0.04594 81  GLU B CB    
1647 N N     . VAL B 18  ? 1.02456 1.41904 1.31709 -0.24890 0.14012  -0.04303 82  VAL B N     
1648 C CA    . VAL B 18  ? 0.98133 1.36571 1.25819 -0.24430 0.12158  -0.03908 82  VAL B CA    
1649 C C     . VAL B 18  ? 0.91844 1.33403 1.23175 -0.23616 0.10432  -0.04182 82  VAL B C     
1650 O O     . VAL B 18  ? 0.87970 1.29693 1.19644 -0.23762 0.08720  -0.04047 82  VAL B O     
1651 C CB    . VAL B 18  ? 0.92583 1.28656 1.16876 -0.23722 0.12584  -0.03542 82  VAL B CB    
1652 N N     . ASN B 19  ? 0.64162 1.08109 0.98183 -0.22651 0.10821  -0.04569 83  ASN B N     
1653 C CA    . ASN B 19  ? 0.60347 1.06939 0.97525 -0.21569 0.09082  -0.04752 83  ASN B CA    
1654 C C     . ASN B 19  ? 0.66710 1.15336 1.07024 -0.22087 0.08015  -0.05044 83  ASN B C     
1655 O O     . ASN B 19  ? 0.56490 1.06569 0.98607 -0.21344 0.06124  -0.05055 83  ASN B O     
1656 C CB    . ASN B 19  ? 0.56342 1.04874 0.95727 -0.20346 0.09837  -0.05109 83  ASN B CB    
1657 C CG    . ASN B 19  ? 0.57404 1.06762 0.97467 -0.18783 0.08247  -0.04959 83  ASN B CG    
1658 O OD1   . ASN B 19  ? 0.58394 1.08139 0.98998 -0.18501 0.06311  -0.04746 83  ASN B OD1   
1659 N ND2   . ASN B 19  ? 0.55569 1.05082 0.95537 -0.17675 0.09055  -0.05068 83  ASN B ND2   
1660 N N     . ARG B 20  ? 0.62985 1.11667 1.03973 -0.23286 0.09152  -0.05272 84  ARG B N     
1661 C CA    . ARG B 20  ? 0.57726 1.08061 1.01466 -0.23904 0.08080  -0.05546 84  ARG B CA    
1662 C C     . ARG B 20  ? 0.52562 1.01122 0.94113 -0.24410 0.06520  -0.05204 84  ARG B C     
1663 O O     . ARG B 20  ? 0.52447 1.02344 0.95882 -0.24210 0.04688  -0.05338 84  ARG B O     
1664 C CB    . ARG B 20  ? 0.58034 1.08809 1.03069 -0.25043 0.09812  -0.05862 84  ARG B CB    
1665 N N     . MET B 21  ? 0.69169 1.14561 1.06617 -0.25007 0.07194  -0.04753 85  MET B N     
1666 C CA    . MET B 21  ? 0.66680 1.10040 1.01651 -0.25387 0.05799  -0.04376 85  MET B CA    
1667 C C     . MET B 21  ? 0.61667 1.05403 0.96538 -0.24262 0.03819  -0.04158 85  MET B C     
1668 O O     . MET B 21  ? 0.59215 1.02647 0.93827 -0.24352 0.02169  -0.04073 85  MET B O     
1669 C CB    . MET B 21  ? 0.64464 1.04156 0.94887 -0.25951 0.06895  -0.03859 85  MET B CB    
1670 C CG    . MET B 21  ? 0.64984 1.02211 0.92337 -0.25988 0.05464  -0.03359 85  MET B CG    
1671 S SD    . MET B 21  ? 0.66730 1.00514 0.89475 -0.25414 0.05838  -0.02660 85  MET B SD    
1672 C CE    . MET B 21  ? 0.55239 0.91465 0.80196 -0.23974 0.05226  -0.02772 85  MET B CE    
1673 N N     . MET B 22  ? 0.83385 1.27725 1.18430 -0.23133 0.03965  -0.04069 86  MET B N     
1674 C CA    . MET B 22  ? 0.84262 1.28796 1.19082 -0.21936 0.02175  -0.03782 86  MET B CA    
1675 C C     . MET B 22  ? 0.77443 1.24475 1.15602 -0.21451 0.00387  -0.04118 86  MET B C     
1676 O O     . MET B 22  ? 0.83296 1.29699 1.20563 -0.21125 -0.01387 -0.03870 86  MET B O     
1677 C CB    . MET B 22  ? 0.91377 1.36459 1.26393 -0.20732 0.02809  -0.03720 86  MET B CB    
1678 C CG    . MET B 22  ? 0.76484 1.19360 1.08367 -0.20058 0.02178  -0.03090 86  MET B CG    
1679 S SD    . MET B 22  ? 0.92510 1.35079 1.23650 -0.19281 0.03886  -0.03109 86  MET B SD    
1680 C CE    . MET B 22  ? 0.72540 1.12060 1.00180 -0.20843 0.05914  -0.02985 86  MET B CE    
1681 N N     . LYS B 23  ? 0.56814 1.06534 0.98739 -0.21394 0.00830  -0.04666 87  LYS B N     
1682 C CA    . LYS B 23  ? 0.62844 1.14878 1.08091 -0.20960 -0.00890 -0.04993 87  LYS B CA    
1683 C C     . LYS B 23  ? 0.61521 1.12846 1.06327 -0.22064 -0.01822 -0.05097 87  LYS B C     
1684 O O     . LYS B 23  ? 0.64873 1.16758 1.10478 -0.21603 -0.03815 -0.05141 87  LYS B O     
1685 C CB    . LYS B 23  ? 0.66687 1.21543 1.15977 -0.20792 -0.00054 -0.05495 87  LYS B CB    
1686 N N     . LEU B 24  ? 0.49909 0.99891 0.93385 -0.23455 -0.00414 -0.05143 88  LEU B N     
1687 C CA    . LEU B 24  ? 0.48682 0.97720 0.91500 -0.24475 -0.01202 -0.05229 88  LEU B CA    
1688 C C     . LEU B 24  ? 0.48086 0.94801 0.87505 -0.24154 -0.02661 -0.04761 88  LEU B C     
1689 O O     . LEU B 24  ? 0.47561 0.94363 0.87311 -0.24217 -0.04312 -0.04908 88  LEU B O     
1690 C CB    . LEU B 24  ? 0.53968 1.01592 0.95544 -0.25865 0.00721  -0.05245 88  LEU B CB    
1691 N N     . ILE B 25  ? 0.57591 1.02155 0.93708 -0.23770 -0.02091 -0.04189 89  ILE B N     
1692 C CA    . ILE B 25  ? 0.50641 0.92924 0.83511 -0.23351 -0.03401 -0.03638 89  ILE B CA    
1693 C C     . ILE B 25  ? 0.49535 0.93403 0.84064 -0.22111 -0.05502 -0.03705 89  ILE B C     
1694 O O     . ILE B 25  ? 0.51177 0.94188 0.84623 -0.22063 -0.07042 -0.03627 89  ILE B O     
1695 C CB    . ILE B 25  ? 0.48026 0.88005 0.77634 -0.23017 -0.02419 -0.03005 89  ILE B CB    
1696 C CG1   . ILE B 25  ? 0.48637 0.86369 0.75881 -0.24182 -0.00565 -0.02872 89  ILE B CG1   
1697 C CG2   . ILE B 25  ? 0.51112 0.89070 0.77934 -0.22314 -0.03885 -0.02375 89  ILE B CG2   
1698 C CD1   . ILE B 25  ? 0.47875 0.82195 0.70875 -0.24050 -0.00168 -0.02161 89  ILE B CD1   
1699 N N     . ILE B 26  ? 0.57771 1.03833 0.94834 -0.20995 -0.05578 -0.03845 90  ILE B N     
1700 C CA    . ILE B 26  ? 0.57876 1.05213 0.96352 -0.19579 -0.07541 -0.03828 90  ILE B CA    
1701 C C     . ILE B 26  ? 0.58656 1.07554 0.99623 -0.19831 -0.08973 -0.04385 90  ILE B C     
1702 O O     . ILE B 26  ? 0.63554 1.11838 1.03604 -0.19331 -0.10789 -0.04305 90  ILE B O     
1703 C CB    . ILE B 26  ? 0.62756 1.12063 1.03634 -0.18280 -0.07169 -0.03875 90  ILE B CB    
1704 N N     . ASN B 27  ? 1.24289 1.75140 1.68388 -0.20598 -0.08178 -0.04943 91  ASN B N     
1705 C CA    . ASN B 27  ? 1.29441 1.81961 1.76347 -0.20842 -0.09591 -0.05464 91  ASN B CA    
1706 C C     . ASN B 27  ? 1.23467 1.74104 1.68120 -0.21766 -0.10387 -0.05534 91  ASN B C     
1707 O O     . ASN B 27  ? 1.23663 1.74701 1.69029 -0.21424 -0.12325 -0.05789 91  ASN B O     
1708 C CB    . ASN B 27  ? 1.32193 1.86998 1.82743 -0.21620 -0.08345 -0.05926 91  ASN B CB    
1709 N N     . SER B 28  ? 0.64156 1.12584 1.05958 -0.22873 -0.08936 -0.05295 92  SER B N     
1710 C CA    . SER B 28  ? 0.63052 1.09608 1.02776 -0.23815 -0.09427 -0.05347 92  SER B CA    
1711 C C     . SER B 28  ? 0.66084 1.10234 1.02053 -0.23185 -0.10696 -0.04841 92  SER B C     
1712 O O     . SER B 28  ? 0.69327 1.11989 1.03613 -0.23756 -0.11380 -0.04909 92  SER B O     
1713 C CB    . SER B 28  ? 0.64656 1.09552 1.02680 -0.25158 -0.07340 -0.05198 92  SER B CB    
1714 O OG    . SER B 28  ? 0.74200 1.16391 1.08210 -0.24987 -0.06529 -0.04480 92  SER B OG    
1715 N N     . LEU B 29  ? 0.43065 0.86712 0.77655 -0.22006 -0.10985 -0.04302 93  LEU B N     
1716 C CA    . LEU B 29  ? 0.42323 0.83190 0.72886 -0.21567 -0.11753 -0.03625 93  LEU B CA    
1717 C C     . LEU B 29  ? 0.39192 0.80608 0.69863 -0.19916 -0.13437 -0.03375 93  LEU B C     
1718 O O     . LEU B 29  ? 0.39564 0.78725 0.67030 -0.19314 -0.13786 -0.02623 93  LEU B O     
1719 C CB    . LEU B 29  ? 0.41129 0.79532 0.68542 -0.21941 -0.10091 -0.02915 93  LEU B CB    
1720 C CG    . LEU B 29  ? 0.37765 0.74425 0.63606 -0.23431 -0.08719 -0.02965 93  LEU B CG    
1721 C CD1   . LEU B 29  ? 0.37685 0.72130 0.60839 -0.23652 -0.07031 -0.02357 93  LEU B CD1   
1722 C CD2   . LEU B 29  ? 0.40461 0.75216 0.64127 -0.23869 -0.09718 -0.02918 93  LEU B CD2   
1723 N N     . TYR B 30  ? 0.40449 0.84639 0.74726 -0.19111 -0.14477 -0.03937 94  TYR B N     
1724 C CA    . TYR B 30  ? 0.37153 0.81747 0.71503 -0.17378 -0.16041 -0.03689 94  TYR B CA    
1725 C C     . TYR B 30  ? 0.37308 0.80294 0.69228 -0.16988 -0.17797 -0.03583 94  TYR B C     
1726 O O     . TYR B 30  ? 0.40473 0.82568 0.70792 -0.15610 -0.18808 -0.03053 94  TYR B O     
1727 C CB    . TYR B 30  ? 0.44980 0.92751 0.83856 -0.16562 -0.16697 -0.04296 94  TYR B CB    
1728 C CG    . TYR B 30  ? 0.45991 0.95351 0.87577 -0.17064 -0.17919 -0.05116 94  TYR B CG    
1729 C CD1   . TYR B 30  ? 0.51258 1.00424 0.92425 -0.16234 -0.20086 -0.05383 94  TYR B CD1   
1730 C CD2   . TYR B 30  ? 0.47023 0.98016 0.91549 -0.18328 -0.16904 -0.05597 94  TYR B CD2   
1731 C CE1   . TYR B 30  ? 0.47226 0.97772 0.90968 -0.16680 -0.21347 -0.06139 94  TYR B CE1   
1732 C CE2   . TYR B 30  ? 0.51719 1.04135 0.98918 -0.18834 -0.18087 -0.06209 94  TYR B CE2   
1733 C CZ    . TYR B 30  ? 0.49848 1.02023 0.96725 -0.18028 -0.20391 -0.06464 94  TYR B CZ    
1734 O OH    . TYR B 30  ? 0.51890 1.05404 1.01452 -0.18568 -0.21735 -0.06968 94  TYR B OH    
1735 N N     . LYS B 31  ? 0.46642 0.89150 0.78198 -0.18108 -0.18119 -0.04058 95  LYS B N     
1736 C CA    . LYS B 31  ? 0.49018 0.89929 0.78101 -0.17739 -0.19708 -0.04008 95  LYS B CA    
1737 C C     . LYS B 31  ? 0.43957 0.81344 0.68341 -0.17868 -0.19147 -0.02988 95  LYS B C     
1738 O O     . LYS B 31  ? 0.52054 0.87788 0.73919 -0.17018 -0.20336 -0.02565 95  LYS B O     
1739 C CB    . LYS B 31  ? 0.52403 0.93935 0.82757 -0.18846 -0.20239 -0.04899 95  LYS B CB    
1740 N N     . ASN B 32  ? 0.80602 1.16651 1.03706 -0.18855 -0.17332 -0.02562 96  ASN B N     
1741 C CA    . ASN B 32  ? 0.80016 1.12522 0.98847 -0.19108 -0.16715 -0.01648 96  ASN B CA    
1742 C C     . ASN B 32  ? 0.76317 1.08266 0.94639 -0.18823 -0.15396 -0.01002 96  ASN B C     
1743 O O     . ASN B 32  ? 0.76195 1.07586 0.94231 -0.19837 -0.13771 -0.00987 96  ASN B O     
1744 C CB    . ASN B 32  ? 0.83508 1.14452 1.00913 -0.20637 -0.15854 -0.01845 96  ASN B CB    
1745 C CG    . ASN B 32  ? 0.81875 1.09705 0.95495 -0.20607 -0.16437 -0.01314 96  ASN B CG    
1746 O OD1   . ASN B 32  ? 0.84970 1.12370 0.97614 -0.19551 -0.17889 -0.01104 96  ASN B OD1   
1747 N ND2   . ASN B 32  ? 0.83679 1.09190 0.95058 -0.21673 -0.15237 -0.01059 96  ASN B ND2   
1748 N N     . LYS B 33  ? 0.33318 0.65291 0.51440 -0.17353 -0.16112 -0.00470 97  LYS B N     
1749 C CA    . LYS B 33  ? 0.31641 0.63401 0.49728 -0.16851 -0.15079 0.00068  97  LYS B CA    
1750 C C     . LYS B 33  ? 0.31401 0.59493 0.45625 -0.16972 -0.14474 0.01003  97  LYS B C     
1751 O O     . LYS B 33  ? 0.30225 0.57707 0.44104 -0.17063 -0.13280 0.01318  97  LYS B O     
1752 C CB    . LYS B 33  ? 0.30817 0.64336 0.50807 -0.15054 -0.16076 0.00200  97  LYS B CB    
1753 C CG    . LYS B 33  ? 0.30414 0.67647 0.54752 -0.14785 -0.16103 -0.00672 97  LYS B CG    
1754 C CD    . LYS B 33  ? 0.30024 0.68516 0.55829 -0.12826 -0.17339 -0.00545 97  LYS B CD    
1755 C CE    . LYS B 33  ? 0.29707 0.71698 0.59966 -0.12445 -0.17407 -0.01432 97  LYS B CE    
1756 N NZ    . LYS B 33  ? 0.30520 0.73657 0.62133 -0.10915 -0.19243 -0.01712 97  LYS B NZ    
1757 N N     A GLU B 34  ? 0.46273 0.51491 0.46509 -0.00551 -0.14188 0.00070  98  GLU B N     
1758 N N     B GLU B 34  ? 0.46339 0.51576 0.46579 -0.00555 -0.14222 0.00075  98  GLU B N     
1759 C CA    A GLU B 34  ? 0.47425 0.50535 0.44611 -0.00396 -0.12952 -0.00408 98  GLU B CA    
1760 C CA    B GLU B 34  ? 0.47616 0.50708 0.44664 -0.00447 -0.13080 -0.00446 98  GLU B CA    
1761 C C     A GLU B 34  ? 0.45232 0.47459 0.42380 -0.01084 -0.12030 -0.01345 98  GLU B C     
1762 C C     B GLU B 34  ? 0.45196 0.47447 0.42381 -0.01076 -0.12031 -0.01332 98  GLU B C     
1763 O O     A GLU B 34  ? 0.43668 0.44308 0.38733 -0.00941 -0.10945 -0.01720 98  GLU B O     
1764 O O     B GLU B 34  ? 0.43510 0.44228 0.38755 -0.00887 -0.10874 -0.01656 98  GLU B O     
1765 C CB    A GLU B 34  ? 0.51096 0.52974 0.44693 -0.00390 -0.13652 -0.00560 98  GLU B CB    
1766 C CB    B GLU B 34  ? 0.51081 0.53017 0.44681 -0.00605 -0.13827 -0.00725 98  GLU B CB    
1767 C CG    A GLU B 34  ? 0.51626 0.53190 0.44121 -0.01317 -0.14280 -0.01398 98  GLU B CG    
1768 C CG    B GLU B 34  ? 0.51849 0.53769 0.45039 -0.01606 -0.14544 -0.01553 98  GLU B CG    
1769 C CD    A GLU B 34  ? 0.54082 0.57483 0.48511 -0.01669 -0.15718 -0.01093 98  GLU B CD    
1770 C CD    B GLU B 34  ? 0.56060 0.57126 0.46245 -0.01667 -0.14990 -0.01696 98  GLU B CD    
1771 O OE1   A GLU B 34  ? 0.59347 0.63986 0.54939 -0.01021 -0.16255 -0.00136 98  GLU B OE1   
1772 O OE1   B GLU B 34  ? 0.54156 0.54851 0.42831 -0.00953 -0.14790 -0.01052 98  GLU B OE1   
1773 O OE2   A GLU B 34  ? 0.54597 0.58173 0.49409 -0.02576 -0.16269 -0.01796 98  GLU B OE2   
1774 O OE2   B GLU B 34  ? 0.58990 0.59664 0.48295 -0.02445 -0.15494 -0.02455 98  GLU B OE2   
1775 N N     . ILE B 35  ? 0.40333 0.43573 0.39886 -0.01806 -0.12393 -0.01656 99  ILE B N     
1776 C CA    . ILE B 35  ? 0.37570 0.39894 0.37251 -0.02406 -0.11416 -0.02414 99  ILE B CA    
1777 C C     . ILE B 35  ? 0.37523 0.39403 0.37799 -0.01841 -0.09631 -0.02142 99  ILE B C     
1778 O O     . ILE B 35  ? 0.31456 0.32187 0.31113 -0.02124 -0.08690 -0.02662 99  ILE B O     
1779 C CB    . ILE B 35  ? 0.38967 0.42546 0.41388 -0.03335 -0.12105 -0.02674 99  ILE B CB    
1780 N N     . PHE B 36  ? 0.27755 0.30391 0.29106 -0.01049 -0.09184 -0.01327 100 PHE B N     
1781 C CA    . PHE B 36  ? 0.19309 0.21373 0.20998 -0.00595 -0.07598 -0.01104 100 PHE B CA    
1782 C C     . PHE B 36  ? 0.27586 0.27892 0.26621 -0.00515 -0.06841 -0.01508 100 PHE B C     
1783 O O     . PHE B 36  ? 0.22246 0.21830 0.21355 -0.00623 -0.05796 -0.01722 100 PHE B O     
1784 C CB    . PHE B 36  ? 0.21602 0.24349 0.24261 0.00260  -0.07312 -0.00227 100 PHE B CB    
1785 C CG    . PHE B 36  ? 0.25586 0.27398 0.25858 0.00849  -0.07309 0.00075  100 PHE B CG    
1786 C CD1   . PHE B 36  ? 0.24058 0.26138 0.23220 0.01016  -0.08542 0.00336  100 PHE B CD1   
1787 C CD2   . PHE B 36  ? 0.25134 0.25755 0.24227 0.01173  -0.06095 0.00125  100 PHE B CD2   
1788 C CE1   . PHE B 36  ? 0.27451 0.28549 0.24334 0.01528  -0.08399 0.00665  100 PHE B CE1   
1789 C CE2   . PHE B 36  ? 0.24341 0.24147 0.21452 0.01623  -0.06010 0.00433  100 PHE B CE2   
1790 C CZ    . PHE B 36  ? 0.27098 0.27102 0.23088 0.01820  -0.07075 0.00718  100 PHE B CZ    
1791 N N     . LEU B 37  ? 0.30003 0.29607 0.26698 -0.00309 -0.07334 -0.01563 101 LEU B N     
1792 C CA    . LEU B 37  ? 0.27676 0.25788 0.22178 -0.00173 -0.06509 -0.01873 101 LEU B CA    
1793 C C     . LEU B 37  ? 0.34611 0.31865 0.28676 -0.00770 -0.06288 -0.02670 101 LEU B C     
1794 O O     . LEU B 37  ? 0.31289 0.27653 0.24850 -0.00670 -0.05304 -0.02822 101 LEU B O     
1795 C CB    . LEU B 37  ? 0.31498 0.28973 0.23559 0.00150  -0.06947 -0.01762 101 LEU B CB    
1796 C CG    . LEU B 37  ? 0.30095 0.26328 0.20335 0.00489  -0.05878 -0.01800 101 LEU B CG    
1797 C CD1   . LEU B 37  ? 0.32796 0.29142 0.24250 0.00792  -0.04814 -0.01376 101 LEU B CD1   
1798 C CD2   . LEU B 37  ? 0.34566 0.30295 0.22635 0.00882  -0.06146 -0.01470 101 LEU B CD2   
1799 N N     . ARG B 38  ? 0.38003 0.35474 0.32309 -0.01416 -0.07246 -0.03157 102 ARG B N     
1800 C CA    . ARG B 38  ? 0.41888 0.38397 0.35950 -0.02041 -0.07006 -0.03913 102 ARG B CA    
1801 C C     . ARG B 38  ? 0.39262 0.35875 0.35101 -0.02105 -0.05985 -0.03770 102 ARG B C     
1802 O O     . ARG B 38  ? 0.39906 0.35350 0.34965 -0.02068 -0.05144 -0.04023 102 ARG B O     
1803 C CB    . ARG B 38  ? 0.48205 0.45086 0.42703 -0.02880 -0.08285 -0.04409 102 ARG B CB    
1804 C CG    . ARG B 38  ? 0.51874 0.47181 0.45158 -0.03539 -0.08174 -0.05330 102 ARG B CG    
1805 C CD    . ARG B 38  ? 0.56602 0.52273 0.50566 -0.04564 -0.09497 -0.05853 102 ARG B CD    
1806 N NE    . ARG B 38  ? 0.57998 0.55263 0.55283 -0.05023 -0.09595 -0.05523 102 ARG B NE    
1807 C CZ    . ARG B 38  ? 0.60045 0.59175 0.59351 -0.05328 -0.10759 -0.05161 102 ARG B CZ    
1808 N NH1   . ARG B 38  ? 0.68467 0.68130 0.66723 -0.05211 -0.12059 -0.05020 102 ARG B NH1   
1809 N NH2   . ARG B 38  ? 0.59678 0.60195 0.62183 -0.05723 -0.10549 -0.04860 102 ARG B NH2   
1810 N N     . GLU B 39  ? 0.25238 0.23194 0.23432 -0.02148 -0.06003 -0.03307 103 GLU B N     
1811 C CA    . GLU B 39  ? 0.24366 0.22267 0.24047 -0.02298 -0.05008 -0.03194 103 GLU B CA    
1812 C C     . GLU B 39  ? 0.24443 0.21489 0.23143 -0.01721 -0.03934 -0.02907 103 GLU B C     
1813 O O     . GLU B 39  ? 0.25631 0.21744 0.24082 -0.01867 -0.03205 -0.03058 103 GLU B O     
1814 C CB    . GLU B 39  ? 0.21970 0.21461 0.24318 -0.02344 -0.05065 -0.02705 103 GLU B CB    
1815 C CG    . GLU B 39  ? 0.25801 0.26467 0.29756 -0.03037 -0.06211 -0.02910 103 GLU B CG    
1816 C CD    . GLU B 39  ? 0.33127 0.32908 0.36890 -0.03943 -0.06292 -0.03620 103 GLU B CD    
1817 O OE1   . GLU B 39  ? 0.35334 0.34241 0.39251 -0.04080 -0.05209 -0.03689 103 GLU B OE1   
1818 O OE2   . GLU B 39  ? 0.32963 0.32772 0.36292 -0.04547 -0.07463 -0.04106 103 GLU B OE2   
1819 N N     . LEU B 40  ? 0.24288 0.21596 0.22416 -0.01101 -0.03891 -0.02455 104 LEU B N     
1820 C CA    . LEU B 40  ? 0.24622 0.21190 0.21900 -0.00671 -0.03020 -0.02183 104 LEU B CA    
1821 C C     . LEU B 40  ? 0.22730 0.18153 0.18363 -0.00673 -0.02794 -0.02548 104 LEU B C     
1822 O O     . LEU B 40  ? 0.25502 0.20247 0.20939 -0.00628 -0.02131 -0.02492 104 LEU B O     
1823 C CB    . LEU B 40  ? 0.20149 0.17110 0.17102 -0.00102 -0.03080 -0.01658 104 LEU B CB    
1824 C CG    . LEU B 40  ? 0.17114 0.15132 0.15797 0.00092  -0.03177 -0.01196 104 LEU B CG    
1825 C CD1   . LEU B 40  ? 0.17379 0.15443 0.15502 0.00705  -0.03160 -0.00648 104 LEU B CD1   
1826 C CD2   . LEU B 40  ? 0.18187 0.16075 0.18088 -0.00048 -0.02289 -0.01121 104 LEU B CD2   
1827 N N     . ILE B 41  ? 0.27640 0.22783 0.22043 -0.00699 -0.03334 -0.02902 105 ILE B N     
1828 C CA    . ILE B 41  ? 0.30084 0.24086 0.22982 -0.00597 -0.02971 -0.03258 105 ILE B CA    
1829 C C     . ILE B 41  ? 0.29252 0.22483 0.22520 -0.01004 -0.02691 -0.03674 105 ILE B C     
1830 O O     . ILE B 41  ? 0.27176 0.19554 0.19939 -0.00799 -0.02077 -0.03703 105 ILE B O     
1831 C CB    . ILE B 41  ? 0.39469 0.33120 0.30700 -0.00560 -0.03539 -0.03603 105 ILE B CB    
1832 C CG1   . ILE B 41  ? 0.31084 0.24861 0.21313 0.00017  -0.03315 -0.03120 105 ILE B CG1   
1833 C CG2   . ILE B 41  ? 0.40878 0.33176 0.30847 -0.00725 -0.03294 -0.04282 105 ILE B CG2   
1834 C CD1   . ILE B 41  ? 0.42244 0.35728 0.30646 0.00066  -0.03961 -0.03303 105 ILE B CD1   
1835 N N     . SER B 42  ? 0.29989 0.23529 0.24283 -0.01588 -0.03137 -0.03938 106 SER B N     
1836 C CA    . SER B 42  ? 0.30331 0.22989 0.24980 -0.02038 -0.02812 -0.04288 106 SER B CA    
