data_9BR3
# 
_entry.id   9BR3 
# 
_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   9BR3         pdb_00009br3 10.2210/pdb9br3/pdb 
WWPDB D_1000283309 ?            ?                   
# 
_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       2025-03-26 
_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                        9BR3 
_pdbx_database_status.recvd_initial_deposition_date   2024-05-10 
_pdbx_database_status.SG_entry                        N 
_pdbx_database_status.deposit_site                    RCSB 
_pdbx_database_status.process_site                    RCSB 
_pdbx_database_status.status_code_cs                  ? 
_pdbx_database_status.status_code_nmr_data            ? 
_pdbx_database_status.methods_development_category    ? 
_pdbx_database_status.pdb_format_compatible           N 
# 
_pdbx_contact_author.id                 2 
_pdbx_contact_author.email              donald.lorimer@ucb.com 
_pdbx_contact_author.name_first         Donald 
_pdbx_contact_author.name_last          Lorimer 
_pdbx_contact_author.name_mi            D 
_pdbx_contact_author.role               'principal investigator/group leader' 
_pdbx_contact_author.identifier_ORCID   0000-0002-9638-8083 
# 
loop_
_audit_author.name 
_audit_author.pdbx_ordinal 
_audit_author.identifier_ORCID 
'Abendroth, J.' 1 ? 
'Lorimer, D.D.' 2 ? 
'Vu, B.'        3 ? 
'Tanaka, N.'    4 ? 
# 
_citation.abstract                  ? 
_citation.abstract_id_CAS           ? 
_citation.book_id_ISBN              ? 
_citation.book_publisher            ? 
_citation.book_publisher_city       ? 
_citation.book_title                ? 
_citation.coordinate_linkage        ? 
_citation.country                   US 
_citation.database_id_Medline       ? 
_citation.details                   ? 
_citation.id                        primary 
_citation.journal_abbrev            'Cancer Discov' 
_citation.journal_id_ASTM           ? 
_citation.journal_id_CSD            ? 
_citation.journal_id_ISSN           2159-8290 
_citation.journal_full              ? 
_citation.journal_issue             ? 
_citation.journal_volume            ? 
_citation.language                  ? 
_citation.page_first                ? 
_citation.page_last                 ? 
_citation.title                     
'Restoration of the Tumor Suppressor Function of Y220C-Mutant p53 by Rezatapopt, a Small Molecule Reactivator.' 
_citation.year                      2025 
_citation.database_id_CSD           ? 
_citation.pdbx_database_id_DOI      10.1158/2159-8290.CD-24-1421 
_citation.pdbx_database_id_PubMed   39945593 
_citation.pdbx_database_id_patent   ? 
_citation.unpublished_flag          ? 
# 
loop_
_citation_author.citation_id 
_citation_author.name 
_citation_author.ordinal 
_citation_author.identifier_ORCID 
primary 'Puzio-Kuter, A.M.' 1  0009-0008-3298-8152 
primary 'Xu, L.'            2  0009-0004-6709-2103 
primary 'McBrayer, M.K.'    3  0009-0003-7149-5178 
primary 'Dominique, R.'     4  0009-0003-1111-7298 
primary 'Li, H.H.'          5  0009-0009-8872-142X 
primary 'Fahr, B.J.'        6  0009-0002-8658-5961 
primary 'Brown, A.M.'       7  0009-0002-6900-9428 
primary 'Wiebesiek, A.E.'   8  0009-0009-0433-4829 
primary 'Russo, B.M.'       9  0009-0005-5686-3600 
primary 'Mulligan, C.L.'    10 0009-0002-2864-1742 
primary 'Yang, H.'          11 0009-0000-0957-7330 
primary 'Battaglia, J.'     12 0009-0000-4754-3625 
primary 'Robell, K.A.'      13 0009-0008-7376-7831 
primary 'Thomas, D.H.'      14 0009-0006-0175-9416 
primary 'Huang, K.S.'       15 0000-0002-5556-9945 
primary 'Solovyov, A.'      16 0000-0002-7682-4706 
primary 'Greenbaum, B.D.'   17 0000-0001-6153-8793 
primary 'Oliner, J.D.'      18 0009-0005-7397-3975 
primary 'Davis, T.W.'       19 0009-0004-2234-6122 
primary 'Dumble, M.L.'      20 0009-0007-7944-4921 
primary 'Johnson, M.L.'     21 0000-0001-9874-1314 
primary 'Xiong, S.'         22 0000-0003-3984-1774 
primary 'Yang, P.'          23 0009-0004-9574-9547 
primary 'Lozano, G.'        24 0000-0001-8985-4886 
primary 'Fellous, M.M.'     25 0009-0004-7801-1970 
primary 'Vu, B.T.'          26 0009-0001-8350-7071 
primary 'Schram, A.M.'      27 0000-0002-6070-2413 
primary 'Levine, A.J.'      28 0000-0002-1871-6387 
primary 'Poyurovsky, M.V.'  29 0000-0002-3024-778X 
# 
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 'Cellular tumor antigen p53' 24674.943 2   ? Y220C ? ? 
2 non-polymer syn 
'2-{3-[4-(methanesulfonyl)-2-methoxyanilino]prop-1-yn-1-yl}-N-(1-methylpiperidin-4-yl)-1-(2,2,2-trifluoroethyl)-1H-indol-4-amine' 
548.620   2   ? ?     ? ? 
3 non-polymer syn 'ZINC ION' 65.409    2   ? ?     ? ? 
4 water       nat water 18.015    526 ? ?     ? ? 
# 
_entity_name_com.entity_id   1 
_entity_name_com.name        'Antigen NY-CO-13,Phosphoprotein p53,Tumor suppressor p53' 
# 
_entity_poly.entity_id                      1 
_entity_poly.type                           'polypeptide(L)' 
_entity_poly.nstd_linkage                   no 
_entity_poly.nstd_monomer                   no 
_entity_poly.pdbx_seq_one_letter_code       
;GSSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKLFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTE
VVRRCPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSVVVPCEPPEVGSDCTTIHYNYMCYSSCMGGMNRRPI
LTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNT
;
_entity_poly.pdbx_seq_one_letter_code_can   
;GSSSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKLFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTE
VVRRCPHHERCSDSDGLAPPQHLIRVEGNLRAEYLDDRNTFRHSVVVPCEPPEVGSDCTTIHYNYMCYSSCMGGMNRRPI
LTIITLEDSSGNLLGRDSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNT
;
_entity_poly.pdbx_strand_id                 A,B 
_entity_poly.pdbx_target_identifier         ? 
# 
loop_
_pdbx_entity_nonpoly.entity_id 
_pdbx_entity_nonpoly.name 
_pdbx_entity_nonpoly.comp_id 
2 
'2-{3-[4-(methanesulfonyl)-2-methoxyanilino]prop-1-yn-1-yl}-N-(1-methylpiperidin-4-yl)-1-(2,2,2-trifluoroethyl)-1H-indol-4-amine' 
A1ARO 
3 'ZINC ION' ZN    
4 water HOH   
# 
loop_
_entity_poly_seq.entity_id 
_entity_poly_seq.num 
_entity_poly_seq.mon_id 
_entity_poly_seq.hetero 
1 1   GLY n 
1 2   SER n 
1 3   SER n 
1 4   SER n 
1 5   SER n 
1 6   VAL n 
1 7   PRO n 
1 8   SER n 
1 9   GLN n 
1 10  LYS n 
1 11  THR n 
1 12  TYR n 
1 13  GLN n 
1 14  GLY n 
1 15  SER n 
1 16  TYR n 
1 17  GLY n 
1 18  PHE n 
1 19  ARG n 
1 20  LEU n 
1 21  GLY n 
1 22  PHE n 
1 23  LEU n 
1 24  HIS n 
1 25  SER n 
1 26  GLY n 
1 27  THR n 
1 28  ALA n 
1 29  LYS n 
1 30  SER n 
1 31  VAL n 
1 32  THR n 
1 33  CYS n 
1 34  THR n 
1 35  TYR n 
1 36  SER n 
1 37  PRO n 
1 38  ALA n 
1 39  LEU n 
1 40  ASN n 
1 41  LYS n 
1 42  LEU n 
1 43  PHE n 
1 44  CYS n 
1 45  GLN n 
1 46  LEU n 
1 47  ALA n 
1 48  LYS n 
1 49  THR n 
1 50  CYS n 
1 51  PRO n 
1 52  VAL n 
1 53  GLN n 
1 54  LEU n 
1 55  TRP n 
1 56  VAL n 
1 57  ASP n 
1 58  SER n 
1 59  THR n 
1 60  PRO n 
1 61  PRO n 
1 62  PRO n 
1 63  GLY n 
1 64  THR n 
1 65  ARG n 
1 66  VAL n 
1 67  ARG n 
1 68  ALA n 
1 69  MET n 
1 70  ALA n 
1 71  ILE n 
1 72  TYR n 
1 73  LYS n 
1 74  GLN n 
1 75  SER n 
1 76  GLN n 
1 77  HIS n 
1 78  MET n 
1 79  THR n 
1 80  GLU n 
1 81  VAL n 
1 82  VAL n 
1 83  ARG n 
1 84  ARG n 
1 85  CYS n 
1 86  PRO n 
1 87  HIS n 
1 88  HIS n 
1 89  GLU n 
1 90  ARG n 
1 91  CYS n 
1 92  SER n 
1 93  ASP n 
1 94  SER n 
1 95  ASP n 
1 96  GLY n 
1 97  LEU n 
1 98  ALA n 
1 99  PRO n 
1 100 PRO n 
1 101 GLN n 
1 102 HIS n 
1 103 LEU n 
1 104 ILE n 
1 105 ARG n 
1 106 VAL n 
1 107 GLU n 
1 108 GLY n 
1 109 ASN n 
1 110 LEU n 
1 111 ARG n 
1 112 ALA n 
1 113 GLU n 
1 114 TYR n 
1 115 LEU n 
1 116 ASP n 
1 117 ASP n 
1 118 ARG n 
1 119 ASN n 
1 120 THR n 
1 121 PHE n 
1 122 ARG n 
1 123 HIS n 
1 124 SER n 
1 125 VAL n 
1 126 VAL n 
1 127 VAL n 
1 128 PRO n 
1 129 CYS n 
1 130 GLU n 
1 131 PRO n 
1 132 PRO n 
1 133 GLU n 
1 134 VAL n 
1 135 GLY n 
1 136 SER n 
1 137 ASP n 
1 138 CYS n 
1 139 THR n 
1 140 THR n 
1 141 ILE n 
1 142 HIS n 
1 143 TYR n 
1 144 ASN n 
1 145 TYR n 
1 146 MET n 
1 147 CYS n 
1 148 TYR n 
1 149 SER n 
1 150 SER n 
1 151 CYS n 
1 152 MET n 
1 153 GLY n 
1 154 GLY n 
1 155 MET n 
1 156 ASN n 
1 157 ARG n 
1 158 ARG n 
1 159 PRO n 
1 160 ILE n 
1 161 LEU n 
1 162 THR n 
1 163 ILE n 
1 164 ILE n 
1 165 THR n 
1 166 LEU n 
1 167 GLU n 
1 168 ASP n 
1 169 SER n 
1 170 SER n 
1 171 GLY n 
1 172 ASN n 
1 173 LEU n 
1 174 LEU n 
1 175 GLY n 
1 176 ARG n 
1 177 ASP n 
1 178 SER n 
1 179 PHE n 
1 180 GLU n 
1 181 VAL n 
1 182 ARG n 
1 183 VAL n 
1 184 CYS n 
1 185 ALA n 
1 186 CYS n 
1 187 PRO n 
1 188 GLY n 
1 189 ARG n 
1 190 ASP n 
1 191 ARG n 
1 192 ARG n 
1 193 THR n 
1 194 GLU n 
1 195 GLU n 
1 196 GLU n 
1 197 ASN n 
1 198 LEU n 
1 199 ARG n 
1 200 LYS n 
1 201 LYS n 
1 202 GLY n 
1 203 GLU n 
1 204 PRO n 
1 205 HIS n 
1 206 HIS n 
1 207 GLU n 
1 208 LEU n 
1 209 PRO n 
1 210 PRO n 
1 211 GLY n 
1 212 SER n 
1 213 THR n 
1 214 LYS n 
1 215 ARG n 
1 216 ALA n 
1 217 LEU n 
1 218 PRO n 
1 219 ASN n 
1 220 ASN n 
1 221 THR 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                   221 
_entity_src_gen.gene_src_common_name               human 
_entity_src_gen.gene_src_genus                     ? 
_entity_src_gen.pdbx_gene_src_gene                 'TP53, P53' 
_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 BL21(DE3)' 
_entity_src_gen.pdbx_host_org_ncbi_taxonomy_id     469008 
_entity_src_gen.host_org_genus                     ? 
_entity_src_gen.pdbx_host_org_gene                 ? 
_entity_src_gen.pdbx_host_org_organ                ? 
_entity_src_gen.host_org_species                   ? 
_entity_src_gen.pdbx_host_org_tissue               ? 
_entity_src_gen.pdbx_host_org_tissue_fraction      ? 
_entity_src_gen.pdbx_host_org_strain               ? 
_entity_src_gen.pdbx_host_org_variant              ? 
_entity_src_gen.pdbx_host_org_cell_line            ? 
_entity_src_gen.pdbx_host_org_atcc                 ? 
_entity_src_gen.pdbx_host_org_culture_collection   ? 
_entity_src_gen.pdbx_host_org_cell                 ? 
_entity_src_gen.pdbx_host_org_organelle            ? 
_entity_src_gen.pdbx_host_org_cellular_location    ? 
_entity_src_gen.pdbx_host_org_vector_type          ? 
_entity_src_gen.pdbx_host_org_vector               ? 
_entity_src_gen.host_org_details                   ? 
_entity_src_gen.expression_system_id               ? 
_entity_src_gen.plasmid_name                       ? 
_entity_src_gen.plasmid_details                    ? 
_entity_src_gen.pdbx_description                   ? 
# 
loop_
_chem_comp.id 
_chem_comp.type 
_chem_comp.mon_nstd_flag 
_chem_comp.name 
_chem_comp.pdbx_synonyms 
_chem_comp.formula 
_chem_comp.formula_weight 
A1ARO non-polymer         . 
'2-{3-[4-(methanesulfonyl)-2-methoxyanilino]prop-1-yn-1-yl}-N-(1-methylpiperidin-4-yl)-1-(2,2,2-trifluoroethyl)-1H-indol-4-amine' 
? 'C27 H31 F3 N4 O3 S' 548.620 
ALA   'L-peptide linking' y ALANINE ? 'C3 H7 N O2'         89.093  
ARG   'L-peptide linking' y ARGININE ? 'C6 H15 N4 O2 1'     175.209 
ASN   'L-peptide linking' y ASPARAGINE ? 'C4 H8 N2 O3'        132.118 
ASP   'L-peptide linking' y 'ASPARTIC ACID' ? 'C4 H7 N O4'         133.103 
CYS   'L-peptide linking' y CYSTEINE ? 'C3 H7 N O2 S'       121.158 
GLN   'L-peptide linking' y GLUTAMINE ? 'C5 H10 N2 O3'       146.144 
GLU   'L-peptide linking' y 'GLUTAMIC ACID' ? 'C5 H9 N O4'         147.129 
GLY   'peptide linking'   y GLYCINE ? 'C2 H5 N O2'         75.067  
HIS   'L-peptide linking' y HISTIDINE ? 'C6 H10 N3 O2 1'     156.162 
HOH   non-polymer         . WATER ? 'H2 O'               18.015  
ILE   'L-peptide linking' y ISOLEUCINE ? 'C6 H13 N O2'        131.173 
LEU   'L-peptide linking' y LEUCINE ? 'C6 H13 N O2'        131.173 
LYS   'L-peptide linking' y LYSINE ? 'C6 H15 N2 O2 1'     147.195 
MET   'L-peptide linking' y METHIONINE ? 'C5 H11 N O2 S'      149.211 
PHE   'L-peptide linking' y PHENYLALANINE ? 'C9 H11 N O2'        165.189 
PRO   'L-peptide linking' y PROLINE ? 'C5 H9 N O2'         115.130 
SER   'L-peptide linking' y SERINE ? 'C3 H7 N O3'         105.093 
THR   'L-peptide linking' y THREONINE ? 'C4 H9 N O3'         119.119 
TRP   'L-peptide linking' y TRYPTOPHAN ? 'C11 H12 N2 O2'      204.225 
TYR   'L-peptide linking' y TYROSINE ? 'C9 H11 N O3'        181.189 
VAL   'L-peptide linking' y VALINE ? 'C5 H11 N O2'        117.146 
ZN    non-polymer         . 'ZINC ION' ? 'Zn 2'               65.409  
# 
loop_
_pdbx_poly_seq_scheme.asym_id 
_pdbx_poly_seq_scheme.entity_id 
_pdbx_poly_seq_scheme.seq_id 
_pdbx_poly_seq_scheme.mon_id 
_pdbx_poly_seq_scheme.ndb_seq_num 
_pdbx_poly_seq_scheme.pdb_seq_num 
_pdbx_poly_seq_scheme.auth_seq_num 
_pdbx_poly_seq_scheme.pdb_mon_id 
_pdbx_poly_seq_scheme.auth_mon_id 
_pdbx_poly_seq_scheme.pdb_strand_id 
_pdbx_poly_seq_scheme.pdb_ins_code 
_pdbx_poly_seq_scheme.hetero 
A 1 1   GLY 1   92  ?   ?   ?   A . n 
A 1 2   SER 2   93  ?   ?   ?   A . n 
A 1 3   SER 3   94  ?   ?   ?   A . n 
A 1 4   SER 4   95  95  SER SER A . n 
A 1 5   SER 5   96  96  SER SER A . n 
A 1 6   VAL 6   97  97  VAL VAL A . n 
A 1 7   PRO 7   98  98  PRO PRO A . n 
A 1 8   SER 8   99  99  SER SER A . n 
A 1 9   GLN 9   100 100 GLN GLN A . n 
A 1 10  LYS 10  101 101 LYS LYS A . n 
A 1 11  THR 11  102 102 THR THR A . n 
A 1 12  TYR 12  103 103 TYR TYR A . n 
A 1 13  GLN 13  104 104 GLN GLN A . n 
A 1 14  GLY 14  105 105 GLY GLY A . n 
A 1 15  SER 15  106 106 SER SER A . n 
A 1 16  TYR 16  107 107 TYR TYR A . n 
A 1 17  GLY 17  108 108 GLY GLY A . n 
A 1 18  PHE 18  109 109 PHE PHE A . n 
A 1 19  ARG 19  110 110 ARG ARG A . n 
A 1 20  LEU 20  111 111 LEU LEU A . n 
A 1 21  GLY 21  112 112 GLY GLY A . n 
A 1 22  PHE 22  113 113 PHE PHE A . n 
A 1 23  LEU 23  114 114 LEU LEU A . n 
A 1 24  HIS 24  115 115 HIS HIS A . n 
A 1 25  SER 25  116 116 SER SER A . n 
A 1 26  GLY 26  117 117 GLY GLY A . n 
A 1 27  THR 27  118 118 THR THR A . n 
A 1 28  ALA 28  119 119 ALA ALA A . n 
A 1 29  LYS 29  120 120 LYS LYS A . n 
A 1 30  SER 30  121 121 SER SER A . n 
A 1 31  VAL 31  122 122 VAL VAL A . n 
A 1 32  THR 32  123 123 THR THR A . n 
A 1 33  CYS 33  124 124 CYS CYS A . n 
A 1 34  THR 34  125 125 THR THR A . n 
A 1 35  TYR 35  126 126 TYR TYR A . n 
A 1 36  SER 36  127 127 SER SER A . n 
A 1 37  PRO 37  128 128 PRO PRO A . n 
A 1 38  ALA 38  129 129 ALA ALA A . n 
A 1 39  LEU 39  130 130 LEU LEU A . n 
A 1 40  ASN 40  131 131 ASN ASN A . n 
A 1 41  LYS 41  132 132 LYS LYS A . n 
A 1 42  LEU 42  133 133 LEU LEU A . n 
A 1 43  PHE 43  134 134 PHE PHE A . n 
A 1 44  CYS 44  135 135 CYS CYS A . n 
A 1 45  GLN 45  136 136 GLN GLN A . n 
A 1 46  LEU 46  137 137 LEU LEU A . n 
A 1 47  ALA 47  138 138 ALA ALA A . n 
A 1 48  LYS 48  139 139 LYS LYS A . n 
A 1 49  THR 49  140 140 THR THR A . n 
A 1 50  CYS 50  141 141 CYS CYS A . n 
A 1 51  PRO 51  142 142 PRO PRO A . n 
A 1 52  VAL 52  143 143 VAL VAL A . n 
A 1 53  GLN 53  144 144 GLN GLN A . n 
A 1 54  LEU 54  145 145 LEU LEU A . n 
A 1 55  TRP 55  146 146 TRP TRP A . n 
A 1 56  VAL 56  147 147 VAL VAL A . n 
A 1 57  ASP 57  148 148 ASP ASP A . n 
A 1 58  SER 58  149 149 SER SER A . n 
A 1 59  THR 59  150 150 THR THR A . n 
A 1 60  PRO 60  151 151 PRO PRO A . n 
A 1 61  PRO 61  152 152 PRO PRO A . n 
A 1 62  PRO 62  153 153 PRO PRO A . n 
A 1 63  GLY 63  154 154 GLY GLY A . n 
A 1 64  THR 64  155 155 THR THR A . n 
A 1 65  ARG 65  156 156 ARG ARG A . n 
A 1 66  VAL 66  157 157 VAL VAL A . n 
A 1 67  ARG 67  158 158 ARG ARG A . n 
A 1 68  ALA 68  159 159 ALA ALA A . n 
A 1 69  MET 69  160 160 MET MET A . n 
A 1 70  ALA 70  161 161 ALA ALA A . n 
A 1 71  ILE 71  162 162 ILE ILE A . n 
A 1 72  TYR 72  163 163 TYR TYR A . n 
A 1 73  LYS 73  164 164 LYS LYS A . n 
A 1 74  GLN 74  165 165 GLN GLN A . n 
A 1 75  SER 75  166 166 SER SER A . n 
A 1 76  GLN 76  167 167 GLN GLN A . n 
A 1 77  HIS 77  168 168 HIS HIS A . n 
A 1 78  MET 78  169 169 MET MET A . n 
A 1 79  THR 79  170 170 THR THR A . n 
A 1 80  GLU 80  171 171 GLU GLU A . n 
A 1 81  VAL 81  172 172 VAL VAL A . n 
A 1 82  VAL 82  173 173 VAL VAL A . n 
A 1 83  ARG 83  174 174 ARG ARG A . n 
A 1 84  ARG 84  175 175 ARG ARG A . n 
A 1 85  CYS 85  176 176 CYS CYS A . n 
A 1 86  PRO 86  177 177 PRO PRO A . n 
A 1 87  HIS 87  178 178 HIS HIS A . n 
A 1 88  HIS 88  179 179 HIS HIS A . n 
A 1 89  GLU 89  180 180 GLU GLU A . n 
A 1 90  ARG 90  181 181 ARG ARG A . n 
A 1 91  CYS 91  182 182 CYS CYS A . n 
A 1 92  SER 92  183 183 SER SER A . n 
A 1 93  ASP 93  184 184 ASP ASP A . n 
A 1 94  SER 94  185 185 SER SER A . n 
A 1 95  ASP 95  186 186 ASP ASP A . n 
A 1 96  GLY 96  187 187 GLY GLY A . n 
A 1 97  LEU 97  188 188 LEU LEU A . n 
A 1 98  ALA 98  189 189 ALA ALA A . n 
A 1 99  PRO 99  190 190 PRO PRO A . n 
A 1 100 PRO 100 191 191 PRO PRO A . n 
A 1 101 GLN 101 192 192 GLN GLN A . n 
A 1 102 HIS 102 193 193 HIS HIS A . n 
A 1 103 LEU 103 194 194 LEU LEU A . n 
A 1 104 ILE 104 195 195 ILE ILE A . n 
A 1 105 ARG 105 196 196 ARG ARG A . n 
A 1 106 VAL 106 197 197 VAL VAL A . n 
A 1 107 GLU 107 198 198 GLU GLU A . n 
A 1 108 GLY 108 199 199 GLY GLY A . n 
A 1 109 ASN 109 200 200 ASN ASN A . n 
A 1 110 LEU 110 201 201 LEU LEU A . n 
A 1 111 ARG 111 202 202 ARG ARG A . n 
A 1 112 ALA 112 203 203 ALA ALA A . n 
A 1 113 GLU 113 204 204 GLU GLU A . n 
A 1 114 TYR 114 205 205 TYR TYR A . n 
A 1 115 LEU 115 206 206 LEU LEU A . n 
A 1 116 ASP 116 207 207 ASP ASP A . n 
A 1 117 ASP 117 208 208 ASP ASP A . n 
A 1 118 ARG 118 209 209 ARG ARG A . n 
A 1 119 ASN 119 210 210 ASN ASN A . n 
A 1 120 THR 120 211 211 THR THR A . n 
A 1 121 PHE 121 212 212 PHE PHE A . n 
A 1 122 ARG 122 213 213 ARG ARG A . n 
A 1 123 HIS 123 214 214 HIS HIS A . n 
A 1 124 SER 124 215 215 SER SER A . n 
A 1 125 VAL 125 216 216 VAL VAL A . n 
A 1 126 VAL 126 217 217 VAL VAL A . n 
A 1 127 VAL 127 218 218 VAL VAL A . n 
A 1 128 PRO 128 219 219 PRO PRO A . n 
A 1 129 CYS 129 220 220 CYS CYS A . n 
A 1 130 GLU 130 221 221 GLU GLU A . n 
A 1 131 PRO 131 222 222 PRO PRO A . n 
A 1 132 PRO 132 223 223 PRO PRO A . n 
A 1 133 GLU 133 224 224 GLU GLU A . n 
A 1 134 VAL 134 225 225 VAL VAL A . n 
A 1 135 GLY 135 226 226 GLY GLY A . n 
A 1 136 SER 136 227 227 SER SER A . n 
A 1 137 ASP 137 228 228 ASP ASP A . n 
A 1 138 CYS 138 229 229 CYS CYS A . n 
A 1 139 THR 139 230 230 THR THR A . n 
A 1 140 THR 140 231 231 THR THR A . n 
A 1 141 ILE 141 232 232 ILE ILE A . n 
A 1 142 HIS 142 233 233 HIS HIS A . n 
A 1 143 TYR 143 234 234 TYR TYR A . n 
A 1 144 ASN 144 235 235 ASN ASN A . n 
A 1 145 TYR 145 236 236 TYR TYR A . n 
A 1 146 MET 146 237 237 MET MET A . n 
A 1 147 CYS 147 238 238 CYS CYS A . n 
A 1 148 TYR 148 239 239 TYR TYR A . n 
A 1 149 SER 149 240 240 SER SER A . n 
A 1 150 SER 150 241 241 SER SER A . n 
A 1 151 CYS 151 242 242 CYS CYS A . n 
A 1 152 MET 152 243 243 MET MET A . n 
A 1 153 GLY 153 244 244 GLY GLY A . n 
A 1 154 GLY 154 245 245 GLY GLY A . n 
A 1 155 MET 155 246 246 MET MET A . n 
A 1 156 ASN 156 247 247 ASN ASN A . n 
A 1 157 ARG 157 248 248 ARG ARG A . n 
A 1 158 ARG 158 249 249 ARG ARG A . n 
A 1 159 PRO 159 250 250 PRO PRO A . n 
A 1 160 ILE 160 251 251 ILE ILE A . n 
A 1 161 LEU 161 252 252 LEU LEU A . n 
A 1 162 THR 162 253 253 THR THR A . n 
A 1 163 ILE 163 254 254 ILE ILE A . n 
A 1 164 ILE 164 255 255 ILE ILE A . n 
A 1 165 THR 165 256 256 THR THR A . n 
A 1 166 LEU 166 257 257 LEU LEU A . n 
A 1 167 GLU 167 258 258 GLU GLU A . n 
A 1 168 ASP 168 259 259 ASP ASP A . n 
A 1 169 SER 169 260 260 SER SER A . n 
A 1 170 SER 170 261 261 SER SER A . n 
A 1 171 GLY 171 262 262 GLY GLY A . n 
A 1 172 ASN 172 263 263 ASN ASN A . n 
A 1 173 LEU 173 264 264 LEU LEU A . n 
A 1 174 LEU 174 265 265 LEU LEU A . n 
A 1 175 GLY 175 266 266 GLY GLY A . n 
A 1 176 ARG 176 267 267 ARG ARG A . n 
A 1 177 ASP 177 268 268 ASP ASP A . n 
A 1 178 SER 178 269 269 SER SER A . n 
A 1 179 PHE 179 270 270 PHE PHE A . n 
A 1 180 GLU 180 271 271 GLU GLU A . n 
A 1 181 VAL 181 272 272 VAL VAL A . n 
A 1 182 ARG 182 273 273 ARG ARG A . n 
A 1 183 VAL 183 274 274 VAL VAL A . n 
A 1 184 CYS 184 275 275 CYS CYS A . n 
A 1 185 ALA 185 276 276 ALA ALA A . n 
A 1 186 CYS 186 277 277 CYS CYS A . n 
A 1 187 PRO 187 278 278 PRO PRO A . n 
A 1 188 GLY 188 279 279 GLY GLY A . n 
A 1 189 ARG 189 280 280 ARG ARG A . n 
A 1 190 ASP 190 281 281 ASP ASP A . n 
A 1 191 ARG 191 282 282 ARG ARG A . n 
A 1 192 ARG 192 283 283 ARG ARG A . n 
A 1 193 THR 193 284 284 THR THR A . n 
A 1 194 GLU 194 285 285 GLU GLU A . n 
A 1 195 GLU 195 286 286 GLU GLU A . n 
A 1 196 GLU 196 287 287 GLU GLU A . n 
A 1 197 ASN 197 288 288 ASN ASN A . n 
A 1 198 LEU 198 289 289 LEU LEU A . n 
A 1 199 ARG 199 290 290 ARG ARG A . n 
A 1 200 LYS 200 291 291 LYS LYS A . n 
A 1 201 LYS 201 292 ?   ?   ?   A . n 
A 1 202 GLY 202 293 ?   ?   ?   A . n 
A 1 203 GLU 203 294 ?   ?   ?   A . n 
A 1 204 PRO 204 295 ?   ?   ?   A . n 
A 1 205 HIS 205 296 ?   ?   ?   A . n 
A 1 206 HIS 206 297 ?   ?   ?   A . n 
A 1 207 GLU 207 298 ?   ?   ?   A . n 
A 1 208 LEU 208 299 ?   ?   ?   A . n 
A 1 209 PRO 209 300 ?   ?   ?   A . n 
A 1 210 PRO 210 301 ?   ?   ?   A . n 
A 1 211 GLY 211 302 ?   ?   ?   A . n 
A 1 212 SER 212 303 ?   ?   ?   A . n 
A 1 213 THR 213 304 ?   ?   ?   A . n 
A 1 214 LYS 214 305 ?   ?   ?   A . n 
A 1 215 ARG 215 306 ?   ?   ?   A . n 
A 1 216 ALA 216 307 ?   ?   ?   A . n 
A 1 217 LEU 217 308 ?   ?   ?   A . n 
A 1 218 PRO 218 309 ?   ?   ?   A . n 
A 1 219 ASN 219 310 ?   ?   ?   A . n 
A 1 220 ASN 220 311 ?   ?   ?   A . n 
A 1 221 THR 221 312 ?   ?   ?   A . n 
B 1 1   GLY 1   92  92  GLY GLY B . n 
B 1 2   SER 2   93  93  SER SER B . n 
B 1 3   SER 3   94  94  SER SER B . n 
B 1 4   SER 4   95  95  SER SER B . n 
B 1 5   SER 5   96  96  SER SER B . n 
B 1 6   VAL 6   97  97  VAL VAL B . n 
B 1 7   PRO 7   98  98  PRO PRO B . n 
B 1 8   SER 8   99  99  SER SER B . n 
B 1 9   GLN 9   100 100 GLN GLN B . n 
B 1 10  LYS 10  101 101 LYS LYS B . n 
B 1 11  THR 11  102 102 THR THR B . n 
B 1 12  TYR 12  103 103 TYR TYR B . n 
B 1 13  GLN 13  104 104 GLN GLN B . n 
B 1 14  GLY 14  105 105 GLY GLY B . n 
B 1 15  SER 15  106 106 SER SER B . n 
B 1 16  TYR 16  107 107 TYR TYR B . n 
B 1 17  GLY 17  108 108 GLY GLY B . n 
B 1 18  PHE 18  109 109 PHE PHE B . n 
B 1 19  ARG 19  110 110 ARG ARG B . n 
B 1 20  LEU 20  111 111 LEU LEU B . n 
B 1 21  GLY 21  112 112 GLY GLY B . n 
B 1 22  PHE 22  113 113 PHE PHE B . n 
B 1 23  LEU 23  114 114 LEU LEU B . n 
B 1 24  HIS 24  115 115 HIS HIS B . n 
B 1 25  SER 25  116 116 SER SER B . n 
B 1 26  GLY 26  117 117 GLY GLY B . n 
B 1 27  THR 27  118 118 THR THR B . n 
B 1 28  ALA 28  119 119 ALA ALA B . n 
B 1 29  LYS 29  120 120 LYS LYS B . n 
B 1 30  SER 30  121 121 SER SER B . n 
B 1 31  VAL 31  122 122 VAL VAL B . n 
B 1 32  THR 32  123 123 THR THR B . n 
B 1 33  CYS 33  124 124 CYS CYS B . n 
B 1 34  THR 34  125 125 THR THR B . n 
B 1 35  TYR 35  126 126 TYR TYR B . n 
B 1 36  SER 36  127 127 SER SER B . n 
B 1 37  PRO 37  128 128 PRO PRO B . n 
B 1 38  ALA 38  129 129 ALA ALA B . n 
B 1 39  LEU 39  130 130 LEU LEU B . n 
B 1 40  ASN 40  131 131 ASN ASN B . n 
B 1 41  LYS 41  132 132 LYS LYS B . n 
B 1 42  LEU 42  133 133 LEU LEU B . n 
B 1 43  PHE 43  134 134 PHE PHE B . n 
B 1 44  CYS 44  135 135 CYS CYS B . n 
B 1 45  GLN 45  136 136 GLN GLN B . n 
B 1 46  LEU 46  137 137 LEU LEU B . n 
B 1 47  ALA 47  138 138 ALA ALA B . n 
B 1 48  LYS 48  139 139 LYS LYS B . n 
B 1 49  THR 49  140 140 THR THR B . n 
B 1 50  CYS 50  141 141 CYS CYS B . n 
B 1 51  PRO 51  142 142 PRO PRO B . n 
B 1 52  VAL 52  143 143 VAL VAL B . n 
B 1 53  GLN 53  144 144 GLN GLN B . n 
B 1 54  LEU 54  145 145 LEU LEU B . n 
B 1 55  TRP 55  146 146 TRP TRP B . n 
B 1 56  VAL 56  147 147 VAL VAL B . n 
B 1 57  ASP 57  148 148 ASP ASP B . n 
B 1 58  SER 58  149 149 SER SER B . n 
B 1 59  THR 59  150 150 THR THR B . n 
B 1 60  PRO 60  151 151 PRO PRO B . n 
B 1 61  PRO 61  152 152 PRO PRO B . n 
B 1 62  PRO 62  153 153 PRO PRO B . n 
B 1 63  GLY 63  154 154 GLY GLY B . n 
B 1 64  THR 64  155 155 THR THR B . n 
B 1 65  ARG 65  156 156 ARG ARG B . n 
B 1 66  VAL 66  157 157 VAL VAL B . n 
B 1 67  ARG 67  158 158 ARG ARG B . n 
B 1 68  ALA 68  159 159 ALA ALA B . n 
B 1 69  MET 69  160 160 MET MET B . n 
B 1 70  ALA 70  161 161 ALA ALA B . n 
B 1 71  ILE 71  162 162 ILE ILE B . n 
B 1 72  TYR 72  163 163 TYR TYR B . n 
B 1 73  LYS 73  164 164 LYS LYS B . n 
B 1 74  GLN 74  165 165 GLN GLN B . n 
B 1 75  SER 75  166 166 SER SER B . n 
B 1 76  GLN 76  167 167 GLN GLN B . n 
B 1 77  HIS 77  168 168 HIS HIS B . n 
B 1 78  MET 78  169 169 MET MET B . n 
B 1 79  THR 79  170 170 THR THR B . n 
B 1 80  GLU 80  171 171 GLU GLU B . n 
B 1 81  VAL 81  172 172 VAL VAL B . n 
B 1 82  VAL 82  173 173 VAL VAL B . n 
B 1 83  ARG 83  174 174 ARG ARG B . n 
B 1 84  ARG 84  175 175 ARG ARG B . n 
B 1 85  CYS 85  176 176 CYS CYS B . n 
B 1 86  PRO 86  177 177 PRO PRO B . n 
B 1 87  HIS 87  178 178 HIS HIS B . n 
B 1 88  HIS 88  179 179 HIS HIS B . n 
B 1 89  GLU 89  180 180 GLU GLU B . n 
B 1 90  ARG 90  181 181 ARG ARG B . n 
B 1 91  CYS 91  182 182 CYS CYS B . n 
B 1 92  SER 92  183 183 SER SER B . n 
B 1 93  ASP 93  184 184 ASP ASP B . n 
B 1 94  SER 94  185 185 SER SER B . n 
B 1 95  ASP 95  186 186 ASP ASP B . n 
B 1 96  GLY 96  187 187 GLY GLY B . n 
B 1 97  LEU 97  188 188 LEU LEU B . n 
B 1 98  ALA 98  189 189 ALA ALA B . n 
B 1 99  PRO 99  190 190 PRO PRO B . n 
B 1 100 PRO 100 191 191 PRO PRO B . n 
B 1 101 GLN 101 192 192 GLN GLN B . n 
B 1 102 HIS 102 193 193 HIS HIS B . n 
B 1 103 LEU 103 194 194 LEU LEU B . n 
B 1 104 ILE 104 195 195 ILE ILE B . n 
B 1 105 ARG 105 196 196 ARG ARG B . n 
B 1 106 VAL 106 197 197 VAL VAL B . n 
B 1 107 GLU 107 198 198 GLU GLU B . n 
B 1 108 GLY 108 199 199 GLY GLY B . n 
B 1 109 ASN 109 200 200 ASN ASN B . n 
B 1 110 LEU 110 201 201 LEU LEU B . n 
B 1 111 ARG 111 202 202 ARG ARG B . n 
B 1 112 ALA 112 203 203 ALA ALA B . n 
B 1 113 GLU 113 204 204 GLU GLU B . n 
B 1 114 TYR 114 205 205 TYR TYR B . n 
B 1 115 LEU 115 206 206 LEU LEU B . n 
B 1 116 ASP 116 207 207 ASP ASP B . n 
B 1 117 ASP 117 208 208 ASP ASP B . n 
B 1 118 ARG 118 209 209 ARG ARG B . n 
B 1 119 ASN 119 210 210 ASN ASN B . n 
B 1 120 THR 120 211 211 THR THR B . n 
B 1 121 PHE 121 212 212 PHE PHE B . n 
B 1 122 ARG 122 213 213 ARG ARG B . n 
B 1 123 HIS 123 214 214 HIS HIS B . n 
B 1 124 SER 124 215 215 SER SER B . n 
B 1 125 VAL 125 216 216 VAL VAL B . n 
B 1 126 VAL 126 217 217 VAL VAL B . n 
B 1 127 VAL 127 218 218 VAL VAL B . n 
B 1 128 PRO 128 219 219 PRO PRO B . n 
B 1 129 CYS 129 220 220 CYS CYS B . n 
B 1 130 GLU 130 221 221 GLU GLU B . n 
B 1 131 PRO 131 222 222 PRO PRO B . n 
B 1 132 PRO 132 223 223 PRO PRO B . n 
B 1 133 GLU 133 224 224 GLU GLU B . n 
B 1 134 VAL 134 225 225 VAL VAL B . n 
B 1 135 GLY 135 226 226 GLY GLY B . n 
B 1 136 SER 136 227 227 SER SER B . n 
B 1 137 ASP 137 228 228 ASP ASP B . n 
B 1 138 CYS 138 229 229 CYS CYS B . n 
B 1 139 THR 139 230 230 THR THR B . n 
B 1 140 THR 140 231 231 THR THR B . n 
B 1 141 ILE 141 232 232 ILE ILE B . n 
B 1 142 HIS 142 233 233 HIS HIS B . n 
B 1 143 TYR 143 234 234 TYR TYR B . n 
B 1 144 ASN 144 235 235 ASN ASN B . n 
B 1 145 TYR 145 236 236 TYR TYR B . n 
B 1 146 MET 146 237 237 MET MET B . n 
B 1 147 CYS 147 238 238 CYS CYS B . n 
B 1 148 TYR 148 239 239 TYR TYR B . n 
B 1 149 SER 149 240 240 SER SER B . n 
B 1 150 SER 150 241 241 SER SER B . n 
B 1 151 CYS 151 242 242 CYS CYS B . n 
B 1 152 MET 152 243 243 MET MET B . n 
B 1 153 GLY 153 244 244 GLY GLY B . n 
B 1 154 GLY 154 245 245 GLY GLY B . n 
B 1 155 MET 155 246 246 MET MET B . n 
B 1 156 ASN 156 247 247 ASN ASN B . n 
B 1 157 ARG 157 248 248 ARG ARG B . n 
B 1 158 ARG 158 249 249 ARG ARG B . n 
B 1 159 PRO 159 250 250 PRO PRO B . n 
B 1 160 ILE 160 251 251 ILE ILE B . n 
B 1 161 LEU 161 252 252 LEU LEU B . n 
B 1 162 THR 162 253 253 THR THR B . n 
B 1 163 ILE 163 254 254 ILE ILE B . n 
B 1 164 ILE 164 255 255 ILE ILE B . n 
B 1 165 THR 165 256 256 THR THR B . n 
B 1 166 LEU 166 257 257 LEU LEU B . n 
B 1 167 GLU 167 258 258 GLU GLU B . n 
B 1 168 ASP 168 259 259 ASP ASP B . n 
B 1 169 SER 169 260 260 SER SER B . n 
B 1 170 SER 170 261 261 SER SER B . n 
B 1 171 GLY 171 262 262 GLY GLY B . n 
B 1 172 ASN 172 263 263 ASN ASN B . n 
B 1 173 LEU 173 264 264 LEU LEU B . n 
B 1 174 LEU 174 265 265 LEU LEU B . n 
B 1 175 GLY 175 266 266 GLY GLY B . n 
B 1 176 ARG 176 267 267 ARG ARG B . n 
B 1 177 ASP 177 268 268 ASP ASP B . n 
B 1 178 SER 178 269 269 SER SER B . n 
B 1 179 PHE 179 270 270 PHE PHE B . n 
B 1 180 GLU 180 271 271 GLU GLU B . n 
B 1 181 VAL 181 272 272 VAL VAL B . n 
B 1 182 ARG 182 273 273 ARG ARG B . n 
B 1 183 VAL 183 274 274 VAL VAL B . n 
B 1 184 CYS 184 275 275 CYS CYS B . n 
B 1 185 ALA 185 276 276 ALA ALA B . n 
B 1 186 CYS 186 277 277 CYS CYS B . n 
B 1 187 PRO 187 278 278 PRO PRO B . n 
B 1 188 GLY 188 279 279 GLY GLY B . n 
B 1 189 ARG 189 280 280 ARG ARG B . n 
B 1 190 ASP 190 281 281 ASP ASP B . n 
B 1 191 ARG 191 282 282 ARG ARG B . n 
B 1 192 ARG 192 283 283 ARG ARG B . n 
B 1 193 THR 193 284 284 THR THR B . n 
B 1 194 GLU 194 285 285 GLU GLU B . n 
B 1 195 GLU 195 286 286 GLU GLU B . n 
B 1 196 GLU 196 287 287 GLU GLU B . n 
B 1 197 ASN 197 288 288 ASN ASN B . n 
B 1 198 LEU 198 289 289 LEU LEU B . n 
B 1 199 ARG 199 290 290 ARG ARG B . n 
B 1 200 LYS 200 291 291 LYS LYS B . n 
B 1 201 LYS 201 292 292 LYS LYS B . n 
B 1 202 GLY 202 293 ?   ?   ?   B . n 
B 1 203 GLU 203 294 ?   ?   ?   B . n 
B 1 204 PRO 204 295 ?   ?   ?   B . n 
B 1 205 HIS 205 296 ?   ?   ?   B . n 
B 1 206 HIS 206 297 ?   ?   ?   B . n 
B 1 207 GLU 207 298 ?   ?   ?   B . n 
B 1 208 LEU 208 299 ?   ?   ?   B . n 
B 1 209 PRO 209 300 ?   ?   ?   B . n 
B 1 210 PRO 210 301 ?   ?   ?   B . n 
B 1 211 GLY 211 302 ?   ?   ?   B . n 
B 1 212 SER 212 303 ?   ?   ?   B . n 
B 1 213 THR 213 304 ?   ?   ?   B . n 
B 1 214 LYS 214 305 ?   ?   ?   B . n 
B 1 215 ARG 215 306 ?   ?   ?   B . n 
B 1 216 ALA 216 307 ?   ?   ?   B . n 
B 1 217 LEU 217 308 ?   ?   ?   B . n 
B 1 218 PRO 218 309 ?   ?   ?   B . n 
B 1 219 ASN 219 310 ?   ?   ?   B . n 
B 1 220 ASN 220 311 ?   ?   ?   B . n 
B 1 221 THR 221 312 ?   ?   ?   B . n 
# 
_pdbx_entity_instance_feature.ordinal        1 
_pdbx_entity_instance_feature.comp_id        A1ARO 
_pdbx_entity_instance_feature.asym_id        ? 
_pdbx_entity_instance_feature.seq_num        ? 
_pdbx_entity_instance_feature.auth_comp_id   A1ARO 
_pdbx_entity_instance_feature.auth_asym_id   ? 
_pdbx_entity_instance_feature.auth_seq_num   ? 
_pdbx_entity_instance_feature.feature_type   'SUBJECT OF INVESTIGATION' 
_pdbx_entity_instance_feature.details        ? 
# 
loop_
_pdbx_nonpoly_scheme.asym_id 
_pdbx_nonpoly_scheme.entity_id 
_pdbx_nonpoly_scheme.mon_id 
_pdbx_nonpoly_scheme.ndb_seq_num 
_pdbx_nonpoly_scheme.pdb_seq_num 
_pdbx_nonpoly_scheme.auth_seq_num 
_pdbx_nonpoly_scheme.pdb_mon_id 
_pdbx_nonpoly_scheme.auth_mon_id 
_pdbx_nonpoly_scheme.pdb_strand_id 
_pdbx_nonpoly_scheme.pdb_ins_code 
C 2 A1ARO 1   401 300 A1ARO 709 A . 
D 3 ZN    1   402 301 ZN    ZN  A . 
E 2 A1ARO 1   401 300 A1ARO 709 B . 
F 3 ZN    1   402 301 ZN    ZN  B . 
G 4 HOH   1   501 326 HOH   HOH A . 
G 4 HOH   2   502 285 HOH   HOH A . 
G 4 HOH   3   503 324 HOH   HOH A . 
G 4 HOH   4   504 154 HOH   HOH A . 
G 4 HOH   5   505 236 HOH   HOH A . 
G 4 HOH   6   506 260 HOH   HOH A . 
G 4 HOH   7   507 85  HOH   HOH A . 
G 4 HOH   8   508 153 HOH   HOH A . 
G 4 HOH   9   509 189 HOH   HOH A . 
G 4 HOH   10  510 312 HOH   HOH A . 
G 4 HOH   11  511 26  HOH   HOH A . 
G 4 HOH   12  512 273 HOH   HOH A . 
G 4 HOH   13  513 311 HOH   HOH A . 
G 4 HOH   14  514 395 HOH   HOH A . 
G 4 HOH   15  515 496 HOH   HOH A . 
G 4 HOH   16  516 305 HOH   HOH A . 
G 4 HOH   17  517 278 HOH   HOH A . 
G 4 HOH   18  518 277 HOH   HOH A . 
G 4 HOH   19  519 31  HOH   HOH A . 
G 4 HOH   20  520 325 HOH   HOH A . 
G 4 HOH   21  521 111 HOH   HOH A . 
G 4 HOH   22  522 379 HOH   HOH A . 
G 4 HOH   23  523 222 HOH   HOH A . 
G 4 HOH   24  524 105 HOH   HOH A . 
G 4 HOH   25  525 77  HOH   HOH A . 
G 4 HOH   26  526 181 HOH   HOH A . 
G 4 HOH   27  527 7   HOH   HOH A . 
G 4 HOH   28  528 226 HOH   HOH A . 
G 4 HOH   29  529 145 HOH   HOH A . 
G 4 HOH   30  530 437 HOH   HOH A . 
G 4 HOH   31  531 415 HOH   HOH A . 
G 4 HOH   32  532 5   HOH   HOH A . 
G 4 HOH   33  533 433 HOH   HOH A . 
G 4 HOH   34  534 220 HOH   HOH A . 
G 4 HOH   35  535 274 HOH   HOH A . 
G 4 HOH   36  536 27  HOH   HOH A . 
G 4 HOH   37  537 92  HOH   HOH A . 
G 4 HOH   38  538 49  HOH   HOH A . 
G 4 HOH   39  539 294 HOH   HOH A . 
G 4 HOH   40  540 2   HOH   HOH A . 
G 4 HOH   41  541 190 HOH   HOH A . 
G 4 HOH   42  542 163 HOH   HOH A . 
G 4 HOH   43  543 199 HOH   HOH A . 
G 4 HOH   44  544 68  HOH   HOH A . 
G 4 HOH   45  545 32  HOH   HOH A . 
G 4 HOH   46  546 168 HOH   HOH A . 
G 4 HOH   47  547 272 HOH   HOH A . 
G 4 HOH   48  548 98  HOH   HOH A . 
G 4 HOH   49  549 341 HOH   HOH A . 
G 4 HOH   50  550 104 HOH   HOH A . 
G 4 HOH   51  551 461 HOH   HOH A . 
G 4 HOH   52  552 125 HOH   HOH A . 
G 4 HOH   53  553 25  HOH   HOH A . 
G 4 HOH   54  554 340 HOH   HOH A . 
G 4 HOH   55  555 56  HOH   HOH A . 
G 4 HOH   56  556 333 HOH   HOH A . 
G 4 HOH   57  557 3   HOH   HOH A . 
G 4 HOH   58  558 322 HOH   HOH A . 
G 4 HOH   59  559 182 HOH   HOH A . 
G 4 HOH   60  560 40  HOH   HOH A . 
G 4 HOH   61  561 127 HOH   HOH A . 
G 4 HOH   62  562 269 HOH   HOH A . 
G 4 HOH   63  563 96  HOH   HOH A . 
G 4 HOH   64  564 33  HOH   HOH A . 
G 4 HOH   65  565 41  HOH   HOH A . 
G 4 HOH   66  566 4   HOH   HOH A . 
G 4 HOH   67  567 95  HOH   HOH A . 
G 4 HOH   68  568 178 HOH   HOH A . 
G 4 HOH   69  569 169 HOH   HOH A . 
G 4 HOH   70  570 93  HOH   HOH A . 
G 4 HOH   71  571 128 HOH   HOH A . 
G 4 HOH   72  572 449 HOH   HOH A . 
G 4 HOH   73  573 28  HOH   HOH A . 
G 4 HOH   74  574 216 HOH   HOH A . 
G 4 HOH   75  575 15  HOH   HOH A . 
G 4 HOH   76  576 73  HOH   HOH A . 
G 4 HOH   77  577 19  HOH   HOH A . 
G 4 HOH   78  578 464 HOH   HOH A . 
G 4 HOH   79  579 103 HOH   HOH A . 
G 4 HOH   80  580 87  HOH   HOH A . 
G 4 HOH   81  581 370 HOH   HOH A . 
G 4 HOH   82  582 43  HOH   HOH A . 
G 4 HOH   83  583 66  HOH   HOH A . 
G 4 HOH   84  584 51  HOH   HOH A . 
G 4 HOH   85  585 120 HOH   HOH A . 
G 4 HOH   86  586 286 HOH   HOH A . 
G 4 HOH   87  587 8   HOH   HOH A . 
G 4 HOH   88  588 259 HOH   HOH A . 
G 4 HOH   89  589 152 HOH   HOH A . 
G 4 HOH   90  590 348 HOH   HOH A . 
G 4 HOH   91  591 391 HOH   HOH A . 
G 4 HOH   92  592 202 HOH   HOH A . 
G 4 HOH   93  593 30  HOH   HOH A . 
G 4 HOH   94  594 465 HOH   HOH A . 
G 4 HOH   95  595 185 HOH   HOH A . 
G 4 HOH   96  596 310 HOH   HOH A . 
G 4 HOH   97  597 194 HOH   HOH A . 
G 4 HOH   98  598 519 HOH   HOH A . 
G 4 HOH   99  599 146 HOH   HOH A . 
G 4 HOH   100 600 201 HOH   HOH A . 
G 4 HOH   101 601 76  HOH   HOH A . 
G 4 HOH   102 602 399 HOH   HOH A . 
G 4 HOH   103 603 198 HOH   HOH A . 
G 4 HOH   104 604 36  HOH   HOH A . 
G 4 HOH   105 605 432 HOH   HOH A . 
G 4 HOH   106 606 89  HOH   HOH A . 
G 4 HOH   107 607 143 HOH   HOH A . 
G 4 HOH   108 608 246 HOH   HOH A . 
G 4 HOH   109 609 235 HOH   HOH A . 
G 4 HOH   110 610 304 HOH   HOH A . 
G 4 HOH   111 611 380 HOH   HOH A . 
G 4 HOH   112 612 238 HOH   HOH A . 
G 4 HOH   113 613 446 HOH   HOH A . 
G 4 HOH   114 614 115 HOH   HOH A . 
G 4 HOH   115 615 297 HOH   HOH A . 
G 4 HOH   116 616 210 HOH   HOH A . 
G 4 HOH   117 617 522 HOH   HOH A . 
G 4 HOH   118 618 71  HOH   HOH A . 
G 4 HOH   119 619 179 HOH   HOH A . 
G 4 HOH   120 620 233 HOH   HOH A . 
G 4 HOH   121 621 242 HOH   HOH A . 
G 4 HOH   122 622 70  HOH   HOH A . 
G 4 HOH   123 623 315 HOH   HOH A . 
G 4 HOH   124 624 331 HOH   HOH A . 
G 4 HOH   125 625 6   HOH   HOH A . 
G 4 HOH   126 626 288 HOH   HOH A . 
G 4 HOH   127 627 476 HOH   HOH A . 
G 4 HOH   128 628 225 HOH   HOH A . 
G 4 HOH   129 629 525 HOH   HOH A . 
G 4 HOH   130 630 241 HOH   HOH A . 
G 4 HOH   131 631 488 HOH   HOH A . 
G 4 HOH   132 632 334 HOH   HOH A . 
G 4 HOH   133 633 126 HOH   HOH A . 
G 4 HOH   134 634 57  HOH   HOH A . 
G 4 HOH   135 635 400 HOH   HOH A . 
G 4 HOH   136 636 301 HOH   HOH A . 
G 4 HOH   137 637 356 HOH   HOH A . 
G 4 HOH   138 638 90  HOH   HOH A . 
G 4 HOH   139 639 316 HOH   HOH A . 
G 4 HOH   140 640 59  HOH   HOH A . 
G 4 HOH   141 641 228 HOH   HOH A . 
G 4 HOH   142 642 293 HOH   HOH A . 
G 4 HOH   143 643 440 HOH   HOH A . 
G 4 HOH   144 644 81  HOH   HOH A . 
G 4 HOH   145 645 147 HOH   HOH A . 
G 4 HOH   146 646 318 HOH   HOH A . 
G 4 HOH   147 647 117 HOH   HOH A . 
G 4 HOH   148 648 218 HOH   HOH A . 
G 4 HOH   149 649 74  HOH   HOH A . 
G 4 HOH   150 650 106 HOH   HOH A . 
G 4 HOH   151 651 211 HOH   HOH A . 
G 4 HOH   152 652 369 HOH   HOH A . 
G 4 HOH   153 653 336 HOH   HOH A . 
G 4 HOH   154 654 377 HOH   HOH A . 
G 4 HOH   155 655 419 HOH   HOH A . 
G 4 HOH   156 656 175 HOH   HOH A . 
G 4 HOH   157 657 513 HOH   HOH A . 
G 4 HOH   158 658 157 HOH   HOH A . 
G 4 HOH   159 659 151 HOH   HOH A . 
G 4 HOH   160 660 492 HOH   HOH A . 
G 4 HOH   161 661 387 HOH   HOH A . 
G 4 HOH   162 662 122 HOH   HOH A . 
G 4 HOH   163 663 197 HOH   HOH A . 
G 4 HOH   164 664 252 HOH   HOH A . 
G 4 HOH   165 665 313 HOH   HOH A . 
G 4 HOH   166 666 23  HOH   HOH A . 
G 4 HOH   167 667 244 HOH   HOH A . 
G 4 HOH   168 668 162 HOH   HOH A . 
G 4 HOH   169 669 123 HOH   HOH A . 
G 4 HOH   170 670 88  HOH   HOH A . 
G 4 HOH   171 671 435 HOH   HOH A . 
G 4 HOH   172 672 428 HOH   HOH A . 
G 4 HOH   173 673 114 HOH   HOH A . 
G 4 HOH   174 674 35  HOH   HOH A . 
G 4 HOH   175 675 180 HOH   HOH A . 
G 4 HOH   176 676 234 HOH   HOH A . 
G 4 HOH   177 677 394 HOH   HOH A . 
G 4 HOH   178 678 212 HOH   HOH A . 
G 4 HOH   179 679 365 HOH   HOH A . 
G 4 HOH   180 680 347 HOH   HOH A . 
G 4 HOH   181 681 319 HOH   HOH A . 
G 4 HOH   182 682 509 HOH   HOH A . 
G 4 HOH   183 683 424 HOH   HOH A . 
G 4 HOH   184 684 75  HOH   HOH A . 
G 4 HOH   185 685 384 HOH   HOH A . 
G 4 HOH   186 686 46  HOH   HOH A . 
G 4 HOH   187 687 500 HOH   HOH A . 
G 4 HOH   188 688 452 HOH   HOH A . 
G 4 HOH   189 689 250 HOH   HOH A . 
G 4 HOH   190 690 191 HOH   HOH A . 
G 4 HOH   191 691 350 HOH   HOH A . 
G 4 HOH   192 692 511 HOH   HOH A . 
G 4 HOH   193 693 473 HOH   HOH A . 
G 4 HOH   194 694 489 HOH   HOH A . 
G 4 HOH   195 695 442 HOH   HOH A . 
G 4 HOH   196 696 388 HOH   HOH A . 
G 4 HOH   197 697 524 HOH   HOH A . 
G 4 HOH   198 698 296 HOH   HOH A . 
G 4 HOH   199 699 256 HOH   HOH A . 
G 4 HOH   200 700 360 HOH   HOH A . 
G 4 HOH   201 701 243 HOH   HOH A . 
G 4 HOH   202 702 483 HOH   HOH A . 
G 4 HOH   203 703 327 HOH   HOH A . 
G 4 HOH   204 704 14  HOH   HOH A . 
G 4 HOH   205 705 378 HOH   HOH A . 
G 4 HOH   206 706 405 HOH   HOH A . 
G 4 HOH   207 707 364 HOH   HOH A . 
G 4 HOH   208 708 239 HOH   HOH A . 
G 4 HOH   209 709 478 HOH   HOH A . 
G 4 HOH   210 710 450 HOH   HOH A . 
G 4 HOH   211 711 94  HOH   HOH A . 
G 4 HOH   212 712 510 HOH   HOH A . 
G 4 HOH   213 713 361 HOH   HOH A . 
G 4 HOH   214 714 393 HOH   HOH A . 
G 4 HOH   215 715 448 HOH   HOH A . 
G 4 HOH   216 716 460 HOH   HOH A . 
G 4 HOH   217 717 262 HOH   HOH A . 
G 4 HOH   218 718 455 HOH   HOH A . 
G 4 HOH   219 719 362 HOH   HOH A . 
G 4 HOH   220 720 411 HOH   HOH A . 
G 4 HOH   221 721 410 HOH   HOH A . 
G 4 HOH   222 722 150 HOH   HOH A . 
G 4 HOH   223 723 61  HOH   HOH A . 
G 4 HOH   224 724 512 HOH   HOH A . 
G 4 HOH   225 725 282 HOH   HOH A . 
G 4 HOH   226 726 470 HOH   HOH A . 
G 4 HOH   227 727 192 HOH   HOH A . 
G 4 HOH   228 728 404 HOH   HOH A . 
G 4 HOH   229 729 422 HOH   HOH A . 
G 4 HOH   230 730 490 HOH   HOH A . 
G 4 HOH   231 731 447 HOH   HOH A . 
G 4 HOH   232 732 501 HOH   HOH A . 
G 4 HOH   233 733 445 HOH   HOH A . 
G 4 HOH   234 734 306 HOH   HOH A . 
G 4 HOH   235 735 469 HOH   HOH A . 
G 4 HOH   236 736 339 HOH   HOH A . 
G 4 HOH   237 737 453 HOH   HOH A . 
G 4 HOH   238 738 139 HOH   HOH A . 
G 4 HOH   239 739 430 HOH   HOH A . 
G 4 HOH   240 740 83  HOH   HOH A . 
G 4 HOH   241 741 475 HOH   HOH A . 
G 4 HOH   242 742 371 HOH   HOH A . 
G 4 HOH   243 743 354 HOH   HOH A . 
G 4 HOH   244 744 487 HOH   HOH A . 
G 4 HOH   245 745 417 HOH   HOH A . 
G 4 HOH   246 746 454 HOH   HOH A . 
G 4 HOH   247 747 426 HOH   HOH A . 
G 4 HOH   248 748 171 HOH   HOH A . 
G 4 HOH   249 749 398 HOH   HOH A . 
G 4 HOH   250 750 367 HOH   HOH A . 
G 4 HOH   251 751 397 HOH   HOH A . 
G 4 HOH   252 752 134 HOH   HOH A . 
G 4 HOH   253 753 479 HOH   HOH A . 
G 4 HOH   254 754 214 HOH   HOH A . 
G 4 HOH   255 755 477 HOH   HOH A . 
G 4 HOH   256 756 418 HOH   HOH A . 
G 4 HOH   257 757 203 HOH   HOH A . 
G 4 HOH   258 758 474 HOH   HOH A . 
G 4 HOH   259 759 160 HOH   HOH A . 
G 4 HOH   260 760 321 HOH   HOH A . 
G 4 HOH   261 761 409 HOH   HOH A . 
G 4 HOH   262 762 441 HOH   HOH A . 
H 4 HOH   1   501 320 HOH   HOH B . 
H 4 HOH   2   502 208 HOH   HOH B . 
H 4 HOH   3   503 135 HOH   HOH B . 
H 4 HOH   4   504 414 HOH   HOH B . 
H 4 HOH   5   505 121 HOH   HOH B . 
H 4 HOH   6   506 174 HOH   HOH B . 
H 4 HOH   7   507 267 HOH   HOH B . 
H 4 HOH   8   508 349 HOH   HOH B . 
H 4 HOH   9   509 80  HOH   HOH B . 
H 4 HOH   10  510 200 HOH   HOH B . 
H 4 HOH   11  511 344 HOH   HOH B . 
H 4 HOH   12  512 29  HOH   HOH B . 
H 4 HOH   13  513 193 HOH   HOH B . 
H 4 HOH   14  514 131 HOH   HOH B . 
H 4 HOH   15  515 132 HOH   HOH B . 
H 4 HOH   16  516 39  HOH   HOH B . 
H 4 HOH   17  517 300 HOH   HOH B . 
H 4 HOH   18  518 295 HOH   HOH B . 
H 4 HOH   19  519 22  HOH   HOH B . 
H 4 HOH   20  520 100 HOH   HOH B . 
H 4 HOH   21  521 196 HOH   HOH B . 
H 4 HOH   22  522 266 HOH   HOH B . 
H 4 HOH   23  523 498 HOH   HOH B . 
H 4 HOH   24  524 280 HOH   HOH B . 
H 4 HOH   25  525 308 HOH   HOH B . 
H 4 HOH   26  526 119 HOH   HOH B . 
H 4 HOH   27  527 281 HOH   HOH B . 
H 4 HOH   28  528 137 HOH   HOH B . 
H 4 HOH   29  529 392 HOH   HOH B . 
H 4 HOH   30  530 186 HOH   HOH B . 
H 4 HOH   31  531 101 HOH   HOH B . 
H 4 HOH   32  532 284 HOH   HOH B . 
H 4 HOH   33  533 20  HOH   HOH B . 
H 4 HOH   34  534 44  HOH   HOH B . 
H 4 HOH   35  535 52  HOH   HOH B . 
H 4 HOH   36  536 45  HOH   HOH B . 
H 4 HOH   37  537 38  HOH   HOH B . 
H 4 HOH   38  538 138 HOH   HOH B . 
H 4 HOH   39  539 82  HOH   HOH B . 
H 4 HOH   40  540 53  HOH   HOH B . 
H 4 HOH   41  541 48  HOH   HOH B . 
H 4 HOH   42  542 13  HOH   HOH B . 
H 4 HOH   43  543 18  HOH   HOH B . 
H 4 HOH   44  544 16  HOH   HOH B . 
H 4 HOH   45  545 161 HOH   HOH B . 
H 4 HOH   46  546 343 HOH   HOH B . 
H 4 HOH   47  547 429 HOH   HOH B . 
H 4 HOH   48  548 332 HOH   HOH B . 
H 4 HOH   49  549 97  HOH   HOH B . 
H 4 HOH   50  550 118 HOH   HOH B . 
H 4 HOH   51  551 60  HOH   HOH B . 
H 4 HOH   52  552 79  HOH   HOH B . 
H 4 HOH   53  553 247 HOH   HOH B . 
H 4 HOH   54  554 17  HOH   HOH B . 
H 4 HOH   55  555 521 HOH   HOH B . 
H 4 HOH   56  556 457 HOH   HOH B . 
H 4 HOH   57  557 155 HOH   HOH B . 
H 4 HOH   58  558 330 HOH   HOH B . 
H 4 HOH   59  559 62  HOH   HOH B . 
H 4 HOH   60  560 133 HOH   HOH B . 
H 4 HOH   61  561 78  HOH   HOH B . 
H 4 HOH   62  562 408 HOH   HOH B . 
H 4 HOH   63  563 223 HOH   HOH B . 
H 4 HOH   64  564 63  HOH   HOH B . 
H 4 HOH   65  565 58  HOH   HOH B . 
H 4 HOH   66  566 279 HOH   HOH B . 
H 4 HOH   67  567 11  HOH   HOH B . 
H 4 HOH   68  568 108 HOH   HOH B . 
H 4 HOH   69  569 263 HOH   HOH B . 
H 4 HOH   70  570 439 HOH   HOH B . 
H 4 HOH   71  571 270 HOH   HOH B . 
H 4 HOH   72  572 12  HOH   HOH B . 
H 4 HOH   73  573 486 HOH   HOH B . 
H 4 HOH   74  574 396 HOH   HOH B . 
H 4 HOH   75  575 54  HOH   HOH B . 
H 4 HOH   76  576 221 HOH   HOH B . 
H 4 HOH   77  577 109 HOH   HOH B . 
H 4 HOH   78  578 156 HOH   HOH B . 
H 4 HOH   79  579 72  HOH   HOH B . 
H 4 HOH   80  580 412 HOH   HOH B . 
H 4 HOH   81  581 385 HOH   HOH B . 
H 4 HOH   82  582 219 HOH   HOH B . 
H 4 HOH   83  583 204 HOH   HOH B . 
H 4 HOH   84  584 255 HOH   HOH B . 
H 4 HOH   85  585 69  HOH   HOH B . 
H 4 HOH   86  586 366 HOH   HOH B . 
H 4 HOH   87  587 37  HOH   HOH B . 
H 4 HOH   88  588 251 HOH   HOH B . 
H 4 HOH   89  589 290 HOH   HOH B . 
H 4 HOH   90  590 335 HOH   HOH B . 
H 4 HOH   91  591 1   HOH   HOH B . 
H 4 HOH   92  592 172 HOH   HOH B . 
H 4 HOH   93  593 376 HOH   HOH B . 
H 4 HOH   94  594 141 HOH   HOH B . 
H 4 HOH   95  595 229 HOH   HOH B . 
H 4 HOH   96  596 47  HOH   HOH B . 
H 4 HOH   97  597 130 HOH   HOH B . 
H 4 HOH   98  598 183 HOH   HOH B . 
H 4 HOH   99  599 389 HOH   HOH B . 
H 4 HOH   100 600 124 HOH   HOH B . 
H 4 HOH   101 601 526 HOH   HOH B . 
H 4 HOH   102 602 21  HOH   HOH B . 
H 4 HOH   103 603 421 HOH   HOH B . 
H 4 HOH   104 604 375 HOH   HOH B . 
H 4 HOH   105 605 374 HOH   HOH B . 
H 4 HOH   106 606 227 HOH   HOH B . 
H 4 HOH   107 607 65  HOH   HOH B . 
H 4 HOH   108 608 206 HOH   HOH B . 
H 4 HOH   109 609 355 HOH   HOH B . 
H 4 HOH   110 610 24  HOH   HOH B . 
H 4 HOH   111 611 275 HOH   HOH B . 
H 4 HOH   112 612 102 HOH   HOH B . 
H 4 HOH   113 613 10  HOH   HOH B . 
H 4 HOH   114 614 253 HOH   HOH B . 
H 4 HOH   115 615 64  HOH   HOH B . 
H 4 HOH   116 616 50  HOH   HOH B . 
H 4 HOH   117 617 42  HOH   HOH B . 
H 4 HOH   118 618 144 HOH   HOH B . 
H 4 HOH   119 619 434 HOH   HOH B . 
H 4 HOH   120 620 177 HOH   HOH B . 
H 4 HOH   121 621 328 HOH   HOH B . 
H 4 HOH   122 622 140 HOH   HOH B . 
H 4 HOH   123 623 254 HOH   HOH B . 
H 4 HOH   124 624 264 HOH   HOH B . 
H 4 HOH   125 625 67  HOH   HOH B . 
H 4 HOH   126 626 337 HOH   HOH B . 
H 4 HOH   127 627 289 HOH   HOH B . 
H 4 HOH   128 628 298 HOH   HOH B . 
H 4 HOH   129 629 129 HOH   HOH B . 
H 4 HOH   130 630 224 HOH   HOH B . 
H 4 HOH   131 631 142 HOH   HOH B . 
H 4 HOH   132 632 148 HOH   HOH B . 
H 4 HOH   133 633 507 HOH   HOH B . 
H 4 HOH   134 634 237 HOH   HOH B . 
H 4 HOH   135 635 245 HOH   HOH B . 
H 4 HOH   136 636 258 HOH   HOH B . 
H 4 HOH   137 637 184 HOH   HOH B . 
H 4 HOH   138 638 287 HOH   HOH B . 
H 4 HOH   139 639 484 HOH   HOH B . 
H 4 HOH   140 640 205 HOH   HOH B . 
H 4 HOH   141 641 456 HOH   HOH B . 
H 4 HOH   142 642 240 HOH   HOH B . 
H 4 HOH   143 643 495 HOH   HOH B . 
H 4 HOH   144 644 188 HOH   HOH B . 
H 4 HOH   145 645 420 HOH   HOH B . 
H 4 HOH   146 646 338 HOH   HOH B . 
H 4 HOH   147 647 165 HOH   HOH B . 
H 4 HOH   148 648 136 HOH   HOH B . 
H 4 HOH   149 649 213 HOH   HOH B . 
H 4 HOH   150 650 84  HOH   HOH B . 
H 4 HOH   151 651 149 HOH   HOH B . 
H 4 HOH   152 652 459 HOH   HOH B . 
H 4 HOH   153 653 209 HOH   HOH B . 
H 4 HOH   154 654 176 HOH   HOH B . 
H 4 HOH   155 655 170 HOH   HOH B . 
H 4 HOH   156 656 110 HOH   HOH B . 
H 4 HOH   157 657 317 HOH   HOH B . 
H 4 HOH   158 658 159 HOH   HOH B . 
H 4 HOH   159 659 438 HOH   HOH B . 
H 4 HOH   160 660 359 HOH   HOH B . 
H 4 HOH   161 661 116 HOH   HOH B . 
H 4 HOH   162 662 99  HOH   HOH B . 
H 4 HOH   163 663 472 HOH   HOH B . 
H 4 HOH   164 664 381 HOH   HOH B . 
H 4 HOH   165 665 480 HOH   HOH B . 
H 4 HOH   166 666 485 HOH   HOH B . 
H 4 HOH   167 667 352 HOH   HOH B . 
H 4 HOH   168 668 265 HOH   HOH B . 
H 4 HOH   169 669 86  HOH   HOH B . 
H 4 HOH   170 670 164 HOH   HOH B . 
H 4 HOH   171 671 158 HOH   HOH B . 
H 4 HOH   172 672 34  HOH   HOH B . 
H 4 HOH   173 673 276 HOH   HOH B . 
H 4 HOH   174 674 443 HOH   HOH B . 
H 4 HOH   175 675 187 HOH   HOH B . 
H 4 HOH   176 676 342 HOH   HOH B . 
H 4 HOH   177 677 215 HOH   HOH B . 
H 4 HOH   178 678 346 HOH   HOH B . 
H 4 HOH   179 679 231 HOH   HOH B . 
H 4 HOH   180 680 514 HOH   HOH B . 
H 4 HOH   181 681 518 HOH   HOH B . 
H 4 HOH   182 682 504 HOH   HOH B . 
H 4 HOH   183 683 195 HOH   HOH B . 
H 4 HOH   184 684 386 HOH   HOH B . 
H 4 HOH   185 685 248 HOH   HOH B . 
H 4 HOH   186 686 167 HOH   HOH B . 
H 4 HOH   187 687 9   HOH   HOH B . 
H 4 HOH   188 688 217 HOH   HOH B . 
H 4 HOH   189 689 283 HOH   HOH B . 
H 4 HOH   190 690 390 HOH   HOH B . 
H 4 HOH   191 691 413 HOH   HOH B . 
H 4 HOH   192 692 291 HOH   HOH B . 
H 4 HOH   193 693 173 HOH   HOH B . 
H 4 HOH   194 694 302 HOH   HOH B . 
H 4 HOH   195 695 427 HOH   HOH B . 
H 4 HOH   196 696 444 HOH   HOH B . 
H 4 HOH   197 697 508 HOH   HOH B . 
H 4 HOH   198 698 372 HOH   HOH B . 
H 4 HOH   199 699 407 HOH   HOH B . 
H 4 HOH   200 700 268 HOH   HOH B . 
H 4 HOH   201 701 307 HOH   HOH B . 
H 4 HOH   202 702 261 HOH   HOH B . 
H 4 HOH   203 703 482 HOH   HOH B . 
H 4 HOH   204 704 112 HOH   HOH B . 
H 4 HOH   205 705 494 HOH   HOH B . 
H 4 HOH   206 706 351 HOH   HOH B . 
H 4 HOH   207 707 382 HOH   HOH B . 
H 4 HOH   208 708 368 HOH   HOH B . 
H 4 HOH   209 709 345 HOH   HOH B . 
H 4 HOH   210 710 358 HOH   HOH B . 
H 4 HOH   211 711 323 HOH   HOH B . 
H 4 HOH   212 712 383 HOH   HOH B . 
H 4 HOH   213 713 416 HOH   HOH B . 
H 4 HOH   214 714 436 HOH   HOH B . 
H 4 HOH   215 715 230 HOH   HOH B . 
H 4 HOH   216 716 517 HOH   HOH B . 
H 4 HOH   217 717 516 HOH   HOH B . 
H 4 HOH   218 718 505 HOH   HOH B . 
H 4 HOH   219 719 314 HOH   HOH B . 
H 4 HOH   220 720 506 HOH   HOH B . 
H 4 HOH   221 721 166 HOH   HOH B . 
H 4 HOH   222 722 232 HOH   HOH B . 
H 4 HOH   223 723 491 HOH   HOH B . 
H 4 HOH   224 724 329 HOH   HOH B . 
H 4 HOH   225 725 373 HOH   HOH B . 
H 4 HOH   226 726 462 HOH   HOH B . 
H 4 HOH   227 727 403 HOH   HOH B . 
H 4 HOH   228 728 401 HOH   HOH B . 
H 4 HOH   229 729 493 HOH   HOH B . 
H 4 HOH   230 730 523 HOH   HOH B . 
H 4 HOH   231 731 463 HOH   HOH B . 
H 4 HOH   232 732 353 HOH   HOH B . 
H 4 HOH   233 733 292 HOH   HOH B . 
H 4 HOH   234 734 257 HOH   HOH B . 
H 4 HOH   235 735 467 HOH   HOH B . 
H 4 HOH   236 736 503 HOH   HOH B . 
H 4 HOH   237 737 458 HOH   HOH B . 
H 4 HOH   238 738 357 HOH   HOH B . 
H 4 HOH   239 739 249 HOH   HOH B . 
H 4 HOH   240 740 309 HOH   HOH B . 
H 4 HOH   241 741 451 HOH   HOH B . 
H 4 HOH   242 742 515 HOH   HOH B . 
H 4 HOH   243 743 207 HOH   HOH B . 
H 4 HOH   244 744 402 HOH   HOH B . 
H 4 HOH   245 745 468 HOH   HOH B . 
H 4 HOH   246 746 423 HOH   HOH B . 
H 4 HOH   247 747 55  HOH   HOH B . 
H 4 HOH   248 748 363 HOH   HOH B . 
H 4 HOH   249 749 299 HOH   HOH B . 
H 4 HOH   250 750 499 HOH   HOH B . 
H 4 HOH   251 751 502 HOH   HOH B . 
H 4 HOH   252 752 91  HOH   HOH B . 
H 4 HOH   253 753 520 HOH   HOH B . 
H 4 HOH   254 754 471 HOH   HOH B . 
H 4 HOH   255 755 271 HOH   HOH B . 
H 4 HOH   256 756 481 HOH   HOH B . 
H 4 HOH   257 757 431 HOH   HOH B . 
H 4 HOH   258 758 497 HOH   HOH B . 
H 4 HOH   259 759 113 HOH   HOH B . 
H 4 HOH   260 760 107 HOH   HOH B . 
H 4 HOH   261 761 303 HOH   HOH B . 
H 4 HOH   262 762 425 HOH   HOH B . 
H 4 HOH   263 763 466 HOH   HOH B . 
H 4 HOH   264 764 406 HOH   HOH B . 
# 
loop_
_pdbx_unobs_or_zero_occ_atoms.id 
_pdbx_unobs_or_zero_occ_atoms.PDB_model_num 
_pdbx_unobs_or_zero_occ_atoms.polymer_flag 
_pdbx_unobs_or_zero_occ_atoms.occupancy_flag 
_pdbx_unobs_or_zero_occ_atoms.auth_asym_id 
_pdbx_unobs_or_zero_occ_atoms.auth_comp_id 
_pdbx_unobs_or_zero_occ_atoms.auth_seq_id 
_pdbx_unobs_or_zero_occ_atoms.PDB_ins_code 
_pdbx_unobs_or_zero_occ_atoms.auth_atom_id 
_pdbx_unobs_or_zero_occ_atoms.label_alt_id 
_pdbx_unobs_or_zero_occ_atoms.label_asym_id 
_pdbx_unobs_or_zero_occ_atoms.label_comp_id 
_pdbx_unobs_or_zero_occ_atoms.label_seq_id 
_pdbx_unobs_or_zero_occ_atoms.label_atom_id 
1  1 Y 1 A VAL 97  ? CG1 ? A VAL 6   CG1 
2  1 Y 1 A VAL 97  ? CG2 ? A VAL 6   CG2 
3  1 Y 1 A LYS 120 ? CG  ? A LYS 29  CG  
4  1 Y 1 A LYS 120 ? CD  ? A LYS 29  CD  
5  1 Y 1 A LYS 120 ? CE  ? A LYS 29  CE  
6  1 Y 1 A LYS 120 ? NZ  ? A LYS 29  NZ  
7  1 Y 1 A ARG 202 ? CG  ? A ARG 111 CG  
8  1 Y 1 A ARG 202 ? CD  ? A ARG 111 CD  
9  1 Y 1 A ARG 202 ? NE  ? A ARG 111 NE  
10 1 Y 1 A ARG 202 ? CZ  ? A ARG 111 CZ  
11 1 Y 1 A ARG 202 ? NH1 ? A ARG 111 NH1 
12 1 Y 1 A ARG 202 ? NH2 ? A ARG 111 NH2 
13 1 Y 1 A ARG 209 ? CG  ? A ARG 118 CG  
14 1 Y 1 A ARG 209 ? CD  ? A ARG 118 CD  
15 1 Y 1 A ARG 209 ? NE  ? A ARG 118 NE  
16 1 Y 1 A ARG 209 ? CZ  ? A ARG 118 CZ  
17 1 Y 1 A ARG 209 ? NH1 ? A ARG 118 NH1 
18 1 Y 1 A ARG 209 ? NH2 ? A ARG 118 NH2 
19 1 Y 1 A GLU 224 ? CG  ? A GLU 133 CG  
20 1 Y 1 A GLU 224 ? CD  ? A GLU 133 CD  
21 1 Y 1 A GLU 224 ? OE1 ? A GLU 133 OE1 
22 1 Y 1 A GLU 224 ? OE2 ? A GLU 133 OE2 
23 1 Y 1 A ARG 280 ? CG  ? A ARG 189 CG  
24 1 Y 1 A ARG 280 ? CD  ? A ARG 189 CD  
25 1 Y 1 A ARG 280 ? NE  ? A ARG 189 NE  
26 1 Y 1 A ARG 280 ? CZ  ? A ARG 189 CZ  
27 1 Y 1 A ARG 280 ? NH1 ? A ARG 189 NH1 
28 1 Y 1 A ARG 280 ? NH2 ? A ARG 189 NH2 
29 1 Y 1 A ARG 290 ? CG  ? A ARG 199 CG  
30 1 Y 1 A ARG 290 ? CD  ? A ARG 199 CD  
31 1 Y 1 A ARG 290 ? NE  ? A ARG 199 NE  
32 1 Y 1 A ARG 290 ? CZ  ? A ARG 199 CZ  
33 1 Y 1 A ARG 290 ? NH1 ? A ARG 199 NH1 
34 1 Y 1 A ARG 290 ? NH2 ? A ARG 199 NH2 
35 1 Y 1 A LYS 291 ? CG  ? A LYS 200 CG  
36 1 Y 1 A LYS 291 ? CD  ? A LYS 200 CD  
37 1 Y 1 A LYS 291 ? CE  ? A LYS 200 CE  
38 1 Y 1 A LYS 291 ? NZ  ? A LYS 200 NZ  
39 1 Y 1 B LYS 120 ? CG  ? B LYS 29  CG  
40 1 Y 1 B LYS 120 ? CD  ? B LYS 29  CD  
41 1 Y 1 B LYS 120 ? CE  ? B LYS 29  CE  
42 1 Y 1 B LYS 120 ? NZ  ? B LYS 29  NZ  
43 1 Y 1 B ARG 202 ? CG  ? B ARG 111 CG  
44 1 Y 1 B ARG 202 ? CD  ? B ARG 111 CD  
45 1 Y 1 B ARG 202 ? NE  ? B ARG 111 NE  
46 1 Y 1 B ARG 202 ? CZ  ? B ARG 111 CZ  
47 1 Y 1 B ARG 202 ? NH1 ? B ARG 111 NH1 
48 1 Y 1 B ARG 202 ? NH2 ? B ARG 111 NH2 
49 1 Y 1 B ARG 209 ? CG  ? B ARG 118 CG  
50 1 Y 1 B ARG 209 ? CD  ? B ARG 118 CD  
51 1 Y 1 B ARG 209 ? NE  ? B ARG 118 NE  
52 1 Y 1 B ARG 209 ? CZ  ? B ARG 118 CZ  
53 1 Y 1 B ARG 209 ? NH1 ? B ARG 118 NH1 
54 1 Y 1 B ARG 209 ? NH2 ? B ARG 118 NH2 
55 1 Y 1 B ARG 280 ? CG  ? B ARG 189 CG  
56 1 Y 1 B ARG 280 ? CD  ? B ARG 189 CD  
57 1 Y 1 B ARG 280 ? NE  ? B ARG 189 NE  
58 1 Y 1 B ARG 280 ? CZ  ? B ARG 189 CZ  
59 1 Y 1 B ARG 280 ? NH1 ? B ARG 189 NH1 
60 1 Y 1 B ARG 280 ? NH2 ? B ARG 189 NH2 
61 1 Y 1 B ARG 290 ? CG  ? B ARG 199 CG  
62 1 Y 1 B ARG 290 ? CD  ? B ARG 199 CD  
63 1 Y 1 B ARG 290 ? NE  ? B ARG 199 NE  
64 1 Y 1 B ARG 290 ? CZ  ? B ARG 199 CZ  
65 1 Y 1 B ARG 290 ? NH1 ? B ARG 199 NH1 
66 1 Y 1 B ARG 290 ? NH2 ? B ARG 199 NH2 
67 1 Y 1 B LYS 291 ? CG  ? B LYS 200 CG  
68 1 Y 1 B LYS 291 ? CD  ? B LYS 200 CD  
69 1 Y 1 B LYS 291 ? CE  ? B LYS 200 CE  
70 1 Y 1 B LYS 291 ? NZ  ? B LYS 200 NZ  
71 1 Y 1 B LYS 292 ? CG  ? B LYS 201 CG  
72 1 Y 1 B LYS 292 ? CD  ? B LYS 201 CD  
73 1 Y 1 B LYS 292 ? CE  ? B LYS 201 CE  
74 1 Y 1 B LYS 292 ? NZ  ? B LYS 201 NZ  
# 
loop_
_software.citation_id 
_software.classification 
_software.compiler_name 
_software.compiler_version 
_software.contact_author 
_software.contact_author_email 
_software.date 
_software.description 
_software.dependencies 
_software.hardware 
_software.language 
_software.location 
_software.mods 
_software.name 
_software.os 
_software.os_version 
_software.type 
_software.version 
_software.pdbx_ordinal 
? 'data reduction'  ? ? ? ? ? ? ? ? ? ? ? XDS         ? ? ? .           1 
? 'data scaling'    ? ? ? ? ? ? ? ? ? ? ? XSCALE      ? ? ? .           2 
? refinement        ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? 1.11.1_2575 3 
? 'data extraction' ? ? ? ? ? ? ? ? ? ? ? PDB_EXTRACT ? ? ? 3.28        4 
? phasing           ? ? ? ? ? ? ? ? ? ? ? PHENIX      ? ? ? .           5 
# 
_cell.angle_alpha                  90.000 
_cell.angle_alpha_esd              ? 
_cell.angle_beta                   90.000 
_cell.angle_beta_esd               ? 
_cell.angle_gamma                  90.000 
_cell.angle_gamma_esd              ? 
_cell.entry_id                     9BR3 
_cell.details                      ? 
_cell.formula_units_Z              ? 
_cell.length_a                     64.960 
_cell.length_a_esd                 ? 
_cell.length_b                     71.210 
_cell.length_b_esd                 ? 
_cell.length_c                     104.850 
_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                         9BR3 
_symmetry.cell_setting                     ? 
_symmetry.Int_Tables_number                19 
_symmetry.space_group_name_Hall            ? 
_symmetry.space_group_name_H-M             'P 21 21 21' 
_symmetry.pdbx_full_space_group_name_H-M   ? 
# 
_exptl.absorpt_coefficient_mu     ? 
_exptl.absorpt_correction_T_max   ? 
_exptl.absorpt_correction_T_min   ? 
_exptl.absorpt_correction_type    ? 
_exptl.absorpt_process_details    ? 
_exptl.entry_id                   9BR3 
_exptl.crystals_number            1 
_exptl.details                    ? 
_exptl.method                     'X-RAY DIFFRACTION' 
_exptl.method_details             ? 
# 
_exptl_crystal.colour                       ? 
_exptl_crystal.density_diffrn               ? 
_exptl_crystal.density_Matthews             2.46 
_exptl_crystal.density_method               ? 
_exptl_crystal.density_percent_sol          49.99 
_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    
;p53, CID 3799, at 6.93mg/ml; Optimization screen PMV1-opt1 e3: 16% PEG 8000, 20% glycerol, 20mM K2HPO4; protein + 1mM BSI 107743; cryo: direct; crystal tracking ID 285723e3, puck tai0-7
;
_exptl_crystal_grow.pdbx_pH_range   ? 
