data_8QSA
# 
_entry.id   8QSA 
# 
_audit_conform.dict_name       mmcif_pdbx.dic 
_audit_conform.dict_version    5.403 
_audit_conform.dict_location   http://mmcif.pdb.org/dictionaries/ascii/mmcif_pdbx.dic 
# 
loop_
_database_2.database_id 
_database_2.database_code 
_database_2.pdbx_database_accession 
_database_2.pdbx_DOI 
PDB   8QSA         pdb_00008qsa 10.2210/pdb8qsa/pdb 
WWPDB D_1292132199 ?            ?                   
# 
_pdbx_audit_revision_history.ordinal             1 
_pdbx_audit_revision_history.data_content_type   'Structure model' 
_pdbx_audit_revision_history.major_revision      1 
_pdbx_audit_revision_history.minor_revision      0 
_pdbx_audit_revision_history.revision_date       2025-04-23 
_pdbx_audit_revision_history.part_number         ? 
# 
_pdbx_audit_revision_details.ordinal             1 
_pdbx_audit_revision_details.revision_ordinal    1 
_pdbx_audit_revision_details.data_content_type   'Structure model' 
_pdbx_audit_revision_details.provider            repository 
_pdbx_audit_revision_details.type                'Initial release' 
_pdbx_audit_revision_details.description         ? 
_pdbx_audit_revision_details.details             ? 
# 
_pdbx_database_status.status_code                     REL 
_pdbx_database_status.status_code_sf                  REL 
_pdbx_database_status.status_code_mr                  ? 
_pdbx_database_status.entry_id                        8QSA 
_pdbx_database_status.recvd_initial_deposition_date   2023-10-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    PDBE 
_pdbx_database_status.process_site                    PDBE 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           Y 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              michelle.arkin@ucsf.edu 
_pdbx_contact_author.name_first         Michelle 
_pdbx_contact_author.name_last          Arkin 
_pdbx_contact_author.name_mi            ? 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9366-6770 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Konstantinidou, M.' 1  ? 
'Vickery, H.'        2  ? 
'Pennings, M.A.M.'   3  ? 
'Virta, J.'          4  ? 
'Visser, E.J.'       5  ? 
'Oetelaar, M.C.M.'   6  ? 
'Overmans, M.'       7  ? 
'Neitz, J.'          8  ? 
'Ottmann, C.'        9  ? 
'Brunsveld, L.'      10 ? 
'Arkin, M.R.'        11 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   ? 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'To Be Published' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            0353 
_citation.journal_id_ISSN           ? 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     'Small molecule stabilization of the 14-3-3sigma/CRAF complex inhibits the MAPK pathway' 
_citation.year                      ? 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      ? 
_citation.pdbx_database_id_PubMed   ? 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Konstantinidou, M.' 1  ? 
primary 'Vickery, H.'        2  ? 
primary 'Pennings, M.A.M.'   3  ? 
primary 'Virta, J.'          4  ? 
primary 'Visser, E.J.'       5  ? 
primary 'Oetelaar, M.C.M.'   6  ? 
primary 'Overmans, M.'       7  ? 
primary 'Neitz, J.'          8  ? 
primary 'Ottmann, C.'        9  ? 
primary 'Brunsveld, L.'      10 ? 
primary 'Arkin, M.R.'        11 ? 
# 
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 '14-3-3 protein sigma'                                                                                     
26542.914 1   ? ? ? ? 
2 polymer     syn 'C-RAF peptide'                                                                                            
1208.175  1   ? ? ? ? 
3 non-polymer syn 'CHLORIDE ION'                                                                                             
35.453    1   ? ? ? ? 
4 non-polymer syn 'MAGNESIUM ION'                                                                                            
24.305    3   ? ? ? ? 
5 non-polymer syn '1-[(5~{R})-2-(4-bromanyl-3-fluoranyl-phenyl)sulfonyl-2,7-diazaspiro[4.4]nonan-7-yl]-2-chloranyl-ethanone' 
439.727   1   ? ? ? ? 
6 water       nat water                                                                                                      
18.015    171 ? ? ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Epithelial cell marker protein 1,Stratifin' 
# 
loop_
_entity_poly.entity_id 
_entity_poly.type 
_entity_poly.nstd_linkage 
_entity_poly.nstd_monomer 
_entity_poly.pdbx_seq_one_letter_code 
_entity_poly.pdbx_seq_one_letter_code_can 
_entity_poly.pdbx_strand_id 
_entity_poly.pdbx_target_identifier 
1 'polypeptide(L)' no no  
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
;GAMGSMERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSE
EKGPEVREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAM
DISKKEMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
A ? 
2 'polypeptide(L)' no yes 'QRST(SEP)TPNVH' QRSTSTPNVH P ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
3 'CHLORIDE ION'                                                                                             CL  
4 'MAGNESIUM ION'                                                                                            MG  
5 '1-[(5~{R})-2-(4-bromanyl-3-fluoranyl-phenyl)sulfonyl-2,7-diazaspiro[4.4]nonan-7-yl]-2-chloranyl-ethanone' WQ9 
6 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   ALA n 
1 3   MET n 
1 4   GLY n 
1 5   SER n 
1 6   MET n 
1 7   GLU n 
1 8   ARG n 
1 9   ALA n 
1 10  SER n 
1 11  LEU n 
1 12  ILE n 
1 13  GLN n 
1 14  LYS n 
1 15  ALA n 
1 16  LYS n 
1 17  LEU n 
1 18  ALA n 
1 19  GLU n 
1 20  GLN n 
1 21  ALA n 
1 22  GLU n 
1 23  ARG n 
1 24  TYR n 
1 25  GLU n 
1 26  ASP n 
1 27  MET n 
1 28  ALA n 
1 29  ALA n 
1 30  PHE n 
1 31  MET n 
1 32  LYS n 
1 33  GLY n 
1 34  ALA n 
1 35  VAL n 
1 36  GLU n 
1 37  LYS n 
1 38  GLY n 
1 39  GLU n 
1 40  GLU n 
1 41  LEU n 
1 42  SER n 
1 43  CYS n 
1 44  GLU n 
1 45  GLU n 
1 46  ARG n 
1 47  ASN n 
1 48  LEU n 
1 49  LEU n 
1 50  SER n 
1 51  VAL n 
1 52  ALA n 
1 53  TYR n 
1 54  LYS n 
1 55  ASN n 
1 56  VAL n 
1 57  VAL n 
1 58  GLY n 
1 59  GLY n 
1 60  GLN n 
1 61  ARG n 
1 62  ALA n 
1 63  ALA n 
1 64  TRP n 
1 65  ARG n 
1 66  VAL n 
1 67  LEU n 
1 68  SER n 
1 69  SER n 
1 70  ILE n 
1 71  GLU n 
1 72  GLN n 
1 73  LYS n 
1 74  SER n 
1 75  ASN n 
1 76  GLU n 
1 77  GLU n 
1 78  GLY n 
1 79  SER n 
1 80  GLU n 
1 81  GLU n 
1 82  LYS n 
1 83  GLY n 
1 84  PRO n 
1 85  GLU n 
1 86  VAL n 
1 87  ARG n 
1 88  GLU n 
1 89  TYR n 
1 90  ARG n 
1 91  GLU n 
1 92  LYS n 
1 93  VAL n 
1 94  GLU n 
1 95  THR n 
1 96  GLU n 
1 97  LEU n 
1 98  GLN n 
1 99  GLY n 
1 100 VAL n 
1 101 CYS n 
1 102 ASP n 
1 103 THR n 
1 104 VAL n 
1 105 LEU n 
1 106 GLY n 
1 107 LEU n 
1 108 LEU n 
1 109 ASP n 
1 110 SER n 
1 111 HIS n 
1 112 LEU n 
1 113 ILE n 
1 114 LYS n 
1 115 GLU n 
1 116 ALA n 
1 117 GLY n 
1 118 ASP n 
1 119 ALA n 
1 120 GLU n 
1 121 SER n 
1 122 ARG n 
1 123 VAL n 
1 124 PHE n 
1 125 TYR n 
1 126 LEU n 
1 127 LYS n 
1 128 MET n 
1 129 LYS n 
1 130 GLY n 
1 131 ASP n 
1 132 TYR n 
1 133 TYR n 
1 134 ARG n 
1 135 TYR n 
1 136 LEU n 
1 137 ALA n 
1 138 GLU n 
1 139 VAL n 
1 140 ALA n 
1 141 THR n 
1 142 GLY n 
1 143 ASP n 
1 144 ASP n 
1 145 LYS n 
1 146 LYS n 
1 147 ARG n 
1 148 ILE n 
1 149 ILE n 
1 150 ASP n 
1 151 SER n 
1 152 ALA n 
1 153 ARG n 
1 154 SER n 
1 155 ALA n 
1 156 TYR n 
1 157 GLN n 
1 158 GLU n 
1 159 ALA n 
1 160 MET n 
1 161 ASP n 
1 162 ILE n 
1 163 SER n 
1 164 LYS n 
1 165 LYS n 
1 166 GLU n 
1 167 MET n 
1 168 PRO n 
1 169 PRO n 
1 170 THR n 
1 171 ASN n 
1 172 PRO n 
1 173 ILE n 
1 174 ARG n 
1 175 LEU n 
1 176 GLY n 
1 177 LEU n 
1 178 ALA n 
1 179 LEU n 
1 180 ASN n 
1 181 PHE n 
1 182 SER n 
1 183 VAL n 
1 184 PHE n 
1 185 HIS n 
1 186 TYR n 
1 187 GLU n 
1 188 ILE n 
1 189 ALA n 
1 190 ASN n 
1 191 SER n 
1 192 PRO n 
1 193 GLU n 
1 194 GLU n 
1 195 ALA n 
1 196 ILE n 
1 197 SER n 
1 198 LEU n 
1 199 ALA n 
1 200 LYS n 
1 201 THR n 
1 202 THR n 
1 203 PHE n 
1 204 ASP n 
1 205 GLU n 
1 206 ALA n 
1 207 MET n 
1 208 ALA n 
1 209 ASP n 
1 210 LEU n 
1 211 HIS n 
1 212 THR n 
1 213 LEU n 
1 214 SER n 
1 215 GLU n 
1 216 ASP n 
1 217 SER n 
1 218 TYR n 
1 219 LYS n 
1 220 ASP n 
1 221 SER n 
1 222 THR n 
1 223 LEU n 
1 224 ILE n 
1 225 MET n 
1 226 GLN n 
1 227 LEU n 
1 228 LEU n 
1 229 ARG n 
1 230 ASP n 
1 231 ASN n 
1 232 LEU n 
1 233 THR n 
1 234 LEU n 
1 235 TRP n 
1 236 THR n 
2 1   GLN n 
2 2   ARG n 
2 3   SER n 
2 4   THR n 
2 5   SEP n 
2 6   THR n 
2 7   PRO n 
2 8   ASN n 
2 9   VAL n 
2 10  HIS n 
# 
_entity_src_gen.entity_id                          1 
_entity_src_gen.pdbx_src_id                        1 
_entity_src_gen.pdbx_alt_source_flag               sample 
_entity_src_gen.pdbx_seq_type                      'Biological sequence' 
_entity_src_gen.pdbx_beg_seq_num                   1 
_entity_src_gen.pdbx_end_seq_num                   236 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'SFN, HME1' 
_entity_src_gen.gene_src_species                   ? 
_entity_src_gen.gene_src_strain                    ? 
_entity_src_gen.gene_src_tissue                    ? 
_entity_src_gen.gene_src_tissue_fraction           ? 
_entity_src_gen.gene_src_details                   ? 
_entity_src_gen.pdbx_gene_src_fragment             ? 
_entity_src_gen.pdbx_gene_src_scientific_name      'Homo sapiens' 
_entity_src_gen.pdbx_gene_src_ncbi_taxonomy_id     9606 
_entity_src_gen.pdbx_gene_src_variant              ? 
_entity_src_gen.pdbx_gene_src_cell_line            ? 
_entity_src_gen.pdbx_gene_src_atcc                 ? 
_entity_src_gen.pdbx_gene_src_organ                ? 
_entity_src_gen.pdbx_gene_src_organelle            ? 
_entity_src_gen.pdbx_gene_src_cell                 ? 
_entity_src_gen.pdbx_gene_src_cellular_location    ? 
_entity_src_gen.host_org_common_name               ? 
_entity_src_gen.pdbx_host_org_scientific_name      'Escherichia coli' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     562 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
_pdbx_entity_src_syn.entity_id              2 
_pdbx_entity_src_syn.pdbx_src_id            1 
_pdbx_entity_src_syn.pdbx_alt_source_flag   sample 
_pdbx_entity_src_syn.pdbx_beg_seq_num       1 
_pdbx_entity_src_syn.pdbx_end_seq_num       10 
_pdbx_entity_src_syn.organism_scientific    'Homo sapiens' 
_pdbx_entity_src_syn.organism_common_name   ? 
_pdbx_entity_src_syn.ncbi_taxonomy_id       9606 
_pdbx_entity_src_syn.details                ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
ALA 'L-peptide linking' y ALANINE ?               'C3 H7 N O2'              89.093  
ARG 'L-peptide linking' y ARGININE ?               'C6 H15 N4 O2 1'          175.209 
ASN 'L-peptide linking' y ASPARAGINE ?               'C4 H8 N2 O3'             132.118 
ASP 'L-peptide linking' y 'ASPARTIC ACID' ?               'C4 H7 N O4'              133.103 
CL  non-polymer         . 'CHLORIDE ION' ?               'Cl -1'                   35.453  
CYS 'L-peptide linking' y CYSTEINE ?               'C3 H7 N O2 S'            121.158 
GLN 'L-peptide linking' y GLUTAMINE ?               'C5 H10 N2 O3'            146.144 
GLU 'L-peptide linking' y 'GLUTAMIC ACID' ?               'C5 H9 N O4'              147.129 
GLY 'peptide linking'   y GLYCINE ?               'C2 H5 N O2'              75.067  
HIS 'L-peptide linking' y HISTIDINE ?               'C6 H10 N3 O2 1'          156.162 
HOH non-polymer         . WATER ?               'H2 O'                    18.015  
ILE 'L-peptide linking' y ISOLEUCINE ?               'C6 H13 N O2'             131.173 
LEU 'L-peptide linking' y LEUCINE ?               'C6 H13 N O2'             131.173 
LYS 'L-peptide linking' y LYSINE ?               'C6 H15 N2 O2 1'          147.195 
MET 'L-peptide linking' y METHIONINE ?               'C5 H11 N O2 S'           149.211 
MG  non-polymer         . 'MAGNESIUM ION' ?               'Mg 2'                    24.305  
PHE 'L-peptide linking' y PHENYLALANINE ?               'C9 H11 N O2'             165.189 
PRO 'L-peptide linking' y PROLINE ?               'C5 H9 N O2'              115.130 
SEP 'L-peptide linking' n PHOSPHOSERINE PHOSPHONOSERINE 'C3 H8 N O6 P'            185.072 
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 
WQ9 non-polymer         . 
'1-[(5~{R})-2-(4-bromanyl-3-fluoranyl-phenyl)sulfonyl-2,7-diazaspiro[4.4]nonan-7-yl]-2-chloranyl-ethanone' ?               
'C15 H17 Br Cl F N2 O3 S' 439.727 
# 
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   -4  -4  GLY GLY A . n 
A 1 2   ALA 2   -3  -3  ALA ALA A . n 
A 1 3   MET 3   -2  -2  MET MET A . n 
A 1 4   GLY 4   -1  -1  GLY GLY A . n 
A 1 5   SER 5   0   0   SER SER A . n 
A 1 6   MET 6   1   1   MET MET A . n 
A 1 7   GLU 7   2   2   GLU GLU A . n 
A 1 8   ARG 8   3   3   ARG ARG A . n 
A 1 9   ALA 9   4   4   ALA ALA A . n 
A 1 10  SER 10  5   5   SER SER A . n 
A 1 11  LEU 11  6   6   LEU LEU A . n 
A 1 12  ILE 12  7   7   ILE ILE A . n 
A 1 13  GLN 13  8   8   GLN GLN A . n 
A 1 14  LYS 14  9   9   LYS LYS A . n 
A 1 15  ALA 15  10  10  ALA ALA A . n 
A 1 16  LYS 16  11  11  LYS LYS A . n 
A 1 17  LEU 17  12  12  LEU LEU A . n 
A 1 18  ALA 18  13  13  ALA ALA A . n 
A 1 19  GLU 19  14  14  GLU GLU A . n 
A 1 20  GLN 20  15  15  GLN GLN A . n 
A 1 21  ALA 21  16  16  ALA ALA A . n 
A 1 22  GLU 22  17  17  GLU GLU A . n 
A 1 23  ARG 23  18  18  ARG ARG A . n 
A 1 24  TYR 24  19  19  TYR TYR A . n 
A 1 25  GLU 25  20  20  GLU GLU A . n 
A 1 26  ASP 26  21  21  ASP ASP A . n 
A 1 27  MET 27  22  22  MET MET A . n 
A 1 28  ALA 28  23  23  ALA ALA A . n 
A 1 29  ALA 29  24  24  ALA ALA A . n 
A 1 30  PHE 30  25  25  PHE PHE A . n 
A 1 31  MET 31  26  26  MET MET A . n 
A 1 32  LYS 32  27  27  LYS LYS A . n 
A 1 33  GLY 33  28  28  GLY GLY A . n 
A 1 34  ALA 34  29  29  ALA ALA A . n 
A 1 35  VAL 35  30  30  VAL VAL A . n 
A 1 36  GLU 36  31  31  GLU GLU A . n 
A 1 37  LYS 37  32  32  LYS LYS A . n 
A 1 38  GLY 38  33  33  GLY GLY A . n 
A 1 39  GLU 39  34  34  GLU GLU A . n 
A 1 40  GLU 40  35  35  GLU GLU A . n 
A 1 41  LEU 41  36  36  LEU LEU A . n 
A 1 42  SER 42  37  37  SER SER A . n 
A 1 43  CYS 43  38  38  CYS CSO A . n 
A 1 44  GLU 44  39  39  GLU GLU A . n 
A 1 45  GLU 45  40  40  GLU GLU A . n 
A 1 46  ARG 46  41  41  ARG ARG A . n 
A 1 47  ASN 47  42  42  ASN ASN A . n 
A 1 48  LEU 48  43  43  LEU LEU A . n 
A 1 49  LEU 49  44  44  LEU LEU A . n 
A 1 50  SER 50  45  45  SER SER A . n 
A 1 51  VAL 51  46  46  VAL VAL A . n 
A 1 52  ALA 52  47  47  ALA ALA A . n 
A 1 53  TYR 53  48  48  TYR TYR A . n 
A 1 54  LYS 54  49  49  LYS LYS A . n 
A 1 55  ASN 55  50  50  ASN ASN A . n 
A 1 56  VAL 56  51  51  VAL VAL A . n 
A 1 57  VAL 57  52  52  VAL VAL A . n 
A 1 58  GLY 58  53  53  GLY GLY A . n 
A 1 59  GLY 59  54  54  GLY GLY A . n 
A 1 60  GLN 60  55  55  GLN GLN A . n 
A 1 61  ARG 61  56  56  ARG ARG A . n 
A 1 62  ALA 62  57  57  ALA ALA A . n 
A 1 63  ALA 63  58  58  ALA ALA A . n 
A 1 64  TRP 64  59  59  TRP TRP A . n 
A 1 65  ARG 65  60  60  ARG ARG A . n 
A 1 66  VAL 66  61  61  VAL VAL A . n 
A 1 67  LEU 67  62  62  LEU LEU A . n 
A 1 68  SER 68  63  63  SER SER A . n 
A 1 69  SER 69  64  64  SER SER A . n 
A 1 70  ILE 70  65  65  ILE ILE A . n 
A 1 71  GLU 71  66  66  GLU GLU A . n 
A 1 72  GLN 72  67  67  GLN GLN A . n 
A 1 73  LYS 73  68  68  LYS LYS A . n 
A 1 74  SER 74  69  69  SER SER A . n 
A 1 75  ASN 75  70  70  ASN ASN A . n 
A 1 76  GLU 76  71  71  GLU GLU A . n 
A 1 77  GLU 77  72  ?   ?   ?   A . n 
A 1 78  GLY 78  73  ?   ?   ?   A . n 
A 1 79  SER 79  74  ?   ?   ?   A . n 
A 1 80  GLU 80  75  ?   ?   ?   A . n 
A 1 81  GLU 81  76  ?   ?   ?   A . n 
A 1 82  LYS 82  77  77  LYS LYS A . n 
A 1 83  GLY 83  78  78  GLY GLY A . n 
A 1 84  PRO 84  79  79  PRO PRO A . n 
A 1 85  GLU 85  80  80  GLU GLU A . n 
A 1 86  VAL 86  81  81  VAL VAL A . n 
A 1 87  ARG 87  82  82  ARG ARG A . n 
A 1 88  GLU 88  83  83  GLU GLU A . n 
A 1 89  TYR 89  84  84  TYR TYR A . n 
A 1 90  ARG 90  85  85  ARG ARG A . n 
A 1 91  GLU 91  86  86  GLU GLU A . n 
A 1 92  LYS 92  87  87  LYS LYS A . n 
A 1 93  VAL 93  88  88  VAL VAL A . n 
A 1 94  GLU 94  89  89  GLU GLU A . n 
A 1 95  THR 95  90  90  THR THR A . n 
A 1 96  GLU 96  91  91  GLU GLU A . n 
A 1 97  LEU 97  92  92  LEU LEU A . n 
A 1 98  GLN 98  93  93  GLN GLN A . n 
A 1 99  GLY 99  94  94  GLY GLY A . n 
A 1 100 VAL 100 95  95  VAL VAL A . n 
A 1 101 CYS 101 96  96  CYS CYS A . n 
A 1 102 ASP 102 97  97  ASP ASP A . n 
A 1 103 THR 103 98  98  THR THR A . n 
A 1 104 VAL 104 99  99  VAL VAL A . n 
A 1 105 LEU 105 100 100 LEU LEU A . n 
A 1 106 GLY 106 101 101 GLY GLY A . n 
A 1 107 LEU 107 102 102 LEU LEU A . n 
A 1 108 LEU 108 103 103 LEU LEU A . n 
A 1 109 ASP 109 104 104 ASP ASP A . n 
A 1 110 SER 110 105 105 SER SER A . n 
A 1 111 HIS 111 106 106 HIS HIS A . n 
A 1 112 LEU 112 107 107 LEU LEU A . n 
A 1 113 ILE 113 108 108 ILE ILE A . n 
A 1 114 LYS 114 109 109 LYS LYS A . n 
A 1 115 GLU 115 110 110 GLU GLU A . n 
A 1 116 ALA 116 111 111 ALA ALA A . n 
A 1 117 GLY 117 112 112 GLY GLY A . n 
A 1 118 ASP 118 113 113 ASP ASP A . n 
A 1 119 ALA 119 114 114 ALA ALA A . n 
A 1 120 GLU 120 115 115 GLU GLU A . n 
A 1 121 SER 121 116 116 SER SER A . n 
A 1 122 ARG 122 117 117 ARG ARG A . n 
A 1 123 VAL 123 118 118 VAL VAL A . n 
A 1 124 PHE 124 119 119 PHE PHE A . n 
A 1 125 TYR 125 120 120 TYR TYR A . n 
A 1 126 LEU 126 121 121 LEU LEU A . n 
A 1 127 LYS 127 122 122 LYS LYS A . n 
A 1 128 MET 128 123 123 MET MET A . n 
A 1 129 LYS 129 124 124 LYS LYS A . n 
A 1 130 GLY 130 125 125 GLY GLY A . n 
A 1 131 ASP 131 126 126 ASP ASP A . n 
A 1 132 TYR 132 127 127 TYR TYR A . n 
A 1 133 TYR 133 128 128 TYR TYR A . n 
A 1 134 ARG 134 129 129 ARG ARG A . n 
A 1 135 TYR 135 130 130 TYR TYR A . n 
A 1 136 LEU 136 131 131 LEU LEU A . n 
A 1 137 ALA 137 132 132 ALA ALA A . n 
A 1 138 GLU 138 133 133 GLU GLU A . n 
A 1 139 VAL 139 134 134 VAL VAL A . n 
A 1 140 ALA 140 135 135 ALA ALA A . n 
A 1 141 THR 141 136 136 THR THR A . n 
A 1 142 GLY 142 137 137 GLY GLY A . n 
A 1 143 ASP 143 138 138 ASP ASP A . n 
A 1 144 ASP 144 139 139 ASP ASP A . n 
A 1 145 LYS 145 140 140 LYS LYS A . n 
A 1 146 LYS 146 141 141 LYS LYS A . n 
A 1 147 ARG 147 142 142 ARG ARG A . n 
A 1 148 ILE 148 143 143 ILE ILE A . n 
A 1 149 ILE 149 144 144 ILE ILE A . n 
A 1 150 ASP 150 145 145 ASP ASP A . n 
A 1 151 SER 151 146 146 SER SER A . n 
A 1 152 ALA 152 147 147 ALA ALA A . n 
A 1 153 ARG 153 148 148 ARG ARG A . n 
A 1 154 SER 154 149 149 SER SER A . n 
A 1 155 ALA 155 150 150 ALA ALA A . n 
A 1 156 TYR 156 151 151 TYR TYR A . n 
A 1 157 GLN 157 152 152 GLN GLN A . n 
A 1 158 GLU 158 153 153 GLU GLU A . n 
A 1 159 ALA 159 154 154 ALA ALA A . n 
A 1 160 MET 160 155 155 MET MET A . n 
A 1 161 ASP 161 156 156 ASP ASP A . n 
A 1 162 ILE 162 157 157 ILE ILE A . n 
A 1 163 SER 163 158 158 SER SER A . n 
A 1 164 LYS 164 159 159 LYS LYS A . n 
A 1 165 LYS 165 160 160 LYS LYS A . n 
A 1 166 GLU 166 161 161 GLU GLU A . n 
A 1 167 MET 167 162 162 MET MET A . n 
A 1 168 PRO 168 163 163 PRO PRO A . n 
A 1 169 PRO 169 164 164 PRO PRO A . n 
A 1 170 THR 170 165 165 THR THR A . n 
A 1 171 ASN 171 166 166 ASN ASN A . n 
A 1 172 PRO 172 167 167 PRO PRO A . n 
A 1 173 ILE 173 168 168 ILE ILE A . n 
A 1 174 ARG 174 169 169 ARG ARG A . n 
A 1 175 LEU 175 170 170 LEU LEU A . n 
A 1 176 GLY 176 171 171 GLY GLY A . n 
A 1 177 LEU 177 172 172 LEU LEU A . n 
A 1 178 ALA 178 173 173 ALA ALA A . n 
A 1 179 LEU 179 174 174 LEU LEU A . n 
A 1 180 ASN 180 175 175 ASN ASN A . n 
A 1 181 PHE 181 176 176 PHE PHE A . n 
A 1 182 SER 182 177 177 SER SER A . n 
A 1 183 VAL 183 178 178 VAL VAL A . n 
A 1 184 PHE 184 179 179 PHE PHE A . n 
A 1 185 HIS 185 180 180 HIS HIS A . n 
A 1 186 TYR 186 181 181 TYR TYR A . n 
A 1 187 GLU 187 182 182 GLU GLU A . n 
A 1 188 ILE 188 183 183 ILE ILE A . n 
A 1 189 ALA 189 184 184 ALA ALA A . n 
A 1 190 ASN 190 185 185 ASN ASN A . n 
A 1 191 SER 191 186 186 SER SER A . n 
A 1 192 PRO 192 187 187 PRO PRO A . n 
A 1 193 GLU 193 188 188 GLU GLU A . n 
A 1 194 GLU 194 189 189 GLU GLU A . n 
A 1 195 ALA 195 190 190 ALA ALA A . n 
A 1 196 ILE 196 191 191 ILE ILE A . n 
A 1 197 SER 197 192 192 SER SER A . n 
A 1 198 LEU 198 193 193 LEU LEU A . n 
A 1 199 ALA 199 194 194 ALA ALA A . n 
A 1 200 LYS 200 195 195 LYS LYS A . n 
A 1 201 THR 201 196 196 THR THR A . n 
A 1 202 THR 202 197 197 THR THR A . n 
A 1 203 PHE 203 198 198 PHE PHE A . n 
A 1 204 ASP 204 199 199 ASP ASP A . n 
A 1 205 GLU 205 200 200 GLU GLU A . n 
A 1 206 ALA 206 201 201 ALA ALA A . n 
A 1 207 MET 207 202 202 MET MET A . n 
A 1 208 ALA 208 203 203 ALA ALA A . n 
A 1 209 ASP 209 204 204 ASP ASP A . n 
A 1 210 LEU 210 205 205 LEU LEU A . n 
A 1 211 HIS 211 206 206 HIS HIS A . n 
A 1 212 THR 212 207 207 THR THR A . n 
A 1 213 LEU 213 208 208 LEU LEU A . n 
A 1 214 SER 214 209 209 SER SER A . n 
A 1 215 GLU 215 210 210 GLU GLU A . n 
A 1 216 ASP 216 211 211 ASP ASP A . n 
A 1 217 SER 217 212 212 SER SER A . n 
A 1 218 TYR 218 213 213 TYR TYR A . n 
A 1 219 LYS 219 214 214 LYS LYS A . n 
A 1 220 ASP 220 215 215 ASP ASP A . n 
A 1 221 SER 221 216 216 SER SER A . n 
A 1 222 THR 222 217 217 THR THR A . n 
A 1 223 LEU 223 218 218 LEU LEU A . n 
A 1 224 ILE 224 219 219 ILE ILE A . n 
A 1 225 MET 225 220 220 MET MET A . n 
A 1 226 GLN 226 221 221 GLN GLN A . n 
A 1 227 LEU 227 222 222 LEU LEU A . n 
A 1 228 LEU 228 223 223 LEU LEU A . n 
A 1 229 ARG 229 224 224 ARG ARG A . n 
A 1 230 ASP 230 225 225 ASP ASP A . n 
A 1 231 ASN 231 226 226 ASN ASN A . n 
A 1 232 LEU 232 227 227 LEU LEU A . n 
A 1 233 THR 233 228 228 THR THR A . n 
A 1 234 LEU 234 229 229 LEU LEU A . n 
A 1 235 TRP 235 230 230 TRP TRP A . n 
A 1 236 THR 236 231 231 THR THR A . n 
B 2 1   GLN 1   255 255 GLN GLN P . n 
B 2 2   ARG 2   256 256 ARG ARG P . n 
B 2 3   SER 3   257 257 SER SER P . n 
B 2 4   THR 4   258 258 THR THR P . n 
B 2 5   SEP 5   259 259 SEP SEP P . n 
B 2 6   THR 6   260 260 THR THR P . n 
B 2 7   PRO 7   261 261 PRO PRO P . n 
B 2 8   ASN 8   262 262 ASN ASN P . n 
B 2 9   VAL 9   263 263 VAL VAL P . n 
B 2 10  HIS 10  264 264 HIS HIS P . n 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 3 CL  1   301 232 CL  CL  A . 
D 4 MG  1   302 233 MG  MG  A . 
E 4 MG  1   303 234 MG  MG  A . 
F 4 MG  1   304 235 MG  MG  A . 
G 5 WQ9 1   305 236 WQ9 384 A . 
H 6 HOH 1   401 179 HOH HOH A . 
H 6 HOH 2   402 170 HOH HOH A . 
H 6 HOH 3   403 50  HOH HOH A . 
H 6 HOH 4   404 175 HOH HOH A . 
H 6 HOH 5   405 139 HOH HOH A . 
H 6 HOH 6   406 1   HOH HOH A . 
H 6 HOH 7   407 100 HOH HOH A . 
H 6 HOH 8   408 184 HOH HOH A . 
H 6 HOH 9   409 149 HOH HOH A . 
H 6 HOH 10  410 45  HOH HOH A . 
H 6 HOH 11  411 20  HOH HOH A . 
H 6 HOH 12  412 114 HOH HOH A . 
H 6 HOH 13  413 165 HOH HOH A . 
H 6 HOH 14  414 58  HOH HOH A . 
H 6 HOH 15  415 91  HOH HOH A . 
H 6 HOH 16  416 73  HOH HOH A . 
H 6 HOH 17  417 39  HOH HOH A . 
H 6 HOH 18  418 31  HOH HOH A . 
H 6 HOH 19  419 111 HOH HOH A . 
H 6 HOH 20  420 48  HOH HOH A . 
H 6 HOH 21  421 37  HOH HOH A . 
H 6 HOH 22  422 82  HOH HOH A . 
H 6 HOH 23  423 99  HOH HOH A . 
H 6 HOH 24  424 109 HOH HOH A . 
H 6 HOH 25  425 22  HOH HOH A . 
H 6 HOH 26  426 163 HOH HOH A . 
H 6 HOH 27  427 80  HOH HOH A . 
H 6 HOH 28  428 75  HOH HOH A . 
H 6 HOH 29  429 8   HOH HOH A . 
H 6 HOH 30  430 2   HOH HOH A . 
H 6 HOH 31  431 98  HOH HOH A . 
H 6 HOH 32  432 70  HOH HOH A . 
H 6 HOH 33  433 52  HOH HOH A . 
H 6 HOH 34  434 137 HOH HOH A . 
H 6 HOH 35  435 19  HOH HOH A . 
H 6 HOH 36  436 110 HOH HOH A . 
H 6 HOH 37  437 74  HOH HOH A . 
H 6 HOH 38  438 117 HOH HOH A . 
H 6 HOH 39  439 34  HOH HOH A . 
H 6 HOH 40  440 89  HOH HOH A . 
H 6 HOH 41  441 46  HOH HOH A . 
H 6 HOH 42  442 13  HOH HOH A . 
H 6 HOH 43  443 78  HOH HOH A . 
H 6 HOH 44  444 17  HOH HOH A . 
H 6 HOH 45  445 86  HOH HOH A . 
H 6 HOH 46  446 118 HOH HOH A . 
H 6 HOH 47  447 54  HOH HOH A . 
H 6 HOH 48  448 32  HOH HOH A . 
H 6 HOH 49  449 95  HOH HOH A . 
H 6 HOH 50  450 9   HOH HOH A . 
H 6 HOH 51  451 27  HOH HOH A . 
H 6 HOH 52  452 14  HOH HOH A . 
H 6 HOH 53  453 162 HOH HOH A . 
H 6 HOH 54  454 26  HOH HOH A . 
H 6 HOH 55  455 67  HOH HOH A . 
H 6 HOH 56  456 11  HOH HOH A . 
H 6 HOH 57  457 71  HOH HOH A . 
H 6 HOH 58  458 30  HOH HOH A . 
H 6 HOH 59  459 64  HOH HOH A . 
H 6 HOH 60  460 85  HOH HOH A . 
H 6 HOH 61  461 36  HOH HOH A . 
H 6 HOH 62  462 93  HOH HOH A . 
H 6 HOH 63  463 115 HOH HOH A . 
H 6 HOH 64  464 69  HOH HOH A . 
H 6 HOH 65  465 122 HOH HOH A . 
H 6 HOH 66  466 15  HOH HOH A . 
H 6 HOH 67  467 143 HOH HOH A . 
H 6 HOH 68  468 92  HOH HOH A . 
H 6 HOH 69  469 47  HOH HOH A . 
H 6 HOH 70  470 61  HOH HOH A . 
H 6 HOH 71  471 33  HOH HOH A . 
H 6 HOH 72  472 132 HOH HOH A . 
H 6 HOH 73  473 28  HOH HOH A . 
H 6 HOH 74  474 66  HOH HOH A . 
H 6 HOH 75  475 150 HOH HOH A . 
H 6 HOH 76  476 79  HOH HOH A . 
H 6 HOH 77  477 178 HOH HOH A . 
H 6 HOH 78  478 56  HOH HOH A . 
H 6 HOH 79  479 23  HOH HOH A . 
H 6 HOH 80  480 96  HOH HOH A . 
H 6 HOH 81  481 167 HOH HOH A . 
H 6 HOH 82  482 38  HOH HOH A . 
H 6 HOH 83  483 63  HOH HOH A . 
H 6 HOH 84  484 29  HOH HOH A . 
H 6 HOH 85  485 155 HOH HOH A . 
H 6 HOH 86  486 55  HOH HOH A . 
H 6 HOH 87  487 166 HOH HOH A . 
H 6 HOH 88  488 87  HOH HOH A . 
H 6 HOH 89  489 10  HOH HOH A . 
H 6 HOH 90  490 21  HOH HOH A . 
H 6 HOH 91  491 185 HOH HOH A . 
H 6 HOH 92  492 106 HOH HOH A . 
H 6 HOH 93  493 158 HOH HOH A . 
H 6 HOH 94  494 88  HOH HOH A . 
H 6 HOH 95  495 41  HOH HOH A . 
H 6 HOH 96  496 153 HOH HOH A . 
H 6 HOH 97  497 6   HOH HOH A . 
H 6 HOH 98  498 136 HOH HOH A . 
H 6 HOH 99  499 43  HOH HOH A . 
H 6 HOH 100 500 5   HOH HOH A . 
H 6 HOH 101 501 126 HOH HOH A . 
H 6 HOH 102 502 160 HOH HOH A . 
H 6 HOH 103 503 181 HOH HOH A . 
H 6 HOH 104 504 120 HOH HOH A . 
H 6 HOH 105 505 24  HOH HOH A . 
H 6 HOH 106 506 59  HOH HOH A . 
H 6 HOH 107 507 171 HOH HOH A . 
H 6 HOH 108 508 125 HOH HOH A . 
H 6 HOH 109 509 7   HOH HOH A . 
H 6 HOH 110 510 12  HOH HOH A . 
H 6 HOH 111 511 51  HOH HOH A . 
H 6 HOH 112 512 140 HOH HOH A . 
H 6 HOH 113 513 3   HOH HOH A . 
H 6 HOH 114 514 77  HOH HOH A . 
H 6 HOH 115 515 40  HOH HOH A . 
H 6 HOH 116 516 112 HOH HOH A . 
H 6 HOH 117 517 134 HOH HOH A . 
H 6 HOH 118 518 42  HOH HOH A . 
H 6 HOH 119 519 152 HOH HOH A . 
H 6 HOH 120 520 180 HOH HOH A . 
H 6 HOH 121 521 62  HOH HOH A . 
H 6 HOH 122 522 173 HOH HOH A . 
H 6 HOH 123 523 83  HOH HOH A . 
H 6 HOH 124 524 108 HOH HOH A . 
H 6 HOH 125 525 151 HOH HOH A . 
H 6 HOH 126 526 60  HOH HOH A . 
H 6 HOH 127 527 105 HOH HOH A . 
H 6 HOH 128 528 123 HOH HOH A . 
H 6 HOH 129 529 84  HOH HOH A . 
H 6 HOH 130 530 157 HOH HOH A . 
H 6 HOH 131 531 4   HOH HOH A . 
H 6 HOH 132 532 182 HOH HOH A . 
H 6 HOH 133 533 131 HOH HOH A . 
H 6 HOH 134 534 133 HOH HOH A . 
H 6 HOH 135 535 138 HOH HOH A . 
H 6 HOH 136 536 142 HOH HOH A . 
H 6 HOH 137 537 135 HOH HOH A . 
H 6 HOH 138 538 145 HOH HOH A . 
H 6 HOH 139 539 103 HOH HOH A . 
H 6 HOH 140 540 68  HOH HOH A . 
H 6 HOH 141 541 49  HOH HOH A . 
H 6 HOH 142 542 16  HOH HOH A . 
H 6 HOH 143 543 72  HOH HOH A . 
H 6 HOH 144 544 172 HOH HOH A . 
H 6 HOH 145 545 124 HOH HOH A . 
H 6 HOH 146 546 144 HOH HOH A . 
H 6 HOH 147 547 164 HOH HOH A . 
H 6 HOH 148 548 90  HOH HOH A . 
H 6 HOH 149 549 141 HOH HOH A . 
H 6 HOH 150 550 81  HOH HOH A . 
H 6 HOH 151 551 104 HOH HOH A . 
H 6 HOH 152 552 94  HOH HOH A . 
H 6 HOH 153 553 169 HOH HOH A . 
H 6 HOH 154 554 57  HOH HOH A . 
H 6 HOH 155 555 113 HOH HOH A . 
H 6 HOH 156 556 128 HOH HOH A . 
H 6 HOH 157 557 148 HOH HOH A . 
H 6 HOH 158 558 127 HOH HOH A . 
H 6 HOH 159 559 183 HOH HOH A . 
H 6 HOH 160 560 119 HOH HOH A . 
H 6 HOH 161 561 130 HOH HOH A . 
I 6 HOH 1   301 65  HOH HOH P . 
I 6 HOH 2   302 35  HOH HOH P . 
I 6 HOH 3   303 116 HOH HOH P . 
I 6 HOH 4   304 107 HOH HOH P . 
I 6 HOH 5   305 44  HOH HOH P . 
I 6 HOH 6   306 53  HOH HOH P . 
I 6 HOH 7   307 18  HOH HOH P . 
I 6 HOH 8   308 25  HOH HOH P . 
I 6 HOH 9   309 154 HOH HOH P . 
I 6 HOH 10  310 146 HOH HOH P . 
# 
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 GLU 71  ? CG  ? A GLU 76 CG  
2  1 Y 1 A GLU 71  ? CD  ? A GLU 76 CD  
3  1 Y 1 A GLU 71  ? OE1 ? A GLU 76 OE1 
4  1 Y 1 A GLU 71  ? OE2 ? A GLU 76 OE2 
5  1 Y 1 A LYS 77  ? CG  ? A LYS 82 CG  
6  1 Y 1 A LYS 77  ? CD  ? A LYS 82 CD  
7  1 Y 1 A LYS 77  ? CE  ? A LYS 82 CE  
8  1 Y 1 A LYS 77  ? NZ  ? A LYS 82 NZ  
9  1 Y 1 P HIS 264 ? CG  ? B HIS 10 CG  
10 1 Y 1 P HIS 264 ? ND1 ? B HIS 10 ND1 
11 1 Y 1 P HIS 264 ? CD2 ? B HIS 10 CD2 
12 1 Y 1 P HIS 264 ? CE1 ? B HIS 10 CE1 
13 1 Y 1 P HIS 264 ? NE2 ? B HIS 10 NE2 
# 
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'   ? ? ? ? ? ? ? ? ? ? ? Aimless  ? ? ? .                    3 
? phasing          ? ? ? ? ? ? ? ? ? ? ? MOLREP   ? ? ? .                    4 
# 
_cell.angle_alpha                  90.00 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.00 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.00 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     8QSA 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     62.253 
_cell.length_a_esd                 ? 
_cell.length_b                     149.416 
_cell.length_b_esd                 ? 
_cell.length_c                     76.762 
_cell.length_c_esd                 ? 
_cell.volume                       ? 
_cell.volume_esd                   ? 
_cell.Z_PDB                        8 
_cell.reciprocal_angle_alpha       ? 
_cell.reciprocal_angle_beta        ? 
_cell.reciprocal_angle_gamma       ? 
_cell.reciprocal_angle_alpha_esd   ? 
_cell.reciprocal_angle_beta_esd    ? 
_cell.reciprocal_angle_gamma_esd   ? 
_cell.reciprocal_length_a          ? 
_cell.reciprocal_length_b          ? 
_cell.reciprocal_length_c          ? 
_cell.reciprocal_length_a_esd      ? 
_cell.reciprocal_length_b_esd      ? 
_cell.reciprocal_length_c_esd      ? 
_cell.pdbx_unique_axis             ? 
_cell.pdbx_esd_method              ? 
# 
_symmetry.entry_id                         8QSA 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                21 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'C 2 2 2' 
_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                   8QSA 
_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             3.22 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          61.76 
_exptl_crystal.description                  ? 
_exptl_crystal.F_000                        ? 
_exptl_crystal.id                           1 
_exptl_crystal.preparation                  ? 
_exptl_crystal.size_max                     ? 
_exptl_crystal.size_mid                     ? 
_exptl_crystal.size_min                     ? 
_exptl_crystal.size_rad                     ? 
_exptl_crystal.colour_lustre                ? 
_exptl_crystal.colour_modifier              ? 
_exptl_crystal.colour_primary               ? 
_exptl_crystal.density_meas                 ? 
_exptl_crystal.density_meas_esd             ? 
_exptl_crystal.density_meas_gt              ? 
_exptl_crystal.density_meas_lt              ? 
_exptl_crystal.density_meas_temp            ? 
_exptl_crystal.density_meas_temp_esd        ? 
_exptl_crystal.density_meas_temp_gt         ? 
_exptl_crystal.density_meas_temp_lt         ? 
_exptl_crystal.pdbx_crystal_image_url       ? 
_exptl_crystal.pdbx_crystal_image_format    ? 
_exptl_crystal.pdbx_mosaicity               ? 
_exptl_crystal.pdbx_mosaicity_esd           ? 
_exptl_crystal.pdbx_mosaic_method           ? 
_exptl_crystal.pdbx_mosaic_block_size       ? 
_exptl_crystal.pdbx_mosaic_block_size_esd   ? 
# 
_exptl_crystal_grow.apparatus       ? 
_exptl_crystal_grow.atmosphere      ? 
_exptl_crystal_grow.crystal_id      1 
_exptl_crystal_grow.details         ? 
_exptl_crystal_grow.method          'VAPOR DIFFUSION, SITTING DROP' 
_exptl_crystal_grow.method_ref      ? 
_exptl_crystal_grow.pH              ? 
_exptl_crystal_grow.pressure        ? 
_exptl_crystal_grow.pressure_esd    ? 
_exptl_crystal_grow.seeding         ? 
_exptl_crystal_grow.seeding_ref     ? 
_exptl_crystal_grow.temp_details    ? 
_exptl_crystal_grow.temp_esd        ? 
_exptl_crystal_grow.time            ? 
_exptl_crystal_grow.pdbx_details    
;0.095 M HEPES pH=7.1-7.7
0.19 M CaCl2 
5% glycerol
24-29% PEG400
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            277 
# 
_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 PILATUS 6M' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2023-04-30 
_diffrn_detector.pdbx_frequency               ? 
_diffrn_detector.id                           ? 
_diffrn_detector.number_of_axes               ? 
# 
_diffrn_radiation.collimation                      ? 
_diffrn_radiation.diffrn_id                        1 
_diffrn_radiation.filter_edge                      ? 
_diffrn_radiation.inhomogeneity                    ? 
_diffrn_radiation.monochromator                    ? 
_diffrn_radiation.polarisn_norm                    ? 
_diffrn_radiation.polarisn_ratio                   ? 
_diffrn_radiation.probe                            ? 
_diffrn_radiation.type                             ? 
_diffrn_radiation.xray_symbol                      ? 
_diffrn_radiation.wavelength_id                    1 
_diffrn_radiation.pdbx_monochromatic_or_laue_m_l   M 
_diffrn_radiation.pdbx_wavelength_list             ? 
_diffrn_radiation.pdbx_wavelength                  ? 
_diffrn_radiation.pdbx_diffrn_protocol             'SINGLE WAVELENGTH' 
_diffrn_radiation.pdbx_analyzer                    ? 
_diffrn_radiation.pdbx_scattering_type             x-ray 
# 
_diffrn_radiation_wavelength.id           1 
_diffrn_radiation_wavelength.wavelength   0.885603 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'ESRF BEAMLINE ID23-1' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.885603 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   ID23-1 
_diffrn_source.pdbx_synchrotron_site       ESRF 
# 
_reflns.B_iso_Wilson_estimate                          ? 
_reflns.entry_id                                       8QSA 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.80 
_reflns.d_resolution_low                               76.76 
_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                                     33021 
_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                           98.3 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                13.3 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          20.0 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               ? 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                ? 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       ? 
_reflns.pdbx_diffrn_id                                 1 
_reflns.pdbx_ordinal                                   1 
_reflns.pdbx_CC_half                                   0.998 
_reflns.pdbx_CC_star                                   ? 
_reflns.pdbx_R_split                                   ? 
_reflns.pdbx_Rmerge_I_obs                              ? 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
_reflns_shell.d_res_high                                    1.80 
_reflns_shell.d_res_low                                     1.84 
_reflns_shell.meanI_over_sigI_all                           ? 
_reflns_shell.meanI_over_sigI_obs                           2.3 
_reflns_shell.number_measured_all                           ? 
_reflns_shell.number_measured_obs                           ? 
_reflns_shell.number_possible                               ? 
_reflns_shell.number_unique_all                             ? 
_reflns_shell.number_unique_obs                             1946 
_reflns_shell.percent_possible_obs                          ? 
_reflns_shell.Rmerge_F_all                                  ? 
_reflns_shell.Rmerge_F_obs                                  ? 
_reflns_shell.meanI_over_sigI_gt                            ? 
_reflns_shell.meanI_over_uI_all                             ? 
_reflns_shell.meanI_over_uI_gt                              ? 
_reflns_shell.number_measured_gt                            ? 
_reflns_shell.number_unique_gt                              ? 
_reflns_shell.percent_possible_gt                           ? 
_reflns_shell.Rmerge_F_gt                                   ? 
_reflns_shell.Rmerge_I_gt                                   ? 
_reflns_shell.pdbx_redundancy                               ? 
_reflns_shell.pdbx_chi_squared                              ? 
_reflns_shell.pdbx_netI_over_sigmaI_all                     ? 
_reflns_shell.pdbx_netI_over_sigmaI_obs                     ? 
_reflns_shell.pdbx_Rrim_I_all                               ? 
_reflns_shell.pdbx_Rpim_I_all                               ? 
_reflns_shell.pdbx_rejects                                  ? 
_reflns_shell.pdbx_ordinal                                  1 
_reflns_shell.pdbx_diffrn_id                                1 
_reflns_shell.pdbx_CC_half                                  0.890 
_reflns_shell.pdbx_CC_star                                  ? 
_reflns_shell.pdbx_R_split                                  ? 
_reflns_shell.percent_possible_all                          ? 
_reflns_shell.Rmerge_I_all                                  ? 
_reflns_shell.Rmerge_I_obs                                  ? 
_reflns_shell.pdbx_Rsym_value                               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal             ? 
_reflns_shell.pdbx_percent_possible_spherical               ? 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous   ? 
_reflns_shell.pdbx_percent_possible_spherical_anomalous     ? 
_reflns_shell.pdbx_redundancy_anomalous                     ? 
_reflns_shell.pdbx_CC_half_anomalous                        ? 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous             ? 
_reflns_shell.pdbx_percent_possible_anomalous               ? 
# 
_refine.aniso_B[1][1]                            ? 
_refine.aniso_B[1][2]                            ? 
_refine.aniso_B[1][3]                            ? 
_refine.aniso_B[2][2]                            ? 
_refine.aniso_B[2][3]                            ? 
_refine.aniso_B[3][3]                            ? 
_refine.B_iso_max                                ? 
_refine.B_iso_mean                               ? 
_refine.B_iso_min                                ? 
_refine.correlation_coeff_Fo_to_Fc               ? 
_refine.correlation_coeff_Fo_to_Fc_free          ? 
_refine.details                                  ? 
_refine.diff_density_max                         ? 
_refine.diff_density_max_esd                     ? 
_refine.diff_density_min                         ? 
_refine.diff_density_min_esd                     ? 
_refine.diff_density_rms                         ? 
_refine.diff_density_rms_esd                     ? 
_refine.entry_id                                 8QSA 
_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                            1.80 
_refine.ls_d_res_low                             33.59 
_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                     32997 
_refine.ls_number_reflns_R_free                  1673 
_refine.ls_number_reflns_R_work                  ? 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    98.23 
_refine.ls_percent_reflns_R_free                 5.07 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1979 
_refine.ls_R_factor_R_free                       0.2417 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1956 
_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                          1.35 
_refine.pdbx_ls_sigma_Fsqd                       ? 
_refine.pdbx_data_cutoff_high_absF               ? 
_refine.pdbx_data_cutoff_high_rms_absF           ? 
_refine.pdbx_data_cutoff_low_absF                ? 
_refine.pdbx_isotropic_thermal_model             ? 
_refine.pdbx_ls_cross_valid_method               THROUGHOUT 
_refine.pdbx_method_to_determine_struct          'MOLECULAR REPLACEMENT' 
_refine.pdbx_starting_model                      ? 
_refine.pdbx_stereochemistry_target_values       ML 
_refine.pdbx_R_Free_selection_details            RANDOM 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.10 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.90 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 26.99 
_refine.pdbx_overall_SU_R_free_Cruickshank_DPI   ? 
_refine.pdbx_overall_SU_R_free_Blow_DPI          ? 
_refine.pdbx_overall_SU_R_Blow_DPI               ? 
_refine.pdbx_TLS_residual_ADP_flag               ? 
_refine.pdbx_diffrn_id                           1 
_refine.overall_SU_B                             ? 
_refine.overall_SU_ML                            0.21 
_refine.overall_SU_R_Cruickshank_DPI             ? 
_refine.overall_SU_R_free                        ? 
_refine.overall_FOM_free_R_set                   ? 
_refine.overall_FOM_work_R_set                   ? 
_refine.pdbx_average_fsc_overall                 ? 
_refine.pdbx_average_fsc_work                    ? 
_refine.pdbx_average_fsc_free                    ? 
# 
_refine_hist.pdbx_refine_id                   'X-RAY DIFFRACTION' 
_refine_hist.cycle_id                         LAST 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.80 
_refine_hist.d_res_low                        33.59 
_refine_hist.number_atoms_solvent             171 
_refine_hist.number_atoms_total               2088 
_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        1884 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         33 
_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' ? 0.006 ? 405 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 1.162 ? 540 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 9.610 ? 279 ? f_dihedral_angle_d ? ? 
'X-RAY DIFFRACTION' ? 0.177 ? 290 ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.008 ? 336 ? f_plane_restr      ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.80 1.85  . . 146 2592 100.00 . . . . 0.2901 . . . . . . . . . . . 0.3080 
'X-RAY DIFFRACTION' 1.85 1.91  . . 140 2590 100.00 . . . . 0.2599 . . . . . . . . . . . 0.2872 
'X-RAY DIFFRACTION' 1.91 1.98  . . 141 2636 100.00 . . . . 0.2484 . . . . . . . . . . . 0.2940 
'X-RAY DIFFRACTION' 1.98 2.06  . . 118 2473 99.00  . . . . 0.2284 . . . . . . . . . . . 0.2907 
'X-RAY DIFFRACTION' 2.07 2.15  . . 124 2259 100.00 . . . . 0.1972 . . . . . . . . . . . 0.2479 
'X-RAY DIFFRACTION' 2.15 2.27  . . 136 2634 100.00 . . . . 0.1874 . . . . . . . . . . . 0.2047 
'X-RAY DIFFRACTION' 2.27 2.41  . . 145 2638 100.00 . . . . 0.1943 . . . . . . . . . . . 0.2066 
'X-RAY DIFFRACTION' 2.41 2.60  . . 128 2677 100.00 . . . . 0.2069 . . . . . . . . . . . 0.2355 
'X-RAY DIFFRACTION' 2.60 2.86  . . 152 2638 100.00 . . . . 0.2195 . . . . . . . . . . . 0.2800 
'X-RAY DIFFRACTION' 2.86 3.27  . . 150 2667 100.00 . . . . 0.2180 . . . . . . . . . . . 0.2747 
'X-RAY DIFFRACTION' 3.27 4.12  . . 152 2700 100.00 . . . . 0.1803 . . . . . . . . . . . 0.2090 
'X-RAY DIFFRACTION' 4.12 33.59 . . 141 2820 100.00 . . . . 0.1762 . . . . . . . . . . . 0.2404 
# 
_struct.entry_id                     8QSA 
_struct.title                        'Ternary structure of 14-3-3s, C-RAF phosphopeptide (pS259) and compound 86 (1084384)' 
_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        8QSA 
_struct_keywords.text            'Stabilizer, protein-protein interaction, PEPTIDE BINDING PROTEIN' 
_struct_keywords.pdbx_keywords   'PEPTIDE BINDING PROTEIN' 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 2 ? 
C N N 3 ? 
D N N 4 ? 
E N N 4 ? 
F N N 4 ? 
G N N 5 ? 
H N N 6 ? 
I N N 6 ? 
# 
loop_
_struct_ref.id 
_struct_ref.db_name 
_struct_ref.db_code 
_struct_ref.pdbx_db_accession 
_struct_ref.pdbx_db_isoform 
_struct_ref.entity_id 
_struct_ref.pdbx_seq_one_letter_code 
_struct_ref.pdbx_align_begin 
1 UNP 1433S_HUMAN P31947 ? 1 
;MERASLIQKAKLAEQAERYEDMAAFMKGAVEKGEELSCEERNLLSVAYKNVVGGQRAAWRVLSSIEQKSNEEGSEEKGPE
VREYREKVETELQGVCDTVLGLLDSHLIKEAGDAESRVFYLKMKGDYYRYLAEVATGDDKKRIIDSARSAYQEAMDISKK
EMPPTNPIRLGLALNFSVFHYEIANSPEEAISLAKTTFDEAMADLHTLSEDSYKDSTLIMQLLRDNLTLWT
;
1 
2 PDB 8QSA        8QSA   ? 2 ? 1 
# 
loop_
_struct_ref_seq.align_id 
_struct_ref_seq.ref_id 
_struct_ref_seq.pdbx_PDB_id_code 
_struct_ref_seq.pdbx_strand_id 
_struct_ref_seq.seq_align_beg 
_struct_ref_seq.pdbx_seq_align_beg_ins_code 
_struct_ref_seq.seq_align_end 
_struct_ref_seq.pdbx_seq_align_end_ins_code 
_struct_ref_seq.pdbx_db_accession 
_struct_ref_seq.db_align_beg 
_struct_ref_seq.pdbx_db_align_beg_ins_code 
_struct_ref_seq.db_align_end 
_struct_ref_seq.pdbx_db_align_end_ins_code 
_struct_ref_seq.pdbx_auth_seq_align_beg 
_struct_ref_seq.pdbx_auth_seq_align_end 
1 1 8QSA A 6 ? 236 ? P31947 1   ? 231 ? 1   231 
2 2 8QSA P 1 ? 10  ? 8QSA   255 ? 264 ? 255 264 
# 
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 8QSA GLY A 1 ? UNP P31947 ? ? 'expression tag' -4 1 
1 8QSA ALA A 2 ? UNP P31947 ? ? 'expression tag' -3 2 
1 8QSA MET A 3 ? UNP P31947 ? ? 'expression tag' -2 3 
1 8QSA GLY A 4 ? UNP P31947 ? ? 'expression tag' -1 4 
1 8QSA SER A 5 ? UNP P31947 ? ? 'expression tag' 0  5 
# 
_pdbx_struct_assembly.id                   1 
_pdbx_struct_assembly.details              author_defined_assembly 
_pdbx_struct_assembly.method_details       ? 
_pdbx_struct_assembly.oligomeric_details   tetrameric 
_pdbx_struct_assembly.oligomeric_count     4 
# 
loop_
_pdbx_struct_assembly_prop.biol_id 
_pdbx_struct_assembly_prop.type 
_pdbx_struct_assembly_prop.value 
_pdbx_struct_assembly_prop.details 
1 'ABSA (A^2)' 5700  ? 
1 MORE         -79   ? 
1 'SSA (A^2)'  22930 ? 
# 
_pdbx_struct_assembly_gen.assembly_id       1 
_pdbx_struct_assembly_gen.oper_expression   1,2 
_pdbx_struct_assembly_gen.asym_id_list      A,B,C,D,E,F,G,H,I 
# 
_pdbx_struct_assembly_auth_evidence.id                     1 
_pdbx_struct_assembly_auth_evidence.assembly_id            1 
_pdbx_struct_assembly_auth_evidence.experimental_support   none 
_pdbx_struct_assembly_auth_evidence.details                ? 
# 
loop_
_pdbx_struct_oper_list.id 
_pdbx_struct_oper_list.type 
_pdbx_struct_oper_list.name 
_pdbx_struct_oper_list.symmetry_operation 
_pdbx_struct_oper_list.matrix[1][1] 
_pdbx_struct_oper_list.matrix[1][2] 
_pdbx_struct_oper_list.matrix[1][3] 
_pdbx_struct_oper_list.vector[1] 
_pdbx_struct_oper_list.matrix[2][1] 
_pdbx_struct_oper_list.matrix[2][2] 
_pdbx_struct_oper_list.matrix[2][3] 
_pdbx_struct_oper_list.vector[2] 
_pdbx_struct_oper_list.matrix[3][1] 
_pdbx_struct_oper_list.matrix[3][2] 
_pdbx_struct_oper_list.matrix[3][3] 
_pdbx_struct_oper_list.vector[3] 
1 'identity operation'         1_555 x,y,z       1.0000000000  0.0000000000 0.0000000000 0.0000000000  0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 1.0000000000  0.0000000000  
2 'crystal symmetry operation' 3_656 -x+1,y,-z+1 -1.0000000000 0.0000000000 0.0000000000 62.2530000000 0.0000000000 1.0000000000 
0.0000000000 0.0000000000 0.0000000000 0.0000000000 -1.0000000000 76.7620000000 
# 
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 GLU A 7   ? ALA A 21  ? GLU A 2   ALA A 16  1 ? 15 
HELX_P HELX_P2  AA2 ARG A 23  ? LYS A 37  ? ARG A 18  LYS A 32  1 ? 15 
HELX_P HELX_P3  AA3 SER A 42  ? SER A 74  ? SER A 37  SER A 69  1 ? 33 
HELX_P HELX_P4  AA4 PRO A 84  ? HIS A 111 ? PRO A 79  HIS A 106 1 ? 28 
HELX_P HELX_P5  AA5 ASP A 118 ? VAL A 139 ? ASP A 113 VAL A 134 1 ? 22 
HELX_P HELX_P6  AA6 GLY A 142 ? MET A 167 ? GLY A 137 MET A 162 1 ? 26 
HELX_P HELX_P7  AA7 ASN A 171 ? ILE A 188 ? ASN A 166 ILE A 183 1 ? 18 
HELX_P HELX_P8  AA8 SER A 191 ? ASP A 209 ? SER A 186 ASP A 204 1 ? 19 
HELX_P HELX_P9  AA9 LEU A 210 ? LEU A 213 ? LEU A 205 LEU A 208 5 ? 4  
HELX_P HELX_P10 AB1 SER A 217 ? THR A 236 ? SER A 212 THR A 231 1 ? 20 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
covale1 covale one  ? A CYS 43 SG  ? ? ? 1_555 G WQ9 . C2 ? ? A CYS 38  A WQ9 305 1_555 ? ? ? ? ? ? ? 1.767 ? ? 
covale2 covale both ? B THR 4  C   ? ? ? 1_555 B SEP 5 N  ? ? P THR 258 P SEP 259 1_555 ? ? ? ? ? ? ? 1.327 ? ? 
covale3 covale both ? B SEP 5  C   ? ? ? 1_555 B THR 6 N  ? ? P SEP 259 P THR 260 1_555 ? ? ? ? ? ? ? 1.332 ? ? 
metalc1 metalc ?    ? A GLU 7  OE1 ? ? ? 1_555 F MG  . MG ? ? A GLU 2   A MG  304 1_555 ? ? ? ? ? ? ? 2.705 ? ? 
metalc2 metalc ?    ? A GLU 94 OE1 ? ? ? 1_555 D MG  . MG ? ? A GLU 89  A MG  302 1_555 ? ? ? ? ? ? ? 2.609 ? ? 
metalc3 metalc ?    ? D MG  .  MG  ? ? ? 1_555 H HOH . O  ? ? A MG  302 A HOH 401 1_555 ? ? ? ? ? ? ? 2.282 ? ? 
metalc4 metalc ?    ? F MG  .  MG  ? ? ? 1_555 H HOH . O  ? ? A MG  304 A HOH 560 1_555 ? ? ? ? ? ? ? 2.979 ? ? 
# 
loop_
_struct_conn_type.id 
_struct_conn_type.criteria 
_struct_conn_type.reference 
covale ? ? 
metalc ? ? 
# 
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 OE1 ? A GLU 7  ? A GLU 2  ? 1_555 MG ? F MG . ? A MG 304 ? 1_555 O ? H HOH . ? A HOH 560 ? 1_555 114.0 ? 
2 OE1 ? A GLU 94 ? A GLU 89 ? 1_555 MG ? D MG . ? A MG 302 ? 1_555 O ? H HOH . ? A HOH 401 ? 1_555 55.0  ? 
# 
loop_
_pdbx_modification_feature.ordinal 
_pdbx_modification_feature.label_comp_id 
_pdbx_modification_feature.label_asym_id 
_pdbx_modification_feature.label_seq_id 
_pdbx_modification_feature.label_alt_id 
_pdbx_modification_feature.modified_residue_label_comp_id 
_pdbx_modification_feature.modified_residue_label_asym_id 
_pdbx_modification_feature.modified_residue_label_seq_id 
_pdbx_modification_feature.modified_residue_label_alt_id 
_pdbx_modification_feature.auth_comp_id 
_pdbx_modification_feature.auth_asym_id 
_pdbx_modification_feature.auth_seq_id 
_pdbx_modification_feature.PDB_ins_code 
_pdbx_modification_feature.symmetry 
_pdbx_modification_feature.modified_residue_auth_comp_id 
_pdbx_modification_feature.modified_residue_auth_asym_id 
_pdbx_modification_feature.modified_residue_auth_seq_id 
_pdbx_modification_feature.modified_residue_PDB_ins_code 
_pdbx_modification_feature.modified_residue_symmetry 
_pdbx_modification_feature.comp_id_linking_atom 
_pdbx_modification_feature.modified_residue_id_linking_atom 
_pdbx_modification_feature.modified_residue_id 
_pdbx_modification_feature.ref_pcm_id 
_pdbx_modification_feature.ref_comp_id 
_pdbx_modification_feature.type 
_pdbx_modification_feature.category 
1 SEP B 5 ? .   . .  . SEP P 259 ? 1_555 .   . .  . .     .  .  SER 1 SEP Phosphorylation 'Named protein modification'     
2 WQ9 G . ? CYS A 43 ? WQ9 A 305 ? 1_555 CYS A 38 ? 1_555 C2 SG CYS 1 WQ9 None            'Covalent chemical modification' 
# 
_pdbx_entry_details.entry_id                   8QSA 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.has_protein_modification   Y 
# 
loop_
_pdbx_validate_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 ARG A 18  ? ? -103.06 78.02  
2 1 THR A 136 ? ? -135.59 -67.16 
# 
_pdbx_struct_mod_residue.id               1 
_pdbx_struct_mod_residue.label_asym_id    A 
_pdbx_struct_mod_residue.label_comp_id    CYS 
_pdbx_struct_mod_residue.label_seq_id     43 
_pdbx_struct_mod_residue.auth_asym_id     A 
_pdbx_struct_mod_residue.auth_comp_id     CYS 
_pdbx_struct_mod_residue.auth_seq_id      38 
_pdbx_struct_mod_residue.PDB_ins_code     ? 
_pdbx_struct_mod_residue.parent_comp_id   CYS 
_pdbx_struct_mod_residue.details          'modified residue' 
# 
_pdbx_struct_special_symmetry.id              1 
_pdbx_struct_special_symmetry.PDB_model_num   1 
_pdbx_struct_special_symmetry.auth_asym_id    A 
_pdbx_struct_special_symmetry.auth_comp_id    HOH 
_pdbx_struct_special_symmetry.auth_seq_id     449 
_pdbx_struct_special_symmetry.PDB_ins_code    ? 
_pdbx_struct_special_symmetry.label_asym_id   H 
_pdbx_struct_special_symmetry.label_comp_id   HOH 
_pdbx_struct_special_symmetry.label_seq_id    . 
# 
_pdbx_refine_tls.id               1 
_pdbx_refine_tls.pdbx_refine_id   'X-RAY DIFFRACTION' 
_pdbx_refine_tls.details          ? 
_pdbx_refine_tls.method           refined 
_pdbx_refine_tls.origin_x         23.4119 
_pdbx_refine_tls.origin_y         20.3036 
_pdbx_refine_tls.origin_z         21.4058 
_pdbx_refine_tls.T[1][1]          0.3832 
_pdbx_refine_tls.T[1][1]_esd      ? 
_pdbx_refine_tls.T[1][2]          -0.0159 
_pdbx_refine_tls.T[1][2]_esd      ? 
_pdbx_refine_tls.T[1][3]          -0.0652 
_pdbx_refine_tls.T[1][3]_esd      ? 
_pdbx_refine_tls.T[2][2]          0.3825 
_pdbx_refine_tls.T[2][2]_esd      ? 
_pdbx_refine_tls.T[2][3]          0.0149 
_pdbx_refine_tls.T[2][3]_esd      ? 
_pdbx_refine_tls.T[3][3]          0.3668 
_pdbx_refine_tls.T[3][3]_esd      ? 
_pdbx_refine_tls.L[1][1]          0.6781 
_pdbx_refine_tls.L[1][1]_esd      ? 
_pdbx_refine_tls.L[1][2]          0.0041 
_pdbx_refine_tls.L[1][2]_esd      ? 
_pdbx_refine_tls.L[1][3]          -0.6778 
_pdbx_refine_tls.L[1][3]_esd      ? 
_pdbx_refine_tls.L[2][2]          1.0134 
_pdbx_refine_tls.L[2][2]_esd      ? 
_pdbx_refine_tls.L[2][3]          0.7193 
_pdbx_refine_tls.L[2][3]_esd      ? 
_pdbx_refine_tls.L[3][3]          2.4555 
_pdbx_refine_tls.L[3][3]_esd      ? 
_pdbx_refine_tls.S[1][1]          -0.0420 
_pdbx_refine_tls.S[1][1]_esd      ? 
_pdbx_refine_tls.S[1][2]          0.2388 
_pdbx_refine_tls.S[1][2]_esd      ? 
_pdbx_refine_tls.S[1][3]          0.0689 
_pdbx_refine_tls.S[1][3]_esd      ? 
_pdbx_refine_tls.S[2][1]          -0.1240 
_pdbx_refine_tls.S[2][1]_esd      ? 
_pdbx_refine_tls.S[2][2]          -0.0512 
_pdbx_refine_tls.S[2][2]_esd      ? 
_pdbx_refine_tls.S[2][3]          0.0820 
_pdbx_refine_tls.S[2][3]_esd      ? 
_pdbx_refine_tls.S[3][1]          -0.0004 
_pdbx_refine_tls.S[3][1]_esd      ? 
_pdbx_refine_tls.S[3][2]          -0.4289 
_pdbx_refine_tls.S[3][2]_esd      ? 
_pdbx_refine_tls.S[3][3]          0.1127 
_pdbx_refine_tls.S[3][3]_esd      ? 
# 
_pdbx_refine_tls_group.id                  1 
_pdbx_refine_tls_group.pdbx_refine_id      'X-RAY DIFFRACTION' 
_pdbx_refine_tls_group.refine_tls_id       1 
_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   all 
# 
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 GLU 72 ? A GLU 77 
2 1 Y 1 A GLY 73 ? A GLY 78 
3 1 Y 1 A SER 74 ? A SER 79 
4 1 Y 1 A GLU 75 ? A GLU 80 
5 1 Y 1 A GLU 76 ? A GLU 81 
# 
loop_
_chem_comp_atom.comp_id 
_chem_comp_atom.atom_id 
_chem_comp_atom.type_symbol 
_chem_comp_atom.pdbx_aromatic_flag 
_chem_comp_atom.pdbx_stereo_config 
_chem_comp_atom.pdbx_ordinal 
ALA N    N  N N 1   
ALA CA   C  N S 2   
ALA C    C  N N 3   
ALA O    O  N N 4   
ALA CB   C  N N 5   
ALA OXT  O  N N 6   
ALA H    H  N N 7   
ALA H2   H  N N 8   
ALA HA   H  N N 9   
ALA HB1  H  N N 10  
ALA HB2  H  N N 11  
ALA HB3  H  N N 12  
ALA HXT  H  N N 13  
ARG N    N  N N 14  
ARG CA   C  N S 15  
ARG C    C  N N 16  
ARG O    O  N N 17  
ARG CB   C  N N 18  
ARG CG   C  N N 19  
ARG CD   C  N N 20  
ARG NE   N  N N 21  
ARG CZ   C  N N 22  
ARG NH1  N  N N 23  
ARG NH2  N  N N 24  
ARG OXT  O  N N 25  
ARG H    H  N N 26  
ARG H2   H  N N 27  
ARG HA   H  N N 28  
ARG HB2  H  N N 29  
ARG HB3  H  N N 30  
ARG HG2  H  N N 31  
ARG HG3  H  N N 32  
ARG HD2  H  N N 33  
ARG HD3  H  N N 34  
ARG HE   H  N N 35  
ARG HH11 H  N N 36  
ARG HH12 H  N N 37  
ARG HH21 H  N N 38  
ARG HH22 H  N N 39  
ARG HXT  H  N N 40  
ASN N    N  N N 41  
ASN CA   C  N S 42  
ASN C    C  N N 43  
ASN O    O  N N 44  
ASN CB   C  N N 45  
ASN CG   C  N N 46  
ASN OD1  O  N N 47  
ASN ND2  N  N N 48  
ASN OXT  O  N N 49  
ASN H    H  N N 50  
ASN H2   H  N N 51  
ASN HA   H  N N 52  
ASN HB2  H  N N 53  
ASN HB3  H  N N 54  
ASN HD21 H  N N 55  
ASN HD22 H  N N 56  
ASN HXT  H  N N 57  
ASP N    N  N N 58  
ASP CA   C  N S 59  
ASP C    C  N N 60  
ASP O    O  N N 61  
ASP CB   C  N N 62  
ASP CG   C  N N 63  
ASP OD1  O  N N 64  
ASP OD2  O  N N 65  
ASP OXT  O  N N 66  
ASP H    H  N N 67  
ASP H2   H  N N 68  
ASP HA   H  N N 69  
ASP HB2  H  N N 70  
ASP HB3  H  N N 71  
ASP HD2  H  N N 72  
ASP HXT  H  N N 73  
CL  CL   CL N N 74  
CYS N    N  N N 75  
CYS CA   C  N R 76  
CYS C    C  N N 77  
CYS O    O  N N 78  
CYS CB   C  N N 79  
CYS SG   S  N N 80  
CYS OXT  O  N N 81  
CYS H    H  N N 82  
CYS H2   H  N N 83  
CYS HA   H  N N 84  
CYS HB2  H  N N 85  
CYS HB3  H  N N 86  
CYS HG   H  N N 87  
CYS HXT  H  N N 88  
GLN N    N  N N 89  
GLN CA   C  N S 90  
GLN C    C  N N 91  
GLN O    O  N N 92  
GLN CB   C  N N 93  
GLN CG   C  N N 94  
GLN CD   C  N N 95  
GLN OE1  O  N N 96  
GLN NE2  N  N N 97  
GLN OXT  O  N N 98  
GLN H    H  N N 99  
GLN H2   H  N N 100 
GLN HA   H  N N 101 
GLN HB2  H  N N 102 
GLN HB3  H  N N 103 
GLN HG2  H  N N 104 
GLN HG3  H  N N 105 
GLN HE21 H  N N 106 
GLN HE22 H  N N 107 
GLN HXT  H  N N 108 
GLU N    N  N N 109 
GLU CA   C  N S 110 
GLU C    C  N N 111 
GLU O    O  N N 112 
GLU CB   C  N N 113 
GLU CG   C  N N 114 
GLU CD   C  N N 115 
GLU OE1  O  N N 116 
GLU OE2  O  N N 117 
GLU OXT  O  N N 118 
GLU H    H  N N 119 
GLU H2   H  N N 120 
GLU HA   H  N N 121 
GLU HB2  H  N N 122 
GLU HB3  H  N N 123 
GLU HG2  H  N N 124 
GLU HG3  H  N N 125 
GLU HE2  H  N N 126 
GLU HXT  H  N N 127 
GLY N    N  N N 128 
GLY CA   C  N N 129 
GLY C    C  N N 130 
GLY O    O  N N 131 
GLY OXT  O  N N 132 
GLY H    H  N N 133 
GLY H2   H  N N 134 
GLY HA2  H  N N 135 
GLY HA3  H  N N 136 
GLY HXT  H  N N 137 
HIS N    N  N N 138 
HIS CA   C  N S 139 
HIS C    C  N N 140 
HIS O    O  N N 141 
HIS CB   C  N N 142 
HIS CG   C  Y N 143 
HIS ND1  N  Y N 144 
HIS CD2  C  Y N 145 
HIS CE1  C  Y N 146 
HIS NE2  N  Y N 147 
HIS OXT  O  N N 148 
HIS H    H  N N 149 
HIS H2   H  N N 150 
HIS HA   H  N N 151 
HIS HB2  H  N N 152 
HIS HB3  H  N N 153 
HIS HD1  H  N N 154 
HIS HD2  H  N N 155 
HIS HE1  H  N N 156 
HIS HE2  H  N N 157 
HIS HXT  H  N N 158 
HOH O    O  N N 159 
HOH H1   H  N N 160 
HOH H2   H  N N 161 
ILE N    N  N N 162 
ILE CA   C  N S 163 
ILE C    C  N N 164 
ILE O    O  N N 165 
ILE CB   C  N S 166 
ILE CG1  C  N N 167 
ILE CG2  C  N N 168 
ILE CD1  C  N N 169 
ILE OXT  O  N N 170 
ILE H    H  N N 171 
ILE H2   H  N N 172 
ILE HA   H  N N 173 
ILE HB   H  N N 174 
ILE HG12 H  N N 175 
ILE HG13 H  N N 176 
ILE HG21 H  N N 177 
ILE HG22 H  N N 178 
ILE HG23 H  N N 179 
ILE HD11 H  N N 180 
ILE HD12 H  N N 181 
ILE HD13 H  N N 182 
ILE HXT  H  N N 183 
LEU N    N  N N 184 
LEU CA   C  N S 185 
LEU C    C  N N 186 
LEU O    O  N N 187 
LEU CB   C  N N 188 
LEU CG   C  N N 189 
LEU CD1  C  N N 190 
LEU CD2  C  N N 191 
LEU OXT  O  N N 192 
LEU H    H  N N 193 
LEU H2   H  N N 194 
LEU HA   H  N N 195 
LEU HB2  H  N N 196 
LEU HB3  H  N N 197 
LEU HG   H  N N 198 
LEU HD11 H  N N 199 
LEU HD12 H  N N 200 
LEU HD13 H  N N 201 
LEU HD21 H  N N 202 
LEU HD22 H  N N 203 
LEU HD23 H  N N 204 
LEU HXT  H  N N 205 
LYS N    N  N N 206 
LYS CA   C  N S 207 
LYS C    C  N N 208 
LYS O    O  N N 209 
LYS CB   C  N N 210 
LYS CG   C  N N 211 
LYS CD   C  N N 212 
LYS CE   C  N N 213 
LYS NZ   N  N N 214 
LYS OXT  O  N N 215 
LYS H    H  N N 216 
LYS H2   H  N N 217 
LYS HA   H  N N 218 
LYS HB2  H  N N 219 
LYS HB3  H  N N 220 
LYS HG2  H  N N 221 
LYS HG3  H  N N 222 
LYS HD2  H  N N 223 
LYS HD3  H  N N 224 
LYS HE2  H  N N 225 
LYS HE3  H  N N 226 
LYS HZ1  H  N N 227 
LYS HZ2  H  N N 228 
LYS HZ3  H  N N 229 
LYS HXT  H  N N 230 
MET N    N  N N 231 
MET CA   C  N S 232 
MET C    C  N N 233 
MET O    O  N N 234 
MET CB   C  N N 235 
MET CG   C  N N 236 
MET SD   S  N N 237 
MET CE   C  N N 238 
MET OXT  O  N N 239 
MET H    H  N N 240 
MET H2   H  N N 241 
MET HA   H  N N 242 
MET HB2  H  N N 243 
MET HB3  H  N N 244 
MET HG2  H  N N 245 
MET HG3  H  N N 246 
MET HE1  H  N N 247 
MET HE2  H  N N 248 
MET HE3  H  N N 249 
MET HXT  H  N N 250 
MG  MG   MG N N 251 
PHE N    N  N N 252 
PHE CA   C  N S 253 
PHE C    C  N N 254 
PHE O    O  N N 255 
PHE CB   C  N N 256 
PHE CG   C  Y N 257 
PHE CD1  C  Y N 258 
PHE CD2  C  Y N 259 
PHE CE1  C  Y N 260 
PHE CE2  C  Y N 261 
PHE CZ   C  Y N 262 
PHE OXT  O  N N 263 
PHE H    H  N N 264 
PHE H2   H  N N 265 
PHE HA   H  N N 266 
PHE HB2  H  N N 267 
PHE HB3  H  N N 268 
PHE HD1  H  N N 269 
PHE HD2  H  N N 270 
PHE HE1  H  N N 271 
PHE HE2  H  N N 272 
PHE HZ   H  N N 273 
PHE HXT  H  N N 274 
PRO N    N  N N 275 
PRO CA   C  N S 276 
PRO C    C  N N 277 
PRO O    O  N N 278 
PRO CB   C  N N 279 
PRO CG   C  N N 280 
PRO CD   C  N N 281 
PRO OXT  O  N N 282 
PRO H    H  N N 283 
PRO HA   H  N N 284 
PRO HB2  H  N N 285 
PRO HB3  H  N N 286 
PRO HG2  H  N N 287 
PRO HG3  H  N N 288 
PRO HD2  H  N N 289 
PRO HD3  H  N N 290 
PRO HXT  H  N N 291 
SEP N    N  N N 292 
SEP CA   C  N S 293 
SEP CB   C  N N 294 
SEP OG   O  N N 295 
SEP C    C  N N 296 
SEP O    O  N N 297 
SEP OXT  O  N N 298 
SEP P    P  N N 299 
SEP O1P  O  N N 300 
SEP O2P  O  N N 301 
SEP O3P  O  N N 302 
SEP H    H  N N 303 
SEP H2   H  N N 304 
SEP HA   H  N N 305 
SEP HB2  H  N N 306 
SEP HB3  H  N N 307 
SEP HXT  H  N N 308 
SEP HOP2 H  N N 309 
SEP HOP3 H  N N 310 
SER N    N  N N 311 
SER CA   C  N S 312 
SER C    C  N N 313 
SER O    O  N N 314 
SER CB   C  N N 315 
SER OG   O  N N 316 
SER OXT  O  N N 317 
SER H    H  N N 318 
SER H2   H  N N 319 
SER HA   H  N N 320 
SER HB2  H  N N 321 
SER HB3  H  N N 322 
SER HG   H  N N 323 
SER HXT  H  N N 324 
THR N    N  N N 325 
THR CA   C  N S 326 
THR C    C  N N 327 
THR O    O  N N 328 
THR CB   C  N R 329 
THR OG1  O  N N 330 
THR CG2  C  N N 331 
THR OXT  O  N N 332 
THR H    H  N N 333 
THR H2   H  N N 334 
THR HA   H  N N 335 
THR HB   H  N N 336 
THR HG1  H  N N 337 
THR HG21 H  N N 338 
THR HG22 H  N N 339 
THR HG23 H  N N 340 
THR HXT  H  N N 341 
TRP N    N  N N 342 
TRP CA   C  N S 343 
TRP C    C  N N 344 
TRP O    O  N N 345 
TRP CB   C  N N 346 
TRP CG   C  Y N 347 
TRP CD1  C  Y N 348 
TRP CD2  C  Y N 349 
TRP NE1  N  Y N 350 
TRP CE2  C  Y N 351 
TRP CE3  C  Y N 352 
TRP CZ2  C  Y N 353 
TRP CZ3  C  Y N 354 
TRP CH2  C  Y N 355 
TRP OXT  O  N N 356 
TRP H    H  N N 357 
TRP H2   H  N N 358 
TRP HA   H  N N 359 
TRP HB2  H  N N 360 
TRP HB3  H  N N 361 
TRP HD1  H  N N 362 
TRP HE1  H  N N 363 
TRP HE3  H  N N 364 
TRP HZ2  H  N N 365 
TRP HZ3  H  N N 366 
TRP HH2  H  N N 367 
TRP HXT  H  N N 368 
TYR N    N  N N 369 
TYR CA   C  N S 370 
TYR C    C  N N 371 
TYR O    O  N N 372 
TYR CB   C  N N 373 
TYR CG   C  Y N 374 
TYR CD1  C  Y N 375 
TYR CD2  C  Y N 376 
TYR CE1  C  Y N 377 
TYR CE2  C  Y N 378 
TYR CZ   C  Y N 379 
TYR OH   O  N N 380 
TYR OXT  O  N N 381 
TYR H    H  N N 382 
TYR H2   H  N N 383 
TYR HA   H  N N 384 
TYR HB2  H  N N 385 
TYR HB3  H  N N 386 
TYR HD1  H  N N 387 
TYR HD2  H  N N 388 
TYR HE1  H  N N 389 
TYR HE2  H  N N 390 
TYR HH   H  N N 391 
TYR HXT  H  N N 392 
VAL N    N  N N 393 
VAL CA   C  N S 394 
VAL C    C  N N 395 
VAL O    O  N N 396 
VAL CB   C  N N 397 
VAL CG1  C  N N 398 
VAL CG2  C  N N 399 
VAL OXT  O  N N 400 
VAL H    H  N N 401 
VAL H2   H  N N 402 
VAL HA   H  N N 403 
VAL HB   H  N N 404 
VAL HG11 H  N N 405 
VAL HG12 H  N N 406 
VAL HG13 H  N N 407 
VAL HG21 H  N N 408 
VAL HG22 H  N N 409 
VAL HG23 H  N N 410 
VAL HXT  H  N N 411 
WQ9 O1   O  N N 412 
WQ9 C1   C  N N 413 
WQ9 C2   C  N N 414 
WQ9 N1   N  N N 415 
WQ9 C3   C  N N 416 
WQ9 C4   C  N N 417 
WQ9 C5   C  N R 418 
WQ9 C6   C  N N 419 
WQ9 C7   C  N N 420 
WQ9 N2   N  N N 421 
WQ9 S1   S  N N 422 
WQ9 O2   O  N N 423 
WQ9 O3   O  N N 424 
WQ9 C8   C  Y N 425 
WQ9 C9   C  Y N 426 
WQ9 C10  C  Y N 427 
WQ9 C11  C  Y N 428 
WQ9 BR1  BR N N 429 
WQ9 C12  C  Y N 430 
WQ9 F1   F  N N 431 
WQ9 C13  C  Y N 432 
WQ9 C14  C  N N 433 
WQ9 C15  C  N N 434 
WQ9 H1   H  N N 435 
WQ9 H2   H  N N 436 
WQ9 H4   H  N N 437 
WQ9 H5   H  N N 438 
WQ9 H6   H  N N 439 
WQ9 H7   H  N N 440 
WQ9 H8   H  N N 441 
WQ9 H9   H  N N 442 
WQ9 H10  H  N N 443 
WQ9 H11  H  N N 444 
WQ9 H12  H  N N 445 
WQ9 H13  H  N N 446 
WQ9 H14  H  N N 447 
WQ9 H15  H  N N 448 
WQ9 H16  H  N N 449 
WQ9 H17  H  N N 450 
WQ9 H18  H  N N 451 
WQ9 CL1  CL N N 452 
# 
loop_
_chem_comp_bond.comp_id 
_chem_comp_bond.atom_id_1 
_chem_comp_bond.atom_id_2 
_chem_comp_bond.value_order 
_chem_comp_bond.pdbx_aromatic_flag 
_chem_comp_bond.pdbx_stereo_config 
_chem_comp_bond.pdbx_ordinal 
ALA N   CA   sing N N 1   
ALA N   H    sing N N 2   
ALA N   H2   sing N N 3   
ALA CA  C    sing N N 4   
ALA CA  CB   sing N N 5   
ALA CA  HA   sing N N 6   
ALA C   O    doub N N 7   
ALA C   OXT  sing N N 8   
ALA CB  HB1  sing N N 9   
ALA CB  HB2  sing N N 10  
ALA CB  HB3  sing N N 11  
ALA OXT HXT  sing N N 12  
ARG N   CA   sing N N 13  
ARG N   H    sing N N 14  
ARG N   H2   sing N N 15  
ARG CA  C    sing N N 16  
ARG CA  CB   sing N N 17  
ARG CA  HA   sing N N 18  
ARG C   O    doub N N 19  
ARG C   OXT  sing N N 20  
ARG CB  CG   sing N N 21  
ARG CB  HB2  sing N N 22  
ARG CB  HB3  sing N N 23  
ARG CG  CD   sing N N 24  
ARG CG  HG2  sing N N 25  
ARG CG  HG3  sing N N 26  
ARG CD  NE   sing N N 27  
ARG CD  HD2  sing N N 28  
ARG CD  HD3  sing N N 29  
ARG NE  CZ   sing N N 30  
ARG NE  HE   sing N N 31  
ARG CZ  NH1  sing N N 32  
ARG CZ  NH2  doub N N 33  
ARG NH1 HH11 sing N N 34  
ARG NH1 HH12 sing N N 35  
ARG NH2 HH21 sing N N 36  
ARG NH2 HH22 sing N N 37  
ARG OXT HXT  sing N N 38  
ASN N   CA   sing N N 39  
ASN N   H    sing N N 40  
ASN N   H2   sing N N 41  
ASN CA  C    sing N N 42  
ASN CA  CB   sing N N 43  
ASN CA  HA   sing N N 44  
ASN C   O    doub N N 45  
ASN C   OXT  sing N N 46  
ASN CB  CG   sing N N 47  
ASN CB  HB2  sing N N 48  
ASN CB  HB3  sing N N 49  
ASN CG  OD1  doub N N 50  
ASN CG  ND2  sing N N 51  
ASN ND2 HD21 sing N N 52  
ASN ND2 HD22 sing N N 53  
ASN OXT HXT  sing N N 54  
ASP N   CA   sing N N 55  
ASP N   H    sing N N 56  
ASP N   H2   sing N N 57  
ASP CA  C    sing N N 58  
ASP CA  CB   sing N N 59  
ASP CA  HA   sing N N 60  
ASP C   O    doub N N 61  
ASP C   OXT  sing N N 62  
ASP CB  CG   sing N N 63  
ASP CB  HB2  sing N N 64  
ASP CB  HB3  sing N N 65  
ASP CG  OD1  doub N N 66  
ASP CG  OD2  sing N N 67  
ASP OD2 HD2  sing N N 68  
ASP OXT HXT  sing N N 69  
CYS N   CA   sing N N 70  
CYS N   H    sing N N 71  
CYS N   H2   sing N N 72  
CYS CA  C    sing N N 73  
CYS CA  CB   sing N N 74  
CYS CA  HA   sing N N 75  
CYS C   O    doub N N 76  
CYS C   OXT  sing N N 77  
CYS CB  SG   sing N N 78  
CYS CB  HB2  sing N N 79  
CYS CB  HB3  sing N N 80  
CYS SG  HG   sing N N 81  
CYS OXT HXT  sing N N 82  
GLN N   CA   sing N N 83  
GLN N   H    sing N N 84  
GLN N   H2   sing N N 85  
GLN CA  C    sing N N 86  
GLN CA  CB   sing N N 87  
GLN CA  HA   sing N N 88  
GLN C   O    doub N N 89  
GLN C   OXT  sing N N 90  
GLN CB  CG   sing N N 91  
GLN CB  HB2  sing N N 92  
GLN CB  HB3  sing N N 93  
GLN CG  CD   sing N N 94  
GLN CG  HG2  sing N N 95  
GLN CG  HG3  sing N N 96  
GLN CD  OE1  doub N N 97  
GLN CD  NE2  sing N N 98  
GLN NE2 HE21 sing N N 99  
GLN NE2 HE22 sing N N 100 
GLN OXT HXT  sing N N 101 
GLU N   CA   sing N N 102 
GLU N   H    sing N N 103 
GLU N   H2   sing N N 104 
GLU CA  C    sing N N 105 
GLU CA  CB   sing N N 106 
GLU CA  HA   sing N N 107 
GLU C   O    doub N N 108 
GLU C   OXT  sing N N 109 
GLU CB  CG   sing N N 110 
GLU CB  HB2  sing N N 111 
GLU CB  HB3  sing N N 112 
GLU CG  CD   sing N N 113 
GLU CG  HG2  sing N N 114 
GLU CG  HG3  sing N N 115 
GLU CD  OE1  doub N N 116 
GLU CD  OE2  sing N N 117 
GLU OE2 HE2  sing N N 118 
GLU OXT HXT  sing N N 119 
GLY N   CA   sing N N 120 
GLY N   H    sing N N 121 
GLY N   H2   sing N N 122 
GLY CA  C    sing N N 123 
GLY CA  HA2  sing N N 124 
GLY CA  HA3  sing N N 125 
GLY C   O    doub N N 126 
GLY C   OXT  sing N N 127 
GLY OXT HXT  sing N N 128 
HIS N   CA   sing N N 129 
HIS N   H    sing N N 130 
HIS N   H2   sing N N 131 
HIS CA  C    sing N N 132 
HIS CA  CB   sing N N 133 
HIS CA  HA   sing N N 134 
HIS C   O    doub N N 135 
HIS C   OXT  sing N N 136 
HIS CB  CG   sing N N 137 
HIS CB  HB2  sing N N 138 
HIS CB  HB3  sing N N 139 
HIS CG  ND1  sing Y N 140 
HIS CG  CD2  doub Y N 141 
HIS ND1 CE1  doub Y N 142 
HIS ND1 HD1  sing N N 143 
HIS CD2 NE2  sing Y N 144 
HIS CD2 HD2  sing N N 145 
HIS CE1 NE2  sing Y N 146 
HIS CE1 HE1  sing N N 147 
HIS NE2 HE2  sing N N 148 
HIS OXT HXT  sing N N 149 
HOH O   H1   sing N N 150 
HOH O   H2   sing N N 151 
ILE N   CA   sing N N 152 
ILE N   H    sing N N 153 
ILE N   H2   sing N N 154 
ILE CA  C    sing N N 155 
ILE CA  CB   sing N N 156 
ILE CA  HA   sing N N 157 
ILE C   O    doub N N 158 
ILE C   OXT  sing N N 159 
ILE CB  CG1  sing N N 160 
ILE CB  CG2  sing N N 161 
ILE CB  HB   sing N N 162 
ILE CG1 CD1  sing N N 163 
ILE CG1 HG12 sing N N 164 
ILE CG1 HG13 sing N N 165 
ILE CG2 HG21 sing N N 166 
ILE CG2 HG22 sing N N 167 
ILE CG2 HG23 sing N N 168 
ILE CD1 HD11 sing N N 169 
ILE CD1 HD12 sing N N 170 
ILE CD1 HD13 sing N N 171 
ILE OXT HXT  sing N N 172 
LEU N   CA   sing N N 173 
LEU N   H    sing N N 174 
LEU N   H2   sing N N 175 
LEU CA  C    sing N N 176 
LEU CA  CB   sing N N 177 
LEU CA  HA   sing N N 178 
LEU C   O    doub N N 179 
LEU C   OXT  sing N N 180 
LEU CB  CG   sing N N 181 
LEU CB  HB2  sing N N 182 
LEU CB  HB3  sing N N 183 
LEU CG  CD1  sing N N 184 
LEU CG  CD2  sing N N 185 
LEU CG  HG   sing N N 186 
LEU CD1 HD11 sing N N 187 
LEU CD1 HD12 sing N N 188 
LEU CD1 HD13 sing N N 189 
LEU CD2 HD21 sing N N 190 
LEU CD2 HD22 sing N N 191 
LEU CD2 HD23 sing N N 192 
LEU OXT HXT  sing N N 193 
LYS N   CA   sing N N 194 
LYS N   H    sing N N 195 
LYS N   H2   sing N N 196 
LYS CA  C    sing N N 197 
LYS CA  CB   sing N N 198 
LYS CA  HA   sing N N 199 
LYS C   O    doub N N 200 
LYS C   OXT  sing N N 201 
LYS CB  CG   sing N N 202 
LYS CB  HB2  sing N N 203 
LYS CB  HB3  sing N N 204 
LYS CG  CD   sing N N 205 
LYS CG  HG2  sing N N 206 
LYS CG  HG3  sing N N 207 
LYS CD  CE   sing N N 208 
LYS CD  HD2  sing N N 209 
LYS CD  HD3  sing N N 210 
LYS CE  NZ   sing N N 211 
LYS CE  HE2  sing N N 212 
LYS CE  HE3  sing N N 213 
LYS NZ  HZ1  sing N N 214 
LYS NZ  HZ2  sing N N 215 
LYS NZ  HZ3  sing N N 216 
LYS OXT HXT  sing N N 217 
MET N   CA   sing N N 218 
MET N   H    sing N N 219 
MET N   H2   sing N N 220 
MET CA  C    sing N N 221 
MET CA  CB   sing N N 222 
MET CA  HA   sing N N 223 
MET C   O    doub N N 224 
MET C   OXT  sing N N 225 
MET CB  CG   sing N N 226 
MET CB  HB2  sing N N 227 
MET CB  HB3  sing N N 228 
MET CG  SD   sing N N 229 
MET CG  HG2  sing N N 230 
MET CG  HG3  sing N N 231 
MET SD  CE   sing N N 232 
MET CE  HE1  sing N N 233 
MET CE  HE2  sing N N 234 
MET CE  HE3  sing N N 235 
MET OXT HXT  sing N N 236 
PHE N   CA   sing N N 237 
PHE N   H    sing N N 238 
PHE N   H2   sing N N 239 
PHE CA  C    sing N N 240 
PHE CA  CB   sing N N 241 
PHE CA  HA   sing N N 242 
PHE C   O    doub N N 243 
PHE C   OXT  sing N N 244 
PHE CB  CG   sing N N 245 
PHE CB  HB2  sing N N 246 
PHE CB  HB3  sing N N 247 
PHE CG  CD1  doub Y N 248 
PHE CG  CD2  sing Y N 249 
PHE CD1 CE1  sing Y N 250 
PHE CD1 HD1  sing N N 251 
PHE CD2 CE2  doub Y N 252 
PHE CD2 HD2  sing N N 253 
PHE CE1 CZ   doub Y N 254 
PHE CE1 HE1  sing N N 255 
PHE CE2 CZ   sing Y N 256 
PHE CE2 HE2  sing N N 257 
PHE CZ  HZ   sing N N 258 
PHE OXT HXT  sing N N 259 
PRO N   CA   sing N N 260 
PRO N   CD   sing N N 261 
PRO N   H    sing N N 262 
PRO CA  C    sing N N 263 
PRO CA  CB   sing N N 264 
PRO CA  HA   sing N N 265 
PRO C   O    doub N N 266 
PRO C   OXT  sing N N 267 
PRO CB  CG   sing N N 268 
PRO CB  HB2  sing N N 269 
PRO CB  HB3  sing N N 270 
PRO CG  CD   sing N N 271 
PRO CG  HG2  sing N N 272 
PRO CG  HG3  sing N N 273 
PRO CD  HD2  sing N N 274 
PRO CD  HD3  sing N N 275 
PRO OXT HXT  sing N N 276 
SEP N   CA   sing N N 277 
SEP N   H    sing N N 278 
SEP N   H2   sing N N 279 
SEP CA  CB   sing N N 280 
SEP CA  C    sing N N 281 
SEP CA  HA   sing N N 282 
SEP CB  OG   sing N N 283 
SEP CB  HB2  sing N N 284 
SEP CB  HB3  sing N N 285 
SEP OG  P    sing N N 286 
SEP C   O    doub N N 287 
SEP C   OXT  sing N N 288 
SEP OXT HXT  sing N N 289 
SEP P   O1P  doub N N 290 
SEP P   O2P  sing N N 291 
SEP P   O3P  sing N N 292 
SEP O2P HOP2 sing N N 293 
SEP O3P HOP3 sing N N 294 
SER N   CA   sing N N 295 
SER N   H    sing N N 296 
SER N   H2   sing N N 297 
SER CA  C    sing N N 298 
SER CA  CB   sing N N 299 
SER CA  HA   sing N N 300 
SER C   O    doub N N 301 
SER C   OXT  sing N N 302 
SER CB  OG   sing N N 303 
SER CB  HB2  sing N N 304 
SER CB  HB3  sing N N 305 
SER OG  HG   sing N N 306 
SER OXT HXT  sing N N 307 
THR N   CA   sing N N 308 
THR N   H    sing N N 309 
THR N   H2   sing N N 310 
THR CA  C    sing N N 311 
THR CA  CB   sing N N 312 
THR CA  HA   sing N N 313 
THR C   O    doub N N 314 
THR C   OXT  sing N N 315 
THR CB  OG1  sing N N 316 
THR CB  CG2  sing N N 317 
THR CB  HB   sing N N 318 
THR OG1 HG1  sing N N 319 
THR CG2 HG21 sing N N 320 
THR CG2 HG22 sing N N 321 
THR CG2 HG23 sing N N 322 
THR OXT HXT  sing N N 323 
TRP N   CA   sing N N 324 
TRP N   H    sing N N 325 
TRP N   H2   sing N N 326 
TRP CA  C    sing N N 327 
TRP CA  CB   sing N N 328 
TRP CA  HA   sing N N 329 
TRP C   O    doub N N 330 
TRP C   OXT  sing N N 331 
TRP CB  CG   sing N N 332 
TRP CB  HB2  sing N N 333 
TRP CB  HB3  sing N N 334 
TRP CG  CD1  doub Y N 335 
TRP CG  CD2  sing Y N 336 
TRP CD1 NE1  sing Y N 337 
TRP CD1 HD1  sing N N 338 
TRP CD2 CE2  doub Y N 339 
TRP CD2 CE3  sing Y N 340 
TRP NE1 CE2  sing Y N 341 
TRP NE1 HE1  sing N N 342 
TRP CE2 CZ2  sing Y N 343 
TRP CE3 CZ3  doub Y N 344 
TRP CE3 HE3  sing N N 345 
TRP CZ2 CH2  doub Y N 346 
TRP CZ2 HZ2  sing N N 347 
TRP CZ3 CH2  sing Y N 348 
TRP CZ3 HZ3  sing N N 349 
TRP CH2 HH2  sing N N 350 
TRP OXT HXT  sing N N 351 
TYR N   CA   sing N N 352 
TYR N   H    sing N N 353 
TYR N   H2   sing N N 354 
TYR CA  C    sing N N 355 
TYR CA  CB   sing N N 356 
TYR CA  HA   sing N N 357 
TYR C   O    doub N N 358 
TYR C   OXT  sing N N 359 
TYR CB  CG   sing N N 360 
TYR CB  HB2  sing N N 361 
TYR CB  HB3  sing N N 362 
TYR CG  CD1  doub Y N 363 
TYR CG  CD2  sing Y N 364 
TYR CD1 CE1  sing Y N 365 
TYR CD1 HD1  sing N N 366 
TYR CD2 CE2  doub Y N 367 
TYR CD2 HD2  sing N N 368 
TYR CE1 CZ   doub Y N 369 
TYR CE1 HE1  sing N N 370 
TYR CE2 CZ   sing Y N 371 
TYR CE2 HE2  sing N N 372 
TYR CZ  OH   sing N N 373 
TYR OH  HH   sing N N 374 
TYR OXT HXT  sing N N 375 
VAL N   CA   sing N N 376 
VAL N   H    sing N N 377 
VAL N   H2   sing N N 378 
VAL CA  C    sing N N 379 
VAL CA  CB   sing N N 380 
VAL CA  HA   sing N N 381 
VAL C   O    doub N N 382 
VAL C   OXT  sing N N 383 
VAL CB  CG1  sing N N 384 
VAL CB  CG2  sing N N 385 
VAL CB  HB   sing N N 386 
VAL CG1 HG11 sing N N 387 
VAL CG1 HG12 sing N N 388 
VAL CG1 HG13 sing N N 389 
VAL CG2 HG21 sing N N 390 
VAL CG2 HG22 sing N N 391 
VAL CG2 HG23 sing N N 392 
VAL OXT HXT  sing N N 393 
WQ9 C2  C1   sing N N 394 
WQ9 O1  C1   doub N N 395 
WQ9 C1  N1   sing N N 396 
WQ9 N1  C3   sing N N 397 
WQ9 N1  C15  sing N N 398 
WQ9 C3  C4   sing N N 399 
WQ9 C15 C5   sing N N 400 
WQ9 O2  S1   doub N N 401 
WQ9 C14 C5   sing N N 402 
WQ9 C14 N2   sing N N 403 
WQ9 F1  C12  sing N N 404 
WQ9 C4  C5   sing N N 405 
WQ9 C5  C6   sing N N 406 
WQ9 C13 C12  doub Y N 407 
WQ9 C13 C8   sing Y N 408 
WQ9 N2  S1   sing N N 409 
WQ9 N2  C7   sing N N 410 
WQ9 S1  C8   sing N N 411 
WQ9 S1  O3   doub N N 412 
WQ9 C12 C11  sing Y N 413 
WQ9 C8  C9   doub Y N 414 
WQ9 C6  C7   sing N N 415 
WQ9 C11 BR1  sing N N 416 
WQ9 C11 C10  doub Y N 417 
WQ9 C9  C10  sing Y N 418 
WQ9 C2  H1   sing N N 419 
WQ9 C2  H2   sing N N 420 
WQ9 C3  H4   sing N N 421 
WQ9 C3  H5   sing N N 422 
WQ9 C4  H6   sing N N 423 
WQ9 C4  H7   sing N N 424 
WQ9 C6  H8   sing N N 425 
WQ9 C6  H9   sing N N 426 
WQ9 C7  H10  sing N N 427 
WQ9 C7  H11  sing N N 428 
WQ9 C9  H12  sing N N 429 
WQ9 C10 H13  sing N N 430 
WQ9 C13 H14  sing N N 431 
WQ9 C14 H15  sing N N 432 
WQ9 C14 H16  sing N N 433 
WQ9 C15 H17  sing N N 434 
WQ9 C15 H18  sing N N 435 
WQ9 C2  CL1  sing N N 436 
# 
_pdbx_audit_support.funding_organization   
'National Institutes of Health/National Institute of General Medical Sciences (NIH/NIGMS)' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           GM147696 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   3IQU 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    8QSA 
_atom_sites.Cartn_transf_matrix[1][1]   ? 