1837 C C     . SER B 42  ? 0.28404 0.20975 0.23920 -0.01920 -0.02025 -0.03812 106 SER B C     
1838 O O     . SER B 42  ? 0.24652 0.16144 0.19741 -0.01893 -0.01518 -0.03867 106 SER B O     
1839 C CB    . SER B 42  ? 0.31997 0.25048 0.27639 -0.02820 -0.03518 -0.04687 106 SER B CB    
1840 O OG    . SER B 42  ? 0.38535 0.32643 0.36213 -0.03050 -0.03348 -0.04274 106 SER B OG    
1841 N N     . ASN B 43  ? 0.21640 0.15180 0.18202 -0.01805 -0.01896 -0.03320 107 ASN B N     
1842 C CA    . ASN B 43  ? 0.18466 0.11650 0.15290 -0.01682 -0.01145 -0.02896 107 ASN B CA    
1843 C C     . ASN B 43  ? 0.19484 0.12008 0.15086 -0.01201 -0.00864 -0.02696 107 ASN B C     
1844 O O     . ASN B 43  ? 0.21991 0.13680 0.17290 -0.01190 -0.00452 -0.02549 107 ASN B O     
1845 C CB    . ASN B 43  ? 0.15792 0.09898 0.13626 -0.01557 -0.00962 -0.02465 107 ASN B CB    
1846 C CG    . ASN B 43  ? 0.23267 0.18271 0.22825 -0.01984 -0.01134 -0.02532 107 ASN B CG    
1847 O OD1   . ASN B 43  ? 0.25750 0.20630 0.25762 -0.02517 -0.01412 -0.02915 107 ASN B OD1   
1848 N ND2   . ASN B 43  ? 0.23851 0.19761 0.24514 -0.01765 -0.00952 -0.02151 107 ASN B ND2   
1849 N N     . ALA B 44  ? 0.25822 0.18756 0.20799 -0.00807 -0.01102 -0.02614 108 ALA B N     
1850 C CA    . ALA B 44  ? 0.24629 0.17173 0.18798 -0.00394 -0.00832 -0.02388 108 ALA B CA    
1851 C C     . ALA B 44  ? 0.28959 0.20564 0.22639 -0.00343 -0.00643 -0.02657 108 ALA B C     
1852 O O     . ALA B 44  ? 0.27023 0.18197 0.20632 -0.00131 -0.00336 -0.02355 108 ALA B O     
1853 C CB    . ALA B 44  ? 0.20526 0.13581 0.14108 -0.00047 -0.01028 -0.02296 108 ALA B CB    
1854 N N     . SER B 45  ? 0.24485 0.15672 0.17833 -0.00551 -0.00859 -0.03213 109 SER B N     
1855 C CA    . SER B 45  ? 0.20567 0.10594 0.13358 -0.00443 -0.00559 -0.03511 109 SER B CA    
1856 C C     . SER B 45  ? 0.17987 0.07295 0.11336 -0.00702 -0.00284 -0.03373 109 SER B C     
1857 O O     . SER B 45  ? 0.20294 0.08736 0.13404 -0.00394 0.00077  -0.03236 109 SER B O     
1858 C CB    . SER B 45  ? 0.30053 0.19502 0.22008 -0.00684 -0.00861 -0.04238 109 SER B CB    
1859 O OG    . SER B 45  ? 0.29632 0.17682 0.20918 -0.00527 -0.00434 -0.04584 109 SER B OG    
1860 N N     . ASP B 46  ? 0.24425 0.14063 0.18568 -0.01218 -0.00384 -0.03325 110 ASP B N     
1861 C CA    . ASP B 46  ? 0.21387 0.10232 0.15875 -0.01476 0.00009  -0.03091 110 ASP B CA    
1862 C C     . ASP B 46  ? 0.26812 0.15548 0.21030 -0.01083 0.00267  -0.02442 110 ASP B C     
1863 O O     . ASP B 46  ? 0.26653 0.14393 0.20590 -0.00993 0.00524  -0.02175 110 ASP B O     
1864 C CB    . ASP B 46  ? 0.23605 0.12960 0.19128 -0.02082 0.00030  -0.03101 110 ASP B CB    
1865 C CG    . ASP B 46  ? 0.30733 0.20103 0.26772 -0.02669 -0.00337 -0.03707 110 ASP B CG    
1866 O OD1   . ASP B 46  ? 0.30096 0.18673 0.25321 -0.02638 -0.00535 -0.04183 110 ASP B OD1   
1867 O OD2   . ASP B 46  ? 0.33070 0.23220 0.30360 -0.03176 -0.00418 -0.03713 110 ASP B OD2   
1868 N N     . ALA B 47  ? 0.25950 0.15615 0.20198 -0.00889 0.00137  -0.02158 111 ALA B N     
1869 C CA    . ALA B 47  ? 0.21410 0.10978 0.15311 -0.00661 0.00221  -0.01593 111 ALA B CA    
1870 C C     . ALA B 47  ? 0.21607 0.10950 0.15252 -0.00173 0.00152  -0.01390 111 ALA B C     
1871 O O     . ALA B 47  ? 0.25477 0.14402 0.18925 -0.00044 0.00125  -0.00906 111 ALA B O     
1872 C CB    . ALA B 47  ? 0.24765 0.15220 0.18731 -0.00625 0.00110  -0.01428 111 ALA B CB    
1873 N N     . LEU B 48  ? 0.24908 0.14536 0.18549 0.00124  0.00128  -0.01711 112 LEU B N     
1874 C CA    . LEU B 48  ? 0.29287 0.18735 0.22949 0.00675  0.00270  -0.01519 112 LEU B CA    
1875 C C     . LEU B 48  ? 0.27406 0.15621 0.21008 0.00804  0.00511  -0.01559 112 LEU B C     
1876 O O     . LEU B 48  ? 0.28971 0.16949 0.22848 0.01242  0.00571  -0.01067 112 LEU B O     
1877 C CB    . LEU B 48  ? 0.23170 0.13039 0.16600 0.00969  0.00391  -0.01875 112 LEU B CB    
1878 C CG    . LEU B 48  ? 0.25275 0.16241 0.18777 0.00914  0.00194  -0.01650 112 LEU B CG    
1879 C CD1   . LEU B 48  ? 0.22858 0.14078 0.15761 0.00947  0.00178  -0.02088 112 LEU B CD1   
1880 C CD2   . LEU B 48  ? 0.25184 0.16734 0.19200 0.01248  0.00259  -0.01056 112 LEU B CD2   
1881 N N     . ASP B 49  ? 0.25221 0.12630 0.18569 0.00431  0.00621  -0.02102 113 ASP B N     
1882 C CA    . ASP B 49  ? 0.23299 0.09292 0.16545 0.00445  0.00896  -0.02078 113 ASP B CA    
1883 C C     . ASP B 49  ? 0.29377 0.15059 0.22686 0.00418  0.00843  -0.01340 113 ASP B C     
1884 O O     . ASP B 49  ? 0.32354 0.17257 0.25666 0.00854  0.00947  -0.00896 113 ASP B O     
1885 C CB    . ASP B 49  ? 0.29140 0.14482 0.22289 -0.00200 0.00943  -0.02731 113 ASP B CB    
1886 C CG    . ASP B 49  ? 0.33464 0.18680 0.26241 -0.00143 0.00947  -0.03452 113 ASP B CG    
1887 O OD1   . ASP B 49  ? 0.32807 0.17822 0.25190 0.00502  0.01199  -0.03473 113 ASP B OD1   
1888 O OD2   . ASP B 49  ? 0.29330 0.14587 0.22182 -0.00748 0.00717  -0.03993 113 ASP B OD2   
1889 N N     . LYS B 50  ? 0.31513 0.17685 0.24763 -0.00047 0.00699  -0.01165 114 LYS B N     
1890 C CA    . LYS B 50  ? 0.25895 0.11369 0.18718 -0.00174 0.00718  -0.00543 114 LYS B CA    
1891 C C     . LYS B 50  ? 0.30725 0.16471 0.23452 0.00330  0.00335  0.00138  114 LYS B C     
1892 O O     . LYS B 50  ? 0.34648 0.19487 0.27120 0.00583  0.00274  0.00670  114 LYS B O     
1893 C CB    . LYS B 50  ? 0.33369 0.19160 0.25997 -0.00729 0.00819  -0.00546 114 LYS B CB    
1894 C CG    . LYS B 50  ? 0.41997 0.27770 0.35164 -0.01264 0.01149  -0.01077 114 LYS B CG    
1895 N N     . ILE B 51  ? 0.31160 0.18162 0.24199 0.00475  0.00030  0.00181  115 ILE B N     
1896 C CA    . ILE B 51  ? 0.32957 0.20422 0.26199 0.00828  -0.00440 0.00846  115 ILE B CA    
1897 C C     . ILE B 51  ? 0.32107 0.19452 0.26127 0.01531  -0.00353 0.01072  115 ILE B C     
1898 O O     . ILE B 51  ? 0.33186 0.20515 0.27512 0.01876  -0.00746 0.01787  115 ILE B O     
1899 C CB    . ILE B 51  ? 0.32233 0.21012 0.25772 0.00734  -0.00711 0.00825  115 ILE B CB    
1900 C CG1   . ILE B 51  ? 0.28002 0.17270 0.21804 0.00861  -0.01345 0.01544  115 ILE B CG1   
1901 C CG2   . ILE B 51  ? 0.28051 0.17635 0.22273 0.01045  -0.00403 0.00371  115 ILE B CG2   
1902 C CD1   . ILE B 51  ? 0.29489 0.17830 0.22119 0.00472  -0.01777 0.01988  115 ILE B CD1   
1903 N N     . ARG B 52  ? 0.28096 0.15275 0.22406 0.01775  0.00152  0.00490  116 ARG B N     
1904 C CA    . ARG B 52  ? 0.25889 0.12707 0.20861 0.02527  0.00457  0.00651  116 ARG B CA    
1905 C C     . ARG B 52  ? 0.27187 0.12425 0.21843 0.02672  0.00582  0.00946  116 ARG B C     
1906 O O     . ARG B 52  ? 0.31298 0.16281 0.26619 0.03372  0.00586  0.01532  116 ARG B O     
1907 C CB    . ARG B 52  ? 0.27352 0.14158 0.22287 0.02706  0.01028  -0.00138 116 ARG B CB    
1908 C CG    . ARG B 52  ? 0.34673 0.20680 0.29990 0.03480  0.01636  -0.00195 116 ARG B CG    
1909 C CD    . ARG B 52  ? 0.38285 0.23162 0.32640 0.03284  0.02157  -0.01203 116 ARG B CD    
1910 N NE    . ARG B 52  ? 0.43971 0.28179 0.38457 0.04079  0.02919  -0.01407 116 ARG B NE    
1911 C CZ    . ARG B 52  ? 0.47593 0.30875 0.41271 0.03924  0.03343  -0.02218 116 ARG B CZ    
1912 N NH1   . ARG B 52  ? 0.49463 0.32461 0.42288 0.03031  0.02998  -0.02893 116 ARG B NH1   
1913 N NH2   . ARG B 52  ? 0.47952 0.30867 0.41858 0.04615  0.04054  -0.02299 116 ARG B NH2   
1914 N N     . LEU B 53  ? 0.28156 0.12337 0.21940 0.02042  0.00716  0.00635  117 LEU B N     
1915 C CA    . LEU B 53  ? 0.32615 0.15369 0.26030 0.02057  0.00823  0.01060  117 LEU B CA    
1916 C C     . LEU B 53  ? 0.33788 0.16586 0.26887 0.02155  0.00213  0.02044  117 LEU B C     
1917 O O     . LEU B 53  ? 0.35876 0.18198 0.29241 0.02608  0.00085  0.02697  117 LEU B O     
1918 C CB    . LEU B 53  ? 0.31668 0.14044 0.24682 0.01214  0.01131  0.00533  117 LEU B CB    
1919 C CG    . LEU B 53  ? 0.36418 0.18573 0.29734 0.01024  0.01543  -0.00347 117 LEU B CG    
1920 C CD1   . LEU B 53  ? 0.35045 0.17331 0.28303 0.00119  0.01641  -0.00768 117 LEU B CD1   
1921 C CD2   . LEU B 53  ? 0.37887 0.19001 0.31444 0.01473  0.01861  -0.00259 117 LEU B CD2   
1922 N N     A ILE B 54  ? 0.32006 0.15580 0.24592 0.01670  -0.00210 0.02129  118 ILE B N     
1923 N N     B ILE B 54  ? 0.32004 0.15593 0.24602 0.01677  -0.00215 0.02133  118 ILE B N     
1924 C CA    A ILE B 54  ? 0.33042 0.16586 0.24966 0.01611  -0.00918 0.02969  118 ILE B CA    
1925 C CA    B ILE B 54  ? 0.33085 0.16607 0.25013 0.01623  -0.00917 0.02979  118 ILE B CA    
1926 C C     A ILE B 54  ? 0.35033 0.19485 0.28114 0.02346  -0.01533 0.03669  118 ILE B C     
1927 C C     B ILE B 54  ? 0.35058 0.19514 0.28144 0.02350  -0.01537 0.03674  118 ILE B C     
1928 O O     A ILE B 54  ? 0.36198 0.20185 0.29056 0.02609  -0.02103 0.04531  118 ILE B O     
1929 O O     B ILE B 54  ? 0.36542 0.20565 0.29390 0.02598  -0.02133 0.04541  118 ILE B O     
1930 C CB    A ILE B 54  ? 0.31925 0.16177 0.23126 0.00940  -0.01146 0.02734  118 ILE B CB    
1931 C CB    B ILE B 54  ? 0.32081 0.16254 0.23230 0.00942  -0.01153 0.02769  118 ILE B CB    
1932 C CG1   A ILE B 54  ? 0.30723 0.14212 0.21044 0.00285  -0.00493 0.02260  118 ILE B CG1   
1933 C CG1   B ILE B 54  ? 0.30489 0.13940 0.20822 0.00296  -0.00476 0.02265  118 ILE B CG1   
1934 C CG2   A ILE B 54  ? 0.31619 0.15997 0.22069 0.00829  -0.02041 0.03477  118 ILE B CG2   
1935 C CG2   B ILE B 54  ? 0.32646 0.16799 0.22956 0.00837  -0.02029 0.03545  118 ILE B CG2   
1936 C CD1   A ILE B 54  ? 0.28065 0.12052 0.17846 -0.00229 -0.00469 0.01941  118 ILE B CD1   
1937 C CD1   B ILE B 54  ? 0.33688 0.16226 0.23117 0.00092  -0.00328 0.02673  118 ILE B CD1   
1938 N N     . SER B 55  ? 0.32653 0.18484 0.27107 0.02706  -0.01387 0.03355  119 SER B N     
1939 C CA    . SER B 55  ? 0.35592 0.22569 0.31618 0.03421  -0.01811 0.04029  119 SER B CA    
1940 C C     . SER B 55  ? 0.37662 0.23723 0.34402 0.04295  -0.01556 0.04536  119 SER B C     
1941 O O     . SER B 55  ? 0.38902 0.25860 0.37089 0.04956  -0.02023 0.05348  119 SER B O     
1942 C CB    . SER B 55  ? 0.31787 0.20269 0.29040 0.03607  -0.01416 0.03544  119 SER B CB    
1943 O OG    . SER B 55  ? 0.37831 0.25696 0.35399 0.04106  -0.00463 0.02972  119 SER B OG    
1944 N N     . LEU B 56  ? 0.30235 0.14549 0.26170 0.04324  -0.00823 0.04113  120 LEU B N     
1945 C CA    . LEU B 56  ? 0.36002 0.19443 0.32641 0.05058  -0.00549 0.04567  120 LEU B CA    
1946 C C     . LEU B 56  ? 0.37321 0.20681 0.33834 0.05090  -0.01418 0.05675  120 LEU B C     
1947 O O     . LEU B 56  ? 0.40177 0.23797 0.38001 0.05857  -0.01721 0.06452  120 LEU B O     
1948 C CB    . LEU B 56  ? 0.36205 0.18264 0.32156 0.04696  0.00299  0.03735  120 LEU B CB    
1949 C CG    . LEU B 56  ? 0.32330 0.14330 0.28278 0.04599  0.01100  0.02588  120 LEU B CG    
1950 C CD1   . LEU B 56  ? 0.33810 0.14556 0.29012 0.04012  0.01611  0.01883  120 LEU B CD1   
1951 C CD2   . LEU B 56  ? 0.32102 0.14636 0.29352 0.05562  0.01555  0.02572  120 LEU B CD2   
1952 N N     . THR B 57  ? 0.42930 0.25969 0.37855 0.04248  -0.01808 0.05730  121 THR B N     
1953 C CA    . THR B 57  ? 0.46002 0.28864 0.40243 0.04135  -0.02516 0.06654  121 THR B CA    
1954 C C     . THR B 57  ? 0.51598 0.35773 0.45660 0.03914  -0.03629 0.07146  121 THR B C     
1955 O O     . THR B 57  ? 0.55518 0.40128 0.49767 0.04213  -0.04408 0.08048  121 THR B O     
1956 C CB    . THR B 57  ? 0.47139 0.28710 0.39533 0.03318  -0.02092 0.06303  121 THR B CB    
1957 O OG1   . THR B 57  ? 0.50366 0.32242 0.41707 0.02526  -0.02038 0.05612  121 THR B OG1   
1958 C CG2   . THR B 57  ? 0.49723 0.30152 0.42366 0.03346  -0.01100 0.05717  121 THR B CG2   
1959 N N     . ASP B 58  ? 0.40736 0.25559 0.34429 0.03349  -0.03758 0.06533  122 ASP B N     
1960 C CA    . ASP B 58  ? 0.40875 0.26734 0.34104 0.02811  -0.04781 0.06770  122 ASP B CA    
1961 C C     . ASP B 58  ? 0.44315 0.31957 0.39721 0.03265  -0.05300 0.07035  122 ASP B C     
1962 O O     . ASP B 58  ? 0.40408 0.28646 0.36626 0.03289  -0.04717 0.06393  122 ASP B O     
1963 C CB    . ASP B 58  ? 0.39744 0.25120 0.31308 0.01883  -0.04455 0.05950  122 ASP B CB    
1964 C CG    . ASP B 58  ? 0.51540 0.37617 0.42305 0.01215  -0.05379 0.06038  122 ASP B CG    
1965 O OD1   . ASP B 58  ? 0.40405 0.27731 0.32262 0.01364  -0.06388 0.06629  122 ASP B OD1   
1966 O OD2   . ASP B 58  ? 0.46341 0.31746 0.35515 0.00511  -0.05012 0.05434  122 ASP B OD2   
1967 N N     . GLU B 59  ? 0.60370 0.49212 0.56881 0.03553  -0.06253 0.07871  123 GLU B N     
1968 C CA    . GLU B 59  ? 0.61458 0.52315 0.60642 0.04043  -0.06593 0.08213  123 GLU B CA    
1969 C C     . GLU B 59  ? 0.53806 0.45742 0.53200 0.03293  -0.06941 0.07819  123 GLU B C     
1970 O O     . GLU B 59  ? 0.56120 0.49620 0.57665 0.03614  -0.06574 0.07737  123 GLU B O     
1971 C CB    . GLU B 59  ? 0.58001 0.50014 0.58348 0.04390  -0.07612 0.09149  123 GLU B CB    
1972 N N     . ASN B 60  ? 0.48679 0.39874 0.45832 0.02291  -0.07351 0.07439  124 ASN B N     
1973 C CA    . ASN B 60  ? 0.43776 0.35779 0.40845 0.01516  -0.07703 0.07076  124 ASN B CA    
1974 C C     . ASN B 60  ? 0.43123 0.34345 0.38874 0.01124  -0.06522 0.05967  124 ASN B C     
1975 O O     . ASN B 60  ? 0.40552 0.32089 0.35751 0.00434  -0.06613 0.05539  124 ASN B O     
1976 C CB    . ASN B 60  ? 0.43385 0.35300 0.39016 0.00631  -0.08817 0.07225  124 ASN B CB    
1977 N N     . ALA B 61  ? 0.38187 0.28418 0.33556 0.01544  -0.05453 0.05520  125 ALA B N     
1978 C CA    . ALA B 61  ? 0.41414 0.31005 0.35685 0.01156  -0.04492 0.04556  125 ALA B CA    
1979 C C     . ALA B 61  ? 0.31380 0.22370 0.26759 0.01046  -0.04145 0.04069  125 ALA B C     
1980 O O     . ALA B 61  ? 0.33240 0.24004 0.27623 0.00492  -0.03887 0.03516  125 ALA B O     
1981 C CB    . ALA B 61  ? 0.35978 0.24544 0.30139 0.01604  -0.03530 0.04188  125 ALA B CB    
1982 N N     . LEU B 62  ? 0.34112 0.26493 0.31553 0.01605  -0.04058 0.04327  126 LEU B N     
1983 C CA    . LEU B 62  ? 0.30621 0.24208 0.29069 0.01577  -0.03563 0.03941  126 LEU B CA    
1984 C C     . LEU B 62  ? 0.36813 0.31708 0.36211 0.01127  -0.04340 0.04384  126 LEU B C     
1985 O O     . LEU B 62  ? 0.38337 0.34295 0.38780 0.01117  -0.03913 0.04221  126 LEU B O     
1986 C CB    . LEU B 62  ? 0.29855 0.24000 0.29838 0.02449  -0.02707 0.03879  126 LEU B CB    
1987 C CG    . LEU B 62  ? 0.32913 0.25622 0.31991 0.02830  -0.01975 0.03389  126 LEU B CG    
1988 C CD1   . LEU B 62  ? 0.35244 0.28216 0.35520 0.03667  -0.01063 0.03236  126 LEU B CD1   
1989 C CD2   . LEU B 62  ? 0.30557 0.22490 0.28004 0.02237  -0.01620 0.02564  126 LEU B CD2   
1990 N N     . ALA B 63  ? 0.35485 0.30208 0.34399 0.00679  -0.05491 0.04936  127 ALA B N     
1991 C CA    . ALA B 63  ? 0.30174 0.26181 0.30199 0.00159  -0.06412 0.05400  127 ALA B CA    
1992 C C     . ALA B 63  ? 0.41035 0.37048 0.40352 -0.00563 -0.06129 0.04822  127 ALA B C     
1993 O O     . ALA B 63  ? 0.37233 0.34581 0.38095 -0.00833 -0.06315 0.05043  127 ALA B O     
1994 C CB    . ALA B 63  ? 0.38358 0.33804 0.37382 -0.00320 -0.07847 0.06005  127 ALA B CB    
1995 N N     . GLY B 64  ? 0.69936 0.64482 0.67090 -0.00868 -0.05630 0.04141  128 GLY B N     
1996 C CA    . GLY B 64  ? 0.67800 0.62176 0.64251 -0.01456 -0.05337 0.03656  128 GLY B CA    
1997 C C     . GLY B 64  ? 0.71698 0.67048 0.69426 -0.01063 -0.04378 0.03390  128 GLY B C     
1998 O O     . GLY B 64  ? 0.76592 0.72274 0.74476 -0.01486 -0.04259 0.03274  128 GLY B O     
1999 N N     . ASN B 65  ? 0.50423 0.46039 0.48867 -0.00278 -0.03664 0.03291  129 ASN B N     
2000 C CA    . ASN B 65  ? 0.47093 0.43356 0.46291 0.00129  -0.02714 0.03005  129 ASN B CA    
2001 C C     . ASN B 65  ? 0.48964 0.45452 0.49090 0.00983  -0.02198 0.03078  129 ASN B C     
2002 O O     . ASN B 65  ? 0.47342 0.42792 0.46514 0.01229  -0.02030 0.02781  129 ASN B O     
2003 C CB    . ASN B 65  ? 0.42491 0.37824 0.40112 -0.00029 -0.02179 0.02328  129 ASN B CB    
2004 C CG    . ASN B 65  ? 0.44239 0.40163 0.42244 0.00106  -0.01503 0.02158  129 ASN B CG    
2005 O OD1   . ASN B 65  ? 0.49179 0.45787 0.48162 0.00630  -0.00955 0.02247  129 ASN B OD1   
2006 N ND2   . ASN B 65  ? 0.44387 0.39883 0.41480 -0.00321 -0.01453 0.01934  129 ASN B ND2   
2007 N N     . GLU B 66  ? 0.52385 0.50122 0.54395 0.01422  -0.01861 0.03476  130 GLU B N     
2008 C CA    . GLU B 66  ? 0.55210 0.53028 0.58203 0.02303  -0.01347 0.03626  130 GLU B CA    
2009 C C     . GLU B 66  ? 0.60514 0.57586 0.62628 0.02792  -0.00224 0.02928  130 GLU B C     
2010 O O     . GLU B 66  ? 0.59835 0.56506 0.62320 0.03503  0.00321  0.02882  130 GLU B O     
2011 C CB    . GLU B 66  ? 0.52130 0.51625 0.57737 0.02670  -0.01327 0.04399  130 GLU B CB    
2012 N N     . GLU B 67  ? 0.40300 0.37048 0.41162 0.02432  0.00083  0.02395  131 GLU B N     
2013 C CA    . GLU B 67  ? 0.42986 0.39057 0.42831 0.02793  0.00956  0.01753  131 GLU B CA    
2014 C C     . GLU B 67  ? 0.42046 0.36838 0.40190 0.02536  0.00743  0.01117  131 GLU B C     
2015 O O     . GLU B 67  ? 0.39291 0.33780 0.36873 0.02012  0.00107  0.01133  131 GLU B O     
2016 C CB    . GLU B 67  ? 0.47980 0.44569 0.47587 0.02624  0.01411  0.01680  131 GLU B CB    
2017 C CG    . GLU B 67  ? 0.41165 0.37202 0.39233 0.02069  0.01077  0.01280  131 GLU B CG    
2018 C CD    . GLU B 67  ? 0.45023 0.41478 0.42862 0.01938  0.01483  0.01365  131 GLU B CD    
2019 O OE1   . GLU B 67  ? 0.46967 0.44348 0.46068 0.01812  0.01595  0.01907  131 GLU B OE1   
2020 O OE2   . GLU B 67  ? 0.42367 0.38224 0.38805 0.01926  0.01640  0.00940  131 GLU B OE2   
2021 N N     . LEU B 68  ? 0.24952 0.18939 0.22263 0.02879  0.01337  0.00539  132 LEU B N     
2022 C CA    . LEU B 68  ? 0.27490 0.20370 0.23472 0.02603  0.01174  -0.00092 132 LEU B CA    
2023 C C     . LEU B 68  ? 0.27002 0.19672 0.21839 0.02564  0.01504  -0.00659 132 LEU B C     
2024 O O     . LEU B 68  ? 0.25422 0.17344 0.19553 0.02882  0.02004  -0.01131 132 LEU B O     
2025 C CB    . LEU B 68  ? 0.28456 0.20297 0.24456 0.02966  0.01397  -0.00250 132 LEU B CB    
2026 C CG    . LEU B 68  ? 0.29282 0.21029 0.26056 0.03000  0.00944  0.00342  132 LEU B CG    