_exptl_crystal_grow.temp            289 
# 
_diffrn.ambient_environment              ? 
_diffrn.ambient_temp                     100 
_diffrn.ambient_temp_details             ? 
_diffrn.ambient_temp_esd                 ? 
_diffrn.crystal_id                       1 
_diffrn.crystal_support                  ? 
_diffrn.crystal_treatment                ? 
_diffrn.details                          ? 
_diffrn.id                               1 
_diffrn.ambient_pressure                 ? 
_diffrn.ambient_pressure_esd             ? 
_diffrn.ambient_pressure_gt              ? 
_diffrn.ambient_pressure_lt              ? 
_diffrn.ambient_temp_gt                  ? 
_diffrn.ambient_temp_lt                  ? 
_diffrn.pdbx_serial_crystal_experiment   N 
# 
_diffrn_detector.details                      ? 
_diffrn_detector.detector                     CCD 
_diffrn_detector.diffrn_id                    1 
_diffrn_detector.type                         'RAYONIX MX-300' 
_diffrn_detector.area_resol_mean              ? 
_diffrn_detector.dtime                        ? 
_diffrn_detector.pdbx_frames_total            ? 
_diffrn_detector.pdbx_collection_time_total   ? 
_diffrn_detector.pdbx_collection_date         2016-11-09 
_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   0.97872 
_diffrn_radiation_wavelength.wt           1.0 
# 
_diffrn_source.current                     ? 
_diffrn_source.details                     ? 
_diffrn_source.diffrn_id                   1 
_diffrn_source.power                       ? 
_diffrn_source.size                        ? 
_diffrn_source.source                      SYNCHROTRON 
_diffrn_source.target                      ? 
_diffrn_source.type                        'APS BEAMLINE 21-ID-F' 
_diffrn_source.voltage                     ? 
_diffrn_source.take-off_angle              ? 
_diffrn_source.pdbx_wavelength_list        0.97872 
_diffrn_source.pdbx_wavelength             ? 
_diffrn_source.pdbx_synchrotron_beamline   21-ID-F 
_diffrn_source.pdbx_synchrotron_site       APS 
# 
_reflns.B_iso_Wilson_estimate                          13.594 
_reflns.entry_id                                       9BR3 
_reflns.data_reduction_details                         ? 
_reflns.data_reduction_method                          ? 
_reflns.d_resolution_high                              1.900 
_reflns.d_resolution_low                               47.991 
_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                                     38106 
_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                           97.600 
_reflns.R_free_details                                 ? 
_reflns.Rmerge_F_all                                   ? 
_reflns.Rmerge_F_obs                                   ? 
_reflns.Friedel_coverage                               ? 
_reflns.number_gt                                      ? 
_reflns.threshold_expression                           ? 
_reflns.pdbx_redundancy                                6.097 
_reflns.pdbx_netI_over_av_sigmaI                       ? 
_reflns.pdbx_netI_over_sigmaI                          14.910 
_reflns.pdbx_res_netI_over_av_sigmaI_2                 ? 
_reflns.pdbx_res_netI_over_sigmaI_2                    ? 
_reflns.pdbx_chi_squared                               0.938 
_reflns.pdbx_scaling_rejects                           ? 
_reflns.pdbx_d_res_high_opt                            ? 
_reflns.pdbx_d_res_low_opt                             ? 
_reflns.pdbx_d_res_opt_method                          ? 
_reflns.phase_calculation_details                      ? 
_reflns.pdbx_Rrim_I_all                                0.107 
_reflns.pdbx_Rpim_I_all                                ? 
_reflns.pdbx_d_opt                                     ? 
_reflns.pdbx_number_measured_all                       232344 
_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                              0.098 
_reflns.pdbx_Rmerge_I_all                              ? 
_reflns.pdbx_Rsym_value                                ? 
_reflns.pdbx_CC_split_method                           ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_1_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_2_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[1]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[2]   ? 
_reflns.pdbx_aniso_diffraction_limit_axis_3_ortho[3]   ? 
_reflns.pdbx_aniso_diffraction_limit_1                 ? 
_reflns.pdbx_aniso_diffraction_limit_2                 ? 
_reflns.pdbx_aniso_diffraction_limit_3                 ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_1_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_2_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[1]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[2]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvector_3_ortho[3]     ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_1               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_2               ? 
_reflns.pdbx_aniso_B_tensor_eigenvalue_3               ? 
_reflns.pdbx_orthogonalization_convention              ? 
_reflns.pdbx_percent_possible_ellipsoidal              ? 
_reflns.pdbx_percent_possible_spherical                ? 
_reflns.pdbx_percent_possible_ellipsoidal_anomalous    ? 
_reflns.pdbx_percent_possible_spherical_anomalous      ? 
_reflns.pdbx_redundancy_anomalous                      ? 
_reflns.pdbx_CC_half_anomalous                         ? 
_reflns.pdbx_absDiff_over_sigma_anomalous              ? 
_reflns.pdbx_percent_possible_anomalous                ? 
_reflns.pdbx_observed_signal_threshold                 ? 
_reflns.pdbx_signal_type                               ? 
_reflns.pdbx_signal_details                            ? 
_reflns.pdbx_signal_software_id                        ? 
# 
loop_
_reflns_shell.d_res_high 
_reflns_shell.d_res_low 
_reflns_shell.meanI_over_sigI_all 
_reflns_shell.meanI_over_sigI_obs 
_reflns_shell.number_measured_all 
_reflns_shell.number_measured_obs 
_reflns_shell.number_possible 
_reflns_shell.number_unique_all 
_reflns_shell.number_unique_obs 
_reflns_shell.percent_possible_obs 
_reflns_shell.Rmerge_F_all 
_reflns_shell.Rmerge_F_obs 
_reflns_shell.meanI_over_sigI_gt 
_reflns_shell.meanI_over_uI_all 
_reflns_shell.meanI_over_uI_gt 
_reflns_shell.number_measured_gt 
_reflns_shell.number_unique_gt 
_reflns_shell.percent_possible_gt 
_reflns_shell.Rmerge_F_gt 
_reflns_shell.Rmerge_I_gt 
_reflns_shell.pdbx_redundancy 
_reflns_shell.pdbx_chi_squared 
_reflns_shell.pdbx_netI_over_sigmaI_all 
_reflns_shell.pdbx_netI_over_sigmaI_obs 
_reflns_shell.pdbx_Rrim_I_all 
_reflns_shell.pdbx_Rpim_I_all 
_reflns_shell.pdbx_rejects 
_reflns_shell.pdbx_ordinal 
_reflns_shell.pdbx_diffrn_id 
_reflns_shell.pdbx_CC_half 
_reflns_shell.pdbx_CC_star 
_reflns_shell.pdbx_R_split 
_reflns_shell.percent_possible_all 
_reflns_shell.Rmerge_I_all 
_reflns_shell.Rmerge_I_obs 
_reflns_shell.pdbx_Rsym_value 
_reflns_shell.pdbx_percent_possible_ellipsoidal 
_reflns_shell.pdbx_percent_possible_spherical 
_reflns_shell.pdbx_percent_possible_ellipsoidal_anomalous 
_reflns_shell.pdbx_percent_possible_spherical_anomalous 
_reflns_shell.pdbx_redundancy_anomalous 
_reflns_shell.pdbx_CC_half_anomalous 
_reflns_shell.pdbx_absDiff_over_sigma_anomalous 
_reflns_shell.pdbx_percent_possible_anomalous 
1.900 1.950  ? 4.170  ? 12266 2831 ? 2297 ? ? ? ? ? ? ? ? ? ? ? 5.340 ? ? ? 0.432 ? ? 1  1 0.933 ? ? 81.100 ? 0.390 ? ? ? ? ? ? ? 
? ? 
1.950 2.000  ? 5.080  ? 15286 2782 ? 2721 ? ? ? ? ? ? ? ? ? ? ? 5.618 ? ? ? 0.372 ? ? 2  1 0.933 ? ? 97.800 ? 0.337 ? ? ? ? ? ? ? 
? ? 
2.000 2.060  ? 6.090  ? 16594 2703 ? 2656 ? ? ? ? ? ? ? ? ? ? ? 6.248 ? ? ? 0.334 ? ? 3  1 0.958 ? ? 98.300 ? 0.306 ? ? ? ? ? ? ? 
? ? 
2.060 2.120  ? 7.070  ? 16162 2613 ? 2571 ? ? ? ? ? ? ? ? ? ? ? 6.286 ? ? ? 0.291 ? ? 4  1 0.969 ? ? 98.400 ? 0.267 ? ? ? ? ? ? ? 
? ? 
2.120 2.190  ? 8.460  ? 15926 2568 ? 2532 ? ? ? ? ? ? ? ? ? ? ? 6.290 ? ? ? 0.236 ? ? 5  1 0.982 ? ? 98.600 ? 0.217 ? ? ? ? ? ? ? 
? ? 
2.190 2.270  ? 9.530  ? 15105 2446 ? 2409 ? ? ? ? ? ? ? ? ? ? ? 6.270 ? ? ? 0.209 ? ? 6  1 0.983 ? ? 98.500 ? 0.192 ? ? ? ? ? ? ? 
? ? 
2.270 2.360  ? 10.720 ? 14870 2398 ? 2370 ? ? ? ? ? ? ? ? ? ? ? 6.274 ? ? ? 0.180 ? ? 7  1 0.988 ? ? 98.800 ? 0.165 ? ? ? ? ? ? ? 
? ? 
2.360 2.450  ? 11.300 ? 14188 2300 ? 2262 ? ? ? ? ? ? ? ? ? ? ? 6.272 ? ? ? 0.167 ? ? 8  1 0.990 ? ? 98.300 ? 0.153 ? ? ? ? ? ? ? 
? ? 
2.450 2.560  ? 12.530 ? 13613 2194 ? 2171 ? ? ? ? ? ? ? ? ? ? ? 6.270 ? ? ? 0.147 ? ? 9  1 0.991 ? ? 99.000 ? 0.135 ? ? ? ? ? ? ? 
? ? 
2.560 2.690  ? 13.850 ? 13224 2132 ? 2116 ? ? ? ? ? ? ? ? ? ? ? 6.250 ? ? ? 0.131 ? ? 10 1 0.993 ? ? 99.200 ? 0.121 ? ? ? ? ? ? ? 
? ? 
2.690 2.830  ? 16.130 ? 12464 2019 ? 2003 ? ? ? ? ? ? ? ? ? ? ? 6.223 ? ? ? 0.112 ? ? 11 1 0.994 ? ? 99.200 ? 0.103 ? ? ? ? ? ? ? 
? ? 
2.830 3.000  ? 18.210 ? 11754 1901 ? 1883 ? ? ? ? ? ? ? ? ? ? ? 6.242 ? ? ? 0.094 ? ? 12 1 0.997 ? ? 99.100 ? 0.086 ? ? ? ? ? ? ? 
? ? 
3.000 3.210  ? 22.420 ? 11089 1798 ? 1792 ? ? ? ? ? ? ? ? ? ? ? 6.188 ? ? ? 0.074 ? ? 13 1 0.998 ? ? 99.700 ? 0.067 ? ? ? ? ? ? ? 
? ? 
3.210 3.470  ? 25.960 ? 10278 1681 ? 1670 ? ? ? ? ? ? ? ? ? ? ? 6.154 ? ? ? 0.062 ? ? 14 1 0.998 ? ? 99.300 ? 0.056 ? ? ? ? ? ? ? 
? ? 
3.470 3.800  ? 28.930 ? 9466  1558 ? 1549 ? ? ? ? ? ? ? ? ? ? ? 6.111 ? ? ? 0.054 ? ? 15 1 0.998 ? ? 99.400 ? 0.049 ? ? ? ? ? ? ? 
? ? 
3.800 4.250  ? 32.210 ? 8580  1420 ? 1412 ? ? ? ? ? ? ? ? ? ? ? 6.076 ? ? ? 0.045 ? ? 16 1 0.999 ? ? 99.400 ? 0.041 ? ? ? ? ? ? ? 
? ? 
4.250 4.910  ? 33.730 ? 7591  1264 ? 1260 ? ? ? ? ? ? ? ? ? ? ? 6.025 ? ? ? 0.043 ? ? 17 1 0.999 ? ? 99.700 ? 0.039 ? ? ? ? ? ? ? 
? ? 
4.910 6.010  ? 31.810 ? 6403  1082 ? 1079 ? ? ? ? ? ? ? ? ? ? ? 5.934 ? ? ? 0.043 ? ? 18 1 0.999 ? ? 99.700 ? 0.039 ? ? ? ? ? ? ? 
? ? 
6.010 8.500  ? 29.280 ? 4884  851  ? 850  ? ? ? ? ? ? ? ? ? ? ? 5.746 ? ? ? 0.047 ? ? 19 1 0.999 ? ? 99.900 ? 0.043 ? ? ? ? ? ? ? 
? ? 
8.500 47.991 ? 32.860 ? 2601  511  ? 503  ? ? ? ? ? ? ? ? ? ? ? 5.171 ? ? ? 0.038 ? ? 20 1 0.998 ? ? 98.400 ? 0.034 ? ? ? ? ? ? ? 
? ? 
# 
_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                                73.670 
_refine.B_iso_mean                               17.8918 
_refine.B_iso_min                                5.290 
_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                                 9BR3 
_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                            1.9000 
_refine.ls_d_res_low                             47.9910 
_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                     38095 
_refine.ls_number_reflns_R_free                  2036 
_refine.ls_number_reflns_R_work                  36059 
_refine.ls_number_restraints                     ? 
_refine.ls_percent_reflns_obs                    97.5500 
_refine.ls_percent_reflns_R_free                 5.3400 
_refine.ls_R_factor_all                          ? 
_refine.ls_R_factor_obs                          0.1537 
_refine.ls_R_factor_R_free                       0.1910 
_refine.ls_R_factor_R_free_error                 ? 
_refine.ls_R_factor_R_free_error_details         ? 
_refine.ls_R_factor_R_work                       0.1516 
_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                          1.340 
_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            0 
_refine.pdbx_stereochem_target_val_spec_case     ? 
_refine.pdbx_overall_ESU_R                       ? 
_refine.pdbx_overall_ESU_R_Free                  ? 
_refine.pdbx_solvent_vdw_probe_radii             1.1100 
_refine.pdbx_solvent_ion_probe_radii             ? 
_refine.pdbx_solvent_shrinkage_radii             0.9000 
_refine.pdbx_real_space_R                        ? 
_refine.pdbx_density_correlation                 ? 
_refine.pdbx_pd_number_of_powder_patterns        ? 
_refine.pdbx_pd_number_of_points                 ? 
_refine.pdbx_pd_meas_number_of_points            ? 
_refine.pdbx_pd_proc_ls_prof_R_factor            ? 
_refine.pdbx_pd_proc_ls_prof_wR_factor           ? 
_refine.pdbx_pd_Marquardt_correlation_coeff      ? 
_refine.pdbx_pd_Fsqrd_R_factor                   ? 
_refine.pdbx_pd_ls_matrix_band_width             ? 
_refine.pdbx_overall_phase_error                 18.0200 
_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                            0.1600 
_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                         final 
_refine_hist.details                          ? 
_refine_hist.d_res_high                       1.9000 
_refine_hist.d_res_low                        47.9910 
_refine_hist.number_atoms_solvent             531 
_refine_hist.number_atoms_total               3650 
_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       398 
_refine_hist.pdbx_B_iso_mean_ligand           18.04 
_refine_hist.pdbx_B_iso_mean_solvent          27.58 
_refine_hist.pdbx_number_atoms_protein        3041 
_refine_hist.pdbx_number_atoms_nucleic_acid   0 
_refine_hist.pdbx_number_atoms_ligand         78 
_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' ? 0.007  ? 3290 ? f_bond_d           ? ? 
'X-RAY DIFFRACTION' ? 0.829  ? 4514 ? f_angle_d          ? ? 
'X-RAY DIFFRACTION' ? 0.056  ? 494  ? f_chiral_restr     ? ? 
'X-RAY DIFFRACTION' ? 0.007  ? 587  ? f_plane_restr      ? ? 
'X-RAY DIFFRACTION' ? 14.985 ? 2018 ? f_dihedral_angle_d ? ? 
# 
loop_
_refine_ls_shell.pdbx_refine_id 
_refine_ls_shell.d_res_high 
_refine_ls_shell.d_res_low 
_refine_ls_shell.number_reflns_all 
_refine_ls_shell.number_reflns_obs 
_refine_ls_shell.number_reflns_R_free 
_refine_ls_shell.number_reflns_R_work 
_refine_ls_shell.percent_reflns_obs 
_refine_ls_shell.percent_reflns_R_free 
_refine_ls_shell.R_factor_all 
_refine_ls_shell.R_factor_obs 
_refine_ls_shell.R_factor_R_free_error 
_refine_ls_shell.R_factor_R_work 
_refine_ls_shell.redundancy_reflns_all 
_refine_ls_shell.redundancy_reflns_obs 
_refine_ls_shell.wR_factor_all 
_refine_ls_shell.wR_factor_obs 
_refine_ls_shell.wR_factor_R_free 
_refine_ls_shell.wR_factor_R_work 
_refine_ls_shell.pdbx_R_complete 
_refine_ls_shell.pdbx_total_number_of_bins_used 
_refine_ls_shell.pdbx_phase_error 
_refine_ls_shell.pdbx_fsc_work 
_refine_ls_shell.pdbx_fsc_free 
_refine_ls_shell.R_factor_R_free 
'X-RAY DIFFRACTION' 1.9    1.9441 . . 114 1932 80.0000  . . . 0.0000 0.1873 . . . . . . . . . . . 0.2452 
'X-RAY DIFFRACTION' 1.9441 1.9928 . . 129 2342 97.0000  . . . 0.0000 0.1760 . . . . . . . . . . . 0.2083 
'X-RAY DIFFRACTION' 1.9928 2.0466 . . 132 2380 98.0000  . . . 0.0000 0.1657 . . . . . . . . . . . 0.2269 
'X-RAY DIFFRACTION' 2.0466 2.1069 . . 142 2398 98.0000  . . . 0.0000 0.1625 . . . . . . . . . . . 0.2214 
'X-RAY DIFFRACTION' 2.1069 2.1749 . . 155 2376 99.0000  . . . 0.0000 0.1488 . . . . . . . . . . . 0.1889 
'X-RAY DIFFRACTION' 2.1749 2.2526 . . 137 2385 99.0000  . . . 0.0000 0.1422 . . . . . . . . . . . 0.1847 
'X-RAY DIFFRACTION' 2.2526 2.3428 . . 133 2417 99.0000  . . . 0.0000 0.1458 . . . . . . . . . . . 0.1985 
'X-RAY DIFFRACTION' 2.3428 2.4494 . . 119 2435 99.0000  . . . 0.0000 0.1476 . . . . . . . . . . . 0.2019 
'X-RAY DIFFRACTION' 2.4494 2.5785 . . 148 2415 99.0000  . . . 0.0000 0.1543 . . . . . . . . . . . 0.2015 
'X-RAY DIFFRACTION' 2.5785 2.7401 . . 132 2459 99.0000  . . . 0.0000 0.1548 . . . . . . . . . . . 0.1929 
'X-RAY DIFFRACTION' 2.7401 2.9516 . . 154 2428 99.0000  . . . 0.0000 0.1536 . . . . . . . . . . . 0.1933 
'X-RAY DIFFRACTION' 2.9516 3.2486 . . 135 2469 99.0000  . . . 0.0000 0.1485 . . . . . . . . . . . 0.1844 
'X-RAY DIFFRACTION' 3.2486 3.7185 . . 128 2474 100.0000 . . . 0.0000 0.1414 . . . . . . . . . . . 0.1603 
'X-RAY DIFFRACTION' 3.7185 4.6843 . . 129 2514 99.0000  . . . 0.0000 0.1331 . . . . . . . . . . . 0.1588 
'X-RAY DIFFRACTION' 4.6843 47.99  . . 149 2635 100.0000 . . . 0.0000 0.1652 . . . . . . . . . . . 0.2008 
# 
_struct.entry_id                     9BR3 
_struct.title                        'Crystal structure of p53 Y220C mutant in complex with PC-10709' 
_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        9BR3 
_struct_keywords.text            'P53, Y220C mutant, ligand, TRANSFERASE' 
_struct_keywords.pdbx_keywords   TRANSFERASE 
# 
loop_
_struct_asym.id 
_struct_asym.pdbx_blank_PDB_chainid_flag 
_struct_asym.pdbx_modified 
_struct_asym.entity_id 
_struct_asym.details 
A N N 1 ? 
B N N 1 ? 
C N N 2 ? 
D N N 3 ? 
E N N 2 ? 
F N N 3 ? 
G N N 4 ? 
H N N 4 ? 
# 
_struct_ref.id                         1 
_struct_ref.db_name                    UNP 
_struct_ref.db_code                    P53_HUMAN 
_struct_ref.pdbx_db_accession          P04637 
_struct_ref.pdbx_db_isoform            ? 
_struct_ref.entity_id                  1 
_struct_ref.pdbx_seq_one_letter_code   
;SSSVPSQKTYQGSYGFRLGFLHSGTAKSVTCTYSPALNKMFCQLAKTCPVQLWVDSTPPPGTRVRAMAIYKQSQHMTEVV
RRCPHHERCSDSDGLAPPQHLIRVEGNLRVEYLDDRNTFRHSVVVPYEPPEVGSDCTTIHYNYMCNSSCMGGMNRRPILT
IITLEDSSGNLLGRNSFEVRVCACPGRDRRTEEENLRKKGEPHHELPPGSTKRALPNNT
;
_struct_ref.pdbx_align_begin           94 
# 
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 9BR3 A 3 ? 221 ? P04637 94 ? 312 ? 94 312 
2 1 9BR3 B 3 ? 221 ? P04637 94 ? 312 ? 94 312 
# 
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 9BR3 GLY A 1   ? UNP P04637 ?   ?   'expression tag' 92  1  
1 9BR3 SER A 2   ? UNP P04637 ?   ?   'expression tag' 93  2  
1 9BR3 LEU A 42  ? UNP P04637 MET 133 variant          133 3  
1 9BR3 ALA A 112 ? UNP P04637 VAL 203 variant          203 4  
1 9BR3 CYS A 129 ? UNP P04637 TYR 220 variant          220 5  
1 9BR3 TYR A 148 ? UNP P04637 ASN 239 variant          239 6  
1 9BR3 ASP A 177 ? UNP P04637 ASN 268 conflict         268 7  
2 9BR3 GLY B 1   ? UNP P04637 ?   ?   'expression tag' 92  8  
2 9BR3 SER B 2   ? UNP P04637 ?   ?   'expression tag' 93  9  
2 9BR3 LEU B 42  ? UNP P04637 MET 133 variant          133 10 
2 9BR3 ALA B 112 ? UNP P04637 VAL 203 variant          203 11 
2 9BR3 CYS B 129 ? UNP P04637 TYR 220 variant          220 12 
2 9BR3 TYR B 148 ? UNP P04637 ASN 239 variant          239 13 
2 9BR3 ASP B 177 ? UNP P04637 ASN 268 conflict         268 14 
# 
loop_
_pdbx_struct_assembly.id 
_pdbx_struct_assembly.details 
_pdbx_struct_assembly.method_details 
_pdbx_struct_assembly.oligomeric_details 
_pdbx_struct_assembly.oligomeric_count 
1 author_and_software_defined_assembly PISA monomeric 1 
2 author_and_software_defined_assembly PISA monomeric 1 
# 
loop_
_pdbx_struct_assembly_gen.assembly_id 
_pdbx_struct_assembly_gen.oper_expression 
_pdbx_struct_assembly_gen.asym_id_list 
1 1 A,C,D,G 
2 1 B,E,F,H 
# 
_pdbx_struct_oper_list.id                   1 
_pdbx_struct_oper_list.type                 'identity operation' 
_pdbx_struct_oper_list.name                 1_555 
_pdbx_struct_oper_list.symmetry_operation   x,y,z 
_pdbx_struct_oper_list.matrix[1][1]         1.0000000000 
_pdbx_struct_oper_list.matrix[1][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[1][3]         0.0000000000 
_pdbx_struct_oper_list.vector[1]            0.0000000000 
_pdbx_struct_oper_list.matrix[2][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[2][2]         1.0000000000 
_pdbx_struct_oper_list.matrix[2][3]         0.0000000000 
_pdbx_struct_oper_list.vector[2]            0.0000000000 
_pdbx_struct_oper_list.matrix[3][1]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][2]         0.0000000000 
_pdbx_struct_oper_list.matrix[3][3]         1.0000000000 
_pdbx_struct_oper_list.vector[3]            0.0000000000 
# 
loop_
_struct_conf.conf_type_id 
_struct_conf.id 
_struct_conf.pdbx_PDB_helix_id 
_struct_conf.beg_label_comp_id 
_struct_conf.beg_label_asym_id 
_struct_conf.beg_label_seq_id 
_struct_conf.pdbx_beg_PDB_ins_code 
_struct_conf.end_label_comp_id 
_struct_conf.end_label_asym_id 
_struct_conf.end_label_seq_id 
_struct_conf.pdbx_end_PDB_ins_code 
_struct_conf.beg_auth_comp_id 
_struct_conf.beg_auth_asym_id 
_struct_conf.beg_auth_seq_id 
_struct_conf.end_auth_comp_id 
_struct_conf.end_auth_asym_id 
_struct_conf.end_auth_seq_id 
_struct_conf.pdbx_PDB_helix_class 
_struct_conf.details 
_struct_conf.pdbx_PDB_helix_length 
HELX_P HELX_P1 AA1 CYS A 85  ? ARG A 90  ? CYS A 176 ARG A 181 1 ? 6  
HELX_P HELX_P2 AA2 CYS A 186 ? ARG A 199 ? CYS A 277 ARG A 290 1 ? 14 
HELX_P HELX_P3 AA3 GLN B 74  ? MET B 78  ? GLN B 165 MET B 169 5 ? 5  
HELX_P HELX_P4 AA4 HIS B 87  ? CYS B 91  ? HIS B 178 CYS B 182 5 ? 5  
HELX_P HELX_P5 AA5 CYS B 186 ? LYS B 200 ? CYS B 277 LYS B 291 1 ? 15 
# 
_struct_conf_type.id          HELX_P 
_struct_conf_type.criteria    ? 
_struct_conf_type.reference   ? 
# 
loop_
_struct_conn.id 
_struct_conn.conn_type_id 
_struct_conn.pdbx_leaving_atom_flag 
_struct_conn.pdbx_PDB_id 
_struct_conn.ptnr1_label_asym_id 
_struct_conn.ptnr1_label_comp_id 
_struct_conn.ptnr1_label_seq_id 
_struct_conn.ptnr1_label_atom_id 
_struct_conn.pdbx_ptnr1_label_alt_id 
_struct_conn.pdbx_ptnr1_PDB_ins_code 
_struct_conn.pdbx_ptnr1_standard_comp_id 
_struct_conn.ptnr1_symmetry 
_struct_conn.ptnr2_label_asym_id 
_struct_conn.ptnr2_label_comp_id 
_struct_conn.ptnr2_label_seq_id 
_struct_conn.ptnr2_label_atom_id 
_struct_conn.pdbx_ptnr2_label_alt_id 
_struct_conn.pdbx_ptnr2_PDB_ins_code 
_struct_conn.ptnr1_auth_asym_id 
_struct_conn.ptnr1_auth_comp_id 
_struct_conn.ptnr1_auth_seq_id 
_struct_conn.ptnr2_auth_asym_id 
_struct_conn.ptnr2_auth_comp_id 
_struct_conn.ptnr2_auth_seq_id 
_struct_conn.ptnr2_symmetry 
_struct_conn.pdbx_ptnr3_label_atom_id 
_struct_conn.pdbx_ptnr3_label_seq_id 
_struct_conn.pdbx_ptnr3_label_comp_id 
_struct_conn.pdbx_ptnr3_label_asym_id 
_struct_conn.pdbx_ptnr3_label_alt_id 
_struct_conn.pdbx_ptnr3_PDB_ins_code 
_struct_conn.details 
_struct_conn.pdbx_dist_value 
_struct_conn.pdbx_value_order 
_struct_conn.pdbx_role 
metalc1 metalc ? ? A CYS 85  SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 176 A ZN 402 1_555 ? ? ? ? ? ? ? 2.340 ? ? 
metalc2 metalc ? ? A HIS 88  ND1 ? ? ? 1_555 D ZN . ZN ? ? A HIS 179 A ZN 402 1_555 ? ? ? ? ? ? ? 2.027 ? ? 
metalc3 metalc ? ? A CYS 147 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 238 A ZN 402 1_555 ? ? ? ? ? ? ? 2.338 ? ? 
metalc4 metalc ? ? A CYS 151 SG  ? ? ? 1_555 D ZN . ZN ? ? A CYS 242 A ZN 402 1_555 ? ? ? ? ? ? ? 2.320 ? ? 
metalc5 metalc ? ? B CYS 85  SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 176 B ZN 402 1_555 ? ? ? ? ? ? ? 2.392 ? ? 
metalc6 metalc ? ? B HIS 88  ND1 ? ? ? 1_555 F ZN . ZN ? ? B HIS 179 B ZN 402 1_555 ? ? ? ? ? ? ? 2.028 ? ? 
metalc7 metalc ? ? B CYS 147 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 238 B ZN 402 1_555 ? ? ? ? ? ? ? 2.364 ? ? 
metalc8 metalc ? ? B CYS 151 SG  ? ? ? 1_555 F ZN . ZN ? ? B CYS 242 B ZN 402 1_555 ? ? ? ? ? ? ? 2.306 ? ? 
# 
_struct_conn_type.id          metalc 
_struct_conn_type.criteria    ? 
_struct_conn_type.reference   ? 
# 
loop_
_pdbx_struct_conn_angle.id 
_pdbx_struct_conn_angle.ptnr1_label_atom_id 
_pdbx_struct_conn_angle.ptnr1_label_alt_id 
_pdbx_struct_conn_angle.ptnr1_label_asym_id 
_pdbx_struct_conn_angle.ptnr1_label_comp_id 
_pdbx_struct_conn_angle.ptnr1_label_seq_id 
_pdbx_struct_conn_angle.ptnr1_auth_atom_id 
_pdbx_struct_conn_angle.ptnr1_auth_asym_id 
_pdbx_struct_conn_angle.ptnr1_auth_comp_id 
_pdbx_struct_conn_angle.ptnr1_auth_seq_id 
_pdbx_struct_conn_angle.ptnr1_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr1_symmetry 
_pdbx_struct_conn_angle.ptnr2_label_atom_id 
_pdbx_struct_conn_angle.ptnr2_label_alt_id 
_pdbx_struct_conn_angle.ptnr2_label_asym_id 
_pdbx_struct_conn_angle.ptnr2_label_comp_id 
_pdbx_struct_conn_angle.ptnr2_label_seq_id 
_pdbx_struct_conn_angle.ptnr2_auth_atom_id 
_pdbx_struct_conn_angle.ptnr2_auth_asym_id 
_pdbx_struct_conn_angle.ptnr2_auth_comp_id 
_pdbx_struct_conn_angle.ptnr2_auth_seq_id 
_pdbx_struct_conn_angle.ptnr2_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr2_symmetry 
_pdbx_struct_conn_angle.ptnr3_label_atom_id 
_pdbx_struct_conn_angle.ptnr3_label_alt_id 
_pdbx_struct_conn_angle.ptnr3_label_asym_id 
_pdbx_struct_conn_angle.ptnr3_label_comp_id 
_pdbx_struct_conn_angle.ptnr3_label_seq_id 
_pdbx_struct_conn_angle.ptnr3_auth_atom_id 
_pdbx_struct_conn_angle.ptnr3_auth_asym_id 
_pdbx_struct_conn_angle.ptnr3_auth_comp_id 
_pdbx_struct_conn_angle.ptnr3_auth_seq_id 
_pdbx_struct_conn_angle.ptnr3_PDB_ins_code 
_pdbx_struct_conn_angle.ptnr3_symmetry 
_pdbx_struct_conn_angle.value 
_pdbx_struct_conn_angle.value_esd 
1  SG  ? A CYS 85  ? A CYS 176 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 ND1 ? A HIS 88  ? A HIS 179 ? 1_555 104.0 ? 
2  SG  ? A CYS 85  ? A CYS 176 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 SG  ? A CYS 147 ? A CYS 238 ? 1_555 111.3 ? 
3  ND1 ? A HIS 88  ? A HIS 179 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 SG  ? A CYS 147 ? A CYS 238 ? 1_555 109.0 ? 
4  SG  ? A CYS 85  ? A CYS 176 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 SG  ? A CYS 151 ? A CYS 242 ? 1_555 112.5 ? 
5  ND1 ? A HIS 88  ? A HIS 179 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 SG  ? A CYS 151 ? A CYS 242 ? 1_555 104.8 ? 
6  SG  ? A CYS 147 ? A CYS 238 ? 1_555 ZN ? D ZN . ? A ZN 402 ? 1_555 SG  ? A CYS 151 ? A CYS 242 ? 1_555 114.4 ? 
7  SG  ? B CYS 85  ? B CYS 176 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 ND1 ? B HIS 88  ? B HIS 179 ? 1_555 107.1 ? 
8  SG  ? B CYS 85  ? B CYS 176 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 SG  ? B CYS 147 ? B CYS 238 ? 1_555 109.1 ? 
9  ND1 ? B HIS 88  ? B HIS 179 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 SG  ? B CYS 147 ? B CYS 238 ? 1_555 108.3 ? 
10 SG  ? B CYS 85  ? B CYS 176 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 SG  ? B CYS 151 ? B CYS 242 ? 1_555 112.3 ? 
11 ND1 ? B HIS 88  ? B HIS 179 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 SG  ? B CYS 151 ? B CYS 242 ? 1_555 105.2 ? 
12 SG  ? B CYS 147 ? B CYS 238 ? 1_555 ZN ? F ZN . ? B ZN 402 ? 1_555 SG  ? B CYS 151 ? B CYS 242 ? 1_555 114.4 ? 
# 
loop_
_struct_sheet.id 
_struct_sheet.type 
_struct_sheet.number_strands 
_struct_sheet.details 
AA1 ? 4 ? 
AA2 ? 7 ? 
AA3 ? 4 ? 
AA4 ? 7 ? 
# 
loop_
_struct_sheet_order.sheet_id 
_struct_sheet_order.range_id_1 
_struct_sheet_order.range_id_2 
_struct_sheet_order.offset 
_struct_sheet_order.sense 
AA1 1 2 ? anti-parallel 
AA1 2 3 ? anti-parallel 
AA1 3 4 ? anti-parallel 
AA2 1 2 ? anti-parallel 
AA2 2 3 ? parallel      
AA2 3 4 ? anti-parallel 
AA2 4 5 ? anti-parallel 
AA2 5 6 ? anti-parallel 
AA2 6 7 ? anti-parallel 
AA3 1 2 ? anti-parallel 
AA3 2 3 ? anti-parallel 
AA3 3 4 ? anti-parallel 
AA4 1 2 ? anti-parallel 
AA4 2 3 ? parallel      
AA4 3 4 ? anti-parallel 
AA4 4 5 ? anti-parallel 
AA4 5 6 ? anti-parallel 
AA4 6 7 ? anti-parallel 
# 
loop_
_struct_sheet_range.sheet_id 
_struct_sheet_range.id 
_struct_sheet_range.beg_label_comp_id 
_struct_sheet_range.beg_label_asym_id 
_struct_sheet_range.beg_label_seq_id 
_struct_sheet_range.pdbx_beg_PDB_ins_code 
_struct_sheet_range.end_label_comp_id 
_struct_sheet_range.end_label_asym_id 
_struct_sheet_range.end_label_seq_id 
_struct_sheet_range.pdbx_end_PDB_ins_code 
_struct_sheet_range.beg_auth_comp_id 
_struct_sheet_range.beg_auth_asym_id 
_struct_sheet_range.beg_auth_seq_id 
_struct_sheet_range.end_auth_comp_id 
_struct_sheet_range.end_auth_asym_id 
_struct_sheet_range.end_auth_seq_id 
AA1 1 ARG A 19  ? GLY A 21  ? ARG A 110 GLY A 112 
AA1 2 CYS A 50  ? TRP A 55  ? CYS A 141 TRP A 146 
AA1 3 THR A 139 ? TYR A 145 ? THR A 230 TYR A 236 
AA1 4 ILE A 104 ? VAL A 106 ? ILE A 195 VAL A 197 
AA2 1 CYS A 33  ? SER A 36  ? CYS A 124 SER A 127 
AA2 2 LYS A 41  ? CYS A 44  ? LYS A 132 CYS A 135 
AA2 3 LEU A 173 ? VAL A 183 ? LEU A 264 VAL A 274 
AA2 4 ILE A 160 ? GLU A 167 ? ILE A 251 GLU A 258 
AA2 5 ARG A 65  ? TYR A 72  ? ARG A 156 TYR A 163 
AA2 6 HIS A 123 ? PRO A 128 ? HIS A 214 PRO A 219 
AA2 7 GLU A 113 ? ASP A 116 ? GLU A 204 ASP A 207 
AA3 1 ARG B 19  ? GLY B 21  ? ARG B 110 GLY B 112 
AA3 2 CYS B 50  ? TRP B 55  ? CYS B 141 TRP B 146 
AA3 3 THR B 139 ? TYR B 145 ? THR B 230 TYR B 236 
AA3 4 ILE B 104 ? VAL B 106 ? ILE B 195 VAL B 197 
AA4 1 CYS B 33  ? SER B 36  ? CYS B 124 SER B 127 
AA4 2 LYS B 41  ? CYS B 44  ? LYS B 132 CYS B 135 
AA4 3 LEU B 173 ? VAL B 183 ? LEU B 264 VAL B 274 
AA4 4 ILE B 160 ? GLU B 167 ? ILE B 251 GLU B 258 
AA4 5 ARG B 65  ? TYR B 72  ? ARG B 156 TYR B 163 
AA4 6 HIS B 123 ? PRO B 128 ? HIS B 214 PRO B 219 
AA4 7 GLU B 113 ? ASP B 116 ? GLU B 204 ASP B 207 
# 
loop_
_pdbx_struct_sheet_hbond.sheet_id 
_pdbx_struct_sheet_hbond.range_id_1 
_pdbx_struct_sheet_hbond.range_id_2 
_pdbx_struct_sheet_hbond.range_1_label_atom_id 
_pdbx_struct_sheet_hbond.range_1_label_comp_id 
_pdbx_struct_sheet_hbond.range_1_label_asym_id 
_pdbx_struct_sheet_hbond.range_1_label_seq_id 
_pdbx_struct_sheet_hbond.range_1_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_1_auth_atom_id 
_pdbx_struct_sheet_hbond.range_1_auth_comp_id 
_pdbx_struct_sheet_hbond.range_1_auth_asym_id 
_pdbx_struct_sheet_hbond.range_1_auth_seq_id 
_pdbx_struct_sheet_hbond.range_2_label_atom_id 
_pdbx_struct_sheet_hbond.range_2_label_comp_id 
_pdbx_struct_sheet_hbond.range_2_label_asym_id 
_pdbx_struct_sheet_hbond.range_2_label_seq_id 
_pdbx_struct_sheet_hbond.range_2_PDB_ins_code 
_pdbx_struct_sheet_hbond.range_2_auth_atom_id 
_pdbx_struct_sheet_hbond.range_2_auth_comp_id 
_pdbx_struct_sheet_hbond.range_2_auth_asym_id 
_pdbx_struct_sheet_hbond.range_2_auth_seq_id 
AA1 1 2 N GLY A 21  ? N GLY A 112 O GLN A 53  ? O GLN A 144 
AA1 2 3 N LEU A 54  ? N LEU A 145 O THR A 139 ? O THR A 230 
AA1 3 4 O ASN A 144 ? O ASN A 235 N ARG A 105 ? N ARG A 196 
AA2 1 2 N THR A 34  ? N THR A 125 O PHE A 43  ? O PHE A 134 
AA2 2 3 N LEU A 42  ? N LEU A 133 O GLU A 180 ? O GLU A 271 
AA2 3 4 O LEU A 174 ? O LEU A 265 N LEU A 166 ? N LEU A 257 
AA2 4 5 O ILE A 163 ? O ILE A 254 N MET A 69  ? N MET A 160 
AA2 5 6 N ALA A 68  ? N ALA A 159 O VAL A 125 ? O VAL A 216 
AA2 6 7 O SER A 124 ? O SER A 215 N LEU A 115 ? N LEU A 206 
AA3 1 2 N GLY B 21  ? N GLY B 112 O GLN B 53  ? O GLN B 144 
AA3 2 3 N LEU B 54  ? N LEU B 145 O THR B 139 ? O THR B 230 
AA3 3 4 O ASN B 144 ? O ASN B 235 N ARG B 105 ? N ARG B 196 
AA4 1 2 N THR B 34  ? N THR B 125 O PHE B 43  ? O PHE B 134 
AA4 2 3 N LEU B 42  ? N LEU B 133 O GLU B 180 ? O GLU B 271 
AA4 3 4 O PHE B 179 ? O PHE B 270 N THR B 162 ? N THR B 253 
AA4 4 5 O ILE B 163 ? O ILE B 254 N MET B 69  ? N MET B 160 
AA4 5 6 N ALA B 68  ? N ALA B 159 O VAL B 125 ? O VAL B 216 
AA4 6 7 O VAL B 126 ? O VAL B 217 N GLU B 113 ? N GLU B 204 
# 
_pdbx_entry_details.entry_id                   9BR3 
_pdbx_entry_details.has_ligand_of_interest     Y 
_pdbx_entry_details.compound_details           ? 
_pdbx_entry_details.source_details             ? 
_pdbx_entry_details.nonpolymer_details         ? 
_pdbx_entry_details.sequence_details           ? 
_pdbx_entry_details.has_protein_modification   N 
# 
loop_
_pdbx_validate_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 SER B 183 ? ? 36.29   59.21  
2 1 SER B 183 ? ? -16.71  59.21  
3 1 LEU B 188 ? ? -132.20 -47.87 
# 
loop_
_pdbx_refine_tls.id 
_pdbx_refine_tls.pdbx_refine_id 
_pdbx_refine_tls.details 
_pdbx_refine_tls.method 
_pdbx_refine_tls.origin_x 
_pdbx_refine_tls.origin_y 
_pdbx_refine_tls.origin_z 
_pdbx_refine_tls.T[1][1] 
_pdbx_refine_tls.T[1][1]_esd 
_pdbx_refine_tls.T[1][2] 
_pdbx_refine_tls.T[1][2]_esd 
_pdbx_refine_tls.T[1][3] 
_pdbx_refine_tls.T[1][3]_esd 
_pdbx_refine_tls.T[2][2] 
_pdbx_refine_tls.T[2][2]_esd 
_pdbx_refine_tls.T[2][3] 
_pdbx_refine_tls.T[2][3]_esd 
_pdbx_refine_tls.T[3][3] 
_pdbx_refine_tls.T[3][3]_esd 
_pdbx_refine_tls.L[1][1] 
_pdbx_refine_tls.L[1][1]_esd 
_pdbx_refine_tls.L[1][2] 
_pdbx_refine_tls.L[1][2]_esd 
_pdbx_refine_tls.L[1][3] 
_pdbx_refine_tls.L[1][3]_esd 
_pdbx_refine_tls.L[2][2] 
_pdbx_refine_tls.L[2][2]_esd 
_pdbx_refine_tls.L[2][3] 
_pdbx_refine_tls.L[2][3]_esd 
_pdbx_refine_tls.L[3][3] 
_pdbx_refine_tls.L[3][3]_esd 
_pdbx_refine_tls.S[1][1] 
_pdbx_refine_tls.S[1][1]_esd 
_pdbx_refine_tls.S[1][2] 
_pdbx_refine_tls.S[1][2]_esd 
_pdbx_refine_tls.S[1][3] 
_pdbx_refine_tls.S[1][3]_esd 
_pdbx_refine_tls.S[2][1] 
_pdbx_refine_tls.S[2][1]_esd 
_pdbx_refine_tls.S[2][2] 
_pdbx_refine_tls.S[2][2]_esd 
_pdbx_refine_tls.S[2][3] 
_pdbx_refine_tls.S[2][3]_esd 
_pdbx_refine_tls.S[3][1] 
_pdbx_refine_tls.S[3][1]_esd 
_pdbx_refine_tls.S[3][2] 
_pdbx_refine_tls.S[3][2]_esd 
_pdbx_refine_tls.S[3][3] 
_pdbx_refine_tls.S[3][3]_esd 
1  'X-RAY DIFFRACTION' ? refined 140.0819 -61.5125 38.5907 0.1049 ? 0.0325  ? -0.0310 ? 0.1285 ? -0.0003 ? 0.1159 ? 3.4376 ? 
0.6653  ? -0.7265 ? 4.8994 ? -1.4509 ? 4.1019 ? 0.1863  ? 0.2444  ? 0.1848  ? -0.0775 ? -0.2185 ? -0.1357 ? -0.2158 ? 0.3571  ? 
0.0707  ? 
2  'X-RAY DIFFRACTION' ? refined 130.4643 -58.6364 28.6801 0.0600 ? -0.0023 ? -0.0144 ? 0.0966 ? -0.0076 ? 0.0797 ? 0.5262 ? 
0.2033  ? -0.0613 ? 1.7277 ? 0.0368  ? 0.5762 ? -0.0345 ? 0.1036  ? -0.0065 ? -0.1238 ? 0.0747  ? 0.0207  ? 0.0591  ? 0.0153  ? 
-0.0295 ? 
3  'X-RAY DIFFRACTION' ? refined 128.9466 -53.0930 29.7676 0.0562 ? -0.0145 ? -0.0061 ? 0.0984 ? 0.0019  ? 0.0880 ? 0.6801 ? 
-0.0574 ? 0.0642  ? 1.9520 ? -0.1486 ? 0.9382 ? -0.0138 ? 0.0913  ? 0.0769  ? -0.1722 ? 0.0165  ? 0.0567  ? 0.0377  ? 0.0405  ? 
-0.0030 ? 
4  'X-RAY DIFFRACTION' ? refined 171.3886 -52.9057 37.4195 0.0907 ? -0.0057 ? -0.0587 ? 0.1219 ? 0.0173  ? 0.1107 ? 1.9995 ? 
1.5932  ? -0.7604 ? 3.0363 ? -0.3744 ? 1.3245 ? -0.1292 ? -0.0673 ? 0.1376  ? -0.0854 ? -0.0732 ? -0.1753 ? -0.0635 ? 0.2196  ? 
0.1746  ? 
5  'X-RAY DIFFRACTION' ? refined 158.5540 -55.0857 27.8460 0.0720 ? -0.0080 ? -0.0109 ? 0.0884 ? -0.0030 ? 0.0937 ? 0.1845 ? 
-0.1733 ? -0.1143 ? 1.4317 ? -0.2435 ? 2.2138 ? 0.0653  ? 0.0188  ? -0.0315 ? -0.1483 ? -0.0268 ? 0.0955  ? 0.1442  ? -0.0703 ? 
-0.0627 ? 
6  'X-RAY DIFFRACTION' ? refined 168.5728 -39.2569 27.7693 0.0808 ? -0.0224 ? -0.0198 ? 0.0918 ? -0.0053 ? 0.1012 ? 0.3531 ? 
-0.2491 ? 0.3765  ? 2.4030 ? -1.1623 ? 1.3043 ? 0.0585  ? 0.0348  ? 0.0712  ? -0.1316 ? -0.0935 ? -0.1889 ? 0.0581  ? 0.0857  ? 
0.0410  ? 
7  'X-RAY DIFFRACTION' ? refined 159.9245 -36.8969 34.4833 0.1151 ? -0.0139 ? 0.0001  ? 0.0754 ? -0.0128 ? 0.1309 ? 1.7843 ? 
0.0235  ? -0.3757 ? 2.9371 ? 0.1352  ? 2.9439 ? 0.0581  ? -0.0631 ? 0.1677  ? 0.2092  ? -0.0144 ? 0.0903  ? -0.3269 ? -0.0631 ? 
-0.0399 ? 
8  'X-RAY DIFFRACTION' ? refined 155.0589 -53.3903 40.7892 0.1281 ? -0.0608 ? -0.0104 ? 0.1944 ? -0.0152 ? 0.0992 ? 3.9028 ? 
3.9381  ? 0.1346  ? 5.8739 ? 0.5566  ? 0.0986 ? 0.0224  ? -0.0861 ? -0.0881 ? 0.0047  ? -0.1469 ? 0.1320  ? 0.1598  ? -0.3393 ? 
0.0646  ? 
9  'X-RAY DIFFRACTION' ? refined 161.9725 -43.0614 24.0316 0.0844 ? 0.0020  ? -0.0323 ? 0.0762 ? -0.0119 ? 0.0680 ? 3.0327 ? 
0.9716  ? -0.6738 ? 4.1657 ? -1.4479 ? 2.0892 ? 0.0459  ? 0.0858  ? 0.1028  ? -0.1871 ? -0.0677 ? 0.0253  ? -0.0654 ? 0.0208  ? 
0.0159  ? 
10 'X-RAY DIFFRACTION' ? refined 166.3700 -49.7359 32.9739 0.0517 ? -0.0303 ? -0.0066 ? 0.0778 ? -0.0040 ? 0.0857 ? 0.9322 ? 
-0.4337 ? 0.1880  ? 1.2941 ? -0.7535 ? 2.7547 ? 0.0301  ? 0.0438  ? 0.0480  ? -0.0042 ? -0.0189 ? -0.0166 ? -0.0184 ? 0.2339  ? 
0.0331  ? 
11 'X-RAY DIFFRACTION' ? refined 165.4654 -57.1195 12.2212 0.3093 ? 0.1004  ? 0.0407  ? 0.3032 ? -0.0083 ? 0.1162 ? 2.4376 ? 
0.5222  ? -1.5997 ? 2.3272 ? 0.2941  ? 2.2010 ? 0.0209  ? 0.5171  ? -0.2954 ? -0.5966 ? -0.2589 ? -0.2658 ? 0.3910  ? 0.5870  ? 
0.1223  ? 
# 
loop_
_pdbx_refine_tls_group.id 
_pdbx_refine_tls_group.pdbx_refine_id 
_pdbx_refine_tls_group.refine_tls_id 
_pdbx_refine_tls_group.beg_label_asym_id 
_pdbx_refine_tls_group.beg_label_seq_id 
_pdbx_refine_tls_group.beg_auth_asym_id 
_pdbx_refine_tls_group.beg_auth_seq_id 
_pdbx_refine_tls_group.beg_PDB_ins_code 
_pdbx_refine_tls_group.end_label_asym_id 
_pdbx_refine_tls_group.end_label_seq_id 
_pdbx_refine_tls_group.end_auth_asym_id 
_pdbx_refine_tls_group.end_auth_seq_id 
_pdbx_refine_tls_group.end_PDB_ins_code 
_pdbx_refine_tls_group.selection 
_pdbx_refine_tls_group.selection_details 
1  'X-RAY DIFFRACTION' 1  ? ? A 95  ? ? ? A 109 ? ? 
;chain 'A' and (resid 95 through 109 )
;
2  'X-RAY DIFFRACTION' 2  ? ? A 110 ? ? ? A 176 ? ? 
;chain 'A' and (resid 110 through 176 )
;
3  'X-RAY DIFFRACTION' 3  ? ? A 177 ? ? ? A 291 ? ? 
;chain 'A' and (resid 177 through 291 )
;
4  'X-RAY DIFFRACTION' 4  ? ? B 92  ? ? ? B 112 ? ? 
;chain 'B' and (resid 92 through 112 )
;
5  'X-RAY DIFFRACTION' 5  ? ? B 113 ? ? ? B 155 ? ? 
;chain 'B' and (resid 113 through 155 )
;
6  'X-RAY DIFFRACTION' 6  ? ? B 156 ? ? ? B 181 ? ? 
;chain 'B' and (resid 156 through 181 )
;
7  'X-RAY DIFFRACTION' 7  ? ? B 182 ? ? ? B 213 ? ? 
;chain 'B' and (resid 182 through 213 )
;
8  'X-RAY DIFFRACTION' 8  ? ? B 214 ? ? ? B 229 ? ? 
;chain 'B' and (resid 214 through 229 )
;
9  'X-RAY DIFFRACTION' 9  ? ? B 230 ? ? ? B 250 ? ? 
;chain 'B' and (resid 230 through 250 )
;
10 'X-RAY DIFFRACTION' 10 ? ? B 251 ? ? ? B 277 ? ? 
;chain 'B' and (resid 251 through 277 )
;
11 'X-RAY DIFFRACTION' 11 ? ? B 278 ? ? ? B 292 ? ? 
;chain 'B' and (resid 278 through 292 )
;
# 
_phasing.method   MR 
# 
loop_
_pdbx_unobs_or_zero_occ_residues.id 
_pdbx_unobs_or_zero_occ_residues.PDB_model_num 
_pdbx_unobs_or_zero_occ_residues.polymer_flag 
_pdbx_unobs_or_zero_occ_residues.occupancy_flag 
_pdbx_unobs_or_zero_occ_residues.auth_asym_id 
_pdbx_unobs_or_zero_occ_residues.auth_comp_id 
_pdbx_unobs_or_zero_occ_residues.auth_seq_id 
_pdbx_unobs_or_zero_occ_residues.PDB_ins_code 
_pdbx_unobs_or_zero_occ_residues.label_asym_id 
_pdbx_unobs_or_zero_occ_residues.label_comp_id 
_pdbx_unobs_or_zero_occ_residues.label_seq_id 
1  1 Y 1 A GLY 92  ? A GLY 1   
2  1 Y 1 A SER 93  ? A SER 2   
3  1 Y 1 A SER 94  ? A SER 3   
4  1 Y 1 A LYS 292 ? A LYS 201 
5  1 Y 1 A GLY 293 ? A GLY 202 
6  1 Y 1 A GLU 294 ? A GLU 203 
7  1 Y 1 A PRO 295 ? A PRO 204 
8  1 Y 1 A HIS 296 ? A HIS 205 
9  1 Y 1 A HIS 297 ? A HIS 206 
10 1 Y 1 A GLU 298 ? A GLU 207 
11 1 Y 1 A LEU 299 ? A LEU 208 
12 1 Y 1 A PRO 300 ? A PRO 209 
13 1 Y 1 A PRO 301 ? A PRO 210 
14 1 Y 1 A GLY 302 ? A GLY 211 
15 1 Y 1 A SER 303 ? A SER 212 
16 1 Y 1 A THR 304 ? A THR 213 
17 1 Y 1 A LYS 305 ? A LYS 214 
18 1 Y 1 A ARG 306 ? A ARG 215 
19 1 Y 1 A ALA 307 ? A ALA 216 
20 1 Y 1 A LEU 308 ? A LEU 217 
21 1 Y 1 A PRO 309 ? A PRO 218 
22 1 Y 1 A ASN 310 ? A ASN 219 
23 1 Y 1 A ASN 311 ? A ASN 220 
24 1 Y 1 A THR 312 ? A THR 221 
25 1 Y 1 B GLY 293 ? B GLY 202 
26 1 Y 1 B GLU 294 ? B GLU 203 
27 1 Y 1 B PRO 295 ? B PRO 204 
28 1 Y 1 B HIS 296 ? B HIS 205 
29 1 Y 1 B HIS 297 ? B HIS 206 
30 1 Y 1 B GLU 298 ? B GLU 207 
31 1 Y 1 B LEU 299 ? B LEU 208 
32 1 Y 1 B PRO 300 ? B PRO 209 
33 1 Y 1 B PRO 301 ? B PRO 210 
34 1 Y 1 B GLY 302 ? B GLY 211 
35 1 Y 1 B SER 303 ? B SER 212 
36 1 Y 1 B THR 304 ? B THR 213 
37 1 Y 1 B LYS 305 ? B LYS 214 
38 1 Y 1 B ARG 306 ? B ARG 215 
39 1 Y 1 B ALA 307 ? B ALA 216 
40 1 Y 1 B LEU 308 ? B LEU 217 
41 1 Y 1 B PRO 309 ? B PRO 218 
42 1 Y 1 B ASN 310 ? B ASN 219 
43 1 Y 1 B ASN 311 ? B ASN 220 
44 1 Y 1 B THR 312 ? B THR 221 
# 
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 
A1ARO C10  C  N N 1   
A1ARO C11  C  N N 2   
A1ARO C15  C  Y N 3   
A1ARO C16  C  Y N 4   
A1ARO C18  C  N N 5   
A1ARO C19  C  N N 6   
A1ARO C20  C  N N 7   
A1ARO C22  C  N N 8   
A1ARO C23  C  N N 9   
A1ARO C01  C  N N 10  
A1ARO C03  C  Y N 11  
A1ARO C04  C  Y N 12  
A1ARO C05  C  Y N 13  
A1ARO C06  C  Y N 14  
A1ARO C07  C  Y N 15  
A1ARO C08  C  Y N 16  
A1ARO C12  C  N N 17  
A1ARO C13  C  Y N 18  
A1ARO C14  C  Y N 19  
A1ARO C24  C  N N 20  
A1ARO C25  C  Y N 21  
A1ARO C26  C  Y N 22  
A1ARO C27  C  Y N 23  
A1ARO C28  C  Y N 24  
A1ARO C30  C  N N 25  
A1ARO C31  C  N N 26  
A1ARO C36  C  N N 27  
A1ARO F32  F  N N 28  
A1ARO F33  F  N N 29  
A1ARO F34  F  N N 30  
A1ARO N09  N  N N 31  
A1ARO N17  N  N N 32  
A1ARO N21  N  N N 33  
A1ARO N29  N  Y N 34  
A1ARO O02  O  N N 35  
A1ARO O37  O  N N 36  
A1ARO O38  O  N N 37  
A1ARO S35  S  N N 38  
A1ARO H1   H  N N 39  
A1ARO H2   H  N N 40  
A1ARO H3   H  N N 41  
A1ARO H4   H  N N 42  
A1ARO H5   H  N N 43  
A1ARO H6   H  N N 44  
A1ARO H7   H  N N 45  
A1ARO H8   H  N N 46  
A1ARO H9   H  N N 47  
A1ARO H10  H  N N 48  
A1ARO H11  H  N N 49  
A1ARO H12  H  N N 50  
A1ARO H13  H  N N 51  
A1ARO H14  H  N N 52  
A1ARO H15  H  N N 53  
A1ARO H16  H  N N 54  
A1ARO H17  H  N N 55  
A1ARO H18  H  N N 56  
A1ARO H19  H  N N 57  
A1ARO H20  H  N N 58  
A1ARO H21  H  N N 59  
A1ARO H22  H  N N 60  
A1ARO H23  H  N N 61  
A1ARO H24  H  N N 62  
A1ARO H25  H  N N 63  
A1ARO H26  H  N N 64  
A1ARO H27  H  N N 65  
A1ARO H28  H  N N 66  
A1ARO H29  H  N N 67  
A1ARO H30  H  N N 68  
A1ARO H31  H  N N 69  
ALA   N    N  N N 70  
ALA   CA   C  N S 71  
ALA   C    C  N N 72  
ALA   O    O  N N 73  
ALA   CB   C  N N 74  
ALA   OXT  O  N N 75  
ALA   H    H  N N 76  
ALA   H2   H  N N 77  
ALA   HA   H  N N 78  
ALA   HB1  H  N N 79  
ALA   HB2  H  N N 80  
ALA   HB3  H  N N 81  
ALA   HXT  H  N N 82  
ARG   N    N  N N 83  
ARG   CA   C  N S 84  
ARG   C    C  N N 85  
ARG   O    O  N N 86  
ARG   CB   C  N N 87  
ARG   CG   C  N N 88  
ARG   CD   C  N N 89  
ARG   NE   N  N N 90  
ARG   CZ   C  N N 91  
ARG   NH1  N  N N 92  
ARG   NH2  N  N N 93  
ARG   OXT  O  N N 94  
ARG   H    H  N N 95  
ARG   H2   H  N N 96  
ARG   HA   H  N N 97  
ARG   HB2  H  N N 98  
ARG   HB3  H  N N 99  
ARG   HG2  H  N N 100 
ARG   HG3  H  N N 101 
ARG   HD2  H  N N 102 
ARG   HD3  H  N N 103 
ARG   HE   H  N N 104 
ARG   HH11 H  N N 105 
ARG   HH12 H  N N 106 
ARG   HH21 H  N N 107 
ARG   HH22 H  N N 108 
ARG   HXT  H  N N 109 
ASN   N    N  N N 110 
ASN   CA   C  N S 111 
ASN   C    C  N N 112 
ASN   O    O  N N 113 
ASN   CB   C  N N 114 
ASN   CG   C  N N 115 
ASN   OD1  O  N N 116 
ASN   ND2  N  N N 117 
ASN   OXT  O  N N 118 
ASN   H    H  N N 119 
ASN   H2   H  N N 120 
ASN   HA   H  N N 121 
ASN   HB2  H  N N 122 
ASN   HB3  H  N N 123 
ASN   HD21 H  N N 124 
ASN   HD22 H  N N 125 
ASN   HXT  H  N N 126 
ASP   N    N  N N 127 
ASP   CA   C  N S 128 
ASP   C    C  N N 129 
ASP   O    O  N N 130 
ASP   CB   C  N N 131 
ASP   CG   C  N N 132 
ASP   OD1  O  N N 133 
ASP   OD2  O  N N 134 
ASP   OXT  O  N N 135 
ASP   H    H  N N 136 
ASP   H2   H  N N 137 
ASP   HA   H  N N 138 
ASP   HB2  H  N N 139 
ASP   HB3  H  N N 140 
ASP   HD2  H  N N 141 
ASP   HXT  H  N N 142 
CYS   N    N  N N 143 
CYS   CA   C  N R 144 
CYS   C    C  N N 145 
CYS   O    O  N N 146 
CYS   CB   C  N N 147 
CYS   SG   S  N N 148 
CYS   OXT  O  N N 149 
CYS   H    H  N N 150 
CYS   H2   H  N N 151 
CYS   HA   H  N N 152 
CYS   HB2  H  N N 153 
CYS   HB3  H  N N 154 
CYS   HG   H  N N 155 
CYS   HXT  H  N N 156 
GLN   N    N  N N 157 
GLN   CA   C  N S 158 
GLN   C    C  N N 159 
GLN   O    O  N N 160 
GLN   CB   C  N N 161 
GLN   CG   C  N N 162 
GLN   CD   C  N N 163 
GLN   OE1  O  N N 164 
GLN   NE2  N  N N 165 
GLN   OXT  O  N N 166 
GLN   H    H  N N 167 
GLN   H2   H  N N 168 
GLN   HA   H  N N 169 
GLN   HB2  H  N N 170 
GLN   HB3  H  N N 171 
GLN   HG2  H  N N 172 
GLN   HG3  H  N N 173 
GLN   HE21 H  N N 174 
GLN   HE22 H  N N 175 
GLN   HXT  H  N N 176 
GLU   N    N  N N 177 
GLU   CA   C  N S 178 
GLU   C    C  N N 179 
GLU   O    O  N N 180 
GLU   CB   C  N N 181 
GLU   CG   C  N N 182 
GLU   CD   C  N N 183 
GLU   OE1  O  N N 184 
GLU   OE2  O  N N 185 
GLU   OXT  O  N N 186 
GLU   H    H  N N 187 
GLU   H2   H  N N 188 
GLU   HA   H  N N 189 
GLU   HB2  H  N N 190 
GLU   HB3  H  N N 191 
GLU   HG2  H  N N 192 
GLU   HG3  H  N N 193 
GLU   HE2  H  N N 194 
GLU   HXT  H  N N 195 
GLY   N    N  N N 196 
GLY   CA   C  N N 197 
GLY   C    C  N N 198 
GLY   O    O  N N 199 
GLY   OXT  O  N N 200 
GLY   H    H  N N 201 
GLY   H2   H  N N 202 
GLY   HA2  H  N N 203 
GLY   HA3  H  N N 204 
GLY   HXT  H  N N 205 
HIS   N    N  N N 206 
HIS   CA   C  N S 207 
HIS   C    C  N N 208 
HIS   O    O  N N 209 
HIS   CB   C  N N 210 
HIS   CG   C  Y N 211 
HIS   ND1  N  Y N 212 
HIS   CD2  C  Y N 213 
HIS   CE1  C  Y N 214 
HIS   NE2  N  Y N 215 
HIS   OXT  O  N N 216 
HIS   H    H  N N 217 
HIS   H2   H  N N 218 
HIS   HA   H  N N 219 
HIS   HB2  H  N N 220 
HIS   HB3  H  N N 221 
HIS   HD1  H  N N 222 
HIS   HD2  H  N N 223 
HIS   HE1  H  N N 224 
HIS   HE2  H  N N 225 
HIS   HXT  H  N N 226 
HOH   O    O  N N 227 
HOH   H1   H  N N 228 
HOH   H2   H  N N 229 
ILE   N    N  N N 230 
ILE   CA   C  N S 231 
ILE   C    C  N N 232 
ILE   O    O  N N 233 
ILE   CB   C  N S 234 
ILE   CG1  C  N N 235 
ILE   CG2  C  N N 236 
ILE   CD1  C  N N 237 
ILE   OXT  O  N N 238 
ILE   H    H  N N 239 
ILE   H2   H  N N 240 
ILE   HA   H  N N 241 
ILE   HB   H  N N 242 
ILE   HG12 H  N N 243 
ILE   HG13 H  N N 244 
ILE   HG21 H  N N 245 
ILE   HG22 H  N N 246 
ILE   HG23 H  N N 247 
ILE   HD11 H  N N 248 
ILE   HD12 H  N N 249 
ILE   HD13 H  N N 250 
ILE   HXT  H  N N 251 
LEU   N    N  N N 252 
LEU   CA   C  N S 253 
LEU   C    C  N N 254 
LEU   O    O  N N 255 
LEU   CB   C  N N 256 
LEU   CG   C  N N 257 
LEU   CD1  C  N N 258 
LEU   CD2  C  N N 259 
LEU   OXT  O  N N 260 
LEU   H    H  N N 261 
LEU   H2   H  N N 262 
LEU   HA   H  N N 263 
LEU   HB2  H  N N 264 
LEU   HB3  H  N N 265 
LEU   HG   H  N N 266 
LEU   HD11 H  N N 267 
LEU   HD12 H  N N 268 
LEU   HD13 H  N N 269 
LEU   HD21 H  N N 270 
LEU   HD22 H  N N 271 
LEU   HD23 H  N N 272 
LEU   HXT  H  N N 273 
LYS   N    N  N N 274 
LYS   CA   C  N S 275 
LYS   C    C  N N 276 
LYS   O    O  N N 277 
LYS   CB   C  N N 278 
LYS   CG   C  N N 279 
LYS   CD   C  N N 280 
LYS   CE   C  N N 281 
LYS   NZ   N  N N 282 
LYS   OXT  O  N N 283 
LYS   H    H  N N 284 
LYS   H2   H  N N 285 
LYS   HA   H  N N 286 
LYS   HB2  H  N N 287 
LYS   HB3  H  N N 288 
LYS   HG2  H  N N 289 
LYS   HG3  H  N N 290 
LYS   HD2  H  N N 291 
LYS   HD3  H  N N 292 
LYS   HE2  H  N N 293 
LYS   HE3  H  N N 294 
LYS   HZ1  H  N N 295 
LYS   HZ2  H  N N 296 
LYS   HZ3  H  N N 297 
LYS   HXT  H  N N 298 
MET   N    N  N N 299 
MET   CA   C  N S 300 
MET   C    C  N N 301 
MET   O    O  N N 302 
MET   CB   C  N N 303 
MET   CG   C  N N 304 
MET   SD   S  N N 305 
MET   CE   C  N N 306 
MET   OXT  O  N N 307 
MET   H    H  N N 308 
MET   H2   H  N N 309 
MET   HA   H  N N 310 
MET   HB2  H  N N 311 
MET   HB3  H  N N 312 
MET   HG2  H  N N 313 
MET   HG3  H  N N 314 
MET   HE1  H  N N 315 
MET   HE2  H  N N 316 
MET   HE3  H  N N 317 
MET   HXT  H  N N 318 
PHE   N    N  N N 319 
PHE   CA   C  N S 320 
PHE   C    C  N N 321 
PHE   O    O  N N 322 
PHE   CB   C  N N 323 
PHE   CG   C  Y N 324 
PHE   CD1  C  Y N 325 
PHE   CD2  C  Y N 326 
PHE   CE1  C  Y N 327 
PHE   CE2  C  Y N 328 
PHE   CZ   C  Y N 329 
PHE   OXT  O  N N 330 
PHE   H    H  N N 331 
PHE   H2   H  N N 332 
PHE   HA   H  N N 333 
PHE   HB2  H  N N 334 
PHE   HB3  H  N N 335 
PHE   HD1  H  N N 336 
PHE   HD2  H  N N 337 
PHE   HE1  H  N N 338 
PHE   HE2  H  N N 339 
PHE   HZ   H  N N 340 
PHE   HXT  H  N N 341 
PRO   N    N  N N 342 
PRO   CA   C  N S 343 
PRO   C    C  N N 344 
PRO   O    O  N N 345 
PRO   CB   C  N N 346 
PRO   CG   C  N N 347 
PRO   CD   C  N N 348 
PRO   OXT  O  N N 349 
PRO   H    H  N N 350 
PRO   HA   H  N N 351 
PRO   HB2  H  N N 352 
PRO   HB3  H  N N 353 
PRO   HG2  H  N N 354 
PRO   HG3  H  N N 355 
PRO   HD2  H  N N 356 
PRO   HD3  H  N N 357 
PRO   HXT  H  N N 358 
SER   N    N  N N 359 
SER   CA   C  N S 360 
SER   C    C  N N 361 
SER   O    O  N N 362 
SER   CB   C  N N 363 
SER   OG   O  N N 364 
SER   OXT  O  N N 365 
SER   H    H  N N 366 
SER   H2   H  N N 367 
SER   HA   H  N N 368 
SER   HB2  H  N N 369 
SER   HB3  H  N N 370 
SER   HG   H  N N 371 
SER   HXT  H  N N 372 
THR   N    N  N N 373 
THR   CA   C  N S 374 
THR   C    C  N N 375 
THR   O    O  N N 376 
THR   CB   C  N R 377 
THR   OG1  O  N N 378 
THR   CG2  C  N N 379 
THR   OXT  O  N N 380 
THR   H    H  N N 381 
THR   H2   H  N N 382 
THR   HA   H  N N 383 
THR   HB   H  N N 384 
THR   HG1  H  N N 385 
THR   HG21 H  N N 386 
THR   HG22 H  N N 387 
THR   HG23 H  N N 388 
THR   HXT  H  N N 389 
TRP   N    N  N N 390 
TRP   CA   C  N S 391 
TRP   C    C  N N 392 
TRP   O    O  N N 393 
TRP   CB   C  N N 394 
TRP   CG   C  Y N 395 
TRP   CD1  C  Y N 396 
TRP   CD2  C  Y N 397 
TRP   NE1  N  Y N 398 
TRP   CE2  C  Y N 399 
TRP   CE3  C  Y N 400 
TRP   CZ2  C  Y N 401 
TRP   CZ3  C  Y N 402 
TRP   CH2  C  Y N 403 
TRP   OXT  O  N N 404 
TRP   H    H  N N 405 
TRP   H2   H  N N 406 
TRP   HA   H  N N 407 
TRP   HB2  H  N N 408 
TRP   HB3  H  N N 409 
TRP   HD1  H  N N 410 
TRP   HE1  H  N N 411 
TRP   HE3  H  N N 412 
TRP   HZ2  H  N N 413 
TRP   HZ3  H  N N 414 
TRP   HH2  H  N N 415 
TRP   HXT  H  N N 416 
TYR   N    N  N N 417 
TYR   CA   C  N S 418 
TYR   C    C  N N 419 
TYR   O    O  N N 420 
TYR   CB   C  N N 421 
TYR   CG   C  Y N 422 
TYR   CD1  C  Y N 423 
TYR   CD2  C  Y N 424 
TYR   CE1  C  Y N 425 
TYR   CE2  C  Y N 426 
TYR   CZ   C  Y N 427 
TYR   OH   O  N N 428 
TYR   OXT  O  N N 429 
TYR   H    H  N N 430 
TYR   H2   H  N N 431 
TYR   HA   H  N N 432 
TYR   HB2  H  N N 433 
TYR   HB3  H  N N 434 
TYR   HD1  H  N N 435 
TYR   HD2  H  N N 436 
TYR   HE1  H  N N 437 
TYR   HE2  H  N N 438 
TYR   HH   H  N N 439 
TYR   HXT  H  N N 440 
VAL   N    N  N N 441 
VAL   CA   C  N S 442 
VAL   C    C  N N 443 
VAL   O    O  N N 444 
VAL   CB   C  N N 445 
VAL   CG1  C  N N 446 
VAL   CG2  C  N N 447 
VAL   OXT  O  N N 448 
VAL   H    H  N N 449 
VAL   H2   H  N N 450 
VAL   HA   H  N N 451 
VAL   HB   H  N N 452 
VAL   HG11 H  N N 453 
VAL   HG12 H  N N 454 
VAL   HG13 H  N N 455 
VAL   HG21 H  N N 456 
VAL   HG22 H  N N 457 
VAL   HG23 H  N N 458 
VAL   HXT  H  N N 459 
ZN    ZN   ZN N N 460 
# 
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 
A1ARO C26 C27  doub Y N 1   
A1ARO C26 C25  sing Y N 2   
A1ARO C27 C28  sing Y N 3   
A1ARO F33 C31  sing N N 4   
A1ARO F34 C31  sing N N 5   
A1ARO C25 C16  doub Y N 6   
A1ARO C31 C30  sing N N 7   
A1ARO C31 F32  sing N N 8   
A1ARO C30 N29  sing N N 9   
A1ARO C28 N29  sing Y N 10  
A1ARO C28 C15  doub Y N 11  
A1ARO N29 C13  sing Y N 12  
A1ARO C16 C15  sing Y N 13  
A1ARO C16 N17  sing N N 14  
A1ARO C15 C14  sing Y N 15  
A1ARO C23 C24  sing N N 16  
A1ARO C23 N21  sing N N 17  
A1ARO C24 C18  sing N N 18  
A1ARO C18 N17  sing N N 19  
A1ARO C18 C19  sing N N 20  
A1ARO C13 C14  doub Y N 21  
A1ARO C13 C12  sing N N 22  
A1ARO C22 N21  sing N N 23  
A1ARO N21 C20  sing N N 24  
A1ARO C20 C19  sing N N 25  
A1ARO C12 C11  trip N N 26  
A1ARO C11 C10  sing N N 27  
A1ARO C10 N09  sing N N 28  
A1ARO N09 C08  sing N N 29  
A1ARO O02 C03  sing N N 30  
A1ARO O02 C01  sing N N 31  
A1ARO C08 C03  doub Y N 32  
A1ARO C08 C07  sing Y N 33  
A1ARO C03 C04  sing Y N 34  
A1ARO C07 C06  doub Y N 35  
A1ARO C04 C05  doub Y N 36  
A1ARO C06 C05  sing Y N 37  
A1ARO C05 S35  sing N N 38  
A1ARO C36 S35  sing N N 39  
A1ARO S35 O38  doub N N 40  
A1ARO S35 O37  doub N N 41  
A1ARO C10 H1   sing N N 42  
A1ARO C10 H2   sing N N 43  
A1ARO C18 H3   sing N N 44  
A1ARO C19 H4   sing N N 45  
A1ARO C19 H5   sing N N 46  
A1ARO C20 H6   sing N N 47  
A1ARO C20 H7   sing N N 48  
A1ARO C22 H8   sing N N 49  
A1ARO C22 H9   sing N N 50  
A1ARO C22 H10  sing N N 51  
A1ARO C23 H11  sing N N 52  
A1ARO C23 H12  sing N N 53  
A1ARO C01 H13  sing N N 54  
A1ARO C01 H14  sing N N 55  
A1ARO C01 H15  sing N N 56  
A1ARO C04 H16  sing N N 57  
A1ARO C06 H17  sing N N 58  
A1ARO C07 H18  sing N N 59  
A1ARO C14 H19  sing N N 60  
A1ARO C24 H20  sing N N 61  
A1ARO C24 H21  sing N N 62  
A1ARO C25 H22  sing N N 63  
A1ARO C26 H23  sing N N 64  
A1ARO C27 H24  sing N N 65  
A1ARO C30 H25  sing N N 66  
A1ARO C30 H26  sing N N 67  
A1ARO C36 H27  sing N N 68  
A1ARO C36 H28  sing N N 69  
A1ARO C36 H29  sing N N 70  
A1ARO N09 H30  sing N N 71  
A1ARO N17 H31  sing N N 72  
ALA   N   CA   sing N N 73  
ALA   N   H    sing N N 74  
ALA   N   H2   sing N N 75  
ALA   CA  C    sing N N 76  
ALA   CA  CB   sing N N 77  
ALA   CA  HA   sing N N 78  
ALA   C   O    doub N N 79  
ALA   C   OXT  sing N N 80  
ALA   CB  HB1  sing N N 81  
ALA   CB  HB2  sing N N 82  
ALA   CB  HB3  sing N N 83  
ALA   OXT HXT  sing N N 84  
ARG   N   CA   sing N N 85  
ARG   N   H    sing N N 86  
ARG   N   H2   sing N N 87  
ARG   CA  C    sing N N 88  
ARG   CA  CB   sing N N 89  
ARG   CA  HA   sing N N 90  
ARG   C   O    doub N N 91  
ARG   C   OXT  sing N N 92  
ARG   CB  CG   sing N N 93  
ARG   CB  HB2  sing N N 94  
ARG   CB  HB3  sing N N 95  
ARG   CG  CD   sing N N 96  
ARG   CG  HG2  sing N N 97  
ARG   CG  HG3  sing N N 98  
ARG   CD  NE   sing N N 99  
ARG   CD  HD2  sing N N 100 
ARG   CD  HD3  sing N N 101 
ARG   NE  CZ   sing N N 102 
ARG   NE  HE   sing N N 103 
ARG   CZ  NH1  sing N N 104 
ARG   CZ  NH2  doub N N 105 
ARG   NH1 HH11 sing N N 106 
ARG   NH1 HH12 sing N N 107 
ARG   NH2 HH21 sing N N 108 
ARG   NH2 HH22 sing N N 109 
ARG   OXT HXT  sing N N 110 
ASN   N   CA   sing N N 111 
ASN   N   H    sing N N 112 
ASN   N   H2   sing N N 113 
ASN   CA  C    sing N N 114 
ASN   CA  CB   sing N N 115 
ASN   CA  HA   sing N N 116 
ASN   C   O    doub N N 117 
ASN   C   OXT  sing N N 118 
ASN   CB  CG   sing N N 119 
ASN   CB  HB2  sing N N 120 
ASN   CB  HB3  sing N N 121 
ASN   CG  OD1  doub N N 122 
ASN   CG  ND2  sing N N 123 
ASN   ND2 HD21 sing N N 124 
ASN   ND2 HD22 sing N N 125 
ASN   OXT HXT  sing N N 126 
ASP   N   CA   sing N N 127 
ASP   N   H    sing N N 128 
ASP   N   H2   sing N N 129 
ASP   CA  C    sing N N 130 
ASP   CA  CB   sing N N 131 
ASP   CA  HA   sing N N 132 
ASP   C   O    doub N N 133 
ASP   C   OXT  sing N N 134 
ASP   CB  CG   sing N N 135 
ASP   CB  HB2  sing N N 136 
ASP   CB  HB3  sing N N 137 
ASP   CG  OD1  doub N N 138 
ASP   CG  OD2  sing N N 139 
ASP   OD2 HD2  sing N N 140 
ASP   OXT HXT  sing N N 141 
CYS   N   CA   sing N N 142 
CYS   N   H    sing N N 143 
CYS   N   H2   sing N N 144 
CYS   CA  C    sing N N 145 
CYS   CA  CB   sing N N 146 
CYS   CA  HA   sing N N 147 
CYS   C   O    doub N N 148 
CYS   C   OXT  sing N N 149 
CYS   CB  SG   sing N N 150 
CYS   CB  HB2  sing N N 151 
CYS   CB  HB3  sing N N 152 
CYS   SG  HG   sing N N 153 
CYS   OXT HXT  sing N N 154 
GLN   N   CA   sing N N 155 
GLN   N   H    sing N N 156 
GLN   N   H2   sing N N 157 
GLN   CA  C    sing N N 158 
GLN   CA  CB   sing N N 159 
GLN   CA  HA   sing N N 160 
GLN   C   O    doub N N 161 
GLN   C   OXT  sing N N 162 
GLN   CB  CG   sing N N 163 
GLN   CB  HB2  sing N N 164 
GLN   CB  HB3  sing N N 165 
GLN   CG  CD   sing N N 166 
GLN   CG  HG2  sing N N 167 
GLN   CG  HG3  sing N N 168 
GLN   CD  OE1  doub N N 169 
GLN   CD  NE2  sing N N 170 
GLN   NE2 HE21 sing N N 171 
GLN   NE2 HE22 sing N N 172 
GLN   OXT HXT  sing N N 173 
GLU   N   CA   sing N N 174 
GLU   N   H    sing N N 175 
GLU   N   H2   sing N N 176 
GLU   CA  C    sing N N 177 
GLU   CA  CB   sing N N 178 
GLU   CA  HA   sing N N 179 
GLU   C   O    doub N N 180 
GLU   C   OXT  sing N N 181 
GLU   CB  CG   sing N N 182 
GLU   CB  HB2  sing N N 183 
GLU   CB  HB3  sing N N 184 
GLU   CG  CD   sing N N 185 
GLU   CG  HG2  sing N N 186 
GLU   CG  HG3  sing N N 187 
GLU   CD  OE1  doub N N 188 
GLU   CD  OE2  sing N N 189 
GLU   OE2 HE2  sing N N 190 
GLU   OXT HXT  sing N N 191 
GLY   N   CA   sing N N 192 
GLY   N   H    sing N N 193 
GLY   N   H2   sing N N 194 
GLY   CA  C    sing N N 195 
GLY   CA  HA2  sing N N 196 
GLY   CA  HA3  sing N N 197 
GLY   C   O    doub N N 198 
GLY   C   OXT  sing N N 199 
GLY   OXT HXT  sing N N 200 
HIS   N   CA   sing N N 201 
HIS   N   H    sing N N 202 
HIS   N   H2   sing N N 203 
HIS   CA  C    sing N N 204 
HIS   CA  CB   sing N N 205 
HIS   CA  HA   sing N N 206 
HIS   C   O    doub N N 207 
HIS   C   OXT  sing N N 208 
HIS   CB  CG   sing N N 209 
HIS   CB  HB2  sing N N 210 
HIS   CB  HB3  sing N N 211 
HIS   CG  ND1  sing Y N 212 
HIS   CG  CD2  doub Y N 213 
HIS   ND1 CE1  doub Y N 214 
HIS   ND1 HD1  sing N N 215 
HIS   CD2 NE2  sing Y N 216 
HIS   CD2 HD2  sing N N 217 
HIS   CE1 NE2  sing Y N 218 
HIS   CE1 HE1  sing N N 219 
HIS   NE2 HE2  sing N N 220 
HIS   OXT HXT  sing N N 221 
HOH   O   H1   sing N N 222 
HOH   O   H2   sing N N 223 
ILE   N   CA   sing N N 224 
ILE   N   H    sing N N 225 
ILE   N   H2   sing N N 226 
ILE   CA  C    sing N N 227 
ILE   CA  CB   sing N N 228 
ILE   CA  HA   sing N N 229 
ILE   C   O    doub N N 230 
ILE   C   OXT  sing N N 231 
ILE   CB  CG1  sing N N 232 
ILE   CB  CG2  sing N N 233 
ILE   CB  HB   sing N N 234 
ILE   CG1 CD1  sing N N 235 
ILE   CG1 HG12 sing N N 236 
ILE   CG1 HG13 sing N N 237 
ILE   CG2 HG21 sing N N 238 
ILE   CG2 HG22 sing N N 239 
ILE   CG2 HG23 sing N N 240 
ILE   CD1 HD11 sing N N 241 
ILE   CD1 HD12 sing N N 242 
ILE   CD1 HD13 sing N N 243 
ILE   OXT HXT  sing N N 244 
LEU   N   CA   sing N N 245 
LEU   N   H    sing N N 246 
LEU   N   H2   sing N N 247 
LEU   CA  C    sing N N 248 
LEU   CA  CB   sing N N 249 
LEU   CA  HA   sing N N 250 
LEU   C   O    doub N N 251 
LEU   C   OXT  sing N N 252 
LEU   CB  CG   sing N N 253 
LEU   CB  HB2  sing N N 254 
LEU   CB  HB3  sing N N 255 
LEU   CG  CD1  sing N N 256 
LEU   CG  CD2  sing N N 257 
LEU   CG  HG   sing N N 258 
LEU   CD1 HD11 sing N N 259 
LEU   CD1 HD12 sing N N 260 
LEU   CD1 HD13 sing N N 261 
LEU   CD2 HD21 sing N N 262 
LEU   CD2 HD22 sing N N 263 
LEU   CD2 HD23 sing N N 264 
LEU   OXT HXT  sing N N 265 
LYS   N   CA   sing N N 266 
LYS   N   H    sing N N 267 
LYS   N   H2   sing N N 268 
LYS   CA  C    sing N N 269 
LYS   CA  CB   sing N N 270 
LYS   CA  HA   sing N N 271 
LYS   C   O    doub N N 272 
LYS   C   OXT  sing N N 273 
LYS   CB  CG   sing N N 274 
LYS   CB  HB2  sing N N 275 
LYS   CB  HB3  sing N N 276 
LYS   CG  CD   sing N N 277 
LYS   CG  HG2  sing N N 278 
LYS   CG  HG3  sing N N 279 
LYS   CD  CE   sing N N 280 
LYS   CD  HD2  sing N N 281 
LYS   CD  HD3  sing N N 282 
LYS   CE  NZ   sing N N 283 
LYS   CE  HE2  sing N N 284 
LYS   CE  HE3  sing N N 285 
LYS   NZ  HZ1  sing N N 286 
LYS   NZ  HZ2  sing N N 287 
LYS   NZ  HZ3  sing N N 288 
LYS   OXT HXT  sing N N 289 
MET   N   CA   sing N N 290 
MET   N   H    sing N N 291 
MET   N   H2   sing N N 292 
MET   CA  C    sing N N 293 
MET   CA  CB   sing N N 294 
MET   CA  HA   sing N N 295 
MET   C   O    doub N N 296 
MET   C   OXT  sing N N 297 
MET   CB  CG   sing N N 298 
MET   CB  HB2  sing N N 299 
MET   CB  HB3  sing N N 300 
MET   CG  SD   sing N N 301 
MET   CG  HG2  sing N N 302 
MET   CG  HG3  sing N N 303 
MET   SD  CE   sing N N 304 
MET   CE  HE1  sing N N 305 
MET   CE  HE2  sing N N 306 
MET   CE  HE3  sing N N 307 
MET   OXT HXT  sing N N 308 
PHE   N   CA   sing N N 309 
PHE   N   H    sing N N 310 
PHE   N   H2   sing N N 311 
PHE   CA  C    sing N N 312 
PHE   CA  CB   sing N N 313 
PHE   CA  HA   sing N N 314 
PHE   C   O    doub N N 315 
PHE   C   OXT  sing N N 316 
PHE   CB  CG   sing N N 317 
PHE   CB  HB2  sing N N 318 
PHE   CB  HB3  sing N N 319 
PHE   CG  CD1  doub Y N 320 
PHE   CG  CD2  sing Y N 321 
PHE   CD1 CE1  sing Y N 322 
PHE   CD1 HD1  sing N N 323 
PHE   CD2 CE2  doub Y N 324 
PHE   CD2 HD2  sing N N 325 
PHE   CE1 CZ   doub Y N 326 
PHE   CE1 HE1  sing N N 327 
PHE   CE2 CZ   sing Y N 328 
PHE   CE2 HE2  sing N N 329 
PHE   CZ  HZ   sing N N 330 
PHE   OXT HXT  sing N N 331 
PRO   N   CA   sing N N 332 
PRO   N   CD   sing N N 333 
PRO   N   H    sing N N 334 
PRO   CA  C    sing N N 335 
PRO   CA  CB   sing N N 336 
PRO   CA  HA   sing N N 337 
PRO   C   O    doub N N 338 
PRO   C   OXT  sing N N 339 
PRO   CB  CG   sing N N 340 
PRO   CB  HB2  sing N N 341 
PRO   CB  HB3  sing N N 342 
PRO   CG  CD   sing N N 343 
PRO   CG  HG2  sing N N 344 
PRO   CG  HG3  sing N N 345 
PRO   CD  HD2  sing N N 346 
PRO   CD  HD3  sing N N 347 
PRO   OXT HXT  sing N N 348 
SER   N   CA   sing N N 349 
SER   N   H    sing N N 350 
SER   N   H2   sing N N 351 
SER   CA  C    sing N N 352 
SER   CA  CB   sing N N 353 
SER   CA  HA   sing N N 354 
SER   C   O    doub N N 355 
SER   C   OXT  sing N N 356 
SER   CB  OG   sing N N 357 
SER   CB  HB2  sing N N 358 
SER   CB  HB3  sing N N 359 
SER   OG  HG   sing N N 360 
SER   OXT HXT  sing N N 361 
THR   N   CA   sing N N 362 
THR   N   H    sing N N 363 
THR   N   H2   sing N N 364 
THR   CA  C    sing N N 365 
THR   CA  CB   sing N N 366 
THR   CA  HA   sing N N 367 
THR   C   O    doub N N 368 
THR   C   OXT  sing N N 369 
THR   CB  OG1  sing N N 370 
THR   CB  CG2  sing N N 371 
THR   CB  HB   sing N N 372 
THR   OG1 HG1  sing N N 373 
THR   CG2 HG21 sing N N 374 
THR   CG2 HG22 sing N N 375 
THR   CG2 HG23 sing N N 376 
THR   OXT HXT  sing N N 377 
TRP   N   CA   sing N N 378 
TRP   N   H    sing N N 379 
TRP   N   H2   sing N N 380 
TRP   CA  C    sing N N 381 
TRP   CA  CB   sing N N 382 
TRP   CA  HA   sing N N 383 
TRP   C   O    doub N N 384 
TRP   C   OXT  sing N N 385 
TRP   CB  CG   sing N N 386 
TRP   CB  HB2  sing N N 387 
TRP   CB  HB3  sing N N 388 
TRP   CG  CD1  doub Y N 389 
TRP   CG  CD2  sing Y N 390 
TRP   CD1 NE1  sing Y N 391 
TRP   CD1 HD1  sing N N 392 
TRP   CD2 CE2  doub Y N 393 
TRP   CD2 CE3  sing Y N 394 
TRP   NE1 CE2  sing Y N 395 
TRP   NE1 HE1  sing N N 396 
TRP   CE2 CZ2  sing Y N 397 
TRP   CE3 CZ3  doub Y N 398 
TRP   CE3 HE3  sing N N 399 
TRP   CZ2 CH2  doub Y N 400 
TRP   CZ2 HZ2  sing N N 401 
TRP   CZ3 CH2  sing Y N 402 
TRP   CZ3 HZ3  sing N N 403 
TRP   CH2 HH2  sing N N 404 
TRP   OXT HXT  sing N N 405 
TYR   N   CA   sing N N 406 
TYR   N   H    sing N N 407 
TYR   N   H2   sing N N 408 
TYR   CA  C    sing N N 409 
TYR   CA  CB   sing N N 410 
TYR   CA  HA   sing N N 411 
TYR   C   O    doub N N 412 
TYR   C   OXT  sing N N 413 
TYR   CB  CG   sing N N 414 
TYR   CB  HB2  sing N N 415 
TYR   CB  HB3  sing N N 416 
TYR   CG  CD1  doub Y N 417 
TYR   CG  CD2  sing Y N 418 
TYR   CD1 CE1  sing Y N 419 
TYR   CD1 HD1  sing N N 420 
TYR   CD2 CE2  doub Y N 421 
TYR   CD2 HD2  sing N N 422 
TYR   CE1 CZ   doub Y N 423 
TYR   CE1 HE1  sing N N 424 
TYR   CE2 CZ   sing Y N 425 
TYR   CE2 HE2  sing N N 426 
TYR   CZ  OH   sing N N 427 
TYR   OH  HH   sing N N 428 
TYR   OXT HXT  sing N N 429 
VAL   N   CA   sing N N 430 
VAL   N   H    sing N N 431 
VAL   N   H2   sing N N 432 
VAL   CA  C    sing N N 433 
VAL   CA  CB   sing N N 434 
VAL   CA  HA   sing N N 435 
VAL   C   O    doub N N 436 
VAL   C   OXT  sing N N 437 
VAL   CB  CG1  sing N N 438 
VAL   CB  CG2  sing N N 439 
VAL   CB  HB   sing N N 440 
VAL   CG1 HG11 sing N N 441 
VAL   CG1 HG12 sing N N 442 
VAL   CG1 HG13 sing N N 443 
VAL   CG2 HG21 sing N N 444 
VAL   CG2 HG22 sing N N 445 
VAL   CG2 HG23 sing N N 446 
VAL   OXT HXT  sing N N 447 
# 
_pdbx_audit_support.funding_organization   'Other private' 
_pdbx_audit_support.country                'United States' 
_pdbx_audit_support.grant_number           ? 