_atom_sites.Cartn_transf_matrix[1][2]   ? 
_atom_sites.Cartn_transf_matrix[1][3]   ? 
_atom_sites.Cartn_transf_matrix[2][1]   ? 
_atom_sites.Cartn_transf_matrix[2][2]   ? 
_atom_sites.Cartn_transf_matrix[2][3]   ? 
_atom_sites.Cartn_transf_matrix[3][1]   ? 
_atom_sites.Cartn_transf_matrix[3][2]   ? 
_atom_sites.Cartn_transf_matrix[3][3]   ? 
_atom_sites.Cartn_transf_vector[1]      ? 
_atom_sites.Cartn_transf_vector[2]      ? 
_atom_sites.Cartn_transf_vector[3]      ? 
_atom_sites.Cartn_transform_axes        ? 
_atom_sites.fract_transf_matrix[1][1]   0.016063 
_atom_sites.fract_transf_matrix[1][2]   0.000000 
_atom_sites.fract_transf_matrix[1][3]   0.000000 
_atom_sites.fract_transf_matrix[2][1]   0.000000 
_atom_sites.fract_transf_matrix[2][2]   0.006693 
_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]   0.013027 
_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 
BR 
C  
CL 
F  
MG 
N  
O  
P  
S  
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . GLY A 1 1   ? 34.589 39.543 25.506 1.00 75.29 ? -4  GLY A N   1 
ATOM   2    C  CA  . GLY A 1 1   ? 35.386 40.737 25.728 1.00 68.83 ? -4  GLY A CA  1 
ATOM   3    C  C   . GLY A 1 1   ? 36.574 40.444 26.621 1.00 61.89 ? -4  GLY A C   1 
ATOM   4    O  O   . GLY A 1 1   ? 37.682 40.918 26.373 1.00 63.86 ? -4  GLY A O   1 
ATOM   5    N  N   . ALA A 1 2   ? 36.326 39.645 27.661 1.00 58.05 ? -3  ALA A N   1 
ATOM   6    C  CA  . ALA A 1 2   ? 37.382 39.218 28.573 1.00 55.96 ? -3  ALA A CA  1 
ATOM   7    C  C   . ALA A 1 2   ? 38.507 38.484 27.861 1.00 50.96 ? -3  ALA A C   1 
ATOM   8    O  O   . ALA A 1 2   ? 39.630 38.445 28.375 1.00 49.00 ? -3  ALA A O   1 
ATOM   9    C  CB  . ALA A 1 2   ? 36.804 38.319 29.663 1.00 57.94 ? -3  ALA A CB  1 
ATOM   10   N  N   . MET A 1 3   ? 38.242 37.915 26.691 1.00 50.09 ? -2  MET A N   1 
ATOM   11   C  CA  . MET A 1 3   ? 39.228 37.103 26.006 1.00 46.08 ? -2  MET A CA  1 
ATOM   12   C  C   . MET A 1 3   ? 39.896 37.867 24.862 1.00 45.30 ? -2  MET A C   1 
ATOM   13   O  O   . MET A 1 3   ? 40.716 37.297 24.129 1.00 42.39 ? -2  MET A O   1 
ATOM   14   C  CB  . MET A 1 3   ? 38.546 35.855 25.452 1.00 43.67 ? -2  MET A CB  1 
ATOM   15   C  CG  . MET A 1 3   ? 38.390 34.671 26.406 1.00 43.32 ? -2  MET A CG  1 
ATOM   16   S  SD  . MET A 1 3   ? 39.571 34.375 27.735 1.00 44.97 ? -2  MET A SD  1 
ATOM   17   C  CE  . MET A 1 3   ? 38.528 33.673 29.028 1.00 44.15 ? -2  MET A CE  1 
ATOM   18   N  N   . GLY A 1 4   ? 39.544 39.141 24.680 1.00 45.85 ? -1  GLY A N   1 
ATOM   19   C  CA  . GLY A 1 4   ? 39.946 39.861 23.483 1.00 46.37 ? -1  GLY A CA  1 
ATOM   20   C  C   . GLY A 1 4   ? 41.442 40.068 23.344 1.00 44.14 ? -1  GLY A C   1 
ATOM   21   O  O   . GLY A 1 4   ? 41.945 40.213 22.224 1.00 43.13 ? -1  GLY A O   1 
ATOM   22   N  N   . SER A 1 5   ? 42.180 40.082 24.463 1.00 40.89 ? 0   SER A N   1 
ATOM   23   C  CA  . SER A 1 5   ? 43.620 40.312 24.371 1.00 42.08 ? 0   SER A CA  1 
ATOM   24   C  C   . SER A 1 5   ? 44.407 39.042 24.057 1.00 41.44 ? 0   SER A C   1 
ATOM   25   O  O   . SER A 1 5   ? 45.593 39.146 23.735 1.00 42.52 ? 0   SER A O   1 
ATOM   26   C  CB  . SER A 1 5   ? 44.162 40.908 25.671 1.00 42.76 ? 0   SER A CB  1 
ATOM   27   O  OG  . SER A 1 5   ? 43.663 40.161 26.765 1.00 45.75 ? 0   SER A OG  1 
ATOM   28   N  N   . MET A 1 6   ? 43.792 37.862 24.161 1.00 40.95 ? 1   MET A N   1 
ATOM   29   C  CA  . MET A 1 6   ? 44.492 36.603 23.911 1.00 39.60 ? 1   MET A CA  1 
ATOM   30   C  C   . MET A 1 6   ? 44.471 36.178 22.453 1.00 40.66 ? 1   MET A C   1 
ATOM   31   O  O   . MET A 1 6   ? 43.445 36.271 21.776 1.00 39.33 ? 1   MET A O   1 
ATOM   32   C  CB  . MET A 1 6   ? 43.926 35.421 24.702 1.00 40.67 ? 1   MET A CB  1 
ATOM   33   C  CG  . MET A 1 6   ? 45.008 34.594 25.344 1.00 42.85 ? 1   MET A CG  1 
ATOM   34   S  SD  . MET A 1 6   ? 44.352 33.160 26.235 1.00 41.88 ? 1   MET A SD  1 
ATOM   35   C  CE  . MET A 1 6   ? 43.250 33.939 27.391 1.00 38.81 ? 1   MET A CE  1 
ATOM   36   N  N   . GLU A 1 7   ? 45.590 35.623 22.005 1.00 39.78 ? 2   GLU A N   1 
ATOM   37   C  CA  . GLU A 1 7   ? 45.658 35.132 20.636 1.00 39.78 ? 2   GLU A CA  1 
ATOM   38   C  C   . GLU A 1 7   ? 44.729 33.940 20.449 1.00 38.22 ? 2   GLU A C   1 
ATOM   39   O  O   . GLU A 1 7   ? 44.551 33.106 21.347 1.00 37.24 ? 2   GLU A O   1 
ATOM   40   C  CB  . GLU A 1 7   ? 47.083 34.731 20.279 1.00 40.69 ? 2   GLU A CB  1 
ATOM   41   C  CG  . GLU A 1 7   ? 47.978 35.935 20.072 1.00 43.66 ? 2   GLU A CG  1 
ATOM   42   C  CD  . GLU A 1 7   ? 49.357 35.561 19.622 1.00 46.44 ? 2   GLU A CD  1 
ATOM   43   O  OE1 . GLU A 1 7   ? 49.916 36.277 18.771 1.00 46.53 ? 2   GLU A OE1 1 
ATOM   44   O  OE2 . GLU A 1 7   ? 49.812 34.452 19.995 1.00 47.10 ? 2   GLU A OE2 1 
ATOM   45   N  N   . ARG A 1 8   ? 44.154 33.846 19.246 1.00 38.12 ? 3   ARG A N   1 
ATOM   46   C  CA  . ARG A 1 8   ? 43.268 32.726 18.935 1.00 36.83 ? 3   ARG A CA  1 
ATOM   47   C  C   . ARG A 1 8   ? 43.905 31.381 19.270 1.00 36.34 ? 3   ARG A C   1 
ATOM   48   O  O   . ARG A 1 8   ? 43.265 30.523 19.888 1.00 35.72 ? 3   ARG A O   1 
ATOM   49   C  CB  . ARG A 1 8   ? 42.870 32.756 17.460 1.00 37.13 ? 3   ARG A CB  1 
ATOM   50   C  CG  . ARG A 1 8   ? 41.759 31.741 17.116 1.00 37.36 ? 3   ARG A CG  1 
ATOM   51   C  CD  . ARG A 1 8   ? 41.507 31.712 15.624 1.00 40.46 ? 3   ARG A CD  1 
ATOM   52   N  NE  . ARG A 1 8   ? 40.329 30.926 15.281 1.00 38.20 ? 3   ARG A NE  1 
ATOM   53   C  CZ  . ARG A 1 8   ? 40.289 29.602 15.251 1.00 40.59 ? 3   ARG A CZ  1 
ATOM   54   N  NH1 . ARG A 1 8   ? 41.355 28.867 15.537 1.00 40.28 ? 3   ARG A NH1 1 
ATOM   55   N  NH2 . ARG A 1 8   ? 39.150 28.998 14.925 1.00 40.71 ? 3   ARG A NH2 1 
ATOM   56   N  N   . ALA A 1 9   ? 45.155 31.167 18.848 1.00 37.05 ? 4   ALA A N   1 
ATOM   57   C  CA  . ALA A 1 9   ? 45.781 29.861 19.060 1.00 37.01 ? 4   ALA A CA  1 
ATOM   58   C  C   . ALA A 1 9   ? 45.921 29.546 20.547 1.00 37.83 ? 4   ALA A C   1 
ATOM   59   O  O   . ALA A 1 9   ? 45.782 28.383 20.965 1.00 38.68 ? 4   ALA A O   1 
ATOM   60   C  CB  . ALA A 1 9   ? 47.144 29.810 18.378 1.00 39.35 ? 4   ALA A CB  1 
ATOM   61   N  N   . SER A 1 10  ? 46.194 30.567 21.360 1.00 36.99 ? 5   SER A N   1 
ATOM   62   C  CA  . SER A 1 10  ? 46.313 30.370 22.800 1.00 37.42 ? 5   SER A CA  1 
ATOM   63   C  C   . SER A 1 10  ? 44.969 30.046 23.427 1.00 37.39 ? 5   SER A C   1 
ATOM   64   O  O   . SER A 1 10  ? 44.904 29.264 24.389 1.00 35.08 ? 5   SER A O   1 
ATOM   65   C  CB  . SER A 1 10  ? 46.907 31.626 23.447 1.00 37.69 ? 5   SER A CB  1 
ATOM   66   O  OG  . SER A 1 10  ? 48.210 31.870 22.945 1.00 39.08 ? 5   SER A OG  1 
ATOM   67   N  N   . LEU A 1 11  ? 43.887 30.635 22.902 1.00 34.87 ? 6   LEU A N   1 
ATOM   68   C  CA  . LEU A 1 11  ? 42.555 30.309 23.400 1.00 33.73 ? 6   LEU A CA  1 
ATOM   69   C  C   . LEU A 1 11  ? 42.197 28.857 23.116 1.00 34.04 ? 6   LEU A C   1 
ATOM   70   O  O   . LEU A 1 11  ? 41.646 28.163 23.985 1.00 32.95 ? 6   LEU A O   1 
ATOM   71   C  CB  . LEU A 1 11  ? 41.518 31.231 22.784 1.00 33.77 ? 6   LEU A CB  1 
ATOM   72   C  CG  . LEU A 1 11  ? 41.615 32.686 23.259 1.00 34.63 ? 6   LEU A CG  1 
ATOM   73   C  CD1 . LEU A 1 11  ? 40.843 33.573 22.294 1.00 36.24 ? 6   LEU A CD1 1 
ATOM   74   C  CD2 . LEU A 1 11  ? 41.061 32.770 24.677 1.00 34.08 ? 6   LEU A CD2 1 
ATOM   75   N  N   . ILE A 1 12  ? 42.504 28.385 21.904 1.00 34.92 ? 7   ILE A N   1 
ATOM   76   C  CA  . ILE A 1 12  ? 42.287 26.979 21.565 1.00 33.91 ? 7   ILE A CA  1 
ATOM   77   C  C   . ILE A 1 12  ? 43.086 26.085 22.499 1.00 35.13 ? 7   ILE A C   1 
ATOM   78   O  O   . ILE A 1 12  ? 42.573 25.089 23.026 1.00 35.40 ? 7   ILE A O   1 
ATOM   79   C  CB  . ILE A 1 12  ? 42.675 26.703 20.104 1.00 33.31 ? 7   ILE A CB  1 
ATOM   80   C  CG1 . ILE A 1 12  ? 41.805 27.507 19.126 1.00 36.73 ? 7   ILE A CG1 1 
ATOM   81   C  CG2 . ILE A 1 12  ? 42.617 25.192 19.832 1.00 34.24 ? 7   ILE A CG2 1 
ATOM   82   C  CD1 . ILE A 1 12  ? 40.324 27.314 19.319 1.00 35.99 ? 7   ILE A CD1 1 
ATOM   83   N  N   . GLN A 1 13  ? 44.373 26.390 22.654 1.00 33.30 ? 8   GLN A N   1 
ATOM   84   C  CA  . GLN A 1 13  ? 45.240 25.612 23.531 1.00 35.77 ? 8   GLN A CA  1 
ATOM   85   C  C   . GLN A 1 13  ? 44.673 25.551 24.942 1.00 36.74 ? 8   GLN A C   1 
ATOM   86   O  O   . GLN A 1 13  ? 44.643 24.482 25.577 1.00 35.21 ? 8   GLN A O   1 
ATOM   87   C  CB  . GLN A 1 13  ? 46.631 26.241 23.555 1.00 39.82 ? 8   GLN A CB  1 
ATOM   88   C  CG  . GLN A 1 13  ? 47.684 25.454 24.325 1.00 42.35 ? 8   GLN A CG  1 
ATOM   89   C  CD  . GLN A 1 13  ? 49.057 26.119 24.265 1.00 48.63 ? 8   GLN A CD  1 
ATOM   90   O  OE1 . GLN A 1 13  ? 49.276 27.051 23.478 1.00 49.33 ? 8   GLN A OE1 1 
ATOM   91   N  NE2 . GLN A 1 13  ? 49.993 25.637 25.093 1.00 48.44 ? 8   GLN A NE2 1 
ATOM   92   N  N   . LYS A 1 14  ? 44.229 26.701 25.457 1.00 33.66 ? 9   LYS A N   1 
ATOM   93   C  CA  . LYS A 1 14  ? 43.698 26.740 26.813 1.00 34.50 ? 9   LYS A CA  1 
ATOM   94   C  C   . LYS A 1 14  ? 42.363 26.017 26.919 1.00 34.81 ? 9   LYS A C   1 
ATOM   95   O  O   . LYS A 1 14  ? 42.082 25.396 27.950 1.00 33.48 ? 9   LYS A O   1 
ATOM   96   C  CB  . LYS A 1 14  ? 43.602 28.198 27.284 1.00 32.99 ? 9   LYS A CB  1 
ATOM   97   C  CG  . LYS A 1 14  ? 44.978 28.759 27.567 1.00 35.41 ? 9   LYS A CG  1 
ATOM   98   C  CD  . LYS A 1 14  ? 44.932 30.134 28.229 1.00 36.49 ? 9   LYS A CD  1 
ATOM   99   C  CE  . LYS A 1 14  ? 46.325 30.714 28.323 1.00 37.99 ? 9   LYS A CE  1 
ATOM   100  N  NZ  . LYS A 1 14  ? 46.310 32.125 28.858 1.00 37.27 ? 9   LYS A NZ  1 
ATOM   101  N  N   . ALA A 1 15  ? 41.549 26.034 25.863 1.00 33.65 ? 10  ALA A N   1 
ATOM   102  C  CA  . ALA A 1 15  ? 40.323 25.245 25.886 1.00 32.87 ? 10  ALA A CA  1 
ATOM   103  C  C   . ALA A 1 15  ? 40.636 23.766 26.033 1.00 33.66 ? 10  ALA A C   1 
ATOM   104  O  O   . ALA A 1 15  ? 39.935 23.047 26.756 1.00 33.34 ? 10  ALA A O   1 
ATOM   105  C  CB  . ALA A 1 15  ? 39.499 25.485 24.621 1.00 32.88 ? 10  ALA A CB  1 
ATOM   106  N  N   . LYS A 1 16  ? 41.690 23.299 25.364 1.00 32.26 ? 11  LYS A N   1 
ATOM   107  C  CA  . LYS A 1 16  ? 42.064 21.889 25.475 1.00 35.12 ? 11  LYS A CA  1 
ATOM   108  C  C   . LYS A 1 16  ? 42.564 21.558 26.877 1.00 37.65 ? 11  LYS A C   1 
ATOM   109  O  O   . LYS A 1 16  ? 42.275 20.474 27.401 1.00 36.16 ? 11  LYS A O   1 
ATOM   110  C  CB  . LYS A 1 16  ? 43.122 21.545 24.436 1.00 33.20 ? 11  LYS A CB  1 
ATOM   111  C  CG  . LYS A 1 16  ? 42.558 21.520 23.019 1.00 36.97 ? 11  LYS A CG  1 
ATOM   112  C  CD  . LYS A 1 16  ? 43.654 21.276 21.996 1.00 40.63 ? 11  LYS A CD  1 
ATOM   113  C  CE  . LYS A 1 16  ? 43.115 21.394 20.573 1.00 42.33 ? 11  LYS A CE  1 
ATOM   114  N  NZ  . LYS A 1 16  ? 44.235 21.494 19.586 1.00 40.98 ? 11  LYS A NZ  1 
ATOM   115  N  N   . LEU A 1 17  ? 43.326 22.468 27.493 1.00 33.93 ? 12  LEU A N   1 
ATOM   116  C  CA  . LEU A 1 17  ? 43.777 22.256 28.872 1.00 36.32 ? 12  LEU A CA  1 
ATOM   117  C  C   . LEU A 1 17  ? 42.603 22.237 29.836 1.00 36.94 ? 12  LEU A C   1 
ATOM   118  O  O   . LEU A 1 17  ? 42.564 21.425 30.776 1.00 36.96 ? 12  LEU A O   1 
ATOM   119  C  CB  . LEU A 1 17  ? 44.762 23.353 29.290 1.00 35.34 ? 12  LEU A CB  1 
ATOM   120  C  CG  . LEU A 1 17  ? 46.071 23.439 28.500 1.00 37.33 ? 12  LEU A CG  1 
ATOM   121  C  CD1 . LEU A 1 17  ? 46.785 24.758 28.839 1.00 38.53 ? 12  LEU A CD1 1 
ATOM   122  C  CD2 . LEU A 1 17  ? 46.980 22.240 28.783 1.00 35.65 ? 12  LEU A CD2 1 
ATOM   123  N  N   . ALA A 1 18  ? 41.641 23.131 29.627 1.00 33.53 ? 13  ALA A N   1 
ATOM   124  C  CA  . ALA A 1 18  ? 40.475 23.179 30.500 1.00 34.94 ? 13  ALA A CA  1 
ATOM   125  C  C   . ALA A 1 18  ? 39.647 21.908 30.379 1.00 35.74 ? 13  ALA A C   1 
ATOM   126  O  O   . ALA A 1 18  ? 39.105 21.418 31.382 1.00 34.92 ? 13  ALA A O   1 
ATOM   127  C  CB  . ALA A 1 18  ? 39.633 24.400 30.164 1.00 33.90 ? 13  ALA A CB  1 
ATOM   128  N  N   . GLU A 1 19  ? 39.530 21.368 29.161 1.00 34.22 ? 14  GLU A N   1 
ATOM   129  C  CA  . GLU A 1 19  ? 38.882 20.064 28.994 1.00 35.87 ? 14  GLU A CA  1 
ATOM   130  C  C   . GLU A 1 19  ? 39.602 18.994 29.804 1.00 36.48 ? 14  GLU A C   1 
ATOM   131  O  O   . GLU A 1 19  ? 38.964 18.181 30.494 1.00 37.47 ? 14  GLU A O   1 
ATOM   132  C  CB  . GLU A 1 19  ? 38.832 19.665 27.518 1.00 34.17 ? 14  GLU A CB  1 
ATOM   133  C  CG  . GLU A 1 19  ? 38.047 18.349 27.302 1.00 38.27 ? 14  GLU A CG  1 
ATOM   134  C  CD  . GLU A 1 19  ? 37.947 17.925 25.850 1.00 41.58 ? 14  GLU A CD  1 
ATOM   135  O  OE1 . GLU A 1 19  ? 38.842 18.272 25.051 1.00 40.53 ? 14  GLU A OE1 1 
ATOM   136  O  OE2 . GLU A 1 19  ? 36.950 17.253 25.503 1.00 43.91 ? 14  GLU A OE2 1 
ATOM   137  N  N   . GLN A 1 20  ? 40.935 18.966 29.722 1.00 35.18 ? 15  GLN A N   1 
ATOM   138  C  CA  . GLN A 1 20  ? 41.698 17.981 30.487 1.00 36.01 ? 15  GLN A CA  1 
ATOM   139  C  C   . GLN A 1 20  ? 41.487 18.142 31.986 1.00 38.06 ? 15  GLN A C   1 
ATOM   140  O  O   . GLN A 1 20  ? 41.481 17.152 32.734 1.00 36.63 ? 15  GLN A O   1 
ATOM   141  C  CB  . GLN A 1 20  ? 43.185 18.072 30.160 1.00 37.26 ? 15  GLN A CB  1 
ATOM   142  C  CG  . GLN A 1 20  ? 43.552 17.610 28.758 1.00 39.25 ? 15  GLN A CG  1 
ATOM   143  C  CD  . GLN A 1 20  ? 45.016 17.860 28.441 1.00 45.98 ? 15  GLN A CD  1 
ATOM   144  O  OE1 . GLN A 1 20  ? 45.414 18.984 28.126 1.00 47.93 ? 15  GLN A OE1 1 
ATOM   145  N  NE2 . GLN A 1 20  ? 45.836 16.827 28.589 1.00 49.42 ? 15  GLN A NE2 1 
ATOM   146  N  N   . ALA A 1 21  ? 41.344 19.369 32.448 1.00 35.64 ? 16  ALA A N   1 
ATOM   147  C  CA  . ALA A 1 21  ? 41.157 19.667 33.855 1.00 38.21 ? 16  ALA A CA  1 
ATOM   148  C  C   . ALA A 1 21  ? 39.697 19.586 34.285 1.00 36.33 ? 16  ALA A C   1 
ATOM   149  O  O   . ALA A 1 21  ? 39.407 19.814 35.465 1.00 38.19 ? 16  ALA A O   1 
ATOM   150  C  CB  . ALA A 1 21  ? 41.720 21.058 34.168 1.00 36.98 ? 16  ALA A CB  1 
ATOM   151  N  N   . GLU A 1 22  ? 38.788 19.254 33.366 1.00 35.69 ? 17  GLU A N   1 
ATOM   152  C  CA  . GLU A 1 22  ? 37.350 19.205 33.648 1.00 39.39 ? 17  GLU A CA  1 
ATOM   153  C  C   . GLU A 1 22  ? 36.846 20.559 34.152 1.00 38.68 ? 17  GLU A C   1 
ATOM   154  O  O   . GLU A 1 22  ? 35.963 20.656 35.007 1.00 39.48 ? 17  GLU A O   1 
ATOM   155  C  CB  . GLU A 1 22  ? 37.021 18.064 34.628 1.00 40.02 ? 17  GLU A CB  1 
ATOM   156  C  CG  . GLU A 1 22  ? 37.289 16.707 33.994 1.00 42.39 ? 17  GLU A CG  1 
ATOM   157  C  CD  . GLU A 1 22  ? 37.163 15.561 34.973 1.00 51.55 ? 17  GLU A CD  1 
ATOM   158  O  OE1 . GLU A 1 22  ? 38.172 14.866 35.217 1.00 55.02 ? 17  GLU A OE1 1 
ATOM   159  O  OE2 . GLU A 1 22  ? 36.053 15.370 35.506 1.00 52.44 ? 17  GLU A OE2 1 
ATOM   160  N  N   . ARG A 1 23  ? 37.412 21.629 33.598 1.00 37.91 ? 18  ARG A N   1 
ATOM   161  C  CA  . ARG A 1 23  ? 36.984 22.994 33.894 1.00 35.29 ? 18  ARG A CA  1 
ATOM   162  C  C   . ARG A 1 23  ? 36.142 23.504 32.724 1.00 36.81 ? 18  ARG A C   1 
ATOM   163  O  O   . ARG A 1 23  ? 36.611 24.256 31.863 1.00 34.48 ? 18  ARG A O   1 
ATOM   164  C  CB  . ARG A 1 23  ? 38.207 23.867 34.136 1.00 36.11 ? 18  ARG A CB  1 
ATOM   165  C  CG  . ARG A 1 23  ? 38.993 23.465 35.382 1.00 38.43 ? 18  ARG A CG  1 
ATOM   166  C  CD  . ARG A 1 23  ? 38.426 24.166 36.575 1.00 38.14 ? 18  ARG A CD  1 
ATOM   167  N  NE  . ARG A 1 23  ? 38.654 25.599 36.452 1.00 37.67 ? 18  ARG A NE  1 
ATOM   168  C  CZ  . ARG A 1 23  ? 38.572 26.470 37.442 1.00 41.54 ? 18  ARG A CZ  1 
ATOM   169  N  NH1 . ARG A 1 23  ? 38.294 26.087 38.680 1.00 39.52 ? 18  ARG A NH1 1 
ATOM   170  N  NH2 . ARG A 1 23  ? 38.774 27.758 37.186 1.00 36.46 ? 18  ARG A NH2 1 
ATOM   171  N  N   . TYR A 1 24  ? 34.879 23.067 32.672 1.00 34.22 ? 19  TYR A N   1 
ATOM   172  C  CA  . TYR A 1 24  ? 34.126 23.279 31.436 1.00 34.77 ? 19  TYR A CA  1 
ATOM   173  C  C   . TYR A 1 24  ? 33.631 24.704 31.292 1.00 34.89 ? 19  TYR A C   1 
ATOM   174  O  O   . TYR A 1 24  ? 33.431 25.170 30.164 1.00 33.31 ? 19  TYR A O   1 
ATOM   175  C  CB  . TYR A 1 24  ? 32.953 22.312 31.340 1.00 33.64 ? 19  TYR A CB  1 
ATOM   176  C  CG  . TYR A 1 24  ? 33.451 20.890 31.276 1.00 36.13 ? 19  TYR A CG  1 
ATOM   177  C  CD1 . TYR A 1 24  ? 34.048 20.401 30.126 1.00 38.37 ? 19  TYR A CD1 1 
ATOM   178  C  CD2 . TYR A 1 24  ? 33.377 20.055 32.388 1.00 39.30 ? 19  TYR A CD2 1 
ATOM   179  C  CE1 . TYR A 1 24  ? 34.525 19.105 30.062 1.00 38.18 ? 19  TYR A CE1 1 
ATOM   180  C  CE2 . TYR A 1 24  ? 33.860 18.762 32.337 1.00 40.72 ? 19  TYR A CE2 1 
ATOM   181  C  CZ  . TYR A 1 24  ? 34.437 18.301 31.180 1.00 41.07 ? 19  TYR A CZ  1 
ATOM   182  O  OH  . TYR A 1 24  ? 34.900 17.013 31.123 1.00 44.83 ? 19  TYR A OH  1 
ATOM   183  N  N   . GLU A 1 25  ? 33.402 25.404 32.403 1.00 32.80 ? 20  GLU A N   1 
ATOM   184  C  CA  . GLU A 1 25  ? 33.037 26.811 32.292 1.00 36.83 ? 20  GLU A CA  1 
ATOM   185  C  C   . GLU A 1 25  ? 34.188 27.623 31.706 1.00 34.25 ? 20  GLU A C   1 
ATOM   186  O  O   . GLU A 1 25  ? 33.968 28.511 30.871 1.00 34.41 ? 20  GLU A O   1 
ATOM   187  C  CB  . GLU A 1 25  ? 32.628 27.344 33.673 1.00 39.87 ? 20  GLU A CB  1 
ATOM   188  C  CG  . GLU A 1 25  ? 31.220 26.899 34.101 1.00 43.47 ? 20  GLU A CG  1 
ATOM   189  C  CD  . GLU A 1 25  ? 30.462 27.936 34.932 1.00 54.75 ? 20  GLU A CD  1 
ATOM   190  O  OE1 . GLU A 1 25  ? 31.107 28.880 35.458 1.00 53.58 ? 20  GLU A OE1 1 
ATOM   191  O  OE2 . GLU A 1 25  ? 29.213 27.802 35.050 1.00 55.38 ? 20  GLU A OE2 1 
ATOM   192  N  N   . ASP A 1 26  ? 35.417 27.357 32.158 1.00 34.81 ? 21  ASP A N   1 
ATOM   193  C  CA  . ASP A 1 26  ? 36.587 27.987 31.552 1.00 33.94 ? 21  ASP A CA  1 
ATOM   194  C  C   . ASP A 1 26  ? 36.699 27.592 30.090 1.00 33.09 ? 21  ASP A C   1 
ATOM   195  O  O   . ASP A 1 26  ? 37.006 28.426 29.224 1.00 34.06 ? 21  ASP A O   1 
ATOM   196  C  CB  . ASP A 1 26  ? 37.868 27.550 32.259 1.00 34.35 ? 21  ASP A CB  1 
ATOM   197  C  CG  . ASP A 1 26  ? 38.008 28.104 33.655 1.00 38.96 ? 21  ASP A CG  1 
ATOM   198  O  OD1 . ASP A 1 26  ? 37.231 28.997 34.043 1.00 36.98 ? 21  ASP A OD1 1 
ATOM   199  O  OD2 . ASP A 1 26  ? 38.924 27.631 34.352 1.00 39.01 ? 21  ASP A OD2 1 
ATOM   200  N  N   . MET A 1 27  ? 36.506 26.307 29.797 1.00 31.97 ? 22  MET A N   1 
ATOM   201  C  CA  . MET A 1 27  ? 36.723 25.907 28.409 1.00 30.87 ? 22  MET A CA  1 
ATOM   202  C  C   . MET A 1 27  ? 35.665 26.538 27.500 1.00 34.34 ? 22  MET A C   1 
ATOM   203  O  O   . MET A 1 27  ? 35.993 26.958 26.383 1.00 33.29 ? 22  MET A O   1 
ATOM   204  C  CB  . MET A 1 27  ? 36.899 24.368 28.326 1.00 34.48 ? 22  MET A CB  1 
ATOM   205  C  CG  . MET A 1 27  ? 36.692 23.638 27.011 1.00 30.04 ? 22  MET A CG  1 
ATOM   206  S  SD  . MET A 1 27  ? 35.998 21.951 27.178 1.00 32.41 ? 22  MET A SD  1 
ATOM   207  C  CE  . MET A 1 27  ? 36.392 21.409 25.502 1.00 32.32 ? 22  MET A CE  1 
ATOM   208  N  N   . ALA A 1 28  ? 34.440 26.752 27.997 1.00 32.11 ? 23  ALA A N   1 
ATOM   209  C  CA  . ALA A 1 28  ? 33.456 27.466 27.186 1.00 32.94 ? 23  ALA A CA  1 
ATOM   210  C  C   . ALA A 1 28  ? 33.855 28.925 26.999 1.00 33.82 ? 23  ALA A C   1 
ATOM   211  O  O   . ALA A 1 28  ? 33.712 29.470 25.901 1.00 33.11 ? 23  ALA A O   1 
ATOM   212  C  CB  . ALA A 1 28  ? 32.062 27.368 27.810 1.00 32.83 ? 23  ALA A CB  1 
ATOM   213  N  N   . ALA A 1 29  ? 34.383 29.564 28.049 1.00 32.69 ? 24  ALA A N   1 
ATOM   214  C  CA  . ALA A 1 29  ? 34.813 30.959 27.915 1.00 34.36 ? 24  ALA A CA  1 
ATOM   215  C  C   . ALA A 1 29  ? 35.944 31.088 26.904 1.00 32.96 ? 24  ALA A C   1 
ATOM   216  O  O   . ALA A 1 29  ? 35.967 32.029 26.106 1.00 34.09 ? 24  ALA A O   1 
ATOM   217  C  CB  . ALA A 1 29  ? 35.253 31.502 29.274 1.00 35.82 ? 24  ALA A CB  1 
ATOM   218  N  N   . PHE A 1 30  ? 36.886 30.139 26.916 1.00 33.49 ? 25  PHE A N   1 
ATOM   219  C  CA  . PHE A 1 30  ? 37.990 30.179 25.964 1.00 33.83 ? 25  PHE A CA  1 
ATOM   220  C  C   . PHE A 1 30  ? 37.484 30.010 24.537 1.00 33.26 ? 25  PHE A C   1 
ATOM   221  O  O   . PHE A 1 30  ? 37.924 30.719 23.617 1.00 34.35 ? 25  PHE A O   1 
ATOM   222  C  CB  . PHE A 1 30  ? 39.003 29.075 26.284 1.00 32.72 ? 25  PHE A CB  1 
ATOM   223  C  CG  . PHE A 1 30  ? 39.798 29.311 27.537 1.00 34.39 ? 25  PHE A CG  1 
ATOM   224  C  CD1 . PHE A 1 30  ? 40.324 30.566 27.817 1.00 32.78 ? 25  PHE A CD1 1 
ATOM   225  C  CD2 . PHE A 1 30  ? 40.055 28.264 28.410 1.00 34.93 ? 25  PHE A CD2 1 
ATOM   226  C  CE1 . PHE A 1 30  ? 41.065 30.783 28.960 1.00 37.06 ? 25  PHE A CE1 1 
ATOM   227  C  CE2 . PHE A 1 30  ? 40.805 28.481 29.553 1.00 34.18 ? 25  PHE A CE2 1 
ATOM   228  C  CZ  . PHE A 1 30  ? 41.309 29.734 29.828 1.00 36.18 ? 25  PHE A CZ  1 
ATOM   229  N  N   . MET A 1 31  ? 36.551 29.081 24.337 1.00 31.98 ? 26  MET A N   1 
ATOM   230  C  CA  . MET A 1 31  ? 36.028 28.840 22.990 1.00 32.62 ? 26  MET A CA  1 
ATOM   231  C  C   . MET A 1 31  ? 35.159 29.994 22.511 1.00 36.09 ? 26  MET A C   1 
ATOM   232  O  O   . MET A 1 31  ? 35.148 30.307 21.313 1.00 34.82 ? 26  MET A O   1 
ATOM   233  C  CB  . MET A 1 31  ? 35.237 27.532 22.955 1.00 31.75 ? 26  MET A CB  1 
ATOM   234  C  CG  . MET A 1 31  ? 36.102 26.270 22.952 1.00 34.99 ? 26  MET A CG  1 
ATOM   235  S  SD  . MET A 1 31  ? 37.541 26.354 21.878 1.00 34.08 ? 26  MET A SD  1 
ATOM   236  C  CE  . MET A 1 31  ? 36.737 26.621 20.289 1.00 35.99 ? 26  MET A CE  1 
ATOM   237  N  N   . LYS A 1 32  ? 34.396 30.615 23.416 1.00 33.95 ? 27  LYS A N   1 
ATOM   238  C  CA  . LYS A 1 32  ? 33.683 31.831 23.039 1.00 36.61 ? 27  LYS A CA  1 
ATOM   239  C  C   . LYS A 1 32  ? 34.662 32.895 22.559 1.00 37.79 ? 27  LYS A C   1 
ATOM   240  O  O   . LYS A 1 32  ? 34.437 33.538 21.524 1.00 37.61 ? 27  LYS A O   1 
ATOM   241  C  CB  . LYS A 1 32  ? 32.853 32.352 24.220 1.00 37.28 ? 27  LYS A CB  1 
ATOM   242  C  CG  . LYS A 1 32  ? 32.156 33.710 23.961 1.00 41.80 ? 27  LYS A CG  1 
ATOM   243  C  CD  . LYS A 1 32  ? 31.155 34.029 25.082 1.00 42.95 ? 27  LYS A CD  1 
ATOM   244  C  CE  . LYS A 1 32  ? 30.389 35.336 24.841 1.00 52.44 ? 27  LYS A CE  1 
ATOM   245  N  NZ  . LYS A 1 32  ? 31.279 36.517 24.892 1.00 53.01 ? 27  LYS A NZ  1 
ATOM   246  N  N   . GLY A 1 33  ? 35.771 33.073 23.284 1.00 35.19 ? 28  GLY A N   1 
ATOM   247  C  CA  . GLY A 1 33  ? 36.784 34.025 22.839 1.00 36.78 ? 28  GLY A CA  1 
ATOM   248  C  C   . GLY A 1 33  ? 37.354 33.656 21.484 1.00 38.64 ? 28  GLY A C   1 
ATOM   249  O  O   . GLY A 1 33  ? 37.587 34.520 20.642 1.00 37.80 ? 28  GLY A O   1 
ATOM   250  N  N   . ALA A 1 34  ? 37.564 32.362 21.243 1.00 36.17 ? 29  ALA A N   1 
ATOM   251  C  CA  . ALA A 1 34  ? 38.077 31.966 19.936 1.00 37.58 ? 29  ALA A CA  1 
ATOM   252  C  C   . ALA A 1 34  ? 37.065 32.265 18.847 1.00 37.16 ? 29  ALA A C   1 
ATOM   253  O  O   . ALA A 1 34  ? 37.432 32.754 17.772 1.00 37.56 ? 29  ALA A O   1 
ATOM   254  C  CB  . ALA A 1 34  ? 38.430 30.479 19.925 1.00 35.53 ? 29  ALA A CB  1 
ATOM   255  N  N   . VAL A 1 35  ? 35.788 31.959 19.096 1.00 36.13 ? 30  VAL A N   1 
ATOM   256  C  CA  . VAL A 1 35  ? 34.766 32.233 18.086 1.00 38.17 ? 30  VAL A CA  1 
ATOM   257  C  C   . VAL A 1 35  ? 34.749 33.716 17.754 1.00 39.59 ? 30  VAL A C   1 
ATOM   258  O  O   . VAL A 1 35  ? 34.612 34.108 16.588 1.00 40.25 ? 30  VAL A O   1 
ATOM   259  C  CB  . VAL A 1 35  ? 33.385 31.756 18.565 1.00 38.07 ? 30  VAL A CB  1 
ATOM   260  C  CG1 . VAL A 1 35  ? 32.292 32.288 17.648 1.00 39.73 ? 30  VAL A CG1 1 
ATOM   261  C  CG2 . VAL A 1 35  ? 33.333 30.207 18.635 1.00 37.01 ? 30  VAL A CG2 1 
ATOM   262  N  N   . GLU A 1 36  ? 34.917 34.563 18.772 1.00 38.72 ? 31  GLU A N   1 
ATOM   263  C  CA  . GLU A 1 36  ? 34.823 36.003 18.599 1.00 39.82 ? 31  GLU A CA  1 
ATOM   264  C  C   . GLU A 1 36  ? 35.980 36.580 17.801 1.00 41.31 ? 31  GLU A C   1 
ATOM   265  O  O   . GLU A 1 36  ? 35.907 37.741 17.397 1.00 42.28 ? 31  GLU A O   1 
ATOM   266  C  CB  . GLU A 1 36  ? 34.702 36.668 19.972 1.00 42.18 ? 31  GLU A CB  1 
ATOM   267  C  CG  . GLU A 1 36  ? 33.307 36.482 20.528 1.00 44.34 ? 31  GLU A CG  1 
ATOM   268  C  CD  . GLU A 1 36  ? 33.154 36.882 21.977 1.00 48.61 ? 31  GLU A CD  1 
ATOM   269  O  OE1 . GLU A 1 36  ? 34.174 37.008 22.696 1.00 48.46 ? 31  GLU A OE1 1 
ATOM   270  O  OE2 . GLU A 1 36  ? 31.992 37.054 22.397 1.00 51.74 ? 31  GLU A OE2 1 
ATOM   271  N  N   . LYS A 1 37  ? 37.026 35.799 17.529 1.00 41.26 ? 32  LYS A N   1 
ATOM   272  C  CA  . LYS A 1 37  ? 38.047 36.266 16.604 1.00 40.81 ? 32  LYS A CA  1 
ATOM   273  C  C   . LYS A 1 37  ? 37.516 36.380 15.180 1.00 43.50 ? 32  LYS A C   1 
ATOM   274  O  O   . LYS A 1 37  ? 38.145 37.034 14.347 1.00 42.14 ? 32  LYS A O   1 
ATOM   275  C  CB  . LYS A 1 37  ? 39.258 35.339 16.639 1.00 39.98 ? 32  LYS A CB  1 
ATOM   276  C  CG  . LYS A 1 37  ? 39.883 35.167 18.020 1.00 38.25 ? 32  LYS A CG  1 
ATOM   277  C  CD  . LYS A 1 37  ? 40.350 36.509 18.616 1.00 39.72 ? 32  LYS A CD  1 
ATOM   278  C  CE  . LYS A 1 37  ? 41.042 36.284 19.951 1.00 40.32 ? 32  LYS A CE  1 
ATOM   279  N  NZ  . LYS A 1 37  ? 41.122 37.529 20.807 1.00 42.45 ? 32  LYS A NZ  1 
ATOM   280  N  N   . GLY A 1 38  ? 36.382 35.759 14.883 1.00 42.68 ? 33  GLY A N   1 
ATOM   281  C  CA  . GLY A 1 38  ? 35.756 35.938 13.593 1.00 43.59 ? 33  GLY A CA  1 
ATOM   282  C  C   . GLY A 1 38  ? 36.254 35.020 12.503 1.00 44.14 ? 33  GLY A C   1 
ATOM   283  O  O   . GLY A 1 38  ? 35.887 35.223 11.342 1.00 47.03 ? 33  GLY A O   1 
ATOM   284  N  N   . GLU A 1 39  ? 37.072 34.020 12.825 1.00 44.14 ? 34  GLU A N   1 
ATOM   285  C  CA  . GLU A 1 39  ? 37.473 33.011 11.852 1.00 43.33 ? 34  GLU A CA  1 
ATOM   286  C  C   . GLU A 1 39  ? 36.642 31.752 12.020 1.00 42.24 ? 34  GLU A C   1 
ATOM   287  O  O   . GLU A 1 39  ? 36.068 31.501 13.081 1.00 40.95 ? 34  GLU A O   1 
ATOM   288  C  CB  . GLU A 1 39  ? 38.964 32.674 11.966 1.00 44.89 ? 34  GLU A CB  1 
ATOM   289  C  CG  . GLU A 1 39  ? 39.848 33.860 12.330 1.00 50.56 ? 34  GLU A CG  1 
ATOM   290  C  CD  . GLU A 1 39  ? 40.215 34.698 11.132 1.00 60.38 ? 34  GLU A CD  1 
ATOM   291  O  OE1 . GLU A 1 39  ? 41.366 35.191 11.080 1.00 67.25 ? 34  GLU A OE1 1 
ATOM   292  O  OE2 . GLU A 1 39  ? 39.379 34.831 10.211 1.00 61.82 ? 34  GLU A OE2 1 
ATOM   293  N  N   . GLU A 1 40  ? 36.578 30.961 10.949 1.00 43.23 ? 35  GLU A N   1 
ATOM   294  C  CA  . GLU A 1 40  ? 35.797 29.738 11.009 1.00 40.77 ? 35  GLU A CA  1 
ATOM   295  C  C   . GLU A 1 40  ? 36.424 28.787 12.013 1.00 42.40 ? 35  GLU A C   1 
ATOM   296  O  O   . GLU A 1 40  ? 37.607 28.882 12.342 1.00 42.78 ? 35  GLU A O   1 
ATOM   297  C  CB  . GLU A 1 40  ? 35.731 29.041 9.654  1.00 46.17 ? 35  GLU A CB  1 
ATOM   298  C  CG  . GLU A 1 40  ? 35.022 29.813 8.581  1.00 50.55 ? 35  GLU A CG  1 
ATOM   299  C  CD  . GLU A 1 40  ? 35.087 29.093 7.253  1.00 57.68 ? 35  GLU A CD  1 
ATOM   300  O  OE1 . GLU A 1 40  ? 36.175 28.568 6.910  1.00 58.97 ? 35  GLU A OE1 1 
ATOM   301  O  OE2 . GLU A 1 40  ? 34.062 29.095 6.537  1.00 63.37 ? 35  GLU A OE2 1 
ATOM   302  N  N   . LEU A 1 41  ? 35.617 27.857 12.501 1.00 40.01 ? 36  LEU A N   1 
ATOM   303  C  CA  . LEU A 1 41  ? 36.118 26.825 13.394 1.00 38.23 ? 36  LEU A CA  1 
ATOM   304  C  C   . LEU A 1 41  ? 36.256 25.514 12.641 1.00 39.79 ? 36  LEU A C   1 
ATOM   305  O  O   . LEU A 1 41  ? 35.371 25.137 11.867 1.00 40.47 ? 36  LEU A O   1 
ATOM   306  C  CB  . LEU A 1 41  ? 35.185 26.636 14.586 1.00 37.33 ? 36  LEU A CB  1 
ATOM   307  C  CG  . LEU A 1 41  ? 35.447 27.524 15.797 1.00 39.42 ? 36  LEU A CG  1 
ATOM   308  C  CD1 . LEU A 1 41  ? 35.214 28.979 15.468 1.00 42.05 ? 36  LEU A CD1 1 
ATOM   309  C  CD2 . LEU A 1 41  ? 34.551 27.044 16.938 1.00 39.24 ? 36  LEU A CD2 1 
ATOM   310  N  N   . SER A 1 42  ? 37.370 24.827 12.864 1.00 38.53 ? 37  SER A N   1 
ATOM   311  C  CA  . SER A 1 42  ? 37.557 23.509 12.280 1.00 39.79 ? 37  SER A CA  1 
ATOM   312  C  C   . SER A 1 42  ? 36.580 22.536 12.933 1.00 38.46 ? 37  SER A C   1 
ATOM   313  O  O   . SER A 1 42  ? 36.103 22.746 14.048 1.00 36.08 ? 37  SER A O   1 
ATOM   314  C  CB  . SER A 1 42  ? 38.994 23.020 12.458 1.00 41.69 ? 37  SER A CB  1 
ATOM   315  O  OG  . SER A 1 42  ? 39.291 22.753 13.822 1.00 38.14 ? 37  SER A OG  1 
ATOM   316  N  N   . CYS A 1 43  ? 36.524 21.218 12.389 1.00 37.86 ? 38  CYS A N   1 
ATOM   317  C  CA  . CYS A 1 43  ? 35.754 20.158 13.036 1.00 38.34 ? 38  CYS A CA  1 
ATOM   318  C  C   . CYS A 1 43  ? 36.249 19.902 14.464 1.00 37.82 ? 38  CYS A C   1 
ATOM   319  O  O   . CYS A 1 43  ? 35.456 19.853 15.414 1.00 35.15 ? 38  CYS A O   1 
ATOM   320  C  CB  . CYS A 1 43  ? 35.846 18.897 12.167 1.00 39.95 ? 38  CYS A CB  1 
ATOM   321  S  SG  . CYS A 1 43  ? 35.254 17.388 12.945 1.00 41.50 ? 38  CYS A SG  1 
ATOM   322  N  N   . GLU A 1 44  ? 37.656 19.836 14.708 1.00 36.59 ? 39  GLU A N   1 
ATOM   323  C  CA  . GLU A 1 44  ? 38.217 19.708 16.071 1.00 38.95 ? 39  GLU A CA  1 
ATOM   324  C  C   . GLU A 1 44  ? 37.734 20.814 16.989 1.00 37.44 ? 39  GLU A C   1 
ATOM   325  O  O   . GLU A 1 44  ? 37.421 20.594 18.166 1.00 35.73 ? 39  GLU A O   1 
ATOM   326  C  CB  . GLU A 1 44  ? 39.744 19.763 16.046 1.00 42.16 ? 39  GLU A CB  1 
ATOM   327  C  CG  . GLU A 1 44  ? 40.401 19.121 17.264 1.00 46.60 ? 39  GLU A CG  1 
ATOM   328  C  CD  . GLU A 1 44  ? 41.918 19.127 17.178 1.00 50.55 ? 39  GLU A CD  1 
ATOM   329  O  OE1 . GLU A 1 44  ? 42.456 19.517 16.117 1.00 54.88 ? 39  GLU A OE1 1 
ATOM   330  O  OE2 . GLU A 1 44  ? 42.571 18.789 18.188 1.00 55.68 ? 39  GLU A OE2 1 
ATOM   331  N  N   . GLU A 1 45  ? 37.715 22.026 16.442 1.00 37.83 ? 40  GLU A N   1 
ATOM   332  C  CA  . GLU A 1 45  ? 37.404 23.178 17.279 1.00 34.98 ? 40  GLU A CA  1 
ATOM   333  C  C   . GLU A 1 45  ? 35.914 23.253 17.576 1.00 35.18 ? 40  GLU A C   1 
ATOM   334  O  O   . GLU A 1 45  ? 35.518 23.619 18.687 1.00 34.64 ? 40  GLU A O   1 
ATOM   335  C  CB  . GLU A 1 45  ? 37.900 24.458 16.606 1.00 35.92 ? 40  GLU A CB  1 
ATOM   336  C  CG  . GLU A 1 45  ? 39.420 24.483 16.506 1.00 38.03 ? 40  GLU A CG  1 
ATOM   337  C  CD  . GLU A 1 45  ? 39.941 25.590 15.618 1.00 38.36 ? 40  GLU A CD  1 
ATOM   338  O  OE1 . GLU A 1 45  ? 39.186 26.044 14.725 1.00 38.72 ? 40  GLU A OE1 1 
ATOM   339  O  OE2 . GLU A 1 45  ? 41.113 25.989 15.801 1.00 37.99 ? 40  GLU A OE2 1 
ATOM   340  N  N   . ARG A 1 46  ? 35.074 22.897 16.606 1.00 34.25 ? 41  ARG A N   1 
ATOM   341  C  CA  . ARG A 1 46  ? 33.647 22.791 16.876 1.00 35.60 ? 41  ARG A CA  1 
ATOM   342  C  C   . ARG A 1 46  ? 33.375 21.784 17.974 1.00 34.85 ? 41  ARG A C   1 
ATOM   343  O  O   . ARG A 1 46  ? 32.473 21.980 18.799 1.00 33.20 ? 41  ARG A O   1 
ATOM   344  C  CB  . ARG A 1 46  ? 32.896 22.398 15.606 1.00 35.75 ? 41  ARG A CB  1 
ATOM   345  C  CG  . ARG A 1 46  ? 33.008 23.459 14.550 1.00 37.74 ? 41  ARG A CG  1 
ATOM   346  C  CD  . ARG A 1 46  ? 32.025 23.215 13.424 1.00 38.96 ? 41  ARG A CD  1 
ATOM   347  N  NE  . ARG A 1 46  ? 32.379 22.060 12.615 1.00 43.22 ? 41  ARG A NE  1 
ATOM   348  C  CZ  . ARG A 1 46  ? 33.074 22.085 11.481 1.00 43.95 ? 41  ARG A CZ  1 
ATOM   349  N  NH1 . ARG A 1 46  ? 33.618 23.196 11.020 1.00 44.52 ? 41  ARG A NH1 1 
ATOM   350  N  NH2 . ARG A 1 46  ? 33.215 20.959 10.789 1.00 42.77 ? 41  ARG A NH2 1 
ATOM   351  N  N   . ASN A 1 47  ? 34.149 20.699 18.009 1.00 33.43 ? 42  ASN A N   1 
ATOM   352  C  CA  . ASN A 1 47  ? 33.978 19.739 19.090 1.00 34.90 ? 42  ASN A CA  1 
ATOM   353  C  C   . ASN A 1 47  ? 34.291 20.371 20.434 1.00 35.66 ? 42  ASN A C   1 
ATOM   354  O  O   . ASN A 1 47  ? 33.585 20.128 21.416 1.00 34.38 ? 42  ASN A O   1 
ATOM   355  C  CB  . ASN A 1 47  ? 34.854 18.516 18.881 1.00 37.06 ? 42  ASN A CB  1 
ATOM   356  C  CG  . ASN A 1 47  ? 34.516 17.430 19.855 1.00 40.89 ? 42  ASN A CG  1 
ATOM   357  O  OD1 . ASN A 1 47  ? 33.373 16.979 19.906 1.00 39.06 ? 42  ASN A OD1 1 
ATOM   358  N  ND2 . ASN A 1 47  ? 35.479 17.043 20.674 1.00 43.59 ? 42  ASN A ND2 1 
ATOM   359  N  N   . LEU A 1 48  ? 35.346 21.186 20.500 1.00 33.37 ? 43  LEU A N   1 
ATOM   360  C  CA  . LEU A 1 48  ? 35.675 21.839 21.766 1.00 34.50 ? 43  LEU A CA  1 
ATOM   361  C  C   . LEU A 1 48  ? 34.538 22.752 22.208 1.00 33.81 ? 43  LEU A C   1 
ATOM   362  O  O   . LEU A 1 48  ? 34.124 22.735 23.376 1.00 32.90 ? 43  LEU A O   1 
ATOM   363  C  CB  . LEU A 1 48  ? 36.982 22.634 21.627 1.00 34.22 ? 43  LEU A CB  1 
ATOM   364  C  CG  . LEU A 1 48  ? 38.262 21.817 21.388 1.00 36.34 ? 43  LEU A CG  1 
ATOM   365  C  CD1 . LEU A 1 48  ? 39.435 22.736 21.041 1.00 36.88 ? 43  LEU A CD1 1 
ATOM   366  C  CD2 . LEU A 1 48  ? 38.596 20.964 22.617 1.00 36.11 ? 43  LEU A CD2 1 
ATOM   367  N  N   . LEU A 1 49  ? 34.021 23.556 21.274 1.00 32.96 ? 44  LEU A N   1 
ATOM   368  C  CA  . LEU A 1 49  ? 32.895 24.437 21.567 1.00 32.98 ? 44  LEU A CA  1 
ATOM   369  C  C   . LEU A 1 49  ? 31.707 23.632 22.064 1.00 32.95 ? 44  LEU A C   1 
ATOM   370  O  O   . LEU A 1 49  ? 31.089 23.960 23.085 1.00 33.39 ? 44  LEU A O   1 
ATOM   371  C  CB  . LEU A 1 49  ? 32.521 25.224 20.306 1.00 33.01 ? 44  LEU A CB  1 
ATOM   372  C  CG  . LEU A 1 49  ? 31.325 26.173 20.408 1.00 32.30 ? 44  LEU A CG  1 
ATOM   373  C  CD1 . LEU A 1 49  ? 31.705 27.386 21.269 1.00 33.81 ? 44  LEU A CD1 1 
ATOM   374  C  CD2 . LEU A 1 49  ? 30.869 26.604 19.022 1.00 33.96 ? 44  LEU A CD2 1 
ATOM   375  N  N   . SER A 1 50  ? 31.399 22.549 21.353 1.00 33.28 ? 45  SER A N   1 
ATOM   376  C  CA  . SER A 1 50  ? 30.251 21.718 21.687 1.00 32.84 ? 45  SER A CA  1 
ATOM   377  C  C   . SER A 1 50  ? 30.402 21.101 23.065 1.00 33.10 ? 45  SER A C   1 
ATOM   378  O  O   . SER A 1 50  ? 29.484 21.171 23.890 1.00 33.41 ? 45  SER A O   1 
ATOM   379  C  CB  . SER A 1 50  ? 30.100 20.620 20.633 1.00 33.84 ? 45  SER A CB  1 
ATOM   380  O  OG  . SER A 1 50  ? 28.972 19.827 20.915 1.00 33.61 ? 45  SER A OG  1 
ATOM   381  N  N   . VAL A 1 51  ? 31.552 20.469 23.321 1.00 31.65 ? 46  VAL A N   1 
ATOM   382  C  CA  . VAL A 1 51  ? 31.771 19.787 24.601 1.00 33.90 ? 46  VAL A CA  1 
ATOM   383  C  C   . VAL A 1 51  ? 31.667 20.760 25.772 1.00 34.13 ? 46  VAL A C   1 
ATOM   384  O  O   . VAL A 1 51  ? 31.103 20.431 26.832 1.00 34.27 ? 46  VAL A O   1 
ATOM   385  C  CB  . VAL A 1 51  ? 33.139 19.081 24.591 1.00 36.96 ? 46  VAL A CB  1 
ATOM   386  C  CG1 . VAL A 1 51  ? 33.534 18.654 25.999 1.00 36.16 ? 46  VAL A CG1 1 
ATOM   387  C  CG2 . VAL A 1 51  ? 33.124 17.884 23.632 1.00 36.76 ? 46  VAL A CG2 1 
ATOM   388  N  N   . ALA A 1 52  ? 32.267 21.943 25.632 1.00 31.62 ? 47  ALA A N   1 
ATOM   389  C  CA  . ALA A 1 52  ? 32.276 22.891 26.740 1.00 32.75 ? 47  ALA A CA  1 
ATOM   390  C  C   . ALA A 1 52  ? 30.862 23.320 27.099 1.00 32.61 ? 47  ALA A C   1 
ATOM   391  O  O   . ALA A 1 52  ? 30.426 23.179 28.247 1.00 33.80 ? 47  ALA A O   1 
ATOM   392  C  CB  . ALA A 1 52  ? 33.136 24.103 26.375 1.00 32.55 ? 47  ALA A CB  1 
ATOM   393  N  N   . TYR A 1 53  ? 30.122 23.844 26.121 1.00 32.64 ? 48  TYR A N   1 
ATOM   394  C  CA  . TYR A 1 53  ? 28.803 24.365 26.443 1.00 32.83 ? 48  TYR A CA  1 
ATOM   395  C  C   . TYR A 1 53  ? 27.825 23.267 26.807 1.00 33.75 ? 48  TYR A C   1 
ATOM   396  O  O   . TYR A 1 53  ? 26.937 23.504 27.631 1.00 34.12 ? 48  TYR A O   1 
ATOM   397  C  CB  . TYR A 1 53  ? 28.258 25.200 25.296 1.00 31.98 ? 48  TYR A CB  1 
ATOM   398  C  CG  . TYR A 1 53  ? 28.767 26.612 25.365 1.00 32.58 ? 48  TYR A CG  1 
ATOM   399  C  CD1 . TYR A 1 53  ? 28.399 27.439 26.421 1.00 33.06 ? 48  TYR A CD1 1 
ATOM   400  C  CD2 . TYR A 1 53  ? 29.657 27.102 24.414 1.00 32.33 ? 48  TYR A CD2 1 
ATOM   401  C  CE1 . TYR A 1 53  ? 28.870 28.736 26.503 1.00 34.21 ? 48  TYR A CE1 1 
ATOM   402  C  CE2 . TYR A 1 53  ? 30.139 28.418 24.498 1.00 34.92 ? 48  TYR A CE2 1 
ATOM   403  C  CZ  . TYR A 1 53  ? 29.742 29.211 25.552 1.00 35.48 ? 48  TYR A CZ  1 
ATOM   404  O  OH  . TYR A 1 53  ? 30.210 30.506 25.648 1.00 36.30 ? 48  TYR A OH  1 
ATOM   405  N  N   . LYS A 1 54  ? 27.964 22.065 26.220 1.00 33.85 ? 49  LYS A N   1 
ATOM   406  C  CA  . LYS A 1 54  ? 27.055 20.983 26.586 1.00 34.12 ? 49  LYS A CA  1 
ATOM   407  C  C   . LYS A 1 54  ? 27.259 20.563 28.033 1.00 34.75 ? 49  LYS A C   1 
ATOM   408  O  O   . LYS A 1 54  ? 26.288 20.242 28.724 1.00 35.31 ? 49  LYS A O   1 
ATOM   409  C  CB  . LYS A 1 54  ? 27.241 19.769 25.670 1.00 36.50 ? 49  LYS A CB  1 
ATOM   410  C  CG  . LYS A 1 54  ? 26.366 18.563 26.019 1.00 42.95 ? 49  LYS A CG  1 
ATOM   411  C  CD  . LYS A 1 54  ? 25.961 17.797 24.742 1.00 43.02 ? 49  LYS A CD  1 
ATOM   412  C  CE  . LYS A 1 54  ? 24.692 16.937 24.904 1.00 46.57 ? 49  LYS A CE  1 
ATOM   413  N  NZ  . LYS A 1 54  ? 23.761 17.322 26.010 1.00 45.58 ? 49  LYS A NZ  1 
ATOM   414  N  N   . ASN A 1 55  ? 28.517 20.508 28.485 1.00 33.60 ? 50  ASN A N   1 
ATOM   415  C  CA  . ASN A 1 55  ? 28.797 20.232 29.893 1.00 34.90 ? 50  ASN A CA  1 
ATOM   416  C  C   . ASN A 1 55  ? 28.202 21.287 30.808 1.00 34.89 ? 50  ASN A C   1 
ATOM   417  O  O   . ASN A 1 55  ? 27.630 20.958 31.858 1.00 33.55 ? 50  ASN A O   1 
ATOM   418  C  CB  . ASN A 1 55  ? 30.302 20.119 30.141 1.00 35.88 ? 50  ASN A CB  1 
ATOM   419  C  CG  . ASN A 1 55  ? 30.827 18.723 29.928 1.00 40.73 ? 50  ASN A CG  1 
ATOM   420  O  OD1 . ASN A 1 55  ? 30.700 17.881 30.822 1.00 41.69 ? 50  ASN A OD1 1 
ATOM   421  N  ND2 . ASN A 1 55  ? 31.428 18.462 28.781 1.00 39.45 ? 50  ASN A ND2 1 
ATOM   422  N  N   . VAL A 1 56  ? 28.374 22.561 30.458 1.00 31.69 ? 51  VAL A N   1 
ATOM   423  C  CA  . VAL A 1 56  ? 27.870 23.636 31.303 1.00 34.64 ? 51  VAL A CA  1 
ATOM   424  C  C   . VAL A 1 56  ? 26.354 23.570 31.392 1.00 36.12 ? 51  VAL A C   1 
ATOM   425  O  O   . VAL A 1 56  ? 25.778 23.515 32.488 1.00 35.37 ? 51  VAL A O   1 
ATOM   426  C  CB  . VAL A 1 56  ? 28.347 24.999 30.774 1.00 35.47 ? 51  VAL A CB  1 
ATOM   427  C  CG1 . VAL A 1 56  ? 27.692 26.128 31.562 1.00 36.02 ? 51  VAL A CG1 1 
ATOM   428  C  CG2 . VAL A 1 56  ? 29.867 25.070 30.860 1.00 34.43 ? 51  VAL A CG2 1 
ATOM   429  N  N   . VAL A 1 57  ? 25.683 23.554 30.239 1.00 34.12 ? 52  VAL A N   1 
ATOM   430  C  CA  . VAL A 1 57  ? 24.228 23.554 30.258 1.00 34.49 ? 52  VAL A CA  1 
ATOM   431  C  C   . VAL A 1 57  ? 23.705 22.210 30.764 1.00 35.77 ? 52  VAL A C   1 
ATOM   432  O  O   . VAL A 1 57  ? 22.629 22.149 31.368 1.00 36.03 ? 52  VAL A O   1 
ATOM   433  C  CB  . VAL A 1 57  ? 23.684 23.930 28.861 1.00 35.43 ? 52  VAL A CB  1 
ATOM   434  C  CG1 . VAL A 1 57  ? 23.725 22.748 27.913 1.00 36.49 ? 52  VAL A CG1 1 
ATOM   435  C  CG2 . VAL A 1 57  ? 22.276 24.469 28.959 1.00 39.15 ? 52  VAL A CG2 1 
ATOM   436  N  N   . GLY A 1 58  ? 24.462 21.125 30.556 1.00 33.49 ? 53  GLY A N   1 
ATOM   437  C  CA  . GLY A 1 58  ? 24.043 19.828 31.076 1.00 36.48 ? 53  GLY A CA  1 
ATOM   438  C  C   . GLY A 1 58  ? 23.932 19.817 32.587 1.00 37.67 ? 53  GLY A C   1 
ATOM   439  O  O   . GLY A 1 58  ? 22.981 19.261 33.149 1.00 37.50 ? 53  GLY A O   1 
ATOM   440  N  N   . GLY A 1 59  ? 24.900 20.436 33.268 1.00 35.73 ? 54  GLY A N   1 
ATOM   441  C  CA  . GLY A 1 59  ? 24.828 20.504 34.714 1.00 39.34 ? 54  GLY A CA  1 
ATOM   442  C  C   . GLY A 1 59  ? 23.678 21.382 35.163 1.00 36.98 ? 54  GLY A C   1 
ATOM   443  O  O   . GLY A 1 59  ? 23.002 21.076 36.146 1.00 37.34 ? 54  GLY A O   1 
ATOM   444  N  N   . GLN A 1 60  ? 23.414 22.457 34.419 1.00 34.67 ? 55  GLN A N   1 
ATOM   445  C  CA  . GLN A 1 60  ? 22.284 23.321 34.751 1.00 34.54 ? 55  GLN A CA  1 
ATOM   446  C  C   . GLN A 1 60  ? 20.960 22.609 34.527 1.00 37.57 ? 55  GLN A C   1 
ATOM   447  O  O   . GLN A 1 60  ? 20.048 22.737 35.348 1.00 34.70 ? 55  GLN A O   1 
ATOM   448  C  CB  . GLN A 1 60  ? 22.328 24.613 33.938 1.00 36.02 ? 55  GLN A CB  1 
ATOM   449  C  CG  . GLN A 1 60  ? 23.508 25.506 34.264 1.00 36.12 ? 55  GLN A CG  1 
ATOM   450  C  CD  . GLN A 1 60  ? 23.641 26.626 33.255 1.00 37.45 ? 55  GLN A CD  1 
ATOM   451  O  OE1 . GLN A 1 60  ? 23.381 26.433 32.062 1.00 37.64 ? 55  GLN A OE1 1 
ATOM   452  N  NE2 . GLN A 1 60  ? 24.034 27.801 33.721 1.00 39.27 ? 55  GLN A NE2 1 
ATOM   453  N  N   . ARG A 1 61  ? 20.824 21.858 33.416 1.00 33.40 ? 56  ARG A N   1 
ATOM   454  C  CA  . ARG A 1 61  ? 19.589 21.113 33.200 1.00 35.17 ? 56  ARG A CA  1 
ATOM   455  C  C   . ARG A 1 61  ? 19.383 20.074 34.291 1.00 38.05 ? 56  ARG A C   1 
ATOM   456  O  O   . ARG A 1 61  ? 18.267 19.900 34.798 1.00 35.50 ? 56  ARG A O   1 
ATOM   457  C  CB  . ARG A 1 61  ? 19.606 20.425 31.824 1.00 38.50 ? 56  ARG A CB  1 
ATOM   458  C  CG  . ARG A 1 61  ? 19.641 21.389 30.653 1.00 36.60 ? 56  ARG A CG  1 
ATOM   459  C  CD  . ARG A 1 61  ? 20.047 20.655 29.360 1.00 39.52 ? 56  ARG A CD  1 
ATOM   460  N  NE  . ARG A 1 61  ? 19.030 19.714 28.901 1.00 39.49 ? 56  ARG A NE  1 
ATOM   461  C  CZ  . ARG A 1 61  ? 19.280 18.647 28.145 1.00 42.81 ? 56  ARG A CZ  1 
ATOM   462  N  NH1 . ARG A 1 61  ? 20.513 18.313 27.800 1.00 40.33 ? 56  ARG A NH1 1 
ATOM   463  N  NH2 . ARG A 1 61  ? 18.266 17.901 27.720 1.00 39.95 ? 56  ARG A NH2 1 
ATOM   464  N  N   . ALA A 1 62  ? 20.447 19.354 34.650 1.00 35.82 ? 57  ALA A N   1 
ATOM   465  C  CA  . ALA A 1 62  ? 20.330 18.350 35.700 1.00 37.73 ? 57  ALA A CA  1 
ATOM   466  C  C   . ALA A 1 62  ? 19.888 18.986 37.012 1.00 37.37 ? 57  ALA A C   1 
ATOM   467  O  O   . ALA A 1 62  ? 19.000 18.462 37.692 1.00 36.93 ? 57  ALA A O   1 
ATOM   468  C  CB  . ALA A 1 62  ? 21.657 17.612 35.872 1.00 38.63 ? 57  ALA A CB  1 
ATOM   469  N  N   . ALA A 1 63  ? 20.472 20.134 37.360 1.00 34.84 ? 58  ALA A N   1 
ATOM   470  C  CA  . ALA A 1 63  ? 20.072 20.835 38.579 1.00 37.32 ? 58  ALA A CA  1 
ATOM   471  C  C   . ALA A 1 63  ? 18.629 21.308 38.486 1.00 37.06 ? 58  ALA A C   1 
ATOM   472  O  O   . ALA A 1 63  ? 17.841 21.135 39.424 1.00 33.92 ? 58  ALA A O   1 
ATOM   473  C  CB  . ALA A 1 63  ? 21.009 22.020 38.840 1.00 36.33 ? 58  ALA A CB  1 
ATOM   474  N  N   . TRP A 1 64  ? 18.268 21.916 37.349 1.00 36.76 ? 59  TRP A N   1 
ATOM   475  C  CA  . TRP A 1 64  ? 16.905 22.397 37.163 1.00 36.05 ? 59  TRP A CA  1 
ATOM   476  C  C   . TRP A 1 64  ? 15.902 21.267 37.327 1.00 38.83 ? 59  TRP A C   1 
ATOM   477  O  O   . TRP A 1 64  ? 14.838 21.458 37.925 1.00 38.34 ? 59  TRP A O   1 
ATOM   478  C  CB  . TRP A 1 64  ? 16.766 23.049 35.783 1.00 35.74 ? 59  TRP A CB  1 
ATOM   479  C  CG  . TRP A 1 64  ? 15.452 23.700 35.556 1.00 38.90 ? 59  TRP A CG  1 
ATOM   480  C  CD1 . TRP A 1 64  ? 15.144 25.020 35.757 1.00 40.75 ? 59  TRP A CD1 1 
ATOM   481  C  CD2 . TRP A 1 64  ? 14.257 23.078 35.076 1.00 41.60 ? 59  TRP A CD2 1 
ATOM   482  N  NE1 . TRP A 1 64  ? 13.826 25.254 35.433 1.00 40.22 ? 59  TRP A NE1 1 
ATOM   483  C  CE2 . TRP A 1 64  ? 13.258 24.079 35.016 1.00 41.50 ? 59  TRP A CE2 1 
ATOM   484  C  CE3 . TRP A 1 64  ? 13.930 21.773 34.689 1.00 41.36 ? 59  TRP A CE3 1 
ATOM   485  C  CZ2 . TRP A 1 64  ? 11.961 23.814 34.594 1.00 43.47 ? 59  TRP A CZ2 1 
ATOM   486  C  CZ3 . TRP A 1 64  ? 12.640 21.511 34.267 1.00 43.52 ? 59  TRP A CZ3 1 
ATOM   487  C  CH2 . TRP A 1 64  ? 11.670 22.530 34.218 1.00 44.48 ? 59  TRP A CH2 1 
ATOM   488  N  N   . ARG A 1 65  ? 16.221 20.080 36.788 1.00 37.98 ? 60  ARG A N   1 
ATOM   489  C  CA  . ARG A 1 65  ? 15.309 18.946 36.896 1.00 40.69 ? 60  ARG A CA  1 
ATOM   490  C  C   . ARG A 1 65  ? 15.147 18.494 38.340 1.00 38.57 ? 60  ARG A C   1 
ATOM   491  O  O   . ARG A 1 65  ? 14.037 18.154 38.762 1.00 40.48 ? 60  ARG A O   1 
ATOM   492  C  CB  . ARG A 1 65  ? 15.801 17.788 36.030 1.00 40.45 ? 60  ARG A CB  1 
ATOM   493  C  CG  . ARG A 1 65  ? 15.545 18.010 34.560 1.00 43.77 ? 60  ARG A CG  1 
ATOM   494  C  CD  . ARG A 1 65  ? 16.114 16.858 33.757 1.00 50.32 ? 60  ARG A CD  1 
ATOM   495  N  NE  . ARG A 1 65  ? 16.082 17.112 32.322 1.00 55.26 ? 60  ARG A NE  1 
ATOM   496  C  CZ  . ARG A 1 65  ? 17.040 16.754 31.476 1.00 56.45 ? 60  ARG A CZ  1 
ATOM   497  N  NH1 . ARG A 1 65  ? 18.167 16.204 31.903 1.00 56.09 ? 60  ARG A NH1 1 
ATOM   498  N  NH2 . ARG A 1 65  ? 16.855 16.936 30.168 1.00 54.67 ? 60  ARG A NH2 1 
ATOM   499  N  N   . VAL A 1 66  ? 16.238 18.471 39.108 1.00 37.37 ? 61  VAL A N   1 
ATOM   500  C  CA  . VAL A 1 66  ? 16.129 18.140 40.534 1.00 38.94 ? 61  VAL A CA  1 
ATOM   501  C  C   . VAL A 1 66  ? 15.210 19.128 41.234 1.00 41.70 ? 61  VAL A C   1 
ATOM   502  O  O   . VAL A 1 66  ? 14.286 18.742 41.965 1.00 40.72 ? 61  VAL A O   1 
ATOM   503  C  CB  . VAL A 1 66  ? 17.521 18.111 41.192 1.00 39.35 ? 61  VAL A CB  1 
ATOM   504  C  CG1 . VAL A 1 66  ? 17.403 18.076 42.714 1.00 40.18 ? 61  VAL A CG1 1 
ATOM   505  C  CG2 . VAL A 1 66  ? 18.322 16.924 40.678 1.00 41.31 ? 61  VAL A CG2 1 
ATOM   506  N  N   . LEU A 1 67  ? 15.467 20.425 41.044 1.00 39.23 ? 62  LEU A N   1 
ATOM   507  C  CA  . LEU A 1 67  ? 14.702 21.434 41.763 1.00 38.76 ? 62  LEU A CA  1 
ATOM   508  C  C   . LEU A 1 67  ? 13.251 21.449 41.311 1.00 42.69 ? 62  LEU A C   1 
ATOM   509  O  O   . LEU A 1 67  ? 12.345 21.640 42.131 1.00 42.92 ? 62  LEU A O   1 
ATOM   510  C  CB  . LEU A 1 67  ? 15.346 22.810 41.577 1.00 35.91 ? 62  LEU A CB  1 
ATOM   511  C  CG  . LEU A 1 67  ? 16.792 22.893 42.049 1.00 36.88 ? 62  LEU A CG  1 
ATOM   512  C  CD1 . LEU A 1 67  ? 17.421 24.212 41.653 1.00 36.44 ? 62  LEU A CD1 1 
ATOM   513  C  CD2 . LEU A 1 67  ? 16.840 22.749 43.561 1.00 35.50 ? 62  LEU A CD2 1 
ATOM   514  N  N   . SER A 1 68  ? 13.008 21.257 40.009 1.00 41.11 ? 63  SER A N   1 
ATOM   515  C  CA  . SER A 1 68  ? 11.635 21.252 39.524 1.00 42.62 ? 63  SER A CA  1 
ATOM   516  C  C   . SER A 1 68  ? 10.853 20.080 40.106 1.00 47.90 ? 63  SER A C   1 
ATOM   517  O  O   . SER A 1 68  ? 9.675  20.220 40.453 1.00 51.67 ? 63  SER A O   1 
ATOM   518  C  CB  . SER A 1 68  ? 11.620 21.209 37.995 1.00 44.31 ? 63  SER A CB  1 
ATOM   519  O  OG  . SER A 1 68  ? 10.297 21.087 37.520 1.00 50.62 ? 63  SER A OG  1 
ATOM   520  N  N   . SER A 1 69  ? 11.493 18.918 40.228 1.00 44.76 ? 64  SER A N   1 
ATOM   521  C  CA  . SER A 1 69  ? 10.813 17.774 40.827 1.00 48.21 ? 64  SER A CA  1 
ATOM   522  C  C   . SER A 1 69  ? 10.462 18.041 42.288 1.00 51.77 ? 64  SER A C   1 
ATOM   523  O  O   . SER A 1 69  ? 9.362  17.700 42.740 1.00 53.89 ? 64  SER A O   1 
ATOM   524  C  CB  . SER A 1 69  ? 11.678 16.523 40.700 1.00 48.88 ? 64  SER A CB  1 
ATOM   525  O  OG  . SER A 1 69  ? 11.058 15.431 41.345 1.00 53.23 ? 64  SER A OG  1 
ATOM   526  N  N   . ILE A 1 70  ? 11.387 18.648 43.039 1.00 48.05 ? 65  ILE A N   1 
ATOM   527  C  CA  . ILE A 1 70  ? 11.107 19.020 44.424 1.00 51.48 ? 65  ILE A CA  1 
ATOM   528  C  C   . ILE A 1 70  ? 9.968  20.023 44.475 1.00 55.87 ? 65  ILE A C   1 
ATOM   529  O  O   . ILE A 1 70  ? 9.076  19.937 45.329 1.00 57.53 ? 65  ILE A O   1 
ATOM   530  C  CB  . ILE A 1 70  ? 12.377 19.579 45.090 1.00 45.49 ? 65  ILE A CB  1 
ATOM   531  C  CG1 . ILE A 1 70  ? 13.452 18.494 45.163 1.00 46.07 ? 65  ILE A CG1 1 
ATOM   532  C  CG2 . ILE A 1 70  ? 12.060 20.184 46.486 1.00 46.65 ? 65  ILE A CG2 1 
ATOM   533  C  CD1 . ILE A 1 70  ? 14.807 18.996 45.654 1.00 45.86 ? 65  ILE A CD1 1 
ATOM   534  N  N   . GLU A 1 71  ? 9.983  20.987 43.552 1.00 51.66 ? 66  GLU A N   1 
ATOM   535  C  CA  . GLU A 1 71  ? 8.930  21.990 43.488 1.00 54.19 ? 66  GLU A CA  1 
ATOM   536  C  C   . GLU A 1 71  ? 7.575  21.358 43.204 1.00 61.65 ? 66  GLU A C   1 
ATOM   537  O  O   . GLU A 1 71  ? 6.567  21.736 43.810 1.00 65.41 ? 66  GLU A O   1 
ATOM   538  C  CB  . GLU A 1 71  ? 9.278  23.023 42.421 1.00 51.99 ? 66  GLU A CB  1 
ATOM   539  C  CG  . GLU A 1 71  ? 8.400  24.250 42.435 1.00 52.45 ? 66  GLU A CG  1 
ATOM   540  C  CD  . GLU A 1 71  ? 8.777  25.219 41.342 1.00 50.15 ? 66  GLU A CD  1 
ATOM   541  O  OE1 . GLU A 1 71  ? 9.691  24.898 40.560 1.00 46.96 ? 66  GLU A OE1 1 
ATOM   542  O  OE2 . GLU A 1 71  ? 8.166  26.299 41.264 1.00 50.29 ? 66  GLU A OE2 1 
ATOM   543  N  N   . GLN A 1 72  ? 7.529  20.385 42.293 1.00 59.53 ? 67  GLN A N   1 
ATOM   544  C  CA  . GLN A 1 72  ? 6.247  19.772 41.967 1.00 64.99 ? 67  GLN A CA  1 
ATOM   545  C  C   . GLN A 1 72  ? 5.753  18.867 43.088 1.00 67.52 ? 67  GLN A C   1 
ATOM   546  O  O   . GLN A 1 72  ? 4.542  18.782 43.322 1.00 72.31 ? 67  GLN A O   1 
ATOM   547  C  CB  . GLN A 1 72  ? 6.352  18.996 40.653 1.00 65.21 ? 67  GLN A CB  1 
ATOM   548  C  CG  . GLN A 1 72  ? 6.469  19.838 39.350 1.00 69.81 ? 67  GLN A CG  1 
ATOM   549  C  CD  . GLN A 1 72  ? 5.720  21.189 39.315 1.00 75.24 ? 67  GLN A CD  1 
ATOM   550  O  OE1 . GLN A 1 72  ? 4.874  21.505 40.161 1.00 78.12 ? 67  GLN A OE1 1 
ATOM   551  N  NE2 . GLN A 1 72  ? 6.064  22.003 38.321 1.00 75.15 ? 67  GLN A NE2 1 
ATOM   552  N  N   . LYS A 1 73  ? 6.663  18.189 43.791 1.00 65.63 ? 68  LYS A N   1 
ATOM   553  C  CA  . LYS A 1 73  ? 6.250  17.372 44.929 1.00 70.98 ? 68  LYS A CA  1 
ATOM   554  C  C   . LYS A 1 73  ? 5.673  18.233 46.046 1.00 72.24 ? 68  LYS A C   1 
ATOM   555  O  O   . LYS A 1 73  ? 4.711  17.833 46.712 1.00 74.96 ? 68  LYS A O   1 
ATOM   556  C  CB  . LYS A 1 73  ? 7.428  16.548 45.448 1.00 70.13 ? 68  LYS A CB  1 
ATOM   557  C  CG  . LYS A 1 73  ? 7.022  15.288 46.196 1.00 73.93 ? 68  LYS A CG  1 
ATOM   558  C  CD  . LYS A 1 73  ? 7.377  14.041 45.401 1.00 76.11 ? 68  LYS A CD  1 
ATOM   559  C  CE  . LYS A 1 73  ? 6.585  12.831 45.880 1.00 77.70 ? 68  LYS A CE  1 
ATOM   560  N  NZ  . LYS A 1 73  ? 5.331  12.650 45.094 1.00 77.48 ? 68  LYS A NZ  1 
ATOM   561  N  N   . SER A 1 74  ? 6.247  19.414 46.269 1.00 70.72 ? 69  SER A N   1 
ATOM   562  C  CA  . SER A 1 74  ? 5.758  20.322 47.298 1.00 72.73 ? 69  SER A CA  1 
ATOM   563  C  C   . SER A 1 74  ? 4.483  21.051 46.892 1.00 74.51 ? 69  SER A C   1 
ATOM   564  O  O   . SER A 1 74  ? 3.933  21.802 47.706 1.00 76.55 ? 69  SER A O   1 
ATOM   565  C  CB  . SER A 1 74  ? 6.841  21.340 47.659 1.00 70.98 ? 69  SER A CB  1 
ATOM   566  O  OG  . SER A 1 74  ? 6.908  22.369 46.686 1.00 70.91 ? 69  SER A OG  1 
ATOM   567  N  N   . ASN A 1 75  ? 4.008  20.857 45.663 1.00 75.70 ? 70  ASN A N   1 
ATOM   568  C  CA  . ASN A 1 75  ? 2.732  21.397 45.215 1.00 78.10 ? 70  ASN A CA  1 
ATOM   569  C  C   . ASN A 1 75  ? 1.646  20.335 45.119 1.00 80.20 ? 70  ASN A C   1 
ATOM   570  O  O   . ASN A 1 75  ? 0.520  20.656 44.725 1.00 82.30 ? 70  ASN A O   1 
ATOM   571  C  CB  . ASN A 1 75  ? 2.891  22.088 43.853 1.00 76.78 ? 70  ASN A CB  1 
ATOM   572  C  CG  . ASN A 1 75  ? 3.619  23.415 43.948 1.00 76.87 ? 70  ASN A CG  1 
ATOM   573  O  OD1 . ASN A 1 75  ? 3.719  24.012 45.023 1.00 76.66 ? 70  ASN A OD1 1 
ATOM   574  N  ND2 . ASN A 1 75  ? 4.136  23.884 42.818 1.00 74.39 ? 70  ASN A ND2 1 
ATOM   575  N  N   . GLU A 1 76  ? 1.952  19.085 45.459 1.00 80.61 ? 71  GLU A N   1 
ATOM   576  C  CA  . GLU A 1 76  ? 0.990  17.993 45.332 1.00 83.04 ? 71  GLU A CA  1 
ATOM   577  C  C   . GLU A 1 76  ? 0.356  17.650 46.680 1.00 86.60 ? 71  GLU A C   1 
ATOM   578  O  O   . GLU A 1 76  ? -0.862 17.482 46.783 1.00 86.57 ? 71  GLU A O   1 
ATOM   579  C  CB  . GLU A 1 76  ? 1.665  16.754 44.735 1.00 80.91 ? 71  GLU A CB  1 
ATOM   580  N  N   . LYS A 1 82  ? 6.249  24.810 52.612 1.00 78.63 ? 77  LYS A N   1 
ATOM   581  C  CA  . LYS A 1 82  ? 5.366  25.571 51.736 1.00 76.06 ? 77  LYS A CA  1 
ATOM   582  C  C   . LYS A 1 82  ? 5.821  27.024 51.600 1.00 68.59 ? 77  LYS A C   1 
ATOM   583  O  O   . LYS A 1 82  ? 4.996  27.916 51.421 1.00 69.16 ? 77  LYS A O   1 
ATOM   584  C  CB  . LYS A 1 82  ? 3.925  25.522 52.255 1.00 80.69 ? 77  LYS A CB  1 
ATOM   585  N  N   . GLY A 1 83  ? 7.130  27.257 51.687 1.00 62.14 ? 78  GLY A N   1 
ATOM   586  C  CA  . GLY A 1 83  ? 7.686  28.579 51.501 1.00 56.05 ? 78  GLY A CA  1 
ATOM   587  C  C   . GLY A 1 83  ? 8.065  28.835 50.053 1.00 50.01 ? 78  GLY A C   1 