2027 C CD1   . LEU B 68  ? 0.24269 0.14805 0.21020 0.03465  0.01313  0.00220  132 LEU B CD1   
2028 C CD2   . LEU B 68  ? 0.27759 0.19304 0.23864 0.02299  0.00295  0.00368  132 LEU B CD2   
2029 N N     . THR B 69  ? 0.23101 0.16270 0.17582 0.02174  0.01196  -0.00613 133 THR B N     
2030 C CA    . THR B 69  ? 0.23118 0.16198 0.16519 0.02186  0.01395  -0.00959 133 THR B CA    
2031 C C     . THR B 69  ? 0.23127 0.16248 0.16013 0.01715  0.00811  -0.01117 133 THR B C     
2032 O O     . THR B 69  ? 0.21383 0.14622 0.14754 0.01388  0.00427  -0.00939 133 THR B O     
2033 C CB    . THR B 69  ? 0.24314 0.18102 0.17985 0.02389  0.01853  -0.00533 133 THR B CB    
2034 O OG1   . THR B 69  ? 0.23702 0.18171 0.18029 0.01999  0.01438  -0.00061 133 THR B OG1   
2035 C CG2   . THR B 69  ? 0.27218 0.21259 0.21888 0.02910  0.02552  -0.00247 133 THR B CG2   
2036 N N     . VAL B 70  ? 0.17657 0.10609 0.09491 0.01722  0.00776  -0.01436 134 VAL B N     
2037 C CA    . VAL B 70  ? 0.20252 0.13489 0.11780 0.01440  0.00278  -0.01425 134 VAL B CA    
2038 C C     . VAL B 70  ? 0.23142 0.16659 0.14065 0.01639  0.00507  -0.01107 134 VAL B C     
2039 O O     . VAL B 70  ? 0.24611 0.17811 0.14674 0.01936  0.00966  -0.01214 134 VAL B O     
2040 C CB    . VAL B 70  ? 0.19511 0.12357 0.10389 0.01226  -0.00189 -0.01999 134 VAL B CB    
2041 C CG1   . VAL B 70  ? 0.21542 0.14942 0.12555 0.01033  -0.00726 -0.01835 134 VAL B CG1   
2042 C CG2   . VAL B 70  ? 0.22848 0.15266 0.14316 0.00986  -0.00270 -0.02284 134 VAL B CG2   
2043 N N     . LYS B 71  ? 0.25080 0.19011 0.16336 0.01490  0.00301  -0.00704 135 LYS B N     
2044 C CA    . LYS B 71  ? 0.28353 0.22419 0.19076 0.01640  0.00548  -0.00295 135 LYS B CA    
2045 C C     . LYS B 71  ? 0.28934 0.23075 0.19388 0.01571  0.00043  -0.00168 135 LYS B C     
2046 O O     . LYS B 71  ? 0.29305 0.23594 0.20570 0.01372  -0.00179 -0.00056 135 LYS B O     
2047 C CB    . LYS B 71  ? 0.29859 0.24279 0.21519 0.01550  0.00954  0.00225  135 LYS B CB    
2048 C CG    . LYS B 71  ? 0.28472 0.23041 0.20477 0.01794  0.01593  0.00290  135 LYS B CG    
2049 C CD    . LYS B 71  ? 0.26005 0.21187 0.19417 0.01596  0.01786  0.00818  135 LYS B CD    
2050 C CE    . LYS B 71  ? 0.31171 0.26731 0.25286 0.01946  0.02524  0.00984  135 LYS B CE    
2051 N NZ    . LYS B 71  ? 0.36127 0.32531 0.32076 0.01707  0.02453  0.01495  135 LYS B NZ    
2052 N N     . ILE B 72  ? 0.26674 0.20634 0.15923 0.01775  -0.00114 -0.00159 136 ILE B N     
2053 C CA    . ILE B 72  ? 0.23470 0.17579 0.12493 0.01833  -0.00695 0.00051  136 ILE B CA    
2054 C C     . ILE B 72  ? 0.25898 0.19806 0.14272 0.02049  -0.00345 0.00680  136 ILE B C     
2055 O O     . ILE B 72  ? 0.29049 0.22600 0.16330 0.02203  0.00144  0.00784  136 ILE B O     
2056 C CB    . ILE B 72  ? 0.24457 0.18466 0.12473 0.01849  -0.01378 -0.00363 136 ILE B CB    
2057 C CG1   . ILE B 72  ? 0.23671 0.17861 0.12603 0.01525  -0.01742 -0.00936 136 ILE B CG1   
2058 C CG2   . ILE B 72  ? 0.26111 0.20388 0.13850 0.02023  -0.02041 0.00047  136 ILE B CG2   
2059 C CD1   . ILE B 72  ? 0.30443 0.24175 0.18214 0.01385  -0.02150 -0.01557 136 ILE B CD1   
2060 N N     . LYS B 73  ? 0.22921 0.16915 0.11922 0.02074  -0.00462 0.01114  137 LYS B N     
2061 C CA    . LYS B 73  ? 0.27604 0.21210 0.15844 0.02287  -0.00165 0.01751  137 LYS B CA    
2062 C C     . LYS B 73  ? 0.26993 0.20598 0.15460 0.02538  -0.00638 0.02160  137 LYS B C     
2063 O O     . LYS B 73  ? 0.23981 0.17815 0.13683 0.02474  -0.00793 0.02083  137 LYS B O     
2064 C CB    . LYS B 73  ? 0.56704 0.50120 0.45503 0.02045  0.00605  0.02048  137 LYS B CB    
2065 C CG    . LYS B 73  ? 0.55748 0.49069 0.45695 0.01762  0.00658  0.02153  137 LYS B CG    
2066 C CD    . LYS B 73  ? 0.55624 0.48863 0.46004 0.01398  0.01259  0.02388  137 LYS B CD    
2067 C CE    . LYS B 73  ? 0.55554 0.48241 0.46444 0.01054  0.01387  0.02666  137 LYS B CE    
2068 N NZ    . LYS B 73  ? 0.55042 0.47905 0.46812 0.00482  0.01565  0.02641  137 LYS B NZ    
2069 N N     . CYS B 74  ? 0.27960 0.21238 0.15151 0.02879  -0.00823 0.02631  138 CYS B N     
2070 C CA    . CYS B 74  ? 0.31540 0.24746 0.18894 0.03264  -0.01239 0.03221  138 CYS B CA    
2071 C C     . CYS B 74  ? 0.30460 0.22891 0.17875 0.03297  -0.00488 0.03826  138 CYS B C     
2072 O O     . CYS B 74  ? 0.35600 0.27471 0.22003 0.03211  0.00115  0.04115  138 CYS B O     
2073 C CB    . CYS B 74  ? 0.31203 0.24302 0.16952 0.03629  -0.01943 0.03548  138 CYS B CB    
2074 S SG    . CYS B 74  ? 0.39434 0.32758 0.23869 0.03414  -0.02583 0.02794  138 CYS B SG    
2075 N N     . ASP B 75  ? 0.29908 0.22203 0.18476 0.03411  -0.00444 0.04022  139 ASP B N     
2076 C CA    . ASP B 75  ? 0.35018 0.26299 0.23445 0.03499  0.00158  0.04641  139 ASP B CA    
2077 C C     . ASP B 75  ? 0.37625 0.28736 0.25920 0.04204  -0.00310 0.05323  139 ASP B C     
2078 O O     . ASP B 75  ? 0.35858 0.27067 0.25388 0.04508  -0.00422 0.05398  139 ASP B O     
2079 C CB    . ASP B 75  ? 0.34034 0.24874 0.23551 0.03101  0.00680  0.04363  139 ASP B CB    
2080 C CG    . ASP B 75  ? 0.36872 0.26409 0.26048 0.03001  0.01353  0.04898  139 ASP B CG    
2081 O OD1   . ASP B 75  ? 0.45923 0.35012 0.34587 0.03451  0.01346  0.05528  139 ASP B OD1   
2082 O OD2   . ASP B 75  ? 0.37722 0.26735 0.27209 0.02390  0.01818  0.04653  139 ASP B OD2   
2083 N N     . LYS B 76  ? 0.36935 0.27887 0.23909 0.04421  -0.00523 0.05788  140 LYS B N     
2084 C CA    . LYS B 76  ? 0.37632 0.28672 0.24633 0.04984  -0.01110 0.06433  140 LYS B CA    
2085 C C     . LYS B 76  ? 0.36609 0.26793 0.24457 0.05193  -0.00526 0.06927  140 LYS B C     
2086 O O     . LYS B 76  ? 0.45589 0.35932 0.34342 0.05784  -0.00931 0.07360  140 LYS B O     
2087 C CB    . LYS B 76  ? 0.46662 0.37621 0.32058 0.04928  -0.01309 0.06705  140 LYS B CB    
2088 C CG    . LYS B 76  ? 0.48015 0.39529 0.33117 0.05393  -0.02457 0.07161  140 LYS B CG    
2089 C CD    . LYS B 76  ? 0.50069 0.41209 0.33256 0.05267  -0.02529 0.07435  140 LYS B CD    
2090 C CE    . LYS B 76  ? 0.51914 0.42939 0.34965 0.05750  -0.03189 0.08360  140 LYS B CE    
2091 N NZ    . LYS B 76  ? 0.51267 0.43248 0.36068 0.06230  -0.04181 0.08578  140 LYS B NZ    
2092 N N     . GLU B 77  ? 0.51159 0.40452 0.38835 0.04695  0.00411  0.06860  141 GLU B N     
2093 C CA    . GLU B 77  ? 0.52680 0.40938 0.40913 0.04773  0.00983  0.07222  141 GLU B CA    
2094 C C     . GLU B 77  ? 0.57239 0.45337 0.46814 0.05053  0.01083  0.07017  141 GLU B C     
2095 O O     . GLU B 77  ? 0.62894 0.50353 0.53060 0.05462  0.01303  0.07384  141 GLU B O     
2096 C CB    . GLU B 77  ? 0.49687 0.37142 0.37623 0.04022  0.01851  0.07064  141 GLU B CB    
2097 N N     . LYS B 78  ? 0.39356 0.27935 0.29391 0.04862  0.01007  0.06433  142 LYS B N     
2098 C CA    . LYS B 78  ? 0.35049 0.23367 0.26259 0.05047  0.01298  0.06151  142 LYS B CA    
2099 C C     . LYS B 78  ? 0.30018 0.19705 0.22336 0.05580  0.00589  0.06091  142 LYS B C     
2100 O O     . LYS B 78  ? 0.35339 0.25211 0.28893 0.05589  0.00888  0.05678  142 LYS B O     
2101 C CB    . LYS B 78  ? 0.37643 0.25385 0.28690 0.04229  0.01839  0.05442  142 LYS B CB    
2102 C CG    . LYS B 78  ? 0.48807 0.35785 0.39151 0.03477  0.02311  0.05386  142 LYS B CG    
2103 C CD    . LYS B 78  ? 0.44296 0.29967 0.34897 0.03183  0.02962  0.05175  142 LYS B CD    
2104 C CE    . LYS B 78  ? 0.53587 0.38756 0.43837 0.02145  0.03230  0.04717  142 LYS B CE    
2105 N NZ    . LYS B 78  ? 0.55498 0.40494 0.45363 0.01782  0.03389  0.05119  142 LYS B NZ    
2106 N N     . ASN B 79  ? 0.37873 0.28662 0.29860 0.05854  -0.00355 0.06366  143 ASN B N     
2107 C CA    . ASN B 79  ? 0.35124 0.27554 0.28432 0.06121  -0.01241 0.06211  143 ASN B CA    
2108 C C     . ASN B 79  ? 0.31826 0.25005 0.25867 0.05455  -0.01150 0.05241  143 ASN B C     
2109 O O     . ASN B 79  ? 0.32990 0.27034 0.28717 0.05582  -0.01239 0.05027  143 ASN B O     
2110 C CB    . ASN B 79  ? 0.39253 0.31883 0.34307 0.06976  -0.01225 0.06814  143 ASN B CB    
2111 C CG    . ASN B 79  ? 0.38300 0.32860 0.34997 0.07286  -0.02314 0.06885  143 ASN B CG    
2112 O OD1   . ASN B 79  ? 0.38026 0.33463 0.33969 0.07169  -0.03437 0.06939  143 ASN B OD1   
2113 N ND2   . ASN B 79  ? 0.42147 0.37331 0.41089 0.07608  -0.01942 0.06835  143 ASN B ND2   
2114 N N     . LEU B 80  ? 0.27741 0.20613 0.20623 0.04765  -0.00926 0.04710  144 LEU B N     
2115 C CA    . LEU B 80  ? 0.26295 0.19653 0.19724 0.04169  -0.00803 0.03882  144 LEU B CA    
2116 C C     . LEU B 80  ? 0.27890 0.21871 0.20418 0.03782  -0.01341 0.03460  144 LEU B C     
2117 O O     . LEU B 80  ? 0.26478 0.20045 0.17569 0.03741  -0.01332 0.03657  144 LEU B O     
2118 C CB    . LEU B 80  ? 0.24296 0.16519 0.17451 0.03678  0.00109  0.03575  144 LEU B CB    
2119 C CG    . LEU B 80  ? 0.26232 0.17317 0.19839 0.03930  0.00842  0.03814  144 LEU B CG    
2120 C CD1   . LEU B 80  ? 0.21404 0.11246 0.14268 0.03238  0.01505  0.03440  144 LEU B CD1   
2121 C CD2   . LEU B 80  ? 0.24305 0.15963 0.19479 0.04293  0.00939  0.03689  144 LEU B CD2   
2122 N N     . LEU B 81  ? 0.24425 0.19267 0.17770 0.03507  -0.01694 0.02885  145 LEU B N     
2123 C CA    . LEU B 81  ? 0.21758 0.16917 0.14348 0.03082  -0.02012 0.02323  145 LEU B CA    
2124 C C     . LEU B 81  ? 0.21594 0.16590 0.14725 0.02591  -0.01482 0.01756  145 LEU B C     
2125 O O     . LEU B 81  ? 0.19745 0.14965 0.14103 0.02529  -0.01326 0.01597  145 LEU B O     
2126 C CB    . LEU B 81  ? 0.21911 0.18066 0.14885 0.03115  -0.03015 0.02145  145 LEU B CB    
2127 C CG    . LEU B 81  ? 0.21095 0.17366 0.13280 0.02657  -0.03347 0.01456  145 LEU B CG    
2128 C CD1   . LEU B 81  ? 0.25335 0.20850 0.15427 0.02690  -0.03177 0.01495  145 LEU B CD1   
2129 C CD2   . LEU B 81  ? 0.29001 0.26188 0.21779 0.02545  -0.04415 0.01247  145 LEU B CD2   
2130 N N     . HIS B 82  ? 0.21337 0.15931 0.13597 0.02277  -0.01162 0.01518  146 HIS B N     
2131 C CA    . HIS B 82  ? 0.19386 0.13793 0.12055 0.01849  -0.00783 0.01099  146 HIS B CA    
2132 C C     . HIS B 82  ? 0.24016 0.18732 0.16421 0.01641  -0.01034 0.00596  146 HIS B C     
2133 O O     . HIS B 82  ? 0.22525 0.17193 0.13951 0.01733  -0.01112 0.00568  146 HIS B O     
2134 C CB    . HIS B 82  ? 0.17269 0.11013 0.09523 0.01631  -0.00231 0.01295  146 HIS B CB    
2135 C CG    . HIS B 82  ? 0.22101 0.15184 0.14352 0.01751  0.00096  0.01739  146 HIS B CG    
2136 N ND1   . HIS B 82  ? 0.22365 0.14890 0.15093 0.01635  0.00399  0.01669  146 HIS B ND1   
2137 C CD2   . HIS B 82  ? 0.21899 0.14561 0.13574 0.01976  0.00258  0.02258  146 HIS B CD2   
2138 C CE1   . HIS B 82  ? 0.23010 0.14745 0.15487 0.01788  0.00730  0.02075  146 HIS B CE1   
2139 N NE2   . HIS B 82  ? 0.22837 0.14667 0.14746 0.01989  0.00631  0.02471  146 HIS B NE2   
2140 N N     . VAL B 83  ? 0.15777 0.10620 0.08918 0.01374  -0.01052 0.00205  147 VAL B N     
2141 C CA    . VAL B 83  ? 0.16141 0.10999 0.09055 0.01163  -0.01175 -0.00275 147 VAL B CA    
2142 C C     . VAL B 83  ? 0.14736 0.09196 0.07935 0.00903  -0.00758 -0.00357 147 VAL B C     
2143 O O     . VAL B 83  ? 0.14069 0.08391 0.07878 0.00712  -0.00637 -0.00416 147 VAL B O     
2144 C CB    . VAL B 83  ? 0.15868 0.11163 0.09356 0.01018  -0.01688 -0.00637 147 VAL B CB    
2145 C CG1   . VAL B 83  ? 0.18483 0.13471 0.11426 0.00808  -0.01775 -0.01158 147 VAL B CG1   
2146 C CG2   . VAL B 83  ? 0.17244 0.13090 0.10661 0.01261  -0.02326 -0.00422 147 VAL B CG2   
2147 N N     . THR B 84  ? 0.17655 0.11927 0.10425 0.00910  -0.00522 -0.00307 148 THR B N     
2148 C CA    . THR B 84  ? 0.17714 0.11711 0.10793 0.00681  -0.00301 -0.00234 148 THR B CA    
2149 C C     . THR B 84  ? 0.20873 0.14802 0.13979 0.00706  -0.00275 -0.00496 148 THR B C     
2150 O O     . THR B 84  ? 0.22013 0.16016 0.14720 0.00946  -0.00168 -0.00621 148 THR B O     
2151 C CB    . THR B 84  ? 0.18696 0.12661 0.11710 0.00633  -0.00082 0.00185  148 THR B CB    
2152 O OG1   . THR B 84  ? 0.25063 0.18761 0.17985 0.00589  -0.00031 0.00412  148 THR B OG1   
2153 C CG2   . THR B 84  ? 0.18401 0.12217 0.11772 0.00345  -0.00089 0.00288  148 THR B CG2   
2154 N N     . ASP B 85  ? 0.21077 0.14686 0.14501 0.00494  -0.00303 -0.00573 149 ASP B N     
2155 C CA    . ASP B 85  ? 0.25858 0.19223 0.19383 0.00563  -0.00252 -0.00730 149 ASP B CA    
2156 C C     . ASP B 85  ? 0.25976 0.19185 0.19792 0.00430  -0.00289 -0.00365 149 ASP B C     
2157 O O     . ASP B 85  ? 0.26186 0.19197 0.19877 0.00142  -0.00392 -0.00170 149 ASP B O     
2158 C CB    . ASP B 85  ? 0.22468 0.15453 0.16009 0.00409  -0.00344 -0.01147 149 ASP B CB    
2159 C CG    . ASP B 85  ? 0.26914 0.19548 0.20677 0.00081  -0.00321 -0.01052 149 ASP B CG    
2160 O OD1   . ASP B 85  ? 0.23557 0.15731 0.17226 -0.00009 -0.00278 -0.00821 149 ASP B OD1   
2161 O OD2   . ASP B 85  ? 0.23491 0.16307 0.17507 -0.00063 -0.00328 -0.01160 149 ASP B OD2   
2162 N N     . THR B 86  ? 0.19888 0.13133 0.14042 0.00662  -0.00220 -0.00254 150 THR B N     
2163 C CA    . THR B 86  ? 0.20083 0.13279 0.14636 0.00567  -0.00450 0.00170  150 THR B CA    
2164 C C     . THR B 86  ? 0.21925 0.14377 0.16330 0.00573  -0.00517 0.00093  150 THR B C     
2165 O O     . THR B 86  ? 0.24949 0.17338 0.19799 0.00796  -0.00623 0.00408  150 THR B O     
2166 C CB    . THR B 86  ? 0.21127 0.15053 0.16552 0.00879  -0.00337 0.00536  150 THR B CB    
2167 O OG1   . THR B 86  ? 0.22416 0.16264 0.17961 0.01382  0.00118  0.00283  150 THR B OG1   
2168 C CG2   . THR B 86  ? 0.23226 0.17746 0.18758 0.00760  -0.00215 0.00695  150 THR B CG2   
2169 N N     . GLY B 87  ? 0.21525 0.13422 0.15447 0.00353  -0.00422 -0.00272 151 GLY B N     
2170 C CA    . GLY B 87  ? 0.23724 0.14764 0.17446 0.00263  -0.00376 -0.00329 151 GLY B CA    
2171 C C     . GLY B 87  ? 0.24308 0.14739 0.17480 -0.00075 -0.00552 0.00024  151 GLY B C     
2172 O O     . GLY B 87  ? 0.24434 0.15057 0.17396 -0.00218 -0.00844 0.00348  151 GLY B O     
2173 N N     . VAL B 88  ? 0.26283 0.15829 0.19068 -0.00279 -0.00338 -0.00069 152 VAL B N     
2174 C CA    . VAL B 88  ? 0.27178 0.15779 0.19067 -0.00554 -0.00411 0.00305  152 VAL B CA    
2175 C C     . VAL B 88  ? 0.26186 0.14677 0.17364 -0.00905 -0.00360 0.00317  152 VAL B C     
2176 O O     . VAL B 88  ? 0.30945 0.18677 0.21056 -0.01143 -0.00587 0.00646  152 VAL B O     
2177 C CB    . VAL B 88  ? 0.28924 0.16507 0.20558 -0.00714 0.00005  0.00208  152 VAL B CB    
2178 C CG1   . VAL B 88  ? 0.32494 0.20273 0.24499 -0.01013 0.00495  -0.00250 152 VAL B CG1   
2179 C CG2   . VAL B 88  ? 0.28772 0.15143 0.19178 -0.00923 -0.00047 0.00699  152 VAL B CG2   
2180 N N     . GLY B 89  ? 0.24758 0.13855 0.16374 -0.00927 -0.00094 -0.00019 153 GLY B N     
2181 C CA    . GLY B 89  ? 0.24678 0.13447 0.15619 -0.01177 0.00100  -0.00015 153 GLY B CA    
2182 C C     . GLY B 89  ? 0.24868 0.12630 0.15173 -0.01436 0.00720  -0.00074 153 GLY B C     
2183 O O     . GLY B 89  ? 0.24844 0.12285 0.15375 -0.01477 0.00963  -0.00102 153 GLY B O     
2184 N N     . MET B 90  ? 0.36529 0.23650 0.25978 -0.01625 0.01074  -0.00086 154 MET B N     
2185 C CA    . MET B 90  ? 0.32796 0.19061 0.21815 -0.01796 0.01957  -0.00173 154 MET B CA    
2186 C C     . MET B 90  ? 0.34348 0.19448 0.21553 -0.02023 0.02152  -0.00092 154 MET B C     
2187 O O     . MET B 90  ? 0.36843 0.21919 0.23704 -0.02032 0.02000  -0.00165 154 MET B O     
2188 C CB    . MET B 90  ? 0.31228 0.18540 0.21815 -0.01584 0.02416  -0.00425 154 MET B CB    
2189 C CG    . MET B 90  ? 0.34305 0.22371 0.26385 -0.01590 0.02586  -0.00566 154 MET B CG    
2190 S SD    . MET B 90  ? 0.31522 0.20944 0.25573 -0.01385 0.02947  -0.00744 154 MET B SD    
2191 C CE    . MET B 90  ? 0.25856 0.15953 0.19764 -0.01027 0.02261  -0.00727 154 MET B CE    
2192 N N     . THR B 91  ? 0.29334 0.13423 0.15257 -0.02217 0.02470  0.00019  155 THR B N     
2193 C CA    . THR B 91  ? 0.31238 0.13973 0.15058 -0.02463 0.02679  -0.00043 155 THR B CA    
2194 C C     . THR B 91  ? 0.30837 0.13274 0.14698 -0.02362 0.03794  -0.00302 155 THR B C     
2195 O O     . THR B 91  ? 0.28807 0.12181 0.14527 -0.02104 0.04338  -0.00366 155 THR B O     
2196 C CB    . THR B 91  ? 0.34395 0.15947 0.16732 -0.02649 0.02811  0.00073  155 THR B CB    
2197 O OG1   . THR B 91  ? 0.32954 0.14472 0.15969 -0.02560 0.03963  0.00012  155 THR B OG1   
2198 C CG2   . THR B 91  ? 0.32023 0.13911 0.14600 -0.02629 0.01780  0.00451  155 THR B CG2   
2199 N N     . ARG B 92  ? 0.32674 0.14110 0.16114 0.01118  0.00994  -0.01835 156 ARG B N     
2200 C CA    . ARG B 92  ? 0.31969 0.12912 0.14446 0.01267  0.01645  -0.01356 156 ARG B CA    
2201 C C     . ARG B 92  ? 0.38591 0.16092 0.18913 -0.00265 0.00722  -0.01299 156 ARG B C     
2202 O O     . ARG B 92  ? 0.41646 0.20843 0.22462 -0.00905 0.00057  -0.00646 156 ARG B O     
2203 C CB    . ARG B 92  ? 0.28936 0.12740 0.13811 0.01970  0.02942  -0.00533 156 ARG B CB    
2204 C CG    . ARG B 92  ? 0.26264 0.10678 0.11290 0.02611  0.03845  0.00038  156 ARG B CG    
2205 C CD    . ARG B 92  ? 0.30348 0.14859 0.16003 0.02552  0.04952  0.00638  156 ARG B CD    
2206 N NE    . ARG B 92  ? 0.26248 0.14563 0.14662 0.03227  0.05579  0.01352  156 ARG B NE    
2207 C CZ    . ARG B 92  ? 0.32130 0.23257 0.22104 0.02304  0.05894  0.02713  156 ARG B CZ    
2208 N NH1   . ARG B 92  ? 0.26560 0.17049 0.16766 0.00461  0.05032  0.03223  156 ARG B NH1   
2209 N NH2   . ARG B 92  ? 0.29516 0.24836 0.22488 0.02927  0.06053  0.03186  156 ARG B NH2   
2210 N N     . GLU B 93  ? 0.37558 0.14424 0.18492 -0.01274 0.00254  -0.00973 157 GLU B N     
2211 C CA    . GLU B 93  ? 0.42645 0.19192 0.24008 -0.03556 -0.01088 0.00141  157 GLU B CA    
2212 C C     . GLU B 93  ? 0.46626 0.22382 0.26843 -0.04781 -0.02978 -0.00104 157 GLU B C     
2213 O O     . GLU B 93  ? 0.45451 0.24060 0.27190 -0.06024 -0.03719 0.00996  157 GLU B O     
2214 C CB    . GLU B 93  ? 0.40024 0.15508 0.21679 -0.04302 -0.01470 0.00213  157 GLU B CB    
2215 C CG    . GLU B 93  ? 0.47214 0.22217 0.29024 -0.06958 -0.03157 0.01290  157 GLU B CG    
2216 C CD    . GLU B 93  ? 0.50694 0.25768 0.33198 -0.07218 -0.03340 0.01354  157 GLU B CD    