_pdbx_audit_support.ordinal                1 
# 
_pdbx_initial_refinement_model.id               1 
_pdbx_initial_refinement_model.entity_id_list   ? 
_pdbx_initial_refinement_model.type             'experimental model' 
_pdbx_initial_refinement_model.source_name      PDB 
_pdbx_initial_refinement_model.accession_code   2vuk 
_pdbx_initial_refinement_model.details          ? 
# 
_atom_sites.entry_id                    9BR3 
_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]   0.015394 
_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]   0.014043 
_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]   0.009537 
_atom_sites.fract_transf_vector[1]      0.000000 
_atom_sites.fract_transf_vector[2]      0.000000 
_atom_sites.fract_transf_vector[3]      0.000000 
_atom_sites.solution_primary            ? 
_atom_sites.solution_secondary          ? 
_atom_sites.solution_hydrogens          ? 
_atom_sites.special_details             ? 
# 
loop_
_atom_type.symbol 
C  
F  
N  
O  
S  
ZN 
# 
loop_
_atom_site.group_PDB 
_atom_site.id 
_atom_site.type_symbol 
_atom_site.label_atom_id 
_atom_site.label_alt_id 
_atom_site.label_comp_id 
_atom_site.label_asym_id 
_atom_site.label_entity_id 
_atom_site.label_seq_id 
_atom_site.pdbx_PDB_ins_code 
_atom_site.Cartn_x 
_atom_site.Cartn_y 
_atom_site.Cartn_z 
_atom_site.occupancy 
_atom_site.B_iso_or_equiv 
_atom_site.pdbx_formal_charge 
_atom_site.auth_seq_id 
_atom_site.auth_comp_id 
_atom_site.auth_asym_id 
_atom_site.auth_atom_id 
_atom_site.pdbx_PDB_model_num 
ATOM   1    N  N   . SER   A 1 4   ? 145.799 -43.297 32.662 1.00 59.64 ? 95  SER   A N   1 
ATOM   2    C  CA  . SER   A 1 4   ? 145.192 -43.820 33.882 1.00 62.35 ? 95  SER   A CA  1 
ATOM   3    C  C   . SER   A 1 4   ? 145.737 -45.208 34.211 1.00 62.36 ? 95  SER   A C   1 
ATOM   4    O  O   . SER   A 1 4   ? 146.346 -45.859 33.358 1.00 66.41 ? 95  SER   A O   1 
ATOM   5    C  CB  . SER   A 1 4   ? 143.665 -43.870 33.747 1.00 59.24 ? 95  SER   A CB  1 
ATOM   6    O  OG  . SER   A 1 4   ? 143.118 -42.570 33.598 1.00 61.04 ? 95  SER   A OG  1 
ATOM   7    N  N   . SER   A 1 5   ? 145.517 -45.652 35.448 1.00 53.69 ? 96  SER   A N   1 
ATOM   8    C  CA  A SER   A 1 5   ? 145.987 -46.963 35.869 0.29 51.18 ? 96  SER   A CA  1 
ATOM   9    C  CA  B SER   A 1 5   ? 145.988 -46.963 35.869 0.71 51.38 ? 96  SER   A CA  1 
ATOM   10   C  C   . SER   A 1 5   ? 145.285 -48.064 35.079 1.00 52.10 ? 96  SER   A C   1 
ATOM   11   O  O   . SER   A 1 5   ? 144.218 -47.864 34.490 1.00 49.86 ? 96  SER   A O   1 
ATOM   12   C  CB  A SER   A 1 5   ? 145.754 -47.162 37.367 0.29 48.19 ? 96  SER   A CB  1 
ATOM   13   C  CB  B SER   A 1 5   ? 145.758 -47.167 37.369 0.71 48.27 ? 96  SER   A CB  1 
ATOM   14   O  OG  A SER   A 1 5   ? 144.810 -48.193 37.602 0.29 42.64 ? 96  SER   A OG  1 
ATOM   15   O  OG  B SER   A 1 5   ? 146.172 -48.462 37.776 0.71 44.52 ? 96  SER   A OG  1 
ATOM   16   N  N   . VAL   A 1 6   ? 145.899 -49.245 35.083 1.00 50.05 ? 97  VAL   A N   1 
ATOM   17   C  CA  . VAL   A 1 6   ? 145.441 -50.386 34.298 1.00 43.95 ? 97  VAL   A CA  1 
ATOM   18   C  C   . VAL   A 1 6   ? 144.746 -51.361 35.245 1.00 35.73 ? 97  VAL   A C   1 
ATOM   19   O  O   . VAL   A 1 6   ? 145.420 -51.961 36.095 1.00 38.51 ? 97  VAL   A O   1 
ATOM   20   C  CB  . VAL   A 1 6   ? 146.607 -51.068 33.572 1.00 43.73 ? 97  VAL   A CB  1 
ATOM   21   N  N   . PRO   A 1 7   ? 143.433 -51.545 35.147 1.00 28.71 ? 98  PRO   A N   1 
ATOM   22   C  CA  . PRO   A 1 7   ? 142.798 -52.624 35.906 1.00 25.24 ? 98  PRO   A CA  1 
ATOM   23   C  C   . PRO   A 1 7   ? 143.179 -53.967 35.307 1.00 22.06 ? 98  PRO   A C   1 
ATOM   24   O  O   . PRO   A 1 7   ? 143.298 -54.108 34.089 1.00 23.49 ? 98  PRO   A O   1 
ATOM   25   C  CB  . PRO   A 1 7   ? 141.299 -52.334 35.756 1.00 27.15 ? 98  PRO   A CB  1 
ATOM   26   C  CG  . PRO   A 1 7   ? 141.200 -51.548 34.483 1.00 33.38 ? 98  PRO   A CG  1 
ATOM   27   C  CD  . PRO   A 1 7   ? 142.457 -50.734 34.398 1.00 34.75 ? 98  PRO   A CD  1 
ATOM   28   N  N   . SER   A 1 8   ? 143.400 -54.953 36.169 1.00 16.92 ? 99  SER   A N   1 
ATOM   29   C  CA  . SER   A 1 8   ? 143.770 -56.274 35.673 1.00 20.68 ? 99  SER   A CA  1 
ATOM   30   C  C   . SER   A 1 8   ? 142.625 -56.888 34.875 1.00 19.57 ? 99  SER   A C   1 
ATOM   31   O  O   . SER   A 1 8   ? 141.452 -56.697 35.199 1.00 17.39 ? 99  SER   A O   1 
ATOM   32   C  CB  . SER   A 1 8   ? 144.139 -57.204 36.826 1.00 24.73 ? 99  SER   A CB  1 
ATOM   33   O  OG  . SER   A 1 8   ? 144.259 -58.540 36.358 1.00 23.34 ? 99  SER   A OG  1 
ATOM   34   N  N   . GLN   A 1 9   ? 142.969 -57.629 33.826 1.00 17.07 ? 100 GLN   A N   1 
ATOM   35   C  CA  . GLN   A 1 9   ? 141.983 -58.402 33.082 1.00 20.87 ? 100 GLN   A CA  1 
ATOM   36   C  C   . GLN   A 1 9   ? 142.213 -59.899 33.219 1.00 20.49 ? 100 GLN   A C   1 
ATOM   37   O  O   . GLN   A 1 9   ? 141.639 -60.679 32.453 1.00 21.81 ? 100 GLN   A O   1 
ATOM   38   C  CB  . GLN   A 1 9   ? 141.988 -58.000 31.607 1.00 23.49 ? 100 GLN   A CB  1 
ATOM   39   C  CG  . GLN   A 1 9   ? 143.272 -58.345 30.876 1.00 28.51 ? 100 GLN   A CG  1 
ATOM   40   C  CD  . GLN   A 1 9   ? 143.166 -58.120 29.383 1.00 34.20 ? 100 GLN   A CD  1 
ATOM   41   O  OE1 . GLN   A 1 9   ? 143.479 -57.038 28.887 1.00 29.99 ? 100 GLN   A OE1 1 
ATOM   42   N  NE2 . GLN   A 1 9   ? 142.723 -59.147 28.654 1.00 32.26 ? 100 GLN   A NE2 1 
ATOM   43   N  N   . LYS   A 1 10  ? 143.027 -60.319 34.185 1.00 17.58 ? 101 LYS   A N   1 
ATOM   44   C  CA  . LYS   A 1 10  ? 143.432 -61.713 34.288 1.00 15.35 ? 101 LYS   A CA  1 
ATOM   45   C  C   . LYS   A 1 10  ? 142.305 -62.533 34.896 1.00 13.67 ? 101 LYS   A C   1 
ATOM   46   O  O   . LYS   A 1 10  ? 141.784 -62.193 35.960 1.00 13.42 ? 101 LYS   A O   1 
ATOM   47   C  CB  . LYS   A 1 10  ? 144.700 -61.830 35.127 1.00 18.75 ? 101 LYS   A CB  1 
ATOM   48   C  CG  . LYS   A 1 10  ? 145.204 -63.244 35.331 1.00 26.46 ? 101 LYS   A CG  1 
ATOM   49   C  CD  . LYS   A 1 10  ? 146.721 -63.238 35.408 1.00 33.37 ? 101 LYS   A CD  1 
ATOM   50   C  CE  . LYS   A 1 10  ? 147.279 -64.546 35.930 1.00 34.09 ? 101 LYS   A CE  1 
ATOM   51   N  NZ  . LYS   A 1 10  ? 146.487 -65.709 35.473 1.00 39.76 ? 101 LYS   A NZ  1 
ATOM   52   N  N   . THR   A 1 11  ? 141.920 -63.602 34.205 1.00 12.95 ? 102 THR   A N   1 
ATOM   53   C  CA  . THR   A 1 11  ? 140.876 -64.485 34.708 1.00 11.45 ? 102 THR   A CA  1 
ATOM   54   C  C   . THR   A 1 11  ? 141.278 -65.063 36.058 1.00 11.38 ? 102 THR   A C   1 
ATOM   55   O  O   . THR   A 1 11  ? 142.402 -65.545 36.232 1.00 11.46 ? 102 THR   A O   1 
ATOM   56   C  CB  . THR   A 1 11  ? 140.616 -65.603 33.700 1.00 15.80 ? 102 THR   A CB  1 
ATOM   57   O  OG1 . THR   A 1 11  ? 140.145 -65.030 32.465 1.00 20.07 ? 102 THR   A OG1 1 
ATOM   58   C  CG2 . THR   A 1 11  ? 139.594 -66.567 34.228 1.00 16.65 ? 102 THR   A CG2 1 
ATOM   59   N  N   . TYR   A 1 12  ? 140.356 -65.013 37.016 1.00 10.38 ? 103 TYR   A N   1 
ATOM   60   C  CA  . TYR   A 1 12  ? 140.643 -65.456 38.376 1.00 9.69  ? 103 TYR   A CA  1 
ATOM   61   C  C   . TYR   A 1 12  ? 139.371 -66.054 38.962 1.00 8.31  ? 103 TYR   A C   1 
ATOM   62   O  O   . TYR   A 1 12  ? 138.434 -65.317 39.279 1.00 8.74  ? 103 TYR   A O   1 
ATOM   63   C  CB  . TYR   A 1 12  ? 141.148 -64.291 39.221 1.00 9.04  ? 103 TYR   A CB  1 
ATOM   64   C  CG  . TYR   A 1 12  ? 141.375 -64.642 40.675 1.00 10.96 ? 103 TYR   A CG  1 
ATOM   65   C  CD1 . TYR   A 1 12  ? 142.326 -65.581 41.043 1.00 13.74 ? 103 TYR   A CD1 1 
ATOM   66   C  CD2 . TYR   A 1 12  ? 140.655 -64.001 41.681 1.00 14.89 ? 103 TYR   A CD2 1 
ATOM   67   C  CE1 . TYR   A 1 12  ? 142.539 -65.896 42.383 1.00 18.13 ? 103 TYR   A CE1 1 
ATOM   68   C  CE2 . TYR   A 1 12  ? 140.866 -64.299 43.012 1.00 18.33 ? 103 TYR   A CE2 1 
ATOM   69   C  CZ  . TYR   A 1 12  ? 141.799 -65.248 43.356 1.00 24.43 ? 103 TYR   A CZ  1 
ATOM   70   O  OH  . TYR   A 1 12  ? 141.994 -65.540 44.687 1.00 34.55 ? 103 TYR   A OH  1 
ATOM   71   N  N   . GLN   A 1 13  ? 139.312 -67.385 39.080 1.00 8.56  ? 104 GLN   A N   1 
ATOM   72   C  CA  . GLN   A 1 13  ? 138.086 -67.980 39.616 1.00 10.12 ? 104 GLN   A CA  1 
ATOM   73   C  C   . GLN   A 1 13  ? 137.948 -67.753 41.117 1.00 10.45 ? 104 GLN   A C   1 
ATOM   74   O  O   . GLN   A 1 13  ? 136.824 -67.654 41.625 1.00 13.70 ? 104 GLN   A O   1 
ATOM   75   C  CB  . GLN   A 1 13  ? 138.018 -69.475 39.301 1.00 9.88  ? 104 GLN   A CB  1 
ATOM   76   C  CG  . GLN   A 1 13  ? 137.724 -69.769 37.832 1.00 12.03 ? 104 GLN   A CG  1 
ATOM   77   C  CD  . GLN   A 1 13  ? 136.950 -71.074 37.617 1.00 24.25 ? 104 GLN   A CD  1 
ATOM   78   O  OE1 . GLN   A 1 13  ? 136.579 -71.771 38.571 1.00 26.14 ? 104 GLN   A OE1 1 
ATOM   79   N  NE2 . GLN   A 1 13  ? 136.704 -71.402 36.361 1.00 24.70 ? 104 GLN   A NE2 1 
ATOM   80   N  N   . GLY   A 1 14  ? 139.059 -67.680 41.848 1.00 12.99 ? 105 GLY   A N   1 
ATOM   81   C  CA  . GLY   A 1 14  ? 138.978 -67.407 43.277 1.00 10.45 ? 105 GLY   A CA  1 
ATOM   82   C  C   . GLY   A 1 14  ? 138.429 -68.593 44.060 1.00 11.57 ? 105 GLY   A C   1 
ATOM   83   O  O   . GLY   A 1 14  ? 138.184 -69.674 43.529 1.00 14.94 ? 105 GLY   A O   1 
ATOM   84   N  N   . SER   A 1 15  ? 138.205 -68.359 45.356 1.00 10.54 ? 106 SER   A N   1 
ATOM   85   C  CA  A SER   A 1 15  ? 137.790 -69.425 46.265 0.53 15.32 ? 106 SER   A CA  1 
ATOM   86   C  CA  B SER   A 1 15  ? 137.809 -69.454 46.235 0.47 15.22 ? 106 SER   A CA  1 
ATOM   87   C  C   . SER   A 1 15  ? 136.393 -69.950 45.966 1.00 17.54 ? 106 SER   A C   1 
ATOM   88   O  O   . SER   A 1 15  ? 136.076 -71.089 46.334 1.00 15.34 ? 106 SER   A O   1 
ATOM   89   C  CB  A SER   A 1 15  ? 137.839 -68.932 47.714 0.53 16.55 ? 106 SER   A CB  1 
ATOM   90   C  CB  B SER   A 1 15  ? 137.946 -69.038 47.703 0.47 16.87 ? 106 SER   A CB  1 
ATOM   91   O  OG  A SER   A 1 15  ? 139.105 -68.378 48.025 0.53 14.09 ? 106 SER   A OG  1 
ATOM   92   O  OG  B SER   A 1 15  ? 137.189 -67.880 47.991 0.47 17.78 ? 106 SER   A OG  1 
ATOM   93   N  N   . TYR   A 1 16  ? 135.539 -69.146 45.337 1.00 12.61 ? 107 TYR   A N   1 
ATOM   94   C  CA  . TYR   A 1 16  ? 134.159 -69.553 45.088 1.00 8.72  ? 107 TYR   A CA  1 
ATOM   95   C  C   . TYR   A 1 16  ? 133.955 -70.134 43.697 1.00 8.73  ? 107 TYR   A C   1 
ATOM   96   O  O   . TYR   A 1 16  ? 132.837 -70.547 43.375 1.00 13.00 ? 107 TYR   A O   1 
ATOM   97   C  CB  . TYR   A 1 16  ? 133.201 -68.370 45.325 1.00 8.74  ? 107 TYR   A CB  1 
ATOM   98   C  CG  . TYR   A 1 16  ? 133.314 -67.849 46.739 1.00 15.80 ? 107 TYR   A CG  1 
ATOM   99   C  CD1 . TYR   A 1 16  ? 132.728 -68.535 47.792 1.00 17.39 ? 107 TYR   A CD1 1 
ATOM   100  C  CD2 . TYR   A 1 16  ? 134.051 -66.700 47.031 1.00 17.06 ? 107 TYR   A CD2 1 
ATOM   101  C  CE1 . TYR   A 1 16  ? 132.850 -68.089 49.091 1.00 14.43 ? 107 TYR   A CE1 1 
ATOM   102  C  CE2 . TYR   A 1 16  ? 134.183 -66.252 48.336 1.00 16.18 ? 107 TYR   A CE2 1 
ATOM   103  C  CZ  . TYR   A 1 16  ? 133.576 -66.954 49.358 1.00 18.24 ? 107 TYR   A CZ  1 
ATOM   104  O  OH  . TYR   A 1 16  ? 133.683 -66.524 50.666 1.00 25.26 ? 107 TYR   A OH  1 
ATOM   105  N  N   . GLY   A 1 17  ? 135.010 -70.219 42.883 1.00 11.85 ? 108 GLY   A N   1 
ATOM   106  C  CA  . GLY   A 1 17  ? 134.881 -70.786 41.550 1.00 12.12 ? 108 GLY   A CA  1 
ATOM   107  C  C   . GLY   A 1 17  ? 134.019 -69.927 40.642 1.00 10.83 ? 108 GLY   A C   1 
ATOM   108  O  O   . GLY   A 1 17  ? 133.134 -70.434 39.950 1.00 9.73  ? 108 GLY   A O   1 
ATOM   109  N  N   . PHE   A 1 18  ? 134.287 -68.622 40.634 1.00 9.39  ? 109 PHE   A N   1 
ATOM   110  C  CA  . PHE   A 1 18  ? 133.498 -67.661 39.869 1.00 9.58  ? 109 PHE   A CA  1 
ATOM   111  C  C   . PHE   A 1 18  ? 133.850 -67.710 38.383 1.00 8.91  ? 109 PHE   A C   1 
ATOM   112  O  O   . PHE   A 1 18  ? 135.030 -67.694 38.019 1.00 10.44 ? 109 PHE   A O   1 
ATOM   113  C  CB  . PHE   A 1 18  ? 133.738 -66.249 40.415 1.00 9.46  ? 109 PHE   A CB  1 
ATOM   114  C  CG  . PHE   A 1 18  ? 133.078 -65.162 39.607 1.00 10.53 ? 109 PHE   A CG  1 
ATOM   115  C  CD1 . PHE   A 1 18  ? 131.706 -64.971 39.682 1.00 9.17  ? 109 PHE   A CD1 1 
ATOM   116  C  CD2 . PHE   A 1 18  ? 133.832 -64.332 38.773 1.00 8.36  ? 109 PHE   A CD2 1 
ATOM   117  C  CE1 . PHE   A 1 18  ? 131.085 -63.977 38.942 1.00 12.66 ? 109 PHE   A CE1 1 
ATOM   118  C  CE2 . PHE   A 1 18  ? 133.218 -63.339 38.024 1.00 10.91 ? 109 PHE   A CE2 1 
ATOM   119  C  CZ  . PHE   A 1 18  ? 131.845 -63.162 38.106 1.00 13.53 ? 109 PHE   A CZ  1 
ATOM   120  N  N   . ARG   A 1 19  ? 132.822 -67.749 37.527 1.00 7.30  ? 110 ARG   A N   1 
ATOM   121  C  CA  . ARG   A 1 19  ? 133.003 -67.574 36.087 1.00 9.47  ? 110 ARG   A CA  1 
ATOM   122  C  C   . ARG   A 1 19  ? 131.669 -67.171 35.464 1.00 10.17 ? 110 ARG   A C   1 
ATOM   123  O  O   . ARG   A 1 19  ? 130.605 -67.292 36.078 1.00 10.43 ? 110 ARG   A O   1 
ATOM   124  C  CB  . ARG   A 1 19  ? 133.536 -68.848 35.411 1.00 8.99  ? 110 ARG   A CB  1 
ATOM   125  C  CG  . ARG   A 1 19  ? 132.494 -69.963 35.341 1.00 7.65  ? 110 ARG   A CG  1 
ATOM   126  C  CD  . ARG   A 1 19  ? 132.368 -70.721 36.675 1.00 12.32 ? 110 ARG   A CD  1 
ATOM   127  N  NE  . ARG   A 1 19  ? 131.565 -71.925 36.498 1.00 9.26  ? 110 ARG   A NE  1 
ATOM   128  C  CZ  . ARG   A 1 19  ? 131.267 -72.784 37.465 1.00 16.23 ? 110 ARG   A CZ  1 
ATOM   129  N  NH1 . ARG   A 1 19  ? 131.701 -72.572 38.701 1.00 13.40 ? 110 ARG   A NH1 1 
ATOM   130  N  NH2 . ARG   A 1 19  ? 130.527 -73.854 37.193 1.00 12.30 ? 110 ARG   A NH2 1 
ATOM   131  N  N   . LEU   A 1 20  ? 131.743 -66.697 34.227 1.00 11.50 ? 111 LEU   A N   1 
ATOM   132  C  CA  . LEU   A 1 20  ? 130.582 -66.223 33.492 1.00 7.26  ? 111 LEU   A CA  1 
ATOM   133  C  C   . LEU   A 1 20  ? 129.967 -67.330 32.645 1.00 10.02 ? 111 LEU   A C   1 
ATOM   134  O  O   . LEU   A 1 20  ? 130.599 -68.348 32.339 1.00 11.69 ? 111 LEU   A O   1 
ATOM   135  C  CB  . LEU   A 1 20  ? 130.968 -65.057 32.583 1.00 8.60  ? 111 LEU   A CB  1 
ATOM   136  C  CG  . LEU   A 1 20  ? 131.545 -63.836 33.294 1.00 6.25  ? 111 LEU   A CG  1 
ATOM   137  C  CD1 . LEU   A 1 20  ? 131.963 -62.787 32.233 1.00 8.07  ? 111 LEU   A CD1 1 
ATOM   138  C  CD2 . LEU   A 1 20  ? 130.552 -63.226 34.297 1.00 6.10  ? 111 LEU   A CD2 1 
ATOM   139  N  N   . GLY   A 1 21  ? 128.715 -67.105 32.251 1.00 6.88  ? 112 GLY   A N   1 
ATOM   140  C  CA  . GLY   A 1 21  ? 128.067 -67.938 31.258 1.00 7.18  ? 112 GLY   A CA  1 
ATOM   141  C  C   . GLY   A 1 21  ? 127.226 -67.071 30.345 1.00 9.15  ? 112 GLY   A C   1 
ATOM   142  O  O   . GLY   A 1 21  ? 126.869 -65.946 30.691 1.00 8.14  ? 112 GLY   A O   1 
ATOM   143  N  N   . PHE   A 1 22  ? 126.941 -67.593 29.152 1.00 8.45  ? 113 PHE   A N   1 
ATOM   144  C  CA  . PHE   A 1 22  ? 126.127 -66.869 28.188 1.00 7.68  ? 113 PHE   A CA  1 
ATOM   145  C  C   . PHE   A 1 22  ? 125.061 -67.786 27.607 1.00 11.28 ? 113 PHE   A C   1 
ATOM   146  O  O   . PHE   A 1 22  ? 125.266 -68.996 27.478 1.00 12.49 ? 113 PHE   A O   1 
ATOM   147  C  CB  . PHE   A 1 22  ? 126.998 -66.283 27.076 1.00 7.73  ? 113 PHE   A CB  1 
ATOM   148  C  CG  . PHE   A 1 22  ? 128.037 -65.345 27.591 1.00 9.54  ? 113 PHE   A CG  1 
ATOM   149  C  CD1 . PHE   A 1 22  ? 129.250 -65.827 28.055 1.00 8.15  ? 113 PHE   A CD1 1 
ATOM   150  C  CD2 . PHE   A 1 22  ? 127.782 -63.994 27.680 1.00 11.65 ? 113 PHE   A CD2 1 
ATOM   151  C  CE1 . PHE   A 1 22  ? 130.208 -64.968 28.578 1.00 6.98  ? 113 PHE   A CE1 1 
ATOM   152  C  CE2 . PHE   A 1 22  ? 128.747 -63.123 28.188 1.00 9.52  ? 113 PHE   A CE2 1 
ATOM   153  C  CZ  . PHE   A 1 22  ? 129.960 -63.619 28.633 1.00 8.90  ? 113 PHE   A CZ  1 
ATOM   154  N  N   . LEU   A 1 23  ? 123.915 -67.198 27.263 1.00 8.79  ? 114 LEU   A N   1 
ATOM   155  C  CA  . LEU   A 1 23  ? 122.877 -67.953 26.578 1.00 10.52 ? 114 LEU   A CA  1 
ATOM   156  C  C   . LEU   A 1 23  ? 123.354 -68.362 25.185 1.00 13.20 ? 114 LEU   A C   1 
ATOM   157  O  O   . LEU   A 1 23  ? 124.308 -67.808 24.639 1.00 13.45 ? 114 LEU   A O   1 
ATOM   158  C  CB  . LEU   A 1 23  ? 121.598 -67.128 26.455 1.00 9.18  ? 114 LEU   A CB  1 
ATOM   159  C  CG  . LEU   A 1 23  ? 120.944 -66.694 27.766 1.00 15.67 ? 114 LEU   A CG  1 
ATOM   160  C  CD1 . LEU   A 1 23  ? 119.699 -65.864 27.479 1.00 20.28 ? 114 LEU   A CD1 1 
ATOM   161  C  CD2 . LEU   A 1 23  ? 120.613 -67.914 28.614 1.00 15.21 ? 114 LEU   A CD2 1 
ATOM   162  N  N   . HIS   A 1 24  ? 122.677 -69.340 24.603 1.00 9.92  ? 115 HIS   A N   1 
ATOM   163  C  CA  . HIS   A 1 24  ? 122.990 -69.766 23.239 1.00 10.52 ? 115 HIS   A CA  1 
ATOM   164  C  C   . HIS   A 1 24  ? 121.872 -69.233 22.355 1.00 13.55 ? 115 HIS   A C   1 
ATOM   165  O  O   . HIS   A 1 24  ? 120.855 -69.893 22.143 1.00 18.92 ? 115 HIS   A O   1 
ATOM   166  C  CB  . HIS   A 1 24  ? 123.143 -71.283 23.165 1.00 12.85 ? 115 HIS   A CB  1 
ATOM   167  C  CG  . HIS   A 1 24  ? 124.305 -71.783 23.966 1.00 14.82 ? 115 HIS   A CG  1 
ATOM   168  N  ND1 . HIS   A 1 24  ? 124.224 -72.019 25.319 1.00 16.52 ? 115 HIS   A ND1 1 
ATOM   169  C  CD2 . HIS   A 1 24  ? 125.593 -72.012 23.619 1.00 15.32 ? 115 HIS   A CD2 1 
ATOM   170  C  CE1 . HIS   A 1 24  ? 125.408 -72.394 25.771 1.00 17.40 ? 115 HIS   A CE1 1 
ATOM   171  N  NE2 . HIS   A 1 24  ? 126.257 -72.396 24.759 1.00 14.21 ? 115 HIS   A NE2 1 
ATOM   172  N  N   . SER   A 1 25  ? 122.072 -68.025 21.836 1.00 13.32 ? 116 SER   A N   1 
ATOM   173  C  CA  . SER   A 1 25  ? 121.011 -67.288 21.167 1.00 16.23 ? 116 SER   A CA  1 
ATOM   174  C  C   . SER   A 1 25  ? 121.018 -67.442 19.652 1.00 17.82 ? 116 SER   A C   1 
ATOM   175  O  O   . SER   A 1 25  ? 120.092 -66.946 18.993 1.00 17.79 ? 116 SER   A O   1 
ATOM   176  C  CB  . SER   A 1 25  ? 121.110 -65.806 21.532 1.00 16.17 ? 116 SER   A CB  1 
ATOM   177  O  OG  . SER   A 1 25  ? 120.944 -65.648 22.932 1.00 19.87 ? 116 SER   A OG  1 
ATOM   178  N  N   . GLY   A 1 26  ? 122.027 -68.102 19.082 1.00 13.33 ? 117 GLY   A N   1 
ATOM   179  C  CA  . GLY   A 1 26  ? 122.082 -68.275 17.644 1.00 14.37 ? 117 GLY   A CA  1 
ATOM   180  C  C   . GLY   A 1 26  ? 122.527 -67.012 16.925 1.00 13.32 ? 117 GLY   A C   1 
ATOM   181  O  O   . GLY   A 1 26  ? 122.904 -66.002 17.528 1.00 12.98 ? 117 GLY   A O   1 
ATOM   182  N  N   . THR   A 1 27  ? 122.486 -67.080 15.595 1.00 14.22 ? 118 THR   A N   1 
ATOM   183  C  CA  . THR   A 1 27  ? 122.986 -65.981 14.774 1.00 19.42 ? 118 THR   A CA  1 
ATOM   184  C  C   . THR   A 1 27  ? 121.973 -65.508 13.739 1.00 22.50 ? 118 THR   A C   1 
ATOM   185  O  O   . THR   A 1 27  ? 122.372 -64.942 12.717 1.00 21.90 ? 118 THR   A O   1 
ATOM   186  C  CB  . THR   A 1 27  ? 124.288 -66.375 14.080 1.00 18.41 ? 118 THR   A CB  1 
ATOM   187  O  OG1 . THR   A 1 27  ? 124.039 -67.476 13.200 1.00 23.33 ? 118 THR   A OG1 1 
ATOM   188  C  CG2 . THR   A 1 27  ? 125.321 -66.789 15.115 1.00 20.52 ? 118 THR   A CG2 1 
ATOM   189  N  N   . ALA   A 1 28  ? 120.680 -65.720 13.982 1.00 20.46 ? 119 ALA   A N   1 
ATOM   190  C  CA  . ALA   A 1 28  ? 119.655 -65.193 13.090 1.00 24.17 ? 119 ALA   A CA  1 
ATOM   191  C  C   . ALA   A 1 28  ? 119.783 -63.678 12.947 1.00 26.62 ? 119 ALA   A C   1 
ATOM   192  O  O   . ALA   A 1 28  ? 120.284 -62.979 13.838 1.00 23.27 ? 119 ALA   A O   1 
ATOM   193  C  CB  . ALA   A 1 28  ? 118.260 -65.554 13.603 1.00 20.84 ? 119 ALA   A CB  1 
ATOM   194  N  N   . LYS   A 1 29  ? 119.319 -63.174 11.798 1.00 25.40 ? 120 LYS   A N   1 
ATOM   195  C  CA  . LYS   A 1 29  ? 119.452 -61.754 11.492 1.00 26.81 ? 120 LYS   A CA  1 
ATOM   196  C  C   . LYS   A 1 29  ? 118.793 -60.887 12.553 1.00 29.14 ? 120 LYS   A C   1 
ATOM   197  O  O   . LYS   A 1 29  ? 119.261 -59.776 12.824 1.00 30.03 ? 120 LYS   A O   1 
ATOM   198  C  CB  . LYS   A 1 29  ? 118.849 -61.451 10.116 1.00 26.71 ? 120 LYS   A CB  1 
ATOM   199  N  N   . SER   A 1 30  ? 117.730 -61.383 13.176 1.00 27.23 ? 121 SER   A N   1 
ATOM   200  C  CA  . SER   A 1 30  ? 116.984 -60.608 14.152 1.00 32.12 ? 121 SER   A CA  1 
ATOM   201  C  C   . SER   A 1 30  ? 117.568 -60.660 15.562 1.00 31.20 ? 121 SER   A C   1 
ATOM   202  O  O   . SER   A 1 30  ? 117.093 -59.913 16.427 1.00 28.67 ? 121 SER   A O   1 
ATOM   203  C  CB  . SER   A 1 30  ? 115.535 -61.095 14.190 1.00 32.15 ? 121 SER   A CB  1 
ATOM   204  O  OG  . SER   A 1 30  ? 115.480 -62.465 14.540 1.00 37.74 ? 121 SER   A OG  1 
ATOM   205  N  N   . VAL   A 1 31  ? 118.567 -61.509 15.828 1.00 26.31 ? 122 VAL   A N   1 
ATOM   206  C  CA  . VAL   A 1 31  ? 119.049 -61.657 17.201 1.00 20.50 ? 122 VAL   A CA  1 
ATOM   207  C  C   . VAL   A 1 31  ? 119.569 -60.315 17.713 1.00 18.99 ? 122 VAL   A C   1 
ATOM   208  O  O   . VAL   A 1 31  ? 120.216 -59.556 16.983 1.00 25.11 ? 122 VAL   A O   1 
ATOM   209  C  CB  . VAL   A 1 31  ? 120.115 -62.768 17.289 1.00 20.17 ? 122 VAL   A CB  1 
ATOM   210  C  CG1 . VAL   A 1 31  ? 121.476 -62.299 16.807 1.00 22.15 ? 122 VAL   A CG1 1 
ATOM   211  C  CG2 . VAL   A 1 31  ? 120.216 -63.294 18.713 1.00 25.82 ? 122 VAL   A CG2 1 
ATOM   212  N  N   . THR   A 1 32  ? 119.250 -59.994 18.968 1.00 20.97 ? 123 THR   A N   1 
ATOM   213  C  CA  . THR   A 1 32  ? 119.675 -58.721 19.547 1.00 19.57 ? 123 THR   A CA  1 
ATOM   214  C  C   . THR   A 1 32  ? 120.945 -58.830 20.376 1.00 15.54 ? 123 THR   A C   1 
ATOM   215  O  O   . THR   A 1 32  ? 121.589 -57.806 20.633 1.00 16.53 ? 123 THR   A O   1 
ATOM   216  C  CB  . THR   A 1 32  ? 118.571 -58.122 20.428 1.00 23.83 ? 123 THR   A CB  1 
ATOM   217  O  OG1 . THR   A 1 32  ? 118.202 -59.068 21.433 1.00 19.46 ? 123 THR   A OG1 1 
ATOM   218  C  CG2 . THR   A 1 32  ? 117.344 -57.757 19.592 1.00 24.25 ? 123 THR   A CG2 1 
ATOM   219  N  N   . CYS   A 1 33  ? 121.306 -60.037 20.803 1.00 14.51 ? 124 CYS   A N   1 
ATOM   220  C  CA  . CYS   A 1 33  ? 122.498 -60.278 21.600 1.00 11.68 ? 124 CYS   A CA  1 
ATOM   221  C  C   . CYS   A 1 33  ? 122.933 -61.713 21.339 1.00 12.90 ? 124 CYS   A C   1 
ATOM   222  O  O   . CYS   A 1 33  ? 122.096 -62.618 21.342 1.00 11.74 ? 124 CYS   A O   1 
ATOM   223  C  CB  . CYS   A 1 33  ? 122.214 -60.053 23.093 1.00 13.10 ? 124 CYS   A CB  1 
ATOM   224  S  SG  . CYS   A 1 33  ? 123.627 -60.278 24.179 1.00 18.23 ? 124 CYS   A SG  1 
ATOM   225  N  N   . THR   A 1 34  ? 124.214 -61.925 21.071 1.00 11.06 ? 125 THR   A N   1 
ATOM   226  C  CA  . THR   A 1 34  ? 124.664 -63.290 20.835 1.00 12.10 ? 125 THR   A CA  1 
ATOM   227  C  C   . THR   A 1 34  ? 126.137 -63.398 21.189 1.00 10.46 ? 125 THR   A C   1 
ATOM   228  O  O   . THR   A 1 34  ? 126.905 -62.459 20.970 1.00 11.23 ? 125 THR   A O   1 
ATOM   229  C  CB  . THR   A 1 34  ? 124.417 -63.738 19.383 1.00 17.94 ? 125 THR   A CB  1 
ATOM   230  O  OG1 . THR   A 1 34  ? 124.754 -65.127 19.258 1.00 16.68 ? 125 THR   A OG1 1 
ATOM   231  C  CG2 . THR   A 1 34  ? 125.250 -62.913 18.395 1.00 14.45 ? 125 THR   A CG2 1 
ATOM   232  N  N   . TYR   A 1 35  ? 126.520 -64.543 21.751 1.00 9.43  ? 126 TYR   A N   1 
ATOM   233  C  CA  . TYR   A 1 35  ? 127.847 -64.726 22.316 1.00 9.06  ? 126 TYR   A CA  1 
ATOM   234  C  C   . TYR   A 1 35  ? 128.588 -65.804 21.537 1.00 10.10 ? 126 TYR   A C   1 
ATOM   235  O  O   . TYR   A 1 35  ? 128.040 -66.882 21.287 1.00 9.89  ? 126 TYR   A O   1 
ATOM   236  C  CB  . TYR   A 1 35  ? 127.776 -65.110 23.802 1.00 8.51  ? 126 TYR   A CB  1 
ATOM   237  C  CG  . TYR   A 1 35  ? 129.143 -65.465 24.357 1.00 8.74  ? 126 TYR   A CG  1 
ATOM   238  C  CD1 . TYR   A 1 35  ? 130.085 -64.476 24.608 1.00 8.01  ? 126 TYR   A CD1 1 
ATOM   239  C  CD2 . TYR   A 1 35  ? 129.499 -66.785 24.591 1.00 8.44  ? 126 TYR   A CD2 1 
ATOM   240  C  CE1 . TYR   A 1 35  ? 131.357 -64.794 25.090 1.00 8.95  ? 126 TYR   A CE1 1 
ATOM   241  C  CE2 . TYR   A 1 35  ? 130.762 -67.118 25.066 1.00 8.35  ? 126 TYR   A CE2 1 
ATOM   242  C  CZ  . TYR   A 1 35  ? 131.683 -66.121 25.315 1.00 8.11  ? 126 TYR   A CZ  1 
ATOM   243  O  OH  . TYR   A 1 35  ? 132.939 -66.445 25.792 1.00 9.53  ? 126 TYR   A OH  1 
ATOM   244  N  N   . SER   A 1 36  ? 129.836 -65.512 21.171 1.00 11.71 ? 127 SER   A N   1 
ATOM   245  C  CA  . SER   A 1 36  ? 130.682 -66.472 20.479 1.00 10.13 ? 127 SER   A CA  1 
ATOM   246  C  C   . SER   A 1 36  ? 131.671 -67.080 21.455 1.00 9.82  ? 127 SER   A C   1 
ATOM   247  O  O   . SER   A 1 36  ? 132.611 -66.389 21.878 1.00 9.56  ? 127 SER   A O   1 
ATOM   248  C  CB  . SER   A 1 36  ? 131.433 -65.801 19.327 1.00 10.63 ? 127 SER   A CB  1 
ATOM   249  O  OG  . SER   A 1 36  ? 132.402 -66.701 18.805 1.00 13.96 ? 127 SER   A OG  1 
ATOM   250  N  N   . PRO   A 1 37  ? 131.523 -68.346 21.829 1.00 10.60 ? 128 PRO   A N   1 
ATOM   251  C  CA  . PRO   A 1 37  ? 132.576 -68.983 22.637 1.00 12.29 ? 128 PRO   A CA  1 
ATOM   252  C  C   . PRO   A 1 37  ? 133.926 -69.020 21.938 1.00 12.48 ? 128 PRO   A C   1 
ATOM   253  O  O   . PRO   A 1 37  ? 134.958 -68.867 22.595 1.00 14.53 ? 128 PRO   A O   1 
ATOM   254  C  CB  . PRO   A 1 37  ? 132.021 -70.401 22.879 1.00 14.11 ? 128 PRO   A CB  1 
ATOM   255  C  CG  . PRO   A 1 37  ? 130.539 -70.268 22.707 1.00 15.56 ? 128 PRO   A CG  1 
ATOM   256  C  CD  . PRO   A 1 37  ? 130.356 -69.222 21.636 1.00 10.17 ? 128 PRO   A CD  1 
ATOM   257  N  N   . ALA   A 1 38  ? 133.952 -69.246 20.618 1.00 13.99 ? 129 ALA   A N   1 
ATOM   258  C  CA  . ALA   A 1 38  ? 135.229 -69.356 19.924 1.00 11.56 ? 129 ALA   A CA  1 
ATOM   259  C  C   . ALA   A 1 38  ? 135.997 -68.046 19.976 1.00 18.76 ? 129 ALA   A C   1 
ATOM   260  O  O   . ALA   A 1 38  ? 137.226 -68.051 20.085 1.00 18.84 ? 129 ALA   A O   1 
ATOM   261  C  CB  . ALA   A 1 38  ? 135.012 -69.781 18.477 1.00 12.41 ? 129 ALA   A CB  1 
ATOM   262  N  N   . LEU   A 1 39  ? 135.295 -66.921 19.934 1.00 17.19 ? 130 LEU   A N   1 
ATOM   263  C  CA  . LEU   A 1 39  ? 135.933 -65.614 19.970 1.00 16.42 ? 130 LEU   A CA  1 
ATOM   264  C  C   . LEU   A 1 39  ? 135.979 -65.010 21.369 1.00 18.08 ? 130 LEU   A C   1 
ATOM   265  O  O   . LEU   A 1 39  ? 136.596 -63.955 21.540 1.00 16.69 ? 130 LEU   A O   1 
ATOM   266  C  CB  . LEU   A 1 39  ? 135.211 -64.650 19.013 1.00 13.70 ? 130 LEU   A CB  1 
ATOM   267  C  CG  . LEU   A 1 39  ? 135.129 -65.102 17.550 1.00 15.75 ? 130 LEU   A CG  1 
ATOM   268  C  CD1 . LEU   A 1 39  ? 134.166 -64.229 16.752 1.00 20.65 ? 130 LEU   A CD1 1 
ATOM   269  C  CD2 . LEU   A 1 39  ? 136.506 -65.091 16.924 1.00 19.77 ? 130 LEU   A CD2 1 
ATOM   270  N  N   . ASN   A 1 40  ? 135.382 -65.671 22.367 1.00 11.40 ? 131 ASN   A N   1 
ATOM   271  C  CA  . ASN   A 1 40  ? 135.059 -65.063 23.666 1.00 9.37  ? 131 ASN   A CA  1 
ATOM   272  C  C   . ASN   A 1 40  ? 134.539 -63.633 23.487 1.00 9.56  ? 131 ASN   A C   1 
ATOM   273  O  O   . ASN   A 1 40  ? 135.032 -62.676 24.087 1.00 11.60 ? 131 ASN   A O   1 
ATOM   274  C  CB  . ASN   A 1 40  ? 136.264 -65.100 24.618 1.00 10.85 ? 131 ASN   A CB  1 
ATOM   275  C  CG  . ASN   A 1 40  ? 135.904 -64.634 26.027 1.00 13.61 ? 131 ASN   A CG  1 
ATOM   276  O  OD1 . ASN   A 1 40  ? 134.767 -64.795 26.466 1.00 10.08 ? 131 ASN   A OD1 1 
ATOM   277  N  ND2 . ASN   A 1 40  ? 136.866 -64.028 26.727 1.00 8.10  ? 131 ASN   A ND2 1 
ATOM   278  N  N   . LYS   A 1 41  ? 133.516 -63.489 22.651 1.00 9.12  ? 132 LYS   A N   1 
ATOM   279  C  CA  . LYS   A 1 41  ? 133.071 -62.173 22.213 1.00 12.18 ? 132 LYS   A CA  1 
ATOM   280  C  C   . LYS   A 1 41  ? 131.549 -62.100 22.198 1.00 13.60 ? 132 LYS   A C   1 
ATOM   281  O  O   . LYS   A 1 41  ? 130.882 -62.938 21.582 1.00 9.84  ? 132 LYS   A O   1 
ATOM   282  C  CB  . LYS   A 1 41  ? 133.639 -61.857 20.819 1.00 9.68  ? 132 LYS   A CB  1 
ATOM   283  C  CG  . LYS   A 1 41  ? 133.368 -60.440 20.335 1.00 9.49  ? 132 LYS   A CG  1 
ATOM   284  C  CD  . LYS   A 1 41  ? 134.186 -60.169 19.069 1.00 10.22 ? 132 LYS   A CD  1 
ATOM   285  C  CE  . LYS   A 1 41  ? 134.035 -58.731 18.637 1.00 14.35 ? 132 LYS   A CE  1 
ATOM   286  N  NZ  . LYS   A 1 41  ? 135.107 -58.397 17.661 1.00 17.12 ? 132 LYS   A NZ  1 
ATOM   287  N  N   . LEU   A 1 42  ? 131.011 -61.093 22.870 1.00 11.31 ? 133 LEU   A N   1 
ATOM   288  C  CA  . LEU   A 1 42  ? 129.583 -60.814 22.867 1.00 9.85  ? 133 LEU   A CA  1 
ATOM   289  C  C   . LEU   A 1 42  ? 129.282 -59.767 21.800 1.00 11.07 ? 133 LEU   A C   1 
ATOM   290  O  O   . LEU   A 1 42  ? 129.967 -58.747 21.722 1.00 11.22 ? 133 LEU   A O   1 
ATOM   291  C  CB  . LEU   A 1 42  ? 129.136 -60.313 24.242 1.00 9.80  ? 133 LEU   A CB  1 
ATOM   292  C  CG  . LEU   A 1 42  ? 127.630 -60.071 24.438 1.00 13.12 ? 133 LEU   A CG  1 
ATOM   293  C  CD1 . LEU   A 1 42  ? 126.902 -61.389 24.611 1.00 13.56 ? 133 LEU   A CD1 1 
ATOM   294  C  CD2 . LEU   A 1 42  ? 127.392 -59.166 25.641 1.00 16.12 ? 133 LEU   A CD2 1 
ATOM   295  N  N   . PHE   A 1 43  ? 128.268 -60.031 20.982 1.00 9.90  ? 134 PHE   A N   1 
ATOM   296  C  CA  . PHE   A 1 43  ? 127.801 -59.128 19.936 1.00 9.81  ? 134 PHE   A CA  1 
ATOM   297  C  C   . PHE   A 1 43  ? 126.406 -58.659 20.310 1.00 13.90 ? 134 PHE   A C   1 
ATOM   298  O  O   . PHE   A 1 43  ? 125.525 -59.488 20.552 1.00 13.36 ? 134 PHE   A O   1 
ATOM   299  C  CB  . PHE   A 1 43  ? 127.725 -59.836 18.577 1.00 11.10 ? 134 PHE   A CB  1 
ATOM   300  C  CG  . PHE   A 1 43  ? 129.034 -60.359 18.078 1.00 14.16 ? 134 PHE   A CG  1 
ATOM   301  C  CD1 . PHE   A 1 43  ? 129.591 -61.507 18.619 1.00 10.40 ? 134 PHE   A CD1 1 
ATOM   302  C  CD2 . PHE   A 1 43  ? 129.699 -59.711 17.044 1.00 12.11 ? 134 PHE   A CD2 1 
ATOM   303  C  CE1 . PHE   A 1 43  ? 130.792 -61.992 18.149 1.00 14.27 ? 134 PHE   A CE1 1 
ATOM   304  C  CE2 . PHE   A 1 43  ? 130.901 -60.188 16.565 1.00 11.51 ? 134 PHE   A CE2 1 
ATOM   305  C  CZ  . PHE   A 1 43  ? 131.449 -61.331 17.115 1.00 17.56 ? 134 PHE   A CZ  1 
ATOM   306  N  N   . CYS   A 1 44  ? 126.186 -57.347 20.335 1.00 10.90 ? 135 CYS   A N   1 
ATOM   307  C  CA  . CYS   A 1 44  ? 124.882 -56.890 20.786 1.00 12.05 ? 135 CYS   A CA  1 
ATOM   308  C  C   . CYS   A 1 44  ? 124.492 -55.604 20.083 1.00 14.92 ? 135 CYS   A C   1 
ATOM   309  O  O   . CYS   A 1 44  ? 125.326 -54.889 19.524 1.00 12.63 ? 135 CYS   A O   1 
ATOM   310  C  CB  . CYS   A 1 44  ? 124.850 -56.670 22.295 1.00 12.96 ? 135 CYS   A CB  1 
ATOM   311  S  SG  . CYS   A 1 44  ? 126.071 -55.456 22.841 1.00 15.59 ? 135 CYS   A SG  1 
ATOM   312  N  N   . GLN   A 1 45  ? 123.205 -55.313 20.156 1.00 15.92 ? 136 GLN   A N   1 
ATOM   313  C  CA  . GLN   A 1 45  ? 122.663 -54.073 19.634 1.00 18.62 ? 136 GLN   A CA  1 
ATOM   314  C  C   . GLN   A 1 45  ? 122.692 -52.988 20.702 1.00 19.03 ? 136 GLN   A C   1 
ATOM   315  O  O   . GLN   A 1 45  ? 122.790 -53.260 21.902 1.00 17.70 ? 136 GLN   A O   1 
ATOM   316  C  CB  . GLN   A 1 45  ? 121.237 -54.285 19.136 1.00 16.33 ? 136 GLN   A CB  1 
ATOM   317  C  CG  . GLN   A 1 45  ? 121.168 -55.111 17.883 1.00 21.17 ? 136 GLN   A CG  1 
ATOM   318  C  CD  . GLN   A 1 45  ? 119.749 -55.365 17.443 1.00 28.85 ? 136 GLN   A CD  1 
ATOM   319  O  OE1 . GLN   A 1 45  ? 118.804 -55.033 18.149 1.00 28.80 ? 136 GLN   A OE1 1 
ATOM   320  N  NE2 . GLN   A 1 45  ? 119.592 -55.955 16.272 1.00 30.92 ? 136 GLN   A NE2 1 
ATOM   321  N  N   . LEU   A 1 46  ? 122.592 -51.744 20.234 1.00 17.20 ? 137 LEU   A N   1 
ATOM   322  C  CA  . LEU   A 1 46  ? 122.663 -50.578 21.100 1.00 10.39 ? 137 LEU   A CA  1 
ATOM   323  C  C   . LEU   A 1 46  ? 121.502 -50.554 22.084 1.00 10.75 ? 137 LEU   A C   1 
ATOM   324  O  O   . LEU   A 1 46  ? 120.340 -50.644 21.681 1.00 13.24 ? 137 LEU   A O   1 
ATOM   325  C  CB  . LEU   A 1 46  ? 122.633 -49.312 20.234 1.00 15.80 ? 137 LEU   A CB  1 
ATOM   326  C  CG  . LEU   A 1 46  ? 122.728 -47.966 20.945 1.00 19.78 ? 137 LEU   A CG  1 
ATOM   327  C  CD1 . LEU   A 1 46  ? 124.119 -47.787 21.447 1.00 21.19 ? 137 LEU   A CD1 1 
ATOM   328  C  CD2 . LEU   A 1 46  ? 122.363 -46.824 19.996 1.00 18.62 ? 137 LEU   A CD2 1 
ATOM   329  N  N   . ALA   A 1 47  ? 121.817 -50.426 23.378 1.00 9.66  ? 138 ALA   A N   1 
ATOM   330  C  CA  . ALA   A 1 47  ? 120.810 -50.215 24.425 1.00 14.56 ? 138 ALA   A CA  1 
ATOM   331  C  C   . ALA   A 1 47  ? 119.830 -51.383 24.535 1.00 20.89 ? 138 ALA   A C   1 
ATOM   332  O  O   . ALA   A 1 47  ? 118.680 -51.203 24.945 1.00 26.36 ? 138 ALA   A O   1 
ATOM   333  C  CB  . ALA   A 1 47  ? 120.034 -48.907 24.209 1.00 13.62 ? 138 ALA   A CB  1 
ATOM   334  N  N   . LYS   A 1 48  ? 120.254 -52.582 24.156 1.00 16.41 ? 139 LYS   A N   1 
ATOM   335  C  CA  . LYS   A 1 48  ? 119.405 -53.759 24.243 1.00 16.65 ? 139 LYS   A CA  1 
ATOM   336  C  C   . LYS   A 1 48  ? 119.892 -54.663 25.366 1.00 13.95 ? 139 LYS   A C   1 
ATOM   337  O  O   . LYS   A 1 48  ? 121.039 -54.584 25.789 1.00 14.36 ? 139 LYS   A O   1 
ATOM   338  C  CB  . LYS   A 1 48  ? 119.394 -54.538 22.925 1.00 17.03 ? 139 LYS   A CB  1 
ATOM   339  C  CG  . LYS   A 1 48  ? 118.727 -53.797 21.775 1.00 29.21 ? 139 LYS   A CG  1 
ATOM   340  C  CD  . LYS   A 1 48  ? 117.297 -53.430 22.120 1.00 35.84 ? 139 LYS   A CD  1 
ATOM   341  C  CE  . LYS   A 1 48  ? 116.589 -52.861 20.907 1.00 45.44 ? 139 LYS   A CE  1 
ATOM   342  N  NZ  . LYS   A 1 48  ? 116.637 -53.831 19.779 1.00 51.72 ? 139 LYS   A NZ  1 
ATOM   343  N  N   . THR   A 1 49  ? 119.005 -55.539 25.826 1.00 13.27 ? 140 THR   A N   1 
ATOM   344  C  CA  . THR   A 1 49  ? 119.323 -56.428 26.939 1.00 12.97 ? 140 THR   A CA  1 
ATOM   345  C  C   . THR   A 1 49  ? 120.432 -57.403 26.566 1.00 14.92 ? 140 THR   A C   1 
ATOM   346  O  O   . THR   A 1 49  ? 120.315 -58.130 25.577 1.00 15.58 ? 140 THR   A O   1 
ATOM   347  C  CB  . THR   A 1 49  ? 118.077 -57.210 27.350 1.00 12.26 ? 140 THR   A CB  1 
ATOM   348  O  OG1 . THR   A 1 49  ? 117.011 -56.301 27.650 1.00 12.31 ? 140 THR   A OG1 1 
ATOM   349  C  CG2 . THR   A 1 49  ? 118.376 -58.053 28.575 1.00 14.84 ? 140 THR   A CG2 1 
ATOM   350  N  N   . CYS   A 1 50  ? 121.491 -57.441 27.379 1.00 10.43 ? 141 CYS   A N   1 
ATOM   351  C  CA  . CYS   A 1 50  ? 122.569 -58.428 27.258 1.00 11.67 ? 141 CYS   A CA  1 
ATOM   352  C  C   . CYS   A 1 50  ? 122.611 -59.292 28.510 1.00 11.71 ? 141 CYS   A C   1 
ATOM   353  O  O   . CYS   A 1 50  ? 123.165 -58.864 29.540 1.00 10.90 ? 141 CYS   A O   1 
ATOM   354  C  CB  . CYS   A 1 50  ? 123.921 -57.749 27.061 1.00 12.42 ? 141 CYS   A CB  1 
ATOM   355  S  SG  . CYS   A 1 50  ? 123.992 -56.709 25.616 1.00 16.09 ? 141 CYS   A SG  1 
ATOM   356  N  N   . PRO   A 1 51  ? 122.044 -60.498 28.480 1.00 10.47 ? 142 PRO   A N   1 
ATOM   357  C  CA  . PRO   A 1 51  ? 122.095 -61.370 29.664 1.00 12.30 ? 142 PRO   A CA  1 
ATOM   358  C  C   . PRO   A 1 51  ? 123.491 -61.934 29.864 1.00 12.96 ? 142 PRO   A C   1 
ATOM   359  O  O   . PRO   A 1 51  ? 124.098 -62.478 28.939 1.00 11.39 ? 142 PRO   A O   1 
ATOM   360  C  CB  . PRO   A 1 51  ? 121.094 -62.489 29.341 1.00 11.24 ? 142 PRO   A CB  1 
ATOM   361  C  CG  . PRO   A 1 51  ? 120.428 -62.107 28.028 1.00 12.63 ? 142 PRO   A CG  1 
ATOM   362  C  CD  . PRO   A 1 51  ? 121.366 -61.145 27.345 1.00 12.26 ? 142 PRO   A CD  1 
ATOM   363  N  N   . VAL   A 1 52  ? 123.996 -61.803 31.083 1.00 9.61  ? 143 VAL   A N   1 
ATOM   364  C  CA  . VAL   A 1 52  ? 125.268 -62.391 31.468 1.00 6.91  ? 143 VAL   A CA  1 
ATOM   365  C  C   . VAL   A 1 52  ? 125.023 -63.222 32.716 1.00 11.73 ? 143 VAL   A C   1 
ATOM   366  O  O   . VAL   A 1 52  ? 124.548 -62.695 33.729 1.00 9.52  ? 143 VAL   A O   1 
ATOM   367  C  CB  . VAL   A 1 52  ? 126.344 -61.322 31.716 1.00 10.85 ? 143 VAL   A CB  1 
ATOM   368  C  CG1 . VAL   A 1 52  ? 127.653 -61.965 32.164 1.00 9.53  ? 143 VAL   A CG1 1 
ATOM   369  C  CG2 . VAL   A 1 52  ? 126.568 -60.517 30.450 1.00 9.41  ? 143 VAL   A CG2 1 
ATOM   370  N  N   . GLN   A 1 53  ? 125.348 -64.513 32.644 1.00 8.30  ? 144 GLN   A N   1 
ATOM   371  C  CA  . GLN   A 1 53  ? 125.185 -65.421 33.770 1.00 6.86  ? 144 GLN   A CA  1 
ATOM   372  C  C   . GLN   A 1 53  ? 126.384 -65.363 34.711 1.00 8.82  ? 144 GLN   A C   1 
ATOM   373  O  O   . GLN   A 1 53  ? 127.533 -65.224 34.283 1.00 11.29 ? 144 GLN   A O   1 
ATOM   374  C  CB  . GLN   A 1 53  ? 125.013 -66.865 33.291 1.00 7.16  ? 144 GLN   A CB  1 
ATOM   375  C  CG  . GLN   A 1 53  ? 123.790 -67.095 32.427 1.00 13.37 ? 144 GLN   A CG  1 
ATOM   376  C  CD  . GLN   A 1 53  ? 123.751 -68.504 31.850 1.00 14.87 ? 144 GLN   A CD  1 
ATOM   377  O  OE1 . GLN   A 1 53  ? 124.780 -69.178 31.748 1.00 10.07 ? 144 GLN   A OE1 1 
ATOM   378  N  NE2 . GLN   A 1 53  ? 122.563 -68.956 31.477 1.00 17.00 ? 144 GLN   A NE2 1 
ATOM   379  N  N   . LEU   A 1 54  ? 126.100 -65.544 35.999 1.00 7.24  ? 145 LEU   A N   1 
ATOM   380  C  CA  . LEU   A 1 54  ? 127.105 -65.627 37.051 1.00 6.75  ? 145 LEU   A CA  1 
ATOM   381  C  C   . LEU   A 1 54  ? 127.045 -67.027 37.642 1.00 8.32  ? 145 LEU   A C   1 
ATOM   382  O  O   . LEU   A 1 54  ? 125.985 -67.453 38.113 1.00 8.92  ? 145 LEU   A O   1 
ATOM   383  C  CB  . LEU   A 1 54  ? 126.843 -64.579 38.134 1.00 6.99  ? 145 LEU   A CB  1 
ATOM   384  C  CG  . LEU   A 1 54  ? 126.665 -63.156 37.607 1.00 9.91  ? 145 LEU   A CG  1 
ATOM   385  C  CD1 . LEU   A 1 54  ? 126.320 -62.255 38.798 1.00 11.52 ? 145 LEU   A CD1 1 
ATOM   386  C  CD2 . LEU   A 1 54  ? 127.935 -62.683 36.890 1.00 10.01 ? 145 LEU   A CD2 1 
ATOM   387  N  N   . TRP   A 1 55  ? 128.171 -67.743 37.598 1.00 9.00  ? 146 TRP   A N   1 
ATOM   388  C  CA  . TRP   A 1 55  ? 128.284 -69.094 38.127 1.00 9.30  ? 146 TRP   A CA  1 
ATOM   389  C  C   . TRP   A 1 55  ? 129.329 -69.130 39.233 1.00 9.45  ? 146 TRP   A C   1 
ATOM   390  O  O   . TRP   A 1 55  ? 130.392 -68.512 39.112 1.00 7.52  ? 146 TRP   A O   1 
ATOM   391  C  CB  . TRP   A 1 55  ? 128.684 -70.092 37.016 1.00 8.09  ? 146 TRP   A CB  1 
ATOM   392  C  CG  . TRP   A 1 55  ? 127.641 -70.265 35.977 1.00 7.64  ? 146 TRP   A CG  1 
ATOM   393  C  CD1 . TRP   A 1 55  ? 127.477 -69.518 34.846 1.00 12.06 ? 146 TRP   A CD1 1 
ATOM   394  C  CD2 . TRP   A 1 55  ? 126.589 -71.235 35.971 1.00 13.10 ? 146 TRP   A CD2 1 
ATOM   395  N  NE1 . TRP   A 1 55  ? 126.394 -69.970 34.132 1.00 9.83  ? 146 TRP   A NE1 1 
ATOM   396  C  CE2 . TRP   A 1 55  ? 125.835 -71.027 34.795 1.00 8.84  ? 146 TRP   A CE2 1 
ATOM   397  C  CE3 . TRP   A 1 55  ? 126.223 -72.274 36.830 1.00 8.44  ? 146 TRP   A CE3 1 
ATOM   398  C  CZ2 . TRP   A 1 55  ? 124.727 -71.811 34.467 1.00 8.49  ? 146 TRP   A CZ2 1 
ATOM   399  C  CZ3 . TRP   A 1 55  ? 125.114 -73.062 36.493 1.00 8.73  ? 146 TRP   A CZ3 1 
ATOM   400  C  CH2 . TRP   A 1 55  ? 124.381 -72.817 35.333 1.00 8.71  ? 146 TRP   A CH2 1 
ATOM   401  N  N   . VAL   A 1 56  ? 129.018 -69.840 40.323 1.00 10.99 ? 147 VAL   A N   1 
ATOM   402  C  CA  . VAL   A 1 56  ? 130.002 -70.153 41.356 1.00 11.63 ? 147 VAL   A CA  1 
ATOM   403  C  C   . VAL   A 1 56  ? 129.832 -71.614 41.739 1.00 13.56 ? 147 VAL   A C   1 
ATOM   404  O  O   . VAL   A 1 56  ? 128.755 -72.194 41.577 1.00 10.83 ? 147 VAL   A O   1 
ATOM   405  C  CB  . VAL   A 1 56  ? 129.878 -69.251 42.613 1.00 11.86 ? 147 VAL   A CB  1 
ATOM   406  C  CG1 . VAL   A 1 56  ? 130.398 -67.844 42.324 1.00 11.71 ? 147 VAL   A CG1 1 
ATOM   407  C  CG2 . VAL   A 1 56  ? 128.431 -69.212 43.134 1.00 8.68  ? 147 VAL   A CG2 1 
ATOM   408  N  N   . ASP   A 1 57  ? 130.923 -72.217 42.219 1.00 12.16 ? 148 ASP   A N   1 
ATOM   409  C  CA  . ASP   A 1 57  ? 130.869 -73.550 42.808 1.00 12.35 ? 148 ASP   A CA  1 
ATOM   410  C  C   . ASP   A 1 57  ? 130.336 -73.529 44.231 1.00 18.77 ? 148 ASP   A C   1 
ATOM   411  O  O   . ASP   A 1 57  ? 129.824 -74.546 44.702 1.00 15.51 ? 148 ASP   A O   1 
ATOM   412  C  CB  . ASP   A 1 57  ? 132.260 -74.194 42.814 1.00 13.48 ? 148 ASP   A CB  1 
ATOM   413  C  CG  . ASP   A 1 57  ? 132.798 -74.456 41.420 1.00 18.24 ? 148 ASP   A CG  1 
ATOM   414  O  OD1 . ASP   A 1 57  ? 132.001 -74.780 40.509 1.00 18.26 ? 148 ASP   A OD1 1 
ATOM   415  O  OD2 . ASP   A 1 57  ? 134.032 -74.356 41.246 1.00 15.44 ? 148 ASP   A OD2 1 
ATOM   416  N  N   . SER   A 1 58  ? 130.468 -72.411 44.939 1.00 14.18 ? 149 SER   A N   1 
ATOM   417  C  CA  . SER   A 1 58  ? 129.891 -72.310 46.274 1.00 17.07 ? 149 SER   A CA  1 
ATOM   418  C  C   . SER   A 1 58  ? 129.491 -70.865 46.524 1.00 14.51 ? 149 SER   A C   1 
ATOM   419  O  O   . SER   A 1 58  ? 130.135 -69.930 46.040 1.00 11.35 ? 149 SER   A O   1 
ATOM   420  C  CB  . SER   A 1 58  ? 130.838 -72.815 47.371 1.00 24.46 ? 149 SER   A CB  1 
ATOM   421  O  OG  . SER   A 1 58  ? 132.088 -72.168 47.334 1.00 28.62 ? 149 SER   A OG  1 
ATOM   422  N  N   . THR   A 1 59  ? 128.416 -70.705 47.272 1.00 12.93 ? 150 THR   A N   1 
ATOM   423  C  CA  . THR   A 1 59  ? 127.793 -69.409 47.495 1.00 11.28 ? 150 THR   A CA  1 
ATOM   424  C  C   . THR   A 1 59  ? 128.691 -68.458 48.277 1.00 14.45 ? 150 THR   A C   1 
ATOM   425  O  O   . THR   A 1 59  ? 129.123 -68.801 49.381 1.00 11.26 ? 150 THR   A O   1 
ATOM   426  C  CB  . THR   A 1 59  ? 126.494 -69.635 48.239 1.00 15.11 ? 150 THR   A CB  1 
ATOM   427  O  OG1 . THR   A 1 59  ? 125.628 -70.406 47.397 1.00 15.08 ? 150 THR   A OG1 1 
ATOM   428  C  CG2 . THR   A 1 59  ? 125.843 -68.307 48.607 1.00 12.27 ? 150 THR   A CG2 1 
ATOM   429  N  N   . PRO   A 1 60  ? 128.983 -67.270 47.762 1.00 12.94 ? 151 PRO   A N   1 
ATOM   430  C  CA  . PRO   A 1 60  ? 129.759 -66.295 48.529 1.00 10.24 ? 151 PRO   A CA  1 
ATOM   431  C  C   . PRO   A 1 60  ? 128.885 -65.583 49.549 1.00 11.96 ? 151 PRO   A C   1 
ATOM   432  O  O   . PRO   A 1 60  ? 127.660 -65.777 49.580 1.00 13.37 ? 151 PRO   A O   1 
ATOM   433  C  CB  . PRO   A 1 60  ? 130.269 -65.329 47.443 1.00 10.01 ? 151 PRO   A CB  1 
ATOM   434  C  CG  . PRO   A 1 60  ? 129.211 -65.383 46.388 1.00 10.52 ? 151 PRO   A CG  1 
ATOM   435  C  CD  . PRO   A 1 60  ? 128.732 -66.818 46.378 1.00 10.30 ? 151 PRO   A CD  1 
ATOM   436  N  N   . PRO   A 1 61  ? 129.480 -64.753 50.410 1.00 14.75 ? 152 PRO   A N   1 
ATOM   437  C  CA  . PRO   A 1 61  ? 128.712 -64.167 51.511 1.00 11.54 ? 152 PRO   A CA  1 
ATOM   438  C  C   . PRO   A 1 61  ? 127.674 -63.173 51.022 1.00 12.04 ? 152 PRO   A C   1 
ATOM   439  O  O   . PRO   A 1 61  ? 127.831 -62.558 49.953 1.00 12.25 ? 152 PRO   A O   1 
ATOM   440  C  CB  . PRO   A 1 61  ? 129.792 -63.462 52.353 1.00 13.17 ? 152 PRO   A CB  1 
ATOM   441  C  CG  . PRO   A 1 61  ? 131.014 -64.285 52.115 1.00 11.98 ? 152 PRO   A CG  1 
ATOM   442  C  CD  . PRO   A 1 61  ? 130.929 -64.675 50.657 1.00 11.14 ? 152 PRO   A CD  1 
ATOM   443  N  N   . PRO   A 1 62  ? 126.592 -62.982 51.776 1.00 14.51 ? 153 PRO   A N   1 
ATOM   444  C  CA  . PRO   A 1 62  ? 125.734 -61.809 51.569 1.00 12.54 ? 153 PRO   A CA  1 
ATOM   445  C  C   . PRO   A 1 62  ? 126.554 -60.529 51.636 1.00 13.12 ? 153 PRO   A C   1 
ATOM   446  O  O   . PRO   A 1 62  ? 127.424 -60.369 52.495 1.00 11.75 ? 153 PRO   A O   1 
ATOM   447  C  CB  . PRO   A 1 62  ? 124.736 -61.878 52.732 1.00 14.98 ? 153 PRO   A CB  1 
ATOM   448  C  CG  . PRO   A 1 62  ? 124.845 -63.264 53.293 1.00 18.31 ? 153 PRO   A CG  1 
ATOM   449  C  CD  . PRO   A 1 62  ? 126.230 -63.748 52.982 1.00 17.89 ? 153 PRO   A CD  1 
ATOM   450  N  N   . GLY   A 1 63  ? 126.243 -59.598 50.750 1.00 10.74 ? 154 GLY   A N   1 
ATOM   451  C  CA  . GLY   A 1 63  ? 127.024 -58.390 50.613 1.00 10.48 ? 154 GLY   A CA  1 
ATOM   452  C  C   . GLY   A 1 63  ? 128.061 -58.458 49.513 1.00 10.46 ? 154 GLY   A C   1 
ATOM   453  O  O   . GLY   A 1 63  ? 128.659 -57.427 49.181 1.00 9.50  ? 154 GLY   A O   1 
ATOM   454  N  N   . THR   A 1 64  ? 128.297 -59.644 48.954 1.00 10.61 ? 155 THR   A N   1 
ATOM   455  C  CA  . THR   A 1 64  ? 129.094 -59.763 47.740 1.00 8.91  ? 155 THR   A CA  1 
ATOM   456  C  C   . THR   A 1 64  ? 128.428 -58.977 46.620 1.00 10.75 ? 155 THR   A C   1 
ATOM   457  O  O   . THR   A 1 64  ? 127.196 -58.935 46.524 1.00 8.42  ? 155 THR   A O   1 
ATOM   458  C  CB  . THR   A 1 64  ? 129.234 -61.244 47.364 1.00 9.66  ? 155 THR   A CB  1 
ATOM   459  O  OG1 . THR   A 1 64  ? 129.837 -61.939 48.462 1.00 9.49  ? 155 THR   A OG1 1 
ATOM   460  C  CG2 . THR   A 1 64  ? 130.113 -61.422 46.137 1.00 8.34  ? 155 THR   A CG2 1 
ATOM   461  N  N   . ARG   A 1 65  ? 129.244 -58.345 45.771 1.00 8.65  ? 156 ARG   A N   1 
ATOM   462  C  CA  . ARG   A 1 65  ? 128.747 -57.537 44.665 1.00 7.47  ? 156 ARG   A CA  1 
ATOM   463  C  C   . ARG   A 1 65  ? 129.470 -57.929 43.376 1.00 8.59  ? 156 ARG   A C   1 
ATOM   464  O  O   . ARG   A 1 65  ? 130.501 -58.609 43.394 1.00 7.89  ? 156 ARG   A O   1 
ATOM   465  C  CB  . ARG   A 1 65  ? 128.926 -56.038 44.936 1.00 9.06  ? 156 ARG   A CB  1 
ATOM   466  C  CG  . ARG   A 1 65  ? 128.245 -55.521 46.213 1.00 9.37  ? 156 ARG   A CG  1 
ATOM   467  C  CD  . ARG   A 1 65  ? 127.893 -54.036 46.074 1.00 10.26 ? 156 ARG   A CD  1 
ATOM   468  N  NE  . ARG   A 1 65  ? 129.084 -53.184 46.056 1.00 8.83  ? 156 ARG   A NE  1 
ATOM   469  C  CZ  . ARG   A 1 65  ? 129.054 -51.862 45.943 1.00 10.46 ? 156 ARG   A CZ  1 
ATOM   470  N  NH1 . ARG   A 1 65  ? 127.894 -51.233 45.823 1.00 10.03 ? 156 ARG   A NH1 1 
ATOM   471  N  NH2 . ARG   A 1 65  ? 130.184 -51.169 45.945 1.00 8.63  ? 156 ARG   A NH2 1 
ATOM   472  N  N   . VAL   A 1 66  ? 128.920 -57.491 42.243 1.00 8.65  ? 157 VAL   A N   1 
ATOM   473  C  CA  A VAL   A 1 66  ? 129.482 -57.798 40.934 0.35 8.49  ? 157 VAL   A CA  1 
ATOM   474  C  CA  B VAL   A 1 66  ? 129.454 -57.807 40.919 0.65 8.43  ? 157 VAL   A CA  1 
ATOM   475  C  C   . VAL   A 1 66  ? 129.596 -56.502 40.147 1.00 8.30  ? 157 VAL   A C   1 
ATOM   476  O  O   . VAL   A 1 66  ? 128.601 -55.792 39.953 1.00 7.55  ? 157 VAL   A O   1 
ATOM   477  C  CB  A VAL   A 1 66  ? 128.640 -58.829 40.171 0.35 8.82  ? 157 VAL   A CB  1 
ATOM   478  C  CB  B VAL   A 1 66  ? 128.552 -58.787 40.147 0.65 8.75  ? 157 VAL   A CB  1 
ATOM   479  C  CG1 A VAL   A 1 66  ? 127.190 -58.541 40.379 0.35 8.71  ? 157 VAL   A CG1 1 
ATOM   480  C  CG1 B VAL   A 1 66  ? 129.145 -59.104 38.769 0.65 6.01  ? 157 VAL   A CG1 1 
ATOM   481  C  CG2 A VAL   A 1 66  ? 128.989 -58.816 38.684 0.35 8.76  ? 157 VAL   A CG2 1 
ATOM   482  C  CG2 B VAL   A 1 66  ? 128.339 -60.073 40.937 0.65 10.24 ? 157 VAL   A CG2 1 
ATOM   483  N  N   . ARG   A 1 67  ? 130.812 -56.200 39.693 1.00 6.59  ? 158 ARG   A N   1 
ATOM   484  C  CA  . ARG   A 1 67  ? 131.127 -54.958 38.993 1.00 5.87  ? 158 ARG   A CA  1 
ATOM   485  C  C   . ARG   A 1 67  ? 131.466 -55.234 37.534 1.00 7.66  ? 158 ARG   A C   1 
ATOM   486  O  O   . ARG   A 1 67  ? 132.127 -56.231 37.222 1.00 7.38  ? 158 ARG   A O   1 
ATOM   487  C  CB  . ARG   A 1 67  ? 132.307 -54.256 39.662 1.00 6.03  ? 158 ARG   A CB  1 
ATOM   488  C  CG  . ARG   A 1 67  ? 132.659 -52.857 39.108 1.00 5.98  ? 158 ARG   A CG  1 
ATOM   489  C  CD  . ARG   A 1 67  ? 133.855 -52.266 39.866 1.00 7.23  ? 158 ARG   A CD  1 
ATOM   490  N  NE  . ARG   A 1 67  ? 133.570 -52.226 41.305 1.00 7.74  ? 158 ARG   A NE  1 
ATOM   491  C  CZ  . ARG   A 1 67  ? 132.912 -51.239 41.898 1.00 12.28 ? 158 ARG   A CZ  1 
ATOM   492  N  NH1 . ARG   A 1 67  ? 132.513 -50.186 41.188 1.00 10.91 ? 158 ARG   A NH1 1 
ATOM   493  N  NH2 . ARG   A 1 67  ? 132.644 -51.297 43.198 1.00 10.03 ? 158 ARG   A NH2 1 
ATOM   494  N  N   . ALA   A 1 68  ? 131.024 -54.341 36.645 1.00 5.59  ? 159 ALA   A N   1 
ATOM   495  C  CA  . ALA   A 1 68  ? 131.393 -54.378 35.235 1.00 5.52  ? 159 ALA   A CA  1 
ATOM   496  C  C   . ALA   A 1 68  ? 132.171 -53.118 34.872 1.00 7.50  ? 159 ALA   A C   1 
ATOM   497  O  O   . ALA   A 1 68  ? 131.808 -52.012 35.280 1.00 6.83  ? 159 ALA   A O   1 
ATOM   498  C  CB  . ALA   A 1 68  ? 130.162 -54.489 34.325 1.00 5.85  ? 159 ALA   A CB  1 
ATOM   499  N  N   . MET   A 1 69  ? 133.232 -53.287 34.094 1.00 6.69  ? 160 MET   A N   1 
ATOM   500  C  CA  . MET   A 1 69  ? 134.026 -52.162 33.608 1.00 8.35  ? 160 MET   A CA  1 
ATOM   501  C  C   . MET   A 1 69  ? 134.519 -52.501 32.208 1.00 8.37  ? 160 MET   A C   1 
ATOM   502  O  O   . MET   A 1 69  ? 134.904 -53.641 31.952 1.00 8.00  ? 160 MET   A O   1 
ATOM   503  C  CB  . MET   A 1 69  ? 135.210 -51.888 34.549 1.00 7.42  ? 160 MET   A CB  1 
ATOM   504  C  CG  . MET   A 1 69  ? 136.189 -50.818 34.066 1.00 11.06 ? 160 MET   A CG  1 
ATOM   505  S  SD  . MET   A 1 69  ? 137.642 -50.711 35.148 1.00 13.12 ? 160 MET   A SD  1 
ATOM   506  C  CE  . MET   A 1 69  ? 136.893 -50.167 36.699 1.00 13.36 ? 160 MET   A CE  1 
ATOM   507  N  N   . ALA   A 1 70  ? 134.517 -51.516 31.314 1.00 7.15  ? 161 ALA   A N   1 
ATOM   508  C  CA  . ALA   A 1 70  ? 135.053 -51.684 29.971 1.00 7.83  ? 161 ALA   A CA  1 
ATOM   509  C  C   . ALA   A 1 70  ? 136.488 -51.165 29.897 1.00 7.66  ? 161 ALA   A C   1 
ATOM   510  O  O   . ALA   A 1 70  ? 136.817 -50.125 30.487 1.00 9.76  ? 161 ALA   A O   1 
ATOM   511  C  CB  . ALA   A 1 70  ? 134.175 -50.943 28.948 1.00 8.58  ? 161 ALA   A CB  1 
ATOM   512  N  N   . ILE   A 1 71  ? 137.344 -51.888 29.164 1.00 6.81  ? 162 ILE   A N   1 
ATOM   513  C  CA  . ILE   A 1 71  ? 138.677 -51.406 28.813 1.00 7.23  ? 162 ILE   A CA  1 
ATOM   514  C  C   . ILE   A 1 71  ? 138.928 -51.684 27.334 1.00 7.92  ? 162 ILE   A C   1 
ATOM   515  O  O   . ILE   A 1 71  ? 138.411 -52.655 26.771 1.00 8.98  ? 162 ILE   A O   1 
ATOM   516  C  CB  . ILE   A 1 71  ? 139.799 -52.040 29.674 1.00 11.14 ? 162 ILE   A CB  1 
ATOM   517  C  CG1 . ILE   A 1 71  ? 139.944 -53.524 29.379 1.00 17.28 ? 162 ILE   A CG1 1 
ATOM   518  C  CG2 . ILE   A 1 71  ? 139.530 -51.838 31.177 1.00 20.22 ? 162 ILE   A CG2 1 
ATOM   519  C  CD1 . ILE   A 1 71  ? 141.237 -54.111 29.929 1.00 24.17 ? 162 ILE   A CD1 1 
ATOM   520  N  N   . TYR   A 1 72  ? 139.736 -50.832 26.702 1.00 9.13  ? 163 TYR   A N   1 
ATOM   521  C  CA  . TYR   A 1 72  ? 140.139 -51.103 25.327 1.00 9.69  ? 163 TYR   A CA  1 
ATOM   522  C  C   . TYR   A 1 72  ? 141.069 -52.307 25.292 1.00 8.89  ? 163 TYR   A C   1 
ATOM   523  O  O   . TYR   A 1 72  ? 141.946 -52.462 26.146 1.00 9.65  ? 163 TYR   A O   1 
ATOM   524  C  CB  . TYR   A 1 72  ? 140.811 -49.888 24.684 1.00 9.10  ? 163 TYR   A CB  1 
ATOM   525  C  CG  . TYR   A 1 72  ? 139.815 -48.796 24.394 1.00 9.14  ? 163 TYR   A CG  1 
ATOM   526  C  CD1 . TYR   A 1 72  ? 138.826 -48.986 23.424 1.00 9.03  ? 163 TYR   A CD1 1 
ATOM   527  C  CD2 . TYR   A 1 72  ? 139.842 -47.591 25.096 1.00 8.84  ? 163 TYR   A CD2 1 
ATOM   528  C  CE1 . TYR   A 1 72  ? 137.884 -48.016 23.157 1.00 9.00  ? 163 TYR   A CE1 1 
ATOM   529  C  CE2 . TYR   A 1 72  ? 138.884 -46.591 24.840 1.00 8.78  ? 163 TYR   A CE2 1 
ATOM   530  C  CZ  . TYR   A 1 72  ? 137.911 -46.824 23.863 1.00 8.87  ? 163 TYR   A CZ  1 
ATOM   531  O  OH  . TYR   A 1 72  ? 136.942 -45.885 23.576 1.00 11.83 ? 163 TYR   A OH  1 
ATOM   532  N  N   . LYS   A 1 73  ? 140.856 -53.169 24.294 1.00 11.73 ? 164 LYS   A N   1 
ATOM   533  C  CA  . LYS   A 1 73  ? 141.591 -54.428 24.190 1.00 12.56 ? 164 LYS   A CA  1 
ATOM   534  C  C   . LYS   A 1 73  ? 143.020 -54.225 23.690 1.00 16.37 ? 164 LYS   A C   1 
ATOM   535  O  O   . LYS   A 1 73  ? 143.938 -54.934 24.121 1.00 15.00 ? 164 LYS   A O   1 
ATOM   536  C  CB  . LYS   A 1 73  ? 140.833 -55.383 23.263 1.00 14.18 ? 164 LYS   A CB  1 
ATOM   537  C  CG  . LYS   A 1 73  ? 141.566 -56.687 22.976 1.00 20.13 ? 164 LYS   A CG  1 
ATOM   538  C  CD  . LYS   A 1 73  ? 140.850 -57.481 21.903 1.00 26.00 ? 164 LYS   A CD  1 
ATOM   539  C  CE  . LYS   A 1 73  ? 141.580 -58.780 21.584 1.00 28.92 ? 164 LYS   A CE  1 
ATOM   540  N  NZ  . LYS   A 1 73  ? 140.844 -59.504 20.522 1.00 29.74 ? 164 LYS   A NZ  1 
ATOM   541  N  N   . GLN   A 1 74  ? 143.234 -53.278 22.779 1.00 14.06 ? 165 GLN   A N   1 
ATOM   542  C  CA  . GLN   A 1 74  ? 144.550 -53.108 22.177 1.00 12.89 ? 165 GLN   A CA  1 
ATOM   543  C  C   . GLN   A 1 74  ? 145.504 -52.376 23.108 1.00 15.64 ? 165 GLN   A C   1 
ATOM   544  O  O   . GLN   A 1 74  ? 145.122 -51.430 23.802 1.00 16.27 ? 165 GLN   A O   1 
ATOM   545  C  CB  . GLN   A 1 74  ? 144.458 -52.339 20.865 1.00 14.20 ? 165 GLN   A CB  1 
ATOM   546  C  CG  . GLN   A 1 74  ? 143.730 -53.073 19.758 1.00 18.53 ? 165 GLN   A CG  1 
ATOM   547  C  CD  . GLN   A 1 74  ? 143.246 -52.099 18.713 1.00 21.51 ? 165 GLN   A CD  1 
ATOM   548  O  OE1 . GLN   A 1 74  ? 142.410 -51.248 18.995 1.00 21.89 ? 165 GLN   A OE1 1 
ATOM   549  N  NE2 . GLN   A 1 74  ? 143.803 -52.186 17.513 1.00 27.23 ? 165 GLN   A NE2 1 
ATOM   550  N  N   . SER   A 1 75  ? 146.770 -52.797 23.065 1.00 14.89 ? 166 SER   A N   1 
ATOM   551  C  CA  . SER   A 1 75  ? 147.800 -52.275 23.963 1.00 16.95 ? 166 SER   A CA  1 
ATOM   552  C  C   . SER   A 1 75  ? 147.862 -50.748 23.962 1.00 18.42 ? 166 SER   A C   1 
ATOM   553  O  O   . SER   A 1 75  ? 147.962 -50.114 25.022 1.00 14.72 ? 166 SER   A O   1 
ATOM   554  C  CB  . SER   A 1 75  ? 149.156 -52.859 23.560 1.00 20.94 ? 166 SER   A CB  1 
ATOM   555  O  OG  . SER   A 1 75  ? 150.214 -52.206 24.239 1.00 24.18 ? 166 SER   A OG  1 
ATOM   556  N  N   . GLN   A 1 76  ? 147.824 -50.135 22.779 1.00 14.67 ? 167 GLN   A N   1 
ATOM   557  C  CA  . GLN   A 1 76  ? 148.032 -48.694 22.717 1.00 14.96 ? 167 GLN   A CA  1 
ATOM   558  C  C   . GLN   A 1 76  ? 146.830 -47.897 23.194 1.00 14.64 ? 167 GLN   A C   1 
ATOM   559  O  O   . GLN   A 1 76  ? 146.934 -46.671 23.318 1.00 16.36 ? 167 GLN   A O   1 
ATOM   560  C  CB  . GLN   A 1 76  ? 148.394 -48.257 21.294 1.00 16.44 ? 167 GLN   A CB  1 
ATOM   561  C  CG  . GLN   A 1 76  ? 147.270 -48.409 20.266 1.00 20.30 ? 167 GLN   A CG  1 
ATOM   562  C  CD  . GLN   A 1 76  ? 147.303 -49.746 19.544 1.00 24.66 ? 167 GLN   A CD  1 
ATOM   563  O  OE1 . GLN   A 1 76  ? 147.566 -50.788 20.147 1.00 24.24 ? 167 GLN   A OE1 1 