ATOM   588  O  O   . GLY A 1 83  ? 7.894  27.978 49.184 1.00 49.12 ? 78  GLY A O   1 
ATOM   589  N  N   . PRO A 1 84  ? 8.575  30.033 49.759 1.00 48.48 ? 79  PRO A N   1 
ATOM   590  C  CA  . PRO A 1 84  ? 8.955  30.352 48.381 1.00 44.99 ? 79  PRO A CA  1 
ATOM   591  C  C   . PRO A 1 84  ? 10.336 29.853 47.986 1.00 44.63 ? 79  PRO A C   1 
ATOM   592  O  O   . PRO A 1 84  ? 10.724 30.047 46.833 1.00 40.11 ? 79  PRO A O   1 
ATOM   593  C  CB  . PRO A 1 84  ? 8.906  31.888 48.368 1.00 46.46 ? 79  PRO A CB  1 
ATOM   594  C  CG  . PRO A 1 84  ? 9.341  32.249 49.749 1.00 48.53 ? 79  PRO A CG  1 
ATOM   595  C  CD  . PRO A 1 84  ? 8.714  31.200 50.649 1.00 48.96 ? 79  PRO A CD  1 
ATOM   596  N  N   . GLU A 1 85  ? 11.085 29.217 48.898 1.00 42.05 ? 80  GLU A N   1 
ATOM   597  C  CA  . GLU A 1 85  ? 12.511 28.987 48.662 1.00 39.42 ? 80  GLU A CA  1 
ATOM   598  C  C   . GLU A 1 85  ? 12.767 28.052 47.476 1.00 40.33 ? 80  GLU A C   1 
ATOM   599  O  O   . GLU A 1 85  ? 13.663 28.313 46.663 1.00 37.92 ? 80  GLU A O   1 
ATOM   600  C  CB  . GLU A 1 85  ? 13.172 28.453 49.938 1.00 39.95 ? 80  GLU A CB  1 
ATOM   601  C  CG  . GLU A 1 85  ? 13.291 29.497 51.074 1.00 42.75 ? 80  GLU A CG  1 
ATOM   602  C  CD  . GLU A 1 85  ? 12.041 29.603 51.931 1.00 44.90 ? 80  GLU A CD  1 
ATOM   603  O  OE1 . GLU A 1 85  ? 11.040 28.921 51.633 1.00 44.61 ? 80  GLU A OE1 1 
ATOM   604  O  OE2 . GLU A 1 85  ? 12.059 30.365 52.918 1.00 43.63 ? 80  GLU A OE2 1 
ATOM   605  N  N   . VAL A 1 86  ? 12.010 26.953 47.353 1.00 39.86 ? 81  VAL A N   1 
ATOM   606  C  CA  . VAL A 1 86  ? 12.258 26.029 46.241 1.00 39.16 ? 81  VAL A CA  1 
ATOM   607  C  C   . VAL A 1 86  ? 12.021 26.727 44.905 1.00 39.86 ? 81  VAL A C   1 
ATOM   608  O  O   . VAL A 1 86  ? 12.827 26.611 43.973 1.00 37.29 ? 81  VAL A O   1 
ATOM   609  C  CB  . VAL A 1 86  ? 11.398 24.757 46.362 1.00 40.60 ? 81  VAL A CB  1 
ATOM   610  C  CG1 . VAL A 1 86  ? 11.599 23.880 45.121 1.00 44.20 ? 81  VAL A CG1 1 
ATOM   611  C  CG2 . VAL A 1 86  ? 11.794 23.972 47.581 1.00 44.43 ? 81  VAL A CG2 1 
ATOM   612  N  N   . ARG A 1 87  ? 10.913 27.469 44.792 1.00 40.13 ? 82  ARG A N   1 
ATOM   613  C  CA  . ARG A 1 87  ? 10.633 28.165 43.538 1.00 41.00 ? 82  ARG A CA  1 
ATOM   614  C  C   . ARG A 1 87  ? 11.689 29.228 43.259 1.00 40.30 ? 82  ARG A C   1 
ATOM   615  O  O   . ARG A 1 87  ? 12.188 29.337 42.135 1.00 38.37 ? 82  ARG A O   1 
ATOM   616  C  CB  . ARG A 1 87  ? 9.241  28.804 43.575 1.00 42.99 ? 82  ARG A CB  1 
ATOM   617  C  CG  . ARG A 1 87  ? 8.972  29.710 42.369 1.00 44.53 ? 82  ARG A CG  1 
ATOM   618  C  CD  . ARG A 1 87  ? 7.656  30.476 42.488 1.00 48.74 ? 82  ARG A CD  1 
ATOM   619  N  NE  . ARG A 1 87  ? 7.555  31.244 43.725 1.00 47.59 ? 82  ARG A NE  1 
ATOM   620  C  CZ  . ARG A 1 87  ? 8.182  32.392 43.961 1.00 48.72 ? 82  ARG A CZ  1 
ATOM   621  N  NH1 . ARG A 1 87  ? 8.988  32.943 43.067 1.00 46.74 ? 82  ARG A NH1 1 
ATOM   622  N  NH2 . ARG A 1 87  ? 7.990  33.007 45.124 1.00 49.18 ? 82  ARG A NH2 1 
ATOM   623  N  N   . GLU A 1 88  ? 12.053 30.014 44.277 1.00 38.98 ? 83  GLU A N   1 
ATOM   624  C  CA  . GLU A 1 88  ? 13.067 31.048 44.076 1.00 39.63 ? 83  GLU A CA  1 
ATOM   625  C  C   . GLU A 1 88  ? 14.372 30.453 43.585 1.00 38.16 ? 83  GLU A C   1 
ATOM   626  O  O   . GLU A 1 88  ? 15.002 30.991 42.671 1.00 38.44 ? 83  GLU A O   1 
ATOM   627  C  CB  . GLU A 1 88  ? 13.313 31.822 45.367 1.00 40.12 ? 83  GLU A CB  1 
ATOM   628  C  CG  . GLU A 1 88  ? 12.151 32.674 45.825 1.00 40.33 ? 83  GLU A CG  1 
ATOM   629  C  CD  . GLU A 1 88  ? 12.383 33.245 47.214 1.00 43.20 ? 83  GLU A CD  1 
ATOM   630  O  OE1 . GLU A 1 88  ? 13.270 32.725 47.933 1.00 41.03 ? 83  GLU A OE1 1 
ATOM   631  O  OE2 . GLU A 1 88  ? 11.690 34.219 47.586 1.00 42.40 ? 83  GLU A OE2 1 
ATOM   632  N  N   . TYR A 1 89  ? 14.798 29.337 44.176 1.00 36.30 ? 84  TYR A N   1 
ATOM   633  C  CA  . TYR A 1 89  ? 16.070 28.762 43.768 1.00 37.25 ? 84  TYR A CA  1 
ATOM   634  C  C   . TYR A 1 89  ? 15.953 28.084 42.399 1.00 36.30 ? 84  TYR A C   1 
ATOM   635  O  O   . TYR A 1 89  ? 16.877 28.166 41.582 1.00 36.34 ? 84  TYR A O   1 
ATOM   636  C  CB  . TYR A 1 89  ? 16.573 27.800 44.849 1.00 38.83 ? 84  TYR A CB  1 
ATOM   637  C  CG  . TYR A 1 89  ? 17.944 27.271 44.552 1.00 37.08 ? 84  TYR A CG  1 
ATOM   638  C  CD1 . TYR A 1 89  ? 18.938 28.108 44.073 1.00 37.81 ? 84  TYR A CD1 1 
ATOM   639  C  CD2 . TYR A 1 89  ? 18.240 25.925 44.727 1.00 39.29 ? 84  TYR A CD2 1 
ATOM   640  C  CE1 . TYR A 1 89  ? 20.189 27.624 43.769 1.00 38.91 ? 84  TYR A CE1 1 
ATOM   641  C  CE2 . TYR A 1 89  ? 19.487 25.435 44.434 1.00 38.43 ? 84  TYR A CE2 1 
ATOM   642  C  CZ  . TYR A 1 89  ? 20.457 26.288 43.965 1.00 37.15 ? 84  TYR A CZ  1 
ATOM   643  O  OH  . TYR A 1 89  ? 21.692 25.775 43.670 1.00 39.63 ? 84  TYR A OH  1 
ATOM   644  N  N   . ARG A 1 90  ? 14.815 27.446 42.110 1.00 36.17 ? 85  ARG A N   1 
ATOM   645  C  CA  . ARG A 1 90  ? 14.610 26.911 40.762 1.00 38.07 ? 85  ARG A CA  1 
ATOM   646  C  C   . ARG A 1 90  ? 14.651 28.031 39.730 1.00 38.25 ? 85  ARG A C   1 
ATOM   647  O  O   . ARG A 1 90  ? 15.262 27.880 38.665 1.00 38.25 ? 85  ARG A O   1 
ATOM   648  C  CB  . ARG A 1 90  ? 13.284 26.149 40.676 1.00 38.46 ? 85  ARG A CB  1 
ATOM   649  C  CG  . ARG A 1 90  ? 13.056 25.379 39.356 1.00 40.89 ? 85  ARG A CG  1 
ATOM   650  C  CD  . ARG A 1 90  ? 12.255 26.194 38.347 1.00 42.76 ? 85  ARG A CD  1 
ATOM   651  N  NE  . ARG A 1 90  ? 10.944 26.557 38.873 1.00 42.55 ? 85  ARG A NE  1 
ATOM   652  C  CZ  . ARG A 1 90  ? 10.271 27.648 38.533 1.00 44.99 ? 85  ARG A CZ  1 
ATOM   653  N  NH1 . ARG A 1 90  ? 10.707 28.466 37.584 1.00 44.63 ? 85  ARG A NH1 1 
ATOM   654  N  NH2 . ARG A 1 90  ? 9.133  27.930 39.164 1.00 45.43 ? 85  ARG A NH2 1 
ATOM   655  N  N   . GLU A 1 91  ? 14.027 29.174 40.042 1.00 36.86 ? 86  GLU A N   1 
ATOM   656  C  CA  . GLU A 1 91  ? 14.053 30.320 39.133 1.00 39.68 ? 86  GLU A CA  1 
ATOM   657  C  C   . GLU A 1 91  ? 15.475 30.839 38.943 1.00 38.13 ? 86  GLU A C   1 
ATOM   658  O  O   . GLU A 1 91  ? 15.850 31.262 37.845 1.00 38.51 ? 86  GLU A O   1 
ATOM   659  C  CB  . GLU A 1 91  ? 13.144 31.442 39.654 1.00 39.83 ? 86  GLU A CB  1 
ATOM   660  C  CG  . GLU A 1 91  ? 11.669 31.331 39.258 1.00 44.55 ? 86  GLU A CG  1 
ATOM   661  C  CD  . GLU A 1 91  ? 10.739 32.177 40.144 1.00 48.09 ? 86  GLU A CD  1 
ATOM   662  O  OE1 . GLU A 1 91  ? 9.505  31.983 40.098 1.00 48.78 ? 86  GLU A OE1 1 
ATOM   663  O  OE2 . GLU A 1 91  ? 11.244 33.064 40.867 1.00 53.40 ? 86  GLU A OE2 1 
ATOM   664  N  N   . LYS A 1 92  ? 16.276 30.816 40.009 1.00 37.83 ? 87  LYS A N   1 
ATOM   665  C  CA  . LYS A 1 92  ? 17.685 31.197 39.930 1.00 38.26 ? 87  LYS A CA  1 
ATOM   666  C  C   . LYS A 1 92  ? 18.441 30.350 38.918 1.00 38.36 ? 87  LYS A C   1 
ATOM   667  O  O   . LYS A 1 92  ? 19.130 30.871 38.032 1.00 36.72 ? 87  LYS A O   1 
ATOM   668  C  CB  . LYS A 1 92  ? 18.333 31.019 41.299 1.00 38.23 ? 87  LYS A CB  1 
ATOM   669  C  CG  . LYS A 1 92  ? 19.765 31.519 41.435 1.00 43.82 ? 87  LYS A CG  1 
ATOM   670  C  CD  . LYS A 1 92  ? 20.145 31.511 42.924 1.00 47.52 ? 87  LYS A CD  1 
ATOM   671  C  CE  . LYS A 1 92  ? 21.654 31.494 43.165 1.00 47.55 ? 87  LYS A CE  1 
ATOM   672  N  NZ  . LYS A 1 92  ? 22.052 32.727 43.927 1.00 52.60 ? 87  LYS A NZ  1 
ATOM   673  N  N   . VAL A 1 93  ? 18.372 29.035 39.086 1.00 37.15 ? 88  VAL A N   1 
ATOM   674  C  CA  . VAL A 1 93  ? 19.068 28.117 38.188 1.00 36.13 ? 88  VAL A CA  1 
ATOM   675  C  C   . VAL A 1 93  ? 18.522 28.245 36.770 1.00 37.27 ? 88  VAL A C   1 
ATOM   676  O  O   . VAL A 1 93  ? 19.275 28.235 35.793 1.00 34.08 ? 88  VAL A O   1 
ATOM   677  C  CB  . VAL A 1 93  ? 18.944 26.678 38.719 1.00 36.04 ? 88  VAL A CB  1 
ATOM   678  C  CG1 . VAL A 1 93  ? 19.495 25.673 37.715 1.00 36.74 ? 88  VAL A CG1 1 
ATOM   679  C  CG2 . VAL A 1 93  ? 19.674 26.531 40.058 1.00 37.07 ? 88  VAL A CG2 1 
ATOM   680  N  N   . GLU A 1 94  ? 17.207 28.386 36.643 1.00 36.96 ? 89  GLU A N   1 
ATOM   681  C  CA  . GLU A 1 94  ? 16.581 28.575 35.338 1.00 38.07 ? 89  GLU A CA  1 
ATOM   682  C  C   . GLU A 1 94  ? 17.118 29.811 34.628 1.00 39.31 ? 89  GLU A C   1 
ATOM   683  O  O   . GLU A 1 94  ? 17.422 29.771 33.428 1.00 37.90 ? 89  GLU A O   1 
ATOM   684  C  CB  . GLU A 1 94  ? 15.071 28.666 35.536 1.00 40.74 ? 89  GLU A CB  1 
ATOM   685  C  CG  . GLU A 1 94  ? 14.238 29.043 34.327 1.00 43.01 ? 89  GLU A CG  1 
ATOM   686  C  CD  . GLU A 1 94  ? 12.768 28.777 34.587 1.00 46.22 ? 89  GLU A CD  1 
ATOM   687  O  OE1 . GLU A 1 94  ? 11.930 29.621 34.190 1.00 51.14 ? 89  GLU A OE1 1 
ATOM   688  O  OE2 . GLU A 1 94  ? 12.447 27.704 35.152 1.00 43.97 ? 89  GLU A OE2 1 
ATOM   689  N  N   . THR A 1 95  ? 17.251 30.917 35.352 1.00 37.08 ? 90  THR A N   1 
ATOM   690  C  CA  . THR A 1 95  ? 17.726 32.144 34.727 1.00 40.35 ? 90  THR A CA  1 
ATOM   691  C  C   . THR A 1 95  ? 19.158 31.989 34.232 1.00 39.23 ? 90  THR A C   1 
ATOM   692  O  O   . THR A 1 95  ? 19.508 32.481 33.150 1.00 39.64 ? 90  THR A O   1 
ATOM   693  C  CB  . THR A 1 95  ? 17.592 33.288 35.727 1.00 41.08 ? 90  THR A CB  1 
ATOM   694  O  OG1 . THR A 1 95  ? 16.195 33.497 35.960 1.00 42.66 ? 90  THR A OG1 1 
ATOM   695  C  CG2 . THR A 1 95  ? 18.197 34.558 35.180 1.00 41.60 ? 90  THR A CG2 1 
ATOM   696  N  N   . GLU A 1 96  ? 19.993 31.290 35.007 1.00 36.11 ? 91  GLU A N   1 
ATOM   697  C  CA  . GLU A 1 96  ? 21.365 31.021 34.592 1.00 39.92 ? 91  GLU A CA  1 
ATOM   698  C  C   . GLU A 1 96  ? 21.393 30.129 33.354 1.00 38.12 ? 91  GLU A C   1 
ATOM   699  O  O   . GLU A 1 96  ? 22.209 30.337 32.453 1.00 36.18 ? 91  GLU A O   1 
ATOM   700  C  CB  . GLU A 1 96  ? 22.120 30.363 35.754 1.00 38.48 ? 91  GLU A CB  1 
ATOM   701  C  CG  . GLU A 1 96  ? 22.460 31.381 36.839 1.00 44.47 ? 91  GLU A CG  1 
ATOM   702  C  CD  . GLU A 1 96  ? 23.335 30.843 37.968 1.00 45.27 ? 91  GLU A CD  1 
ATOM   703  O  OE1 . GLU A 1 96  ? 24.099 29.870 37.776 1.00 40.98 ? 91  GLU A OE1 1 
ATOM   704  O  OE2 . GLU A 1 96  ? 23.257 31.452 39.057 1.00 48.39 ? 91  GLU A OE2 1 
ATOM   705  N  N   . LEU A 1 97  ? 20.518 29.121 33.312 1.00 37.58 ? 92  LEU A N   1 
ATOM   706  C  CA  . LEU A 1 97  ? 20.466 28.216 32.161 1.00 37.02 ? 92  LEU A CA  1 
ATOM   707  C  C   . LEU A 1 97  ? 20.070 28.969 30.901 1.00 39.83 ? 92  LEU A C   1 
ATOM   708  O  O   . LEU A 1 97  ? 20.689 28.810 29.839 1.00 40.50 ? 92  LEU A O   1 
ATOM   709  C  CB  . LEU A 1 97  ? 19.478 27.078 32.441 1.00 37.04 ? 92  LEU A CB  1 
ATOM   710  C  CG  . LEU A 1 97  ? 19.222 25.974 31.411 1.00 38.68 ? 92  LEU A CG  1 
ATOM   711  C  CD1 . LEU A 1 97  ? 18.738 24.726 32.147 1.00 39.15 ? 92  LEU A CD1 1 
ATOM   712  C  CD2 . LEU A 1 97  ? 18.189 26.370 30.373 1.00 40.63 ? 92  LEU A CD2 1 
ATOM   713  N  N   . GLN A 1 98  ? 19.020 29.788 31.001 1.00 39.12 ? 93  GLN A N   1 
ATOM   714  C  CA  . GLN A 1 98  ? 18.595 30.603 29.869 1.00 40.78 ? 93  GLN A CA  1 
ATOM   715  C  C   . GLN A 1 98  ? 19.711 31.532 29.401 1.00 42.46 ? 93  GLN A C   1 
ATOM   716  O  O   . GLN A 1 98  ? 19.884 31.749 28.193 1.00 41.14 ? 93  GLN A O   1 
ATOM   717  C  CB  . GLN A 1 98  ? 17.345 31.385 30.272 1.00 42.36 ? 93  GLN A CB  1 
ATOM   718  C  CG  . GLN A 1 98  ? 16.173 30.489 30.681 1.00 43.75 ? 93  GLN A CG  1 
ATOM   719  C  CD  . GLN A 1 98  ? 14.987 31.288 31.177 1.00 44.65 ? 93  GLN A CD  1 
ATOM   720  O  OE1 . GLN A 1 98  ? 15.150 32.174 32.020 1.00 43.39 ? 93  GLN A OE1 1 
ATOM   721  N  NE2 . GLN A 1 98  ? 13.803 30.992 30.672 1.00 46.77 ? 93  GLN A NE2 1 
ATOM   722  N  N   . GLY A 1 99  ? 20.495 32.072 30.337 1.00 41.78 ? 94  GLY A N   1 
ATOM   723  C  CA  . GLY A 1 99  ? 21.588 32.949 29.947 1.00 41.14 ? 94  GLY A CA  1 
ATOM   724  C  C   . GLY A 1 99  ? 22.652 32.227 29.144 1.00 39.92 ? 94  GLY A C   1 
ATOM   725  O  O   . GLY A 1 99  ? 23.202 32.774 28.178 1.00 39.96 ? 94  GLY A O   1 
ATOM   726  N  N   . VAL A 1 100 ? 22.950 30.984 29.525 1.00 38.66 ? 95  VAL A N   1 
ATOM   727  C  CA  . VAL A 1 100 ? 23.929 30.212 28.776 1.00 39.28 ? 95  VAL A CA  1 
ATOM   728  C  C   . VAL A 1 100 ? 23.384 29.877 27.392 1.00 39.12 ? 95  VAL A C   1 
ATOM   729  O  O   . VAL A 1 100 ? 24.094 29.997 26.390 1.00 40.18 ? 95  VAL A O   1 
ATOM   730  C  CB  . VAL A 1 100 ? 24.336 28.955 29.568 1.00 39.00 ? 95  VAL A CB  1 
ATOM   731  C  CG1 . VAL A 1 100 ? 25.178 28.020 28.701 1.00 40.27 ? 95  VAL A CG1 1 
ATOM   732  C  CG2 . VAL A 1 100 ? 25.108 29.368 30.827 1.00 41.06 ? 95  VAL A CG2 1 
ATOM   733  N  N   . CYS A 1 101 ? 22.109 29.485 27.307 1.00 37.67 ? 96  CYS A N   1 
ATOM   734  C  CA  . CYS A 1 101 ? 21.515 29.210 26.002 1.00 40.55 ? 96  CYS A CA  1 
ATOM   735  C  C   . CYS A 1 101 ? 21.484 30.466 25.145 1.00 39.57 ? 96  CYS A C   1 
ATOM   736  O  O   . CYS A 1 101 ? 21.704 30.404 23.929 1.00 39.59 ? 96  CYS A O   1 
ATOM   737  C  CB  . CYS A 1 101 ? 20.099 28.657 26.146 1.00 40.43 ? 96  CYS A CB  1 
ATOM   738  S  SG  . CYS A 1 101 ? 19.964 27.035 26.932 1.00 39.70 ? 96  CYS A SG  1 
ATOM   739  N  N   . ASP A 1 102 ? 21.201 31.614 25.763 1.00 40.46 ? 97  ASP A N   1 
ATOM   740  C  CA  . ASP A 1 102 ? 21.188 32.870 25.027 1.00 41.49 ? 97  ASP A CA  1 
ATOM   741  C  C   . ASP A 1 102 ? 22.578 33.198 24.505 1.00 41.21 ? 97  ASP A C   1 
ATOM   742  O  O   . ASP A 1 102 ? 22.733 33.696 23.378 1.00 43.33 ? 97  ASP A O   1 
ATOM   743  C  CB  . ASP A 1 102 ? 20.672 33.982 25.939 1.00 43.27 ? 97  ASP A CB  1 
ATOM   744  C  CG  . ASP A 1 102 ? 19.156 34.027 25.997 1.00 47.95 ? 97  ASP A CG  1 
ATOM   745  O  OD1 . ASP A 1 102 ? 18.504 33.347 25.174 1.00 50.02 ? 97  ASP A OD1 1 
ATOM   746  O  OD2 . ASP A 1 102 ? 18.614 34.710 26.890 1.00 50.06 ? 97  ASP A OD2 1 
ATOM   747  N  N   . THR A 1 103 ? 23.601 32.909 25.309 1.00 41.02 ? 98  THR A N   1 
ATOM   748  C  CA  . THR A 1 103 ? 24.977 33.128 24.883 1.00 42.39 ? 98  THR A CA  1 
ATOM   749  C  C   . THR A 1 103 ? 25.326 32.262 23.679 1.00 39.31 ? 98  THR A C   1 
ATOM   750  O  O   . THR A 1 103 ? 25.914 32.744 22.704 1.00 40.39 ? 98  THR A O   1 
ATOM   751  C  CB  . THR A 1 103 ? 25.931 32.837 26.035 1.00 42.83 ? 98  THR A CB  1 
ATOM   752  O  OG1 . THR A 1 103 ? 25.701 33.783 27.088 1.00 43.95 ? 98  THR A OG1 1 
ATOM   753  C  CG2 . THR A 1 103 ? 27.384 32.916 25.554 1.00 40.41 ? 98  THR A CG2 1 
ATOM   754  N  N   . VAL A 1 104 ? 24.976 30.976 23.734 1.00 39.36 ? 99  VAL A N   1 
ATOM   755  C  CA  . VAL A 1 104 ? 25.298 30.069 22.636 1.00 37.52 ? 99  VAL A CA  1 
ATOM   756  C  C   . VAL A 1 104 ? 24.545 30.475 21.373 1.00 39.96 ? 99  VAL A C   1 
ATOM   757  O  O   . VAL A 1 104 ? 25.123 30.554 20.277 1.00 37.43 ? 99  VAL A O   1 
ATOM   758  C  CB  . VAL A 1 104 ? 24.991 28.615 23.044 1.00 36.88 ? 99  VAL A CB  1 
ATOM   759  C  CG1 . VAL A 1 104 ? 24.969 27.692 21.822 1.00 38.82 ? 99  VAL A CG1 1 
ATOM   760  C  CG2 . VAL A 1 104 ? 26.019 28.142 24.048 1.00 36.88 ? 99  VAL A CG2 1 
ATOM   761  N  N   . LEU A 1 105 ? 23.244 30.741 21.508 1.00 39.08 ? 100 LEU A N   1 
ATOM   762  C  CA  . LEU A 1 105 ? 22.444 31.145 20.353 1.00 41.95 ? 100 LEU A CA  1 
ATOM   763  C  C   . LEU A 1 105 ? 22.936 32.459 19.759 1.00 41.95 ? 100 LEU A C   1 
ATOM   764  O  O   . LEU A 1 105 ? 22.890 32.646 18.533 1.00 43.62 ? 100 LEU A O   1 
ATOM   765  C  CB  . LEU A 1 105 ? 20.973 31.245 20.760 1.00 43.44 ? 100 LEU A CB  1 
ATOM   766  C  CG  . LEU A 1 105 ? 20.346 29.873 21.059 1.00 42.92 ? 100 LEU A CG  1 
ATOM   767  C  CD1 . LEU A 1 105 ? 19.044 30.013 21.828 1.00 43.51 ? 100 LEU A CD1 1 
ATOM   768  C  CD2 . LEU A 1 105 ? 20.113 29.121 19.749 1.00 43.74 ? 100 LEU A CD2 1 
ATOM   769  N  N   . GLY A 1 106 ? 23.417 33.370 20.606 1.00 41.36 ? 101 GLY A N   1 
ATOM   770  C  CA  . GLY A 1 106 ? 23.994 34.604 20.112 1.00 45.41 ? 101 GLY A CA  1 
ATOM   771  C  C   . GLY A 1 106 ? 25.258 34.374 19.311 1.00 45.54 ? 101 GLY A C   1 
ATOM   772  O  O   . GLY A 1 106 ? 25.454 34.990 18.262 1.00 46.60 ? 101 GLY A O   1 
ATOM   773  N  N   . LEU A 1 107 ? 26.127 33.474 19.784 1.00 41.18 ? 102 LEU A N   1 
ATOM   774  C  CA  . LEU A 1 107 ? 27.335 33.151 19.028 1.00 43.86 ? 102 LEU A CA  1 
ATOM   775  C  C   . LEU A 1 107 ? 26.989 32.504 17.694 1.00 42.60 ? 102 LEU A C   1 
ATOM   776  O  O   . LEU A 1 107 ? 27.626 32.786 16.673 1.00 44.22 ? 102 LEU A O   1 
ATOM   777  C  CB  . LEU A 1 107 ? 28.252 32.220 19.829 1.00 40.45 ? 102 LEU A CB  1 
ATOM   778  C  CG  . LEU A 1 107 ? 29.007 32.729 21.059 1.00 43.11 ? 102 LEU A CG  1 
ATOM   779  C  CD1 . LEU A 1 107 ? 29.555 31.548 21.855 1.00 41.04 ? 102 LEU A CD1 1 
ATOM   780  C  CD2 . LEU A 1 107 ? 30.138 33.681 20.633 1.00 44.07 ? 102 LEU A CD2 1 
ATOM   781  N  N   . LEU A 1 108 ? 26.007 31.601 17.691 1.00 41.93 ? 103 LEU A N   1 
ATOM   782  C  CA  . LEU A 1 108 ? 25.582 30.982 16.443 1.00 41.69 ? 103 LEU A CA  1 
ATOM   783  C  C   . LEU A 1 108 ? 25.109 32.032 15.449 1.00 44.20 ? 103 LEU A C   1 
ATOM   784  O  O   . LEU A 1 108 ? 25.522 32.028 14.281 1.00 44.21 ? 103 LEU A O   1 
ATOM   785  C  CB  . LEU A 1 108 ? 24.473 29.968 16.715 1.00 41.69 ? 103 LEU A CB  1 
ATOM   786  C  CG  . LEU A 1 108 ? 24.965 28.712 17.448 1.00 40.22 ? 103 LEU A CG  1 
ATOM   787  C  CD1 . LEU A 1 108 ? 23.786 27.917 18.003 1.00 40.82 ? 103 LEU A CD1 1 
ATOM   788  C  CD2 . LEU A 1 108 ? 25.802 27.852 16.508 1.00 39.65 ? 103 LEU A CD2 1 
ATOM   789  N  N   . ASP A 1 109 ? 24.241 32.942 15.897 1.00 44.12 ? 104 ASP A N   1 
ATOM   790  C  CA  . ASP A 1 109 ? 23.672 33.951 15.000 1.00 45.02 ? 104 ASP A CA  1 
ATOM   791  C  C   . ASP A 1 109 ? 24.702 34.994 14.579 1.00 47.70 ? 104 ASP A C   1 
ATOM   792  O  O   . ASP A 1 109 ? 24.724 35.422 13.414 1.00 48.37 ? 104 ASP A O   1 
ATOM   793  C  CB  . ASP A 1 109 ? 22.464 34.609 15.675 1.00 48.57 ? 104 ASP A CB  1 
ATOM   794  C  CG  . ASP A 1 109 ? 21.622 35.430 14.710 1.00 55.67 ? 104 ASP A CG  1 
ATOM   795  O  OD1 . ASP A 1 109 ? 21.914 36.639 14.558 1.00 56.31 ? 104 ASP A OD1 1 
ATOM   796  O  OD2 . ASP A 1 109 ? 20.698 34.873 14.071 1.00 58.48 ? 104 ASP A OD2 1 
ATOM   797  N  N   . SER A 1 110 ? 25.555 35.423 15.505 1.00 46.98 ? 105 SER A N   1 
ATOM   798  C  CA  . SER A 1 110 ? 26.478 36.513 15.221 1.00 46.56 ? 105 SER A CA  1 
ATOM   799  C  C   . SER A 1 110 ? 27.704 36.050 14.452 1.00 46.72 ? 105 SER A C   1 
ATOM   800  O  O   . SER A 1 110 ? 28.245 36.817 13.649 1.00 45.37 ? 105 SER A O   1 
ATOM   801  C  CB  . SER A 1 110 ? 26.910 37.187 16.526 1.00 51.45 ? 105 SER A CB  1 
ATOM   802  O  OG  . SER A 1 110 ? 25.854 37.954 17.093 1.00 54.81 ? 105 SER A OG  1 
ATOM   803  N  N   . HIS A 1 111 ? 28.135 34.814 14.649 1.00 43.81 ? 106 HIS A N   1 
ATOM   804  C  CA  . HIS A 1 111 ? 29.462 34.435 14.174 1.00 45.04 ? 106 HIS A CA  1 
ATOM   805  C  C   . HIS A 1 111 ? 29.496 33.160 13.349 1.00 45.30 ? 106 HIS A C   1 
ATOM   806  O  O   . HIS A 1 111 ? 30.259 33.082 12.382 1.00 47.36 ? 106 HIS A O   1 
ATOM   807  C  CB  . HIS A 1 111 ? 30.393 34.268 15.383 1.00 44.64 ? 106 HIS A CB  1 
ATOM   808  C  CG  . HIS A 1 111 ? 30.796 35.564 16.005 1.00 46.03 ? 106 HIS A CG  1 
ATOM   809  N  ND1 . HIS A 1 111 ? 31.733 36.398 15.436 1.00 47.56 ? 106 HIS A ND1 1 
ATOM   810  C  CD2 . HIS A 1 111 ? 30.367 36.186 17.127 1.00 48.39 ? 106 HIS A CD2 1 
ATOM   811  C  CE1 . HIS A 1 111 ? 31.881 37.470 16.192 1.00 45.01 ? 106 HIS A CE1 1 
ATOM   812  N  NE2 . HIS A 1 111 ? 31.062 37.369 17.222 1.00 50.46 ? 106 HIS A NE2 1 
ATOM   813  N  N   . LEU A 1 112 ? 28.702 32.159 13.702 1.00 41.78 ? 107 LEU A N   1 
ATOM   814  C  CA  . LEU A 1 112 ? 28.975 30.800 13.244 1.00 43.43 ? 107 LEU A CA  1 
ATOM   815  C  C   . LEU A 1 112 ? 28.089 30.328 12.097 1.00 44.17 ? 107 LEU A C   1 
ATOM   816  O  O   . LEU A 1 112 ? 28.571 29.617 11.212 1.00 43.53 ? 107 LEU A O   1 
ATOM   817  C  CB  . LEU A 1 112 ? 28.848 29.831 14.417 1.00 42.54 ? 107 LEU A CB  1 
ATOM   818  C  CG  . LEU A 1 112 ? 29.882 30.103 15.509 1.00 41.98 ? 107 LEU A CG  1 
ATOM   819  C  CD1 . LEU A 1 112 ? 29.572 29.284 16.754 1.00 39.45 ? 107 LEU A CD1 1 
ATOM   820  C  CD2 . LEU A 1 112 ? 31.288 29.806 14.992 1.00 43.06 ? 107 LEU A CD2 1 
ATOM   821  N  N   . ILE A 1 113 ? 26.804 30.663 12.104 1.00 43.39 ? 108 ILE A N   1 
ATOM   822  C  CA  . ILE A 1 113 ? 25.890 30.188 11.072 1.00 44.72 ? 108 ILE A CA  1 
ATOM   823  C  C   . ILE A 1 113 ? 26.095 31.040 9.825  1.00 47.10 ? 108 ILE A C   1 
ATOM   824  O  O   . ILE A 1 113 ? 25.901 32.262 9.854  1.00 47.52 ? 108 ILE A O   1 
ATOM   825  C  CB  . ILE A 1 113 ? 24.432 30.230 11.553 1.00 44.46 ? 108 ILE A CB  1 
ATOM   826  C  CG1 . ILE A 1 113 ? 24.197 29.157 12.617 1.00 45.52 ? 108 ILE A CG1 1 
ATOM   827  C  CG2 . ILE A 1 113 ? 23.475 30.014 10.390 1.00 47.67 ? 108 ILE A CG2 1 
ATOM   828  C  CD1 . ILE A 1 113 ? 22.838 29.247 13.340 1.00 44.23 ? 108 ILE A CD1 1 
ATOM   829  N  N   . LYS A 1 114 ? 26.519 30.403 8.734  1.00 47.07 ? 109 LYS A N   1 
ATOM   830  C  CA  . LYS A 1 114 ? 26.817 31.105 7.491  1.00 52.30 ? 109 LYS A CA  1 
ATOM   831  C  C   . LYS A 1 114 ? 26.189 30.372 6.314  1.00 54.29 ? 109 LYS A C   1 
ATOM   832  O  O   . LYS A 1 114 ? 25.839 29.191 6.399  1.00 51.31 ? 109 LYS A O   1 
ATOM   833  C  CB  . LYS A 1 114 ? 28.335 31.233 7.248  1.00 52.81 ? 109 LYS A CB  1 
ATOM   834  C  CG  . LYS A 1 114 ? 29.142 31.745 8.428  1.00 51.93 ? 109 LYS A CG  1 
ATOM   835  C  CD  . LYS A 1 114 ? 28.850 33.201 8.732  1.00 57.73 ? 109 LYS A CD  1 
ATOM   836  C  CE  . LYS A 1 114 ? 30.143 33.966 9.011  1.00 59.10 ? 109 LYS A CE  1 
ATOM   837  N  NZ  . LYS A 1 114 ? 31.196 33.582 8.020  1.00 63.59 ? 109 LYS A NZ  1 
ATOM   838  N  N   . GLU A 1 115 ? 26.069 31.091 5.193  1.00 57.13 ? 110 GLU A N   1 
ATOM   839  C  CA  . GLU A 1 115 ? 25.624 30.457 3.958  1.00 59.37 ? 110 GLU A CA  1 
ATOM   840  C  C   . GLU A 1 115 ? 26.709 29.557 3.382  1.00 57.87 ? 110 GLU A C   1 
ATOM   841  O  O   . GLU A 1 115 ? 26.416 28.483 2.846  1.00 60.68 ? 110 GLU A O   1 
ATOM   842  C  CB  . GLU A 1 115 ? 25.224 31.524 2.938  1.00 64.07 ? 110 GLU A CB  1 
ATOM   843  C  CG  . GLU A 1 115 ? 24.027 32.364 3.347  1.00 69.39 ? 110 GLU A CG  1 
ATOM   844  C  CD  . GLU A 1 115 ? 22.704 31.721 2.977  1.00 76.01 ? 110 GLU A CD  1 
ATOM   845  O  OE1 . GLU A 1 115 ? 22.461 30.567 3.395  1.00 75.96 ? 110 GLU A OE1 1 
ATOM   846  O  OE2 . GLU A 1 115 ? 21.915 32.368 2.249  1.00 78.57 ? 110 GLU A OE2 1 
ATOM   847  N  N   . ALA A 1 116 ? 27.967 29.976 3.488  1.00 58.64 ? 111 ALA A N   1 
ATOM   848  C  CA  . ALA A 1 116 ? 29.089 29.219 2.957  1.00 56.48 ? 111 ALA A CA  1 
ATOM   849  C  C   . ALA A 1 116 ? 29.554 28.176 3.972  1.00 57.37 ? 111 ALA A C   1 
ATOM   850  O  O   . ALA A 1 116 ? 28.945 27.979 5.028  1.00 54.99 ? 111 ALA A O   1 
ATOM   851  C  CB  . ALA A 1 116 ? 30.223 30.163 2.569  1.00 61.56 ? 111 ALA A CB  1 
ATOM   852  N  N   . GLY A 1 117 ? 30.655 27.503 3.657  1.00 57.62 ? 112 GLY A N   1 
ATOM   853  C  CA  . GLY A 1 117 ? 31.182 26.446 4.488  1.00 57.64 ? 112 GLY A CA  1 
ATOM   854  C  C   . GLY A 1 117 ? 30.758 25.078 3.989  1.00 55.13 ? 112 GLY A C   1 
ATOM   855  O  O   . GLY A 1 117 ? 29.815 24.926 3.206  1.00 52.44 ? 112 GLY A O   1 
ATOM   856  N  N   . ASP A 1 118 ? 31.480 24.060 4.447  1.00 53.18 ? 113 ASP A N   1 
ATOM   857  C  CA  . ASP A 1 118 ? 31.125 22.707 4.066  1.00 53.49 ? 113 ASP A CA  1 
ATOM   858  C  C   . ASP A 1 118 ? 29.838 22.282 4.778  1.00 50.01 ? 113 ASP A C   1 
ATOM   859  O  O   . ASP A 1 118 ? 29.339 22.959 5.680  1.00 47.75 ? 113 ASP A O   1 
ATOM   860  C  CB  . ASP A 1 118 ? 32.273 21.734 4.359  1.00 53.53 ? 113 ASP A CB  1 
ATOM   861  C  CG  . ASP A 1 118 ? 32.696 21.722 5.825  1.00 54.71 ? 113 ASP A CG  1 
ATOM   862  O  OD1 . ASP A 1 118 ? 33.738 21.099 6.126  1.00 56.03 ? 113 ASP A OD1 1 
ATOM   863  O  OD2 . ASP A 1 118 ? 32.009 22.324 6.679  1.00 52.77 ? 113 ASP A OD2 1 
ATOM   864  N  N   . ALA A 1 119 ? 29.296 21.141 4.345  1.00 50.58 ? 114 ALA A N   1 
ATOM   865  C  CA  . ALA A 1 119 ? 28.032 20.656 4.895  1.00 50.45 ? 114 ALA A CA  1 
ATOM   866  C  C   . ALA A 1 119 ? 28.137 20.367 6.385  1.00 47.13 ? 114 ALA A C   1 
ATOM   867  O  O   . ALA A 1 119 ? 27.199 20.642 7.142  1.00 46.33 ? 114 ALA A O   1 
ATOM   868  C  CB  . ALA A 1 119 ? 27.584 19.398 4.154  1.00 52.73 ? 114 ALA A CB  1 
ATOM   869  N  N   . GLU A 1 120 ? 29.250 19.771 6.815  1.00 45.11 ? 115 GLU A N   1 
ATOM   870  C  CA  . GLU A 1 120 ? 29.455 19.474 8.230  1.00 47.76 ? 115 GLU A CA  1 
ATOM   871  C  C   . GLU A 1 120 ? 29.235 20.698 9.099  1.00 44.99 ? 115 GLU A C   1 
ATOM   872  O  O   . GLU A 1 120 ? 28.507 20.644 10.101 1.00 43.21 ? 115 GLU A O   1 
ATOM   873  C  CB  . GLU A 1 120 ? 30.866 18.932 8.429  1.00 48.28 ? 115 GLU A CB  1 
ATOM   874  C  CG  . GLU A 1 120 ? 31.123 17.680 7.628  1.00 52.14 ? 115 GLU A CG  1 
ATOM   875  C  CD  . GLU A 1 120 ? 31.801 16.636 8.456  1.00 47.74 ? 115 GLU A CD  1 
ATOM   876  O  OE1 . GLU A 1 120 ? 31.292 15.495 8.575  1.00 49.71 ? 115 GLU A OE1 1 
ATOM   877  O  OE2 . GLU A 1 120 ? 32.904 16.958 8.933  1.00 48.82 ? 115 GLU A OE2 1 
ATOM   878  N  N   . SER A 1 121 ? 29.882 21.809 8.746  1.00 45.68 ? 116 SER A N   1 
ATOM   879  C  CA  . SER A 1 121 ? 29.773 23.005 9.572  1.00 44.87 ? 116 SER A CA  1 
ATOM   880  C  C   . SER A 1 121 ? 28.348 23.534 9.568  1.00 43.17 ? 116 SER A C   1 
ATOM   881  O  O   . SER A 1 121 ? 27.778 23.822 10.624 1.00 41.79 ? 116 SER A O   1 
ATOM   882  C  CB  . SER A 1 121 ? 30.755 24.075 9.094  1.00 46.30 ? 116 SER A CB  1 
ATOM   883  O  OG  . SER A 1 121 ? 30.404 24.552 7.812  1.00 50.73 ? 116 SER A OG  1 
ATOM   884  N  N   . ARG A 1 122 ? 27.742 23.652 8.389  1.00 43.10 ? 117 ARG A N   1 
ATOM   885  C  CA  . ARG A 1 122 ? 26.396 24.208 8.339  1.00 44.08 ? 117 ARG A CA  1 
ATOM   886  C  C   . ARG A 1 122 ? 25.407 23.334 9.099  1.00 42.40 ? 117 ARG A C   1 
ATOM   887  O  O   . ARG A 1 122 ? 24.581 23.846 9.865  1.00 42.47 ? 117 ARG A O   1 
ATOM   888  C  CB  . ARG A 1 122 ? 25.962 24.389 6.890  1.00 46.29 ? 117 ARG A CB  1 
ATOM   889  C  CG  . ARG A 1 122 ? 26.606 25.604 6.237  1.00 49.09 ? 117 ARG A CG  1 
ATOM   890  C  CD  . ARG A 1 122 ? 26.122 25.780 4.798  1.00 50.68 ? 117 ARG A CD  1 
ATOM   891  N  NE  . ARG A 1 122 ? 26.868 24.929 3.879  1.00 53.31 ? 117 ARG A NE  1 
ATOM   892  C  CZ  . ARG A 1 122 ? 26.347 23.924 3.185  1.00 55.29 ? 117 ARG A CZ  1 
ATOM   893  N  NH1 . ARG A 1 122 ? 25.057 23.633 3.248  1.00 54.49 ? 117 ARG A NH1 1 
ATOM   894  N  NH2 . ARG A 1 122 ? 27.138 23.197 2.400  1.00 55.06 ? 117 ARG A NH2 1 
ATOM   895  N  N   . VAL A 1 123 ? 25.475 22.017 8.900  1.00 41.52 ? 118 VAL A N   1 
ATOM   896  C  CA  . VAL A 1 123 ? 24.567 21.126 9.613  1.00 41.63 ? 118 VAL A CA  1 
ATOM   897  C  C   . VAL A 1 123 ? 24.857 21.178 11.107 1.00 40.17 ? 118 VAL A C   1 
ATOM   898  O  O   . VAL A 1 123 ? 23.938 21.207 11.941 1.00 38.82 ? 118 VAL A O   1 
ATOM   899  C  CB  . VAL A 1 123 ? 24.668 19.686 9.075  1.00 40.48 ? 118 VAL A CB  1 
ATOM   900  C  CG1 . VAL A 1 123 ? 23.835 18.756 9.918  1.00 42.09 ? 118 VAL A CG1 1 
ATOM   901  C  CG2 . VAL A 1 123 ? 24.197 19.585 7.602  1.00 42.85 ? 118 VAL A CG2 1 
ATOM   902  N  N   . PHE A 1 124 ? 26.136 21.188 11.474 1.00 39.63 ? 119 PHE A N   1 
ATOM   903  C  CA  . PHE A 1 124 ? 26.450 21.152 12.895 1.00 39.41 ? 119 PHE A CA  1 
ATOM   904  C  C   . PHE A 1 124 ? 25.906 22.376 13.621 1.00 39.65 ? 119 PHE A C   1 
ATOM   905  O  O   . PHE A 1 124 ? 25.353 22.251 14.722 1.00 38.48 ? 119 PHE A O   1 
ATOM   906  C  CB  . PHE A 1 124 ? 27.947 21.037 13.139 1.00 38.71 ? 119 PHE A CB  1 
ATOM   907  C  CG  . PHE A 1 124 ? 28.311 21.324 14.562 1.00 39.57 ? 119 PHE A CG  1 
ATOM   908  C  CD1 . PHE A 1 124 ? 28.131 20.360 15.536 1.00 38.52 ? 119 PHE A CD1 1 
ATOM   909  C  CD2 . PHE A 1 124 ? 28.756 22.586 14.930 1.00 39.01 ? 119 PHE A CD2 1 
ATOM   910  C  CE1 . PHE A 1 124 ? 28.433 20.626 16.858 1.00 39.12 ? 119 PHE A CE1 1 
ATOM   911  C  CE2 . PHE A 1 124 ? 29.058 22.866 16.245 1.00 38.20 ? 119 PHE A CE2 1 
ATOM   912  C  CZ  . PHE A 1 124 ? 28.899 21.879 17.215 1.00 36.98 ? 119 PHE A CZ  1 
ATOM   913  N  N   . TYR A 1 125 ? 26.087 23.576 13.047 1.00 37.94 ? 120 TYR A N   1 
ATOM   914  C  CA  . TYR A 1 125 ? 25.649 24.784 13.747 1.00 40.23 ? 120 TYR A CA  1 
ATOM   915  C  C   . TYR A 1 125 ? 24.130 24.875 13.799 1.00 39.16 ? 120 TYR A C   1 
ATOM   916  O  O   . TYR A 1 125 ? 23.561 25.324 14.802 1.00 39.27 ? 120 TYR A O   1 
ATOM   917  C  CB  . TYR A 1 125 ? 26.246 26.037 13.092 1.00 38.70 ? 120 TYR A CB  1 
ATOM   918  C  CG  . TYR A 1 125 ? 27.744 26.144 13.266 1.00 38.66 ? 120 TYR A CG  1 
ATOM   919  C  CD1 . TYR A 1 125 ? 28.330 26.077 14.529 1.00 39.58 ? 120 TYR A CD1 1 
ATOM   920  C  CD2 . TYR A 1 125 ? 28.578 26.302 12.168 1.00 41.84 ? 120 TYR A CD2 1 
ATOM   921  C  CE1 . TYR A 1 125 ? 29.701 26.163 14.683 1.00 38.38 ? 120 TYR A CE1 1 
ATOM   922  C  CE2 . TYR A 1 125 ? 29.941 26.394 12.314 1.00 40.99 ? 120 TYR A CE2 1 
ATOM   923  C  CZ  . TYR A 1 125 ? 30.499 26.326 13.570 1.00 38.87 ? 120 TYR A CZ  1 
ATOM   924  O  OH  . TYR A 1 125 ? 31.870 26.405 13.689 1.00 41.02 ? 120 TYR A OH  1 
ATOM   925  N  N   . LEU A 1 126 ? 23.450 24.457 12.732 1.00 39.80 ? 121 LEU A N   1 
ATOM   926  C  CA  . LEU A 1 126 ? 21.995 24.488 12.758 1.00 38.46 ? 121 LEU A CA  1 
ATOM   927  C  C   . LEU A 1 126 ? 21.452 23.462 13.739 1.00 39.52 ? 121 LEU A C   1 
ATOM   928  O  O   . LEU A 1 126 ? 20.459 23.723 14.425 1.00 40.35 ? 121 LEU A O   1 
ATOM   929  C  CB  . LEU A 1 126 ? 21.435 24.260 11.350 1.00 40.52 ? 121 LEU A CB  1 
ATOM   930  C  CG  . LEU A 1 126 ? 21.620 25.452 10.409 1.00 43.87 ? 121 LEU A CG  1 
ATOM   931  C  CD1 . LEU A 1 126 ? 21.372 25.033 8.959  1.00 43.25 ? 121 LEU A CD1 1 
ATOM   932  C  CD2 . LEU A 1 126 ? 20.705 26.588 10.813 1.00 48.06 ? 121 LEU A CD2 1 
ATOM   933  N  N   . LYS A 1 127 ? 22.085 22.287 13.809 1.00 38.68 ? 122 LYS A N   1 
ATOM   934  C  CA  . LYS A 1 127 ? 21.791 21.336 14.882 1.00 39.00 ? 122 LYS A CA  1 
ATOM   935  C  C   . LYS A 1 127 ? 21.994 21.972 16.251 1.00 39.28 ? 122 LYS A C   1 
ATOM   936  O  O   . LYS A 1 127 ? 21.152 21.823 17.143 1.00 38.27 ? 122 LYS A O   1 
ATOM   937  C  CB  . LYS A 1 127 ? 22.669 20.095 14.747 1.00 37.01 ? 122 LYS A CB  1 
ATOM   938  C  CG  . LYS A 1 127 ? 22.538 19.086 15.905 1.00 37.12 ? 122 LYS A CG  1 
ATOM   939  C  CD  . LYS A 1 127 ? 23.629 18.037 15.832 1.00 36.60 ? 122 LYS A CD  1 
ATOM   940  C  CE  . LYS A 1 127 ? 23.646 17.159 17.108 1.00 36.78 ? 122 LYS A CE  1 
ATOM   941  N  NZ  . LYS A 1 127 ? 23.959 17.945 18.382 1.00 36.94 ? 122 LYS A NZ  1 
ATOM   942  N  N   . MET A 1 128 ? 23.133 22.645 16.452 1.00 38.00 ? 123 MET A N   1 
ATOM   943  C  CA  . MET A 1 128 ? 23.361 23.306 17.739 1.00 35.96 ? 123 MET A CA  1 
ATOM   944  C  C   . MET A 1 128 ? 22.252 24.297 18.050 1.00 37.94 ? 123 MET A C   1 
ATOM   945  O  O   . MET A 1 128 ? 21.769 24.372 19.184 1.00 36.66 ? 123 MET A O   1 
ATOM   946  C  CB  . MET A 1 128 ? 24.692 24.041 17.746 1.00 37.26 ? 123 MET A CB  1 
ATOM   947  C  CG  . MET A 1 128 ? 25.336 24.132 19.124 1.00 39.39 ? 123 MET A CG  1 
ATOM   948  S  SD  . MET A 1 128 ? 26.909 24.997 19.027 1.00 42.68 ? 123 MET A SD  1 
ATOM   949  C  CE  . MET A 1 128 ? 27.387 25.003 20.772 1.00 36.66 ? 123 MET A CE  1 
ATOM   950  N  N   . LYS A 1 129 ? 21.838 25.079 17.055 1.00 38.04 ? 124 LYS A N   1 
ATOM   951  C  CA  . LYS A 1 129 ? 20.767 26.038 17.296 1.00 40.31 ? 124 LYS A CA  1 
ATOM   952  C  C   . LYS A 1 129 ? 19.488 25.325 17.718 1.00 40.74 ? 124 LYS A C   1 
ATOM   953  O  O   . LYS A 1 129 ? 18.805 25.758 18.656 1.00 39.79 ? 124 LYS A O   1 
ATOM   954  C  CB  . LYS A 1 129 ? 20.543 26.879 16.042 1.00 38.15 ? 124 LYS A CB  1 
ATOM   955  C  CG  . LYS A 1 129 ? 19.486 27.961 16.187 1.00 40.45 ? 124 LYS A CG  1 
ATOM   956  C  CD  . LYS A 1 129 ? 19.473 28.830 14.933 1.00 44.22 ? 124 LYS A CD  1 
ATOM   957  C  CE  . LYS A 1 129 ? 18.284 29.775 14.896 1.00 46.80 ? 124 LYS A CE  1 
ATOM   958  N  NZ  . LYS A 1 129 ? 18.398 30.668 13.712 1.00 52.75 ? 124 LYS A NZ  1 
ATOM   959  N  N   . GLY A 1 130 ? 19.157 24.220 17.050 1.00 38.72 ? 125 GLY A N   1 
ATOM   960  C  CA  . GLY A 1 130 ? 17.998 23.446 17.463 1.00 40.80 ? 125 GLY A CA  1 
ATOM   961  C  C   . GLY A 1 130 ? 18.118 22.951 18.894 1.00 40.31 ? 125 GLY A C   1 
ATOM   962  O  O   . GLY A 1 130 ? 17.161 23.027 19.670 1.00 40.48 ? 125 GLY A O   1 
ATOM   963  N  N   . ASP A 1 131 ? 19.307 22.468 19.271 1.00 38.03 ? 126 ASP A N   1 
ATOM   964  C  CA  . ASP A 1 131 ? 19.507 21.936 20.618 1.00 37.77 ? 126 ASP A CA  1 
ATOM   965  C  C   . ASP A 1 131 ? 19.294 23.009 21.681 1.00 38.84 ? 126 ASP A C   1 
ATOM   966  O  O   . ASP A 1 131 ? 18.622 22.765 22.688 1.00 37.87 ? 126 ASP A O   1 
ATOM   967  C  CB  . ASP A 1 131 ? 20.907 21.349 20.764 1.00 38.78 ? 126 ASP A CB  1 
ATOM   968  C  CG  . ASP A 1 131 ? 21.101 20.051 19.991 1.00 38.26 ? 126 ASP A CG  1 
ATOM   969  O  OD1 . ASP A 1 131 ? 20.109 19.383 19.609 1.00 39.21 ? 126 ASP A OD1 1 
ATOM   970  O  OD2 . ASP A 1 131 ? 22.277 19.709 19.768 1.00 39.54 ? 126 ASP A OD2 1 
ATOM   971  N  N   . TYR A 1 132 ? 19.880 24.201 21.488 1.00 37.55 ? 127 TYR A N   1 
ATOM   972  C  CA  . TYR A 1 132 ? 19.832 25.180 22.568 1.00 39.17 ? 127 TYR A CA  1 
ATOM   973  C  C   . TYR A 1 132 ? 18.479 25.872 22.640 1.00 40.24 ? 127 TYR A C   1 
ATOM   974  O  O   . TYR A 1 132 ? 18.063 26.270 23.730 1.00 40.46 ? 127 TYR A O   1 
ATOM   975  C  CB  . TYR A 1 132 ? 21.003 26.166 22.454 1.00 38.91 ? 127 TYR A CB  1 
ATOM   976  C  CG  . TYR A 1 132 ? 22.237 25.505 23.002 1.00 37.75 ? 127 TYR A CG  1 
ATOM   977  C  CD1 . TYR A 1 132 ? 22.994 24.654 22.209 1.00 38.23 ? 127 TYR A CD1 1 
ATOM   978  C  CD2 . TYR A 1 132 ? 22.602 25.649 24.341 1.00 37.13 ? 127 TYR A CD2 1 
ATOM   979  C  CE1 . TYR A 1 132 ? 24.093 23.994 22.714 1.00 38.04 ? 127 TYR A CE1 1 
ATOM   980  C  CE2 . TYR A 1 132 ? 23.702 24.994 24.852 1.00 37.35 ? 127 TYR A CE2 1 
ATOM   981  C  CZ  . TYR A 1 132 ? 24.451 24.176 24.034 1.00 36.40 ? 127 TYR A CZ  1 
ATOM   982  O  OH  . TYR A 1 132 ? 25.537 23.509 24.551 1.00 36.28 ? 127 TYR A OH  1 
ATOM   983  N  N   . TYR A 1 133 ? 17.745 25.950 21.528 1.00 38.00 ? 128 TYR A N   1 
ATOM   984  C  CA  . TYR A 1 133 ? 16.335 26.307 21.624 1.00 41.14 ? 128 TYR A CA  1 
ATOM   985  C  C   . TYR A 1 133 ? 15.546 25.218 22.340 1.00 41.95 ? 128 TYR A C   1 
ATOM   986  O  O   . TYR A 1 133 ? 14.657 25.514 23.149 1.00 45.05 ? 128 TYR A O   1 
ATOM   987  C  CB  . TYR A 1 133 ? 15.751 26.568 20.232 1.00 42.48 ? 128 TYR A CB  1 
ATOM   988  C  CG  . TYR A 1 133 ? 15.917 28.003 19.781 1.00 46.35 ? 128 TYR A CG  1 
ATOM   989  C  CD1 . TYR A 1 133 ? 15.395 29.046 20.532 1.00 47.49 ? 128 TYR A CD1 1 
ATOM   990  C  CD2 . TYR A 1 133 ? 16.593 28.311 18.607 1.00 46.93 ? 128 TYR A CD2 1 
ATOM   991  C  CE1 . TYR A 1 133 ? 15.538 30.358 20.127 1.00 48.91 ? 128 TYR A CE1 1 
ATOM   992  C  CE2 . TYR A 1 133 ? 16.741 29.623 18.187 1.00 48.58 ? 128 TYR A CE2 1 
ATOM   993  C  CZ  . TYR A 1 133 ? 16.214 30.642 18.957 1.00 49.71 ? 128 TYR A CZ  1 
ATOM   994  O  OH  . TYR A 1 133 ? 16.364 31.947 18.562 1.00 51.35 ? 128 TYR A OH  1 
ATOM   995  N  N   . ARG A 1 134 ? 15.876 23.952 22.079 1.00 40.95 ? 129 ARG A N   1 
ATOM   996  C  CA  . ARG A 1 134 ? 15.203 22.867 22.782 1.00 40.29 ? 129 ARG A CA  1 
ATOM   997  C  C   . ARG A 1 134 ? 15.441 22.964 24.286 1.00 40.68 ? 129 ARG A C   1 
ATOM   998  O  O   . ARG A 1 134 ? 14.518 22.764 25.078 1.00 40.78 ? 129 ARG A O   1 
ATOM   999  C  CB  . ARG A 1 134 ? 15.674 21.516 22.247 1.00 41.38 ? 129 ARG A CB  1 
ATOM   1000 C  CG  . ARG A 1 134 ? 15.229 20.317 23.089 1.00 39.01 ? 129 ARG A CG  1 
ATOM   1001 C  CD  . ARG A 1 134 ? 15.261 19.015 22.273 1.00 42.47 ? 129 ARG A CD  1 
ATOM   1002 N  NE  . ARG A 1 134 ? 16.617 18.708 21.830 1.00 40.67 ? 129 ARG A NE  1 
ATOM   1003 C  CZ  . ARG A 1 134 ? 17.499 18.011 22.534 1.00 39.22 ? 129 ARG A CZ  1 
ATOM   1004 N  NH1 . ARG A 1 134 ? 17.189 17.489 23.712 1.00 38.84 ? 129 ARG A NH1 1 
ATOM   1005 N  NH2 . ARG A 1 134 ? 18.724 17.828 22.043 1.00 38.09 ? 129 ARG A NH2 1 
ATOM   1006 N  N   . TYR A 1 135 ? 16.666 23.288 24.697 1.00 39.67 ? 130 TYR A N   1 
ATOM   1007 C  CA  . TYR A 1 135 ? 16.930 23.430 26.127 1.00 41.24 ? 130 TYR A CA  1 
ATOM   1008 C  C   . TYR A 1 135 ? 16.134 24.590 26.713 1.00 42.23 ? 130 TYR A C   1 
ATOM   1009 O  O   . TYR A 1 135 ? 15.612 24.486 27.828 1.00 40.91 ? 130 TYR A O   1 
ATOM   1010 C  CB  . TYR A 1 135 ? 18.430 23.597 26.382 1.00 39.31 ? 130 TYR A CB  1 
ATOM   1011 C  CG  . TYR A 1 135 ? 19.276 22.476 25.791 1.00 38.02 ? 130 TYR A CG  1 
ATOM   1012 C  CD1 . TYR A 1 135 ? 18.770 21.185 25.663 1.00 39.25 ? 130 TYR A CD1 1 
ATOM   1013 C  CD2 . TYR A 1 135 ? 20.566 22.719 25.336 1.00 37.35 ? 130 TYR A CD2 1 
ATOM   1014 C  CE1 . TYR A 1 135 ? 19.534 20.160 25.123 1.00 38.90 ? 130 TYR A CE1 1 
ATOM   1015 C  CE2 . TYR A 1 135 ? 21.341 21.699 24.791 1.00 38.08 ? 130 TYR A CE2 1 
ATOM   1016 C  CZ  . TYR A 1 135 ? 20.816 20.417 24.685 1.00 40.76 ? 130 TYR A CZ  1 
ATOM   1017 O  OH  . TYR A 1 135 ? 21.577 19.396 24.134 1.00 38.90 ? 130 TYR A OH  1 
ATOM   1018 N  N   . LEU A 1 136 ? 16.006 25.692 25.968 1.00 39.49 ? 131 LEU A N   1 
ATOM   1019 C  CA  . LEU A 1 136 ? 15.139 26.784 26.417 1.00 42.63 ? 131 LEU A CA  1 
ATOM   1020 C  C   . LEU A 1 136 ? 13.691 26.325 26.503 1.00 44.91 ? 131 LEU A C   1 
ATOM   1021 O  O   . LEU A 1 136 ? 12.952 26.748 27.399 1.00 45.99 ? 131 LEU A O   1 
ATOM   1022 C  CB  . LEU A 1 136 ? 15.244 27.996 25.480 1.00 45.03 ? 131 LEU A CB  1 
ATOM   1023 C  CG  . LEU A 1 136 ? 16.498 28.868 25.549 1.00 43.26 ? 131 LEU A CG  1 
ATOM   1024 C  CD1 . LEU A 1 136 ? 16.416 30.013 24.559 1.00 46.61 ? 131 LEU A CD1 1 
ATOM   1025 C  CD2 . LEU A 1 136 ? 16.717 29.385 26.968 1.00 44.16 ? 131 LEU A CD2 1 
ATOM   1026 N  N   . ALA A 1 137 ? 13.268 25.458 25.579 1.00 42.64 ? 132 ALA A N   1 
ATOM   1027 C  CA  . ALA A 1 137 ? 11.891 24.981 25.587 1.00 44.72 ? 132 ALA A CA  1 
ATOM   1028 C  C   . ALA A 1 137 ? 11.612 24.078 26.783 1.00 45.79 ? 132 ALA A C   1 
ATOM   1029 O  O   . ALA A 1 137 ? 10.470 24.014 27.254 1.00 46.69 ? 132 ALA A O   1 
ATOM   1030 C  CB  . ALA A 1 137 ? 11.577 24.247 24.278 1.00 45.20 ? 132 ALA A CB  1 
ATOM   1031 N  N   . GLU A 1 138 ? 12.637 23.389 27.297 1.00 43.13 ? 133 GLU A N   1 
ATOM   1032 C  CA  . GLU A 1 138 ? 12.440 22.540 28.466 1.00 44.07 ? 133 GLU A CA  1 
ATOM   1033 C  C   . GLU A 1 138 ? 11.985 23.341 29.684 1.00 44.70 ? 133 GLU A C   1 
ATOM   1034 O  O   . GLU A 1 138 ? 11.297 22.797 30.553 1.00 45.42 ? 133 GLU A O   1 
ATOM   1035 C  CB  . GLU A 1 138 ? 13.728 21.773 28.785 1.00 43.50 ? 133 GLU A CB  1 
ATOM   1036 C  CG  . GLU A 1 138 ? 14.041 20.662 27.783 1.00 44.32 ? 133 GLU A CG  1 
ATOM   1037 C  CD  . GLU A 1 138 ? 15.375 19.978 28.029 1.00 43.33 ? 133 GLU A CD  1 
ATOM   1038 O  OE1 . GLU A 1 138 ? 16.196 20.503 28.803 1.00 41.87 ? 133 GLU A OE1 1 
ATOM   1039 O  OE2 . GLU A 1 138 ? 15.606 18.901 27.446 1.00 42.52 ? 133 GLU A OE2 1 
ATOM   1040 N  N   . VAL A 1 139 ? 12.324 24.629 29.755 1.00 45.21 ? 134 VAL A N   1 
ATOM   1041 C  CA  . VAL A 1 139 ? 12.003 25.443 30.921 1.00 45.47 ? 134 VAL A CA  1 
ATOM   1042 C  C   . VAL A 1 139 ? 11.055 26.597 30.594 1.00 50.39 ? 134 VAL A C   1 
ATOM   1043 O  O   . VAL A 1 139 ? 10.798 27.438 31.451 1.00 48.22 ? 134 VAL A O   1 
ATOM   1044 C  CB  . VAL A 1 139 ? 13.283 25.966 31.600 1.00 46.63 ? 134 VAL A CB  1 
ATOM   1045 C  CG1 . VAL A 1 139 ? 14.257 24.821 31.858 1.00 43.54 ? 134 VAL A CG1 1 
ATOM   1046 C  CG2 . VAL A 1 139 ? 13.932 27.063 30.773 1.00 44.93 ? 134 VAL A CG2 1 
ATOM   1047 N  N   . ALA A 1 140 ? 10.515 26.652 29.382 1.00 52.02 ? 135 ALA A N   1 
ATOM   1048 C  CA  . ALA A 1 140 ? 9.657  27.764 28.990 1.00 58.67 ? 135 ALA A CA  1 
ATOM   1049 C  C   . ALA A 1 140 ? 8.200  27.511 29.383 1.00 65.62 ? 135 ALA A C   1 
ATOM   1050 O  O   . ALA A 1 140 ? 7.791  26.380 29.652 1.00 65.99 ? 135 ALA A O   1 
ATOM   1051 C  CB  . ALA A 1 140 ? 9.752  28.006 27.480 1.00 56.20 ? 135 ALA A CB  1 
ATOM   1052 N  N   . THR A 1 141 ? 7.407  28.589 29.388 1.00 70.04 ? 136 THR A N   1 
ATOM   1053 C  CA  . THR A 1 141 ? 5.983  28.484 29.705 1.00 75.45 ? 136 THR A CA  1 
ATOM   1054 C  C   . THR A 1 141 ? 5.081  29.284 28.762 1.00 79.44 ? 136 THR A C   1 
ATOM   1055 O  O   . THR A 1 141 ? 4.298  28.700 28.004 1.00 81.07 ? 136 THR A O   1 
ATOM   1056 C  CB  . THR A 1 141 ? 5.718  28.936 31.143 1.00 80.24 ? 136 THR A CB  1 
ATOM   1057 O  OG1 . THR A 1 141 ? 6.365  30.194 31.374 1.00 81.81 ? 136 THR A OG1 1 
ATOM   1058 C  CG2 . THR A 1 141 ? 6.222  27.901 32.142 1.00 76.39 ? 136 THR A CG2 1 
ATOM   1059 N  N   . GLY A 1 142 ? 5.168  30.615 28.804 1.00 80.14 ? 137 GLY A N   1 
ATOM   1060 C  CA  . GLY A 1 142 ? 4.144  31.456 28.204 1.00 80.40 ? 137 GLY A CA  1 
ATOM   1061 C  C   . GLY A 1 142 ? 4.233  31.707 26.710 1.00 82.67 ? 137 GLY A C   1 
ATOM   1062 O  O   . GLY A 1 142 ? 4.507  30.791 25.927 1.00 80.08 ? 137 GLY A O   1 
ATOM   1063 N  N   . ASP A 1 143 ? 3.970  32.956 26.305 1.00 84.60 ? 138 ASP A N   1 
ATOM   1064 C  CA  . ASP A 1 143 ? 4.122  33.337 24.903 1.00 86.11 ? 138 ASP A CA  1 
ATOM   1065 C  C   . ASP A 1 143 ? 5.526  33.049 24.400 1.00 83.08 ? 138 ASP A C   1 
ATOM   1066 O  O   . ASP A 1 143 ? 5.724  32.834 23.198 1.00 82.56 ? 138 ASP A O   1 
ATOM   1067 C  CB  . ASP A 1 143 ? 3.805  34.822 24.713 1.00 86.14 ? 138 ASP A CB  1 
ATOM   1068 C  CG  . ASP A 1 143 ? 2.326  35.089 24.560 1.00 82.92 ? 138 ASP A CG  1 
ATOM   1069 O  OD1 . ASP A 1 143 ? 1.579  34.142 24.228 1.00 84.01 ? 138 ASP A OD1 1 
ATOM   1070 O  OD2 . ASP A 1 143 ? 1.913  36.253 24.764 1.00 78.45 ? 138 ASP A OD2 1 
ATOM   1071 N  N   . ASP A 1 144 ? 6.511  33.056 25.298 1.00 79.25 ? 139 ASP A N   1 
ATOM   1072 C  CA  . ASP A 1 144 ? 7.869  32.714 24.900 1.00 78.24 ? 139 ASP A CA  1 
ATOM   1073 C  C   . ASP A 1 144 ? 7.947  31.279 24.389 1.00 72.57 ? 139 ASP A C   1 
ATOM   1074 O  O   . ASP A 1 144 ? 8.671  30.996 23.427 1.00 70.62 ? 139 ASP A O   1 
ATOM   1075 C  CB  . ASP A 1 144 ? 8.823  32.923 26.076 1.00 78.85 ? 139 ASP A CB  1 
ATOM   1076 C  CG  . ASP A 1 144 ? 10.222 33.296 25.630 1.00 80.04 ? 139 ASP A CG  1 
ATOM   1077 O  OD1 . ASP A 1 144 ? 10.388 33.655 24.440 1.00 81.51 ? 139 ASP A OD1 1 
ATOM   1078 O  OD2 . ASP A 1 144 ? 11.155 33.209 26.459 1.00 77.40 ? 139 ASP A OD2 1 
ATOM   1079 N  N   . LYS A 1 145 ? 7.174  30.368 24.993 1.00 73.84 ? 140 LYS A N   1 
ATOM   1080 C  CA  . LYS A 1 145 ? 7.341  28.942 24.720 1.00 69.86 ? 140 LYS A CA  1 
ATOM   1081 C  C   . LYS A 1 145 ? 6.976  28.591 23.283 1.00 68.56 ? 140 LYS A C   1 
ATOM   1082 O  O   . LYS A 1 145 ? 7.647  27.763 22.652 1.00 64.10 ? 140 LYS A O   1 
ATOM   1083 C  CB  . LYS A 1 145 ? 6.501  28.115 25.692 1.00 69.75 ? 140 LYS A CB  1 
ATOM   1084 C  CG  . LYS A 1 145 ? 6.562  26.620 25.422 1.00 67.05 ? 140 LYS A CG  1 
ATOM   1085 C  CD  . LYS A 1 145 ? 6.737  25.808 26.695 1.00 65.59 ? 140 LYS A CD  1 
ATOM   1086 C  CE  . LYS A 1 145 ? 6.702  24.315 26.398 1.00 62.37 ? 140 LYS A CE  1 
ATOM   1087 N  NZ  . LYS A 1 145 ? 5.409  23.708 26.813 1.00 65.33 ? 140 LYS A NZ  1 
ATOM   1088 N  N   . LYS A 1 146 ? 5.905  29.186 22.755 1.00 70.23 ? 141 LYS A N   1 
ATOM   1089 C  CA  . LYS A 1 146 ? 5.560  28.964 21.355 1.00 69.19 ? 141 LYS A CA  1 
ATOM   1090 C  C   . LYS A 1 146 ? 6.686  29.432 20.443 1.00 64.92 ? 141 LYS A C   1 
ATOM   1091 O  O   . LYS A 1 146 ? 7.141  28.687 19.571 1.00 65.38 ? 141 LYS A O   1 
ATOM   1092 C  CB  . LYS A 1 146 ? 4.251  29.681 21.009 1.00 72.99 ? 141 LYS A CB  1 
ATOM   1093 C  CG  . LYS A 1 146 ? 3.030  29.190 21.779 1.00 75.70 ? 141 LYS A CG  1 
ATOM   1094 C  CD  . LYS A 1 146 ? 1.735  29.717 21.160 1.00 79.22 ? 141 LYS A CD  1 
ATOM   1095 C  CE  . LYS A 1 146 ? 0.559  29.571 22.118 1.00 80.41 ? 141 LYS A CE  1 
ATOM   1096 N  NZ  . LYS A 1 146 ? 0.437  28.186 22.657 1.00 81.75 ? 141 LYS A NZ  1 
ATOM   1097 N  N   . ARG A 1 147 ? 7.162  30.665 20.650 1.00 66.26 ? 142 ARG A N   1 
ATOM   1098 C  CA  . ARG A 1 147 ? 8.252  31.198 19.837 1.00 66.06 ? 142 ARG A CA  1 
ATOM   1099 C  C   . ARG A 1 147 ? 9.469  30.273 19.861 1.00 62.30 ? 142 ARG A C   1 
ATOM   1100 O  O   . ARG A 1 147 ? 10.062 29.984 18.813 1.00 58.52 ? 142 ARG A O   1 
ATOM   1101 C  CB  . ARG A 1 147 ? 8.637  32.599 20.327 1.00 69.34 ? 142 ARG A CB  1 
ATOM   1102 C  CG  . ARG A 1 147 ? 7.584  33.688 20.078 1.00 72.35 ? 142 ARG A CG  1 
ATOM   1103 C  CD  . ARG A 1 147 ? 8.209  35.089 20.102 1.00 74.73 ? 142 ARG A CD  1 
ATOM   1104 N  NE  . ARG A 1 147 ? 8.261  35.703 21.429 1.00 77.44 ? 142 ARG A NE  1 
ATOM   1105 C  CZ  . ARG A 1 147 ? 7.214  36.133 22.124 1.00 76.27 ? 142 ARG A CZ  1 
ATOM   1106 N  NH1 . ARG A 1 147 ? 5.984  36.070 21.640 1.00 74.01 ? 142 ARG A NH1 1 
ATOM   1107 N  NH2 . ARG A 1 147 ? 7.409  36.652 23.333 1.00 76.91 ? 142 ARG A NH2 1 
ATOM   1108 N  N   . ILE A 1 148 ? 9.835  29.775 21.046 1.00 62.74 ? 143 ILE A N   1 
ATOM   1109 C  CA  . ILE A 1 148 ? 11.026 28.936 21.171 1.00 61.07 ? 143 ILE A CA  1 
ATOM   1110 C  C   . ILE A 1 148 ? 10.838 27.603 20.457 1.00 58.61 ? 143 ILE A C   1 
ATOM   1111 O  O   . ILE A 1 148 ? 11.736 27.134 19.750 1.00 56.13 ? 143 ILE A O   1 
ATOM   1112 C  CB  . ILE A 1 148 ? 11.402 28.720 22.650 1.00 57.94 ? 143 ILE A CB  1 
ATOM   1113 C  CG1 . ILE A 1 148 ? 11.899 30.007 23.305 1.00 61.50 ? 143 ILE A CG1 1 
ATOM   1114 C  CG2 . ILE A 1 148 ? 12.418 27.601 22.794 1.00 53.34 ? 143 ILE A CG2 1 
ATOM   1115 C  CD1 . ILE A 1 148 ? 11.289 30.258 24.657 1.00 64.96 ? 143 ILE A CD1 1 
ATOM   1116 N  N   . ILE A 1 149 ? 9.684  26.959 20.648 1.00 58.23 ? 144 ILE A N   1 
ATOM   1117 C  CA  . ILE A 1 149 ? 9.470  25.639 20.056 1.00 57.47 ? 144 ILE A CA  1 
ATOM   1118 C  C   . ILE A 1 149 ? 9.530  25.710 18.530 1.00 58.01 ? 144 ILE A C   1 
ATOM   1119 O  O   . ILE A 1 149 ? 10.134 24.850 17.878 1.00 57.36 ? 144 ILE A O   1 
ATOM   1120 C  CB  . ILE A 1 149 ? 8.142  25.040 20.551 1.00 58.61 ? 144 ILE A CB  1 
ATOM   1121 C  CG1 . ILE A 1 149 ? 8.249  24.690 22.041 1.00 58.17 ? 144 ILE A CG1 1 
ATOM   1122 C  CG2 . ILE A 1 149 ? 7.769  23.820 19.727 1.00 58.59 ? 144 ILE A CG2 1 
ATOM   1123 C  CD1 . ILE A 1 149 ? 7.285  23.623 22.498 1.00 56.36 ? 144 ILE A CD1 1 
ATOM   1124 N  N   . ASP A 1 150 ? 8.927  26.741 17.937 1.00 58.06 ? 145 ASP A N   1 
ATOM   1125 C  CA  . ASP A 1 150 ? 9.003  26.868 16.483 1.00 59.20 ? 145 ASP A CA  1 
ATOM   1126 C  C   . ASP A 1 150 ? 10.418 27.187 16.022 1.00 57.03 ? 145 ASP A C   1 
ATOM   1127 O  O   . ASP A 1 150 ? 10.823 26.757 14.936 1.00 56.06 ? 145 ASP A O   1 
ATOM   1128 C  CB  . ASP A 1 150 ? 8.034  27.936 15.969 1.00 62.84 ? 145 ASP A CB  1 
ATOM   1129 C  CG  . ASP A 1 150 ? 6.584  27.614 16.281 1.00 66.40 ? 145 ASP A CG  1 
ATOM   1130 O  OD1 . ASP A 1 150 ? 5.822  28.549 16.615 1.00 69.73 ? 145 ASP A OD1 1 
ATOM   1131 O  OD2 . ASP A 1 150 ? 6.209  26.422 16.207 1.00 66.89 ? 145 ASP A OD2 1 
ATOM   1132 N  N   . SER A 1 151 ? 11.184 27.928 16.827 1.00 56.51 ? 146 SER A N   1 
ATOM   1133 C  CA  . SER A 1 151 ? 12.558 28.236 16.448 1.00 54.81 ? 146 SER A CA  1 
ATOM   1134 C  C   . SER A 1 151 ? 13.418 26.982 16.442 1.00 53.78 ? 146 SER A C   1 
ATOM   1135 O  O   . SER A 1 151 ? 14.239 26.793 15.537 1.00 52.83 ? 146 SER A O   1 
ATOM   1136 C  CB  . SER A 1 151 ? 13.147 29.289 17.385 1.00 52.92 ? 146 SER A CB  1 
ATOM   1137 O  OG  . SER A 1 151 ? 12.550 30.555 17.164 1.00 56.35 ? 146 SER A OG  1 
ATOM   1138 N  N   . ALA A 1 152 ? 13.246 26.116 17.446 1.00 53.26 ? 147 ALA A N   1 
ATOM   1139 C  CA  . ALA A 1 152 ? 13.961 24.844 17.464 1.00 52.13 ? 147 ALA A CA  1 
ATOM   1140 C  C   . ALA A 1 152 ? 13.614 24.002 16.243 1.00 52.45 ? 147 ALA A C   1 
ATOM   1141 O  O   . ALA A 1 152 ? 14.505 23.499 15.550 1.00 48.93 ? 147 ALA A O   1 
ATOM   1142 C  CB  . ALA A 1 152 ? 13.640 24.076 18.744 1.00 48.61 ? 147 ALA A CB  1 
ATOM   1143 N  N   . ARG A 1 153 ? 12.318 23.831 15.970 1.00 51.49 ? 148 ARG A N   1 
ATOM   1144 C  CA  . ARG A 1 153 ? 11.913 22.992 14.845 1.00 52.68 ? 148 ARG A CA  1 
ATOM   1145 C  C   . ARG A 1 153 ? 12.479 23.519 13.532 1.00 52.46 ? 148 ARG A C   1 
ATOM   1146 O  O   . ARG A 1 153 ? 12.994 22.742 12.718 1.00 52.35 ? 148 ARG A O   1 
ATOM   1147 C  CB  . ARG A 1 153 ? 10.388 22.885 14.772 1.00 55.42 ? 148 ARG A CB  1 
ATOM   1148 C  CG  . ARG A 1 153 ? 9.892  22.027 13.604 1.00 57.72 ? 148 ARG A CG  1 
ATOM   1149 C  CD  . ARG A 1 153 ? 8.369  21.998 13.488 1.00 59.82 ? 148 ARG A CD  1 
ATOM   1150 N  NE  . ARG A 1 153 ? 7.720  21.523 14.706 1.00 60.02 ? 148 ARG A NE  1 
ATOM   1151 C  CZ  . ARG A 1 153 ? 7.008  22.294 15.517 1.00 61.24 ? 148 ARG A CZ  1 
ATOM   1152 N  NH1 . ARG A 1 153 ? 6.867  23.590 15.290 1.00 63.33 ? 148 ARG A NH1 1 
ATOM   1153 N  NH2 . ARG A 1 153 ? 6.418  21.751 16.577 1.00 61.47 ? 148 ARG A NH2 1 
ATOM   1154 N  N   . SER A 1 154 ? 12.405 24.837 13.308 1.00 52.21 ? 149 SER A N   1 
ATOM   1155 C  CA  . SER A 1 154 ? 12.891 25.393 12.045 1.00 53.42 ? 149 SER A CA  1 
ATOM   1156 C  C   . SER A 1 154 ? 14.387 25.161 11.878 1.00 51.14 ? 149 SER A C   1 
ATOM   1157 O  O   . SER A 1 154 ? 14.852 24.845 10.776 1.00 49.48 ? 149 SER A O   1 
ATOM   1158 C  CB  . SER A 1 154 ? 12.571 26.888 11.949 1.00 57.86 ? 149 SER A CB  1 
ATOM   1159 O  OG  . SER A 1 154 ? 11.211 27.159 12.250 1.00 60.69 ? 149 SER A OG  1 
ATOM   1160 N  N   . ALA A 1 155 ? 15.155 25.301 12.960 1.00 51.41 ? 150 ALA A N   1 
ATOM   1161 C  CA  . ALA A 1 155 ? 16.593 25.077 12.866 1.00 49.35 ? 150 ALA A CA  1 
ATOM   1162 C  C   . ALA A 1 155 ? 16.897 23.610 12.598 1.00 48.30 ? 150 ALA A C   1 
ATOM   1163 O  O   . ALA A 1 155 ? 17.750 23.291 11.762 1.00 45.76 ? 150 ALA A O   1 
ATOM   1164 C  CB  . ALA A 1 155 ? 17.292 25.556 14.143 1.00 46.19 ? 150 ALA A CB  1 
ATOM   1165 N  N   . TYR A 1 156 ? 16.211 22.703 13.300 1.00 46.44 ? 151 TYR A N   1 
ATOM   1166 C  CA  . TYR A 1 156 ? 16.400 21.281 13.045 1.00 46.50 ? 151 TYR A CA  1 
ATOM   1167 C  C   . TYR A 1 156 ? 16.020 20.937 11.614 1.00 48.25 ? 151 TYR A C   1 
ATOM   1168 O  O   . TYR A 1 156 ? 16.729 20.184 10.938 1.00 46.11 ? 151 TYR A O   1 
ATOM   1169 C  CB  . TYR A 1 156 ? 15.561 20.441 14.006 1.00 45.80 ? 151 TYR A CB  1 
ATOM   1170 C  CG  . TYR A 1 156 ? 16.132 20.263 15.409 1.00 44.57 ? 151 TYR A CG  1 
ATOM   1171 C  CD1 . TYR A 1 156 ? 17.470 19.943 15.610 1.00 42.15 ? 151 TYR A CD1 1 
ATOM   1172 C  CD2 . TYR A 1 156 ? 15.314 20.387 16.519 1.00 46.15 ? 151 TYR A CD2 1 
ATOM   1173 C  CE1 . TYR A 1 156 ? 17.987 19.768 16.906 1.00 41.06 ? 151 TYR A CE1 1 
ATOM   1174 C  CE2 . TYR A 1 156 ? 15.815 20.216 17.807 1.00 42.72 ? 151 TYR A CE2 1 
ATOM   1175 C  CZ  . TYR A 1 156 ? 17.148 19.905 17.995 1.00 42.47 ? 151 TYR A CZ  1 
ATOM   1176 O  OH  . TYR A 1 156 ? 17.634 19.729 19.281 1.00 38.04 ? 151 TYR A OH  1 
ATOM   1177 N  N   . GLN A 1 157 ? 14.898 21.477 11.138 1.00 49.00 ? 152 GLN A N   1 
ATOM   1178 C  CA  . GLN A 1 157 ? 14.433 21.131 9.800  1.00 50.43 ? 152 GLN A CA  1 
ATOM   1179 C  C   . GLN A 1 157 ? 15.412 21.617 8.742  1.00 50.90 ? 152 GLN A C   1 
ATOM   1180 O  O   . GLN A 1 157 ? 15.705 20.889 7.786  1.00 48.54 ? 152 GLN A O   1 
ATOM   1181 C  CB  . GLN A 1 157 ? 13.036 21.702 9.552  1.00 51.64 ? 152 GLN A CB  1 
ATOM   1182 C  CG  . GLN A 1 157 ? 12.302 21.082 8.354  1.00 58.43 ? 152 GLN A CG  1 
ATOM   1183 C  CD  . GLN A 1 157 ? 12.214 19.560 8.427  1.00 60.00 ? 152 GLN A CD  1 
ATOM   1184 O  OE1 . GLN A 1 157 ? 12.828 18.853 7.626  1.00 63.15 ? 152 GLN A OE1 1 
ATOM   1185 N  NE2 . GLN A 1 157 ? 11.457 19.052 9.400  1.00 61.32 ? 152 GLN A NE2 1 