2217 O OE1   . GLU B 93  ? 0.48980 0.23430 0.31125 -0.05749 -0.03175 0.00296  157 GLU B OE1   
2218 O OE2   . GLU B 93  ? 0.52617 0.28971 0.36287 -0.08951 -0.03647 0.02592  157 GLU B OE2   
2219 N N     . GLU B 94  ? 0.48438 0.21722 0.26714 -0.04194 -0.03631 -0.01451 158 GLU B N     
2220 C CA    . GLU B 94  ? 0.59912 0.32201 0.36974 -0.05276 -0.05375 -0.01750 158 GLU B CA    
2221 C C     . GLU B 94  ? 0.54513 0.28793 0.31656 -0.05034 -0.05343 -0.01552 158 GLU B C     
2222 O O     . GLU B 94  ? 0.55687 0.31213 0.33255 -0.06359 -0.06694 -0.00945 158 GLU B O     
2223 C CB    . GLU B 94  ? 0.54808 0.27138 0.31942 -0.04052 -0.05357 -0.02616 158 GLU B CB    
2224 C CG    . GLU B 94  ? 0.52922 0.24757 0.30736 -0.04264 -0.05678 -0.02550 158 GLU B CG    
2225 C CD    . GLU B 94  ? 0.59733 0.31823 0.38008 -0.03285 -0.05690 -0.03420 158 GLU B CD    
2226 O OE1   . GLU B 94  ? 0.50229 0.24164 0.29612 -0.01938 -0.04527 -0.03971 158 GLU B OE1   
2227 O OE2   . GLU B 94  ? 0.77162 0.47870 0.54962 -0.04026 -0.06875 -0.03488 158 GLU B OE2   
2228 N N     . LEU B 95  ? 0.47581 0.23071 0.24844 -0.03174 -0.03730 -0.01860 159 LEU B N     
2229 C CA    . LEU B 95  ? 0.44310 0.22575 0.22213 -0.02679 -0.03631 -0.01385 159 LEU B CA    
2230 C C     . LEU B 95  ? 0.49260 0.31785 0.30248 -0.03397 -0.03622 0.00309  159 LEU B C     
2231 O O     . LEU B 95  ? 0.48239 0.32888 0.29941 -0.03927 -0.04545 0.00854  159 LEU B O     
2232 C CB    . LEU B 95  ? 0.38912 0.17216 0.16005 -0.00607 -0.01968 -0.02088 159 LEU B CB    
2233 C CG    . LEU B 95  ? 0.39033 0.16665 0.16130 0.00209  -0.01639 -0.02951 159 LEU B CG    
2234 C CD1   . LEU B 95  ? 0.35154 0.15677 0.14853 0.01642  0.00023  -0.02550 159 LEU B CD1   
2235 C CD2   . LEU B 95  ? 0.41146 0.18306 0.16960 -0.00255 -0.02786 -0.03389 159 LEU B CD2   
2236 N N     . VAL B 96  ? 0.41797 0.25778 0.24674 -0.03365 -0.02567 0.01068  160 VAL B N     
2237 C CA    . VAL B 96  ? 0.40953 0.29339 0.26913 -0.04058 -0.02454 0.02520  160 VAL B CA    
2238 C C     . VAL B 96  ? 0.49306 0.38166 0.35828 -0.06448 -0.04184 0.03171  160 VAL B C     
2239 O O     . VAL B 96  ? 0.52272 0.44424 0.40501 -0.07216 -0.04907 0.03929  160 VAL B O     
2240 C CB    . VAL B 96  ? 0.40790 0.30626 0.28509 -0.03405 -0.00774 0.03066  160 VAL B CB    
2241 C CG1   . VAL B 96  ? 0.44728 0.39135 0.35642 -0.04506 -0.00805 0.04440  160 VAL B CG1   
2242 C CG2   . VAL B 96  ? 0.33146 0.23272 0.20669 -0.01031 0.00942  0.02579  160 VAL B CG2   
2243 N N     . LYS B 97  ? 0.48122 0.33643 0.33153 -0.07653 -0.04956 0.02825  161 LYS B N     
2244 C CA    . LYS B 97  ? 0.51648 0.36919 0.36748 -0.10081 -0.06696 0.03386  161 LYS B CA    
2245 C C     . LYS B 97  ? 0.63477 0.45814 0.46175 -0.10545 -0.08343 0.02453  161 LYS B C     
2246 O O     . LYS B 97  ? 0.71579 0.50375 0.52458 -0.11640 -0.09536 0.01938  161 LYS B O     
2247 C CB    . LYS B 97  ? 0.61147 0.44223 0.45862 -0.11216 -0.06745 0.03620  161 LYS B CB    
2248 C CG    . LYS B 97  ? 0.57551 0.43366 0.44494 -0.10862 -0.05106 0.04506  161 LYS B CG    
2249 C CD    . LYS B 97  ? 0.51941 0.35078 0.38108 -0.12036 -0.05282 0.04712  161 LYS B CD    
2250 C CE    . LYS B 97  ? 0.51031 0.36946 0.39349 -0.11589 -0.03540 0.05538  161 LYS B CE    
2251 N NZ    . LYS B 97  ? 0.51368 0.34350 0.38700 -0.12392 -0.03528 0.05661  161 LYS B NZ    
2252 N N     . ASN B 98  ? 0.83144 0.66944 0.65796 -0.09702 -0.08490 0.02221  162 ASN B N     
2253 C CA    . ASN B 98  ? 0.74962 0.56227 0.55271 -0.09852 -0.09833 0.01236  162 ASN B CA    
2254 C C     . ASN B 98  ? 0.85361 0.67951 0.66259 -0.11814 -0.11646 0.01873  162 ASN B C     
2255 O O     . ASN B 98  ? 0.92485 0.74798 0.72331 -0.11736 -0.12582 0.01416  162 ASN B O     
2256 C CB    . ASN B 98  ? 0.82081 0.63834 0.61612 -0.07914 -0.09021 0.00592  162 ASN B CB    
2257 C CG    . ASN B 98  ? 0.80013 0.66280 0.61923 -0.07516 -0.08722 0.01639  162 ASN B CG    
2258 O OD1   . ASN B 98  ? 0.80947 0.69219 0.63869 -0.08725 -0.10009 0.02250  162 ASN B OD1   
2259 N ND2   . ASN B 98  ? 0.77250 0.65141 0.60104 -0.05786 -0.07082 0.01791  162 ASN B ND2   
2260 N N     . LEU B 99  ? 1.01967 0.85880 0.84369 -0.13673 -0.12184 0.02882  163 LEU B N     
2261 C CA    . LEU B 99  ? 1.02698 0.89708 0.86756 -0.15471 -0.13410 0.03822  163 LEU B CA    
2262 C C     . LEU B 99  ? 0.99815 0.91819 0.86542 -0.14525 -0.12566 0.04505  163 LEU B C     
2263 O O     . LEU B 99  ? 1.00295 0.94660 0.87895 -0.15059 -0.13569 0.04772  163 LEU B O     
2264 C CB    . LEU B 99  ? 1.05820 0.90769 0.88017 -0.16414 -0.15298 0.03234  163 LEU B CB    
2265 N N     . GLY B 100 ? 0.82940 0.76497 0.70960 -0.13046 -0.10789 0.04721  164 GLY B N     
2266 C CA    . GLY B 100 ? 0.80093 0.78321 0.70768 -0.11984 -0.09932 0.05309  164 GLY B CA    
2267 C C     . GLY B 100 ? 0.77138 0.76889 0.69385 -0.10919 -0.08043 0.05676  164 GLY B C     
2268 O O     . GLY B 100 ? 0.76778 0.77519 0.70250 -0.12203 -0.07725 0.06313  164 GLY B O     
2269 N N     . THR B 124 ? 1.00430 0.80123 0.73053 -0.21379 -0.29647 -0.00775 188 THR B N     
2270 C CA    . THR B 124 ? 0.98031 0.77792 0.70946 -0.20608 -0.28511 -0.00675 188 THR B CA    
2271 C C     . THR B 124 ? 0.97804 0.74787 0.68922 -0.19206 -0.27408 -0.01726 188 THR B C     
2272 O O     . THR B 124 ? 0.96338 0.72558 0.67459 -0.18655 -0.26450 -0.01807 188 THR B O     
2273 C CB    . THR B 124 ? 0.95762 0.78494 0.69836 -0.19982 -0.28310 -0.00191 188 THR B CB    
2274 N N     . SER B 125 ? 1.12433 0.88151 0.82157 -0.18653 -0.27502 -0.02555 189 SER B N     
2275 C CA    . SER B 125 ? 1.12076 0.85873 0.80360 -0.17277 -0.26340 -0.03653 189 SER B CA    
2276 C C     . SER B 125 ? 1.12201 0.84025 0.80362 -0.17146 -0.25800 -0.04048 189 SER B C     
2277 O O     . SER B 125 ? 1.10460 0.81761 0.78504 -0.16137 -0.24603 -0.04385 189 SER B O     
2278 C CB    . SER B 125 ? 1.13928 0.86993 0.80993 -0.17058 -0.26675 -0.04442 189 SER B CB    
2279 N N     . GLU B 126 ? 0.87975 0.58702 0.56178 -0.18121 -0.26703 -0.03986 190 GLU B N     
2280 C CA    . GLU B 126 ? 0.85524 0.54435 0.53704 -0.18080 -0.26419 -0.04173 190 GLU B CA    
2281 C C     . GLU B 126 ? 0.94661 0.64290 0.63973 -0.18914 -0.26463 -0.03076 190 GLU B C     
2282 O O     . GLU B 126 ? 0.88508 0.56847 0.57794 -0.18525 -0.25860 -0.03182 190 GLU B O     
2283 C CB    . GLU B 126 ? 0.90656 0.58008 0.58349 -0.18795 -0.27438 -0.04471 190 GLU B CB    
2284 N N     . LEU B 127 ? 1.10952 0.82875 0.81394 -0.20033 -0.27129 -0.02050 191 LEU B N     
2285 C CA    . LEU B 127 ? 1.07361 0.80513 0.79134 -0.21019 -0.27136 -0.00988 191 LEU B CA    
2286 C C     . LEU B 127 ? 1.12062 0.85419 0.84035 -0.19914 -0.25841 -0.01075 191 LEU B C     
2287 O O     . LEU B 127 ? 1.09340 0.81691 0.81469 -0.20026 -0.25401 -0.00853 191 LEU B O     
2288 C CB    . LEU B 127 ? 1.10650 0.87006 0.83971 -0.22273 -0.27968 -0.00017 191 LEU B CB    
2289 N N     . ILE B 128 ? 1.07123 0.81662 0.78970 -0.18797 -0.25221 -0.01397 192 ILE B N     
2290 C CA    . ILE B 128 ? 0.95395 0.70382 0.67466 -0.17763 -0.24009 -0.01420 192 ILE B CA    
2291 C C     . ILE B 128 ? 0.95884 0.68212 0.66868 -0.16573 -0.22939 -0.02343 192 ILE B C     
2292 O O     . ILE B 128 ? 0.92623 0.64686 0.63970 -0.16211 -0.22121 -0.02187 192 ILE B O     
2293 C CB    . ILE B 128 ? 0.80724 0.57386 0.52652 -0.16746 -0.23652 -0.01567 192 ILE B CB    
2294 N N     . GLY B 129 ? 1.02226 0.72864 0.72058 -0.15902 -0.22891 -0.03344 193 GLY B N     
2295 C CA    . GLY B 129 ? 1.01429 0.70229 0.70646 -0.14630 -0.21832 -0.04320 193 GLY B CA    
2296 C C     . GLY B 129 ? 1.01623 0.69030 0.71183 -0.15149 -0.22061 -0.03995 193 GLY B C     
2297 O O     . GLY B 129 ? 1.00890 0.67693 0.70607 -0.14274 -0.21063 -0.04216 193 GLY B O     
2298 N N     . GLN B 130 ? 0.92321 0.59225 0.61973 -0.16580 -0.23384 -0.03428 194 GLN B N     
2299 C CA    . GLN B 130 ? 0.97193 0.62706 0.66995 -0.17267 -0.23776 -0.02947 194 GLN B CA    
2300 C C     . GLN B 130 ? 0.91199 0.57991 0.62037 -0.18265 -0.23679 -0.01729 194 GLN B C     
2301 O O     . GLN B 130 ? 0.83860 0.49546 0.54755 -0.18497 -0.23580 -0.01371 194 GLN B O     
2302 C CB    . GLN B 130 ? 1.02641 0.67179 0.72066 -0.18530 -0.25225 -0.02710 194 GLN B CB    
2303 N N     . PHE B 131 ? 1.26644 0.95955 0.98390 -0.18831 -0.23705 -0.01101 195 PHE B N     
2304 C CA    . PHE B 131 ? 1.26283 0.97569 0.99409 -0.19926 -0.23621 0.00056  195 PHE B CA    
2305 C C     . PHE B 131 ? 1.19749 0.91023 0.93056 -0.18759 -0.22270 -0.00128 195 PHE B C     
2306 O O     . PHE B 131 ? 1.20706 0.93311 0.95127 -0.19582 -0.22037 0.00757  195 PHE B O     
2307 C CB    . PHE B 131 ? 1.30014 1.04605 1.04398 -0.20786 -0.24170 0.00702  195 PHE B CB    
2308 C CG    . PHE B 131 ? 1.26615 1.03802 1.02786 -0.22629 -0.24634 0.02006  195 PHE B CG    
2309 C CD1   . PHE B 131 ? 1.35750 1.12304 1.12223 -0.23400 -0.24340 0.02622  195 PHE B CD1   
2310 C CD2   . PHE B 131 ? 1.24363 1.04855 1.01988 -0.23563 -0.25326 0.02594  195 PHE B CD2   
2311 C CE1   . PHE B 131 ? 1.34218 1.13501 1.12389 -0.25173 -0.24605 0.03811  195 PHE B CE1   
2312 C CE2   . PHE B 131 ? 1.32582 1.16033 1.12131 -0.25222 -0.25586 0.03704  195 PHE B CE2   
2313 C CZ    . PHE B 131 ? 1.40062 1.22952 1.19866 -0.26090 -0.25171 0.04320  195 PHE B CZ    
2314 N N     . GLY B 132 ? 0.78555 0.48563 0.50890 -0.16900 -0.21294 -0.01257 196 GLY B N     
2315 C CA    . GLY B 132 ? 0.71940 0.42135 0.44405 -0.15633 -0.19910 -0.01526 196 GLY B CA    
2316 C C     . GLY B 132 ? 0.71596 0.44147 0.44546 -0.15276 -0.19517 -0.01342 196 GLY B C     
2317 O O     . GLY B 132 ? 0.69756 0.42600 0.42782 -0.14248 -0.18368 -0.01509 196 GLY B O     
2318 N N     . VAL B 133 ? 0.71050 0.45370 0.44330 -0.15983 -0.20454 -0.01001 197 VAL B N     
2319 C CA    . VAL B 133 ? 0.67479 0.44509 0.41422 -0.15655 -0.20349 -0.00644 197 VAL B CA    
2320 C C     . VAL B 133 ? 0.60722 0.37165 0.33274 -0.14178 -0.19907 -0.01554 197 VAL B C     
2321 O O     . VAL B 133 ? 0.60723 0.39188 0.33527 -0.13713 -0.19933 -0.01277 197 VAL B O     
2322 C CB    . VAL B 133 ? 0.68997 0.49134 0.44676 -0.17281 -0.21622 0.00455  197 VAL B CB    
2323 N N     . GLY B 134 ? 0.47813 0.51066 0.43311 -0.11165 0.00836  -0.04040 198 GLY B N     
2324 C CA    . GLY B 134 ? 0.46600 0.50221 0.41947 -0.10681 0.00104  -0.04066 198 GLY B CA    
2325 C C     . GLY B 134 ? 0.42693 0.47085 0.39021 -0.09420 -0.00157 -0.03656 198 GLY B C     
2326 O O     . GLY B 134 ? 0.45027 0.50685 0.41878 -0.08670 -0.00808 -0.03512 198 GLY B O     
2327 N N     . PHE B 135 ? 0.31824 0.35274 0.28344 -0.08789 0.00419  -0.03257 199 PHE B N     
2328 C CA    . PHE B 135 ? 0.29684 0.33622 0.27179 -0.07291 0.00335  -0.02711 199 PHE B CA    
2329 C C     . PHE B 135 ? 0.26353 0.33244 0.25965 -0.06833 -0.00138 -0.02735 199 PHE B C     
2330 O O     . PHE B 135 ? 0.25557 0.32902 0.25659 -0.05688 -0.00500 -0.02340 199 PHE B O     
2331 C CB    . PHE B 135 ? 0.29552 0.32306 0.26980 -0.06950 0.00992  -0.02424 199 PHE B CB    
2332 C CG    . PHE B 135 ? 0.23865 0.28019 0.22956 -0.05959 0.01007  -0.02144 199 PHE B CG    
2333 C CD1   . PHE B 135 ? 0.23697 0.27312 0.22823 -0.04790 0.00890  -0.01689 199 PHE B CD1   
2334 C CD2   . PHE B 135 ? 0.20301 0.26233 0.20859 -0.06260 0.01223  -0.02384 199 PHE B CD2   
2335 C CE1   . PHE B 135 ? 0.26071 0.30663 0.26558 -0.03986 0.00950  -0.01485 199 PHE B CE1   
2336 C CE2   . PHE B 135 ? 0.23511 0.30473 0.25432 -0.05338 0.01290  -0.02209 199 PHE B CE2   
2337 C CZ    . PHE B 135 ? 0.25332 0.31508 0.27169 -0.04218 0.01137  -0.01762 199 PHE B CZ    
2338 N N     . TYR B 136 ? 0.21501 0.30404 0.22365 -0.07683 -0.00101 -0.03183 200 TYR B N     
2339 C CA    . TYR B 136 ? 0.24267 0.36152 0.27316 -0.07098 -0.00503 -0.03242 200 TYR B CA    
2340 C C     . TYR B 136 ? 0.25251 0.38690 0.28563 -0.06866 -0.01456 -0.03300 200 TYR B C     
2341 O O     . TYR B 136 ? 0.27187 0.43093 0.32241 -0.06130 -0.01927 -0.03266 200 TYR B O     
2342 C CB    . TYR B 136 ? 0.27305 0.40698 0.31485 -0.07848 -0.00057 -0.03660 200 TYR B CB    
2343 C CG    . TYR B 136 ? 0.25883 0.38312 0.30113 -0.07682 0.00778  -0.03531 200 TYR B CG    
2344 C CD1   . TYR B 136 ? 0.27236 0.40816 0.32956 -0.06629 0.00905  -0.03385 200 TYR B CD1   
2345 C CD2   . TYR B 136 ? 0.28420 0.38617 0.31004 -0.08491 0.01413  -0.03543 200 TYR B CD2   
2346 C CE1   . TYR B 136 ? 0.33538 0.46149 0.39083 -0.06488 0.01614  -0.03316 200 TYR B CE1   
2347 C CE2   . TYR B 136 ? 0.29177 0.38504 0.31592 -0.08274 0.02059  -0.03400 200 TYR B CE2   
2348 C CZ    . TYR B 136 ? 0.37467 0.48051 0.41357 -0.07321 0.02141  -0.03316 200 TYR B CZ    
2349 O OH    . TYR B 136 ? 0.41774 0.51488 0.45358 -0.07118 0.02715  -0.03229 200 TYR B OH    
2350 N N     . SER B 137 ? 0.39662 0.51694 0.41202 -0.07387 -0.01768 -0.03386 201 SER B N     
2351 C CA    . SER B 137 ? 0.35666 0.48774 0.37037 -0.06954 -0.02703 -0.03317 201 SER B CA    
2352 C C     . SER B 137 ? 0.35127 0.47518 0.36366 -0.05302 -0.02899 -0.02563 201 SER B C     
2353 O O     . SER B 137 ? 0.39180 0.52462 0.40269 -0.04713 -0.03680 -0.02352 201 SER B O     
2354 C CB    . SER B 137 ? 0.38572 0.50074 0.37791 -0.07981 -0.02895 -0.03673 201 SER B CB    
2355 O OG    . SER B 137 ? 0.38101 0.46461 0.35446 -0.07551 -0.02382 -0.03324 201 SER B OG    
2356 N N     . ALA B 138 ? 0.34922 0.45664 0.36073 -0.04622 -0.02216 -0.02152 202 ALA B N     
2357 C CA    . ALA B 138 ? 0.30680 0.40752 0.31817 -0.03221 -0.02293 -0.01467 202 ALA B CA    
2358 C C     . ALA B 138 ? 0.28484 0.40787 0.31403 -0.02267 -0.02787 -0.01268 202 ALA B C     
2359 O O     . ALA B 138 ? 0.29162 0.41164 0.31846 -0.01180 -0.03136 -0.00698 202 ALA B O     
2360 C CB    . ALA B 138 ? 0.30357 0.38572 0.31282 -0.02880 -0.01469 -0.01199 202 ALA B CB    
2361 N N     . PHE B 139 ? 0.18911 0.33411 0.23561 -0.02622 -0.02780 -0.01717 203 PHE B N     
2362 C CA    . PHE B 139 ? 0.23859 0.40668 0.30376 -0.01581 -0.03216 -0.01600 203 PHE B CA    
2363 C C     . PHE B 139 ? 0.25964 0.44810 0.32699 -0.01367 -0.04315 -0.01607 203 PHE B C     
2364 O O     . PHE B 139 ? 0.27300 0.48292 0.35617 -0.00365 -0.04808 -0.01494 203 PHE B O     
2365 C CB    . PHE B 139 ? 0.21180 0.39839 0.29558 -0.02004 -0.02722 -0.02143 203 PHE B CB    
2366 C CG    . PHE B 139 ? 0.22802 0.39858 0.31220 -0.01767 -0.01785 -0.02044 203 PHE B CG    
2367 C CD1   . PHE B 139 ? 0.17588 0.33965 0.26435 -0.00407 -0.01655 -0.01596 203 PHE B CD1   
2368 C CD2   . PHE B 139 ? 0.19311 0.35391 0.27157 -0.02943 -0.01051 -0.02398 203 PHE B CD2   
2369 C CE1   . PHE B 139 ? 0.19325 0.34300 0.28133 -0.00300 -0.00850 -0.01593 203 PHE B CE1   
2370 C CE2   . PHE B 139 ? 0.19368 0.34086 0.27122 -0.02725 -0.00290 -0.02311 203 PHE B CE2   
2371 C CZ    . PHE B 139 ? 0.15224 0.29490 0.23501 -0.01446 -0.00208 -0.01953 203 PHE B CZ    
2372 N N     . LEU B 140 ? 0.22420 0.40685 0.27571 -0.02226 -0.04735 -0.01766 204 LEU B N     
2373 C CA    . LEU B 140 ? 0.24247 0.44171 0.29218 -0.01903 -0.05875 -0.01682 204 LEU B CA    
2374 C C     . LEU B 140 ? 0.27788 0.46374 0.31727 -0.00405 -0.06238 -0.00785 204 LEU B C     
2375 O O     . LEU B 140 ? 0.27023 0.47188 0.31148 0.00384  -0.07221 -0.00505 204 LEU B O     
2376 C CB    . LEU B 140 ? 0.28273 0.47777 0.31607 -0.03375 -0.06180 -0.02212 204 LEU B CB    
2377 C CG    . LEU B 140 ? 0.29780 0.49866 0.33671 -0.04971 -0.05726 -0.03034 204 LEU B CG    
2378 C CD1   . LEU B 140 ? 0.26337 0.44518 0.27981 -0.06248 -0.05698 -0.03427 204 LEU B CD1   
2379 C CD2   . LEU B 140 ? 0.33144 0.55937 0.38918 -0.04851 -0.06148 -0.03285 204 LEU B CD2   
2380 N N     . VAL B 141 ? 0.34165 0.49921 0.36966 -0.00033 -0.05476 -0.00317 205 VAL B N     
2381 C CA    . VAL B 141 ? 0.31157 0.45350 0.32820 0.01186  -0.05629 0.00547  205 VAL B CA    
2382 C C     . VAL B 141 ? 0.25164 0.38132 0.27580 0.02133  -0.04917 0.01004  205 VAL B C     
2383 O O     . VAL B 141 ? 0.28845 0.40436 0.30432 0.03121  -0.04954 0.01747  205 VAL B O     
2384 C CB    . VAL B 141 ? 0.32015 0.43854 0.31219 0.00667  -0.05408 0.00698  205 VAL B CB    
2385 C CG1   . VAL B 141 ? 0.33392 0.46206 0.31556 -0.00242 -0.06154 0.00208  205 VAL B CG1   
2386 C CG2   . VAL B 141 ? 0.31848 0.41795 0.30705 -0.00048 -0.04338 0.00431  205 VAL B CG2   
2387 N N     . ALA B 142 ? 0.23300 0.36586 0.27087 0.01788  -0.04240 0.00575  206 ALA B N     
2388 C CA    . ALA B 142 ? 0.27294 0.39203 0.31570 0.02458  -0.03499 0.00866  206 ALA B CA    
2389 C C     . ALA B 142 ? 0.19527 0.33316 0.25940 0.02935  -0.03414 0.00537  206 ALA B C     
2390 O O     . ALA B 142 ? 0.21786 0.37332 0.29272 0.02123  -0.03333 -0.00128 206 ALA B O     
2391 C CB    . ALA B 142 ? 0.18331 0.28357 0.21834 0.01591  -0.02613 0.00661  206 ALA B CB    
2392 N N     . ASP B 143 ? 0.20357 0.33666 0.27298 0.04230  -0.03359 0.00986  207 ASP B N     
2393 C CA    . ASP B 143 ? 0.20924 0.35635 0.29787 0.04861  -0.03099 0.00652  207 ASP B CA    
2394 C C     . ASP B 143 ? 0.18851 0.32535 0.28003 0.04227  -0.02077 0.00224  207 ASP B C     
2395 O O     . ASP B 143 ? 0.20495 0.35525 0.31167 0.04402  -0.01721 -0.00258 207 ASP B O     
2396 C CB    . ASP B 143 ? 0.26727 0.40792 0.35785 0.06548  -0.03335 0.01279  207 ASP B CB    
2397 C CG    . ASP B 143 ? 0.25354 0.41355 0.34786 0.07483  -0.04443 0.01592  207 ASP B CG    
2398 O OD1   . ASP B 143 ? 0.31335 0.50013 0.41997 0.06995  -0.04859 0.01032  207 ASP B OD1   
2399 O OD2   . ASP B 143 ? 0.24250 0.38860 0.32605 0.08569  -0.04847 0.02398  207 ASP B OD2   
2400 N N     . LYS B 144 ? 0.24664 0.36117 0.32385 0.03553  -0.01609 0.00382  208 LYS B N     
2401 C CA    . LYS B 144 ? 0.18715 0.29039 0.26434 0.03003  -0.00753 0.00066  208 LYS B CA    
2402 C C     . LYS B 144 ? 0.18033 0.26923 0.24260 0.02017  -0.00561 0.00122  208 LYS B C     
2403 O O     . LYS B 144 ? 0.22194 0.29938 0.27206 0.02148  -0.00806 0.00596  208 LYS B O     
2404 C CB    . LYS B 144 ? 0.22234 0.30869 0.29912 0.03850  -0.00326 0.00365  208 LYS B CB    
2405 C CG    . LYS B 144 ? 0.22339 0.30782 0.30711 0.03627  0.00424  -0.00159 208 LYS B CG    
2406 C CD    . LYS B 144 ? 0.27101 0.34775 0.36005 0.04783  0.00637  -0.00039 208 LYS B CD    