ATOM   564  N  NE2 . GLN   A 1 76  ? 147.038 -49.721 18.239 1.00 19.17 ? 167 GLN   A NE2 1 
ATOM   565  N  N   . HIS   A 1 77  ? 145.700 -48.552 23.461 1.00 13.26 ? 168 HIS   A N   1 
ATOM   566  C  CA  . HIS   A 1 77  ? 144.500 -47.859 23.906 1.00 15.26 ? 168 HIS   A CA  1 
ATOM   567  C  C   . HIS   A 1 77  ? 144.061 -48.228 25.310 1.00 12.89 ? 168 HIS   A C   1 
ATOM   568  O  O   . HIS   A 1 77  ? 143.163 -47.567 25.850 1.00 9.81  ? 168 HIS   A O   1 
ATOM   569  C  CB  . HIS   A 1 77  ? 143.339 -48.133 22.938 1.00 14.56 ? 168 HIS   A CB  1 
ATOM   570  C  CG  . HIS   A 1 77  ? 143.617 -47.686 21.535 1.00 15.75 ? 168 HIS   A CG  1 
ATOM   571  N  ND1 . HIS   A 1 77  ? 143.977 -46.393 21.229 1.00 17.33 ? 168 HIS   A ND1 1 
ATOM   572  C  CD2 . HIS   A 1 77  ? 143.591 -48.359 20.361 1.00 16.34 ? 168 HIS   A CD2 1 
ATOM   573  C  CE1 . HIS   A 1 77  ? 144.158 -46.285 19.925 1.00 21.29 ? 168 HIS   A CE1 1 
ATOM   574  N  NE2 . HIS   A 1 77  ? 143.931 -47.465 19.376 1.00 18.39 ? 168 HIS   A NE2 1 
ATOM   575  N  N   . MET   A 1 78  ? 144.684 -49.232 25.927 1.00 10.35 ? 169 MET   A N   1 
ATOM   576  C  CA  A MET   A 1 78  ? 144.168 -49.745 27.190 0.61 13.52 ? 169 MET   A CA  1 
ATOM   577  C  CA  B MET   A 1 78  ? 144.172 -49.748 27.191 0.39 13.44 ? 169 MET   A CA  1 
ATOM   578  C  C   . MET   A 1 78  ? 144.212 -48.699 28.298 1.00 11.94 ? 169 MET   A C   1 
ATOM   579  O  O   . MET   A 1 78  ? 143.418 -48.771 29.236 1.00 10.77 ? 169 MET   A O   1 
ATOM   580  C  CB  A MET   A 1 78  ? 144.936 -51.001 27.605 0.61 13.65 ? 169 MET   A CB  1 
ATOM   581  C  CB  B MET   A 1 78  ? 144.949 -51.003 27.600 0.39 14.45 ? 169 MET   A CB  1 
ATOM   582  C  CG  A MET   A 1 78  ? 146.440 -50.843 27.674 0.61 20.10 ? 169 MET   A CG  1 
ATOM   583  C  CG  B MET   A 1 78  ? 146.118 -50.767 28.542 0.39 21.11 ? 169 MET   A CG  1 
ATOM   584  S  SD  A MET   A 1 78  ? 147.227 -52.412 28.117 0.61 27.87 ? 169 MET   A SD  1 
ATOM   585  S  SD  B MET   A 1 78  ? 145.649 -50.742 30.288 0.39 22.40 ? 169 MET   A SD  1 
ATOM   586  C  CE  A MET   A 1 78  ? 148.952 -52.006 27.850 0.61 15.11 ? 169 MET   A CE  1 
ATOM   587  C  CE  B MET   A 1 78  ? 144.983 -52.394 30.504 0.39 22.77 ? 169 MET   A CE  1 
ATOM   588  N  N   . THR   A 1 79  ? 145.127 -47.724 28.224 1.00 13.15 ? 170 THR   A N   1 
ATOM   589  C  CA  . THR   A 1 79  ? 145.153 -46.726 29.294 1.00 12.12 ? 170 THR   A CA  1 
ATOM   590  C  C   . THR   A 1 79  ? 144.113 -45.622 29.107 1.00 15.35 ? 170 THR   A C   1 
ATOM   591  O  O   . THR   A 1 79  ? 143.952 -44.784 30.002 1.00 14.10 ? 170 THR   A O   1 
ATOM   592  C  CB  . THR   A 1 79  ? 146.548 -46.099 29.451 1.00 14.62 ? 170 THR   A CB  1 
ATOM   593  O  OG1 . THR   A 1 79  ? 146.950 -45.441 28.244 1.00 13.14 ? 170 THR   A OG1 1 
ATOM   594  C  CG2 . THR   A 1 79  ? 147.594 -47.154 29.818 1.00 16.14 ? 170 THR   A CG2 1 
ATOM   595  N  N   . GLU   A 1 80  ? 143.398 -45.602 27.986 1.00 11.26 ? 171 GLU   A N   1 
ATOM   596  C  CA  . GLU   A 1 80  ? 142.352 -44.609 27.760 1.00 13.86 ? 171 GLU   A CA  1 
ATOM   597  C  C   . GLU   A 1 80  ? 141.045 -45.063 28.396 1.00 12.88 ? 171 GLU   A C   1 
ATOM   598  O  O   . GLU   A 1 80  ? 140.603 -46.193 28.172 1.00 13.85 ? 171 GLU   A O   1 
ATOM   599  C  CB  . GLU   A 1 80  ? 142.137 -44.384 26.264 1.00 11.92 ? 171 GLU   A CB  1 
ATOM   600  C  CG  . GLU   A 1 80  ? 141.159 -43.250 25.936 1.00 17.43 ? 171 GLU   A CG  1 
ATOM   601  C  CD  . GLU   A 1 80  ? 140.981 -43.036 24.438 1.00 21.48 ? 171 GLU   A CD  1 
ATOM   602  O  OE1 . GLU   A 1 80  ? 139.859 -42.687 24.011 1.00 23.36 ? 171 GLU   A OE1 1 
ATOM   603  O  OE2 . GLU   A 1 80  ? 141.966 -43.214 23.689 1.00 21.40 ? 171 GLU   A OE2 1 
ATOM   604  N  N   . VAL   A 1 81  ? 140.404 -44.170 29.158 1.00 8.41  ? 172 VAL   A N   1 
ATOM   605  C  CA  . VAL   A 1 81  ? 139.085 -44.484 29.706 1.00 7.87  ? 172 VAL   A CA  1 
ATOM   606  C  C   . VAL   A 1 81  ? 138.104 -44.751 28.574 1.00 9.60  ? 172 VAL   A C   1 
ATOM   607  O  O   . VAL   A 1 81  ? 137.987 -43.960 27.629 1.00 8.39  ? 172 VAL   A O   1 
ATOM   608  C  CB  . VAL   A 1 81  ? 138.586 -43.342 30.606 1.00 7.80  ? 172 VAL   A CB  1 
ATOM   609  C  CG1 . VAL   A 1 81  ? 137.144 -43.592 31.051 1.00 7.38  ? 172 VAL   A CG1 1 
ATOM   610  C  CG2 . VAL   A 1 81  ? 139.522 -43.162 31.809 1.00 17.96 ? 172 VAL   A CG2 1 
ATOM   611  N  N   . VAL   A 1 82  ? 137.400 -45.876 28.658 1.00 7.46  ? 173 VAL   A N   1 
ATOM   612  C  CA  . VAL   A 1 82  ? 136.302 -46.160 27.739 1.00 7.48  ? 173 VAL   A CA  1 
ATOM   613  C  C   . VAL   A 1 82  ? 135.095 -45.345 28.183 1.00 7.26  ? 173 VAL   A C   1 
ATOM   614  O  O   . VAL   A 1 82  ? 134.644 -45.469 29.326 1.00 7.95  ? 173 VAL   A O   1 
ATOM   615  C  CB  . VAL   A 1 82  ? 135.960 -47.657 27.714 1.00 7.52  ? 173 VAL   A CB  1 
ATOM   616  C  CG1 . VAL   A 1 82  ? 134.755 -47.890 26.805 1.00 9.48  ? 173 VAL   A CG1 1 
ATOM   617  C  CG2 . VAL   A 1 82  ? 137.139 -48.460 27.226 1.00 7.43  ? 173 VAL   A CG2 1 
ATOM   618  N  N   . ARG   A 1 83  ? 134.562 -44.525 27.278 1.00 7.84  ? 174 ARG   A N   1 
ATOM   619  C  CA  . ARG   A 1 83  ? 133.430 -43.666 27.599 1.00 12.71 ? 174 ARG   A CA  1 
ATOM   620  C  C   . ARG   A 1 83  ? 132.517 -43.535 26.391 1.00 14.09 ? 174 ARG   A C   1 
ATOM   621  O  O   . ARG   A 1 83  ? 132.885 -43.872 25.260 1.00 10.30 ? 174 ARG   A O   1 
ATOM   622  C  CB  . ARG   A 1 83  ? 133.894 -42.268 28.035 1.00 11.23 ? 174 ARG   A CB  1 
ATOM   623  C  CG  . ARG   A 1 83  ? 134.724 -41.559 26.974 1.00 8.26  ? 174 ARG   A CG  1 
ATOM   624  C  CD  . ARG   A 1 83  ? 135.027 -40.102 27.348 1.00 12.92 ? 174 ARG   A CD  1 
ATOM   625  N  NE  . ARG   A 1 83  ? 135.803 -39.991 28.579 1.00 15.09 ? 174 ARG   A NE  1 
ATOM   626  C  CZ  . ARG   A 1 83  ? 135.298 -39.719 29.781 1.00 15.27 ? 174 ARG   A CZ  1 
ATOM   627  N  NH1 . ARG   A 1 83  ? 136.105 -39.665 30.824 1.00 12.79 ? 174 ARG   A NH1 1 
ATOM   628  N  NH2 . ARG   A 1 83  ? 133.991 -39.531 29.950 1.00 8.04  ? 174 ARG   A NH2 1 
ATOM   629  N  N   . ARG   A 1 84  ? 131.320 -43.001 26.633 1.00 7.92  ? 175 ARG   A N   1 
ATOM   630  C  CA  . ARG   A 1 84  ? 130.414 -42.741 25.530 1.00 8.80  ? 175 ARG   A CA  1 
ATOM   631  C  C   . ARG   A 1 84  ? 130.908 -41.572 24.692 1.00 13.63 ? 175 ARG   A C   1 
ATOM   632  O  O   . ARG   A 1 84  ? 131.606 -40.682 25.186 1.00 8.92  ? 175 ARG   A O   1 
ATOM   633  C  CB  . ARG   A 1 84  ? 129.005 -42.459 26.041 1.00 8.39  ? 175 ARG   A CB  1 
ATOM   634  C  CG  . ARG   A 1 84  ? 128.321 -43.702 26.579 1.00 8.03  ? 175 ARG   A CG  1 
ATOM   635  C  CD  . ARG   A 1 84  ? 126.924 -43.323 27.037 1.00 10.46 ? 175 ARG   A CD  1 
ATOM   636  N  NE  . ARG   A 1 84  ? 125.910 -43.446 25.995 1.00 8.70  ? 175 ARG   A NE  1 
ATOM   637  C  CZ  . ARG   A 1 84  ? 124.685 -42.955 26.118 1.00 13.02 ? 175 ARG   A CZ  1 
ATOM   638  N  NH1 . ARG   A 1 84  ? 124.372 -42.257 27.208 1.00 9.53  ? 175 ARG   A NH1 1 
ATOM   639  N  NH2 . ARG   A 1 84  ? 123.777 -43.152 25.162 1.00 9.62  ? 175 ARG   A NH2 1 
ATOM   640  N  N   . CYS   A 1 85  ? 130.517 -41.582 23.410 1.00 9.41  ? 176 CYS   A N   1 
ATOM   641  C  CA  . CYS   A 1 85  ? 130.993 -40.637 22.414 1.00 10.05 ? 176 CYS   A CA  1 
ATOM   642  C  C   . CYS   A 1 85  ? 130.375 -39.253 22.637 1.00 12.32 ? 176 CYS   A C   1 
ATOM   643  O  O   . CYS   A 1 85  ? 129.426 -39.097 23.413 1.00 13.46 ? 176 CYS   A O   1 
ATOM   644  C  CB  . CYS   A 1 85  ? 130.654 -41.165 21.012 1.00 10.59 ? 176 CYS   A CB  1 
ATOM   645  S  SG  . CYS   A 1 85  ? 128.874 -41.022 20.590 1.00 12.28 ? 176 CYS   A SG  1 
ATOM   646  N  N   . PRO   A 1 86  ? 130.897 -38.220 21.962 1.00 12.79 ? 177 PRO   A N   1 
ATOM   647  C  CA  . PRO   A 1 86  ? 130.349 -36.867 22.168 1.00 17.60 ? 177 PRO   A CA  1 
ATOM   648  C  C   . PRO   A 1 86  ? 128.878 -36.762 21.846 1.00 22.20 ? 177 PRO   A C   1 
ATOM   649  O  O   . PRO   A 1 86  ? 128.178 -35.953 22.464 1.00 26.37 ? 177 PRO   A O   1 
ATOM   650  C  CB  . PRO   A 1 86  ? 131.190 -35.994 21.225 1.00 18.56 ? 177 PRO   A CB  1 
ATOM   651  C  CG  . PRO   A 1 86  ? 132.468 -36.737 21.046 1.00 14.31 ? 177 PRO   A CG  1 
ATOM   652  C  CD  . PRO   A 1 86  ? 132.103 -38.208 21.118 1.00 13.42 ? 177 PRO   A CD  1 
ATOM   653  N  N   . HIS   A 1 87  ? 128.370 -37.563 20.907 1.00 16.81 ? 178 HIS   A N   1 
ATOM   654  C  CA  . HIS   A 1 87  ? 126.945 -37.500 20.620 1.00 13.82 ? 178 HIS   A CA  1 
ATOM   655  C  C   . HIS   A 1 87  ? 126.131 -38.143 21.735 1.00 14.17 ? 178 HIS   A C   1 
ATOM   656  O  O   . HIS   A 1 87  ? 125.150 -37.560 22.216 1.00 15.79 ? 178 HIS   A O   1 
ATOM   657  C  CB  . HIS   A 1 87  ? 126.619 -38.173 19.285 1.00 18.44 ? 178 HIS   A CB  1 
ATOM   658  C  CG  . HIS   A 1 87  ? 125.156 -38.407 19.095 1.00 14.62 ? 178 HIS   A CG  1 
ATOM   659  N  ND1 . HIS   A 1 87  ? 124.264 -37.383 18.857 1.00 17.43 ? 178 HIS   A ND1 1 
ATOM   660  C  CD2 . HIS   A 1 87  ? 124.417 -39.539 19.168 1.00 17.10 ? 178 HIS   A CD2 1 
ATOM   661  C  CE1 . HIS   A 1 87  ? 123.043 -37.879 18.763 1.00 17.37 ? 178 HIS   A CE1 1 
ATOM   662  N  NE2 . HIS   A 1 87  ? 123.107 -39.183 18.964 1.00 16.19 ? 178 HIS   A NE2 1 
ATOM   663  N  N   . HIS   A 1 88  ? 126.496 -39.357 22.145 1.00 12.28 ? 179 HIS   A N   1 
ATOM   664  C  CA  . HIS   A 1 88  ? 125.600 -40.074 23.046 1.00 12.35 ? 179 HIS   A CA  1 
ATOM   665  C  C   . HIS   A 1 88  ? 125.682 -39.548 24.472 1.00 14.85 ? 179 HIS   A C   1 
ATOM   666  O  O   . HIS   A 1 88  ? 124.684 -39.613 25.201 1.00 11.04 ? 179 HIS   A O   1 
ATOM   667  C  CB  . HIS   A 1 88  ? 125.877 -41.582 23.000 1.00 11.15 ? 179 HIS   A CB  1 
ATOM   668  C  CG  . HIS   A 1 88  ? 125.226 -42.263 21.834 1.00 11.65 ? 179 HIS   A CG  1 
ATOM   669  N  ND1 . HIS   A 1 88  ? 125.945 -42.827 20.803 1.00 11.97 ? 179 HIS   A ND1 1 
ATOM   670  C  CD2 . HIS   A 1 88  ? 123.920 -42.432 21.518 1.00 15.09 ? 179 HIS   A CD2 1 
ATOM   671  C  CE1 . HIS   A 1 88  ? 125.111 -43.331 19.910 1.00 15.51 ? 179 HIS   A CE1 1 
ATOM   672  N  NE2 . HIS   A 1 88  ? 123.876 -43.100 20.318 1.00 15.50 ? 179 HIS   A NE2 1 
ATOM   673  N  N   . GLU   A 1 89  ? 126.822 -38.975 24.878 1.00 12.57 ? 180 GLU   A N   1 
ATOM   674  C  CA  . GLU   A 1 89  ? 126.889 -38.443 26.238 1.00 15.22 ? 180 GLU   A CA  1 
ATOM   675  C  C   . GLU   A 1 89  ? 126.035 -37.196 26.394 1.00 11.35 ? 180 GLU   A C   1 
ATOM   676  O  O   . GLU   A 1 89  ? 125.694 -36.833 27.526 1.00 14.15 ? 180 GLU   A O   1 
ATOM   677  C  CB  . GLU   A 1 89  ? 128.341 -38.144 26.653 1.00 10.68 ? 180 GLU   A CB  1 
ATOM   678  C  CG  . GLU   A 1 89  ? 128.935 -36.909 25.985 1.00 11.44 ? 180 GLU   A CG  1 
ATOM   679  C  CD  . GLU   A 1 89  ? 130.241 -36.445 26.623 1.00 14.87 ? 180 GLU   A CD  1 
ATOM   680  O  OE1 . GLU   A 1 89  ? 130.800 -37.153 27.483 1.00 15.97 ? 180 GLU   A OE1 1 
ATOM   681  O  OE2 . GLU   A 1 89  ? 130.715 -35.359 26.250 1.00 18.03 ? 180 GLU   A OE2 1 
ATOM   682  N  N   . ARG   A 1 90  ? 125.653 -36.554 25.289 1.00 12.10 ? 181 ARG   A N   1 
ATOM   683  C  CA  . ARG   A 1 90  ? 124.828 -35.351 25.316 1.00 12.79 ? 181 ARG   A CA  1 
ATOM   684  C  C   . ARG   A 1 90  ? 123.373 -35.604 24.933 1.00 13.13 ? 181 ARG   A C   1 
ATOM   685  O  O   . ARG   A 1 90  ? 122.604 -34.640 24.819 1.00 14.05 ? 181 ARG   A O   1 
ATOM   686  C  CB  . ARG   A 1 90  ? 125.417 -34.288 24.383 1.00 13.59 ? 181 ARG   A CB  1 
ATOM   687  C  CG  . ARG   A 1 90  ? 126.819 -33.854 24.759 1.00 13.48 ? 181 ARG   A CG  1 
ATOM   688  C  CD  . ARG   A 1 90  ? 127.351 -32.792 23.791 1.00 14.42 ? 181 ARG   A CD  1 
ATOM   689  N  NE  . ARG   A 1 90  ? 126.597 -31.548 23.847 1.00 15.16 ? 181 ARG   A NE  1 
ATOM   690  C  CZ  . ARG   A 1 90  ? 125.967 -30.997 22.811 1.00 16.02 ? 181 ARG   A CZ  1 
ATOM   691  N  NH1 . ARG   A 1 90  ? 125.976 -31.591 21.620 1.00 16.28 ? 181 ARG   A NH1 1 
ATOM   692  N  NH2 . ARG   A 1 90  ? 125.326 -29.838 22.963 1.00 16.74 ? 181 ARG   A NH2 1 
ATOM   693  N  N   . CYS   A 1 91  ? 122.963 -36.859 24.741 1.00 12.74 ? 182 CYS   A N   1 
ATOM   694  C  CA  A CYS   A 1 91  ? 121.609 -37.079 24.244 0.75 18.33 ? 182 CYS   A CA  1 
ATOM   695  C  CA  B CYS   A 1 91  ? 121.627 -37.212 24.267 0.25 18.70 ? 182 CYS   A CA  1 
ATOM   696  C  C   . CYS   A 1 91  ? 120.564 -37.189 25.355 1.00 19.51 ? 182 CYS   A C   1 
ATOM   697  O  O   . CYS   A 1 91  ? 119.391 -37.431 25.050 1.00 17.32 ? 182 CYS   A O   1 
ATOM   698  C  CB  A CYS   A 1 91  ? 121.557 -38.309 23.330 0.75 18.75 ? 182 CYS   A CB  1 
ATOM   699  C  CB  B CYS   A 1 91  ? 121.636 -38.608 23.637 0.25 18.99 ? 182 CYS   A CB  1 
ATOM   700  S  SG  A CYS   A 1 91  ? 121.552 -39.900 24.158 0.75 17.77 ? 182 CYS   A SG  1 
ATOM   701  S  SG  B CYS   A 1 91  ? 122.292 -38.696 21.970 0.25 20.07 ? 182 CYS   A SG  1 
ATOM   702  N  N   . SER   A 1 92  ? 120.947 -36.966 26.616 1.00 18.60 ? 183 SER   A N   1 
ATOM   703  C  CA  A SER   A 1 92  ? 119.988 -36.843 27.719 0.64 18.43 ? 183 SER   A CA  1 
ATOM   704  C  CA  B SER   A 1 92  ? 119.998 -36.845 27.726 0.36 18.97 ? 183 SER   A CA  1 
ATOM   705  C  C   . SER   A 1 92  ? 119.110 -38.086 27.838 1.00 17.89 ? 183 SER   A C   1 
ATOM   706  O  O   . SER   A 1 92  ? 117.882 -38.001 27.874 1.00 21.03 ? 183 SER   A O   1 
ATOM   707  C  CB  A SER   A 1 92  ? 119.117 -35.591 27.553 0.64 23.09 ? 183 SER   A CB  1 
ATOM   708  C  CB  B SER   A 1 92  ? 119.156 -35.572 27.584 0.36 22.63 ? 183 SER   A CB  1 
ATOM   709  O  OG  A SER   A 1 92  ? 119.880 -34.405 27.600 0.64 22.51 ? 183 SER   A OG  1 
ATOM   710  O  OG  B SER   A 1 92  ? 118.272 -35.409 28.681 0.36 24.48 ? 183 SER   A OG  1 
ATOM   711  N  N   . ASP   A 1 93  ? 119.750 -39.259 27.892 1.00 14.35 ? 184 ASP   A N   1 
ATOM   712  C  CA  . ASP   A 1 93  ? 119.007 -40.509 27.977 1.00 12.46 ? 184 ASP   A CA  1 
ATOM   713  C  C   . ASP   A 1 93  ? 119.290 -41.278 29.266 1.00 12.16 ? 184 ASP   A C   1 
ATOM   714  O  O   . ASP   A 1 93  ? 119.066 -42.486 29.307 1.00 12.38 ? 184 ASP   A O   1 
ATOM   715  C  CB  . ASP   A 1 93  ? 119.287 -41.387 26.750 1.00 13.27 ? 184 ASP   A CB  1 
ATOM   716  C  CG  . ASP   A 1 93  ? 120.747 -41.839 26.652 1.00 16.81 ? 184 ASP   A CG  1 
ATOM   717  O  OD1 . ASP   A 1 93  ? 121.563 -41.522 27.541 1.00 14.25 ? 184 ASP   A OD1 1 
ATOM   718  O  OD2 . ASP   A 1 93  ? 121.080 -42.526 25.663 1.00 14.38 ? 184 ASP   A OD2 1 
ATOM   719  N  N   . SER   A 1 94  ? 119.767 -40.614 30.321 1.00 11.03 ? 185 SER   A N   1 
ATOM   720  C  CA  . SER   A 1 94  ? 120.008 -41.319 31.577 1.00 14.10 ? 185 SER   A CA  1 
ATOM   721  C  C   . SER   A 1 94  ? 118.701 -41.825 32.175 1.00 15.21 ? 185 SER   A C   1 
ATOM   722  O  O   . SER   A 1 94  ? 117.672 -41.149 32.116 1.00 13.69 ? 185 SER   A O   1 
ATOM   723  C  CB  . SER   A 1 94  ? 120.714 -40.418 32.592 1.00 16.31 ? 185 SER   A CB  1 
ATOM   724  O  OG  . SER   A 1 94  ? 120.887 -41.105 33.836 1.00 11.79 ? 185 SER   A OG  1 
ATOM   725  N  N   . ASP   A 1 95  ? 118.747 -43.023 32.751 1.00 13.27 ? 186 ASP   A N   1 
ATOM   726  C  CA  . ASP   A 1 95  ? 117.611 -43.569 33.480 1.00 15.82 ? 186 ASP   A CA  1 
ATOM   727  C  C   . ASP   A 1 95  ? 117.458 -42.968 34.872 1.00 18.77 ? 186 ASP   A C   1 
ATOM   728  O  O   . ASP   A 1 95  ? 116.536 -43.350 35.598 1.00 14.68 ? 186 ASP   A O   1 
ATOM   729  C  CB  . ASP   A 1 95  ? 117.735 -45.094 33.590 1.00 15.86 ? 186 ASP   A CB  1 
ATOM   730  C  CG  . ASP   A 1 95  ? 118.962 -45.545 34.404 1.00 18.71 ? 186 ASP   A CG  1 
ATOM   731  O  OD1 . ASP   A 1 95  ? 119.878 -44.730 34.703 1.00 12.33 ? 186 ASP   A OD1 1 
ATOM   732  O  OD2 . ASP   A 1 95  ? 118.994 -46.740 34.756 1.00 15.55 ? 186 ASP   A OD2 1 
ATOM   733  N  N   . GLY   A 1 96  ? 118.330 -42.044 35.262 1.00 17.76 ? 187 GLY   A N   1 
ATOM   734  C  CA  . GLY   A 1 96  ? 118.328 -41.497 36.595 1.00 20.75 ? 187 GLY   A CA  1 
ATOM   735  C  C   . GLY   A 1 96  ? 119.409 -42.052 37.497 1.00 20.01 ? 187 GLY   A C   1 
ATOM   736  O  O   . GLY   A 1 96  ? 119.707 -41.441 38.520 1.00 19.59 ? 187 GLY   A O   1 
ATOM   737  N  N   . LEU   A 1 97  ? 120.000 -43.194 37.148 1.00 14.55 ? 188 LEU   A N   1 
ATOM   738  C  CA  . LEU   A 1 97  ? 121.129 -43.744 37.887 1.00 11.84 ? 188 LEU   A CA  1 
ATOM   739  C  C   . LEU   A 1 97  ? 122.431 -43.628 37.112 1.00 11.33 ? 188 LEU   A C   1 
ATOM   740  O  O   . LEU   A 1 97  ? 123.453 -43.221 37.672 1.00 9.91  ? 188 LEU   A O   1 
ATOM   741  C  CB  . LEU   A 1 97  ? 120.877 -45.219 38.243 1.00 11.60 ? 188 LEU   A CB  1 
ATOM   742  C  CG  . LEU   A 1 97  ? 119.614 -45.527 39.049 1.00 16.58 ? 188 LEU   A CG  1 
ATOM   743  C  CD1 . LEU   A 1 97  ? 119.459 -47.030 39.221 1.00 17.16 ? 188 LEU   A CD1 1 
ATOM   744  C  CD2 . LEU   A 1 97  ? 119.671 -44.811 40.397 1.00 20.39 ? 188 LEU   A CD2 1 
ATOM   745  N  N   . ALA   A 1 98  ? 122.419 -43.968 35.832 1.00 10.54 ? 189 ALA   A N   1 
ATOM   746  C  CA  . ALA   A 1 98  ? 123.666 -43.987 35.076 1.00 11.56 ? 189 ALA   A CA  1 
ATOM   747  C  C   . ALA   A 1 98  ? 124.064 -42.571 34.671 1.00 12.57 ? 189 ALA   A C   1 
ATOM   748  O  O   . ALA   A 1 98  ? 123.244 -41.844 34.098 1.00 12.20 ? 189 ALA   A O   1 
ATOM   749  C  CB  . ALA   A 1 98  ? 123.517 -44.859 33.835 1.00 7.75  ? 189 ALA   A CB  1 
ATOM   750  N  N   . PRO   A 1 99  ? 125.303 -42.150 34.923 1.00 11.10 ? 190 PRO   A N   1 
ATOM   751  C  CA  . PRO   A 1 99  ? 125.766 -40.899 34.333 1.00 9.33  ? 190 PRO   A CA  1 
ATOM   752  C  C   . PRO   A 1 99  ? 125.763 -41.008 32.825 1.00 9.40  ? 190 PRO   A C   1 
ATOM   753  O  O   . PRO   A 1 99  ? 126.005 -42.094 32.261 1.00 10.36 ? 190 PRO   A O   1 
ATOM   754  C  CB  . PRO   A 1 99  ? 127.190 -40.749 34.891 1.00 12.26 ? 190 PRO   A CB  1 
ATOM   755  C  CG  . PRO   A 1 99  ? 127.208 -41.618 36.131 1.00 12.09 ? 190 PRO   A CG  1 
ATOM   756  C  CD  . PRO   A 1 99  ? 126.327 -42.778 35.777 1.00 7.78  ? 190 PRO   A CD  1 
ATOM   757  N  N   . PRO   A 1 100 ? 125.465 -39.913 32.118 1.00 10.00 ? 191 PRO   A N   1 
ATOM   758  C  CA  . PRO   A 1 100 ? 125.381 -39.986 30.649 1.00 11.09 ? 191 PRO   A CA  1 
ATOM   759  C  C   . PRO   A 1 100 ? 126.682 -40.399 29.968 1.00 11.80 ? 191 PRO   A C   1 
ATOM   760  O  O   . PRO   A 1 100 ? 126.639 -40.805 28.796 1.00 9.36  ? 191 PRO   A O   1 
ATOM   761  C  CB  . PRO   A 1 100 ? 124.971 -38.559 30.250 1.00 10.38 ? 191 PRO   A CB  1 
ATOM   762  C  CG  . PRO   A 1 100 ? 125.388 -37.701 31.390 1.00 10.53 ? 191 PRO   A CG  1 
ATOM   763  C  CD  . PRO   A 1 100 ? 125.125 -38.572 32.613 1.00 12.52 ? 191 PRO   A CD  1 
ATOM   764  N  N   . GLN   A 1 101 ? 127.835 -40.290 30.644 1.00 8.84  ? 192 GLN   A N   1 
ATOM   765  C  CA  . GLN   A 1 101 ? 129.107 -40.690 30.041 1.00 9.41  ? 192 GLN   A CA  1 
ATOM   766  C  C   . GLN   A 1 101 ? 129.345 -42.202 30.049 1.00 11.56 ? 192 GLN   A C   1 
ATOM   767  O  O   . GLN   A 1 101 ? 130.243 -42.679 29.335 1.00 8.30  ? 192 GLN   A O   1 
ATOM   768  C  CB  . GLN   A 1 101 ? 130.281 -40.017 30.765 1.00 8.92  ? 192 GLN   A CB  1 
ATOM   769  C  CG  . GLN   A 1 101 ? 130.242 -38.473 30.764 1.00 9.54  ? 192 GLN   A CG  1 
ATOM   770  C  CD  . GLN   A 1 101 ? 129.607 -37.906 32.018 1.00 9.58  ? 192 GLN   A CD  1 
ATOM   771  O  OE1 . GLN   A 1 101 ? 128.638 -38.456 32.534 1.00 9.46  ? 192 GLN   A OE1 1 
ATOM   772  N  NE2 . GLN   A 1 101 ? 130.161 -36.797 32.525 1.00 12.00 ? 192 GLN   A NE2 1 
ATOM   773  N  N   . HIS   A 1 102 ? 128.599 -42.958 30.856 1.00 9.28  ? 193 HIS   A N   1 
ATOM   774  C  CA  . HIS   A 1 102 ? 128.936 -44.357 31.106 1.00 11.49 ? 193 HIS   A CA  1 
ATOM   775  C  C   . HIS   A 1 102 ? 128.448 -45.252 29.974 1.00 7.68  ? 193 HIS   A C   1 
ATOM   776  O  O   . HIS   A 1 102 ? 127.261 -45.248 29.636 1.00 8.63  ? 193 HIS   A O   1 
ATOM   777  C  CB  . HIS   A 1 102 ? 128.337 -44.840 32.429 1.00 7.32  ? 193 HIS   A CB  1 
ATOM   778  C  CG  . HIS   A 1 102 ? 129.119 -44.434 33.644 1.00 7.13  ? 193 HIS   A CG  1 
ATOM   779  N  ND1 . HIS   A 1 102 ? 129.280 -45.269 34.732 1.00 6.87  ? 193 HIS   A ND1 1 
ATOM   780  C  CD2 . HIS   A 1 102 ? 129.776 -43.290 33.946 1.00 7.45  ? 193 HIS   A CD2 1 
ATOM   781  C  CE1 . HIS   A 1 102 ? 129.995 -44.652 35.655 1.00 7.05  ? 193 HIS   A CE1 1 
ATOM   782  N  NE2 . HIS   A 1 102 ? 130.305 -43.447 35.208 1.00 8.32  ? 193 HIS   A NE2 1 
ATOM   783  N  N   . LEU   A 1 103 ? 129.360 -46.064 29.438 1.00 7.36  ? 194 LEU   A N   1 
ATOM   784  C  CA  . LEU   A 1 103 ? 129.015 -46.991 28.363 1.00 8.42  ? 194 LEU   A CA  1 
ATOM   785  C  C   . LEU   A 1 103 ? 128.105 -48.116 28.844 1.00 7.14  ? 194 LEU   A C   1 
ATOM   786  O  O   . LEU   A 1 103 ? 127.130 -48.467 28.162 1.00 7.38  ? 194 LEU   A O   1 
ATOM   787  C  CB  . LEU   A 1 103 ? 130.286 -47.586 27.764 1.00 7.55  ? 194 LEU   A CB  1 
ATOM   788  C  CG  . LEU   A 1 103 ? 130.032 -48.643 26.674 1.00 9.99  ? 194 LEU   A CG  1 
ATOM   789  C  CD1 . LEU   A 1 103 ? 129.423 -47.962 25.437 1.00 8.54  ? 194 LEU   A CD1 1 
ATOM   790  C  CD2 . LEU   A 1 103 ? 131.310 -49.407 26.308 1.00 8.78  ? 194 LEU   A CD2 1 
ATOM   791  N  N   . ILE   A 1 104 ? 128.424 -48.722 29.992 1.00 6.75  ? 195 ILE   A N   1 
ATOM   792  C  CA  . ILE   A 1 104 ? 127.720 -49.913 30.476 1.00 7.43  ? 195 ILE   A CA  1 
ATOM   793  C  C   . ILE   A 1 104 ? 126.691 -49.512 31.519 1.00 7.35  ? 195 ILE   A C   1 
ATOM   794  O  O   . ILE   A 1 104 ? 127.032 -48.900 32.539 1.00 9.54  ? 195 ILE   A O   1 
ATOM   795  C  CB  . ILE   A 1 104 ? 128.689 -50.942 31.074 1.00 8.25  ? 195 ILE   A CB  1 
ATOM   796  C  CG1 . ILE   A 1 104 ? 129.760 -51.320 30.055 1.00 8.57  ? 195 ILE   A CG1 1 
ATOM   797  C  CG2 . ILE   A 1 104 ? 127.915 -52.183 31.536 1.00 6.11  ? 195 ILE   A CG2 1 
ATOM   798  C  CD1 . ILE   A 1 104 ? 130.793 -52.285 30.622 1.00 8.47  ? 195 ILE   A CD1 1 
ATOM   799  N  N   . ARG   A 1 105 ? 125.444 -49.895 31.292 1.00 6.66  ? 196 ARG   A N   1 
ATOM   800  C  CA  . ARG   A 1 105 ? 124.403 -49.761 32.295 1.00 6.87  ? 196 ARG   A CA  1 
ATOM   801  C  C   . ARG   A 1 105 ? 123.903 -51.137 32.697 1.00 7.41  ? 196 ARG   A C   1 
ATOM   802  O  O   . ARG   A 1 105 ? 123.994 -52.090 31.929 1.00 6.67  ? 196 ARG   A O   1 
ATOM   803  C  CB  . ARG   A 1 105 ? 123.231 -48.953 31.767 1.00 7.54  ? 196 ARG   A CB  1 
ATOM   804  C  CG  . ARG   A 1 105 ? 123.622 -47.598 31.201 1.00 7.41  ? 196 ARG   A CG  1 
ATOM   805  C  CD  . ARG   A 1 105 ? 122.372 -46.813 30.876 1.00 8.37  ? 196 ARG   A CD  1 
ATOM   806  N  NE  . ARG   A 1 105 ? 122.721 -45.449 30.489 1.00 12.05 ? 196 ARG   A NE  1 
ATOM   807  C  CZ  . ARG   A 1 105 ? 121.857 -44.556 30.036 1.00 8.96  ? 196 ARG   A CZ  1 
ATOM   808  N  NH1 . ARG   A 1 105 ? 120.570 -44.870 29.911 1.00 10.88 ? 196 ARG   A NH1 1 
ATOM   809  N  NH2 . ARG   A 1 105 ? 122.285 -43.350 29.706 1.00 11.01 ? 196 ARG   A NH2 1 
ATOM   810  N  N   . VAL   A 1 106 ? 123.336 -51.224 33.892 1.00 6.71  ? 197 VAL   A N   1 
ATOM   811  C  CA  . VAL   A 1 106 ? 122.570 -52.399 34.303 1.00 8.05  ? 197 VAL   A CA  1 
ATOM   812  C  C   . VAL   A 1 106 ? 121.091 -52.098 34.115 1.00 11.17 ? 197 VAL   A C   1 
ATOM   813  O  O   . VAL   A 1 106 ? 120.609 -51.026 34.505 1.00 12.41 ? 197 VAL   A O   1 
ATOM   814  C  CB  . VAL   A 1 106 ? 122.885 -52.791 35.754 1.00 7.79  ? 197 VAL   A CB  1 
ATOM   815  C  CG1 . VAL   A 1 106 ? 121.868 -53.825 36.266 1.00 11.77 ? 197 VAL   A CG1 1 
ATOM   816  C  CG2 . VAL   A 1 106 ? 124.303 -53.359 35.827 1.00 8.31  ? 197 VAL   A CG2 1 
ATOM   817  N  N   . GLU   A 1 107 ? 120.380 -53.027 33.485 1.00 7.64  ? 198 GLU   A N   1 
ATOM   818  C  CA  . GLU   A 1 107 ? 118.953 -52.904 33.238 1.00 10.31 ? 198 GLU   A CA  1 
ATOM   819  C  C   . GLU   A 1 107 ? 118.184 -53.617 34.339 1.00 15.36 ? 198 GLU   A C   1 
ATOM   820  O  O   . GLU   A 1 107 ? 118.512 -54.756 34.686 1.00 15.17 ? 198 GLU   A O   1 
ATOM   821  C  CB  . GLU   A 1 107 ? 118.593 -53.514 31.880 1.00 9.91  ? 198 GLU   A CB  1 
ATOM   822  C  CG  . GLU   A 1 107 ? 117.113 -53.501 31.563 1.00 15.61 ? 198 GLU   A CG  1 
ATOM   823  C  CD  . GLU   A 1 107 ? 116.801 -54.171 30.235 1.00 22.99 ? 198 GLU   A CD  1 
ATOM   824  O  OE1 . GLU   A 1 107 ? 117.752 -54.517 29.495 1.00 19.90 ? 198 GLU   A OE1 1 
ATOM   825  O  OE2 . GLU   A 1 107 ? 115.602 -54.343 29.928 1.00 28.28 ? 198 GLU   A OE2 1 
ATOM   826  N  N   . GLY   A 1 108 ? 117.160 -52.955 34.874 1.00 9.16  ? 199 GLY   A N   1 
ATOM   827  C  CA  . GLY   A 1 108 ? 116.218 -53.631 35.745 1.00 19.84 ? 199 GLY   A CA  1 
ATOM   828  C  C   . GLY   A 1 108 ? 116.715 -53.963 37.133 1.00 23.35 ? 199 GLY   A C   1 
ATOM   829  O  O   . GLY   A 1 108 ? 116.284 -54.969 37.718 1.00 26.61 ? 199 GLY   A O   1 
ATOM   830  N  N   . ASN   A 1 109 ? 117.613 -53.155 37.686 1.00 16.64 ? 200 ASN   A N   1 
ATOM   831  C  CA  . ASN   A 1 109 ? 118.057 -53.341 39.065 1.00 15.86 ? 200 ASN   A CA  1 
ATOM   832  C  C   . ASN   A 1 109 ? 118.186 -51.954 39.680 1.00 18.05 ? 200 ASN   A C   1 
ATOM   833  O  O   . ASN   A 1 109 ? 119.111 -51.202 39.351 1.00 17.08 ? 200 ASN   A O   1 
ATOM   834  C  CB  . ASN   A 1 109 ? 119.374 -54.127 39.139 1.00 18.75 ? 200 ASN   A CB  1 
ATOM   835  C  CG  . ASN   A 1 109 ? 119.716 -54.583 40.564 1.00 18.08 ? 200 ASN   A CG  1 
ATOM   836  O  OD1 . ASN   A 1 109 ? 119.395 -53.904 41.535 1.00 19.60 ? 200 ASN   A OD1 1 
ATOM   837  N  ND2 . ASN   A 1 109 ? 120.379 -55.734 40.684 1.00 11.81 ? 200 ASN   A ND2 1 
ATOM   838  N  N   . LEU   A 1 110 ? 117.240 -51.609 40.550 1.00 18.96 ? 201 LEU   A N   1 
ATOM   839  C  CA  . LEU   A 1 110 ? 117.247 -50.306 41.200 1.00 19.29 ? 201 LEU   A CA  1 
ATOM   840  C  C   . LEU   A 1 110 ? 118.395 -50.146 42.187 1.00 13.59 ? 201 LEU   A C   1 
ATOM   841  O  O   . LEU   A 1 110 ? 118.660 -49.024 42.627 1.00 17.97 ? 201 LEU   A O   1 
ATOM   842  C  CB  . LEU   A 1 110 ? 115.911 -50.087 41.910 1.00 27.53 ? 201 LEU   A CB  1 
ATOM   843  C  CG  . LEU   A 1 110 ? 114.687 -50.074 40.990 1.00 35.99 ? 201 LEU   A CG  1 
ATOM   844  C  CD1 . LEU   A 1 110 ? 113.409 -49.932 41.797 1.00 42.89 ? 201 LEU   A CD1 1 
ATOM   845  C  CD2 . LEU   A 1 110 ? 114.798 -48.960 39.959 1.00 36.36 ? 201 LEU   A CD2 1 
ATOM   846  N  N   . ARG   A 1 111 ? 119.092 -51.223 42.530 1.00 12.67 ? 202 ARG   A N   1 
ATOM   847  C  CA  . ARG   A 1 111 ? 120.246 -51.158 43.417 1.00 14.52 ? 202 ARG   A CA  1 
ATOM   848  C  C   . ARG   A 1 111 ? 121.556 -51.003 42.659 1.00 13.84 ? 202 ARG   A C   1 
ATOM   849  O  O   . ARG   A 1 111 ? 122.626 -51.059 43.273 1.00 12.78 ? 202 ARG   A O   1 
ATOM   850  C  CB  . ARG   A 1 111 ? 120.302 -52.402 44.312 1.00 18.31 ? 202 ARG   A CB  1 
ATOM   851  N  N   . ALA   A 1 112 ? 121.499 -50.802 41.347 1.00 12.10 ? 203 ALA   A N   1 
ATOM   852  C  CA  . ALA   A 1 112 ? 122.714 -50.556 40.586 1.00 11.10 ? 203 ALA   A CA  1 
ATOM   853  C  C   . ALA   A 1 112 ? 123.357 -49.239 41.011 1.00 14.61 ? 203 ALA   A C   1 
ATOM   854  O  O   . ALA   A 1 112 ? 122.682 -48.217 41.174 1.00 13.22 ? 203 ALA   A O   1 
ATOM   855  C  CB  . ALA   A 1 112 ? 122.407 -50.539 39.084 1.00 13.46 ? 203 ALA   A CB  1 
ATOM   856  N  N   . GLU   A 1 113 ? 124.675 -49.268 41.186 1.00 7.81  ? 204 GLU   A N   1 
ATOM   857  C  CA  . GLU   A 1 113 ? 125.458 -48.095 41.534 1.00 7.47  ? 204 GLU   A CA  1 
ATOM   858  C  C   . GLU   A 1 113 ? 126.526 -47.854 40.477 1.00 10.52 ? 204 GLU   A C   1 
ATOM   859  O  O   . GLU   A 1 113 ? 127.129 -48.799 39.962 1.00 9.20  ? 204 GLU   A O   1 
ATOM   860  C  CB  . GLU   A 1 113 ? 126.114 -48.251 42.908 1.00 13.10 ? 204 GLU   A CB  1 
ATOM   861  C  CG  . GLU   A 1 113 ? 125.088 -48.390 44.024 1.00 19.52 ? 204 GLU   A CG  1 
ATOM   862  C  CD  . GLU   A 1 113 ? 125.712 -48.551 45.407 1.00 27.43 ? 204 GLU   A CD  1 
ATOM   863  O  OE1 . GLU   A 1 113 ? 124.935 -48.726 46.368 1.00 26.60 ? 204 GLU   A OE1 1 
ATOM   864  O  OE2 . GLU   A 1 113 ? 126.963 -48.505 45.535 1.00 23.10 ? 204 GLU   A OE2 1 
ATOM   865  N  N   . TYR   A 1 114 ? 126.775 -46.585 40.180 1.00 8.85  ? 205 TYR   A N   1 
ATOM   866  C  CA  . TYR   A 1 114 ? 127.704 -46.185 39.130 1.00 8.44  ? 205 TYR   A CA  1 
ATOM   867  C  C   . TYR   A 1 114 ? 128.877 -45.447 39.758 1.00 10.95 ? 205 TYR   A C   1 
ATOM   868  O  O   . TYR   A 1 114 ? 128.672 -44.533 40.565 1.00 12.17 ? 205 TYR   A O   1 
ATOM   869  C  CB  . TYR   A 1 114 ? 126.979 -45.299 38.101 1.00 7.18  ? 205 TYR   A CB  1 
ATOM   870  C  CG  . TYR   A 1 114 ? 125.984 -46.090 37.306 1.00 7.03  ? 205 TYR   A CG  1 
ATOM   871  C  CD1 . TYR   A 1 114 ? 124.718 -46.375 37.813 1.00 8.74  ? 205 TYR   A CD1 1 
ATOM   872  C  CD2 . TYR   A 1 114 ? 126.331 -46.619 36.067 1.00 8.84  ? 205 TYR   A CD2 1 
ATOM   873  C  CE1 . TYR   A 1 114 ? 123.815 -47.139 37.089 1.00 7.73  ? 205 TYR   A CE1 1 
ATOM   874  C  CE2 . TYR   A 1 114 ? 125.431 -47.384 35.337 1.00 6.74  ? 205 TYR   A CE2 1 
ATOM   875  C  CZ  . TYR   A 1 114 ? 124.186 -47.638 35.854 1.00 7.48  ? 205 TYR   A CZ  1 
ATOM   876  O  OH  . TYR   A 1 114 ? 123.298 -48.393 35.123 1.00 8.60  ? 205 TYR   A OH  1 
ATOM   877  N  N   . LEU   A 1 115 ? 130.096 -45.847 39.406 1.00 7.13  ? 206 LEU   A N   1 
ATOM   878  C  CA  . LEU   A 1 115 ? 131.304 -45.251 39.970 1.00 10.45 ? 206 LEU   A CA  1 
ATOM   879  C  C   . LEU   A 1 115 ? 132.079 -44.490 38.902 1.00 12.37 ? 206 LEU   A C   1 
ATOM   880  O  O   . LEU   A 1 115 ? 132.342 -45.030 37.823 1.00 9.24  ? 206 LEU   A O   1 
ATOM   881  C  CB  . LEU   A 1 115 ? 132.207 -46.324 40.595 1.00 8.99  ? 206 LEU   A CB  1 
ATOM   882  C  CG  . LEU   A 1 115 ? 133.511 -45.822 41.243 1.00 7.93  ? 206 LEU   A CG  1 
ATOM   883  C  CD1 . LEU   A 1 115 ? 133.256 -44.900 42.450 1.00 9.53  ? 206 LEU   A CD1 1 
ATOM   884  C  CD2 . LEU   A 1 115 ? 134.421 -46.979 41.644 1.00 11.82 ? 206 LEU   A CD2 1 
ATOM   885  N  N   . ASP   A 1 116 ? 132.429 -43.230 39.200 1.00 9.80  ? 207 ASP   A N   1 
ATOM   886  C  CA  . ASP   A 1 116 ? 133.518 -42.519 38.530 1.00 9.54  ? 207 ASP   A CA  1 
ATOM   887  C  C   . ASP   A 1 116 ? 134.717 -42.631 39.466 1.00 13.23 ? 207 ASP   A C   1 
ATOM   888  O  O   . ASP   A 1 116 ? 134.723 -42.009 40.533 1.00 11.05 ? 207 ASP   A O   1 
ATOM   889  C  CB  . ASP   A 1 116 ? 133.209 -41.034 38.297 1.00 16.76 ? 207 ASP   A CB  1 
ATOM   890  C  CG  . ASP   A 1 116 ? 132.067 -40.776 37.315 1.00 22.31 ? 207 ASP   A CG  1 
ATOM   891  O  OD1 . ASP   A 1 116 ? 131.865 -41.547 36.365 1.00 20.80 ? 207 ASP   A OD1 1 
ATOM   892  O  OD2 . ASP   A 1 116 ? 131.393 -39.730 37.484 1.00 28.20 ? 207 ASP   A OD2 1 
ATOM   893  N  N   . ASP   A 1 117 ? 135.726 -43.409 39.084 1.00 9.70  ? 208 ASP   A N   1 
ATOM   894  C  CA  . ASP   A 1 117 ? 136.875 -43.600 39.965 1.00 13.06 ? 208 ASP   A CA  1 
ATOM   895  C  C   . ASP   A 1 117 ? 137.629 -42.287 40.165 1.00 16.35 ? 208 ASP   A C   1 
ATOM   896  O  O   . ASP   A 1 117 ? 138.036 -41.626 39.201 1.00 11.57 ? 208 ASP   A O   1 
ATOM   897  C  CB  . ASP   A 1 117 ? 137.811 -44.668 39.400 1.00 13.90 ? 208 ASP   A CB  1 
ATOM   898  C  CG  . ASP   A 1 117 ? 138.845 -45.136 40.422 1.00 19.51 ? 208 ASP   A CG  1 
ATOM   899  O  OD1 . ASP   A 1 117 ? 139.808 -44.388 40.715 1.00 17.77 ? 208 ASP   A OD1 1 
ATOM   900  O  OD2 . ASP   A 1 117 ? 138.673 -46.247 40.957 1.00 17.22 ? 208 ASP   A OD2 1 
ATOM   901  N  N   . ARG   A 1 118 ? 137.821 -41.908 41.429 1.00 14.81 ? 209 ARG   A N   1 
ATOM   902  C  CA  . ARG   A 1 118 ? 138.422 -40.614 41.719 1.00 15.74 ? 209 ARG   A CA  1 
ATOM   903  C  C   . ARG   A 1 118 ? 139.883 -40.540 41.290 1.00 22.84 ? 209 ARG   A C   1 
ATOM   904  O  O   . ARG   A 1 118 ? 140.385 -39.440 41.032 1.00 22.62 ? 209 ARG   A O   1 
ATOM   905  C  CB  . ARG   A 1 118 ? 138.299 -40.293 43.213 1.00 20.22 ? 209 ARG   A CB  1 
ATOM   906  N  N   . ASN   A 1 119 ? 140.570 -41.675 41.188 1.00 21.59 ? 210 ASN   A N   1 
ATOM   907  C  CA  . ASN   A 1 119 ? 141.977 -41.682 40.804 1.00 21.39 ? 210 ASN   A CA  1 
ATOM   908  C  C   . ASN   A 1 119 ? 142.204 -41.981 39.329 1.00 19.59 ? 210 ASN   A C   1 
ATOM   909  O  O   . ASN   A 1 119 ? 143.066 -41.355 38.705 1.00 20.66 ? 210 ASN   A O   1 
ATOM   910  C  CB  . ASN   A 1 119 ? 142.743 -42.703 41.647 1.00 22.91 ? 210 ASN   A CB  1 
ATOM   911  C  CG  . ASN   A 1 119 ? 142.798 -42.318 43.100 1.00 31.96 ? 210 ASN   A CG  1 
ATOM   912  O  OD1 . ASN   A 1 119 ? 142.874 -41.137 43.434 1.00 35.20 ? 210 ASN   A OD1 1 
ATOM   913  N  ND2 . ASN   A 1 119 ? 142.753 -43.311 43.978 1.00 42.26 ? 210 ASN   A ND2 1 
ATOM   914  N  N   . THR   A 1 120 ? 141.464 -42.927 38.754 1.00 12.99 ? 211 THR   A N   1 
ATOM   915  C  CA  . THR   A 1 120 ? 141.687 -43.340 37.374 1.00 17.58 ? 211 THR   A CA  1 
ATOM   916  C  C   . THR   A 1 120 ? 140.680 -42.764 36.394 1.00 16.38 ? 211 THR   A C   1 
ATOM   917  O  O   . THR   A 1 120 ? 140.881 -42.899 35.182 1.00 15.70 ? 211 THR   A O   1 
ATOM   918  C  CB  . THR   A 1 120 ? 141.643 -44.866 37.257 1.00 17.82 ? 211 THR   A CB  1 
ATOM   919  O  OG1 . THR   A 1 120 ? 140.295 -45.307 37.481 1.00 20.89 ? 211 THR   A OG1 1 
ATOM   920  C  CG2 . THR   A 1 120 ? 142.564 -45.501 38.281 1.00 21.33 ? 211 THR   A CG2 1 
ATOM   921  N  N   . PHE   A 1 121 ? 139.595 -42.165 36.880 1.00 14.14 ? 212 PHE   A N   1 
ATOM   922  C  CA  . PHE   A 1 121 ? 138.502 -41.634 36.067 1.00 11.72 ? 212 PHE   A CA  1 
ATOM   923  C  C   . PHE   A 1 121 ? 137.778 -42.712 35.267 1.00 12.27 ? 212 PHE   A C   1 
ATOM   924  O  O   . PHE   A 1 121 ? 136.947 -42.391 34.405 1.00 12.09 ? 212 PHE   A O   1 
ATOM   925  C  CB  . PHE   A 1 121 ? 138.990 -40.523 35.136 1.00 14.95 ? 212 PHE   A CB  1 
ATOM   926  C  CG  . PHE   A 1 121 ? 139.871 -39.520 35.832 1.00 19.23 ? 212 PHE   A CG  1 
ATOM   927  C  CD1 . PHE   A 1 121 ? 139.342 -38.673 36.788 1.00 17.32 ? 212 PHE   A CD1 1 
ATOM   928  C  CD2 . PHE   A 1 121 ? 141.228 -39.450 35.553 1.00 28.94 ? 212 PHE   A CD2 1 
ATOM   929  C  CE1 . PHE   A 1 121 ? 140.151 -37.751 37.443 1.00 21.29 ? 212 PHE   A CE1 1 
ATOM   930  C  CE2 . PHE   A 1 121 ? 142.047 -38.526 36.208 1.00 29.12 ? 212 PHE   A CE2 1 
ATOM   931  C  CZ  . PHE   A 1 121 ? 141.502 -37.682 37.151 1.00 24.61 ? 212 PHE   A CZ  1 
ATOM   932  N  N   . ARG   A 1 122 ? 138.041 -43.982 35.537 1.00 9.03  ? 213 ARG   A N   1 
ATOM   933  C  CA  . ARG   A 1 122 ? 137.317 -45.035 34.833 1.00 12.10 ? 213 ARG   A CA  1 
ATOM   934  C  C   . ARG   A 1 122 ? 135.914 -45.219 35.398 1.00 12.22 ? 213 ARG   A C   1 
ATOM   935  O  O   . ARG   A 1 122 ? 135.644 -44.925 36.569 1.00 13.31 ? 213 ARG   A O   1 
ATOM   936  C  CB  . ARG   A 1 122 ? 138.084 -46.348 34.922 1.00 14.61 ? 213 ARG   A CB  1 
ATOM   937  C  CG  . ARG   A 1 122 ? 139.343 -46.316 34.101 1.00 12.05 ? 213 ARG   A CG  1 
ATOM   938  C  CD  . ARG   A 1 122 ? 139.929 -47.689 34.018 1.00 14.68 ? 213 ARG   A CD  1 
ATOM   939  N  NE  . ARG   A 1 122 ? 141.258 -47.653 33.431 1.00 11.22 ? 213 ARG   A NE  1 
ATOM   940  C  CZ  . ARG   A 1 122 ? 141.497 -47.868 32.144 1.00 12.34 ? 213 ARG   A CZ  1 
ATOM   941  N  NH1 . ARG   A 1 122 ? 140.487 -48.126 31.320 1.00 10.60 ? 213 ARG   A NH1 1 
ATOM   942  N  NH2 . ARG   A 1 122 ? 142.743 -47.847 31.691 1.00 13.85 ? 213 ARG   A NH2 1 
ATOM   943  N  N   . HIS   A 1 123 ? 135.024 -45.731 34.550 1.00 9.20  ? 214 HIS   A N   1 
ATOM   944  C  CA  . HIS   A 1 123 ? 133.617 -45.918 34.880 1.00 7.43  ? 214 HIS   A CA  1 
ATOM   945  C  C   . HIS   A 1 123 ? 133.344 -47.382 35.201 1.00 6.78  ? 214 HIS   A C   1 
ATOM   946  O  O   . HIS   A 1 123 ? 133.930 -48.282 34.599 1.00 11.90 ? 214 HIS   A O   1 
ATOM   947  C  CB  . HIS   A 1 123 ? 132.710 -45.502 33.716 1.00 8.86  ? 214 HIS   A CB  1 
ATOM   948  C  CG  . HIS   A 1 123 ? 132.968 -44.117 33.201 1.00 12.30 ? 214 HIS   A CG  1 
ATOM   949  N  ND1 . HIS   A 1 123 ? 132.532 -43.693 31.962 1.00 10.66 ? 214 HIS   A ND1 1 
ATOM   950  C  CD2 . HIS   A 1 123 ? 133.609 -43.061 33.757 1.00 9.92  ? 214 HIS   A CD2 1 
ATOM   951  C  CE1 . HIS   A 1 123 ? 132.904 -42.438 31.771 1.00 10.70 ? 214 HIS   A CE1 1 
ATOM   952  N  NE2 . HIS   A 1 123 ? 133.549 -42.027 32.851 1.00 11.95 ? 214 HIS   A NE2 1 
ATOM   953  N  N   . SER   A 1 124 ? 132.414 -47.614 36.126 1.00 6.98  ? 215 SER   A N   1 
ATOM   954  C  CA  . SER   A 1 124 ? 131.957 -48.972 36.383 1.00 6.42  ? 215 SER   A CA  1 
ATOM   955  C  C   . SER   A 1 124 ? 130.553 -48.925 36.959 1.00 8.11  ? 215 SER   A C   1 
ATOM   956  O  O   . SER   A 1 124 ? 130.085 -47.884 37.431 1.00 7.09  ? 215 SER   A O   1 
ATOM   957  C  CB  . SER   A 1 124 ? 132.922 -49.727 37.314 1.00 7.27  ? 215 SER   A CB  1 
ATOM   958  O  OG  . SER   A 1 124 ? 133.069 -49.059 38.555 1.00 7.91  ? 215 SER   A OG  1 
ATOM   959  N  N   . VAL   A 1 125 ? 129.868 -50.064 36.880 1.00 6.01  ? 216 VAL   A N   1 
ATOM   960  C  CA  . VAL   A 1 125 ? 128.539 -50.227 37.452 1.00 6.05  ? 216 VAL   A CA  1 
ATOM   961  C  C   . VAL   A 1 125 ? 128.550 -51.513 38.270 1.00 7.24  ? 216 VAL   A C   1 
ATOM   962  O  O   . VAL   A 1 125 ? 129.072 -52.536 37.813 1.00 6.99  ? 216 VAL   A O   1 
ATOM   963  C  CB  . VAL   A 1 125 ? 127.435 -50.248 36.372 1.00 6.38  ? 216 VAL   A CB  1 
ATOM   964  C  CG1 . VAL   A 1 125 ? 127.681 -51.350 35.309 1.00 9.04  ? 216 VAL   A CG1 1 
ATOM   965  C  CG2 . VAL   A 1 125 ? 126.052 -50.391 37.009 1.00 7.30  ? 216 VAL   A CG2 1 
ATOM   966  N  N   . VAL   A 1 126 ? 127.992 -51.458 39.478 1.00 6.20  ? 217 VAL   A N   1 
ATOM   967  C  CA  . VAL   A 1 126 ? 128.072 -52.566 40.429 1.00 6.28  ? 217 VAL   A CA  1 
ATOM   968  C  C   . VAL   A 1 126 ? 126.693 -52.800 41.041 1.00 6.70  ? 217 VAL   A C   1 
ATOM   969  O  O   . VAL   A 1 126 ? 125.949 -51.841 41.293 1.00 8.76  ? 217 VAL   A O   1 
ATOM   970  C  CB  . VAL   A 1 126 ? 129.159 -52.290 41.505 1.00 6.51  ? 217 VAL   A CB  1 
ATOM   971  C  CG1 . VAL   A 1 126 ? 128.943 -50.948 42.223 1.00 8.28  ? 217 VAL   A CG1 1 
ATOM   972  C  CG2 . VAL   A 1 126 ? 129.251 -53.436 42.523 1.00 11.56 ? 217 VAL   A CG2 1 
ATOM   973  N  N   . VAL   A 1 127 ? 126.338 -54.074 41.233 1.00 8.96  ? 218 VAL   A N   1 
ATOM   974  C  CA  . VAL   A 1 127 ? 125.066 -54.473 41.841 1.00 6.94  ? 218 VAL   A CA  1 
ATOM   975  C  C   . VAL   A 1 127 ? 125.338 -55.512 42.921 1.00 8.47  ? 218 VAL   A C   1 
ATOM   976  O  O   . VAL   A 1 127 ? 126.352 -56.223 42.889 1.00 8.47  ? 218 VAL   A O   1 
ATOM   977  C  CB  . VAL   A 1 127 ? 124.071 -55.055 40.801 1.00 12.94 ? 218 VAL   A CB  1 
ATOM   978  C  CG1 . VAL   A 1 127 ? 123.481 -53.972 39.879 1.00 12.58 ? 218 VAL   A CG1 1 
ATOM   979  C  CG2 . VAL   A 1 127 ? 124.709 -56.158 39.998 1.00 14.57 ? 218 VAL   A CG2 1 
ATOM   980  N  N   . PRO   A 1 128 ? 124.429 -55.648 43.878 1.00 10.49 ? 219 PRO   A N   1 
ATOM   981  C  CA  . PRO   A 1 128 ? 124.508 -56.788 44.799 1.00 12.08 ? 219 PRO   A CA  1 
ATOM   982  C  C   . PRO   A 1 128 ? 124.279 -58.081 44.037 1.00 13.02 ? 219 PRO   A C   1 
ATOM   983  O  O   . PRO   A 1 128 ? 123.594 -58.104 43.011 1.00 12.06 ? 219 PRO   A O   1 
ATOM   984  C  CB  . PRO   A 1 128 ? 123.365 -56.531 45.794 1.00 11.44 ? 219 PRO   A CB  1 
ATOM   985  C  CG  . PRO   A 1 128 ? 122.989 -55.096 45.617 1.00 10.54 ? 219 PRO   A CG  1 
ATOM   986  C  CD  . PRO   A 1 128 ? 123.308 -54.748 44.189 1.00 8.12  ? 219 PRO   A CD  1 
ATOM   987  N  N   . CYS   A 1 129 ? 124.870 -59.172 44.520 1.00 19.31 ? 220 CYS   A N   1 
ATOM   988  C  CA  A CYS   A 1 129 ? 124.638 -60.523 44.007 0.34 18.74 ? 220 CYS   A CA  1 
ATOM   989  C  CA  B CYS   A 1 129 ? 124.476 -60.444 43.948 0.66 19.20 ? 220 CYS   A CA  1 
ATOM   990  C  C   . CYS   A 1 129 ? 123.775 -61.297 44.992 1.00 18.15 ? 220 CYS   A C   1 
ATOM   991  O  O   . CYS   A 1 129 ? 123.946 -61.140 46.207 1.00 15.36 ? 220 CYS   A O   1 
ATOM   992  C  CB  A CYS   A 1 129 ? 125.943 -61.306 43.822 0.34 17.61 ? 220 CYS   A CB  1 
ATOM   993  C  CB  B CYS   A 1 129 ? 125.647 -61.190 43.305 0.66 18.63 ? 220 CYS   A CB  1 
ATOM   994  S  SG  A CYS   A 1 129 ? 127.352 -60.442 43.125 0.34 15.59 ? 220 CYS   A SG  1 
ATOM   995  S  SG  B CYS   A 1 129 ? 126.945 -61.758 44.352 0.66 18.05 ? 220 CYS   A SG  1 
ATOM   996  N  N   . GLU   A 1 130 ? 122.908 -62.154 44.482 1.00 24.74 ? 221 GLU   A N   1 
ATOM   997  C  CA  . GLU   A 1 130 ? 122.015 -62.988 45.267 1.00 32.87 ? 221 GLU   A CA  1 
ATOM   998  C  C   . GLU   A 1 130 ? 122.112 -64.402 44.733 1.00 26.59 ? 221 GLU   A C   1 
ATOM   999  O  O   . GLU   A 1 130 ? 122.538 -64.607 43.595 1.00 26.18 ? 221 GLU   A O   1 
ATOM   1000 C  CB  . GLU   A 1 130 ? 120.566 -62.495 45.162 1.00 42.21 ? 221 GLU   A CB  1 
ATOM   1001 C  CG  . GLU   A 1 130 ? 120.433 -61.150 44.484 1.00 47.99 ? 221 GLU   A CG  1 
ATOM   1002 C  CD  . GLU   A 1 130 ? 119.676 -60.173 45.339 1.00 56.77 ? 221 GLU   A CD  1 
ATOM   1003 O  OE1 . GLU   A 1 130 ? 118.451 -60.355 45.499 1.00 59.07 ? 221 GLU   A OE1 1 
ATOM   1004 O  OE2 . GLU   A 1 130 ? 120.311 -59.240 45.872 1.00 61.71 ? 221 GLU   A OE2 1 
ATOM   1005 N  N   . PRO   A 1 131 ? 121.736 -65.399 45.526 1.00 25.75 ? 222 PRO   A N   1 
ATOM   1006 C  CA  . PRO   A 1 131 ? 121.707 -66.767 45.021 1.00 24.09 ? 222 PRO   A CA  1 
ATOM   1007 C  C   . PRO   A 1 131 ? 120.632 -66.915 43.961 1.00 29.27 ? 222 PRO   A C   1 
ATOM   1008 O  O   . PRO   A 1 131 ? 119.749 -66.051 43.844 1.00 28.13 ? 222 PRO   A O   1 
ATOM   1009 C  CB  . PRO   A 1 131 ? 121.390 -67.604 46.271 1.00 25.87 ? 222 PRO   A CB  1 
ATOM   1010 C  CG  . PRO   A 1 131 ? 121.688 -66.702 47.426 1.00 25.39 ? 222 PRO   A CG  1 
ATOM   1011 C  CD  . PRO   A 1 131 ? 121.353 -65.335 46.945 1.00 21.97 ? 222 PRO   A CD  1 
ATOM   1012 N  N   . PRO   A 1 132 ? 120.694 -67.976 43.152 1.00 27.67 ? 223 PRO   A N   1 
ATOM   1013 C  CA  . PRO   A 1 132 ? 119.708 -68.147 42.075 1.00 19.19 ? 223 PRO   A CA  1 
ATOM   1014 C  C   . PRO   A 1 132 ? 118.298 -68.301 42.619 1.00 24.77 ? 223 PRO   A C   1 
ATOM   1015 O  O   . PRO   A 1 132 ? 118.088 -68.796 43.728 1.00 26.74 ? 223 PRO   A O   1 
ATOM   1016 C  CB  . PRO   A 1 132 ? 120.163 -69.437 41.376 1.00 18.17 ? 223 PRO   A CB  1 
ATOM   1017 C  CG  . PRO   A 1 132 ? 121.604 -69.602 41.757 1.00 24.34 ? 223 PRO   A CG  1 
ATOM   1018 C  CD  . PRO   A 1 132 ? 121.712 -69.040 43.148 1.00 25.19 ? 223 PRO   A CD  1 
ATOM   1019 N  N   . GLU   A 1 133 ? 117.327 -67.895 41.804 1.00 30.33 ? 224 GLU   A N   1 
ATOM   1020 C  CA  . GLU   A 1 133 ? 115.928 -68.147 42.117 1.00 37.69 ? 224 GLU   A CA  1 
ATOM   1021 C  C   . GLU   A 1 133 ? 115.665 -69.647 42.227 1.00 40.43 ? 224 GLU   A C   1 
ATOM   1022 O  O   . GLU   A 1 133 ? 116.433 -70.485 41.738 1.00 37.27 ? 224 GLU   A O   1 
ATOM   1023 C  CB  . GLU   A 1 133 ? 115.019 -67.529 41.051 1.00 38.07 ? 224 GLU   A CB  1 
ATOM   1024 N  N   . VAL   A 1 134 ? 114.556 -69.985 42.885 1.00 44.39 ? 225 VAL   A N   1 
ATOM   1025 C  CA  . VAL   A 1 134 ? 114.211 -71.388 43.077 1.00 45.89 ? 225 VAL   A CA  1 
ATOM   1026 C  C   . VAL   A 1 134 ? 114.056 -72.063 41.723 1.00 42.43 ? 225 VAL   A C   1 
ATOM   1027 O  O   . VAL   A 1 134 ? 113.364 -71.558 40.831 1.00 45.11 ? 225 VAL   A O   1 
ATOM   1028 C  CB  . VAL   A 1 134 ? 112.934 -71.509 43.918 1.00 45.24 ? 225 VAL   A CB  1 
ATOM   1029 C  CG1 . VAL   A 1 134 ? 112.915 -72.844 44.645 1.00 41.01 ? 225 VAL   A CG1 1 
ATOM   1030 C  CG2 . VAL   A 1 134 ? 112.835 -70.335 44.891 1.00 44.98 ? 225 VAL   A CG2 1 
ATOM   1031 N  N   . GLY   A 1 135 ? 114.724 -73.202 41.556 1.00 40.85 ? 226 GLY   A N   1 
ATOM   1032 C  CA  . GLY   A 1 135 ? 114.727 -73.910 40.294 1.00 40.69 ? 226 GLY   A CA  1 
ATOM   1033 C  C   . GLY   A 1 135 ? 115.734 -73.425 39.272 1.00 38.70 ? 226 GLY   A C   1 
ATOM   1034 O  O   . GLY   A 1 135 ? 115.779 -73.981 38.166 1.00 40.98 ? 226 GLY   A O   1 
ATOM   1035 N  N   . SER   A 1 136 ? 116.534 -72.408 39.587 1.00 27.15 ? 227 SER   A N   1 
ATOM   1036 C  CA  . SER   A 1 136 ? 117.582 -71.937 38.694 1.00 22.23 ? 227 SER   A CA  1 
ATOM   1037 C  C   . SER   A 1 136 ? 118.947 -72.336 39.248 1.00 19.56 ? 227 SER   A C   1 
ATOM   1038 O  O   . SER   A 1 136 ? 119.109 -72.521 40.457 1.00 21.12 ? 227 SER   A O   1 
ATOM   1039 C  CB  . SER   A 1 136 ? 117.501 -70.418 38.511 1.00 27.72 ? 227 SER   A CB  1 
ATOM   1040 O  OG  . SER   A 1 136 ? 118.465 -69.961 37.576 1.00 37.69 ? 227 SER   A OG  1 
ATOM   1041 N  N   . ASP   A 1 137 ? 119.937 -72.466 38.361 1.00 17.05 ? 228 ASP   A N   1 
ATOM   1042 C  CA  . ASP   A 1 137 ? 121.283 -72.862 38.772 1.00 16.90 ? 228 ASP   A CA  1 
ATOM   1043 C  C   . ASP   A 1 137 ? 122.299 -71.729 38.708 1.00 14.46 ? 228 ASP   A C   1 
ATOM   1044 O  O   . ASP   A 1 137 ? 123.451 -71.927 39.111 1.00 10.40 ? 228 ASP   A O   1 
ATOM   1045 C  CB  . ASP   A 1 137 ? 121.779 -74.039 37.923 1.00 13.14 ? 228 ASP   A CB  1 
ATOM   1046 C  CG  . ASP   A 1 137 ? 120.959 -75.290 38.135 1.00 18.34 ? 228 ASP   A CG  1 
ATOM   1047 O  OD1 . ASP   A 1 137 ? 120.718 -75.644 39.302 1.00 22.89 ? 228 ASP   A OD1 1 
ATOM   1048 O  OD2 . ASP   A 1 137 ? 120.573 -75.925 37.131 1.00 23.42 ? 228 ASP   A OD2 1 
ATOM   1049 N  N   . CYS   A 1 138 ? 121.914 -70.554 38.212 1.00 11.21 ? 229 CYS   A N   1 
ATOM   1050 C  CA  . CYS   A 1 138 ? 122.807 -69.411 38.136 1.00 9.49  ? 229 CYS   A CA  1 
ATOM   1051 C  C   . CYS   A 1 138 ? 121.967 -68.148 38.259 1.00 12.19 ? 229 CYS   A C   1 
ATOM   1052 O  O   . CYS   A 1 138 ? 120.740 -68.183 38.163 1.00 18.13 ? 229 CYS   A O   1 
ATOM   1053 C  CB  . CYS   A 1 138 ? 123.612 -69.405 36.833 1.00 11.74 ? 229 CYS   A CB  1 
ATOM   1054 S  SG  . CYS   A 1 138 ? 122.606 -69.112 35.355 1.00 14.68 ? 229 CYS   A SG  1 
ATOM   1055 N  N   . THR   A 1 139 ? 122.630 -67.032 38.506 1.00 11.54 ? 230 THR   A N   1 
ATOM   1056 C  CA  . THR   A 1 139 ? 121.953 -65.747 38.433 1.00 10.87 ? 230 THR   A CA  1 
ATOM   1057 C  C   . THR   A 1 139 ? 122.363 -65.052 37.143 1.00 14.36 ? 230 THR   A C   1 
ATOM   1058 O  O   . THR   A 1 139 ? 123.361 -65.411 36.510 1.00 14.10 ? 230 THR   A O   1 
ATOM   1059 C  CB  . THR   A 1 139 ? 122.272 -64.871 39.649 1.00 20.41 ? 230 THR   A CB  1 
ATOM   1060 O  OG1 . THR   A 1 139 ? 123.656 -64.539 39.657 1.00 22.28 ? 230 THR   A OG1 1 
ATOM   1061 C  CG2 . THR   A 1 139 ? 121.959 -65.620 40.912 1.00 15.20 ? 230 THR   A CG2 1 
ATOM   1062 N  N   . THR   A 1 140 ? 121.567 -64.069 36.745 1.00 9.11  ? 231 THR   A N   1 
ATOM   1063 C  CA  . THR   A 1 140 ? 121.779 -63.374 35.484 1.00 8.95  ? 231 THR   A CA  1 
ATOM   1064 C  C   . THR   A 1 140 ? 121.705 -61.874 35.732 1.00 13.65 ? 231 THR   A C   1 
ATOM   1065 O  O   . THR   A 1 140 ? 120.791 -61.395 36.412 1.00 11.04 ? 231 THR   A O   1 
ATOM   1066 C  CB  . THR   A 1 140 ? 120.733 -63.819 34.448 1.00 14.85 ? 231 THR   A CB  1 
ATOM   1067 O  OG1 . THR   A 1 140 ? 120.887 -65.224 34.197 1.00 19.51 ? 231 THR   A OG1 1 
ATOM   1068 C  CG2 . THR   A 1 140 ? 120.898 -63.067 33.124 1.00 14.60 ? 231 THR   A CG2 1 
ATOM   1069 N  N   . ILE   A 1 141 ? 122.681 -61.140 35.215 1.00 8.03  ? 232 ILE   A N   1 
ATOM   1070 C  CA  . ILE   A 1 141 ? 122.625 -59.685 35.173 1.00 7.75  ? 232 ILE   A CA  1 
ATOM   1071 C  C   . ILE   A 1 141 ? 122.328 -59.276 33.741 1.00 10.00 ? 232 ILE   A C   1 
ATOM   1072 O  O   . ILE   A 1 141 ? 122.816 -59.905 32.795 1.00 11.11 ? 232 ILE   A O   1 
ATOM   1073 C  CB  . ILE   A 1 141 ? 123.940 -59.052 35.657 1.00 10.77 ? 232 ILE   A CB  1 
ATOM   1074 C  CG1 . ILE   A 1 141 ? 124.245 -59.518 37.073 1.00 19.23 ? 232 ILE   A CG1 1 
ATOM   1075 C  CG2 . ILE   A 1 141 ? 123.856 -57.511 35.631 1.00 10.09 ? 232 ILE   A CG2 1 
ATOM   1076 C  CD1 . ILE   A 1 141 ? 125.520 -58.989 37.539 1.00 17.38 ? 232 ILE   A CD1 1 
ATOM   1077 N  N   . HIS   A 1 142 ? 121.501 -58.251 33.576 1.00 10.06 ? 233 HIS   A N   1 
ATOM   1078 C  CA  A HIS   A 1 142 ? 121.210 -57.716 32.257 0.35 10.00 ? 233 HIS   A CA  1 
ATOM   1079 C  CA  B HIS   A 1 142 ? 121.185 -57.700 32.264 0.65 10.01 ? 233 HIS   A CA  1 
ATOM   1080 C  C   . HIS   A 1 142 ? 121.941 -56.391 32.095 1.00 8.65  ? 233 HIS   A C   1 
ATOM   1081 O  O   . HIS   A 1 142 ? 121.675 -55.430 32.824 1.00 9.37  ? 233 HIS   A O   1 
ATOM   1082 C  CB  A HIS   A 1 142 ? 119.705 -57.574 32.058 0.35 11.68 ? 233 HIS   A CB  1 
ATOM   1083 C  CB  B HIS   A 1 142 ? 119.686 -57.453 32.099 0.65 11.17 ? 233 HIS   A CB  1 
ATOM   1084 C  CG  A HIS   A 1 142 ? 118.964 -58.860 32.254 0.35 13.03 ? 233 HIS   A CG  1 
ATOM   1085 C  CG  B HIS   A 1 142 ? 118.875 -58.698 31.903 0.65 13.76 ? 233 HIS   A CG  1 
ATOM   1086 N  ND1 A HIS   A 1 142 ? 118.537 -59.290 33.492 0.35 13.50 ? 233 HIS   A ND1 1 
ATOM   1087 N  ND1 B HIS   A 1 142 ? 117.495 -58.689 31.891 0.65 13.91 ? 233 HIS   A ND1 1 
ATOM   1088 C  CD2 A HIS   A 1 142 ? 118.609 -59.829 31.378 0.35 14.39 ? 233 HIS   A CD2 1 
ATOM   1089 C  CD2 B HIS   A 1 142 ? 119.245 -59.984 31.699 0.65 13.70 ? 233 HIS   A CD2 1 
ATOM   1090 C  CE1 A HIS   A 1 142 ? 117.928 -60.455 33.365 0.35 14.60 ? 233 HIS   A CE1 1 
ATOM   1091 C  CE1 B HIS   A 1 142 ? 117.052 -59.919 31.696 0.65 16.06 ? 233 HIS   A CE1 1 
ATOM   1092 N  NE2 A HIS   A 1 142 ? 117.957 -60.804 32.092 0.35 14.12 ? 233 HIS   A NE2 1 
ATOM   1093 N  NE2 B HIS   A 1 142 ? 118.094 -60.724 31.576 0.65 14.41 ? 233 HIS   A NE2 1 
ATOM   1094 N  N   . TYR   A 1 143 ? 122.866 -56.355 31.142 1.00 9.49  ? 234 TYR   A N   1 
ATOM   1095 C  CA  . TYR   A 1 143 ? 123.629 -55.158 30.822 1.00 8.59  ? 234 TYR   A CA  1 
ATOM   1096 C  C   . TYR   A 1 143 ? 123.093 -54.516 29.545 1.00 9.51  ? 234 TYR   A C   1 
ATOM   1097 O  O   . TYR   A 1 143 ? 122.493 -55.184 28.697 1.00 7.72  ? 234 TYR   A O   1 
ATOM   1098 C  CB  . TYR   A 1 143 ? 125.113 -55.491 30.657 1.00 7.11  ? 234 TYR   A CB  1 
ATOM   1099 C  CG  . TYR   A 1 143 ? 125.806 -55.890 31.946 1.00 7.92  ? 234 TYR   A CG  1 
ATOM   1100 C  CD1 . TYR   A 1 143 ? 126.091 -54.948 32.922 1.00 7.84  ? 234 TYR   A CD1 1 
ATOM   1101 C  CD2 . TYR   A 1 143 ? 126.189 -57.210 32.169 1.00 11.88 ? 234 TYR   A CD2 1 
ATOM   1102 C  CE1 . TYR   A 1 143 ? 126.735 -55.319 34.107 1.00 8.07  ? 234 TYR   A CE1 1 
ATOM   1103 C  CE2 . TYR   A 1 143 ? 126.832 -57.587 33.346 1.00 9.77  ? 234 TYR   A CE2 1 
ATOM   1104 C  CZ  . TYR   A 1 143 ? 127.104 -56.637 34.301 1.00 5.84  ? 234 TYR   A CZ  1 
ATOM   1105 O  OH  . TYR   A 1 143 ? 127.734 -57.003 35.466 1.00 6.65  ? 234 TYR   A OH  1 
ATOM   1106 N  N   . ASN   A 1 144 ? 123.299 -53.201 29.428 1.00 10.50 ? 235 ASN   A N   1 
ATOM   1107 C  CA  . ASN   A 1 144 ? 123.028 -52.444 28.210 1.00 11.41 ? 235 ASN   A CA  1 
ATOM   1108 C  C   . ASN   A 1 144 ? 124.294 -51.684 27.841 1.00 8.18  ? 235 ASN   A C   1 
ATOM   1109 O  O   . ASN   A 1 144 ? 124.917 -51.062 28.709 1.00 11.52 ? 235 ASN   A O   1 
ATOM   1110 C  CB  . ASN   A 1 144 ? 121.893 -51.411 28.366 1.00 12.08 ? 235 ASN   A CB  1 
ATOM   1111 C  CG  . ASN   A 1 144 ? 120.555 -52.008 28.766 1.00 16.08 ? 235 ASN   A CG  1 
ATOM   1112 O  OD1 . ASN   A 1 144 ? 119.745 -51.324 29.392 1.00 22.76 ? 235 ASN   A OD1 1 
ATOM   1113 N  ND2 . ASN   A 1 144 ? 120.296 -53.248 28.385 1.00 15.11 ? 235 ASN   A ND2 1 
ATOM   1114 N  N   . TYR   A 1 145 ? 124.664 -51.710 26.566 1.00 7.91  ? 236 TYR   A N   1 
ATOM   1115 C  CA  . TYR   A 1 145 ? 125.805 -50.956 26.064 1.00 8.39  ? 236 TYR   A CA  1 
ATOM   1116 C  C   . TYR   A 1 145 ? 125.273 -49.760 25.288 1.00 9.60  ? 236 TYR   A C   1 
ATOM   1117 O  O   . TYR   A 1 145 ? 124.456 -49.928 24.373 1.00 9.01  ? 236 TYR   A O   1 
ATOM   1118 C  CB  . TYR   A 1 145 ? 126.698 -51.830 25.182 1.00 8.13  ? 236 TYR   A CB  1 
ATOM   1119 C  CG  . TYR   A 1 145 ? 127.430 -52.890 25.979 1.00 7.68  ? 236 TYR   A CG  1 
ATOM   1120 C  CD1 . TYR   A 1 145 ? 126.825 -54.106 26.266 1.00 7.61  ? 236 TYR   A CD1 1 
ATOM   1121 C  CD2 . TYR   A 1 145 ? 128.709 -52.662 26.464 1.00 12.13 ? 236 TYR   A CD2 1 
ATOM   1122 C  CE1 . TYR   A 1 145 ? 127.479 -55.078 27.012 1.00 8.72  ? 236 TYR   A CE1 1 
ATOM   1123 C  CE2 . TYR   A 1 145 ? 129.375 -53.630 27.217 1.00 7.13  ? 236 TYR   A CE2 1 
ATOM   1124 C  CZ  . TYR   A 1 145 ? 128.749 -54.832 27.491 1.00 13.19 ? 236 TYR   A CZ  1 
ATOM   1125 O  OH  . TYR   A 1 145 ? 129.406 -55.799 28.235 1.00 10.04 ? 236 TYR   A OH  1 
ATOM   1126 N  N   . MET   A 1 146 ? 125.732 -48.562 25.650 1.00 8.65  ? 237 MET   A N   1 
ATOM   1127 C  CA  . MET   A 1 146 ? 125.039 -47.343 25.249 1.00 8.86  ? 237 MET   A CA  1 
ATOM   1128 C  C   . MET   A 1 146 ? 125.731 -46.573 24.126 1.00 9.39  ? 237 MET   A C   1 
ATOM   1129 O  O   . MET   A 1 146 ? 125.317 -45.449 23.828 1.00 10.77 ? 237 MET   A O   1 
ATOM   1130 C  CB  . MET   A 1 146 ? 124.827 -46.435 26.462 1.00 8.60  ? 237 MET   A CB  1 
ATOM   1131 C  CG  . MET   A 1 146 ? 124.014 -47.105 27.594 1.00 8.26  ? 237 MET   A CG  1 
ATOM   1132 S  SD  . MET   A 1 146 ? 122.401 -47.757 27.110 1.00 11.42 ? 237 MET   A SD  1 
ATOM   1133 C  CE  . MET   A 1 146 ? 121.571 -46.274 26.539 1.00 14.07 ? 237 MET   A CE  1 
ATOM   1134 N  N   . CYS   A 1 147 ? 126.758 -47.146 23.499 1.00 9.44  ? 238 CYS   A N   1 
ATOM   1135 C  CA  . CYS   A 1 147 ? 127.332 -46.635 22.253 1.00 10.12 ? 238 CYS   A CA  1 
ATOM   1136 C  C   . CYS   A 1 147 ? 127.595 -47.805 21.322 1.00 11.28 ? 238 CYS   A C   1 
ATOM   1137 O  O   . CYS   A 1 147 ? 127.840 -48.921 21.782 1.00 10.13 ? 238 CYS   A O   1 
ATOM   1138 C  CB  . CYS   A 1 147 ? 128.666 -45.908 22.467 1.00 14.24 ? 238 CYS   A CB  1 
ATOM   1139 S  SG  . CYS   A 1 147 ? 128.558 -44.164 22.812 1.00 11.80 ? 238 CYS   A SG  1 
ATOM   1140 N  N   . TYR   A 1 148 ? 127.576 -47.541 20.010 1.00 11.94 ? 239 TYR   A N   1 
ATOM   1141 C  CA  . TYR   A 1 148 ? 128.097 -48.513 19.062 1.00 11.73 ? 239 TYR   A CA  1 
ATOM   1142 C  C   . TYR   A 1 148 ? 129.613 -48.578 19.150 1.00 11.66 ? 239 TYR   A C   1 
ATOM   1143 O  O   . TYR   A 1 148 ? 130.277 -47.588 19.453 1.00 11.63 ? 239 TYR   A O   1 
ATOM   1144 C  CB  . TYR   A 1 148 ? 127.707 -48.143 17.632 1.00 15.17 ? 239 TYR   A CB  1 