ATOM   1186 N  N   . GLU A 1 158 ? 15.957 22.827 8.902  1.00 47.96 ? 153 GLU A N   1 
ATOM   1187 C  CA  . GLU A 1 158 ? 16.922 23.281 7.909  1.00 51.18 ? 153 GLU A CA  1 
ATOM   1188 C  C   . GLU A 1 158 ? 18.161 22.397 7.932  1.00 49.89 ? 153 GLU A C   1 
ATOM   1189 O  O   . GLU A 1 158 ? 18.711 22.058 6.880  1.00 46.70 ? 153 GLU A O   1 
ATOM   1190 C  CB  . GLU A 1 158 ? 17.297 24.748 8.125  1.00 50.86 ? 153 GLU A CB  1 
ATOM   1191 C  CG  . GLU A 1 158 ? 18.164 25.247 6.972  1.00 56.42 ? 153 GLU A CG  1 
ATOM   1192 C  CD  . GLU A 1 158 ? 18.578 26.705 7.057  1.00 59.74 ? 153 GLU A CD  1 
ATOM   1193 O  OE1 . GLU A 1 158 ? 18.152 27.418 7.995  1.00 57.69 ? 153 GLU A OE1 1 
ATOM   1194 O  OE2 . GLU A 1 158 ? 19.307 27.139 6.133  1.00 60.78 ? 153 GLU A OE2 1 
ATOM   1195 N  N   . ALA A 1 159 ? 18.580 21.975 9.128  1.00 46.42 ? 154 ALA A N   1 
ATOM   1196 C  CA  . ALA A 1 159 ? 19.727 21.083 9.236  1.00 47.42 ? 154 ALA A CA  1 
ATOM   1197 C  C   . ALA A 1 159 ? 19.439 19.733 8.586  1.00 46.61 ? 154 ALA A C   1 
ATOM   1198 O  O   . ALA A 1 159 ? 20.308 19.171 7.912  1.00 42.33 ? 154 ALA A O   1 
ATOM   1199 C  CB  . ALA A 1 159 ? 20.125 20.911 10.705 1.00 44.05 ? 154 ALA A CB  1 
ATOM   1200 N  N   . MET A 1 160 ? 18.229 19.192 8.777  1.00 44.68 ? 155 MET A N   1 
ATOM   1201 C  CA  . MET A 1 160 ? 17.890 17.924 8.133  1.00 46.70 ? 155 MET A CA  1 
ATOM   1202 C  C   . MET A 1 160 ? 17.880 18.032 6.612  1.00 47.07 ? 155 MET A C   1 
ATOM   1203 O  O   . MET A 1 160 ? 18.399 17.142 5.929  1.00 47.93 ? 155 MET A O   1 
ATOM   1204 C  CB  . MET A 1 160 ? 16.553 17.379 8.635  1.00 47.37 ? 155 MET A CB  1 
ATOM   1205 C  CG  . MET A 1 160 ? 16.481 17.206 10.130 1.00 48.92 ? 155 MET A CG  1 
ATOM   1206 S  SD  . MET A 1 160 ? 16.981 15.512 10.524 1.00 48.66 ? 155 MET A SD  1 
ATOM   1207 C  CE  . MET A 1 160 ? 16.293 14.594 9.150  1.00 51.64 ? 155 MET A CE  1 
ATOM   1208 N  N   . ASP A 1 161 ? 17.279 19.094 6.060  1.00 48.53 ? 156 ASP A N   1 
ATOM   1209 C  CA  . ASP A 1 161 ? 17.271 19.240 4.603  1.00 48.60 ? 156 ASP A CA  1 
ATOM   1210 C  C   . ASP A 1 161 ? 18.681 19.223 4.038  1.00 48.34 ? 156 ASP A C   1 
ATOM   1211 O  O   . ASP A 1 161 ? 18.939 18.569 3.019  1.00 49.93 ? 156 ASP A O   1 
ATOM   1212 C  CB  . ASP A 1 161 ? 16.542 20.515 4.176  1.00 53.87 ? 156 ASP A CB  1 
ATOM   1213 C  CG  . ASP A 1 161 ? 15.108 20.568 4.667  1.00 58.39 ? 156 ASP A CG  1 
ATOM   1214 O  OD1 . ASP A 1 161 ? 14.515 21.668 4.670  1.00 63.03 ? 156 ASP A OD1 1 
ATOM   1215 O  OD2 . ASP A 1 161 ? 14.558 19.497 5.005  1.00 62.14 ? 156 ASP A OD2 1 
ATOM   1216 N  N   . ILE A 1 162 ? 19.608 19.926 4.689  1.00 49.13 ? 157 ILE A N   1 
ATOM   1217 C  CA  . ILE A 1 162 ? 20.982 19.960 4.200  1.00 49.25 ? 157 ILE A CA  1 
ATOM   1218 C  C   . ILE A 1 162 ? 21.644 18.596 4.365  1.00 48.28 ? 157 ILE A C   1 
ATOM   1219 O  O   . ILE A 1 162 ? 22.306 18.099 3.450  1.00 47.33 ? 157 ILE A O   1 
ATOM   1220 C  CB  . ILE A 1 162 ? 21.779 21.067 4.911  1.00 48.11 ? 157 ILE A CB  1 
ATOM   1221 C  CG1 . ILE A 1 162 ? 21.226 22.453 4.560  1.00 51.78 ? 157 ILE A CG1 1 
ATOM   1222 C  CG2 . ILE A 1 162 ? 23.245 20.976 4.557  1.00 48.94 ? 157 ILE A CG2 1 
ATOM   1223 C  CD1 . ILE A 1 162 ? 21.576 23.514 5.599  1.00 51.97 ? 157 ILE A CD1 1 
ATOM   1224 N  N   . SER A 1 163 ? 21.476 17.964 5.534  1.00 44.00 ? 158 SER A N   1 
ATOM   1225 C  CA  . SER A 1 163 ? 22.164 16.697 5.770  1.00 43.88 ? 158 SER A CA  1 
ATOM   1226 C  C   . SER A 1 163 ? 21.709 15.604 4.808  1.00 45.46 ? 158 SER A C   1 
ATOM   1227 O  O   . SER A 1 163 ? 22.509 14.743 4.431  1.00 43.35 ? 158 SER A O   1 
ATOM   1228 C  CB  . SER A 1 163 ? 21.958 16.243 7.219  1.00 43.74 ? 158 SER A CB  1 
ATOM   1229 O  OG  . SER A 1 163 ? 20.639 15.759 7.411  1.00 46.19 ? 158 SER A OG  1 
ATOM   1230 N  N   . LYS A 1 164 ? 20.440 15.610 4.404  1.00 44.98 ? 159 LYS A N   1 
ATOM   1231 C  CA  . LYS A 1 164 ? 19.959 14.557 3.522  1.00 44.85 ? 159 LYS A CA  1 
ATOM   1232 C  C   . LYS A 1 164 ? 20.471 14.744 2.098  1.00 48.00 ? 159 LYS A C   1 
ATOM   1233 O  O   . LYS A 1 164 ? 20.605 13.769 1.357  1.00 46.19 ? 159 LYS A O   1 
ATOM   1234 C  CB  . LYS A 1 164 ? 18.435 14.520 3.541  1.00 48.47 ? 159 LYS A CB  1 
ATOM   1235 C  CG  . LYS A 1 164 ? 17.840 14.017 4.845  1.00 48.33 ? 159 LYS A CG  1 
ATOM   1236 C  CD  . LYS A 1 164 ? 16.408 13.536 4.633  1.00 54.94 ? 159 LYS A CD  1 
ATOM   1237 C  CE  . LYS A 1 164 ? 15.487 14.025 5.740  1.00 55.53 ? 159 LYS A CE  1 
ATOM   1238 N  NZ  . LYS A 1 164 ? 14.661 15.171 5.254  1.00 59.44 ? 159 LYS A NZ  1 
ATOM   1239 N  N   . LYS A 1 165 ? 20.788 15.977 1.718  1.00 47.09 ? 160 LYS A N   1 
ATOM   1240 C  CA  . LYS A 1 165 ? 21.233 16.298 0.369  1.00 50.21 ? 160 LYS A CA  1 
ATOM   1241 C  C   . LYS A 1 165 ? 22.747 16.223 0.211  1.00 49.64 ? 160 LYS A C   1 
ATOM   1242 O  O   . LYS A 1 165 ? 23.241 15.888 -0.876 1.00 47.26 ? 160 LYS A O   1 
ATOM   1243 C  CB  . LYS A 1 165 ? 20.737 17.698 0.001  1.00 51.84 ? 160 LYS A CB  1 
ATOM   1244 C  CG  . LYS A 1 165 ? 19.277 17.716 -0.414 1.00 60.20 ? 160 LYS A CG  1 
ATOM   1245 C  CD  . LYS A 1 165 ? 18.802 19.111 -0.820 1.00 68.35 ? 160 LYS A CD  1 
ATOM   1246 C  CE  . LYS A 1 165 ? 17.343 19.343 -0.425 1.00 71.56 ? 160 LYS A CE  1 
ATOM   1247 N  NZ  . LYS A 1 165 ? 16.969 20.788 -0.408 1.00 72.79 ? 160 LYS A NZ  1 
ATOM   1248 N  N   . GLU A 1 166 ? 23.480 16.485 1.287  1.00 46.62 ? 161 GLU A N   1 
ATOM   1249 C  CA  . GLU A 1 166 ? 24.913 16.733 1.278  1.00 47.31 ? 161 GLU A CA  1 
ATOM   1250 C  C   . GLU A 1 166 ? 25.725 15.657 1.987  1.00 47.49 ? 161 GLU A C   1 
ATOM   1251 O  O   . GLU A 1 166 ? 26.954 15.653 1.857  1.00 48.82 ? 161 GLU A O   1 
ATOM   1252 C  CB  . GLU A 1 166 ? 25.187 18.077 1.966  1.00 50.49 ? 161 GLU A CB  1 
ATOM   1253 C  CG  . GLU A 1 166 ? 24.247 19.220 1.576  1.00 54.36 ? 161 GLU A CG  1 
ATOM   1254 C  CD  . GLU A 1 166 ? 24.951 20.467 1.097  1.00 56.77 ? 161 GLU A CD  1 
ATOM   1255 O  OE1 . GLU A 1 166 ? 26.194 20.454 0.972  1.00 58.33 ? 161 GLU A OE1 1 
ATOM   1256 O  OE2 . GLU A 1 166 ? 24.251 21.491 0.912  1.00 57.51 ? 161 GLU A OE2 1 
ATOM   1257 N  N   . MET A 1 167 ? 25.087 14.761 2.741  1.00 44.52 ? 162 MET A N   1 
ATOM   1258 C  CA  . MET A 1 167 ? 25.808 13.890 3.656  1.00 42.61 ? 162 MET A CA  1 
ATOM   1259 C  C   . MET A 1 167 ? 25.360 12.445 3.490  1.00 42.01 ? 162 MET A C   1 
ATOM   1260 O  O   . MET A 1 167 ? 24.170 12.191 3.252  1.00 40.85 ? 162 MET A O   1 
ATOM   1261 C  CB  . MET A 1 167 ? 25.541 14.333 5.104  1.00 43.50 ? 162 MET A CB  1 
ATOM   1262 C  CG  . MET A 1 167 ? 26.348 15.517 5.562  1.00 43.70 ? 162 MET A CG  1 
ATOM   1263 S  SD  . MET A 1 167 ? 25.846 15.953 7.241  1.00 46.74 ? 162 MET A SD  1 
ATOM   1264 C  CE  . MET A 1 167 ? 27.359 16.700 7.819  1.00 45.99 ? 162 MET A CE  1 
ATOM   1265 N  N   . PRO A 1 168 ? 26.268 11.473 3.638  1.00 40.63 ? 163 PRO A N   1 
ATOM   1266 C  CA  . PRO A 1 168 ? 25.835 10.078 3.631  1.00 43.85 ? 163 PRO A CA  1 
ATOM   1267 C  C   . PRO A 1 168 ? 24.962 9.785  4.836  1.00 39.80 ? 163 PRO A C   1 
ATOM   1268 O  O   . PRO A 1 168 ? 25.072 10.451 5.882  1.00 41.87 ? 163 PRO A O   1 
ATOM   1269 C  CB  . PRO A 1 168 ? 27.158 9.292  3.692  1.00 42.57 ? 163 PRO A CB  1 
ATOM   1270 C  CG  . PRO A 1 168 ? 28.092 10.207 4.349  1.00 40.68 ? 163 PRO A CG  1 
ATOM   1271 C  CD  . PRO A 1 168 ? 27.712 11.596 3.874  1.00 43.58 ? 163 PRO A CD  1 
ATOM   1272 N  N   . PRO A 1 169 ? 24.087 8.785  4.740  1.00 39.58 ? 164 PRO A N   1 
ATOM   1273 C  CA  . PRO A 1 169 ? 23.171 8.499  5.849  1.00 41.51 ? 164 PRO A CA  1 
ATOM   1274 C  C   . PRO A 1 169 ? 23.851 7.930  7.088  1.00 39.53 ? 164 PRO A C   1 
ATOM   1275 O  O   . PRO A 1 169 ? 23.175 7.814  8.111  1.00 42.37 ? 164 PRO A O   1 
ATOM   1276 C  CB  . PRO A 1 169 ? 22.185 7.492  5.240  1.00 43.83 ? 164 PRO A CB  1 
ATOM   1277 C  CG  . PRO A 1 169 ? 22.873 6.933  4.078  1.00 44.39 ? 164 PRO A CG  1 
ATOM   1278 C  CD  . PRO A 1 169 ? 23.831 7.938  3.563  1.00 43.40 ? 164 PRO A CD  1 
ATOM   1279 N  N   . THR A 1 170 ? 25.141 7.576  7.041  1.00 38.37 ? 165 THR A N   1 
ATOM   1280 C  CA  . THR A 1 170 ? 25.876 7.213  8.260  1.00 39.42 ? 165 THR A CA  1 
ATOM   1281 C  C   . THR A 1 170 ? 26.692 8.358  8.836  1.00 38.47 ? 165 THR A C   1 
ATOM   1282 O  O   . THR A 1 170 ? 27.375 8.165  9.858  1.00 36.46 ? 165 THR A O   1 
ATOM   1283 C  CB  . THR A 1 170 ? 26.841 6.059  8.006  1.00 38.32 ? 165 THR A CB  1 
ATOM   1284 O  OG1 . THR A 1 170 ? 27.795 6.474  7.027  1.00 41.10 ? 165 THR A OG1 1 
ATOM   1285 C  CG2 . THR A 1 170 ? 26.110 4.787  7.554  1.00 38.67 ? 165 THR A CG2 1 
ATOM   1286 N  N   . ASN A 1 171 ? 26.681 9.525  8.216  1.00 36.77 ? 166 ASN A N   1 
ATOM   1287 C  CA  . ASN A 1 171 ? 27.495 10.618 8.741  1.00 37.39 ? 166 ASN A CA  1 
ATOM   1288 C  C   . ASN A 1 171 ? 27.110 10.914 10.191 1.00 38.17 ? 166 ASN A C   1 
ATOM   1289 O  O   . ASN A 1 171 ? 25.922 11.105 10.487 1.00 37.56 ? 166 ASN A O   1 
ATOM   1290 C  CB  . ASN A 1 171 ? 27.340 11.872 7.893  1.00 38.73 ? 166 ASN A CB  1 
ATOM   1291 C  CG  . ASN A 1 171 ? 28.080 13.064 8.492  1.00 38.56 ? 166 ASN A CG  1 
ATOM   1292 O  OD1 . ASN A 1 171 ? 27.610 13.684 9.447  1.00 38.93 ? 166 ASN A OD1 1 
ATOM   1293 N  ND2 . ASN A 1 171 ? 29.248 13.374 7.939  1.00 39.40 ? 166 ASN A ND2 1 
ATOM   1294 N  N   . PRO A 1 172 ? 28.076 10.969 11.115 1.00 35.96 ? 167 PRO A N   1 
ATOM   1295 C  CA  . PRO A 1 172 ? 27.725 11.096 12.546 1.00 37.67 ? 167 PRO A CA  1 
ATOM   1296 C  C   . PRO A 1 172 ? 27.015 12.393 12.902 1.00 37.82 ? 167 PRO A C   1 
ATOM   1297 O  O   . PRO A 1 172 ? 26.186 12.401 13.821 1.00 37.29 ? 167 PRO A O   1 
ATOM   1298 C  CB  . PRO A 1 172 ? 29.083 10.987 13.260 1.00 39.40 ? 167 PRO A CB  1 
ATOM   1299 C  CG  . PRO A 1 172 ? 30.117 11.309 12.225 1.00 41.59 ? 167 PRO A CG  1 
ATOM   1300 C  CD  . PRO A 1 172 ? 29.530 10.882 10.884 1.00 36.14 ? 167 PRO A CD  1 
ATOM   1301 N  N   . ILE A 1 173 ? 27.310 13.493 12.206 1.00 36.00 ? 168 ILE A N   1 
ATOM   1302 C  CA  . ILE A 1 173 ? 26.572 14.726 12.446 1.00 37.04 ? 168 ILE A CA  1 
ATOM   1303 C  C   . ILE A 1 173 ? 25.137 14.588 11.947 1.00 36.47 ? 168 ILE A C   1 
ATOM   1304 O  O   . ILE A 1 173 ? 24.186 15.007 12.618 1.00 36.64 ? 168 ILE A O   1 
ATOM   1305 C  CB  . ILE A 1 173 ? 27.305 15.913 11.794 1.00 37.26 ? 168 ILE A CB  1 
ATOM   1306 C  CG1 . ILE A 1 173 ? 28.726 16.032 12.353 1.00 38.11 ? 168 ILE A CG1 1 
ATOM   1307 C  CG2 . ILE A 1 173 ? 26.531 17.211 12.005 1.00 42.03 ? 168 ILE A CG2 1 
ATOM   1308 C  CD1 . ILE A 1 173 ? 29.557 17.135 11.699 1.00 43.11 ? 168 ILE A CD1 1 
ATOM   1309 N  N   . ARG A 1 174 ? 24.952 13.982 10.778 1.00 36.06 ? 169 ARG A N   1 
ATOM   1310 C  CA  . ARG A 1 174 ? 23.598 13.722 10.299 1.00 37.00 ? 169 ARG A CA  1 
ATOM   1311 C  C   . ARG A 1 174 ? 22.845 12.822 11.265 1.00 38.04 ? 169 ARG A C   1 
ATOM   1312 O  O   . ARG A 1 174 ? 21.681 13.078 11.589 1.00 38.29 ? 169 ARG A O   1 
ATOM   1313 C  CB  . ARG A 1 174 ? 23.646 13.085 8.905  1.00 36.24 ? 169 ARG A CB  1 
ATOM   1314 C  CG  . ARG A 1 174 ? 22.297 12.641 8.381  1.00 38.44 ? 169 ARG A CG  1 
ATOM   1315 C  CD  . ARG A 1 174 ? 22.371 12.262 6.878  1.00 39.66 ? 169 ARG A CD  1 
ATOM   1316 N  NE  . ARG A 1 174 ? 21.138 11.634 6.408  1.00 43.93 ? 169 ARG A NE  1 
ATOM   1317 C  CZ  . ARG A 1 174 ? 20.925 11.227 5.164  1.00 44.35 ? 169 ARG A CZ  1 
ATOM   1318 N  NH1 . ARG A 1 174 ? 21.856 11.346 4.229  1.00 42.54 ? 169 ARG A NH1 1 
ATOM   1319 N  NH2 . ARG A 1 174 ? 19.753 10.677 4.850  1.00 44.41 ? 169 ARG A NH2 1 
ATOM   1320 N  N   . LEU A 1 175 ? 23.501 11.766 11.742 1.00 37.65 ? 170 LEU A N   1 
ATOM   1321 C  CA  . LEU A 1 175 ? 22.868 10.863 12.698 1.00 36.74 ? 170 LEU A CA  1 
ATOM   1322 C  C   . LEU A 1 175 ? 22.542 11.579 14.011 1.00 36.95 ? 170 LEU A C   1 
ATOM   1323 O  O   . LEU A 1 175 ? 21.420 11.482 14.521 1.00 36.51 ? 170 LEU A O   1 
ATOM   1324 C  CB  . LEU A 1 175 ? 23.783 9.671  12.946 1.00 36.64 ? 170 LEU A CB  1 
ATOM   1325 C  CG  . LEU A 1 175 ? 23.951 8.728  11.752 1.00 37.14 ? 170 LEU A CG  1 
ATOM   1326 C  CD1 . LEU A 1 175 ? 25.000 7.683  12.087 1.00 38.85 ? 170 LEU A CD1 1 
ATOM   1327 C  CD2 . LEU A 1 175 ? 22.618 8.103  11.440 1.00 37.89 ? 170 LEU A CD2 1 
ATOM   1328 N  N   . GLY A 1 176 ? 23.515 12.295 14.577 1.00 34.47 ? 171 GLY A N   1 
ATOM   1329 C  CA  . GLY A 1 176 ? 23.269 12.979 15.846 1.00 38.63 ? 171 GLY A CA  1 
ATOM   1330 C  C   . GLY A 1 176 ? 22.169 14.019 15.737 1.00 38.63 ? 171 GLY A C   1 
ATOM   1331 O  O   . GLY A 1 176 ? 21.359 14.185 16.654 1.00 37.04 ? 171 GLY A O   1 
ATOM   1332 N  N   . LEU A 1 177 ? 22.128 14.738 14.613 1.00 37.81 ? 172 LEU A N   1 
ATOM   1333 C  CA  . LEU A 1 177 ? 21.034 15.667 14.363 1.00 38.76 ? 172 LEU A CA  1 
ATOM   1334 C  C   . LEU A 1 177 ? 19.688 14.947 14.353 1.00 39.57 ? 172 LEU A C   1 
ATOM   1335 O  O   . LEU A 1 177 ? 18.737 15.387 15.006 1.00 40.35 ? 172 LEU A O   1 
ATOM   1336 C  CB  . LEU A 1 177 ? 21.267 16.398 13.038 1.00 37.48 ? 172 LEU A CB  1 
ATOM   1337 C  CG  . LEU A 1 177 ? 20.013 16.992 12.416 1.00 40.86 ? 172 LEU A CG  1 
ATOM   1338 C  CD1 . LEU A 1 177 ? 19.519 18.171 13.247 1.00 39.88 ? 172 LEU A CD1 1 
ATOM   1339 C  CD2 . LEU A 1 177 ? 20.310 17.424 10.975 1.00 41.84 ? 172 LEU A CD2 1 
ATOM   1340 N  N   . ALA A 1 178 ? 19.581 13.843 13.604 1.00 38.96 ? 173 ALA A N   1 
ATOM   1341 C  CA  . ALA A 1 178 ? 18.306 13.127 13.548 1.00 39.83 ? 173 ALA A CA  1 
ATOM   1342 C  C   . ALA A 1 178 ? 17.930 12.575 14.916 1.00 41.28 ? 173 ALA A C   1 
ATOM   1343 O  O   . ALA A 1 178 ? 16.767 12.663 15.335 1.00 42.90 ? 173 ALA A O   1 
ATOM   1344 C  CB  . ALA A 1 178 ? 18.366 12.011 12.503 1.00 41.05 ? 173 ALA A CB  1 
ATOM   1345 N  N   . LEU A 1 179 ? 18.899 12.005 15.630 1.00 38.42 ? 174 LEU A N   1 
ATOM   1346 C  CA  . LEU A 1 179 ? 18.641 11.580 17.001 1.00 39.88 ? 174 LEU A CA  1 
ATOM   1347 C  C   . LEU A 1 179 ? 18.071 12.730 17.825 1.00 40.79 ? 174 LEU A C   1 
ATOM   1348 O  O   . LEU A 1 179 ? 17.051 12.572 18.501 1.00 41.22 ? 174 LEU A O   1 
ATOM   1349 C  CB  . LEU A 1 179 ? 19.920 11.057 17.654 1.00 39.98 ? 174 LEU A CB  1 
ATOM   1350 C  CG  . LEU A 1 179 ? 19.768 10.674 19.146 1.00 38.03 ? 174 LEU A CG  1 
ATOM   1351 C  CD1 . LEU A 1 179 ? 18.892 9.430  19.280 1.00 41.41 ? 174 LEU A CD1 1 
ATOM   1352 C  CD2 . LEU A 1 179 ? 21.124 10.442 19.752 1.00 36.55 ? 174 LEU A CD2 1 
ATOM   1353 N  N   . ASN A 1 180 ? 18.700 13.910 17.756 1.00 37.95 ? 175 ASN A N   1 
ATOM   1354 C  CA  . ASN A 1 180 ? 18.256 15.010 18.615 1.00 39.76 ? 175 ASN A CA  1 
ATOM   1355 C  C   . ASN A 1 180 ? 16.921 15.569 18.147 1.00 42.53 ? 175 ASN A C   1 
ATOM   1356 O  O   . ASN A 1 180 ? 16.086 15.965 18.969 1.00 40.95 ? 175 ASN A O   1 
ATOM   1357 C  CB  . ASN A 1 180 ? 19.311 16.118 18.675 1.00 37.10 ? 175 ASN A CB  1 
ATOM   1358 C  CG  . ASN A 1 180 ? 20.458 15.764 19.589 1.00 40.54 ? 175 ASN A CG  1 
ATOM   1359 O  OD1 . ASN A 1 180 ? 20.590 14.613 20.005 1.00 37.33 ? 175 ASN A OD1 1 
ATOM   1360 N  ND2 . ASN A 1 180 ? 21.291 16.750 19.920 1.00 36.55 ? 175 ASN A ND2 1 
ATOM   1361 N  N   . PHE A 1 181 ? 16.700 15.615 16.828 1.00 41.22 ? 176 PHE A N   1 
ATOM   1362 C  CA  . PHE A 1 181 ? 15.395 16.019 16.322 1.00 44.12 ? 176 PHE A CA  1 
ATOM   1363 C  C   . PHE A 1 181 ? 14.304 15.066 16.796 1.00 44.70 ? 176 PHE A C   1 
ATOM   1364 O  O   . PHE A 1 181 ? 13.191 15.500 17.117 1.00 46.48 ? 176 PHE A O   1 
ATOM   1365 C  CB  . PHE A 1 181 ? 15.431 16.092 14.790 1.00 42.21 ? 176 PHE A CB  1 
ATOM   1366 C  CG  . PHE A 1 181 ? 14.334 16.928 14.182 1.00 46.86 ? 176 PHE A CG  1 
ATOM   1367 C  CD1 . PHE A 1 181 ? 13.580 17.798 14.952 1.00 49.21 ? 176 PHE A CD1 1 
ATOM   1368 C  CD2 . PHE A 1 181 ? 14.065 16.844 12.818 1.00 48.21 ? 176 PHE A CD2 1 
ATOM   1369 C  CE1 . PHE A 1 181 ? 12.575 18.571 14.375 1.00 49.72 ? 176 PHE A CE1 1 
ATOM   1370 C  CE2 . PHE A 1 181 ? 13.064 17.611 12.240 1.00 50.49 ? 176 PHE A CE2 1 
ATOM   1371 C  CZ  . PHE A 1 181 ? 12.317 18.474 13.015 1.00 51.05 ? 176 PHE A CZ  1 
ATOM   1372 N  N   . SER A 1 182 ? 14.594 13.761 16.846 1.00 45.13 ? 177 SER A N   1 
ATOM   1373 C  CA  . SER A 1 182 ? 13.561 12.828 17.288 1.00 47.53 ? 177 SER A CA  1 
ATOM   1374 C  C   . SER A 1 182 ? 13.266 13.012 18.774 1.00 46.37 ? 177 SER A C   1 
ATOM   1375 O  O   . SER A 1 182 ? 12.110 12.901 19.197 1.00 49.01 ? 177 SER A O   1 
ATOM   1376 C  CB  . SER A 1 182 ? 13.946 11.376 16.964 1.00 47.02 ? 177 SER A CB  1 
ATOM   1377 O  OG  . SER A 1 182 ? 15.007 10.889 17.770 1.00 47.77 ? 177 SER A OG  1 
ATOM   1378 N  N   . VAL A 1 183 ? 14.291 13.322 19.574 1.00 46.34 ? 178 VAL A N   1 
ATOM   1379 C  CA  . VAL A 1 183 ? 14.061 13.656 20.979 1.00 46.51 ? 178 VAL A CA  1 
ATOM   1380 C  C   . VAL A 1 183 ? 13.175 14.892 21.090 1.00 48.11 ? 178 VAL A C   1 
ATOM   1381 O  O   . VAL A 1 183 ? 12.248 14.939 21.910 1.00 49.24 ? 178 VAL A O   1 
ATOM   1382 C  CB  . VAL A 1 183 ? 15.405 13.851 21.706 1.00 44.60 ? 178 VAL A CB  1 
ATOM   1383 C  CG1 . VAL A 1 183 ? 15.181 14.391 23.142 1.00 45.55 ? 178 VAL A CG1 1 
ATOM   1384 C  CG2 . VAL A 1 183 ? 16.179 12.547 21.735 1.00 45.74 ? 178 VAL A CG2 1 
ATOM   1385 N  N   . PHE A 1 184 ? 13.447 15.909 20.265 1.00 46.68 ? 179 PHE A N   1 
ATOM   1386 C  CA  . PHE A 1 184 ? 12.580 17.082 20.193 1.00 48.62 ? 179 PHE A CA  1 
ATOM   1387 C  C   . PHE A 1 184 ? 11.131 16.682 19.946 1.00 51.65 ? 179 PHE A C   1 
ATOM   1388 O  O   . PHE A 1 184 ? 10.221 17.117 20.661 1.00 51.92 ? 179 PHE A O   1 
ATOM   1389 C  CB  . PHE A 1 184 ? 13.067 18.030 19.092 1.00 46.71 ? 179 PHE A CB  1 
ATOM   1390 C  CG  . PHE A 1 184 ? 12.095 19.126 18.759 1.00 48.70 ? 179 PHE A CG  1 
ATOM   1391 C  CD1 . PHE A 1 184 ? 12.073 20.297 19.495 1.00 49.46 ? 179 PHE A CD1 1 
ATOM   1392 C  CD2 . PHE A 1 184 ? 11.205 18.989 17.704 1.00 51.65 ? 179 PHE A CD2 1 
ATOM   1393 C  CE1 . PHE A 1 184 ? 11.182 21.316 19.183 1.00 52.50 ? 179 PHE A CE1 1 
ATOM   1394 C  CE2 . PHE A 1 184 ? 10.309 20.003 17.388 1.00 53.66 ? 179 PHE A CE2 1 
ATOM   1395 C  CZ  . PHE A 1 184 ? 10.298 21.167 18.138 1.00 53.86 ? 179 PHE A CZ  1 
ATOM   1396 N  N   . HIS A 1 185 ? 10.900 15.856 18.922 1.00 51.70 ? 180 HIS A N   1 
ATOM   1397 C  CA  . HIS A 1 185 ? 9.541  15.424 18.615 1.00 55.79 ? 180 HIS A CA  1 
ATOM   1398 C  C   . HIS A 1 185 ? 8.895  14.730 19.809 1.00 56.97 ? 180 HIS A C   1 
ATOM   1399 O  O   . HIS A 1 185 ? 7.729  14.985 20.132 1.00 59.33 ? 180 HIS A O   1 
ATOM   1400 C  CB  . HIS A 1 185 ? 9.545  14.484 17.410 1.00 55.70 ? 180 HIS A CB  1 
ATOM   1401 C  CG  . HIS A 1 185 ? 9.741  15.174 16.095 1.00 57.51 ? 180 HIS A CG  1 
ATOM   1402 N  ND1 . HIS A 1 185 ? 9.065  16.323 15.746 1.00 58.32 ? 180 HIS A ND1 1 
ATOM   1403 C  CD2 . HIS A 1 185 ? 10.522 14.861 15.033 1.00 55.61 ? 180 HIS A CD2 1 
ATOM   1404 C  CE1 . HIS A 1 185 ? 9.429  16.695 14.532 1.00 57.82 ? 180 HIS A CE1 1 
ATOM   1405 N  NE2 . HIS A 1 185 ? 10.313 15.825 14.077 1.00 57.03 ? 180 HIS A NE2 1 
ATOM   1406 N  N   . TYR A 1 186 ? 9.637  13.850 20.474 1.00 52.63 ? 181 TYR A N   1 
ATOM   1407 C  CA  . TYR A 1 186 ? 9.041  13.039 21.527 1.00 55.06 ? 181 TYR A CA  1 
ATOM   1408 C  C   . TYR A 1 186 ? 8.838  13.845 22.804 1.00 56.57 ? 181 TYR A C   1 
ATOM   1409 O  O   . TYR A 1 186 ? 7.756  13.810 23.403 1.00 57.90 ? 181 TYR A O   1 
ATOM   1410 C  CB  . TYR A 1 186 ? 9.913  11.807 21.794 1.00 55.56 ? 181 TYR A CB  1 
ATOM   1411 C  CG  . TYR A 1 186 ? 9.260  10.784 22.701 1.00 58.09 ? 181 TYR A CG  1 
ATOM   1412 C  CD1 . TYR A 1 186 ? 9.246  10.948 24.081 1.00 58.17 ? 181 TYR A CD1 1 
ATOM   1413 C  CD2 . TYR A 1 186 ? 8.623  9.671  22.166 1.00 60.77 ? 181 TYR A CD2 1 
ATOM   1414 C  CE1 . TYR A 1 186 ? 8.638  10.016 24.897 1.00 60.75 ? 181 TYR A CE1 1 
ATOM   1415 C  CE2 . TYR A 1 186 ? 8.008  8.741  22.975 1.00 61.91 ? 181 TYR A CE2 1 
ATOM   1416 C  CZ  . TYR A 1 186 ? 8.021  8.919  24.339 1.00 61.82 ? 181 TYR A CZ  1 
ATOM   1417 O  OH  . TYR A 1 186 ? 7.409  7.988  25.146 1.00 67.76 ? 181 TYR A OH  1 
ATOM   1418 N  N   . GLU A 1 187 ? 9.862  14.585 23.227 1.00 53.59 ? 182 GLU A N   1 
ATOM   1419 C  CA  . GLU A 1 187 ? 9.865  15.203 24.549 1.00 54.83 ? 182 GLU A CA  1 
ATOM   1420 C  C   . GLU A 1 187 ? 9.334  16.627 24.549 1.00 55.00 ? 182 GLU A C   1 
ATOM   1421 O  O   . GLU A 1 187 ? 8.761  17.060 25.553 1.00 56.73 ? 182 GLU A O   1 
ATOM   1422 C  CB  . GLU A 1 187 ? 11.284 15.181 25.123 1.00 52.19 ? 182 GLU A CB  1 
ATOM   1423 C  CG  . GLU A 1 187 ? 11.857 13.770 25.260 1.00 54.61 ? 182 GLU A CG  1 
ATOM   1424 C  CD  . GLU A 1 187 ? 11.342 13.025 26.484 1.00 59.00 ? 182 GLU A CD  1 
ATOM   1425 O  OE1 . GLU A 1 187 ? 11.608 11.808 26.606 1.00 59.33 ? 182 GLU A OE1 1 
ATOM   1426 O  OE2 . GLU A 1 187 ? 10.701 13.665 27.343 1.00 60.98 ? 182 GLU A OE2 1 
ATOM   1427 N  N   . ILE A 1 188 ? 9.494  17.360 23.453 1.00 55.30 ? 183 ILE A N   1 
ATOM   1428 C  CA  . ILE A 1 188 ? 9.130  18.774 23.389 1.00 55.52 ? 183 ILE A CA  1 
ATOM   1429 C  C   . ILE A 1 188 ? 7.840  18.990 22.611 1.00 58.82 ? 183 ILE A C   1 
ATOM   1430 O  O   . ILE A 1 188 ? 6.932  19.674 23.081 1.00 57.92 ? 183 ILE A O   1 
ATOM   1431 C  CB  . ILE A 1 188 ? 10.289 19.598 22.784 1.00 54.41 ? 183 ILE A CB  1 
ATOM   1432 C  CG1 . ILE A 1 188 ? 11.597 19.315 23.530 1.00 51.87 ? 183 ILE A CG1 1 
ATOM   1433 C  CG2 . ILE A 1 188 ? 9.951  21.084 22.764 1.00 52.56 ? 183 ILE A CG2 1 
ATOM   1434 C  CD1 . ILE A 1 188 ? 11.647 19.927 24.906 1.00 48.47 ? 183 ILE A CD1 1 
ATOM   1435 N  N   . ALA A 1 189 ? 7.750  18.426 21.410 1.00 57.05 ? 184 ALA A N   1 
ATOM   1436 C  CA  . ALA A 1 189 ? 6.626  18.683 20.521 1.00 61.92 ? 184 ALA A CA  1 
ATOM   1437 C  C   . ALA A 1 189 ? 5.431  17.780 20.782 1.00 66.42 ? 184 ALA A C   1 
ATOM   1438 O  O   . ALA A 1 189 ? 4.379  17.986 20.166 1.00 70.52 ? 184 ALA A O   1 
ATOM   1439 C  CB  . ALA A 1 189 ? 7.058  18.528 19.057 1.00 60.31 ? 184 ALA A CB  1 
ATOM   1440 N  N   . ASN A 1 190 ? 5.574  16.786 21.657 1.00 65.61 ? 185 ASN A N   1 
ATOM   1441 C  CA  . ASN A 1 190 ? 4.503  15.837 21.959 1.00 70.56 ? 185 ASN A CA  1 
ATOM   1442 C  C   . ASN A 1 190 ? 4.012  15.138 20.693 1.00 70.42 ? 185 ASN A C   1 
ATOM   1443 O  O   . ASN A 1 190 ? 2.810  14.992 20.466 1.00 73.54 ? 185 ASN A O   1 
ATOM   1444 C  CB  . ASN A 1 190 ? 3.350  16.526 22.690 1.00 75.07 ? 185 ASN A CB  1 
ATOM   1445 C  CG  . ASN A 1 190 ? 3.748  17.004 24.071 1.00 80.88 ? 185 ASN A CG  1 
ATOM   1446 O  OD1 . ASN A 1 190 ? 3.844  18.209 24.322 1.00 79.07 ? 185 ASN A OD1 1 
ATOM   1447 N  ND2 . ASN A 1 190 ? 4.004  16.059 24.973 1.00 84.57 ? 185 ASN A ND2 1 
ATOM   1448 N  N   . SER A 1 191 ? 4.955  14.711 19.852 1.00 68.21 ? 186 SER A N   1 
ATOM   1449 C  CA  . SER A 1 191 ? 4.662  14.000 18.610 1.00 68.05 ? 186 SER A CA  1 
ATOM   1450 C  C   . SER A 1 191 ? 5.411  12.674 18.613 1.00 66.99 ? 186 SER A C   1 
ATOM   1451 O  O   . SER A 1 191 ? 6.387  12.499 17.872 1.00 66.58 ? 186 SER A O   1 
ATOM   1452 C  CB  . SER A 1 191 ? 5.052  14.829 17.388 1.00 68.94 ? 186 SER A CB  1 
ATOM   1453 O  OG  . SER A 1 191 ? 4.763  16.198 17.595 1.00 70.73 ? 186 SER A OG  1 
ATOM   1454 N  N   . PRO A 1 192 ? 4.973  11.712 19.426 1.00 68.18 ? 187 PRO A N   1 
ATOM   1455 C  CA  . PRO A 1 192 ? 5.683  10.422 19.472 1.00 69.05 ? 187 PRO A CA  1 
ATOM   1456 C  C   . PRO A 1 192 ? 5.734  9.712  18.130 1.00 69.63 ? 187 PRO A C   1 
ATOM   1457 O  O   . PRO A 1 192 ? 6.731  9.039  17.836 1.00 67.43 ? 187 PRO A O   1 
ATOM   1458 C  CB  . PRO A 1 192 ? 4.896  9.604  20.508 1.00 72.61 ? 187 PRO A CB  1 
ATOM   1459 C  CG  . PRO A 1 192 ? 3.730  10.425 20.920 1.00 73.26 ? 187 PRO A CG  1 
ATOM   1460 C  CD  . PRO A 1 192 ? 3.703  11.707 20.168 1.00 71.53 ? 187 PRO A CD  1 
ATOM   1461 N  N   . GLU A 1 193 ? 4.692  9.844  17.305 1.00 70.44 ? 188 GLU A N   1 
ATOM   1462 C  CA  . GLU A 1 193 ? 4.692  9.202  15.995 1.00 71.30 ? 188 GLU A CA  1 
ATOM   1463 C  C   . GLU A 1 193 ? 5.813  9.748  15.120 1.00 67.18 ? 188 GLU A C   1 
ATOM   1464 O  O   . GLU A 1 193 ? 6.531  8.988  14.460 1.00 63.88 ? 188 GLU A O   1 
ATOM   1465 C  CB  . GLU A 1 193 ? 3.334  9.400  15.316 1.00 75.29 ? 188 GLU A CB  1 
ATOM   1466 C  CG  . GLU A 1 193 ? 2.175  9.650  16.277 1.00 81.28 ? 188 GLU A CG  1 
ATOM   1467 C  CD  . GLU A 1 193 ? 1.834  8.445  17.147 1.00 84.69 ? 188 GLU A CD  1 
ATOM   1468 O  OE1 . GLU A 1 193 ? 2.389  7.347  16.910 1.00 84.88 ? 188 GLU A OE1 1 
ATOM   1469 O  OE2 . GLU A 1 193 ? 1.016  8.604  18.082 1.00 85.76 ? 188 GLU A OE2 1 
ATOM   1470 N  N   . GLU A 1 194 ? 5.973  11.074 15.105 1.00 68.16 ? 189 GLU A N   1 
ATOM   1471 C  CA  . GLU A 1 194 ? 7.048  11.696 14.336 1.00 65.26 ? 189 GLU A CA  1 
ATOM   1472 C  C   . GLU A 1 194 ? 8.414  11.294 14.872 1.00 61.91 ? 189 GLU A C   1 
ATOM   1473 O  O   . GLU A 1 194 ? 9.343  11.039 14.098 1.00 56.97 ? 189 GLU A O   1 
ATOM   1474 C  CB  . GLU A 1 194 ? 6.896  13.216 14.374 1.00 66.65 ? 189 GLU A CB  1 
ATOM   1475 C  CG  . GLU A 1 194 ? 7.306  13.922 13.102 1.00 71.31 ? 189 GLU A CG  1 
ATOM   1476 C  CD  . GLU A 1 194 ? 6.387  15.084 12.777 1.00 78.01 ? 189 GLU A CD  1 
ATOM   1477 O  OE1 . GLU A 1 194 ? 5.239  15.087 13.276 1.00 80.68 ? 189 GLU A OE1 1 
ATOM   1478 O  OE2 . GLU A 1 194 ? 6.812  15.990 12.024 1.00 80.43 ? 189 GLU A OE2 1 
ATOM   1479 N  N   . ALA A 1 195 ? 8.560  11.259 16.199 1.00 63.01 ? 190 ALA A N   1 
ATOM   1480 C  CA  . ALA A 1 195 ? 9.822  10.844 16.799 1.00 60.47 ? 190 ALA A CA  1 
ATOM   1481 C  C   . ALA A 1 195 ? 10.171 9.414  16.407 1.00 60.11 ? 190 ALA A C   1 
ATOM   1482 O  O   . ALA A 1 195 ? 11.308 9.124  16.019 1.00 58.40 ? 190 ALA A O   1 
ATOM   1483 C  CB  . ALA A 1 195 ? 9.743  10.979 18.322 1.00 58.89 ? 190 ALA A CB  1 
ATOM   1484 N  N   . ILE A 1 196 ? 9.200  8.506  16.503 1.00 59.97 ? 191 ILE A N   1 
ATOM   1485 C  CA  . ILE A 1 196 ? 9.460  7.101  16.207 1.00 60.39 ? 191 ILE A CA  1 
ATOM   1486 C  C   . ILE A 1 196 ? 9.778  6.922  14.728 1.00 58.93 ? 191 ILE A C   1 
ATOM   1487 O  O   . ILE A 1 196 ? 10.744 6.245  14.359 1.00 57.15 ? 191 ILE A O   1 
ATOM   1488 C  CB  . ILE A 1 196 ? 8.263  6.233  16.635 1.00 62.13 ? 191 ILE A CB  1 
ATOM   1489 C  CG1 . ILE A 1 196 ? 8.384  5.855  18.114 1.00 63.57 ? 191 ILE A CG1 1 
ATOM   1490 C  CG2 . ILE A 1 196 ? 8.186  4.974  15.803 1.00 62.14 ? 191 ILE A CG2 1 
ATOM   1491 C  CD1 . ILE A 1 196 ? 7.042  5.749  18.825 1.00 66.32 ? 191 ILE A CD1 1 
ATOM   1492 N  N   . SER A 1 197 ? 8.978  7.538  13.858 1.00 57.40 ? 192 SER A N   1 
ATOM   1493 C  CA  . SER A 1 197 ? 9.213  7.369  12.431 1.00 59.01 ? 192 SER A CA  1 
ATOM   1494 C  C   . SER A 1 197 ? 10.527 8.017  12.006 1.00 55.32 ? 192 SER A C   1 
ATOM   1495 O  O   . SER A 1 197 ? 11.233 7.474  11.152 1.00 55.00 ? 192 SER A O   1 
ATOM   1496 C  CB  . SER A 1 197 ? 8.027  7.909  11.628 1.00 62.30 ? 192 SER A CB  1 
ATOM   1497 O  OG  . SER A 1 197 ? 8.269  9.218  11.152 1.00 68.08 ? 192 SER A OG  1 
ATOM   1498 N  N   . LEU A 1 198 ? 10.904 9.150  12.611 1.00 56.27 ? 193 LEU A N   1 
ATOM   1499 C  CA  . LEU A 1 198 ? 12.192 9.743  12.254 1.00 54.07 ? 193 LEU A CA  1 
ATOM   1500 C  C   . LEU A 1 198 ? 13.349 8.865  12.718 1.00 53.14 ? 193 LEU A C   1 
ATOM   1501 O  O   . LEU A 1 198 ? 14.303 8.636  11.963 1.00 50.56 ? 193 LEU A O   1 
ATOM   1502 C  CB  . LEU A 1 198 ? 12.330 11.154 12.829 1.00 54.30 ? 193 LEU A CB  1 
ATOM   1503 C  CG  . LEU A 1 198 ? 13.693 11.846 12.640 1.00 49.54 ? 193 LEU A CG  1 
ATOM   1504 C  CD1 . LEU A 1 198 ? 14.089 11.957 11.184 1.00 51.89 ? 193 LEU A CD1 1 
ATOM   1505 C  CD2 . LEU A 1 198 ? 13.693 13.220 13.285 1.00 49.16 ? 193 LEU A CD2 1 
ATOM   1506 N  N   . ALA A 1 199 ? 13.280 8.354  13.950 1.00 51.79 ? 194 ALA A N   1 
ATOM   1507 C  CA  . ALA A 1 199 ? 14.374 7.544  14.469 1.00 50.89 ? 194 ALA A CA  1 
ATOM   1508 C  C   . ALA A 1 199 ? 14.481 6.221  13.724 1.00 51.34 ? 194 ALA A C   1 
ATOM   1509 O  O   . ALA A 1 199 ? 15.586 5.739  13.457 1.00 49.93 ? 194 ALA A O   1 
ATOM   1510 C  CB  . ALA A 1 199 ? 14.185 7.305  15.969 1.00 53.90 ? 194 ALA A CB  1 
ATOM   1511 N  N   . LYS A 1 200 ? 13.348 5.610  13.394 1.00 51.66 ? 195 LYS A N   1 
ATOM   1512 C  CA  . LYS A 1 200 ? 13.392 4.350  12.659 1.00 52.87 ? 195 LYS A CA  1 
ATOM   1513 C  C   . LYS A 1 200 ? 13.918 4.561  11.242 1.00 50.95 ? 195 LYS A C   1 
ATOM   1514 O  O   . LYS A 1 200 ? 14.775 3.804  10.766 1.00 51.44 ? 195 LYS A O   1 
ATOM   1515 C  CB  . LYS A 1 200 ? 12.008 3.704  12.639 1.00 53.82 ? 195 LYS A CB  1 
ATOM   1516 C  CG  . LYS A 1 200 ? 11.864 2.641  11.574 1.00 56.56 ? 195 LYS A CG  1 
ATOM   1517 C  CD  . LYS A 1 200 ? 10.635 1.788  11.795 1.00 60.69 ? 195 LYS A CD  1 
ATOM   1518 C  CE  . LYS A 1 200 ? 10.749 0.472  11.031 1.00 64.07 ? 195 LYS A CE  1 
ATOM   1519 N  NZ  . LYS A 1 200 ? 11.746 -0.422 11.693 1.00 66.83 ? 195 LYS A NZ  1 
ATOM   1520 N  N   . THR A 1 201 ? 13.412 5.585  10.547 1.00 51.97 ? 196 THR A N   1 
ATOM   1521 C  CA  . THR A 1 201 ? 13.916 5.887  9.210  1.00 48.24 ? 196 THR A CA  1 
ATOM   1522 C  C   . THR A 1 201 ? 15.414 6.152  9.227  1.00 48.08 ? 196 THR A C   1 
ATOM   1523 O  O   . THR A 1 201 ? 16.147 5.701  8.338  1.00 49.17 ? 196 THR A O   1 
ATOM   1524 C  CB  . THR A 1 201 ? 13.181 7.093  8.621  1.00 51.10 ? 196 THR A CB  1 
ATOM   1525 O  OG1 . THR A 1 201 ? 11.789 6.784  8.469  1.00 58.66 ? 196 THR A OG1 1 
ATOM   1526 C  CG2 . THR A 1 201 ? 13.770 7.471  7.257  1.00 53.81 ? 196 THR A CG2 1 
ATOM   1527 N  N   . THR A 1 202 ? 15.881 6.926  10.205 1.00 49.47 ? 197 THR A N   1 
ATOM   1528 C  CA  . THR A 1 202 ? 17.301 7.228  10.286 1.00 47.45 ? 197 THR A CA  1 
ATOM   1529 C  C   . THR A 1 202 ? 18.121 5.967  10.509 1.00 46.26 ? 197 THR A C   1 
ATOM   1530 O  O   . THR A 1 202 ? 19.147 5.756  9.854  1.00 43.72 ? 197 THR A O   1 
ATOM   1531 C  CB  . THR A 1 202 ? 17.548 8.229  11.412 1.00 44.63 ? 197 THR A CB  1 
ATOM   1532 O  OG1 . THR A 1 202 ? 16.755 9.394  11.170 1.00 45.00 ? 197 THR A OG1 1 
ATOM   1533 C  CG2 . THR A 1 202 ? 18.996 8.603  11.444 1.00 41.73 ? 197 THR A CG2 1 
ATOM   1534 N  N   . PHE A 1 203 ? 17.696 5.126  11.456 1.00 45.22 ? 198 PHE A N   1 
ATOM   1535 C  CA  . PHE A 1 203 ? 18.431 3.896  11.717 1.00 45.69 ? 198 PHE A CA  1 
ATOM   1536 C  C   . PHE A 1 203 ? 18.437 2.994  10.491 1.00 45.78 ? 198 PHE A C   1 
ATOM   1537 O  O   . PHE A 1 203 ? 19.489 2.502  10.073 1.00 45.19 ? 198 PHE A O   1 
ATOM   1538 C  CB  . PHE A 1 203 ? 17.833 3.145  12.911 1.00 47.05 ? 198 PHE A CB  1 
ATOM   1539 C  CG  . PHE A 1 203 ? 18.560 1.869  13.236 1.00 45.99 ? 198 PHE A CG  1 
ATOM   1540 C  CD1 . PHE A 1 203 ? 19.645 1.880  14.101 1.00 48.77 ? 198 PHE A CD1 1 
ATOM   1541 C  CD2 . PHE A 1 203 ? 18.177 0.664  12.671 1.00 49.78 ? 198 PHE A CD2 1 
ATOM   1542 C  CE1 . PHE A 1 203 ? 20.332 0.715  14.385 1.00 50.41 ? 198 PHE A CE1 1 
ATOM   1543 C  CE2 . PHE A 1 203 ? 18.856 -0.499 12.961 1.00 51.63 ? 198 PHE A CE2 1 
ATOM   1544 C  CZ  . PHE A 1 203 ? 19.933 -0.475 13.819 1.00 48.14 ? 198 PHE A CZ  1 
ATOM   1545 N  N   . ASP A 1 204 ? 17.261 2.752  9.911  1.00 47.36 ? 199 ASP A N   1 
ATOM   1546 C  CA  . ASP A 1 204 ? 17.184 1.825  8.784  1.00 45.73 ? 199 ASP A CA  1 
ATOM   1547 C  C   . ASP A 1 204 ? 17.988 2.334  7.595  1.00 46.20 ? 199 ASP A C   1 
ATOM   1548 O  O   . ASP A 1 204 ? 18.621 1.550  6.881  1.00 46.51 ? 199 ASP A O   1 
ATOM   1549 C  CB  . ASP A 1 204 ? 15.725 1.603  8.387  1.00 48.27 ? 199 ASP A CB  1 
ATOM   1550 C  CG  . ASP A 1 204 ? 14.951 0.783  9.414  1.00 54.64 ? 199 ASP A CG  1 
ATOM   1551 O  OD1 . ASP A 1 204 ? 15.577 0.094  10.251 1.00 51.15 ? 199 ASP A OD1 1 
ATOM   1552 O  OD2 . ASP A 1 204 ? 13.705 0.841  9.383  1.00 57.38 ? 199 ASP A OD2 1 
ATOM   1553 N  N   . GLU A 1 205 ? 17.983 3.646  7.370  1.00 46.71 ? 200 GLU A N   1 
ATOM   1554 C  CA  . GLU A 1 205 ? 18.687 4.171  6.206  1.00 48.64 ? 200 GLU A CA  1 
ATOM   1555 C  C   . GLU A 1 205 ? 20.194 4.139  6.415  1.00 45.46 ? 200 GLU A C   1 
ATOM   1556 O  O   . GLU A 1 205 ? 20.950 3.931  5.460  1.00 44.53 ? 200 GLU A O   1 
ATOM   1557 C  CB  . GLU A 1 205 ? 18.181 5.578  5.890  1.00 46.97 ? 200 GLU A CB  1 
ATOM   1558 C  CG  . GLU A 1 205 ? 16.832 5.528  5.163  1.00 51.03 ? 200 GLU A CG  1 
ATOM   1559 C  CD  . GLU A 1 205 ? 16.347 6.886  4.696  1.00 54.29 ? 200 GLU A CD  1 
ATOM   1560 O  OE1 . GLU A 1 205 ? 17.041 7.882  4.974  1.00 53.52 ? 200 GLU A OE1 1 
ATOM   1561 O  OE2 . GLU A 1 205 ? 15.303 6.949  3.997  1.00 55.94 ? 200 GLU A OE2 1 
ATOM   1562 N  N   . ALA A 1 206 ? 20.647 4.315  7.655  1.00 43.62 ? 201 ALA A N   1 
ATOM   1563 C  CA  . ALA A 1 206 ? 22.060 4.122  7.961  1.00 43.70 ? 201 ALA A CA  1 
ATOM   1564 C  C   . ALA A 1 206 ? 22.459 2.672  7.749  1.00 43.56 ? 201 ALA A C   1 
ATOM   1565 O  O   . ALA A 1 206 ? 23.535 2.383  7.209  1.00 43.00 ? 201 ALA A O   1 
ATOM   1566 C  CB  . ALA A 1 206 ? 22.355 4.557  9.408  1.00 41.73 ? 201 ALA A CB  1 
ATOM   1567 N  N   . MET A 1 207 ? 21.579 1.739  8.120  1.00 43.60 ? 202 MET A N   1 
ATOM   1568 C  CA  . MET A 1 207 ? 21.925 0.328  8.003  1.00 44.12 ? 202 MET A CA  1 
ATOM   1569 C  C   . MET A 1 207 ? 21.947 -0.074 6.533  1.00 44.57 ? 202 MET A C   1 
ATOM   1570 O  O   . MET A 1 207 ? 22.840 -0.803 6.081  1.00 44.59 ? 202 MET A O   1 
ATOM   1571 C  CB  . MET A 1 207 ? 20.897 -0.508 8.761  1.00 44.74 ? 202 MET A CB  1 
ATOM   1572 C  CG  . MET A 1 207 ? 21.297 -0.488 10.250 1.00 46.47 ? 202 MET A CG  1 
ATOM   1573 S  SD  . MET A 1 207 ? 22.640 -1.505 10.801 1.00 54.03 ? 202 MET A SD  1 
ATOM   1574 C  CE  . MET A 1 207 ? 22.103 -3.121 10.338 1.00 52.92 ? 202 MET A CE  1 
ATOM   1575 N  N   . ALA A 1 208 ? 20.968 0.413  5.775  1.00 45.14 ? 203 ALA A N   1 
ATOM   1576 C  CA  . ALA A 1 208 ? 20.904 0.092  4.354  1.00 46.98 ? 203 ALA A CA  1 
ATOM   1577 C  C   . ALA A 1 208 ? 22.144 0.585  3.621  1.00 45.62 ? 203 ALA A C   1 
ATOM   1578 O  O   . ALA A 1 208 ? 22.596 -0.053 2.679  1.00 49.37 ? 203 ALA A O   1 
ATOM   1579 C  CB  . ALA A 1 208 ? 19.643 0.691  3.743  1.00 47.98 ? 203 ALA A CB  1 
ATOM   1580 N  N   . ASP A 1 209 ? 22.732 1.693  4.054  1.00 43.92 ? 204 ASP A N   1 
ATOM   1581 C  CA  . ASP A 1 209 ? 23.929 2.210  3.400  1.00 45.47 ? 204 ASP A CA  1 
ATOM   1582 C  C   . ASP A 1 209 ? 25.116 2.168  4.367  1.00 42.75 ? 204 ASP A C   1 
ATOM   1583 O  O   . ASP A 1 209 ? 25.917 3.101  4.454  1.00 40.91 ? 204 ASP A O   1 
ATOM   1584 C  CB  . ASP A 1 209 ? 23.687 3.612  2.831  1.00 42.86 ? 204 ASP A CB  1 
ATOM   1585 C  CG  . ASP A 1 209 ? 22.922 3.593  1.490  1.00 46.97 ? 204 ASP A CG  1 
ATOM   1586 O  OD1 . ASP A 1 209 ? 23.114 2.651  0.689  1.00 47.26 ? 204 ASP A OD1 1 
ATOM   1587 O  OD2 . ASP A 1 209 ? 22.112 4.515  1.243  1.00 45.95 ? 204 ASP A OD2 1 
ATOM   1588 N  N   . LEU A 1 210 ? 25.252 1.038  5.074  1.00 42.24 ? 205 LEU A N   1 
ATOM   1589 C  CA  . LEU A 1 210 ? 26.278 0.900  6.110  1.00 41.70 ? 205 LEU A CA  1 
ATOM   1590 C  C   . LEU A 1 210 ? 27.683 1.027  5.540  1.00 41.44 ? 205 LEU A C   1 
ATOM   1591 O  O   . LEU A 1 210 ? 28.595 1.489  6.229  1.00 41.55 ? 205 LEU A O   1 
ATOM   1592 C  CB  . LEU A 1 210 ? 26.115 -0.448 6.810  1.00 42.96 ? 205 LEU A CB  1 
ATOM   1593 C  CG  . LEU A 1 210 ? 26.945 -0.740 8.050  1.00 42.97 ? 205 LEU A CG  1 
ATOM   1594 C  CD1 . LEU A 1 210 ? 26.511 0.178  9.184  1.00 45.10 ? 205 LEU A CD1 1 
ATOM   1595 C  CD2 . LEU A 1 210 ? 26.789 -2.229 8.425  1.00 45.72 ? 205 LEU A CD2 1 
ATOM   1596 N  N   . HIS A 1 211 ? 27.870 0.654  4.273  1.00 41.70 ? 206 HIS A N   1 
ATOM   1597 C  CA  . HIS A 1 211 ? 29.162 0.774  3.600  1.00 41.96 ? 206 HIS A CA  1 
ATOM   1598 C  C   . HIS A 1 211 ? 29.698 2.202  3.545  1.00 40.37 ? 206 HIS A C   1 
ATOM   1599 O  O   . HIS A 1 211 ? 30.862 2.378  3.168  1.00 40.14 ? 206 HIS A O   1 
ATOM   1600 C  CB  . HIS A 1 211 ? 29.043 0.268  2.159  1.00 43.24 ? 206 HIS A CB  1 
ATOM   1601 C  CG  . HIS A 1 211 ? 28.059 1.044  1.349  1.00 43.00 ? 206 HIS A CG  1 
ATOM   1602 N  ND1 . HIS A 1 211 ? 28.430 2.014  0.440  1.00 44.51 ? 206 HIS A ND1 1 
ATOM   1603 C  CD2 . HIS A 1 211 ? 26.707 1.015  1.337  1.00 45.51 ? 206 HIS A CD2 1 
ATOM   1604 C  CE1 . HIS A 1 211 ? 27.347 2.533  -0.111 1.00 45.58 ? 206 HIS A CE1 1 
ATOM   1605 N  NE2 . HIS A 1 211 ? 26.288 1.940  0.412  1.00 44.20 ? 206 HIS A NE2 1 
ATOM   1606 N  N   . THR A 1 212 ? 28.877 3.215  3.827  1.00 39.87 ? 207 THR A N   1 
ATOM   1607 C  CA  . THR A 1 212 ? 29.325 4.600  3.773  1.00 39.14 ? 207 THR A CA  1 
ATOM   1608 C  C   . THR A 1 212 ? 29.979 5.042  5.075  1.00 40.45 ? 207 THR A C   1 
ATOM   1609 O  O   . THR A 1 212 ? 30.324 6.221  5.222  1.00 39.93 ? 207 THR A O   1 
ATOM   1610 C  CB  . THR A 1 212 ? 28.160 5.548  3.434  1.00 40.39 ? 207 THR A CB  1 
ATOM   1611 O  OG1 . THR A 1 212 ? 27.180 5.529  4.480  1.00 40.24 ? 207 THR A OG1 1 
ATOM   1612 C  CG2 . THR A 1 212 ? 27.483 5.113  2.122  1.00 40.43 ? 207 THR A CG2 1 
ATOM   1613 N  N   . LEU A 1 213 ? 30.148 4.130  6.026  1.00 38.45 ? 208 LEU A N   1 
ATOM   1614 C  CA  . LEU A 1 213 ? 30.856 4.498  7.248  1.00 39.70 ? 208 LEU A CA  1 
ATOM   1615 C  C   . LEU A 1 213 ? 32.258 4.969  6.891  1.00 40.53 ? 208 LEU A C   1 
ATOM   1616 O  O   . LEU A 1 213 ? 32.907 4.424  5.989  1.00 38.91 ? 208 LEU A O   1 
ATOM   1617 C  CB  . LEU A 1 213 ? 30.933 3.305  8.215  1.00 40.77 ? 208 LEU A CB  1 
ATOM   1618 C  CG  . LEU A 1 213 ? 29.678 2.889  8.974  1.00 39.66 ? 208 LEU A CG  1 
ATOM   1619 C  CD1 . LEU A 1 213 ? 29.884 1.525  9.659  1.00 41.51 ? 208 LEU A CD1 1 
ATOM   1620 C  CD2 . LEU A 1 213 ? 29.296 3.933  10.010 1.00 37.36 ? 208 LEU A CD2 1 
ATOM   1621 N  N   . SER A 1 214 ? 32.724 5.987  7.600  1.00 39.88 ? 209 SER A N   1 
ATOM   1622 C  CA  . SER A 1 214 ? 34.024 6.586  7.353  1.00 42.45 ? 209 SER A CA  1 
ATOM   1623 C  C   . SER A 1 214 ? 35.048 6.055  8.348  1.00 43.11 ? 209 SER A C   1 
ATOM   1624 O  O   . SER A 1 214 ? 34.748 5.919  9.534  1.00 40.30 ? 209 SER A O   1 
ATOM   1625 C  CB  . SER A 1 214 ? 33.926 8.108  7.465  1.00 45.16 ? 209 SER A CB  1 
ATOM   1626 O  OG  . SER A 1 214 ? 35.210 8.694  7.481  1.00 48.48 ? 209 SER A OG  1 
ATOM   1627 N  N   . GLU A 1 215 ? 36.260 5.764  7.857  1.00 42.29 ? 210 GLU A N   1 
ATOM   1628 C  CA  . GLU A 1 215 ? 37.324 5.287  8.741  1.00 46.05 ? 210 GLU A CA  1 
ATOM   1629 C  C   . GLU A 1 215 ? 37.563 6.195  9.940  1.00 45.75 ? 210 GLU A C   1 
ATOM   1630 O  O   . GLU A 1 215 ? 37.918 5.715  11.025 1.00 44.70 ? 210 GLU A O   1 
ATOM   1631 C  CB  . GLU A 1 215 ? 38.635 5.156  7.978  1.00 49.03 ? 210 GLU A CB  1 
ATOM   1632 C  CG  . GLU A 1 215 ? 38.595 4.290  6.770  1.00 50.46 ? 210 GLU A CG  1 
ATOM   1633 C  CD  . GLU A 1 215 ? 39.914 4.317  6.043  1.00 56.01 ? 210 GLU A CD  1 
ATOM   1634 O  OE1 . GLU A 1 215 ? 40.953 4.127  6.719  1.00 55.36 ? 210 GLU A OE1 1 
ATOM   1635 O  OE2 . GLU A 1 215 ? 39.916 4.497  4.803  1.00 58.24 ? 210 GLU A OE2 1 
ATOM   1636 N  N   . ASP A 1 216 ? 37.405 7.499  9.774  1.00 42.92 ? 211 ASP A N   1 
ATOM   1637 C  CA  . ASP A 1 216 ? 37.768 8.411  10.846 1.00 44.59 ? 211 ASP A CA  1 
ATOM   1638 C  C   . ASP A 1 216 ? 36.629 8.692  11.825 1.00 43.58 ? 211 ASP A C   1 
ATOM   1639 O  O   . ASP A 1 216 ? 36.860 9.348  12.840 1.00 41.70 ? 211 ASP A O   1 
ATOM   1640 C  CB  . ASP A 1 216 ? 38.315 9.717  10.249 1.00 51.79 ? 211 ASP A CB  1 
ATOM   1641 C  CG  . ASP A 1 216 ? 37.310 10.433 9.372  1.00 53.54 ? 211 ASP A CG  1 
ATOM   1642 O  OD1 . ASP A 1 216 ? 37.746 11.046 8.369  1.00 62.42 ? 211 ASP A OD1 1 
ATOM   1643 O  OD2 . ASP A 1 216 ? 36.096 10.400 9.668  1.00 58.72 ? 211 ASP A OD2 1 
ATOM   1644 N  N   . SER A 1 217 ? 35.418 8.180  11.580 1.00 43.35 ? 212 SER A N   1 
ATOM   1645 C  CA  . SER A 1 217 ? 34.286 8.524  12.432 1.00 40.64 ? 212 SER A CA  1 
ATOM   1646 C  C   . SER A 1 217 ? 33.323 7.362  12.668 1.00 38.16 ? 212 SER A C   1 
ATOM   1647 O  O   . SER A 1 217 ? 32.250 7.587  13.247 1.00 36.90 ? 212 SER A O   1 
ATOM   1648 C  CB  . SER A 1 217 ? 33.510 9.698  11.815 1.00 39.42 ? 212 SER A CB  1 
ATOM   1649 O  OG  . SER A 1 217 ? 33.050 9.324  10.514 1.00 40.25 ? 212 SER A OG  1 
ATOM   1650 N  N   . TYR A 1 218 ? 33.661 6.143  12.246 1.00 38.66 ? 213 TYR A N   1 
ATOM   1651 C  CA  . TYR A 1 218 ? 32.679 5.062  12.273 1.00 38.52 ? 213 TYR A CA  1 
ATOM   1652 C  C   . TYR A 1 218 ? 32.270 4.714  13.692 1.00 39.31 ? 213 TYR A C   1 
ATOM   1653 O  O   . TYR A 1 218 ? 31.122 4.323  13.917 1.00 40.13 ? 213 TYR A O   1 
ATOM   1654 C  CB  . TYR A 1 218 ? 33.206 3.814  11.557 1.00 38.56 ? 213 TYR A CB  1 
ATOM   1655 C  CG  . TYR A 1 218 ? 34.298 3.068  12.290 1.00 40.87 ? 213 TYR A CG  1 
ATOM   1656 C  CD1 . TYR A 1 218 ? 33.992 2.040  13.195 1.00 42.24 ? 213 TYR A CD1 1 
ATOM   1657 C  CD2 . TYR A 1 218 ? 35.633 3.377  12.079 1.00 42.72 ? 213 TYR A CD2 1 
ATOM   1658 C  CE1 . TYR A 1 218 ? 35.001 1.354  13.864 1.00 41.98 ? 213 TYR A CE1 1 
ATOM   1659 C  CE2 . TYR A 1 218 ? 36.644 2.699  12.737 1.00 44.70 ? 213 TYR A CE2 1 
ATOM   1660 C  CZ  . TYR A 1 218 ? 36.319 1.691  13.636 1.00 45.62 ? 213 TYR A CZ  1 
ATOM   1661 O  OH  . TYR A 1 218 ? 37.326 1.021  14.285 1.00 46.82 ? 213 TYR A OH  1 
ATOM   1662 N  N   . LYS A 1 219 ? 33.171 4.886  14.663 1.00 36.57 ? 214 LYS A N   1 
ATOM   1663 C  CA  . LYS A 1 219 ? 32.796 4.595  16.041 1.00 40.73 ? 214 LYS A CA  1 
ATOM   1664 C  C   . LYS A 1 219 ? 31.721 5.557  16.522 1.00 38.92 ? 214 LYS A C   1 
ATOM   1665 O  O   . LYS A 1 219 ? 30.816 5.168  17.273 1.00 39.36 ? 214 LYS A O   1 
ATOM   1666 C  CB  . LYS A 1 219 ? 34.039 4.647  16.925 1.00 41.60 ? 214 LYS A CB  1 
ATOM   1667 C  CG  . LYS A 1 219 ? 35.024 3.547  16.561 1.00 42.45 ? 214 LYS A CG  1 
ATOM   1668 C  CD  . LYS A 1 219 ? 36.167 3.433  17.565 1.00 51.20 ? 214 LYS A CD  1 
ATOM   1669 C  CE  . LYS A 1 219 ? 37.436 4.078  17.027 1.00 52.95 ? 214 LYS A CE  1 
ATOM   1670 N  NZ  . LYS A 1 219 ? 38.430 4.323  18.118 1.00 59.57 ? 214 LYS A NZ  1 
ATOM   1671 N  N   . ASP A 1 220 ? 31.798 6.820  16.090 1.00 39.19 ? 215 ASP A N   1 
ATOM   1672 C  CA  . ASP A 1 220 ? 30.760 7.785  16.422 1.00 38.51 ? 215 ASP A CA  1 
ATOM   1673 C  C   . ASP A 1 220 ? 29.443 7.417  15.758 1.00 36.87 ? 215 ASP A C   1 
ATOM   1674 O  O   . ASP A 1 220 ? 28.383 7.463  16.390 1.00 35.27 ? 215 ASP A O   1 
ATOM   1675 C  CB  . ASP A 1 220 ? 31.193 9.192  16.003 1.00 38.85 ? 215 ASP A CB  1 
ATOM   1676 C  CG  . ASP A 1 220 ? 32.291 9.757  16.891 1.00 43.34 ? 215 ASP A CG  1 
ATOM   1677 O  OD1 . ASP A 1 220 ? 32.545 9.192  17.973 1.00 45.82 ? 215 ASP A OD1 1 
ATOM   1678 O  OD2 . ASP A 1 220 ? 32.886 10.786 16.513 1.00 47.13 ? 215 ASP A OD2 1 
ATOM   1679 N  N   . SER A 1 221 ? 29.486 7.090  14.464 1.00 35.61 ? 216 SER A N   1 
ATOM   1680 C  CA  . SER A 1 221 ? 28.263 6.700  13.771 1.00 34.69 ? 216 SER A CA  1 
ATOM   1681 C  C   . SER A 1 221 ? 27.585 5.533  14.469 1.00 37.18 ? 216 SER A C   1 
ATOM   1682 O  O   . SER A 1 221 ? 26.379 5.569  14.733 1.00 36.49 ? 216 SER A O   1 
ATOM   1683 C  CB  . SER A 1 221 ? 28.581 6.340  12.317 1.00 34.39 ? 216 SER A CB  1 
ATOM   1684 O  OG  . SER A 1 221 ? 29.149 7.458  11.671 1.00 36.55 ? 216 SER A OG  1 
ATOM   1685 N  N   . THR A 1 222 ? 28.346 4.490  14.794 1.00 36.56 ? 217 THR A N   1 
ATOM   1686 C  CA  . THR A 1 222 ? 27.691 3.298  15.322 1.00 39.04 ? 217 THR A CA  1 
ATOM   1687 C  C   . THR A 1 222 ? 27.178 3.535  16.732 1.00 37.93 ? 217 THR A C   1 
ATOM   1688 O  O   . THR A 1 222 ? 26.191 2.913  17.141 1.00 38.39 ? 217 THR A O   1 
ATOM   1689 C  CB  . THR A 1 222 ? 28.624 2.083  15.241 1.00 39.37 ? 217 THR A CB  1 
ATOM   1690 O  OG1 . THR A 1 222 ? 29.865 2.352  15.899 1.00 42.37 ? 217 THR A OG1 1 
ATOM   1691 C  CG2 . THR A 1 222 ? 28.922 1.764  13.800 1.00 42.30 ? 217 THR A CG2 1 
ATOM   1692 N  N   . LEU A 1 223 ? 27.786 4.469  17.468 1.00 35.86 ? 218 LEU A N   1 
ATOM   1693 C  CA  . LEU A 1 223 ? 27.243 4.835  18.770 1.00 39.11 ? 218 LEU A CA  1 
ATOM   1694 C  C   . LEU A 1 223 ? 25.871 5.491  18.625 1.00 38.89 ? 218 LEU A C   1 
ATOM   1695 O  O   . LEU A 1 223 ? 24.920 5.113  19.310 1.00 36.49 ? 218 LEU A O   1 
ATOM   1696 C  CB  . LEU A 1 223 ? 28.221 5.759  19.505 1.00 39.75 ? 218 LEU A CB  1 
ATOM   1697 C  CG  . LEU A 1 223 ? 27.698 6.394  20.798 1.00 39.28 ? 218 LEU A CG  1 
ATOM   1698 C  CD1 . LEU A 1 223 ? 27.107 5.341  21.709 1.00 44.19 ? 218 LEU A CD1 1 
ATOM   1699 C  CD2 . LEU A 1 223 ? 28.816 7.137  21.484 1.00 43.04 ? 218 LEU A CD2 1 
ATOM   1700 N  N   . ILE A 1 224 ? 25.735 6.461  17.720 1.00 37.85 ? 219 ILE A N   1 
ATOM   1701 C  CA  . ILE A 1 224 ? 24.438 7.112  17.547 1.00 36.45 ? 219 ILE A CA  1 
ATOM   1702 C  C   . ILE A 1 224 ? 23.400 6.114  17.045 1.00 38.03 ? 219 ILE A C   1 
ATOM   1703 O  O   . ILE A 1 224 ? 22.226 6.168  17.432 1.00 39.02 ? 219 ILE A O   1 
ATOM   1704 C  CB  . ILE A 1 224 ? 24.557 8.323  16.602 1.00 38.05 ? 219 ILE A CB  1 
ATOM   1705 C  CG1 . ILE A 1 224 ? 25.620 9.311  17.102 1.00 37.59 ? 219 ILE A CG1 1 
ATOM   1706 C  CG2 . ILE A 1 224 ? 23.205 9.030  16.454 1.00 39.00 ? 219 ILE A CG2 1 
ATOM   1707 C  CD1 . ILE A 1 224 ? 25.376 9.849  18.514 1.00 39.41 ? 219 ILE A CD1 1 
ATOM   1708 N  N   . MET A 1 225 ? 23.800 5.210  16.152 1.00 37.99 ? 220 MET A N   1 
ATOM   1709 C  CA  . MET A 1 225 ? 22.859 4.195  15.681 1.00 39.00 ? 220 MET A CA  1 
ATOM   1710 C  C   . MET A 1 225 ? 22.299 3.388  16.843 1.00 41.17 ? 220 MET A C   1 
ATOM   1711 O  O   . MET A 1 225 ? 21.090 3.126  16.907 1.00 42.63 ? 220 MET A O   1 
ATOM   1712 C  CB  . MET A 1 225 ? 23.538 3.282  14.667 1.00 41.80 ? 220 MET A CB  1 
ATOM   1713 C  CG  . MET A 1 225 ? 23.760 4.002  13.347 1.00 41.60 ? 220 MET A CG  1 
ATOM   1714 S  SD  . MET A 1 225 ? 24.825 3.107  12.228 1.00 43.41 ? 220 MET A SD  1 
ATOM   1715 C  CE  . MET A 1 225 ? 23.847 1.633  11.932 1.00 43.38 ? 220 MET A CE  1 
ATOM   1716 N  N   . GLN A 1 226 ? 23.159 3.010  17.786 1.00 40.03 ? 221 GLN A N   1 
ATOM   1717 C  CA  . GLN A 1 226 ? 22.694 2.282  18.964 1.00 44.12 ? 221 GLN A CA  1 
ATOM   1718 C  C   . GLN A 1 226 ? 21.773 3.144  19.823 1.00 45.05 ? 221 GLN A C   1 
ATOM   1719 O  O   . GLN A 1 226 ? 20.803 2.636  20.400 1.00 46.37 ? 221 GLN A O   1 
ATOM   1720 C  CB  . GLN A 1 226 ? 23.886 1.795  19.785 1.00 45.18 ? 221 GLN A CB  1 
ATOM   1721 C  CG  . GLN A 1 226 ? 23.500 0.942  20.989 1.00 49.70 ? 221 GLN A CG  1 
ATOM   1722 C  CD  . GLN A 1 226 ? 22.784 -0.321 20.583 1.00 50.20 ? 221 GLN A CD  1 
ATOM   1723 O  OE1 . GLN A 1 226 ? 23.289 -1.101 19.777 1.00 51.98 ? 221 GLN A OE1 1 
ATOM   1724 N  NE2 . GLN A 1 226 ? 21.595 -0.533 21.135 1.00 56.59 ? 221 GLN A NE2 1 
ATOM   1725 N  N   . LEU A 1 227 ? 22.046 4.453  19.914 1.00 41.92 ? 222 LEU A N   1 
ATOM   1726 C  CA  . LEU A 1 227 ? 21.180 5.319  20.712 1.00 45.41 ? 222 LEU A CA  1 
ATOM   1727 C  C   . LEU A 1 227 ? 19.821 5.501  20.049 1.00 45.81 ? 222 LEU A C   1 
ATOM   1728 O  O   . LEU A 1 227 ? 18.796 5.567  20.736 1.00 45.00 ? 222 LEU A O   1 
ATOM   1729 C  CB  . LEU A 1 227 ? 21.845 6.673  20.951 1.00 40.22 ? 222 LEU A CB  1 
ATOM   1730 C  CG  . LEU A 1 227 ? 23.150 6.653  21.744 1.00 41.24 ? 222 LEU A CG  1 
ATOM   1731 C  CD1 . LEU A 1 227 ? 23.673 8.074  21.966 1.00 40.18 ? 222 LEU A CD1 1 
ATOM   1732 C  CD2 . LEU A 1 227 ? 22.937 5.939  23.073 1.00 43.19 ? 222 LEU A CD2 1 
ATOM   1733 N  N   . LEU A 1 228 ? 19.786 5.579  18.715 1.00 44.36 ? 223 LEU A N   1 
ATOM   1734 C  CA  . LEU A 1 228 ? 18.505 5.541  18.015 1.00 45.70 ? 223 LEU A CA  1 
ATOM   1735 C  C   . LEU A 1 228 ? 17.715 4.286  18.370 1.00 48.65 ? 223 LEU A C   1 
ATOM   1736 O  O   . LEU A 1 228 ? 16.507 4.353  18.624 1.00 50.76 ? 223 LEU A O   1 
ATOM   1737 C  CB  . LEU A 1 228 ? 18.718 5.607  16.500 1.00 43.24 ? 223 LEU A CB  1 
ATOM   1738 C  CG  . LEU A 1 228 ? 19.209 6.957  15.995 1.00 43.01 ? 223 LEU A CG  1 
ATOM   1739 C  CD1 . LEU A 1 228 ? 19.758 6.788  14.573 1.00 41.72 ? 223 LEU A CD1 1 
ATOM   1740 C  CD2 . LEU A 1 228 ? 18.084 7.967  16.017 1.00 43.16 ? 223 LEU A CD2 1 
ATOM   1741 N  N   . ARG A 1 229 ? 18.380 3.131  18.392 1.00 46.21 ? 224 ARG A N   1 
ATOM   1742 C  CA  . ARG A 1 229 ? 17.675 1.890  18.714 1.00 48.67 ? 224 ARG A CA  1 
ATOM   1743 C  C   . ARG A 1 229 ? 17.245 1.845  20.174 1.00 53.40 ? 224 ARG A C   1 
ATOM   1744 O  O   . ARG A 1 229 ? 16.197 1.267  20.486 1.00 56.38 ? 224 ARG A O   1 
ATOM   1745 C  CB  . ARG A 1 229 ? 18.549 0.681  18.382 1.00 51.34 ? 224 ARG A CB  1 
ATOM   1746 C  CG  . ARG A 1 229 ? 18.250 0.068  17.028 1.00 58.27 ? 224 ARG A CG  1 
ATOM   1747 C  CD  . ARG A 1 229 ? 17.601 -1.307 17.146 1.00 57.35 ? 224 ARG A CD  1 
ATOM   1748 N  NE  . ARG A 1 229 ? 17.729 -2.086 15.919 1.00 65.64 ? 224 ARG A NE  1 
ATOM   1749 C  CZ  . ARG A 1 229 ? 18.482 -3.174 15.786 1.00 66.74 ? 224 ARG A CZ  1 
ATOM   1750 N  NH1 . ARG A 1 229 ? 19.216 -3.636 16.787 1.00 68.14 ? 224 ARG A NH1 1 
ATOM   1751 N  NH2 . ARG A 1 229 ? 18.492 -3.819 14.620 1.00 68.47 ? 224 ARG A NH2 1 
ATOM   1752 N  N   . ASP A 1 230 ? 18.036 2.432  21.076 1.00 51.55 ? 225 ASP A N   1 
ATOM   1753 C  CA  . ASP A 1 230 ? 17.631 2.508  22.479 1.00 53.41 ? 225 ASP A CA  1 
ATOM   1754 C  C   . ASP A 1 230 ? 16.350 3.319  22.629 1.00 55.51 ? 225 ASP A C   1 
ATOM   1755 O  O   . ASP A 1 230 ? 15.416 2.904  23.326 1.00 55.60 ? 225 ASP A O   1 
ATOM   1756 C  CB  . ASP A 1 230 ? 18.740 3.123  23.330 1.00 50.59 ? 225 ASP A CB  1 
ATOM   1757 C  CG  . ASP A 1 230 ? 19.991 2.269  23.392 1.00 49.00 ? 225 ASP A CG  1 
ATOM   1758 O  OD1 . ASP A 1 230 ? 19.941 1.090  22.994 1.00 56.96 ? 225 ASP A OD1 1 
ATOM   1759 O  OD2 . ASP A 1 230 ? 21.032 2.791  23.858 1.00 52.38 ? 225 ASP A OD2 1 
ATOM   1760 N  N   . ASN A 1 231 ? 16.298 4.494  21.992 1.00 52.98 ? 226 ASN A N   1 
ATOM   1761 C  CA  . ASN A 1 231 ? 15.087 5.308  22.037 1.00 56.72 ? 226 ASN A CA  1 
ATOM   1762 C  C   . ASN A 1 231 ? 13.901 4.578  21.418 1.00 58.91 ? 226 ASN A C   1 
ATOM   1763 O  O   . ASN A 1 231 ? 12.788 4.631  21.951 1.00 61.46 ? 226 ASN A O   1 
ATOM   1764 C  CB  . ASN A 1 231 ? 15.317 6.642  21.328 1.00 54.44 ? 226 ASN A CB  1 
ATOM   1765 C  CG  . ASN A 1 231 ? 16.058 7.641  22.199 1.00 51.39 ? 226 ASN A CG  1 
ATOM   1766 O  OD1 . ASN A 1 231 ? 16.192 7.446  23.407 1.00 52.46 ? 226 ASN A OD1 1 
ATOM   1767 N  ND2 . ASN A 1 231 ? 16.534 8.720  21.591 1.00 48.76 ? 226 ASN A ND2 1 
ATOM   1768 N  N   . LEU A 1 232 ? 14.109 3.909  20.283 1.00 56.65 ? 227 LEU A N   1 
ATOM   1769 C  CA  . LEU A 1 232 ? 13.011 3.169  19.670 1.00 59.05 ? 227 LEU A CA  1 
ATOM   1770 C  C   . LEU A 1 232 ? 12.499 2.077  20.600 1.00 63.74 ? 227 LEU A C   1 
ATOM   1771 O  O   . LEU A 1 232 ? 11.293 1.806  20.651 1.00 65.75 ? 227 LEU A O   1 
ATOM   1772 C  CB  . LEU A 1 232 ? 13.455 2.580  18.334 1.00 56.95 ? 227 LEU A CB  1 
ATOM   1773 C  CG  . LEU A 1 232 ? 13.543 3.646  17.248 1.00 55.81 ? 227 LEU A CG  1 
ATOM   1774 C  CD1 . LEU A 1 232 ? 14.263 3.114  16.025 1.00 54.70 ? 227 LEU A CD1 1 
ATOM   1775 C  CD2 . LEU A 1 232 ? 12.143 4.140  16.893 1.00 58.66 ? 227 LEU A CD2 1 
ATOM   1776 N  N   . THR A 1 233 ? 13.399 1.439  21.347 1.00 59.04 ? 228 THR A N   1 
ATOM   1777 C  CA  . THR A 1 233 ? 12.965 0.411  22.284 1.00 64.17 ? 228 THR A CA  1 
ATOM   1778 C  C   . THR A 1 233 ? 12.187 1.029  23.437 1.00 66.46 ? 228 THR A C   1 
ATOM   1779 O  O   . THR A 1 233 ? 11.160 0.487  23.868 1.00 69.69 ? 228 THR A O   1 
ATOM   1780 C  CB  . THR A 1 233 ? 14.177 -0.371 22.797 1.00 64.93 ? 228 THR A CB  1 
ATOM   1781 O  OG1 . THR A 1 233 ? 14.703 -1.179 21.739 1.00 64.31 ? 228 THR A OG1 1 
ATOM   1782 C  CG2 . THR A 1 233 ? 13.793 -1.270 23.969 1.00 68.81 ? 228 THR A CG2 1 
ATOM   1783 N  N   . LEU A 1 234 ? 12.650 2.177  23.931 1.00 64.75 ? 229 LEU A N   1 
ATOM   1784 C  CA  . LEU A 1 234 ? 11.959 2.851  25.024 1.00 66.20 ? 229 LEU A CA  1 