2407 C CE    . LYS B 144 ? 0.23303 0.30591 0.32670 0.04554  0.01401  -0.00623 208 LYS B CE    
2408 N NZ    . LYS B 144 ? 0.28485 0.34900 0.36936 0.03370  0.01752  -0.00781 208 LYS B NZ    
2409 N N     . VAL B 145 ? 0.17619 0.26519 0.23849 0.01097  -0.00091 -0.00342 209 VAL B N     
2410 C CA    . VAL B 145 ? 0.14467 0.21896 0.19324 0.00328  0.00155  -0.00305 209 VAL B CA    
2411 C C     . VAL B 145 ? 0.15624 0.22013 0.20470 0.00204  0.00805  -0.00419 209 VAL B C     
2412 O O     . VAL B 145 ? 0.17903 0.25050 0.23602 0.00065  0.01133  -0.00814 209 VAL B O     
2413 C CB    . VAL B 145 ? 0.15873 0.23998 0.20361 -0.00709 0.00039  -0.00707 209 VAL B CB    
2414 C CG1   . VAL B 145 ? 0.18316 0.24625 0.21262 -0.01309 0.00335  -0.00652 209 VAL B CG1   
2415 C CG2   . VAL B 145 ? 0.19123 0.28476 0.23641 -0.00669 -0.00686 -0.00681 209 VAL B CG2   
2416 N N     A ILE B 146 ? 0.13247 0.18058 0.17132 0.00231  0.00997  -0.00113 210 ILE B N     
2417 N N     B ILE B 146 ? 0.13061 0.17876 0.16982 0.00280  0.00990  -0.00097 210 ILE B N     
2418 C CA    A ILE B 146 ? 0.14705 0.18650 0.18512 0.00096  0.01495  -0.00213 210 ILE B CA    
2419 C CA    B ILE B 146 ? 0.14717 0.18640 0.18494 0.00095  0.01488  -0.00202 210 ILE B CA    
2420 C C     A ILE B 146 ? 0.13216 0.16262 0.15899 -0.00429 0.01617  -0.00178 210 ILE B C     
2421 C C     B ILE B 146 ? 0.13147 0.16291 0.15812 -0.00482 0.01582  -0.00202 210 ILE B C     
2422 O O     A ILE B 146 ? 0.13423 0.15776 0.15305 -0.00326 0.01492  0.00125  210 ILE B O     
2423 O O     B ILE B 146 ? 0.11203 0.13826 0.13031 -0.00480 0.01387  0.00037  210 ILE B O     
2424 C CB    A ILE B 146 ? 0.15567 0.18628 0.19509 0.00687  0.01642  0.00089  210 ILE B CB    
2425 C CB    B ILE B 146 ? 0.15658 0.18585 0.19442 0.00630  0.01650  0.00121  210 ILE B CB    
2426 C CG1   A ILE B 146 ? 0.14900 0.18540 0.19824 0.01369  0.01557  0.00059  210 ILE B CG1   
2427 C CG1   B ILE B 146 ? 0.14151 0.17440 0.18908 0.01273  0.01666  0.00068  210 ILE B CG1   
2428 C CG2   A ILE B 146 ? 0.14026 0.16403 0.17887 0.00410  0.02074  -0.00098 210 ILE B CG2   
2429 C CG2   B ILE B 146 ? 0.14279 0.16464 0.17798 0.00296  0.02047  -0.00012 210 ILE B CG2   
2430 C CD1   A ILE B 146 ? 0.15542 0.17953 0.20318 0.01938  0.01673  0.00439  210 ILE B CD1   
2431 C CD1   B ILE B 146 ? 0.16658 0.19907 0.21354 0.01975  0.01255  0.00540  210 ILE B CD1   
2432 N N     . VAL B 147 ? 0.16459 0.19452 0.18984 -0.00920 0.01887  -0.00472 211 VAL B N     
2433 C CA    . VAL B 147 ? 0.13492 0.15522 0.14889 -0.01277 0.01995  -0.00421 211 VAL B CA    
2434 C C     . VAL B 147 ? 0.22241 0.23780 0.23629 -0.01120 0.02245  -0.00390 211 VAL B C     
2435 O O     . VAL B 147 ? 0.17724 0.19604 0.19527 -0.01261 0.02441  -0.00649 211 VAL B O     
2436 C CB    . VAL B 147 ? 0.15978 0.18108 0.16896 -0.01997 0.02076  -0.00705 211 VAL B CB    
2437 C CG1   . VAL B 147 ? 0.13208 0.13959 0.12747 -0.02206 0.02192  -0.00587 211 VAL B CG1   
2438 C CG2   . VAL B 147 ? 0.15243 0.18157 0.16324 -0.02294 0.01778  -0.00833 211 VAL B CG2   
2439 N N     . THR B 148 ? 0.16698 0.17596 0.17648 -0.00844 0.02243  -0.00119 212 THR B N     
2440 C CA    . THR B 148 ? 0.17980 0.18675 0.18951 -0.00743 0.02389  -0.00107 212 THR B CA    
2441 C C     . THR B 148 ? 0.16064 0.16126 0.16003 -0.00771 0.02375  -0.00023 212 THR B C     
2442 O O     . THR B 148 ? 0.17786 0.17327 0.17075 -0.00627 0.02333  0.00141  212 THR B O     
2443 C CB    . THR B 148 ? 0.15564 0.16225 0.16954 -0.00429 0.02451  0.00118  212 THR B CB    
2444 O OG1   . THR B 148 ? 0.12549 0.13399 0.14672 -0.00321 0.02479  0.00098  212 THR B OG1   
2445 C CG2   . THR B 148 ? 0.17831 0.18629 0.19407 -0.00452 0.02557  0.00047  212 THR B CG2   
2446 N N     . SER B 149 ? 0.21269 0.21235 0.20884 -0.00913 0.02414  -0.00134 213 SER B N     
2447 C CA    . SER B 149 ? 0.23593 0.22680 0.22019 -0.00834 0.02382  0.00012  213 SER B CA    
2448 C C     . SER B 149 ? 0.20955 0.20143 0.19192 -0.00624 0.02307  0.00048  213 SER B C     
2449 O O     . SER B 149 ? 0.21712 0.21457 0.20359 -0.00866 0.02320  -0.00161 213 SER B O     
2450 C CB    . SER B 149 ? 0.22969 0.21415 0.20538 -0.01377 0.02463  -0.00092 213 SER B CB    
2451 O OG    . SER B 149 ? 0.23316 0.20427 0.19484 -0.01260 0.02472  0.00094  213 SER B OG    
2452 N N     . LYS B 150 ? 0.14310 0.12982 0.11870 -0.00119 0.02213  0.00286  214 LYS B N     
2453 C CA    . LYS B 150 ? 0.12850 0.11719 0.10123 0.00243  0.02013  0.00385  214 LYS B CA    
2454 C C     . LYS B 150 ? 0.16418 0.13870 0.12132 0.00614  0.01967  0.00664  214 LYS B C     
2455 O O     . LYS B 150 ? 0.19413 0.16107 0.14658 0.01032  0.02054  0.00800  214 LYS B O     
2456 C CB    . LYS B 150 ? 0.11367 0.11384 0.09682 0.00701  0.01915  0.00407  214 LYS B CB    
2457 C CG    . LYS B 150 ? 0.14991 0.15434 0.13020 0.01230  0.01596  0.00533  214 LYS B CG    
2458 C CD    . LYS B 150 ? 0.15679 0.17173 0.14245 0.00838  0.01377  0.00274  214 LYS B CD    
2459 C CE    . LYS B 150 ? 0.10989 0.13207 0.09296 0.01414  0.00916  0.00407  214 LYS B CE    
2460 N NZ    . LYS B 150 ? 0.17106 0.17940 0.13684 0.01867  0.00746  0.00769  214 LYS B NZ    
2461 N N     . HIS B 151 ? 0.21799 0.18711 0.16542 0.00465  0.01871  0.00747  215 HIS B N     
2462 C CA    . HIS B 151 ? 0.24684 0.19953 0.17674 0.00838  0.01818  0.01092  215 HIS B CA    
2463 C C     . HIS B 151 ? 0.28187 0.24041 0.21028 0.01619  0.01395  0.01321  215 HIS B C     
2464 O O     . HIS B 151 ? 0.22891 0.20294 0.16708 0.01476  0.01174  0.01123  215 HIS B O     
2465 C CB    . HIS B 151 ? 0.23499 0.17637 0.15280 -0.00005 0.02059  0.01077  215 HIS B CB    
2466 C CG    . HIS B 151 ? 0.27222 0.19132 0.16893 0.00194  0.02123  0.01467  215 HIS B CG    
2467 N ND1   . HIS B 151 ? 0.27365 0.18581 0.15758 0.00685  0.01873  0.01850  215 HIS B ND1   
2468 C CD2   . HIS B 151 ? 0.28757 0.18785 0.17196 -0.00078 0.02413  0.01535  215 HIS B CD2   
2469 C CE1   . HIS B 151 ? 0.23712 0.12529 0.10117 0.00787  0.02040  0.02204  215 HIS B CE1   
2470 N NE2   . HIS B 151 ? 0.29199 0.17205 0.15599 0.00276  0.02397  0.01981  215 HIS B NE2   
2471 N N     . ASN B 152 ? 0.26534 0.21131 0.18112 0.02476  0.01257  0.01714  216 ASN B N     
2472 C CA    . ASN B 152 ? 0.23928 0.19275 0.15405 0.03421  0.00746  0.01978  216 ASN B CA    
2473 C C     . ASN B 152 ? 0.25976 0.21601 0.16786 0.03005  0.00461  0.02019  216 ASN B C     
2474 O O     . ASN B 152 ? 0.29737 0.26908 0.21096 0.03440  -0.00052 0.02018  216 ASN B O     
2475 C CB    . ASN B 152 ? 0.28916 0.22445 0.18844 0.04534  0.00682  0.02444  216 ASN B CB    
2476 C CG    . ASN B 152 ? 0.29969 0.23880 0.20791 0.05323  0.00855  0.02356  216 ASN B CG    
2477 O OD1   . ASN B 152 ? 0.25916 0.21826 0.18603 0.05184  0.00906  0.02037  216 ASN B OD1   
2478 N ND2   . ASN B 152 ? 0.29404 0.21232 0.18748 0.06136  0.01013  0.02629  216 ASN B ND2   
2479 N N     . ASN B 153 ? 0.24244 0.18564 0.13901 0.02094  0.00801  0.01999  217 ASN B N     
2480 C CA    . ASN B 153 ? 0.25176 0.19398 0.13756 0.01669  0.00660  0.02064  217 ASN B CA    
2481 C C     . ASN B 153 ? 0.27079 0.22833 0.16895 0.00698  0.00844  0.01481  217 ASN B C     
2482 O O     . ASN B 153 ? 0.27704 0.23156 0.16508 0.00111  0.00957  0.01424  217 ASN B O     
2483 C CB    . ASN B 153 ? 0.27434 0.19162 0.13748 0.01206  0.01046  0.02415  217 ASN B CB    
2484 C CG    . ASN B 153 ? 0.34457 0.24107 0.19014 0.02201  0.00880  0.03041  217 ASN B CG    
2485 O OD1   . ASN B 153 ? 0.38162 0.28437 0.23087 0.03434  0.00373  0.03268  217 ASN B OD1   
2486 N ND2   . ASN B 153 ? 0.32774 0.20189 0.15779 0.01638  0.01302  0.03214  217 ASN B ND2   
2487 N N     . ASP B 154 ? 0.19046 0.16259 0.10857 0.00533  0.00934  0.01057  218 ASP B N     
2488 C CA    . ASP B 154 ? 0.16260 0.14474 0.09076 -0.00314 0.01207  0.00509  218 ASP B CA    
2489 C C     . ASP B 154 ? 0.16369 0.16080 0.11194 -0.00228 0.01149  0.00177  218 ASP B C     
2490 O O     . ASP B 154 ? 0.17762 0.17690 0.13232 0.00322  0.01049  0.00356  218 ASP B O     
2491 C CB    . ASP B 154 ? 0.19240 0.16547 0.11736 -0.01078 0.01804  0.00385  218 ASP B CB    
2492 C CG    . ASP B 154 ? 0.24688 0.22776 0.17667 -0.01842 0.02141  -0.00134 218 ASP B CG    
2493 O OD1   . ASP B 154 ? 0.22784 0.21944 0.16368 -0.01852 0.01953  -0.00474 218 ASP B OD1   
2494 O OD2   . ASP B 154 ? 0.18726 0.16379 0.11475 -0.02465 0.02633  -0.00258 218 ASP B OD2   
2495 N N     . THR B 155 ? 0.16845 0.17435 0.12537 -0.00794 0.01291  -0.00319 219 THR B N     
2496 C CA    . THR B 155 ? 0.11982 0.13631 0.09366 -0.00838 0.01326  -0.00612 219 THR B CA    
2497 C C     . THR B 155 ? 0.16029 0.17244 0.14080 -0.00950 0.01726  -0.00592 219 THR B C     
2498 O O     . THR B 155 ? 0.17982 0.18355 0.15387 -0.01153 0.01980  -0.00499 219 THR B O     
2499 C CB    . THR B 155 ? 0.18439 0.20844 0.16325 -0.01379 0.01360  -0.01179 219 THR B CB    
2500 O OG1   . THR B 155 ? 0.15141 0.16943 0.12427 -0.01852 0.01766  -0.01419 219 THR B OG1   
2501 C CG2   . THR B 155 ? 0.14258 0.17447 0.11634 -0.01269 0.00811  -0.01241 219 THR B CG2   
2502 N N     . GLN B 156 ? 0.17404 0.19241 0.16687 -0.00850 0.01763  -0.00660 220 GLN B N     
2503 C CA    . GLN B 156 ? 0.12656 0.14181 0.12525 -0.00899 0.02055  -0.00615 220 GLN B CA    
2504 C C     . GLN B 156 ? 0.16674 0.18163 0.16880 -0.01331 0.02336  -0.00964 220 GLN B C     
2505 O O     . GLN B 156 ? 0.16980 0.18835 0.17524 -0.01592 0.02397  -0.01346 220 GLN B O     
2506 C CB    . GLN B 156 ? 0.15267 0.17353 0.16168 -0.00732 0.02079  -0.00561 220 GLN B CB    
2507 C CG    . GLN B 156 ? 0.11117 0.12749 0.12208 -0.00585 0.02276  -0.00333 220 GLN B CG    
2508 C CD    . GLN B 156 ? 0.18220 0.20276 0.19967 -0.00397 0.02366  -0.00174 220 GLN B CD    
2509 O OE1   . GLN B 156 ? 0.18122 0.20580 0.19800 -0.00045 0.02277  -0.00025 220 GLN B OE1   
2510 N NE2   . GLN B 156 ? 0.10626 0.12562 0.12955 -0.00576 0.02583  -0.00174 220 GLN B NE2   
2511 N N     . HIS B 157 ? 0.17437 0.18559 0.17582 -0.01390 0.02508  -0.00882 221 HIS B N     
2512 C CA    . HIS B 157 ? 0.19627 0.20982 0.20246 -0.01661 0.02778  -0.01206 221 HIS B CA    
2513 C C     . HIS B 157 ? 0.20560 0.22003 0.21874 -0.01470 0.02801  -0.01076 221 HIS B C     
2514 O O     . HIS B 157 ? 0.18575 0.19719 0.19642 -0.01280 0.02651  -0.00748 221 HIS B O     
2515 C CB    . HIS B 157 ? 0.17639 0.18821 0.17430 -0.02063 0.02960  -0.01312 221 HIS B CB    
2516 C CG    . HIS B 157 ? 0.17085 0.18235 0.16140 -0.02290 0.03004  -0.01516 221 HIS B CG    
2517 N ND1   . HIS B 157 ? 0.19354 0.20010 0.17267 -0.02188 0.02734  -0.01228 221 HIS B ND1   
2518 C CD2   . HIS B 157 ? 0.13980 0.15512 0.13177 -0.02545 0.03261  -0.01987 221 HIS B CD2   
2519 C CE1   . HIS B 157 ? 0.21030 0.21825 0.18350 -0.02421 0.02761  -0.01479 221 HIS B CE1   
2520 N NE2   . HIS B 157 ? 0.18943 0.20236 0.16993 -0.02689 0.03116  -0.01979 221 HIS B NE2   
2521 N N     . ILE B 158 ? 0.15247 0.17098 0.17355 -0.01453 0.02985  -0.01352 222 ILE B N     
2522 C CA    . ILE B 158 ? 0.14066 0.16155 0.16840 -0.01169 0.02930  -0.01227 222 ILE B CA    
2523 C C     . ILE B 158 ? 0.19418 0.22260 0.22554 -0.01352 0.03085  -0.01517 222 ILE B C     
2524 O O     . ILE B 158 ? 0.16447 0.19657 0.19897 -0.01447 0.03388  -0.01925 222 ILE B O     
2525 C CB    . ILE B 158 ? 0.13565 0.15456 0.17060 -0.00794 0.02994  -0.01236 222 ILE B CB    
2526 C CG1   . ILE B 158 ? 0.16660 0.18028 0.19914 -0.00793 0.02922  -0.00984 222 ILE B CG1   
2527 C CG2   . ILE B 158 ? 0.12938 0.15052 0.16971 -0.00359 0.02865  -0.01032 222 ILE B CG2   
2528 C CD1   . ILE B 158 ? 0.10828 0.11715 0.14583 -0.00675 0.03095  -0.01037 222 ILE B CD1   
2529 N N     . TRP B 159 ? 0.17720 0.20893 0.20818 -0.01449 0.02906  -0.01365 223 TRP B N     
2530 C CA    . TRP B 159 ? 0.16045 0.20340 0.19769 -0.01666 0.02998  -0.01644 223 TRP B CA    
2531 C C     . TRP B 159 ? 0.17445 0.22420 0.22109 -0.01077 0.02701  -0.01518 223 TRP B C     
2532 O O     . TRP B 159 ? 0.18525 0.22995 0.22829 -0.00834 0.02361  -0.01132 223 TRP B O     
2533 C CB    . TRP B 159 ? 0.15797 0.19952 0.18646 -0.02377 0.02973  -0.01611 223 TRP B CB    
2534 C CG    . TRP B 159 ? 0.19867 0.25317 0.23303 -0.02869 0.03025  -0.01897 223 TRP B CG    
2535 C CD1   . TRP B 159 ? 0.22024 0.28005 0.25347 -0.03624 0.03447  -0.02229 223 TRP B CD1   
2536 C CD2   . TRP B 159 ? 0.21143 0.27603 0.25273 -0.02754 0.02629  -0.01878 223 TRP B CD2   
2537 N NE1   . TRP B 159 ? 0.20138 0.27572 0.24250 -0.04044 0.03373  -0.02468 223 TRP B NE1   
2538 C CE2   . TRP B 159 ? 0.21877 0.29707 0.26525 -0.03484 0.02812  -0.02270 223 TRP B CE2   
2539 C CE3   . TRP B 159 ? 0.21376 0.27796 0.25693 -0.02132 0.02138  -0.01566 223 TRP B CE3   
2540 C CZ2   . TRP B 159 ? 0.25332 0.34702 0.30829 -0.03602 0.02428  -0.02407 223 TRP B CZ2   
2541 C CZ3   . TRP B 159 ? 0.22273 0.30019 0.27210 -0.02175 0.01731  -0.01645 223 TRP B CZ3   
2542 C CH2   . TRP B 159 ? 0.19394 0.28700 0.24987 -0.02903 0.01834  -0.02085 223 TRP B CH2   
2543 N N     . GLU B 160 ? 0.21980 0.28075 0.27770 -0.00758 0.02837  -0.01826 224 GLU B N     
2544 C CA    . GLU B 160 ? 0.21877 0.28688 0.28560 -0.00014 0.02493  -0.01665 224 GLU B CA    
2545 C C     . GLU B 160 ? 0.24249 0.33059 0.32056 -0.00085 0.02479  -0.02034 224 GLU B C     
2546 O O     . GLU B 160 ? 0.26651 0.36240 0.34876 -0.00467 0.02959  -0.02508 224 GLU B O     
2547 C CB    . GLU B 160 ? 0.26380 0.32408 0.33449 0.00800  0.02646  -0.01612 224 GLU B CB    
2548 C CG    . GLU B 160 ? 0.28195 0.34848 0.36160 0.01104  0.03124  -0.02166 224 GLU B CG    
2549 C CD    . GLU B 160 ? 0.35722 0.44056 0.45052 0.01819  0.03008  -0.02335 224 GLU B CD    
2550 O OE1   . GLU B 160 ? 0.34593 0.43074 0.44186 0.02507  0.02498  -0.01911 224 GLU B OE1   
2551 O OE2   . GLU B 160 ? 0.36651 0.46257 0.46783 0.01730  0.03443  -0.02900 224 GLU B OE2   
2552 N N     . SER B 161 ? 0.31797 0.41581 0.40079 0.00245  0.01930  -0.01834 225 SER B N     
2553 C CA    . SER B 161 ? 0.29523 0.41648 0.39154 0.00231  0.01828  -0.02211 225 SER B CA    
2554 C C     . SER B 161 ? 0.30638 0.43731 0.40837 0.01017  0.01077  -0.01892 225 SER B C     
2555 O O     . SER B 161 ? 0.31139 0.43079 0.40318 0.01166  0.00626  -0.01393 225 SER B O     
2556 C CB    . SER B 161 ? 0.29112 0.42016 0.38427 -0.01074 0.01962  -0.02533 225 SER B CB    
2557 O OG    . SER B 161 ? 0.33693 0.48975 0.44326 -0.01173 0.01766  -0.02860 225 SER B OG    
2558 N N     . ASP B 162 ? 0.43122 0.58482 0.54945 0.01541  0.00954  -0.02196 226 ASP B N     
2559 C CA    . ASP B 162 ? 0.43374 0.60308 0.55950 0.02280  0.00133  -0.01968 226 ASP B CA    
2560 C C     . ASP B 162 ? 0.41444 0.60668 0.54767 0.01407  -0.00137 -0.02372 226 ASP B C     
2561 O O     . ASP B 162 ? 0.45986 0.66710 0.60064 0.01977  -0.00806 -0.02262 226 ASP B O     
2562 C CB    . ASP B 162 ? 0.39374 0.56613 0.53024 0.03873  0.00094  -0.01830 226 ASP B CB    
2563 C CG    . ASP B 162 ? 0.39697 0.57907 0.54436 0.03858  0.00650  -0.02285 226 ASP B CG    
2564 O OD1   . ASP B 162 ? 0.39427 0.58422 0.54217 0.02676  0.01030  -0.02714 226 ASP B OD1   
2565 O OD2   . ASP B 162 ? 0.40543 0.58563 0.55954 0.05079  0.00743  -0.02175 226 ASP B OD2   
2566 N N     . SER B 163 ? 0.39416 0.58403 0.52184 -0.00000 0.00366  -0.02748 227 SER B N     
2567 C CA    . SER B 163 ? 0.41287 0.61556 0.54250 -0.01130 0.00377  -0.03144 227 SER B CA    
2568 C C     . SER B 163 ? 0.47539 0.69007 0.61668 -0.00952 0.00862  -0.03479 227 SER B C     
2569 O O     . SER B 163 ? 0.49016 0.71528 0.63313 -0.01937 0.01011  -0.03839 227 SER B O     
2570 C CB    . SER B 163 ? 0.39460 0.61250 0.52672 -0.01255 -0.00539 -0.03111 227 SER B CB    
2571 N N     . ASN B 164 ? 0.38367 0.59618 0.53193 0.00196  0.01181  -0.03405 228 ASN B N     
2572 C CA    . ASN B 164 ? 0.41044 0.63408 0.56891 0.00355  0.01726  -0.03757 228 ASN B CA    
2573 C C     . ASN B 164 ? 0.42441 0.63363 0.57320 -0.00338 0.02614  -0.03982 228 ASN B C     
2574 O O     . ASN B 164 ? 0.48523 0.70002 0.63264 -0.01323 0.03037  -0.04322 228 ASN B O     
2575 C CB    . ASN B 164 ? 0.46244 0.69107 0.63295 0.02028  0.01611  -0.03587 228 ASN B CB    
2576 C CG    . ASN B 164 ? 0.49727 0.74284 0.67789 0.02800  0.00679  -0.03359 228 ASN B CG    
2577 O OD1   . ASN B 164 ? 0.47025 0.73234 0.65434 0.02025  0.00257  -0.03542 228 ASN B OD1   
2578 N ND2   . ASN B 164 ? 0.55214 0.79206 0.73598 0.04325  0.00344  -0.02949 228 ASN B ND2   
2579 N N     . GLU B 165 ? 0.45992 0.65045 0.60112 0.00159  0.02877  -0.03797 229 GLU B N     
2580 C CA    . GLU B 165 ? 0.46683 0.64088 0.59538 -0.00496 0.03533  -0.03937 229 GLU B CA    
2581 C C     . GLU B 165 ? 0.44301 0.59802 0.55866 -0.00721 0.03349  -0.03614 229 GLU B C     
2582 O O     . GLU B 165 ? 0.40103 0.55682 0.51756 -0.00486 0.02786  -0.03329 229 GLU B O     
2583 C CB    . GLU B 165 ? 0.44788 0.61896 0.57995 0.00312  0.04096  -0.04148 229 GLU B CB    
2584 C CG    . GLU B 165 ? 0.51846 0.69127 0.66071 0.01839  0.03874  -0.03973 229 GLU B CG    
2585 C CD    . GLU B 165 ? 0.70295 0.87886 0.85158 0.02606  0.04481  -0.04302 229 GLU B CD    
2586 O OE1   . GLU B 165 ? 0.68857 0.88340 0.85061 0.03004  0.04508  -0.04457 229 GLU B OE1   
2587 O OE2   . GLU B 165 ? 0.73171 0.89146 0.87185 0.02807  0.04932  -0.04448 229 GLU B OE2   
2588 N N     . PHE B 166 ? 0.34348 0.48228 0.44691 -0.01168 0.03807  -0.03665 230 PHE B N     
2589 C CA    . PHE B 166 ? 0.21613 0.33746 0.30841 -0.01284 0.03699  -0.03376 230 PHE B CA    
2590 C C     . PHE B 166 ? 0.27766 0.38487 0.36127 -0.01292 0.04171  -0.03513 230 PHE B C     
2591 O O     . PHE B 166 ? 0.26658 0.37637 0.34953 -0.01481 0.04592  -0.03836 230 PHE B O     
2592 C CB    . PHE B 166 ? 0.28113 0.39730 0.36269 -0.02321 0.03513  -0.03209 230 PHE B CB    
2593 C CG    . PHE B 166 ? 0.26687 0.37580 0.33658 -0.03292 0.03920  -0.03354 230 PHE B CG    
2594 C CD1   . PHE B 166 ? 0.31787 0.43784 0.39028 -0.03927 0.04064  -0.03621 230 PHE B CD1   
2595 C CD2   . PHE B 166 ? 0.26826 0.35965 0.32384 -0.03556 0.04133  -0.03213 230 PHE B CD2   
2596 C CE1   . PHE B 166 ? 0.30854 0.42058 0.36892 -0.04815 0.04471  -0.03735 230 PHE B CE1   