ATOM   1145 C  CG  . TYR   A 1 148 ? 126.259 -48.351 17.320 1.00 16.93 ? 239 TYR   A CG  1 
ATOM   1146 C  CD1 . TYR   A 1 148 ? 125.728 -49.637 17.253 1.00 18.26 ? 239 TYR   A CD1 1 
ATOM   1147 C  CD2 . TYR   A 1 148 ? 125.418 -47.269 17.077 1.00 19.01 ? 239 TYR   A CD2 1 
ATOM   1148 C  CE1 . TYR   A 1 148 ? 124.394 -49.835 16.947 1.00 24.65 ? 239 TYR   A CE1 1 
ATOM   1149 C  CE2 . TYR   A 1 148 ? 124.077 -47.456 16.776 1.00 20.07 ? 239 TYR   A CE2 1 
ATOM   1150 C  CZ  . TYR   A 1 148 ? 123.575 -48.743 16.704 1.00 22.30 ? 239 TYR   A CZ  1 
ATOM   1151 O  OH  . TYR   A 1 148 ? 122.250 -48.953 16.405 1.00 28.61 ? 239 TYR   A OH  1 
ATOM   1152 N  N   . SER   A 1 149 ? 130.171 -49.751 18.833 1.00 12.58 ? 240 SER   A N   1 
ATOM   1153 C  CA  . SER   A 1 149 ? 131.622 -49.850 18.668 1.00 12.01 ? 240 SER   A CA  1 
ATOM   1154 C  C   . SER   A 1 149 ? 132.159 -48.814 17.675 1.00 13.49 ? 240 SER   A C   1 
ATOM   1155 O  O   . SER   A 1 149 ? 133.289 -48.329 17.826 1.00 13.06 ? 240 SER   A O   1 
ATOM   1156 C  CB  . SER   A 1 149 ? 132.003 -51.266 18.215 1.00 12.27 ? 240 SER   A CB  1 
ATOM   1157 O  OG  . SER   A 1 149 ? 131.884 -52.188 19.290 1.00 11.45 ? 240 SER   A OG  1 
ATOM   1158 N  N   . SER   A 1 150 ? 131.363 -48.453 16.669 1.00 13.62 ? 241 SER   A N   1 
ATOM   1159 C  CA  . SER   A 1 150 ? 131.777 -47.519 15.622 1.00 16.34 ? 241 SER   A CA  1 
ATOM   1160 C  C   . SER   A 1 150 ? 131.602 -46.044 15.991 1.00 14.57 ? 241 SER   A C   1 
ATOM   1161 O  O   . SER   A 1 150 ? 131.895 -45.180 15.154 1.00 15.48 ? 241 SER   A O   1 
ATOM   1162 C  CB  . SER   A 1 150 ? 130.980 -47.796 14.346 1.00 18.99 ? 241 SER   A CB  1 
ATOM   1163 O  OG  . SER   A 1 150 ? 129.617 -47.479 14.568 1.00 21.26 ? 241 SER   A OG  1 
ATOM   1164 N  N   . CYS   A 1 151 ? 131.125 -45.721 17.190 1.00 13.64 ? 242 CYS   A N   1 
ATOM   1165 C  CA  . CYS   A 1 151 ? 130.822 -44.327 17.524 1.00 13.66 ? 242 CYS   A CA  1 
ATOM   1166 C  C   . CYS   A 1 151 ? 132.092 -43.476 17.522 1.00 15.67 ? 242 CYS   A C   1 
ATOM   1167 O  O   . CYS   A 1 151 ? 132.996 -43.692 18.337 1.00 14.88 ? 242 CYS   A O   1 
ATOM   1168 C  CB  . CYS   A 1 151 ? 130.138 -44.246 18.892 1.00 12.83 ? 242 CYS   A CB  1 
ATOM   1169 S  SG  . CYS   A 1 151 ? 128.317 -44.473 18.916 1.00 16.08 ? 242 CYS   A SG  1 
ATOM   1170 N  N   . MET   A 1 152 ? 132.138 -42.479 16.636 1.00 14.98 ? 243 MET   A N   1 
ATOM   1171 C  CA  . MET   A 1 152 ? 133.332 -41.648 16.507 1.00 15.54 ? 243 MET   A CA  1 
ATOM   1172 C  C   . MET   A 1 152 ? 133.470 -40.706 17.699 1.00 14.98 ? 243 MET   A C   1 
ATOM   1173 O  O   . MET   A 1 152 ? 132.485 -40.140 18.184 1.00 15.00 ? 243 MET   A O   1 
ATOM   1174 C  CB  . MET   A 1 152 ? 133.292 -40.850 15.201 1.00 19.86 ? 243 MET   A CB  1 
ATOM   1175 C  CG  . MET   A 1 152 ? 133.305 -41.742 13.967 1.00 24.19 ? 243 MET   A CG  1 
ATOM   1176 S  SD  . MET   A 1 152 ? 134.658 -42.956 14.053 1.00 28.67 ? 243 MET   A SD  1 
ATOM   1177 C  CE  . MET   A 1 152 ? 136.033 -41.878 13.612 1.00 30.78 ? 243 MET   A CE  1 
ATOM   1178 N  N   . GLY   A 1 153 ? 134.704 -40.537 18.170 1.00 16.52 ? 244 GLY   A N   1 
ATOM   1179 C  CA  . GLY   A 1 153 ? 134.954 -39.805 19.397 1.00 15.70 ? 244 GLY   A CA  1 
ATOM   1180 C  C   . GLY   A 1 153 ? 134.683 -40.585 20.664 1.00 24.25 ? 244 GLY   A C   1 
ATOM   1181 O  O   . GLY   A 1 153 ? 134.965 -40.078 21.761 1.00 21.94 ? 244 GLY   A O   1 
ATOM   1182 N  N   . GLY   A 1 154 ? 134.117 -41.783 20.557 1.00 17.29 ? 245 GLY   A N   1 
ATOM   1183 C  CA  . GLY   A 1 154 ? 134.052 -42.711 21.669 1.00 14.07 ? 245 GLY   A CA  1 
ATOM   1184 C  C   . GLY   A 1 154 ? 134.929 -43.912 21.370 1.00 14.66 ? 245 GLY   A C   1 
ATOM   1185 O  O   . GLY   A 1 154 ? 136.128 -43.759 21.122 1.00 14.15 ? 245 GLY   A O   1 
ATOM   1186 N  N   . MET   A 1 155 ? 134.339 -45.110 21.344 1.00 11.56 ? 246 MET   A N   1 
ATOM   1187 C  CA  . MET   A 1 155 ? 135.132 -46.304 21.052 1.00 11.69 ? 246 MET   A CA  1 
ATOM   1188 C  C   . MET   A 1 155 ? 135.812 -46.225 19.687 1.00 12.81 ? 246 MET   A C   1 
ATOM   1189 O  O   . MET   A 1 155 ? 136.901 -46.784 19.506 1.00 13.75 ? 246 MET   A O   1 
ATOM   1190 C  CB  . MET   A 1 155 ? 134.247 -47.544 21.167 1.00 16.20 ? 246 MET   A CB  1 
ATOM   1191 C  CG  . MET   A 1 155 ? 133.952 -47.898 22.624 1.00 11.05 ? 246 MET   A CG  1 
ATOM   1192 S  SD  . MET   A 1 155 ? 132.922 -49.367 22.789 1.00 12.51 ? 246 MET   A SD  1 
ATOM   1193 C  CE  . MET   A 1 155 ? 131.294 -48.715 22.405 1.00 10.45 ? 246 MET   A CE  1 
ATOM   1194 N  N   . ASN   A 1 156 ? 135.214 -45.524 18.721 1.00 13.38 ? 247 ASN   A N   1 
ATOM   1195 C  CA  . ASN   A 1 156 ? 135.941 -45.134 17.507 1.00 14.88 ? 247 ASN   A CA  1 
ATOM   1196 C  C   . ASN   A 1 156 ? 136.424 -46.362 16.729 1.00 17.05 ? 247 ASN   A C   1 
ATOM   1197 O  O   . ASN   A 1 156 ? 137.524 -46.373 16.175 1.00 17.84 ? 247 ASN   A O   1 
ATOM   1198 C  CB  . ASN   A 1 156 ? 137.124 -44.221 17.868 1.00 19.46 ? 247 ASN   A CB  1 
ATOM   1199 C  CG  . ASN   A 1 156 ? 137.298 -43.055 16.911 1.00 24.10 ? 247 ASN   A CG  1 
ATOM   1200 O  OD1 . ASN   A 1 156 ? 136.591 -42.048 17.005 1.00 25.09 ? 247 ASN   A OD1 1 
ATOM   1201 N  ND2 . ASN   A 1 156 ? 138.266 -43.170 16.004 1.00 24.95 ? 247 ASN   A ND2 1 
ATOM   1202 N  N   . ARG   A 1 157 ? 135.598 -47.413 16.702 1.00 17.22 ? 248 ARG   A N   1 
ATOM   1203 C  CA  . ARG   A 1 157 ? 135.862 -48.710 16.071 1.00 15.06 ? 248 ARG   A CA  1 
ATOM   1204 C  C   . ARG   A 1 157 ? 136.931 -49.529 16.797 1.00 20.36 ? 248 ARG   A C   1 
ATOM   1205 O  O   . ARG   A 1 157 ? 137.383 -50.551 16.268 1.00 22.55 ? 248 ARG   A O   1 
ATOM   1206 C  CB  . ARG   A 1 157 ? 136.235 -48.563 14.582 1.00 21.56 ? 248 ARG   A CB  1 
ATOM   1207 C  CG  . ARG   A 1 157 ? 135.360 -47.562 13.837 1.00 23.17 ? 248 ARG   A CG  1 
ATOM   1208 C  CD  . ARG   A 1 157 ? 135.639 -47.509 12.333 1.00 35.55 ? 248 ARG   A CD  1 
ATOM   1209 N  NE  . ARG   A 1 157 ? 134.911 -48.567 11.641 1.00 45.12 ? 248 ARG   A NE  1 
ATOM   1210 C  CZ  . ARG   A 1 157 ? 133.680 -48.438 11.146 1.00 52.74 ? 248 ARG   A CZ  1 
ATOM   1211 N  NH1 . ARG   A 1 157 ? 133.098 -49.465 10.542 1.00 58.78 ? 248 ARG   A NH1 1 
ATOM   1212 N  NH2 . ARG   A 1 157 ? 133.031 -47.283 11.247 1.00 50.46 ? 248 ARG   A NH2 1 
ATOM   1213 N  N   . ARG   A 1 158 ? 137.329 -49.136 18.016 1.00 14.02 ? 249 ARG   A N   1 
ATOM   1214 C  CA  . ARG   A 1 158 ? 138.317 -49.917 18.759 1.00 13.80 ? 249 ARG   A CA  1 
ATOM   1215 C  C   . ARG   A 1 158 ? 137.627 -51.019 19.567 1.00 13.01 ? 249 ARG   A C   1 
ATOM   1216 O  O   . ARG   A 1 158 ? 136.610 -50.757 20.221 1.00 12.74 ? 249 ARG   A O   1 
ATOM   1217 C  CB  . ARG   A 1 158 ? 139.127 -49.014 19.692 1.00 13.63 ? 249 ARG   A CB  1 
ATOM   1218 C  CG  . ARG   A 1 158 ? 139.973 -47.977 18.922 1.00 15.77 ? 249 ARG   A CG  1 
ATOM   1219 C  CD  . ARG   A 1 158 ? 140.573 -46.902 19.845 1.00 18.74 ? 249 ARG   A CD  1 
ATOM   1220 N  NE  . ARG   A 1 158 ? 139.565 -46.048 20.473 1.00 16.05 ? 249 ARG   A NE  1 
ATOM   1221 C  CZ  . ARG   A 1 158 ? 139.841 -45.131 21.394 1.00 17.76 ? 249 ARG   A CZ  1 
ATOM   1222 N  NH1 . ARG   A 1 158 ? 141.101 -44.953 21.793 1.00 14.09 ? 249 ARG   A NH1 1 
ATOM   1223 N  NH2 . ARG   A 1 158 ? 138.867 -44.390 21.911 1.00 13.02 ? 249 ARG   A NH2 1 
ATOM   1224 N  N   . PRO   A 1 159 ? 138.135 -52.248 19.544 1.00 13.01 ? 250 PRO   A N   1 
ATOM   1225 C  CA  . PRO   A 1 159 ? 137.521 -53.311 20.354 1.00 14.04 ? 250 PRO   A CA  1 
ATOM   1226 C  C   . PRO   A 1 159 ? 137.713 -53.068 21.844 1.00 11.35 ? 250 PRO   A C   1 
ATOM   1227 O  O   . PRO   A 1 159 ? 138.736 -52.539 22.287 1.00 11.55 ? 250 PRO   A O   1 
ATOM   1228 C  CB  . PRO   A 1 159 ? 138.260 -54.579 19.905 1.00 16.84 ? 250 PRO   A CB  1 
ATOM   1229 C  CG  . PRO   A 1 159 ? 139.556 -54.075 19.301 1.00 19.46 ? 250 PRO   A CG  1 
ATOM   1230 C  CD  . PRO   A 1 159 ? 139.253 -52.737 18.713 1.00 16.39 ? 250 PRO   A CD  1 
ATOM   1231 N  N   . ILE   A 1 160 ? 136.712 -53.479 22.625 1.00 10.52 ? 251 ILE   A N   1 
ATOM   1232 C  CA  . ILE   A 1 160 ? 136.767 -53.382 24.077 1.00 9.79  ? 251 ILE   A CA  1 
ATOM   1233 C  C   . ILE   A 1 160 ? 136.572 -54.763 24.682 1.00 9.42  ? 251 ILE   A C   1 
ATOM   1234 O  O   . ILE   A 1 160 ? 135.995 -55.670 24.073 1.00 9.55  ? 251 ILE   A O   1 
ATOM   1235 C  CB  . ILE   A 1 160 ? 135.712 -52.414 24.652 1.00 9.20  ? 251 ILE   A CB  1 
ATOM   1236 C  CG1 . ILE   A 1 160 ? 134.301 -52.909 24.314 1.00 13.03 ? 251 ILE   A CG1 1 
ATOM   1237 C  CG2 . ILE   A 1 160 ? 135.961 -50.985 24.145 1.00 9.61  ? 251 ILE   A CG2 1 
ATOM   1238 C  CD1 . ILE   A 1 160 ? 133.231 -52.394 25.269 1.00 10.34 ? 251 ILE   A CD1 1 
ATOM   1239 N  N   . LEU   A 1 161 ? 137.069 -54.906 25.901 1.00 9.06  ? 252 LEU   A N   1 
ATOM   1240 C  CA  . LEU   A 1 161 ? 136.706 -55.985 26.806 1.00 9.45  ? 252 LEU   A CA  1 
ATOM   1241 C  C   . LEU   A 1 161 ? 135.778 -55.441 27.884 1.00 9.07  ? 252 LEU   A C   1 
ATOM   1242 O  O   . LEU   A 1 161 ? 135.895 -54.287 28.297 1.00 11.69 ? 252 LEU   A O   1 
ATOM   1243 C  CB  . LEU   A 1 161 ? 137.945 -56.582 27.480 1.00 12.13 ? 252 LEU   A CB  1 
ATOM   1244 C  CG  . LEU   A 1 161 ? 139.092 -56.923 26.546 1.00 23.62 ? 252 LEU   A CG  1 
ATOM   1245 C  CD1 . LEU   A 1 161 ? 140.228 -57.531 27.343 1.00 28.76 ? 252 LEU   A CD1 1 
ATOM   1246 C  CD2 . LEU   A 1 161 ? 138.601 -57.876 25.459 1.00 24.04 ? 252 LEU   A CD2 1 
ATOM   1247 N  N   . THR   A 1 162 ? 134.857 -56.280 28.339 1.00 7.68  ? 253 THR   A N   1 
ATOM   1248 C  CA  . THR   A 1 162 ? 134.166 -56.044 29.596 1.00 6.98  ? 253 THR   A CA  1 
ATOM   1249 C  C   . THR   A 1 162 ? 134.806 -56.939 30.641 1.00 11.39 ? 253 THR   A C   1 
ATOM   1250 O  O   . THR   A 1 162 ? 134.955 -58.143 30.413 1.00 9.30  ? 253 THR   A O   1 
ATOM   1251 C  CB  . THR   A 1 162 ? 132.669 -56.323 29.483 1.00 8.62  ? 253 THR   A CB  1 
ATOM   1252 O  OG1 . THR   A 1 162 ? 132.103 -55.414 28.525 1.00 10.92 ? 253 THR   A OG1 1 
ATOM   1253 C  CG2 . THR   A 1 162 ? 131.982 -56.134 30.847 1.00 9.15  ? 253 THR   A CG2 1 
ATOM   1254 N  N   . ILE   A 1 163 ? 135.248 -56.340 31.748 1.00 7.52  ? 254 ILE   A N   1 
ATOM   1255 C  CA  . ILE   A 1 163 ? 135.795 -57.083 32.878 1.00 6.81  ? 254 ILE   A CA  1 
ATOM   1256 C  C   . ILE   A 1 163 ? 134.707 -57.174 33.934 1.00 6.41  ? 254 ILE   A C   1 
ATOM   1257 O  O   . ILE   A 1 163 ? 134.193 -56.150 34.396 1.00 6.22  ? 254 ILE   A O   1 
ATOM   1258 C  CB  . ILE   A 1 163 ? 137.048 -56.406 33.453 1.00 7.75  ? 254 ILE   A CB  1 
ATOM   1259 C  CG1 . ILE   A 1 163 ? 138.119 -56.233 32.375 1.00 11.76 ? 254 ILE   A CG1 1 
ATOM   1260 C  CG2 . ILE   A 1 163 ? 137.580 -57.212 34.643 1.00 7.26  ? 254 ILE   A CG2 1 
ATOM   1261 C  CD1 . ILE   A 1 163 ? 139.251 -55.331 32.800 1.00 19.33 ? 254 ILE   A CD1 1 
ATOM   1262 N  N   . ILE   A 1 164 ? 134.366 -58.389 34.346 1.00 6.38  ? 255 ILE   A N   1 
ATOM   1263 C  CA  . ILE   A 1 164 ? 133.398 -58.606 35.411 1.00 6.16  ? 255 ILE   A CA  1 
ATOM   1264 C  C   . ILE   A 1 164 ? 134.159 -59.062 36.646 1.00 10.98 ? 255 ILE   A C   1 
ATOM   1265 O  O   . ILE   A 1 164 ? 134.913 -60.042 36.586 1.00 6.64  ? 255 ILE   A O   1 
ATOM   1266 C  CB  . ILE   A 1 164 ? 132.340 -59.652 35.025 1.00 6.55  ? 255 ILE   A CB  1 
ATOM   1267 C  CG1 . ILE   A 1 164 ? 131.620 -59.262 33.734 1.00 6.07  ? 255 ILE   A CG1 1 
ATOM   1268 C  CG2 . ILE   A 1 164 ? 131.348 -59.803 36.156 1.00 6.59  ? 255 ILE   A CG2 1 
ATOM   1269 C  CD1 . ILE   A 1 164 ? 130.888 -57.936 33.813 1.00 5.88  ? 255 ILE   A CD1 1 
ATOM   1270 N  N   . THR   A 1 165 ? 133.959 -58.374 37.767 1.00 7.85  ? 256 THR   A N   1 
ATOM   1271 C  CA  A THR   A 1 165 ? 134.637 -58.751 38.998 0.62 7.25  ? 256 THR   A CA  1 
ATOM   1272 C  CA  B THR   A 1 165 ? 134.645 -58.687 39.015 0.38 7.96  ? 256 THR   A CA  1 
ATOM   1273 C  C   . THR   A 1 165 ? 133.631 -59.030 40.097 1.00 8.18  ? 256 THR   A C   1 
ATOM   1274 O  O   . THR   A 1 165 ? 132.653 -58.295 40.282 1.00 7.50  ? 256 THR   A O   1 
ATOM   1275 C  CB  A THR   A 1 165 ? 135.605 -57.684 39.481 0.62 10.97 ? 256 THR   A CB  1 
ATOM   1276 C  CB  B THR   A 1 165 ? 135.506 -57.506 39.469 0.38 10.28 ? 256 THR   A CB  1 
ATOM   1277 O  OG1 A THR   A 1 165 ? 134.938 -56.424 39.514 0.62 9.77  ? 256 THR   A OG1 1 
ATOM   1278 O  OG1 B THR   A 1 165 ? 136.547 -57.275 38.510 0.38 13.53 ? 256 THR   A OG1 1 
ATOM   1279 C  CG2 A THR   A 1 165 ? 136.832 -57.619 38.570 0.62 12.33 ? 256 THR   A CG2 1 
ATOM   1280 C  CG2 B THR   A 1 165 ? 136.128 -57.787 40.823 0.38 9.58  ? 256 THR   A CG2 1 
ATOM   1281 N  N   . LEU   A 1 166 ? 133.881 -60.120 40.810 1.00 7.59  ? 257 LEU   A N   1 
ATOM   1282 C  CA  . LEU   A 1 166 ? 133.166 -60.450 42.026 1.00 11.67 ? 257 LEU   A CA  1 
ATOM   1283 C  C   . LEU   A 1 166 ? 133.945 -59.824 43.179 1.00 11.15 ? 257 LEU   A C   1 
ATOM   1284 O  O   . LEU   A 1 166 ? 135.165 -59.994 43.265 1.00 12.85 ? 257 LEU   A O   1 
ATOM   1285 C  CB  . LEU   A 1 166 ? 133.071 -61.970 42.181 1.00 7.32  ? 257 LEU   A CB  1 
ATOM   1286 C  CG  . LEU   A 1 166 ? 132.138 -62.528 43.257 1.00 10.21 ? 257 LEU   A CG  1 
ATOM   1287 C  CD1 . LEU   A 1 166 ? 130.692 -62.314 42.845 1.00 8.69  ? 257 LEU   A CD1 1 
ATOM   1288 C  CD2 . LEU   A 1 166 ? 132.423 -64.012 43.462 1.00 9.68  ? 257 LEU   A CD2 1 
ATOM   1289 N  N   . GLU   A 1 167 ? 133.255 -59.073 44.037 1.00 8.97  ? 258 GLU   A N   1 
ATOM   1290 C  CA  . GLU   A 1 167 ? 133.895 -58.279 45.073 1.00 8.49  ? 258 GLU   A CA  1 
ATOM   1291 C  C   . GLU   A 1 167 ? 133.205 -58.524 46.402 1.00 8.43  ? 258 GLU   A C   1 
ATOM   1292 O  O   . GLU   A 1 167 ? 131.987 -58.708 46.451 1.00 8.88  ? 258 GLU   A O   1 
ATOM   1293 C  CB  . GLU   A 1 167 ? 133.809 -56.755 44.813 1.00 9.47  ? 258 GLU   A CB  1 
ATOM   1294 C  CG  . GLU   A 1 167 ? 134.404 -56.234 43.539 1.00 14.27 ? 258 GLU   A CG  1 
ATOM   1295 C  CD  . GLU   A 1 167 ? 134.140 -54.731 43.356 1.00 18.03 ? 258 GLU   A CD  1 
ATOM   1296 O  OE1 . GLU   A 1 167 ? 133.249 -54.160 44.040 1.00 16.83 ? 258 GLU   A OE1 1 
ATOM   1297 O  OE2 . GLU   A 1 167 ? 134.840 -54.123 42.530 1.00 16.99 ? 258 GLU   A OE2 1 
ATOM   1298 N  N   . ASP   A 1 168 ? 133.966 -58.447 47.484 1.00 9.07  ? 259 ASP   A N   1 
ATOM   1299 C  CA  . ASP   A 1 168 ? 133.298 -58.431 48.779 1.00 9.62  ? 259 ASP   A CA  1 
ATOM   1300 C  C   . ASP   A 1 168 ? 132.689 -57.052 49.037 1.00 9.62  ? 259 ASP   A C   1 
ATOM   1301 O  O   . ASP   A 1 168 ? 132.789 -56.131 48.219 1.00 10.29 ? 259 ASP   A O   1 
ATOM   1302 C  CB  . ASP   A 1 168 ? 134.249 -58.879 49.890 1.00 10.44 ? 259 ASP   A CB  1 
ATOM   1303 C  CG  . ASP   A 1 168 ? 135.389 -57.897 50.170 1.00 15.52 ? 259 ASP   A CG  1 
ATOM   1304 O  OD1 . ASP   A 1 168 ? 135.340 -56.707 49.801 1.00 13.38 ? 259 ASP   A OD1 1 
ATOM   1305 O  OD2 . ASP   A 1 168 ? 136.359 -58.341 50.812 1.00 18.39 ? 259 ASP   A OD2 1 
ATOM   1306 N  N   . SER   A 1 169 ? 132.050 -56.894 50.198 1.00 10.22 ? 260 SER   A N   1 
ATOM   1307 C  CA  . SER   A 1 169 ? 131.353 -55.642 50.480 1.00 10.34 ? 260 SER   A CA  1 
ATOM   1308 C  C   . SER   A 1 169 ? 132.295 -54.441 50.572 1.00 12.74 ? 260 SER   A C   1 
ATOM   1309 O  O   . SER   A 1 169 ? 131.838 -53.299 50.425 1.00 13.83 ? 260 SER   A O   1 
ATOM   1310 C  CB  . SER   A 1 169 ? 130.534 -55.781 51.768 1.00 11.13 ? 260 SER   A CB  1 
ATOM   1311 O  OG  . SER   A 1 169 ? 131.355 -56.062 52.886 1.00 14.13 ? 260 SER   A OG  1 
ATOM   1312 N  N   . SER   A 1 170 ? 133.588 -54.660 50.817 1.00 11.45 ? 261 SER   A N   1 
ATOM   1313 C  CA  . SER   A 1 170 ? 134.576 -53.583 50.807 1.00 11.12 ? 261 SER   A CA  1 
ATOM   1314 C  C   . SER   A 1 170 ? 135.136 -53.286 49.422 1.00 14.69 ? 261 SER   A C   1 
ATOM   1315 O  O   . SER   A 1 170 ? 135.887 -52.313 49.274 1.00 14.39 ? 261 SER   A O   1 
ATOM   1316 C  CB  . SER   A 1 170 ? 135.749 -53.916 51.731 1.00 13.43 ? 261 SER   A CB  1 
ATOM   1317 O  OG  . SER   A 1 170 ? 135.373 -53.873 53.094 1.00 15.38 ? 261 SER   A OG  1 
ATOM   1318 N  N   . GLY   A 1 171 ? 134.813 -54.098 48.422 1.00 14.33 ? 262 GLY   A N   1 
ATOM   1319 C  CA  . GLY   A 1 171 ? 135.391 -53.960 47.097 1.00 14.13 ? 262 GLY   A CA  1 
ATOM   1320 C  C   . GLY   A 1 171 ? 136.624 -54.799 46.839 1.00 14.87 ? 262 GLY   A C   1 
ATOM   1321 O  O   . GLY   A 1 171 ? 137.240 -54.649 45.776 1.00 15.42 ? 262 GLY   A O   1 
ATOM   1322 N  N   . ASN   A 1 172 ? 137.014 -55.663 47.774 1.00 9.97  ? 263 ASN   A N   1 
ATOM   1323 C  CA  . ASN   A 1 172 ? 138.159 -56.541 47.561 1.00 10.60 ? 263 ASN   A CA  1 
ATOM   1324 C  C   . ASN   A 1 172 ? 137.833 -57.629 46.544 1.00 11.41 ? 263 ASN   A C   1 
ATOM   1325 O  O   . ASN   A 1 172 ? 136.714 -58.139 46.486 1.00 9.30  ? 263 ASN   A O   1 
ATOM   1326 C  CB  . ASN   A 1 172 ? 138.589 -57.201 48.868 1.00 11.13 ? 263 ASN   A CB  1 
ATOM   1327 C  CG  . ASN   A 1 172 ? 139.009 -56.196 49.914 1.00 20.00 ? 263 ASN   A CG  1 
ATOM   1328 O  OD1 . ASN   A 1 172 ? 139.735 -55.248 49.621 1.00 21.96 ? 263 ASN   A OD1 1 
ATOM   1329 N  ND2 . ASN   A 1 172 ? 138.532 -56.384 51.140 1.00 23.91 ? 263 ASN   A ND2 1 
ATOM   1330 N  N   . LEU   A 1 173 ? 138.847 -58.020 45.780 1.00 10.05 ? 264 LEU   A N   1 
ATOM   1331 C  CA  . LEU   A 1 173 ? 138.661 -58.970 44.690 1.00 14.80 ? 264 LEU   A CA  1 
ATOM   1332 C  C   . LEU   A 1 173 ? 138.363 -60.368 45.217 1.00 12.67 ? 264 LEU   A C   1 
ATOM   1333 O  O   . LEU   A 1 173 ? 139.105 -60.898 46.046 1.00 10.89 ? 264 LEU   A O   1 
ATOM   1334 C  CB  . LEU   A 1 173 ? 139.913 -59.013 43.812 1.00 16.16 ? 264 LEU   A CB  1 
ATOM   1335 C  CG  . LEU   A 1 173 ? 139.866 -60.058 42.685 1.00 17.64 ? 264 LEU   A CG  1 
ATOM   1336 C  CD1 . LEU   A 1 173 ? 139.011 -59.565 41.559 1.00 14.24 ? 264 LEU   A CD1 1 
ATOM   1337 C  CD2 . LEU   A 1 173 ? 141.253 -60.401 42.184 1.00 22.16 ? 264 LEU   A CD2 1 
ATOM   1338 N  N   . LEU   A 1 174 ? 137.272 -60.963 44.732 1.00 9.02  ? 265 LEU   A N   1 
ATOM   1339 C  CA  . LEU   A 1 174 ? 136.981 -62.377 44.954 1.00 9.21  ? 265 LEU   A CA  1 
ATOM   1340 C  C   . LEU   A 1 174 ? 137.083 -63.217 43.689 1.00 10.28 ? 265 LEU   A C   1 
ATOM   1341 O  O   . LEU   A 1 174 ? 137.315 -64.422 43.788 1.00 9.36  ? 265 LEU   A O   1 
ATOM   1342 C  CB  . LEU   A 1 174 ? 135.570 -62.558 45.537 1.00 9.04  ? 265 LEU   A CB  1 
ATOM   1343 C  CG  . LEU   A 1 174 ? 135.278 -61.810 46.851 1.00 11.08 ? 265 LEU   A CG  1 
ATOM   1344 C  CD1 . LEU   A 1 174 ? 133.817 -62.001 47.275 1.00 13.39 ? 265 LEU   A CD1 1 
ATOM   1345 C  CD2 . LEU   A 1 174 ? 136.207 -62.295 47.935 1.00 11.40 ? 265 LEU   A CD2 1 
ATOM   1346 N  N   . GLY   A 1 175 ? 136.913 -62.615 42.516 1.00 8.45  ? 266 GLY   A N   1 
ATOM   1347 C  CA  . GLY   A 1 175 ? 136.928 -63.366 41.269 1.00 9.18  ? 266 GLY   A CA  1 
ATOM   1348 C  C   . GLY   A 1 175 ? 136.845 -62.412 40.104 1.00 9.76  ? 266 GLY   A C   1 
ATOM   1349 O  O   . GLY   A 1 175 ? 136.400 -61.267 40.250 1.00 12.37 ? 266 GLY   A O   1 
ATOM   1350 N  N   . ARG   A 1 176 ? 137.288 -62.893 38.939 1.00 7.96  ? 267 ARG   A N   1 
ATOM   1351 C  CA  . ARG   A 1 176 ? 137.322 -62.040 37.760 1.00 7.71  ? 267 ARG   A CA  1 
ATOM   1352 C  C   . ARG   A 1 176 ? 137.186 -62.869 36.489 1.00 10.90 ? 267 ARG   A C   1 
ATOM   1353 O  O   . ARG   A 1 176 ? 137.763 -63.955 36.388 1.00 8.20  ? 267 ARG   A O   1 
ATOM   1354 C  CB  . ARG   A 1 176 ? 138.628 -61.225 37.702 1.00 9.83  ? 267 ARG   A CB  1 
ATOM   1355 C  CG  . ARG   A 1 176 ? 138.667 -60.241 36.542 1.00 10.84 ? 267 ARG   A CG  1 
ATOM   1356 C  CD  . ARG   A 1 176 ? 140.033 -59.600 36.360 1.00 13.50 ? 267 ARG   A CD  1 
ATOM   1357 N  NE  . ARG   A 1 176 ? 140.475 -58.841 37.525 1.00 18.15 ? 267 ARG   A NE  1 
ATOM   1358 C  CZ  . ARG   A 1 176 ? 141.480 -59.197 38.321 1.00 23.06 ? 267 ARG   A CZ  1 
ATOM   1359 N  NH1 . ARG   A 1 176 ? 142.166 -60.315 38.098 1.00 18.83 ? 267 ARG   A NH1 1 
ATOM   1360 N  NH2 . ARG   A 1 176 ? 141.800 -58.422 39.345 1.00 24.25 ? 267 ARG   A NH2 1 
ATOM   1361 N  N   . ASP   A 1 177 ? 136.459 -62.319 35.509 1.00 7.43  ? 268 ASP   A N   1 
ATOM   1362 C  CA  . ASP   A 1 177 ? 136.291 -62.928 34.192 1.00 7.57  ? 268 ASP   A CA  1 
ATOM   1363 C  C   . ASP   A 1 177 ? 136.133 -61.779 33.204 1.00 7.41  ? 268 ASP   A C   1 
ATOM   1364 O  O   . ASP   A 1 177 ? 136.041 -60.613 33.600 1.00 8.06  ? 268 ASP   A O   1 
ATOM   1365 C  CB  . ASP   A 1 177 ? 135.078 -63.872 34.160 1.00 7.43  ? 268 ASP   A CB  1 
ATOM   1366 C  CG  . ASP   A 1 177 ? 135.182 -64.973 33.103 1.00 12.43 ? 268 ASP   A CG  1 
ATOM   1367 O  OD1 . ASP   A 1 177 ? 136.008 -64.871 32.162 1.00 12.10 ? 268 ASP   A OD1 1 
ATOM   1368 O  OD2 . ASP   A 1 177 ? 134.410 -65.950 33.221 1.00 13.07 ? 268 ASP   A OD2 1 
ATOM   1369 N  N   . SER   A 1 178 ? 136.126 -62.100 31.915 1.00 9.49  ? 269 SER   A N   1 
ATOM   1370 C  CA  . SER   A 1 178 ? 136.046 -61.038 30.919 1.00 9.11  ? 269 SER   A CA  1 
ATOM   1371 C  C   . SER   A 1 178 ? 135.644 -61.611 29.566 1.00 8.22  ? 269 SER   A C   1 
ATOM   1372 O  O   . SER   A 1 178 ? 135.747 -62.816 29.315 1.00 11.43 ? 269 SER   A O   1 
ATOM   1373 C  CB  . SER   A 1 178 ? 137.384 -60.281 30.797 1.00 8.73  ? 269 SER   A CB  1 
ATOM   1374 O  OG  . SER   A 1 178 ? 138.405 -61.139 30.302 1.00 8.66  ? 269 SER   A OG  1 
ATOM   1375 N  N   . PHE   A 1 179 ? 135.195 -60.712 28.689 1.00 8.92  ? 270 PHE   A N   1 
ATOM   1376 C  CA  . PHE   A 1 179 ? 134.797 -61.069 27.334 1.00 8.77  ? 270 PHE   A CA  1 
ATOM   1377 C  C   . PHE   A 1 179 ? 134.903 -59.824 26.469 1.00 9.59  ? 270 PHE   A C   1 
ATOM   1378 O  O   . PHE   A 1 179 ? 134.711 -58.704 26.953 1.00 10.41 ? 270 PHE   A O   1 
ATOM   1379 C  CB  . PHE   A 1 179 ? 133.371 -61.631 27.290 1.00 8.17  ? 270 PHE   A CB  1 
ATOM   1380 C  CG  . PHE   A 1 179 ? 132.327 -60.732 27.958 1.00 7.61  ? 270 PHE   A CG  1 
ATOM   1381 C  CD1 . PHE   A 1 179 ? 132.112 -60.787 29.322 1.00 7.78  ? 270 PHE   A CD1 1 
ATOM   1382 C  CD2 . PHE   A 1 179 ? 131.560 -59.850 27.205 1.00 8.05  ? 270 PHE   A CD2 1 
ATOM   1383 C  CE1 . PHE   A 1 179 ? 131.155 -59.981 29.935 1.00 7.19  ? 270 PHE   A CE1 1 
ATOM   1384 C  CE2 . PHE   A 1 179 ? 130.590 -59.029 27.814 1.00 10.11 ? 270 PHE   A CE2 1 
ATOM   1385 C  CZ  . PHE   A 1 179 ? 130.387 -59.103 29.174 1.00 10.75 ? 270 PHE   A CZ  1 
ATOM   1386 N  N   . GLU   A 1 180 ? 135.194 -60.034 25.192 1.00 9.19  ? 271 GLU   A N   1 
ATOM   1387 C  CA  . GLU   A 1 180 ? 135.195 -58.941 24.227 1.00 9.50  ? 271 GLU   A CA  1 
ATOM   1388 C  C   . GLU   A 1 180 ? 133.754 -58.572 23.863 1.00 9.29  ? 271 GLU   A C   1 
ATOM   1389 O  O   . GLU   A 1 180 ? 132.839 -59.399 23.967 1.00 9.17  ? 271 GLU   A O   1 
ATOM   1390 C  CB  . GLU   A 1 180 ? 136.000 -59.358 22.988 1.00 10.44 ? 271 GLU   A CB  1 
ATOM   1391 C  CG  . GLU   A 1 180 ? 136.160 -58.270 21.951 1.00 12.12 ? 271 GLU   A CG  1 
ATOM   1392 C  CD  . GLU   A 1 180 ? 137.127 -58.629 20.834 1.00 19.51 ? 271 GLU   A CD  1 
ATOM   1393 O  OE1 . GLU   A 1 180 ? 137.917 -59.589 20.991 1.00 18.56 ? 271 GLU   A OE1 1 
ATOM   1394 O  OE2 . GLU   A 1 180 ? 137.088 -57.938 19.795 1.00 20.06 ? 271 GLU   A OE2 1 
ATOM   1395 N  N   . VAL   A 1 181 ? 133.542 -57.316 23.448 1.00 9.34  ? 272 VAL   A N   1 
ATOM   1396 C  CA  . VAL   A 1 181 ? 132.200 -56.835 23.114 1.00 9.25  ? 272 VAL   A CA  1 
ATOM   1397 C  C   . VAL   A 1 181 ? 132.245 -56.088 21.790 1.00 10.87 ? 272 VAL   A C   1 
ATOM   1398 O  O   . VAL   A 1 181 ? 133.123 -55.247 21.576 1.00 11.91 ? 272 VAL   A O   1 
ATOM   1399 C  CB  . VAL   A 1 181 ? 131.613 -55.917 24.205 1.00 15.72 ? 272 VAL   A CB  1 
ATOM   1400 C  CG1 . VAL   A 1 181 ? 130.220 -55.394 23.771 1.00 13.18 ? 272 VAL   A CG1 1 
ATOM   1401 C  CG2 . VAL   A 1 181 ? 131.523 -56.642 25.528 1.00 16.53 ? 272 VAL   A CG2 1 
ATOM   1402 N  N   . ARG   A 1 182 ? 131.296 -56.384 20.910 1.00 10.56 ? 273 ARG   A N   1 
ATOM   1403 C  CA  . ARG   A 1 182 ? 131.030 -55.540 19.751 1.00 12.54 ? 273 ARG   A CA  1 
ATOM   1404 C  C   . ARG   A 1 182 ? 129.577 -55.088 19.806 1.00 14.34 ? 273 ARG   A C   1 
ATOM   1405 O  O   . ARG   A 1 182 ? 128.663 -55.919 19.793 1.00 14.82 ? 273 ARG   A O   1 
ATOM   1406 C  CB  . ARG   A 1 182 ? 131.320 -56.285 18.449 1.00 13.45 ? 273 ARG   A CB  1 
ATOM   1407 C  CG  . ARG   A 1 182 ? 130.973 -55.491 17.203 1.00 16.95 ? 273 ARG   A CG  1 
ATOM   1408 C  CD  . ARG   A 1 182 ? 131.432 -56.219 15.967 1.00 15.57 ? 273 ARG   A CD  1 
ATOM   1409 N  NE  . ARG   A 1 182 ? 130.802 -55.679 14.761 1.00 20.20 ? 273 ARG   A NE  1 
ATOM   1410 C  CZ  . ARG   A 1 182 ? 131.181 -54.565 14.151 1.00 33.48 ? 273 ARG   A CZ  1 
ATOM   1411 N  NH1 . ARG   A 1 182 ? 132.194 -53.851 14.631 1.00 36.92 ? 273 ARG   A NH1 1 
ATOM   1412 N  NH2 . ARG   A 1 182 ? 130.543 -54.166 13.056 1.00 38.55 ? 273 ARG   A NH2 1 
ATOM   1413 N  N   . VAL   A 1 183 ? 129.361 -53.780 19.872 1.00 12.91 ? 274 VAL   A N   1 
ATOM   1414 C  CA  . VAL   A 1 183 ? 128.019 -53.216 19.824 1.00 11.88 ? 274 VAL   A CA  1 
ATOM   1415 C  C   . VAL   A 1 183 ? 127.771 -52.786 18.390 1.00 12.46 ? 274 VAL   A C   1 
ATOM   1416 O  O   . VAL   A 1 183 ? 128.483 -51.923 17.867 1.00 14.87 ? 274 VAL   A O   1 
ATOM   1417 C  CB  . VAL   A 1 183 ? 127.860 -52.041 20.798 1.00 13.10 ? 274 VAL   A CB  1 
ATOM   1418 C  CG1 . VAL   A 1 183 ? 126.383 -51.701 20.986 1.00 10.35 ? 274 VAL   A CG1 1 
ATOM   1419 C  CG2 . VAL   A 1 183 ? 128.536 -52.367 22.133 1.00 9.49  ? 274 VAL   A CG2 1 
ATOM   1420 N  N   . CYS   A 1 184 ? 126.776 -53.392 17.747 1.00 12.46 ? 275 CYS   A N   1 
ATOM   1421 C  CA  . CYS   A 1 184 ? 126.616 -53.252 16.307 1.00 13.60 ? 275 CYS   A CA  1 
ATOM   1422 C  C   . CYS   A 1 184 ? 125.146 -53.391 15.942 1.00 21.13 ? 275 CYS   A C   1 
ATOM   1423 O  O   . CYS   A 1 184 ? 124.317 -53.821 16.749 1.00 20.90 ? 275 CYS   A O   1 
ATOM   1424 C  CB  . CYS   A 1 184 ? 127.451 -54.292 15.553 1.00 15.73 ? 275 CYS   A CB  1 
ATOM   1425 S  SG  . CYS   A 1 184 ? 127.071 -56.006 16.060 1.00 18.94 ? 275 CYS   A SG  1 
ATOM   1426 N  N   . ALA   A 1 185 ? 124.835 -53.043 14.694 1.00 15.22 ? 276 ALA   A N   1 
ATOM   1427 C  CA  . ALA   A 1 185 ? 123.446 -53.073 14.244 1.00 18.41 ? 276 ALA   A CA  1 
ATOM   1428 C  C   . ALA   A 1 185 ? 122.923 -54.491 14.028 1.00 20.96 ? 276 ALA   A C   1 
ATOM   1429 O  O   . ALA   A 1 185 ? 121.745 -54.749 14.294 1.00 19.36 ? 276 ALA   A O   1 
ATOM   1430 C  CB  . ALA   A 1 185 ? 123.296 -52.262 12.958 1.00 22.25 ? 276 ALA   A CB  1 
ATOM   1431 N  N   . CYS   A 1 186 ? 123.757 -55.426 13.563 1.00 17.05 ? 277 CYS   A N   1 
ATOM   1432 C  CA  A CYS   A 1 186 ? 123.320 -56.792 13.271 0.67 21.38 ? 277 CYS   A CA  1 
ATOM   1433 C  CA  B CYS   A 1 186 ? 123.327 -56.792 13.262 0.33 21.58 ? 277 CYS   A CA  1 
ATOM   1434 C  C   . CYS   A 1 186 ? 124.273 -57.794 13.910 1.00 21.23 ? 277 CYS   A C   1 
ATOM   1435 O  O   . CYS   A 1 186 ? 125.155 -58.352 13.240 1.00 16.93 ? 277 CYS   A O   1 
ATOM   1436 C  CB  A CYS   A 1 186 ? 123.207 -57.034 11.766 0.67 26.40 ? 277 CYS   A CB  1 
ATOM   1437 C  CB  B CYS   A 1 186 ? 123.252 -57.019 11.752 0.33 25.81 ? 277 CYS   A CB  1 
ATOM   1438 S  SG  A CYS   A 1 186 ? 122.380 -58.604 11.371 0.67 26.27 ? 277 CYS   A SG  1 
ATOM   1439 S  SG  B CYS   A 1 186 ? 122.122 -55.908 10.897 0.33 28.49 ? 277 CYS   A SG  1 
ATOM   1440 N  N   . PRO   A 1 187 ? 124.098 -58.071 15.207 1.00 17.54 ? 278 PRO   A N   1 
ATOM   1441 C  CA  . PRO   A 1 187 ? 125.002 -59.019 15.893 1.00 20.46 ? 278 PRO   A CA  1 
ATOM   1442 C  C   . PRO   A 1 187 ? 125.075 -60.399 15.261 1.00 19.92 ? 278 PRO   A C   1 
ATOM   1443 O  O   . PRO   A 1 187 ? 126.159 -60.990 15.229 1.00 15.37 ? 278 PRO   A O   1 
ATOM   1444 C  CB  . PRO   A 1 187 ? 124.417 -59.096 17.310 1.00 16.18 ? 278 PRO   A CB  1 
ATOM   1445 C  CG  . PRO   A 1 187 ? 123.650 -57.836 17.483 1.00 19.92 ? 278 PRO   A CG  1 
ATOM   1446 C  CD  . PRO   A 1 187 ? 123.142 -57.436 16.126 1.00 18.41 ? 278 PRO   A CD  1 
ATOM   1447 N  N   . GLY   A 1 188 ? 123.953 -60.939 14.778 1.00 18.24 ? 279 GLY   A N   1 
ATOM   1448 C  CA  . GLY   A 1 188 ? 123.980 -62.275 14.200 1.00 16.98 ? 279 GLY   A CA  1 
ATOM   1449 C  C   . GLY   A 1 188 ? 124.886 -62.369 12.988 1.00 28.03 ? 279 GLY   A C   1 
ATOM   1450 O  O   . GLY   A 1 188 ? 125.719 -63.275 12.884 1.00 18.14 ? 279 GLY   A O   1 
ATOM   1451 N  N   . ARG   A 1 189 ? 124.730 -61.439 12.044 1.00 18.69 ? 280 ARG   A N   1 
ATOM   1452 C  CA  . ARG   A 1 189 ? 125.590 -61.457 10.866 1.00 19.76 ? 280 ARG   A CA  1 
ATOM   1453 C  C   . ARG   A 1 189 ? 127.044 -61.220 11.258 1.00 20.77 ? 280 ARG   A C   1 
ATOM   1454 O  O   . ARG   A 1 189 ? 127.952 -61.903 10.767 1.00 20.26 ? 280 ARG   A O   1 
ATOM   1455 C  CB  . ARG   A 1 189 ? 125.117 -60.411 9.852  1.00 29.47 ? 280 ARG   A CB  1 
ATOM   1456 N  N   . ASP   A 1 190 ? 127.280 -60.284 12.174 1.00 17.96 ? 281 ASP   A N   1 
ATOM   1457 C  CA  . ASP   A 1 190 ? 128.650 -59.962 12.544 1.00 18.53 ? 281 ASP   A CA  1 
ATOM   1458 C  C   . ASP   A 1 190 ? 129.319 -61.124 13.254 1.00 17.00 ? 281 ASP   A C   1 
ATOM   1459 O  O   . ASP   A 1 190 ? 130.493 -61.408 12.997 1.00 19.52 ? 281 ASP   A O   1 
ATOM   1460 C  CB  . ASP   A 1 190 ? 128.679 -58.694 13.390 1.00 17.36 ? 281 ASP   A CB  1 
ATOM   1461 C  CG  . ASP   A 1 190 ? 128.430 -57.452 12.543 1.00 24.08 ? 281 ASP   A CG  1 
ATOM   1462 O  OD1 . ASP   A 1 190 ? 128.273 -57.625 11.312 1.00 24.93 ? 281 ASP   A OD1 1 
ATOM   1463 O  OD2 . ASP   A 1 190 ? 128.394 -56.329 13.081 1.00 23.58 ? 281 ASP   A OD2 1 
ATOM   1464 N  N   . ARG   A 1 191 ? 128.593 -61.821 14.133 1.00 17.17 ? 282 ARG   A N   1 
ATOM   1465 C  CA  . ARG   A 1 191 ? 129.166 -63.014 14.750 1.00 16.06 ? 282 ARG   A CA  1 
ATOM   1466 C  C   . ARG   A 1 191 ? 129.482 -64.074 13.699 1.00 19.22 ? 282 ARG   A C   1 
ATOM   1467 O  O   . ARG   A 1 191 ? 130.553 -64.695 13.727 1.00 19.13 ? 282 ARG   A O   1 
ATOM   1468 C  CB  . ARG   A 1 191 ? 128.221 -63.585 15.806 1.00 15.30 ? 282 ARG   A CB  1 
ATOM   1469 C  CG  . ARG   A 1 191 ? 128.700 -64.945 16.300 1.00 15.26 ? 282 ARG   A CG  1 
ATOM   1470 C  CD  . ARG   A 1 191 ? 127.902 -65.487 17.482 1.00 16.00 ? 282 ARG   A CD  1 
ATOM   1471 N  NE  . ARG   A 1 191 ? 128.269 -66.874 17.721 1.00 14.75 ? 282 ARG   A NE  1 
ATOM   1472 C  CZ  . ARG   A 1 191 ? 127.514 -67.759 18.366 1.00 18.81 ? 282 ARG   A CZ  1 
ATOM   1473 N  NH1 . ARG   A 1 191 ? 126.337 -67.407 18.867 1.00 14.25 ? 282 ARG   A NH1 1 
ATOM   1474 N  NH2 . ARG   A 1 191 ? 127.942 -69.004 18.500 1.00 14.97 ? 282 ARG   A NH2 1 
ATOM   1475 N  N   . ARG   A 1 192 ? 128.545 -64.312 12.777 1.00 18.28 ? 283 ARG   A N   1 
ATOM   1476 C  CA  . ARG   A 1 192 ? 128.783 -65.282 11.711 1.00 24.51 ? 283 ARG   A CA  1 
ATOM   1477 C  C   . ARG   A 1 192 ? 130.016 -64.905 10.898 1.00 29.57 ? 283 ARG   A C   1 
ATOM   1478 O  O   . ARG   A 1 192 ? 130.878 -65.749 10.625 1.00 27.69 ? 283 ARG   A O   1 
ATOM   1479 C  CB  . ARG   A 1 192 ? 127.553 -65.381 10.808 1.00 27.99 ? 283 ARG   A CB  1 
ATOM   1480 C  CG  . ARG   A 1 192 ? 126.708 -66.617 11.044 1.00 35.87 ? 283 ARG   A CG  1 
ATOM   1481 C  CD  . ARG   A 1 192 ? 125.554 -66.729 10.043 1.00 39.69 ? 283 ARG   A CD  1 
ATOM   1482 N  NE  . ARG   A 1 192 ? 124.500 -65.749 10.308 1.00 42.67 ? 283 ARG   A NE  1 
ATOM   1483 C  CZ  . ARG   A 1 192 ? 124.131 -64.782 9.473  1.00 42.57 ? 283 ARG   A CZ  1 
ATOM   1484 N  NH1 . ARG   A 1 192 ? 124.716 -64.651 8.287  1.00 47.64 ? 283 ARG   A NH1 1 
ATOM   1485 N  NH2 . ARG   A 1 192 ? 123.156 -63.951 9.822  1.00 38.51 ? 283 ARG   A NH2 1 
ATOM   1486 N  N   . THR   A 1 193 ? 130.116 -63.630 10.512 1.00 31.77 ? 284 THR   A N   1 
ATOM   1487 C  CA  . THR   A 1 193 ? 131.264 -63.161 9.745  1.00 32.07 ? 284 THR   A CA  1 
ATOM   1488 C  C   . THR   A 1 193 ? 132.566 -63.357 10.512 1.00 31.34 ? 284 THR   A C   1 
ATOM   1489 O  O   . THR   A 1 193 ? 133.534 -63.907 9.976  1.00 29.30 ? 284 THR   A O   1 
ATOM   1490 C  CB  . THR   A 1 193 ? 131.085 -61.686 9.382  1.00 31.39 ? 284 THR   A CB  1 
ATOM   1491 O  OG1 . THR   A 1 193 ? 130.002 -61.547 8.456  1.00 29.24 ? 284 THR   A OG1 1 
ATOM   1492 C  CG2 . THR   A 1 193 ? 132.353 -61.138 8.761  1.00 32.48 ? 284 THR   A CG2 1 
ATOM   1493 N  N   . GLU   A 1 194 ? 132.622 -62.890 11.765 1.00 28.33 ? 285 GLU   A N   1 
ATOM   1494 C  CA  . GLU   A 1 194 ? 133.875 -62.996 12.506 1.00 25.56 ? 285 GLU   A CA  1 
ATOM   1495 C  C   . GLU   A 1 194 ? 134.233 -64.454 12.777 1.00 24.20 ? 285 GLU   A C   1 
ATOM   1496 O  O   . GLU   A 1 194 ? 135.414 -64.821 12.750 1.00 27.37 ? 285 GLU   A O   1 
ATOM   1497 C  CB  . GLU   A 1 194 ? 133.800 -62.185 13.804 1.00 20.87 ? 285 GLU   A CB  1 
ATOM   1498 C  CG  . GLU   A 1 194 ? 133.618 -60.684 13.536 1.00 22.64 ? 285 GLU   A CG  1 
ATOM   1499 C  CD  . GLU   A 1 194 ? 133.989 -59.815 14.721 1.00 26.03 ? 285 GLU   A CD  1 
ATOM   1500 O  OE1 . GLU   A 1 194 ? 134.589 -60.330 15.690 1.00 28.38 ? 285 GLU   A OE1 1 
ATOM   1501 O  OE2 . GLU   A 1 194 ? 133.678 -58.611 14.677 1.00 30.07 ? 285 GLU   A OE2 1 
ATOM   1502 N  N   . GLU   A 1 195 ? 133.230 -65.311 13.014 1.00 22.18 ? 286 GLU   A N   1 
ATOM   1503 C  CA  . GLU   A 1 195 ? 133.534 -66.732 13.166 1.00 19.12 ? 286 GLU   A CA  1 
ATOM   1504 C  C   . GLU   A 1 195 ? 133.967 -67.344 11.839 1.00 28.95 ? 286 GLU   A C   1 
ATOM   1505 O  O   . GLU   A 1 195 ? 134.826 -68.232 11.816 1.00 29.32 ? 286 GLU   A O   1 
ATOM   1506 C  CB  . GLU   A 1 195 ? 132.341 -67.498 13.749 1.00 18.63 ? 286 GLU   A CB  1 
ATOM   1507 C  CG  . GLU   A 1 195 ? 132.088 -67.202 15.227 1.00 19.00 ? 286 GLU   A CG  1 
ATOM   1508 C  CD  . GLU   A 1 195 ? 131.115 -68.170 15.902 1.00 23.73 ? 286 GLU   A CD  1 
ATOM   1509 O  OE1 . GLU   A 1 195 ? 130.613 -69.107 15.246 1.00 24.00 ? 286 GLU   A OE1 1 
ATOM   1510 O  OE2 . GLU   A 1 195 ? 130.857 -67.992 17.115 1.00 18.88 ? 286 GLU   A OE2 1 
ATOM   1511 N  N   . GLU   A 1 196 ? 133.400 -66.883 10.727 1.00 33.35 ? 287 GLU   A N   1 
ATOM   1512 C  CA  . GLU   A 1 196 ? 133.887 -67.356 9.437  1.00 42.53 ? 287 GLU   A CA  1 
ATOM   1513 C  C   . GLU   A 1 196 ? 135.323 -66.905 9.202  1.00 39.49 ? 287 GLU   A C   1 
ATOM   1514 O  O   . GLU   A 1 196 ? 136.160 -67.698 8.756  1.00 48.12 ? 287 GLU   A O   1 
ATOM   1515 C  CB  . GLU   A 1 196 ? 132.974 -66.878 8.309  1.00 51.59 ? 287 GLU   A CB  1 
ATOM   1516 C  CG  . GLU   A 1 196 ? 133.383 -67.389 6.937  1.00 61.68 ? 287 GLU   A CG  1 
ATOM   1517 C  CD  . GLU   A 1 196 ? 133.504 -68.902 6.893  1.00 69.50 ? 287 GLU   A CD  1 
ATOM   1518 O  OE1 . GLU   A 1 196 ? 132.681 -69.585 7.538  1.00 71.34 ? 287 GLU   A OE1 1 
ATOM   1519 O  OE2 . GLU   A 1 196 ? 134.427 -69.408 6.218  1.00 73.67 ? 287 GLU   A OE2 1 
ATOM   1520 N  N   . ASN   A 1 197 ? 135.629 -65.641 9.511  1.00 37.14 ? 288 ASN   A N   1 
ATOM   1521 C  CA  . ASN   A 1 197 ? 137.008 -65.170 9.415  1.00 39.17 ? 288 ASN   A CA  1 
ATOM   1522 C  C   . ASN   A 1 197 ? 137.945 -66.028 10.253 1.00 37.63 ? 288 ASN   A C   1 
ATOM   1523 O  O   . ASN   A 1 197 ? 139.047 -66.368 9.810  1.00 39.08 ? 288 ASN   A O   1 
ATOM   1524 C  CB  . ASN   A 1 197 ? 137.107 -63.708 9.847  1.00 38.96 ? 288 ASN   A CB  1 
ATOM   1525 C  CG  . ASN   A 1 197 ? 136.532 -62.759 8.819  1.00 43.98 ? 288 ASN   A CG  1 
ATOM   1526 O  OD1 . ASN   A 1 197 ? 136.297 -63.140 7.674  1.00 45.47 ? 288 ASN   A OD1 1 
ATOM   1527 N  ND2 . ASN   A 1 197 ? 136.305 -61.513 9.222  1.00 46.40 ? 288 ASN   A ND2 1 
ATOM   1528 N  N   . LEU   A 1 198 ? 137.525 -66.388 11.467 1.00 31.84 ? 289 LEU   A N   1 
ATOM   1529 C  CA  . LEU   A 1 198 ? 138.363 -67.227 12.316 1.00 31.60 ? 289 LEU   A CA  1 
ATOM   1530 C  C   . LEU   A 1 198 ? 138.672 -68.556 11.641 1.00 37.16 ? 289 LEU   A C   1 
ATOM   1531 O  O   . LEU   A 1 198 ? 139.788 -69.074 11.753 1.00 41.95 ? 289 LEU   A O   1 
ATOM   1532 C  CB  . LEU   A 1 198 ? 137.678 -67.458 13.661 1.00 33.34 ? 289 LEU   A CB  1 
ATOM   1533 C  CG  . LEU   A 1 198 ? 138.559 -68.067 14.749 1.00 34.09 ? 289 LEU   A CG  1 
ATOM   1534 C  CD1 . LEU   A 1 198 ? 139.739 -67.149 15.058 1.00 32.19 ? 289 LEU   A CD1 1 
ATOM   1535 C  CD2 . LEU   A 1 198 ? 137.741 -68.349 16.004 1.00 31.49 ? 289 LEU   A CD2 1 
ATOM   1536 N  N   . ARG   A 1 199 ? 137.703 -69.109 10.909 1.00 42.79 ? 290 ARG   A N   1 
ATOM   1537 C  CA  . ARG   A 1 199 ? 137.862 -70.417 10.280 1.00 54.12 ? 290 ARG   A CA  1 
ATOM   1538 C  C   . ARG   A 1 199 ? 138.920 -70.383 9.182  1.00 55.54 ? 290 ARG   A C   1 
ATOM   1539 O  O   . ARG   A 1 199 ? 139.257 -71.422 8.606  1.00 60.41 ? 290 ARG   A O   1 
ATOM   1540 C  CB  . ARG   A 1 199 ? 136.526 -70.908 9.716  1.00 58.27 ? 290 ARG   A CB  1 
ATOM   1541 N  N   . LYS   A 1 200 ? 139.458 -69.204 8.894  1.00 52.86 ? 291 LYS   A N   1 
ATOM   1542 C  CA  . LYS   A 1 200 ? 140.501 -69.070 7.885  1.00 52.96 ? 291 LYS   A CA  1 
ATOM   1543 C  C   . LYS   A 1 200 ? 141.863 -68.771 8.523  1.00 53.56 ? 291 LYS   A C   1 
ATOM   1544 O  O   . LYS   A 1 200 ? 141.959 -68.029 9.504  1.00 52.37 ? 291 LYS   A O   1 
ATOM   1545 C  CB  . LYS   A 1 200 ? 140.127 -67.977 6.881  1.00 48.65 ? 291 LYS   A CB  1 
ATOM   1546 N  N   . GLY   B 1 1   ? 174.267 -31.385 27.566 1.00 51.03 ? 92  GLY   B N   1 
ATOM   1547 C  CA  . GLY   B 1 1   ? 174.868 -31.483 28.885 1.00 47.51 ? 92  GLY   B CA  1 
ATOM   1548 C  C   . GLY   B 1 1   ? 175.448 -32.852 29.176 1.00 40.57 ? 92  GLY   B C   1 
ATOM   1549 O  O   . GLY   B 1 1   ? 174.824 -33.866 28.864 1.00 25.51 ? 92  GLY   B O   1 
ATOM   1550 N  N   . SER   B 1 2   ? 176.633 -32.888 29.792 1.00 49.40 ? 93  SER   B N   1 
ATOM   1551 C  CA  . SER   B 1 2   ? 177.377 -34.125 29.988 1.00 44.55 ? 93  SER   B CA  1 
ATOM   1552 C  C   . SER   B 1 2   ? 177.636 -34.371 31.469 1.00 39.96 ? 93  SER   B C   1 
ATOM   1553 O  O   . SER   B 1 2   ? 178.147 -33.494 32.175 1.00 41.94 ? 93  SER   B O   1 
ATOM   1554 C  CB  . SER   B 1 2   ? 178.703 -34.103 29.226 1.00 42.60 ? 93  SER   B CB  1 
ATOM   1555 O  OG  . SER   B 1 2   ? 179.753 -33.673 30.069 1.00 46.68 ? 93  SER   B OG  1 
ATOM   1556 N  N   . SER   B 1 3   ? 177.309 -35.581 31.913 1.00 28.82 ? 94  SER   B N   1 
ATOM   1557 C  CA  . SER   B 1 3   ? 177.480 -36.043 33.280 1.00 21.10 ? 94  SER   B CA  1 
ATOM   1558 C  C   . SER   B 1 3   ? 178.953 -36.322 33.584 1.00 24.97 ? 94  SER   B C   1 
ATOM   1559 O  O   . SER   B 1 3   ? 179.751 -36.624 32.693 1.00 26.83 ? 94  SER   B O   1 
ATOM   1560 C  CB  . SER   B 1 3   ? 176.650 -37.314 33.487 1.00 18.72 ? 94  SER   B CB  1 
ATOM   1561 O  OG  . SER   B 1 3   ? 176.878 -37.927 34.743 1.00 23.76 ? 94  SER   B OG  1 
ATOM   1562 N  N   . SER   B 1 4   ? 179.310 -36.238 34.868 1.00 21.19 ? 95  SER   B N   1 
ATOM   1563 C  CA  . SER   B 1 4   ? 180.655 -36.621 35.288 1.00 20.86 ? 95  SER   B CA  1 
ATOM   1564 C  C   . SER   B 1 4   ? 180.812 -38.128 35.466 1.00 26.79 ? 95  SER   B C   1 
ATOM   1565 O  O   . SER   B 1 4   ? 181.899 -38.580 35.844 1.00 29.30 ? 95  SER   B O   1 
ATOM   1566 C  CB  . SER   B 1 4   ? 181.036 -35.910 36.592 1.00 24.80 ? 95  SER   B CB  1 
ATOM   1567 O  OG  . SER   B 1 4   ? 180.121 -36.241 37.629 1.00 29.88 ? 95  SER   B OG  1 
ATOM   1568 N  N   . SER   B 1 5   ? 179.772 -38.914 35.202 1.00 20.10 ? 96  SER   B N   1 
ATOM   1569 C  CA  . SER   B 1 5   ? 179.847 -40.354 35.393 1.00 19.04 ? 96  SER   B CA  1 
ATOM   1570 C  C   . SER   B 1 5   ? 178.878 -41.041 34.437 1.00 18.95 ? 96  SER   B C   1 
ATOM   1571 O  O   . SER   B 1 5   ? 178.136 -40.396 33.692 1.00 21.07 ? 96  SER   B O   1 
ATOM   1572 C  CB  . SER   B 1 5   ? 179.547 -40.731 36.847 1.00 21.91 ? 96  SER   B CB  1 
ATOM   1573 O  OG  . SER   B 1 5   ? 178.208 -40.409 37.175 1.00 21.09 ? 96  SER   B OG  1 
ATOM   1574 N  N   . VAL   B 1 6   ? 178.905 -42.369 34.455 1.00 16.04 ? 97  VAL   B N   1 
ATOM   1575 C  CA  . VAL   B 1 6   ? 177.975 -43.188 33.683 1.00 15.20 ? 97  VAL   B CA  1 
ATOM   1576 C  C   . VAL   B 1 6   ? 177.402 -44.231 34.632 1.00 14.24 ? 97  VAL   B C   1 
ATOM   1577 O  O   . VAL   B 1 6   ? 178.174 -44.947 35.280 1.00 14.30 ? 97  VAL   B O   1 
ATOM   1578 C  CB  . VAL   B 1 6   ? 178.666 -43.865 32.487 1.00 15.53 ? 97  VAL   B CB  1 
ATOM   1579 C  CG1 . VAL   B 1 6   ? 177.672 -44.735 31.718 1.00 14.84 ? 97  VAL   B CG1 1 
ATOM   1580 C  CG2 . VAL   B 1 6   ? 179.322 -42.820 31.569 1.00 19.14 ? 97  VAL   B CG2 1 
ATOM   1581 N  N   . PRO   B 1 7   ? 176.083 -44.372 34.745 1.00 13.87 ? 98  PRO   B N   1 
ATOM   1582 C  CA  . PRO   B 1 7   ? 175.535 -45.433 35.604 1.00 12.68 ? 98  PRO   B CA  1 
ATOM   1583 C  C   . PRO   B 1 7   ? 175.917 -46.812 35.093 1.00 18.25 ? 98  PRO   B C   1 
ATOM   1584 O  O   . PRO   B 1 7   ? 175.959 -47.059 33.886 1.00 15.57 ? 98  PRO   B O   1 
ATOM   1585 C  CB  . PRO   B 1 7   ? 174.020 -45.210 35.533 1.00 14.80 ? 98  PRO   B CB  1 
ATOM   1586 C  CG  . PRO   B 1 7   ? 173.797 -44.406 34.326 1.00 17.58 ? 98  PRO   B CG  1 
ATOM   1587 C  CD  . PRO   B 1 7   ? 175.026 -43.561 34.117 1.00 16.10 ? 98  PRO   B CD  1 
ATOM   1588 N  N   . SER   B 1 8   ? 176.176 -47.723 36.027 1.00 14.65 ? 99  SER   B N   1 
ATOM   1589 C  CA  . SER   B 1 8   ? 176.450 -49.095 35.635 1.00 17.01 ? 99  SER   B CA  1 
ATOM   1590 C  C   . SER   B 1 8   ? 175.254 -49.675 34.898 1.00 14.77 ? 99  SER   B C   1 
ATOM   1591 O  O   . SER   B 1 8   ? 174.101 -49.367 35.209 1.00 14.38 ? 99  SER   B O   1 
ATOM   1592 C  CB  . SER   B 1 8   ? 176.762 -49.953 36.853 1.00 18.94 ? 99  SER   B CB  1 
ATOM   1593 O  OG  . SER   B 1 8   ? 176.954 -51.296 36.450 1.00 27.59 ? 99  SER   B OG  1 
ATOM   1594 N  N   . GLN   B 1 9   ? 175.533 -50.504 33.897 1.00 13.91 ? 100 GLN   B N   1 
ATOM   1595 C  CA  . GLN   B 1 9   ? 174.486 -51.257 33.224 1.00 13.83 ? 100 GLN   B CA  1 
ATOM   1596 C  C   . GLN   B 1 9   ? 174.618 -52.757 33.467 1.00 15.12 ? 100 GLN   B C   1 
ATOM   1597 O  O   . GLN   B 1 9   ? 174.011 -53.560 32.752 1.00 14.84 ? 100 GLN   B O   1 
ATOM   1598 C  CB  . GLN   B 1 9   ? 174.489 -50.949 31.730 1.00 19.27 ? 100 GLN   B CB  1 
ATOM   1599 C  CG  . GLN   B 1 9   ? 175.668 -51.510 30.978 1.00 25.44 ? 100 GLN   B CG  1 
ATOM   1600 C  CD  . GLN   B 1 9   ? 175.674 -51.059 29.536 1.00 32.03 ? 100 GLN   B CD  1 
ATOM   1601 O  OE1 . GLN   B 1 9   ? 176.025 -49.916 29.235 1.00 34.73 ? 100 GLN   B OE1 1 
ATOM   1602 N  NE2 . GLN   B 1 9   ? 175.278 -51.947 28.639 1.00 22.24 ? 100 GLN   B NE2 1 
ATOM   1603 N  N   . LYS   B 1 10  ? 175.384 -53.149 34.476 1.00 14.76 ? 101 LYS   B N   1 
ATOM   1604 C  CA  . LYS   B 1 10  ? 175.639 -54.564 34.717 1.00 12.02 ? 101 LYS   B CA  1 
ATOM   1605 C  C   . LYS   B 1 10  ? 174.387 -55.245 35.265 1.00 11.43 ? 101 LYS   B C   1 
ATOM   1606 O  O   . LYS   B 1 10  ? 173.847 -54.829 36.295 1.00 13.63 ? 101 LYS   B O   1 
ATOM   1607 C  CB  . LYS   B 1 10  ? 176.808 -54.715 35.683 1.00 12.63 ? 101 LYS   B CB  1 
ATOM   1608 C  CG  . LYS   B 1 10  ? 177.203 -56.161 35.989 1.00 19.72 ? 101 LYS   B CG  1 
ATOM   1609 C  CD  . LYS   B 1 10  ? 178.260 -56.198 37.091 1.00 28.86 ? 101 LYS   B CD  1 
ATOM   1610 C  CE  . LYS   B 1 10  ? 178.660 -57.619 37.429 1.00 38.37 ? 101 LYS   B CE  1 
ATOM   1611 N  NZ  . LYS   B 1 10  ? 179.039 -58.353 36.191 1.00 47.15 ? 101 LYS   B NZ  1 
ATOM   1612 N  N   . THR   B 1 11  ? 173.938 -56.301 34.584 1.00 13.97 ? 102 THR   B N   1 
ATOM   1613 C  CA  . THR   B 1 11  ? 172.821 -57.103 35.078 1.00 9.22  ? 102 THR   B CA  1 
ATOM   1614 C  C   . THR   B 1 11  ? 173.158 -57.688 36.438 1.00 12.50 ? 102 THR   B C   1 
ATOM   1615 O  O   . THR   B 1 11  ? 174.230 -58.277 36.627 1.00 10.39 ? 102 THR   B O   1 
ATOM   1616 C  CB  . THR   B 1 11  ? 172.503 -58.236 34.097 1.00 15.32 ? 102 THR   B CB  1 
ATOM   1617 O  OG1 . THR   B 1 11  ? 172.171 -57.685 32.816 1.00 15.10 ? 102 THR   B OG1 1 
ATOM   1618 C  CG2 . THR   B 1 11  ? 171.342 -59.091 34.618 1.00 13.02 ? 102 THR   B CG2 1 
ATOM   1619 N  N   . TYR   B 1 12  ? 172.225 -57.556 37.377 1.00 11.24 ? 103 TYR   B N   1 
ATOM   1620 C  CA  . TYR   B 1 12  ? 172.450 -57.969 38.758 1.00 8.84  ? 103 TYR   B CA  1 
ATOM   1621 C  C   . TYR   B 1 12  ? 171.117 -58.448 39.322 1.00 9.58  ? 103 TYR   B C   1 
ATOM   1622 O  O   . TYR   B 1 12  ? 170.226 -57.637 39.593 1.00 9.69  ? 103 TYR   B O   1 
ATOM   1623 C  CB  . TYR   B 1 12  ? 173.035 -56.807 39.569 1.00 11.52 ? 103 TYR   B CB  1 
ATOM   1624 C  CG  . TYR   B 1 12  ? 173.156 -57.055 41.059 1.00 14.16 ? 103 TYR   B CG  1 
ATOM   1625 C  CD1 . TYR   B 1 12  ? 173.850 -58.149 41.548 1.00 21.66 ? 103 TYR   B CD1 1 
ATOM   1626 C  CD2 . TYR   B 1 12  ? 172.605 -56.159 41.977 1.00 14.56 ? 103 TYR   B CD2 1 
ATOM   1627 C  CE1 . TYR   B 1 12  ? 173.967 -58.370 42.925 1.00 24.49 ? 103 TYR   B CE1 1 
ATOM   1628 C  CE2 . TYR   B 1 12  ? 172.714 -56.365 43.337 1.00 19.13 ? 103 TYR   B CE2 1 
ATOM   1629 C  CZ  . TYR   B 1 12  ? 173.396 -57.472 43.806 1.00 23.19 ? 103 TYR   B CZ  1 
ATOM   1630 O  OH  . TYR   B 1 12  ? 173.501 -57.672 45.161 1.00 27.67 ? 103 TYR   B OH  1 
ATOM   1631 N  N   . GLN   B 1 13  ? 170.950 -59.766 39.461 1.00 8.86  ? 104 GLN   B N   1 
ATOM   1632 C  CA  . GLN   B 1 13  ? 169.686 -60.260 40.011 1.00 8.67  ? 104 GLN   B CA  1 
ATOM   1633 C  C   . GLN   B 1 13  ? 169.562 -59.961 41.503 1.00 10.32 ? 104 GLN   B C   1 
ATOM   1634 O  O   . GLN   B 1 13  ? 168.447 -59.750 42.000 1.00 10.15 ? 104 GLN   B O   1 
ATOM   1635 C  CB  . GLN   B 1 13  ? 169.531 -61.761 39.757 1.00 8.25  ? 104 GLN   B CB  1 
ATOM   1636 C  CG  . GLN   B 1 13  ? 169.272 -62.110 38.277 1.00 13.00 ? 104 GLN   B CG  1 
ATOM   1637 C  CD  . GLN   B 1 13  ? 168.382 -63.345 38.090 1.00 19.99 ? 104 GLN   B CD  1 
ATOM   1638 O  OE1 . GLN   B 1 13  ? 168.120 -64.083 39.034 1.00 20.64 ? 104 GLN   B OE1 1 
ATOM   1639 N  NE2 . GLN   B 1 13  ? 167.922 -63.569 36.864 1.00 18.90 ? 104 GLN   B NE2 1 
ATOM   1640 N  N   . GLY   B 1 14  ? 170.672 -59.961 42.232 1.00 10.46 ? 105 GLY   B N   1 
ATOM   1641 C  CA  . GLY   B 1 14  ? 170.629 -59.637 43.653 1.00 14.40 ? 105 GLY   B CA  1 
ATOM   1642 C  C   . GLY   B 1 14  ? 169.974 -60.743 44.473 1.00 13.09 ? 105 GLY   B C   1 
ATOM   1643 O  O   . GLY   B 1 14  ? 169.614 -61.808 43.969 1.00 10.69 ? 105 GLY   B O   1 
ATOM   1644 N  N   . SER   B 1 15  ? 169.793 -60.460 45.767 1.00 10.87 ? 106 SER   B N   1 
ATOM   1645 C  CA  A SER   B 1 15  ? 169.298 -61.478 46.694 0.60 12.34 ? 106 SER   B CA  1 
ATOM   1646 C  CA  B SER   B 1 15  ? 169.319 -61.517 46.656 0.40 12.38 ? 106 SER   B CA  1 
ATOM   1647 C  C   . SER   B 1 15  ? 167.881 -61.933 46.365 1.00 13.79 ? 106 SER   B C   1 
ATOM   1648 O  O   . SER   B 1 15  ? 167.482 -63.029 46.778 1.00 12.45 ? 106 SER   B O   1 
ATOM   1649 C  CB  A SER   B 1 15  ? 169.341 -60.953 48.135 0.60 13.38 ? 106 SER   B CB  1 
ATOM   1650 C  CB  B SER   B 1 15  ? 169.455 -61.096 48.124 0.40 13.57 ? 106 SER   B CB  1 
ATOM   1651 O  OG  A SER   B 1 15  ? 170.600 -60.374 48.443 0.60 14.77 ? 106 SER   B OG  1 
ATOM   1652 O  OG  B SER   B 1 15  ? 168.492 -60.127 48.483 0.40 14.08 ? 106 SER   B OG  1 
ATOM   1653 N  N   . TYR   B 1 16  ? 167.103 -61.114 45.646 1.00 8.74  ? 107 TYR   B N   1 
ATOM   1654 C  CA  . TYR   B 1 16  ? 165.704 -61.428 45.373 1.00 8.89  ? 107 TYR   B CA  1 
ATOM   1655 C  C   . TYR   B 1 16  ? 165.478 -62.031 43.991 1.00 9.85  ? 107 TYR   B C   1 
ATOM   1656 O  O   . TYR   B 1 16  ? 164.344 -62.406 43.670 1.00 10.30 ? 107 TYR   B O   1 
ATOM   1657 C  CB  . TYR   B 1 16  ? 164.842 -60.169 45.559 1.00 11.11 ? 107 TYR   B CB  1 
ATOM   1658 C  CG  . TYR   B 1 16  ? 165.002 -59.636 46.958 1.00 9.04  ? 107 TYR   B CG  1 
ATOM   1659 C  CD1 . TYR   B 1 16  ? 164.390 -60.272 48.030 1.00 9.44  ? 107 TYR   B CD1 1 
ATOM   1660 C  CD2 . TYR   B 1 16  ? 165.820 -58.547 47.217 1.00 13.64 ? 107 TYR   B CD2 1 
ATOM   1661 C  CE1 . TYR   B 1 16  ? 164.569 -59.815 49.332 1.00 12.10 ? 107 TYR   B CE1 1 
ATOM   1662 C  CE2 . TYR   B 1 16  ? 166.003 -58.084 48.509 1.00 14.64 ? 107 TYR   B CE2 1 
ATOM   1663 C  CZ  . TYR   B 1 16  ? 165.372 -58.720 49.557 1.00 19.86 ? 107 TYR   B CZ  1 
ATOM   1664 O  OH  . TYR   B 1 16  ? 165.555 -58.262 50.838 1.00 24.71 ? 107 TYR   B OH  1 
ATOM   1665 N  N   . GLY   B 1 17  ? 166.525 -62.170 43.186 1.00 8.95  ? 108 GLY   B N   1 
ATOM   1666 C  CA  . GLY   B 1 17  ? 166.368 -62.737 41.857 1.00 10.13 ? 108 GLY   B CA  1 
ATOM   1667 C  C   . GLY   B 1 17  ? 165.602 -61.826 40.920 1.00 12.78 ? 108 GLY   B C   1 
ATOM   1668 O  O   . GLY   B 1 17  ? 164.721 -62.293 40.186 1.00 9.97  ? 108 GLY   B O   1 
ATOM   1669 N  N   . PHE   B 1 18  ? 165.915 -60.536 40.929 1.00 9.19  ? 109 PHE   B N   1 
ATOM   1670 C  CA  . PHE   B 1 18  ? 165.185 -59.556 40.130 1.00 9.09  ? 109 PHE   B CA  1 
ATOM   1671 C  C   . PHE   B 1 18  ? 165.548 -59.653 38.650 1.00 12.55 ? 109 PHE   B C   1 
ATOM   1672 O  O   . PHE   B 1 18  ? 166.729 -59.749 38.293 1.00 11.05 ? 109 PHE   B O   1 
ATOM   1673 C  CB  . PHE   B 1 18  ? 165.497 -58.149 40.641 1.00 10.01 ? 109 PHE   B CB  1 
ATOM   1674 C  CG  . PHE   B 1 18  ? 164.942 -57.043 39.783 1.00 8.74  ? 109 PHE   B CG  1 
ATOM   1675 C  CD1 . PHE   B 1 18  ? 163.594 -56.733 39.825 1.00 14.86 ? 109 PHE   B CD1 1 
ATOM   1676 C  CD2 . PHE   B 1 18  ? 165.782 -56.282 38.969 1.00 8.04  ? 109 PHE   B CD2 1 
ATOM   1677 C  CE1 . PHE   B 1 18  ? 163.083 -55.703 39.058 1.00 16.16 ? 109 PHE   B CE1 1 
ATOM   1678 C  CE2 . PHE   B 1 18  ? 165.278 -55.260 38.202 1.00 11.30 ? 109 PHE   B CE2 1 
ATOM   1679 C  CZ  . PHE   B 1 18  ? 163.931 -54.968 38.239 1.00 13.37 ? 109 PHE   B CZ  1 
ATOM   1680 N  N   . ARG   B 1 19  ? 164.527 -59.611 37.790 1.00 6.40  ? 110 ARG   B N   1 
ATOM   1681 C  CA  . ARG   B 1 19  ? 164.744 -59.501 36.349 1.00 7.32  ? 110 ARG   B CA  1 
ATOM   1682 C  C   . ARG   B 1 19  ? 163.462 -59.019 35.688 1.00 9.81  ? 110 ARG   B C   1 
ATOM   1683 O  O   . ARG   B 1 19  ? 162.372 -59.095 36.263 1.00 8.59  ? 110 ARG   B O   1 
ATOM   1684 C  CB  . ARG   B 1 19  ? 165.184 -60.833 35.719 1.00 8.88  ? 110 ARG   B CB  1 
ATOM   1685 C  CG  . ARG   B 1 19  ? 164.099 -61.914 35.644 1.00 8.61  ? 110 ARG   B CG  1 
ATOM   1686 C  CD  . ARG   B 1 19  ? 163.896 -62.642 36.990 1.00 7.28  ? 110 ARG   B CD  1 
ATOM   1687 N  NE  . ARG   B 1 19  ? 162.987 -63.772 36.832 1.00 8.67  ? 110 ARG   B NE  1 
ATOM   1688 C  CZ  . ARG   B 1 19  ? 162.613 -64.578 37.824 1.00 17.27 ? 110 ARG   B CZ  1 
ATOM   1689 N  NH1 . ARG   B 1 19  ? 163.059 -64.373 39.058 1.00 10.89 ? 110 ARG   B NH1 1 
ATOM   1690 N  NH2 . ARG   B 1 19  ? 161.776 -65.580 37.586 1.00 13.70 ? 110 ARG   B NH2 1 
ATOM   1691 N  N   . LEU   B 1 20  ? 163.604 -58.557 34.452 1.00 8.25  ? 111 LEU   B N   1 
ATOM   1692 C  CA  . LEU   B 1 20  ? 162.484 -58.040 33.686 1.00 7.78  ? 111 LEU   B CA  1 
ATOM   1693 C  C   . LEU   B 1 20  ? 161.828 -59.151 32.882 1.00 8.20  ? 111 LEU   B C   1 
ATOM   1694 O  O   . LEU   B 1 20  ? 162.382 -60.245 32.711 1.00 15.54 ? 111 LEU   B O   1 
ATOM   1695 C  CB  . LEU   B 1 20  ? 162.949 -56.920 32.751 1.00 8.31  ? 111 LEU   B CB  1 
ATOM   1696 C  CG  . LEU   B 1 20  ? 163.612 -55.734 33.462 1.00 8.07  ? 111 LEU   B CG  1 
ATOM   1697 C  CD1 . LEU   B 1 20  ? 164.188 -54.752 32.432 1.00 8.70  ? 111 LEU   B CD1 1 
ATOM   1698 C  CD2 . LEU   B 1 20  ? 162.654 -55.010 34.423 1.00 8.03  ? 111 LEU   B CD2 1 
ATOM   1699 N  N   . GLY   B 1 21  ? 160.626 -58.865 32.404 1.00 8.80  ? 112 GLY   B N   1 
ATOM   1700 C  CA  . GLY   B 1 21  ? 159.973 -59.717 31.426 1.00 9.54  ? 112 GLY   B CA  1 
ATOM   1701 C  C   . GLY   B 1 21  ? 159.230 -58.861 30.426 1.00 10.64 ? 112 GLY   B C   1 
ATOM   1702 O  O   . GLY   B 1 21  ? 158.813 -57.744 30.727 1.00 12.26 ? 112 GLY   B O   1 
ATOM   1703 N  N   . PHE   B 1 22  ? 159.068 -59.392 29.219 1.00 7.46  ? 113 PHE   B N   1 
ATOM   1704 C  CA  . PHE   B 1 22  ? 158.377 -58.676 28.158 1.00 8.98  ? 113 PHE   B CA  1 
ATOM   1705 C  C   . PHE   B 1 22  ? 157.324 -59.570 27.520 1.00 13.14 ? 113 PHE   B C   1 
ATOM   1706 O  O   . PHE   B 1 22  ? 157.479 -60.791 27.456 1.00 9.94  ? 113 PHE   B O   1 
ATOM   1707 C  CB  . PHE   B 1 22  ? 159.345 -58.191 27.088 1.00 7.73  ? 113 PHE   B CB  1 
ATOM   1708 C  CG  . PHE   B 1 22  ? 160.326 -57.185 27.587 1.00 9.29  ? 113 PHE   B CG  1 
ATOM   1709 C  CD1 . PHE   B 1 22  ? 160.083 -55.834 27.448 1.00 13.33 ? 113 PHE   B CD1 1 
ATOM   1710 C  CD2 . PHE   B 1 22  ? 161.505 -57.593 28.196 1.00 9.60  ? 113 PHE   B CD2 1 
ATOM   1711 C  CE1 . PHE   B 1 22  ? 160.995 -54.895 27.928 1.00 12.34 ? 113 PHE   B CE1 1 
ATOM   1712 C  CE2 . PHE   B 1 22  ? 162.420 -56.666 28.675 1.00 14.34 ? 113 PHE   B CE2 1 
ATOM   1713 C  CZ  . PHE   B 1 22  ? 162.165 -55.315 28.544 1.00 6.46  ? 113 PHE   B CZ  1 
ATOM   1714 N  N   . LEU   B 1 23  ? 156.258 -58.944 27.031 1.00 11.52 ? 114 LEU   B N   1 
ATOM   1715 C  CA  . LEU   B 1 23  ? 155.231 -59.682 26.312 1.00 15.01 ? 114 LEU   B CA  1 
ATOM   1716 C  C   . LEU   B 1 23  ? 155.740 -60.078 24.931 1.00 13.33 ? 114 LEU   B C   1 
ATOM   1717 O  O   . LEU   B 1 23  ? 156.761 -59.579 24.446 1.00 15.31 ? 114 LEU   B O   1 
ATOM   1718 C  CB  . LEU   B 1 23  ? 153.959 -58.846 26.177 1.00 12.98 ? 114 LEU   B CB  1 
ATOM   1719 C  CG  . LEU   B 1 23  ? 153.399 -58.323 27.500 1.00 19.31 ? 114 LEU   B CG  1 
ATOM   1720 C  CD1 . LEU   B 1 23  ? 152.114 -57.557 27.247 1.00 25.03 ? 114 LEU   B CD1 1 
ATOM   1721 C  CD2 . LEU   B 1 23  ? 153.159 -59.479 28.446 1.00 22.38 ? 114 LEU   B CD2 1 
ATOM   1722 N  N   . HIS   B 1 24  ? 155.013 -60.988 24.291 1.00 12.10 ? 115 HIS   B N   1 
ATOM   1723 C  CA  . HIS   B 1 24  ? 155.310 -61.429 22.928 1.00 11.79 ? 115 HIS   B CA  1 
ATOM   1724 C  C   . HIS   B 1 24  ? 154.252 -60.798 22.024 1.00 17.15 ? 115 HIS   B C   1 