ATOM   1785 C  C   . LEU A 1 234 ? 10.591 3.360  24.579 1.00 68.75 ? 229 LEU A C   1 
ATOM   1786 O  O   . LEU A 1 234 ? 9.620  3.294  25.343 1.00 69.80 ? 229 LEU A O   1 
ATOM   1787 C  CB  . LEU A 1 234 ? 12.832 3.990  25.557 1.00 64.50 ? 229 LEU A CB  1 
ATOM   1788 C  CG  . LEU A 1 234 ? 12.251 4.988  26.558 1.00 68.57 ? 229 LEU A CG  1 
ATOM   1789 C  CD1 . LEU A 1 234 ? 12.384 4.449  27.965 1.00 75.09 ? 229 LEU A CD1 1 
ATOM   1790 C  CD2 . LEU A 1 234 ? 12.957 6.334  26.441 1.00 66.44 ? 229 LEU A CD2 1 
ATOM   1791 N  N   . TRP A 1 235 ? 10.482 3.837  23.339 1.00 64.90 ? 230 TRP A N   1 
ATOM   1792 C  CA  . TRP A 1 235 ? 9.230  4.397  22.845 1.00 65.94 ? 230 TRP A CA  1 
ATOM   1793 C  C   . TRP A 1 235 ? 8.253  3.347  22.329 1.00 71.29 ? 230 TRP A C   1 
ATOM   1794 O  O   . TRP A 1 235 ? 7.114  3.702  22.007 1.00 72.47 ? 230 TRP A O   1 
ATOM   1795 C  CB  . TRP A 1 235 ? 9.509  5.402  21.725 1.00 65.44 ? 230 TRP A CB  1 
ATOM   1796 C  CG  . TRP A 1 235 ? 10.439 6.499  22.108 1.00 61.83 ? 230 TRP A CG  1 
ATOM   1797 C  CD1 . TRP A 1 235 ? 10.786 6.880  23.371 1.00 62.03 ? 230 TRP A CD1 1 
ATOM   1798 C  CD2 . TRP A 1 235 ? 11.159 7.358  21.217 1.00 59.73 ? 230 TRP A CD2 1 
ATOM   1799 N  NE1 . TRP A 1 235 ? 11.672 7.931  23.321 1.00 61.06 ? 230 TRP A NE1 1 
ATOM   1800 C  CE2 . TRP A 1 235 ? 11.918 8.240  22.009 1.00 58.13 ? 230 TRP A CE2 1 
ATOM   1801 C  CE3 . TRP A 1 235 ? 11.233 7.467  19.823 1.00 59.19 ? 230 TRP A CE3 1 
ATOM   1802 C  CZ2 . TRP A 1 235 ? 12.739 9.221  21.456 1.00 56.56 ? 230 TRP A CZ2 1 
ATOM   1803 C  CZ3 . TRP A 1 235 ? 12.054 8.443  19.277 1.00 57.58 ? 230 TRP A CZ3 1 
ATOM   1804 C  CH2 . TRP A 1 235 ? 12.795 9.305  20.093 1.00 55.26 ? 230 TRP A CH2 1 
ATOM   1805 N  N   . THR A 1 236 ? 8.664  2.085  22.220 1.00 69.98 ? 231 THR A N   1 
ATOM   1806 C  CA  . THR A 1 236 ? 7.779  1.025  21.745 1.00 72.88 ? 231 THR A CA  1 
ATOM   1807 C  C   . THR A 1 236 ? 7.671  -0.118 22.757 1.00 75.68 ? 231 THR A C   1 
ATOM   1808 O  O   . THR A 1 236 ? 6.793  -0.967 22.629 1.00 80.32 ? 231 THR A O   1 
ATOM   1809 C  CB  . THR A 1 236 ? 8.249  0.453  20.391 1.00 76.17 ? 231 THR A CB  1 
ATOM   1810 O  OG1 . THR A 1 236 ? 9.579  -0.060 20.523 1.00 75.39 ? 231 THR A OG1 1 
ATOM   1811 C  CG2 . THR A 1 236 ? 8.221  1.522  19.307 1.00 71.92 ? 231 THR A CG2 1 
ATOM   1812 O  OXT . THR A 1 236 ? 8.429  -0.225 23.728 1.00 75.15 ? 231 THR A OXT 1 
ATOM   1813 N  N   . GLN B 2 1   ? 11.940 7.461  32.659 1.00 94.12 ? 255 GLN P N   1 
ATOM   1814 C  CA  . GLN B 2 1   ? 13.218 7.460  31.956 1.00 89.84 ? 255 GLN P CA  1 
ATOM   1815 C  C   . GLN B 2 1   ? 13.198 8.404  30.758 1.00 84.19 ? 255 GLN P C   1 
ATOM   1816 O  O   . GLN B 2 1   ? 12.311 8.331  29.908 1.00 83.28 ? 255 GLN P O   1 
ATOM   1817 C  CB  . GLN B 2 1   ? 13.575 6.050  31.497 1.00 89.80 ? 255 GLN P CB  1 
ATOM   1818 C  CG  . GLN B 2 1   ? 14.875 5.979  30.728 1.00 89.57 ? 255 GLN P CG  1 
ATOM   1819 C  CD  . GLN B 2 1   ? 15.234 4.566  30.331 1.00 92.57 ? 255 GLN P CD  1 
ATOM   1820 O  OE1 . GLN B 2 1   ? 14.593 3.605  30.761 1.00 96.15 ? 255 GLN P OE1 1 
ATOM   1821 N  NE2 . GLN B 2 1   ? 16.264 4.429  29.503 1.00 92.11 ? 255 GLN P NE2 1 
ATOM   1822 N  N   . ARG B 2 2   ? 14.189 9.285  30.691 1.00 82.01 ? 256 ARG P N   1 
ATOM   1823 C  CA  . ARG B 2 2   ? 14.240 10.291 29.644 1.00 75.22 ? 256 ARG P CA  1 
ATOM   1824 C  C   . ARG B 2 2   ? 14.748 9.692  28.338 1.00 69.23 ? 256 ARG P C   1 
ATOM   1825 O  O   . ARG B 2 2   ? 15.469 8.688  28.322 1.00 67.67 ? 256 ARG P O   1 
ATOM   1826 C  CB  . ARG B 2 2   ? 15.143 11.450 30.067 1.00 72.83 ? 256 ARG P CB  1 
ATOM   1827 C  CG  . ARG B 2 2   ? 14.735 12.809 29.523 1.00 69.44 ? 256 ARG P CG  1 
ATOM   1828 C  CD  . ARG B 2 2   ? 15.216 13.904 30.464 1.00 69.16 ? 256 ARG P CD  1 
ATOM   1829 N  NE  . ARG B 2 2   ? 14.154 14.406 31.330 1.00 71.14 ? 256 ARG P NE  1 
ATOM   1830 C  CZ  . ARG B 2 2   ? 14.155 14.299 32.652 1.00 70.92 ? 256 ARG P CZ  1 
ATOM   1831 N  NH1 . ARG B 2 2   ? 15.110 13.641 33.292 1.00 70.91 ? 256 ARG P NH1 1 
ATOM   1832 N  NH2 . ARG B 2 2   ? 13.175 14.868 33.353 1.00 70.92 ? 256 ARG P NH2 1 
ATOM   1833 N  N   . SER B 2 3   ? 14.355 10.311 27.232 1.00 64.53 ? 257 SER P N   1 
ATOM   1834 C  CA  . SER B 2 3   ? 14.952 9.936  25.964 1.00 58.21 ? 257 SER P CA  1 
ATOM   1835 C  C   . SER B 2 3   ? 16.430 10.306 25.969 1.00 54.41 ? 257 SER P C   1 
ATOM   1836 O  O   . SER B 2 3   ? 16.876 11.187 26.711 1.00 54.84 ? 257 SER P O   1 
ATOM   1837 C  CB  . SER B 2 3   ? 14.230 10.618 24.804 1.00 56.44 ? 257 SER P CB  1 
ATOM   1838 O  OG  . SER B 2 3   ? 12.861 10.258 24.774 1.00 58.41 ? 257 SER P OG  1 
ATOM   1839 N  N   . THR B 2 4   ? 17.199 9.614  25.138 1.00 50.62 ? 258 THR P N   1 
ATOM   1840 C  CA  . THR B 2 4   ? 18.628 9.877  25.071 1.00 46.09 ? 258 THR P CA  1 
ATOM   1841 C  C   . THR B 2 4   ? 18.967 10.697 23.844 1.00 42.92 ? 258 THR P C   1 
ATOM   1842 O  O   . THR B 2 4   ? 18.595 10.325 22.728 1.00 43.61 ? 258 THR P O   1 
ATOM   1843 C  CB  . THR B 2 4   ? 19.444 8.582  25.035 1.00 47.41 ? 258 THR P CB  1 
ATOM   1844 O  OG1 . THR B 2 4   ? 19.090 7.765  26.155 1.00 45.74 ? 258 THR P OG1 1 
ATOM   1845 C  CG2 . THR B 2 4   ? 20.926 8.896  25.107 1.00 46.73 ? 258 THR P CG2 1 
HETATM 1846 N  N   . SEP B 2 5   ? 19.682 11.795 24.056 1.00 40.31 ? 259 SEP P N   1 
HETATM 1847 C  CA  . SEP B 2 5   ? 20.136 12.650 22.961 1.00 38.33 ? 259 SEP P CA  1 
HETATM 1848 C  CB  . SEP B 2 5   ? 19.919 14.140 23.293 1.00 38.19 ? 259 SEP P CB  1 
HETATM 1849 O  OG  . SEP B 2 5   ? 20.648 14.491 24.459 1.00 37.52 ? 259 SEP P OG  1 
HETATM 1850 C  C   . SEP B 2 5   ? 21.610 12.379 22.686 1.00 39.58 ? 259 SEP P C   1 
HETATM 1851 O  O   . SEP B 2 5   ? 22.238 11.572 23.380 1.00 38.32 ? 259 SEP P O   1 
HETATM 1852 P  P   . SEP B 2 5   ? 20.350 16.000 24.989 1.00 37.92 ? 259 SEP P P   1 
HETATM 1853 O  O1P . SEP B 2 5   ? 20.699 17.050 23.831 1.00 36.83 ? 259 SEP P O1P 1 
HETATM 1854 O  O2P . SEP B 2 5   ? 18.814 16.105 25.427 1.00 39.30 ? 259 SEP P O2P 1 
HETATM 1855 O  O3P . SEP B 2 5   ? 21.335 16.114 26.237 1.00 39.23 ? 259 SEP P O3P 1 
ATOM   1856 N  N   . THR B 2 6   ? 22.165 13.047 21.676 1.00 37.82 ? 260 THR P N   1 
ATOM   1857 C  CA  . THR B 2 6   ? 23.589 12.914 21.387 1.00 38.16 ? 260 THR P CA  1 
ATOM   1858 C  C   . THR B 2 6   ? 24.482 13.257 22.584 1.00 39.95 ? 260 THR P C   1 
ATOM   1859 O  O   . THR B 2 6   ? 24.273 14.271 23.239 1.00 39.33 ? 260 THR P O   1 
ATOM   1860 C  CB  . THR B 2 6   ? 23.971 13.756 20.133 1.00 40.16 ? 260 THR P CB  1 
ATOM   1861 O  OG1 . THR B 2 6   ? 22.926 13.659 19.127 1.00 41.07 ? 260 THR P OG1 1 
ATOM   1862 C  CG2 . THR B 2 6   ? 25.286 13.316 19.555 1.00 43.92 ? 260 THR P CG2 1 
ATOM   1863 N  N   . PRO B 2 7   ? 25.443 12.381 22.883 1.00 40.65 ? 261 PRO P N   1 
ATOM   1864 C  CA  . PRO B 2 7   ? 26.341 12.591 24.023 1.00 43.05 ? 261 PRO P CA  1 
ATOM   1865 C  C   . PRO B 2 7   ? 27.594 13.370 23.634 1.00 45.24 ? 261 PRO P C   1 
ATOM   1866 O  O   . PRO B 2 7   ? 27.864 13.615 22.464 1.00 43.30 ? 261 PRO P O   1 
ATOM   1867 C  CB  . PRO B 2 7   ? 26.710 11.157 24.428 1.00 41.85 ? 261 PRO P CB  1 
ATOM   1868 C  CG  . PRO B 2 7   ? 26.734 10.433 23.114 1.00 45.32 ? 261 PRO P CG  1 
ATOM   1869 C  CD  . PRO B 2 7   ? 25.652 11.060 22.262 1.00 41.66 ? 261 PRO P CD  1 
ATOM   1870 N  N   . ASN B 2 8   ? 28.375 13.741 24.654 1.00 43.97 ? 262 ASN P N   1 
ATOM   1871 C  CA  . ASN B 2 8   ? 29.712 14.284 24.410 1.00 45.32 ? 262 ASN P CA  1 
ATOM   1872 C  C   . ASN B 2 8   ? 30.721 13.173 24.132 1.00 51.74 ? 262 ASN P C   1 
ATOM   1873 O  O   . ASN B 2 8   ? 30.684 12.115 24.766 1.00 56.79 ? 262 ASN P O   1 
ATOM   1874 C  CB  . ASN B 2 8   ? 30.176 15.084 25.616 1.00 47.38 ? 262 ASN P CB  1 
ATOM   1875 C  CG  . ASN B 2 8   ? 29.401 16.373 25.786 1.00 43.94 ? 262 ASN P CG  1 
ATOM   1876 O  OD1 . ASN B 2 8   ? 29.354 17.213 24.893 1.00 39.47 ? 262 ASN P OD1 1 
ATOM   1877 N  ND2 . ASN B 2 8   ? 28.757 16.517 26.934 1.00 47.47 ? 262 ASN P ND2 1 
ATOM   1878 N  N   . VAL B 2 9   ? 31.645 13.418 23.200 1.00 55.25 ? 263 VAL P N   1 
ATOM   1879 C  CA  . VAL B 2 9   ? 32.755 12.501 22.948 1.00 62.66 ? 263 VAL P CA  1 
ATOM   1880 C  C   . VAL B 2 9   ? 34.016 13.284 22.603 1.00 63.69 ? 263 VAL P C   1 
ATOM   1881 O  O   . VAL B 2 9   ? 33.960 14.368 22.012 1.00 61.50 ? 263 VAL P O   1 
ATOM   1882 C  CB  . VAL B 2 9   ? 32.464 11.475 21.821 1.00 62.71 ? 263 VAL P CB  1 
ATOM   1883 C  CG1 . VAL B 2 9   ? 31.180 10.698 22.085 1.00 58.84 ? 263 VAL P CG1 1 
ATOM   1884 C  CG2 . VAL B 2 9   ? 32.410 12.165 20.460 1.00 59.14 ? 263 VAL P CG2 1 
ATOM   1885 N  N   . HIS B 2 10  ? 35.160 12.724 22.996 1.00 67.41 ? 264 HIS P N   1 
ATOM   1886 C  CA  . HIS B 2 10  ? 36.484 13.174 22.544 1.00 70.50 ? 264 HIS P CA  1 
ATOM   1887 C  C   . HIS B 2 10  ? 36.810 14.660 22.784 1.00 65.44 ? 264 HIS P C   1 
ATOM   1888 O  O   . HIS B 2 10  ? 36.164 15.389 23.550 1.00 58.51 ? 264 HIS P O   1 
ATOM   1889 C  CB  . HIS B 2 10  ? 36.645 12.860 21.050 1.00 71.87 ? 264 HIS P CB  1 
ATOM   1890 O  OXT . HIS B 2 10  ? 37.777 15.165 22.204 1.00 64.56 ? 264 HIS P OXT 1 
HETATM 1891 CL CL  . CL  C 3 .   ? 17.655 31.805 45.302 1.00 41.15 ? 301 CL  A CL  1 
HETATM 1892 MG MG  . MG  D 4 .   ? 12.336 32.170 34.570 1.00 66.08 ? 302 MG  A MG  1 
HETATM 1893 MG MG  . MG  E 4 .   ? -0.035 22.998 53.778 1.00 99.86 ? 303 MG  A MG  1 
HETATM 1894 MG MG  . MG  F 4 .   ? 49.295 38.633 17.596 1.00 52.42 ? 304 MG  A MG  1 
HETATM 1895 O  O1  . WQ9 G 5 .   ? 32.168 19.388 12.902 1.00 41.14 ? 305 WQ9 A O1  1 
HETATM 1896 C  C1  . WQ9 G 5 .   ? 32.642 18.320 13.265 1.00 40.80 ? 305 WQ9 A C1  1 
HETATM 1897 C  C2  . WQ9 G 5 .   ? 33.589 17.536 12.372 1.00 41.34 ? 305 WQ9 A C2  1 
HETATM 1898 N  N1  . WQ9 G 5 .   ? 32.378 17.829 14.489 1.00 40.22 ? 305 WQ9 A N1  1 
HETATM 1899 C  C3  . WQ9 G 5 .   ? 32.389 16.449 14.972 1.00 40.84 ? 305 WQ9 A C3  1 
HETATM 1900 C  C4  . WQ9 G 5 .   ? 32.097 16.732 16.439 1.00 38.65 ? 305 WQ9 A C4  1 
HETATM 1901 C  C5  . WQ9 G 5 .   ? 31.022 17.858 16.471 1.00 39.22 ? 305 WQ9 A C5  1 
HETATM 1902 C  C6  . WQ9 G 5 .   ? 30.822 18.167 17.963 1.00 38.47 ? 305 WQ9 A C6  1 
HETATM 1903 C  C7  . WQ9 G 5 .   ? 29.635 17.324 18.344 1.00 38.67 ? 305 WQ9 A C7  1 
HETATM 1904 N  N2  . WQ9 G 5 .   ? 28.909 17.137 17.069 1.00 36.73 ? 305 WQ9 A N2  1 
HETATM 1905 S  S1  . WQ9 G 5 .   ? 27.542 16.267 17.128 1.00 40.14 ? 305 WQ9 A S1  1 
HETATM 1906 O  O2  . WQ9 G 5 .   ? 27.056 16.189 15.783 1.00 40.93 ? 305 WQ9 A O2  1 
HETATM 1907 O  O3  . WQ9 G 5 .   ? 26.729 16.861 18.140 1.00 43.64 ? 305 WQ9 A O3  1 
HETATM 1908 C  C8  . WQ9 G 5 .   ? 27.968 14.641 17.667 1.00 41.18 ? 305 WQ9 A C8  1 
HETATM 1909 C  C9  . WQ9 G 5 .   ? 28.318 14.414 18.990 1.00 39.77 ? 305 WQ9 A C9  1 
HETATM 1910 C  C10 . WQ9 G 5 .   ? 28.653 13.140 19.420 1.00 43.45 ? 305 WQ9 A C10 1 
HETATM 1911 C  C11 . WQ9 G 5 .   ? 28.635 12.079 18.535 1.00 42.58 ? 305 WQ9 A C11 1 
HETATM 1912 BR BR1 . WQ9 G 5 .   ? 29.085 10.321 19.110 1.00 56.64 ? 305 WQ9 A BR1 1 
HETATM 1913 C  C12 . WQ9 G 5 .   ? 28.286 12.332 17.221 1.00 40.33 ? 305 WQ9 A C12 1 
HETATM 1914 F  F1  . WQ9 G 5 .   ? 28.264 11.323 16.350 1.00 43.60 ? 305 WQ9 A F1  1 
HETATM 1915 C  C13 . WQ9 G 5 .   ? 27.948 13.588 16.767 1.00 38.08 ? 305 WQ9 A C13 1 
HETATM 1916 C  C14 . WQ9 G 5 .   ? 29.948 16.836 16.060 1.00 38.00 ? 305 WQ9 A C14 1 
HETATM 1917 C  C15 . WQ9 G 5 .   ? 32.049 18.665 15.648 1.00 39.77 ? 305 WQ9 A C15 1 
HETATM 1918 O  O   . HOH H 6 .   ? 10.291 31.198 34.283 1.00 55.91 ? 401 HOH A O   1 
HETATM 1919 O  O   . HOH H 6 .   ? 41.638 39.177 27.106 1.00 47.25 ? 402 HOH A O   1 
HETATM 1920 O  O   . HOH H 6 .   ? 32.201 7.790  19.757 1.00 46.86 ? 403 HOH A O   1 
HETATM 1921 O  O   . HOH H 6 .   ? 31.476 13.938 10.304 1.00 44.94 ? 404 HOH A O   1 
HETATM 1922 O  O   . HOH H 6 .   ? 46.076 19.871 26.047 1.00 49.00 ? 405 HOH A O   1 
HETATM 1923 O  O   . HOH H 6 .   ? 41.634 41.847 20.534 1.00 43.84 ? 406 HOH A O   1 
HETATM 1924 O  O   . HOH H 6 .   ? 39.645 2.428  3.647  1.00 60.93 ? 407 HOH A O   1 
HETATM 1925 O  O   . HOH H 6 .   ? 19.081 30.150 11.438 1.00 56.65 ? 408 HOH A O   1 
HETATM 1926 O  O   . HOH H 6 .   ? 21.783 21.792 0.664  1.00 58.74 ? 409 HOH A O   1 
HETATM 1927 O  O   . HOH H 6 .   ? 36.352 38.187 23.082 1.00 50.22 ? 410 HOH A O   1 
HETATM 1928 O  O   . HOH H 6 .   ? 43.307 24.760 16.065 1.00 41.30 ? 411 HOH A O   1 
HETATM 1929 O  O   . HOH H 6 .   ? 15.184 33.471 42.157 1.00 42.04 ? 412 HOH A O   1 
HETATM 1930 O  O   . HOH H 6 .   ? 15.149 28.709 14.138 1.00 53.50 ? 413 HOH A O   1 
HETATM 1931 O  O   . HOH H 6 .   ? 23.897 27.784 7.290  1.00 50.53 ? 414 HOH A O   1 
HETATM 1932 O  O   . HOH H 6 .   ? 38.377 5.878  13.548 1.00 46.63 ? 415 HOH A O   1 
HETATM 1933 O  O   . HOH H 6 .   ? 23.491 19.091 27.855 1.00 45.79 ? 416 HOH A O   1 
HETATM 1934 O  O   . HOH H 6 .   ? 32.582 11.343 8.992  1.00 42.00 ? 417 HOH A O   1 
HETATM 1935 O  O   . HOH H 6 .   ? 41.792 22.200 14.063 1.00 44.74 ? 418 HOH A O   1 
HETATM 1936 O  O   . HOH H 6 .   ? 33.938 19.971 8.447  1.00 50.09 ? 419 HOH A O   1 
HETATM 1937 O  O   . HOH H 6 .   ? 20.821 32.297 14.460 1.00 49.97 ? 420 HOH A O   1 
HETATM 1938 O  O   . HOH H 6 .   ? 25.583 0.397  16.688 1.00 44.01 ? 421 HOH A O   1 
HETATM 1939 O  O   . HOH H 6 .   ? 26.782 23.528 34.918 1.00 38.66 ? 422 HOH A O   1 
HETATM 1940 O  O   . HOH H 6 .   ? 28.154 29.460 33.303 1.00 48.64 ? 423 HOH A O   1 
HETATM 1941 O  O   . HOH H 6 .   ? 39.930 18.008 37.307 1.00 43.59 ? 424 HOH A O   1 
HETATM 1942 O  O   . HOH H 6 .   ? 31.446 8.022  3.659  1.00 49.00 ? 425 HOH A O   1 
HETATM 1943 O  O   . HOH H 6 .   ? 45.291 19.086 19.805 1.00 49.91 ? 426 HOH A O   1 
HETATM 1944 O  O   . HOH H 6 .   ? 23.112 25.414 3.356  1.00 53.95 ? 427 HOH A O   1 
HETATM 1945 O  O   . HOH H 6 .   ? 40.707 39.552 30.527 1.00 47.63 ? 428 HOH A O   1 
HETATM 1946 O  O   . HOH H 6 .   ? 37.636 32.188 15.116 1.00 38.35 ? 429 HOH A O   1 
HETATM 1947 O  O   . HOH H 6 .   ? 29.334 17.541 22.233 1.00 38.08 ? 430 HOH A O   1 
HETATM 1948 O  O   . HOH H 6 .   ? 20.192 33.480 45.684 1.00 44.85 ? 431 HOH A O   1 
HETATM 1949 O  O   . HOH H 6 .   ? 15.552 19.602 31.519 1.00 44.80 ? 432 HOH A O   1 
HETATM 1950 O  O   . HOH H 6 .   ? 26.901 21.988 22.824 1.00 39.45 ? 433 HOH A O   1 
HETATM 1951 O  O   . HOH H 6 .   ? 19.902 4.766  3.143  1.00 48.30 ? 434 HOH A O   1 
HETATM 1952 O  O   . HOH H 6 .   ? 16.791 22.930 29.776 1.00 38.35 ? 435 HOH A O   1 
HETATM 1953 O  O   . HOH H 6 .   ? 29.998 37.858 20.774 1.00 54.11 ? 436 HOH A O   1 
HETATM 1954 O  O   . HOH H 6 .   ? 8.574  27.269 46.673 1.00 42.96 ? 437 HOH A O   1 
HETATM 1955 O  O   . HOH H 6 .   ? 11.051 20.140 30.973 1.00 47.34 ? 438 HOH A O   1 
HETATM 1956 O  O   . HOH H 6 .   ? 32.997 27.632 11.550 1.00 44.41 ? 439 HOH A O   1 
HETATM 1957 O  O   . HOH H 6 .   ? 26.702 35.342 22.706 1.00 48.39 ? 440 HOH A O   1 
HETATM 1958 O  O   . HOH H 6 .   ? 37.448 20.893 9.855  1.00 41.82 ? 441 HOH A O   1 
HETATM 1959 O  O   . HOH H 6 .   ? 31.188 7.376  9.875  1.00 38.15 ? 442 HOH A O   1 
HETATM 1960 O  O   . HOH H 6 .   ? 33.835 19.428 36.174 1.00 44.18 ? 443 HOH A O   1 
HETATM 1961 O  O   . HOH H 6 .   ? 31.781 30.078 30.457 1.00 39.47 ? 444 HOH A O   1 
HETATM 1962 O  O   . HOH H 6 .   ? 31.246 15.814 21.154 1.00 43.75 ? 445 HOH A O   1 
HETATM 1963 O  O   . HOH H 6 .   ? 17.180 5.763  25.313 1.00 53.26 ? 446 HOH A O   1 
HETATM 1964 O  O   . HOH H 6 .   ? 31.238 29.582 10.617 1.00 47.52 ? 447 HOH A O   1 
HETATM 1965 O  O   . HOH H 6 .   ? 30.547 31.512 28.170 1.00 39.40 ? 448 HOH A O   1 
HETATM 1966 O  O   . HOH H 6 .   ? 23.226 0.000  0.000  0.50 47.34 ? 449 HOH A O   1 
HETATM 1967 O  O   . HOH H 6 .   ? 41.640 18.429 25.678 1.00 38.35 ? 450 HOH A O   1 
HETATM 1968 O  O   . HOH H 6 .   ? 9.164  23.658 38.164 1.00 50.20 ? 451 HOH A O   1 
HETATM 1969 O  O   . HOH H 6 .   ? 18.679 15.737 37.435 1.00 42.56 ? 452 HOH A O   1 
HETATM 1970 O  O   . HOH H 6 .   ? 42.677 5.198  8.584  1.00 59.16 ? 453 HOH A O   1 
HETATM 1971 O  O   . HOH H 6 .   ? 38.231 37.137 21.230 1.00 44.67 ? 454 HOH A O   1 
HETATM 1972 O  O   . HOH H 6 .   ? 9.931  26.953 34.303 1.00 47.85 ? 455 HOH A O   1 
HETATM 1973 O  O   . HOH H 6 .   ? 24.051 32.377 32.719 1.00 42.31 ? 456 HOH A O   1 
HETATM 1974 O  O   . HOH H 6 .   ? 16.923 10.700 8.740  1.00 48.38 ? 457 HOH A O   1 
HETATM 1975 O  O   . HOH H 6 .   ? 40.755 26.588 12.514 1.00 44.25 ? 458 HOH A O   1 
HETATM 1976 O  O   . HOH H 6 .   ? 35.568 16.048 27.582 1.00 41.96 ? 459 HOH A O   1 
HETATM 1977 O  O   . HOH H 6 .   ? 25.096 17.321 20.834 1.00 42.41 ? 460 HOH A O   1 
HETATM 1978 O  O   . HOH H 6 .   ? 18.321 9.108  7.111  1.00 45.49 ? 461 HOH A O   1 
HETATM 1979 O  O   . HOH H 6 .   ? 19.002 12.232 8.078  1.00 46.55 ? 462 HOH A O   1 
HETATM 1980 O  O   . HOH H 6 .   ? -1.050 34.982 23.914 1.00 68.78 ? 463 HOH A O   1 
HETATM 1981 O  O   . HOH H 6 .   ? 29.372 27.133 7.671  1.00 48.48 ? 464 HOH A O   1 
HETATM 1982 O  O   . HOH H 6 .   ? 18.944 34.790 31.701 1.00 44.32 ? 465 HOH A O   1 
HETATM 1983 O  O   . HOH H 6 .   ? 26.604 21.070 20.140 1.00 38.53 ? 466 HOH A O   1 
HETATM 1984 O  O   . HOH H 6 .   ? 26.663 34.284 11.614 1.00 49.45 ? 467 HOH A O   1 
HETATM 1985 O  O   . HOH H 6 .   ? 33.851 32.830 14.128 1.00 45.27 ? 468 HOH A O   1 
HETATM 1986 O  O   . HOH H 6 .   ? 31.172 3.037  19.039 1.00 45.49 ? 469 HOH A O   1 
HETATM 1987 O  O   . HOH H 6 .   ? 34.698 34.438 26.742 1.00 37.44 ? 470 HOH A O   1 
HETATM 1988 O  O   . HOH H 6 .   ? 14.799 17.472 25.182 1.00 44.62 ? 471 HOH A O   1 
HETATM 1989 O  O   . HOH H 6 .   ? 20.388 33.376 38.233 1.00 43.88 ? 472 HOH A O   1 
HETATM 1990 O  O   . HOH H 6 .   ? 46.264 26.169 19.299 1.00 37.41 ? 473 HOH A O   1 
HETATM 1991 O  O   . HOH H 6 .   ? 37.969 31.852 8.670  1.00 49.61 ? 474 HOH A O   1 
HETATM 1992 O  O   . HOH H 6 .   ? 13.575 31.891 27.036 1.00 56.45 ? 475 HOH A O   1 
HETATM 1993 O  O   . HOH H 6 .   ? 49.196 23.126 26.097 1.00 49.38 ? 476 HOH A O   1 
HETATM 1994 O  O   . HOH H 6 .   ? 17.475 -1.852 9.477  1.00 54.43 ? 477 HOH A O   1 
HETATM 1995 O  O   . HOH H 6 .   ? 13.281 29.410 28.303 1.00 46.77 ? 478 HOH A O   1 
HETATM 1996 O  O   . HOH H 6 .   ? 20.343 7.758  8.192  1.00 45.59 ? 479 HOH A O   1 
HETATM 1997 O  O   . HOH H 6 .   ? 25.259 -1.050 2.527  1.00 46.83 ? 480 HOH A O   1 
HETATM 1998 O  O   . HOH H 6 .   ? 40.297 29.236 11.457 1.00 49.90 ? 481 HOH A O   1 
HETATM 1999 O  O   . HOH H 6 .   ? 17.779 -1.176 6.793  1.00 51.59 ? 482 HOH A O   1 
HETATM 2000 O  O   . HOH H 6 .   ? 27.522 27.766 9.173  1.00 43.13 ? 483 HOH A O   1 
HETATM 2001 O  O   . HOH H 6 .   ? 29.863 8.374  7.559  1.00 37.70 ? 484 HOH A O   1 
HETATM 2002 O  O   . HOH H 6 .   ? 11.936 17.548 36.889 1.00 46.08 ? 485 HOH A O   1 
HETATM 2003 O  O   . HOH H 6 .   ? 46.563 22.376 25.147 1.00 40.68 ? 486 HOH A O   1 
HETATM 2004 O  O   . HOH H 6 .   ? 42.610 22.166 17.300 1.00 43.91 ? 487 HOH A O   1 
HETATM 2005 O  O   . HOH H 6 .   ? 24.773 26.717 9.636  1.00 43.85 ? 488 HOH A O   1 
HETATM 2006 O  O   . HOH H 6 .   ? 38.329 18.404 19.822 1.00 40.34 ? 489 HOH A O   1 
HETATM 2007 O  O   . HOH H 6 .   ? 46.602 32.898 17.032 1.00 41.21 ? 490 HOH A O   1 
HETATM 2008 O  O   . HOH H 6 .   ? 24.454 19.703 21.680 1.00 56.21 ? 491 HOH A O   1 
HETATM 2009 O  O   . HOH H 6 .   ? 31.519 28.512 7.809  1.00 52.37 ? 492 HOH A O   1 
HETATM 2010 O  O   . HOH H 6 .   ? 13.635 26.102 8.458  1.00 64.73 ? 493 HOH A O   1 
HETATM 2011 O  O   . HOH H 6 .   ? 19.753 14.300 9.792  1.00 44.19 ? 494 HOH A O   1 
HETATM 2012 O  O   . HOH H 6 .   ? 39.553 19.442 12.540 1.00 42.70 ? 495 HOH A O   1 
HETATM 2013 O  O   . HOH H 6 .   ? 20.700 35.293 22.018 1.00 51.79 ? 496 HOH A O   1 
HETATM 2014 O  O   . HOH H 6 .   ? 46.064 23.631 20.385 1.00 40.69 ? 497 HOH A O   1 
HETATM 2015 O  O   . HOH H 6 .   ? 10.698 15.047 11.284 1.00 56.57 ? 498 HOH A O   1 
HETATM 2016 O  O   . HOH H 6 .   ? 32.757 15.869 28.455 1.00 45.57 ? 499 HOH A O   1 
HETATM 2017 O  O   . HOH H 6 .   ? 35.643 6.463  14.739 1.00 42.94 ? 500 HOH A O   1 
HETATM 2018 O  O   . HOH H 6 .   ? 49.735 28.733 21.088 1.00 55.22 ? 501 HOH A O   1 
HETATM 2019 O  O   . HOH H 6 .   ? 9.573  21.228 10.134 1.00 62.10 ? 502 HOH A O   1 
HETATM 2020 O  O   . HOH H 6 .   ? 12.053 20.660 3.341  1.00 75.41 ? 503 HOH A O   1 
HETATM 2021 O  O   . HOH H 6 .   ? 14.527 15.928 42.912 1.00 49.80 ? 504 HOH A O   1 
HETATM 2022 O  O   . HOH H 6 .   ? 23.611 35.728 28.109 1.00 45.47 ? 505 HOH A O   1 
HETATM 2023 O  O   . HOH H 6 .   ? 26.094 33.048 29.955 1.00 48.91 ? 506 HOH A O   1 
HETATM 2024 O  O   . HOH H 6 .   ? 25.323 20.435 17.387 1.00 40.75 ? 507 HOH A O   1 
HETATM 2025 O  O   . HOH H 6 .   ? 35.192 28.569 36.225 1.00 51.97 ? 508 HOH A O   1 
HETATM 2026 O  O   . HOH H 6 .   ? 44.254 29.422 16.199 1.00 41.31 ? 509 HOH A O   1 
HETATM 2027 O  O   . HOH H 6 .   ? 36.909 21.065 37.858 1.00 43.46 ? 510 HOH A O   1 
HETATM 2028 O  O   . HOH H 6 .   ? 10.220 26.080 49.679 1.00 46.08 ? 511 HOH A O   1 
HETATM 2029 O  O   . HOH H 6 .   ? 40.965 18.404 20.760 1.00 53.33 ? 512 HOH A O   1 
HETATM 2030 O  O   . HOH H 6 .   ? 35.706 25.898 34.846 1.00 38.46 ? 513 HOH A O   1 
HETATM 2031 O  O   . HOH H 6 .   ? 12.528 15.036 44.015 1.00 57.68 ? 514 HOH A O   1 
HETATM 2032 O  O   . HOH H 6 .   ? 49.234 32.590 17.605 1.00 45.91 ? 515 HOH A O   1 
HETATM 2033 O  O   . HOH H 6 .   ? 40.771 40.024 19.012 1.00 55.15 ? 516 HOH A O   1 
HETATM 2034 O  O   . HOH H 6 .   ? 6.225  29.097 45.513 1.00 52.29 ? 517 HOH A O   1 
HETATM 2035 O  O   . HOH H 6 .   ? 30.745 10.904 6.789  1.00 42.24 ? 518 HOH A O   1 
HETATM 2036 O  O   . HOH H 6 .   ? 15.912 33.151 27.044 1.00 62.48 ? 519 HOH A O   1 
HETATM 2037 O  O   . HOH H 6 .   ? 15.856 32.037 14.907 1.00 65.43 ? 520 HOH A O   1 
HETATM 2038 O  O   . HOH H 6 .   ? 26.152 34.228 5.437  1.00 61.74 ? 521 HOH A O   1 
HETATM 2039 O  O   . HOH H 6 .   ? 18.625 14.349 29.303 1.00 53.01 ? 522 HOH A O   1 
HETATM 2040 O  O   . HOH H 6 .   ? 28.348 33.243 4.180  1.00 60.50 ? 523 HOH A O   1 
HETATM 2041 O  O   . HOH H 6 .   ? 5.585  31.930 47.112 1.00 53.24 ? 524 HOH A O   1 
HETATM 2042 O  O   . HOH H 6 .   ? 33.950 25.072 6.405  1.00 63.33 ? 525 HOH A O   1 
HETATM 2043 O  O   . HOH H 6 .   ? 33.531 26.119 9.282  1.00 47.91 ? 526 HOH A O   1 
HETATM 2044 O  O   . HOH H 6 .   ? 41.217 43.490 22.354 1.00 54.26 ? 527 HOH A O   1 
HETATM 2045 O  O   . HOH H 6 .   ? 27.617 36.579 20.297 1.00 49.84 ? 528 HOH A O   1 
HETATM 2046 O  O   . HOH H 6 .   ? 25.160 23.683 37.217 1.00 40.65 ? 529 HOH A O   1 
HETATM 2047 O  O   . HOH H 6 .   ? 13.106 18.876 31.562 1.00 53.23 ? 530 HOH A O   1 
HETATM 2048 O  O   . HOH H 6 .   ? 33.914 23.808 36.035 1.00 52.88 ? 531 HOH A O   1 
HETATM 2049 O  O   . HOH H 6 .   ? 28.927 1.682  19.512 1.00 56.89 ? 532 HOH A O   1 
HETATM 2050 O  O   . HOH H 6 .   ? 38.237 39.518 19.787 1.00 46.51 ? 533 HOH A O   1 
HETATM 2051 O  O   . HOH H 6 .   ? 38.016 16.436 18.113 1.00 46.04 ? 534 HOH A O   1 
HETATM 2052 O  O   . HOH H 6 .   ? 38.829 16.550 13.580 1.00 54.38 ? 535 HOH A O   1 
HETATM 2053 O  O   . HOH H 6 .   ? 19.450 7.481  2.226  1.00 59.03 ? 536 HOH A O   1 
HETATM 2054 O  O   . HOH H 6 .   ? 16.278 14.820 38.362 1.00 50.21 ? 537 HOH A O   1 
HETATM 2055 O  O   . HOH H 6 .   ? 43.678 43.062 20.558 1.00 48.34 ? 538 HOH A O   1 
HETATM 2056 O  O   . HOH H 6 .   ? 16.766 34.202 43.713 1.00 44.47 ? 539 HOH A O   1 
HETATM 2057 O  O   . HOH H 6 .   ? 16.280 22.198 32.377 1.00 41.21 ? 540 HOH A O   1 
HETATM 2058 O  O   . HOH H 6 .   ? 27.873 31.322 29.183 1.00 45.27 ? 541 HOH A O   1 
HETATM 2059 O  O   . HOH H 6 .   ? 45.664 31.595 14.971 1.00 44.08 ? 542 HOH A O   1 
HETATM 2060 O  O   . HOH H 6 .   ? 49.134 26.507 19.567 1.00 48.70 ? 543 HOH A O   1 
HETATM 2061 O  O   . HOH H 6 .   ? 19.392 12.389 31.126 1.00 60.81 ? 544 HOH A O   1 
HETATM 2062 O  O   . HOH H 6 .   ? 44.006 33.428 13.676 1.00 55.83 ? 545 HOH A O   1 
HETATM 2063 O  O   . HOH H 6 .   ? 38.378 43.155 22.994 1.00 54.08 ? 546 HOH A O   1 
HETATM 2064 O  O   . HOH H 6 .   ? 43.258 3.000  2.798  1.00 52.91 ? 547 HOH A O   1 
HETATM 2065 O  O   . HOH H 6 .   ? 14.709 14.900 26.643 1.00 54.12 ? 548 HOH A O   1 
HETATM 2066 O  O   . HOH H 6 .   ? 8.635  25.084 35.708 1.00 55.59 ? 549 HOH A O   1 
HETATM 2067 O  O   . HOH H 6 .   ? 47.376 22.184 22.330 1.00 43.51 ? 550 HOH A O   1 
HETATM 2068 O  O   . HOH H 6 .   ? 29.183 29.416 31.137 1.00 48.22 ? 551 HOH A O   1 
HETATM 2069 O  O   . HOH H 6 .   ? 14.223 11.683 7.650  1.00 55.01 ? 552 HOH A O   1 
HETATM 2070 O  O   . HOH H 6 .   ? 32.505 13.883 12.902 1.00 42.44 ? 553 HOH A O   1 
HETATM 2071 O  O   . HOH H 6 .   ? 45.180 26.880 16.860 1.00 41.27 ? 554 HOH A O   1 
HETATM 2072 O  O   . HOH H 6 .   ? 29.804 7.868  1.196  1.00 46.09 ? 555 HOH A O   1 
HETATM 2073 O  O   . HOH H 6 .   ? 21.142 15.101 39.562 1.00 60.81 ? 556 HOH A O   1 
HETATM 2074 O  O   . HOH H 6 .   ? 15.351 14.313 41.064 1.00 57.85 ? 557 HOH A O   1 
HETATM 2075 O  O   . HOH H 6 .   ? 32.213 34.028 28.500 1.00 48.58 ? 558 HOH A O   1 
HETATM 2076 O  O   . HOH H 6 .   ? 9.641  19.301 33.139 1.00 52.21 ? 559 HOH A O   1 
HETATM 2077 O  O   . HOH H 6 .   ? 50.848 39.198 15.118 1.00 52.48 ? 560 HOH A O   1 
HETATM 2078 O  O   . HOH H 6 .   ? 50.506 30.192 17.142 1.00 56.06 ? 561 HOH A O   1 
HETATM 2079 O  O   . HOH I 6 .   ? 23.303 11.383 25.654 1.00 43.31 ? 301 HOH P O   1 
HETATM 2080 O  O   . HOH I 6 .   ? 22.730 16.370 22.447 1.00 39.36 ? 302 HOH P O   1 
HETATM 2081 O  O   . HOH I 6 .   ? 20.993 14.600 28.267 1.00 45.07 ? 303 HOH P O   1 
HETATM 2082 O  O   . HOH I 6 .   ? 39.056 17.399 22.452 1.00 50.44 ? 304 HOH P O   1 
HETATM 2083 O  O   . HOH I 6 .   ? 17.315 14.163 26.584 1.00 47.97 ? 305 HOH P O   1 
HETATM 2084 O  O   . HOH I 6 .   ? 27.725 12.786 27.315 1.00 46.99 ? 306 HOH P O   1 
HETATM 2085 O  O   . HOH I 6 .   ? 27.173 16.331 21.660 1.00 41.99 ? 307 HOH P O   1 
HETATM 2086 O  O   . HOH I 6 .   ? 20.796 12.128 26.872 1.00 42.56 ? 308 HOH P O   1 
HETATM 2087 O  O   . HOH I 6 .   ? 25.560 13.640 27.410 1.00 54.23 ? 309 HOH P O   1 
HETATM 2088 O  O   . HOH I 6 .   ? 26.437 7.473  24.767 1.00 46.64 ? 310 HOH P 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   . GLY A 1   ? 1.0983 0.7819 0.9807 -0.0398 0.0290  0.0304  -4  GLY A N   
2    C  CA  . GLY A 1   ? 1.0307 0.6862 0.8982 -0.0537 0.0427  0.0250  -4  GLY A CA  
3    C  C   . GLY A 1   ? 0.9284 0.6072 0.8159 -0.0711 0.0441  0.0115  -4  GLY A C   
4    O  O   . GLY A 1   ? 0.9573 0.6288 0.8402 -0.0882 0.0546  0.0044  -4  GLY A O   
5    N  N   . ALA A 2   ? 0.8629 0.5708 0.7721 -0.0664 0.0333  0.0076  -3  ALA A N   
6    C  CA  . ALA A 2   ? 0.8206 0.5557 0.7500 -0.0794 0.0317  -0.0048 -3  ALA A CA  
7    C  C   . ALA A 2   ? 0.7458 0.5036 0.6869 -0.0892 0.0323  -0.0097 -3  ALA A C   
8    O  O   . ALA A 2   ? 0.7108 0.4868 0.6642 -0.1028 0.0348  -0.0213 -3  ALA A O   
9    C  CB  . ALA A 2   ? 0.8312 0.5919 0.7785 -0.0695 0.0191  -0.0059 -3  ALA A CB  
10   N  N   . MET A 3   ? 0.7356 0.4943 0.6733 -0.0825 0.0301  -0.0019 -2  MET A N   
11   C  CA  . MET A 3   ? 0.6733 0.4549 0.6228 -0.0898 0.0301  -0.0063 -2  MET A CA  
12   C  C   . MET A 3   ? 0.6763 0.4362 0.6088 -0.1017 0.0436  -0.0063 -2  MET A C   
13   O  O   . MET A 3   ? 0.6316 0.4076 0.5714 -0.1085 0.0457  -0.0097 -2  MET A O   
14   C  CB  . MET A 3   ? 0.6349 0.4328 0.5916 -0.0759 0.0194  0.0013  -2  MET A CB  
15   C  CG  . MET A 3   ? 0.6134 0.4415 0.5909 -0.0687 0.0073  -0.0018 -2  MET A CG  
16   S  SD  . MET A 3   ? 0.6182 0.4743 0.6161 -0.0778 0.0049  -0.0157 -2  MET A SD  
17   C  CE  . MET A 3   ? 0.6022 0.4679 0.6075 -0.0642 -0.0073 -0.0131 -2  MET A CE  
18   N  N   . GLY A 4   ? 0.7043 0.4257 0.6122 -0.1040 0.0536  -0.0023 -1  GLY A N   
19   C  CA  . GLY A 4   ? 0.7279 0.4210 0.6129 -0.1127 0.0667  0.0006  -1  GLY A CA  
20   C  C   . GLY A 4   ? 0.6942 0.3974 0.5855 -0.1352 0.0780  -0.0123 -1  GLY A C   
21   O  O   . GLY A 4   ? 0.6892 0.3812 0.5684 -0.1432 0.0872  -0.0112 -1  GLY A O   
22   N  N   . SER A 5   ? 0.6392 0.3651 0.5493 -0.1461 0.0776  -0.0253 0   SER A N   
23   C  CA  . SER A 5   ? 0.6468 0.3872 0.5648 -0.1683 0.0884  -0.0395 0   SER A CA  
24   C  C   . SER A 5   ? 0.6150 0.4002 0.5594 -0.1686 0.0814  -0.0453 0   SER A C   
25   O  O   . SER A 5   ? 0.6214 0.4215 0.5728 -0.1858 0.0907  -0.0565 0   SER A O   
26   C  CB  . SER A 5   ? 0.6497 0.3986 0.5765 -0.1811 0.0914  -0.0527 0   SER A CB  
27   O  OG  . SER A 5   ? 0.6725 0.4471 0.6187 -0.1673 0.0756  -0.0524 0   SER A OG  
28   N  N   . MET A 6   ? 0.5970 0.4036 0.5555 -0.1504 0.0663  -0.0387 1   MET A N   
29   C  CA  . MET A 6   ? 0.5590 0.4051 0.5405 -0.1483 0.0595  -0.0437 1   MET A CA  
30   C  C   . MET A 6   ? 0.5778 0.4169 0.5502 -0.1461 0.0630  -0.0367 1   MET A C   
31   O  O   . MET A 6   ? 0.5760 0.3888 0.5297 -0.1355 0.0615  -0.0237 1   MET A O   
32   C  CB  . MET A 6   ? 0.5583 0.4295 0.5575 -0.1309 0.0426  -0.0408 1   MET A CB  
33   C  CG  . MET A 6   ? 0.5627 0.4770 0.5883 -0.1336 0.0371  -0.0533 1   MET A CG  
34   S  SD  . MET A 6   ? 0.5379 0.4751 0.5784 -0.1127 0.0187  -0.0489 1   MET A SD  
35   C  CE  . MET A 6   ? 0.5099 0.4245 0.5401 -0.1082 0.0153  -0.0442 1   MET A CE  
36   N  N   . GLU A 7   ? 0.5526 0.4191 0.5398 -0.1546 0.0664  -0.0459 2   GLU A N   
37   C  CA  . GLU A 7   ? 0.5564 0.4191 0.5362 -0.1531 0.0698  -0.0405 2   GLU A CA  
38   C  C   . GLU A 7   ? 0.5326 0.4030 0.5166 -0.1330 0.0558  -0.0303 2   GLU A C   
39   O  O   . GLU A 7   ? 0.5066 0.4002 0.5082 -0.1228 0.0438  -0.0320 2   GLU A O   
40   C  CB  . GLU A 7   ? 0.5515 0.4459 0.5489 -0.1658 0.0764  -0.0539 2   GLU A CB  
41   C  CG  . GLU A 7   ? 0.5960 0.4784 0.5843 -0.1890 0.0939  -0.0637 2   GLU A CG  
42   C  CD  . GLU A 7   ? 0.6143 0.5301 0.6203 -0.2022 0.1015  -0.0776 2   GLU A CD  
43   O  OE1 . GLU A 7   ? 0.6256 0.5250 0.6172 -0.2194 0.1177  -0.0813 2   GLU A OE1 
44   O  OE2 . GLU A 7   ? 0.6002 0.5570 0.6325 -0.1934 0.0912  -0.0836 2   GLU A OE2 
45   N  N   . ARG A 8   ? 0.5442 0.3942 0.5100 -0.1282 0.0579  -0.0200 3   ARG A N   
46   C  CA  . ARG A 8   ? 0.5248 0.3817 0.4928 -0.1116 0.0460  -0.0113 3   ARG A CA  
47   C  C   . ARG A 8   ? 0.4978 0.3921 0.4908 -0.1073 0.0386  -0.0187 3   ARG A C   
48   O  O   . ARG A 8   ? 0.4833 0.3886 0.4851 -0.0945 0.0268  -0.0157 3   ARG A O   
49   C  CB  . ARG A 8   ? 0.5428 0.3788 0.4894 -0.1101 0.0507  -0.0023 3   ARG A CB  
50   C  CG  . ARG A 8   ? 0.5448 0.3845 0.4901 -0.0938 0.0386  0.0069  3   ARG A CG  
51   C  CD  . ARG A 8   ? 0.5963 0.4197 0.5213 -0.0935 0.0431  0.0142  3   ARG A CD  
52   N  NE  . ARG A 8   ? 0.5685 0.3935 0.4893 -0.0793 0.0322  0.0227  3   ARG A NE  
53   C  CZ  . ARG A 8   ? 0.5865 0.4342 0.5214 -0.0738 0.0249  0.0205  3   ARG A CZ  
54   N  NH1 . ARG A 8   ? 0.5685 0.4395 0.5225 -0.0787 0.0263  0.0109  3   ARG A NH1 
55   N  NH2 . ARG A 8   ? 0.5902 0.4374 0.5191 -0.0630 0.0161  0.0276  3   ARG A NH2 
56   N  N   . ALA A 9   ? 0.4969 0.4103 0.5004 -0.1175 0.0459  -0.0286 4   ALA A N   
57   C  CA  . ALA A 9   ? 0.4778 0.4254 0.5031 -0.1110 0.0392  -0.0353 4   ALA A CA  
58   C  C   . ALA A 9   ? 0.4748 0.4440 0.5184 -0.1050 0.0297  -0.0411 4   ALA A C   
59   O  O   . ALA A 9   ? 0.4766 0.4625 0.5307 -0.0922 0.0197  -0.0407 4   ALA A O   
60   C  CB  . ALA A 9   ? 0.4981 0.4645 0.5323 -0.1230 0.0497  -0.0461 4   ALA A CB  
61   N  N   . SER A 10  ? 0.4644 0.4314 0.5095 -0.1143 0.0332  -0.0467 5   SER A N   
62   C  CA  . SER A 10  ? 0.4584 0.4447 0.5186 -0.1093 0.0242  -0.0525 5   SER A CA  
63   C  C   . SER A 10  ? 0.4655 0.4367 0.5184 -0.0951 0.0136  -0.0418 5   SER A C   
64   O  O   . SER A 10  ? 0.4269 0.4151 0.4909 -0.0850 0.0035  -0.0436 5   SER A O   
65   C  CB  . SER A 10  ? 0.4616 0.4473 0.5230 -0.1249 0.0319  -0.0617 5   SER A CB  
66   O  OG  . SER A 10  ? 0.4697 0.4746 0.5404 -0.1396 0.0421  -0.0738 5   SER A OG  
67   N  N   . LEU A 11  ? 0.4506 0.3902 0.4840 -0.0937 0.0159  -0.0309 6   LEU A N   
68   C  CA  . LEU A 11  ? 0.4421 0.3700 0.4694 -0.0805 0.0064  -0.0214 6   LEU A CA  
69   C  C   . LEU A 11  ? 0.4405 0.3802 0.4726 -0.0685 -0.0018 -0.0176 6   LEU A C   
70   O  O   . LEU A 11  ? 0.4230 0.3690 0.4601 -0.0587 -0.0109 -0.0160 6   LEU A O   
71   C  CB  . LEU A 11  ? 0.4607 0.3558 0.4666 -0.0801 0.0105  -0.0113 6   LEU A CB  
72   C  CG  . LEU A 11  ? 0.4810 0.3570 0.4779 -0.0896 0.0183  -0.0137 6   LEU A CG  
73   C  CD1 . LEU A 11  ? 0.5211 0.3627 0.4932 -0.0889 0.0248  -0.0037 6   LEU A CD1 
74   C  CD2 . LEU A 11  ? 0.4709 0.3500 0.4740 -0.0836 0.0108  -0.0146 6   LEU A CD2 
75   N  N   . ILE A 12  ? 0.4523 0.3931 0.4812 -0.0698 0.0022  -0.0164 7   ILE A N   
76   C  CA  . ILE A 12  ? 0.4351 0.3860 0.4674 -0.0599 -0.0040 -0.0142 7   ILE A CA  
77   C  C   . ILE A 12  ? 0.4363 0.4127 0.4857 -0.0546 -0.0095 -0.0223 7   ILE A C   
78   O  O   . ILE A 12  ? 0.4384 0.4177 0.4890 -0.0439 -0.0174 -0.0197 7   ILE A O   
79   C  CB  . ILE A 12  ? 0.4303 0.3791 0.4564 -0.0639 0.0028  -0.0134 7   ILE A CB  
80   C  CG1 . ILE A 12  ? 0.4892 0.4114 0.4948 -0.0667 0.0071  -0.0041 7   ILE A CG1 
81   C  CG2 . ILE A 12  ? 0.4369 0.3969 0.4670 -0.0545 -0.0026 -0.0131 7   ILE A CG2 
82   C  CD1 . ILE A 12  ? 0.4869 0.3970 0.4834 -0.0566 -0.0011 0.0051  7   ILE A CD1 
83   N  N   . GLN A 13  ? 0.4027 0.3980 0.4644 -0.0620 -0.0048 -0.0325 8   GLN A N   
84   C  CA  . GLN A 13  ? 0.4194 0.4422 0.4975 -0.0555 -0.0105 -0.0411 8   GLN A CA  
85   C  C   . GLN A 13  ? 0.4315 0.4537 0.5108 -0.0482 -0.0195 -0.0397 8   GLN A C   
86   O  O   . GLN A 13  ? 0.4080 0.4392 0.4906 -0.0360 -0.0274 -0.0397 8   GLN A O   
87   C  CB  . GLN A 13  ? 0.4585 0.5041 0.5504 -0.0668 -0.0038 -0.0536 8   GLN A CB  
88   C  CG  . GLN A 13  ? 0.4729 0.5529 0.5832 -0.0591 -0.0096 -0.0639 8   GLN A CG  
89   C  CD  . GLN A 13  ? 0.5383 0.6455 0.6639 -0.0720 -0.0023 -0.0779 8   GLN A CD  
90   O  OE1 . GLN A 13  ? 0.5519 0.6497 0.6728 -0.0876 0.0090  -0.0797 8   GLN A OE1 
91   N  NE2 . GLN A 13  ? 0.5187 0.6601 0.6617 -0.0654 -0.0082 -0.0883 8   GLN A NE2 
92   N  N   . LYS A 14  ? 0.3984 0.4078 0.4729 -0.0553 -0.0178 -0.0385 9   LYS A N   
93   C  CA  . LYS A 14  ? 0.4092 0.4174 0.4841 -0.0496 -0.0254 -0.0378 9   LYS A CA  
94   C  C   . LYS A 14  ? 0.4223 0.4138 0.4866 -0.0388 -0.0315 -0.0276 9   LYS A C   
95   O  O   . LYS A 14  ? 0.4038 0.3993 0.4692 -0.0303 -0.0389 -0.0274 9   LYS A O   
96   C  CB  . LYS A 14  ? 0.3948 0.3923 0.4663 -0.0608 -0.0205 -0.0400 9   LYS A CB  
97   C  CG  . LYS A 14  ? 0.4138 0.4336 0.4981 -0.0719 -0.0159 -0.0530 9   LYS A CG  
98   C  CD  . LYS A 14  ? 0.4323 0.4414 0.5126 -0.0836 -0.0110 -0.0569 9   LYS A CD  
99   C  CE  . LYS A 14  ? 0.4397 0.4718 0.5321 -0.0979 -0.0044 -0.0712 9   LYS A CE  
100  N  NZ  . LYS A 14  ? 0.4377 0.4552 0.5233 -0.1121 0.0028  -0.0758 9   LYS A NZ  
101  N  N   . ALA A 15  ? 0.4171 0.3909 0.4704 -0.0392 -0.0284 -0.0196 10  ALA A N   
102  C  CA  . ALA A 15  ? 0.4138 0.3765 0.4586 -0.0303 -0.0338 -0.0116 10  ALA A CA  
103  C  C   . ALA A 15  ? 0.4191 0.3926 0.4671 -0.0214 -0.0385 -0.0133 10  ALA A C   
104  O  O   . ALA A 15  ? 0.4180 0.3870 0.4617 -0.0140 -0.0440 -0.0105 10  ALA A O   
105  C  CB  . ALA A 15  ? 0.4232 0.3698 0.4563 -0.0322 -0.0301 -0.0041 10  ALA A CB  
106  N  N   . LYS A 16  ? 0.3951 0.3815 0.4492 -0.0218 -0.0355 -0.0181 11  LYS A N   
107  C  CA  . LYS A 16  ? 0.4281 0.4227 0.4835 -0.0117 -0.0391 -0.0199 11  LYS A CA  
108  C  C   . LYS A 16  ? 0.4539 0.4610 0.5155 -0.0040 -0.0456 -0.0248 11  LYS A C   
109  O  O   . LYS A 16  ? 0.4388 0.4413 0.4940 0.0064  -0.0504 -0.0227 11  LYS A O   
110  C  CB  . LYS A 16  ? 0.3978 0.4046 0.4589 -0.0133 -0.0339 -0.0247 11  LYS A CB  
111  C  CG  . LYS A 16  ? 0.4537 0.4463 0.5048 -0.0183 -0.0284 -0.0192 11  LYS A CG  
112  C  CD  . LYS A 16  ? 0.4941 0.4989 0.5508 -0.0211 -0.0220 -0.0247 11  LYS A CD  
113  C  CE  . LYS A 16  ? 0.5246 0.5145 0.5693 -0.0272 -0.0163 -0.0192 11  LYS A CE  
114  N  NZ  . LYS A 16  ? 0.5019 0.5031 0.5520 -0.0333 -0.0081 -0.0252 11  LYS A NZ  
115  N  N   . LEU A 17  ? 0.3983 0.4202 0.4706 -0.0093 -0.0455 -0.0315 12  LEU A N   
116  C  CA  . LEU A 17  ? 0.4224 0.4577 0.4998 -0.0022 -0.0524 -0.0365 12  LEU A CA  
117  C  C   . LEU A 17  ? 0.4398 0.4574 0.5064 0.0013  -0.0572 -0.0303 12  LEU A C   
118  O  O   . LEU A 17  ? 0.4413 0.4595 0.5034 0.0118  -0.0634 -0.0302 12  LEU A O   
119  C  CB  . LEU A 17  ? 0.3987 0.4544 0.4895 -0.0114 -0.0506 -0.0461 12  LEU A CB  
120  C  CG  . LEU A 17  ? 0.4116 0.4909 0.5158 -0.0163 -0.0454 -0.0550 12  LEU A CG  
121  C  CD1 . LEU A 17  ? 0.4184 0.5123 0.5331 -0.0307 -0.0411 -0.0644 12  LEU A CD1 
122  C  CD2 . LEU A 17  ? 0.3804 0.4824 0.4919 -0.0018 -0.0511 -0.0603 12  LEU A CD2 
123  N  N   . ALA A 18  ? 0.4039 0.4050 0.4651 -0.0068 -0.0539 -0.0253 13  ALA A N   
124  C  CA  . ALA A 18  ? 0.4298 0.4158 0.4820 -0.0042 -0.0574 -0.0202 13  ALA A CA  
125  C  C   . ALA A 18  ? 0.4476 0.4213 0.4888 0.0039  -0.0597 -0.0142 13  ALA A C   
126  O  O   . ALA A 18  ? 0.4419 0.4089 0.4759 0.0095  -0.0638 -0.0125 13  ALA A O   
127  C  CB  . ALA A 18  ? 0.4224 0.3945 0.4713 -0.0129 -0.0530 -0.0163 13  ALA A CB  
128  N  N   . GLU A 19  ? 0.4309 0.4003 0.4691 0.0035  -0.0563 -0.0114 14  GLU A N   
129  C  CA  . GLU A 19  ? 0.4593 0.4173 0.4862 0.0097  -0.0573 -0.0074 14  GLU A CA  
130  C  C   . GLU A 19  ? 0.4666 0.4288 0.4906 0.0206  -0.0613 -0.0104 14  GLU A C   
131  O  O   . GLU A 19  ? 0.4876 0.4367 0.4993 0.0262  -0.0635 -0.0077 14  GLU A O   
132  C  CB  . GLU A 19  ? 0.4396 0.3945 0.4640 0.0070  -0.0527 -0.0054 14  GLU A CB  
133  C  CG  . GLU A 19  ? 0.5007 0.4416 0.5116 0.0110  -0.0526 -0.0020 14  GLU A CG  
134  C  CD  . GLU A 19  ? 0.5450 0.4827 0.5521 0.0076  -0.0481 -0.0006 14  GLU A CD  
135  O  OE1 . GLU A 19  ? 0.5261 0.4734 0.5405 0.0055  -0.0452 -0.0031 14  GLU A OE1 
136  O  OE2 . GLU A 19  ? 0.5820 0.5080 0.5783 0.0061  -0.0471 0.0024  14  GLU A OE2 
137  N  N   . GLN A 20  ? 0.4408 0.4210 0.4747 0.0243  -0.0620 -0.0164 15  GLN A N   
138  C  CA  . GLN A 20  ? 0.4504 0.4365 0.4811 0.0375  -0.0666 -0.0195 15  GLN A CA  
139  C  C   . GLN A 20  ? 0.4783 0.4630 0.5047 0.0418  -0.0725 -0.0198 15  GLN A C   
140  O  O   . GLN A 20  ? 0.4673 0.4433 0.4810 0.0532  -0.0761 -0.0184 15  GLN A O   
141  C  CB  . GLN A 20  ? 0.4527 0.4648 0.4982 0.0407  -0.0667 -0.0274 15  GLN A CB  
142  C  CG  . GLN A 20  ? 0.4768 0.4901 0.5243 0.0396  -0.0608 -0.0278 15  GLN A CG  
143  C  CD  . GLN A 20  ? 0.5466 0.5892 0.6112 0.0408  -0.0599 -0.0369 15  GLN A CD  
144  O  OE1 . GLN A 20  ? 0.5625 0.6188 0.6398 0.0288  -0.0565 -0.0413 15  GLN A OE1 
145  N  NE2 . GLN A 20  ? 0.5871 0.6394 0.6514 0.0554  -0.0625 -0.0404 15  GLN A NE2 
146  N  N   . ALA A 21  ? 0.4427 0.4340 0.4773 0.0331  -0.0730 -0.0217 16  ALA A N   
147  C  CA  . ALA A 21  ? 0.4767 0.4676 0.5076 0.0355  -0.0780 -0.0227 16  ALA A CA  
148  C  C   . ALA A 21  ? 0.4651 0.4326 0.4825 0.0329  -0.0770 -0.0160 16  ALA A C   
149  O  O   . ALA A 21  ? 0.4914 0.4558 0.5038 0.0343  -0.0804 -0.0164 16  ALA A O   
150  C  CB  . ALA A 21  ? 0.4505 0.4589 0.4958 0.0262  -0.0780 -0.0291 16  ALA A CB  
151  N  N   . GLU A 22  ? 0.4638 0.4168 0.4754 0.0290  -0.0724 -0.0107 17  GLU A N   
152  C  CA  . GLU A 22  ? 0.5201 0.4553 0.5214 0.0252  -0.0707 -0.0057 17  GLU A CA  
153  C  C   . GLU A 22  ? 0.5080 0.4456 0.5159 0.0179  -0.0705 -0.0062 17  GLU A C   
154  O  O   . GLU A 22  ? 0.5236 0.4519 0.5245 0.0173  -0.0711 -0.0045 17  GLU A O   
155  C  CB  . GLU A 22  ? 0.5385 0.4593 0.5226 0.0332  -0.0727 -0.0040 17  GLU A CB  
156  C  CG  . GLU A 22  ? 0.5752 0.4868 0.5488 0.0398  -0.0709 -0.0025 17  GLU A CG  
157  C  CD  . GLU A 22  ? 0.7040 0.5978 0.6570 0.0490  -0.0721 -0.0009 17  GLU A CD  
158  O  OE1 . GLU A 22  ? 0.7490 0.6447 0.6968 0.0610  -0.0751 -0.0025 17  GLU A OE1 
159  O  OE2 . GLU A 22  ? 0.7246 0.6023 0.6657 0.0446  -0.0697 0.0017  17  GLU A OE2 
160  N  N   . ARG A 23  ? 0.4906 0.4391 0.5108 0.0119  -0.0688 -0.0088 18  ARG A N   
161  C  CA  . ARG A 23  ? 0.4564 0.4035 0.4811 0.0048  -0.0671 -0.0093 18  ARG A CA  
162  C  C   . ARG A 23  ? 0.4783 0.4175 0.5029 -0.0004 -0.0624 -0.0045 18  ARG A C   
163  O  O   . ARG A 23  ? 0.4459 0.3882 0.4760 -0.0056 -0.0589 -0.0052 18  ARG A O   
164  C  CB  . ARG A 23  ? 0.4583 0.4203 0.4936 0.0009  -0.0672 -0.0162 18  ARG A CB  
165  C  CG  . ARG A 23  ? 0.4837 0.4572 0.5193 0.0069  -0.0732 -0.0217 18  ARG A CG  
166  C  CD  . ARG A 23  ? 0.4834 0.4508 0.5150 0.0046  -0.0745 -0.0226 18  ARG A CD  
167  N  NE  . ARG A 23  ? 0.4741 0.4441 0.5132 -0.0057 -0.0704 -0.0264 18  ARG A NE  
168  C  CZ  . ARG A 23  ? 0.5236 0.4925 0.5621 -0.0098 -0.0705 -0.0302 18  ARG A CZ  
169  N  NH1 . ARG A 23  ? 0.5009 0.4682 0.5323 -0.0046 -0.0754 -0.0308 18  ARG A NH1 
170  N  NH2 . ARG A 23  ? 0.4584 0.4255 0.5013 -0.0199 -0.0650 -0.0336 18  ARG A NH2 
171  N  N   . TYR A 24  ? 0.4513 0.3804 0.4684 0.0009  -0.0621 0.0002  19  TYR A N   
172  C  CA  . TYR A 24  ? 0.4600 0.3851 0.4761 -0.0019 -0.0590 0.0045  19  TYR A CA  
173  C  C   . TYR A 24  ? 0.4622 0.3832 0.4804 -0.0053 -0.0566 0.0061  19  TYR A C   
174  O  O   . TYR A 24  ? 0.4431 0.3617 0.4607 -0.0071 -0.0539 0.0092  19  TYR A O   
175  C  CB  . TYR A 24  ? 0.4501 0.3696 0.4584 -0.0004 -0.0592 0.0075  19  TYR A CB  
176  C  CG  . TYR A 24  ? 0.4841 0.4021 0.4864 0.0028  -0.0599 0.0064  19  TYR A CG  
177  C  CD1 . TYR A 24  ? 0.5114 0.4320 0.5143 0.0026  -0.0583 0.0066  19  TYR A CD1 
178  C  CD2 . TYR A 24  ? 0.5290 0.4410 0.5232 0.0066  -0.0616 0.0053  19  TYR A CD2 
179  C  CE1 . TYR A 24  ? 0.5125 0.4295 0.5086 0.0067  -0.0582 0.0055  19  TYR A CE1 
180  C  CE2 . TYR A 24  ? 0.5516 0.4582 0.5372 0.0111  -0.0616 0.0047  19  TYR A CE2 
181  C  CZ  . TYR A 24  ? 0.5548 0.4640 0.5417 0.0115  -0.0599 0.0047  19  TYR A CZ  
182  O  OH  . TYR A 24  ? 0.6083 0.5098 0.5851 0.0170  -0.0592 0.0041  19  TYR A OH  
183  N  N   . GLU A 25  ? 0.4364 0.3548 0.4551 -0.0054 -0.0571 0.0043  20  GLU A N   
184  C  CA  . GLU A 25  ? 0.4898 0.4011 0.5085 -0.0077 -0.0539 0.0055  20  GLU A CA  
185  C  C   . GLU A 25  ? 0.4561 0.3675 0.4779 -0.0132 -0.0502 0.0030  20  GLU A C   
186  O  O   . GLU A 25  ? 0.4624 0.3647 0.4805 -0.0151 -0.0460 0.0061  20  GLU A O   
187  C  CB  . GLU A 25  ? 0.5298 0.4375 0.5476 -0.0070 -0.0546 0.0030  20  GLU A CB  
188  C  CG  . GLU A 25  ? 0.5773 0.4830 0.5914 -0.0029 -0.0559 0.0057  20  GLU A CG  
189  C  CD  . GLU A 25  ? 0.7228 0.6218 0.7355 -0.0019 -0.0540 0.0050  20  GLU A CD  
190  O  OE1 . GLU A 25  ? 0.7095 0.6037 0.7225 -0.0048 -0.0522 0.0018  20  GLU A OE1 
191  O  OE2 . GLU A 25  ? 0.7312 0.6305 0.7424 0.0014  -0.0539 0.0070  20  GLU A OE2 
192  N  N   . ASP A 26  ? 0.4578 0.3795 0.4854 -0.0158 -0.0514 -0.0029 21  ASP A N   
193  C  CA  . ASP A 26  ? 0.4439 0.3697 0.4759 -0.0228 -0.0471 -0.0069 21  ASP A CA  
194  C  C   . ASP A 26  ? 0.4338 0.3592 0.4643 -0.0232 -0.0445 -0.0033 21  ASP A C   
195  O  O   . ASP A 26  ? 0.4492 0.3679 0.4772 -0.0290 -0.0386 -0.0026 21  ASP A O   
196  C  CB  . ASP A 26  ? 0.4404 0.3839 0.4808 -0.0239 -0.0500 -0.0150 21  ASP A CB  
197  C  CG  . ASP A 26  ? 0.4977 0.4435 0.5393 -0.0255 -0.0520 -0.0202 21  ASP A CG  
198  O  OD1 . ASP A 26  ? 0.4791 0.4109 0.5152 -0.0275 -0.0495 -0.0183 21  ASP A OD1 
199  O  OD2 . ASP A 26  ? 0.4907 0.4530 0.5383 -0.0241 -0.0562 -0.0265 21  ASP A OD2 
200  N  N   . MET A 27  ? 0.4177 0.3488 0.4481 -0.0176 -0.0482 -0.0012 22  MET A N   
201  C  CA  . MET A 27  ? 0.4041 0.3357 0.4329 -0.0187 -0.0455 0.0012  22  MET A CA  
202  C  C   . MET A 27  ? 0.4554 0.3737 0.4756 -0.0190 -0.0429 0.0080  22  MET A C   
203  O  O   . MET A 27  ? 0.4447 0.3587 0.4613 -0.0228 -0.0383 0.0097  22  MET A O   
204  C  CB  . MET A 27  ? 0.4471 0.3864 0.4764 -0.0131 -0.0490 0.0007  22  MET A CB  
205  C  CG  . MET A 27  ? 0.3932 0.3305 0.4179 -0.0127 -0.0472 0.0040  22  MET A CG  
206  S  SD  . MET A 27  ? 0.4262 0.3611 0.4440 -0.0062 -0.0509 0.0057  22  MET A SD  
207  C  CE  . MET A 27  ? 0.4258 0.3616 0.4407 -0.0084 -0.0468 0.0066  22  MET A CE  
208  N  N   . ALA A 28  ? 0.4307 0.3425 0.4468 -0.0149 -0.0453 0.0117  23  ALA A N   
209  C  CA  . ALA A 28  ? 0.4474 0.3489 0.4555 -0.0130 -0.0436 0.0177  23  ALA A CA  
210  C  C   . ALA A 28  ? 0.4645 0.3529 0.4677 -0.0169 -0.0378 0.0181  23  ALA A C   
211  O  O   . ALA A 28  ? 0.4617 0.3402 0.4560 -0.0171 -0.0343 0.0225  23  ALA A O   
212  C  CB  . ALA A 28  ? 0.4466 0.3477 0.4531 -0.0071 -0.0473 0.0202  23  ALA A CB  
213  N  N   . ALA A 29  ? 0.4495 0.3362 0.4564 -0.0205 -0.0362 0.0132  24  ALA A N   
214  C  CA  . ALA A 29  ? 0.4779 0.3493 0.4782 -0.0263 -0.0291 0.0125  24  ALA A CA  
215  C  C   . ALA A 29  ? 0.4606 0.3319 0.4597 -0.0344 -0.0232 0.0104  24  ALA A C   
216  O  O   . ALA A 29  ? 0.4848 0.3385 0.4721 -0.0376 -0.0164 0.0135  24  ALA A O   
217  C  CB  . ALA A 29  ? 0.4946 0.3667 0.4997 -0.0305 -0.0284 0.0058  24  ALA A CB  
218  N  N   . PHE A 30  ? 0.4574 0.3475 0.4676 -0.0374 -0.0252 0.0050  25  PHE A N   
219  C  CA  . PHE A 30  ? 0.4602 0.3539 0.4712 -0.0453 -0.0192 0.0018  25  PHE A CA  
220  C  C   . PHE A 30  ? 0.4598 0.3439 0.4600 -0.0427 -0.0173 0.0093  25  PHE A C   
221  O  O   . PHE A 30  ? 0.4806 0.3529 0.4717 -0.0492 -0.0095 0.0102  25  PHE A O   
222  C  CB  . PHE A 30  ? 0.4332 0.3514 0.4587 -0.0457 -0.0227 -0.0053 25  PHE A CB  
223  C  CG  . PHE A 30  ? 0.4465 0.3778 0.4825 -0.0494 -0.0240 -0.0142 25  PHE A CG  
224  C  CD1 . PHE A 30  ? 0.4287 0.3536 0.4632 -0.0600 -0.0172 -0.0193 25  PHE A CD1 
225  C  CD2 . PHE A 30  ? 0.4441 0.3934 0.4896 -0.0427 -0.0317 -0.0178 25  PHE A CD2 
226  C  CE1 . PHE A 30  ? 0.4749 0.4143 0.5191 -0.0644 -0.0187 -0.0286 25  PHE A CE1 
227  C  CE2 . PHE A 30  ? 0.4271 0.3904 0.4813 -0.0453 -0.0338 -0.0262 25  PHE A CE2 
228  C  CZ  . PHE A 30  ? 0.4532 0.4136 0.5079 -0.0565 -0.0277 -0.0320 25  PHE A CZ  
229  N  N   . MET A 31  ? 0.4423 0.3308 0.4419 -0.0339 -0.0239 0.0142  26  MET A N   
230  C  CA  . MET A 31  ? 0.4559 0.3384 0.4453 -0.0313 -0.0232 0.0205  26  MET A CA  
231  C  C   . MET A 31  ? 0.5120 0.3737 0.4857 -0.0282 -0.0207 0.0277  26  MET A C   
232  O  O   . MET A 31  ? 0.5036 0.3548 0.4648 -0.0290 -0.0168 0.0321  26  MET A O   
233  C  CB  . MET A 31  ? 0.4400 0.3337 0.4326 -0.0244 -0.0305 0.0224  26  MET A CB  
234  C  CG  . MET A 31  ? 0.4729 0.3817 0.4747 -0.0258 -0.0317 0.0171  26  MET A CG  
235  S  SD  . MET A 31  ? 0.4602 0.3719 0.4627 -0.0339 -0.0240 0.0132  26  MET A SD  
236  C  CE  . MET A 31  ? 0.4948 0.3926 0.4801 -0.0333 -0.0216 0.0213  26  MET A CE  
237  N  N   . LYS A 32  ? 0.4874 0.3425 0.4602 -0.0233 -0.0229 0.0291  27  LYS A N   
238  C  CA  . LYS A 32  ? 0.5338 0.3670 0.4904 -0.0187 -0.0196 0.0355  27  LYS A CA  
239  C  C   . LYS A 32  ? 0.5590 0.3727 0.5043 -0.0280 -0.0091 0.0344  27  LYS A C   
240  O  O   . LYS A 32  ? 0.5690 0.3637 0.4962 -0.0261 -0.0046 0.0407  27  LYS A O   
241  C  CB  . LYS A 32  ? 0.5427 0.3723 0.5013 -0.0125 -0.0224 0.0356  27  LYS A CB  
242  C  CG  . LYS A 32  ? 0.6145 0.4188 0.5552 -0.0059 -0.0183 0.0418  27  LYS A CG  
243  C  CD  . LYS A 32  ? 0.6275 0.4324 0.5719 0.0025  -0.0221 0.0418  27  LYS A CD  
244  C  CE  . LYS A 32  ? 0.7624 0.5419 0.6882 0.0121  -0.0183 0.0481  27  LYS A CE  
245  N  NZ  . LYS A 32  ? 0.7833 0.5351 0.6957 0.0037  -0.0076 0.0466  27  LYS A NZ  
246  N  N   . GLY A 33  ? 0.5213 0.3399 0.4761 -0.0386 -0.0047 0.0261  28  GLY A N   
247  C  CA  . GLY A 33  ? 0.5499 0.3524 0.4951 -0.0506 0.0066  0.0230  28  GLY A CA  
248  C  C   . GLY A 33  ? 0.5753 0.3783 0.5147 -0.0553 0.0109  0.0244  28  GLY A C   
249  O  O   . GLY A 33  ? 0.5785 0.3583 0.4994 -0.0604 0.0201  0.0274  28  GLY A O   
250  N  N   . ALA A 34  ? 0.5314 0.3585 0.4844 -0.0535 0.0049  0.0223  29  ALA A N   
251  C  CA  . ALA A 34  ? 0.5508 0.3788 0.4981 -0.0576 0.0092  0.0233  29  ALA A CA  
252  C  C   . ALA A 34  ? 0.5589 0.3678 0.4852 -0.0496 0.0086  0.0340  29  ALA A C   
253  O  O   . ALA A 34  ? 0.5748 0.3675 0.4848 -0.0546 0.0165  0.0367  29  ALA A O   
254  C  CB  . ALA A 34  ? 0.5100 0.3655 0.4744 -0.0557 0.0029  0.0191  29  ALA A CB  
255  N  N   . VAL A 35  ? 0.5450 0.3569 0.4710 -0.0370 -0.0007 0.0397  30  VAL A N   
256  C  CA  . VAL A 35  ? 0.5817 0.3801 0.4886 -0.0276 -0.0028 0.0492  30  VAL A CA  
257  C  C   . VAL A 35  ? 0.6183 0.3840 0.5020 -0.0277 0.0057  0.0543  30  VAL A C   
258  O  O   . VAL A 35  ? 0.6395 0.3877 0.5021 -0.0257 0.0094  0.0608  30  VAL A O   
259  C  CB  . VAL A 35  ? 0.5743 0.3850 0.4871 -0.0147 -0.0138 0.0525  30  VAL A CB  
260  C  CG1 . VAL A 35  ? 0.6063 0.4042 0.4991 -0.0033 -0.0164 0.0618  30  VAL A CG1 
261  C  CG2 . VAL A 35  ? 0.5463 0.3841 0.4758 -0.0153 -0.0208 0.0483  30  VAL A CG2 
262  N  N   . GLU A 36  ? 0.6105 0.3651 0.4956 -0.0304 0.0096  0.0514  31  GLU A N   
263  C  CA  . GLU A 36  ? 0.6442 0.3634 0.5051 -0.0300 0.0185  0.0560  31  GLU A CA  
264  C  C   . GLU A 36  ? 0.6746 0.3742 0.5207 -0.0444 0.0319  0.0540  31  GLU A C   
265  O  O   . GLU A 36  ? 0.7074 0.3718 0.5270 -0.0444 0.0409  0.0591  31  GLU A O   
266  C  CB  . GLU A 36  ? 0.6739 0.3875 0.5411 -0.0302 0.0194  0.0521  31  GLU A CB  
267  C  CG  . GLU A 36  ? 0.6970 0.4190 0.5688 -0.0135 0.0086  0.0568  31  GLU A CG  
268  C  CD  . GLU A 36  ? 0.7474 0.4701 0.6294 -0.0135 0.0081  0.0518  31  GLU A CD  
269  O  OE1 . GLU A 36  ? 0.7414 0.4671 0.6329 -0.0270 0.0133  0.0432  31  GLU A OE1 
270  O  OE2 . GLU A 36  ? 0.7875 0.5100 0.6683 0.0002  0.0021  0.0560  31  GLU A OE2 
271  N  N   . LYS A 37  ? 0.6623 0.3825 0.5230 -0.0564 0.0342  0.0467  32  LYS A N   
272  C  CA  . LYS A 37  ? 0.6669 0.3708 0.5129 -0.0701 0.0474  0.0447  32  LYS A CA  
273  C  C   . LYS A 37  ? 0.7162 0.4005 0.5360 -0.0629 0.0486  0.0551  32  LYS A C   
274  O  O   . LYS A 37  ? 0.7142 0.3742 0.5128 -0.0725 0.0609  0.0561  32  LYS A O   
275  C  CB  . LYS A 37  ? 0.6382 0.3730 0.5079 -0.0827 0.0490  0.0338  32  LYS A CB  
276  C  CG  . LYS A 37  ? 0.6001 0.3576 0.4954 -0.0892 0.0470  0.0228  32  LYS A CG  
277  C  CD  . LYS A 37  ? 0.6297 0.3644 0.5150 -0.1006 0.0582  0.0183  32  LYS A CD  
278  C  CE  . LYS A 37  ? 0.6198 0.3813 0.5311 -0.1078 0.0556  0.0062  32  LYS A CE  
279  N  NZ  . LYS A 37  ? 0.6568 0.3968 0.5591 -0.1154 0.0630  0.0025  32  LYS A NZ  
280  N  N   . GLY A 38  ? 0.7023 0.3971 0.5224 -0.0470 0.0364  0.0624  33  GLY A N   
281  C  CA  . GLY A 38  ? 0.7285 0.4056 0.5222 -0.0381 0.0359  0.0725  33  GLY A CA  
282  C  C   . GLY A 38  ? 0.7304 0.4216 0.5252 -0.0439 0.0364  0.0711  33  GLY A C   
283  O  O   . GLY A 38  ? 0.7808 0.4554 0.5508 -0.0386 0.0376  0.0790  33  GLY A O   
284  N  N   . GLU A 39  ? 0.7119 0.4322 0.5330 -0.0536 0.0357  0.0614  34  GLU A N   
285  C  CA  . GLU A 39  ? 0.6954 0.4314 0.5196 -0.0575 0.0354  0.0595  34  GLU A CA  
286  C  C   . GLU A 39  ? 0.6666 0.4308 0.5075 -0.0472 0.0215  0.0597  34  GLU A C   
287  O  O   . GLU A 39  ? 0.6404 0.4180 0.4975 -0.0408 0.0133  0.0583  34  GLU A O   
288  C  CB  . GLU A 39  ? 0.7051 0.4548 0.5456 -0.0740 0.0447  0.0483  34  GLU A CB  
289  C  CG  . GLU A 39  ? 0.7857 0.5159 0.6195 -0.0872 0.0581  0.0438  34  GLU A CG  
290  C  CD  . GLU A 39  ? 0.9312 0.6292 0.7337 -0.0950 0.0714  0.0482  34  GLU A CD  
291  O  OE1 . GLU A 39  ? 1.0204 0.7126 0.8221 -0.1119 0.0852  0.0403  34  GLU A OE1 
292  O  OE2 . GLU A 39  ? 0.9636 0.6435 0.7417 -0.0847 0.0685  0.0588  34  GLU A OE2 
293  N  N   . GLU A 40  ? 0.6785 0.4503 0.5138 -0.0468 0.0198  0.0610  35  GLU A N   