2597 C CE2   . PHE B 166 ? 0.26823 0.35228 0.31171 -0.04352 0.04458  -0.03292 230 PHE B CE2   
2598 C CZ    . PHE B 166 ? 0.26780 0.36127 0.31321 -0.04992 0.04653  -0.03546 230 PHE B CZ    
2599 N N     . SER B 167 ? 0.28660 0.37974 0.36366 -0.01115 0.04094  -0.03298 231 SER B N     
2600 C CA    . SER B 167 ? 0.26036 0.34049 0.32799 -0.01262 0.04425  -0.03444 231 SER B CA    
2601 C C     . SER B 167 ? 0.22119 0.28858 0.27749 -0.01674 0.04258  -0.03111 231 SER B C     
2602 O O     . SER B 167 ? 0.22078 0.28727 0.27730 -0.01649 0.03928  -0.02767 231 SER B O     
2603 C CB    . SER B 167 ? 0.29731 0.37354 0.37082 -0.00409 0.04608  -0.03669 231 SER B CB    
2604 O OG    . SER B 167 ? 0.27412 0.34501 0.35171 0.00187  0.04341  -0.03378 231 SER B OG    
2605 N N     . VAL B 168 ? 0.18783 0.24594 0.23351 -0.02036 0.04461  -0.03213 232 VAL B N     
2606 C CA    . VAL B 168 ? 0.17411 0.22138 0.20900 -0.02321 0.04314  -0.02905 232 VAL B CA    
2607 C C     . VAL B 168 ? 0.19218 0.23288 0.22380 -0.02186 0.04458  -0.03145 232 VAL B C     
2608 O O     . VAL B 168 ? 0.16732 0.20837 0.19510 -0.02397 0.04745  -0.03529 232 VAL B O     
2609 C CB    . VAL B 168 ? 0.15379 0.19669 0.17567 -0.03043 0.04336  -0.02732 232 VAL B CB    
2610 C CG1   . VAL B 168 ? 0.20136 0.23261 0.21145 -0.03087 0.04124  -0.02386 232 VAL B CG1   
2611 C CG2   . VAL B 168 ? 0.13708 0.18431 0.16050 -0.03361 0.04188  -0.02557 232 VAL B CG2   
2612 N N     . ILE B 169 ? 0.12668 0.15998 0.15798 -0.01869 0.04105  -0.02868 233 ILE B N     
2613 C CA    . ILE B 169 ? 0.14515 0.17280 0.17390 -0.01868 0.04153  -0.03135 233 ILE B CA    
2614 C C     . ILE B 169 ? 0.15481 0.17743 0.17617 -0.02015 0.03742  -0.02761 233 ILE B C     
2615 O O     . ILE B 169 ? 0.16339 0.18479 0.18371 -0.01892 0.03457  -0.02274 233 ILE B O     
2616 C CB    . ILE B 169 ? 0.21246 0.23676 0.25029 -0.01366 0.04246  -0.03300 233 ILE B CB    
2617 C CG1   . ILE B 169 ? 0.12702 0.14742 0.16785 -0.01047 0.03882  -0.02723 233 ILE B CG1   
2618 C CG2   . ILE B 169 ? 0.18113 0.21152 0.22753 -0.00968 0.04634  -0.03675 233 ILE B CG2   
2619 C CD1   . ILE B 169 ? 0.18667 0.19919 0.23289 -0.00630 0.03993  -0.02765 233 ILE B CD1   
2620 N N     . ALA B 170 ? 0.18282 0.20356 0.19919 -0.02253 0.03710  -0.03043 234 ALA B N     
2621 C CA    . ALA B 170 ? 0.17830 0.19789 0.19159 -0.02278 0.03288  -0.02758 234 ALA B CA    
2622 C C     . ALA B 170 ? 0.18673 0.20442 0.20893 -0.02031 0.03223  -0.02569 234 ALA B C     
2623 O O     . ALA B 170 ? 0.18360 0.19797 0.21166 -0.01972 0.03476  -0.02854 234 ALA B O     
2624 C CB    . ALA B 170 ? 0.22715 0.24781 0.23451 -0.02634 0.03191  -0.03179 234 ALA B CB    
2625 N N     . ASP B 171 ? 0.15805 0.17640 0.18008 -0.01860 0.02947  -0.02081 235 ASP B N     
2626 C CA    . ASP B 171 ? 0.15060 0.16688 0.17944 -0.01695 0.02971  -0.01849 235 ASP B CA    
2627 C C     . ASP B 171 ? 0.16580 0.18230 0.19773 -0.02066 0.03010  -0.02185 235 ASP B C     
2628 O O     . ASP B 171 ? 0.17687 0.19960 0.20715 -0.02279 0.02748  -0.02233 235 ASP B O     
2629 C CB    . ASP B 171 ? 0.16830 0.18593 0.19539 -0.01442 0.02760  -0.01322 235 ASP B CB    
2630 C CG    . ASP B 171 ? 0.21298 0.22787 0.24505 -0.01282 0.02876  -0.01019 235 ASP B CG    
2631 O OD1   . ASP B 171 ? 0.14970 0.16102 0.18628 -0.01443 0.03082  -0.01175 235 ASP B OD1   
2632 O OD2   . ASP B 171 ? 0.20909 0.22361 0.23877 -0.01009 0.02799  -0.00623 235 ASP B OD2   
2633 N N     . PRO B 172 ? 0.16391 0.17364 0.20004 -0.02153 0.03310  -0.02428 236 PRO B N     
2634 C CA    . PRO B 172 ? 0.13335 0.14133 0.17142 -0.02705 0.03396  -0.02817 236 PRO B CA    
2635 C C     . PRO B 172 ? 0.15127 0.16437 0.19302 -0.02935 0.03275  -0.02497 236 PRO B C     
2636 O O     . PRO B 172 ? 0.16615 0.18291 0.21016 -0.03551 0.03250  -0.02853 236 PRO B O     
2637 C CB    . PRO B 172 ? 0.17141 0.16651 0.21157 -0.02597 0.03816  -0.03001 236 PRO B CB    
2638 C CG    . PRO B 172 ? 0.16289 0.15612 0.20458 -0.01898 0.03817  -0.02430 236 PRO B CG    
2639 C CD    . PRO B 172 ? 0.14574 0.14852 0.18481 -0.01720 0.03561  -0.02325 236 PRO B CD    
2640 N N     . ARG B 173 ? 0.14887 0.16355 0.19139 -0.02514 0.03225  -0.01899 237 ARG B N     
2641 C CA    . ARG B 173 ? 0.18243 0.20372 0.22879 -0.02678 0.03216  -0.01627 237 ARG B CA    
2642 C C     . ARG B 173 ? 0.18918 0.22415 0.23538 -0.02586 0.02819  -0.01637 237 ARG B C     
2643 O O     . ARG B 173 ? 0.20157 0.24568 0.25266 -0.02642 0.02811  -0.01481 237 ARG B O     
2644 C CB    . ARG B 173 ? 0.14034 0.15688 0.18583 -0.02227 0.03379  -0.01021 237 ARG B CB    
2645 C CG    . ARG B 173 ? 0.19092 0.19399 0.23530 -0.02106 0.03657  -0.00890 237 ARG B CG    
2646 C CD    . ARG B 173 ? 0.20939 0.20912 0.25039 -0.01549 0.03639  -0.00310 237 ARG B CD    
2647 N NE    . ARG B 173 ? 0.16128 0.16494 0.19927 -0.01140 0.03331  -0.00306 237 ARG B NE    
2648 C CZ    . ARG B 173 ? 0.12834 0.13007 0.16280 -0.00723 0.03215  0.00046  237 ARG B CZ    
2649 N NH1   . ARG B 173 ? 0.14459 0.14064 0.17706 -0.00540 0.03332  0.00470  237 ARG B NH1   
2650 N NH2   . ARG B 173 ? 0.14124 0.14644 0.17299 -0.00562 0.02981  -0.00038 237 ARG B NH2   
2651 N N     . GLY B 174 ? 0.20323 0.23987 0.24359 -0.02396 0.02520  -0.01787 238 GLY B N     
2652 C CA    . GLY B 174 ? 0.20062 0.24771 0.23864 -0.02133 0.02096  -0.01686 238 GLY B CA    
2653 C C     . GLY B 174 ? 0.17823 0.22417 0.21330 -0.01451 0.02069  -0.01137 238 GLY B C     
2654 O O     . GLY B 174 ? 0.20372 0.24049 0.23602 -0.01235 0.02293  -0.00882 238 GLY B O     
2655 N N     . ASN B 175 ? 0.21299 0.26864 0.24826 -0.01068 0.01763  -0.00989 239 ASN B N     
2656 C CA    . ASN B 175 ? 0.15636 0.20936 0.18687 -0.00325 0.01744  -0.00539 239 ASN B CA    
2657 C C     . ASN B 175 ? 0.16974 0.22618 0.20758 -0.00235 0.02107  -0.00357 239 ASN B C     
2658 O O     . ASN B 175 ? 0.18353 0.25308 0.22855 -0.00047 0.02082  -0.00352 239 ASN B O     
2659 C CB    . ASN B 175 ? 0.16586 0.22656 0.19262 0.00237  0.01274  -0.00438 239 ASN B CB    
2660 C CG    . ASN B 175 ? 0.15237 0.20795 0.17318 0.01109  0.01306  -0.00017 239 ASN B CG    
2661 O OD1   . ASN B 175 ? 0.16297 0.20814 0.18047 0.01189  0.01656  0.00157  239 ASN B OD1   
2662 N ND2   . ASN B 175 ? 0.18133 0.24371 0.19977 0.01819  0.00910  0.00133  239 ASN B ND2   
2663 N N     . THR B 176 ? 0.13207 0.17793 0.16799 -0.00351 0.02452  -0.00203 240 THR B N     
2664 C CA    . THR B 176 ? 0.10401 0.15062 0.14306 -0.00241 0.02835  0.00041  240 THR B CA    
2665 C C     . THR B 176 ? 0.11279 0.15349 0.14358 0.00443  0.02881  0.00336  240 THR B C     
2666 O O     . THR B 176 ? 0.17237 0.21682 0.20490 0.00705  0.03187  0.00487  240 THR B O     
2667 C CB    . THR B 176 ? 0.11778 0.15560 0.15770 -0.00694 0.03155  0.00101  240 THR B CB    
2668 O OG1   . THR B 176 ? 0.15489 0.18151 0.18715 -0.00494 0.03055  0.00220  240 THR B OG1   
2669 C CG2   . THR B 176 ? 0.13360 0.17286 0.17967 -0.01375 0.03188  -0.00252 240 THR B CG2   
2670 N N     . LEU B 177 ? 0.14480 0.17580 0.16589 0.00670  0.02653  0.00380  241 LEU B N     
2671 C CA    . LEU B 177 ? 0.15383 0.17631 0.16535 0.01194  0.02732  0.00583  241 LEU B CA    
2672 C C     . LEU B 177 ? 0.16676 0.19267 0.17566 0.01917  0.02608  0.00643  241 LEU B C     
2673 O O     . LEU B 177 ? 0.14607 0.16698 0.14916 0.02473  0.02812  0.00761  241 LEU B O     
2674 C CB    . LEU B 177 ? 0.16737 0.17715 0.16894 0.01005  0.02596  0.00577  241 LEU B CB    
2675 C CG    . LEU B 177 ? 0.14114 0.14788 0.14454 0.00494  0.02629  0.00519  241 LEU B CG    
2676 C CD1   . LEU B 177 ? 0.15738 0.15688 0.15320 0.00267  0.02469  0.00419  241 LEU B CD1   
2677 C CD2   . LEU B 177 ? 0.17834 0.18204 0.18002 0.00574  0.02827  0.00701  241 LEU B CD2   
2678 N N     . GLY B 178 ? 0.17458 0.20810 0.18633 0.01998  0.02260  0.00558  242 GLY B N     
2679 C CA    . GLY B 178 ? 0.21574 0.25166 0.22362 0.02861  0.02023  0.00687  242 GLY B CA    
2680 C C     . GLY B 178 ? 0.27235 0.28998 0.26363 0.03144  0.01859  0.00863  242 GLY B C     
2681 O O     . GLY B 178 ? 0.21911 0.23559 0.20463 0.03388  0.01481  0.00956  242 GLY B O     
2682 N N     . ARG B 179 ? 0.16584 0.16854 0.14815 0.03041  0.02149  0.00910  243 ARG B N     
2683 C CA    . ARG B 179 ? 0.16624 0.14982 0.13268 0.02918  0.02115  0.00998  243 ARG B CA    
2684 C C     . ARG B 179 ? 0.15850 0.13302 0.12097 0.02491  0.02417  0.00898  243 ARG B C     
2685 O O     . ARG B 179 ? 0.17300 0.15075 0.13889 0.02758  0.02664  0.00875  243 ARG B O     
2686 C CB    . ARG B 179 ? 0.16621 0.13862 0.12033 0.03875  0.02025  0.01236  243 ARG B CB    
2687 C CG    . ARG B 179 ? 0.15716 0.10565 0.09208 0.03643  0.02088  0.01345  243 ARG B CG    
2688 C CD    . ARG B 179 ? 0.17587 0.10772 0.09644 0.04690  0.02149  0.01572  243 ARG B CD    
2689 N NE    . ARG B 179 ? 0.16882 0.09675 0.08888 0.05110  0.02524  0.01411  243 ARG B NE    
2690 C CZ    . ARG B 179 ? 0.20453 0.14532 0.13405 0.06045  0.02629  0.01394  243 ARG B CZ    
2691 N NH1   . ARG B 179 ? 0.22426 0.18366 0.16543 0.06676  0.02320  0.01525  243 ARG B NH1   
2692 N NH2   . ARG B 179 ? 0.24912 0.18548 0.17647 0.06303  0.03068  0.01200  243 ARG B NH2   
2693 N N     . GLY B 180 ? 0.22962 0.19458 0.18508 0.01788  0.02399  0.00818  244 GLY B N     
2694 C CA    . GLY B 180 ? 0.17764 0.13577 0.12897 0.01335  0.02558  0.00687  244 GLY B CA    
2695 C C     . GLY B 180 ? 0.15125 0.11732 0.11091 0.00564  0.02487  0.00535  244 GLY B C     
2696 O O     . GLY B 180 ? 0.16842 0.14104 0.13392 0.00280  0.02390  0.00479  244 GLY B O     
2697 N N     . THR B 181 ? 0.20279 0.16878 0.16272 0.00298  0.02522  0.00453  245 THR B N     
2698 C CA    . THR B 181 ? 0.19727 0.17009 0.16391 -0.00298 0.02403  0.00315  245 THR B CA    
2699 C C     . THR B 181 ? 0.17374 0.15136 0.14458 -0.00184 0.02376  0.00390  245 THR B C     
2700 O O     . THR B 181 ? 0.18944 0.16079 0.15215 0.00014  0.02449  0.00426  245 THR B O     
2701 C CB    . THR B 181 ? 0.20125 0.16666 0.15916 -0.00942 0.02362  0.00117  245 THR B CB    
2702 O OG1   . THR B 181 ? 0.17490 0.13337 0.12635 -0.01091 0.02451  0.00128  245 THR B OG1   
2703 C CG2   . THR B 181 ? 0.15694 0.13344 0.12415 -0.01452 0.02223  -0.00062 245 THR B CG2   
2704 N N     . THR B 182 ? 0.15342 0.14038 0.13504 -0.00279 0.02295  0.00415  246 THR B N     
2705 C CA    . THR B 182 ? 0.15433 0.14422 0.13795 -0.00189 0.02200  0.00561  246 THR B CA    
2706 C C     . THR B 182 ? 0.17135 0.16706 0.15908 -0.00516 0.01916  0.00410  246 THR B C     
2707 O O     . THR B 182 ? 0.17868 0.18018 0.17463 -0.00652 0.01927  0.00262  246 THR B O     
2708 C CB    . THR B 182 ? 0.15623 0.15032 0.14806 0.00086  0.02366  0.00787  246 THR B CB    
2709 O OG1   . THR B 182 ? 0.19756 0.19023 0.18759 0.00346  0.02645  0.00883  246 THR B OG1   
2710 C CG2   . THR B 182 ? 0.15636 0.15062 0.14744 0.00220  0.02263  0.01046  246 THR B CG2   
2711 N N     . ILE B 183 ? 0.17929 0.17469 0.16127 -0.00640 0.01665  0.00395  247 ILE B N     
2712 C CA    . ILE B 183 ? 0.16565 0.17069 0.15331 -0.00849 0.01301  0.00267  247 ILE B CA    
2713 C C     . ILE B 183 ? 0.19354 0.20176 0.18426 -0.00321 0.01106  0.00630  247 ILE B C     
2714 O O     . ILE B 183 ? 0.22515 0.22868 0.20664 -0.00173 0.01009  0.00839  247 ILE B O     
2715 C CB    . ILE B 183 ? 0.17624 0.18042 0.15521 -0.01417 0.01047  -0.00020 247 ILE B CB    
2716 C CG1   . ILE B 183 ? 0.17790 0.17173 0.14811 -0.01931 0.01333  -0.00280 247 ILE B CG1   
2717 C CG2   . ILE B 183 ? 0.18572 0.20509 0.17394 -0.01661 0.00631  -0.00212 247 ILE B CG2   
2718 C CD1   . ILE B 183 ? 0.15551 0.15360 0.13264 -0.02304 0.01527  -0.00463 247 ILE B CD1   
2719 N N     . THR B 184 ? 0.13797 0.15236 0.13979 -0.00011 0.01085  0.00716  248 THR B N     
2720 C CA    . THR B 184 ? 0.11260 0.12683 0.11602 0.00561  0.00924  0.01134  248 THR B CA    
2721 C C     . THR B 184 ? 0.15438 0.18040 0.16400 0.00771  0.00399  0.01074  248 THR B C     
2722 O O     . THR B 184 ? 0.15150 0.18704 0.17169 0.00683  0.00400  0.00729  248 THR B O     
2723 C CB    . THR B 184 ? 0.12686 0.13667 0.13705 0.00838  0.01308  0.01277  248 THR B CB    
2724 O OG1   . THR B 184 ? 0.14435 0.14710 0.15017 0.00625  0.01722  0.01313  248 THR B OG1   
2725 C CG2   . THR B 184 ? 0.11864 0.12427 0.12843 0.01422  0.01201  0.01765  248 THR B CG2   
2726 N N     . LEU B 185 ? 0.15751 0.18424 0.16045 0.01071  -0.00048 0.01395  249 LEU B N     
2727 C CA    . LEU B 185 ? 0.14618 0.18669 0.15481 0.01388  -0.00696 0.01386  249 LEU B CA    
2728 C C     . LEU B 185 ? 0.15482 0.19175 0.16501 0.02347  -0.00850 0.01967  249 LEU B C     
2729 O O     . LEU B 185 ? 0.21271 0.23738 0.21134 0.02599  -0.00783 0.02494  249 LEU B O     
2730 C CB    . LEU B 185 ? 0.21672 0.26146 0.21487 0.01007  -0.01234 0.01293  249 LEU B CB    
2731 C CG    . LEU B 185 ? 0.25902 0.30591 0.25372 -0.00004 -0.01160 0.00677  249 LEU B CG    
2732 C CD1   . LEU B 185 ? 0.22583 0.25529 0.20808 -0.00342 -0.00589 0.00663  249 LEU B CD1   
2733 C CD2   . LEU B 185 ? 0.26834 0.32561 0.25774 -0.00371 -0.01876 0.00456  249 LEU B CD2   
2734 N N     . VAL B 186 ? 0.16902 0.21544 0.19248 0.02900  -0.00991 0.01879  250 VAL B N     
2735 C CA    . VAL B 186 ? 0.22659 0.26996 0.25090 0.03980  -0.01279 0.02439  250 VAL B CA    
2736 C C     . VAL B 186 ? 0.22265 0.28153 0.24616 0.04328  -0.02199 0.02552  250 VAL B C     
2737 O O     . VAL B 186 ? 0.26885 0.34817 0.30541 0.04370  -0.02578 0.02113  250 VAL B O     
2738 C CB    . VAL B 186 ? 0.24553 0.29082 0.28382 0.04569  -0.00977 0.02248  250 VAL B CB    
2739 C CG1   . VAL B 186 ? 0.25045 0.28464 0.28573 0.05737  -0.01130 0.02918  250 VAL B CG1   
2740 C CG2   . VAL B 186 ? 0.20840 0.24345 0.24836 0.03944  -0.00162 0.01898  250 VAL B CG2   
2741 N N     . LEU B 187 ? 0.24014 0.29070 0.24819 0.04534  -0.02556 0.03118  251 LEU B N     
2742 C CA    . LEU B 187 ? 0.25975 0.32499 0.26361 0.04637  -0.03496 0.03154  251 LEU B CA    
2743 C C     . LEU B 187 ? 0.30801 0.38661 0.32172 0.05873  -0.04216 0.03462  251 LEU B C     
2744 O O     . LEU B 187 ? 0.25751 0.32466 0.27247 0.06874  -0.04016 0.03982  251 LEU B O     
2745 C CB    . LEU B 187 ? 0.25770 0.30881 0.23966 0.04505  -0.03612 0.03662  251 LEU B CB    
2746 C CG    . LEU B 187 ? 0.27129 0.31352 0.24427 0.03374  -0.03011 0.03236  251 LEU B CG    
2747 C CD1   . LEU B 187 ? 0.24679 0.27425 0.19824 0.03332  -0.02933 0.03717  251 LEU B CD1   
2748 C CD2   . LEU B 187 ? 0.26402 0.32180 0.24177 0.02471  -0.03323 0.02423  251 LEU B CD2   
2749 N N     . LYS B 188 ? 0.26483 0.36804 0.28571 0.05803  -0.05060 0.03105  252 LYS B N     
2750 C CA    . LYS B 188 ? 0.23890 0.35808 0.26827 0.07113  -0.05926 0.03445  252 LYS B CA    
2751 C C     . LYS B 188 ? 0.31158 0.41524 0.32119 0.08007  -0.06433 0.04441  252 LYS B C     
2752 O O     . LYS B 188 ? 0.30142 0.38821 0.29131 0.07385  -0.06231 0.04711  252 LYS B O     
2753 C CB    . LYS B 188 ? 0.24421 0.39625 0.28544 0.06668  -0.06783 0.02800  252 LYS B CB    
2754 C CG    . LYS B 188 ? 0.22611 0.39371 0.28598 0.05729  -0.06229 0.01862  252 LYS B CG    
2755 C CD    . LYS B 188 ? 0.30391 0.49662 0.36821 0.04541  -0.06834 0.01134  252 LYS B CD    
2756 C CE    . LYS B 188 ? 0.31321 0.53194 0.40138 0.04562  -0.06870 0.00535  252 LYS B CE    
2757 N NZ    . LYS B 188 ? 0.27675 0.49506 0.37720 0.04143  -0.05835 0.00057  252 LYS B NZ    
2758 N N     . GLU B 189 ? 0.38995 0.49587 0.40436 0.09268  -0.06930 0.04891  253 GLU B N     
2759 C CA    . GLU B 189 ? 0.39269 0.47911 0.38791 0.09888  -0.07257 0.05794  253 GLU B CA    
2760 C C     . GLU B 189 ? 0.42525 0.51765 0.40426 0.09247  -0.08012 0.05846  253 GLU B C     
2761 O O     . GLU B 189 ? 0.46676 0.53854 0.42396 0.09260  -0.07960 0.06524  253 GLU B O     
2762 C CB    . GLU B 189 ? 0.43771 0.52719 0.44237 0.11129  -0.07710 0.06109  253 GLU B CB    
2763 N N     . GLU B 190 ? 0.36575 0.48511 0.35435 0.08559  -0.08651 0.05085  254 GLU B N     
2764 C CA    . GLU B 190 ? 0.43922 0.56355 0.41193 0.07872  -0.09402 0.05013  254 GLU B CA    
2765 C C     . GLU B 190 ? 0.40373 0.52221 0.36329 0.06567  -0.08948 0.04561  254 GLU B C     
2766 O O     . GLU B 190 ? 0.41032 0.52834 0.35347 0.05872  -0.09403 0.04412  254 GLU B O     
2767 C CB    . GLU B 190 ? 0.41095 0.56574 0.39881 0.07696  -0.10389 0.04411  254 GLU B CB    
2768 C CG    . GLU B 190 ? 0.43643 0.61382 0.44238 0.06546  -0.10194 0.03306  254 GLU B CG    
2769 C CD    . GLU B 190 ? 0.46058 0.64709 0.49098 0.07021  -0.09584 0.03034  254 GLU B CD    
2770 O OE1   . GLU B 190 ? 0.43896 0.61212 0.47179 0.08268  -0.09263 0.03660  254 GLU B OE1   
2771 O OE2   . GLU B 190 ? 0.40388 0.60923 0.44992 0.06047  -0.09359 0.02153  254 GLU B OE2   
2772 N N     . ALA B 191 ? 0.32075 0.43210 0.28646 0.06154  -0.07986 0.04295  255 ALA B N     
2773 C CA    . ALA B 191 ? 0.32569 0.42295 0.27991 0.04783  -0.07212 0.03807  255 ALA B CA    
2774 C C     . ALA B 191 ? 0.28911 0.35646 0.22573 0.04948  -0.06336 0.04478  255 ALA B C     
2775 O O     . ALA B 191 ? 0.26938 0.32392 0.20154 0.04072  -0.05444 0.04120  255 ALA B O     
2776 C CB    . ALA B 191 ? 0.21828 0.32167 0.19043 0.03890  -0.06502 0.02961  255 ALA B CB    
2777 N N     . SER B 192 ? 0.32312 0.37945 0.24964 0.06062  -0.06562 0.05456  256 SER B N     
2778 C CA    . SER B 192 ? 0.30488 0.33357 0.21639 0.06158  -0.05635 0.06128  256 SER B CA    
2779 C C     . SER B 192 ? 0.31698 0.33465 0.20594 0.05336  -0.05336 0.06074  256 SER B C     
2780 O O     . SER B 192 ? 0.35147 0.35018 0.23202 0.05012  -0.04311 0.06295  256 SER B O     
2781 C CB    . SER B 192 ? 0.41353 0.43016 0.31909 0.07298  -0.05872 0.07112  256 SER B CB    
2782 O OG    . SER B 192 ? 0.42933 0.45880 0.33295 0.07703  -0.07013 0.07227  256 SER B OG    
2783 N N     . ASP B 193 ? 0.39107 0.42099 0.27025 0.04965  -0.06175 0.05721  257 ASP B N     
2784 C CA    . ASP B 193 ? 0.39825 0.41712 0.25509 0.04181  -0.05828 0.05526  257 ASP B CA    
2785 C C     . ASP B 193 ? 0.36447 0.37642 0.22665 0.03199  -0.04756 0.04768  257 ASP B C     
2786 O O     . ASP B 193 ? 0.34572 0.34362 0.19122 0.02762  -0.04074 0.04719  257 ASP B O     