ATOM   1725 O  O   . HIS   B 1 24  ? 153.164 -61.343 21.825 1.00 18.30 ? 115 HIS   B O   1 
ATOM   1726 C  CB  . HIS   B 1 24  ? 155.329 -62.953 22.836 1.00 14.60 ? 115 HIS   B CB  1 
ATOM   1727 C  CG  . HIS   B 1 24  ? 156.320 -63.583 23.764 1.00 17.99 ? 115 HIS   B CG  1 
ATOM   1728 N  ND1 . HIS   B 1 24  ? 155.969 -64.093 24.994 1.00 19.29 ? 115 HIS   B ND1 1 
ATOM   1729 C  CD2 . HIS   B 1 24  ? 157.664 -63.733 23.662 1.00 17.48 ? 115 HIS   B CD2 1 
ATOM   1730 C  CE1 . HIS   B 1 24  ? 157.052 -64.544 25.605 1.00 19.71 ? 115 HIS   B CE1 1 
ATOM   1731 N  NE2 . HIS   B 1 24  ? 158.094 -64.334 24.819 1.00 15.10 ? 115 HIS   B NE2 1 
ATOM   1732 N  N   . SER   B 1 25  ? 154.597 -59.646 21.464 1.00 14.56 ? 116 SER   B N   1 
ATOM   1733 C  CA  . SER   B 1 25  ? 153.641 -58.796 20.780 1.00 14.91 ? 116 SER   B CA  1 
ATOM   1734 C  C   . SER   B 1 25  ? 153.680 -58.947 19.266 1.00 19.21 ? 116 SER   B C   1 
ATOM   1735 O  O   . SER   B 1 25  ? 152.785 -58.427 18.585 1.00 16.08 ? 116 SER   B O   1 
ATOM   1736 C  CB  . SER   B 1 25  ? 153.903 -57.334 21.156 1.00 13.66 ? 116 SER   B CB  1 
ATOM   1737 O  OG  . SER   B 1 25  ? 153.770 -57.149 22.557 1.00 14.89 ? 116 SER   B OG  1 
ATOM   1738 N  N   . GLY   B 1 26  ? 154.687 -59.635 18.724 1.00 13.74 ? 117 GLY   B N   1 
ATOM   1739 C  CA  . GLY   B 1 26  ? 154.765 -59.841 17.287 1.00 12.27 ? 117 GLY   B CA  1 
ATOM   1740 C  C   . GLY   B 1 26  ? 155.356 -58.637 16.576 1.00 17.96 ? 117 GLY   B C   1 
ATOM   1741 O  O   . GLY   B 1 26  ? 155.775 -57.649 17.187 1.00 15.65 ? 117 GLY   B O   1 
ATOM   1742 N  N   . THR   B 1 27  ? 155.369 -58.717 15.242 1.00 14.69 ? 118 THR   B N   1 
ATOM   1743 C  CA  . THR   B 1 27  ? 156.004 -57.689 14.422 1.00 16.75 ? 118 THR   B CA  1 
ATOM   1744 C  C   . THR   B 1 27  ? 155.088 -57.199 13.306 1.00 21.20 ? 118 THR   B C   1 
ATOM   1745 O  O   . THR   B 1 27  ? 155.569 -56.738 12.265 1.00 14.76 ? 118 THR   B O   1 
ATOM   1746 C  CB  . THR   B 1 27  ? 157.321 -58.194 13.830 1.00 20.81 ? 118 THR   B CB  1 
ATOM   1747 O  OG1 . THR   B 1 27  ? 157.065 -59.316 12.980 1.00 19.24 ? 118 THR   B OG1 1 
ATOM   1748 C  CG2 . THR   B 1 27  ? 158.292 -58.606 14.937 1.00 17.57 ? 118 THR   B CG2 1 
ATOM   1749 N  N   . ALA   B 1 28  ? 153.774 -57.282 13.499 1.00 20.29 ? 119 ALA   B N   1 
ATOM   1750 C  CA  . ALA   B 1 28  ? 152.860 -56.739 12.504 1.00 22.32 ? 119 ALA   B CA  1 
ATOM   1751 C  C   . ALA   B 1 28  ? 153.118 -55.252 12.308 1.00 22.49 ? 119 ALA   B C   1 
ATOM   1752 O  O   . ALA   B 1 28  ? 153.562 -54.551 13.221 1.00 14.33 ? 119 ALA   B O   1 
ATOM   1753 C  CB  . ALA   B 1 28  ? 151.405 -56.958 12.916 1.00 25.26 ? 119 ALA   B CB  1 
ATOM   1754 N  N   . LYS   B 1 29  ? 152.827 -54.776 11.095 1.00 21.91 ? 120 LYS   B N   1 
ATOM   1755 C  CA  . LYS   B 1 29  ? 153.005 -53.363 10.771 1.00 20.92 ? 120 LYS   B CA  1 
ATOM   1756 C  C   . LYS   B 1 29  ? 152.288 -52.453 11.765 1.00 24.30 ? 120 LYS   B C   1 
ATOM   1757 O  O   . LYS   B 1 29  ? 152.751 -51.334 12.030 1.00 19.94 ? 120 LYS   B O   1 
ATOM   1758 C  CB  . LYS   B 1 29  ? 152.506 -53.092 9.351  1.00 22.20 ? 120 LYS   B CB  1 
ATOM   1759 N  N   . SER   B 1 30  ? 151.182 -52.921 12.347 1.00 20.97 ? 121 SER   B N   1 
ATOM   1760 C  CA  . SER   B 1 30  ? 150.363 -52.099 13.231 1.00 24.02 ? 121 SER   B CA  1 
ATOM   1761 C  C   . SER   B 1 30  ? 150.795 -52.126 14.694 1.00 22.76 ? 121 SER   B C   1 
ATOM   1762 O  O   . SER   B 1 30  ? 150.214 -51.390 15.501 1.00 21.91 ? 121 SER   B O   1 
ATOM   1763 C  CB  . SER   B 1 30  ? 148.902 -52.545 13.145 1.00 27.91 ? 121 SER   B CB  1 
ATOM   1764 O  OG  . SER   B 1 30  ? 148.793 -53.905 13.519 1.00 30.05 ? 121 SER   B OG  1 
ATOM   1765 N  N   . VAL   B 1 31  ? 151.780 -52.948 15.069 1.00 15.70 ? 122 VAL   B N   1 
ATOM   1766 C  CA  . VAL   B 1 31  ? 152.144 -53.076 16.477 1.00 15.30 ? 122 VAL   B CA  1 
ATOM   1767 C  C   . VAL   B 1 31  ? 152.814 -51.791 16.959 1.00 18.72 ? 122 VAL   B C   1 
ATOM   1768 O  O   . VAL   B 1 31  ? 153.571 -51.144 16.224 1.00 17.91 ? 122 VAL   B O   1 
ATOM   1769 C  CB  . VAL   B 1 31  ? 153.043 -54.310 16.693 1.00 17.30 ? 122 VAL   B CB  1 
ATOM   1770 C  CG1 . VAL   B 1 31  ? 154.502 -54.027 16.321 1.00 18.38 ? 122 VAL   B CG1 1 
ATOM   1771 C  CG2 . VAL   B 1 31  ? 152.940 -54.803 18.111 1.00 15.02 ? 122 VAL   B CG2 1 
ATOM   1772 N  N   . THR   B 1 32  ? 152.517 -51.400 18.200 1.00 11.50 ? 123 THR   B N   1 
ATOM   1773 C  CA  . THR   B 1 32  ? 152.998 -50.138 18.753 1.00 15.64 ? 123 THR   B CA  1 
ATOM   1774 C  C   . THR   B 1 32  ? 154.092 -50.317 19.790 1.00 14.07 ? 123 THR   B C   1 
ATOM   1775 O  O   . THR   B 1 32  ? 154.742 -49.333 20.162 1.00 13.44 ? 123 THR   B O   1 
ATOM   1776 C  CB  . THR   B 1 32  ? 151.837 -49.356 19.377 1.00 13.35 ? 123 THR   B CB  1 
ATOM   1777 O  OG1 . THR   B 1 32  ? 151.398 -50.026 20.566 1.00 11.60 ? 123 THR   B OG1 1 
ATOM   1778 C  CG2 . THR   B 1 32  ? 150.670 -49.284 18.377 1.00 14.53 ? 123 THR   B CG2 1 
ATOM   1779 N  N   . CYS   B 1 33  ? 154.317 -51.541 20.250 1.00 11.18 ? 124 CYS   B N   1 
ATOM   1780 C  CA  . CYS   B 1 33  ? 155.368 -51.842 21.213 1.00 10.92 ? 124 CYS   B CA  1 
ATOM   1781 C  C   . CYS   B 1 33  ? 155.702 -53.312 21.025 1.00 13.39 ? 124 CYS   B C   1 
ATOM   1782 O  O   . CYS   B 1 33  ? 154.800 -54.155 21.067 1.00 11.06 ? 124 CYS   B O   1 
ATOM   1783 C  CB  . CYS   B 1 33  ? 154.897 -51.551 22.650 1.00 10.74 ? 124 CYS   B CB  1 
ATOM   1784 S  SG  . CYS   B 1 33  ? 156.070 -51.999 23.937 1.00 14.96 ? 124 CYS   B SG  1 
ATOM   1785 N  N   . THR   B 1 34  ? 156.970 -53.623 20.766 1.00 8.95  ? 125 THR   B N   1 
ATOM   1786 C  CA  . THR   B 1 34  ? 157.358 -55.013 20.605 1.00 10.48 ? 125 THR   B CA  1 
ATOM   1787 C  C   . THR   B 1 34  ? 158.800 -55.188 21.060 1.00 8.39  ? 125 THR   B C   1 
ATOM   1788 O  O   . THR   B 1 34  ? 159.635 -54.319 20.826 1.00 11.38 ? 125 THR   B O   1 
ATOM   1789 C  CB  . THR   B 1 34  ? 157.177 -55.462 19.143 1.00 12.82 ? 125 THR   B CB  1 
ATOM   1790 O  OG1 . THR   B 1 34  ? 157.454 -56.859 19.034 1.00 13.40 ? 125 THR   B OG1 1 
ATOM   1791 C  CG2 . THR   B 1 34  ? 158.101 -54.676 18.210 1.00 10.49 ? 125 THR   B CG2 1 
ATOM   1792 N  N   . TYR   B 1 35  ? 159.084 -56.320 21.704 1.00 8.30  ? 126 TYR   B N   1 
ATOM   1793 C  CA  . TYR   B 1 35  ? 160.381 -56.579 22.305 1.00 8.09  ? 126 TYR   B CA  1 
ATOM   1794 C  C   . TYR   B 1 35  ? 161.084 -57.718 21.580 1.00 9.41  ? 126 TYR   B C   1 
ATOM   1795 O  O   . TYR   B 1 35  ? 160.491 -58.777 21.356 1.00 9.11  ? 126 TYR   B O   1 
ATOM   1796 C  CB  . TYR   B 1 35  ? 160.243 -56.922 23.794 1.00 7.97  ? 126 TYR   B CB  1 
ATOM   1797 C  CG  . TYR   B 1 35  ? 161.565 -57.345 24.404 1.00 8.11  ? 126 TYR   B CG  1 
ATOM   1798 C  CD1 . TYR   B 1 35  ? 162.519 -56.394 24.770 1.00 7.36  ? 126 TYR   B CD1 1 
ATOM   1799 C  CD2 . TYR   B 1 35  ? 161.862 -58.689 24.605 1.00 8.26  ? 126 TYR   B CD2 1 
ATOM   1800 C  CE1 . TYR   B 1 35  ? 163.737 -56.778 25.326 1.00 9.01  ? 126 TYR   B CE1 1 
ATOM   1801 C  CE2 . TYR   B 1 35  ? 163.067 -59.084 25.166 1.00 8.02  ? 126 TYR   B CE2 1 
ATOM   1802 C  CZ  . TYR   B 1 35  ? 163.998 -58.129 25.517 1.00 10.48 ? 126 TYR   B CZ  1 
ATOM   1803 O  OH  . TYR   B 1 35  ? 165.199 -58.528 26.056 1.00 11.40 ? 126 TYR   B OH  1 
ATOM   1804 N  N   . SER   B 1 36  ? 162.357 -57.500 21.236 1.00 13.87 ? 127 SER   B N   1 
ATOM   1805 C  CA  . SER   B 1 36  ? 163.201 -58.507 20.604 1.00 10.02 ? 127 SER   B CA  1 
ATOM   1806 C  C   . SER   B 1 36  ? 164.117 -59.142 21.636 1.00 12.05 ? 127 SER   B C   1 
ATOM   1807 O  O   . SER   B 1 36  ? 165.075 -58.487 22.081 1.00 8.97  ? 127 SER   B O   1 
ATOM   1808 C  CB  . SER   B 1 36  ? 164.038 -57.877 19.488 1.00 10.82 ? 127 SER   B CB  1 
ATOM   1809 O  OG  . SER   B 1 36  ? 164.974 -58.838 19.001 1.00 11.96 ? 127 SER   B OG  1 
ATOM   1810 N  N   . PRO   B 1 37  ? 163.898 -60.405 22.029 1.00 13.77 ? 128 PRO   B N   1 
ATOM   1811 C  CA  . PRO   B 1 37  ? 164.886 -61.073 22.889 1.00 9.58  ? 128 PRO   B CA  1 
ATOM   1812 C  C   . PRO   B 1 37  ? 166.230 -61.279 22.211 1.00 11.29 ? 128 PRO   B C   1 
ATOM   1813 O  O   . PRO   B 1 37  ? 167.257 -61.233 22.895 1.00 10.26 ? 128 PRO   B O   1 
ATOM   1814 C  CB  . PRO   B 1 37  ? 164.214 -62.412 23.232 1.00 13.22 ? 128 PRO   B CB  1 
ATOM   1815 C  CG  . PRO   B 1 37  ? 162.755 -62.191 22.977 1.00 16.40 ? 128 PRO   B CG  1 
ATOM   1816 C  CD  . PRO   B 1 37  ? 162.692 -61.226 21.832 1.00 13.64 ? 128 PRO   B CD  1 
ATOM   1817 N  N   . ALA   B 1 38  ? 166.263 -61.495 20.889 1.00 10.71 ? 129 ALA   B N   1 
ATOM   1818 C  CA  . ALA   B 1 38  ? 167.540 -61.723 20.224 1.00 13.59 ? 129 ALA   B CA  1 
ATOM   1819 C  C   . ALA   B 1 38  ? 168.429 -60.487 20.290 1.00 17.43 ? 129 ALA   B C   1 
ATOM   1820 O  O   . ALA   B 1 38  ? 169.654 -60.602 20.408 1.00 13.99 ? 129 ALA   B O   1 
ATOM   1821 C  CB  . ALA   B 1 38  ? 167.314 -62.128 18.770 1.00 15.72 ? 129 ALA   B CB  1 
ATOM   1822 N  N   . LEU   B 1 39  ? 167.833 -59.307 20.226 1.00 10.62 ? 130 LEU   B N   1 
ATOM   1823 C  CA  . LEU   B 1 39  ? 168.581 -58.060 20.277 1.00 11.37 ? 130 LEU   B CA  1 
ATOM   1824 C  C   . LEU   B 1 39  ? 168.608 -57.436 21.664 1.00 15.07 ? 130 LEU   B C   1 
ATOM   1825 O  O   . LEU   B 1 39  ? 169.303 -56.429 21.853 1.00 13.26 ? 130 LEU   B O   1 
ATOM   1826 C  CB  . LEU   B 1 39  ? 167.971 -57.047 19.293 1.00 10.36 ? 130 LEU   B CB  1 
ATOM   1827 C  CG  . LEU   B 1 39  ? 167.939 -57.415 17.812 1.00 11.02 ? 130 LEU   B CG  1 
ATOM   1828 C  CD1 . LEU   B 1 39  ? 166.995 -56.495 17.039 1.00 10.78 ? 130 LEU   B CD1 1 
ATOM   1829 C  CD2 . LEU   B 1 39  ? 169.346 -57.356 17.229 1.00 15.09 ? 130 LEU   B CD2 1 
ATOM   1830 N  N   . ASN   B 1 40  ? 167.867 -58.003 22.616 1.00 11.37 ? 131 ASN   B N   1 
ATOM   1831 C  CA  . ASN   B 1 40  ? 167.530 -57.374 23.900 1.00 11.49 ? 131 ASN   B CA  1 
ATOM   1832 C  C   . ASN   B 1 40  ? 167.142 -55.912 23.693 1.00 11.67 ? 131 ASN   B C   1 
ATOM   1833 O  O   . ASN   B 1 40  ? 167.733 -54.989 24.253 1.00 13.23 ? 131 ASN   B O   1 
ATOM   1834 C  CB  . ASN   B 1 40  ? 168.674 -57.504 24.912 1.00 9.11  ? 131 ASN   B CB  1 
ATOM   1835 C  CG  . ASN   B 1 40  ? 168.314 -56.911 26.288 1.00 8.55  ? 131 ASN   B CG  1 
ATOM   1836 O  OD1 . ASN   B 1 40  ? 167.162 -56.977 26.730 1.00 8.13  ? 131 ASN   B OD1 1 
ATOM   1837 N  ND2 . ASN   B 1 40  ? 169.300 -56.311 26.949 1.00 14.76 ? 131 ASN   B ND2 1 
ATOM   1838 N  N   . LYS   B 1 41  ? 166.109 -55.712 22.879 1.00 8.33  ? 132 LYS   B N   1 
ATOM   1839 C  CA  . LYS   B 1 41  ? 165.776 -54.373 22.408 1.00 8.15  ? 132 LYS   B CA  1 
ATOM   1840 C  C   . LYS   B 1 41  ? 164.266 -54.205 22.279 1.00 7.84  ? 132 LYS   B C   1 
ATOM   1841 O  O   . LYS   B 1 41  ? 163.591 -55.029 21.654 1.00 8.62  ? 132 LYS   B O   1 
ATOM   1842 C  CB  . LYS   B 1 41  ? 166.464 -54.094 21.063 1.00 8.71  ? 132 LYS   B CB  1 
ATOM   1843 C  CG  . LYS   B 1 41  ? 166.259 -52.671 20.535 1.00 8.67  ? 132 LYS   B CG  1 
ATOM   1844 C  CD  . LYS   B 1 41  ? 167.217 -52.399 19.376 1.00 10.96 ? 132 LYS   B CD  1 
ATOM   1845 C  CE  . LYS   B 1 41  ? 167.037 -50.994 18.830 1.00 10.10 ? 132 LYS   B CE  1 
ATOM   1846 N  NZ  . LYS   B 1 41  ? 168.126 -50.651 17.882 1.00 12.92 ? 132 LYS   B NZ  1 
ATOM   1847 N  N   . LEU   B 1 42  ? 163.751 -53.137 22.874 1.00 7.47  ? 133 LEU   B N   1 
ATOM   1848 C  CA  . LEU   B 1 42  ? 162.341 -52.775 22.801 1.00 11.18 ? 133 LEU   B CA  1 
ATOM   1849 C  C   . LEU   B 1 42  ? 162.138 -51.789 21.662 1.00 13.12 ? 133 LEU   B C   1 
ATOM   1850 O  O   . LEU   B 1 42  ? 162.889 -50.818 21.544 1.00 12.25 ? 133 LEU   B O   1 
ATOM   1851 C  CB  . LEU   B 1 42  ? 161.886 -52.133 24.116 1.00 7.44  ? 133 LEU   B CB  1 
ATOM   1852 C  CG  . LEU   B 1 42  ? 160.427 -51.673 24.124 1.00 10.86 ? 133 LEU   B CG  1 
ATOM   1853 C  CD1 . LEU   B 1 42  ? 159.536 -52.887 24.065 1.00 12.44 ? 133 LEU   B CD1 1 
ATOM   1854 C  CD2 . LEU   B 1 42  ? 160.115 -50.842 25.357 1.00 10.18 ? 133 LEU   B CD2 1 
ATOM   1855 N  N   . PHE   B 1 43  ? 161.126 -52.030 20.829 1.00 7.80  ? 134 PHE   B N   1 
ATOM   1856 C  CA  . PHE   B 1 43  ? 160.763 -51.092 19.774 1.00 9.33  ? 134 PHE   B CA  1 
ATOM   1857 C  C   . PHE   B 1 43  ? 159.364 -50.580 20.068 1.00 10.27 ? 134 PHE   B C   1 
ATOM   1858 O  O   . PHE   B 1 43  ? 158.444 -51.381 20.251 1.00 10.77 ? 134 PHE   B O   1 
ATOM   1859 C  CB  . PHE   B 1 43  ? 160.777 -51.748 18.388 1.00 11.58 ? 134 PHE   B CB  1 
ATOM   1860 C  CG  . PHE   B 1 43  ? 162.102 -52.340 17.989 1.00 13.45 ? 134 PHE   B CG  1 
ATOM   1861 C  CD1 . PHE   B 1 43  ? 162.537 -53.535 18.543 1.00 10.26 ? 134 PHE   B CD1 1 
ATOM   1862 C  CD2 . PHE   B 1 43  ? 162.893 -51.708 17.038 1.00 11.76 ? 134 PHE   B CD2 1 
ATOM   1863 C  CE1 . PHE   B 1 43  ? 163.751 -54.086 18.174 1.00 11.09 ? 134 PHE   B CE1 1 
ATOM   1864 C  CE2 . PHE   B 1 43  ? 164.107 -52.253 16.646 1.00 9.59  ? 134 PHE   B CE2 1 
ATOM   1865 C  CZ  . PHE   B 1 43  ? 164.538 -53.452 17.214 1.00 9.55  ? 134 PHE   B CZ  1 
ATOM   1866 N  N   . CYS   B 1 44  ? 159.193 -49.260 20.066 1.00 9.07  ? 135 CYS   B N   1 
ATOM   1867 C  CA  . CYS   B 1 44  ? 157.912 -48.682 20.451 1.00 11.67 ? 135 CYS   B CA  1 
ATOM   1868 C  C   . CYS   B 1 44  ? 157.675 -47.370 19.717 1.00 15.61 ? 135 CYS   B C   1 
ATOM   1869 O  O   . CYS   B 1 44  ? 158.616 -46.670 19.329 1.00 13.82 ? 135 CYS   B O   1 
ATOM   1870 C  CB  . CYS   B 1 44  ? 157.846 -48.441 21.959 1.00 10.84 ? 135 CYS   B CB  1 
ATOM   1871 S  SG  . CYS   B 1 44  ? 159.051 -47.198 22.557 1.00 14.31 ? 135 CYS   B SG  1 
ATOM   1872 N  N   . GLN   B 1 45  ? 156.400 -47.041 19.544 1.00 11.03 ? 136 GLN   B N   1 
ATOM   1873 C  CA  . GLN   B 1 45  ? 156.020 -45.764 18.972 1.00 10.67 ? 136 GLN   B CA  1 
ATOM   1874 C  C   . GLN   B 1 45  ? 156.092 -44.670 20.030 1.00 9.74  ? 136 GLN   B C   1 
ATOM   1875 O  O   . GLN   B 1 45  ? 156.090 -44.929 21.235 1.00 10.97 ? 136 GLN   B O   1 
ATOM   1876 C  CB  . GLN   B 1 45  ? 154.607 -45.836 18.389 1.00 10.88 ? 136 GLN   B CB  1 
ATOM   1877 C  CG  . GLN   B 1 45  ? 154.508 -46.714 17.143 1.00 15.10 ? 136 GLN   B CG  1 
ATOM   1878 C  CD  . GLN   B 1 45  ? 153.084 -46.833 16.622 1.00 19.93 ? 136 GLN   B CD  1 
ATOM   1879 O  OE1 . GLN   B 1 45  ? 152.129 -46.523 17.328 1.00 19.15 ? 136 GLN   B OE1 1 
ATOM   1880 N  NE2 . GLN   B 1 45  ? 152.941 -47.262 15.375 1.00 21.14 ? 136 GLN   B NE2 1 
ATOM   1881 N  N   . LEU   B 1 46  ? 156.126 -43.428 19.552 1.00 14.52 ? 137 LEU   B N   1 
ATOM   1882 C  CA  . LEU   B 1 46  ? 156.186 -42.256 20.420 1.00 14.52 ? 137 LEU   B CA  1 
ATOM   1883 C  C   . LEU   B 1 46  ? 155.023 -42.211 21.406 1.00 11.70 ? 137 LEU   B C   1 
ATOM   1884 O  O   . LEU   B 1 46  ? 153.858 -42.215 20.999 1.00 13.67 ? 137 LEU   B O   1 
ATOM   1885 C  CB  . LEU   B 1 46  ? 156.174 -40.997 19.559 1.00 10.41 ? 137 LEU   B CB  1 
ATOM   1886 C  CG  . LEU   B 1 46  ? 156.211 -39.671 20.319 1.00 17.06 ? 137 LEU   B CG  1 
ATOM   1887 C  CD1 . LEU   B 1 46  ? 157.537 -39.517 20.996 1.00 13.88 ? 137 LEU   B CD1 1 
ATOM   1888 C  CD2 . LEU   B 1 46  ? 155.957 -38.494 19.375 1.00 17.17 ? 137 LEU   B CD2 1 
ATOM   1889 N  N   . ALA   B 1 47  ? 155.349 -42.140 22.699 1.00 10.31 ? 138 ALA   B N   1 
ATOM   1890 C  CA  . ALA   B 1 47  ? 154.423 -41.921 23.809 1.00 10.62 ? 138 ALA   B CA  1 
ATOM   1891 C  C   . ALA   B 1 47  ? 153.410 -43.047 23.988 1.00 17.58 ? 138 ALA   B C   1 
ATOM   1892 O  O   . ALA   B 1 47  ? 152.430 -42.874 24.717 1.00 24.57 ? 138 ALA   B O   1 
ATOM   1893 C  CB  . ALA   B 1 47  ? 153.671 -40.586 23.675 1.00 15.89 ? 138 ALA   B CB  1 
ATOM   1894 N  N   . LYS   B 1 48  ? 153.616 -44.199 23.365 1.00 9.94  ? 139 LYS   B N   1 
ATOM   1895 C  CA  . LYS   B 1 48  ? 152.666 -45.289 23.515 1.00 10.09 ? 139 LYS   B CA  1 
ATOM   1896 C  C   . LYS   B 1 48  ? 153.035 -46.153 24.720 1.00 12.87 ? 139 LYS   B C   1 
ATOM   1897 O  O   . LYS   B 1 48  ? 154.174 -46.160 25.181 1.00 9.52  ? 139 LYS   B O   1 
ATOM   1898 C  CB  . LYS   B 1 48  ? 152.613 -46.141 22.241 1.00 11.30 ? 139 LYS   B CB  1 
ATOM   1899 C  CG  . LYS   B 1 48  ? 152.137 -45.367 20.987 1.00 11.64 ? 139 LYS   B CG  1 
ATOM   1900 C  CD  . LYS   B 1 48  ? 150.821 -44.674 21.208 1.00 23.27 ? 139 LYS   B CD  1 
ATOM   1901 C  CE  . LYS   B 1 48  ? 150.434 -43.794 20.007 1.00 32.79 ? 139 LYS   B CE  1 
ATOM   1902 N  NZ  . LYS   B 1 48  ? 150.589 -44.523 18.729 1.00 36.24 ? 139 LYS   B NZ  1 
ATOM   1903 N  N   . THR   B 1 49  ? 152.049 -46.897 25.216 1.00 9.18  ? 140 THR   B N   1 
ATOM   1904 C  CA  . THR   B 1 49  ? 152.238 -47.706 26.416 1.00 8.76  ? 140 THR   B CA  1 
ATOM   1905 C  C   . THR   B 1 49  ? 153.204 -48.863 26.169 1.00 11.97 ? 140 THR   B C   1 
ATOM   1906 O  O   . THR   B 1 49  ? 153.027 -49.639 25.227 1.00 14.86 ? 140 THR   B O   1 
ATOM   1907 C  CB  . THR   B 1 49  ? 150.889 -48.249 26.880 1.00 12.17 ? 140 THR   B CB  1 
ATOM   1908 O  OG1 . THR   B 1 49  ? 149.976 -47.158 27.050 1.00 10.70 ? 140 THR   B OG1 1 
ATOM   1909 C  CG2 . THR   B 1 49  ? 151.052 -48.997 28.189 1.00 14.61 ? 140 THR   B CG2 1 
ATOM   1910 N  N   . CYS   B 1 50  ? 154.214 -48.989 27.035 1.00 8.99  ? 141 CYS   B N   1 
ATOM   1911 C  CA  . CYS   B 1 50  ? 155.210 -50.062 26.965 1.00 8.95  ? 141 CYS   B CA  1 
ATOM   1912 C  C   . CYS   B 1 50  ? 155.145 -50.883 28.236 1.00 10.84 ? 141 CYS   B C   1 
ATOM   1913 O  O   . CYS   B 1 50  ? 155.701 -50.472 29.271 1.00 9.78  ? 141 CYS   B O   1 
ATOM   1914 C  CB  . CYS   B 1 50  ? 156.621 -49.504 26.788 1.00 10.68 ? 141 CYS   B CB  1 
ATOM   1915 S  SG  . CYS   B 1 50  ? 156.843 -48.587 25.255 1.00 10.95 ? 141 CYS   B SG  1 
ATOM   1916 N  N   . PRO   B 1 51  ? 154.496 -52.044 28.215 1.00 9.35  ? 142 PRO   B N   1 
ATOM   1917 C  CA  . PRO   B 1 51  ? 154.401 -52.860 29.431 1.00 9.07  ? 142 PRO   B CA  1 
ATOM   1918 C  C   . PRO   B 1 51  ? 155.706 -53.602 29.675 1.00 14.07 ? 142 PRO   B C   1 
ATOM   1919 O  O   . PRO   B 1 51  ? 156.244 -54.263 28.780 1.00 11.47 ? 142 PRO   B O   1 
ATOM   1920 C  CB  . PRO   B 1 51  ? 153.257 -53.839 29.121 1.00 10.18 ? 142 PRO   B CB  1 
ATOM   1921 C  CG  . PRO   B 1 51  ? 152.721 -53.451 27.769 1.00 14.59 ? 142 PRO   B CG  1 
ATOM   1922 C  CD  . PRO   B 1 51  ? 153.765 -52.643 27.085 1.00 13.38 ? 142 PRO   B CD  1 
ATOM   1923 N  N   . VAL   B 1 52  ? 156.205 -53.507 30.903 1.00 11.62 ? 143 VAL   B N   1 
ATOM   1924 C  CA  . VAL   B 1 52  ? 157.422 -54.197 31.305 1.00 8.61  ? 143 VAL   B CA  1 
ATOM   1925 C  C   . VAL   B 1 52  ? 157.113 -54.969 32.580 1.00 11.50 ? 143 VAL   B C   1 
ATOM   1926 O  O   . VAL   B 1 52  ? 156.634 -54.392 33.563 1.00 9.80  ? 143 VAL   B O   1 
ATOM   1927 C  CB  . VAL   B 1 52  ? 158.594 -53.224 31.507 1.00 10.31 ? 143 VAL   B CB  1 
ATOM   1928 C  CG1 . VAL   B 1 52  ? 159.872 -53.966 31.924 1.00 8.54  ? 143 VAL   B CG1 1 
ATOM   1929 C  CG2 . VAL   B 1 52  ? 158.853 -52.460 30.200 1.00 12.24 ? 143 VAL   B CG2 1 
ATOM   1930 N  N   . GLN   B 1 53  ? 157.367 -56.269 32.558 1.00 6.66  ? 144 GLN   B N   1 
ATOM   1931 C  CA  . GLN   B 1 53  ? 157.088 -57.089 33.730 1.00 7.71  ? 144 GLN   B CA  1 
ATOM   1932 C  C   . GLN   B 1 53  ? 158.237 -57.024 34.716 1.00 9.94  ? 144 GLN   B C   1 
ATOM   1933 O  O   . GLN   B 1 53  ? 159.406 -56.932 34.333 1.00 9.08  ? 144 GLN   B O   1 
ATOM   1934 C  CB  . GLN   B 1 53  ? 156.859 -58.547 33.333 1.00 8.97  ? 144 GLN   B CB  1 
ATOM   1935 C  CG  . GLN   B 1 53  ? 155.716 -58.735 32.378 1.00 11.84 ? 144 GLN   B CG  1 
ATOM   1936 C  CD  . GLN   B 1 53  ? 155.574 -60.167 31.942 1.00 14.89 ? 144 GLN   B CD  1 
ATOM   1937 O  OE1 . GLN   B 1 53  ? 156.545 -60.915 31.903 1.00 12.89 ? 144 GLN   B OE1 1 
ATOM   1938 N  NE2 . GLN   B 1 53  ? 154.354 -60.564 31.630 1.00 20.43 ? 144 GLN   B NE2 1 
ATOM   1939 N  N   . LEU   B 1 54  ? 157.898 -57.137 36.002 1.00 8.16  ? 145 LEU   B N   1 
ATOM   1940 C  CA  . LEU   B 1 54  ? 158.892 -57.220 37.061 1.00 9.66  ? 145 LEU   B CA  1 
ATOM   1941 C  C   . LEU   B 1 54  ? 158.767 -58.580 37.732 1.00 8.33  ? 145 LEU   B C   1 
ATOM   1942 O  O   . LEU   B 1 54  ? 157.684 -58.946 38.206 1.00 10.00 ? 145 LEU   B O   1 
ATOM   1943 C  CB  . LEU   B 1 54  ? 158.708 -56.092 38.079 1.00 13.61 ? 145 LEU   B CB  1 
ATOM   1944 C  CG  . LEU   B 1 54  ? 158.656 -54.667 37.515 1.00 10.47 ? 145 LEU   B CG  1 
ATOM   1945 C  CD1 . LEU   B 1 54  ? 158.305 -53.708 38.665 1.00 14.57 ? 145 LEU   B CD1 1 
ATOM   1946 C  CD2 . LEU   B 1 54  ? 159.976 -54.267 36.877 1.00 8.29  ? 145 LEU   B CD2 1 
ATOM   1947 N  N   . TRP   B 1 55  ? 159.872 -59.315 37.776 1.00 7.26  ? 146 TRP   B N   1 
ATOM   1948 C  CA  . TRP   B 1 55  ? 159.924 -60.656 38.337 1.00 9.31  ? 146 TRP   B CA  1 
ATOM   1949 C  C   . TRP   B 1 55  ? 160.960 -60.727 39.446 1.00 7.73  ? 146 TRP   B C   1 
ATOM   1950 O  O   . TRP   B 1 55  ? 162.072 -60.216 39.293 1.00 11.04 ? 146 TRP   B O   1 
ATOM   1951 C  CB  . TRP   B 1 55  ? 160.301 -61.693 37.267 1.00 7.88  ? 146 TRP   B CB  1 
ATOM   1952 C  CG  . TRP   B 1 55  ? 159.263 -61.910 36.202 1.00 8.76  ? 146 TRP   B CG  1 
ATOM   1953 C  CD1 . TRP   B 1 55  ? 159.136 -61.233 35.025 1.00 11.59 ? 146 TRP   B CD1 1 
ATOM   1954 C  CD2 . TRP   B 1 55  ? 158.237 -62.901 36.205 1.00 10.87 ? 146 TRP   B CD2 1 
ATOM   1955 N  NE1 . TRP   B 1 55  ? 158.089 -61.737 34.298 1.00 11.19 ? 146 TRP   B NE1 1 
ATOM   1956 C  CE2 . TRP   B 1 55  ? 157.518 -62.763 35.000 1.00 10.27 ? 146 TRP   B CE2 1 
ATOM   1957 C  CE3 . TRP   B 1 55  ? 157.858 -63.898 37.108 1.00 11.81 ? 146 TRP   B CE3 1 
ATOM   1958 C  CZ2 . TRP   B 1 55  ? 156.441 -63.576 34.680 1.00 13.40 ? 146 TRP   B CZ2 1 
ATOM   1959 C  CZ3 . TRP   B 1 55  ? 156.788 -64.702 36.793 1.00 13.96 ? 146 TRP   B CZ3 1 
ATOM   1960 C  CH2 . TRP   B 1 55  ? 156.088 -64.536 35.592 1.00 13.33 ? 146 TRP   B CH2 1 
ATOM   1961 N  N   . VAL   B 1 56  ? 160.606 -61.402 40.547 1.00 8.12  ? 147 VAL   B N   1 
ATOM   1962 C  CA  . VAL   B 1 56  ? 161.570 -61.790 41.572 1.00 8.64  ? 147 VAL   B CA  1 
ATOM   1963 C  C   . VAL   B 1 56  ? 161.301 -63.229 41.989 1.00 9.06  ? 147 VAL   B C   1 
ATOM   1964 O  O   . VAL   B 1 56  ? 160.181 -63.732 41.864 1.00 10.82 ? 147 VAL   B O   1 
ATOM   1965 C  CB  . VAL   B 1 56  ? 161.522 -60.876 42.818 1.00 11.04 ? 147 VAL   B CB  1 
ATOM   1966 C  CG1 . VAL   B 1 56  ? 162.118 -59.499 42.514 1.00 9.82  ? 147 VAL   B CG1 1 
ATOM   1967 C  CG2 . VAL   B 1 56  ? 160.106 -60.756 43.316 1.00 8.89  ? 147 VAL   B CG2 1 
ATOM   1968 N  N   . ASP   B 1 57  ? 162.341 -63.895 42.497 1.00 11.78 ? 148 ASP   B N   1 
ATOM   1969 C  CA  . ASP   B 1 57  ? 162.151 -65.215 43.093 1.00 11.14 ? 148 ASP   B CA  1 
ATOM   1970 C  C   . ASP   B 1 57  ? 161.562 -65.133 44.495 1.00 16.68 ? 148 ASP   B C   1 
ATOM   1971 O  O   . ASP   B 1 57  ? 160.898 -66.075 44.932 1.00 12.47 ? 148 ASP   B O   1 
ATOM   1972 C  CB  . ASP   B 1 57  ? 163.473 -65.976 43.161 1.00 11.89 ? 148 ASP   B CB  1 
ATOM   1973 C  CG  . ASP   B 1 57  ? 164.017 -66.314 41.792 1.00 15.94 ? 148 ASP   B CG  1 
ATOM   1974 O  OD1 . ASP   B 1 57  ? 163.202 -66.565 40.885 1.00 17.67 ? 148 ASP   B OD1 1 
ATOM   1975 O  OD2 . ASP   B 1 57  ? 165.254 -66.311 41.626 1.00 20.71 ? 148 ASP   B OD2 1 
ATOM   1976 N  N   . SER   B 1 58  ? 161.829 -64.051 45.218 1.00 10.34 ? 149 SER   B N   1 
ATOM   1977 C  CA  . SER   B 1 58  ? 161.301 -63.861 46.564 1.00 13.84 ? 149 SER   B CA  1 
ATOM   1978 C  C   . SER   B 1 58  ? 160.958 -62.392 46.764 1.00 11.68 ? 149 SER   B C   1 
ATOM   1979 O  O   . SER   B 1 58  ? 161.609 -61.500 46.214 1.00 9.76  ? 149 SER   B O   1 
ATOM   1980 C  CB  . SER   B 1 58  ? 162.287 -64.350 47.644 1.00 20.86 ? 149 SER   B CB  1 
ATOM   1981 O  OG  . SER   B 1 58  ? 163.586 -63.829 47.447 1.00 27.93 ? 149 SER   B OG  1 
ATOM   1982 N  N   . THR   B 1 59  ? 159.917 -62.153 47.552 1.00 13.62 ? 150 THR   B N   1 
ATOM   1983 C  CA  . THR   B 1 59  ? 159.361 -60.815 47.697 1.00 14.25 ? 150 THR   B CA  1 
ATOM   1984 C  C   . THR   B 1 59  ? 160.307 -59.908 48.476 1.00 12.28 ? 150 THR   B C   1 
ATOM   1985 O  O   . THR   B 1 59  ? 160.693 -60.258 49.602 1.00 10.31 ? 150 THR   B O   1 
ATOM   1986 C  CB  . THR   B 1 59  ? 158.012 -60.911 48.406 1.00 15.91 ? 150 THR   B CB  1 
ATOM   1987 O  OG1 . THR   B 1 59  ? 157.076 -61.603 47.567 1.00 13.20 ? 150 THR   B OG1 1 
ATOM   1988 C  CG2 . THR   B 1 59  ? 157.484 -59.520 48.758 1.00 13.29 ? 150 THR   B CG2 1 
ATOM   1989 N  N   . PRO   B 1 60  ? 160.713 -58.765 47.925 1.00 10.43 ? 151 PRO   B N   1 
ATOM   1990 C  CA  . PRO   B 1 60  ? 161.582 -57.832 48.660 1.00 9.37  ? 151 PRO   B CA  1 
ATOM   1991 C  C   . PRO   B 1 60  ? 160.783 -57.020 49.667 1.00 9.61  ? 151 PRO   B C   1 
ATOM   1992 O  O   . PRO   B 1 60  ? 159.550 -57.116 49.719 1.00 11.55 ? 151 PRO   B O   1 
ATOM   1993 C  CB  . PRO   B 1 60  ? 162.155 -56.944 47.540 1.00 8.86  ? 151 PRO   B CB  1 
ATOM   1994 C  CG  . PRO   B 1 60  ? 161.061 -56.924 46.508 1.00 16.34 ? 151 PRO   B CG  1 
ATOM   1995 C  CD  . PRO   B 1 60  ? 160.479 -58.315 46.534 1.00 8.69  ? 151 PRO   B CD  1 
ATOM   1996 N  N   . PRO   B 1 61  ? 161.448 -56.216 50.501 1.00 13.00 ? 152 PRO   B N   1 
ATOM   1997 C  CA  . PRO   B 1 61  ? 160.739 -55.555 51.599 1.00 13.61 ? 152 PRO   B CA  1 
ATOM   1998 C  C   . PRO   B 1 61  ? 159.764 -54.502 51.098 1.00 10.35 ? 152 PRO   B C   1 
ATOM   1999 O  O   . PRO   B 1 61  ? 159.971 -53.898 50.033 1.00 10.97 ? 152 PRO   B O   1 
ATOM   2000 C  CB  . PRO   B 1 61  ? 161.875 -54.914 52.416 1.00 15.45 ? 152 PRO   B CB  1 
ATOM   2001 C  CG  . PRO   B 1 61  ? 163.037 -55.849 52.196 1.00 12.43 ? 152 PRO   B CG  1 
ATOM   2002 C  CD  . PRO   B 1 61  ? 162.907 -56.259 50.736 1.00 10.13 ? 152 PRO   B CD  1 
ATOM   2003 N  N   . PRO   B 1 62  ? 158.673 -54.263 51.832 1.00 11.39 ? 153 PRO   B N   1 
ATOM   2004 C  CA  . PRO   B 1 62  ? 157.887 -53.038 51.631 1.00 10.39 ? 153 PRO   B CA  1 
ATOM   2005 C  C   . PRO   B 1 62  ? 158.793 -51.817 51.603 1.00 10.31 ? 153 PRO   B C   1 
ATOM   2006 O  O   . PRO   B 1 62  ? 159.728 -51.701 52.396 1.00 13.65 ? 153 PRO   B O   1 
ATOM   2007 C  CB  . PRO   B 1 62  ? 156.962 -53.000 52.856 1.00 12.59 ? 153 PRO   B CB  1 
ATOM   2008 C  CG  . PRO   B 1 62  ? 156.874 -54.412 53.330 1.00 11.89 ? 153 PRO   B CG  1 
ATOM   2009 C  CD  . PRO   B 1 62  ? 158.186 -55.069 52.966 1.00 11.05 ? 153 PRO   B CD  1 
ATOM   2010 N  N   . GLY   B 1 63  ? 158.509 -50.896 50.687 1.00 9.98  ? 154 GLY   B N   1 
ATOM   2011 C  CA  . GLY   B 1 63  ? 159.338 -49.715 50.519 1.00 14.13 ? 154 GLY   B CA  1 
ATOM   2012 C  C   . GLY   B 1 63  ? 160.401 -49.852 49.455 1.00 12.20 ? 154 GLY   B C   1 
ATOM   2013 O  O   . GLY   B 1 63  ? 161.043 -48.850 49.099 1.00 9.80  ? 154 GLY   B O   1 
ATOM   2014 N  N   . THR   B 1 64  ? 160.617 -51.063 48.952 1.00 9.13  ? 155 THR   B N   1 
ATOM   2015 C  CA  . THR   B 1 64  ? 161.410 -51.263 47.746 1.00 9.46  ? 155 THR   B CA  1 
ATOM   2016 C  C   . THR   B 1 64  ? 160.789 -50.490 46.590 1.00 12.60 ? 155 THR   B C   1 
ATOM   2017 O  O   . THR   B 1 64  ? 159.562 -50.428 46.460 1.00 8.25  ? 155 THR   B O   1 
ATOM   2018 C  CB  . THR   B 1 64  ? 161.469 -52.762 47.408 1.00 8.72  ? 155 THR   B CB  1 
ATOM   2019 O  OG1 . THR   B 1 64  ? 162.034 -53.479 48.513 1.00 9.54  ? 155 THR   B OG1 1 
ATOM   2020 C  CG2 . THR   B 1 64  ? 162.312 -53.018 46.159 1.00 8.11  ? 155 THR   B CG2 1 
ATOM   2021 N  N   . ARG   B 1 65  ? 161.640 -49.903 45.744 1.00 10.13 ? 156 ARG   B N   1 
ATOM   2022 C  CA  . ARG   B 1 65  ? 161.184 -49.112 44.611 1.00 9.78  ? 156 ARG   B CA  1 
ATOM   2023 C  C   . ARG   B 1 65  ? 161.899 -49.573 43.344 1.00 13.80 ? 156 ARG   B C   1 
ATOM   2024 O  O   . ARG   B 1 65  ? 162.881 -50.315 43.387 1.00 8.80  ? 156 ARG   B O   1 
ATOM   2025 C  CB  . ARG   B 1 65  ? 161.416 -47.615 44.836 1.00 9.89  ? 156 ARG   B CB  1 
ATOM   2026 C  CG  . ARG   B 1 65  ? 160.710 -47.061 46.084 1.00 10.84 ? 156 ARG   B CG  1 
ATOM   2027 C  CD  . ARG   B 1 65  ? 160.453 -45.554 45.941 1.00 11.05 ? 156 ARG   B CD  1 
ATOM   2028 N  NE  . ARG   B 1 65  ? 161.684 -44.765 45.981 1.00 11.71 ? 156 ARG   B NE  1 
ATOM   2029 C  CZ  . ARG   B 1 65  ? 161.730 -43.447 45.809 1.00 14.18 ? 156 ARG   B CZ  1 
ATOM   2030 N  NH1 . ARG   B 1 65  ? 160.611 -42.773 45.575 1.00 11.29 ? 156 ARG   B NH1 1 
ATOM   2031 N  NH2 . ARG   B 1 65  ? 162.891 -42.801 45.869 1.00 10.96 ? 156 ARG   B NH2 1 
ATOM   2032 N  N   . VAL   B 1 66  ? 161.376 -49.145 42.202 1.00 8.76  ? 157 VAL   B N   1 
ATOM   2033 C  CA  A VAL   B 1 66  ? 161.947 -49.495 40.911 0.36 8.76  ? 157 VAL   B CA  1 
ATOM   2034 C  CA  B VAL   B 1 66  ? 161.913 -49.504 40.891 0.64 8.40  ? 157 VAL   B CA  1 
ATOM   2035 C  C   . VAL   B 1 66  ? 162.115 -48.216 40.110 1.00 7.90  ? 157 VAL   B C   1 
ATOM   2036 O  O   . VAL   B 1 66  ? 161.163 -47.443 39.941 1.00 9.80  ? 157 VAL   B O   1 
ATOM   2037 C  CB  A VAL   B 1 66  ? 161.088 -50.524 40.153 0.36 8.92  ? 157 VAL   B CB  1 
ATOM   2038 C  CB  B VAL   B 1 66  ? 160.980 -50.458 40.127 0.64 8.73  ? 157 VAL   B CB  1 
ATOM   2039 C  CG1 A VAL   B 1 66  ? 159.639 -50.178 40.269 0.36 8.84  ? 157 VAL   B CG1 1 
ATOM   2040 C  CG1 B VAL   B 1 66  ? 161.539 -50.736 38.751 0.64 7.94  ? 157 VAL   B CG1 1 
ATOM   2041 C  CG2 A VAL   B 1 66  ? 161.509 -50.598 38.702 0.36 8.41  ? 157 VAL   B CG2 1 
ATOM   2042 C  CG2 B VAL   B 1 66  ? 160.796 -51.758 40.904 0.64 8.72  ? 157 VAL   B CG2 1 
ATOM   2043 N  N   . ARG   B 1 67  ? 163.335 -47.985 39.640 1.00 7.53  ? 158 ARG   B N   1 
ATOM   2044 C  CA  . ARG   B 1 67  ? 163.710 -46.760 38.952 1.00 7.75  ? 158 ARG   B CA  1 
ATOM   2045 C  C   . ARG   B 1 67  ? 164.092 -47.069 37.515 1.00 11.97 ? 158 ARG   B C   1 
ATOM   2046 O  O   . ARG   B 1 67  ? 164.697 -48.110 37.228 1.00 7.34  ? 158 ARG   B O   1 
ATOM   2047 C  CB  . ARG   B 1 67  ? 164.880 -46.073 39.673 1.00 7.41  ? 158 ARG   B CB  1 
ATOM   2048 C  CG  . ARG   B 1 67  ? 165.401 -44.787 39.010 1.00 7.24  ? 158 ARG   B CG  1 
ATOM   2049 C  CD  . ARG   B 1 67  ? 166.560 -44.198 39.817 1.00 8.82  ? 158 ARG   B CD  1 
ATOM   2050 N  NE  . ARG   B 1 67  ? 166.213 -44.102 41.239 1.00 10.55 ? 158 ARG   B NE  1 
ATOM   2051 C  CZ  . ARG   B 1 67  ? 165.602 -43.064 41.811 1.00 8.38  ? 158 ARG   B CZ  1 
ATOM   2052 N  NH1 . ARG   B 1 67  ? 165.268 -41.989 41.103 1.00 8.28  ? 158 ARG   B NH1 1 
ATOM   2053 N  NH2 . ARG   B 1 67  ? 165.317 -43.101 43.103 1.00 9.46  ? 158 ARG   B NH2 1 
ATOM   2054 N  N   . ALA   B 1 68  ? 163.741 -46.160 36.614 1.00 7.37  ? 159 ALA   B N   1 
ATOM   2055 C  CA  . ALA   B 1 68  ? 164.094 -46.277 35.208 1.00 6.68  ? 159 ALA   B CA  1 
ATOM   2056 C  C   . ALA   B 1 68  ? 164.919 -45.065 34.819 1.00 8.70  ? 159 ALA   B C   1 
ATOM   2057 O  O   . ALA   B 1 68  ? 164.617 -43.944 35.241 1.00 8.27  ? 159 ALA   B O   1 
ATOM   2058 C  CB  . ALA   B 1 68  ? 162.847 -46.362 34.313 1.00 8.72  ? 159 ALA   B CB  1 
ATOM   2059 N  N   . MET   B 1 69  ? 165.953 -45.292 34.014 1.00 10.89 ? 160 MET   B N   1 
ATOM   2060 C  CA  . MET   B 1 69  ? 166.839 -44.226 33.569 1.00 10.35 ? 160 MET   B CA  1 
ATOM   2061 C  C   . MET   B 1 69  ? 167.346 -44.604 32.183 1.00 8.99  ? 160 MET   B C   1 
ATOM   2062 O  O   . MET   B 1 69  ? 167.568 -45.783 31.915 1.00 10.35 ? 160 MET   B O   1 
ATOM   2063 C  CB  . MET   B 1 69  ? 168.001 -44.052 34.557 1.00 9.19  ? 160 MET   B CB  1 
ATOM   2064 C  CG  . MET   B 1 69  ? 169.039 -43.012 34.165 1.00 17.99 ? 160 MET   B CG  1 
ATOM   2065 S  SD  . MET   B 1 69  ? 170.451 -43.086 35.293 1.00 15.68 ? 160 MET   B SD  1 
ATOM   2066 C  CE  . MET   B 1 69  ? 169.681 -42.528 36.835 1.00 17.40 ? 160 MET   B CE  1 
ATOM   2067 N  N   . ALA   B 1 70  ? 167.535 -43.620 31.309 1.00 6.66  ? 161 ALA   B N   1 
ATOM   2068 C  CA  . ALA   B 1 70  ? 168.070 -43.872 29.977 1.00 9.05  ? 161 ALA   B CA  1 
ATOM   2069 C  C   . ALA   B 1 70  ? 169.491 -43.330 29.871 1.00 7.22  ? 161 ALA   B C   1 
ATOM   2070 O  O   . ALA   B 1 70  ? 169.782 -42.253 30.387 1.00 9.99  ? 161 ALA   B O   1 
ATOM   2071 C  CB  . ALA   B 1 70  ? 167.198 -43.220 28.894 1.00 9.55  ? 161 ALA   B CB  1 
ATOM   2072 N  N   . ILE   B 1 71  ? 170.370 -44.075 29.184 1.00 12.36 ? 162 ILE   B N   1 
ATOM   2073 C  CA  . ILE   B 1 71  ? 171.703 -43.606 28.810 1.00 8.19  ? 162 ILE   B CA  1 
ATOM   2074 C  C   . ILE   B 1 71  ? 171.927 -43.942 27.348 1.00 8.67  ? 162 ILE   B C   1 
ATOM   2075 O  O   . ILE   B 1 71  ? 171.284 -44.830 26.796 1.00 8.68  ? 162 ILE   B O   1 
ATOM   2076 C  CB  . ILE   B 1 71  ? 172.838 -44.223 29.657 1.00 11.02 ? 162 ILE   B CB  1 
ATOM   2077 C  CG1 . ILE   B 1 71  ? 172.897 -45.748 29.482 1.00 11.40 ? 162 ILE   B CG1 1 
ATOM   2078 C  CG2 . ILE   B 1 71  ? 172.680 -43.852 31.110 1.00 13.70 ? 162 ILE   B CG2 1 
ATOM   2079 C  CD1 . ILE   B 1 71  ? 174.234 -46.364 29.991 1.00 12.92 ? 162 ILE   B CD1 1 
ATOM   2080 N  N   . TYR   B 1 72  ? 172.871 -43.230 26.725 1.00 11.17 ? 163 TYR   B N   1 
ATOM   2081 C  CA  . TYR   B 1 72  ? 173.298 -43.589 25.377 1.00 9.93  ? 163 TYR   B CA  1 
ATOM   2082 C  C   . TYR   B 1 72  ? 174.150 -44.849 25.404 1.00 11.38 ? 163 TYR   B C   1 
ATOM   2083 O  O   . TYR   B 1 72  ? 174.984 -45.037 26.293 1.00 12.79 ? 163 TYR   B O   1 
ATOM   2084 C  CB  . TYR   B 1 72  ? 174.072 -42.442 24.719 1.00 10.47 ? 163 TYR   B CB  1 
ATOM   2085 C  CG  . TYR   B 1 72  ? 173.144 -41.308 24.362 1.00 9.97  ? 163 TYR   B CG  1 
ATOM   2086 C  CD1 . TYR   B 1 72  ? 172.191 -41.463 23.357 1.00 9.89  ? 163 TYR   B CD1 1 
ATOM   2087 C  CD2 . TYR   B 1 72  ? 173.182 -40.108 25.059 1.00 9.68  ? 163 TYR   B CD2 1 
ATOM   2088 C  CE1 . TYR   B 1 72  ? 171.314 -40.436 23.041 1.00 9.51  ? 163 TYR   B CE1 1 
ATOM   2089 C  CE2 . TYR   B 1 72  ? 172.312 -39.074 24.749 1.00 9.29  ? 163 TYR   B CE2 1 
ATOM   2090 C  CZ  . TYR   B 1 72  ? 171.380 -39.249 23.738 1.00 16.14 ? 163 TYR   B CZ  1 
ATOM   2091 O  OH  . TYR   B 1 72  ? 170.496 -38.238 23.434 1.00 14.41 ? 163 TYR   B OH  1 
ATOM   2092 N  N   . LYS   B 1 73  ? 173.936 -45.710 24.408 1.00 11.03 ? 164 LYS   B N   1 
ATOM   2093 C  CA  . LYS   B 1 73  ? 174.593 -47.014 24.367 1.00 11.81 ? 164 LYS   B CA  1 
ATOM   2094 C  C   . LYS   B 1 73  ? 176.042 -46.909 23.907 1.00 18.00 ? 164 LYS   B C   1 
ATOM   2095 O  O   . LYS   B 1 73  ? 176.914 -47.617 24.423 1.00 13.38 ? 164 LYS   B O   1 
ATOM   2096 C  CB  . LYS   B 1 73  ? 173.812 -47.950 23.444 1.00 13.95 ? 164 LYS   B CB  1 
ATOM   2097 C  CG  . LYS   B 1 73  ? 174.425 -49.338 23.282 1.00 18.20 ? 164 LYS   B CG  1 
ATOM   2098 C  CD  . LYS   B 1 73  ? 173.678 -50.129 22.216 1.00 26.14 ? 164 LYS   B CD  1 
ATOM   2099 C  CE  . LYS   B 1 73  ? 174.299 -51.503 22.026 1.00 33.67 ? 164 LYS   B CE  1 
ATOM   2100 N  NZ  . LYS   B 1 73  ? 173.769 -52.159 20.806 1.00 38.70 ? 164 LYS   B NZ  1 
ATOM   2101 N  N   . GLN   B 1 74  ? 176.315 -46.048 22.933 1.00 13.35 ? 165 GLN   B N   1 
ATOM   2102 C  CA  . GLN   B 1 74  ? 177.658 -45.936 22.379 1.00 17.60 ? 165 GLN   B CA  1 
ATOM   2103 C  C   . GLN   B 1 74  ? 178.615 -45.275 23.366 1.00 24.31 ? 165 GLN   B C   1 
ATOM   2104 O  O   . GLN   B 1 74  ? 178.279 -44.284 24.019 1.00 13.99 ? 165 GLN   B O   1 
ATOM   2105 C  CB  . GLN   B 1 74  ? 177.616 -45.138 21.082 1.00 19.10 ? 165 GLN   B CB  1 
ATOM   2106 C  CG  . GLN   B 1 74  ? 176.853 -45.844 19.978 1.00 21.82 ? 165 GLN   B CG  1 
ATOM   2107 C  CD  . GLN   B 1 74  ? 176.513 -44.910 18.843 1.00 24.12 ? 165 GLN   B CD  1 
ATOM   2108 O  OE1 . GLN   B 1 74  ? 175.800 -43.927 19.029 1.00 21.67 ? 165 GLN   B OE1 1 
ATOM   2109 N  NE2 . GLN   B 1 74  ? 177.040 -45.201 17.654 1.00 36.33 ? 165 GLN   B NE2 1 
ATOM   2110 N  N   . SER   B 1 75  ? 179.824 -45.834 23.449 1.00 23.85 ? 166 SER   B N   1 
ATOM   2111 C  CA  . SER   B 1 75  ? 180.812 -45.403 24.436 1.00 20.43 ? 166 SER   B CA  1 
ATOM   2112 C  C   . SER   B 1 75  ? 181.072 -43.897 24.365 1.00 20.89 ? 166 SER   B C   1 
ATOM   2113 O  O   . SER   B 1 75  ? 181.157 -43.220 25.397 1.00 16.00 ? 166 SER   B O   1 
ATOM   2114 C  CB  . SER   B 1 75  ? 182.101 -46.209 24.222 1.00 22.11 ? 166 SER   B CB  1 
ATOM   2115 O  OG  . SER   B 1 75  ? 183.241 -45.574 24.763 1.00 30.76 ? 166 SER   B OG  1 
ATOM   2116 N  N   . GLN   B 1 76  ? 181.181 -43.349 23.155 1.00 20.14 ? 167 GLN   B N   1 
ATOM   2117 C  CA  . GLN   B 1 76  ? 181.514 -41.936 23.021 1.00 22.02 ? 167 GLN   B CA  1 
ATOM   2118 C  C   . GLN   B 1 76  ? 180.365 -41.012 23.396 1.00 17.26 ? 167 GLN   B C   1 
ATOM   2119 O  O   . GLN   B 1 76  ? 180.575 -39.797 23.469 1.00 15.95 ? 167 GLN   B O   1 
ATOM   2120 C  CB  . GLN   B 1 76  ? 181.952 -41.623 21.593 1.00 26.24 ? 167 GLN   B CB  1 
ATOM   2121 C  CG  . GLN   B 1 76  ? 180.842 -41.780 20.573 1.00 30.28 ? 167 GLN   B CG  1 
ATOM   2122 C  CD  . GLN   B 1 76  ? 180.886 -43.120 19.880 1.00 34.61 ? 167 GLN   B CD  1 
ATOM   2123 O  OE1 . GLN   B 1 76  ? 181.164 -44.149 20.502 1.00 32.16 ? 167 GLN   B OE1 1 
ATOM   2124 N  NE2 . GLN   B 1 76  ? 180.630 -43.116 18.574 1.00 38.92 ? 167 GLN   B NE2 1 
ATOM   2125 N  N   . HIS   B 1 77  ? 179.161 -41.537 23.612 1.00 14.61 ? 168 HIS   B N   1 
ATOM   2126 C  CA  . HIS   B 1 77  ? 178.019 -40.715 23.990 1.00 13.41 ? 168 HIS   B CA  1 
ATOM   2127 C  C   . HIS   B 1 77  ? 177.511 -41.003 25.399 1.00 12.48 ? 168 HIS   B C   1 
ATOM   2128 O  O   . HIS   B 1 77  ? 176.577 -40.340 25.850 1.00 11.70 ? 168 HIS   B O   1 
ATOM   2129 C  CB  . HIS   B 1 77  ? 176.878 -40.903 22.982 1.00 14.50 ? 168 HIS   B CB  1 
ATOM   2130 C  CG  . HIS   B 1 77  ? 177.236 -40.471 21.592 1.00 13.83 ? 168 HIS   B CG  1 
ATOM   2131 N  ND1 . HIS   B 1 77  ? 177.519 -39.162 21.272 1.00 16.71 ? 168 HIS   B ND1 1 
ATOM   2132 C  CD2 . HIS   B 1 77  ? 177.377 -41.178 20.444 1.00 17.19 ? 168 HIS   B CD2 1 
ATOM   2133 C  CE1 . HIS   B 1 77  ? 177.813 -39.077 19.986 1.00 20.19 ? 168 HIS   B CE1 1 
ATOM   2134 N  NE2 . HIS   B 1 77  ? 177.735 -40.286 19.460 1.00 15.73 ? 168 HIS   B NE2 1 
ATOM   2135 N  N   . MET   B 1 78  ? 178.110 -41.958 26.111 1.00 12.77 ? 169 MET   B N   1 
ATOM   2136 C  CA  . MET   B 1 78  ? 177.517 -42.400 27.370 1.00 11.93 ? 169 MET   B CA  1 
ATOM   2137 C  C   . MET   B 1 78  ? 177.415 -41.281 28.398 1.00 12.36 ? 169 MET   B C   1 
ATOM   2138 O  O   . MET   B 1 78  ? 176.510 -41.304 29.238 1.00 11.33 ? 169 MET   B O   1 
ATOM   2139 C  CB  . MET   B 1 78  ? 178.315 -43.562 27.940 1.00 12.46 ? 169 MET   B CB  1 
ATOM   2140 C  CG  . MET   B 1 78  ? 178.058 -44.867 27.214 1.00 25.08 ? 169 MET   B CG  1 
ATOM   2141 S  SD  . MET   B 1 78  ? 179.044 -46.226 27.880 1.00 21.64 ? 169 MET   B SD  1 
ATOM   2142 C  CE  . MET   B 1 78  ? 177.736 -47.310 28.431 1.00 26.94 ? 169 MET   B CE  1 
ATOM   2143 N  N   . THR   B 1 79  ? 178.325 -40.305 28.367 1.00 13.65 ? 170 THR   B N   1 
ATOM   2144 C  CA  . THR   B 1 79  ? 178.293 -39.254 29.385 1.00 12.23 ? 170 THR   B CA  1 
ATOM   2145 C  C   . THR   B 1 79  ? 177.297 -38.141 29.083 1.00 11.53 ? 170 THR   B C   1 
ATOM   2146 O  O   . THR   B 1 79  ? 177.147 -37.227 29.906 1.00 13.68 ? 170 THR   B O   1 
ATOM   2147 C  CB  . THR   B 1 79  ? 179.676 -38.620 29.567 1.00 13.41 ? 170 THR   B CB  1 
ATOM   2148 O  OG1 . THR   B 1 79  ? 180.082 -38.016 28.334 1.00 14.03 ? 170 THR   B OG1 1 
ATOM   2149 C  CG2 . THR   B 1 79  ? 180.698 -39.663 29.993 1.00 15.84 ? 170 THR   B CG2 1 
ATOM   2150 N  N   . GLU   B 1 80  ? 176.645 -38.159 27.930 1.00 12.62 ? 171 GLU   B N   1 
ATOM   2151 C  CA  . GLU   B 1 80  ? 175.671 -37.125 27.603 1.00 12.95 ? 171 GLU   B CA  1 
ATOM   2152 C  C   . GLU   B 1 80  ? 174.322 -37.511 28.192 1.00 11.66 ? 171 GLU   B C   1 
ATOM   2153 O  O   . GLU   B 1 80  ? 173.847 -38.629 27.980 1.00 12.71 ? 171 GLU   B O   1 
ATOM   2154 C  CB  . GLU   B 1 80  ? 175.550 -36.935 26.092 1.00 16.36 ? 171 GLU   B CB  1 
ATOM   2155 C  CG  . GLU   B 1 80  ? 174.690 -35.733 25.698 1.00 18.94 ? 171 GLU   B CG  1 
ATOM   2156 C  CD  . GLU   B 1 80  ? 174.579 -35.570 24.187 1.00 28.45 ? 171 GLU   B CD  1 
ATOM   2157 O  OE1 . GLU   B 1 80  ? 173.476 -35.223 23.697 1.00 24.53 ? 171 GLU   B OE1 1 
ATOM   2158 O  OE2 . GLU   B 1 80  ? 175.600 -35.792 23.493 1.00 29.37 ? 171 GLU   B OE2 1 
ATOM   2159 N  N   . VAL   B 1 81  ? 173.705 -36.583 28.921 1.00 9.34  ? 172 VAL   B N   1 
ATOM   2160 C  CA  . VAL   B 1 81  ? 172.413 -36.851 29.532 1.00 9.74  ? 172 VAL   B CA  1 
ATOM   2161 C  C   . VAL   B 1 81  ? 171.367 -37.037 28.446 1.00 11.75 ? 172 VAL   B C   1 
ATOM   2162 O  O   . VAL   B 1 81  ? 171.249 -36.209 27.528 1.00 10.45 ? 172 VAL   B O   1 
ATOM   2163 C  CB  . VAL   B 1 81  ? 172.017 -35.712 30.481 1.00 9.98  ? 172 VAL   B CB  1 
ATOM   2164 C  CG1 . VAL   B 1 81  ? 170.595 -35.944 31.034 1.00 8.73  ? 172 VAL   B CG1 1 
ATOM   2165 C  CG2 . VAL   B 1 81  ? 173.023 -35.580 31.613 1.00 14.01 ? 172 VAL   B CG2 1 
ATOM   2166 N  N   . VAL   B 1 82  ? 170.599 -38.121 28.548 1.00 7.78  ? 173 VAL   B N   1 
ATOM   2167 C  CA  . VAL   B 1 82  ? 169.500 -38.371 27.621 1.00 9.43  ? 173 VAL   B CA  1 
ATOM   2168 C  C   . VAL   B 1 82  ? 168.310 -37.517 28.040 1.00 9.45  ? 173 VAL   B C   1 
ATOM   2169 O  O   . VAL   B 1 82  ? 167.858 -37.589 29.192 1.00 7.22  ? 173 VAL   B O   1 
ATOM   2170 C  CB  . VAL   B 1 82  ? 169.120 -39.862 27.601 1.00 10.10 ? 173 VAL   B CB  1 
ATOM   2171 C  CG1 . VAL   B 1 82  ? 167.920 -40.073 26.686 1.00 12.37 ? 173 VAL   B CG1 1 
ATOM   2172 C  CG2 . VAL   B 1 82  ? 170.297 -40.739 27.116 1.00 8.30  ? 173 VAL   B CG2 1 
ATOM   2173 N  N   . ARG   B 1 83  ? 167.786 -36.727 27.103 1.00 9.17  ? 174 ARG   B N   1 
ATOM   2174 C  CA  . ARG   B 1 83  ? 166.671 -35.834 27.391 1.00 10.89 ? 174 ARG   B CA  1 
ATOM   2175 C  C   . ARG   B 1 83  ? 165.828 -35.647 26.136 1.00 11.53 ? 174 ARG   B C   1 
ATOM   2176 O  O   . ARG   B 1 83  ? 166.235 -35.992 25.022 1.00 7.31  ? 174 ARG   B O   1 
ATOM   2177 C  CB  . ARG   B 1 83  ? 167.165 -34.467 27.908 1.00 9.65  ? 174 ARG   B CB  1 
ATOM   2178 C  CG  . ARG   B 1 83  ? 168.122 -33.778 26.926 1.00 8.46  ? 174 ARG   B CG  1 
ATOM   2179 C  CD  . ARG   B 1 83  ? 168.290 -32.292 27.209 1.00 13.74 ? 174 ARG   B CD  1 
ATOM   2180 N  NE  . ARG   B 1 83  ? 168.991 -32.041 28.468 1.00 14.20 ? 174 ARG   B NE  1 
ATOM   2181 C  CZ  . ARG   B 1 83  ? 168.401 -31.702 29.615 1.00 14.63 ? 174 ARG   B CZ  1 
ATOM   2182 N  NH1 . ARG   B 1 83  ? 169.140 -31.501 30.705 1.00 16.50 ? 174 ARG   B NH1 1 
ATOM   2183 N  NH2 . ARG   B 1 83  ? 167.082 -31.558 29.679 1.00 11.27 ? 174 ARG   B NH2 1 
ATOM   2184 N  N   . ARG   B 1 84  ? 164.636 -35.093 26.328 1.00 10.73 ? 175 ARG   B N   1 
ATOM   2185 C  CA  . ARG   B 1 84  ? 163.797 -34.769 25.184 1.00 9.00  ? 175 ARG   B CA  1 
ATOM   2186 C  C   . ARG   B 1 84  ? 164.405 -33.637 24.364 1.00 9.06  ? 175 ARG   B C   1 
ATOM   2187 O  O   . ARG   B 1 84  ? 165.123 -32.777 24.879 1.00 10.24 ? 175 ARG   B O   1 
ATOM   2188 C  CB  . ARG   B 1 84  ? 162.393 -34.382 25.636 1.00 9.45  ? 175 ARG   B CB  1 
ATOM   2189 C  CG  . ARG   B 1 84  ? 161.652 -35.556 26.280 1.00 12.49 ? 175 ARG   B CG  1 
ATOM   2190 C  CD  . ARG   B 1 84  ? 160.283 -35.129 26.736 1.00 13.10 ? 175 ARG   B CD  1 
ATOM   2191 N  NE  . ARG   B 1 84  ? 159.289 -35.242 25.679 1.00 13.98 ? 175 ARG   B NE  1 
ATOM   2192 C  CZ  . ARG   B 1 84  ? 158.072 -34.715 25.737 1.00 8.07  ? 175 ARG   B CZ  1 
ATOM   2193 N  NH1 . ARG   B 1 84  ? 157.702 -33.980 26.782 1.00 8.62  ? 175 ARG   B NH1 1 
ATOM   2194 N  NH2 . ARG   B 1 84  ? 157.230 -34.933 24.741 1.00 9.27  ? 175 ARG   B NH2 1 
ATOM   2195 N  N   . CYS   B 1 85  ? 164.071 -33.629 23.078 1.00 10.44 ? 176 CYS   B N   1 
ATOM   2196 C  CA  . CYS   B 1 85  ? 164.625 -32.677 22.130 1.00 14.53 ? 176 CYS   B CA  1 
ATOM   2197 C  C   . CYS   B 1 85  ? 164.012 -31.285 22.334 1.00 14.13 ? 176 CYS   B C   1 
ATOM   2198 O  O   . CYS   B 1 85  ? 163.049 -31.119 23.095 1.00 11.07 ? 176 CYS   B O   1 
ATOM   2199 C  CB  . CYS   B 1 85  ? 164.392 -33.192 20.708 1.00 8.33  ? 176 CYS   B CB  1 
ATOM   2200 S  SG  . CYS   B 1 85  ? 162.683 -33.002 20.178 1.00 8.88  ? 176 CYS   B SG  1 
ATOM   2201 N  N   . PRO   B 1 86  ? 164.572 -30.253 21.684 1.00 9.03  ? 177 PRO   B N   1 
ATOM   2202 C  CA  . PRO   B 1 86  ? 164.064 -28.886 21.903 1.00 10.38 ? 177 PRO   B CA  1 
ATOM   2203 C  C   . PRO   B 1 86  ? 162.615 -28.702 21.489 1.00 13.80 ? 177 PRO   B C   1 
ATOM   2204 O  O   . PRO   B 1 86  ? 161.971 -27.745 21.939 1.00 12.76 ? 177 PRO   B O   1 
ATOM   2205 C  CB  . PRO   B 1 86  ? 165.004 -28.017 21.046 1.00 8.81  ? 177 PRO   B CB  1 
ATOM   2206 C  CG  . PRO   B 1 86  ? 166.282 -28.820 20.962 1.00 12.94 ? 177 PRO   B CG  1 
ATOM   2207 C  CD  . PRO   B 1 86  ? 165.812 -30.253 20.873 1.00 9.15  ? 177 PRO   B CD  1 
ATOM   2208 N  N   . HIS   B 1 87  ? 162.092 -29.568 20.622 1.00 8.97  ? 178 HIS   B N   1 
ATOM   2209 C  CA  . HIS   B 1 87  ? 160.694 -29.480 20.233 1.00 13.44 ? 178 HIS   B CA  1 
ATOM   2210 C  C   . HIS   B 1 87  ? 159.805 -30.163 21.260 1.00 13.34 ? 178 HIS   B C   1 
ATOM   2211 O  O   . HIS   B 1 87  ? 158.823 -29.579 21.736 1.00 11.55 ? 178 HIS   B O   1 
ATOM   2212 C  CB  . HIS   B 1 87  ? 160.478 -30.110 18.849 1.00 14.58 ? 178 HIS   B CB  1 
ATOM   2213 C  CG  . HIS   B 1 87  ? 159.044 -30.404 18.556 1.00 13.38 ? 178 HIS   B CG  1 
ATOM   2214 N  ND1 . HIS   B 1 87  ? 158.089 -29.415 18.453 1.00 14.10 ? 178 HIS   B ND1 1 
ATOM   2215 C  CD2 . HIS   B 1 87  ? 158.386 -31.579 18.402 1.00 15.34 ? 178 HIS   B CD2 1 
ATOM   2216 C  CE1 . HIS   B 1 87  ? 156.911 -29.966 18.230 1.00 15.20 ? 178 HIS   B CE1 1 
ATOM   2217 N  NE2 . HIS   B 1 87  ? 157.064 -31.277 18.193 1.00 15.10 ? 178 HIS   B NE2 1 
ATOM   2218 N  N   . HIS   B 1 88  ? 160.125 -31.408 21.617 1.00 8.41  ? 179 HIS   B N   1 
ATOM   2219 C  CA  . HIS   B 1 88  ? 159.173 -32.136 22.440 1.00 8.38  ? 179 HIS   B CA  1 
ATOM   2220 C  C   . HIS   B 1 88  ? 159.158 -31.624 23.874 1.00 9.91  ? 179 HIS   B C   1 
ATOM   2221 O  O   . HIS   B 1 88  ? 158.126 -31.732 24.541 1.00 10.95 ? 179 HIS   B O   1 
ATOM   2222 C  CB  . HIS   B 1 88  ? 159.447 -33.640 22.389 1.00 8.26  ? 179 HIS   B CB  1 
ATOM   2223 C  CG  . HIS   B 1 88  ? 158.883 -34.293 21.161 1.00 14.03 ? 179 HIS   B CG  1 
ATOM   2224 N  ND1 . HIS   B 1 88  ? 159.672 -34.907 20.211 1.00 12.00 ? 179 HIS   B ND1 1 
ATOM   2225 C  CD2 . HIS   B 1 88  ? 157.606 -34.400 20.717 1.00 14.79 ? 179 HIS   B CD2 1 
ATOM   2226 C  CE1 . HIS   B 1 88  ? 158.904 -35.369 19.236 1.00 14.48 ? 179 HIS   B CE1 1 
ATOM   2227 N  NE2 . HIS   B 1 88  ? 157.645 -35.078 19.519 1.00 10.82 ? 179 HIS   B NE2 1 
ATOM   2228 N  N   . GLU   B 1 89  ? 160.266 -31.053 24.362 1.00 8.48  ? 180 GLU   B N   1 
ATOM   2229 C  CA  . GLU   B 1 89  ? 160.225 -30.515 25.722 1.00 12.77 ? 180 GLU   B CA  1 
ATOM   2230 C  C   . GLU   B 1 89  ? 159.295 -29.315 25.840 1.00 14.75 ? 180 GLU   B C   1 
ATOM   2231 O  O   . GLU   B 1 89  ? 159.004 -28.885 26.959 1.00 17.42 ? 180 GLU   B O   1 
ATOM   2232 C  CB  . GLU   B 1 89  ? 161.634 -30.134 26.224 1.00 7.81  ? 180 GLU   B CB  1 
ATOM   2233 C  CG  . GLU   B 1 89  ? 162.232 -28.849 25.613 1.00 10.32 ? 180 GLU   B CG  1 
ATOM   2234 C  CD  . GLU   B 1 89  ? 163.496 -28.343 26.332 1.00 17.92 ? 180 GLU   B CD  1 
ATOM   2235 O  OE1 . GLU   B 1 89  ? 164.081 -29.079 27.168 1.00 17.24 ? 180 GLU   B OE1 1 
ATOM   2236 O  OE2 . GLU   B 1 89  ? 163.898 -27.184 26.071 1.00 19.52 ? 180 GLU   B OE2 1 
ATOM   2237 N  N   . ARG   B 1 90  ? 158.819 -28.768 24.721 1.00 11.33 ? 181 ARG   B N   1 
ATOM   2238 C  CA  . ARG   B 1 90  ? 157.952 -27.594 24.741 1.00 12.48 ? 181 ARG   B CA  1 
ATOM   2239 C  C   . ARG   B 1 90  ? 156.558 -27.869 24.189 1.00 11.17 ? 181 ARG   B C   1 
ATOM   2240 O  O   . ARG   B 1 90  ? 155.858 -26.922 23.839 1.00 13.69 ? 181 ARG   B O   1 
ATOM   2241 C  CB  . ARG   B 1 90  ? 158.573 -26.448 23.931 1.00 11.30 ? 181 ARG   B CB  1 
ATOM   2242 C  CG  . ARG   B 1 90  ? 159.893 -25.941 24.453 1.00 12.23 ? 181 ARG   B CG  1 
ATOM   2243 C  CD  . ARG   B 1 90  ? 160.403 -24.758 23.619 1.00 10.68 ? 181 ARG   B CD  1 
ATOM   2244 N  NE  . ARG   B 1 90  ? 159.542 -23.579 23.677 1.00 9.82  ? 181 ARG   B NE  1 
ATOM   2245 C  CZ  . ARG   B 1 90  ? 158.898 -23.065 22.625 1.00 10.12 ? 181 ARG   B CZ  1 
ATOM   2246 N  NH1 . ARG   B 1 90  ? 158.998 -23.643 21.437 1.00 9.99  ? 181 ARG   B NH1 1 
ATOM   2247 N  NH2 . ARG   B 1 90  ? 158.157 -21.963 22.756 1.00 10.66 ? 181 ARG   B NH2 1 
ATOM   2248 N  N   A CYS   B 1 91  ? 156.078 -29.114 24.221 0.52 19.99 ? 182 CYS   B N   1 
ATOM   2249 N  N   B CYS   B 1 91  ? 156.212 -29.123 23.953 0.48 17.44 ? 182 CYS   B N   1 
ATOM   2250 C  CA  A CYS   B 1 91  ? 154.888 -29.527 23.467 0.52 22.79 ? 182 CYS   B CA  1 
ATOM   2251 C  CA  B CYS   B 1 91  ? 154.859 -29.448 23.532 0.48 22.91 ? 182 CYS   B CA  1 
ATOM   2252 C  C   A CYS   B 1 91  ? 153.538 -29.389 24.187 0.52 24.15 ? 182 CYS   B C   1 
ATOM   2253 C  C   B CYS   B 1 91  ? 154.132 -29.862 24.805 0.48 23.18 ? 182 CYS   B C   1 
ATOM   2254 O  O   A CYS   B 1 91  ? 152.517 -29.735 23.590 0.52 24.31 ? 182 CYS   B O   1 
ATOM   2255 O  O   B CYS   B 1 91  ? 154.259 -30.980 25.294 0.48 27.65 ? 182 CYS   B O   1 
ATOM   2256 C  CB  A CYS   B 1 91  ? 155.041 -30.988 23.042 0.52 19.08 ? 182 CYS   B CB  1 
ATOM   2257 C  CB  B CYS   B 1 91  ? 154.830 -30.509 22.439 0.48 21.74 ? 182 CYS   B CB  1 
ATOM   2258 S  SG  A CYS   B 1 91  ? 155.616 -31.169 21.373 0.52 18.70 ? 182 CYS   B SG  1 
ATOM   2259 S  SG  B CYS   B 1 91  ? 155.364 -32.137 22.921 0.48 16.63 ? 182 CYS   B SG  1 
ATOM   2260 N  N   . SER   B 1 92  ? 153.483 -28.885 25.412 1.00 35.87 ? 183 SER   B N   1 
ATOM   2261 C  CA  . SER   B 1 92  ? 152.331 -29.063 26.298 1.00 46.31 ? 183 SER   B CA  1 
ATOM   2262 C  C   . SER   B 1 92  ? 151.652 -30.435 26.180 1.00 40.56 ? 183 SER   B C   1 
ATOM   2263 O  O   . SER   B 1 92  ? 150.471 -30.540 25.848 1.00 42.20 ? 183 SER   B O   1 
ATOM   2264 C  CB  . SER   B 1 92  ? 151.300 -27.963 26.024 1.00 53.24 ? 183 SER   B CB  1 
ATOM   2265 O  OG  . SER   B 1 92  ? 151.931 -26.705 25.834 1.00 55.21 ? 183 SER   B OG  1 
ATOM   2266 N  N   . ASP   B 1 93  ? 152.413 -31.502 26.438 1.00 33.95 ? 184 ASP   B N   1 
ATOM   2267 C  CA  . ASP   B 1 93  ? 151.874 -32.855 26.523 1.00 26.10 ? 184 ASP   B CA  1 
ATOM   2268 C  C   . ASP   B 1 93  ? 152.072 -33.429 27.916 1.00 23.28 ? 184 ASP   B C   1 
ATOM   2269 O  O   . ASP   B 1 93  ? 152.137 -34.651 28.082 1.00 24.50 ? 184 ASP   B O   1 
ATOM   2270 C  CB  . ASP   B 1 93  ? 152.495 -33.775 25.467 1.00 20.00 ? 184 ASP   B CB  1 
ATOM   2271 C  CG  . ASP   B 1 93  ? 154.000 -33.963 25.635 1.00 21.56 ? 184 ASP   B CG  1 
ATOM   2272 O  OD1 . ASP   B 1 93  ? 154.611 -33.409 26.578 1.00 22.74 ? 184 ASP   B OD1 1 
ATOM   2273 O  OD2 . ASP   B 1 93  ? 154.579 -34.692 24.801 1.00 19.48 ? 184 ASP   B OD2 1 
ATOM   2274 N  N   . SER   B 1 94  ? 152.184 -32.554 28.910 1.00 24.83 ? 185 SER   B N   1 
ATOM   2275 C  CA  . SER   B 1 94  ? 152.398 -32.967 30.285 1.00 27.23 ? 185 SER   B CA  1 
ATOM   2276 C  C   . SER   B 1 94  ? 151.222 -33.784 30.794 1.00 31.98 ? 185 SER   B C   1 
ATOM   2277 O  O   . SER   B 1 94  ? 150.066 -33.556 30.427 1.00 32.37 ? 185 SER   B O   1 
ATOM   2278 C  CB  . SER   B 1 94  ? 152.597 -31.742 31.178 1.00 33.78 ? 185 SER   B CB  1 
ATOM   2279 O  OG  . SER   B 1 94  ? 151.981 -31.926 32.440 1.00 33.46 ? 185 SER   B OG  1 
ATOM   2280 N  N   . ASP   B 1 95  ? 151.535 -34.739 31.661 1.00 30.78 ? 186 ASP   B N   1 
ATOM   2281 C  CA  . ASP   B 1 95  ? 150.537 -35.533 32.352 1.00 27.40 ? 186 ASP   B CA  1 
ATOM   2282 C  C   . ASP   B 1 95  ? 150.281 -35.021 33.759 1.00 30.95 ? 186 ASP   B C   1 
ATOM   2283 O  O   . ASP   B 1 95  ? 149.616 -35.700 34.550 1.00 34.90 ? 186 ASP   B O   1 
ATOM   2284 C  CB  . ASP   B 1 95  ? 150.983 -36.992 32.386 1.00 27.64 ? 186 ASP   B CB  1 
ATOM   2285 C  CG  . ASP   B 1 95  ? 152.226 -37.206 33.233 1.00 23.88 ? 186 ASP   B CG  1 
ATOM   2286 O  OD1 . ASP   B 1 95  ? 152.555 -38.383 33.469 1.00 24.90 ? 186 ASP   B OD1 1 
ATOM   2287 O  OD2 . ASP   B 1 95  ? 152.860 -36.218 33.679 1.00 21.25 ? 186 ASP   B OD2 1 
ATOM   2288 N  N   . GLY   B 1 96  ? 150.813 -33.848 34.091 1.00 26.66 ? 187 GLY   B N   1 
ATOM   2289 C  CA  . GLY   B 1 96  ? 150.670 -33.271 35.406 1.00 29.33 ? 187 GLY   B CA  1 
ATOM   2290 C  C   . GLY   B 1 96  ? 151.767 -33.617 36.389 1.00 30.52 ? 187 GLY   B C   1 
ATOM   2291 O  O   . GLY   B 1 96  ? 151.813 -33.023 37.471 1.00 32.50 ? 187 GLY   B O   1 
ATOM   2292 N  N   . LEU   B 1 97  ? 152.657 -34.551 36.056 1.00 23.83 ? 188 LEU   B N   1 
ATOM   2293 C  CA  . LEU   B 1 97  ? 153.651 -34.999 37.025 1.00 18.70 ? 188 LEU   B CA  1 
ATOM   2294 C  C   . LEU   B 1 97  ? 155.050 -35.026 36.419 1.00 15.00 ? 188 LEU   B C   1 
ATOM   2295 O  O   . LEU   B 1 97  ? 156.011 -34.533 37.017 1.00 14.96 ? 188 LEU   B O   1 
ATOM   2296 C  CB  . LEU   B 1 97  ? 153.269 -36.384 37.552 1.00 22.23 ? 188 LEU   B CB  1 
ATOM   2297 C  CG  . LEU   B 1 97  ? 153.997 -36.935 38.769 1.00 28.88 ? 188 LEU   B CG  1 
ATOM   2298 C  CD1 . LEU   B 1 97  ? 153.915 -35.960 39.927 1.00 33.40 ? 188 LEU   B CD1 1 
ATOM   2299 C  CD2 . LEU   B 1 97  ? 153.371 -38.275 39.147 1.00 35.49 ? 188 LEU   B CD2 1 
ATOM   2300 N  N   . ALA   B 1 98  ? 155.177 -35.608 35.241 1.00 11.03 ? 189 ALA   B N   1 
ATOM   2301 C  CA  . ALA   B 1 98  ? 156.478 -35.714 34.603 1.00 11.41 ? 189 ALA   B CA  1 
ATOM   2302 C  C   . ALA   B 1 98  ? 156.989 -34.337 34.193 1.00 16.30 ? 189 ALA   B C   1 
ATOM   2303 O  O   . ALA   B 1 98  ? 156.259 -33.578 33.546 1.00 14.25 ? 189 ALA   B O   1 
ATOM   2304 C  CB  . ALA   B 1 98  ? 156.374 -36.621 33.377 1.00 9.47  ? 189 ALA   B CB  1 