294  C  CA  . GLU A 40  ? 0.6348 0.4312 0.4831 -0.0392 0.0081  0.0603  35  GLU A CA  
295  C  C   . GLU A 40  ? 0.6379 0.4583 0.5148 -0.0440 0.0062  0.0508  35  GLU A C   
296  O  O   . GLU A 40  ? 0.6385 0.4616 0.5254 -0.0537 0.0139  0.0440  35  GLU A O   
297  C  CB  . GLU A 40  ? 0.7063 0.5056 0.5423 -0.0399 0.0080  0.0621  35  GLU A CB  
298  C  CG  . GLU A 40  ? 0.7789 0.5571 0.5847 -0.0330 0.0079  0.0719  35  GLU A CG  
299  C  CD  . GLU A 40  ? 0.8719 0.6540 0.6656 -0.0355 0.0084  0.0724  35  GLU A CD  
300  O  OE1 . GLU A 40  ? 0.8847 0.6713 0.6845 -0.0468 0.0164  0.0660  35  GLU A OE1 
301  O  OE2 . GLU A 40  ? 0.9499 0.7310 0.7271 -0.0258 0.0011  0.0789  35  GLU A OE2 
302  N  N   . LEU A 41  ? 0.5975 0.4360 0.4867 -0.0370 -0.0039 0.0500  36  LEU A N   
303  C  CA  . LEU A 41  ? 0.5607 0.4192 0.4728 -0.0395 -0.0062 0.0420  36  LEU A CA  
304  C  C   . LEU A 41  ? 0.5758 0.4466 0.4895 -0.0410 -0.0072 0.0389  36  LEU A C   
305  O  O   . LEU A 41  ? 0.5879 0.4592 0.4906 -0.0371 -0.0117 0.0428  36  LEU A O   
306  C  CB  . LEU A 41  ? 0.5427 0.4098 0.4659 -0.0320 -0.0150 0.0423  36  LEU A CB  
307  C  CG  . LEU A 41  ? 0.5682 0.4303 0.4992 -0.0325 -0.0136 0.0407  36  LEU A CG  
308  C  CD1 . LEU A 41  ? 0.6150 0.4541 0.5285 -0.0315 -0.0090 0.0469  36  LEU A CD1 
309  C  CD2 . LEU A 41  ? 0.5583 0.4317 0.5009 -0.0257 -0.0222 0.0399  36  LEU A CD2 
310  N  N   . SER A 42  ? 0.5519 0.4332 0.4788 -0.0463 -0.0030 0.0313  37  SER A N   
311  C  CA  . SER A 42  ? 0.5638 0.4552 0.4927 -0.0468 -0.0033 0.0276  37  SER A CA  
312  C  C   . SER A 42  ? 0.5420 0.4424 0.4769 -0.0406 -0.0122 0.0273  37  SER A C   
313  O  O   . SER A 42  ? 0.5083 0.4111 0.4514 -0.0366 -0.0172 0.0278  37  SER A O   
314  C  CB  . SER A 42  ? 0.5800 0.4816 0.5223 -0.0516 0.0032  0.0192  37  SER A CB  
315  O  OG  . SER A 42  ? 0.5256 0.4379 0.4854 -0.0482 -0.0005 0.0147  37  SER A OG  
316  N  N   . CYS A 43  ? 0.5329 0.4393 0.4661 -0.0410 -0.0126 0.0240  38  CYS A N   
317  C  CA  . CYS A 43  ? 0.5354 0.4482 0.4731 -0.0374 -0.0186 0.0221  38  CYS A CA  
318  C  C   . CYS A 43  ? 0.5221 0.4397 0.4751 -0.0342 -0.0200 0.0182  38  CYS A C   
319  O  O   . CYS A 43  ? 0.4864 0.4055 0.4434 -0.0308 -0.0255 0.0193  38  CYS A O   
320  C  CB  . CYS A 43  ? 0.5578 0.4717 0.4885 -0.0399 -0.0161 0.0184  38  CYS A CB  
321  S  SG  . CYS A 43  ? 0.5756 0.4922 0.5092 -0.0378 -0.0196 0.0140  38  CYS A SG  
322  N  N   . GLU A 44  ? 0.5019 0.4238 0.4647 -0.0351 -0.0148 0.0131  39  GLU A N   
323  C  CA  . GLU A 44  ? 0.5248 0.4534 0.5017 -0.0310 -0.0168 0.0092  39  GLU A CA  
324  C  C   . GLU A 44  ? 0.5050 0.4317 0.4859 -0.0304 -0.0205 0.0124  39  GLU A C   
325  O  O   . GLU A 44  ? 0.4805 0.4095 0.4676 -0.0261 -0.0253 0.0116  39  GLU A O   
326  C  CB  . GLU A 44  ? 0.5590 0.4968 0.5460 -0.0324 -0.0111 0.0029  39  GLU A CB  
327  C  CG  . GLU A 44  ? 0.6078 0.5556 0.6073 -0.0257 -0.0139 -0.0024 39  GLU A CG  
328  C  CD  . GLU A 44  ? 0.6490 0.6114 0.6603 -0.0261 -0.0087 -0.0099 39  GLU A CD  
329  O  OE1 . GLU A 44  ? 0.7041 0.6677 0.7133 -0.0329 -0.0017 -0.0114 39  GLU A OE1 
330  O  OE2 . GLU A 44  ? 0.7064 0.6803 0.7287 -0.0197 -0.0116 -0.0148 39  GLU A OE2 
331  N  N   . GLU A 45  ? 0.5139 0.4342 0.4894 -0.0346 -0.0175 0.0159  40  GLU A N   
332  C  CA  . GLU A 45  ? 0.4785 0.3943 0.4565 -0.0342 -0.0192 0.0183  40  GLU A CA  
333  C  C   . GLU A 45  ? 0.4843 0.3959 0.4566 -0.0291 -0.0259 0.0237  40  GLU A C   
334  O  O   . GLU A 45  ? 0.4753 0.3874 0.4534 -0.0261 -0.0295 0.0239  40  GLU A O   
335  C  CB  . GLU A 45  ? 0.4961 0.4020 0.4669 -0.0403 -0.0123 0.0201  40  GLU A CB  
336  C  CG  . GLU A 45  ? 0.5171 0.4311 0.4968 -0.0470 -0.0049 0.0128  40  GLU A CG  
337  C  CD  . GLU A 45  ? 0.5287 0.4308 0.4979 -0.0556 0.0043  0.0139  40  GLU A CD  
338  O  OE1 . GLU A 45  ? 0.5444 0.4308 0.4958 -0.0550 0.0050  0.0212  40  GLU A OE1 
339  O  OE2 . GLU A 45  ? 0.5190 0.4278 0.4967 -0.0631 0.0110  0.0070  40  GLU A OE2 
340  N  N   . ARG A 46  ? 0.4768 0.3865 0.4381 -0.0282 -0.0276 0.0274  41  ARG A N   
341  C  CA  . ARG A 46  ? 0.4942 0.4059 0.4525 -0.0236 -0.0342 0.0306  41  ARG A CA  
342  C  C   . ARG A 46  ? 0.4793 0.3982 0.4466 -0.0219 -0.0378 0.0265  41  ARG A C   
343  O  O   . ARG A 46  ? 0.4568 0.3778 0.4270 -0.0187 -0.0420 0.0276  41  ARG A O   
344  C  CB  . ARG A 46  ? 0.4998 0.4128 0.4458 -0.0238 -0.0357 0.0332  41  ARG A CB  
345  C  CG  . ARG A 46  ? 0.5326 0.4357 0.4656 -0.0239 -0.0327 0.0385  41  ARG A CG  
346  C  CD  . ARG A 46  ? 0.5514 0.4577 0.4711 -0.0220 -0.0364 0.0417  41  ARG A CD  
347  N  NE  . ARG A 46  ? 0.6049 0.5158 0.5215 -0.0274 -0.0341 0.0376  41  ARG A NE  
348  C  CZ  . ARG A 46  ? 0.6198 0.5243 0.5260 -0.0314 -0.0287 0.0382  41  ARG A CZ  
349  N  NH1 . ARG A 46  ? 0.6341 0.5259 0.5316 -0.0319 -0.0239 0.0424  41  ARG A NH1 
350  N  NH2 . ARG A 46  ? 0.6044 0.5135 0.5071 -0.0357 -0.0271 0.0341  41  ARG A NH2 
351  N  N   . ASN A 47  ? 0.4594 0.3809 0.4299 -0.0234 -0.0355 0.0218  42  ASN A N   
352  C  CA  . ASN A 47  ? 0.4757 0.3993 0.4509 -0.0210 -0.0380 0.0185  42  ASN A CA  
353  C  C   . ASN A 47  ? 0.4820 0.4064 0.4667 -0.0182 -0.0397 0.0177  42  ASN A C   
354  O  O   . ASN A 47  ? 0.4652 0.3896 0.4513 -0.0160 -0.0431 0.0175  42  ASN A O   
355  C  CB  . ASN A 47  ? 0.5035 0.4266 0.4779 -0.0210 -0.0347 0.0139  42  ASN A CB  
356  C  CG  . ASN A 47  ? 0.5535 0.4735 0.5267 -0.0181 -0.0365 0.0114  42  ASN A CG  
357  O  OD1 . ASN A 47  ? 0.5331 0.4511 0.5000 -0.0202 -0.0383 0.0120  42  ASN A OD1 
358  N  ND2 . ASN A 47  ? 0.5860 0.5059 0.5643 -0.0133 -0.0361 0.0083  42  ASN A ND2 
359  N  N   . LEU A 48  ? 0.4507 0.3760 0.4413 -0.0193 -0.0369 0.0165  43  LEU A N   
360  C  CA  . LEU A 48  ? 0.4616 0.3886 0.4607 -0.0178 -0.0385 0.0149  43  LEU A CA  
361  C  C   . LEU A 48  ? 0.4553 0.3773 0.4519 -0.0166 -0.0413 0.0191  43  LEU A C   
362  O  O   . LEU A 48  ? 0.4423 0.3651 0.4426 -0.0140 -0.0445 0.0182  43  LEU A O   
363  C  CB  . LEU A 48  ? 0.4548 0.3852 0.4602 -0.0217 -0.0339 0.0116  43  LEU A CB  
364  C  CG  . LEU A 48  ? 0.4765 0.4166 0.4879 -0.0216 -0.0311 0.0057  43  LEU A CG  
365  C  CD1 . LEU A 48  ? 0.4794 0.4250 0.4969 -0.0280 -0.0252 0.0018  43  LEU A CD1 
366  C  CD2 . LEU A 48  ? 0.4690 0.4161 0.4868 -0.0149 -0.0355 0.0018  43  LEU A CD2 
367  N  N   . LEU A 49  ? 0.4489 0.3654 0.4381 -0.0177 -0.0399 0.0237  44  LEU A N   
368  C  CA  . LEU A 49  ? 0.4517 0.3638 0.4375 -0.0142 -0.0425 0.0279  44  LEU A CA  
369  C  C   . LEU A 49  ? 0.4488 0.3676 0.4355 -0.0111 -0.0475 0.0277  44  LEU A C   
370  O  O   . LEU A 49  ? 0.4530 0.3724 0.4434 -0.0083 -0.0498 0.0275  44  LEU A O   
371  C  CB  . LEU A 49  ? 0.4584 0.3630 0.4326 -0.0136 -0.0407 0.0334  44  LEU A CB  
372  C  CG  . LEU A 49  ? 0.4530 0.3528 0.4213 -0.0071 -0.0436 0.0384  44  LEU A CG  
373  C  CD1 . LEU A 49  ? 0.4754 0.3640 0.4451 -0.0069 -0.0405 0.0385  44  LEU A CD1 
374  C  CD2 . LEU A 49  ? 0.4805 0.3750 0.4347 -0.0044 -0.0433 0.0441  44  LEU A CD2 
375  N  N   . SER A 50  ? 0.4527 0.3763 0.4355 -0.0126 -0.0482 0.0268  45  SER A N   
376  C  CA  . SER A 50  ? 0.4451 0.3753 0.4273 -0.0123 -0.0514 0.0254  45  SER A CA  
377  C  C   . SER A 50  ? 0.4471 0.3762 0.4342 -0.0122 -0.0518 0.0218  45  SER A C   
378  O  O   . SER A 50  ? 0.4494 0.3814 0.4385 -0.0110 -0.0539 0.0213  45  SER A O   
379  C  CB  . SER A 50  ? 0.4590 0.3924 0.4344 -0.0161 -0.0505 0.0238  45  SER A CB  
380  O  OG  . SER A 50  ? 0.4544 0.3943 0.4283 -0.0181 -0.0524 0.0213  45  SER A OG  
381  N  N   . VAL A 51  ? 0.4295 0.3550 0.4180 -0.0127 -0.0497 0.0190  46  VAL A N   
382  C  CA  . VAL A 51  ? 0.4585 0.3811 0.4483 -0.0110 -0.0504 0.0160  46  VAL A CA  
383  C  C   . VAL A 51  ? 0.4593 0.3821 0.4552 -0.0086 -0.0524 0.0163  46  VAL A C   
384  O  O   . VAL A 51  ? 0.4620 0.3831 0.4568 -0.0077 -0.0537 0.0151  46  VAL A O   
385  C  CB  . VAL A 51  ? 0.4978 0.4185 0.4881 -0.0092 -0.0485 0.0131  46  VAL A CB  
386  C  CG1 . VAL A 51  ? 0.4884 0.4061 0.4794 -0.0049 -0.0503 0.0107  46  VAL A CG1 
387  C  CG2 . VAL A 51  ? 0.4993 0.4165 0.4811 -0.0110 -0.0459 0.0120  46  VAL A CG2 
388  N  N   . ALA A 52  ? 0.4258 0.3489 0.4266 -0.0085 -0.0516 0.0174  47  ALA A N   
389  C  CA  . ALA A 52  ? 0.4391 0.3607 0.4445 -0.0072 -0.0526 0.0169  47  ALA A CA  
390  C  C   . ALA A 52  ? 0.4379 0.3593 0.4418 -0.0054 -0.0543 0.0191  47  ALA A C   
391  O  O   . ALA A 52  ? 0.4528 0.3739 0.4577 -0.0042 -0.0556 0.0174  47  ALA A O   
392  C  CB  . ALA A 52  ? 0.4363 0.3557 0.4446 -0.0093 -0.0498 0.0171  47  ALA A CB  
393  N  N   . TYR A 53  ? 0.4390 0.3613 0.4398 -0.0045 -0.0542 0.0228  48  TYR A N   
394  C  CA  . TYR A 53  ? 0.4404 0.3657 0.4412 -0.0011 -0.0560 0.0243  48  TYR A CA  
395  C  C   . TYR A 53  ? 0.4494 0.3828 0.4501 -0.0025 -0.0575 0.0217  48  TYR A C   
396  O  O   . TYR A 53  ? 0.4521 0.3891 0.4553 -0.0008 -0.0583 0.0205  48  TYR A O   
397  C  CB  . TYR A 53  ? 0.4312 0.3565 0.4274 0.0025  -0.0563 0.0289  48  TYR A CB  
398  C  CG  . TYR A 53  ? 0.4437 0.3567 0.4376 0.0048  -0.0537 0.0316  48  TYR A CG  
399  C  CD1 . TYR A 53  ? 0.4506 0.3590 0.4466 0.0081  -0.0534 0.0311  48  TYR A CD1 
400  C  CD2 . TYR A 53  ? 0.4454 0.3495 0.4335 0.0026  -0.0503 0.0339  48  TYR A CD2 
401  C  CE1 . TYR A 53  ? 0.4715 0.3653 0.4631 0.0091  -0.0497 0.0328  48  TYR A CE1 
402  C  CE2 . TYR A 53  ? 0.4847 0.3740 0.4681 0.0028  -0.0462 0.0357  48  TYR A CE2 
403  C  CZ  . TYR A 53  ? 0.4931 0.3768 0.4780 0.0060  -0.0459 0.0350  48  TYR A CZ  
404  O  OH  . TYR A 53  ? 0.5117 0.3778 0.4898 0.0052  -0.0406 0.0361  48  TYR A OH  
405  N  N   . LYS A 54  ? 0.4513 0.3867 0.4482 -0.0065 -0.0569 0.0200  49  LYS A N   
406  C  CA  . LYS A 54  ? 0.4540 0.3942 0.4483 -0.0102 -0.0567 0.0166  49  LYS A CA  
407  C  C   . LYS A 54  ? 0.4646 0.3976 0.4583 -0.0106 -0.0556 0.0140  49  LYS A C   
408  O  O   . LYS A 54  ? 0.4709 0.4070 0.4637 -0.0128 -0.0549 0.0115  49  LYS A O   
409  C  CB  . LYS A 54  ? 0.4866 0.4261 0.4742 -0.0151 -0.0549 0.0149  49  LYS A CB  
410  C  CG  . LYS A 54  ? 0.5697 0.5105 0.5516 -0.0213 -0.0528 0.0104  49  LYS A CG  
411  C  CD  . LYS A 54  ? 0.5706 0.5173 0.5469 -0.0269 -0.0517 0.0085  49  LYS A CD  
412  C  CE  . LYS A 54  ? 0.6142 0.5685 0.5867 -0.0351 -0.0495 0.0029  49  LYS A CE  
413  N  NZ  . LYS A 54  ? 0.5973 0.5589 0.5754 -0.0351 -0.0497 0.0009  49  LYS A NZ  
414  N  N   . ASN A 55  ? 0.4530 0.3773 0.4463 -0.0088 -0.0554 0.0140  50  ASN A N   
415  C  CA  . ASN A 55  ? 0.4724 0.3900 0.4636 -0.0075 -0.0554 0.0119  50  ASN A CA  
416  C  C   . ASN A 55  ? 0.4698 0.3898 0.4661 -0.0058 -0.0563 0.0119  50  ASN A C   
417  O  O   . ASN A 55  ? 0.4548 0.3721 0.4477 -0.0067 -0.0555 0.0099  50  ASN A O   
418  C  CB  . ASN A 55  ? 0.4862 0.3992 0.4779 -0.0044 -0.0562 0.0113  50  ASN A CB  
419  C  CG  . ASN A 55  ? 0.5528 0.4590 0.5356 -0.0039 -0.0548 0.0100  50  ASN A CG  
420  O  OD1 . ASN A 55  ? 0.5712 0.4683 0.5448 -0.0028 -0.0541 0.0087  50  ASN A OD1 
421  N  ND2 . ASN A 55  ? 0.5358 0.4440 0.5193 -0.0042 -0.0537 0.0104  50  ASN A ND2 
422  N  N   . VAL A 56  ? 0.4264 0.3489 0.4289 -0.0034 -0.0571 0.0141  51  VAL A N   
423  C  CA  . VAL A 56  ? 0.4627 0.3848 0.4687 -0.0010 -0.0572 0.0140  51  VAL A CA  
424  C  C   . VAL A 56  ? 0.4787 0.4086 0.4853 -0.0007 -0.0569 0.0134  51  VAL A C   
425  O  O   . VAL A 56  ? 0.4693 0.3990 0.4756 -0.0011 -0.0560 0.0108  51  VAL A O   
426  C  CB  . VAL A 56  ? 0.4733 0.3923 0.4823 0.0013  -0.0567 0.0165  51  VAL A CB  
427  C  CG1 . VAL A 56  ? 0.4807 0.3968 0.4913 0.0045  -0.0560 0.0165  51  VAL A CG1 
428  C  CG2 . VAL A 56  ? 0.4612 0.3759 0.4713 -0.0009 -0.0563 0.0150  51  VAL A CG2 
429  N  N   . VAL A 57  ? 0.4501 0.3888 0.4575 -0.0002 -0.0576 0.0150  52  VAL A N   
430  C  CA  . VAL A 57  ? 0.4495 0.4013 0.4598 0.0005  -0.0578 0.0133  52  VAL A CA  
431  C  C   . VAL A 57  ? 0.4659 0.4207 0.4726 -0.0068 -0.0556 0.0086  52  VAL A C   
432  O  O   . VAL A 57  ? 0.4654 0.4291 0.4746 -0.0083 -0.0541 0.0050  52  VAL A O   
433  C  CB  . VAL A 57  ? 0.4574 0.4199 0.4688 0.0041  -0.0601 0.0160  52  VAL A CB  
434  C  CG1 . VAL A 57  ? 0.4705 0.4381 0.4779 -0.0021 -0.0601 0.0146  52  VAL A CG1 
435  C  CG2 . VAL A 57  ? 0.4974 0.4758 0.5142 0.0091  -0.0614 0.0145  52  VAL A CG2 
436  N  N   . GLY A 58  ? 0.4423 0.3882 0.4419 -0.0115 -0.0544 0.0080  53  GLY A N   
437  C  CA  . GLY A 58  ? 0.4841 0.4262 0.4757 -0.0187 -0.0507 0.0039  53  GLY A CA  
438  C  C   . GLY A 58  ? 0.5030 0.4370 0.4913 -0.0189 -0.0487 0.0019  53  GLY A C   
439  O  O   . GLY A 58  ? 0.5013 0.4378 0.4860 -0.0247 -0.0450 -0.0022 53  GLY A O   
440  N  N   . GLY A 59  ? 0.4813 0.4060 0.4702 -0.0136 -0.0507 0.0042  54  GLY A N   
441  C  CA  . GLY A 59  ? 0.5310 0.4481 0.5158 -0.0134 -0.0493 0.0023  54  GLY A CA  
442  C  C   . GLY A 59  ? 0.4949 0.4230 0.4874 -0.0128 -0.0483 0.0004  54  GLY A C   
443  O  O   . GLY A 59  ? 0.5014 0.4277 0.4895 -0.0162 -0.0448 -0.0029 54  GLY A O   
444  N  N   . GLN A 60  ? 0.4587 0.3973 0.4613 -0.0079 -0.0506 0.0025  55  GLN A N   
445  C  CA  . GLN A 60  ? 0.4508 0.4008 0.4607 -0.0048 -0.0498 0.0007  55  GLN A CA  
446  C  C   . GLN A 60  ? 0.4830 0.4493 0.4951 -0.0100 -0.0473 -0.0038 55  GLN A C   
447  O  O   . GLN A 60  ? 0.4435 0.4169 0.4581 -0.0113 -0.0443 -0.0080 55  GLN A O   
448  C  CB  . GLN A 60  ? 0.4658 0.4201 0.4826 0.0035  -0.0527 0.0046  55  GLN A CB  
449  C  CG  . GLN A 60  ? 0.4727 0.4117 0.4878 0.0068  -0.0534 0.0075  55  GLN A CG  
450  C  CD  . GLN A 60  ? 0.4893 0.4273 0.5065 0.0134  -0.0548 0.0118  55  GLN A CD  
451  O  OE1 . GLN A 60  ? 0.4889 0.4347 0.5067 0.0147  -0.0565 0.0141  55  GLN A OE1 
452  N  NE2 . GLN A 60  ? 0.5163 0.4432 0.5327 0.0171  -0.0535 0.0128  55  GLN A NE2 
453  N  N   . ARG A 61  ? 0.4280 0.4017 0.4392 -0.0140 -0.0480 -0.0041 56  ARG A N   
454  C  CA  . ARG A 61  ? 0.4441 0.4351 0.4570 -0.0214 -0.0451 -0.0101 56  ARG A CA  
455  C  C   . ARG A 61  ? 0.4875 0.4679 0.4903 -0.0314 -0.0387 -0.0149 56  ARG A C   
456  O  O   . ARG A 61  ? 0.4499 0.4431 0.4556 -0.0368 -0.0344 -0.0210 56  ARG A O   
457  C  CB  . ARG A 61  ? 0.4843 0.4828 0.4957 -0.0254 -0.0466 -0.0101 56  ARG A CB  
458  C  CG  . ARG A 61  ? 0.4541 0.4638 0.4729 -0.0160 -0.0525 -0.0055 56  ARG A CG  
459  C  CD  . ARG A 61  ? 0.4927 0.5026 0.5064 -0.0202 -0.0539 -0.0045 56  ARG A CD  
460  N  NE  . ARG A 61  ? 0.4864 0.5141 0.5000 -0.0298 -0.0518 -0.0114 56  ARG A NE  
461  C  CZ  . ARG A 61  ? 0.5324 0.5562 0.5379 -0.0384 -0.0499 -0.0134 56  ARG A CZ  
462  N  NH1 . ARG A 61  ? 0.5108 0.5138 0.5079 -0.0376 -0.0498 -0.0088 56  ARG A NH1 
463  N  NH2 . ARG A 61  ? 0.4899 0.5323 0.4959 -0.0482 -0.0477 -0.0209 56  ARG A NH2 
464  N  N   . ALA A 62  ? 0.4715 0.4283 0.4612 -0.0335 -0.0375 -0.0124 57  ALA A N   
465  C  CA  . ALA A 62  ? 0.5058 0.4469 0.4809 -0.0415 -0.0311 -0.0158 57  ALA A CA  
466  C  C   . ALA A 62  ? 0.5007 0.4416 0.4775 -0.0399 -0.0290 -0.0177 57  ALA A C   
467  O  O   . ALA A 62  ? 0.4964 0.4387 0.4679 -0.0483 -0.0224 -0.0233 57  ALA A O   
468  C  CB  . ALA A 62  ? 0.5306 0.4462 0.4908 -0.0397 -0.0316 -0.0117 57  ALA A CB  
469  N  N   . ALA A 63  ? 0.4670 0.4062 0.4505 -0.0302 -0.0337 -0.0138 58  ALA A N   
470  C  CA  . ALA A 63  ? 0.4981 0.4369 0.4831 -0.0282 -0.0317 -0.0159 58  ALA A CA  
471  C  C   . ALA A 63  ? 0.4825 0.4453 0.4801 -0.0293 -0.0290 -0.0211 58  ALA A C   
472  O  O   . ALA A 63  ? 0.4429 0.4080 0.4380 -0.0346 -0.0233 -0.0264 58  ALA A O   
473  C  CB  . ALA A 63  ? 0.4862 0.4184 0.4757 -0.0185 -0.0368 -0.0116 58  ALA A CB  
474  N  N   . TRP A 64  ? 0.4681 0.4498 0.4789 -0.0238 -0.0332 -0.0200 59  TRP A N   
475  C  CA  . TRP A 64  ? 0.4457 0.4544 0.4697 -0.0221 -0.0320 -0.0251 59  TRP A CA  
476  C  C   . TRP A 64  ? 0.4776 0.4985 0.4993 -0.0355 -0.0254 -0.0333 59  TRP A C   
477  O  O   . TRP A 64  ? 0.4636 0.5010 0.4921 -0.0378 -0.0210 -0.0399 59  TRP A O   
478  C  CB  . TRP A 64  ? 0.4327 0.4580 0.4672 -0.0133 -0.0383 -0.0218 59  TRP A CB  
479  C  CG  . TRP A 64  ? 0.4583 0.5129 0.5067 -0.0074 -0.0389 -0.0263 59  TRP A CG  
480  C  CD1 . TRP A 64  ? 0.4776 0.5372 0.5335 0.0061  -0.0409 -0.0245 59  TRP A CD1 
481  C  CD2 . TRP A 64  ? 0.4800 0.5644 0.5363 -0.0138 -0.0373 -0.0341 59  TRP A CD2 
482  N  NE1 . TRP A 64  ? 0.4559 0.5477 0.5244 0.0104  -0.0413 -0.0303 59  TRP A NE1 
483  C  CE2 . TRP A 64  ? 0.4657 0.5754 0.5359 -0.0022 -0.0393 -0.0367 59  TRP A CE2 
484  C  CE3 . TRP A 64  ? 0.4756 0.5677 0.5280 -0.0284 -0.0338 -0.0398 59  TRP A CE3 
485  C  CZ2 . TRP A 64  ? 0.4741 0.6210 0.5565 -0.0045 -0.0389 -0.0453 59  TRP A CZ2 
486  C  CZ3 . TRP A 64  ? 0.4874 0.6148 0.5512 -0.0329 -0.0327 -0.0487 59  TRP A CZ3 
487  C  CH2 . TRP A 64  ? 0.4846 0.6413 0.5643 -0.0207 -0.0357 -0.0517 59  TRP A CH2 
488  N  N   . ARG A 65  ? 0.4730 0.4856 0.4846 -0.0451 -0.0237 -0.0337 60  ARG A N   
489  C  CA  . ARG A 65  ? 0.5062 0.5270 0.5128 -0.0602 -0.0158 -0.0422 60  ARG A CA  
490  C  C   . ARG A 65  ? 0.4895 0.4928 0.4831 -0.0680 -0.0074 -0.0457 60  ARG A C   
491  O  O   . ARG A 65  ? 0.5081 0.5262 0.5037 -0.0781 0.0000  -0.0544 60  ARG A O   
492  C  CB  . ARG A 65  ? 0.5109 0.5202 0.5058 -0.0684 -0.0150 -0.0415 60  ARG A CB  
493  C  CG  . ARG A 65  ? 0.5410 0.5741 0.5481 -0.0653 -0.0210 -0.0414 60  ARG A CG  
494  C  CD  . ARG A 65  ? 0.6332 0.6518 0.6271 -0.0736 -0.0194 -0.0408 60  ARG A CD  
495  N  NE  . ARG A 65  ? 0.6864 0.7238 0.6896 -0.0695 -0.0260 -0.0395 60  ARG A NE  
496  C  CZ  . ARG A 65  ? 0.7088 0.7316 0.7045 -0.0678 -0.0288 -0.0343 60  ARG A CZ  
497  N  NH1 . ARG A 65  ? 0.7198 0.7108 0.7005 -0.0677 -0.0267 -0.0296 60  ARG A NH1 
498  N  NH2 . ARG A 65  ? 0.6776 0.7192 0.6803 -0.0656 -0.0340 -0.0341 60  ARG A NH2 
499  N  N   . VAL A 66  ? 0.4891 0.4622 0.4685 -0.0638 -0.0083 -0.0395 61  VAL A N   
500  C  CA  . VAL A 66  ? 0.5199 0.4748 0.4847 -0.0694 -0.0011 -0.0419 61  VAL A CA  
501  C  C   . VAL A 66  ? 0.5438 0.5182 0.5223 -0.0664 0.0008  -0.0466 61  VAL A C   
502  O  O   . VAL A 66  ? 0.5310 0.5103 0.5058 -0.0765 0.0097  -0.0541 61  VAL A O   
503  C  CB  . VAL A 66  ? 0.5408 0.4643 0.4899 -0.0622 -0.0047 -0.0343 61  VAL A CB  
504  C  CG1 . VAL A 66  ? 0.5614 0.4685 0.4966 -0.0648 0.0010  -0.0361 61  VAL A CG1 
505  C  CG2 . VAL A 66  ? 0.5784 0.4806 0.5105 -0.0657 -0.0043 -0.0310 61  VAL A CG2 
506  N  N   . LEU A 67  ? 0.5045 0.4885 0.4976 -0.0526 -0.0066 -0.0425 62  LEU A N   
507  C  CA  . LEU A 67  ? 0.4900 0.4884 0.4942 -0.0474 -0.0047 -0.0463 62  LEU A CA  
508  C  C   . LEU A 67  ? 0.5226 0.5565 0.5431 -0.0513 -0.0012 -0.0550 62  LEU A C   
509  O  O   . LEU A 67  ? 0.5202 0.5659 0.5448 -0.0546 0.0054  -0.0621 62  LEU A O   
510  C  CB  . LEU A 67  ? 0.4515 0.4481 0.4648 -0.0318 -0.0125 -0.0399 62  LEU A CB  
511  C  CG  . LEU A 67  ? 0.4782 0.4451 0.4781 -0.0285 -0.0162 -0.0330 62  LEU A CG  
512  C  CD1 . LEU A 67  ? 0.4700 0.4359 0.4787 -0.0158 -0.0228 -0.0277 62  LEU A CD1 
513  C  CD2 . LEU A 67  ? 0.4707 0.4208 0.4572 -0.0328 -0.0107 -0.0356 62  LEU A CD2 
514  N  N   . SER A 68  ? 0.4929 0.5462 0.5230 -0.0508 -0.0055 -0.0552 63  SER A N   
515  C  CA  . SER A 68  ? 0.4936 0.5855 0.5402 -0.0540 -0.0033 -0.0645 63  SER A CA  
516  C  C   . SER A 68  ? 0.5618 0.6575 0.6006 -0.0736 0.0081  -0.0747 63  SER A C   
517  O  O   . SER A 68  ? 0.5962 0.7202 0.6470 -0.0778 0.0136  -0.0845 63  SER A O   
518  C  CB  . SER A 68  ? 0.5058 0.6163 0.5613 -0.0501 -0.0108 -0.0625 63  SER A CB  
519  O  OG  . SER A 68  ? 0.5672 0.7182 0.6381 -0.0541 -0.0092 -0.0726 63  SER A OG  
520  N  N   . SER A 69  ? 0.5386 0.6055 0.5565 -0.0858 0.0125  -0.0729 64  SER A N   
521  C  CA  . SER A 69  ? 0.5879 0.6509 0.5931 -0.1057 0.0251  -0.0822 64  SER A CA  
522  C  C   . SER A 69  ? 0.6379 0.6921 0.6371 -0.1081 0.0329  -0.0856 64  SER A C   
523  O  O   . SER A 69  ? 0.6577 0.7299 0.6600 -0.1209 0.0430  -0.0967 64  SER A O   
524  C  CB  . SER A 69  ? 0.6170 0.6436 0.5965 -0.1154 0.0284  -0.0781 64  SER A CB  
525  O  OG  . SER A 69  ? 0.6815 0.6974 0.6439 -0.1350 0.0421  -0.0866 64  SER A OG  
526  N  N   . ILE A 70  ? 0.6024 0.6302 0.5930 -0.0968 0.0289  -0.0770 65  ILE A N   
527  C  CA  . ILE A 70  ? 0.6507 0.6700 0.6354 -0.0976 0.0354  -0.0798 65  ILE A CA  
528  C  C   . ILE A 70  ? 0.6850 0.7430 0.6949 -0.0917 0.0360  -0.0873 65  ILE A C   
529  O  O   . ILE A 70  ? 0.7026 0.7704 0.7128 -0.1004 0.0460  -0.0962 65  ILE A O   
530  C  CB  . ILE A 70  ? 0.5895 0.5770 0.5621 -0.0855 0.0291  -0.0695 65  ILE A CB  
531  C  CG1 . ILE A 70  ? 0.6178 0.5685 0.5641 -0.0904 0.0292  -0.0631 65  ILE A CG1 
532  C  CG2 . ILE A 70  ? 0.6072 0.5892 0.5759 -0.0843 0.0346  -0.0726 65  ILE A CG2 
533  C  CD1 . ILE A 70  ? 0.6270 0.5520 0.5636 -0.0779 0.0212  -0.0536 65  ILE A CD1 
534  N  N   . GLU A 71  ? 0.6176 0.6975 0.6478 -0.0763 0.0258  -0.0838 66  GLU A N   
535  C  CA  . GLU A 71  ? 0.6295 0.7463 0.6832 -0.0669 0.0251  -0.0901 66  GLU A CA  
536  C  C   . GLU A 71  ? 0.7072 0.8620 0.7733 -0.0799 0.0324  -0.1035 66  GLU A C   
537  O  O   . GLU A 71  ? 0.7427 0.9220 0.8205 -0.0806 0.0388  -0.1128 66  GLU A O   
538  C  CB  . GLU A 71  ? 0.5932 0.7209 0.6611 -0.0475 0.0128  -0.0826 66  GLU A CB  
539  C  CG  . GLU A 71  ? 0.5825 0.7399 0.6706 -0.0322 0.0109  -0.0864 66  GLU A CG  
540  C  CD  . GLU A 71  ? 0.5486 0.7111 0.6456 -0.0131 -0.0005 -0.0781 66  GLU A CD  
541  O  OE1 . GLU A 71  ? 0.5167 0.6621 0.6056 -0.0136 -0.0065 -0.0702 66  GLU A OE1 
542  O  OE2 . GLU A 71  ? 0.5396 0.7213 0.6500 0.0028  -0.0029 -0.0794 66  GLU A OE2 
543  N  N   . GLN A 72  ? 0.6790 0.8402 0.7426 -0.0912 0.0323  -0.1056 67  GLN A N   
544  C  CA  . GLN A 72  ? 0.7311 0.9314 0.8070 -0.1055 0.0394  -0.1199 67  GLN A CA  
545  C  C   . GLN A 72  ? 0.7719 0.9606 0.8328 -0.1271 0.0552  -0.1292 67  GLN A C   
546  O  O   . GLN A 72  ? 0.8162 1.0404 0.8908 -0.1365 0.0633  -0.1429 67  GLN A O   
547  C  CB  . GLN A 72  ? 0.7307 0.9402 0.8068 -0.1126 0.0351  -0.1202 67  GLN A CB  
548  C  CG  . GLN A 72  ? 0.7750 1.0085 0.8690 -0.0934 0.0206  -0.1144 67  GLN A CG  
549  C  CD  . GLN A 72  ? 0.8239 1.0931 0.9419 -0.0734 0.0147  -0.1165 67  GLN A CD  
550  O  OE1 . GLN A 72  ? 0.8509 1.1389 0.9783 -0.0744 0.0215  -0.1251 67  GLN A OE1 
551  N  NE2 . GLN A 72  ? 0.8176 1.0940 0.9439 -0.0543 0.0023  -0.1082 67  GLN A NE2 
552  N  N   . LYS A 73  ? 0.7739 0.9140 0.8059 -0.1347 0.0600  -0.1224 68  LYS A N   
553  C  CA  . LYS A 73  ? 0.8539 0.9764 0.8666 -0.1541 0.0756  -0.1300 68  LYS A CA  
554  C  C   . LYS A 73  ? 0.8635 0.9969 0.8845 -0.1487 0.0804  -0.1345 68  LYS A C   
555  O  O   . LYS A 73  ? 0.8938 1.0404 0.9140 -0.1645 0.0938  -0.1467 68  LYS A O   
556  C  CB  . LYS A 73  ? 0.8738 0.9393 0.8513 -0.1590 0.0781  -0.1201 68  LYS A CB  
557  C  CG  . LYS A 73  ? 0.9387 0.9811 0.8894 -0.1830 0.0952  -0.1277 68  LYS A CG  
558  C  CD  . LYS A 73  ? 0.9788 1.0015 0.9115 -0.1957 0.0979  -0.1269 68  LYS A CD  
559  C  CE  . LYS A 73  ? 1.0097 1.0215 0.9213 -0.2230 0.1171  -0.1388 68  LYS A CE  
560  N  NZ  . LYS A 73  ? 0.9819 1.0442 0.9177 -0.2375 0.1221  -0.1543 68  LYS A NZ  
561  N  N   . SER A 74  ? 0.8439 0.9712 0.8721 -0.1276 0.0706  -0.1256 69  SER A N   
562  C  CA  . SER A 74  ? 0.8639 0.9999 0.8996 -0.1207 0.0747  -0.1295 69  SER A CA  
563  C  C   . SER A 74  ? 0.8573 1.0482 0.9254 -0.1142 0.0746  -0.1404 69  SER A C   
564  O  O   . SER A 74  ? 0.8765 1.0792 0.9530 -0.1082 0.0790  -0.1454 69  SER A O   
565  C  CB  . SER A 74  ? 0.8526 0.9612 0.8831 -0.1012 0.0649  -0.1168 69  SER A CB  
566  O  OG  . SER A 74  ? 0.8370 0.9679 0.8896 -0.0819 0.0527  -0.1124 69  SER A OG  
567  N  N   . ASN A 75  ? 0.8550 1.0804 0.9408 -0.1142 0.0693  -0.1444 70  ASN A N   
568  C  CA  . ASN A 75  ? 0.8562 1.1388 0.9724 -0.1085 0.0689  -0.1562 70  ASN A CA  
569  C  C   . ASN A 75  ? 0.8704 1.1847 0.9920 -0.1328 0.0808  -0.1727 70  ASN A C   
570  O  O   . ASN A 75  ? 0.8702 1.2382 1.0185 -0.1302 0.0809  -0.1848 70  ASN A O   
571  C  CB  . ASN A 75  ? 0.8261 1.1311 0.9602 -0.0885 0.0532  -0.1499 70  ASN A CB  
572  C  CG  . ASN A 75  ? 0.8334 1.1189 0.9683 -0.0629 0.0433  -0.1372 70  ASN A CG  
573  O  OD1 . ASN A 75  ? 0.8382 1.1068 0.9679 -0.0579 0.0478  -0.1362 70  ASN A OD1 
574  N  ND2 . ASN A 75  ? 0.8000 1.0867 0.9400 -0.0476 0.0304  -0.1280 70  ASN A ND2 
575  N  N   . GLU A 76  ? 0.8947 1.1772 0.9908 -0.1561 0.0910  -0.1740 71  GLU A N   
576  C  CA  . GLU A 76  ? 0.9170 1.2239 1.0140 -0.1825 0.1040  -0.1900 71  GLU A CA  
577  C  C   . GLU A 76  ? 0.9679 1.2682 1.0541 -0.2001 0.1220  -0.2006 71  GLU A C   
578  O  O   . GLU A 76  ? 0.9472 1.2914 1.0506 -0.2132 0.1320  -0.2177 71  GLU A O   
579  C  CB  . GLU A 76  ? 0.9090 1.1833 0.9820 -0.1986 0.1056  -0.1858 71  GLU A CB  
580  N  N   . LYS A 82  ? 0.9635 1.0407 0.9832 -0.0768 0.0845  -0.1253 77  LYS A N   
581  C  CA  . LYS A 82  ? 0.9062 1.0269 0.9571 -0.0642 0.0808  -0.1304 77  LYS A CA  
582  C  C   . LYS A 82  ? 0.8103 0.9260 0.8699 -0.0413 0.0718  -0.1236 77  LYS A C   
583  O  O   . LYS A 82  ? 0.8009 0.9457 0.8810 -0.0282 0.0721  -0.1291 77  LYS A O   
584  C  CB  . LYS A 82  ? 0.9483 1.1044 1.0132 -0.0718 0.0936  -0.1457 77  LYS A CB  
585  N  N   . GLY A 83  ? 0.7465 0.8252 0.7895 -0.0366 0.0642  -0.1123 78  GLY A N   
586  C  CA  . GLY A 83  ? 0.6709 0.7399 0.7187 -0.0176 0.0564  -0.1057 78  GLY A CA  
587  C  C   . GLY A 83  ? 0.5877 0.6653 0.6470 -0.0064 0.0449  -0.0982 78  GLY A C   
588  O  O   . GLY A 83  ? 0.5697 0.6625 0.6342 -0.0132 0.0423  -0.0983 78  GLY A O   
589  N  N   . PRO A 84  ? 0.5712 0.6378 0.6331 0.0103  0.0385  -0.0919 79  PRO A N   
590  C  CA  . PRO A 84  ? 0.5226 0.5943 0.5927 0.0214  0.0282  -0.0843 79  PRO A CA  
591  C  C   . PRO A 84  ? 0.5322 0.5758 0.5879 0.0153  0.0211  -0.0747 79  PRO A C   
592  O  O   . PRO A 84  ? 0.4724 0.5183 0.5333 0.0228  0.0132  -0.0683 79  PRO A O   
593  C  CB  . PRO A 84  ? 0.5414 0.6077 0.6161 0.0411  0.0267  -0.0822 79  PRO A CB  
594  C  CG  . PRO A 84  ? 0.5817 0.6209 0.6415 0.0365  0.0329  -0.0839 79  PRO A CG  
595  C  CD  . PRO A 84  ? 0.5846 0.6342 0.6414 0.0198  0.0417  -0.0925 79  PRO A CD  
596  N  N   . GLU A 85  ? 0.5141 0.5321 0.5515 0.0029  0.0237  -0.0737 80  GLU A N   
597  C  CA  . GLU A 85  ? 0.4943 0.4851 0.5183 0.0007  0.0166  -0.0649 80  GLU A CA  
598  C  C   . GLU A 85  ? 0.5023 0.5007 0.5291 -0.0037 0.0111  -0.0608 80  GLU A C   
599  O  O   . GLU A 85  ? 0.4752 0.4640 0.5017 0.0019  0.0034  -0.0534 80  GLU A O   
600  C  CB  . GLU A 85  ? 0.5165 0.4815 0.5196 -0.0101 0.0202  -0.0653 80  GLU A CB  
601  C  CG  . GLU A 85  ? 0.5589 0.5097 0.5558 -0.0054 0.0238  -0.0679 80  GLU A CG  
602  C  CD  . GLU A 85  ? 0.5801 0.5451 0.5807 -0.0079 0.0342  -0.0772 80  GLU A CD  
603  O  OE1 . GLU A 85  ? 0.5655 0.5540 0.5753 -0.0133 0.0387  -0.0824 80  GLU A OE1 
604  O  OE2 . GLU A 85  ? 0.5701 0.5234 0.5643 -0.0052 0.0383  -0.0802 80  GLU A OE2 
605  N  N   . VAL A 86  ? 0.4904 0.5051 0.5190 -0.0148 0.0157  -0.0661 81  VAL A N   
606  C  CA  . VAL A 86  ? 0.4795 0.4996 0.5089 -0.0200 0.0112  -0.0629 81  VAL A CA  
607  C  C   . VAL A 86  ? 0.4756 0.5166 0.5224 -0.0073 0.0040  -0.0601 81  VAL A C   
608  O  O   . VAL A 86  ? 0.4463 0.4793 0.4914 -0.0047 -0.0032 -0.0530 81  VAL A O   
609  C  CB  . VAL A 86  ? 0.4940 0.5275 0.5211 -0.0359 0.0191  -0.0707 81  VAL A CB  
610  C  CG1 . VAL A 86  ? 0.5370 0.5769 0.5654 -0.0409 0.0147  -0.0681 81  VAL A CG1 
611  C  CG2 . VAL A 86  ? 0.5595 0.5652 0.5635 -0.0480 0.0259  -0.0715 81  VAL A CG2 
612  N  N   . ARG A 87  ? 0.4647 0.5326 0.5276 0.0017  0.0058  -0.0655 82  ARG A N   
613  C  CA  . ARG A 87  ? 0.4645 0.5517 0.5416 0.0161  -0.0014 -0.0624 82  ARG A CA  
614  C  C   . ARG A 87  ? 0.4664 0.5277 0.5371 0.0287  -0.0075 -0.0528 82  ARG A C   
615  O  O   . ARG A 87  ? 0.4423 0.5017 0.5137 0.0341  -0.0144 -0.0462 82  ARG A O   
616  C  CB  . ARG A 87  ? 0.4725 0.5938 0.5670 0.0260  0.0016  -0.0704 82  ARG A CB  
617  C  CG  . ARG A 87  ? 0.4829 0.6205 0.5886 0.0452  -0.0064 -0.0662 82  ARG A CG  
618  C  CD  . ARG A 87  ? 0.5199 0.6902 0.6420 0.0592  -0.0040 -0.0737 82  ARG A CD  
619  N  NE  . ARG A 87  ? 0.5115 0.6671 0.6297 0.0637  0.0029  -0.0764 82  ARG A NE  
620  C  CZ  . ARG A 87  ? 0.5385 0.6651 0.6476 0.0766  0.0019  -0.0697 82  ARG A CZ  
621  N  NH1 . ARG A 87  ? 0.5221 0.6295 0.6243 0.0861  -0.0054 -0.0596 82  ARG A NH1 
622  N  NH2 . ARG A 87  ? 0.5491 0.6648 0.6548 0.0789  0.0091  -0.0738 82  ARG A NH2 
623  N  N   . GLU A 88  ? 0.4592 0.4993 0.5224 0.0322  -0.0041 -0.0524 83  GLU A N   
624  C  CA  . GLU A 88  ? 0.4785 0.4928 0.5344 0.0417  -0.0083 -0.0447 83  GLU A CA  
625  C  C   . GLU A 88  ? 0.4695 0.4648 0.5157 0.0341  -0.0136 -0.0379 83  GLU A C   
626  O  O   . GLU A 88  ? 0.4760 0.4629 0.5215 0.0413  -0.0188 -0.0314 83  GLU A O   
627  C  CB  . GLU A 88  ? 0.4944 0.4881 0.5418 0.0428  -0.0029 -0.0469 83  GLU A CB  
628  C  CG  . GLU A 88  ? 0.4894 0.4975 0.5454 0.0537  0.0026  -0.0530 83  GLU A CG  
629  C  CD  . GLU A 88  ? 0.5361 0.5234 0.5819 0.0515  0.0090  -0.0565 83  GLU A CD  
630  O  OE1 . GLU A 88  ? 0.5195 0.4871 0.5524 0.0392  0.0093  -0.0557 83  GLU A OE1 
631  O  OE2 . GLU A 88  ? 0.5235 0.5140 0.5733 0.0628  0.0135  -0.0601 83  GLU A OE2 
632  N  N   . TYR A 89  ? 0.4514 0.4389 0.4888 0.0202  -0.0119 -0.0394 84  TYR A N   
633  C  CA  . TYR A 89  ? 0.4722 0.4425 0.5004 0.0146  -0.0169 -0.0335 84  TYR A CA  
634  C  C   . TYR A 89  ? 0.4533 0.4383 0.4878 0.0138  -0.0213 -0.0308 84  TYR A C   
635  O  O   . TYR A 89  ? 0.4578 0.4331 0.4899 0.0160  -0.0266 -0.0247 84  TYR A O   
636  C  CB  . TYR A 89  ? 0.5020 0.4572 0.5161 0.0027  -0.0140 -0.0354 84  TYR A CB  
637  C  CG  . TYR A 89  ? 0.4888 0.4268 0.4932 -0.0007 -0.0194 -0.0298 84  TYR A CG  
638  C  CD1 . TYR A 89  ? 0.5011 0.4290 0.5065 0.0056  -0.0244 -0.0249 84  TYR A CD1 
639  C  CD2 . TYR A 89  ? 0.5225 0.4541 0.5161 -0.0100 -0.0187 -0.0298 84  TYR A CD2 
640  C  CE1 . TYR A 89  ? 0.5210 0.4374 0.5198 0.0027  -0.0291 -0.0209 84  TYR A CE1 
641  C  CE2 . TYR A 89  ? 0.5189 0.4367 0.5044 -0.0110 -0.0237 -0.0250 84  TYR A CE2 
642  C  CZ  . TYR A 89  ? 0.5032 0.4156 0.4926 -0.0046 -0.0291 -0.0209 84  TYR A CZ  
643  O  OH  . TYR A 89  ? 0.5401 0.4425 0.5231 -0.0057 -0.0338 -0.0173 84  TYR A OH  
644  N  N   . ARG A 90  ? 0.4406 0.4502 0.4834 0.0101  -0.0188 -0.0361 85  ARG A N   
645  C  CA  . ARG A 90  ? 0.4571 0.4832 0.5063 0.0098  -0.0231 -0.0346 85  ARG A CA  
646  C  C   . ARG A 90  ? 0.4552 0.4863 0.5116 0.0248  -0.0289 -0.0292 85  ARG A C   
647  O  O   . ARG A 90  ? 0.4570 0.4846 0.5117 0.0261  -0.0341 -0.0238 85  ARG A O   
648  C  CB  . ARG A 90  ? 0.4493 0.5049 0.5073 0.0026  -0.0188 -0.0431 85  ARG A CB  
649  C  CG  . ARG A 90  ? 0.4725 0.5460 0.5353 -0.0014 -0.0226 -0.0433 85  ARG A CG  
650  C  CD  . ARG A 90  ? 0.4816 0.5835 0.5595 0.0123  -0.0277 -0.0435 85  ARG A CD  
651  N  NE  . ARG A 90  ? 0.4656 0.5952 0.5561 0.0158  -0.0235 -0.0522 85  ARG A NE  
652  C  CZ  . ARG A 90  ? 0.4865 0.6348 0.5883 0.0329  -0.0268 -0.0523 85  ARG A CZ  
653  N  NH1 . ARG A 90  ? 0.4845 0.6262 0.5851 0.0476  -0.0341 -0.0440 85  ARG A NH1 
654  N  NH2 . ARG A 90  ? 0.4799 0.6531 0.5932 0.0359  -0.0220 -0.0611 85  ARG A NH2 
655  N  N   . GLU A 91  ? 0.4338 0.4706 0.4962 0.0369  -0.0275 -0.0306 86  GLU A N   
656  C  CA  . GLU A 91  ? 0.4690 0.5049 0.5338 0.0530  -0.0321 -0.0249 86  GLU A CA  
657  C  C   . GLU A 91  ? 0.4639 0.4678 0.5169 0.0537  -0.0343 -0.0171 86  GLU A C   
658  O  O   . GLU A 91  ? 0.4709 0.4703 0.5219 0.0607  -0.0386 -0.0110 86  GLU A O   
659  C  CB  . GLU A 91  ? 0.4665 0.5099 0.5370 0.0667  -0.0289 -0.0281 86  GLU A CB  
660  C  CG  . GLU A 91  ? 0.5080 0.5908 0.5938 0.0737  -0.0293 -0.0345 86  GLU A CG  
661  C  CD  . GLU A 91  ? 0.5477 0.6397 0.6398 0.0842  -0.0241 -0.0404 86  GLU A CD  
662  O  OE1 . GLU A 91  ? 0.5398 0.6675 0.6461 0.0876  -0.0230 -0.0481 86  GLU A OE1 
663  O  OE2 . GLU A 91  ? 0.6271 0.6917 0.7101 0.0891  -0.0207 -0.0379 86  GLU A OE2 
664  N  N   . LYS A 92  ? 0.4701 0.4525 0.5147 0.0460  -0.0312 -0.0178 87  LYS A N   
665  C  CA  . LYS A 92  ? 0.4876 0.4436 0.5224 0.0440  -0.0329 -0.0125 87  LYS A CA  
666  C  C   . LYS A 92  ? 0.4894 0.4456 0.5226 0.0381  -0.0376 -0.0083 87  LYS A C   
667  O  O   . LYS A 92  ? 0.4729 0.4191 0.5030 0.0422  -0.0402 -0.0028 87  LYS A O   
668  C  CB  . LYS A 92  ? 0.4951 0.4352 0.5222 0.0352  -0.0297 -0.0157 87  LYS A CB  
669  C  CG  . LYS A 92  ? 0.5767 0.4933 0.5949 0.0325  -0.0310 -0.0125 87  LYS A CG  
670  C  CD  . LYS A 92  ? 0.6298 0.5350 0.6408 0.0261  -0.0280 -0.0171 87  LYS A CD  
671  C  CE  . LYS A 92  ? 0.6379 0.5274 0.6413 0.0198  -0.0306 -0.0160 87  LYS A CE  
672  N  NZ  . LYS A 92  ? 0.7091 0.5825 0.7069 0.0210  -0.0272 -0.0185 87  LYS A NZ  
673  N  N   . VAL A 93  ? 0.4712 0.4359 0.5045 0.0277  -0.0376 -0.0111 88  VAL A N   
674  C  CA  . VAL A 93  ? 0.4594 0.4234 0.4901 0.0219  -0.0411 -0.0079 88  VAL A CA  
675  C  C   . VAL A 93  ? 0.4665 0.4463 0.5035 0.0282  -0.0446 -0.0053 88  VAL A C   
676  O  O   . VAL A 93  ? 0.4290 0.4025 0.4631 0.0288  -0.0479 -0.0003 88  VAL A O   
677  C  CB  . VAL A 93  ? 0.4586 0.4257 0.4853 0.0102  -0.0389 -0.0119 88  VAL A CB  
678  C  CG1 . VAL A 93  ? 0.4684 0.4356 0.4920 0.0050  -0.0418 -0.0093 88  VAL A CG1 
679  C  CG2 . VAL A 93  ? 0.4811 0.4295 0.4979 0.0054  -0.0367 -0.0133 88  VAL A CG2 
680  N  N   . GLU A 94  ? 0.4521 0.4543 0.4977 0.0332  -0.0440 -0.0090 89  GLU A N   
681  C  CA  . GLU A 94  ? 0.4582 0.4789 0.5095 0.0412  -0.0482 -0.0070 89  GLU A CA  
682  C  C   . GLU A 94  ? 0.4808 0.4860 0.5269 0.0535  -0.0509 0.0004  89  GLU A C   
683  O  O   . GLU A 94  ? 0.4636 0.4694 0.5070 0.0560  -0.0548 0.0051  89  GLU A O   
684  C  CB  . GLU A 94  ? 0.4786 0.5284 0.5411 0.0462  -0.0470 -0.0136 89  GLU A CB  
685  C  CG  . GLU A 94  ? 0.4968 0.5709 0.5663 0.0580  -0.0522 -0.0126 89  GLU A CG  
686  C  CD  . GLU A 94  ? 0.5210 0.6310 0.6040 0.0589  -0.0508 -0.0219 89  GLU A CD  
687  O  OE1 . GLU A 94  ? 0.5749 0.7033 0.6647 0.0749  -0.0537 -0.0221 89  GLU A OE1 
688  O  OE2 . GLU A 94  ? 0.4881 0.6084 0.5742 0.0438  -0.0465 -0.0292 89  GLU A OE2 
689  N  N   . THR A 95  ? 0.4591 0.4482 0.5018 0.0606  -0.0479 0.0014  90  THR A N   
690  C  CA  . THR A 95  ? 0.5096 0.4795 0.5440 0.0716  -0.0486 0.0081  90  THR A CA  
691  C  C   . THR A 95  ? 0.5051 0.4543 0.5310 0.0636  -0.0492 0.0128  90  THR A C   
692  O  O   . THR A 95  ? 0.5154 0.4560 0.5348 0.0692  -0.0510 0.0186  90  THR A O   
693  C  CB  . THR A 95  ? 0.5252 0.4794 0.5561 0.0786  -0.0437 0.0068  90  THR A CB  
694  O  OG1 . THR A 95  ? 0.5349 0.5116 0.5745 0.0888  -0.0433 0.0027  90  THR A OG1 
695  C  CG2 . THR A 95  ? 0.5450 0.4724 0.5633 0.0877  -0.0423 0.0134  90  THR A CG2 
696  N  N   . GLU A 96  ? 0.4683 0.4100 0.4936 0.0510  -0.0478 0.0100  91  GLU A N   
697  C  CA  . GLU A 96  ? 0.5234 0.4506 0.5430 0.0433  -0.0486 0.0130  91  GLU A CA  
698  C  C   . GLU A 96  ? 0.4960 0.4352 0.5170 0.0409  -0.0524 0.0154  91  GLU A C   
699  O  O   . GLU A 96  ? 0.4765 0.4058 0.4923 0.0405  -0.0532 0.0197  91  GLU A O   
700  C  CB  . GLU A 96  ? 0.5074 0.4285 0.5263 0.0327  -0.0472 0.0088  91  GLU A CB  
701  C  CG  . GLU A 96  ? 0.5899 0.4949 0.6048 0.0336  -0.0435 0.0068  91  GLU A CG  
702  C  CD  . GLU A 96  ? 0.6030 0.5018 0.6154 0.0243  -0.0431 0.0029  91  GLU A CD  
703  O  OE1 . GLU A 96  ? 0.5481 0.4491 0.5599 0.0179  -0.0458 0.0031  91  GLU A OE1 
704  O  OE2 . GLU A 96  ? 0.6459 0.5369 0.6557 0.0244  -0.0402 -0.0005 91  GLU A OE2 
705  N  N   . LEU A 97  ? 0.4801 0.4403 0.5075 0.0379  -0.0540 0.0118  92  LEU A N   
706  C  CA  . LEU A 97  ? 0.4688 0.4411 0.4968 0.0344  -0.0571 0.0129  92  LEU A CA  
707  C  C   . LEU A 97  ? 0.5034 0.4805 0.5295 0.0450  -0.0602 0.0177  92  LEU A C   
708  O  O   . LEU A 97  ? 0.5153 0.4875 0.5362 0.0438  -0.0620 0.0217  92  LEU A O   
709  C  CB  . LEU A 97  ? 0.4599 0.4534 0.4939 0.0279  -0.0567 0.0066  92  LEU A CB  
710  C  CG  . LEU A 97  ? 0.4757 0.4839 0.5102 0.0217  -0.0588 0.0053  92  LEU A CG  
711  C  CD1 . LEU A 97  ? 0.4786 0.4948 0.5141 0.0100  -0.0553 -0.0017 92  LEU A CD1 
712  C  CD2 . LEU A 97  ? 0.4912 0.5218 0.5307 0.0302  -0.0628 0.0056  92  LEU A CD2 
713  N  N   . GLN A 98  ? 0.4902 0.4769 0.5194 0.0566  -0.0607 0.0174  93  GLN A N   
714  C  CA  . GLN A 98  ? 0.5118 0.5012 0.5364 0.0699  -0.0640 0.0227  93  GLN A CA  
715  C  C   . GLN A 98  ? 0.5476 0.5066 0.5589 0.0728  -0.0620 0.0298  93  GLN A C   
716  O  O   . GLN A 98  ? 0.5348 0.4903 0.5381 0.0775  -0.0644 0.0351  93  GLN A O   
717  C  CB  . GLN A 98  ? 0.5256 0.5285 0.5553 0.0838  -0.0644 0.0206  93  GLN A CB  
718  C  CG  . GLN A 98  ? 0.5272 0.5641 0.5711 0.0797  -0.0655 0.0121  93  GLN A CG  
719  C  CD  . GLN A 98  ? 0.5312 0.5834 0.5818 0.0937  -0.0651 0.0090  93  GLN A CD  
720  O  OE1 . GLN A 98  ? 0.5227 0.5561 0.5697 0.0993  -0.0610 0.0100  93  GLN A OE1 
721  N  NE2 . GLN A 98  ? 0.5430 0.6304 0.6036 0.0994  -0.0692 0.0046  93  GLN A NE2 
722  N  N   . GLY A 99  ? 0.5475 0.4844 0.5554 0.0689  -0.0572 0.0294  94  GLY A N   
723  C  CA  . GLY A 99  ? 0.5531 0.4616 0.5484 0.0688  -0.0538 0.0345  94  GLY A CA  
724  C  C   . GLY A 99  ? 0.5395 0.4450 0.5324 0.0585  -0.0546 0.0361  94  GLY A C   
725  O  O   . GLY A 99  ? 0.5486 0.4392 0.5306 0.0605  -0.0533 0.0413  94  GLY A O   
726  N  N   . VAL A 100 ? 0.5164 0.4345 0.5180 0.0476  -0.0560 0.0316  95  VAL A N   
727  C  CA  . VAL A 100 ? 0.5253 0.4420 0.5252 0.0389  -0.0566 0.0325  95  VAL A CA  
728  C  C   . VAL A 100 ? 0.5204 0.4488 0.5173 0.0431  -0.0603 0.0358  95  VAL A C   
729  O  O   . VAL A 100 ? 0.5395 0.4586 0.5287 0.0416  -0.0596 0.0396  95  VAL A O   
730  C  CB  . VAL A 100 ? 0.5167 0.4412 0.5238 0.0285  -0.0569 0.0271  95  VAL A CB  
731  C  CG1 . VAL A 100 ? 0.5329 0.4588 0.5384 0.0216  -0.0577 0.0277  95  VAL A CG1 
732  C  CG2 . VAL A 100 ? 0.5469 0.4586 0.5545 0.0247  -0.0539 0.0242  95  VAL A CG2 
733  N  N   . CYS A 101 ? 0.4928 0.4430 0.4955 0.0479  -0.0640 0.0337  96  CYS A N   
734  C  CA  . CYS A 101 ? 0.5254 0.4901 0.5253 0.0523  -0.0683 0.0360  96  CYS A CA  
735  C  C   . CYS A 101 ? 0.5218 0.4726 0.5090 0.0648  -0.0687 0.0433  96  CYS A C   
736  O  O   . CYS A 101 ? 0.5255 0.4748 0.5040 0.0660  -0.0704 0.0474  96  CYS A O   
737  C  CB  . CYS A 101 ? 0.5107 0.5051 0.5204 0.0549  -0.0720 0.0308  96  CYS A CB  
738  S  SG  . CYS A 101 ? 0.4933 0.5023 0.5128 0.0391  -0.0704 0.0221  96  CYS A SG  
739  N  N   . ASP A 102 ? 0.5383 0.4767 0.5222 0.0744  -0.0664 0.0452  97  ASP A N   
740  C  CA  . ASP A 102 ? 0.5634 0.4821 0.5311 0.0873  -0.0654 0.0526  97  ASP A CA  
741  C  C   . ASP A 102 ? 0.5733 0.4641 0.5284 0.0793  -0.0601 0.0567  97  ASP A C   
742  O  O   . ASP A 102 ? 0.6095 0.4877 0.5491 0.0851  -0.0599 0.0630  97  ASP A O   
743  C  CB  . ASP A 102 ? 0.5903 0.4978 0.5560 0.0982  -0.0625 0.0529  97  ASP A CB  
744  C  CG  . ASP A 102 ? 0.6381 0.5726 0.6114 0.1125  -0.0680 0.0510  97  ASP A CG  
745  O  OD1 . ASP A 102 ? 0.6540 0.6147 0.6318 0.1148  -0.0743 0.0502  97  ASP A OD1 
746  O  OD2 . ASP A 102 ? 0.6649 0.5966 0.6407 0.1207  -0.0657 0.0492  97  ASP A OD2 
747  N  N   . THR A 103 ? 0.5719 0.4540 0.5328 0.0660  -0.0557 0.0526  98  THR A N   
748  C  CA  . THR A 103 ? 0.5991 0.4602 0.5514 0.0565  -0.0503 0.0543  98  THR A CA  
749  C  C   . THR A 103 ? 0.5576 0.4279 0.5081 0.0514  -0.0527 0.0557  98  THR A C   
750  O  O   . THR A 103 ? 0.5815 0.4352 0.5180 0.0511  -0.0494 0.0604  98  THR A O   
751  C  CB  . THR A 103 ? 0.6024 0.4605 0.5644 0.0441  -0.0468 0.0481  98  THR A CB  
752  O  OG1 . THR A 103 ? 0.6211 0.4669 0.5818 0.0480  -0.0435 0.0467  98  THR A OG1 
753  C  CG2 . THR A 103 ? 0.5783 0.4222 0.5349 0.0331  -0.0416 0.0479  98  THR A CG2 
754  N  N   . VAL A 104 ? 0.5458 0.4407 0.5088 0.0468  -0.0575 0.0515  99  VAL A N   
755  C  CA  . VAL A 104 ? 0.5203 0.4237 0.4814 0.0412  -0.0593 0.0519  99  VAL A CA  
756  C  C   . VAL A 104 ? 0.5546 0.4603 0.5033 0.0516  -0.0629 0.0576  99  VAL A C   
757  O  O   . VAL A 104 ? 0.5298 0.4255 0.4667 0.0498  -0.0611 0.0615  99  VAL A O   
758  C  CB  . VAL A 104 ? 0.5002 0.4262 0.4748 0.0340  -0.0626 0.0455  99  VAL A CB  
759  C  CG1 . VAL A 104 ? 0.5223 0.4591 0.4934 0.0302  -0.0650 0.0456  99  VAL A CG1 
760  C  CG2 . VAL A 104 ? 0.4998 0.4197 0.4818 0.0242  -0.0592 0.0410  99  VAL A CG2 
761  N  N   . LEU A 105 ? 0.5379 0.4581 0.4889 0.0633  -0.0679 0.0580  100 LEU A N   
762  C  CA  . LEU A 105 ? 0.5763 0.5023 0.5154 0.0758  -0.0727 0.0633  100 LEU A CA  
763  C  C   . LEU A 105 ? 0.5943 0.4881 0.5117 0.0840  -0.0682 0.0717  100 LEU A C   
764  O  O   . LEU A 105 ? 0.6222 0.5111 0.5239 0.0894  -0.0700 0.0771  100 LEU A O   
765  C  CB  . LEU A 105 ? 0.5840 0.5347 0.5319 0.0879  -0.0788 0.0608  100 LEU A CB  
766  C  CG  . LEU A 105 ? 0.5604 0.5444 0.5261 0.0786  -0.0827 0.0522  100 LEU A CG  
767  C  CD1 . LEU A 105 ? 0.5558 0.5635 0.5337 0.0872  -0.0862 0.0476  100 LEU A CD1 
768  C  CD2 . LEU A 105 ? 0.5667 0.5675 0.5277 0.0763  -0.0875 0.0520  100 LEU A CD2 
769  N  N   . GLY A 106 ? 0.5958 0.4657 0.5100 0.0841  -0.0619 0.0725  101 GLY A N   
770  C  CA  . GLY A 106 ? 0.6666 0.5009 0.5579 0.0888  -0.0552 0.0796  101 GLY A CA  
771  C  C   . GLY A 106 ? 0.6761 0.4955 0.5586 0.0755  -0.0496 0.0807  101 GLY A C   
772  O  O   . GLY A 106 ? 0.7037 0.5027 0.5641 0.0802  -0.0469 0.0875  101 GLY A O   
773  N  N   . LEU A 107 ? 0.6124 0.4417 0.5108 0.0596  -0.0477 0.0740  102 LEU A N   
774  C  CA  . LEU A 107 ? 0.6511 0.4712 0.5440 0.0472  -0.0424 0.0738  102 LEU A CA  
775  C  C   . LEU A 107 ? 0.6336 0.4656 0.5193 0.0497  -0.0472 0.0768  102 LEU A C   
776  O  O   . LEU A 107 ? 0.6652 0.4806 0.5343 0.0467  -0.0425 0.0807  102 LEU A O   
777  C  CB  . LEU A 107 ? 0.5972 0.4299 0.5099 0.0326  -0.0408 0.0655  102 LEU A CB  
778  C  CG  . LEU A 107 ? 0.6321 0.4541 0.5519 0.0256  -0.0352 0.0609  102 LEU A CG  
779  C  CD1 . LEU A 107 ? 0.5923 0.4346 0.5323 0.0160  -0.0373 0.0532  102 LEU A CD1 
780  C  CD2 . LEU A 107 ? 0.6582 0.4529 0.5633 0.0180  -0.0250 0.0622  102 LEU A CD2 
781  N  N   . LEU A 108 ? 0.6115 0.4725 0.5089 0.0538  -0.0558 0.0742  103 LEU A N   
782  C  CA  . LEU A 108 ? 0.6063 0.4809 0.4966 0.0560  -0.0609 0.0760  103 LEU A CA  
783  C  C   . LEU A 108 ? 0.6517 0.5102 0.5176 0.0701  -0.0619 0.0849  103 LEU A C   
784  O  O   . LEU A 108 ? 0.6605 0.5092 0.5099 0.0684  -0.0601 0.0888  103 LEU A O   
785  C  CB  . LEU A 108 ? 0.5895 0.4984 0.4960 0.0577  -0.0694 0.0705  103 LEU A CB  
786  C  CG  . LEU A 108 ? 0.5603 0.4823 0.4855 0.0434  -0.0680 0.0623  103 LEU A CG  
787  C  CD1 . LEU A 108 ? 0.5535 0.5044 0.4932 0.0445  -0.0742 0.0564  103 LEU A CD1 
788  C  CD2 . LEU A 108 ? 0.5548 0.4760 0.4757 0.0329  -0.0655 0.0610  103 LEU A CD2 
789  N  N   . ASP A 109 ? 0.6535 0.5078 0.5149 0.0851  -0.0645 0.0884  104 ASP A N   
790  C  CA  . ASP A 109 ? 0.6787 0.5171 0.5147 0.1022  -0.0663 0.0975  104 ASP A CA  
791  C  C   . ASP A 109 ? 0.7356 0.5303 0.5464 0.0997  -0.0555 0.1041  104 ASP A C   
792  O  O   . ASP A 109 ? 0.7581 0.5362 0.5436 0.1062  -0.0548 0.1113  104 ASP A O   
793  C  CB  . ASP A 109 ? 0.7199 0.5667 0.5591 0.1203  -0.0716 0.0986  104 ASP A CB  
794  C  CG  . ASP A 109 ? 0.8201 0.6601 0.6350 0.1421  -0.0768 0.1074  104 ASP A CG  
795  O  OD1 . ASP A 109 ? 0.8494 0.6508 0.6395 0.1511  -0.0703 0.1152  104 ASP A OD1 
796  O  OD2 . ASP A 109 ? 0.8439 0.7157 0.6624 0.1503  -0.0870 0.1063  104 ASP A OD2 
797  N  N   . SER A 110 ? 0.7314 0.5066 0.5472 0.0896  -0.0465 0.1012  105 SER A N   
798  C  CA  . SER A 110 ? 0.7482 0.4810 0.5398 0.0857  -0.0347 0.1060  105 SER A CA  
799  C  C   . SER A 110 ? 0.7541 0.4799 0.5413 0.0685  -0.0279 0.1043  105 SER A C   
800  O  O   . SER A 110 ? 0.7566 0.4502 0.5170 0.0674  -0.0195 0.1101  105 SER A O   
801  C  CB  . SER A 110 ? 0.8132 0.5298 0.6119 0.0803  -0.0274 0.1021  105 SER A CB  
802  O  OG  . SER A 110 ? 0.8590 0.5706 0.6531 0.0980  -0.0308 0.1054  105 SER A OG  
803  N  N   . HIS A 111 ? 0.6999 0.4538 0.5111 0.0557  -0.0306 0.0966  106 HIS A N   
804  C  CA  . HIS A 111 ? 0.7177 0.4650 0.5285 0.0385  -0.0224 0.0932  106 HIS A CA  
805  C  C   . HIS A 111 ? 0.7102 0.4823 0.5286 0.0336  -0.0276 0.0906  106 HIS A C   
806  O  O   . HIS A 111 ? 0.7441 0.5055 0.5498 0.0258  -0.0216 0.0917  106 HIS A O   
807  C  CB  . HIS A 111 ? 0.7042 0.4556 0.5364 0.0247  -0.0171 0.0845  106 HIS A CB  
808  C  CG  . HIS A 111 ? 0.7356 0.4569 0.5566 0.0231  -0.0079 0.0854  106 HIS A CG  
809  N  ND1 . HIS A 111 ? 0.7722 0.4624 0.5724 0.0142  0.0044  0.0871  106 HIS A ND1 
810  C  CD2 . HIS A 111 ? 0.7657 0.4814 0.5915 0.0285  -0.0083 0.0844  106 HIS A CD2 
811  C  CE1 . HIS A 111 ? 0.7505 0.4167 0.5430 0.0134  0.0114  0.0868  106 HIS A CE1 
812  N  NE2 . HIS A 111 ? 0.8095 0.4905 0.6173 0.0225  0.0037  0.0853  106 HIS A NE2 
813  N  N   . LEU A 112 ? 0.6487 0.4524 0.4862 0.0370  -0.0375 0.0867  107 LEU A N   
814  C  CA  . LEU A 112 ? 0.6583 0.4845 0.5074 0.0279  -0.0401 0.0813  107 LEU A CA  
815  C  C   . LEU A 112 ? 0.6666 0.5065 0.5051 0.0351  -0.0477 0.0845  107 LEU A C   
816  O  O   . LEU A 112 ? 0.6585 0.5024 0.4929 0.0274  -0.0460 0.0828  107 LEU A O   
817  C  CB  . LEU A 112 ? 0.6300 0.4801 0.5062 0.0231  -0.0441 0.0733  107 LEU A CB  
818  C  CG  . LEU A 112 ? 0.6222 0.4630 0.5099 0.0144  -0.0373 0.0688  107 LEU A CG  
819  C  CD1 . LEU A 112 ? 0.5758 0.4371 0.4861 0.0129  -0.0421 0.0623  107 LEU A CD1 
820  C  CD2 . LEU A 112 ? 0.6384 0.4724 0.5251 0.0017  -0.0291 0.0656  107 LEU A CD2 
821  N  N   . ILE A 113 ? 0.6546 0.5045 0.4895 0.0497  -0.0561 0.0879  108 ILE A N   
822  C  CA  . ILE A 113 ? 0.6679 0.5367 0.4946 0.0567  -0.0646 0.0895  108 ILE A CA  
823  C  C   . ILE A 113 ? 0.7169 0.5604 0.5122 0.0634  -0.0617 0.0985  108 ILE A C   
824  O  O   . ILE A 113 ? 0.7360 0.5558 0.5138 0.0752  -0.0598 0.1059  108 ILE A O   
825  C  CB  . ILE A 113 ? 0.6533 0.5469 0.4892 0.0703  -0.0749 0.0886  108 ILE A CB  
826  C  CG1 . ILE A 113 ? 0.6485 0.5682 0.5128 0.0610  -0.0772 0.0789  108 ILE A CG1 
827  C  CG2 . ILE A 113 ? 0.6918 0.6041 0.5154 0.0799  -0.0840 0.0908  108 ILE A CG2 
828  C  CD1 . ILE A 113 ? 0.6199 0.5640 0.4967 0.0720  -0.0852 0.0764  108 ILE A CD1 
829  N  N   . LYS A 114 ? 0.7189 0.5645 0.5049 0.0558  -0.0605 0.0979  109 LYS A N   
830  C  CA  . LYS A 114 ? 0.8043 0.6244 0.5584 0.0600  -0.0566 0.1061  109 LYS A CA  
831  C  C   . LYS A 114 ? 0.8256 0.6665 0.5706 0.0628  -0.0647 0.1059  109 LYS A C   
832  O  O   . LYS A 114 ? 0.7712 0.6431 0.5352 0.0561  -0.0702 0.0979  109 LYS A O   
833  C  CB  . LYS A 114 ? 0.8217 0.6157 0.5691 0.0443  -0.0428 0.1054  109 LYS A CB  
834  C  CG  . LYS A 114 ? 0.8112 0.5902 0.5716 0.0369  -0.0341 0.1025  109 LYS A CG  
835  C  CD  . LYS A 114 ? 0.9007 0.6504 0.6424 0.0486  -0.0312 0.1104  109 LYS A CD  
836  C  CE  . LYS A 114 ? 0.9310 0.6490 0.6655 0.0360  -0.0163 0.1097  109 LYS A CE  
837  N  NZ  . LYS A 114 ? 0.9936 0.7041 0.7185 0.0219  -0.0078 0.1080  109 LYS A NZ  
838  N  N   . GLU A 115 ? 0.8788 0.7001 0.5918 0.0723  -0.0647 0.1147  110 GLU A N   
839  C  CA  . GLU A 115 ? 0.9059 0.7438 0.6060 0.0738  -0.0714 0.1147  110 GLU A CA  
840  C  C   . GLU A 115 ? 0.8872 0.7225 0.5890 0.0544  -0.0631 0.1092  110 GLU A C   
841  O  O   . GLU A 115 ? 0.9124 0.7730 0.6203 0.0486  -0.0683 0.1032  110 GLU A O   
842  C  CB  . GLU A 115 ? 0.9858 0.8007 0.6479 0.0908  -0.0736 0.1263  110 GLU A CB  
843  C  CG  . GLU A 115 ? 1.0528 0.8733 0.7106 0.1138  -0.0833 0.1318  110 GLU A CG  
844  C  CD  . GLU A 115 ? 1.1192 0.9842 0.7849 0.1244  -0.0991 0.1279  110 GLU A CD  
845  O  OE1 . GLU A 115 ? 1.0969 0.9974 0.7920 0.1126  -0.1031 0.1170  110 GLU A OE1 
846  O  OE2 . GLU A 115 ? 1.1599 1.0242 0.8011 0.1445  -0.1073 0.1355  110 GLU A OE2 
847  N  N   . ALA A 116 ? 0.9084 0.7143 0.6052 0.0439  -0.0498 0.1103  111 ALA A N   
848  C  CA  . ALA A 116 ? 0.8816 0.6843 0.5801 0.0265  -0.0407 0.1049  111 ALA A CA  
849  C  C   . ALA A 116 ? 0.8743 0.6979 0.6077 0.0141  -0.0391 0.0942  111 ALA A C   
850  O  O   . ALA A 116 ? 0.8312 0.6722 0.5860 0.0181  -0.0454 0.0909  111 ALA A O   
851  C  CB  . ALA A 116 ? 0.9661 0.7302 0.6429 0.0204  -0.0265 0.1100  111 ALA A CB  
852  N  N   . GLY A 117 ? 0.8766 0.6978 0.6147 -0.0004 -0.0302 0.0885  112 GLY A N   
853  C  CA  . GLY A 117 ? 0.8614 0.7000 0.6285 -0.0107 -0.0283 0.0787  112 GLY A CA  
854  C  C   . GLY A 117 ? 0.8199 0.6821 0.5927 -0.0149 -0.0337 0.0722  112 GLY A C   
855  O  O   . GLY A 117 ? 0.7870 0.6592 0.5465 -0.0092 -0.0415 0.0744  112 GLY A O   
856  N  N   . ASP A 118 ? 0.7860 0.6568 0.5778 -0.0250 -0.0291 0.0638  113 ASP A N   
857  C  CA  . ASP A 118 ? 0.7823 0.6716 0.5787 -0.0301 -0.0325 0.0568  113 ASP A CA  
858  C  C   . ASP A 118 ? 0.7268 0.6378 0.5357 -0.0250 -0.0432 0.0544  113 ASP A C   
859  O  O   . ASP A 118 ? 0.6948 0.6073 0.5121 -0.0174 -0.0475 0.0574  113 ASP A O   
860  C  CB  . ASP A 118 ? 0.7780 0.6674 0.5886 -0.0404 -0.0240 0.0487  113 ASP A CB  
861  C  CG  . ASP A 118 ? 0.7844 0.6759 0.6183 -0.0402 -0.0228 0.0458  113 ASP A CG  
862  O  OD1 . ASP A 118 ? 0.7977 0.6886 0.6427 -0.0461 -0.0159 0.0399  113 ASP A OD1 
863  O  OD2 . ASP A 118 ? 0.7567 0.6510 0.5974 -0.0334 -0.0287 0.0489  113 ASP A OD2 
864  N  N   . ALA A 119 ? 0.7283 0.6558 0.5375 -0.0301 -0.0466 0.0480  114 ALA A N   
865  C  CA  . ALA A 119 ? 0.7156 0.6659 0.5352 -0.0277 -0.0557 0.0440  114 ALA A CA  
866  C  C   . ALA A 119 ? 0.6653 0.6180 0.5073 -0.0289 -0.0546 0.0403  114 ALA A C   
867  O  O   . ALA A 119 ? 0.6480 0.6132 0.4993 -0.0232 -0.0612 0.0406  114 ALA A O   
868  C  CB  . ALA A 119 ? 0.7411 0.7063 0.5559 -0.0365 -0.0571 0.0361  114 ALA A CB  
869  N  N   . GLU A 120 ? 0.6404 0.5825 0.4909 -0.0358 -0.0465 0.0364  115 GLU A N   
870  C  CA  . GLU A 120 ? 0.6675 0.6101 0.5369 -0.0362 -0.0453 0.0332  115 GLU A CA  
871  C  C   . GLU A 120 ? 0.6312 0.5708 0.5074 -0.0276 -0.0485 0.0391  115 GLU A C   
872  O  O   . GLU A 120 ? 0.6016 0.5507 0.4893 -0.0249 -0.0529 0.0375  115 GLU A O   
873  C  CB  . GLU A 120 ? 0.6763 0.6069 0.5511 -0.0416 -0.0363 0.0297  115 GLU A CB  
874  C  CG  . GLU A 120 ? 0.7275 0.6586 0.5951 -0.0493 -0.0322 0.0235  115 GLU A CG  
875  C  CD  . GLU A 120 ? 0.6695 0.5965 0.5478 -0.0522 -0.0273 0.0173  115 GLU A CD  
876  O  OE1 . GLU A 120 ? 0.6937 0.6242 0.5707 -0.0567 -0.0274 0.0115  115 GLU A OE1 
877  O  OE2 . GLU A 120 ? 0.6829 0.6027 0.5695 -0.0500 -0.0226 0.0180  115 GLU A OE2 
878  N  N   . SER A 121 ? 0.6479 0.5722 0.5157 -0.0242 -0.0450 0.0454  116 SER A N   
879  C  CA  . SER A 121 ? 0.6387 0.5556 0.5106 -0.0168 -0.0462 0.0506  116 SER A CA  
880  C  C   . SER A 121 ? 0.6149 0.5429 0.4827 -0.0069 -0.0554 0.0543  116 SER A C   
881  O  O   . SER A 121 ? 0.5914 0.5255 0.4709 -0.0020 -0.0590 0.0540  116 SER A O   
882  C  CB  . SER A 121 ? 0.6680 0.5632 0.5280 -0.0169 -0.0389 0.0559  116 SER A CB  
883  O  OG  . SER A 121 ? 0.7337 0.6224 0.5715 -0.0133 -0.0400 0.0616  116 SER A OG  
884  N  N   . ARG A 122 ? 0.6179 0.5505 0.4691 -0.0032 -0.0595 0.0573  117 ARG A N   
885  C  CA  . ARG A 122 ? 0.6271 0.5734 0.4744 0.0084  -0.0689 0.0606  117 ARG A CA  
886  C  C   . ARG A 122 ? 0.5911 0.5640 0.4561 0.0063  -0.0748 0.0530  117 ARG A C   
887  O  O   . ARG A 122 ? 0.5859 0.5685 0.4593 0.0147  -0.0799 0.0538  117 ARG A O   
888  C  CB  . ARG A 122 ? 0.6616 0.6105 0.4868 0.0130  -0.0730 0.0645  117 ARG A CB  
889  C  CG  . ARG A 122 ? 0.7140 0.6341 0.5171 0.0192  -0.0681 0.0741  117 ARG A CG  
890  C  CD  . ARG A 122 ? 0.7420 0.6637 0.5201 0.0252  -0.0728 0.0786  117 ARG A CD  
891  N  NE  . ARG A 122 ? 0.7786 0.6974 0.5493 0.0126  -0.0672 0.0748  117 ARG A NE  
892  C  CZ  . ARG A 122 ? 0.7972 0.7373 0.5664 0.0076  -0.0720 0.0688  117 ARG A CZ  