2787 C CB    . ASP B 193 ? 0.39849 0.43167 0.24646 0.03732  -0.06927 0.05052  257 ASP B CB    
2788 N N     . TYR B 194 ? 0.32549 0.34688 0.20986 0.02918  -0.04568 0.04199  258 TYR B N     
2789 C CA    . TYR B 194 ? 0.31902 0.33286 0.20818 0.02153  -0.03601 0.03596  258 TYR B CA    
2790 C C     . TYR B 194 ? 0.31521 0.31298 0.20561 0.02412  -0.02537 0.04068  258 TYR B C     
2791 O O     . TYR B 194 ? 0.30101 0.29315 0.19515 0.01913  -0.01756 0.03641  258 TYR B O     
2792 C CB    . TYR B 194 ? 0.31943 0.34791 0.22977 0.01733  -0.03742 0.02896  258 TYR B CB    
2793 C CG    . TYR B 194 ? 0.28426 0.32894 0.19357 0.01130  -0.04630 0.02263  258 TYR B CG    
2794 C CD1   . TYR B 194 ? 0.33850 0.37685 0.23128 0.00268  -0.04583 0.01700  258 TYR B CD1   
2795 C CD2   . TYR B 194 ? 0.36940 0.43619 0.29391 0.01417  -0.05511 0.02187  258 TYR B CD2   
2796 C CE1   . TYR B 194 ? 0.42084 0.47329 0.31141 -0.00469 -0.05403 0.01044  258 TYR B CE1   
2797 C CE2   . TYR B 194 ? 0.35890 0.44359 0.28356 0.00712  -0.06357 0.01543  258 TYR B CE2   
2798 C CZ    . TYR B 194 ? 0.42886 0.50560 0.33596 -0.00313 -0.06306 0.00964  258 TYR B CZ    
2799 O OH    . TYR B 194 ? 0.43295 0.52621 0.33900 -0.01203 -0.07124 0.00245  258 TYR B OH    
2800 N N     . LEU B 195 ? 0.32092 0.31110 0.20824 0.03147  -0.02490 0.04920  259 LEU B N     
2801 C CA    . LEU B 195 ? 0.30123 0.27547 0.18637 0.03170  -0.01445 0.05350  259 LEU B CA    
2802 C C     . LEU B 195 ? 0.32395 0.28547 0.18601 0.03020  -0.00997 0.05738  259 LEU B C     
2803 O O     . LEU B 195 ? 0.35465 0.30397 0.21330 0.02960  -0.00091 0.06145  259 LEU B O     
2804 C CB    . LEU B 195 ? 0.35625 0.32503 0.24916 0.03900  -0.01439 0.06035  259 LEU B CB    
2805 C CG    . LEU B 195 ? 0.36047 0.34236 0.27546 0.04192  -0.01858 0.05652  259 LEU B CG    
2806 C CD1   . LEU B 195 ? 0.37342 0.35482 0.28989 0.05272  -0.02478 0.06334  259 LEU B CD1   
2807 C CD2   . LEU B 195 ? 0.27075 0.25020 0.20106 0.03771  -0.01032 0.05221  259 LEU B CD2   
2808 N N     . GLU B 196 ? 0.32045 0.28530 0.16648 0.02882  -0.01577 0.05570  260 GLU B N     
2809 C CA    . GLU B 196 ? 0.37624 0.33148 0.20174 0.02653  -0.01226 0.05809  260 GLU B CA    
2810 C C     . GLU B 196 ? 0.36761 0.32037 0.18845 0.01996  -0.00476 0.05047  260 GLU B C     
2811 O O     . GLU B 196 ? 0.35633 0.31475 0.17880 0.01694  -0.00776 0.04313  260 GLU B O     
2812 C CB    . GLU B 196 ? 0.40802 0.36987 0.22098 0.02777  -0.02319 0.05936  260 GLU B CB    
2813 C CG    . GLU B 196 ? 0.43255 0.39367 0.24620 0.03506  -0.02972 0.06827  260 GLU B CG    
2814 C CD    . GLU B 196 ? 0.47502 0.42080 0.29034 0.03678  -0.02069 0.07528  260 GLU B CD    
2815 O OE1   . GLU B 196 ? 0.49220 0.42877 0.29787 0.03185  -0.01190 0.07596  260 GLU B OE1   
2816 O OE2   . GLU B 196 ? 0.51480 0.45840 0.34167 0.04274  -0.02221 0.07947  260 GLU B OE2   
2817 N N     . LEU B 197 ? 0.33118 0.29628 0.15839 -0.00090 -0.04227 0.01907  261 LEU B N     
2818 C CA    . LEU B 197 ? 0.38795 0.34266 0.20441 -0.00331 -0.02871 0.01745  261 LEU B CA    
2819 C C     . LEU B 197 ? 0.37729 0.33095 0.18078 -0.01305 -0.01948 0.01042  261 LEU B C     
2820 O O     . LEU B 197 ? 0.40104 0.34658 0.19926 -0.01380 -0.00701 0.00540  261 LEU B O     
2821 C CB    . LEU B 197 ? 0.44142 0.39412 0.26027 -0.00397 -0.02927 0.02506  261 LEU B CB    
2822 C CG    . LEU B 197 ? 0.42502 0.36497 0.24389 0.00089  -0.02140 0.02762  261 LEU B CG    
2823 C CD1   . LEU B 197 ? 0.39051 0.32306 0.21619 0.01177  -0.02439 0.02477  261 LEU B CD1   
2824 C CD2   . LEU B 197 ? 0.37889 0.31883 0.20599 0.00123  -0.02735 0.03927  261 LEU B CD2   
2825 N N     . ASP B 198 ? 0.36288 0.32315 0.16281 -0.02040 -0.02596 0.00948  262 ASP B N     
2826 C CA    . ASP B 198 ? 0.37758 0.33414 0.16497 -0.02981 -0.02043 0.00139  262 ASP B CA    
2827 C C     . ASP B 198 ? 0.35702 0.31041 0.14320 -0.03303 -0.02031 -0.00396 262 ASP B C     
2828 O O     . ASP B 198 ? 0.36731 0.31182 0.14526 -0.03863 -0.01097 -0.01117 262 ASP B O     
2829 C CB    . ASP B 198 ? 0.45066 0.41307 0.23248 -0.03610 -0.02905 0.00173  262 ASP B CB    
2830 C CG    . ASP B 198 ? 0.44379 0.41552 0.23756 -0.03550 -0.04415 0.00594  262 ASP B CG    
2831 O OD1   . ASP B 198 ? 0.42881 0.40385 0.23549 -0.02805 -0.04842 0.00939  262 ASP B OD1   
2832 O OD2   . ASP B 198 ? 0.45554 0.43091 0.24561 -0.04139 -0.05167 0.00537  262 ASP B OD2   
2833 N N     . THR B 199 ? 0.31286 0.27300 0.10716 -0.02933 -0.03031 0.00001  263 THR B N     
2834 C CA    . THR B 199 ? 0.36009 0.32340 0.16570 -0.02926 -0.02766 -0.00167 263 THR B CA    
2835 C C     . THR B 199 ? 0.38254 0.34043 0.19546 -0.02121 -0.01118 -0.00225 263 THR B C     
2836 O O     . THR B 199 ? 0.38177 0.33812 0.20345 -0.02601 -0.00272 -0.00583 263 THR B O     
2837 C CB    . THR B 199 ? 0.37219 0.34732 0.19219 -0.02141 -0.03858 0.00436  263 THR B CB    
2838 O OG1   . THR B 199 ? 0.39079 0.37204 0.20906 -0.03111 -0.05431 0.00493  263 THR B OG1   
2839 C CG2   . THR B 199 ? 0.39213 0.37531 0.23350 -0.01540 -0.03032 0.00642  263 THR B CG2   
2840 N N     . ILE B 200 ? 0.40687 0.36066 0.21747 -0.00904 -0.00828 0.00177  264 ILE B N     
2841 C CA    . ILE B 200 ? 0.36414 0.31300 0.18109 0.00009  0.00576  0.00251  264 ILE B CA    
2842 C C     . ILE B 200 ? 0.38420 0.32247 0.19556 -0.00747 0.01795  -0.00264 264 ILE B C     
2843 O O     . ILE B 200 ? 0.38830 0.32440 0.20944 -0.00711 0.02958  -0.00394 264 ILE B O     
2844 C CB    . ILE B 200 ? 0.34885 0.29283 0.16210 0.01583  0.00208  0.00725  264 ILE B CB    
2845 C CG1   . ILE B 200 ? 0.40954 0.36303 0.22894 0.02715  -0.00714 0.01070  264 ILE B CG1   
2846 C CG2   . ILE B 200 ? 0.39233 0.32783 0.20710 0.02431  0.01583  0.00800  264 ILE B CG2   
2847 C CD1   . ILE B 200 ? 0.38939 0.34992 0.21975 0.03785  0.00473  0.01363  264 ILE B CD1   
2848 N N     . LYS B 201 ? 0.32107 0.25327 0.11790 -0.01357 0.01605  -0.00461 265 LYS B N     
2849 C CA    . LYS B 201 ? 0.32546 0.24883 0.11867 -0.01825 0.02828  -0.00984 265 LYS B CA    
2850 C C     . LYS B 201 ? 0.40055 0.32074 0.19247 -0.02858 0.03170  -0.01870 265 LYS B C     
2851 O O     . LYS B 201 ? 0.34066 0.25347 0.13932 -0.02925 0.04277  -0.02284 265 LYS B O     
2852 C CB    . LYS B 201 ? 0.35553 0.28228 0.14689 -0.01964 0.02503  -0.00768 265 LYS B CB    
2853 C CG    . LYS B 201 ? 0.36952 0.29329 0.16914 -0.01198 0.02922  -0.00104 265 LYS B CG    
2854 C CD    . LYS B 201 ? 0.34002 0.26882 0.13614 -0.01365 0.02488  0.00524  265 LYS B CD    
2855 C CE    . LYS B 201 ? 0.27009 0.19387 0.07328 -0.00689 0.02325  0.01508  265 LYS B CE    
2856 N NZ    . LYS B 201 ? 0.31812 0.24537 0.11882 -0.00961 0.02707  0.02250  265 LYS B NZ    
2857 N N     . ASN B 202 ? 0.37451 0.30023 0.16229 -0.03656 0.01973  -0.02130 266 ASN B N     
2858 C CA    . ASN B 202 ? 0.35129 0.27324 0.14305 -0.04628 0.01768  -0.02948 266 ASN B CA    
2859 C C     . ASN B 202 ? 0.34765 0.27480 0.16769 -0.04387 0.02231  -0.02563 266 ASN B C     
2860 O O     . ASN B 202 ? 0.40103 0.32094 0.23076 -0.04933 0.02647  -0.03090 266 ASN B O     
2861 C CB    . ASN B 202 ? 0.38409 0.31095 0.16794 -0.05476 0.00091  -0.03130 266 ASN B CB    
2862 C CG    . ASN B 202 ? 0.40531 0.32475 0.15811 -0.05922 -0.00210 -0.03672 266 ASN B CG    
2863 O OD1   . ASN B 202 ? 0.40649 0.31625 0.15018 -0.05786 0.00763  -0.04311 266 ASN B OD1   
2864 N ND2   . ASN B 202 ? 0.35347 0.28319 0.10504 -0.05968 -0.01478 -0.03126 266 ASN B ND2   
2865 N N     . LEU B 203 ? 0.37526 0.31498 0.20919 -0.03480 0.02137  -0.01574 267 LEU B N     
2866 C CA    . LEU B 203 ? 0.35168 0.30026 0.21259 -0.03028 0.02765  -0.00867 267 LEU B CA    
2867 C C     . LEU B 203 ? 0.35766 0.29873 0.22411 -0.02477 0.04337  -0.00759 267 LEU B C     
2868 O O     . LEU B 203 ? 0.33787 0.28077 0.22605 -0.02749 0.04940  -0.00481 267 LEU B O     
2869 C CB    . LEU B 203 ? 0.37465 0.33767 0.24292 -0.01812 0.02446  0.00109  267 LEU B CB    
2870 C CG    . LEU B 203 ? 0.41467 0.39387 0.30600 -0.01979 0.01759  0.00770  267 LEU B CG    
2871 C CD1   . LEU B 203 ? 0.38816 0.38006 0.28544 -0.00188 0.02076  0.01743  267 LEU B CD1   
2872 C CD2   . LEU B 203 ? 0.46929 0.45107 0.38730 -0.02791 0.02266  0.01026  267 LEU B CD2   
2873 N N     . VAL B 204 ? 0.31320 0.24619 0.16361 -0.01715 0.04901  -0.00805 268 VAL B N     
2874 C CA    . VAL B 204 ? 0.34732 0.27219 0.20276 -0.01191 0.06274  -0.00662 268 VAL B CA    
2875 C C     . VAL B 204 ? 0.42081 0.33427 0.27931 -0.02299 0.06766  -0.01546 268 VAL B C     
2876 O O     . VAL B 204 ? 0.45141 0.36228 0.32723 -0.02287 0.07661  -0.01322 268 VAL B O     
2877 C CB    . VAL B 204 ? 0.32902 0.24613 0.16866 -0.00259 0.06451  -0.00504 268 VAL B CB    
2878 C CG1   . VAL B 204 ? 0.32393 0.23095 0.16916 0.00137  0.07768  -0.00398 268 VAL B CG1   
2879 C CG2   . VAL B 204 ? 0.28084 0.20558 0.11817 0.01061  0.05763  0.00248  268 VAL B CG2   
2880 N N     . LYS B 205 ? 0.49860 0.40442 0.33953 -0.03172 0.06147  -0.02550 269 LYS B N     
2881 C CA    . LYS B 205 ? 0.48269 0.37486 0.32219 -0.04030 0.06417  -0.03649 269 LYS B CA    
2882 C C     . LYS B 205 ? 0.54190 0.43662 0.40610 -0.04786 0.05856  -0.03644 269 LYS B C     
2883 O O     . LYS B 205 ? 0.61786 0.50413 0.49768 -0.05066 0.06406  -0.03892 269 LYS B O     
2884 C CB    . LYS B 205 ? 0.54459 0.42895 0.35563 -0.04584 0.05768  -0.04691 269 LYS B CB    
2885 C CG    . LYS B 205 ? 0.63219 0.51151 0.42400 -0.03973 0.06669  -0.04669 269 LYS B CG    
2886 C CD    . LYS B 205 ? 0.63366 0.49860 0.41036 -0.04203 0.07258  -0.05855 269 LYS B CD    
2887 C CE    . LYS B 205 ? 0.67719 0.55168 0.45604 -0.03343 0.07484  -0.05033 269 LYS B CE    
2888 N NZ    . LYS B 205 ? 0.62885 0.50034 0.42433 -0.02706 0.08594  -0.04567 269 LYS B NZ    
2889 N N     . LYS B 206 ? 0.41054 0.31741 0.28274 -0.05127 0.04677  -0.03204 270 LYS B N     
2890 C CA    . LYS B 206 ? 0.44794 0.35866 0.34876 -0.05949 0.03904  -0.02964 270 LYS B CA    
2891 C C     . LYS B 206 ? 0.48572 0.40571 0.41982 -0.05426 0.05055  -0.01642 270 LYS B C     
2892 O O     . LYS B 206 ? 0.52149 0.44085 0.48432 -0.06175 0.04706  -0.01387 270 LYS B O     
2893 C CB    . LYS B 206 ? 0.42333 0.34756 0.32857 -0.06285 0.02472  -0.02505 270 LYS B CB    
2894 C CG    . LYS B 206 ? 0.53727 0.46614 0.47566 -0.07279 0.01325  -0.02114 270 LYS B CG    
2895 C CD    . LYS B 206 ? 0.50196 0.45453 0.46421 -0.06860 0.01026  -0.00567 270 LYS B CD    
2896 C CE    . LYS B 206 ? 0.60337 0.55755 0.57688 -0.08074 -0.01067 -0.00739 270 LYS B CE    
2897 N N     . TYR B 207 ? 0.57064 0.49814 0.50167 -0.04124 0.06317  -0.00730 271 TYR B N     
2898 C CA    . TYR B 207 ? 0.58740 0.52439 0.54506 -0.03402 0.07542  0.00673  271 TYR B CA    
2899 C C     . TYR B 207 ? 0.63051 0.55590 0.57933 -0.02746 0.08850  0.00555  271 TYR B C     
2900 O O     . TYR B 207 ? 0.62851 0.56158 0.58997 -0.01766 0.09950  0.01807  271 TYR B O     
2901 C CB    . TYR B 207 ? 0.58215 0.53978 0.54603 -0.02142 0.07828  0.02101  271 TYR B CB    
2902 C CG    . TYR B 207 ? 0.66211 0.63439 0.64493 -0.02733 0.06713  0.02596  271 TYR B CG    
2903 C CD1   . TYR B 207 ? 0.63874 0.61445 0.65558 -0.03900 0.06219  0.03040  271 TYR B CD1   
2904 C CD2   . TYR B 207 ? 0.64642 0.62861 0.61668 -0.02133 0.05996  0.02713  271 TYR B CD2   
2905 C CE1   . TYR B 207 ? 0.63127 0.62031 0.66980 -0.04498 0.05058  0.03642  271 TYR B CE1   
2906 C CE2   . TYR B 207 ? 0.63079 0.62677 0.62127 -0.02681 0.04945  0.03250  271 TYR B CE2   
2907 C CZ    . TYR B 207 ? 0.66040 0.66004 0.68537 -0.03879 0.04492  0.03747  271 TYR B CZ    
2908 O OH    . TYR B 207 ? 0.68709 0.70031 0.73614 -0.04482 0.03300  0.04417  271 TYR B OH    
2909 N N     . SER B 208 ? 0.70150 0.60886 0.62936 -0.03192 0.08804  -0.00828 272 SER B N     
2910 C CA    . SER B 208 ? 0.68364 0.57935 0.60784 -0.02691 0.09986  -0.00921 272 SER B CA    
2911 C C     . SER B 208 ? 0.77850 0.67053 0.73239 -0.03206 0.10498  -0.00584 272 SER B C     
2912 O O     . SER B 208 ? 0.73705 0.61825 0.69397 -0.03005 0.11392  -0.00687 272 SER B O     
2913 C CB    . SER B 208 ? 0.62889 0.50845 0.52702 -0.02980 0.09940  -0.02333 272 SER B CB    
2914 O OG    . SER B 208 ? 0.64750 0.51227 0.55120 -0.03831 0.09959  -0.03443 272 SER B OG    
2915 N N     . GLN B 209 ? 0.49005 0.39083 0.46876 -0.03960 0.09755  -0.00127 273 GLN B N     
2916 C CA    . GLN B 209 ? 0.52191 0.42341 0.53764 -0.04499 0.09986  0.00671  273 GLN B CA    
2917 C C     . GLN B 209 ? 0.50199 0.41639 0.53390 -0.03363 0.11468  0.02568  273 GLN B C     
2918 O O     . GLN B 209 ? 0.43925 0.34784 0.49074 -0.03484 0.12157  0.03043  273 GLN B O     
2919 C CB    . GLN B 209 ? 0.52674 0.43898 0.56902 -0.05423 0.08722  0.01189  273 GLN B CB    
2920 C CG    . GLN B 209 ? 0.61762 0.51148 0.66667 -0.06839 0.07217  -0.00282 273 GLN B CG    
2921 C CD    . GLN B 209 ? 0.58885 0.49278 0.66469 -0.07760 0.05657  0.00317  273 GLN B CD    
2922 O OE1   . GLN B 209 ? 0.52790 0.44333 0.64779 -0.08109 0.05622  0.01942  273 GLN B OE1   
2923 N NE2   . GLN B 209 ? 0.55989 0.46096 0.61176 -0.08148 0.04340  -0.00771 273 GLN B NE2   
2924 N N     . PHE B 210 ? 0.50880 0.44026 0.53233 -0.02165 0.11904  0.03688  274 PHE B N     
2925 C CA    . PHE B 210 ? 0.52597 0.47093 0.56071 -0.00820 0.13266  0.05579  274 PHE B CA    
2926 C C     . PHE B 210 ? 0.48516 0.41946 0.49081 0.00419  0.14013  0.05326  274 PHE B C     
2927 O O     . PHE B 210 ? 0.46398 0.40764 0.46551 0.01929  0.14889  0.06654  274 PHE B O     
2928 C CB    . PHE B 210 ? 0.48733 0.45613 0.52878 0.00097  0.13355  0.06969  274 PHE B CB    
2929 N N     . ILE B 211 ? 0.57152 0.48630 0.55723 -0.00096 0.13639  0.03723  275 ILE B N     
2930 C CA    . ILE B 211 ? 0.52532 0.42889 0.48627 0.00913  0.14022  0.03460  275 ILE B CA    
2931 C C     . ILE B 211 ? 0.53099 0.41767 0.49973 0.00320  0.14552  0.02902  275 ILE B C     
2932 O O     . ILE B 211 ? 0.39888 0.27482 0.37047 -0.00852 0.14164  0.01605  275 ILE B O     
2933 C CB    . ILE B 211 ? 0.42992 0.32825 0.36172 0.00998  0.13090  0.02328  275 ILE B CB    
2934 N N     . ASN B 212 ? 0.70304 0.58787 0.67472 0.01320  0.14809  0.03630  276 ASN B N     
2935 C CA    . ASN B 212 ? 0.68803 0.55811 0.66867 0.01029  0.15243  0.03251  276 ASN B CA    
2936 C C     . ASN B 212 ? 0.67295 0.52944 0.63262 0.01458  0.14749  0.02380  276 ASN B C     
2937 O O     . ASN B 212 ? 0.70693 0.54928 0.66889 0.00869  0.15214  0.01540  276 ASN B O     
2938 C CB    . ASN B 212 ? 0.70862 0.58650 0.70648 0.01919  0.15437  0.04571  276 ASN B CB    
2939 C CG    . ASN B 212 ? 0.70836 0.59757 0.73852 0.01185  0.15898  0.05547  276 ASN B CG    
2940 O OD1   . ASN B 212 ? 0.64591 0.53834 0.68696 0.00085  0.15927  0.05430  276 ASN B OD1   
2941 N ND2   . ASN B 212 ? 0.78489 0.68026 0.83288 0.01747  0.16121  0.06637  276 ASN B ND2   
2942 N N     . PHE B 213 ? 0.38916 0.24979 0.33154 0.02461  0.13769  0.02689  277 PHE B N     
2943 C CA    . PHE B 213 ? 0.36709 0.21812 0.29515 0.03072  0.12964  0.02553  277 PHE B CA    
2944 C C     . PHE B 213 ? 0.31874 0.17112 0.23245 0.02573  0.12196  0.01818  277 PHE B C     
2945 O O     . PHE B 213 ? 0.30284 0.16456 0.21295 0.02063  0.12126  0.01436  277 PHE B O     
2946 C CB    . PHE B 213 ? 0.31176 0.16632 0.23158 0.04572  0.12356  0.03501  277 PHE B CB    
2947 C CG    . PHE B 213 ? 0.31252 0.16906 0.24477 0.05253  0.13061  0.04330  277 PHE B CG    
2948 C CD1   . PHE B 213 ? 0.34249 0.21462 0.28774 0.05258  0.13612  0.05057  277 PHE B CD1   
2949 C CD2   . PHE B 213 ? 0.29365 0.14427 0.22835 0.05672  0.13107  0.04389  277 PHE B CD2   
2950 C CE1   . PHE B 213 ? 0.36596 0.24286 0.32507 0.05851  0.14234  0.06026  277 PHE B CE1   
2951 C CE2   . PHE B 213 ? 0.31976 0.17571 0.26661 0.06269  0.13793  0.05131  277 PHE B CE2   
2952 C CZ    . PHE B 213 ? 0.32441 0.19115 0.28324 0.06446  0.14364  0.06058  277 PHE B CZ    
2953 N N     . PRO B 214 ? 0.18750 0.17879 0.19773 0.07692  0.05547  0.01883  278 PRO B N     
2954 C CA    . PRO B 214 ? 0.18801 0.19507 0.20620 0.07296  0.04908  0.01470  278 PRO B CA    
2955 C C     . PRO B 214 ? 0.26675 0.24930 0.27806 0.06667  0.05360  0.01685  278 PRO B C     
2956 O O     . PRO B 214 ? 0.24251 0.20208 0.22611 0.07000  0.06063  0.02058  278 PRO B O     
2957 C CB    . PRO B 214 ? 0.24017 0.27330 0.23277 0.06704  0.03601  0.01159  278 PRO B CB    
2958 C CG    . PRO B 214 ? 0.20677 0.22837 0.17339 0.07882  0.04213  0.01472  278 PRO B CG    
2959 C CD    . PRO B 214 ? 0.21643 0.21886 0.19936 0.08737  0.05358  0.01908  278 PRO B CD    
2960 N N     . ILE B 215 ? 0.25615 0.24137 0.28875 0.05921  0.04823  0.01391  279 ILE B N     
2961 C CA    . ILE B 215 ? 0.28950 0.25317 0.31414 0.05325  0.04986  0.01501  279 ILE B CA    
2962 C C     . ILE B 215 ? 0.30503 0.28176 0.31655 0.03817  0.03409  0.01039  279 ILE B C     
2963 O O     . ILE B 215 ? 0.22321 0.22152 0.25173 0.03508  0.02483  0.00634  279 ILE B O     
2964 C CB    . ILE B 215 ? 0.22369 0.18048 0.27708 0.05149  0.05205  0.01531  279 ILE B CB    
2965 C CG1   . ILE B 215 ? 0.31524 0.27438 0.37951 0.05150  0.05706  0.01849  279 ILE B CG1   
2966 C CG2   . ILE B 215 ? 0.31555 0.25063 0.35597 0.04975  0.05673  0.01779  279 ILE B CG2   
2967 C CD1   . ILE B 215 ? 0.37433 0.32919 0.45705 0.04716  0.06102  0.02094  279 ILE B CD1   
2968 N N     . TYR B 216 ? 0.27212 0.23190 0.25145 0.02978  0.03159  0.01143  280 TYR B N     
2969 C CA    . TYR B 216 ? 0.24027 0.20578 0.20312 0.01344  0.01877  0.00914  280 TYR B CA    
2970 C C     . TYR B 216 ? 0.26440 0.19866 0.21801 0.01115  0.02053  0.00982  280 TYR B C     
2971 O O     . TYR B 216 ? 0.27325 0.17910 0.22000 0.02075  0.03124  0.01260  280 TYR B O     
2972 C CB    . TYR B 216 ? 0.29819 0.26812 0.23006 0.00290  0.01103  0.00922  280 TYR B CB    
2973 C CG    . TYR B 216 ? 0.29431 0.29721 0.23269 0.00625  0.00793  0.00846  280 TYR B CG    
2974 C CD1   . TYR B 216 ? 0.34834 0.34458 0.28302 0.02135  0.01614  0.00974  280 TYR B CD1   
2975 C CD2   . TYR B 216 ? 0.28047 0.32043 0.22701 -0.00376 -0.00189 0.00737  280 TYR B CD2   
2976 C CE1   . TYR B 216 ? 0.31065 0.33515 0.24824 0.02669  0.01270  0.00883  280 TYR B CE1   