ATOM   2305 N  N   . PRO   B 1 99  ? 158.222 -33.978 34.534 1.00 11.44 ? 190 PRO   B N   1 
ATOM   2306 C  CA  . PRO   B 1 99  ? 158.832 -32.784 33.938 1.00 11.15 ? 190 PRO   B CA  1 
ATOM   2307 C  C   . PRO   B 1 99  ? 158.846 -32.914 32.427 1.00 10.75 ? 190 PRO   B C   1 
ATOM   2308 O  O   . PRO   B 1 99  ? 159.048 -34.015 31.893 1.00 9.88  ? 190 PRO   B O   1 
ATOM   2309 C  CB  . PRO   B 1 99  ? 160.259 -32.790 34.508 1.00 13.21 ? 190 PRO   B CB  1 
ATOM   2310 C  CG  . PRO   B 1 99  ? 160.140 -33.616 35.775 1.00 17.17 ? 190 PRO   B CG  1 
ATOM   2311 C  CD  . PRO   B 1 99  ? 159.172 -34.702 35.387 1.00 10.30 ? 190 PRO   B CD  1 
ATOM   2312 N  N   . PRO   B 1 100 ? 158.626 -31.817 31.699 1.00 11.72 ? 191 PRO   B N   1 
ATOM   2313 C  CA  . PRO   B 1 100 ? 158.567 -31.907 30.230 1.00 11.65 ? 191 PRO   B CA  1 
ATOM   2314 C  C   . PRO   B 1 100 ? 159.888 -32.269 29.582 1.00 11.11 ? 191 PRO   B C   1 
ATOM   2315 O  O   . PRO   B 1 100 ? 159.888 -32.642 28.403 1.00 11.02 ? 191 PRO   B O   1 
ATOM   2316 C  CB  . PRO   B 1 100 ? 158.103 -30.504 29.810 1.00 13.10 ? 191 PRO   B CB  1 
ATOM   2317 C  CG  . PRO   B 1 100 ? 158.473 -29.617 30.955 1.00 18.94 ? 191 PRO   B CG  1 
ATOM   2318 C  CD  . PRO   B 1 100 ? 158.360 -30.459 32.199 1.00 14.07 ? 191 PRO   B CD  1 
ATOM   2319 N  N   . GLN   B 1 101 ? 161.006 -32.183 30.314 1.00 12.44 ? 192 GLN   B N   1 
ATOM   2320 C  CA  . GLN   B 1 101 ? 162.310 -32.564 29.777 1.00 10.93 ? 192 GLN   B CA  1 
ATOM   2321 C  C   . GLN   B 1 101 ? 162.553 -34.076 29.786 1.00 10.22 ? 192 GLN   B C   1 
ATOM   2322 O  O   . GLN   B 1 101 ? 163.431 -34.554 29.051 1.00 9.48  ? 192 GLN   B O   1 
ATOM   2323 C  CB  . GLN   B 1 101 ? 163.422 -31.867 30.572 1.00 11.34 ? 192 GLN   B CB  1 
ATOM   2324 C  CG  . GLN   B 1 101 ? 163.363 -30.324 30.569 1.00 12.72 ? 192 GLN   B CG  1 
ATOM   2325 C  CD  . GLN   B 1 101 ? 162.619 -29.776 31.784 1.00 13.17 ? 192 GLN   B CD  1 
ATOM   2326 O  OE1 . GLN   B 1 101 ? 161.678 -30.401 32.270 1.00 14.61 ? 192 GLN   B OE1 1 
ATOM   2327 N  NE2 . GLN   B 1 101 ? 163.060 -28.628 32.299 1.00 14.45 ? 192 GLN   B NE2 1 
ATOM   2328 N  N   . HIS   B 1 102 ? 161.808 -34.837 30.585 1.00 9.03  ? 193 HIS   B N   1 
ATOM   2329 C  CA  . HIS   B 1 102 ? 162.121 -36.252 30.802 1.00 8.23  ? 193 HIS   B CA  1 
ATOM   2330 C  C   . HIS   B 1 102 ? 161.667 -37.138 29.642 1.00 9.87  ? 193 HIS   B C   1 
ATOM   2331 O  O   . HIS   B 1 102 ? 160.498 -37.130 29.254 1.00 8.37  ? 193 HIS   B O   1 
ATOM   2332 C  CB  . HIS   B 1 102 ? 161.489 -36.752 32.101 1.00 8.31  ? 193 HIS   B CB  1 
ATOM   2333 C  CG  . HIS   B 1 102 ? 162.236 -36.345 33.340 1.00 12.59 ? 193 HIS   B CG  1 
ATOM   2334 N  ND1 . HIS   B 1 102 ? 162.381 -37.182 34.430 1.00 8.80  ? 193 HIS   B ND1 1 
ATOM   2335 C  CD2 . HIS   B 1 102 ? 162.873 -35.194 33.664 1.00 13.37 ? 193 HIS   B CD2 1 
ATOM   2336 C  CE1 . HIS   B 1 102 ? 163.073 -36.565 35.371 1.00 8.90  ? 193 HIS   B CE1 1 
ATOM   2337 N  NE2 . HIS   B 1 102 ? 163.391 -35.358 34.931 1.00 10.38 ? 193 HIS   B NE2 1 
ATOM   2338 N  N   . LEU   B 1 103 ? 162.595 -37.951 29.137 1.00 7.63  ? 194 LEU   B N   1 
ATOM   2339 C  CA  . LEU   B 1 103 ? 162.271 -38.903 28.083 1.00 7.46  ? 194 LEU   B CA  1 
ATOM   2340 C  C   . LEU   B 1 103 ? 161.332 -39.998 28.575 1.00 7.97  ? 194 LEU   B C   1 
ATOM   2341 O  O   . LEU   B 1 103 ? 160.373 -40.355 27.880 1.00 7.47  ? 194 LEU   B O   1 
ATOM   2342 C  CB  . LEU   B 1 103 ? 163.557 -39.518 27.534 1.00 7.54  ? 194 LEU   B CB  1 
ATOM   2343 C  CG  . LEU   B 1 103 ? 163.312 -40.635 26.515 1.00 10.98 ? 194 LEU   B CG  1 
ATOM   2344 C  CD1 . LEU   B 1 103 ? 162.808 -40.015 25.211 1.00 11.55 ? 194 LEU   B CD1 1 
ATOM   2345 C  CD2 . LEU   B 1 103 ? 164.580 -41.465 26.293 1.00 8.20  ? 194 LEU   B CD2 1 
ATOM   2346 N  N   . ILE   B 1 104 ? 161.592 -40.565 29.759 1.00 6.78  ? 195 ILE   B N   1 
ATOM   2347 C  CA  . ILE   B 1 104 ? 160.853 -41.733 30.235 1.00 6.61  ? 195 ILE   B CA  1 
ATOM   2348 C  C   . ILE   B 1 104 ? 159.791 -41.298 31.237 1.00 8.45  ? 195 ILE   B C   1 
ATOM   2349 O  O   . ILE   B 1 104 ? 160.110 -40.684 32.262 1.00 8.87  ? 195 ILE   B O   1 
ATOM   2350 C  CB  . ILE   B 1 104 ? 161.792 -42.774 30.868 1.00 6.50  ? 195 ILE   B CB  1 
ATOM   2351 C  CG1 . ILE   B 1 104 ? 162.855 -43.254 29.871 1.00 9.19  ? 195 ILE   B CG1 1 
ATOM   2352 C  CG2 . ILE   B 1 104 ? 160.997 -43.986 31.357 1.00 9.52  ? 195 ILE   B CG2 1 
ATOM   2353 C  CD1 . ILE   B 1 104 ? 163.877 -44.272 30.508 1.00 9.67  ? 195 ILE   B CD1 1 
ATOM   2354 N  N   . ARG   B 1 105 ? 158.538 -41.675 30.987 1.00 7.02  ? 196 ARG   B N   1 
ATOM   2355 C  CA  . ARG   B 1 105 ? 157.488 -41.486 31.978 1.00 7.41  ? 196 ARG   B CA  1 
ATOM   2356 C  C   . ARG   B 1 105 ? 156.969 -42.836 32.436 1.00 7.57  ? 196 ARG   B C   1 
ATOM   2357 O  O   . ARG   B 1 105 ? 157.055 -43.819 31.706 1.00 8.91  ? 196 ARG   B O   1 
ATOM   2358 C  CB  . ARG   B 1 105 ? 156.322 -40.681 31.420 1.00 9.05  ? 196 ARG   B CB  1 
ATOM   2359 C  CG  . ARG   B 1 105 ? 156.728 -39.332 30.886 1.00 10.50 ? 196 ARG   B CG  1 
ATOM   2360 C  CD  . ARG   B 1 105 ? 155.482 -38.574 30.509 1.00 12.78 ? 196 ARG   B CD  1 
ATOM   2361 N  NE  . ARG   B 1 105 ? 155.808 -37.268 29.952 1.00 15.00 ? 196 ARG   B NE  1 
ATOM   2362 C  CZ  . ARG   B 1 105 ? 154.920 -36.478 29.367 1.00 16.41 ? 196 ARG   B CZ  1 
ATOM   2363 N  NH1 . ARG   B 1 105 ? 153.650 -36.864 29.274 1.00 15.80 ? 196 ARG   B NH1 1 
ATOM   2364 N  NH2 . ARG   B 1 105 ? 155.302 -35.306 28.881 1.00 15.46 ? 196 ARG   B NH2 1 
ATOM   2365 N  N   . VAL   B 1 106 ? 156.381 -42.867 33.634 1.00 8.00  ? 197 VAL   B N   1 
ATOM   2366 C  CA  . VAL   B 1 106 ? 155.527 -43.978 34.053 1.00 10.60 ? 197 VAL   B CA  1 
ATOM   2367 C  C   . VAL   B 1 106 ? 154.077 -43.581 33.812 1.00 12.91 ? 197 VAL   B C   1 
ATOM   2368 O  O   . VAL   B 1 106 ? 153.652 -42.489 34.209 1.00 15.16 ? 197 VAL   B O   1 
ATOM   2369 C  CB  . VAL   B 1 106 ? 155.751 -44.350 35.528 1.00 11.76 ? 197 VAL   B CB  1 
ATOM   2370 C  CG1 . VAL   B 1 106 ? 154.678 -45.310 35.986 1.00 13.37 ? 197 VAL   B CG1 1 
ATOM   2371 C  CG2 . VAL   B 1 106 ? 157.117 -44.982 35.718 1.00 8.39  ? 197 VAL   B CG2 1 
ATOM   2372 N  N   . GLU   B 1 107 ? 153.317 -44.466 33.173 1.00 9.93  ? 198 GLU   B N   1 
ATOM   2373 C  CA  . GLU   B 1 107 ? 151.908 -44.236 32.881 1.00 17.09 ? 198 GLU   B CA  1 
ATOM   2374 C  C   . GLU   B 1 107 ? 151.034 -44.858 33.962 1.00 14.87 ? 198 GLU   B C   1 
ATOM   2375 O  O   . GLU   B 1 107 ? 151.242 -46.011 34.343 1.00 19.39 ? 198 GLU   B O   1 
ATOM   2376 C  CB  . GLU   B 1 107 ? 151.544 -44.830 31.516 1.00 12.75 ? 198 GLU   B CB  1 
ATOM   2377 C  CG  . GLU   B 1 107 ? 150.208 -44.399 30.989 1.00 20.48 ? 198 GLU   B CG  1 
ATOM   2378 C  CD  . GLU   B 1 107 ? 150.047 -44.733 29.515 1.00 18.62 ? 198 GLU   B CD  1 
ATOM   2379 O  OE1 . GLU   B 1 107 ? 150.814 -45.585 28.998 1.00 16.02 ? 198 GLU   B OE1 1 
ATOM   2380 O  OE2 . GLU   B 1 107 ? 149.162 -44.131 28.877 1.00 24.95 ? 198 GLU   B OE2 1 
ATOM   2381 N  N   . GLY   B 1 108 ? 150.054 -44.101 34.442 1.00 23.44 ? 199 GLY   B N   1 
ATOM   2382 C  CA  . GLY   B 1 108 ? 149.062 -44.662 35.349 1.00 23.45 ? 199 GLY   B CA  1 
ATOM   2383 C  C   . GLY   B 1 108 ? 149.592 -45.119 36.693 1.00 29.21 ? 199 GLY   B C   1 
ATOM   2384 O  O   . GLY   B 1 108 ? 149.218 -46.199 37.169 1.00 36.59 ? 199 GLY   B O   1 
ATOM   2385 N  N   . ASN   B 1 109 ? 150.467 -44.330 37.312 1.00 24.30 ? 200 ASN   B N   1 
ATOM   2386 C  CA  . ASN   B 1 109 ? 150.880 -44.543 38.697 1.00 19.31 ? 200 ASN   B CA  1 
ATOM   2387 C  C   . ASN   B 1 109 ? 150.971 -43.172 39.355 1.00 16.58 ? 200 ASN   B C   1 
ATOM   2388 O  O   . ASN   B 1 109 ? 151.872 -42.386 39.040 1.00 18.69 ? 200 ASN   B O   1 
ATOM   2389 C  CB  . ASN   B 1 109 ? 152.219 -45.283 38.778 1.00 19.11 ? 200 ASN   B CB  1 
ATOM   2390 C  CG  . ASN   B 1 109 ? 152.508 -45.830 40.175 1.00 23.29 ? 200 ASN   B CG  1 
ATOM   2391 O  OD1 . ASN   B 1 109 ? 152.333 -45.135 41.179 1.00 18.92 ? 200 ASN   B OD1 1 
ATOM   2392 N  ND2 . ASN   B 1 109 ? 152.944 -47.085 40.241 1.00 20.20 ? 200 ASN   B ND2 1 
ATOM   2393 N  N   . LEU   B 1 110 ? 150.051 -42.882 40.277 1.00 23.38 ? 201 LEU   B N   1 
ATOM   2394 C  CA  . LEU   B 1 110 ? 150.057 -41.571 40.919 1.00 30.78 ? 201 LEU   B CA  1 
ATOM   2395 C  C   . LEU   B 1 110 ? 151.206 -41.399 41.911 1.00 29.50 ? 201 LEU   B C   1 
ATOM   2396 O  O   . LEU   B 1 110 ? 151.505 -40.262 42.292 1.00 30.45 ? 201 LEU   B O   1 
ATOM   2397 C  CB  . LEU   B 1 110 ? 148.715 -41.323 41.607 1.00 39.47 ? 201 LEU   B CB  1 
ATOM   2398 C  CG  . LEU   B 1 110 ? 147.538 -41.115 40.646 1.00 43.41 ? 201 LEU   B CG  1 
ATOM   2399 C  CD1 . LEU   B 1 110 ? 146.216 -41.034 41.389 1.00 42.02 ? 201 LEU   B CD1 1 
ATOM   2400 C  CD2 . LEU   B 1 110 ? 147.755 -39.867 39.792 1.00 44.38 ? 201 LEU   B CD2 1 
ATOM   2401 N  N   . ARG   B 1 111 ? 151.860 -42.484 42.333 1.00 20.97 ? 202 ARG   B N   1 
ATOM   2402 C  CA  . ARG   B 1 111 ? 153.009 -42.396 43.226 1.00 16.66 ? 202 ARG   B CA  1 
ATOM   2403 C  C   . ARG   B 1 111 ? 154.342 -42.336 42.477 1.00 16.88 ? 202 ARG   B C   1 
ATOM   2404 O  O   . ARG   B 1 111 ? 155.400 -42.499 43.095 1.00 15.68 ? 202 ARG   B O   1 
ATOM   2405 C  CB  . ARG   B 1 111 ? 153.004 -43.569 44.209 1.00 17.90 ? 202 ARG   B CB  1 
ATOM   2406 N  N   . ALA   B 1 112 ? 154.315 -42.099 41.168 1.00 13.37 ? 203 ALA   B N   1 
ATOM   2407 C  CA  . ALA   B 1 112 ? 155.548 -41.904 40.419 1.00 14.23 ? 203 ALA   B CA  1 
ATOM   2408 C  C   . ALA   B 1 112 ? 156.261 -40.638 40.880 1.00 20.12 ? 203 ALA   B C   1 
ATOM   2409 O  O   . ALA   B 1 112 ? 155.631 -39.606 41.124 1.00 15.00 ? 203 ALA   B O   1 
ATOM   2410 C  CB  . ALA   B 1 112 ? 155.252 -41.815 38.921 1.00 16.33 ? 203 ALA   B CB  1 
ATOM   2411 N  N   . GLU   B 1 113 ? 157.586 -40.720 40.995 1.00 11.05 ? 204 GLU   B N   1 
ATOM   2412 C  CA  . GLU   B 1 113 ? 158.418 -39.568 41.293 1.00 11.27 ? 204 GLU   B CA  1 
ATOM   2413 C  C   . GLU   B 1 113 ? 159.483 -39.422 40.223 1.00 10.32 ? 204 GLU   B C   1 
ATOM   2414 O  O   . GLU   B 1 113 ? 160.043 -40.414 39.741 1.00 9.72  ? 204 GLU   B O   1 
ATOM   2415 C  CB  . GLU   B 1 113 ? 159.096 -39.686 42.660 1.00 18.97 ? 204 GLU   B CB  1 
ATOM   2416 C  CG  . GLU   B 1 113 ? 158.136 -39.893 43.796 1.00 23.95 ? 204 GLU   B CG  1 
ATOM   2417 C  CD  . GLU   B 1 113 ? 158.831 -39.937 45.155 1.00 28.19 ? 204 GLU   B CD  1 
ATOM   2418 O  OE1 . GLU   B 1 113 ? 160.079 -39.797 45.214 1.00 25.13 ? 204 GLU   B OE1 1 
ATOM   2419 O  OE2 . GLU   B 1 113 ? 158.113 -40.109 46.159 1.00 28.73 ? 204 GLU   B OE2 1 
ATOM   2420 N  N   . TYR   B 1 114 ? 159.760 -38.177 39.866 1.00 10.41 ? 205 TYR   B N   1 
ATOM   2421 C  CA  . TYR   B 1 114 ? 160.723 -37.857 38.830 1.00 9.81  ? 205 TYR   B CA  1 
ATOM   2422 C  C   . TYR   B 1 114 ? 161.888 -37.118 39.471 1.00 14.81 ? 205 TYR   B C   1 
ATOM   2423 O  O   . TYR   B 1 114 ? 161.676 -36.177 40.242 1.00 13.86 ? 205 TYR   B O   1 
ATOM   2424 C  CB  . TYR   B 1 114 ? 160.062 -37.012 37.737 1.00 9.60  ? 205 TYR   B CB  1 
ATOM   2425 C  CG  . TYR   B 1 114 ? 159.047 -37.792 36.950 1.00 9.08  ? 205 TYR   B CG  1 
ATOM   2426 C  CD1 . TYR   B 1 114 ? 159.404 -38.420 35.760 1.00 8.94  ? 205 TYR   B CD1 1 
ATOM   2427 C  CD2 . TYR   B 1 114 ? 157.740 -37.942 37.403 1.00 9.58  ? 205 TYR   B CD2 1 
ATOM   2428 C  CE1 . TYR   B 1 114 ? 158.483 -39.164 35.033 1.00 11.40 ? 205 TYR   B CE1 1 
ATOM   2429 C  CE2 . TYR   B 1 114 ? 156.815 -38.698 36.684 1.00 9.35  ? 205 TYR   B CE2 1 
ATOM   2430 C  CZ  . TYR   B 1 114 ? 157.192 -39.297 35.502 1.00 11.74 ? 205 TYR   B CZ  1 
ATOM   2431 O  OH  . TYR   B 1 114 ? 156.278 -40.034 34.778 1.00 10.92 ? 205 TYR   B OH  1 
ATOM   2432 N  N   . LEU   B 1 115 ? 163.109 -37.555 39.174 1.00 10.31 ? 206 LEU   B N   1 
ATOM   2433 C  CA  . LEU   B 1 115 ? 164.312 -36.978 39.770 1.00 12.32 ? 206 LEU   B CA  1 
ATOM   2434 C  C   . LEU   B 1 115 ? 165.164 -36.319 38.692 1.00 12.71 ? 206 LEU   B C   1 
ATOM   2435 O  O   . LEU   B 1 115 ? 165.427 -36.929 37.649 1.00 10.37 ? 206 LEU   B O   1 
ATOM   2436 C  CB  . LEU   B 1 115 ? 165.135 -38.060 40.501 1.00 11.61 ? 206 LEU   B CB  1 
ATOM   2437 C  CG  . LEU   B 1 115 ? 166.477 -37.613 41.091 1.00 12.83 ? 206 LEU   B CG  1 
ATOM   2438 C  CD1 . LEU   B 1 115 ? 166.248 -36.654 42.254 1.00 14.08 ? 206 LEU   B CD1 1 
ATOM   2439 C  CD2 . LEU   B 1 115 ? 167.310 -38.813 41.550 1.00 19.89 ? 206 LEU   B CD2 1 
ATOM   2440 N  N   . ASP   B 1 116 ? 165.573 -35.069 38.940 1.00 14.13 ? 207 ASP   B N   1 
ATOM   2441 C  CA  . ASP   B 1 116 ? 166.731 -34.456 38.291 1.00 18.09 ? 207 ASP   B CA  1 
ATOM   2442 C  C   . ASP   B 1 116 ? 167.898 -34.602 39.262 1.00 18.24 ? 207 ASP   B C   1 
ATOM   2443 O  O   . ASP   B 1 116 ? 167.949 -33.896 40.274 1.00 15.02 ? 207 ASP   B O   1 
ATOM   2444 C  CB  . ASP   B 1 116 ? 166.521 -32.971 37.988 1.00 20.87 ? 207 ASP   B CB  1 
ATOM   2445 C  CG  . ASP   B 1 116 ? 165.341 -32.691 37.067 1.00 24.99 ? 207 ASP   B CG  1 
ATOM   2446 O  OD1 . ASP   B 1 116 ? 164.660 -31.666 37.292 1.00 26.98 ? 207 ASP   B OD1 1 
ATOM   2447 O  OD2 . ASP   B 1 116 ? 165.101 -33.463 36.119 1.00 22.38 ? 207 ASP   B OD2 1 
ATOM   2448 N  N   . ASP   B 1 117 ? 168.831 -35.509 38.971 1.00 13.75 ? 208 ASP   B N   1 
ATOM   2449 C  CA  . ASP   B 1 117 ? 169.940 -35.732 39.895 1.00 15.13 ? 208 ASP   B CA  1 
ATOM   2450 C  C   . ASP   B 1 117 ? 170.812 -34.483 39.987 1.00 17.29 ? 208 ASP   B C   1 
ATOM   2451 O  O   . ASP   B 1 117 ? 171.303 -33.982 38.966 1.00 16.75 ? 208 ASP   B O   1 
ATOM   2452 C  CB  . ASP   B 1 117 ? 170.768 -36.932 39.445 1.00 14.95 ? 208 ASP   B CB  1 
ATOM   2453 C  CG  . ASP   B 1 117 ? 171.715 -37.418 40.524 1.00 16.45 ? 208 ASP   B CG  1 
ATOM   2454 O  OD1 . ASP   B 1 117 ? 172.691 -36.711 40.842 1.00 18.03 ? 208 ASP   B OD1 1 
ATOM   2455 O  OD2 . ASP   B 1 117 ? 171.478 -38.522 41.053 1.00 19.65 ? 208 ASP   B OD2 1 
ATOM   2456 N  N   . ARG   B 1 118 ? 171.010 -33.972 41.207 1.00 18.13 ? 209 ARG   B N   1 
ATOM   2457 C  CA  . ARG   B 1 118 ? 171.745 -32.721 41.347 1.00 19.85 ? 209 ARG   B CA  1 
ATOM   2458 C  C   . ARG   B 1 118 ? 173.238 -32.895 41.109 1.00 25.18 ? 209 ARG   B C   1 
ATOM   2459 O  O   . ARG   B 1 118 ? 173.938 -31.903 40.882 1.00 25.55 ? 209 ARG   B O   1 
ATOM   2460 C  CB  . ARG   B 1 118 ? 171.514 -32.106 42.735 1.00 22.01 ? 209 ARG   B CB  1 
ATOM   2461 N  N   . ASN   B 1 119 ? 173.747 -34.120 41.145 1.00 20.92 ? 210 ASN   B N   1 
ATOM   2462 C  CA  . ASN   B 1 119 ? 175.177 -34.334 40.960 1.00 26.66 ? 210 ASN   B CA  1 
ATOM   2463 C  C   . ASN   B 1 119 ? 175.527 -34.924 39.607 1.00 27.62 ? 210 ASN   B C   1 
ATOM   2464 O  O   . ASN   B 1 119 ? 176.465 -34.455 38.961 1.00 22.65 ? 210 ASN   B O   1 
ATOM   2465 C  CB  . ASN   B 1 119 ? 175.720 -35.243 42.063 1.00 30.16 ? 210 ASN   B CB  1 
ATOM   2466 C  CG  . ASN   B 1 119 ? 175.630 -34.604 43.421 1.00 34.81 ? 210 ASN   B CG  1 
ATOM   2467 O  OD1 . ASN   B 1 119 ? 176.105 -33.485 43.626 1.00 40.79 ? 210 ASN   B OD1 1 
ATOM   2468 N  ND2 . ASN   B 1 119 ? 175.000 -35.297 44.355 1.00 36.43 ? 210 ASN   B ND2 1 
ATOM   2469 N  N   . THR   B 1 120 ? 174.788 -35.937 39.160 1.00 19.65 ? 211 THR   B N   1 
ATOM   2470 C  CA  . THR   B 1 120 ? 175.056 -36.563 37.878 1.00 22.93 ? 211 THR   B CA  1 
ATOM   2471 C  C   . THR   B 1 120 ? 174.283 -35.931 36.735 1.00 22.20 ? 211 THR   B C   1 
ATOM   2472 O  O   . THR   B 1 120 ? 174.591 -36.234 35.578 1.00 20.68 ? 211 THR   B O   1 
ATOM   2473 C  CB  . THR   B 1 120 ? 174.719 -38.056 37.923 1.00 17.85 ? 211 THR   B CB  1 
ATOM   2474 O  OG1 . THR   B 1 120 ? 173.292 -38.217 37.928 1.00 16.45 ? 211 THR   B OG1 1 
ATOM   2475 C  CG2 . THR   B 1 120 ? 175.308 -38.701 39.166 1.00 24.07 ? 211 THR   B CG2 1 
ATOM   2476 N  N   . PHE   B 1 121 ? 173.281 -35.092 37.029 1.00 17.00 ? 212 PHE   B N   1 
ATOM   2477 C  CA  . PHE   B 1 121 ? 172.410 -34.412 36.068 1.00 16.00 ? 212 PHE   B CA  1 
ATOM   2478 C  C   . PHE   B 1 121 ? 171.456 -35.353 35.329 1.00 14.85 ? 212 PHE   B C   1 
ATOM   2479 O  O   . PHE   B 1 121 ? 170.709 -34.899 34.457 1.00 18.98 ? 212 PHE   B O   1 
ATOM   2480 C  CB  . PHE   B 1 121 ? 173.218 -33.611 35.042 1.00 22.02 ? 212 PHE   B CB  1 
ATOM   2481 C  CG  . PHE   B 1 121 ? 174.208 -32.688 35.676 1.00 28.37 ? 212 PHE   B CG  1 
ATOM   2482 C  CD1 . PHE   B 1 121 ? 175.520 -32.640 35.237 1.00 33.76 ? 212 PHE   B CD1 1 
ATOM   2483 C  CD2 . PHE   B 1 121 ? 173.826 -31.881 36.736 1.00 34.02 ? 212 PHE   B CD2 1 
ATOM   2484 C  CE1 . PHE   B 1 121 ? 176.438 -31.789 35.843 1.00 38.70 ? 212 PHE   B CE1 1 
ATOM   2485 C  CE2 . PHE   B 1 121 ? 174.738 -31.026 37.346 1.00 34.25 ? 212 PHE   B CE2 1 
ATOM   2486 C  CZ  . PHE   B 1 121 ? 176.043 -30.987 36.901 1.00 36.98 ? 212 PHE   B CZ  1 
ATOM   2487 N  N   . ARG   B 1 122 ? 171.437 -36.636 35.652 1.00 13.63 ? 213 ARG   B N   1 
ATOM   2488 C  CA  . ARG   B 1 122 ? 170.588 -37.552 34.903 1.00 12.17 ? 213 ARG   B CA  1 
ATOM   2489 C  C   . ARG   B 1 122 ? 169.141 -37.508 35.387 1.00 11.21 ? 213 ARG   B C   1 
ATOM   2490 O  O   . ARG   B 1 122 ? 168.854 -37.187 36.545 1.00 13.74 ? 213 ARG   B O   1 
ATOM   2491 C  CB  . ARG   B 1 122 ? 171.145 -38.961 35.012 1.00 21.91 ? 213 ARG   B CB  1 
ATOM   2492 C  CG  . ARG   B 1 122 ? 172.597 -38.988 34.600 1.00 23.22 ? 213 ARG   B CG  1 
ATOM   2493 C  CD  . ARG   B 1 122 ? 172.917 -40.238 33.880 1.00 19.44 ? 213 ARG   B CD  1 
ATOM   2494 N  NE  . ARG   B 1 122 ? 174.300 -40.288 33.428 1.00 14.77 ? 213 ARG   B NE  1 
ATOM   2495 C  CZ  . ARG   B 1 122 ? 174.654 -40.329 32.151 1.00 14.91 ? 213 ARG   B CZ  1 
ATOM   2496 N  NH1 . ARG   B 1 122 ? 173.719 -40.301 31.193 1.00 13.68 ? 213 ARG   B NH1 1 
ATOM   2497 N  NH2 . ARG   B 1 122 ? 175.937 -40.404 31.837 1.00 16.51 ? 213 ARG   B NH2 1 
ATOM   2498 N  N   . HIS   B 1 123 ? 168.226 -37.813 34.472 1.00 11.49 ? 214 HIS   B N   1 
ATOM   2499 C  CA  . HIS   B 1 123 ? 166.808 -37.926 34.783 1.00 8.61  ? 214 HIS   B CA  1 
ATOM   2500 C  C   . HIS   B 1 123 ? 166.464 -39.377 35.090 1.00 8.33  ? 214 HIS   B C   1 
ATOM   2501 O  O   . HIS   B 1 123 ? 167.010 -40.307 34.486 1.00 8.89  ? 214 HIS   B O   1 
ATOM   2502 C  CB  . HIS   B 1 123 ? 165.932 -37.470 33.616 1.00 10.25 ? 214 HIS   B CB  1 
ATOM   2503 C  CG  . HIS   B 1 123 ? 166.225 -36.085 33.119 1.00 11.04 ? 214 HIS   B CG  1 
ATOM   2504 N  ND1 . HIS   B 1 123 ? 165.844 -35.659 31.864 1.00 13.09 ? 214 HIS   B ND1 1 
ATOM   2505 C  CD2 . HIS   B 1 123 ? 166.826 -35.026 33.713 1.00 10.30 ? 214 HIS   B CD2 1 
ATOM   2506 C  CE1 . HIS   B 1 123 ? 166.214 -34.398 31.696 1.00 13.58 ? 214 HIS   B CE1 1 
ATOM   2507 N  NE2 . HIS   B 1 123 ? 166.802 -33.984 32.807 1.00 12.33 ? 214 HIS   B NE2 1 
ATOM   2508 N  N   . SER   B 1 124 ? 165.512 -39.564 35.999 1.00 7.76  ? 215 SER   B N   1 
ATOM   2509 C  CA  . SER   B 1 124 ? 164.982 -40.900 36.247 1.00 8.01  ? 215 SER   B CA  1 
ATOM   2510 C  C   . SER   B 1 124 ? 163.556 -40.784 36.764 1.00 9.04  ? 215 SER   B C   1 
ATOM   2511 O  O   . SER   B 1 124 ? 163.112 -39.718 37.199 1.00 10.00 ? 215 SER   B O   1 
ATOM   2512 C  CB  . SER   B 1 124 ? 165.862 -41.686 37.231 1.00 9.69  ? 215 SER   B CB  1 
ATOM   2513 O  OG  . SER   B 1 124 ? 165.950 -41.022 38.476 1.00 7.68  ? 215 SER   B OG  1 
ATOM   2514 N  N   . VAL   B 1 125 ? 162.823 -41.894 36.684 1.00 9.15  ? 216 VAL   B N   1 
ATOM   2515 C  CA  . VAL   B 1 125 ? 161.482 -41.978 37.248 1.00 8.34  ? 216 VAL   B CA  1 
ATOM   2516 C  C   . VAL   B 1 125 ? 161.419 -43.233 38.105 1.00 9.37  ? 216 VAL   B C   1 
ATOM   2517 O  O   . VAL   B 1 125 ? 161.895 -44.294 37.694 1.00 7.82  ? 216 VAL   B O   1 
ATOM   2518 C  CB  . VAL   B 1 125 ? 160.394 -41.979 36.154 1.00 9.71  ? 216 VAL   B CB  1 
ATOM   2519 C  CG1 . VAL   B 1 125 ? 160.653 -43.079 35.086 1.00 10.26 ? 216 VAL   B CG1 1 
ATOM   2520 C  CG2 . VAL   B 1 125 ? 159.010 -42.105 36.774 1.00 10.20 ? 216 VAL   B CG2 1 
ATOM   2521 N  N   . VAL   B 1 126 ? 160.841 -43.114 39.301 1.00 7.70  ? 217 VAL   B N   1 
ATOM   2522 C  CA  . VAL   B 1 126 ? 160.847 -44.199 40.279 1.00 7.48  ? 217 VAL   B CA  1 
ATOM   2523 C  C   . VAL   B 1 126 ? 159.443 -44.350 40.859 1.00 9.58  ? 217 VAL   B C   1 
ATOM   2524 O  O   . VAL   B 1 126 ? 158.744 -43.353 41.083 1.00 10.22 ? 217 VAL   B O   1 
ATOM   2525 C  CB  . VAL   B 1 126 ? 161.909 -43.938 41.378 1.00 7.02  ? 217 VAL   B CB  1 
ATOM   2526 C  CG1 . VAL   B 1 126 ? 161.670 -42.590 42.071 1.00 7.32  ? 217 VAL   B CG1 1 
ATOM   2527 C  CG2 . VAL   B 1 126 ? 161.941 -45.062 42.423 1.00 8.80  ? 217 VAL   B CG2 1 
ATOM   2528 N  N   . VAL   B 1 127 ? 159.013 -45.597 41.048 1.00 8.37  ? 218 VAL   B N   1 
ATOM   2529 C  CA  . VAL   B 1 127 ? 157.705 -45.905 41.627 1.00 9.20  ? 218 VAL   B CA  1 
ATOM   2530 C  C   . VAL   B 1 127 ? 157.896 -46.959 42.707 1.00 9.29  ? 218 VAL   B C   1 
ATOM   2531 O  O   . VAL   B 1 127 ? 158.872 -47.728 42.677 1.00 8.85  ? 218 VAL   B O   1 
ATOM   2532 C  CB  . VAL   B 1 127 ? 156.701 -46.421 40.566 1.00 11.51 ? 218 VAL   B CB  1 
ATOM   2533 C  CG1 . VAL   B 1 127 ? 156.387 -45.350 39.516 1.00 13.03 ? 218 VAL   B CG1 1 
ATOM   2534 C  CG2 . VAL   B 1 127 ? 157.244 -47.678 39.912 1.00 16.05 ? 218 VAL   B CG2 1 
ATOM   2535 N  N   . PRO   B 1 128 ? 156.972 -47.029 43.662 1.00 10.93 ? 219 PRO   B N   1 
ATOM   2536 C  CA  . PRO   B 1 128 ? 156.979 -48.140 44.625 1.00 10.77 ? 219 PRO   B CA  1 
ATOM   2537 C  C   . PRO   B 1 128 ? 156.653 -49.442 43.920 1.00 15.69 ? 219 PRO   B C   1 
ATOM   2538 O  O   . PRO   B 1 128 ? 155.955 -49.461 42.901 1.00 14.97 ? 219 PRO   B O   1 
ATOM   2539 C  CB  . PRO   B 1 128 ? 155.857 -47.771 45.606 1.00 16.17 ? 219 PRO   B CB  1 
ATOM   2540 C  CG  . PRO   B 1 128 ? 155.575 -46.313 45.369 1.00 19.91 ? 219 PRO   B CG  1 
ATOM   2541 C  CD  . PRO   B 1 128 ? 155.867 -46.093 43.911 1.00 12.85 ? 219 PRO   B CD  1 
ATOM   2542 N  N   . CYS   B 1 129 ? 157.154 -50.547 44.459 1.00 18.24 ? 220 CYS   B N   1 
ATOM   2543 C  CA  A CYS   B 1 129 ? 156.831 -51.897 44.005 0.35 18.42 ? 220 CYS   B CA  1 
ATOM   2544 C  CA  B CYS   B 1 129 ? 156.656 -51.804 43.941 0.65 18.93 ? 220 CYS   B CA  1 
ATOM   2545 C  C   . CYS   B 1 129 ? 155.945 -52.582 45.035 1.00 17.97 ? 220 CYS   B C   1 
ATOM   2546 O  O   . CYS   B 1 129 ? 156.104 -52.354 46.238 1.00 13.18 ? 220 CYS   B O   1 
ATOM   2547 C  CB  A CYS   B 1 129 ? 158.083 -52.767 43.817 0.35 16.44 ? 220 CYS   B CB  1 
ATOM   2548 C  CB  B CYS   B 1 129 ? 157.752 -52.643 43.277 0.65 18.14 ? 220 CYS   B CB  1 
ATOM   2549 S  SG  A CYS   B 1 129 ? 159.593 -51.969 43.247 0.35 15.14 ? 220 CYS   B SG  1 
ATOM   2550 S  SG  B CYS   B 1 129 ? 159.105 -53.127 44.286 0.65 16.49 ? 220 CYS   B SG  1 
ATOM   2551 N  N   . GLU   B 1 130 ? 155.075 -53.460 44.571 1.00 22.59 ? 221 GLU   B N   1 
ATOM   2552 C  CA  . GLU   B 1 130 ? 154.213 -54.241 45.439 1.00 29.54 ? 221 GLU   B CA  1 
ATOM   2553 C  C   . GLU   B 1 130 ? 154.108 -55.631 44.842 1.00 24.84 ? 221 GLU   B C   1 
ATOM   2554 O  O   . GLU   B 1 130 ? 154.445 -55.834 43.671 1.00 21.21 ? 221 GLU   B O   1 
ATOM   2555 C  CB  . GLU   B 1 130 ? 152.831 -53.587 45.576 1.00 40.66 ? 221 GLU   B CB  1 
ATOM   2556 C  CG  . GLU   B 1 130 ? 152.490 -52.656 44.434 1.00 48.45 ? 221 GLU   B CG  1 
ATOM   2557 C  CD  . GLU   B 1 130 ? 151.790 -51.409 44.920 1.00 57.35 ? 221 GLU   B CD  1 
ATOM   2558 O  OE1 . GLU   B 1 130 ? 150.637 -51.170 44.504 1.00 60.54 ? 221 GLU   B OE1 1 
ATOM   2559 O  OE2 . GLU   B 1 130 ? 152.394 -50.677 45.732 1.00 58.90 ? 221 GLU   B OE2 1 
ATOM   2560 N  N   . PRO   B 1 131 ? 153.678 -56.613 45.628 1.00 22.72 ? 222 PRO   B N   1 
ATOM   2561 C  CA  . PRO   B 1 131 ? 153.576 -57.973 45.119 1.00 24.02 ? 222 PRO   B CA  1 
ATOM   2562 C  C   . PRO   B 1 131 ? 152.437 -58.086 44.125 1.00 24.33 ? 222 PRO   B C   1 
ATOM   2563 O  O   . PRO   B 1 131 ? 151.563 -57.207 44.071 1.00 19.28 ? 222 PRO   B O   1 
ATOM   2564 C  CB  . PRO   B 1 131 ? 153.294 -58.801 46.383 1.00 26.39 ? 222 PRO   B CB  1 
ATOM   2565 C  CG  . PRO   B 1 131 ? 153.644 -57.905 47.528 1.00 28.10 ? 222 PRO   B CG  1 
ATOM   2566 C  CD  . PRO   B 1 131 ? 153.312 -56.546 47.052 1.00 21.15 ? 222 PRO   B CD  1 
ATOM   2567 N  N   . PRO   B 1 132 ? 152.410 -59.152 43.327 1.00 20.69 ? 223 PRO   B N   1 
ATOM   2568 C  CA  . PRO   B 1 132 ? 151.328 -59.316 42.353 1.00 19.75 ? 223 PRO   B CA  1 
ATOM   2569 C  C   . PRO   B 1 132 ? 149.993 -59.544 43.032 1.00 26.78 ? 223 PRO   B C   1 
ATOM   2570 O  O   . PRO   B 1 132 ? 149.910 -60.118 44.121 1.00 29.77 ? 223 PRO   B O   1 
ATOM   2571 C  CB  . PRO   B 1 132 ? 151.748 -60.557 41.552 1.00 22.64 ? 223 PRO   B CB  1 
ATOM   2572 C  CG  . PRO   B 1 132 ? 153.205 -60.727 41.826 1.00 24.80 ? 223 PRO   B CG  1 
ATOM   2573 C  CD  . PRO   B 1 132 ? 153.419 -60.217 43.216 1.00 20.69 ? 223 PRO   B CD  1 
ATOM   2574 N  N   . GLU   B 1 133 ? 148.943 -59.077 42.362 1.00 28.44 ? 224 GLU   B N   1 
ATOM   2575 C  CA  . GLU   B 1 133 ? 147.580 -59.412 42.743 1.00 37.30 ? 224 GLU   B CA  1 
ATOM   2576 C  C   . GLU   B 1 133 ? 147.428 -60.921 42.896 1.00 34.26 ? 224 GLU   B C   1 
ATOM   2577 O  O   . GLU   B 1 133 ? 148.076 -61.705 42.196 1.00 30.34 ? 224 GLU   B O   1 
ATOM   2578 C  CB  . GLU   B 1 133 ? 146.608 -58.887 41.683 1.00 41.70 ? 224 GLU   B CB  1 
ATOM   2579 C  CG  . GLU   B 1 133 ? 145.198 -59.443 41.775 1.00 50.22 ? 224 GLU   B CG  1 
ATOM   2580 C  CD  . GLU   B 1 133 ? 144.555 -59.608 40.413 1.00 53.90 ? 224 GLU   B CD  1 
ATOM   2581 O  OE1 . GLU   B 1 133 ? 144.491 -60.753 39.906 1.00 53.86 ? 224 GLU   B OE1 1 
ATOM   2582 O  OE2 . GLU   B 1 133 ? 144.131 -58.585 39.840 1.00 56.67 ? 224 GLU   B OE2 1 
ATOM   2583 N  N   . VAL   B 1 134 ? 146.573 -61.327 43.838 1.00 32.91 ? 225 VAL   B N   1 
ATOM   2584 C  CA  . VAL   B 1 134 ? 146.264 -62.740 44.008 1.00 31.54 ? 225 VAL   B CA  1 
ATOM   2585 C  C   . VAL   B 1 134 ? 145.888 -63.337 42.657 1.00 30.89 ? 225 VAL   B C   1 
ATOM   2586 O  O   . VAL   B 1 134 ? 145.111 -62.752 41.896 1.00 34.41 ? 225 VAL   B O   1 
ATOM   2587 C  CB  . VAL   B 1 134 ? 145.149 -62.915 45.057 1.00 35.16 ? 225 VAL   B CB  1 
ATOM   2588 C  CG1 . VAL   B 1 134 ? 143.855 -62.226 44.612 1.00 33.85 ? 225 VAL   B CG1 1 
ATOM   2589 C  CG2 . VAL   B 1 134 ? 144.923 -64.388 45.366 1.00 34.93 ? 225 VAL   B CG2 1 
ATOM   2590 N  N   . GLY   B 1 135 ? 146.490 -64.479 42.330 1.00 27.40 ? 226 GLY   B N   1 
ATOM   2591 C  CA  . GLY   B 1 135 ? 146.284 -65.122 41.053 1.00 35.44 ? 226 GLY   B CA  1 
ATOM   2592 C  C   . GLY   B 1 135 ? 147.273 -64.749 39.965 1.00 38.18 ? 226 GLY   B C   1 
ATOM   2593 O  O   . GLY   B 1 135 ? 147.220 -65.339 38.880 1.00 38.20 ? 226 GLY   B O   1 
ATOM   2594 N  N   . SER   B 1 136 ? 148.168 -63.793 40.210 1.00 33.55 ? 227 SER   B N   1 
ATOM   2595 C  CA  A SER   B 1 136 ? 149.157 -63.398 39.221 0.63 30.27 ? 227 SER   B CA  1 
ATOM   2596 C  CA  B SER   B 1 136 ? 149.157 -63.355 39.237 0.37 30.18 ? 227 SER   B CA  1 
ATOM   2597 C  C   . SER   B 1 136 ? 150.560 -63.619 39.766 1.00 26.51 ? 227 SER   B C   1 
ATOM   2598 O  O   . SER   B 1 136 ? 150.782 -63.666 40.980 1.00 23.63 ? 227 SER   B O   1 
ATOM   2599 C  CB  A SER   B 1 136 ? 148.965 -61.940 38.801 0.63 29.75 ? 227 SER   B CB  1 
ATOM   2600 C  CB  B SER   B 1 136 ? 148.995 -61.867 38.914 0.37 29.65 ? 227 SER   B CB  1 
ATOM   2601 O  OG  A SER   B 1 136 ? 147.684 -61.777 38.222 0.63 29.53 ? 227 SER   B OG  1 
ATOM   2602 O  OG  B SER   B 1 136 ? 150.039 -61.415 38.074 0.37 28.30 ? 227 SER   B OG  1 
ATOM   2603 N  N   . ASP   B 1 137 ? 151.512 -63.770 38.840 1.00 17.46 ? 228 ASP   B N   1 
ATOM   2604 C  CA  . ASP   B 1 137 ? 152.877 -64.154 39.171 1.00 20.37 ? 228 ASP   B CA  1 
ATOM   2605 C  C   . ASP   B 1 137 ? 153.911 -63.050 38.992 1.00 22.50 ? 228 ASP   B C   1 
ATOM   2606 O  O   . ASP   B 1 137 ? 155.083 -63.267 39.326 1.00 16.40 ? 228 ASP   B O   1 
ATOM   2607 C  CB  . ASP   B 1 137 ? 153.298 -65.365 38.321 1.00 18.00 ? 228 ASP   B CB  1 
ATOM   2608 C  CG  . ASP   B 1 137 ? 152.497 -66.603 38.656 1.00 29.63 ? 228 ASP   B CG  1 
ATOM   2609 O  OD1 . ASP   B 1 137 ? 152.254 -66.827 39.857 1.00 28.27 ? 228 ASP   B OD1 1 
ATOM   2610 O  OD2 . ASP   B 1 137 ? 152.098 -67.339 37.729 1.00 26.89 ? 228 ASP   B OD2 1 
ATOM   2611 N  N   . CYS   B 1 138 ? 153.534 -61.892 38.458 1.00 15.35 ? 229 CYS   B N   1 
ATOM   2612 C  CA  . CYS   B 1 138 ? 154.477 -60.794 38.313 1.00 14.65 ? 229 CYS   B CA  1 
ATOM   2613 C  C   . CYS   B 1 138 ? 153.700 -59.490 38.364 1.00 13.96 ? 229 CYS   B C   1 
ATOM   2614 O  O   . CYS   B 1 138 ? 152.473 -59.473 38.285 1.00 15.68 ? 229 CYS   B O   1 
ATOM   2615 C  CB  . CYS   B 1 138 ? 155.283 -60.896 37.013 1.00 18.08 ? 229 CYS   B CB  1 
ATOM   2616 S  SG  . CYS   B 1 138 ? 154.300 -60.664 35.483 1.00 19.29 ? 229 CYS   B SG  1 
ATOM   2617 N  N   . THR   B 1 139 ? 154.423 -58.393 38.504 1.00 16.51 ? 230 THR   B N   1 
ATOM   2618 C  CA  . THR   B 1 139 ? 153.811 -57.086 38.360 1.00 15.84 ? 230 THR   B CA  1 
ATOM   2619 C  C   . THR   B 1 139 ? 154.277 -56.458 37.053 1.00 18.01 ? 230 THR   B C   1 
ATOM   2620 O  O   . THR   B 1 139 ? 155.248 -56.900 36.436 1.00 17.86 ? 230 THR   B O   1 
ATOM   2621 C  CB  . THR   B 1 139 ? 154.142 -56.181 39.550 1.00 18.68 ? 230 THR   B CB  1 
ATOM   2622 O  OG1 . THR   B 1 139 ? 155.551 -55.946 39.602 1.00 18.04 ? 230 THR   B OG1 1 
ATOM   2623 C  CG2 . THR   B 1 139 ? 153.709 -56.855 40.842 1.00 18.59 ? 230 THR   B CG2 1 
ATOM   2624 N  N   . THR   B 1 140 ? 153.559 -55.430 36.627 1.00 13.59 ? 231 THR   B N   1 
ATOM   2625 C  CA  . THR   B 1 140 ? 153.839 -54.761 35.369 1.00 12.20 ? 231 THR   B CA  1 
ATOM   2626 C  C   . THR   B 1 140 ? 153.904 -53.262 35.595 1.00 15.47 ? 231 THR   B C   1 
ATOM   2627 O  O   . THR   B 1 140 ? 153.080 -52.699 36.320 1.00 17.52 ? 231 THR   B O   1 
ATOM   2628 C  CB  . THR   B 1 140 ? 152.752 -55.073 34.328 1.00 15.13 ? 231 THR   B CB  1 
ATOM   2629 O  OG1 . THR   B 1 140 ? 152.709 -56.485 34.111 1.00 18.14 ? 231 THR   B OG1 1 
ATOM   2630 C  CG2 . THR   B 1 140 ? 153.049 -54.364 33.009 1.00 15.84 ? 231 THR   B CG2 1 
ATOM   2631 N  N   . ILE   B 1 141 ? 154.895 -52.626 34.989 1.00 10.69 ? 232 ILE   B N   1 
ATOM   2632 C  CA  A ILE   B 1 141 ? 155.000 -51.170 34.940 0.65 10.31 ? 232 ILE   B CA  1 
ATOM   2633 C  CA  B ILE   B 1 141 ? 154.992 -51.176 34.946 0.35 10.31 ? 232 ILE   B CA  1 
ATOM   2634 C  C   . ILE   B 1 141 ? 154.796 -50.733 33.500 1.00 9.68  ? 232 ILE   B C   1 
ATOM   2635 O  O   . ILE   B 1 141 ? 155.260 -51.398 32.567 1.00 12.71 ? 232 ILE   B O   1 
ATOM   2636 C  CB  A ILE   B 1 141 ? 156.359 -50.652 35.448 0.65 12.30 ? 232 ILE   B CB  1 
ATOM   2637 C  CB  B ILE   B 1 141 ? 156.345 -50.712 35.525 0.35 12.16 ? 232 ILE   B CB  1 
ATOM   2638 C  CG1 A ILE   B 1 141 ? 156.564 -50.966 36.916 0.65 16.32 ? 232 ILE   B CG1 1 
ATOM   2639 C  CG1 B ILE   B 1 141 ? 156.474 -49.190 35.479 0.35 11.59 ? 232 ILE   B CG1 1 
ATOM   2640 C  CG2 A ILE   B 1 141 ? 156.472 -49.126 35.247 0.65 10.84 ? 232 ILE   B CG2 1 
ATOM   2641 C  CG2 B ILE   B 1 141 ? 157.500 -51.426 34.851 0.35 9.45  ? 232 ILE   B CG2 1 
ATOM   2642 C  CD1 A ILE   B 1 141 ? 157.821 -50.338 37.414 0.65 20.23 ? 232 ILE   B CD1 1 
ATOM   2643 C  CD1 B ILE   B 1 141 ? 155.817 -48.531 36.647 0.35 15.66 ? 232 ILE   B CD1 1 
ATOM   2644 N  N   . HIS   B 1 142 ? 154.096 -49.626 33.309 1.00 9.84  ? 233 HIS   B N   1 
ATOM   2645 C  CA  A HIS   B 1 142 ? 153.840 -49.125 31.973 0.52 10.23 ? 233 HIS   B CA  1 
ATOM   2646 C  CA  B HIS   B 1 142 ? 153.797 -49.093 31.981 0.48 10.26 ? 233 HIS   B CA  1 
ATOM   2647 C  C   . HIS   B 1 142 ? 154.687 -47.877 31.757 1.00 11.14 ? 233 HIS   B C   1 
ATOM   2648 O  O   . HIS   B 1 142 ? 154.526 -46.868 32.448 1.00 11.21 ? 233 HIS   B O   1 
ATOM   2649 C  CB  A HIS   B 1 142 ? 152.347 -48.876 31.774 0.52 11.12 ? 233 HIS   B CB  1 
ATOM   2650 C  CB  B HIS   B 1 142 ? 152.328 -48.681 31.858 0.48 11.67 ? 233 HIS   B CB  1 
ATOM   2651 C  CG  A HIS   B 1 142 ? 151.514 -50.114 31.928 0.52 12.01 ? 233 HIS   B CG  1 
ATOM   2652 C  CG  B HIS   B 1 142 ? 151.362 -49.821 31.773 0.48 13.31 ? 233 HIS   B CG  1 
ATOM   2653 N  ND1 A HIS   B 1 142 ? 151.259 -50.693 33.153 0.52 13.86 ? 233 HIS   B ND1 1 
ATOM   2654 N  ND1 B HIS   B 1 142 ? 151.744 -51.113 31.487 0.48 10.56 ? 233 HIS   B ND1 1 
ATOM   2655 C  CD2 A HIS   B 1 142 ? 150.902 -50.899 31.008 0.52 11.12 ? 233 HIS   B CD2 1 
ATOM   2656 C  CD2 B HIS   B 1 142 ? 150.015 -49.850 31.914 0.48 12.16 ? 233 HIS   B CD2 1 
ATOM   2657 C  CE1 A HIS   B 1 142 ? 150.512 -51.771 32.983 0.52 13.08 ? 233 HIS   B CE1 1 
ATOM   2658 C  CE1 B HIS   B 1 142 ? 150.677 -51.892 31.471 0.48 12.97 ? 233 HIS   B CE1 1 
ATOM   2659 N  NE2 A HIS   B 1 142 ? 150.283 -51.919 31.690 0.52 12.08 ? 233 HIS   B NE2 1 
ATOM   2660 N  NE2 B HIS   B 1 142 ? 149.615 -51.149 31.724 0.48 14.01 ? 233 HIS   B NE2 1 
ATOM   2661 N  N   . TYR   B 1 143 ? 155.610 -47.962 30.806 1.00 8.25  ? 234 TYR   B N   1 
ATOM   2662 C  CA  . TYR   B 1 143 ? 156.463 -46.830 30.477 1.00 9.40  ? 234 TYR   B CA  1 
ATOM   2663 C  C   . TYR   B 1 143 ? 156.010 -46.174 29.173 1.00 7.35  ? 234 TYR   B C   1 
ATOM   2664 O  O   . TYR   B 1 143 ? 155.384 -46.812 28.325 1.00 8.97  ? 234 TYR   B O   1 
ATOM   2665 C  CB  . TYR   B 1 143 ? 157.927 -47.273 30.372 1.00 10.38 ? 234 TYR   B CB  1 
ATOM   2666 C  CG  . TYR   B 1 143 ? 158.549 -47.677 31.698 1.00 8.98  ? 234 TYR   B CG  1 
ATOM   2667 C  CD1 . TYR   B 1 143 ? 158.864 -49.005 31.974 1.00 9.39  ? 234 TYR   B CD1 1 
ATOM   2668 C  CD2 . TYR   B 1 143 ? 158.832 -46.733 32.665 1.00 7.44  ? 234 TYR   B CD2 1 
ATOM   2669 C  CE1 . TYR   B 1 143 ? 159.465 -49.367 33.185 1.00 7.71  ? 234 TYR   B CE1 1 
ATOM   2670 C  CE2 . TYR   B 1 143 ? 159.420 -47.098 33.891 1.00 8.18  ? 234 TYR   B CE2 1 
ATOM   2671 C  CZ  . TYR   B 1 143 ? 159.725 -48.409 34.137 1.00 8.30  ? 234 TYR   B CZ  1 
ATOM   2672 O  OH  . TYR   B 1 143 ? 160.305 -48.752 35.344 1.00 9.32  ? 234 TYR   B OH  1 
ATOM   2673 N  N   . ASN   B 1 144 ? 156.297 -44.872 29.045 1.00 7.33  ? 235 ASN   B N   1 
ATOM   2674 C  CA  . ASN   B 1 144 ? 156.164 -44.135 27.794 1.00 10.20 ? 235 ASN   B CA  1 
ATOM   2675 C  C   . ASN   B 1 144 ? 157.506 -43.496 27.460 1.00 12.05 ? 235 ASN   B C   1 
ATOM   2676 O  O   . ASN   B 1 144 ? 158.188 -42.979 28.348 1.00 12.06 ? 235 ASN   B O   1 
ATOM   2677 C  CB  . ASN   B 1 144 ? 155.143 -42.990 27.864 1.00 11.68 ? 235 ASN   B CB  1 
ATOM   2678 C  CG  . ASN   B 1 144 ? 153.771 -43.416 28.287 1.00 15.29 ? 235 ASN   B CG  1 
ATOM   2679 O  OD1 . ASN   B 1 144 ? 153.064 -42.641 28.926 1.00 16.96 ? 235 ASN   B OD1 1 
ATOM   2680 N  ND2 . ASN   B 1 144 ? 153.359 -44.619 27.911 1.00 16.26 ? 235 ASN   B ND2 1 
ATOM   2681 N  N   . TYR   B 1 145 ? 157.871 -43.499 26.185 1.00 6.40  ? 236 TYR   B N   1 
ATOM   2682 C  CA  . TYR   B 1 145 ? 159.068 -42.812 25.713 1.00 6.76  ? 236 TYR   B CA  1 
ATOM   2683 C  C   . TYR   B 1 145 ? 158.619 -41.629 24.870 1.00 9.69  ? 236 TYR   B C   1 
ATOM   2684 O  O   . TYR   B 1 145 ? 157.916 -41.813 23.865 1.00 9.42  ? 236 TYR   B O   1 
ATOM   2685 C  CB  . TYR   B 1 145 ? 159.973 -43.743 24.905 1.00 6.00  ? 236 TYR   B CB  1 
ATOM   2686 C  CG  . TYR   B 1 145 ? 160.594 -44.814 25.766 1.00 7.82  ? 236 TYR   B CG  1 
ATOM   2687 C  CD1 . TYR   B 1 145 ? 159.882 -45.965 26.070 1.00 11.42 ? 236 TYR   B CD1 1 
ATOM   2688 C  CD2 . TYR   B 1 145 ? 161.869 -44.664 26.303 1.00 10.38 ? 236 TYR   B CD2 1 
ATOM   2689 C  CE1 . TYR   B 1 145 ? 160.427 -46.953 26.868 1.00 7.49  ? 236 TYR   B CE1 1 
ATOM   2690 C  CE2 . TYR   B 1 145 ? 162.430 -45.660 27.116 1.00 7.20  ? 236 TYR   B CE2 1 
ATOM   2691 C  CZ  . TYR   B 1 145 ? 161.691 -46.799 27.387 1.00 5.54  ? 236 TYR   B CZ  1 
ATOM   2692 O  OH  . TYR   B 1 145 ? 162.199 -47.800 28.178 1.00 9.71  ? 236 TYR   B OH  1 
ATOM   2693 N  N   . MET   B 1 146 ? 159.036 -40.425 25.269 1.00 9.03  ? 237 MET   B N   1 
ATOM   2694 C  CA  . MET   B 1 146 ? 158.385 -39.203 24.815 1.00 7.98  ? 237 MET   B CA  1 
ATOM   2695 C  C   . MET   B 1 146 ? 159.171 -38.463 23.733 1.00 8.26  ? 237 MET   B C   1 
ATOM   2696 O  O   . MET   B 1 146 ? 158.901 -37.286 23.490 1.00 9.97  ? 237 MET   B O   1 
ATOM   2697 C  CB  . MET   B 1 146 ? 158.128 -38.280 26.006 1.00 9.57  ? 237 MET   B CB  1 
ATOM   2698 C  CG  . MET   B 1 146 ? 157.363 -38.949 27.121 1.00 15.93 ? 237 MET   B CG  1 
ATOM   2699 S  SD  . MET   B 1 146 ? 155.716 -39.459 26.617 1.00 14.95 ? 237 MET   B SD  1 
ATOM   2700 C  CE  . MET   B 1 146 ? 155.087 -37.920 25.928 1.00 15.16 ? 237 MET   B CE  1 
ATOM   2701 N  N   . CYS   B 1 147 ? 160.130 -39.126 23.091 1.00 8.26  ? 238 CYS   B N   1 
ATOM   2702 C  CA  . CYS   B 1 147 ? 160.848 -38.599 21.936 1.00 11.54 ? 238 CYS   B CA  1 
ATOM   2703 C  C   . CYS   B 1 147 ? 161.141 -39.747 20.993 1.00 12.18 ? 238 CYS   B C   1 
ATOM   2704 O  O   . CYS   B 1 147 ? 161.313 -40.885 21.436 1.00 14.51 ? 238 CYS   B O   1 
ATOM   2705 C  CB  . CYS   B 1 147 ? 162.185 -37.972 22.312 1.00 19.71 ? 238 CYS   B CB  1 
ATOM   2706 S  SG  . CYS   B 1 147 ? 162.246 -36.207 22.310 1.00 14.79 ? 238 CYS   B SG  1 
ATOM   2707 N  N   . TYR   B 1 148 ? 161.244 -39.444 19.699 1.00 10.27 ? 239 TYR   B N   1 
ATOM   2708 C  CA  . TYR   B 1 148 ? 161.734 -40.440 18.761 1.00 10.36 ? 239 TYR   B CA  1 
ATOM   2709 C  C   . TYR   B 1 148 ? 163.245 -40.592 18.899 1.00 11.10 ? 239 TYR   B C   1 
ATOM   2710 O  O   . TYR   B 1 148 ? 163.949 -39.643 19.256 1.00 11.30 ? 239 TYR   B O   1 
ATOM   2711 C  CB  . TYR   B 1 148 ? 161.395 -40.042 17.324 1.00 13.17 ? 239 TYR   B CB  1 
ATOM   2712 C  CG  . TYR   B 1 148 ? 159.935 -40.178 16.943 1.00 15.67 ? 239 TYR   B CG  1 
ATOM   2713 C  CD1 . TYR   B 1 148 ? 159.345 -41.432 16.831 1.00 16.40 ? 239 TYR   B CD1 1 
ATOM   2714 C  CD2 . TYR   B 1 148 ? 159.164 -39.058 16.646 1.00 14.23 ? 239 TYR   B CD2 1 
ATOM   2715 C  CE1 . TYR   B 1 148 ? 158.031 -41.570 16.459 1.00 20.36 ? 239 TYR   B CE1 1 
ATOM   2716 C  CE2 . TYR   B 1 148 ? 157.830 -39.187 16.275 1.00 21.78 ? 239 TYR   B CE2 1 
ATOM   2717 C  CZ  . TYR   B 1 148 ? 157.275 -40.452 16.183 1.00 20.03 ? 239 TYR   B CZ  1 
ATOM   2718 O  OH  . TYR   B 1 148 ? 155.966 -40.624 15.816 1.00 21.95 ? 239 TYR   B OH  1 
ATOM   2719 N  N   . SER   B 1 149 ? 163.750 -41.792 18.581 1.00 12.31 ? 240 SER   B N   1 
ATOM   2720 C  CA  . SER   B 1 149 ? 165.200 -41.974 18.525 1.00 12.51 ? 240 SER   B CA  1 
ATOM   2721 C  C   . SER   B 1 149 ? 165.838 -41.000 17.545 1.00 10.59 ? 240 SER   B C   1 
ATOM   2722 O  O   . SER   B 1 149 ? 166.997 -40.604 17.723 1.00 11.56 ? 240 SER   B O   1 
ATOM   2723 C  CB  . SER   B 1 149 ? 165.547 -43.413 18.137 1.00 14.32 ? 240 SER   B CB  1 
ATOM   2724 O  OG  . SER   B 1 149 ? 165.330 -44.266 19.254 1.00 11.06 ? 240 SER   B OG  1 
ATOM   2725 N  N   . SER   B 1 150 ? 165.090 -40.578 16.538 1.00 11.44 ? 241 SER   B N   1 
ATOM   2726 C  CA  . SER   B 1 150 ? 165.601 -39.735 15.468 1.00 12.82 ? 241 SER   B CA  1 
ATOM   2727 C  C   . SER   B 1 150 ? 165.535 -38.238 15.774 1.00 13.62 ? 241 SER   B C   1 
ATOM   2728 O  O   . SER   B 1 150 ? 166.045 -37.446 14.976 1.00 15.78 ? 241 SER   B O   1 
ATOM   2729 C  CB  . SER   B 1 150 ? 164.826 -40.018 14.177 1.00 17.22 ? 241 SER   B CB  1 
ATOM   2730 O  OG  . SER   B 1 150 ? 163.469 -39.642 14.340 1.00 20.59 ? 241 SER   B OG  1 
ATOM   2731 N  N   . CYS   B 1 151 ? 164.944 -37.824 16.897 1.00 11.77 ? 242 CYS   B N   1 
ATOM   2732 C  CA  . CYS   B 1 151 ? 164.687 -36.396 17.113 1.00 15.80 ? 242 CYS   B CA  1 
ATOM   2733 C  C   . CYS   B 1 151 ? 165.970 -35.567 17.073 1.00 12.83 ? 242 CYS   B C   1 
ATOM   2734 O  O   . CYS   B 1 151 ? 166.920 -35.821 17.822 1.00 14.05 ? 242 CYS   B O   1 
ATOM   2735 C  CB  . CYS   B 1 151 ? 163.973 -36.178 18.448 1.00 17.72 ? 242 CYS   B CB  1 
ATOM   2736 S  SG  . CYS   B 1 151 ? 162.172 -36.433 18.392 1.00 13.20 ? 242 CYS   B SG  1 
ATOM   2737 N  N   . MET   B 1 152 ? 165.972 -34.547 16.218 1.00 14.16 ? 243 MET   B N   1 
ATOM   2738 C  CA  . MET   B 1 152 ? 167.122 -33.665 16.071 1.00 15.12 ? 243 MET   B CA  1 
ATOM   2739 C  C   . MET   B 1 152 ? 167.302 -32.808 17.316 1.00 15.39 ? 243 MET   B C   1 
ATOM   2740 O  O   . MET   B 1 152 ? 166.330 -32.302 17.884 1.00 14.53 ? 243 MET   B O   1 
ATOM   2741 C  CB  . MET   B 1 152 ? 166.940 -32.762 14.855 1.00 21.09 ? 243 MET   B CB  1 
ATOM   2742 C  CG  . MET   B 1 152 ? 166.913 -33.518 13.549 1.00 36.65 ? 243 MET   B CG  1 
ATOM   2743 S  SD  . MET   B 1 152 ? 168.522 -34.261 13.231 1.00 41.08 ? 243 MET   B SD  1 
ATOM   2744 C  CE  . MET   B 1 152 ? 169.515 -32.791 13.007 1.00 33.81 ? 243 MET   B CE  1 
ATOM   2745 N  N   . GLY   B 1 153 ? 168.555 -32.621 17.720 1.00 15.08 ? 244 GLY   B N   1 
ATOM   2746 C  CA  . GLY   B 1 153 ? 168.837 -31.937 18.969 1.00 17.18 ? 244 GLY   B CA  1 
ATOM   2747 C  C   . GLY   B 1 153 ? 168.502 -32.729 20.212 1.00 20.69 ? 244 GLY   B C   1 
ATOM   2748 O  O   . GLY   B 1 153 ? 168.688 -32.216 21.321 1.00 20.57 ? 244 GLY   B O   1 
ATOM   2749 N  N   . GLY   B 1 154 ? 167.988 -33.950 20.061 1.00 14.93 ? 245 GLY   B N   1 
ATOM   2750 C  CA  . GLY   B 1 154 ? 167.777 -34.878 21.162 1.00 11.43 ? 245 GLY   B CA  1 
ATOM   2751 C  C   . GLY   B 1 154 ? 168.612 -36.125 20.942 1.00 18.44 ? 245 GLY   B C   1 
ATOM   2752 O  O   . GLY   B 1 154 ? 169.828 -36.025 20.757 1.00 16.23 ? 245 GLY   B O   1 
ATOM   2753 N  N   . MET   B 1 155 ? 167.985 -37.302 20.926 1.00 14.96 ? 246 MET   B N   1 
ATOM   2754 C  CA  . MET   B 1 155 ? 168.755 -38.525 20.714 1.00 11.97 ? 246 MET   B CA  1 
ATOM   2755 C  C   . MET   B 1 155 ? 169.457 -38.521 19.362 1.00 13.36 ? 246 MET   B C   1 
ATOM   2756 O  O   . MET   B 1 155 ? 170.536 -39.108 19.227 1.00 19.49 ? 246 MET   B O   1 
ATOM   2757 C  CB  . MET   B 1 155 ? 167.837 -39.744 20.878 1.00 11.49 ? 246 MET   B CB  1 
ATOM   2758 C  CG  . MET   B 1 155 ? 167.406 -39.939 22.336 1.00 12.76 ? 246 MET   B CG  1 
ATOM   2759 S  SD  . MET   B 1 155 ? 166.363 -41.374 22.660 1.00 12.93 ? 246 MET   B SD  1 
ATOM   2760 C  CE  . MET   B 1 155 ? 164.751 -40.760 22.158 1.00 16.12 ? 246 MET   B CE  1 
ATOM   2761 N  N   . ASN   B 1 156 ? 168.886 -37.837 18.363 1.00 12.42 ? 247 ASN   B N   1 
ATOM   2762 C  CA  . ASN   B 1 156 ? 169.544 -37.617 17.073 1.00 13.37 ? 247 ASN   B CA  1 
ATOM   2763 C  C   . ASN   B 1 156 ? 170.109 -38.921 16.504 1.00 17.49 ? 247 ASN   B C   1 
ATOM   2764 O  O   . ASN   B 1 156 ? 171.277 -39.007 16.103 1.00 15.10 ? 247 ASN   B O   1 
ATOM   2765 C  CB  . ASN   B 1 156 ? 170.637 -36.551 17.199 1.00 22.00 ? 247 ASN   B CB  1 
ATOM   2766 C  CG  . ASN   B 1 156 ? 171.179 -36.104 15.850 1.00 30.68 ? 247 ASN   B CG  1 
ATOM   2767 O  OD1 . ASN   B 1 156 ? 170.505 -36.215 14.825 1.00 35.59 ? 247 ASN   B OD1 1 
ATOM   2768 N  ND2 . ASN   B 1 156 ? 172.409 -35.610 15.842 1.00 31.43 ? 247 ASN   B ND2 1 
ATOM   2769 N  N   . ARG   B 1 157 ? 169.263 -39.954 16.495 1.00 13.21 ? 248 ARG   B N   1 
ATOM   2770 C  CA  . ARG   B 1 157 ? 169.527 -41.267 15.910 1.00 18.57 ? 248 ARG   B CA  1 
ATOM   2771 C  C   . ARG   B 1 157 ? 170.495 -42.118 16.726 1.00 19.34 ? 248 ARG   B C   1 
ATOM   2772 O  O   . ARG   B 1 157 ? 170.880 -43.201 16.275 1.00 23.05 ? 248 ARG   B O   1 
ATOM   2773 C  CB  . ARG   B 1 157 ? 170.037 -41.150 14.465 1.00 15.87 ? 248 ARG   B CB  1 
ATOM   2774 C  CG  . ARG   B 1 157 ? 169.109 -40.329 13.581 1.00 18.44 ? 248 ARG   B CG  1 
ATOM   2775 C  CD  . ARG   B 1 157 ? 169.446 -40.444 12.101 1.00 34.26 ? 248 ARG   B CD  1 
ATOM   2776 N  NE  . ARG   B 1 157 ? 168.416 -39.795 11.285 1.00 48.98 ? 248 ARG   B NE  1 
ATOM   2777 C  CZ  . ARG   B 1 157 ? 167.295 -40.389 10.873 1.00 51.20 ? 248 ARG   B CZ  1 
ATOM   2778 N  NH1 . ARG   B 1 157 ? 167.048 -41.657 11.192 1.00 49.02 ? 248 ARG   B NH1 1 
ATOM   2779 N  NH2 . ARG   B 1 157 ? 166.415 -39.712 10.141 1.00 51.09 ? 248 ARG   B NH2 1 
ATOM   2780 N  N   . ARG   B 1 158 ? 170.900 -41.675 17.903 1.00 12.99 ? 249 ARG   B N   1 
ATOM   2781 C  CA  . ARG   B 1 158 ? 171.793 -42.496 18.728 1.00 15.50 ? 249 ARG   B CA  1 
ATOM   2782 C  C   . ARG   B 1 158 ? 170.987 -43.519 19.520 1.00 14.30 ? 249 ARG   B C   1 
ATOM   2783 O  O   . ARG   B 1 158 ? 169.963 -43.162 20.115 1.00 14.40 ? 249 ARG   B O   1 
ATOM   2784 C  CB  . ARG   B 1 158 ? 172.599 -41.605 19.676 1.00 13.29 ? 249 ARG   B CB  1 
ATOM   2785 C  CG  . ARG   B 1 158 ? 173.550 -40.684 18.920 1.00 15.82 ? 249 ARG   B CG  1 
ATOM   2786 C  CD  . ARG   B 1 158 ? 174.170 -39.602 19.794 1.00 21.11 ? 249 ARG   B CD  1 
ATOM   2787 N  NE  . ARG   B 1 158 ? 173.180 -38.656 20.304 1.00 17.58 ? 249 ARG   B NE  1 
ATOM   2788 C  CZ  . ARG   B 1 158 ? 173.471 -37.647 21.119 1.00 20.53 ? 249 ARG   B CZ  1 
ATOM   2789 N  NH1 . ARG   B 1 158 ? 174.722 -37.460 21.520 1.00 18.97 ? 249 ARG   B NH1 1 
ATOM   2790 N  NH2 . ARG   B 1 158 ? 172.511 -36.833 21.539 1.00 18.17 ? 249 ARG   B NH2 1 
ATOM   2791 N  N   . PRO   B 1 159 ? 171.401 -44.789 19.551 1.00 13.44 ? 250 PRO   B N   1 
ATOM   2792 C  CA  . PRO   B 1 159 ? 170.678 -45.769 20.370 1.00 13.41 ? 250 PRO   B CA  1 
ATOM   2793 C  C   . PRO   B 1 159 ? 170.860 -45.507 21.860 1.00 12.60 ? 250 PRO   B C   1 
ATOM   2794 O  O   . PRO   B 1 159 ? 171.905 -45.030 22.311 1.00 11.58 ? 250 PRO   B O   1 
ATOM   2795 C  CB  . PRO   B 1 159 ? 171.305 -47.110 19.963 1.00 15.17 ? 250 PRO   B CB  1 
ATOM   2796 C  CG  . PRO   B 1 159 ? 172.627 -46.767 19.412 1.00 22.63 ? 250 PRO   B CG  1 
ATOM   2797 C  CD  . PRO   B 1 159 ? 172.450 -45.425 18.739 1.00 16.30 ? 250 PRO   B CD  1 
ATOM   2798 N  N   . ILE   B 1 160 ? 169.827 -45.853 22.630 1.00 11.91 ? 251 ILE   B N   1 
ATOM   2799 C  CA  . ILE   B 1 160 ? 169.856 -45.733 24.083 1.00 9.14  ? 251 ILE   B CA  1 
ATOM   2800 C  C   . ILE   B 1 160 ? 169.584 -47.090 24.713 1.00 8.67  ? 251 ILE   B C   1 
ATOM   2801 O  O   . ILE   B 1 160 ? 169.080 -48.021 24.077 1.00 9.73  ? 251 ILE   B O   1 
ATOM   2802 C  CB  . ILE   B 1 160 ? 168.833 -44.706 24.613 1.00 8.74  ? 251 ILE   B CB  1 
ATOM   2803 C  CG1 . ILE   B 1 160 ? 167.417 -45.101 24.168 1.00 14.63 ? 251 ILE   B CG1 1 
ATOM   2804 C  CG2 . ILE   B 1 160 ? 169.210 -43.276 24.152 1.00 9.50  ? 251 ILE   B CG2 1 
ATOM   2805 C  CD1 . ILE   B 1 160 ? 166.305 -44.517 25.048 1.00 11.09 ? 251 ILE   B CD1 1 
ATOM   2806 N  N   . LEU   B 1 161 ? 169.920 -47.179 25.995 1.00 8.34  ? 252 LEU   B N   1 
ATOM   2807 C  CA  . LEU   B 1 161 ? 169.554 -48.287 26.858 1.00 12.38 ? 252 LEU   B CA  1 
ATOM   2808 C  C   . LEU   B 1 161 ? 168.668 -47.736 27.955 1.00 14.23 ? 252 LEU   B C   1 
ATOM   2809 O  O   . LEU   B 1 161 ? 168.898 -46.628 28.432 1.00 11.65 ? 252 LEU   B O   1 
ATOM   2810 C  CB  . LEU   B 1 161 ? 170.782 -48.931 27.516 1.00 16.84 ? 252 LEU   B CB  1 
ATOM   2811 C  CG  . LEU   B 1 161 ? 172.006 -49.161 26.647 1.00 30.52 ? 252 LEU   B CG  1 
ATOM   2812 C  CD1 . LEU   B 1 161 ? 173.166 -49.671 27.488 1.00 32.92 ? 252 LEU   B CD1 1 
ATOM   2813 C  CD2 . LEU   B 1 161 ? 171.637 -50.156 25.562 1.00 35.73 ? 252 LEU   B CD2 1 
ATOM   2814 N  N   . THR   B 1 162 ? 167.671 -48.501 28.369 1.00 7.24  ? 253 THR   B N   1 
ATOM   2815 C  CA  . THR   B 1 162 ? 166.964 -48.194 29.602 1.00 8.59  ? 253 THR   B CA  1 
ATOM   2816 C  C   . THR   B 1 162 ? 167.545 -49.090 30.685 1.00 10.00 ? 253 THR   B C   1 
ATOM   2817 O  O   . THR   B 1 162 ? 167.706 -50.294 30.469 1.00 10.70 ? 253 THR   B O   1 
ATOM   2818 C  CB  . THR   B 1 162 ? 165.453 -48.408 29.461 1.00 8.30  ? 253 THR   B CB  1 
ATOM   2819 O  OG1 . THR   B 1 162 ? 164.931 -47.491 28.479 1.00 10.39 ? 253 THR   B OG1 1 
ATOM   2820 C  CG2 . THR   B 1 162 ? 164.747 -48.156 30.799 1.00 5.66  ? 253 THR   B CG2 1 
ATOM   2821 N  N   . ILE   B 1 163 ? 167.902 -48.499 31.822 1.00 6.29  ? 254 ILE   B N   1 
ATOM   2822 C  CA  . ILE   B 1 163 ? 168.402 -49.250 32.976 1.00 6.72  ? 254 ILE   B CA  1 
ATOM   2823 C  C   . ILE   B 1 163 ? 167.323 -49.221 34.042 1.00 5.93  ? 254 ILE   B C   1 
ATOM   2824 O  O   . ILE   B 1 163 ? 166.906 -48.142 34.480 1.00 9.38  ? 254 ILE   B O   1 
ATOM   2825 C  CB  . ILE   B 1 163 ? 169.720 -48.667 33.514 1.00 9.20  ? 254 ILE   B CB  1 
ATOM   2826 C  CG1 . ILE   B 1 163 ? 170.777 -48.687 32.419 1.00 7.47  ? 254 ILE   B CG1 1 
ATOM   2827 C  CG2 . ILE   B 1 163 ? 170.182 -49.458 34.757 1.00 7.49  ? 254 ILE   B CG2 1 
ATOM   2828 C  CD1 . ILE   B 1 163 ? 171.984 -47.778 32.703 1.00 8.30  ? 254 ILE   B CD1 1 
ATOM   2829 N  N   . ILE   B 1 164 ? 166.857 -50.404 34.448 1.00 5.72  ? 255 ILE   B N   1 
ATOM   2830 C  CA  . ILE   B 1 164 ? 165.857 -50.554 35.501 1.00 8.48  ? 255 ILE   B CA  1 
ATOM   2831 C  C   . ILE   B 1 164 ? 166.574 -51.059 36.743 1.00 11.12 ? 255 ILE   B C   1 
ATOM   2832 O  O   . ILE   B 1 164 ? 167.209 -52.120 36.703 1.00 7.42  ? 255 ILE   B O   1 
ATOM   2833 C  CB  . ILE   B 1 164 ? 164.746 -51.537 35.098 1.00 9.50  ? 255 ILE   B CB  1 
ATOM   2834 C  CG1 . ILE   B 1 164 ? 164.098 -51.142 33.775 1.00 9.84  ? 255 ILE   B CG1 1 
ATOM   2835 C  CG2 . ILE   B 1 164 ? 163.691 -51.623 36.189 1.00 6.92  ? 255 ILE   B CG2 1 
ATOM   2836 C  CD1 . ILE   B 1 164 ? 163.391 -49.826 33.807 1.00 9.72  ? 255 ILE   B CD1 1 
ATOM   2837 N  N   . THR   B 1 165 ? 166.471 -50.323 37.851 1.00 7.27  ? 256 THR   B N   1 
ATOM   2838 C  CA  A THR   B 1 165 ? 167.090 -50.732 39.103 0.28 8.97  ? 256 THR   B CA  1 
ATOM   2839 C  CA  B THR   B 1 165 ? 167.092 -50.728 39.105 0.72 8.83  ? 256 THR   B CA  1 
ATOM   2840 C  C   . THR   B 1 165 ? 166.023 -50.961 40.163 1.00 11.20 ? 256 THR   B C   1 
ATOM   2841 O  O   . THR   B 1 165 ? 165.049 -50.198 40.262 1.00 9.41  ? 256 THR   B O   1 
ATOM   2842 C  CB  A THR   B 1 165 ? 168.102 -49.691 39.594 0.28 9.84  ? 256 THR   B CB  1 
ATOM   2843 C  CB  B THR   B 1 165 ? 168.120 -49.688 39.602 0.72 8.91  ? 256 THR   B CB  1 
ATOM   2844 O  OG1 A THR   B 1 165 ? 168.593 -50.065 40.888 0.28 7.87  ? 256 THR   B OG1 1 
ATOM   2845 O  OG1 B THR   B 1 165 ? 167.564 -48.372 39.542 0.72 15.15 ? 256 THR   B OG1 1 
ATOM   2846 C  CG2 A THR   B 1 165 ? 167.452 -48.346 39.689 0.28 12.76 ? 256 THR   B CG2 1 
ATOM   2847 C  CG2 B THR   B 1 165 ? 169.379 -49.738 38.753 0.72 6.94  ? 256 THR   B CG2 1 
ATOM   2848 N  N   . LEU   B 1 166 ? 166.203 -52.038 40.923 1.00 11.46 ? 257 LEU   B N   1 
ATOM   2849 C  CA  . LEU   B 1 166 ? 165.437 -52.319 42.128 1.00 9.80  ? 257 LEU   B CA  1 
ATOM   2850 C  C   . LEU   B 1 166 ? 166.228 -51.712 43.284 1.00 6.83  ? 257 LEU   B C   1 
ATOM   2851 O  O   . LEU   B 1 166 ? 167.430 -51.967 43.402 1.00 8.36  ? 257 LEU   B O   1 
ATOM   2852 C  CB  . LEU   B 1 166 ? 165.272 -53.833 42.304 1.00 9.01  ? 257 LEU   B CB  1 
ATOM   2853 C  CG  . LEU   B 1 166 ? 164.260 -54.325 43.338 1.00 9.17  ? 257 LEU   B CG  1 
ATOM   2854 C  CD1 . LEU   B 1 166 ? 162.837 -54.020 42.864 1.00 8.65  ? 257 LEU   B CD1 1 
ATOM   2855 C  CD2 . LEU   B 1 166 ? 164.434 -55.815 43.615 1.00 9.60  ? 257 LEU   B CD2 1 
ATOM   2856 N  N   . GLU   B 1 167 ? 165.589 -50.851 44.078 1.00 10.00 ? 258 GLU   B N   1 
ATOM   2857 C  CA  . GLU   B 1 167 ? 166.263 -50.093 45.127 1.00 8.65  ? 258 GLU   B CA  1 
ATOM   2858 C  C   . GLU   B 1 167 ? 165.556 -50.304 46.453 1.00 8.07  ? 258 GLU   B C   1 
ATOM   2859 O  O   . GLU   B 1 167 ? 164.337 -50.450 46.490 1.00 7.94  ? 258 GLU   B O   1 
ATOM   2860 C  CB  . GLU   B 1 167 ? 166.253 -48.579 44.878 1.00 8.25  ? 258 GLU   B CB  1 
ATOM   2861 C  CG  . GLU   B 1 167 ? 166.850 -48.084 43.599 1.00 19.56 ? 258 GLU   B CG  1 
ATOM   2862 C  CD  . GLU   B 1 167 ? 166.682 -46.563 43.444 1.00 16.15 ? 258 GLU   B CD  1 
ATOM   2863 O  OE1 . GLU   B 1 167 ? 165.843 -45.947 44.152 1.00 15.42 ? 258 GLU   B OE1 1 
ATOM   2864 O  OE2 . GLU   B 1 167 ? 167.410 -45.992 42.611 1.00 20.04 ? 258 GLU   B OE2 1 
ATOM   2865 N  N   . ASP   B 1 168 ? 166.308 -50.249 47.553 1.00 10.08 ? 259 ASP   B N   1 
ATOM   2866 C  CA  . ASP   B 1 168 ? 165.622 -50.198 48.832 1.00 9.23  ? 259 ASP   B CA  1 
ATOM   2867 C  C   . ASP   B 1 168 ? 165.132 -48.772 49.091 1.00 13.32 ? 259 ASP   B C   1 
ATOM   2868 O  O   . ASP   B 1 168 ? 165.259 -47.877 48.246 1.00 10.03 ? 259 ASP   B O   1 
ATOM   2869 C  CB  . ASP   B 1 168 ? 166.505 -50.738 49.961 1.00 9.85  ? 259 ASP   B CB  1 
ATOM   2870 C  CG  . ASP   B 1 168 ? 167.737 -49.887 50.252 1.00 14.15 ? 259 ASP   B CG  1 
ATOM   2871 O  OD1 . ASP   B 1 168 ? 167.812 -48.696 49.879 1.00 12.58 ? 259 ASP   B OD1 1 
ATOM   2872 O  OD2 . ASP   B 1 168 ? 168.650 -50.436 50.910 1.00 16.64 ? 259 ASP   B OD2 1 
ATOM   2873 N  N   . SER   B 1 169 ? 164.581 -48.546 50.283 1.00 10.43 ? 260 SER   B N   1 
ATOM   2874 C  CA  . SER   B 1 169 ? 163.932 -47.269 50.572 1.00 10.99 ? 260 SER   B CA  1 
ATOM   2875 C  C   . SER   B 1 169 ? 164.920 -46.107 50.663 1.00 15.02 ? 260 SER   B C   1 
ATOM   2876 O  O   . SER   B 1 169 ? 164.506 -44.947 50.531 1.00 14.36 ? 260 SER   B O   1 
ATOM   2877 C  CB  . SER   B 1 169 ? 163.120 -47.385 51.865 1.00 11.77 ? 260 SER   B CB  1 
ATOM   2878 O  OG  . SER   B 1 169 ? 163.929 -47.725 52.985 1.00 12.79 ? 260 SER   B OG  1 
ATOM   2879 N  N   . SER   B 1 170 ? 166.204 -46.389 50.882 1.00 13.00 ? 261 SER   B N   1 
ATOM   2880 C  CA  . SER   B 1 170 ? 167.267 -45.391 50.873 1.00 13.74 ? 261 SER   B CA  1 
ATOM   2881 C  C   . SER   B 1 170 ? 167.835 -45.121 49.490 1.00 12.11 ? 261 SER   B C   1 
ATOM   2882 O  O   . SER   B 1 170 ? 168.636 -44.190 49.345 1.00 12.80 ? 261 SER   B O   1 
ATOM   2883 C  CB  . SER   B 1 170 ? 168.425 -45.833 51.775 1.00 15.90 ? 261 SER   B CB  1 
ATOM   2884 O  OG  . SER   B 1 170 ? 168.039 -45.849 53.128 1.00 17.91 ? 261 SER   B OG  1 