893  N  NH1 . ARG A 122 ? 0.7756 0.7443 0.5505 0.0133  -0.0828 0.0655  117 ARG A NH1 
894  N  NH2 . ARG A 122 ? 0.7989 0.7325 0.5607 -0.0039 -0.0652 0.0652  117 ARG A NH2 
895  N  N   . VAL A 123 ? 0.5747 0.5582 0.4445 -0.0052 -0.0733 0.0450  118 VAL A N   
896  C  CA  . VAL A 123 ? 0.5640 0.5696 0.4481 -0.0098 -0.0769 0.0370  118 VAL A CA  
897  C  C   . VAL A 123 ? 0.5422 0.5412 0.4427 -0.0102 -0.0738 0.0357  118 VAL A C   
898  O  O   . VAL A 123 ? 0.5165 0.5305 0.4280 -0.0074 -0.0779 0.0330  118 VAL A O   
899  C  CB  . VAL A 123 ? 0.5479 0.5602 0.4298 -0.0232 -0.0739 0.0286  118 VAL A CB  
900  C  CG1 . VAL A 123 ? 0.5582 0.5879 0.4530 -0.0301 -0.0752 0.0198  118 VAL A CG1 
901  C  CG2 . VAL A 123 ? 0.5798 0.6032 0.4452 -0.0233 -0.0782 0.0284  118 VAL A CG2 
902  N  N   . PHE A 124 ? 0.5417 0.5199 0.4442 -0.0138 -0.0665 0.0371  119 PHE A N   
903  C  CA  . PHE A 124 ? 0.5357 0.5088 0.4528 -0.0144 -0.0641 0.0353  119 PHE A CA  
904  C  C   . PHE A 124 ? 0.5372 0.5105 0.4588 -0.0040 -0.0678 0.0401  119 PHE A C   
905  O  O   . PHE A 124 ? 0.5157 0.4971 0.4492 -0.0033 -0.0695 0.0371  119 PHE A O   
906  C  CB  . PHE A 124 ? 0.5324 0.4868 0.4514 -0.0187 -0.0565 0.0354  119 PHE A CB  
907  C  CG  . PHE A 124 ? 0.5409 0.4898 0.4726 -0.0169 -0.0551 0.0349  119 PHE A CG  
908  C  CD1 . PHE A 124 ? 0.5230 0.4767 0.4639 -0.0208 -0.0549 0.0292  119 PHE A CD1 
909  C  CD2 . PHE A 124 ? 0.5374 0.4750 0.4697 -0.0115 -0.0538 0.0399  119 PHE A CD2 
910  C  CE1 . PHE A 124 ? 0.5288 0.4777 0.4798 -0.0188 -0.0541 0.0288  119 PHE A CE1 
911  C  CE2 . PHE A 124 ? 0.5247 0.4585 0.4682 -0.0105 -0.0529 0.0388  119 PHE A CE2 
912  C  CZ  . PHE A 124 ? 0.5038 0.4442 0.4570 -0.0137 -0.0535 0.0333  119 PHE A CZ  
913  N  N   . TYR A 125 ? 0.5232 0.4849 0.4336 0.0040  -0.0681 0.0476  120 TYR A N   
914  C  CA  . TYR A 125 ? 0.5531 0.5102 0.4654 0.0146  -0.0703 0.0524  120 TYR A CA  
915  C  C   . TYR A 125 ? 0.5308 0.5111 0.4461 0.0230  -0.0786 0.0513  120 TYR A C   
916  O  O   . TYR A 125 ? 0.5273 0.5125 0.4523 0.0287  -0.0805 0.0509  120 TYR A O   
917  C  CB  . TYR A 125 ? 0.5470 0.4808 0.4426 0.0207  -0.0669 0.0607  120 TYR A CB  
918  C  CG  . TYR A 125 ? 0.5532 0.4666 0.4492 0.0121  -0.0578 0.0604  120 TYR A CG  
919  C  CD1 . TYR A 125 ? 0.5610 0.4711 0.4719 0.0078  -0.0545 0.0567  120 TYR A CD1 
920  C  CD2 . TYR A 125 ? 0.6031 0.5024 0.4844 0.0081  -0.0525 0.0632  120 TYR A CD2 
921  C  CE1 . TYR A 125 ? 0.5496 0.4462 0.4625 0.0002  -0.0468 0.0551  120 TYR A CE1 
922  C  CE2 . TYR A 125 ? 0.5964 0.4812 0.4798 -0.0003 -0.0438 0.0615  120 TYR A CE2 
923  C  CZ  . TYR A 125 ? 0.5639 0.4490 0.4639 -0.0041 -0.0413 0.0572  120 TYR A CZ  
924  O  OH  . TYR A 125 ? 0.5932 0.4688 0.4966 -0.0123 -0.0332 0.0543  120 TYR A OH  
925  N  N   . LEU A 126 ? 0.5359 0.5328 0.4435 0.0237  -0.0836 0.0502  121 LEU A N   
926  C  CA  . LEU A 126 ? 0.5079 0.5330 0.4203 0.0313  -0.0920 0.0475  121 LEU A CA  
927  C  C   . LEU A 126 ? 0.5089 0.5532 0.4395 0.0218  -0.0918 0.0378  121 LEU A C   
928  O  O   . LEU A 126 ? 0.5099 0.5722 0.4509 0.0278  -0.0958 0.0353  121 LEU A O   
929  C  CB  . LEU A 126 ? 0.5332 0.5740 0.4325 0.0336  -0.0978 0.0475  121 LEU A CB  
930  C  CG  . LEU A 126 ? 0.5884 0.6121 0.4664 0.0472  -0.0996 0.0580  121 LEU A CG  
931  C  CD1 . LEU A 126 ? 0.5820 0.6169 0.4445 0.0462  -0.1040 0.0578  121 LEU A CD1 
932  C  CD2 . LEU A 126 ? 0.6397 0.6691 0.5174 0.0654  -0.1055 0.0627  121 LEU A CD2 
933  N  N   . LYS A 127 ? 0.4990 0.5386 0.4323 0.0074  -0.0865 0.0323  122 LYS A N   
934  C  CA  . LYS A 127 ? 0.4958 0.5438 0.4425 -0.0022 -0.0839 0.0242  122 LYS A CA  
935  C  C   . LYS A 127 ? 0.4996 0.5368 0.4561 0.0025  -0.0818 0.0264  122 LYS A C   
936  O  O   . LYS A 127 ? 0.4785 0.5300 0.4456 0.0021  -0.0830 0.0216  122 LYS A O   
937  C  CB  . LYS A 127 ? 0.4757 0.5113 0.4192 -0.0158 -0.0773 0.0198  122 LYS A CB  
938  C  CG  . LYS A 127 ? 0.4741 0.5099 0.4266 -0.0253 -0.0730 0.0125  122 LYS A CG  
939  C  CD  . LYS A 127 ? 0.4759 0.4924 0.4225 -0.0345 -0.0660 0.0102  122 LYS A CD  
940  C  CE  . LYS A 127 ? 0.4788 0.4882 0.4305 -0.0413 -0.0612 0.0049  122 LYS A CE  
941  N  NZ  . LYS A 127 ? 0.4807 0.4815 0.4414 -0.0340 -0.0614 0.0089  122 LYS A NZ  
942  N  N   . MET A 128 ? 0.4929 0.5052 0.4459 0.0056  -0.0778 0.0325  123 MET A N   
943  C  CA  . MET A 128 ? 0.4678 0.4696 0.4290 0.0095  -0.0758 0.0340  123 MET A CA  
944  C  C   . MET A 128 ? 0.4878 0.5016 0.4523 0.0216  -0.0808 0.0361  123 MET A C   
945  O  O   . MET A 128 ? 0.4662 0.4857 0.4411 0.0226  -0.0807 0.0331  123 MET A O   
946  C  CB  . MET A 128 ? 0.4945 0.4707 0.4504 0.0108  -0.0711 0.0396  123 MET A CB  
947  C  CG  . MET A 128 ? 0.5221 0.4873 0.4872 0.0084  -0.0673 0.0380  123 MET A CG  
948  S  SD  . MET A 128 ? 0.5739 0.5141 0.5336 0.0078  -0.0614 0.0424  123 MET A SD  
949  C  CE  . MET A 128 ? 0.4952 0.4303 0.4673 0.0054  -0.0591 0.0386  123 MET A CE  
950  N  N   . LYS A 129 ? 0.4915 0.5083 0.4457 0.0319  -0.0851 0.0414  124 LYS A N   
951  C  CA  . LYS A 129 ? 0.5157 0.5441 0.4717 0.0462  -0.0902 0.0436  124 LYS A CA  
952  C  C   . LYS A 129 ? 0.5054 0.5673 0.4751 0.0440  -0.0944 0.0350  124 LYS A C   
953  O  O   . LYS A 129 ? 0.4872 0.5580 0.4668 0.0500  -0.0952 0.0330  124 LYS A O   
954  C  CB  . LYS A 129 ? 0.4950 0.5204 0.4341 0.0589  -0.0946 0.0510  124 LYS A CB  
955  C  CG  . LYS A 129 ? 0.5215 0.5562 0.4592 0.0775  -0.1000 0.0544  124 LYS A CG  
956  C  CD  . LYS A 129 ? 0.5803 0.6037 0.4960 0.0910  -0.1033 0.0633  124 LYS A CD  
957  C  CE  . LYS A 129 ? 0.6095 0.6466 0.5219 0.1124  -0.1104 0.0664  124 LYS A CE  
958  N  NZ  . LYS A 129 ? 0.7000 0.7184 0.5859 0.1266  -0.1127 0.0765  124 LYS A NZ  
959  N  N   . GLY A 130 ? 0.4734 0.5541 0.4437 0.0341  -0.0961 0.0288  125 GLY A N   
960  C  CA  . GLY A 130 ? 0.4849 0.5974 0.4680 0.0282  -0.0982 0.0188  125 GLY A CA  
961  C  C   . GLY A 130 ? 0.4771 0.5833 0.4713 0.0191  -0.0922 0.0138  125 GLY A C   
962  O  O   . GLY A 130 ? 0.4690 0.5946 0.4746 0.0209  -0.0932 0.0086  125 GLY A O   
963  N  N   . ASP A 131 ? 0.4583 0.5379 0.4489 0.0102  -0.0859 0.0153  126 ASP A N   
964  C  CA  . ASP A 131 ? 0.4554 0.5264 0.4532 0.0022  -0.0804 0.0111  126 ASP A CA  
965  C  C   . ASP A 131 ? 0.4680 0.5349 0.4727 0.0122  -0.0806 0.0139  126 ASP A C   
966  O  O   . ASP A 131 ? 0.4495 0.5266 0.4629 0.0091  -0.0789 0.0083  126 ASP A O   
967  C  CB  . ASP A 131 ? 0.4795 0.5231 0.4709 -0.0055 -0.0748 0.0131  126 ASP A CB  
968  C  CG  . ASP A 131 ? 0.4747 0.5195 0.4594 -0.0174 -0.0725 0.0084  126 ASP A CG  
969  O  OD1 . ASP A 131 ? 0.4793 0.5456 0.4650 -0.0238 -0.0737 0.0016  126 ASP A OD1 
970  O  OD2 . ASP A 131 ? 0.4999 0.5244 0.4780 -0.0204 -0.0689 0.0110  126 ASP A OD2 
971  N  N   . TYR A 132 ? 0.4592 0.5090 0.4584 0.0234  -0.0817 0.0222  127 TYR A N   
972  C  CA  . TYR A 132 ? 0.4813 0.5219 0.4851 0.0314  -0.0804 0.0245  127 TYR A CA  
973  C  C   . TYR A 132 ? 0.4852 0.5487 0.4949 0.0434  -0.0849 0.0232  127 TYR A C   
974  O  O   . TYR A 132 ? 0.4849 0.5500 0.5022 0.0467  -0.0833 0.0210  127 TYR A O   
975  C  CB  . TYR A 132 ? 0.4908 0.5021 0.4855 0.0365  -0.0779 0.0324  127 TYR A CB  
976  C  CG  . TYR A 132 ? 0.4818 0.4756 0.4768 0.0252  -0.0729 0.0310  127 TYR A CG  
977  C  CD1 . TYR A 132 ? 0.4911 0.4807 0.4809 0.0171  -0.0716 0.0307  127 TYR A CD1 
978  C  CD2 . TYR A 132 ? 0.4756 0.4593 0.4760 0.0231  -0.0696 0.0292  127 TYR A CD2 
979  C  CE1 . TYR A 132 ? 0.4928 0.4691 0.4833 0.0088  -0.0674 0.0289  127 TYR A CE1 
980  C  CE2 . TYR A 132 ? 0.4826 0.4535 0.4830 0.0145  -0.0661 0.0274  127 TYR A CE2 
981  C  CZ  . TYR A 132 ? 0.4732 0.4408 0.4690 0.0081  -0.0651 0.0274  127 TYR A CZ  
982  O  OH  . TYR A 132 ? 0.4752 0.4319 0.4712 0.0018  -0.0621 0.0254  127 TYR A OH  
983  N  N   . TYR A 133 ? 0.4511 0.5348 0.4580 0.0500  -0.0908 0.0235  128 TYR A N   
984  C  CA  . TYR A 133 ? 0.4776 0.5923 0.4933 0.0602  -0.0957 0.0194  128 TYR A CA  
985  C  C   . TYR A 133 ? 0.4745 0.6149 0.5043 0.0471  -0.0936 0.0080  128 TYR A C   
986  O  O   . TYR A 133 ? 0.5044 0.6621 0.5452 0.0517  -0.0936 0.0032  128 TYR A O   
987  C  CB  . TYR A 133 ? 0.4906 0.6241 0.4994 0.0706  -0.1034 0.0217  128 TYR A CB  
988  C  CG  . TYR A 133 ? 0.5503 0.6652 0.5458 0.0904  -0.1060 0.0323  128 TYR A CG  
989  C  CD1 . TYR A 133 ? 0.5642 0.6773 0.5629 0.1052  -0.1061 0.0342  128 TYR A CD1 
990  C  CD2 . TYR A 133 ? 0.5696 0.6662 0.5473 0.0942  -0.1075 0.0402  128 TYR A CD2 
991  C  CE1 . TYR A 133 ? 0.5947 0.6859 0.5778 0.1237  -0.1073 0.0440  128 TYR A CE1 
992  C  CE2 . TYR A 133 ? 0.6031 0.6780 0.5647 0.1118  -0.1085 0.0502  128 TYR A CE2 
993  C  CZ  . TYR A 133 ? 0.6180 0.6891 0.5817 0.1266  -0.1083 0.0521  128 TYR A CZ  
994  O  OH  . TYR A 133 ? 0.6540 0.6987 0.5984 0.1443  -0.1082 0.0621  128 TYR A OH  
995  N  N   . ARG A 134 ? 0.4623 0.6032 0.4905 0.0303  -0.0908 0.0031  129 ARG A N   
996  C  CA  . ARG A 134 ? 0.4449 0.6037 0.4824 0.0156  -0.0868 -0.0079 129 ARG A CA  
997  C  C   . ARG A 134 ? 0.4538 0.5961 0.4957 0.0128  -0.0807 -0.0087 129 ARG A C   
998  O  O   . ARG A 134 ? 0.4454 0.6068 0.4972 0.0093  -0.0784 -0.0163 129 ARG A O   
999  C  CB  . ARG A 134 ? 0.4630 0.6161 0.4932 -0.0016 -0.0833 -0.0119 129 ARG A CB  
1000 C  CG  . ARG A 134 ? 0.4297 0.5889 0.4638 -0.0190 -0.0763 -0.0223 129 ARG A CG  
1001 C  CD  . ARG A 134 ? 0.4748 0.6376 0.5013 -0.0348 -0.0737 -0.0285 129 ARG A CD  
1002 N  NE  . ARG A 134 ? 0.4671 0.5975 0.4806 -0.0365 -0.0717 -0.0215 129 ARG A NE  
1003 C  CZ  . ARG A 134 ? 0.4607 0.5623 0.4671 -0.0443 -0.0648 -0.0208 129 ARG A CZ  
1004 N  NH1 . ARG A 134 ? 0.4569 0.5539 0.4647 -0.0522 -0.0588 -0.0260 129 ARG A NH1 
1005 N  NH2 . ARG A 134 ? 0.4579 0.5348 0.4544 -0.0435 -0.0638 -0.0148 129 ARG A NH2 
1006 N  N   . TYR A 135 ? 0.4548 0.5633 0.4893 0.0141  -0.0778 -0.0014 130 TYR A N   
1007 C  CA  . TYR A 135 ? 0.4789 0.5719 0.5163 0.0121  -0.0728 -0.0021 130 TYR A CA  
1008 C  C   . TYR A 135 ? 0.4851 0.5890 0.5305 0.0255  -0.0745 -0.0018 130 TYR A C   
1009 O  O   . TYR A 135 ? 0.4642 0.5738 0.5164 0.0222  -0.0708 -0.0072 130 TYR A O   
1010 C  CB  . TYR A 135 ? 0.4687 0.5275 0.4974 0.0114  -0.0703 0.0047  130 TYR A CB  
1011 C  CG  . TYR A 135 ? 0.4588 0.5064 0.4794 0.0004  -0.0683 0.0044  130 TYR A CG  
1012 C  CD1 . TYR A 135 ? 0.4709 0.5298 0.4906 -0.0121 -0.0658 -0.0029 130 TYR A CD1 
1013 C  CD2 . TYR A 135 ? 0.4600 0.4858 0.4733 0.0023  -0.0682 0.0108  130 TYR A CD2 
1014 C  CE1 . TYR A 135 ? 0.4738 0.5199 0.4844 -0.0211 -0.0633 -0.0032 130 TYR A CE1 
1015 C  CE2 . TYR A 135 ? 0.4747 0.4912 0.4810 -0.0064 -0.0662 0.0101  130 TYR A CE2 
1016 C  CZ  . TYR A 135 ? 0.5062 0.5318 0.5107 -0.0173 -0.0638 0.0034  130 TYR A CZ  
1017 O  OH  . TYR A 135 ? 0.4895 0.5033 0.4852 -0.0250 -0.0610 0.0027  130 TYR A OH  
1018 N  N   . LEU A 136 ? 0.4504 0.5563 0.4935 0.0411  -0.0797 0.0044  131 LEU A N   
1019 C  CA  . LEU A 136 ? 0.4844 0.6017 0.5339 0.0561  -0.0814 0.0044  131 LEU A CA  
1020 C  C   . LEU A 136 ? 0.4950 0.6532 0.5580 0.0550  -0.0831 -0.0056 131 LEU A C   
1021 O  O   . LEU A 136 ? 0.5018 0.6717 0.5740 0.0601  -0.0812 -0.0099 131 LEU A O   
1022 C  CB  . LEU A 136 ? 0.5205 0.6296 0.5609 0.0743  -0.0864 0.0134  131 LEU A CB  
1023 C  CG  . LEU A 136 ? 0.5159 0.5848 0.5431 0.0782  -0.0833 0.0226  131 LEU A CG  
1024 C  CD1 . LEU A 136 ? 0.5651 0.6258 0.5802 0.0959  -0.0873 0.0309  131 LEU A CD1 
1025 C  CD2 . LEU A 136 ? 0.5316 0.5841 0.5621 0.0781  -0.0778 0.0215  131 LEU A CD2 
1026 N  N   . ALA A 137 ? 0.4579 0.6396 0.5225 0.0474  -0.0862 -0.0104 132 ALA A N   
1027 C  CA  . ALA A 137 ? 0.4653 0.6901 0.5436 0.0442  -0.0875 -0.0217 132 ALA A CA  
1028 C  C   . ALA A 137 ? 0.4757 0.7033 0.5607 0.0267  -0.0791 -0.0311 132 ALA A C   
1029 O  O   . ALA A 137 ? 0.4722 0.7315 0.5704 0.0258  -0.0778 -0.0406 132 ALA A O   
1030 C  CB  . ALA A 137 ? 0.4641 0.7123 0.5409 0.0383  -0.0925 -0.0253 132 ALA A CB  
1031 N  N   . GLU A 138 ? 0.4561 0.6510 0.5315 0.0135  -0.0730 -0.0288 133 GLU A N   
1032 C  CA  . GLU A 138 ? 0.4687 0.6601 0.5457 -0.0022 -0.0645 -0.0365 133 GLU A CA  
1033 C  C   . GLU A 138 ? 0.4736 0.6665 0.5583 0.0055  -0.0617 -0.0379 133 GLU A C   
1034 O  O   . GLU A 138 ? 0.4769 0.6817 0.5670 -0.0051 -0.0553 -0.0470 133 GLU A O   
1035 C  CB  . GLU A 138 ? 0.4792 0.6321 0.5417 -0.0134 -0.0596 -0.0321 133 GLU A CB  
1036 C  CG  . GLU A 138 ? 0.4926 0.6444 0.5470 -0.0253 -0.0594 -0.0339 133 GLU A CG  
1037 C  CD  . GLU A 138 ? 0.4975 0.6114 0.5374 -0.0326 -0.0553 -0.0289 133 GLU A CD  
1038 O  OE1 . GLU A 138 ? 0.4883 0.5779 0.5248 -0.0266 -0.0545 -0.0228 133 GLU A OE1 
1039 O  OE2 . GLU A 138 ? 0.4917 0.6009 0.5232 -0.0442 -0.0528 -0.0318 133 GLU A OE2 
1040 N  N   . VAL A 139 ? 0.4845 0.6647 0.5686 0.0232  -0.0654 -0.0296 134 VAL A N   
1041 C  CA  . VAL A 139 ? 0.4872 0.6641 0.5765 0.0310  -0.0622 -0.0305 134 VAL A CA  
1042 C  C   . VAL A 139 ? 0.5380 0.7398 0.6370 0.0510  -0.0673 -0.0305 134 VAL A C   
1043 O  O   . VAL A 139 ? 0.5107 0.7082 0.6130 0.0606  -0.0649 -0.0304 134 VAL A O   
1044 C  CB  . VAL A 139 ? 0.5196 0.6544 0.5976 0.0331  -0.0599 -0.0219 134 VAL A CB  
1045 C  CG1 . VAL A 139 ? 0.4916 0.6035 0.5594 0.0163  -0.0559 -0.0216 134 VAL A CG1 
1046 C  CG2 . VAL A 139 ? 0.5057 0.6244 0.5770 0.0485  -0.0653 -0.0117 134 VAL A CG2 
1047 N  N   . ALA A 140 ? 0.5488 0.7766 0.6513 0.0586  -0.0744 -0.0308 135 ALA A N   
1048 C  CA  . ALA A 140 ? 0.6231 0.8736 0.7324 0.0809  -0.0804 -0.0298 135 ALA A CA  
1049 C  C   . ALA A 140 ? 0.6891 0.9869 0.8172 0.0803  -0.0794 -0.0430 135 ALA A C   
1050 O  O   . ALA A 140 ? 0.6851 1.0019 0.8202 0.0607  -0.0748 -0.0534 135 ALA A O   
1051 C  CB  . ALA A 140 ? 0.5921 0.8491 0.6943 0.0917  -0.0893 -0.0236 135 ALA A CB  
1052 N  N   . THR A 141 ? 0.7364 1.0532 0.8717 0.1024  -0.0833 -0.0430 136 THR A N   
1053 C  CA  . THR A 141 ? 0.7815 1.1485 0.9369 0.1050  -0.0830 -0.0562 136 THR A CA  
1054 C  C   . THR A 141 ? 0.8178 1.2207 0.9799 0.1301  -0.0932 -0.0561 136 THR A C   
1055 O  O   . THR A 141 ? 0.8201 1.2672 0.9929 0.1269  -0.0985 -0.0647 136 THR A O   
1056 C  CB  . THR A 141 ? 0.8426 1.2021 1.0039 0.1063  -0.0747 -0.0600 136 THR A CB  
1057 O  OG1 . THR A 141 ? 0.8793 1.2008 1.0282 0.1250  -0.0753 -0.0482 136 THR A OG1 
1058 C  CG2 . THR A 141 ? 0.8018 1.1409 0.9597 0.0796  -0.0645 -0.0645 136 THR A CG2 
1059 N  N   . GLY A 142 ? 0.8354 1.2196 0.9901 0.1555  -0.0959 -0.0469 137 GLY A N   
1060 C  CA  . GLY A 142 ? 0.8245 1.2440 0.9862 0.1829  -0.1043 -0.0481 137 GLY A CA  
1061 C  C   . GLY A 142 ? 0.8555 1.2800 1.0057 0.1975  -0.1156 -0.0403 137 GLY A C   
1062 O  O   . GLY A 142 ? 0.8206 1.2532 0.9687 0.1817  -0.1186 -0.0417 137 GLY A O   
1063 N  N   . ASP A 143 ? 0.8848 1.3037 1.0259 0.2284  -0.1214 -0.0321 138 ASP A N   
1064 C  CA  . ASP A 143 ? 0.9104 1.3264 1.0352 0.2451  -0.1318 -0.0227 138 ASP A CA  
1065 C  C   . ASP A 143 ? 0.8956 1.2620 0.9992 0.2300  -0.1295 -0.0116 138 ASP A C   
1066 O  O   . ASP A 143 ? 0.8914 1.2611 0.9843 0.2319  -0.1368 -0.0070 138 ASP A O   
1067 C  CB  . ASP A 143 ? 0.9196 1.3221 1.0313 0.2811  -0.1359 -0.0134 138 ASP A CB  
1068 C  CG  . ASP A 143 ? 0.8524 1.3156 0.9825 0.3034  -0.1437 -0.0231 138 ASP A CG  
1069 O  OD1 . ASP A 143 ? 0.8409 1.3598 0.9912 0.2918  -0.1486 -0.0360 138 ASP A OD1 
1070 O  OD2 . ASP A 143 ? 0.8005 1.2560 0.9241 0.3327  -0.1447 -0.0184 138 ASP A OD2 
1071 N  N   . ASP A 144 ? 0.8641 1.1857 0.9612 0.2156  -0.1195 -0.0076 139 ASP A N   
1072 C  CA  . ASP A 144 ? 0.8715 1.1501 0.9513 0.1999  -0.1167 0.0012  139 ASP A CA  
1073 C  C   . ASP A 144 ? 0.7892 1.0911 0.8769 0.1759  -0.1183 -0.0060 139 ASP A C   
1074 O  O   . ASP A 144 ? 0.7746 1.0601 0.8485 0.1708  -0.1211 0.0004  139 ASP A O   
1075 C  CB  . ASP A 144 ? 0.8955 1.1299 0.9703 0.1885  -0.1062 0.0043  139 ASP A CB  
1076 C  CG  . ASP A 144 ? 0.9355 1.1182 0.9874 0.1854  -0.1037 0.0167  139 ASP A CG  
1077 O  OD1 . ASP A 144 ? 0.9613 1.1373 0.9984 0.1966  -0.1095 0.0245  139 ASP A OD1 
1078 O  OD2 . ASP A 144 ? 0.9139 1.0644 0.9626 0.1712  -0.0960 0.0180  139 ASP A OD2 
1079 N  N   . LYS A 145 ? 0.7858 1.1256 0.8943 0.1610  -0.1158 -0.0199 140 LYS A N   
1080 C  CA  . LYS A 145 ? 0.7292 1.0825 0.8427 0.1346  -0.1141 -0.0274 140 LYS A CA  
1081 C  C   . LYS A 145 ? 0.7040 1.0861 0.8148 0.1378  -0.1237 -0.0285 140 LYS A C   
1082 O  O   . LYS A 145 ? 0.6542 1.0245 0.7567 0.1215  -0.1233 -0.0273 140 LYS A O   
1083 C  CB  . LYS A 145 ? 0.7100 1.0963 0.8438 0.1180  -0.1080 -0.0426 140 LYS A CB  
1084 C  CG  . LYS A 145 ? 0.6705 1.0699 0.8072 0.0904  -0.1049 -0.0516 140 LYS A CG  
1085 C  CD  . LYS A 145 ? 0.6548 1.0413 0.7960 0.0678  -0.0933 -0.0586 140 LYS A CD  
1086 C  CE  . LYS A 145 ? 0.6102 1.0082 0.7516 0.0411  -0.0892 -0.0680 140 LYS A CE  
1087 N  NZ  . LYS A 145 ? 0.6257 1.0714 0.7853 0.0295  -0.0854 -0.0850 140 LYS A NZ  
1088 N  N   . LYS A 146 ? 0.7097 1.1312 0.8275 0.1591  -0.1325 -0.0313 141 LYS A N   
1089 C  CA  . LYS A 146 ? 0.6888 1.1380 0.8020 0.1650  -0.1430 -0.0317 141 LYS A CA  
1090 C  C   . LYS A 146 ? 0.6590 1.0621 0.7456 0.1722  -0.1455 -0.0159 141 LYS A C   
1091 O  O   . LYS A 146 ? 0.6682 1.0691 0.7468 0.1590  -0.1474 -0.0155 141 LYS A O   
1092 C  CB  . LYS A 146 ? 0.7172 1.2152 0.8409 0.1913  -0.1529 -0.0363 141 LYS A CB  
1093 C  CG  . LYS A 146 ? 0.7237 1.2765 0.8759 0.1838  -0.1507 -0.0541 141 LYS A CG  
1094 C  CD  . LYS A 146 ? 0.7451 1.3562 0.9087 0.2090  -0.1627 -0.0605 141 LYS A CD  
1095 C  CE  . LYS A 146 ? 0.7339 1.3949 0.9262 0.2070  -0.1591 -0.0769 141 LYS A CE  
1096 N  NZ  . LYS A 146 ? 0.7400 1.4189 0.9473 0.1702  -0.1496 -0.0919 141 LYS A NZ  
1097 N  N   . ARG A 147 ? 0.6938 1.0581 0.7656 0.1921  -0.1444 -0.0034 142 ARG A N   
1098 C  CA  . ARG A 147 ? 0.7158 1.0334 0.7609 0.1983  -0.1450 0.0114  142 ARG A CA  
1099 C  C   . ARG A 147 ? 0.6801 0.9671 0.7198 0.1709  -0.1377 0.0125  142 ARG A C   
1100 O  O   . ARG A 147 ? 0.6410 0.9162 0.6662 0.1665  -0.1403 0.0176  142 ARG A O   
1101 C  CB  . ARG A 147 ? 0.7762 1.0518 0.8067 0.2185  -0.1412 0.0227  142 ARG A CB  
1102 C  CG  . ARG A 147 ? 0.8085 1.1040 0.8363 0.2513  -0.1488 0.0250  142 ARG A CG  
1103 C  CD  . ARG A 147 ? 0.8657 1.1066 0.8671 0.2715  -0.1451 0.0396  142 ARG A CD  
1104 N  NE  . ARG A 147 ? 0.9050 1.1251 0.9121 0.2738  -0.1363 0.0387  142 ARG A NE  
1105 C  CZ  . ARG A 147 ? 0.8762 1.1239 0.8979 0.2894  -0.1374 0.0323  142 ARG A CZ  
1106 N  NH1 . ARG A 147 ? 0.8261 1.1263 0.8598 0.3061  -0.1473 0.0259  142 ARG A NH1 
1107 N  NH2 . ARG A 147 ? 0.8915 1.1147 0.9160 0.2887  -0.1282 0.0318  142 ARG A NH2 
1108 N  N   . ILE A 148 ? 0.6860 0.9612 0.7367 0.1531  -0.1286 0.0075  143 ILE A N   
1109 C  CA  . ILE A 148 ? 0.6768 0.9216 0.7218 0.1298  -0.1216 0.0089  143 ILE A CA  
1110 C  C   . ILE A 148 ? 0.6352 0.9067 0.6850 0.1116  -0.1237 0.0006  143 ILE A C   
1111 O  O   . ILE A 148 ? 0.6150 0.8655 0.6524 0.1018  -0.1227 0.0049  143 ILE A O   
1112 C  CB  . ILE A 148 ? 0.6401 0.8673 0.6942 0.1171  -0.1121 0.0054  143 ILE A CB  
1113 C  CG1 . ILE A 148 ? 0.7001 0.8915 0.7453 0.1314  -0.1085 0.0143  143 ILE A CG1 
1114 C  CG2 . ILE A 148 ? 0.5896 0.7964 0.6407 0.0931  -0.1060 0.0040  143 ILE A CG2 
1115 C  CD1 . ILE A 148 ? 0.7363 0.9365 0.7954 0.1331  -0.1040 0.0080  143 ILE A CD1 
1116 N  N   . ILE A 149 ? 0.6091 0.9268 0.6767 0.1058  -0.1257 -0.0124 144 ILE A N   
1117 C  CA  . ILE A 149 ? 0.5901 0.9320 0.6616 0.0856  -0.1261 -0.0220 144 ILE A CA  
1118 C  C   . ILE A 149 ? 0.5987 0.9484 0.6570 0.0932  -0.1348 -0.0175 144 ILE A C   
1119 O  O   . ILE A 149 ? 0.5967 0.9364 0.6465 0.0775  -0.1331 -0.0181 144 ILE A O   
1120 C  CB  . ILE A 149 ? 0.5805 0.9729 0.6735 0.0776  -0.1258 -0.0381 144 ILE A CB  
1121 C  CG1 . ILE A 149 ? 0.5765 0.9550 0.6786 0.0640  -0.1150 -0.0430 144 ILE A CG1 
1122 C  CG2 . ILE A 149 ? 0.5698 0.9917 0.6648 0.0589  -0.1273 -0.0488 144 ILE A CG2 
1123 C  CD1 . ILE A 149 ? 0.5354 0.9523 0.6536 0.0443  -0.1103 -0.0599 144 ILE A CD1 
1124 N  N   . ASP A 150 ? 0.5953 0.9609 0.6498 0.1183  -0.1441 -0.0126 145 ASP A N   
1125 C  CA  . ASP A 150 ? 0.6134 0.9838 0.6520 0.1270  -0.1526 -0.0073 145 ASP A CA  
1126 C  C   . ASP A 150 ? 0.6118 0.9277 0.6273 0.1264  -0.1487 0.0066  145 ASP A C   
1127 O  O   . ASP A 150 ? 0.6051 0.9172 0.6076 0.1207  -0.1513 0.0087  145 ASP A O   
1128 C  CB  . ASP A 150 ? 0.6510 1.0488 0.6877 0.1568  -0.1638 -0.0044 145 ASP A CB  
1129 C  CG  . ASP A 150 ? 0.6672 1.1273 0.7286 0.1584  -0.1687 -0.0196 145 ASP A CG  
1130 O  OD1 . ASP A 150 ? 0.7014 1.1789 0.7690 0.1818  -0.1733 -0.0188 145 ASP A OD1 
1131 O  OD2 . ASP A 150 ? 0.6588 1.1500 0.7328 0.1357  -0.1672 -0.0331 145 ASP A OD2 
1132 N  N   . SER A 151 ? 0.6208 0.8955 0.6310 0.1311  -0.1419 0.0152  146 SER A N   
1133 C  CA  . SER A 151 ? 0.6226 0.8477 0.6125 0.1286  -0.1370 0.0268  146 SER A CA  
1134 C  C   . SER A 151 ? 0.6128 0.8263 0.6042 0.1025  -0.1304 0.0224  146 SER A C   
1135 O  O   . SER A 151 ? 0.6126 0.8061 0.5886 0.0978  -0.1297 0.0277  146 SER A O   
1136 C  CB  . SER A 151 ? 0.6128 0.7997 0.5981 0.1375  -0.1306 0.0348  146 SER A CB  
1137 O  OG  . SER A 151 ? 0.6594 0.8460 0.6355 0.1639  -0.1359 0.0416  146 SER A OG  
1138 N  N   . ALA A 152 ? 0.5970 0.8212 0.6053 0.0860  -0.1250 0.0127  147 ALA A N   
1139 C  CA  . ALA A 152 ? 0.5861 0.8000 0.5945 0.0627  -0.1186 0.0078  147 ALA A CA  
1140 C  C   . ALA A 152 ? 0.5837 0.8217 0.5876 0.0548  -0.1232 0.0023  147 ALA A C   
1141 O  O   . ALA A 152 ? 0.5500 0.7676 0.5416 0.0455  -0.1206 0.0053  147 ALA A O   
1142 C  CB  . ALA A 152 ? 0.5333 0.7559 0.5577 0.0481  -0.1122 -0.0020 147 ALA A CB  
1143 N  N   . ARG A 153 ? 0.5529 0.8363 0.5670 0.0578  -0.1299 -0.0066 148 ARG A N   
1144 C  CA  . ARG A 153 ? 0.5602 0.8705 0.5708 0.0486  -0.1344 -0.0138 148 ARG A CA  
1145 C  C   . ARG A 153 ? 0.5698 0.8641 0.5595 0.0598  -0.1398 -0.0033 148 ARG A C   
1146 O  O   . ARG A 153 ? 0.5742 0.8614 0.5536 0.0469  -0.1382 -0.0047 148 ARG A O   
1147 C  CB  . ARG A 153 ? 0.5711 0.9375 0.5972 0.0521  -0.1416 -0.0257 148 ARG A CB  
1148 C  CG  . ARG A 153 ? 0.5904 0.9893 0.6133 0.0416  -0.1467 -0.0349 148 ARG A CG  
1149 C  CD  . ARG A 153 ? 0.5910 1.0512 0.6306 0.0460  -0.1548 -0.0478 148 ARG A CD  
1150 N  NE  . ARG A 153 ? 0.5803 1.0596 0.6405 0.0334  -0.1479 -0.0596 148 ARG A NE  
1151 C  CZ  . ARG A 153 ? 0.5847 1.0827 0.6597 0.0480  -0.1500 -0.0607 148 ARG A CZ  
1152 N  NH1 . ARG A 153 ? 0.6127 1.1100 0.6835 0.0767  -0.1584 -0.0502 148 ARG A NH1 
1153 N  NH2 . ARG A 153 ? 0.5756 1.0916 0.6683 0.0336  -0.1426 -0.0727 148 ARG A NH2 
1154 N  N   . SER A 154 ? 0.5724 0.8581 0.5533 0.0837  -0.1455 0.0073  149 SER A N   
1155 C  CA  . SER A 154 ? 0.6011 0.8697 0.5589 0.0951  -0.1502 0.0177  149 SER A CA  
1156 C  C   . SER A 154 ? 0.5925 0.8143 0.5365 0.0831  -0.1411 0.0248  149 SER A C   
1157 O  O   . SER A 154 ? 0.5791 0.7934 0.5076 0.0787  -0.1420 0.0271  149 SER A O   
1158 C  CB  . SER A 154 ? 0.6633 0.9241 0.6108 0.1236  -0.1561 0.0284  149 SER A CB  
1159 O  OG  . SER A 154 ? 0.6795 0.9843 0.6422 0.1368  -0.1640 0.0215  149 SER A OG  
1160 N  N   . ALA A 155 ? 0.6039 0.7959 0.5536 0.0777  -0.1324 0.0275  150 ALA A N   
1161 C  CA  . ALA A 155 ? 0.5946 0.7467 0.5339 0.0667  -0.1239 0.0330  150 ALA A CA  
1162 C  C   . ALA A 155 ? 0.5780 0.7367 0.5206 0.0449  -0.1199 0.0241  150 ALA A C   
1163 O  O   . ALA A 155 ? 0.5564 0.6968 0.4854 0.0385  -0.1170 0.0272  150 ALA A O   
1164 C  CB  . ALA A 155 ? 0.5619 0.6855 0.5078 0.0662  -0.1163 0.0365  150 ALA A CB  
1165 N  N   . TYR A 156 ? 0.5408 0.7237 0.4998 0.0330  -0.1186 0.0128  151 TYR A N   
1166 C  CA  . TYR A 156 ? 0.5401 0.7274 0.4994 0.0123  -0.1140 0.0038  151 TYR A CA  
1167 C  C   . TYR A 156 ? 0.5593 0.7665 0.5076 0.0110  -0.1200 0.0011  151 TYR A C   
1168 O  O   . TYR A 156 ? 0.5404 0.7334 0.4781 -0.0008 -0.1157 0.0001  151 TYR A O   
1169 C  CB  . TYR A 156 ? 0.5178 0.7284 0.4939 0.0000  -0.1112 -0.0084 151 TYR A CB  
1170 C  CG  . TYR A 156 ? 0.5077 0.6941 0.4915 -0.0060 -0.1028 -0.0080 151 TYR A CG  
1171 C  CD1 . TYR A 156 ? 0.4920 0.6415 0.4680 -0.0122 -0.0956 -0.0031 151 TYR A CD1 
1172 C  CD2 . TYR A 156 ? 0.5173 0.7202 0.5158 -0.0052 -0.1022 -0.0133 151 TYR A CD2 
1173 C  CE1 . TYR A 156 ? 0.4829 0.6123 0.4650 -0.0165 -0.0889 -0.0031 151 TYR A CE1 
1174 C  CE2 . TYR A 156 ? 0.4796 0.6604 0.4832 -0.0105 -0.0948 -0.0131 151 TYR A CE2 
1175 C  CZ  . TYR A 156 ? 0.4915 0.6357 0.4863 -0.0158 -0.0887 -0.0078 151 TYR A CZ  
1176 O  OH  . TYR A 156 ? 0.4407 0.5649 0.4396 -0.0199 -0.0823 -0.0077 151 TYR A OH  
1177 N  N   . GLN A 157 ? 0.5568 0.7980 0.5070 0.0236  -0.1300 -0.0005 152 GLN A N   
1178 C  CA  . GLN A 157 ? 0.5704 0.8355 0.5102 0.0224  -0.1368 -0.0043 152 GLN A CA  
1179 C  C   . GLN A 157 ? 0.5942 0.8287 0.5111 0.0293  -0.1369 0.0072  152 GLN A C   
1180 O  O   . GLN A 157 ? 0.5682 0.8025 0.4737 0.0185  -0.1360 0.0040  152 GLN A O   
1181 C  CB  . GLN A 157 ? 0.5682 0.8786 0.5152 0.0376  -0.1486 -0.0081 152 GLN A CB  
1182 C  CG  . GLN A 157 ? 0.6436 0.9914 0.5851 0.0322  -0.1563 -0.0171 152 GLN A CG  
1183 C  CD  . GLN A 157 ? 0.6573 1.0167 0.6056 0.0041  -0.1491 -0.0318 152 GLN A CD  
1184 O  OE1 . GLN A 157 ? 0.7067 1.0515 0.6411 -0.0084 -0.1456 -0.0329 152 GLN A OE1 
1185 N  NE2 . GLN A 157 ? 0.6594 1.0427 0.6276 -0.0063 -0.1460 -0.0433 152 GLN A NE2 
1186 N  N   . GLU A 158 ? 0.5690 0.7756 0.4776 0.0458  -0.1368 0.0201  153 GLU A N   
1187 C  CA  . GLU A 158 ? 0.6279 0.8033 0.5132 0.0503  -0.1350 0.0304  153 GLU A CA  
1188 C  C   . GLU A 158 ? 0.6217 0.7692 0.5048 0.0313  -0.1241 0.0288  153 GLU A C   
1189 O  O   . GLU A 158 ? 0.5899 0.7275 0.4571 0.0257  -0.1225 0.0301  153 GLU A O   
1190 C  CB  . GLU A 158 ? 0.6369 0.7838 0.5118 0.0696  -0.1349 0.0437  153 GLU A CB  
1191 C  CG  . GLU A 158 ? 0.7264 0.8432 0.5742 0.0739  -0.1329 0.0538  153 GLU A CG  
1192 C  CD  . GLU A 158 ? 0.7849 0.8682 0.6169 0.0914  -0.1311 0.0670  153 GLU A CD  
1193 O  OE1 . GLU A 158 ? 0.7556 0.8392 0.5972 0.1024  -0.1322 0.0689  153 GLU A OE1 
1194 O  OE2 . GLU A 158 ? 0.8153 0.8711 0.6231 0.0937  -0.1280 0.0752  153 GLU A OE2 
1195 N  N   . ALA A 159 ? 0.5763 0.7126 0.4748 0.0217  -0.1167 0.0254  154 ALA A N   
1196 C  CA  . ALA A 159 ? 0.5973 0.7095 0.4947 0.0056  -0.1068 0.0232  154 ALA A CA  
1197 C  C   . ALA A 159 ? 0.5822 0.7114 0.4775 -0.0104 -0.1059 0.0126  154 ALA A C   
1198 O  O   . ALA A 159 ? 0.5375 0.6491 0.4217 -0.0191 -0.1004 0.0127  154 ALA A O   
1199 C  CB  . ALA A 159 ? 0.5538 0.6530 0.4670 0.0008  -0.1002 0.0215  154 ALA A CB  
1200 N  N   . MET A 160 ? 0.5427 0.7063 0.4484 -0.0152 -0.1105 0.0025  155 MET A N   
1201 C  CA  . MET A 160 ? 0.5641 0.7440 0.4662 -0.0321 -0.1090 -0.0088 155 MET A CA  
1202 C  C   . MET A 160 ? 0.5727 0.7593 0.4565 -0.0292 -0.1143 -0.0068 155 MET A C   
1203 O  O   . MET A 160 ? 0.5904 0.7672 0.4636 -0.0423 -0.1091 -0.0110 155 MET A O   
1204 C  CB  . MET A 160 ? 0.5550 0.7729 0.4718 -0.0394 -0.1122 -0.0212 155 MET A CB  
1205 C  CG  . MET A 160 ? 0.5713 0.7830 0.5042 -0.0436 -0.1064 -0.0240 155 MET A CG  
1206 S  SD  . MET A 160 ? 0.5754 0.7681 0.5054 -0.0686 -0.0934 -0.0343 155 MET A SD  
1207 C  CE  . MET A 160 ? 0.6076 0.8276 0.5271 -0.0826 -0.0958 -0.0459 155 MET A CE  
1208 N  N   . ASP A 161 ? 0.5877 0.7903 0.4658 -0.0115 -0.1246 -0.0006 156 ASP A N   
1209 C  CA  . ASP A 161 ? 0.5937 0.8013 0.4514 -0.0075 -0.1302 0.0021  156 ASP A CA  
1210 C  C   . ASP A 161 ? 0.6097 0.7767 0.4505 -0.0113 -0.1217 0.0097  156 ASP A C   
1211 O  O   . ASP A 161 ? 0.6347 0.8008 0.4615 -0.0207 -0.1201 0.0061  156 ASP A O   
1212 C  CB  . ASP A 161 ? 0.6576 0.8810 0.5081 0.0159  -0.1420 0.0101  156 ASP A CB  
1213 C  CG  . ASP A 161 ? 0.6937 0.9628 0.5621 0.0215  -0.1511 0.0017  156 ASP A CG  
1214 O  OD1 . ASP A 161 ? 0.7492 1.0295 0.6161 0.0431  -0.1599 0.0084  156 ASP A OD1 
1215 O  OD2 . ASP A 161 ? 0.7281 1.0221 0.6107 0.0041  -0.1490 -0.0122 156 ASP A OD2 
1216 N  N   . ILE A 162 ? 0.6300 0.7645 0.4722 -0.0048 -0.1157 0.0192  157 ILE A N   
1217 C  CA  . ILE A 162 ? 0.6481 0.7467 0.4764 -0.0088 -0.1069 0.0254  157 ILE A CA  
1218 C  C   . ILE A 162 ? 0.6371 0.7269 0.4705 -0.0280 -0.0973 0.0166  157 ILE A C   
1219 O  O   . ILE A 162 ? 0.6337 0.7115 0.4531 -0.0356 -0.0926 0.0156  157 ILE A O   
1220 C  CB  . ILE A 162 ? 0.6431 0.7123 0.4728 0.0015  -0.1026 0.0361  157 ILE A CB  
1221 C  CG1 . ILE A 162 ? 0.6932 0.7632 0.5109 0.0216  -0.1106 0.0461  157 ILE A CG1 
1222 C  CG2 . ILE A 162 ? 0.6677 0.7040 0.4877 -0.0055 -0.0920 0.0399  157 ILE A CG2 
1223 C  CD1 . ILE A 162 ? 0.7004 0.7495 0.5246 0.0316  -0.1075 0.0537  157 ILE A CD1 
1224 N  N   . SER A 163 ? 0.5755 0.6693 0.4270 -0.0355 -0.0939 0.0100  158 SER A N   
1225 C  CA  . SER A 163 ? 0.5779 0.6579 0.4315 -0.0514 -0.0840 0.0027  158 SER A CA  
1226 C  C   . SER A 163 ? 0.5964 0.6911 0.4398 -0.0647 -0.0838 -0.0073 158 SER A C   
1227 O  O   . SER A 163 ? 0.5783 0.6550 0.4136 -0.0751 -0.0754 -0.0108 158 SER A O   
1228 C  CB  . SER A 163 ? 0.5700 0.6504 0.4415 -0.0561 -0.0806 -0.0021 158 SER A CB  
1229 O  OG  . SER A 163 ? 0.5883 0.6995 0.4670 -0.0620 -0.0853 -0.0115 158 SER A OG  
1230 N  N   . LYS A 164 ? 0.5789 0.7074 0.4228 -0.0645 -0.0927 -0.0129 159 LYS A N   
1231 C  CA  . LYS A 164 ? 0.5750 0.7199 0.4094 -0.0790 -0.0924 -0.0241 159 LYS A CA  
1232 C  C   . LYS A 164 ? 0.6247 0.7613 0.4378 -0.0768 -0.0935 -0.0198 159 LYS A C   
1233 O  O   . LYS A 164 ? 0.6059 0.7412 0.4078 -0.0905 -0.0889 -0.0278 159 LYS A O   
1234 C  CB  . LYS A 164 ? 0.6035 0.7919 0.4464 -0.0801 -0.1020 -0.0328 159 LYS A CB  
1235 C  CG  . LYS A 164 ? 0.5919 0.7905 0.4538 -0.0881 -0.0986 -0.0408 159 LYS A CG  
1236 C  CD  . LYS A 164 ? 0.6587 0.9021 0.5267 -0.0974 -0.1046 -0.0546 159 LYS A CD  
1237 C  CE  . LYS A 164 ? 0.6512 0.9188 0.5399 -0.0910 -0.1091 -0.0565 159 LYS A CE  
1238 N  NZ  . LYS A 164 ? 0.6887 0.9894 0.5802 -0.0718 -0.1234 -0.0521 159 LYS A NZ  
1239 N  N   . LYS A 165 ? 0.6188 0.7465 0.4240 -0.0604 -0.0983 -0.0074 160 LYS A N   
1240 C  CA  . LYS A 165 ? 0.6690 0.7875 0.4513 -0.0570 -0.0994 -0.0021 160 LYS A CA  
1241 C  C   . LYS A 165 ? 0.6772 0.7572 0.4516 -0.0604 -0.0875 0.0032  160 LYS A C   
1242 O  O   . LYS A 165 ? 0.6562 0.7269 0.4126 -0.0661 -0.0839 0.0024  160 LYS A O   
1243 C  CB  . LYS A 165 ? 0.6897 0.8165 0.4636 -0.0367 -0.1101 0.0086  160 LYS A CB  
1244 C  CG  . LYS A 165 ? 0.7810 0.9509 0.5553 -0.0322 -0.1233 0.0025  160 LYS A CG  
1245 C  CD  . LYS A 165 ? 0.8861 1.0619 0.6488 -0.0090 -0.1342 0.0139  160 LYS A CD  
1246 C  CE  . LYS A 165 ? 0.9074 1.1271 0.6845 0.0002  -0.1467 0.0085  160 LYS A CE  
1247 N  NZ  . LYS A 165 ? 0.9256 1.1445 0.6956 0.0260  -0.1555 0.0209  160 LYS A NZ  
1248 N  N   . GLU A 166 ? 0.6412 0.7010 0.4292 -0.0578 -0.0813 0.0076  161 GLU A N   
1249 C  CA  . GLU A 166 ? 0.6621 0.6895 0.4460 -0.0574 -0.0714 0.0138  161 GLU A CA  
1250 C  C   . GLU A 166 ? 0.6655 0.6784 0.4604 -0.0685 -0.0609 0.0071  161 GLU A C   
1251 O  O   . GLU A 166 ? 0.6910 0.6812 0.4829 -0.0697 -0.0522 0.0098  161 GLU A O   
1252 C  CB  . GLU A 166 ? 0.7044 0.7199 0.4942 -0.0435 -0.0730 0.0246  161 GLU A CB  
1253 C  CG  . GLU A 166 ? 0.7523 0.7806 0.5327 -0.0287 -0.0840 0.0320  161 GLU A CG  
1254 C  CD  . GLU A 166 ? 0.7968 0.7997 0.5604 -0.0183 -0.0816 0.0440  161 GLU A CD  
1255 O  OE1 . GLU A 166 ? 0.8263 0.8041 0.5860 -0.0242 -0.0711 0.0459  161 GLU A OE1 
1256 O  OE2 . GLU A 166 ? 0.8076 0.8153 0.5621 -0.0038 -0.0897 0.0513  161 GLU A OE2 
1257 N  N   . MET A 167 ? 0.6199 0.6450 0.4268 -0.0761 -0.0611 -0.0016 162 MET A N   
1258 C  CA  . MET A 167 ? 0.5980 0.6063 0.4147 -0.0828 -0.0519 -0.0061 162 MET A CA  
1259 C  C   . MET A 167 ? 0.5903 0.6035 0.4024 -0.0976 -0.0477 -0.0182 162 MET A C   
1260 O  O   . MET A 167 ? 0.5681 0.6053 0.3789 -0.1030 -0.0537 -0.0244 162 MET A O   
1261 C  CB  . MET A 167 ? 0.6021 0.6129 0.4376 -0.0765 -0.0544 -0.0035 162 MET A CB  
1262 C  CG  . MET A 167 ? 0.6075 0.6041 0.4487 -0.0649 -0.0541 0.0067  162 MET A CG  
1263 S  SD  . MET A 167 ? 0.6373 0.6395 0.4989 -0.0588 -0.0576 0.0081  162 MET A SD  
1264 C  CE  . MET A 167 ? 0.6344 0.6115 0.5016 -0.0522 -0.0514 0.0155  162 MET A CE  
1265 N  N   . PRO A 168 ? 0.5811 0.5724 0.3902 -0.1042 -0.0371 -0.0224 163 PRO A N   
1266 C  CA  . PRO A 168 ? 0.6244 0.6146 0.4270 -0.1185 -0.0316 -0.0340 163 PRO A CA  
1267 C  C   . PRO A 168 ? 0.5659 0.5654 0.3808 -0.1218 -0.0333 -0.0383 163 PRO A C   
1268 O  O   . PRO A 168 ? 0.5879 0.5859 0.4170 -0.1125 -0.0359 -0.0321 163 PRO A O   
1269 C  CB  . PRO A 168 ? 0.6200 0.5802 0.4173 -0.1199 -0.0197 -0.0352 163 PRO A CB  
1270 C  CG  . PRO A 168 ? 0.5951 0.5458 0.4047 -0.1069 -0.0201 -0.0256 163 PRO A CG  
1271 C  CD  . PRO A 168 ? 0.6258 0.5926 0.4372 -0.0987 -0.0295 -0.0174 163 PRO A CD  
1272 N  N   . PRO A 169 ? 0.5622 0.5706 0.3710 -0.1361 -0.0310 -0.0495 164 PRO A N   
1273 C  CA  . PRO A 169 ? 0.5798 0.5984 0.3989 -0.1413 -0.0316 -0.0547 164 PRO A CA  
1274 C  C   . PRO A 169 ? 0.5632 0.5533 0.3856 -0.1404 -0.0229 -0.0538 164 PRO A C   
1275 O  O   . PRO A 169 ? 0.5945 0.5902 0.4252 -0.1433 -0.0232 -0.0566 164 PRO A O   
1276 C  CB  . PRO A 169 ? 0.6080 0.6413 0.4162 -0.1597 -0.0293 -0.0684 164 PRO A CB  
1277 C  CG  . PRO A 169 ? 0.6261 0.6443 0.4164 -0.1648 -0.0237 -0.0707 164 PRO A CG  
1278 C  CD  . PRO A 169 ? 0.6154 0.6270 0.4067 -0.1493 -0.0276 -0.0586 164 PRO A CD  
1279 N  N   . THR A 170 ? 0.5604 0.5214 0.3761 -0.1359 -0.0154 -0.0504 165 THR A N   
1280 C  CA  . THR A 170 ? 0.5808 0.5168 0.4004 -0.1305 -0.0092 -0.0479 165 THR A CA  
1281 C  C   . THR A 170 ? 0.5642 0.4989 0.3987 -0.1143 -0.0141 -0.0368 165 THR A C   
1282 O  O   . THR A 170 ? 0.5433 0.4601 0.3820 -0.1081 -0.0103 -0.0343 165 THR A O   
1283 C  CB  . THR A 170 ? 0.5822 0.4875 0.3861 -0.1336 0.0023  -0.0517 165 THR A CB  
1284 O  OG1 . THR A 170 ? 0.6190 0.5219 0.4207 -0.1270 0.0023  -0.0472 165 THR A OG1 
1285 C  CG2 . THR A 170 ? 0.5948 0.4940 0.3806 -0.1514 0.0098  -0.0637 165 THR A CG2 
1286 N  N   . ASN A 171 ? 0.5351 0.4863 0.3756 -0.1072 -0.0218 -0.0304 166 ASN A N   
1287 C  CA  . ASN A 171 ? 0.5402 0.4876 0.3929 -0.0937 -0.0248 -0.0208 166 ASN A CA  
1288 C  C   . ASN A 171 ? 0.5449 0.4944 0.4109 -0.0894 -0.0275 -0.0190 166 ASN A C   
1289 O  O   . ASN A 171 ? 0.5296 0.4972 0.4002 -0.0927 -0.0327 -0.0213 166 ASN A O   
1290 C  CB  . ASN A 171 ? 0.5519 0.5144 0.4055 -0.0875 -0.0322 -0.0142 166 ASN A CB  
1291 C  CG  . ASN A 171 ? 0.5476 0.5050 0.4126 -0.0755 -0.0343 -0.0051 166 ASN A CG  
1292 O  OD1 . ASN A 171 ? 0.5461 0.5104 0.4225 -0.0703 -0.0390 -0.0022 166 ASN A OD1 
1293 N  ND2 . ASN A 171 ? 0.5633 0.5088 0.4249 -0.0721 -0.0300 -0.0015 166 ASN A ND2 
1294 N  N   . PRO A 172 ? 0.5201 0.4535 0.3926 -0.0821 -0.0244 -0.0155 167 PRO A N   
1295 C  CA  . PRO A 172 ? 0.5388 0.4716 0.4211 -0.0791 -0.0261 -0.0147 167 PRO A CA  
1296 C  C   . PRO A 172 ? 0.5301 0.4820 0.4251 -0.0732 -0.0347 -0.0096 167 PRO A C   
1297 O  O   . PRO A 172 ? 0.5189 0.4779 0.4200 -0.0745 -0.0367 -0.0115 167 PRO A O   
1298 C  CB  . PRO A 172 ? 0.5659 0.4796 0.4516 -0.0708 -0.0219 -0.0117 167 PRO A CB  
1299 C  CG  . PRO A 172 ? 0.5952 0.5063 0.4788 -0.0674 -0.0200 -0.0092 167 PRO A CG  
1300 C  CD  . PRO A 172 ? 0.5283 0.4455 0.3993 -0.0764 -0.0191 -0.0131 167 PRO A CD  
1301 N  N   . ILE A 173 ? 0.5040 0.4626 0.4013 -0.0665 -0.0389 -0.0034 168 ILE A N   
1302 C  CA  . ILE A 173 ? 0.5091 0.4833 0.4150 -0.0597 -0.0466 0.0015  168 ILE A CA  
1303 C  C   . ILE A 173 ? 0.4950 0.4921 0.3984 -0.0647 -0.0518 -0.0030 168 ILE A C   
1304 O  O   . ILE A 173 ? 0.4892 0.5014 0.4015 -0.0623 -0.0565 -0.0035 168 ILE A O   
1305 C  CB  . ILE A 173 ? 0.5136 0.4837 0.4182 -0.0515 -0.0483 0.0095  168 ILE A CB  
1306 C  CG1 . ILE A 173 ? 0.5287 0.4810 0.4383 -0.0481 -0.0428 0.0119  168 ILE A CG1 
1307 C  CG2 . ILE A 173 ? 0.5684 0.5504 0.4783 -0.0429 -0.0556 0.0150  168 ILE A CG2 
1308 C  CD1 . ILE A 173 ? 0.5949 0.5411 0.5020 -0.0431 -0.0420 0.0182  168 ILE A CD1 
1309 N  N   . ARG A 174 ? 0.4921 0.4940 0.3839 -0.0719 -0.0509 -0.0072 169 ARG A N   
1310 C  CA  . ARG A 174 ? 0.4962 0.5236 0.3860 -0.0782 -0.0557 -0.0135 169 ARG A CA  
1311 C  C   . ARG A 174 ? 0.5062 0.5383 0.4010 -0.0880 -0.0525 -0.0221 169 ARG A C   
1312 O  O   . ARG A 174 ? 0.4987 0.5548 0.4015 -0.0888 -0.0576 -0.0256 169 ARG A O   
1313 C  CB  . ARG A 174 ? 0.4909 0.5203 0.3656 -0.0862 -0.0541 -0.0178 169 ARG A CB  
1314 C  CG  . ARG A 174 ? 0.5102 0.5679 0.3823 -0.0952 -0.0585 -0.0268 169 ARG A CG  
1315 C  CD  . ARG A 174 ? 0.5298 0.5913 0.3856 -0.1011 -0.0586 -0.0298 169 ARG A CD  
1316 N  NE  . ARG A 174 ? 0.5756 0.6650 0.4285 -0.1128 -0.0616 -0.0409 169 ARG A NE  
1317 C  CZ  . ARG A 174 ? 0.5822 0.6813 0.4214 -0.1200 -0.0627 -0.0460 169 ARG A CZ  
1318 N  NH1 . ARG A 174 ? 0.5695 0.6512 0.3955 -0.1169 -0.0604 -0.0408 169 ARG A NH1 
1319 N  NH2 . ARG A 174 ? 0.5736 0.7017 0.4121 -0.1316 -0.0657 -0.0575 169 ARG A NH2 
1320 N  N   . LEU A 175 ? 0.5110 0.5196 0.4000 -0.0951 -0.0434 -0.0257 170 LEU A N   
1321 C  CA  . LEU A 175 ? 0.5001 0.5064 0.3895 -0.1051 -0.0384 -0.0334 170 LEU A CA  
1322 C  C   . LEU A 175 ? 0.4964 0.5074 0.4000 -0.0977 -0.0416 -0.0298 170 LEU A C   
1323 O  O   . LEU A 175 ? 0.4829 0.5120 0.3924 -0.1036 -0.0428 -0.0356 170 LEU A O   
1324 C  CB  . LEU A 175 ? 0.5138 0.4879 0.3904 -0.1106 -0.0278 -0.0361 170 LEU A CB  
1325 C  CG  . LEU A 175 ? 0.5277 0.4951 0.3881 -0.1207 -0.0225 -0.0422 170 LEU A CG  
1326 C  CD1 . LEU A 175 ? 0.5653 0.4976 0.4132 -0.1216 -0.0121 -0.0432 170 LEU A CD1 
1327 C  CD2 . LEU A 175 ? 0.5324 0.5193 0.3882 -0.1364 -0.0218 -0.0532 170 LEU A CD2 
1328 N  N   . GLY A 176 ? 0.4680 0.4642 0.3775 -0.0857 -0.0425 -0.0211 171 GLY A N   
1329 C  CA  . GLY A 176 ? 0.5157 0.5145 0.4375 -0.0789 -0.0450 -0.0179 171 GLY A CA  
1330 C  C   . GLY A 176 ? 0.5026 0.5302 0.4350 -0.0738 -0.0534 -0.0169 171 GLY A C   
1331 O  O   . GLY A 176 ? 0.4758 0.5146 0.4169 -0.0742 -0.0545 -0.0195 171 GLY A O   
1332 N  N   . LEU A 177 ? 0.4889 0.5283 0.4196 -0.0678 -0.0592 -0.0130 172 LEU A N   
1333 C  CA  . LEU A 177 ? 0.4891 0.5566 0.4270 -0.0609 -0.0677 -0.0121 172 LEU A CA  
1334 C  C   . LEU A 177 ? 0.4893 0.5839 0.4301 -0.0719 -0.0684 -0.0232 172 LEU A C   
1335 O  O   . LEU A 177 ? 0.4885 0.6037 0.4408 -0.0689 -0.0720 -0.0256 172 LEU A O   
1336 C  CB  . LEU A 177 ? 0.4742 0.5458 0.4042 -0.0530 -0.0731 -0.0061 172 LEU A CB  
1337 C  CG  . LEU A 177 ? 0.5054 0.6095 0.4376 -0.0472 -0.0822 -0.0076 172 LEU A CG  
1338 C  CD1 . LEU A 177 ? 0.4865 0.5987 0.4301 -0.0335 -0.0873 -0.0025 172 LEU A CD1 
1339 C  CD2 . LEU A 177 ? 0.5225 0.6264 0.4410 -0.0417 -0.0863 -0.0024 172 LEU A CD2 
1340 N  N   . ALA A 178 ? 0.4846 0.5806 0.4151 -0.0855 -0.0645 -0.0310 173 ALA A N   
1341 C  CA  . ALA A 178 ? 0.4857 0.6090 0.4185 -0.0987 -0.0642 -0.0433 173 ALA A CA  
1342 C  C   . ALA A 178 ? 0.5041 0.6218 0.4427 -0.1070 -0.0574 -0.0489 173 ALA A C   
1343 O  O   . ALA A 178 ? 0.5117 0.6575 0.4606 -0.1109 -0.0594 -0.0560 173 ALA A O   
1344 C  CB  . ALA A 178 ? 0.5068 0.6279 0.4249 -0.1133 -0.0597 -0.0510 173 ALA A CB  
1345 N  N   . LEU A 179 ? 0.4820 0.5643 0.4133 -0.1093 -0.0492 -0.0461 174 LEU A N   
1346 C  CA  . LEU A 179 ? 0.5031 0.5753 0.4370 -0.1150 -0.0428 -0.0496 174 LEU A CA  
1347 C  C   . LEU A 179 ? 0.5028 0.5934 0.4536 -0.1037 -0.0491 -0.0460 174 LEU A C   
1348 O  O   . LEU A 179 ? 0.4999 0.6083 0.4579 -0.1107 -0.0474 -0.0535 174 LEU A O   
1349 C  CB  . LEU A 179 ? 0.5215 0.5526 0.4450 -0.1130 -0.0356 -0.0444 174 LEU A CB  
1350 C  CG  . LEU A 179 ? 0.5020 0.5180 0.4250 -0.1166 -0.0292 -0.0463 174 LEU A CG  
1351 C  CD1 . LEU A 179 ? 0.5483 0.5645 0.4606 -0.1364 -0.0201 -0.0586 174 LEU A CD1 
1352 C  CD2 . LEU A 179 ? 0.4980 0.4780 0.4127 -0.1089 -0.0253 -0.0391 174 LEU A CD2 
1353 N  N   . ASN A 180 ? 0.4662 0.5527 0.4230 -0.0868 -0.0557 -0.0351 175 ASN A N   
1354 C  CA  . ASN A 180 ? 0.4806 0.5789 0.4513 -0.0754 -0.0605 -0.0313 175 ASN A CA  
1355 C  C   . ASN A 180 ? 0.4987 0.6375 0.4797 -0.0723 -0.0679 -0.0360 175 ASN A C   
1356 O  O   . ASN A 180 ? 0.4689 0.6252 0.4617 -0.0700 -0.0689 -0.0391 175 ASN A O   
1357 C  CB  . ASN A 180 ? 0.4526 0.5327 0.4245 -0.0596 -0.0641 -0.0191 175 ASN A CB  
1358 C  CG  . ASN A 180 ? 0.5084 0.5559 0.4759 -0.0602 -0.0579 -0.0156 175 ASN A CG  
1359 O  OD1 . ASN A 180 ? 0.4749 0.5088 0.4347 -0.0711 -0.0509 -0.0209 175 ASN A OD1 
1360 N  ND2 . ASN A 180 ? 0.4611 0.4955 0.4321 -0.0483 -0.0602 -0.0071 175 ASN A ND2 
1361 N  N   . PHE A 181 ? 0.4780 0.6334 0.4547 -0.0715 -0.0732 -0.0368 176 PHE A N   
1362 C  CA  . PHE A 181 ? 0.4976 0.6955 0.4833 -0.0684 -0.0809 -0.0426 176 PHE A CA  
1363 C  C   . PHE A 181 ? 0.4950 0.7165 0.4869 -0.0858 -0.0759 -0.0572 176 PHE A C   
1364 O  O   . PHE A 181 ? 0.5015 0.7572 0.5073 -0.0825 -0.0801 -0.0629 176 PHE A O   
1365 C  CB  . PHE A 181 ? 0.4727 0.6820 0.4491 -0.0657 -0.0872 -0.0413 176 PHE A CB  
1366 C  CG  . PHE A 181 ? 0.5156 0.7653 0.4996 -0.0536 -0.0983 -0.0426 176 PHE A CG  
1367 C  CD1 . PHE A 181 ? 0.5341 0.8031 0.5325 -0.0415 -0.1026 -0.0420 176 PHE A CD1 
1368 C  CD2 . PHE A 181 ? 0.5291 0.7979 0.5047 -0.0532 -0.1047 -0.0446 176 PHE A CD2 
1369 C  CE1 . PHE A 181 ? 0.5258 0.8329 0.5305 -0.0276 -0.1134 -0.0432 176 PHE A CE1 
1370 C  CE2 . PHE A 181 ? 0.5434 0.8505 0.5245 -0.0398 -0.1160 -0.0455 176 PHE A CE2 
1371 C  CZ  . PHE A 181 ? 0.5391 0.8657 0.5349 -0.0263 -0.1204 -0.0448 176 PHE A CZ  
1372 N  N   . SER A 182 ? 0.5102 0.7136 0.4910 -0.1046 -0.0662 -0.0641 177 SER A N   
1373 C  CA  . SER A 182 ? 0.5331 0.7558 0.5170 -0.1237 -0.0595 -0.0789 177 SER A CA  
1374 C  C   . SER A 182 ? 0.5170 0.7348 0.5099 -0.1235 -0.0547 -0.0796 177 SER A C   
1375 O  O   . SER A 182 ? 0.5364 0.7854 0.5403 -0.1314 -0.0534 -0.0903 177 SER A O   
1376 C  CB  . SER A 182 ? 0.5405 0.7396 0.5063 -0.1442 -0.0489 -0.0860 177 SER A CB  
1377 O  OG  . SER A 182 ? 0.5695 0.7221 0.5235 -0.1453 -0.0401 -0.0799 177 SER A OG  
1378 N  N   . VAL A 183 ? 0.5303 0.7115 0.5191 -0.1144 -0.0522 -0.0689 178 VAL A N   
1379 C  CA  . VAL A 183 ? 0.5314 0.7077 0.5281 -0.1118 -0.0488 -0.0684 178 VAL A CA  
1380 C  C   . VAL A 183 ? 0.5333 0.7457 0.5490 -0.0974 -0.0578 -0.0678 178 VAL A C   
1381 O  O   . VAL A 183 ? 0.5373 0.7699 0.5637 -0.1016 -0.0551 -0.0753 178 VAL A O   
1382 C  CB  . VAL A 183 ? 0.5244 0.6574 0.5130 -0.1030 -0.0462 -0.0568 178 VAL A CB  
1383 C  CG1 . VAL A 183 ? 0.5347 0.6642 0.5317 -0.0978 -0.0443 -0.0553 178 VAL A CG1 
1384 C  CG2 . VAL A 183 ? 0.5567 0.6551 0.5262 -0.1160 -0.0366 -0.0585 178 VAL A CG2 
1385 N  N   . PHE A 184 ? 0.5118 0.7315 0.5304 -0.0799 -0.0679 -0.0589 179 PHE A N   
1386 C  CA  . PHE A 184 ? 0.5201 0.7735 0.5536 -0.0638 -0.0770 -0.0580 179 PHE A CA  
1387 C  C   . PHE A 184 ? 0.5387 0.8402 0.5835 -0.0732 -0.0784 -0.0726 179 PHE A C   
1388 O  O   . PHE A 184 ? 0.5286 0.8560 0.5881 -0.0693 -0.0790 -0.0780 179 PHE A O   
1389 C  CB  . PHE A 184 ? 0.4983 0.7496 0.5269 -0.0459 -0.0867 -0.0472 179 PHE A CB  
1390 C  CG  . PHE A 184 ? 0.5078 0.7950 0.5475 -0.0283 -0.0967 -0.0467 179 PHE A CG  
1391 C  CD1 . PHE A 184 ? 0.5171 0.7986 0.5635 -0.0109 -0.0991 -0.0395 179 PHE A CD1 
1392 C  CD2 . PHE A 184 ? 0.5312 0.8577 0.5736 -0.0282 -0.1038 -0.0537 179 PHE A CD2 
1393 C  CE1 . PHE A 184 ? 0.5427 0.8549 0.5973 0.0078  -0.1081 -0.0387 179 PHE A CE1 
1394 C  CE2 . PHE A 184 ? 0.5422 0.9028 0.5937 -0.0091 -0.1139 -0.0531 179 PHE A CE2 
1395 C  CZ  . PHE A 184 ? 0.5457 0.8979 0.6030 0.0096  -0.1158 -0.0453 179 PHE A CZ  
1396 N  N   . HIS A 185 ? 0.5366 0.8526 0.5751 -0.0858 -0.0786 -0.0802 180 HIS A N   
1397 C  CA  . HIS A 185 ? 0.5683 0.9338 0.6178 -0.0969 -0.0798 -0.0959 180 HIS A CA  
1398 C  C   . HIS A 185 ? 0.5792 0.9499 0.6353 -0.1146 -0.0687 -0.1076 180 HIS A C   
1399 O  O   . HIS A 185 ? 0.5893 1.0024 0.6624 -0.1148 -0.0704 -0.1177 180 HIS A O   
1400 C  CB  . HIS A 185 ? 0.5684 0.9414 0.6066 -0.1118 -0.0796 -0.1030 180 HIS A CB  
1401 C  CG  . HIS A 185 ? 0.5889 0.9734 0.6229 -0.0956 -0.0918 -0.0955 180 HIS A CG  
1402 N  ND1 . HIS A 185 ? 0.5838 1.0029 0.6293 -0.0743 -0.1042 -0.0924 180 HIS A ND1 
1403 C  CD2 . HIS A 185 ? 0.5767 0.9417 0.5944 -0.0972 -0.0932 -0.0905 180 HIS A CD2 
1404 C  CE1 . HIS A 185 ? 0.5813 0.9998 0.6160 -0.0636 -0.1126 -0.0853 180 HIS A CE1 
1405 N  NE2 . HIS A 185 ? 0.5872 0.9739 0.6057 -0.0779 -0.1060 -0.0843 180 HIS A NE2 
1406 N  N   . TYR A 186 ? 0.5433 0.8713 0.5851 -0.1289 -0.0570 -0.1067 181 TYR A N   
1407 C  CA  . TYR A 186 ? 0.5738 0.9018 0.6163 -0.1485 -0.0446 -0.1183 181 TYR A CA  
1408 C  C   . TYR A 186 ? 0.5894 0.9165 0.6436 -0.1374 -0.0439 -0.1145 181 TYR A C   
1409 O  O   . TYR A 186 ? 0.5914 0.9500 0.6586 -0.1450 -0.0403 -0.1260 181 TYR A O   
1410 C  CB  . TYR A 186 ? 0.6045 0.8832 0.6235 -0.1658 -0.0321 -0.1179 181 TYR A CB  
1411 C  CG  . TYR A 186 ? 0.6396 0.9145 0.6530 -0.1895 -0.0176 -0.1311 181 TYR A CG  
1412 C  CD1 . TYR A 186 ? 0.6459 0.9040 0.6604 -0.1886 -0.0111 -0.1292 181 TYR A CD1 
1413 C  CD2 . TYR A 186 ? 0.6715 0.9601 0.6775 -0.2140 -0.0097 -0.1463 181 TYR A CD2 
1414 C  CE1 . TYR A 186 ? 0.6830 0.9355 0.6896 -0.2110 0.0032  -0.1412 181 TYR A CE1 
1415 C  CE2 . TYR A 186 ? 0.6902 0.9733 0.6887 -0.2374 0.0051  -0.1590 181 TYR A CE2 
1416 C  CZ  . TYR A 186 ? 0.6955 0.9597 0.6938 -0.2356 0.0116  -0.1561 181 TYR A CZ  
1417 O  OH  . TYR A 186 ? 0.7769 1.0328 0.7650 -0.2596 0.0275  -0.1686 181 TYR A OH  
1418 N  N   . GLU A 187 ? 0.5645 0.8572 0.6143 -0.1202 -0.0471 -0.0993 182 GLU A N   
1419 C  CA  . GLU A 187 ? 0.5818 0.8636 0.6380 -0.1122 -0.0443 -0.0954 182 GLU A CA  
1420 C  C   . GLU A 187 ? 0.5680 0.8793 0.6423 -0.0899 -0.0547 -0.0914 182 GLU A C   
1421 O  O   . GLU A 187 ? 0.5828 0.9048 0.6678 -0.0869 -0.0520 -0.0946 182 GLU A O   
1422 C  CB  . GLU A 187 ? 0.5714 0.7995 0.6121 -0.1072 -0.0411 -0.0826 182 GLU A CB  
1423 C  CG  . GLU A 187 ? 0.6203 0.8142 0.6403 -0.1264 -0.0302 -0.0857 182 GLU A CG  
1424 C  CD  . GLU A 187 ? 0.6808 0.8657 0.6954 -0.1427 -0.0178 -0.0944 182 GLU A CD  
1425 O  OE1 . GLU A 187 ? 0.7002 0.8583 0.6958 -0.1596 -0.0075 -0.0986 182 GLU A OE1 
1426 O  OE2 . GLU A 187 ? 0.6959 0.8976 0.7234 -0.1380 -0.0177 -0.0967 182 GLU A OE2 
1427 N  N   . ILE A 188 ? 0.5672 0.8903 0.6436 -0.0738 -0.0659 -0.0845 183 ILE A N   
1428 C  CA  . ILE A 188 ? 0.5594 0.9020 0.6479 -0.0495 -0.0756 -0.0784 183 ILE A CA  
1429 C  C   . ILE A 188 ? 0.5776 0.9767 0.6806 -0.0449 -0.0834 -0.0883 183 ILE A C   
1430 O  O   . ILE A 188 ? 0.5506 0.9806 0.6694 -0.0344 -0.0861 -0.0927 183 ILE A O   
1431 C  CB  . ILE A 188 ? 0.5598 0.8704 0.6371 -0.0320 -0.0822 -0.0622 183 ILE A CB  
1432 C  CG1 . ILE A 188 ? 0.5489 0.8085 0.6134 -0.0374 -0.0749 -0.0541 183 ILE A CG1 
1433 C  CG2 . ILE A 188 ? 0.5295 0.8526 0.6149 -0.0066 -0.0907 -0.0551 183 ILE A CG2 
1434 C  CD1 . ILE A 188 ? 0.5086 0.7546 0.5784 -0.0313 -0.0710 -0.0515 183 ILE A CD1 
1435 N  N   . ALA A 189 ? 0.5518 0.9664 0.6495 -0.0519 -0.0874 -0.0922 184 ALA A N   
1436 C  CA  . ALA A 189 ? 0.5911 1.0607 0.7009 -0.0452 -0.0970 -0.1007 184 ALA A CA  
1437 C  C   . ALA A 189 ? 0.6291 1.1425 0.7522 -0.0664 -0.0912 -0.1206 184 ALA A C   
1438 O  O   . ALA A 189 ? 0.6585 1.2256 0.7953 -0.0614 -0.0992 -0.1302 184 ALA A O   
1439 C  CB  . ALA A 189 ? 0.5753 1.0437 0.6723 -0.0429 -0.1046 -0.0962 184 ALA A CB  
1440 N  N   . ASN A 190 ? 0.6276 1.1195 0.7459 -0.0899 -0.0774 -0.1275 185 ASN A N   
1441 C  CA  . ASN A 190 ? 0.6753 1.2026 0.8030 -0.1143 -0.0689 -0.1473 185 ASN A CA  
1442 C  C   . ASN A 190 ? 0.6625 1.2240 0.7892 -0.1270 -0.0728 -0.1585 185 ASN A C   
1443 O  O   . ASN A 190 ? 0.6776 1.2957 0.8208 -0.1340 -0.0747 -0.1746 185 ASN A O   
1444 C  CB  . ASN A 190 ? 0.7097 1.2817 0.8609 -0.1056 -0.0703 -0.1558 185 ASN A CB  
1445 C  CG  . ASN A 190 ? 0.7948 1.3327 0.9456 -0.0991 -0.0635 -0.1479 185 ASN A CG  
1446 O  OD1 . ASN A 190 ? 0.7700 1.3067 0.9277 -0.0738 -0.0709 -0.1378 185 ASN A OD1 
1447 N  ND2 . ASN A 190 ? 0.8553 1.3626 0.9955 -0.1218 -0.0489 -0.1524 185 ASN A ND2 
1448 N  N   . SER A 191 ? 0.6519 1.1806 0.7593 -0.1301 -0.0739 -0.1507 186 SER A N   
1449 C  CA  . SER A 191 ? 0.6434 1.1965 0.7455 -0.1431 -0.0769 -0.1602 186 SER A CA  
1450 C  C   . SER A 191 ? 0.6523 1.1606 0.7322 -0.1686 -0.0635 -0.1625 186 SER A C   
1451 O  O   . SER A 191 ? 0.6639 1.1392 0.7267 -0.1656 -0.0655 -0.1528 186 SER A O   
1452 C  CB  . SER A 191 ? 0.6543 1.2128 0.7522 -0.1197 -0.0923 -0.1484 186 SER A CB  
1453 O  OG  . SER A 191 ? 0.6667 1.2428 0.7778 -0.0909 -0.1029 -0.1397 186 SER A OG  
1454 N  N   . PRO A 192 ? 0.6692 1.1739 0.7473 -0.1938 -0.0489 -0.1756 187 PRO A N   
1455 C  CA  . PRO A 192 ? 0.7045 1.1613 0.7578 -0.2169 -0.0350 -0.1775 187 PRO A CA  
1456 C  C   . PRO A 192 ? 0.7128 1.1780 0.7547 -0.2291 -0.0368 -0.1840 187 PRO A C   
1457 O  O   . PRO A 192 ? 0.7083 1.1259 0.7277 -0.2354 -0.0308 -0.1777 187 PRO A O   
1458 C  CB  . PRO A 192 ? 0.7474 1.2095 0.8019 -0.2423 -0.0194 -0.1932 187 PRO A CB  
1459 C  CG  . PRO A 192 ? 0.7274 1.2462 0.8099 -0.2340 -0.0253 -0.2012 187 PRO A CG  
1460 C  CD  . PRO A 192 ? 0.6902 1.2395 0.7880 -0.2035 -0.0444 -0.1913 187 PRO A CD  
1461 N  N   . GLU A 193 ? 0.6982 1.2235 0.7547 -0.2320 -0.0450 -0.1969 188 GLU A N   
1462 C  CA  . GLU A 193 ? 0.7091 1.2456 0.7546 -0.2437 -0.0474 -0.2040 188 GLU A CA  
1463 C  C   . GLU A 193 ? 0.6707 1.1778 0.7039 -0.2223 -0.0577 -0.1856 188 GLU A C   
1464 O  O   . GLU A 193 ? 0.6464 1.1217 0.6589 -0.2329 -0.0528 -0.1844 188 GLU A O   
1465 C  CB  . GLU A 193 ? 0.7273 1.3402 0.7931 -0.2472 -0.0568 -0.2209 188 GLU A CB  
1466 C  CG  . GLU A 193 ? 0.7834 1.4334 0.8714 -0.2484 -0.0521 -0.2310 188 GLU A CG  
1467 C  CD  . GLU A 193 ? 0.8373 1.4650 0.9155 -0.2787 -0.0298 -0.2434 188 GLU A CD  
1468 O  OE1 . GLU A 193 ? 0.8614 1.4481 0.9154 -0.2992 -0.0179 -0.2455 188 GLU A OE1 
1469 O  OE2 . GLU A 193 ? 0.8388 1.4878 0.9318 -0.2811 -0.0236 -0.2507 188 GLU A OE2 
1470 N  N   . GLU A 194 ? 0.6762 1.1926 0.7210 -0.1923 -0.0711 -0.1716 189 GLU A N   
1471 C  CA  . GLU A 194 ? 0.6533 1.1403 0.6860 -0.1718 -0.0799 -0.1538 189 GLU A CA  
1472 C  C   . GLU A 194 ? 0.6394 1.0590 0.6539 -0.1740 -0.0695 -0.1418 189 GLU A C   
1473 O  O   . GLU A 194 ? 0.5924 0.9823 0.5900 -0.1730 -0.0696 -0.1345 189 GLU A O   
1474 C  CB  . GLU A 194 ? 0.6599 1.1660 0.7067 -0.1402 -0.0940 -0.1418 189 GLU A CB  
1475 C  CG  . GLU A 194 ? 0.7208 1.2296 0.7590 -0.1209 -0.1071 -0.1311 189 GLU A CG  
1476 C  CD  . GLU A 194 ? 0.7841 1.3421 0.8379 -0.0972 -0.1222 -0.1303 189 GLU A CD  
1477 O  OE1 . GLU A 194 ? 0.7963 1.3998 0.8694 -0.1009 -0.1230 -0.1433 189 GLU A OE1 
1478 O  OE2 . GLU A 194 ? 0.8199 1.3707 0.8655 -0.0745 -0.1328 -0.1169 189 GLU A OE2 
1479 N  N   . ALA A 195 ? 0.6601 1.0563 0.6778 -0.1760 -0.0609 -0.1396 190 ALA A N   
1480 C  CA  . ALA A 195 ? 0.6539 0.9892 0.6546 -0.1774 -0.0515 -0.1291 190 ALA A CA  
1481 C  C   . ALA A 195 ? 0.6652 0.9740 0.6447 -0.2012 -0.0396 -0.1371 190 ALA A C   
1482 O  O   . ALA A 195 ? 0.6625 0.9312 0.6253 -0.1981 -0.0373 -0.1281 190 ALA A O   
1483 C  CB  . ALA A 195 ? 0.6367 0.9569 0.6438 -0.1772 -0.0443 -0.1278 190 ALA A CB  
1484 N  N   . ILE A 196 ? 0.6562 0.9867 0.6356 -0.2255 -0.0311 -0.1549 191 ILE A N   
1485 C  CA  . ILE A 196 ? 0.6788 0.9805 0.6353 -0.2499 -0.0176 -0.1638 191 ILE A CA  
1486 C  C   . ILE A 196 ? 0.6614 0.9691 0.6086 -0.2500 -0.0237 -0.1639 191 ILE A C   
1487 O  O   . ILE A 196 ? 0.6603 0.9251 0.5862 -0.2541 -0.0171 -0.1594 191 ILE A O   
1488 C  CB  . ILE A 196 ? 0.6922 1.0182 0.6504 -0.2779 -0.0062 -0.1842 191 ILE A CB  
1489 C  CG1 . ILE A 196 ? 0.7244 1.0150 0.6758 -0.2849 0.0072  -0.1833 191 ILE A CG1 
1490 C  CG2 . ILE A 196 ? 0.7019 1.0191 0.6399 -0.3033 0.0035  -0.1972 191 ILE A CG2 