2977 C CE2   . TYR B 216 ? 0.32545 0.39748 0.27808 0.00176  -0.00455 0.00678  280 TYR B CE2   
2978 C CZ    . TYR B 216 ? 0.33118 0.39484 0.27872 0.01711  0.00177  0.00693  280 TYR B CZ    
2979 O OH    . TYR B 216 ? 0.24375 0.33762 0.19464 0.02479  -0.00149 0.00610  280 TYR B OH    
2980 N N     . VAL B 217 ? 0.22593 0.16426 0.17620 -0.00001 0.01096  0.00807  281 VAL B N     
2981 C CA    . VAL B 217 ? 0.24276 0.15003 0.17594 -0.00361 0.00996  0.00852  281 VAL B CA    
2982 C C     . VAL B 217 ? 0.24259 0.14732 0.14526 -0.02300 -0.00062 0.00916  281 VAL B C     
2983 O O     . VAL B 217 ? 0.25145 0.18422 0.16068 -0.03270 -0.00746 0.00927  281 VAL B O     
2984 C CB    . VAL B 217 ? 0.21469 0.12328 0.17340 0.00333  0.00847  0.00617  281 VAL B CB    
2985 C CG1   . VAL B 217 ? 0.22510 0.10314 0.16066 -0.00072 0.00517  0.00654  281 VAL B CG1   
2986 C CG2   . VAL B 217 ? 0.19066 0.09861 0.18408 0.02002  0.01864  0.00619  281 VAL B CG2   
2987 N N     . TRP B 218 ? 0.29314 0.16309 0.16240 -0.02828 -0.00152 0.01012  282 TRP B N     
2988 C CA    . TRP B 218 ? 0.27741 0.13900 0.11870 -0.04914 -0.01247 0.01100  282 TRP B CA    
2989 C C     . TRP B 218 ? 0.32702 0.18895 0.17140 -0.05579 -0.01585 0.01233  282 TRP B C     
2990 O O     . TRP B 218 ? 0.33355 0.16653 0.17067 -0.04775 -0.01326 0.01188  282 TRP B O     
2991 C CB    . TRP B 218 ? 0.35082 0.16523 0.15224 -0.05098 -0.01420 0.01055  282 TRP B CB    
2992 C CG    . TRP B 218 ? 0.41008 0.21124 0.18351 -0.07466 -0.02725 0.01111  282 TRP B CG    
2993 C CD1   . TRP B 218 ? 0.41335 0.17734 0.15971 -0.08366 -0.03153 0.01222  282 TRP B CD1   
2994 C CD2   . TRP B 218 ? 0.39433 0.21820 0.16578 -0.09278 -0.03822 0.01089  282 TRP B CD2   
2995 N NE1   . TRP B 218 ? 0.47285 0.23335 0.20151 -0.10827 -0.04405 0.01322  282 TRP B NE1   
2996 C CE2   . TRP B 218 ? 0.45826 0.25769 0.20470 -0.11466 -0.04878 0.01231  282 TRP B CE2   
2997 C CE3   . TRP B 218 ? 0.42725 0.29005 0.21690 -0.09219 -0.04063 0.00972  282 TRP B CE3   
2998 C CZ2   . TRP B 218 ? 0.48939 0.30512 0.23416 -0.13807 -0.06206 0.01280  282 TRP B CZ2   
2999 C CZ3   . TRP B 218 ? 0.46280 0.34363 0.24928 -0.11303 -0.05420 0.00964  282 TRP B CZ3   
3000 C CH2   . TRP B 218 ? 0.45844 0.31708 0.22529 -0.13667 -0.06495 0.01123  282 TRP B CH2   
3001 N N     . SER B 219 ? 0.31210 0.20660 0.16633 -0.06794 -0.02077 0.01444  283 SER B N     
3002 C CA    . SER B 219 ? 0.30071 0.19738 0.15597 -0.07082 -0.02240 0.01659  283 SER B CA    
3003 C C     . SER B 219 ? 0.32153 0.19816 0.14740 -0.09267 -0.02764 0.02165  283 SER B C     
3004 O O     . SER B 219 ? 0.37019 0.27078 0.19916 -0.10645 -0.02919 0.02687  283 SER B O     
3005 C CB    . SER B 219 ? 0.25727 0.19958 0.13897 -0.06691 -0.02202 0.01703  283 SER B CB    
3006 O OG    . SER B 219 ? 0.31193 0.25183 0.19615 -0.05884 -0.02271 0.01680  283 SER B OG    
3007 N N     . SER B 220 ? 0.54894 0.37976 0.34576 -0.09533 -0.02948 0.02083  284 SER B N     
3008 C CA    . SER B 220 ? 0.62151 0.42442 0.38721 -0.11739 -0.03582 0.02509  284 SER B CA    
3009 C C     . SER B 220 ? 0.70544 0.45774 0.44120 -0.10785 -0.03657 0.02086  284 SER B C     
3010 O O     . SER B 220 ? 0.60313 0.34377 0.34330 -0.08676 -0.03073 0.01691  284 SER B O     
3011 C CB    . SER B 220 ? 0.60478 0.42736 0.37157 -0.13828 -0.04306 0.02652  284 SER B CB    
3012 O OG    . SER B 220 ? 0.67220 0.48823 0.42584 -0.16076 -0.04828 0.03215  284 SER B OG    
3013 N N     . LYS B 221 ? 0.83834 0.57004 0.54877 -0.11978 -0.04262 0.02139  285 LYS B N     
3014 C CA    . LYS B 221 ? 0.87241 0.56448 0.55232 -0.10958 -0.04412 0.01739  285 LYS B CA    
3015 C C     . LYS B 221 ? 0.88878 0.56587 0.55241 -0.10859 -0.04798 0.01538  285 LYS B C     
3016 O O     . LYS B 221 ? 0.87503 0.57138 0.55095 -0.11747 -0.05077 0.01655  285 LYS B O     
3017 C CB    . LYS B 221 ? 0.91007 0.58213 0.56552 -0.12360 -0.04979 0.02009  285 LYS B CB    
3018 N N     . GLY B 226 ? 0.87758 0.63425 0.57828 -0.18324 -0.06949 0.03122  327 GLY B N     
3019 C CA    . GLY B 226 ? 0.87183 0.66828 0.59752 -0.20269 -0.07567 0.03485  327 GLY B CA    
3020 C C     . GLY B 226 ? 0.86423 0.67089 0.59710 -0.19788 -0.08225 0.02913  327 GLY B C     
3021 O O     . GLY B 226 ? 0.87522 0.64757 0.58579 -0.18162 -0.08273 0.02325  327 GLY B O     
3022 N N     . LYS B 227 ? 1.24785 1.10198 1.01129 -0.20917 -0.08687 0.03044  328 LYS B N     
3023 C CA    . LYS B 227 ? 1.24064 1.10871 1.01169 -0.20106 -0.09408 0.02323  328 LYS B CA    
3024 C C     . LYS B 227 ? 1.20493 1.13939 1.01766 -0.20590 -0.09286 0.02571  328 LYS B C     
3025 O O     . LYS B 227 ? 1.21621 1.17665 1.04766 -0.22290 -0.09917 0.02979  328 LYS B O     
3026 C CB    . LYS B 227 ? 1.28747 1.12415 1.03797 -0.20824 -0.10919 0.01939  328 LYS B CB    
3027 N N     . THR B 228 ? 0.98098 0.94220 0.80833 -0.18920 -0.08462 0.02328  329 THR B N     
3028 C CA    . THR B 228 ? 0.94754 0.97031 0.81096 -0.18677 -0.08246 0.02502  329 THR B CA    
3029 C C     . THR B 228 ? 0.91729 0.94951 0.78319 -0.16199 -0.07659 0.01905  329 THR B C     
3030 O O     . THR B 228 ? 0.91389 0.91869 0.76428 -0.15025 -0.06967 0.01708  329 THR B O     
3031 C CB    . THR B 228 ? 0.93032 0.98937 0.81643 -0.19710 -0.07325 0.03506  329 THR B CB    
3032 N N     . VAL B 229 ? 0.62925 0.69856 0.51394 -0.15261 -0.07931 0.01630  330 VAL B N     
3033 C CA    . VAL B 229 ? 0.65822 0.73698 0.54496 -0.12796 -0.07262 0.01212  330 VAL B CA    
3034 C C     . VAL B 229 ? 0.65827 0.76591 0.56574 -0.12087 -0.06050 0.01671  330 VAL B C     
3035 O O     . VAL B 229 ? 0.59791 0.70010 0.50493 -0.10059 -0.05245 0.01422  330 VAL B O     
3036 C CB    . VAL B 229 ? 0.61474 0.72144 0.51212 -0.11774 -0.07922 0.00792  330 VAL B CB    
3037 C CG1   . VAL B 229 ? 0.59242 0.75583 0.52567 -0.12250 -0.07676 0.01317  330 VAL B CG1   
3038 C CG2   . VAL B 229 ? 0.60620 0.70441 0.49215 -0.09160 -0.07325 0.00362  330 VAL B CG2   
3039 N N     . TRP B 230 ? 0.67569 0.81054 0.60067 -0.13517 -0.05777 0.02396  331 TRP B N     
3040 C CA    . TRP B 230 ? 0.60493 0.76067 0.54270 -0.12784 -0.04797 0.02794  331 TRP B CA    
3041 C C     . TRP B 230 ? 0.60970 0.71932 0.52941 -0.12306 -0.04210 0.02723  331 TRP B C     
3042 O O     . TRP B 230 ? 0.61967 0.73606 0.54796 -0.11051 -0.03400 0.02849  331 TRP B O     
3043 C CB    . TRP B 230 ? 0.62709 0.82084 0.58323 -0.14217 -0.04454 0.03743  331 TRP B CB    
3044 N N     . ASP B 231 ? 0.49442 0.55615 0.38828 -0.13071 -0.04681 0.02476  332 ASP B N     
3045 C CA    . ASP B 231 ? 0.46562 0.48261 0.34195 -0.12469 -0.04148 0.02418  332 ASP B CA    
3046 C C     . ASP B 231 ? 0.43661 0.43686 0.31565 -0.09906 -0.03414 0.01866  332 ASP B C     
3047 O O     . ASP B 231 ? 0.47499 0.44251 0.34511 -0.09133 -0.02980 0.01775  332 ASP B O     
3048 C CB    . ASP B 231 ? 0.53842 0.50831 0.38340 -0.14061 -0.04904 0.02380  332 ASP B CB    
3049 C CG    . ASP B 231 ? 0.59564 0.56591 0.43632 -0.16582 -0.05246 0.03126  332 ASP B CG    
3050 O OD1   . ASP B 231 ? 0.59188 0.57922 0.44354 -0.16467 -0.04461 0.03708  332 ASP B OD1   
3051 O OD2   . ASP B 231 ? 0.58672 0.53884 0.41277 -0.18459 -0.06231 0.03186  332 ASP B OD2   
3052 N N     . TRP B 232 ? 0.40777 0.42845 0.29948 -0.08582 -0.03249 0.01555  333 TRP B N     
3053 C CA    . TRP B 232 ? 0.34682 0.35731 0.24868 -0.06273 -0.02345 0.01230  333 TRP B CA    
3054 C C     . TRP B 232 ? 0.34442 0.38626 0.27305 -0.05296 -0.01975 0.01248  333 TRP B C     
3055 O O     . TRP B 232 ? 0.36206 0.44337 0.30292 -0.05497 -0.02202 0.01394  333 TRP B O     
3056 C CB    . TRP B 232 ? 0.34679 0.35874 0.24549 -0.05164 -0.02220 0.00982  333 TRP B CB    
3057 C CG    . TRP B 232 ? 0.42303 0.39700 0.28925 -0.05538 -0.02624 0.00831  333 TRP B CG    
3058 C CD1   . TRP B 232 ? 0.40107 0.37810 0.24990 -0.06774 -0.03856 0.00673  333 TRP B CD1   
3059 C CD2   . TRP B 232 ? 0.41015 0.33640 0.25611 -0.04501 -0.01904 0.00780  333 TRP B CD2   
3060 N NE1   . TRP B 232 ? 0.45723 0.38720 0.27161 -0.06493 -0.04078 0.00430  333 TRP B NE1   
3061 C CE2   . TRP B 232 ? 0.45253 0.35106 0.26353 -0.05019 -0.02737 0.00561  333 TRP B CE2   
3062 C CE3   . TRP B 232 ? 0.32722 0.23273 0.18261 -0.03083 -0.00689 0.00893  333 TRP B CE3   
3063 C CZ2   . TRP B 232 ? 0.51070 0.35891 0.29074 -0.03966 -0.02221 0.00502  333 TRP B CZ2   
3064 C CZ3   . TRP B 232 ? 0.35262 0.21363 0.18334 -0.02154 -0.00058 0.00934  333 TRP B CZ3   
3065 C CH2   . TRP B 232 ? 0.43317 0.26472 0.22415 -0.02488 -0.00728 0.00766  333 TRP B CH2   
3066 N N     . GLU B 233 ? 0.30069 0.32474 0.23778 -0.04146 -0.01527 0.01063  334 GLU B N     
3067 C CA    . GLU B 233 ? 0.24792 0.29361 0.20895 -0.02774 -0.01392 0.00831  334 GLU B CA    
3068 C C     . GLU B 233 ? 0.26247 0.30586 0.24113 -0.01091 -0.00806 0.00523  334 GLU B C     
3069 O O     . GLU B 233 ? 0.20031 0.21469 0.17977 -0.00471 -0.00222 0.00479  334 GLU B O     
3070 C CB    . GLU B 233 ? 0.24774 0.27617 0.21056 -0.02379 -0.01556 0.00682  334 GLU B CB    
3071 C CG    . GLU B 233 ? 0.23571 0.28697 0.21578 -0.01156 -0.01856 0.00376  334 GLU B CG    
3072 C CD    . GLU B 233 ? 0.27470 0.30591 0.25561 -0.00406 -0.02304 0.00041  334 GLU B CD    
3073 O OE1   . GLU B 233 ? 0.27250 0.27959 0.23455 -0.01231 -0.02364 0.00288  334 GLU B OE1   
3074 O OE2   . GLU B 233 ? 0.29920 0.33686 0.29776 0.01079  -0.02753 -0.00526 334 GLU B OE2   
3075 N N     . LEU B 234 ? 0.17664 0.24965 0.16893 -0.00272 -0.00832 0.00407  335 LEU B N     
3076 C CA    . LEU B 234 ? 0.12317 0.19284 0.13344 0.01349  -0.00245 0.00183  335 LEU B CA    
3077 C C     . LEU B 234 ? 0.18364 0.24355 0.21727 0.02349  -0.00341 -0.00222 335 LEU B C     
3078 O O     . LEU B 234 ? 0.17494 0.24842 0.21220 0.02506  -0.01085 -0.00503 335 LEU B O     
3079 C CB    . LEU B 234 ? 0.14712 0.24891 0.16089 0.02006  -0.00387 0.00151  335 LEU B CB    
3080 C CG    . LEU B 234 ? 0.15737 0.25498 0.18842 0.03726  0.00176  -0.00044 335 LEU B CG    
3081 C CD1   . LEU B 234 ? 0.16661 0.23615 0.19299 0.04119  0.01215  0.00262  335 LEU B CD1   
3082 C CD2   . LEU B 234 ? 0.19126 0.32019 0.22131 0.04555  -0.00097 -0.00111 335 LEU B CD2   
3083 N N     . MET B 235 ? 0.16300 0.19932 0.21290 0.03110  0.00383  -0.00234 336 MET B N     
3084 C CA    . MET B 235 ? 0.15387 0.18136 0.23180 0.03898  0.00048  -0.00681 336 MET B CA    
3085 C C     . MET B 235 ? 0.16473 0.19711 0.26498 0.04917  0.00114  -0.00905 336 MET B C     
3086 O O     . MET B 235 ? 0.17686 0.20277 0.28101 0.04808  -0.00497 -0.01167 336 MET B O     
3087 C CB    . MET B 235 ? 0.22147 0.22107 0.30694 0.03906  0.00707  -0.00476 336 MET B CB    
3088 C CG    . MET B 235 ? 0.21253 0.19832 0.26417 0.02813  0.00791  -0.00128 336 MET B CG    
3089 S SD    . MET B 235 ? 0.23506 0.22419 0.27419 0.02115  -0.00595 -0.00485 336 MET B SD    
3090 C CE    . MET B 235 ? 0.19226 0.18213 0.26909 0.03517  -0.01401 -0.01231 336 MET B CE    
3091 N N     . ASN B 236 ? 0.14950 0.18761 0.24394 0.05301  0.00782  -0.00622 337 ASN B N     
3092 C CA    . ASN B 236 ? 0.20596 0.23901 0.29902 0.05611  0.00758  -0.00643 337 ASN B CA    
3093 C C     . ASN B 236 ? 0.25396 0.30340 0.33903 0.06075  0.00891  -0.00259 337 ASN B C     
3094 O O     . ASN B 236 ? 0.22876 0.27345 0.30595 0.06558  0.00810  -0.00687 337 ASN B O     
3095 C CB    . ASN B 236 ? 0.20239 0.21617 0.30000 0.05349  0.01648  -0.00340 337 ASN B CB    
3096 C CG    . ASN B 236 ? 0.17216 0.18289 0.25865 0.05565  0.02638  0.00089  337 ASN B CG    
3097 O OD1   . ASN B 236 ? 0.19135 0.21212 0.26833 0.05757  0.02813  0.00224  337 ASN B OD1   
3098 N ND2   . ASN B 236 ? 0.24814 0.24597 0.33436 0.05599  0.03513  0.00571  337 ASN B ND2   
3099 O OXT   . ASN B 236 ? 0.19804 0.26673 0.28252 0.05746  0.00161  -0.00711 337 ASN B OXT   
3100 C C96   . H71 C .   ? 0.90454 0.63374 0.53382 0.14117  0.00101  0.06598  401 H71 A C96   
3101 C C95   . H71 C .   ? 0.86003 0.61417 0.52547 0.16499  0.03307  0.06443  401 H71 A C95   
3102 C C97   . H71 C .   ? 0.88733 0.59017 0.50874 0.20535  0.01775  0.03144  401 H71 A C97   
3103 N N94   . H71 C .   ? 0.70189 0.48862 0.46329 0.19698  0.05041  0.04500  401 H71 A N94   
3104 C C93   . H71 C .   ? 0.49237 0.33787 0.34947 0.22040  0.08486  0.03914  401 H71 A C93   
3126 C "C2'" . H71 C .   ? 0.51551 0.46879 0.42699 0.28856  0.07596  0.03927  401 H71 A "C2'" 
3127 I I     . H71 C .   ? 0.82196 0.69988 0.60271 0.22688  0.07825  0.03143  401 H71 A I     
3128 O O1    . PG4 D .   ? 0.48772 0.67475 0.55144 -0.01186 -0.17380 -0.00399 402 PG4 A O1    
3129 C C1    . PG4 D .   ? 0.60718 0.77561 0.64316 -0.00497 -0.15453 0.00424  402 PG4 A C1    
3130 C C2    . PG4 D .   ? 0.46015 0.61072 0.46532 0.01347  -0.13759 -0.02196 402 PG4 A C2    
3131 O O2    . PG4 D .   ? 0.74166 0.89695 0.71397 0.03365  -0.10977 -0.03098 402 PG4 A O2    
3132 C C3    . PG4 D .   ? 0.61221 0.75068 0.54803 0.05285  -0.10205 -0.05511 402 PG4 A C3    
3133 C C4    . PG4 D .   ? 0.44938 0.60785 0.37341 0.06505  -0.06945 -0.04777 402 PG4 A C4    
3134 O O3    . PG4 D .   ? 0.69044 0.86151 0.61887 0.05880  -0.06674 -0.03387 402 PG4 A O3    
3135 C C5    . PG4 D .   ? 0.32920 0.51117 0.25650 0.06392  -0.04302 -0.02288 402 PG4 A C5    
3136 C C6    . PG4 D .   ? 0.53343 0.72042 0.46101 0.05942  -0.04374 -0.01245 402 PG4 A C6    
3137 O O4    . PG4 D .   ? 0.51473 0.70825 0.42297 0.06559  -0.04585 -0.01705 402 PG4 A O4    
3138 O O1    . PG4 E .   ? 0.32384 0.50602 0.33525 0.03972  -0.04373 0.00627  403 PG4 A O1    
3139 C C1    . PG4 E .   ? 0.28789 0.45973 0.29571 0.04278  -0.03849 -0.00354 403 PG4 A C1    
3140 C C2    . PG4 E .   ? 0.28318 0.45163 0.26279 0.05490  -0.02127 -0.01078 403 PG4 A C2    
3141 O O2    . PG4 E .   ? 0.48973 0.65084 0.47189 0.05568  -0.00238 0.00185  403 PG4 A O2    
3142 C C3    . PG4 E .   ? 0.09226 0.24071 0.07455 0.05686  0.00175  0.00340  403 PG4 A C3    
3143 C C4    . PG4 E .   ? 0.31771 0.43882 0.30349 0.05060  0.00636  0.01443  403 PG4 A C4    
3144 O O3    . PG4 E .   ? 0.40482 0.53870 0.38675 0.05653  0.00706  0.01878  403 PG4 A O3    
3145 O O1    . PG4 F .   ? 0.41097 0.59054 0.26687 0.06444  -0.10972 -0.04314 404 PG4 A O1    
3146 C C1    . PG4 F .   ? 0.46417 0.63133 0.33982 0.05156  -0.12688 -0.04212 404 PG4 A C1    
3147 C C2    . PG4 F .   ? 0.41826 0.56949 0.28920 0.04046  -0.16364 -0.04861 404 PG4 A C2    
3148 O O2    . PG4 F .   ? 0.64822 0.78678 0.53606 0.03023  -0.18242 -0.05154 404 PG4 A O2    
3149 C C3    . PG4 F .   ? 0.49878 0.65850 0.43238 0.00957  -0.18348 -0.02365 404 PG4 A C3    
3150 C C4    . PG4 F .   ? 0.50821 0.66369 0.45996 0.00440  -0.18835 -0.02703 404 PG4 A C4    
3151 O O3    . PG4 F .   ? 0.70214 0.85776 0.65760 0.01610  -0.15912 -0.02513 404 PG4 A O3    
3153 C C96   . H71 H .   ? 0.92715 0.74596 0.35227 -0.07608 -0.00360 0.13185  401 H71 B C96   
3154 C C95   . H71 H .   ? 0.91340 0.67148 0.41558 -0.08592 0.01702  0.12869  401 H71 B C95   
3155 C C97   . H71 H .   ? 0.94843 0.62662 0.42473 -0.11651 0.02392  0.18841  401 H71 B C97   
3156 N N94   . H71 H .   ? 0.75032 0.53878 0.38016 -0.09092 0.00949  0.08622  401 H71 B N94   
3157 C C93   . H71 H .   ? 0.50744 0.37551 0.30684 -0.12281 0.01805  0.08408  401 H71 B C93   
3179 C "C2'" . H71 H .   ? 0.54190 0.47073 0.44933 -0.29647 0.04207  -0.06798 401 H71 B "C2'" 
3180 I I     . H71 H .   ? 0.85910 0.66270 0.65035 -0.23699 0.04927  -0.06703 401 H71 B I     
3182 C C     . ACT J .   ? 0.44554 0.69132 0.62604 -0.09624 -0.11524 -0.10589 403 ACT B C     
3183 O O     . ACT J .   ? 0.50138 0.74371 0.69765 -0.09214 -0.12756 -0.09827 403 ACT B O     
3184 O OXT   . ACT J .   ? 0.51643 0.75513 0.66862 -0.09720 -0.11256 -0.09720 403 ACT B OXT   
3185 C CH3   . ACT J .   ? 0.25701 0.51782 0.45533 -0.10081 -0.09985 -0.13023 403 ACT B CH3   
3186 O O2    . PG4 K .   ? 0.51746 0.63599 0.44641 -0.09638 -0.06736 0.04060  404 PG4 B O2    
3187 C C3    . PG4 K .   ? 0.21725 0.33416 0.14908 -0.09236 -0.07257 0.03871  404 PG4 B C3    
3188 C C4    . PG4 K .   ? 0.39756 0.51977 0.33388 -0.08830 -0.07604 0.03272  404 PG4 B C4    
3189 O O3    . PG4 K .   ? 0.52169 0.64195 0.45957 -0.08552 -0.08285 0.03101  404 PG4 B O3    
3190 C C5    . PG4 K .   ? 0.22377 0.35072 0.16725 -0.08269 -0.08495 0.02449  404 PG4 B C5    
3191 C C6    . PG4 K .   ? 0.46025 0.58637 0.40564 -0.08106 -0.09101 0.02331  404 PG4 B C6    
3192 O O4    . PG4 K .   ? 0.62070 0.75270 0.56664 -0.08183 -0.08810 0.02027  404 PG4 B O4    
3193 C C1    . PEG L .   ? 0.35532 0.54886 0.33454 -0.09898 -0.07101 -0.03606 405 PEG B C1    
3194 O O1    . PEG L .   ? 0.51009 0.69647 0.47359 -0.10006 -0.06508 -0.02594 405 PEG B O1    
3195 C C2    . PEG L .   ? 0.40243 0.59375 0.39234 -0.09302 -0.07916 -0.03583 405 PEG B C2    
3196 O O2    . PEG L .   ? 0.69917 0.89029 0.70606 -0.08939 -0.08916 -0.03997 405 PEG B O2    
3197 C C3    . PEG L .   ? 0.64042 0.82021 0.64277 -0.08446 -0.09385 -0.03180 405 PEG B C3    
3198 C C4    . PEG L .   ? 0.62454 0.79620 0.62594 -0.07903 -0.09954 -0.02538 405 PEG B C4    
3199 O O4    . PEG L .   ? 0.57237 0.73688 0.55575 -0.07942 -0.09207 -0.01617 405 PEG B O4    
3200 C C1    . PEG M .   ? 0.63538 0.78072 0.60581 -0.07514 -0.09439 -0.00024 406 PEG B C1    
3201 O O1    . PEG M .   ? 0.47672 0.62108 0.45886 -0.07070 -0.10460 -0.00372 406 PEG B O1    
3202 C C2    . PEG M .   ? 0.21940 0.36257 0.18294 -0.07773 -0.08900 0.00379  406 PEG B C2    
3203 O O2    . PEG M .   ? 0.43589 0.58295 0.39217 -0.08281 -0.08046 0.00531  406 PEG B O2    
3204 C C3    . PEG M .   ? 0.25351 0.39818 0.20221 -0.08547 -0.07554 0.01233  406 PEG B C3    
3205 C C4    . PEG M .   ? 0.46567 0.61437 0.40908 -0.09093 -0.06783 0.01413  406 PEG B C4    
3206 O O4    . PEG M .   ? 0.63387 0.78988 0.57838 -0.09248 -0.06589 0.00855  406 PEG B O4    
3208 C C     . ACT O .   ? 0.41041 0.54415 0.64416 0.05851  -0.18387 -0.19420 408 ACT B C     
3209 O O     . ACT O .   ? 0.45806 0.56893 0.65203 0.06343  -0.17082 -0.19381 408 ACT B O     
3210 O OXT   . ACT O .   ? 0.38990 0.53337 0.66802 0.06109  -0.18938 -0.24325 408 ACT B OXT   
3211 C CH3   . ACT O .   ? 0.38552 0.55120 0.56137 0.04326  -0.18385 -0.16794 408 ACT B CH3   
# 