1491 C  CD1 . ILE A 196 ? 0.7411 1.0713 0.7075 -0.3011 0.0130  -0.1995 191 ILE A CD1 
1492 N  N   . SER A 197 ? 0.6192 0.9804 0.5812 -0.2441 -0.0366 -0.1690 192 SER A N   
1493 C  CA  . SER A 197 ? 0.6405 1.0095 0.5922 -0.2447 -0.0426 -0.1699 192 SER A CA  
1494 C  C   . SER A 197 ? 0.6087 0.9417 0.5516 -0.2221 -0.0489 -0.1502 192 SER A C   
1495 O  O   . SER A 197 ? 0.6185 0.9277 0.5434 -0.2270 -0.0461 -0.1487 192 SER A O   
1496 C  CB  . SER A 197 ? 0.6540 1.0906 0.6227 -0.2419 -0.0560 -0.1798 192 SER A CB  
1497 O  OG  . SER A 197 ? 0.7197 1.1698 0.6970 -0.2123 -0.0721 -0.1653 192 SER A OG  
1498 N  N   . LEU A 198 ? 0.6190 0.9455 0.5734 -0.1985 -0.0561 -0.1357 193 LEU A N   
1499 C  CA  . LEU A 198 ? 0.6060 0.8970 0.5515 -0.1796 -0.0602 -0.1182 193 LEU A CA  
1500 C  C   . LEU A 198 ? 0.6188 0.8536 0.5467 -0.1877 -0.0470 -0.1140 193 LEU A C   
1501 O  O   . LEU A 198 ? 0.5997 0.8083 0.5130 -0.1852 -0.0459 -0.1081 193 LEU A O   
1502 C  CB  . LEU A 198 ? 0.6025 0.8977 0.5629 -0.1543 -0.0696 -0.1047 193 LEU A CB  
1503 C  CG  . LEU A 198 ? 0.5577 0.8147 0.5100 -0.1360 -0.0722 -0.0871 193 LEU A CG  
1504 C  CD1 . LEU A 198 ? 0.5908 0.8497 0.5310 -0.1318 -0.0782 -0.0837 193 LEU A CD1 
1505 C  CD2 . LEU A 198 ? 0.5467 0.8084 0.5128 -0.1137 -0.0800 -0.0760 193 LEU A CD2 
1506 N  N   . ALA A 199 ? 0.6081 0.8237 0.5358 -0.1966 -0.0368 -0.1172 194 ALA A N   
1507 C  CA  . ALA A 199 ? 0.6208 0.7825 0.5305 -0.2011 -0.0249 -0.1126 194 ALA A CA  
1508 C  C   . ALA A 199 ? 0.6391 0.7842 0.5275 -0.2215 -0.0148 -0.1227 194 ALA A C   
1509 O  O   . ALA A 199 ? 0.6399 0.7456 0.5117 -0.2192 -0.0094 -0.1167 194 ALA A O   
1510 C  CB  . ALA A 199 ? 0.6636 0.8090 0.5754 -0.2056 -0.0165 -0.1139 194 ALA A CB  
1511 N  N   . LYS A 200 ? 0.6332 0.8081 0.5216 -0.2419 -0.0115 -0.1390 195 LYS A N   
1512 C  CA  . LYS A 200 ? 0.6611 0.8199 0.5277 -0.2632 -0.0010 -0.1500 195 LYS A CA  
1513 C  C   . LYS A 200 ? 0.6371 0.8009 0.4977 -0.2559 -0.0088 -0.1459 195 LYS A C   
1514 O  O   . LYS A 200 ? 0.6624 0.7894 0.5026 -0.2605 -0.0009 -0.1447 195 LYS A O   
1515 C  CB  . LYS A 200 ? 0.6606 0.8544 0.5298 -0.2885 0.0045  -0.1700 195 LYS A CB  
1516 C  CG  . LYS A 200 ? 0.7025 0.8939 0.5524 -0.3101 0.0117  -0.1830 195 LYS A CG  
1517 C  CD  . LYS A 200 ? 0.7478 0.9621 0.5958 -0.3398 0.0220  -0.2041 195 LYS A CD  
1518 C  CE  . LYS A 200 ? 0.8081 0.9980 0.6285 -0.3643 0.0353  -0.2165 195 LYS A CE  
1519 N  NZ  . LYS A 200 ? 0.8756 0.9946 0.6690 -0.3671 0.0515  -0.2103 195 LYS A NZ  
1520 N  N   . THR A 201 ? 0.6297 0.8381 0.5066 -0.2437 -0.0240 -0.1437 196 THR A N   
1521 C  CA  . THR A 201 ? 0.5836 0.7959 0.4533 -0.2353 -0.0318 -0.1386 196 THR A CA  
1522 C  C   . THR A 201 ? 0.5998 0.7665 0.4605 -0.2189 -0.0302 -0.1224 196 THR A C   
1523 O  O   . THR A 201 ? 0.6259 0.7719 0.4703 -0.2213 -0.0269 -0.1213 196 THR A O   
1524 C  CB  . THR A 201 ? 0.5972 0.8601 0.4842 -0.2202 -0.0490 -0.1361 196 THR A CB  
1525 O  OG1 . THR A 201 ? 0.6739 0.9852 0.5698 -0.2359 -0.0510 -0.1531 196 THR A OG1 
1526 C  CG2 . THR A 201 ? 0.6353 0.8977 0.5116 -0.2101 -0.0568 -0.1291 196 THR A CG2 
1527 N  N   . THR A 202 ? 0.6181 0.7715 0.4901 -0.2022 -0.0328 -0.1104 197 THR A N   
1528 C  CA  . THR A 202 ? 0.6073 0.7221 0.4734 -0.1870 -0.0314 -0.0962 197 THR A CA  
1529 C  C   . THR A 202 ? 0.6139 0.6836 0.4602 -0.1980 -0.0169 -0.0990 197 THR A C   
1530 O  O   . THR A 202 ? 0.5938 0.6391 0.4282 -0.1934 -0.0143 -0.0940 197 THR A O   
1531 C  CB  . THR A 202 ? 0.5676 0.6785 0.4495 -0.1698 -0.0360 -0.0852 197 THR A CB  
1532 O  OG1 . THR A 202 ? 0.5538 0.7044 0.4517 -0.1585 -0.0489 -0.0827 197 THR A OG1 
1533 C  CG2 . THR A 202 ? 0.5438 0.6206 0.4212 -0.1551 -0.0352 -0.0719 197 THR A CG2 
1534 N  N   . PHE A 203 ? 0.6067 0.6633 0.4481 -0.2116 -0.0068 -0.1070 198 PHE A N   
1535 C  CA  . PHE A 203 ? 0.6356 0.6457 0.4547 -0.2207 0.0077  -0.1094 198 PHE A CA  
1536 C  C   . PHE A 203 ? 0.6446 0.6498 0.4450 -0.2354 0.0135  -0.1188 198 PHE A C   
1537 O  O   . PHE A 203 ? 0.6534 0.6253 0.4385 -0.2316 0.0194  -0.1149 198 PHE A O   
1538 C  CB  . PHE A 203 ? 0.6593 0.6556 0.4727 -0.2344 0.0184  -0.1171 198 PHE A CB  
1539 C  CG  . PHE A 203 ? 0.6723 0.6162 0.4588 -0.2420 0.0338  -0.1190 198 PHE A CG  
1540 C  CD1 . PHE A 203 ? 0.7215 0.6283 0.5032 -0.2264 0.0366  -0.1078 198 PHE A CD1 
1541 C  CD2 . PHE A 203 ? 0.7318 0.6630 0.4966 -0.2639 0.0456  -0.1322 198 PHE A CD2 
1542 C  CE1 . PHE A 203 ? 0.7673 0.6254 0.5226 -0.2303 0.0503  -0.1089 198 PHE A CE1 
1543 C  CE2 . PHE A 203 ? 0.7817 0.6608 0.5190 -0.2691 0.0604  -0.1334 198 PHE A CE2 
1544 C  CZ  . PHE A 203 ? 0.7515 0.5938 0.4837 -0.2511 0.0625  -0.1214 198 PHE A CZ  
1545 N  N   . ASP A 204 ? 0.6526 0.6923 0.4544 -0.2525 0.0122  -0.1321 199 ASP A N   
1546 C  CA  . ASP A 204 ? 0.6399 0.6753 0.4224 -0.2694 0.0186  -0.1429 199 ASP A CA  
1547 C  C   . ASP A 204 ? 0.6461 0.6829 0.4264 -0.2562 0.0109  -0.1348 199 ASP A C   
1548 O  O   . ASP A 204 ? 0.6656 0.6757 0.4259 -0.2624 0.0191  -0.1376 199 ASP A O   
1549 C  CB  . ASP A 204 ? 0.6554 0.7356 0.4429 -0.2899 0.0168  -0.1595 199 ASP A CB  
1550 C  CG  . ASP A 204 ? 0.7402 0.8128 0.5230 -0.3099 0.0292  -0.1713 199 ASP A CG  
1551 O  OD1 . ASP A 204 ? 0.7174 0.7416 0.4846 -0.3113 0.0419  -0.1682 199 ASP A OD1 
1552 O  OD2 . ASP A 204 ? 0.7566 0.8728 0.5509 -0.3239 0.0264  -0.1840 199 ASP A OD2 
1553 N  N   . GLU A 205 ? 0.6368 0.7022 0.4357 -0.2378 -0.0038 -0.1246 200 GLU A N   
1554 C  CA  . GLU A 205 ? 0.6622 0.7290 0.4569 -0.2264 -0.0105 -0.1171 200 GLU A CA  
1555 C  C   . GLU A 205 ? 0.6387 0.6620 0.4264 -0.2131 -0.0047 -0.1055 200 GLU A C   
1556 O  O   . GLU A 205 ? 0.6360 0.6450 0.4110 -0.2117 -0.0023 -0.1039 200 GLU A O   
1557 C  CB  . GLU A 205 ? 0.6215 0.7288 0.4344 -0.2109 -0.0271 -0.1100 200 GLU A CB  
1558 C  CG  . GLU A 205 ? 0.6563 0.8109 0.4718 -0.2231 -0.0341 -0.1227 200 GLU A CG  
1559 C  CD  . GLU A 205 ? 0.6801 0.8735 0.5093 -0.2053 -0.0509 -0.1154 200 GLU A CD  
1560 O  OE1 . GLU A 205 ? 0.6723 0.8531 0.5082 -0.1850 -0.0560 -0.1004 200 GLU A OE1 
1561 O  OE2 . GLU A 205 ? 0.6861 0.9218 0.5175 -0.2115 -0.0589 -0.1248 200 GLU A OE2 
1562 N  N   . ALA A 206 ? 0.6195 0.6228 0.4152 -0.2038 -0.0021 -0.0983 201 ALA A N   
1563 C  CA  . ALA A 206 ? 0.6359 0.5995 0.4248 -0.1924 0.0044  -0.0896 201 ALA A CA  
1564 C  C   . ALA A 206 ? 0.6538 0.5824 0.4188 -0.2054 0.0190  -0.0979 201 ALA A C   
1565 O  O   . ALA A 206 ? 0.6583 0.5629 0.4127 -0.1993 0.0237  -0.0945 201 ALA A O   
1566 C  CB  . ALA A 206 ? 0.6107 0.5628 0.4122 -0.1807 0.0037  -0.0816 201 ALA A CB  
1567 N  N   . MET A 207 ? 0.6588 0.5839 0.4137 -0.2240 0.0271  -0.1098 202 MET A N   
1568 C  CA  . MET A 207 ? 0.6873 0.5733 0.4159 -0.2366 0.0426  -0.1178 202 MET A CA  
1569 C  C   . MET A 207 ? 0.6957 0.5871 0.4108 -0.2465 0.0444  -0.1250 202 MET A C   
1570 O  O   . MET A 207 ? 0.7132 0.5712 0.4098 -0.2456 0.0538  -0.1254 202 MET A O   
1571 C  CB  . MET A 207 ? 0.6998 0.5807 0.4195 -0.2564 0.0518  -0.1295 202 MET A CB  
1572 C  CG  . MET A 207 ? 0.7296 0.5843 0.4518 -0.2455 0.0552  -0.1216 202 MET A CG  
1573 S  SD  . MET A 207 ? 0.8547 0.6463 0.5518 -0.2362 0.0691  -0.1165 202 MET A SD  
1574 C  CE  . MET A 207 ? 0.8621 0.6237 0.5248 -0.2629 0.0873  -0.1329 202 MET A CE  
1575 N  N   . ALA A 208 ? 0.6857 0.6201 0.4094 -0.2548 0.0350  -0.1309 203 ALA A N   
1576 C  CA  . ALA A 208 ? 0.7102 0.6538 0.4208 -0.2645 0.0354  -0.1381 203 ALA A CA  
1577 C  C   . ALA A 208 ? 0.6977 0.6286 0.4068 -0.2472 0.0324  -0.1270 203 ALA A C   
1578 O  O   . ALA A 208 ? 0.7567 0.6717 0.4476 -0.2535 0.0392  -0.1317 203 ALA A O   
1579 C  CB  . ALA A 208 ? 0.7011 0.6983 0.4237 -0.2725 0.0232  -0.1449 203 ALA A CB  
1580 N  N   . ASP A 209 ? 0.6685 0.6047 0.3957 -0.2264 0.0235  -0.1129 204 ASP A N   
1581 C  CA  . ASP A 209 ? 0.6921 0.6172 0.4186 -0.2112 0.0217  -0.1030 204 ASP A CA  
1582 C  C   . ASP A 209 ? 0.6672 0.5595 0.3975 -0.1964 0.0274  -0.0940 204 ASP A C   
1583 O  O   . ASP A 209 ? 0.6390 0.5333 0.3819 -0.1796 0.0217  -0.0828 204 ASP A O   
1584 C  CB  . ASP A 209 ? 0.6424 0.6024 0.3835 -0.2000 0.0067  -0.0947 204 ASP A CB  
1585 C  CG  . ASP A 209 ? 0.6887 0.6761 0.4199 -0.2110 0.0015  -0.1025 204 ASP A CG  
1586 O  OD1 . ASP A 209 ? 0.7036 0.6766 0.4153 -0.2234 0.0102  -0.1111 204 ASP A OD1 
1587 O  OD2 . ASP A 209 ? 0.6602 0.6836 0.4020 -0.2067 -0.0113 -0.1002 204 ASP A OD2 
1588 N  N   . LEU A 210 ? 0.6757 0.5363 0.3930 -0.2029 0.0394  -0.0995 205 LEU A N   
1589 C  CA  . LEU A 210 ? 0.6781 0.5086 0.3976 -0.1883 0.0444  -0.0920 205 LEU A CA  
1590 C  C   . LEU A 210 ? 0.6806 0.4958 0.3982 -0.1744 0.0468  -0.0858 205 LEU A C   
1591 O  O   . LEU A 210 ? 0.6808 0.4880 0.4098 -0.1579 0.0451  -0.0770 205 LEU A O   
1592 C  CB  . LEU A 210 ? 0.7124 0.5081 0.4117 -0.1984 0.0579  -0.0998 205 LEU A CB  
1593 C  CG  . LEU A 210 ? 0.7237 0.4875 0.4215 -0.1843 0.0631  -0.0933 205 LEU A CG  
1594 C  CD1 . LEU A 210 ? 0.7371 0.5203 0.4563 -0.1773 0.0535  -0.0865 205 LEU A CD1 
1595 C  CD2 . LEU A 210 ? 0.7819 0.5046 0.4508 -0.1958 0.0788  -0.1021 205 LEU A CD2 
1596 N  N   . HIS A 211 ? 0.6890 0.5025 0.3929 -0.1814 0.0508  -0.0910 206 HIS A N   
1597 C  CA  . HIS A 211 ? 0.6968 0.4988 0.3987 -0.1699 0.0540  -0.0866 206 HIS A CA  
1598 C  C   . HIS A 211 ? 0.6621 0.4864 0.3855 -0.1553 0.0434  -0.0753 206 HIS A C   
1599 O  O   . HIS A 211 ? 0.6616 0.4771 0.3862 -0.1450 0.0466  -0.0714 206 HIS A O   
1600 C  CB  . HIS A 211 ? 0.7190 0.5212 0.4026 -0.1823 0.0588  -0.0947 206 HIS A CB  
1601 C  CG  . HIS A 211 ? 0.7021 0.5409 0.3907 -0.1907 0.0479  -0.0957 206 HIS A CG  
1602 N  ND1 . HIS A 211 ? 0.7134 0.5702 0.4075 -0.1836 0.0407  -0.0894 206 HIS A ND1 
1603 C  CD2 . HIS A 211 ? 0.7262 0.5879 0.4148 -0.2045 0.0425  -0.1023 206 HIS A CD2 
1604 C  CE1 . HIS A 211 ? 0.7163 0.6039 0.4117 -0.1913 0.0310  -0.0914 206 HIS A CE1 
1605 N  NE2 . HIS A 211 ? 0.6974 0.5910 0.3910 -0.2039 0.0315  -0.0997 206 HIS A NE2 
1606 N  N   . THR A 212 ? 0.6412 0.4937 0.3799 -0.1547 0.0317  -0.0708 207 THR A N   
1607 C  CA  . THR A 212 ? 0.6204 0.4904 0.3762 -0.1416 0.0225  -0.0602 207 THR A CA  
1608 C  C   . THR A 212 ? 0.6342 0.4965 0.4062 -0.1279 0.0212  -0.0529 207 THR A C   
1609 O  O   . THR A 212 ? 0.6183 0.4936 0.4051 -0.1179 0.0143  -0.0445 207 THR A O   
1610 C  CB  . THR A 212 ? 0.6231 0.5256 0.3859 -0.1450 0.0105  -0.0584 207 THR A CB  
1611 O  OG1 . THR A 212 ? 0.6150 0.5273 0.3868 -0.1482 0.0065  -0.0602 207 THR A OG1 
1612 C  CG2 . THR A 212 ? 0.6255 0.5391 0.3716 -0.1585 0.0106  -0.0664 207 THR A CG2 
1613 N  N   . LEU A 213 ? 0.6175 0.4582 0.3853 -0.1274 0.0280  -0.0560 208 LEU A N   
1614 C  CA  . LEU A 213 ? 0.6312 0.4646 0.4127 -0.1136 0.0266  -0.0494 208 LEU A CA  
1615 C  C   . LEU A 213 ? 0.6402 0.4711 0.4287 -0.1013 0.0281  -0.0445 208 LEU A C   
1616 O  O   . LEU A 213 ? 0.6269 0.4474 0.4042 -0.1025 0.0353  -0.0482 208 LEU A O   
1617 C  CB  . LEU A 213 ? 0.6578 0.4633 0.4280 -0.1137 0.0349  -0.0535 208 LEU A CB  
1618 C  CG  . LEU A 213 ? 0.6455 0.4505 0.4111 -0.1247 0.0347  -0.0578 208 LEU A CG  
1619 C  CD1 . LEU A 213 ? 0.6877 0.4562 0.4334 -0.1261 0.0462  -0.0626 208 LEU A CD1 
1620 C  CD2 . LEU A 213 ? 0.6035 0.4268 0.3893 -0.1180 0.0250  -0.0511 208 LEU A CD2 
1621 N  N   . SER A 214 ? 0.6224 0.4635 0.4293 -0.0904 0.0220  -0.0371 209 SER A N   
1622 C  CA  . SER A 214 ? 0.6511 0.4943 0.4675 -0.0803 0.0233  -0.0332 209 SER A CA  
1623 C  C   . SER A 214 ? 0.6629 0.4913 0.4838 -0.0685 0.0277  -0.0335 209 SER A C   
1624 O  O   . SER A 214 ? 0.6276 0.4512 0.4524 -0.0647 0.0251  -0.0321 209 SER A O   
1625 C  CB  . SER A 214 ? 0.6733 0.5368 0.5058 -0.0766 0.0145  -0.0257 209 SER A CB  
1626 O  OG  . SER A 214 ? 0.7112 0.5764 0.5544 -0.0678 0.0166  -0.0228 209 SER A OG  
1627 N  N   . GLU A 215 ? 0.6548 0.4773 0.4749 -0.0620 0.0342  -0.0355 210 GLU A N   
1628 C  CA  . GLU A 215 ? 0.7041 0.5164 0.5292 -0.0482 0.0376  -0.0362 210 GLU A CA  
1629 C  C   . GLU A 215 ? 0.6896 0.5145 0.5342 -0.0396 0.0300  -0.0307 210 GLU A C   
1630 O  O   . GLU A 215 ? 0.6791 0.4944 0.5248 -0.0297 0.0300  -0.0307 210 GLU A O   
1631 C  CB  . GLU A 215 ? 0.7408 0.5543 0.5679 -0.0418 0.0445  -0.0391 210 GLU A CB  
1632 C  CG  . GLU A 215 ? 0.7696 0.5701 0.5776 -0.0490 0.0531  -0.0450 210 GLU A CG  
1633 C  CD  . GLU A 215 ? 0.8366 0.6420 0.6494 -0.0425 0.0598  -0.0479 210 GLU A CD  
1634 O  OE1 . GLU A 215 ? 0.8250 0.6309 0.6477 -0.0283 0.0616  -0.0489 210 GLU A OE1 
1635 O  OE2 . GLU A 215 ? 0.8657 0.6753 0.6719 -0.0511 0.0634  -0.0498 210 GLU A OE2 
1636 N  N   . ASP A 216 ? 0.6426 0.4873 0.5008 -0.0426 0.0237  -0.0261 211 ASP A N   
1637 C  CA  . ASP A 216 ? 0.6538 0.5101 0.5303 -0.0349 0.0176  -0.0218 211 ASP A CA  
1638 C  C   . ASP A 216 ? 0.6403 0.4971 0.5186 -0.0374 0.0106  -0.0184 211 ASP A C   
1639 O  O   . ASP A 216 ? 0.6096 0.4737 0.5012 -0.0312 0.0057  -0.0153 211 ASP A O   
1640 C  CB  . ASP A 216 ? 0.7350 0.6087 0.6240 -0.0364 0.0161  -0.0189 211 ASP A CB  
1641 C  CG  . ASP A 216 ? 0.7574 0.6368 0.6401 -0.0467 0.0128  -0.0155 211 ASP A CG  
1642 O  OD1 . ASP A 216 ? 0.8683 0.7533 0.7501 -0.0500 0.0155  -0.0146 211 ASP A OD1 
1643 O  OD2 . ASP A 216 ? 0.8246 0.7036 0.7028 -0.0511 0.0077  -0.0138 211 ASP A OD2 
1644 N  N   . SER A 217 ? 0.6437 0.4943 0.5091 -0.0469 0.0104  -0.0198 212 SER A N   
1645 C  CA  . SER A 217 ? 0.6068 0.4620 0.4755 -0.0502 0.0041  -0.0174 212 SER A CA  
1646 C  C   . SER A 217 ? 0.5857 0.4260 0.4381 -0.0579 0.0077  -0.0220 212 SER A C   
1647 O  O   . SER A 217 ? 0.5672 0.4134 0.4216 -0.0631 0.0034  -0.0214 212 SER A O   
1648 C  CB  . SER A 217 ? 0.5829 0.4569 0.4578 -0.0561 -0.0022 -0.0137 212 SER A CB  
1649 O  OG  . SER A 217 ? 0.5974 0.4725 0.4595 -0.0651 0.0003  -0.0168 212 SER A OG  
1650 N  N   . TYR A 218 ? 0.6040 0.4249 0.4400 -0.0594 0.0160  -0.0272 213 TYR A N   
1651 C  CA  . TYR A 218 ? 0.6136 0.4190 0.4311 -0.0704 0.0211  -0.0328 213 TYR A CA  
1652 C  C   . TYR A 218 ? 0.6285 0.4216 0.4434 -0.0680 0.0209  -0.0321 213 TYR A C   
1653 O  O   . TYR A 218 ? 0.6426 0.4331 0.4491 -0.0797 0.0222  -0.0356 213 TYR A O   
1654 C  CB  . TYR A 218 ? 0.6285 0.4106 0.4260 -0.0718 0.0316  -0.0386 213 TYR A CB  
1655 C  CG  . TYR A 218 ? 0.6675 0.4265 0.4588 -0.0575 0.0371  -0.0383 213 TYR A CG  
1656 C  CD1 . TYR A 218 ? 0.7000 0.4313 0.4735 -0.0569 0.0426  -0.0404 213 TYR A CD1 
1657 C  CD2 . TYR A 218 ? 0.6857 0.4503 0.4873 -0.0442 0.0371  -0.0364 213 TYR A CD2 
1658 C  CE1 . TYR A 218 ? 0.7070 0.4158 0.4721 -0.0411 0.0470  -0.0395 213 TYR A CE1 
1659 C  CE2 . TYR A 218 ? 0.7182 0.4654 0.5149 -0.0289 0.0411  -0.0366 213 TYR A CE2 
1660 C  CZ  . TYR A 218 ? 0.7457 0.4644 0.5234 -0.0263 0.0456  -0.0377 213 TYR A CZ  
1661 O  OH  . TYR A 218 ? 0.7692 0.4698 0.5397 -0.0087 0.0490  -0.0373 213 TYR A OH  
1662 N  N   . LYS A 219 ? 0.5932 0.3808 0.4155 -0.0537 0.0192  -0.0280 214 LYS A N   
1663 C  CA  . LYS A 219 ? 0.6515 0.4266 0.4695 -0.0509 0.0188  -0.0268 214 LYS A CA  
1664 C  C   . LYS A 219 ? 0.6171 0.4131 0.4486 -0.0577 0.0113  -0.0245 214 LYS A C   
1665 O  O   . LYS A 219 ? 0.6279 0.4158 0.4516 -0.0644 0.0129  -0.0264 214 LYS A O   
1666 C  CB  . LYS A 219 ? 0.6629 0.4314 0.4864 -0.0330 0.0173  -0.0231 214 LYS A CB  
1667 C  CG  . LYS A 219 ? 0.6865 0.4324 0.4943 -0.0242 0.0254  -0.0260 214 LYS A CG  
1668 C  CD  . LYS A 219 ? 0.7985 0.5379 0.6091 -0.0049 0.0236  -0.0233 214 LYS A CD  
1669 C  CE  . LYS A 219 ? 0.8070 0.5682 0.6367 0.0053  0.0207  -0.0230 214 LYS A CE  
1670 N  NZ  . LYS A 219 ? 0.8855 0.6526 0.7254 0.0227  0.0158  -0.0207 214 LYS A NZ  
1671 N  N   . ASP A 220 ? 0.6055 0.4275 0.4561 -0.0561 0.0038  -0.0207 215 ASP A N   
1672 C  CA  . ASP A 220 ? 0.5860 0.4283 0.4488 -0.0610 -0.0033 -0.0185 215 ASP A CA  
1673 C  C   . ASP A 220 ? 0.5656 0.4150 0.4203 -0.0759 -0.0019 -0.0238 215 ASP A C   
1674 O  O   . ASP A 220 ? 0.5429 0.3986 0.3988 -0.0823 -0.0035 -0.0256 215 ASP A O   
1675 C  CB  . ASP A 220 ? 0.5773 0.4409 0.4581 -0.0553 -0.0102 -0.0131 215 ASP A CB  
1676 C  CG  . ASP A 220 ? 0.6306 0.4932 0.5230 -0.0428 -0.0127 -0.0090 215 ASP A CG  
1677 O  OD1 . ASP A 220 ? 0.6679 0.5170 0.5562 -0.0375 -0.0111 -0.0095 215 ASP A OD1 
1678 O  OD2 . ASP A 220 ? 0.6703 0.5457 0.5748 -0.0388 -0.0159 -0.0057 215 ASP A OD2 
1679 N  N   . SER A 221 ? 0.5515 0.4028 0.3985 -0.0820 0.0008  -0.0270 216 SER A N   
1680 C  CA  . SER A 221 ? 0.5394 0.4003 0.3783 -0.0968 0.0018  -0.0334 216 SER A CA  
1681 C  C   . SER A 221 ? 0.5821 0.4248 0.4059 -0.1069 0.0094  -0.0401 216 SER A C   
1682 O  O   . SER A 221 ? 0.5681 0.4245 0.3937 -0.1172 0.0079  -0.0442 216 SER A O   
1683 C  CB  . SER A 221 ? 0.5390 0.3995 0.3681 -0.1016 0.0051  -0.0365 216 SER A CB  
1684 O  OG  . SER A 221 ? 0.5573 0.4331 0.3982 -0.0936 -0.0011 -0.0303 216 SER A OG  
1685 N  N   . THR A 222 ? 0.5900 0.4012 0.3977 -0.1037 0.0181  -0.0415 217 THR A N   
1686 C  CA  . THR A 222 ? 0.6359 0.4240 0.4235 -0.1150 0.0274  -0.0482 217 THR A CA  
1687 C  C   . THR A 222 ? 0.6206 0.4076 0.4130 -0.1136 0.0256  -0.0461 217 THR A C   
1688 O  O   . THR A 222 ? 0.6323 0.4127 0.4136 -0.1272 0.0314  -0.0525 217 THR A O   
1689 C  CB  . THR A 222 ? 0.6602 0.4106 0.4251 -0.1106 0.0381  -0.0500 217 THR A CB  
1690 O  OG1 . THR A 222 ? 0.6994 0.4400 0.4704 -0.0911 0.0355  -0.0427 217 THR A OG1 
1691 C  CG2 . THR A 222 ? 0.6992 0.4509 0.4573 -0.1155 0.0413  -0.0540 217 THR A CG2 
1692 N  N   . LEU A 223 ? 0.5860 0.3812 0.3951 -0.0987 0.0180  -0.0381 218 LEU A N   
1693 C  CA  . LEU A 223 ? 0.6244 0.4221 0.4395 -0.0976 0.0154  -0.0361 218 LEU A CA  
1694 C  C   . LEU A 223 ? 0.6070 0.4357 0.4349 -0.1091 0.0106  -0.0396 218 LEU A C   
1695 O  O   . LEU A 223 ? 0.5791 0.4058 0.4015 -0.1195 0.0146  -0.0444 218 LEU A O   
1696 C  CB  . LEU A 223 ? 0.6259 0.4280 0.4565 -0.0799 0.0080  -0.0276 218 LEU A CB  
1697 C  CG  . LEU A 223 ? 0.6143 0.4237 0.4544 -0.0777 0.0037  -0.0250 218 LEU A CG  
1698 C  CD1 . LEU A 223 ? 0.6917 0.4759 0.5114 -0.0855 0.0123  -0.0291 218 LEU A CD1 
1699 C  CD2 . LEU A 223 ? 0.6577 0.4679 0.5096 -0.0610 -0.0022 -0.0179 218 LEU A CD2 
1700 N  N   . ILE A 224 ? 0.5788 0.4364 0.4229 -0.1073 0.0025  -0.0376 219 ILE A N   
1701 C  CA  . ILE A 224 ? 0.5464 0.4358 0.4027 -0.1153 -0.0031 -0.0408 219 ILE A CA  
1702 C  C   . ILE A 224 ? 0.5700 0.4618 0.4131 -0.1344 0.0037  -0.0518 219 ILE A C   
1703 O  O   . ILE A 224 ? 0.5749 0.4847 0.4229 -0.1442 0.0035  -0.0576 219 ILE A O   
1704 C  CB  . ILE A 224 ? 0.5527 0.4685 0.4244 -0.1077 -0.0129 -0.0357 219 ILE A CB  
1705 C  CG1 . ILE A 224 ? 0.5443 0.4562 0.4279 -0.0913 -0.0180 -0.0260 219 ILE A CG1 
1706 C  CG2 . ILE A 224 ? 0.5494 0.4991 0.4333 -0.1126 -0.0196 -0.0386 219 ILE A CG2 
1707 C  CD1 . ILE A 224 ? 0.5638 0.4766 0.4570 -0.0859 -0.0205 -0.0231 219 ILE A CD1 
1708 N  N   . MET A 225 ? 0.5804 0.4559 0.4070 -0.1405 0.0102  -0.0559 220 MET A N   
1709 C  CA  . MET A 225 ? 0.5983 0.4735 0.4100 -0.1606 0.0181  -0.0677 220 MET A CA  
1710 C  C   . MET A 225 ? 0.6365 0.4917 0.4359 -0.1708 0.0275  -0.0730 220 MET A C   
1711 O  O   . MET A 225 ? 0.6496 0.5214 0.4488 -0.1873 0.0304  -0.0825 220 MET A O   
1712 C  CB  . MET A 225 ? 0.6474 0.5006 0.4402 -0.1646 0.0254  -0.0708 220 MET A CB  
1713 C  CG  . MET A 225 ? 0.6334 0.5111 0.4359 -0.1602 0.0172  -0.0684 220 MET A CG  
1714 S  SD  . MET A 225 ? 0.6721 0.5228 0.4545 -0.1606 0.0253  -0.0702 220 MET A SD  
1715 C  CE  . MET A 225 ? 0.6845 0.5215 0.4424 -0.1856 0.0379  -0.0853 220 MET A CE  
1716 N  N   . GLN A 226 ? 0.6371 0.4578 0.4259 -0.1608 0.0324  -0.0673 221 GLN A N   
1717 C  CA  . GLN A 226 ? 0.7018 0.4988 0.4756 -0.1688 0.0417  -0.0709 221 GLN A CA  
1718 C  C   . GLN A 226 ? 0.6979 0.5229 0.4908 -0.1702 0.0357  -0.0708 221 GLN A C   
1719 O  O   . GLN A 226 ? 0.7179 0.5409 0.5029 -0.1856 0.0432  -0.0787 221 GLN A O   
1720 C  CB  . GLN A 226 ? 0.7344 0.4899 0.4924 -0.1540 0.0463  -0.0635 221 GLN A CB  
1721 C  CG  . GLN A 226 ? 0.8098 0.5329 0.5456 -0.1612 0.0571  -0.0664 221 GLN A CG  
1722 C  CD  . GLN A 226 ? 0.8320 0.5340 0.5415 -0.1833 0.0715  -0.0779 221 GLN A CD  
1723 O  OE1 . GLN A 226 ? 0.8675 0.5478 0.5596 -0.1850 0.0779  -0.0804 221 GLN A OE1 
1724 N  NE2 . GLN A 226 ? 0.9119 0.6202 0.6180 -0.2012 0.0775  -0.0859 221 GLN A NE2 
1725 N  N   . LEU A 227 ? 0.6417 0.4921 0.4590 -0.1550 0.0231  -0.0625 222 LEU A N   
1726 C  CA  . LEU A 227 ? 0.6711 0.5477 0.5066 -0.1548 0.0176  -0.0624 222 LEU A CA  
1727 C  C   . LEU A 227 ? 0.6598 0.5749 0.5059 -0.1693 0.0154  -0.0721 222 LEU A C   
1728 O  O   . LEU A 227 ? 0.6426 0.5730 0.4943 -0.1783 0.0174  -0.0781 222 LEU A O   
1729 C  CB  . LEU A 227 ? 0.5938 0.4844 0.4501 -0.1350 0.0058  -0.0515 222 LEU A CB  
1730 C  CG  . LEU A 227 ? 0.6187 0.4793 0.4689 -0.1199 0.0062  -0.0428 222 LEU A CG  
1731 C  CD1 . LEU A 227 ? 0.5920 0.4705 0.4640 -0.1037 -0.0048 -0.0340 222 LEU A CD1 
1732 C  CD2 . LEU A 227 ? 0.6572 0.4918 0.4920 -0.1241 0.0144  -0.0446 222 LEU A CD2 
1733 N  N   . LEU A 228 ? 0.6346 0.5675 0.4834 -0.1717 0.0114  -0.0744 223 LEU A N   
1734 C  CA  . LEU A 228 ? 0.6373 0.6065 0.4927 -0.1867 0.0100  -0.0854 223 LEU A CA  
1735 C  C   . LEU A 228 ? 0.6846 0.6414 0.5224 -0.2098 0.0236  -0.0985 223 LEU A C   
1736 O  O   . LEU A 228 ? 0.6985 0.6845 0.5455 -0.2222 0.0243  -0.1079 223 LEU A O   
1737 C  CB  . LEU A 228 ? 0.6018 0.5848 0.4564 -0.1866 0.0050  -0.0862 223 LEU A CB  
1738 C  CG  . LEU A 228 ? 0.5868 0.5889 0.4586 -0.1669 -0.0084 -0.0751 223 LEU A CG  
1739 C  CD1 . LEU A 228 ? 0.5736 0.5746 0.4370 -0.1666 -0.0100 -0.0746 223 LEU A CD1 
1740 C  CD2 . LEU A 228 ? 0.5671 0.6133 0.4595 -0.1640 -0.0183 -0.0769 223 LEU A CD2 
1741 N  N   . ARG A 229 ? 0.6769 0.5903 0.4887 -0.2160 0.0353  -0.0998 224 ARG A N   
1742 C  CA  . ARG A 229 ? 0.7215 0.6161 0.5117 -0.2392 0.0504  -0.1123 224 ARG A CA  
1743 C  C   . ARG A 229 ? 0.7858 0.6692 0.5741 -0.2420 0.0562  -0.1126 224 ARG A C   
1744 O  O   . ARG A 229 ? 0.8236 0.7131 0.6053 -0.2631 0.0657  -0.1248 224 ARG A O   
1745 C  CB  . ARG A 229 ? 0.7821 0.6274 0.5414 -0.2427 0.0622  -0.1126 224 ARG A CB  
1746 C  CG  . ARG A 229 ? 0.8698 0.7240 0.6200 -0.2582 0.0657  -0.1228 224 ARG A CG  
1747 C  CD  . ARG A 229 ? 0.8761 0.7045 0.5983 -0.2845 0.0835  -0.1370 224 ARG A CD  
1748 N  NE  . ARG A 229 ? 0.9897 0.8092 0.6950 -0.2964 0.0894  -0.1448 224 ARG A NE  
1749 C  CZ  . ARG A 229 ? 1.0312 0.7991 0.7054 -0.2985 0.1023  -0.1450 224 ARG A CZ  
1750 N  NH1 . ARG A 229 ? 1.0714 0.7912 0.7266 -0.2881 0.1101  -0.1373 224 ARG A NH1 
1751 N  NH2 . ARG A 229 ? 1.0590 0.8232 0.7193 -0.3107 0.1074  -0.1534 224 ARG A NH2 
1752 N  N   . ASP A 230 ? 0.7660 0.6334 0.5592 -0.2223 0.0513  -0.1001 225 ASP A N   
1753 C  CA  . ASP A 230 ? 0.7927 0.6516 0.5849 -0.2236 0.0556  -0.0997 225 ASP A CA  
1754 C  C   . ASP A 230 ? 0.7941 0.7032 0.6120 -0.2305 0.0498  -0.1065 225 ASP A C   
1755 O  O   . ASP A 230 ? 0.7960 0.7076 0.6089 -0.2470 0.0590  -0.1159 225 ASP A O   
1756 C  CB  . ASP A 230 ? 0.7628 0.6015 0.5581 -0.2000 0.0493  -0.0853 225 ASP A CB  
1757 C  CG  . ASP A 230 ? 0.7677 0.5571 0.5370 -0.1915 0.0555  -0.0791 225 ASP A CG  
1758 O  OD1 . ASP A 230 ? 0.8860 0.6482 0.6301 -0.2048 0.0674  -0.0859 225 ASP A OD1 
1759 O  OD2 . ASP A 230 ? 0.8125 0.5909 0.5866 -0.1710 0.0487  -0.0680 225 ASP A OD2 
1760 N  N   . ASN A 231 ? 0.7399 0.6886 0.5845 -0.2174 0.0351  -0.1020 226 ASN A N   
1761 C  CA  . ASN A 231 ? 0.7623 0.7612 0.6317 -0.2208 0.0285  -0.1083 226 ASN A CA  
1762 C  C   . ASN A 231 ? 0.7823 0.8067 0.6492 -0.2454 0.0352  -0.1252 226 ASN A C   
1763 O  O   . ASN A 231 ? 0.8025 0.8535 0.6791 -0.2573 0.0386  -0.1352 226 ASN A O   
1764 C  CB  . ASN A 231 ? 0.7147 0.7459 0.6079 -0.2009 0.0120  -0.0997 226 ASN A CB  
1765 C  CG  . ASN A 231 ? 0.6765 0.6966 0.5794 -0.1796 0.0052  -0.0863 226 ASN A CG  
1766 O  OD1 . ASN A 231 ? 0.7000 0.6973 0.5961 -0.1797 0.0113  -0.0845 226 ASN A OD1 
1767 N  ND2 . ASN A 231 ? 0.6334 0.6687 0.5507 -0.1621 -0.0069 -0.0773 226 ASN A ND2 
1768 N  N   . LEU A 232 ? 0.7595 0.7788 0.6142 -0.2540 0.0375  -0.1297 227 LEU A N   
1769 C  CA  . LEU A 232 ? 0.7829 0.8266 0.6339 -0.2793 0.0444  -0.1472 227 LEU A CA  
1770 C  C   . LEU A 232 ? 0.8582 0.8750 0.6886 -0.3021 0.0625  -0.1577 227 LEU A C   
1771 O  O   . LEU A 232 ? 0.8714 0.9192 0.7077 -0.3227 0.0681  -0.1731 227 LEU A O   
1772 C  CB  . LEU A 232 ? 0.7636 0.7992 0.6011 -0.2846 0.0448  -0.1497 227 LEU A CB  
1773 C  CG  . LEU A 232 ? 0.7291 0.8039 0.5876 -0.2682 0.0275  -0.1439 227 LEU A CG  
1774 C  CD1 . LEU A 232 ? 0.7260 0.7836 0.5685 -0.2697 0.0283  -0.1431 227 LEU A CD1 
1775 C  CD2 . LEU A 232 ? 0.7371 0.8738 0.6177 -0.2763 0.0204  -0.1558 227 LEU A CD2 
1776 N  N   . THR A 233 ? 0.8262 0.7855 0.6314 -0.2984 0.0723  -0.1500 228 THR A N   
1777 C  CA  . THR A 233 ? 0.9103 0.8369 0.6911 -0.3188 0.0905  -0.1586 228 THR A CA  
1778 C  C   . THR A 233 ? 0.9263 0.8752 0.7236 -0.3192 0.0900  -0.1603 228 THR A C   
1779 O  O   . THR A 233 ? 0.9663 0.9235 0.7581 -0.3427 0.1021  -0.1745 228 THR A O   
1780 C  CB  . THR A 233 ? 0.9536 0.8118 0.7015 -0.3105 0.0996  -0.1484 228 THR A CB  
1781 O  OG1 . THR A 233 ? 0.9597 0.7956 0.6883 -0.3158 0.1043  -0.1507 228 THR A OG1 
1782 C  CG2 . THR A 233 ? 1.0249 0.8442 0.7454 -0.3270 0.1177  -0.1540 228 THR A CG2 
1783 N  N   . LEU A 234 ? 0.8945 0.8540 0.7119 -0.2944 0.0768  -0.1470 229 LEU A N   
1784 C  CA  . LEU A 234 ? 0.9003 0.8810 0.7340 -0.2926 0.0758  -0.1480 229 LEU A CA  
1785 C  C   . LEU A 234 ? 0.9017 0.9473 0.7633 -0.3035 0.0710  -0.1616 229 LEU A C   
1786 O  O   . LEU A 234 ? 0.9075 0.9703 0.7743 -0.3174 0.0786  -0.1718 229 LEU A O   
1787 C  CB  . LEU A 234 ? 0.8755 0.8518 0.7234 -0.2634 0.0626  -0.1309 229 LEU A CB  
1788 C  CG  . LEU A 234 ? 0.9110 0.9137 0.7805 -0.2555 0.0577  -0.1296 229 LEU A CG  
1789 C  CD1 . LEU A 234 ? 1.0146 0.9761 0.8625 -0.2608 0.0702  -0.1282 229 LEU A CD1 
1790 C  CD2 . LEU A 234 ? 0.8723 0.8888 0.7633 -0.2275 0.0408  -0.1153 229 LEU A CD2 
1791 N  N   . TRP A 235 ? 0.8347 0.9177 0.7135 -0.2976 0.0588  -0.1626 230 TRP A N   
1792 C  CA  . TRP A 235 ? 0.8168 0.9654 0.7231 -0.3036 0.0517  -0.1748 230 TRP A CA  
1793 C  C   . TRP A 235 ? 0.8813 1.0482 0.7792 -0.3350 0.0633  -0.1952 230 TRP A C   
1794 O  O   . TRP A 235 ? 0.8692 1.0944 0.7900 -0.3427 0.0588  -0.2081 230 TRP A O   
1795 C  CB  . TRP A 235 ? 0.7932 0.9742 0.7192 -0.2824 0.0330  -0.1667 230 TRP A CB  
1796 C  CG  . TRP A 235 ? 0.7494 0.9156 0.6841 -0.2532 0.0217  -0.1480 230 TRP A CG  
1797 C  CD1 . TRP A 235 ? 0.7598 0.9027 0.6944 -0.2434 0.0240  -0.1397 230 TRP A CD1 
1798 C  CD2 . TRP A 235 ? 0.7179 0.8905 0.6611 -0.2314 0.0072  -0.1358 230 TRP A CD2 
1799 N  NE1 . TRP A 235 ? 0.7468 0.8829 0.6905 -0.2175 0.0117  -0.1238 230 TRP A NE1 
1800 C  CE2 . TRP A 235 ? 0.7023 0.8553 0.6509 -0.2100 0.0018  -0.1211 230 TRP A CE2 
1801 C  CE3 . TRP A 235 ? 0.7038 0.8962 0.6490 -0.2286 -0.0012 -0.1363 230 TRP A CE3 
1802 C  CZ2 . TRP A 235 ? 0.6804 0.8323 0.6364 -0.1873 -0.0106 -0.1075 230 TRP A CZ2 
1803 C  CZ3 . TRP A 235 ? 0.6822 0.8721 0.6337 -0.2050 -0.0137 -0.1218 230 TRP A CZ3 
1804 C  CH2 . TRP A 235 ? 0.6578 0.8272 0.6146 -0.1853 -0.0178 -0.1079 230 TRP A CH2 
1805 N  N   . THR A 236 ? 0.8911 1.0111 0.7569 -0.3529 0.0781  -0.1992 231 THR A N   
1806 C  CA  . THR A 236 ? 0.9276 1.0596 0.7819 -0.3854 0.0914  -0.2196 231 THR A CA  
1807 C  C   . THR A 236 ? 0.9899 1.0721 0.8133 -0.4036 0.1142  -0.2236 231 THR A C   
1808 O  O   . THR A 236 ? 1.0487 1.1402 0.8631 -0.4219 0.1285  -0.2352 231 THR A O   
1809 C  CB  . THR A 236 ? 0.9768 1.0998 0.8174 -0.3902 0.0900  -0.2214 231 THR A CB  
1810 O  OG1 . THR A 236 ? 0.9988 1.0548 0.8110 -0.3799 0.0953  -0.2075 231 THR A OG1 
1811 C  CG2 . THR A 236 ? 0.8966 1.0708 0.7652 -0.3706 0.0688  -0.2167 231 THR A CG2 
1812 O  OXT . THR A 236 ? 1.0062 1.0376 0.8115 -0.3977 0.1192  -0.2140 231 THR A OXT 
1813 N  N   . GLN B 1   ? 1.2405 1.2122 1.1235 -0.2226 0.0624  -0.1106 255 GLN P N   
1814 C  CA  . GLN B 1   ? 1.1961 1.1451 1.0725 -0.2074 0.0539  -0.0989 255 GLN P CA  
1815 C  C   . GLN B 1   ? 1.1015 1.0914 1.0059 -0.1954 0.0394  -0.0967 255 GLN P C   
1816 O  O   . GLN B 1   ? 1.0740 1.0996 0.9908 -0.2060 0.0389  -0.1067 255 GLN P O   
1817 C  CB  . GLN B 1   ? 1.2178 1.1301 1.0642 -0.2212 0.0647  -0.1019 255 GLN P CB  
1818 C  CG  . GLN B 1   ? 1.2243 1.1150 1.0642 -0.2060 0.0571  -0.0912 255 GLN P CG  
1819 C  CD  . GLN B 1   ? 1.2860 1.1372 1.0941 -0.2185 0.0687  -0.0943 255 GLN P CD  
1820 O  OE1 . GLN B 1   ? 1.3448 1.1770 1.1314 -0.2385 0.0836  -0.1034 255 GLN P OE1 
1821 N  NE2 . GLN B 1   ? 1.2864 1.1232 1.0900 -0.2071 0.0630  -0.0871 255 GLN P NE2 
1822 N  N   . ARG B 2   ? 1.0731 1.0572 0.9857 -0.1736 0.0278  -0.0840 256 ARG P N   
1823 C  CA  . ARG B 2   ? 0.9682 0.9856 0.9041 -0.1604 0.0144  -0.0802 256 ARG P CA  
1824 C  C   . ARG B 2   ? 0.8970 0.9084 0.8250 -0.1632 0.0129  -0.0798 256 ARG P C   
1825 O  O   . ARG B 2   ? 0.8974 0.8716 0.8022 -0.1685 0.0199  -0.0782 256 ARG P O   
1826 C  CB  . ARG B 2   ? 0.9372 0.9474 0.8826 -0.1382 0.0045  -0.0676 256 ARG P CB  
1827 C  CG  . ARG B 2   ? 0.8728 0.9214 0.8441 -0.1249 -0.0071 -0.0654 256 ARG P CG  
1828 C  CD  . ARG B 2   ? 0.8694 0.9104 0.8481 -0.1089 -0.0120 -0.0569 256 ARG P CD  
1829 N  NE  . ARG B 2   ? 0.8833 0.9460 0.8737 -0.1106 -0.0096 -0.0630 256 ARG P NE  
1830 C  CZ  . ARG B 2   ? 0.8892 0.9337 0.8717 -0.1132 -0.0033 -0.0634 256 ARG P CZ  
1831 N  NH1 . ARG B 2   ? 0.9094 0.9139 0.8711 -0.1145 0.0012  -0.0583 256 ARG P NH1 
1832 N  NH2 . ARG B 2   ? 0.8772 0.9447 0.8725 -0.1137 -0.0014 -0.0691 256 ARG P NH2 
1833 N  N   . SER B 3   ? 0.8194 0.8670 0.7653 -0.1589 0.0038  -0.0812 257 SER P N   
1834 C  CA  . SER B 3   ? 0.7434 0.7856 0.6827 -0.1585 0.0008  -0.0791 257 SER P CA  
1835 C  C   . SER B 3   ? 0.7071 0.7192 0.6409 -0.1412 -0.0045 -0.0655 257 SER P C   
1836 O  O   . SER B 3   ? 0.7116 0.7190 0.6532 -0.1272 -0.0094 -0.0576 257 SER P O   
1837 C  CB  . SER B 3   ? 0.6994 0.7871 0.6579 -0.1555 -0.0089 -0.0827 257 SER P CB  
1838 O  OG  . SER B 3   ? 0.7109 0.8319 0.6764 -0.1717 -0.0045 -0.0969 257 SER P OG  
1839 N  N   . THR B 4   ? 0.6703 0.6627 0.5904 -0.1430 -0.0028 -0.0637 258 THR P N   
1840 C  CA  . THR B 4   ? 0.6230 0.5898 0.5384 -0.1278 -0.0069 -0.0524 258 THR P CA  
1841 C  C   . THR B 4   ? 0.5721 0.5587 0.4999 -0.1177 -0.0169 -0.0476 258 THR P C   
1842 O  O   . THR B 4   ? 0.5767 0.5773 0.5028 -0.1254 -0.0171 -0.0527 258 THR P O   
1843 C  CB  . THR B 4   ? 0.6613 0.5887 0.5516 -0.1334 0.0020  -0.0526 258 THR P CB  
1844 O  OG1 . THR B 4   ? 0.6531 0.5577 0.5271 -0.1433 0.0125  -0.0569 258 THR P OG1 
1845 C  CG2 . THR B 4   ? 0.6607 0.5661 0.5488 -0.1164 -0.0025 -0.0418 258 THR P CG2 
1846 N  N   . SEP B 5   ? 0.5357 0.5219 0.4741 -0.1013 -0.0245 -0.0381 259 SEP P N   
1847 C  CA  . SEP B 5   ? 0.5034 0.5023 0.4504 -0.0909 -0.0328 -0.0322 259 SEP P CA  
1848 C  CB  . SEP B 5   ? 0.4901 0.5068 0.4541 -0.0775 -0.0409 -0.0265 259 SEP P CB  
1849 O  OG  . SEP B 5   ? 0.4882 0.4850 0.4525 -0.0701 -0.0400 -0.0213 259 SEP P OG  
1850 C  C   . SEP B 5   ? 0.5318 0.5029 0.4692 -0.0845 -0.0317 -0.0257 259 SEP P C   
1851 O  O   . SEP B 5   ? 0.5290 0.4731 0.4540 -0.0862 -0.0256 -0.0256 259 SEP P O   
1852 P  P   . SEP B 5   ? 0.4832 0.4946 0.4629 -0.0578 -0.0464 -0.0166 259 SEP P P   
1853 O  O1P . SEP B 5   ? 0.4643 0.4853 0.4496 -0.0471 -0.0538 -0.0102 259 SEP P O1P 
1854 O  O2P . SEP B 5   ? 0.4888 0.5269 0.4775 -0.0630 -0.0459 -0.0241 259 SEP P O2P 
1855 O  O3P . SEP B 5   ? 0.5095 0.4953 0.4857 -0.0526 -0.0443 -0.0121 259 SEP P O3P 
1856 N  N   . THR B 6   ? 0.5058 0.4835 0.4479 -0.0767 -0.0374 -0.0206 260 THR P N   
1857 C  CA  . THR B 6   ? 0.5193 0.4753 0.4551 -0.0703 -0.0364 -0.0152 260 THR P CA  
1858 C  C   . THR B 6   ? 0.5469 0.4860 0.4851 -0.0613 -0.0363 -0.0101 260 THR P C   
1859 O  O   . THR B 6   ? 0.5324 0.4804 0.4817 -0.0549 -0.0406 -0.0070 260 THR P O   
1860 C  CB  . THR B 6   ? 0.5392 0.5067 0.4801 -0.0639 -0.0421 -0.0104 260 THR P CB  
1861 O  OG1 . THR B 6   ? 0.5435 0.5330 0.4840 -0.0706 -0.0443 -0.0151 260 THR P OG1 
1862 C  CG2 . THR B 6   ? 0.5958 0.5445 0.5286 -0.0616 -0.0390 -0.0080 260 THR P CG2 
1863 N  N   . PRO B 7   ? 0.5675 0.4826 0.4943 -0.0604 -0.0315 -0.0099 261 PRO P N   
1864 C  CA  . PRO B 7   ? 0.6025 0.5031 0.5302 -0.0514 -0.0319 -0.0060 261 PRO P CA  
1865 C  C   . PRO B 7   ? 0.6272 0.5288 0.5631 -0.0413 -0.0359 -0.0007 261 PRO P C   
1866 O  O   . PRO B 7   ? 0.5995 0.5081 0.5375 -0.0414 -0.0370 0.0003  261 PRO P O   
1867 C  CB  . PRO B 7   ? 0.6023 0.4769 0.5109 -0.0545 -0.0246 -0.0089 261 PRO P CB  
1868 C  CG  . PRO B 7   ? 0.6496 0.5225 0.5500 -0.0609 -0.0211 -0.0120 261 PRO P CG  
1869 C  CD  . PRO B 7   ? 0.5909 0.4905 0.5014 -0.0677 -0.0248 -0.0142 261 PRO P CD  
1870 N  N   . ASN B 8   ? 0.6122 0.5067 0.5517 -0.0333 -0.0375 0.0019  262 ASN P N   
1871 C  CA  . ASN B 8   ? 0.6271 0.5216 0.5733 -0.0253 -0.0397 0.0050  262 ASN P CA  
1872 C  C   . ASN B 8   ? 0.7167 0.5967 0.6525 -0.0224 -0.0357 0.0035  262 ASN P C   
1873 O  O   . ASN B 8   ? 0.7907 0.6540 0.7131 -0.0223 -0.0321 0.0015  262 ASN P O   
1874 C  CB  . ASN B 8   ? 0.6502 0.5456 0.6046 -0.0186 -0.0431 0.0070  262 ASN P CB  
1875 C  CG  . ASN B 8   ? 0.5984 0.5072 0.5638 -0.0192 -0.0468 0.0090  262 ASN P CG  
1876 O  OD1 . ASN B 8   ? 0.5366 0.4549 0.5082 -0.0192 -0.0485 0.0111  262 ASN P OD1 
1877 N  ND2 . ASN B 8   ? 0.6435 0.5512 0.6092 -0.0193 -0.0474 0.0083  262 ASN P ND2 
1878 N  N   . VAL B 9   ? 0.7582 0.6427 0.6985 -0.0196 -0.0358 0.0042  263 VAL P N   
1879 C  CA  . VAL B 9   ? 0.8580 0.7316 0.7911 -0.0145 -0.0322 0.0025  263 VAL P CA  
1880 C  C   . VAL B 9   ? 0.8632 0.7477 0.8090 -0.0085 -0.0340 0.0034  263 VAL P C   
1881 O  O   . VAL B 9   ? 0.8280 0.7250 0.7837 -0.0116 -0.0359 0.0053  263 VAL P O   
1882 C  CB  . VAL B 9   ? 0.8659 0.7310 0.7859 -0.0208 -0.0267 -0.0002 263 VAL P CB  
1883 C  CG1 . VAL B 9   ? 0.8241 0.6800 0.7314 -0.0297 -0.0237 -0.0028 263 VAL P CG1 
1884 C  CG2 . VAL B 9   ? 0.8136 0.6929 0.7404 -0.0254 -0.0276 0.0006  263 VAL P CG2 
1885 N  N   . HIS B 10  ? 0.9125 0.7921 0.8569 0.0002  -0.0330 0.0017  264 HIS P N   
1886 C  CA  . HIS B 10  ? 0.9440 0.8353 0.8996 0.0051  -0.0330 0.0003  264 HIS P CA  
1887 C  C   . HIS B 10  ? 0.8689 0.7766 0.8410 0.0037  -0.0366 0.0014  264 HIS P C   
1888 O  O   . HIS B 10  ? 0.7792 0.6889 0.7551 0.0019  -0.0401 0.0035  264 HIS P O   
1889 C  CB  . HIS B 10  ? 0.9625 0.8539 0.9143 0.0004  -0.0282 -0.0009 264 HIS P CB  
1890 O  OXT . HIS B 10  ? 0.8510 0.7696 0.8323 0.0040  -0.0351 -0.0004 264 HIS P OXT 
1891 CL CL  . CL  C .   ? 0.5429 0.4636 0.5569 0.0283  -0.0149 -0.0309 301 CL  A CL  
1892 MG MG  . MG  D .   ? 0.7814 0.8705 0.8589 0.1047  -0.0528 -0.0115 302 MG  A MG  
1893 MG MG  . MG  E .   ? 1.1574 1.4015 1.2353 -0.1392 0.1461  -0.1982 303 MG  A MG  
1894 MG MG  . MG  F .   ? 0.7542 0.5580 0.6797 -0.2404 0.1458  -0.0693 304 MG  A MG  
1895 O  O1  . WQ9 G .   ? 0.5716 0.4960 0.4956 -0.0335 -0.0348 0.0266  305 WQ9 A O1  
1896 C  C1  . WQ9 G .   ? 0.5661 0.4900 0.4942 -0.0357 -0.0321 0.0214  305 WQ9 A C1  
1897 C  C2  . WQ9 G .   ? 0.5763 0.4959 0.4987 -0.0396 -0.0257 0.0177  305 WQ9 A C2  
1898 N  N1  . WQ9 G .   ? 0.5555 0.4809 0.4919 -0.0340 -0.0343 0.0189  305 WQ9 A N1  
1899 C  C3  . WQ9 G .   ? 0.5643 0.4870 0.5002 -0.0358 -0.0325 0.0135  305 WQ9 A C3  
1900 C  C4  . WQ9 G .   ? 0.5332 0.4567 0.4785 -0.0319 -0.0359 0.0141  305 WQ9 A C4  
1901 C  C5  . WQ9 G .   ? 0.5372 0.4686 0.4843 -0.0303 -0.0412 0.0185  305 WQ9 A C5  
1902 C  C6  . WQ9 G .   ? 0.5247 0.4560 0.4812 -0.0267 -0.0437 0.0185  305 WQ9 A C6  
1903 C  C7  . WQ9 G .   ? 0.5266 0.4625 0.4803 -0.0300 -0.0454 0.0153  305 WQ9 A C7  
1904 N  N2  . WQ9 G .   ? 0.5020 0.4458 0.4477 -0.0340 -0.0464 0.0149  305 WQ9 A N2  
1905 S  S1  . WQ9 G .   ? 0.5431 0.4967 0.4851 -0.0405 -0.0476 0.0098  305 WQ9 A S1  
1906 O  O2  . WQ9 G .   ? 0.5525 0.5156 0.4869 -0.0439 -0.0491 0.0091  305 WQ9 A O2  
1907 O  O3  . WQ9 G .   ? 0.5820 0.5435 0.5324 -0.0374 -0.0512 0.0105  305 WQ9 A O3  
1908 C  C8  . WQ9 G .   ? 0.5637 0.5022 0.4986 -0.0466 -0.0410 0.0037  305 WQ9 A C8  
1909 C  C9  . WQ9 G .   ? 0.5482 0.4766 0.4864 -0.0436 -0.0396 0.0034  305 WQ9 A C9  
1910 C  C10 . WQ9 G .   ? 0.6032 0.5158 0.5319 -0.0464 -0.0342 -0.0005 305 WQ9 A C10 
1911 C  C11 . WQ9 G .   ? 0.5986 0.5045 0.5149 -0.0531 -0.0294 -0.0047 305 WQ9 A C11 
1912 BR BR1 . WQ9 G .   ? 0.7922 0.6696 0.6903 -0.0556 -0.0204 -0.0097 305 WQ9 A BR1 
1913 C  C12 . WQ9 G .   ? 0.5666 0.4845 0.4814 -0.0573 -0.0309 -0.0051 305 WQ9 A C12 
1914 F  F1  . WQ9 G .   ? 0.6144 0.5259 0.5165 -0.0646 -0.0260 -0.0098 305 WQ9 A F1  
1915 C  C13 . WQ9 G .   ? 0.5297 0.4642 0.4532 -0.0538 -0.0370 -0.0007 305 WQ9 A C13 
1916 C  C14 . WQ9 G .   ? 0.5226 0.4592 0.4621 -0.0356 -0.0422 0.0148  305 WQ9 A C14 
1917 C  C15 . WQ9 G .   ? 0.5461 0.4733 0.4917 -0.0296 -0.0380 0.0214  305 WQ9 A C15 
1918 O  O   . HOH H .   ? 0.6210 0.7798 0.7235 0.1044  -0.0553 -0.0256 401 HOH A O   
1919 O  O   . HOH H .   ? 0.6919 0.4640 0.6392 -0.1325 0.0549  -0.0332 402 HOH A O   
1920 O  O   . HOH H .   ? 0.6979 0.5158 0.5668 -0.0346 -0.0063 -0.0116 403 HOH A O   
1921 O  O   . HOH H .   ? 0.6320 0.5549 0.5205 -0.0578 -0.0237 0.0037  404 HOH A O   
1922 O  O   . HOH H .   ? 0.5691 0.6349 0.6579 0.0107  -0.0430 -0.0453 405 HOH A O   
1923 O  O   . HOH H .   ? 0.7429 0.3589 0.5639 -0.1479 0.1089  0.0017  406 HOH A O   
1924 O  O   . HOH H .   ? 0.9244 0.6980 0.6928 -0.0591 0.0785  -0.0611 407 HOH A O   
1925 O  O   . HOH H .   ? 0.7620 0.7722 0.6182 0.1209  -0.1148 0.0821  408 HOH A O   
1926 O  O   . HOH H .   ? 0.8043 0.8680 0.5597 0.0136  -0.1124 0.0483  409 HOH A O   
1927 O  O   . HOH H .   ? 0.7716 0.4780 0.6584 -0.0570 0.0331  0.0294  410 HOH A O   
1928 O  O   . HOH H .   ? 0.5387 0.4855 0.5449 -0.0666 0.0160  -0.0102 411 HOH A O   
1929 O  O   . HOH H .   ? 0.5298 0.4951 0.5724 0.0660  -0.0192 -0.0250 412 HOH A O   
1930 O  O   . HOH H .   ? 0.6513 0.7942 0.5871 0.1259  -0.1325 0.0500  413 HOH A O   
1931 O  O   . HOH H .   ? 0.7272 0.6646 0.5282 0.0597  -0.0876 0.0853  414 HOH A O   
1932 O  O   . HOH H .   ? 0.6994 0.5130 0.5593 -0.0105 0.0221  -0.0261 415 HOH A O   
1933 O  O   . HOH H .   ? 0.5949 0.5586 0.5862 -0.0243 -0.0528 0.0040  416 HOH A O   
1934 O  O   . HOH H .   ? 0.6096 0.5104 0.4757 -0.0677 -0.0081 -0.0090 417 HOH A O   
1935 O  O   . HOH H .   ? 0.5935 0.5297 0.5767 -0.0535 0.0097  -0.0005 418 HOH A O   
1936 O  O   . HOH H .   ? 0.7058 0.6107 0.5866 -0.0448 -0.0188 0.0310  419 HOH A O   
1937 O  O   . HOH H .   ? 0.7023 0.6316 0.5649 0.1193  -0.0918 0.0889  420 HOH A O   
1938 O  O   . HOH H .   ? 0.7379 0.4657 0.4686 -0.1535 0.0554  -0.0684 421 HOH A O   
1939 O  O   . HOH H .   ? 0.5178 0.4324 0.5185 -0.0014 -0.0556 0.0070  422 HOH A O   
1940 O  O   . HOH H .   ? 0.6494 0.5405 0.6583 0.0079  -0.0499 0.0144  423 HOH A O   
1941 O  O   . HOH H .   ? 0.5713 0.5264 0.5584 0.0574  -0.0896 -0.0162 424 HOH A O   
1942 O  O   . HOH H .   ? 0.7268 0.6171 0.5181 -0.1079 0.0096  -0.0336 425 HOH A O   
1943 O  O   . HOH H .   ? 0.6056 0.6268 0.6639 -0.0131 -0.0120 -0.0329 426 HOH A O   
1944 O  O   . HOH H .   ? 0.7671 0.7522 0.5305 0.0462  -0.1004 0.0765  427 HOH A O   
1945 O  O   . HOH H .   ? 0.6880 0.4718 0.6498 -0.1242 0.0409  -0.0426 428 HOH A O   
1946 O  O   . HOH H .   ? 0.5964 0.3797 0.4811 -0.0567 0.0223  0.0440  429 HOH A O   
1947 O  O   . HOH H .   ? 0.5162 0.4451 0.4854 -0.0230 -0.0482 0.0135  430 HOH A O   
1948 O  O   . HOH H .   ? 0.6105 0.4861 0.6074 0.0266  -0.0174 -0.0271 431 HOH A O   
1949 O  O   . HOH H .   ? 0.5314 0.6073 0.5637 -0.0430 -0.0402 -0.0333 432 HOH A O   
1950 O  O   . HOH H .   ? 0.5205 0.4717 0.5069 -0.0074 -0.0592 0.0247  433 HOH A O   
1951 O  O   . HOH H .   ? 0.6643 0.7349 0.4361 -0.2150 -0.0199 -0.1092 434 HOH A O   
1952 O  O   . HOH H .   ? 0.4474 0.5195 0.4904 -0.0013 -0.0590 -0.0115 435 HOH A O   
1953 O  O   . HOH H .   ? 0.8374 0.5357 0.6827 0.0304  -0.0030 0.0744  436 HOH A O   
1954 O  O   . HOH H .   ? 0.4842 0.5898 0.5583 -0.0097 0.0258  -0.0875 437 HOH A O   
1955 O  O   . HOH H .   ? 0.5064 0.7078 0.5846 -0.0458 -0.0409 -0.0621 438 HOH A O   
1956 O  O   . HOH H .   ? 0.6586 0.5017 0.5271 -0.0180 -0.0203 0.0617  439 HOH A O   
1957 O  O   . HOH H .   ? 0.7134 0.5072 0.6180 0.0563  -0.0354 0.0677  440 HOH A O   
1958 O  O   . HOH H .   ? 0.5929 0.4919 0.5042 -0.0502 -0.0008 0.0230  441 HOH A O   
1959 O  O   . HOH H .   ? 0.5841 0.4483 0.4173 -0.0863 0.0060  -0.0289 442 HOH A O   
1960 O  O   . HOH H .   ? 0.6008 0.5012 0.5766 0.0180  -0.0688 0.0007  443 HOH A O   
1961 O  O   . HOH H .   ? 0.5380 0.4182 0.5434 -0.0072 -0.0428 0.0155  444 HOH A O   
1962 O  O   . HOH H .   ? 0.5969 0.5105 0.5549 -0.0239 -0.0409 0.0098  445 HOH A O   
1963 O  O   . HOH H .   ? 0.7536 0.6652 0.6049 -0.1868 0.0322  -0.0816 446 HOH A O   
1964 O  O   . HOH H .   ? 0.7201 0.5362 0.5492 0.0029  -0.0259 0.0785  447 HOH A O   
1965 O  O   . HOH H .   ? 0.5511 0.4089 0.5369 0.0019  -0.0378 0.0282  448 HOH A O   
1966 O  O   . HOH H .   ? 0.7349 0.6600 0.4037 0.0000  0.0000  -0.1350 449 HOH A O   
1967 O  O   . HOH H .   ? 0.4793 0.4613 0.5164 0.0135  -0.0460 -0.0161 450 HOH A O   
1968 O  O   . HOH H .   ? 0.5406 0.7267 0.6401 -0.0219 -0.0143 -0.0736 451 HOH A O   
1969 O  O   . HOH H .   ? 0.5866 0.5041 0.5264 -0.0706 -0.0093 -0.0296 452 HOH A O   
1970 O  O   . HOH H .   ? 0.8498 0.6853 0.7126 -0.0037 0.0536  -0.0456 453 HOH A O   
1971 O  O   . HOH H .   ? 0.6921 0.4199 0.5852 -0.0765 0.0409  0.0236  454 HOH A O   
1972 O  O   . HOH H .   ? 0.5015 0.7025 0.6141 0.0429  -0.0483 -0.0461 455 HOH A O   
1973 O  O   . HOH H .   ? 0.5737 0.4589 0.5748 0.0401  -0.0463 0.0234  456 HOH A O   
1974 O  O   . HOH H .   ? 0.5888 0.7696 0.4799 -0.1397 -0.0672 -0.0733 457 HOH A O   
1975 O  O   . HOH H .   ? 0.6247 0.4991 0.5575 -0.0714 0.0244  0.0185  458 HOH A O   
1976 O  O   . HOH H .   ? 0.5704 0.4756 0.5484 0.0117  -0.0508 0.0042  459 HOH A O   
1977 O  O   . HOH H .   ? 0.5577 0.5299 0.5236 -0.0350 -0.0543 0.0075  460 HOH A O   
1978 O  O   . HOH H .   ? 0.5779 0.7159 0.4345 -0.1574 -0.0541 -0.0778 461 HOH A O   
1979 O  O   . HOH H .   ? 0.5829 0.7208 0.4651 -0.1104 -0.0715 -0.0475 462 HOH A O   
1980 O  O   . HOH H .   ? 0.6024 1.2281 0.7826 0.3380  -0.1625 -0.0529 463 HOH A O   
1981 O  O   . HOH H .   ? 0.7233 0.5859 0.5330 0.0081  -0.0443 0.0780  464 HOH A O   
1982 O  O   . HOH H .   ? 0.5883 0.5065 0.5892 0.0983  -0.0507 0.0298  465 HOH A O   
1983 O  O   . HOH H .   ? 0.5100 0.4715 0.4827 -0.0125 -0.0600 0.0252  466 HOH A O   
1984 O  O   . HOH H .   ? 0.7791 0.5476 0.5522 0.0774  -0.0451 0.1097  467 HOH A O   
1985 O  O   . HOH H .   ? 0.7054 0.4649 0.5497 -0.0168 0.0019  0.0701  468 HOH A O   
1986 O  O   . HOH H .   ? 0.7400 0.4647 0.5236 -0.0571 0.0269  -0.0286 469 HOH A O   
1987 O  O   . HOH H .   ? 0.5499 0.3595 0.5131 -0.0328 -0.0087 0.0195  470 HOH A O   
1988 O  O   . HOH H .   ? 0.5083 0.6514 0.5355 -0.0609 -0.0547 -0.0422 471 HOH A O   
1989 O  O   . HOH H .   ? 0.5831 0.4855 0.5988 0.0519  -0.0359 0.0022  472 HOH A O   
1990 O  O   . HOH H .   ? 0.4527 0.4574 0.5113 -0.0801 0.0188  -0.0401 473 HOH A O   
1991 O  O   . HOH H .   ? 0.7862 0.5197 0.5790 -0.0637 0.0423  0.0641  474 HOH A O   
1992 O  O   . HOH H .   ? 0.6688 0.7671 0.7089 0.1296  -0.0858 0.0205  475 HOH A O   
1993 O  O   . HOH H .   ? 0.5335 0.6728 0.6701 -0.0264 -0.0291 -0.0773 476 HOH A O   
1994 O  O   . HOH H .   ? 0.8098 0.7358 0.5225 -0.3174 0.0658  -0.1674 477 HOH A O   
1995 O  O   . HOH H .   ? 0.5270 0.6588 0.5911 0.0919  -0.0801 0.0026  478 HOH A O   
1996 O  O   . HOH H .   ? 0.6105 0.6697 0.4520 -0.1621 -0.0325 -0.0734 479 HOH A O   
1997 O  O   . HOH H .   ? 0.7593 0.5943 0.4258 -0.2346 0.0590  -0.1226 480 HOH A O   
1998 O  O   . HOH H .   ? 0.7286 0.5501 0.6172 -0.0790 0.0373  0.0312  481 HOH A O   
1999 O  O   . HOH H .   ? 0.7577 0.7285 0.4741 -0.3119 0.0492  -0.1679 482 HOH A O   
2000 O  O   . HOH H .   ? 0.6438 0.5255 0.4694 0.0266  -0.0577 0.0799  483 HOH A O   
2001 O  O   . HOH H .   ? 0.5692 0.4681 0.3950 -0.0994 -0.0026 -0.0293 484 HOH A O   
2002 O  O   . HOH H .   ? 0.5483 0.6337 0.5689 -0.0930 0.0020  -0.0709 485 HOH A O   
2003 O  O   . HOH H .   ? 0.4574 0.5304 0.5580 -0.0197 -0.0299 -0.0514 486 HOH A O   
2004 O  O   . HOH H .   ? 0.5620 0.5258 0.5807 -0.0439 -0.0010 -0.0106 487 HOH A O   
2005 O  O   . HOH H .   ? 0.6255 0.5683 0.4721 0.0393  -0.0789 0.0726  488 HOH A O   
2006 O  O   . HOH H .   ? 0.5328 0.4702 0.5297 -0.0146 -0.0288 0.0030  489 HOH A O   
2007 O  O   . HOH H .   ? 0.5676 0.4527 0.5454 -0.1504 0.0770  -0.0358 490 HOH A O   
2008 O  O   . HOH H .   ? 0.7240 0.7072 0.7045 -0.0199 -0.0613 0.0147  491 HOH A O   
2009 O  O   . HOH H .   ? 0.7910 0.6088 0.5899 -0.0035 -0.0241 0.0807  492 HOH A O   
2010 O  O   . HOH H .   ? 0.7723 1.0184 0.6686 0.1151  -0.1632 0.0365  493 HOH A O   
2011 O  O   . HOH H .   ? 0.5527 0.6708 0.4556 -0.0807 -0.0763 -0.0272 494 HOH A O   
2012 O  O   . HOH H .   ? 0.5809 0.5046 0.5370 -0.0437 0.0004  0.0067  495 HOH A O   
2013 O  O   . HOH H .   ? 0.7251 0.6031 0.6396 0.1243  -0.0675 0.0747  496 HOH A O   
2014 O  O   . HOH H .   ? 0.4815 0.5101 0.5543 -0.0518 0.0005  -0.0402 497 HOH A O   
2015 O  O   . HOH H .   ? 0.5876 0.9841 0.5777 -0.0865 -0.1141 -0.0869 498 HOH A O   
2016 O  O   . HOH H .   ? 0.6256 0.5159 0.5898 0.0015  -0.0498 0.0075  499 HOH A O   
2017 O  O   . HOH H .   ? 0.6538 0.4677 0.5101 -0.0289 0.0122  -0.0209 500 HOH A O   
2018 O  O   . HOH H .   ? 0.6435 0.7103 0.7442 -0.1202 0.0373  -0.0803 501 HOH A O   
2019 O  O   . HOH H .   ? 0.6422 1.0834 0.6338 0.0386  -0.1642 -0.0395 502 HOH A O   
2020 O  O   . HOH H .   ? 0.8678 1.2546 0.7428 0.0386  -0.1806 -0.0163 503 HOH A O   
2021 O  O   . HOH H .   ? 0.6824 0.6059 0.6040 -0.1042 0.0280  -0.0577 504 HOH A O   
2022 O  O   . HOH H .   ? 0.6479 0.4804 0.5994 0.0751  -0.0420 0.0497  505 HOH A O   
2023 O  O   . HOH H .   ? 0.6724 0.5308 0.6552 0.0350  -0.0431 0.0334  506 HOH A O   
2024 O  O   . HOH H .   ? 0.5356 0.5201 0.4926 -0.0161 -0.0647 0.0244  507 HOH A O   
2025 O  O   . HOH H .   ? 0.6766 0.5961 0.7019 -0.0167 -0.0563 -0.0143 508 HOH A O   
2026 O  O   . HOH H .   ? 0.5615 0.4639 0.5442 -0.1031 0.0432  -0.0130 509 HOH A O   
2027 O  O   . HOH H .   ? 0.5729 0.5096 0.5688 0.0251  -0.0804 -0.0120 510 HOH A O   
2028 O  O   . HOH H .   ? 0.5693 0.5939 0.5875 -0.0366 0.0387  -0.0848 511 HOH A O   
2029 O  O   . HOH H .   ? 0.6813 0.6440 0.7010 -0.0080 -0.0267 -0.0089 512 HOH A O   
2030 O  O   . HOH H .   ? 0.5004 0.4340 0.5271 -0.0073 -0.0619 -0.0096 513 HOH A O   
2031 O  O   . HOH H .   ? 0.7822 0.7158 0.6937 -0.1318 0.0502  -0.0751 514 HOH A O   
2032 O  O   . HOH H .   ? 0.5907 0.5418 0.6117 -0.1727 0.0872  -0.0663 515 HOH A O   
2033 O  O   . HOH H .   ? 0.8736 0.5184 0.7035 -0.1235 0.0905  0.0167  516 HOH A O   
2034 O  O   . HOH H .   ? 0.5601 0.7455 0.6814 0.0239  0.0224  -0.0985 517 HOH A O   
2035 O  O   . HOH H .   ? 0.6161 0.5326 0.4562 -0.0846 -0.0116 -0.0143 518 HOH A O   
2036 O  O   . HOH H .   ? 0.7818 0.8002 0.7921 0.1272  -0.0775 0.0354  519 HOH A O   
2037 O  O   . HOH H .   ? 0.8412 0.9018 0.7432 0.1658  -0.1247 0.0742  520 HOH A O   
2038 O  O   . HOH H .   ? 0.9812 0.7223 0.6422 0.0983  -0.0533 0.1354  521 HOH A O   
2039 O  O   . HOH H .   ? 0.6872 0.6746 0.6524 -0.0817 -0.0250 -0.0327 522 HOH A O   
2040 O  O   . HOH H .   ? 0.9737 0.6979 0.6270 0.0629  -0.0351 0.1294  523 HOH A O   
2041 O  O   . HOH H .   ? 0.5743 0.7482 0.7004 0.0592  0.0300  -0.1016 524 HOH A O   
2042 O  O   . HOH H .   ? 0.9124 0.7604 0.7334 -0.0356 -0.0107 0.0593  525 HOH A O   
2043 O  O   . HOH H .   ? 0.7055 0.5565 0.5584 -0.0270 -0.0167 0.0591  526 HOH A O   
2044 O  O   . HOH H .   ? 0.8914 0.4715 0.6987 -0.1523 0.1163  -0.0039 527 HOH A O   
2045 O  O   . HOH H .   ? 0.7629 0.5086 0.6222 0.0576  -0.0249 0.0804  528 HOH A O   
2046 O  O   . HOH H .   ? 0.5452 0.4580 0.5414 -0.0029 -0.0515 0.0015  529 HOH A O   
2047 O  O   . HOH H .   ? 0.6149 0.7457 0.6620 -0.0592 -0.0336 -0.0526 530 HOH A O   
2048 O  O   . HOH H .   ? 0.6932 0.6140 0.7022 0.0032  -0.0665 -0.0037 531 HOH A O   
2049 O  O   . HOH H .   ? 0.9038 0.6025 0.6552 -0.0878 0.0403  -0.0393 532 HOH A O   
2050 O  O   . HOH H .   ? 0.7620 0.4100 0.5950 -0.0838 0.0653  0.0338  533 HOH A O   
2051 O  O   . HOH H .   ? 0.6146 0.5415 0.5931 -0.0154 -0.0236 0.0018  534 HOH A O   
2052 O  O   . HOH H .   ? 0.7286 0.6526 0.6852 -0.0322 -0.0066 0.0012  535 HOH A O   
2053 O  O   . HOH H .   ? 0.7753 0.9013 0.5665 -0.1814 -0.0490 -0.0901 536 HOH A O   
2054 O  O   . HOH H .   ? 0.6799 0.6136 0.6141 -0.0966 0.0086  -0.0464 537 HOH A O   
2055 O  O   . HOH H .   ? 0.8068 0.4100 0.6198 -0.1903 0.1371  -0.0194 538 HOH A O   
2056 O  O   . HOH H .   ? 0.5814 0.5030 0.6054 0.0566  -0.0146 -0.0255 539 HOH A O   
2057 O  O   . HOH H .   ? 0.4873 0.5493 0.5291 -0.0149 -0.0474 -0.0211 540 HOH A O   
2058 O  O   . HOH H .   ? 0.6197 0.4907 0.6097 0.0183  -0.0451 0.0306  541 HOH A O   
2059 O  O   . HOH H .   ? 0.6152 0.4868 0.5729 -0.1349 0.0726  -0.0197 542 HOH A O   
2060 O  O   . HOH H .   ? 0.5646 0.6274 0.6585 -0.0967 0.0307  -0.0678 543 HOH A O   
2061 O  O   . HOH H .   ? 0.8192 0.7456 0.7456 -0.0933 -0.0094 -0.0341 544 HOH A O   
2062 O  O   . HOH H .   ? 0.8102 0.6041 0.7069 -0.1328 0.0812  0.0028  545 HOH A O   
2063 O  O   . HOH H .   ? 0.8936 0.4646 0.6966 -0.1033 0.0911  0.0188  546 HOH A O   
2064 O  O   . HOH H .   ? 0.8033 0.6043 0.6028 -0.0336 0.0929  -0.0672 547 HOH A O   
2065 O  O   . HOH H .   ? 0.6473 0.7568 0.6522 -0.0965 -0.0334 -0.0563 548 HOH A O   
2066 O  O   . HOH H .   ? 0.5866 0.8178 0.7079 0.0098  -0.0334 -0.0672 549 HOH A O   
2067 O  O   . HOH H .   ? 0.4934 0.5669 0.5927 -0.0314 -0.0127 -0.0534 550 HOH A O   
2068 O  O   . HOH H .   ? 0.6458 0.5347 0.6516 0.0052  -0.0488 0.0194  551 HOH A O   
2069 O  O   . HOH H .   ? 0.6322 0.9168 0.5412 -0.1345 -0.0906 -0.0868 552 HOH A O   
2070 O  O   . HOH H .   ? 0.5964 0.5094 0.5068 -0.0473 -0.0229 0.0039  553 HOH A O   
2071 O  O   . HOH H .   ? 0.5301 0.4876 0.5505 -0.0887 0.0307  -0.0247 554 HOH A O   
2072 O  O   . HOH H .   ? 0.6917 0.6065 0.4530 -0.1271 0.0038  -0.0411 555 HOH A O   
2073 O  O   . HOH H .   ? 0.8527 0.7049 0.7528 -0.0565 -0.0110 -0.0184 556 HOH A O   
2074 O  O   . HOH H .   ? 0.7948 0.7013 0.7019 -0.1109 0.0264  -0.0540 557 HOH A O   
2075 O  O   . HOH H .   ? 0.6853 0.5046 0.6560 -0.0112 -0.0221 0.0238  558 HOH A O   
2076 O  O   . HOH H .   ? 0.5628 0.7764 0.6446 -0.0687 -0.0227 -0.0802 559 HOH A O   
2077 O  O   . HOH H .   ? 0.7717 0.5539 0.6684 -0.2747 0.1811  -0.0773 560 HOH A O   
2078 O  O   . HOH H .   ? 0.6838 0.7023 0.7440 -0.1584 0.0785  -0.0781 561 HOH A O   
2079 O  O   . HOH I .   ? 0.6080 0.5138 0.5237 -0.0764 -0.0215 -0.0200 301 HOH P O   
2080 O  O   . HOH I .   ? 0.5111 0.5030 0.4814 -0.0469 -0.0519 -0.0042 302 HOH P O   
2081 O  O   . HOH I .   ? 0.5981 0.5574 0.5571 -0.0656 -0.0323 -0.0192 303 HOH P O   
2082 O  O   . HOH I .   ? 0.6559 0.5989 0.6618 0.0003  -0.0362 -0.0026 304 HOH P O   
2083 O  O   . HOH I .   ? 0.6017 0.6416 0.5793 -0.0911 -0.0308 -0.0416 305 HOH P O   
2084 O  O   . HOH I .   ? 0.6637 0.5340 0.5876 -0.0342 -0.0330 -0.0008 306 HOH P O   
2085 O  O   . HOH I .   ? 0.5649 0.5057 0.5248 -0.0341 -0.0476 0.0077  307 HOH P O   
2086 O  O   . HOH I .   ? 0.5805 0.5238 0.5128 -0.0879 -0.0209 -0.0290 308 HOH P O   
2087 O  O   . HOH I .   ? 0.7422 0.6397 0.6785 -0.0450 -0.0342 -0.0044 309 HOH P O   
2088 O  O   . HOH I .   ? 0.7044 0.5130 0.5546 -0.0724 -0.0013 -0.0200 310 HOH P O   
# 