ATOM   2885 N  N   . GLY   B 1 171 ? 167.460 -45.914 48.486 1.00 10.92 ? 262 GLY   B N   1 
ATOM   2886 C  CA  . GLY   B 1 171 ? 168.046 -45.825 47.167 1.00 12.76 ? 262 GLY   B CA  1 
ATOM   2887 C  C   . GLY   B 1 171 ? 169.191 -46.781 46.914 1.00 17.40 ? 262 GLY   B C   1 
ATOM   2888 O  O   . GLY   B 1 171 ? 169.770 -46.739 45.825 1.00 15.96 ? 262 GLY   B O   1 
ATOM   2889 N  N   . ASN   B 1 172 ? 169.528 -47.645 47.872 1.00 12.36 ? 263 ASN   B N   1 
ATOM   2890 C  CA  . ASN   B 1 172 ? 170.612 -48.603 47.682 1.00 12.26 ? 263 ASN   B CA  1 
ATOM   2891 C  C   . ASN   B 1 172 ? 170.222 -49.683 46.687 1.00 9.64  ? 263 ASN   B C   1 
ATOM   2892 O  O   . ASN   B 1 172 ? 169.059 -50.081 46.592 1.00 10.42 ? 263 ASN   B O   1 
ATOM   2893 C  CB  . ASN   B 1 172 ? 170.996 -49.267 49.002 1.00 12.47 ? 263 ASN   B CB  1 
ATOM   2894 C  CG  . ASN   B 1 172 ? 171.398 -48.272 50.045 1.00 18.73 ? 263 ASN   B CG  1 
ATOM   2895 O  OD1 . ASN   B 1 172 ? 172.215 -47.382 49.790 1.00 19.67 ? 263 ASN   B OD1 1 
ATOM   2896 N  ND2 . ASN   B 1 172 ? 170.815 -48.396 51.231 1.00 19.11 ? 263 ASN   B ND2 1 
ATOM   2897 N  N   . LEU   B 1 173 ? 171.225 -50.191 45.980 1.00 9.69  ? 264 LEU   B N   1 
ATOM   2898 C  CA  . LEU   B 1 173 ? 170.986 -51.118 44.880 1.00 9.62  ? 264 LEU   B CA  1 
ATOM   2899 C  C   . LEU   B 1 173 ? 170.561 -52.483 45.391 1.00 10.03 ? 264 LEU   B C   1 
ATOM   2900 O  O   . LEU   B 1 173 ? 171.238 -53.077 46.237 1.00 11.78 ? 264 LEU   B O   1 
ATOM   2901 C  CB  . LEU   B 1 173 ? 172.253 -51.256 44.035 1.00 14.09 ? 264 LEU   B CB  1 
ATOM   2902 C  CG  . LEU   B 1 173 ? 172.188 -52.269 42.882 1.00 17.62 ? 264 LEU   B CG  1 
ATOM   2903 C  CD1 . LEU   B 1 173 ? 171.288 -51.761 41.766 1.00 12.59 ? 264 LEU   B CD1 1 
ATOM   2904 C  CD2 . LEU   B 1 173 ? 173.579 -52.592 42.349 1.00 21.73 ? 264 LEU   B CD2 1 
ATOM   2905 N  N   . LEU   B 1 174 ? 169.443 -53.000 44.865 1.00 8.54  ? 265 LEU   B N   1 
ATOM   2906 C  CA  . LEU   B 1 174 ? 169.075 -54.392 45.115 1.00 8.11  ? 265 LEU   B CA  1 
ATOM   2907 C  C   . LEU   B 1 174 ? 169.143 -55.280 43.883 1.00 10.62 ? 265 LEU   B C   1 
ATOM   2908 O  O   . LEU   B 1 174 ? 169.297 -56.500 44.030 1.00 10.05 ? 265 LEU   B O   1 
ATOM   2909 C  CB  . LEU   B 1 174 ? 167.660 -54.486 45.698 1.00 7.90  ? 265 LEU   B CB  1 
ATOM   2910 C  CG  . LEU   B 1 174 ? 167.451 -53.718 47.006 1.00 10.14 ? 265 LEU   B CG  1 
ATOM   2911 C  CD1 . LEU   B 1 174 ? 165.992 -53.885 47.419 1.00 8.24  ? 265 LEU   B CD1 1 
ATOM   2912 C  CD2 . LEU   B 1 174 ? 168.423 -54.197 48.096 1.00 12.25 ? 265 LEU   B CD2 1 
ATOM   2913 N  N   . GLY   B 1 175 ? 169.035 -54.704 42.692 1.00 7.44  ? 266 GLY   B N   1 
ATOM   2914 C  CA  . GLY   B 1 175 ? 168.969 -55.477 41.465 1.00 7.26  ? 266 GLY   B CA  1 
ATOM   2915 C  C   . GLY   B 1 175 ? 169.011 -54.532 40.288 1.00 12.30 ? 266 GLY   B C   1 
ATOM   2916 O  O   . GLY   B 1 175 ? 168.699 -53.344 40.415 1.00 10.61 ? 266 GLY   B O   1 
ATOM   2917 N  N   . ARG   B 1 176 ? 169.396 -55.071 39.135 1.00 7.61  ? 267 ARG   B N   1 
ATOM   2918 C  CA  . ARG   B 1 176 ? 169.491 -54.226 37.950 1.00 6.83  ? 267 ARG   B CA  1 
ATOM   2919 C  C   . ARG   B 1 176 ? 169.312 -55.081 36.703 1.00 11.46 ? 267 ARG   B C   1 
ATOM   2920 O  O   . ARG   B 1 176 ? 169.800 -56.212 36.649 1.00 7.28  ? 267 ARG   B O   1 
ATOM   2921 C  CB  . ARG   B 1 176 ? 170.842 -53.493 37.890 1.00 9.01  ? 267 ARG   B CB  1 
ATOM   2922 C  CG  . ARG   B 1 176 ? 170.980 -52.569 36.667 1.00 7.29  ? 267 ARG   B CG  1 
ATOM   2923 C  CD  . ARG   B 1 176 ? 172.423 -52.096 36.459 1.00 17.29 ? 267 ARG   B CD  1 
ATOM   2924 N  NE  . ARG   B 1 176 ? 172.948 -51.360 37.602 1.00 14.33 ? 267 ARG   B NE  1 
ATOM   2925 C  CZ  . ARG   B 1 176 ? 173.874 -51.800 38.453 1.00 17.05 ? 267 ARG   B CZ  1 
ATOM   2926 N  NH1 . ARG   B 1 176 ? 174.430 -53.004 38.323 1.00 11.51 ? 267 ARG   B NH1 1 
ATOM   2927 N  NH2 . ARG   B 1 176 ? 174.251 -51.019 39.451 1.00 13.87 ? 267 ARG   B NH2 1 
ATOM   2928 N  N   . ASP   B 1 177 ? 168.597 -54.534 35.715 1.00 8.12  ? 268 ASP   B N   1 
ATOM   2929 C  CA  . ASP   B 1 177 ? 168.408 -55.155 34.406 1.00 6.88  ? 268 ASP   B CA  1 
ATOM   2930 C  C   . ASP   B 1 177 ? 168.374 -54.015 33.399 1.00 8.46  ? 268 ASP   B C   1 
ATOM   2931 O  O   . ASP   B 1 177 ? 168.320 -52.848 33.781 1.00 7.99  ? 268 ASP   B O   1 
ATOM   2932 C  CB  . ASP   B 1 177 ? 167.114 -55.980 34.352 1.00 6.46  ? 268 ASP   B CB  1 
ATOM   2933 C  CG  . ASP   B 1 177 ? 167.145 -57.076 33.299 1.00 10.52 ? 268 ASP   B CG  1 
ATOM   2934 O  OD1 . ASP   B 1 177 ? 166.349 -58.036 33.437 1.00 9.96  ? 268 ASP   B OD1 1 
ATOM   2935 O  OD2 . ASP   B 1 177 ? 167.961 -57.001 32.351 1.00 11.49 ? 268 ASP   B OD2 1 
ATOM   2936 N  N   . SER   B 1 178 ? 168.422 -54.342 32.109 1.00 9.45  ? 269 SER   B N   1 
ATOM   2937 C  CA  . SER   B 1 178 ? 168.461 -53.276 31.109 1.00 8.82  ? 269 SER   B CA  1 
ATOM   2938 C  C   . SER   B 1 178 ? 168.108 -53.834 29.737 1.00 7.70  ? 269 SER   B C   1 
ATOM   2939 O  O   . SER   B 1 178 ? 168.139 -55.043 29.505 1.00 7.23  ? 269 SER   B O   1 
ATOM   2940 C  CB  . SER   B 1 178 ? 169.833 -52.596 31.055 1.00 9.68  ? 269 SER   B CB  1 
ATOM   2941 O  OG  . SER   B 1 178 ? 170.833 -53.500 30.599 1.00 9.93  ? 269 SER   B OG  1 
ATOM   2942 N  N   . PHE   B 1 179 ? 167.779 -52.918 28.829 1.00 6.80  ? 270 PHE   B N   1 
ATOM   2943 C  CA  . PHE   B 1 179 ? 167.369 -53.252 27.475 1.00 7.32  ? 270 PHE   B CA  1 
ATOM   2944 C  C   . PHE   B 1 179 ? 167.588 -52.023 26.600 1.00 9.17  ? 270 PHE   B C   1 
ATOM   2945 O  O   . PHE   B 1 179 ? 167.429 -50.891 27.063 1.00 7.09  ? 270 PHE   B O   1 
ATOM   2946 C  CB  . PHE   B 1 179 ? 165.900 -53.726 27.415 1.00 6.86  ? 270 PHE   B CB  1 
ATOM   2947 C  CG  . PHE   B 1 179 ? 164.886 -52.763 28.031 1.00 6.33  ? 270 PHE   B CG  1 
ATOM   2948 C  CD1 . PHE   B 1 179 ? 164.620 -52.773 29.398 1.00 6.52  ? 270 PHE   B CD1 1 
ATOM   2949 C  CD2 . PHE   B 1 179 ? 164.157 -51.885 27.220 1.00 6.71  ? 270 PHE   B CD2 1 
ATOM   2950 C  CE1 . PHE   B 1 179 ? 163.665 -51.904 29.962 1.00 5.68  ? 270 PHE   B CE1 1 
ATOM   2951 C  CE2 . PHE   B 1 179 ? 163.200 -51.012 27.777 1.00 6.50  ? 270 PHE   B CE2 1 
ATOM   2952 C  CZ  . PHE   B 1 179 ? 162.949 -51.037 29.154 1.00 5.71  ? 270 PHE   B CZ  1 
ATOM   2953 N  N   . GLU   B 1 180 ? 167.990 -52.256 25.356 1.00 9.23  ? 271 GLU   B N   1 
ATOM   2954 C  CA  . GLU   B 1 180 ? 168.050 -51.177 24.377 1.00 7.99  ? 271 GLU   B CA  1 
ATOM   2955 C  C   . GLU   B 1 180 ? 166.636 -50.746 23.996 1.00 8.37  ? 271 GLU   B C   1 
ATOM   2956 O  O   . GLU   B 1 180 ? 165.680 -51.526 24.076 1.00 7.50  ? 271 GLU   B O   1 
ATOM   2957 C  CB  . GLU   B 1 180 ? 168.838 -51.640 23.140 1.00 8.85  ? 271 GLU   B CB  1 
ATOM   2958 C  CG  . GLU   B 1 180 ? 169.151 -50.535 22.097 1.00 13.75 ? 271 GLU   B CG  1 
ATOM   2959 C  CD  . GLU   B 1 180 ? 170.068 -51.017 20.974 1.00 21.19 ? 271 GLU   B CD  1 
ATOM   2960 O  OE1 . GLU   B 1 180 ? 170.741 -52.059 21.152 1.00 18.66 ? 271 GLU   B OE1 1 
ATOM   2961 O  OE2 . GLU   B 1 180 ? 170.103 -50.358 19.908 1.00 18.60 ? 271 GLU   B OE2 1 
ATOM   2962 N  N   . VAL   B 1 181 ? 166.499 -49.491 23.559 1.00 9.28  ? 272 VAL   B N   1 
ATOM   2963 C  CA  . VAL   B 1 181 ? 165.204 -48.975 23.126 1.00 7.54  ? 272 VAL   B CA  1 
ATOM   2964 C  C   . VAL   B 1 181 ? 165.383 -48.250 21.809 1.00 13.25 ? 272 VAL   B C   1 
ATOM   2965 O  O   . VAL   B 1 181 ? 166.359 -47.518 21.622 1.00 11.51 ? 272 VAL   B O   1 
ATOM   2966 C  CB  . VAL   B 1 181 ? 164.564 -48.030 24.167 1.00 11.35 ? 272 VAL   B CB  1 
ATOM   2967 C  CG1 . VAL   B 1 181 ? 163.222 -47.488 23.643 1.00 7.86  ? 272 VAL   B CG1 1 
ATOM   2968 C  CG2 . VAL   B 1 181 ? 164.358 -48.768 25.482 1.00 12.59 ? 272 VAL   B CG2 1 
ATOM   2969 N  N   . ARG   B 1 182 ? 164.446 -48.464 20.890 1.00 9.06  ? 273 ARG   B N   1 
ATOM   2970 C  CA  . ARG   B 1 182 ? 164.318 -47.624 19.711 1.00 9.12  ? 273 ARG   B CA  1 
ATOM   2971 C  C   . ARG   B 1 182 ? 162.893 -47.107 19.688 1.00 11.69 ? 273 ARG   B C   1 
ATOM   2972 O  O   . ARG   B 1 182 ? 161.946 -47.899 19.697 1.00 11.28 ? 273 ARG   B O   1 
ATOM   2973 C  CB  . ARG   B 1 182 ? 164.634 -48.400 18.417 1.00 9.60  ? 273 ARG   B CB  1 
ATOM   2974 C  CG  . ARG   B 1 182 ? 164.350 -47.603 17.135 1.00 12.52 ? 273 ARG   B CG  1 
ATOM   2975 C  CD  . ARG   B 1 182 ? 164.748 -48.408 15.902 1.00 11.72 ? 273 ARG   B CD  1 
ATOM   2976 N  NE  . ARG   B 1 182 ? 164.281 -47.801 14.654 1.00 16.62 ? 273 ARG   B NE  1 
ATOM   2977 C  CZ  . ARG   B 1 182 ? 164.873 -46.778 14.052 1.00 25.51 ? 273 ARG   B CZ  1 
ATOM   2978 N  NH1 . ARG   B 1 182 ? 165.946 -46.226 14.600 1.00 31.38 ? 273 ARG   B NH1 1 
ATOM   2979 N  NH2 . ARG   B 1 182 ? 164.379 -46.293 12.913 1.00 27.51 ? 273 ARG   B NH2 1 
ATOM   2980 N  N   . VAL   B 1 183 ? 162.736 -45.790 19.674 1.00 9.87  ? 274 VAL   B N   1 
ATOM   2981 C  CA  . VAL   B 1 183 ? 161.423 -45.174 19.524 1.00 12.30 ? 274 VAL   B CA  1 
ATOM   2982 C  C   . VAL   B 1 183 ? 161.305 -44.751 18.066 1.00 13.14 ? 274 VAL   B C   1 
ATOM   2983 O  O   . VAL   B 1 183 ? 162.133 -43.974 17.576 1.00 10.08 ? 274 VAL   B O   1 
ATOM   2984 C  CB  . VAL   B 1 183 ? 161.241 -43.983 20.477 1.00 8.74  ? 274 VAL   B CB  1 
ATOM   2985 C  CG1 . VAL   B 1 183 ? 159.769 -43.589 20.556 1.00 8.90  ? 274 VAL   B CG1 1 
ATOM   2986 C  CG2 . VAL   B 1 183 ? 161.794 -44.321 21.868 1.00 8.13  ? 274 VAL   B CG2 1 
ATOM   2987 N  N   . CYS   B 1 184 ? 160.299 -45.277 17.367 1.00 10.05 ? 275 CYS   B N   1 
ATOM   2988 C  CA  . CYS   B 1 184 ? 160.221 -45.148 15.915 1.00 12.75 ? 275 CYS   B CA  1 
ATOM   2989 C  C   . CYS   B 1 184 ? 158.767 -45.250 15.469 1.00 13.55 ? 275 CYS   B C   1 
ATOM   2990 O  O   . CYS   B 1 184 ? 157.885 -45.644 16.234 1.00 11.04 ? 275 CYS   B O   1 
ATOM   2991 C  CB  . CYS   B 1 184 ? 161.059 -46.232 15.224 1.00 14.41 ? 275 CYS   B CB  1 
ATOM   2992 S  SG  . CYS   B 1 184 ? 160.661 -47.942 15.780 1.00 14.63 ? 275 CYS   B SG  1 
ATOM   2993 N  N   . ALA   B 1 185 ? 158.532 -44.919 14.192 1.00 16.35 ? 276 ALA   B N   1 
ATOM   2994 C  CA  . ALA   B 1 185 ? 157.169 -44.919 13.664 1.00 18.20 ? 276 ALA   B CA  1 
ATOM   2995 C  C   . ALA   B 1 185 ? 156.620 -46.327 13.465 1.00 16.01 ? 276 ALA   B C   1 
ATOM   2996 O  O   . ALA   B 1 185 ? 155.412 -46.550 13.624 1.00 14.87 ? 276 ALA   B O   1 
ATOM   2997 C  CB  . ALA   B 1 185 ? 157.121 -44.159 12.336 1.00 20.52 ? 276 ALA   B CB  1 
ATOM   2998 N  N   . CYS   B 1 186 ? 157.470 -47.288 13.107 1.00 13.89 ? 277 CYS   B N   1 
ATOM   2999 C  CA  A CYS   B 1 186 ? 157.022 -48.635 12.755 0.74 13.73 ? 277 CYS   B CA  1 
ATOM   3000 C  CA  B CYS   B 1 186 ? 157.038 -48.637 12.740 0.26 15.96 ? 277 CYS   B CA  1 
ATOM   3001 C  C   . CYS   B 1 186 ? 157.881 -49.651 13.494 1.00 13.22 ? 277 CYS   B C   1 
ATOM   3002 O  O   . CYS   B 1 186 ? 158.813 -50.236 12.928 1.00 16.58 ? 277 CYS   B O   1 
ATOM   3003 C  CB  A CYS   B 1 186 ? 157.065 -48.851 11.244 0.74 19.16 ? 277 CYS   B CB  1 
ATOM   3004 C  CB  B CYS   B 1 186 ? 157.164 -48.872 11.235 0.26 19.23 ? 277 CYS   B CB  1 
ATOM   3005 S  SG  A CYS   B 1 186 ? 156.099 -50.281 10.688 0.74 20.68 ? 277 CYS   B SG  1 
ATOM   3006 S  SG  B CYS   B 1 186 ? 156.221 -47.756 10.202 0.26 21.96 ? 277 CYS   B SG  1 
ATOM   3007 N  N   . PRO   B 1 187 ? 157.582 -49.889 14.771 1.00 16.69 ? 278 PRO   B N   1 
ATOM   3008 C  CA  . PRO   B 1 187 ? 158.382 -50.864 15.532 1.00 13.38 ? 278 PRO   B CA  1 
ATOM   3009 C  C   . PRO   B 1 187 ? 158.347 -52.269 14.955 1.00 11.48 ? 278 PRO   B C   1 
ATOM   3010 O  O   . PRO   B 1 187 ? 159.360 -52.975 15.018 1.00 12.80 ? 278 PRO   B O   1 
ATOM   3011 C  CB  . PRO   B 1 187 ? 157.771 -50.805 16.946 1.00 11.79 ? 278 PRO   B CB  1 
ATOM   3012 C  CG  . PRO   B 1 187 ? 156.601 -49.885 16.873 1.00 17.77 ? 278 PRO   B CG  1 
ATOM   3013 C  CD  . PRO   B 1 187 ? 156.704 -49.077 15.630 1.00 17.04 ? 278 PRO   B CD  1 
ATOM   3014 N  N   . GLY   B 1 188 ? 157.215 -52.695 14.391 1.00 13.67 ? 279 GLY   B N   1 
ATOM   3015 C  CA  . GLY   B 1 188 ? 157.146 -54.030 13.813 1.00 16.48 ? 279 GLY   B CA  1 
ATOM   3016 C  C   . GLY   B 1 188 ? 158.134 -54.225 12.678 1.00 18.53 ? 279 GLY   B C   1 
ATOM   3017 O  O   . GLY   B 1 188 ? 158.940 -55.162 12.687 1.00 17.54 ? 279 GLY   B O   1 
ATOM   3018 N  N   . ARG   B 1 189 ? 158.092 -53.340 11.681 1.00 14.43 ? 280 ARG   B N   1 
ATOM   3019 C  CA  . ARG   B 1 189 ? 159.014 -53.490 10.561 1.00 17.95 ? 280 ARG   B CA  1 
ATOM   3020 C  C   . ARG   B 1 189 ? 160.457 -53.306 11.010 1.00 17.21 ? 280 ARG   B C   1 
ATOM   3021 O  O   . ARG   B 1 189 ? 161.362 -53.968 10.485 1.00 17.17 ? 280 ARG   B O   1 
ATOM   3022 C  CB  . ARG   B 1 189 ? 158.666 -52.503 9.440  1.00 20.15 ? 280 ARG   B CB  1 
ATOM   3023 N  N   . ASP   B 1 190 ? 160.690 -52.423 11.983 1.00 14.59 ? 281 ASP   B N   1 
ATOM   3024 C  CA  . ASP   B 1 190 ? 162.056 -52.152 12.409 1.00 19.41 ? 281 ASP   B CA  1 
ATOM   3025 C  C   . ASP   B 1 190 ? 162.622 -53.319 13.199 1.00 17.54 ? 281 ASP   B C   1 
ATOM   3026 O  O   . ASP   B 1 190 ? 163.795 -53.672 13.030 1.00 15.44 ? 281 ASP   B O   1 
ATOM   3027 C  CB  . ASP   B 1 190 ? 162.116 -50.860 13.226 1.00 13.54 ? 281 ASP   B CB  1 
ATOM   3028 C  CG  . ASP   B 1 190 ? 162.089 -49.619 12.342 1.00 24.79 ? 281 ASP   B CG  1 
ATOM   3029 O  OD1 . ASP   B 1 190 ? 162.057 -49.783 11.104 1.00 23.62 ? 281 ASP   B OD1 1 
ATOM   3030 O  OD2 . ASP   B 1 190 ? 162.102 -48.490 12.867 1.00 23.53 ? 281 ASP   B OD2 1 
ATOM   3031 N  N   . ARG   B 1 191 ? 161.806 -53.936 14.061 1.00 13.31 ? 282 ARG   B N   1 
ATOM   3032 C  CA  . ARG   B 1 191 ? 162.267 -55.140 14.740 1.00 13.43 ? 282 ARG   B CA  1 
ATOM   3033 C  C   . ARG   B 1 191 ? 162.598 -56.247 13.740 1.00 15.15 ? 282 ARG   B C   1 
ATOM   3034 O  O   . ARG   B 1 191 ? 163.618 -56.928 13.877 1.00 16.07 ? 282 ARG   B O   1 
ATOM   3035 C  CB  . ARG   B 1 191 ? 161.229 -55.625 15.752 1.00 12.16 ? 282 ARG   B CB  1 
ATOM   3036 C  CG  . ARG   B 1 191 ? 161.631 -56.965 16.364 1.00 12.62 ? 282 ARG   B CG  1 
ATOM   3037 C  CD  . ARG   B 1 191 ? 160.711 -57.427 17.493 1.00 12.30 ? 282 ARG   B CD  1 
ATOM   3038 N  NE  . ARG   B 1 191 ? 160.957 -58.838 17.773 1.00 12.41 ? 282 ARG   B NE  1 
ATOM   3039 C  CZ  . ARG   B 1 191 ? 160.077 -59.657 18.338 1.00 17.02 ? 282 ARG   B CZ  1 
ATOM   3040 N  NH1 . ARG   B 1 191 ? 158.887 -59.196 18.690 1.00 10.90 ? 282 ARG   B NH1 1 
ATOM   3041 N  NH2 . ARG   B 1 191 ? 160.380 -60.946 18.523 1.00 13.29 ? 282 ARG   B NH2 1 
ATOM   3042 N  N   . ARG   B 1 192 ? 161.762 -56.432 12.717 1.00 18.21 ? 283 ARG   B N   1 
ATOM   3043 C  CA  . ARG   B 1 192 ? 162.059 -57.453 11.712 1.00 20.12 ? 283 ARG   B CA  1 
ATOM   3044 C  C   . ARG   B 1 192 ? 163.364 -57.152 10.987 1.00 20.67 ? 283 ARG   B C   1 
ATOM   3045 O  O   . ARG   B 1 192 ? 164.201 -58.044 10.800 1.00 20.82 ? 283 ARG   B O   1 
ATOM   3046 C  CB  . ARG   B 1 192 ? 160.909 -57.563 10.711 1.00 25.13 ? 283 ARG   B CB  1 
ATOM   3047 C  CG  . ARG   B 1 192 ? 159.919 -58.661 11.028 1.00 28.16 ? 283 ARG   B CG  1 
ATOM   3048 C  CD  . ARG   B 1 192 ? 158.827 -58.750 9.968  1.00 36.35 ? 283 ARG   B CD  1 
ATOM   3049 N  NE  . ARG   B 1 192 ? 157.777 -57.755 10.181 1.00 40.59 ? 283 ARG   B NE  1 
ATOM   3050 C  CZ  . ARG   B 1 192 ? 157.451 -56.798 9.314  1.00 38.07 ? 283 ARG   B CZ  1 
ATOM   3051 N  NH1 . ARG   B 1 192 ? 158.086 -56.699 8.150  1.00 39.19 ? 283 ARG   B NH1 1 
ATOM   3052 N  NH2 . ARG   B 1 192 ? 156.475 -55.947 9.609  1.00 28.20 ? 283 ARG   B NH2 1 
ATOM   3053 N  N   . THR   B 1 193 ? 163.560 -55.894 10.588 1.00 18.99 ? 284 THR   B N   1 
ATOM   3054 C  CA  . THR   B 1 193 ? 164.781 -55.506 9.891  1.00 20.40 ? 284 THR   B CA  1 
ATOM   3055 C  C   . THR   B 1 193 ? 166.021 -55.771 10.738 1.00 20.43 ? 284 THR   B C   1 
ATOM   3056 O  O   . THR   B 1 193 ? 166.994 -56.372 10.265 1.00 23.25 ? 284 THR   B O   1 
ATOM   3057 C  CB  . THR   B 1 193 ? 164.701 -54.028 9.497  1.00 27.03 ? 284 THR   B CB  1 
ATOM   3058 O  OG1 . THR   B 1 193 ? 163.551 -53.814 8.665  1.00 25.81 ? 284 THR   B OG1 1 
ATOM   3059 C  CG2 . THR   B 1 193 ? 165.954 -53.600 8.742  1.00 25.17 ? 284 THR   B CG2 1 
ATOM   3060 N  N   . GLU   B 1 194 ? 166.015 -55.319 11.992 1.00 18.83 ? 285 GLU   B N   1 
ATOM   3061 C  CA  . GLU   B 1 194 ? 167.214 -55.461 12.809 1.00 20.49 ? 285 GLU   B CA  1 
ATOM   3062 C  C   . GLU   B 1 194 ? 167.452 -56.910 13.215 1.00 24.16 ? 285 GLU   B C   1 
ATOM   3063 O  O   . GLU   B 1 194 ? 168.607 -57.317 13.391 1.00 24.56 ? 285 GLU   B O   1 
ATOM   3064 C  CB  . GLU   B 1 194 ? 167.129 -54.548 14.035 1.00 19.91 ? 285 GLU   B CB  1 
ATOM   3065 C  CG  . GLU   B 1 194 ? 167.136 -53.064 13.662 1.00 20.68 ? 285 GLU   B CG  1 
ATOM   3066 C  CD  . GLU   B 1 194 ? 167.272 -52.145 14.861 1.00 25.17 ? 285 GLU   B CD  1 
ATOM   3067 O  OE1 . GLU   B 1 194 ? 166.829 -50.974 14.766 1.00 21.37 ? 285 GLU   B OE1 1 
ATOM   3068 O  OE2 . GLU   B 1 194 ? 167.826 -52.592 15.894 1.00 24.29 ? 285 GLU   B OE2 1 
ATOM   3069 N  N   . GLU   B 1 195 ? 166.391 -57.711 13.334 1.00 19.27 ? 286 GLU   B N   1 
ATOM   3070 C  CA  . GLU   B 1 195 ? 166.594 -59.134 13.592 1.00 20.27 ? 286 GLU   B CA  1 
ATOM   3071 C  C   . GLU   B 1 195 ? 167.172 -59.831 12.369 1.00 33.81 ? 286 GLU   B C   1 
ATOM   3072 O  O   . GLU   B 1 195 ? 167.994 -60.746 12.496 1.00 23.99 ? 286 GLU   B O   1 
ATOM   3073 C  CB  . GLU   B 1 195 ? 165.286 -59.791 14.035 1.00 19.27 ? 286 GLU   B CB  1 
ATOM   3074 C  CG  . GLU   B 1 195 ? 164.903 -59.384 15.464 1.00 17.43 ? 286 GLU   B CG  1 
ATOM   3075 C  CD  . GLU   B 1 195 ? 163.781 -60.215 16.060 1.00 22.91 ? 286 GLU   B CD  1 
ATOM   3076 O  OE1 . GLU   B 1 195 ? 163.196 -61.060 15.348 1.00 23.31 ? 286 GLU   B OE1 1 
ATOM   3077 O  OE2 . GLU   B 1 195 ? 163.490 -60.025 17.256 1.00 17.18 ? 286 GLU   B OE2 1 
ATOM   3078 N  N   . GLU   B 1 196 ? 166.777 -59.397 11.174 1.00 22.99 ? 287 GLU   B N   1 
ATOM   3079 C  CA  . GLU   B 1 196 ? 167.374 -59.973 9.975  1.00 29.22 ? 287 GLU   B CA  1 
ATOM   3080 C  C   . GLU   B 1 196 ? 168.821 -59.520 9.812  1.00 28.52 ? 287 GLU   B C   1 
ATOM   3081 O  O   . GLU   B 1 196 ? 169.678 -60.307 9.396  1.00 32.51 ? 287 GLU   B O   1 
ATOM   3082 C  CB  . GLU   B 1 196 ? 166.548 -59.615 8.743  1.00 35.07 ? 287 GLU   B CB  1 
ATOM   3083 C  CG  . GLU   B 1 196 ? 167.076 -60.243 7.451  1.00 47.34 ? 287 GLU   B CG  1 
ATOM   3084 C  CD  . GLU   B 1 196 ? 167.067 -61.764 7.490  1.00 59.31 ? 287 GLU   B CD  1 
ATOM   3085 O  OE1 . GLU   B 1 196 ? 166.157 -62.343 8.121  1.00 63.11 ? 287 GLU   B OE1 1 
ATOM   3086 O  OE2 . GLU   B 1 196 ? 167.974 -62.382 6.890  1.00 66.67 ? 287 GLU   B OE2 1 
ATOM   3087 N  N   . ASN   B 1 197 ? 169.117 -58.258 10.135 1.00 28.80 ? 288 ASN   B N   1 
ATOM   3088 C  CA  . ASN   B 1 197 ? 170.503 -57.799 10.088 1.00 31.67 ? 288 ASN   B CA  1 
ATOM   3089 C  C   . ASN   B 1 197 ? 171.383 -58.632 11.011 1.00 33.91 ? 288 ASN   B C   1 
ATOM   3090 O  O   . ASN   B 1 197 ? 172.497 -59.017 10.638 1.00 32.42 ? 288 ASN   B O   1 
ATOM   3091 C  CB  . ASN   B 1 197 ? 170.593 -56.321 10.465 1.00 31.20 ? 288 ASN   B CB  1 
ATOM   3092 C  CG  . ASN   B 1 197 ? 169.946 -55.412 9.437  1.00 42.63 ? 288 ASN   B CG  1 
ATOM   3093 O  OD1 . ASN   B 1 197 ? 169.794 -55.778 8.271  1.00 45.93 ? 288 ASN   B OD1 1 
ATOM   3094 N  ND2 . ASN   B 1 197 ? 169.568 -54.213 9.865  1.00 46.98 ? 288 ASN   B ND2 1 
ATOM   3095 N  N   . LEU   B 1 198 ? 170.894 -58.924 12.219 1.00 25.85 ? 289 LEU   B N   1 
ATOM   3096 C  CA  . LEU   B 1 198 ? 171.650 -59.760 13.146 1.00 27.28 ? 289 LEU   B CA  1 
ATOM   3097 C  C   . LEU   B 1 198 ? 171.825 -61.169 12.597 1.00 33.18 ? 289 LEU   B C   1 
ATOM   3098 O  O   . LEU   B 1 198 ? 172.901 -61.763 12.727 1.00 33.03 ? 289 LEU   B O   1 
ATOM   3099 C  CB  . LEU   B 1 198 ? 170.954 -59.799 14.509 1.00 26.74 ? 289 LEU   B CB  1 
ATOM   3100 C  CG  . LEU   B 1 198 ? 171.574 -60.696 15.588 1.00 32.09 ? 289 LEU   B CG  1 
ATOM   3101 C  CD1 . LEU   B 1 198 ? 172.971 -60.219 15.991 1.00 31.65 ? 289 LEU   B CD1 1 
ATOM   3102 C  CD2 . LEU   B 1 198 ? 170.661 -60.769 16.798 1.00 32.09 ? 289 LEU   B CD2 1 
ATOM   3103 N  N   . ARG   B 1 199 ? 170.778 -61.722 11.977 1.00 32.67 ? 290 ARG   B N   1 
ATOM   3104 C  CA  . ARG   B 1 199 ? 170.885 -63.071 11.428 1.00 38.07 ? 290 ARG   B CA  1 
ATOM   3105 C  C   . ARG   B 1 199 ? 171.942 -63.131 10.333 1.00 46.67 ? 290 ARG   B C   1 
ATOM   3106 O  O   . ARG   B 1 199 ? 172.678 -64.118 10.224 1.00 51.76 ? 290 ARG   B O   1 
ATOM   3107 C  CB  . ARG   B 1 199 ? 169.528 -63.542 10.903 1.00 37.23 ? 290 ARG   B CB  1 
ATOM   3108 N  N   . LYS   B 1 200 ? 172.053 -62.072 9.531  1.00 47.73 ? 291 LYS   B N   1 
ATOM   3109 C  CA  . LYS   B 1 200 ? 173.046 -62.005 8.465  1.00 52.10 ? 291 LYS   B CA  1 
ATOM   3110 C  C   . LYS   B 1 200 ? 174.453 -61.683 8.967  1.00 58.85 ? 291 LYS   B C   1 
ATOM   3111 O  O   . LYS   B 1 200 ? 175.362 -61.532 8.145  1.00 62.43 ? 291 LYS   B O   1 
ATOM   3112 C  CB  . LYS   B 1 200 ? 172.619 -60.966 7.421  1.00 49.72 ? 291 LYS   B CB  1 
ATOM   3113 N  N   . LYS   B 1 201 ? 174.665 -61.585 10.276 1.00 60.81 ? 292 LYS   B N   1 
ATOM   3114 C  CA  . LYS   B 1 201 ? 175.986 -61.245 10.806 1.00 61.76 ? 292 LYS   B CA  1 
ATOM   3115 C  C   . LYS   B 1 201 ? 176.764 -62.484 11.250 1.00 65.36 ? 292 LYS   B C   1 
ATOM   3116 O  O   . LYS   B 1 201 ? 176.219 -63.587 11.322 1.00 68.79 ? 292 LYS   B O   1 
ATOM   3117 C  CB  . LYS   B 1 201 ? 175.859 -60.262 11.976 1.00 55.34 ? 292 LYS   B CB  1 
HETATM 3118 C  C10 . A1ARO C 2 .   ? 125.875 -63.709 47.467 1.00 14.21 ? 401 A1ARO A C10 1 
HETATM 3119 C  C11 . A1ARO C 2 .   ? 125.656 -64.771 46.462 1.00 12.91 ? 401 A1ARO A C11 1 
HETATM 3120 C  C15 . A1ARO C 2 .   ? 125.139 -68.688 43.704 1.00 13.74 ? 401 A1ARO A C15 1 
HETATM 3121 C  C16 . A1ARO C 2 .   ? 124.939 -70.042 43.396 1.00 14.50 ? 401 A1ARO A C16 1 
HETATM 3122 C  C18 . A1ARO C 2 .   ? 124.914 -72.392 44.278 1.00 17.23 ? 401 A1ARO A C18 1 
HETATM 3123 C  C19 . A1ARO C 2 .   ? 124.231 -73.101 45.464 1.00 21.53 ? 401 A1ARO A C19 1 
HETATM 3124 C  C20 . A1ARO C 2 .   ? 124.387 -74.635 45.316 1.00 22.33 ? 401 A1ARO A C20 1 
HETATM 3125 C  C22 . A1ARO C 2 .   ? 125.979 -76.523 45.133 1.00 30.78 ? 401 A1ARO A C22 1 
HETATM 3126 C  C23 . A1ARO C 2 .   ? 126.470 -74.353 44.056 1.00 28.16 ? 401 A1ARO A C23 1 
HETATM 3127 C  C01 . A1ARO C 2 .   ? 121.280 -61.403 49.642 1.00 25.22 ? 401 A1ARO A C01 1 
HETATM 3128 C  C03 . A1ARO C 2 .   ? 122.671 -63.404 49.508 1.00 16.34 ? 401 A1ARO A C03 1 
HETATM 3129 C  C04 . A1ARO C 2 .   ? 121.957 -64.072 50.460 1.00 14.73 ? 401 A1ARO A C04 1 
HETATM 3130 C  C05 . A1ARO C 2 .   ? 122.401 -65.278 50.940 1.00 20.55 ? 401 A1ARO A C05 1 
HETATM 3131 C  C06 . A1ARO C 2 .   ? 123.564 -65.843 50.486 1.00 11.22 ? 401 A1ARO A C06 1 
HETATM 3132 C  C07 . A1ARO C 2 .   ? 124.298 -65.162 49.520 1.00 13.05 ? 401 A1ARO A C07 1 
HETATM 3133 C  C08 . A1ARO C 2 .   ? 123.870 -63.929 49.015 1.00 14.96 ? 401 A1ARO A C08 1 
HETATM 3134 C  C12 . A1ARO C 2 .   ? 125.520 -65.637 45.654 1.00 13.88 ? 401 A1ARO A C12 1 
HETATM 3135 C  C13 . A1ARO C 2 .   ? 125.384 -66.689 44.705 1.00 11.07 ? 401 A1ARO A C13 1 
HETATM 3136 C  C14 . A1ARO C 2 .   ? 125.194 -67.998 44.958 1.00 16.01 ? 401 A1ARO A C14 1 
HETATM 3137 C  C24 . A1ARO C 2 .   ? 126.387 -72.819 44.208 1.00 20.30 ? 401 A1ARO A C24 1 
HETATM 3138 C  C25 . A1ARO C 2 .   ? 124.959 -70.384 42.052 1.00 14.29 ? 401 A1ARO A C25 1 
HETATM 3139 C  C26 . A1ARO C 2 .   ? 125.145 -69.409 41.052 1.00 14.41 ? 401 A1ARO A C26 1 
HETATM 3140 C  C27 . A1ARO C 2 .   ? 125.330 -68.079 41.340 1.00 12.88 ? 401 A1ARO A C27 1 
HETATM 3141 C  C28 . A1ARO C 2 .   ? 125.329 -67.734 42.696 1.00 11.56 ? 401 A1ARO A C28 1 
HETATM 3142 C  C30 . A1ARO C 2 .   ? 125.712 -65.242 42.640 1.00 11.78 ? 401 A1ARO A C30 1 
HETATM 3143 C  C31 . A1ARO C 2 .   ? 127.152 -65.031 42.247 1.00 15.60 ? 401 A1ARO A C31 1 
HETATM 3144 C  C36 . A1ARO C 2 .   ? 119.786 -66.294 51.346 1.00 27.26 ? 401 A1ARO A C36 1 
HETATM 3145 F  F32 . A1ARO C 2 .   ? 127.982 -65.086 43.302 1.00 18.37 ? 401 A1ARO A F32 1 
HETATM 3146 F  F33 . A1ARO C 2 .   ? 127.537 -66.003 41.393 1.00 15.93 ? 401 A1ARO A F33 1 
HETATM 3147 F  F34 . A1ARO C 2 .   ? 127.341 -63.857 41.632 1.00 15.14 ? 401 A1ARO A F34 1 
HETATM 3148 N  N09 . A1ARO C 2 .   ? 124.604 -63.303 48.052 1.00 17.49 ? 401 A1ARO A N09 1 
HETATM 3149 N  N17 . A1ARO C 2 .   ? 124.766 -70.949 44.414 1.00 13.85 ? 401 A1ARO A N17 1 
HETATM 3150 N  N21 . A1ARO C 2 .   ? 125.784 -75.072 45.145 1.00 27.82 ? 401 A1ARO A N21 1 
HETATM 3151 N  N29 . A1ARO C 2 .   ? 125.492 -66.509 43.309 1.00 13.40 ? 401 A1ARO A N29 1 
HETATM 3152 O  O02 . A1ARO C 2 .   ? 122.285 -62.188 48.983 1.00 20.33 ? 401 A1ARO A O02 1 
HETATM 3153 O  O37 . A1ARO C 2 .   ? 121.204 -65.101 53.390 1.00 37.22 ? 401 A1ARO A O37 1 
HETATM 3154 O  O38 . A1ARO C 2 .   ? 121.990 -67.551 52.412 1.00 28.31 ? 401 A1ARO A O38 1 
HETATM 3155 S  S35 . A1ARO C 2 .   ? 121.402 -66.107 52.177 1.00 26.46 ? 401 A1ARO A S35 1 
HETATM 3156 ZN ZN  . ZN    D 3 .   ? 127.944 -43.160 20.792 1.00 12.14 ? 402 ZN    A ZN  1 
HETATM 3157 C  C10 . A1ARO E 2 .   ? 157.844 -54.942 47.535 1.00 13.45 ? 401 A1ARO B C10 1 
HETATM 3158 C  C11 . A1ARO E 2 .   ? 157.570 -56.001 46.545 1.00 17.81 ? 401 A1ARO B C11 1 
HETATM 3159 C  C15 . A1ARO E 2 .   ? 156.821 -59.925 43.854 1.00 14.01 ? 401 A1ARO B C15 1 
HETATM 3160 C  C16 . A1ARO E 2 .   ? 156.549 -61.271 43.575 1.00 14.48 ? 401 A1ARO B C16 1 
HETATM 3161 C  C18 . A1ARO E 2 .   ? 156.293 -63.591 44.527 1.00 19.09 ? 401 A1ARO B C18 1 
HETATM 3162 C  C19 . A1ARO E 2 .   ? 155.644 -64.164 45.802 1.00 15.85 ? 401 A1ARO B C19 1 
HETATM 3163 C  C20 . A1ARO E 2 .   ? 155.635 -65.704 45.750 1.00 17.45 ? 401 A1ARO B C20 1 
HETATM 3164 C  C22 . A1ARO E 2 .   ? 157.026 -67.746 45.596 1.00 28.92 ? 401 A1ARO B C22 1 
HETATM 3165 C  C23 . A1ARO E 2 .   ? 157.593 -65.721 44.303 1.00 21.26 ? 401 A1ARO B C23 1 
HETATM 3166 C  C01 . A1ARO E 2 .   ? 153.175 -52.540 49.526 1.00 28.22 ? 401 A1ARO B C01 1 
HETATM 3167 C  C03 . A1ARO E 2 .   ? 154.654 -54.484 49.586 1.00 19.46 ? 401 A1ARO B C03 1 
HETATM 3168 C  C04 . A1ARO E 2 .   ? 153.916 -55.111 50.547 1.00 16.26 ? 401 A1ARO B C04 1 
HETATM 3169 C  C05 . A1ARO E 2 .   ? 154.310 -56.328 51.036 1.00 20.89 ? 401 A1ARO B C05 1 
HETATM 3170 C  C06 . A1ARO E 2 .   ? 155.457 -56.936 50.596 1.00 17.73 ? 401 A1ARO B C06 1 
HETATM 3171 C  C07 . A1ARO E 2 .   ? 156.211 -56.297 49.624 1.00 12.52 ? 401 A1ARO B C07 1 
HETATM 3172 C  C08 . A1ARO E 2 .   ? 155.835 -55.060 49.103 1.00 15.34 ? 401 A1ARO B C08 1 
HETATM 3173 C  C12 . A1ARO E 2 .   ? 157.383 -56.874 45.748 1.00 15.29 ? 401 A1ARO B C12 1 
HETATM 3174 C  C13 . A1ARO E 2 .   ? 157.181 -57.928 44.820 1.00 12.80 ? 401 A1ARO B C13 1 
HETATM 3175 C  C14 . A1ARO E 2 .   ? 156.914 -59.217 45.094 1.00 12.03 ? 401 A1ARO B C14 1 
HETATM 3176 C  C24 . A1ARO E 2 .   ? 157.693 -64.189 44.357 1.00 15.56 ? 401 A1ARO B C24 1 
HETATM 3177 C  C25 . A1ARO E 2 .   ? 156.531 -61.638 42.234 1.00 17.63 ? 401 A1ARO B C25 1 
HETATM 3178 C  C26 . A1ARO E 2 .   ? 156.774 -60.698 41.222 1.00 14.83 ? 401 A1ARO B C26 1 
HETATM 3179 C  C27 . A1ARO E 2 .   ? 157.036 -59.374 41.488 1.00 14.89 ? 401 A1ARO B C27 1 
HETATM 3180 C  C28 . A1ARO E 2 .   ? 157.054 -59.006 42.833 1.00 12.45 ? 401 A1ARO B C28 1 
HETATM 3181 C  C30 . A1ARO E 2 .   ? 157.568 -56.546 42.722 1.00 12.09 ? 401 A1ARO B C30 1 
HETATM 3182 C  C31 . A1ARO E 2 .   ? 159.015 -56.381 42.354 1.00 15.32 ? 401 A1ARO B C31 1 
HETATM 3183 C  C36 . A1ARO E 2 .   ? 151.590 -56.818 51.710 1.00 29.90 ? 401 A1ARO B C36 1 
HETATM 3184 F  F32 . A1ARO E 2 .   ? 159.815 -56.407 43.436 1.00 18.68 ? 401 A1ARO B F32 1 
HETATM 3185 F  F33 . A1ARO E 2 .   ? 159.407 -57.391 41.536 1.00 14.00 ? 401 A1ARO B F33 1 
HETATM 3186 F  F34 . A1ARO E 2 .   ? 159.233 -55.240 41.701 1.00 14.32 ? 401 A1ARO B F34 1 
HETATM 3187 N  N09 . A1ARO E 2 .   ? 156.594 -54.480 48.129 1.00 15.04 ? 401 A1ARO B N09 1 
HETATM 3188 N  N17 . A1ARO E 2 .   ? 156.319 -62.134 44.613 1.00 15.84 ? 401 A1ARO B N17 1 
HETATM 3189 N  N21 . A1ARO E 2 .   ? 156.961 -66.285 45.500 1.00 22.03 ? 401 A1ARO B N21 1 
HETATM 3190 N  N29 . A1ARO E 2 .   ? 157.290 -57.779 43.421 1.00 13.59 ? 401 A1ARO B N29 1 
HETATM 3191 O  O02 . A1ARO E 2 .   ? 154.311 -53.274 49.038 1.00 22.58 ? 401 A1ARO B O02 1 
HETATM 3192 O  O37 . A1ARO E 2 .   ? 153.486 -56.209 53.623 1.00 35.85 ? 401 A1ARO B O37 1 
HETATM 3193 O  O38 . A1ARO E 2 .   ? 153.575 -58.634 52.321 1.00 24.61 ? 401 A1ARO B O38 1 
HETATM 3194 S  S35 . A1ARO E 2 .   ? 153.296 -57.085 52.308 1.00 25.61 ? 401 A1ARO B S35 1 
HETATM 3195 ZN ZN  . ZN    F 3 .   ? 161.682 -35.173 20.260 1.00 12.33 ? 402 ZN    B ZN  1 
HETATM 3196 O  O   . HOH   G 4 .   ? 136.645 -54.782 41.366 1.00 28.08 ? 501 HOH   A O   1 
HETATM 3197 O  O   . HOH   G 4 .   ? 148.081 -52.900 19.365 1.00 30.34 ? 502 HOH   A O   1 
HETATM 3198 O  O   . HOH   G 4 .   ? 141.355 -70.019 13.165 1.00 41.27 ? 503 HOH   A O   1 
HETATM 3199 O  O   . HOH   G 4 .   ? 135.010 -73.933 39.159 1.00 28.73 ? 504 HOH   A O   1 
HETATM 3200 O  O   . HOH   G 4 .   ? 136.793 -61.177 15.656 1.00 31.62 ? 505 HOH   A O   1 
HETATM 3201 O  O   . HOH   G 4 .   ? 117.160 -38.576 25.616 1.00 35.65 ? 506 HOH   A O   1 
HETATM 3202 O  O   . HOH   G 4 .   ? 133.594 -52.402 53.913 1.00 13.79 ? 507 HOH   A O   1 
HETATM 3203 O  O   . HOH   G 4 .   ? 118.307 -58.582 23.848 1.00 29.94 ? 508 HOH   A O   1 
HETATM 3204 O  O   . HOH   G 4 .   ? 117.103 -35.905 30.807 1.00 36.59 ? 509 HOH   A O   1 
HETATM 3205 O  O   . HOH   G 4 .   ? 129.066 -47.545 44.591 1.00 30.19 ? 510 HOH   A O   1 
HETATM 3206 O  O   . HOH   G 4 .   ? 140.709 -48.683 28.378 1.00 10.80 ? 511 HOH   A O   1 
HETATM 3207 O  O   . HOH   G 4 .   ? 119.634 -43.184 23.731 1.00 27.05 ? 512 HOH   A O   1 
HETATM 3208 O  O   . HOH   G 4 .   ? 129.617 -76.889 43.846 1.00 23.76 ? 513 HOH   A O   1 
HETATM 3209 O  O   . HOH   G 4 .   ? 117.483 -62.942 30.563 1.00 41.17 ? 514 HOH   A O   1 
HETATM 3210 O  O   . HOH   G 4 .   ? 114.647 -54.291 27.603 1.00 38.27 ? 515 HOH   A O   1 
HETATM 3211 O  O   . HOH   G 4 .   ? 132.127 -37.644 38.733 1.00 31.45 ? 516 HOH   A O   1 
HETATM 3212 O  O   . HOH   G 4 .   ? 136.905 -60.569 11.515 1.00 32.67 ? 517 HOH   A O   1 
HETATM 3213 O  O   . HOH   G 4 .   ? 139.123 -62.567 28.310 1.00 33.85 ? 518 HOH   A O   1 
HETATM 3214 O  O   . HOH   G 4 .   ? 120.851 -48.260 35.845 1.00 15.35 ? 519 HOH   A O   1 
HETATM 3215 O  O   . HOH   G 4 .   ? 135.431 -64.697 51.121 1.00 29.02 ? 520 HOH   A O   1 
HETATM 3216 O  O   . HOH   G 4 .   ? 130.863 -34.065 24.035 1.00 16.24 ? 521 HOH   A O   1 
HETATM 3217 O  O   . HOH   G 4 .   ? 129.517 -70.923 50.789 1.00 30.64 ? 522 HOH   A O   1 
HETATM 3218 O  O   . HOH   G 4 .   ? 132.700 -45.170 12.706 1.00 28.88 ? 523 HOH   A O   1 
HETATM 3219 O  O   . HOH   G 4 .   ? 124.765 -66.755 22.322 1.00 17.51 ? 524 HOH   A O   1 
HETATM 3220 O  O   . HOH   G 4 .   ? 151.092 -49.960 23.305 1.00 17.75 ? 525 HOH   A O   1 
HETATM 3221 O  O   . HOH   G 4 .   ? 129.846 -38.334 35.951 1.00 18.56 ? 526 HOH   A O   1 
HETATM 3222 O  O   . HOH   G 4 .   ? 137.732 -47.741 30.918 1.00 9.31  ? 527 HOH   A O   1 
HETATM 3223 O  O   . HOH   G 4 .   ? 120.312 -66.578 32.064 1.00 26.43 ? 528 HOH   A O   1 
HETATM 3224 O  O   . HOH   G 4 .   ? 121.265 -59.741 14.619 1.00 24.79 ? 529 HOH   A O   1 
HETATM 3225 O  O   . HOH   G 4 .   ? 114.655 -57.299 27.208 1.00 34.05 ? 530 HOH   A O   1 
HETATM 3226 O  O   . HOH   G 4 .   ? 120.172 -78.195 39.330 1.00 34.11 ? 531 HOH   A O   1 
HETATM 3227 O  O   . HOH   G 4 .   ? 131.627 -39.616 27.737 1.00 10.39 ? 532 HOH   A O   1 
HETATM 3228 O  O   . HOH   G 4 .   ? 138.309 -44.968 14.106 1.00 34.22 ? 533 HOH   A O   1 
HETATM 3229 O  O   . HOH   G 4 .   ? 122.720 -39.175 27.704 1.00 25.52 ? 534 HOH   A O   1 
HETATM 3230 O  O   . HOH   G 4 .   ? 132.556 -67.842 52.639 1.00 31.94 ? 535 HOH   A O   1 
HETATM 3231 O  O   . HOH   G 4 .   ? 139.508 -62.215 32.551 1.00 12.54 ? 536 HOH   A O   1 
HETATM 3232 O  O   . HOH   G 4 .   ? 125.083 -70.754 29.660 1.00 13.62 ? 537 HOH   A O   1 
HETATM 3233 O  O   . HOH   G 4 .   ? 129.979 -39.458 17.674 1.00 17.17 ? 538 HOH   A O   1 
HETATM 3234 O  O   . HOH   G 4 .   ? 120.589 -46.894 16.316 1.00 46.86 ? 539 HOH   A O   1 
HETATM 3235 O  O   . HOH   G 4 .   ? 125.137 -43.914 30.484 1.00 7.66  ? 540 HOH   A O   1 
HETATM 3236 O  O   . HOH   G 4 .   ? 119.539 -49.429 31.233 1.00 28.22 ? 541 HOH   A O   1 
HETATM 3237 O  O   . HOH   G 4 .   ? 119.227 -66.617 16.502 1.00 15.63 ? 542 HOH   A O   1 
HETATM 3238 O  O   . HOH   G 4 .   ? 144.362 -44.243 23.172 1.00 24.59 ? 543 HOH   A O   1 
HETATM 3239 O  O   . HOH   G 4 .   ? 132.832 -69.715 31.877 1.00 12.14 ? 544 HOH   A O   1 
HETATM 3240 O  O   . HOH   G 4 .   ? 136.616 -66.677 36.134 1.00 9.98  ? 545 HOH   A O   1 
HETATM 3241 O  O   . HOH   G 4 .   ? 125.037 -59.562 48.060 1.00 19.02 ? 546 HOH   A O   1 
HETATM 3242 O  O   . HOH   G 4 .   ? 134.459 -73.128 45.741 1.00 24.68 ? 547 HOH   A O   1 
HETATM 3243 O  O   . HOH   G 4 .   ? 129.677 -75.623 39.502 1.00 18.93 ? 548 HOH   A O   1 
HETATM 3244 O  O   . HOH   G 4 .   ? 116.347 -50.563 34.008 1.00 38.41 ? 549 HOH   A O   1 
HETATM 3245 O  O   . HOH   G 4 .   ? 121.046 -57.306 42.872 1.00 18.80 ? 550 HOH   A O   1 
HETATM 3246 O  O   . HOH   G 4 .   ? 137.765 -73.012 47.111 1.00 40.86 ? 551 HOH   A O   1 
HETATM 3247 O  O   . HOH   G 4 .   ? 137.534 -48.120 39.412 1.00 14.99 ? 552 HOH   A O   1 
HETATM 3248 O  O   . HOH   G 4 .   ? 136.707 -43.749 25.182 1.00 9.04  ? 553 HOH   A O   1 
HETATM 3249 O  O   . HOH   G 4 .   ? 118.664 -66.729 23.848 1.00 37.05 ? 554 HOH   A O   1 
HETATM 3250 O  O   . HOH   G 4 .   ? 123.207 -36.193 28.312 1.00 14.71 ? 555 HOH   A O   1 
HETATM 3251 O  O   . HOH   G 4 .   ? 128.910 -44.548 43.245 1.00 31.74 ? 556 HOH   A O   1 
HETATM 3252 O  O   . HOH   G 4 .   ? 133.555 -48.902 32.005 1.00 5.99  ? 557 HOH   A O   1 
HETATM 3253 O  O   . HOH   G 4 .   ? 121.411 -75.468 34.608 1.00 29.92 ? 558 HOH   A O   1 
HETATM 3254 O  O   . HOH   G 4 .   ? 121.269 -51.258 17.409 1.00 21.47 ? 559 HOH   A O   1 
HETATM 3255 O  O   . HOH   G 4 .   ? 135.097 -47.318 38.145 1.00 9.68  ? 560 HOH   A O   1 
HETATM 3256 O  O   . HOH   G 4 .   ? 134.887 -55.437 19.534 1.00 24.39 ? 561 HOH   A O   1 
HETATM 3257 O  O   . HOH   G 4 .   ? 123.375 -71.002 48.772 1.00 35.52 ? 562 HOH   A O   1 
HETATM 3258 O  O   . HOH   G 4 .   ? 125.547 -50.202 48.553 1.00 15.31 ? 563 HOH   A O   1 
HETATM 3259 O  O   . HOH   G 4 .   ? 135.638 -66.584 43.811 1.00 10.56 ? 564 HOH   A O   1 
HETATM 3260 O  O   . HOH   G 4 .   ? 147.419 -47.851 26.406 1.00 18.06 ? 565 HOH   A O   1 
HETATM 3261 O  O   . HOH   G 4 .   ? 132.129 -45.793 30.295 1.00 9.60  ? 566 HOH   A O   1 
HETATM 3262 O  O   . HOH   G 4 .   ? 134.112 -51.628 20.820 1.00 18.16 ? 567 HOH   A O   1 
HETATM 3263 O  O   . HOH   G 4 .   ? 132.689 -51.537 46.922 1.00 26.11 ? 568 HOH   A O   1 
HETATM 3264 O  O   . HOH   G 4 .   ? 143.864 -67.177 34.629 1.00 25.43 ? 569 HOH   A O   1 
HETATM 3265 O  O   . HOH   G 4 .   ? 124.210 -42.487 40.179 1.00 23.03 ? 570 HOH   A O   1 
HETATM 3266 O  O   . HOH   G 4 .   ? 146.101 -45.118 25.677 1.00 16.65 ? 571 HOH   A O   1 
HETATM 3267 O  O   . HOH   G 4 .   ? 133.420 -38.867 24.261 1.00 28.49 ? 572 HOH   A O   1 
HETATM 3268 O  O   . HOH   G 4 .   ? 131.723 -69.987 18.764 1.00 13.74 ? 573 HOH   A O   1 
HETATM 3269 O  O   . HOH   G 4 .   ? 120.037 -33.717 24.664 1.00 37.41 ? 574 HOH   A O   1 
HETATM 3270 O  O   . HOH   G 4 .   ? 127.736 -55.109 37.439 1.00 8.76  ? 575 HOH   A O   1 
HETATM 3271 O  O   . HOH   G 4 .   ? 141.316 -51.465 21.494 1.00 11.53 ? 576 HOH   A O   1 
HETATM 3272 O  O   . HOH   G 4 .   ? 135.359 -46.627 31.701 1.00 10.59 ? 577 HOH   A O   1 
HETATM 3273 O  O   . HOH   G 4 .   ? 117.972 -76.553 36.551 1.00 45.67 ? 578 HOH   A O   1 
HETATM 3274 O  O   . HOH   G 4 .   ? 152.064 -54.224 24.328 1.00 17.08 ? 579 HOH   A O   1 
HETATM 3275 O  O   . HOH   G 4 .   ? 124.523 -34.725 19.481 1.00 12.90 ? 580 HOH   A O   1 
HETATM 3276 O  O   . HOH   G 4 .   ? 117.609 -66.602 20.108 1.00 29.77 ? 581 HOH   A O   1 
HETATM 3277 O  O   . HOH   G 4 .   ? 131.909 -54.197 46.482 1.00 9.55  ? 582 HOH   A O   1 
HETATM 3278 O  O   . HOH   G 4 .   ? 119.845 -56.926 35.711 1.00 12.16 ? 583 HOH   A O   1 
HETATM 3279 O  O   . HOH   G 4 .   ? 123.884 -64.353 26.944 1.00 14.90 ? 584 HOH   A O   1 
HETATM 3280 O  O   . HOH   G 4 .   ? 119.208 -50.713 19.177 1.00 19.04 ? 585 HOH   A O   1 
HETATM 3281 O  O   . HOH   G 4 .   ? 119.528 -62.886 22.287 1.00 36.01 ? 586 HOH   A O   1 
HETATM 3282 O  O   . HOH   G 4 .   ? 123.242 -53.367 24.680 1.00 11.41 ? 587 HOH   A O   1 
HETATM 3283 O  O   . HOH   G 4 .   ? 123.098 -69.740 51.169 1.00 44.08 ? 588 HOH   A O   1 
HETATM 3284 O  O   . HOH   G 4 .   ? 139.756 -47.983 37.830 1.00 13.51 ? 589 HOH   A O   1 
HETATM 3285 O  O   . HOH   G 4 .   ? 142.782 -54.496 38.812 1.00 35.93 ? 590 HOH   A O   1 
HETATM 3286 O  O   . HOH   G 4 .   ? 141.484 -60.296 47.293 1.00 34.47 ? 591 HOH   A O   1 
HETATM 3287 O  O   . HOH   G 4 .   ? 124.854 -74.020 40.225 1.00 20.70 ? 592 HOH   A O   1 
HETATM 3288 O  O   . HOH   G 4 .   ? 132.682 -33.797 27.382 1.00 11.89 ? 593 HOH   A O   1 
HETATM 3289 O  O   . HOH   G 4 .   ? 138.153 -72.356 42.899 1.00 34.76 ? 594 HOH   A O   1 
HETATM 3290 O  O   . HOH   G 4 .   ? 129.417 -58.930 9.093  1.00 31.22 ? 595 HOH   A O   1 
HETATM 3291 O  O   . HOH   G 4 .   ? 127.416 -74.419 40.650 1.00 19.32 ? 596 HOH   A O   1 
HETATM 3292 O  O   . HOH   G 4 .   ? 119.446 -66.819 35.931 1.00 24.65 ? 597 HOH   A O   1 
HETATM 3293 O  O   . HOH   G 4 .   ? 148.133 -48.679 39.714 1.00 44.15 ? 598 HOH   A O   1 
HETATM 3294 O  O   . HOH   G 4 .   ? 139.840 -55.444 37.068 1.00 16.52 ? 599 HOH   A O   1 
HETATM 3295 O  O   . HOH   G 4 .   ? 138.845 -39.499 30.454 1.00 29.47 ? 600 HOH   A O   1 
HETATM 3296 O  O   . HOH   G 4 .   ? 126.731 -69.027 22.455 1.00 10.85 ? 601 HOH   A O   1 
HETATM 3297 O  O   . HOH   G 4 .   ? 117.824 -55.228 43.397 1.00 30.66 ? 602 HOH   A O   1 
HETATM 3298 O  O   . HOH   G 4 .   ? 138.468 -41.230 27.731 1.00 17.69 ? 603 HOH   A O   1 
HETATM 3299 O  O   . HOH   G 4 .   ? 130.977 -40.049 34.204 1.00 12.32 ? 604 HOH   A O   1 
HETATM 3300 O  O   . HOH   G 4 .   ? 118.691 -64.799 9.634  1.00 40.90 ? 605 HOH   A O   1 
HETATM 3301 O  O   . HOH   G 4 .   ? 118.824 -50.735 36.617 1.00 22.93 ? 606 HOH   A O   1 
HETATM 3302 O  O   . HOH   G 4 .   ? 116.997 -44.031 28.273 1.00 17.08 ? 607 HOH   A O   1 
HETATM 3303 O  O   . HOH   G 4 .   ? 121.037 -47.542 43.315 1.00 25.25 ? 608 HOH   A O   1 
HETATM 3304 O  O   . HOH   G 4 .   ? 126.173 -54.794 12.328 1.00 25.62 ? 609 HOH   A O   1 
HETATM 3305 O  O   . HOH   G 4 .   ? 132.590 -50.784 49.482 1.00 18.19 ? 610 HOH   A O   1 
HETATM 3306 O  O   . HOH   G 4 .   ? 133.373 -76.334 38.636 1.00 38.66 ? 611 HOH   A O   1 
HETATM 3307 O  O   . HOH   G 4 .   ? 137.566 -66.965 31.165 1.00 27.93 ? 612 HOH   A O   1 
HETATM 3308 O  O   . HOH   G 4 .   ? 122.218 -68.238 11.222 1.00 36.73 ? 613 HOH   A O   1 
HETATM 3309 O  O   . HOH   G 4 .   ? 129.581 -50.755 15.574 1.00 16.00 ? 614 HOH   A O   1 
HETATM 3310 O  O   . HOH   G 4 .   ? 116.092 -44.713 38.006 1.00 39.15 ? 615 HOH   A O   1 
HETATM 3311 O  O   . HOH   G 4 .   ? 143.738 -54.292 27.284 1.00 23.11 ? 616 HOH   A O   1 
HETATM 3312 O  O   . HOH   G 4 .   ? 115.593 -60.095 21.443 1.00 50.23 ? 617 HOH   A O   1 
HETATM 3313 O  O   . HOH   G 4 .   ? 138.453 -65.538 46.098 1.00 20.10 ? 618 HOH   A O   1 
HETATM 3314 O  O   A HOH   G 4 .   ? 128.586 -44.884 14.284 0.56 16.65 ? 619 HOH   A O   1 
HETATM 3315 O  O   B HOH   G 4 .   ? 126.526 -44.686 14.620 0.44 19.48 ? 619 HOH   A O   1 
HETATM 3316 O  O   . HOH   G 4 .   ? 129.696 -72.291 34.432 1.00 20.18 ? 620 HOH   A O   1 
HETATM 3317 O  O   . HOH   G 4 .   ? 144.506 -65.585 38.105 1.00 26.06 ? 621 HOH   A O   1 
HETATM 3318 O  O   . HOH   G 4 .   ? 149.413 -45.601 24.139 1.00 14.97 ? 622 HOH   A O   1 
HETATM 3319 O  O   . HOH   G 4 .   ? 135.688 -73.990 43.502 1.00 24.61 ? 623 HOH   A O   1 
HETATM 3320 O  O   . HOH   G 4 .   ? 132.412 -57.604 12.356 1.00 38.64 ? 624 HOH   A O   1 
HETATM 3321 O  O   . HOH   G 4 .   ? 129.413 -48.087 33.835 1.00 6.80  ? 625 HOH   A O   1 
HETATM 3322 O  O   . HOH   G 4 .   ? 145.743 -57.729 33.247 1.00 31.45 ? 626 HOH   A O   1 
HETATM 3323 O  O   . HOH   G 4 .   ? 127.943 -41.873 39.906 1.00 30.61 ? 627 HOH   A O   1 
HETATM 3324 O  O   . HOH   G 4 .   ? 139.325 -63.176 25.598 1.00 30.84 ? 628 HOH   A O   1 
HETATM 3325 O  O   . HOH   G 4 .   ? 123.173 -62.435 41.502 1.00 25.20 ? 629 HOH   A O   1 
HETATM 3326 O  O   . HOH   G 4 .   ? 141.500 -69.033 41.313 1.00 18.29 ? 630 HOH   A O   1 
HETATM 3327 O  O   . HOH   G 4 .   ? 135.446 -40.055 33.792 1.00 20.08 ? 631 HOH   A O   1 
HETATM 3328 O  O   . HOH   G 4 .   ? 141.246 -50.498 16.510 1.00 35.64 ? 632 HOH   A O   1 
HETATM 3329 O  O   . HOH   G 4 .   ? 118.948 -47.182 30.287 1.00 21.80 ? 633 HOH   A O   1 
HETATM 3330 O  O   . HOH   G 4 .   ? 129.385 -52.804 49.062 1.00 10.59 ? 634 HOH   A O   1 
HETATM 3331 O  O   . HOH   G 4 .   ? 130.040 -68.478 10.694 1.00 36.19 ? 635 HOH   A O   1 
HETATM 3332 O  O   . HOH   G 4 .   ? 137.565 -63.110 13.526 1.00 35.77 ? 636 HOH   A O   1 
HETATM 3333 O  O   . HOH   G 4 .   ? 144.164 -48.094 16.597 1.00 31.48 ? 637 HOH   A O   1 
HETATM 3334 O  O   . HOH   G 4 .   ? 132.638 -35.572 31.791 1.00 15.60 ? 638 HOH   A O   1 
HETATM 3335 O  O   . HOH   G 4 .   ? 137.970 -62.228 19.718 1.00 38.51 ? 639 HOH   A O   1 
HETATM 3336 O  O   . HOH   G 4 .   ? 131.729 -44.809 22.811 1.00 13.47 ? 640 HOH   A O   1 
HETATM 3337 O  O   . HOH   G 4 .   ? 118.122 -67.237 39.119 1.00 26.71 ? 641 HOH   A O   1 
HETATM 3338 O  O   . HOH   G 4 .   ? 117.340 -38.371 32.785 1.00 26.55 ? 642 HOH   A O   1 
HETATM 3339 O  O   . HOH   G 4 .   ? 126.210 -69.357 13.389 1.00 33.79 ? 643 HOH   A O   1 
HETATM 3340 O  O   . HOH   G 4 .   ? 131.557 -48.650 43.518 1.00 14.14 ? 644 HOH   A O   1 
HETATM 3341 O  O   . HOH   G 4 .   ? 129.867 -42.095 14.908 1.00 19.56 ? 645 HOH   A O   1 
HETATM 3342 O  O   . HOH   G 4 .   ? 138.178 -55.946 43.376 1.00 30.00 ? 646 HOH   A O   1 
HETATM 3343 O  O   . HOH   G 4 .   ? 119.103 -63.920 38.243 1.00 18.96 ? 647 HOH   A O   1 
HETATM 3344 O  O   . HOH   G 4 .   ? 122.668 -63.817 24.352 1.00 17.28 ? 648 HOH   A O   1 
HETATM 3345 O  O   . HOH   G 4 .   ? 120.978 -57.163 38.245 1.00 21.98 ? 649 HOH   A O   1 
HETATM 3346 O  O   . HOH   G 4 .   ? 131.141 -41.777 41.342 1.00 18.09 ? 650 HOH   A O   1 
HETATM 3347 O  O   . HOH   G 4 .   ? 121.308 -69.548 14.650 1.00 25.20 ? 651 HOH   A O   1 
HETATM 3348 O  O   . HOH   G 4 .   ? 135.790 -50.022 51.045 1.00 30.31 ? 652 HOH   A O   1 
HETATM 3349 O  O   . HOH   G 4 .   ? 143.696 -57.202 25.909 1.00 31.45 ? 653 HOH   A O   1 
HETATM 3350 O  O   . HOH   G 4 .   ? 119.671 -72.147 35.490 1.00 34.34 ? 654 HOH   A O   1 
HETATM 3351 O  O   . HOH   G 4 .   ? 138.437 -72.969 40.453 1.00 25.42 ? 655 HOH   A O   1 
HETATM 3352 O  O   . HOH   G 4 .   ? 130.199 -67.827 51.902 1.00 27.42 ? 656 HOH   A O   1 
HETATM 3353 O  O   . HOH   G 4 .   ? 128.795 -68.841 12.990 1.00 39.83 ? 657 HOH   A O   1 
HETATM 3354 O  O   . HOH   G 4 .   ? 129.352 -71.259 16.755 1.00 22.95 ? 658 HOH   A O   1 
HETATM 3355 O  O   . HOH   G 4 .   ? 147.448 -55.070 21.370 1.00 25.44 ? 659 HOH   A O   1 
HETATM 3356 O  O   . HOH   G 4 .   ? 120.922 -58.054 48.465 1.00 42.81 ? 660 HOH   A O   1 
HETATM 3357 O  O   . HOH   G 4 .   ? 123.401 -60.024 40.822 1.00 25.41 ? 661 HOH   A O   1 
HETATM 3358 O  O   . HOH   G 4 .   ? 127.502 -36.813 34.662 1.00 17.34 ? 662 HOH   A O   1 
HETATM 3359 O  O   . HOH   G 4 .   ? 123.136 -35.534 21.617 1.00 23.31 ? 663 HOH   A O   1 
HETATM 3360 O  O   . HOH   G 4 .   ? 137.731 -41.506 20.186 1.00 22.73 ? 664 HOH   A O   1 
HETATM 3361 O  O   . HOH   G 4 .   ? 120.418 -70.825 25.714 1.00 30.63 ? 665 HOH   A O   1 
HETATM 3362 O  O   . HOH   G 4 .   ? 135.076 -55.025 36.951 1.00 8.52  ? 666 HOH   A O   1 
HETATM 3363 O  O   . HOH   G 4 .   ? 141.465 -56.731 46.000 1.00 25.40 ? 667 HOH   A O   1 
HETATM 3364 O  O   . HOH   G 4 .   ? 136.190 -52.037 44.095 1.00 27.23 ? 668 HOH   A O   1 
HETATM 3365 O  O   . HOH   G 4 .   ? 143.319 -64.179 31.688 1.00 21.93 ? 669 HOH   A O   1 
HETATM 3366 O  O   . HOH   G 4 .   ? 141.592 -68.903 38.001 1.00 19.70 ? 670 HOH   A O   1 
HETATM 3367 O  O   . HOH   G 4 .   ? 127.283 -48.779 13.312 1.00 37.13 ? 671 HOH   A O   1 
HETATM 3368 O  O   . HOH   G 4 .   ? 122.014 -71.848 27.276 1.00 39.51 ? 672 HOH   A O   1 
HETATM 3369 O  O   . HOH   G 4 .   ? 125.367 -52.094 44.550 1.00 15.62 ? 673 HOH   A O   1 
HETATM 3370 O  O   . HOH   G 4 .   ? 130.918 -48.124 31.474 1.00 7.89  ? 674 HOH   A O   1 
HETATM 3371 O  O   . HOH   G 4 .   ? 121.219 -59.862 38.920 1.00 27.93 ? 675 HOH   A O   1 
HETATM 3372 O  O   . HOH   G 4 .   ? 126.924 -51.642 13.106 1.00 33.41 ? 676 HOH   A O   1 
HETATM 3373 O  O   . HOH   G 4 .   ? 116.834 -50.910 28.932 1.00 36.12 ? 677 HOH   A O   1 
HETATM 3374 O  O   . HOH   G 4 .   ? 136.839 -43.580 43.691 1.00 24.77 ? 678 HOH   A O   1 
HETATM 3375 O  O   . HOH   G 4 .   ? 120.051 -52.572 15.422 1.00 28.61 ? 679 HOH   A O   1 
HETATM 3376 O  O   . HOH   G 4 .   ? 117.686 -58.856 36.318 1.00 44.59 ? 680 HOH   A O   1 
HETATM 3377 O  O   . HOH   G 4 .   ? 121.442 -43.714 18.701 1.00 28.15 ? 681 HOH   A O   1 
HETATM 3378 O  O   . HOH   G 4 .   ? 119.342 -72.365 22.928 1.00 51.78 ? 682 HOH   A O   1 
HETATM 3379 O  O   . HOH   G 4 .   ? 140.588 -63.844 46.735 1.00 36.53 ? 683 HOH   A O   1 
HETATM 3380 O  O   . HOH   G 4 .   ? 141.473 -41.352 29.258 1.00 16.63 ? 684 HOH   A O   1 
HETATM 3381 O  O   . HOH   G 4 .   ? 135.102 -73.963 36.555 1.00 36.36 ? 685 HOH   A O   1 
HETATM 3382 O  O   . HOH   G 4 .   ? 125.116 -44.450 41.554 1.00 12.82 ? 686 HOH   A O   1 
HETATM 3383 O  O   . HOH   G 4 .   ? 119.521 -56.313 45.983 1.00 41.03 ? 687 HOH   A O   1 
HETATM 3384 O  O   . HOH   G 4 .   ? 138.196 -65.215 49.068 1.00 41.31 ? 688 HOH   A O   1 
HETATM 3385 O  O   . HOH   G 4 .   ? 122.767 -75.192 41.515 1.00 32.19 ? 689 HOH   A O   1 
HETATM 3386 O  O   . HOH   G 4 .   ? 117.062 -61.791 20.111 1.00 35.74 ? 690 HOH   A O   1 
HETATM 3387 O  O   . HOH   G 4 .   ? 114.777 -53.403 40.316 1.00 32.96 ? 691 HOH   A O   1 
HETATM 3388 O  O   . HOH   G 4 .   ? 146.842 -55.795 24.553 1.00 46.05 ? 692 HOH   A O   1 
HETATM 3389 O  O   . HOH   G 4 .   ? 129.755 -76.073 47.355 1.00 40.39 ? 693 HOH   A O   1 
HETATM 3390 O  O   . HOH   G 4 .   ? 133.056 -38.942 32.807 1.00 14.04 ? 694 HOH   A O   1 
HETATM 3391 O  O   . HOH   G 4 .   ? 138.605 -51.513 48.070 1.00 41.68 ? 695 HOH   A O   1 
HETATM 3392 O  O   . HOH   G 4 .   ? 139.905 -67.148 30.243 1.00 42.50 ? 696 HOH   A O   1 
HETATM 3393 O  O   . HOH   G 4 .   ? 145.844 -43.169 37.249 1.00 32.52 ? 697 HOH   A O   1 
HETATM 3394 O  O   . HOH   G 4 .   ? 136.390 -37.319 21.945 1.00 55.84 ? 698 HOH   A O   1 
HETATM 3395 O  O   . HOH   G 4 .   ? 136.600 -41.522 23.981 1.00 25.58 ? 699 HOH   A O   1 
HETATM 3396 O  O   . HOH   G 4 .   ? 116.285 -47.660 36.100 1.00 33.35 ? 700 HOH   A O   1 
HETATM 3397 O  O   . HOH   G 4 .   ? 133.141 -50.828 14.585 1.00 22.59 ? 701 HOH   A O   1 
HETATM 3398 O  O   . HOH   G 4 .   ? 127.240 -73.332 48.608 1.00 23.53 ? 702 HOH   A O   1 
HETATM 3399 O  O   . HOH   G 4 .   ? 129.675 -48.133 47.172 1.00 30.57 ? 703 HOH   A O   1 
HETATM 3400 O  O   . HOH   G 4 .   ? 124.445 -70.086 19.803 1.00 9.85  ? 704 HOH   A O   1 
HETATM 3401 O  O   . HOH   G 4 .   ? 137.290 -46.030 43.857 1.00 35.87 ? 705 HOH   A O   1 
HETATM 3402 O  O   . HOH   G 4 .   ? 120.374 -40.833 19.519 1.00 30.24 ? 706 HOH   A O   1 
HETATM 3403 O  O   . HOH   G 4 .   ? 113.501 -54.044 32.389 1.00 28.08 ? 707 HOH   A O   1 
HETATM 3404 O  O   . HOH   G 4 .   ? 139.045 -70.396 34.295 1.00 25.16 ? 708 HOH   A O   1 
HETATM 3405 O  O   . HOH   G 4 .   ? 133.564 -41.377 43.560 1.00 36.40 ? 709 HOH   A O   1 
HETATM 3406 O  O   . HOH   G 4 .   ? 126.743 -67.393 52.341 1.00 41.28 ? 710 HOH   A O   1 
HETATM 3407 O  O   . HOH   G 4 .   ? 136.999 -68.693 34.411 1.00 16.79 ? 711 HOH   A O   1 
HETATM 3408 O  O   . HOH   G 4 .   ? 117.800 -48.494 21.119 1.00 47.21 ? 712 HOH   A O   1 
HETATM 3409 O  O   . HOH   G 4 .   ? 137.968 -60.923 17.890 1.00 38.46 ? 713 HOH   A O   1 
HETATM 3410 O  O   . HOH   G 4 .   ? 134.545 -55.119 16.999 1.00 39.17 ? 714 HOH   A O   1 
HETATM 3411 O  O   . HOH   G 4 .   ? 137.017 -49.639 47.507 1.00 39.45 ? 715 HOH   A O   1 
HETATM 3412 O  O   . HOH   G 4 .   ? 115.338 -56.541 33.406 1.00 40.32 ? 716 HOH   A O   1 
HETATM 3413 O  O   . HOH   G 4 .   ? 120.524 -43.191 20.927 1.00 28.05 ? 717 HOH   A O   1 
HETATM 3414 O  O   . HOH   G 4 .   ? 141.574 -64.248 29.441 1.00 36.12 ? 718 HOH   A O   1 
HETATM 3415 O  O   . HOH   G 4 .   ? 123.700 -57.824 52.246 1.00 27.40 ? 719 HOH   A O   1 
HETATM 3416 O  O   . HOH   G 4 .   ? 142.511 -59.392 25.178 1.00 37.94 ? 720 HOH   A O   1 
HETATM 3417 O  O   . HOH   G 4 .   ? 124.724 -66.728 54.463 1.00 34.96 ? 721 HOH   A O   1 
HETATM 3418 O  O   . HOH   G 4 .   ? 134.884 -50.534 45.865 1.00 21.74 ? 722 HOH   A O   1 
HETATM 3419 O  O   . HOH   G 4 .   ? 128.378 -50.278 49.246 1.00 15.22 ? 723 HOH   A O   1 
HETATM 3420 O  O   . HOH   G 4 .   ? 121.019 -73.325 43.402 1.00 38.27 ? 724 HOH   A O   1 
HETATM 3421 O  O   . HOH   G 4 .   ? 116.340 -49.815 37.137 1.00 32.79 ? 725 HOH   A O   1 
HETATM 3422 O  O   . HOH   G 4 .   ? 124.940 -70.190 16.816 1.00 34.67 ? 726 HOH   A O   1 
HETATM 3423 O  O   . HOH   G 4 .   ? 136.658 -50.361 40.671 1.00 25.06 ? 727 HOH   A O   1 
HETATM 3424 O  O   A HOH   G 4 .   ? 115.927 -56.772 24.176 0.56 15.01 ? 728 HOH   A O   1 
HETATM 3425 O  O   B HOH   G 4 .   ? 116.153 -54.887 25.034 0.44 6.83  ? 728 HOH   A O   1 
HETATM 3426 O  O   . HOH   G 4 .   ? 123.857 -57.158 49.389 1.00 38.63 ? 729 HOH   A O   1 
HETATM 3427 O  O   . HOH   G 4 .   ? 121.684 -63.062 56.423 1.00 50.43 ? 730 HOH   A O   1 
HETATM 3428 O  O   . HOH   G 4 .   ? 145.048 -56.790 20.978 1.00 40.25 ? 731 HOH   A O   1 
HETATM 3429 O  O   . HOH   G 4 .   ? 121.227 -48.269 45.483 1.00 31.76 ? 732 HOH   A O   1 
HETATM 3430 O  O   . HOH   G 4 .   ? 144.817 -66.245 32.030 1.00 46.15 ? 733 HOH   A O   1 
HETATM 3431 O  O   . HOH   G 4 .   ? 119.339 -62.532 24.570 1.00 24.89 ? 734 HOH   A O   1 
HETATM 3432 O  O   . HOH   G 4 .   ? 116.584 -49.039 27.386 1.00 44.24 ? 735 HOH   A O   1 
HETATM 3433 O  O   . HOH   G 4 .   ? 124.820 -43.501 16.577 1.00 38.64 ? 736 HOH   A O   1 
HETATM 3434 O  O   . HOH   G 4 .   ? 141.970 -69.453 44.422 1.00 42.87 ? 737 HOH   A O   1 
HETATM 3435 O  O   . HOH   G 4 .   ? 133.414 -47.995 45.155 1.00 21.79 ? 738 HOH   A O   1 
HETATM 3436 O  O   . HOH   G 4 .   ? 126.602 -44.064 43.868 1.00 40.66 ? 739 HOH   A O   1 
HETATM 3437 O  O   . HOH   G 4 .   ? 137.630 -53.932 36.749 1.00 17.56 ? 740 HOH   A O   1 
HETATM 3438 O  O   . HOH   G 4 .   ? 133.613 -43.409 10.768 1.00 28.87 ? 741 HOH   A O   1 
HETATM 3439 O  O   . HOH   G 4 .   ? 131.772 -77.146 35.389 1.00 36.83 ? 742 HOH   A O   1 
HETATM 3440 O  O   . HOH   G 4 .   ? 124.593 -52.454 47.703 1.00 19.39 ? 743 HOH   A O   1 
HETATM 3441 O  O   . HOH   G 4 .   ? 135.422 -39.147 36.200 1.00 28.11 ? 744 HOH   A O   1 
HETATM 3442 O  O   . HOH   G 4 .   ? 139.881 -55.385 41.440 1.00 38.18 ? 745 HOH   A O   1 
HETATM 3443 O  O   . HOH   G 4 .   ? 128.642 -67.053 53.775 1.00 33.23 ? 746 HOH   A O   1 
HETATM 3444 O  O   . HOH   G 4 .   ? 119.300 -38.431 20.512 1.00 31.23 ? 747 HOH   A O   1 
HETATM 3445 O  O   . HOH   G 4 .   ? 116.506 -45.811 30.407 1.00 21.56 ? 748 HOH   A O   1 
HETATM 3446 O  O   . HOH   G 4 .   ? 127.842 -76.958 41.863 1.00 31.67 ? 749 HOH   A O   1 
HETATM 3447 O  O   . HOH   G 4 .   ? 118.680 -69.394 15.785 1.00 25.68 ? 750 HOH   A O   1 
HETATM 3448 O  O   . HOH   G 4 .   ? 121.059 -72.508 33.372 1.00 41.66 ? 751 HOH   A O   1 
HETATM 3449 O  O   . HOH   G 4 .   ? 125.228 -54.930 48.357 1.00 16.18 ? 752 HOH   A O   1 
HETATM 3450 O  O   . HOH   G 4 .   ? 125.035 -48.409 13.115 1.00 43.30 ? 753 HOH   A O   1 
HETATM 3451 O  O   . HOH   G 4 .   ? 137.600 -52.844 39.387 1.00 23.90 ? 754 HOH   A O   1 
HETATM 3452 O  O   . HOH   G 4 .   ? 115.280 -50.119 31.041 1.00 45.98 ? 755 HOH   A O   1 
HETATM 3453 O  O   . HOH   G 4 .   ? 122.809 -71.492 15.688 1.00 38.86 ? 756 HOH   A O   1 
HETATM 3454 O  O   . HOH   G 4 .   ? 118.261 -65.508 30.632 1.00 34.15 ? 757 HOH   A O   1 
HETATM 3455 O  O   . HOH   G 4 .   ? 123.445 -77.834 42.495 1.00 44.10 ? 758 HOH   A O   1 
HETATM 3456 O  O   . HOH   G 4 .   ? 120.542 -35.857 20.848 1.00 20.80 ? 759 HOH   A O   1 
HETATM 3457 O  O   . HOH   G 4 .   ? 125.982 -41.324 16.130 1.00 35.72 ? 760 HOH   A O   1 
HETATM 3458 O  O   . HOH   G 4 .   ? 134.360 -42.712 45.225 1.00 37.83 ? 761 HOH   A O   1 
HETATM 3459 O  O   . HOH   G 4 .   ? 140.146 -51.894 39.601 1.00 42.18 ? 762 HOH   A O   1 
HETATM 3460 O  O   . HOH   H 4 .   ? 165.371 -29.727 38.376 1.00 29.66 ? 501 HOH   B O   1 
HETATM 3461 O  O   . HOH   H 4 .   ? 162.135 -39.079 44.307 1.00 22.59 ? 502 HOH   B O   1 
HETATM 3462 O  O   . HOH   H 4 .   ? 169.312 -46.877 41.471 1.00 22.74 ? 503 HOH   B O   1 
HETATM 3463 O  O   . HOH   H 4 .   ? 152.089 -40.374 32.206 1.00 36.19 ? 504 HOH   B O   1 
HETATM 3464 O  O   . HOH   H 4 .   ? 166.488 -44.215 53.982 1.00 17.20 ? 505 HOH   B O   1 
HETATM 3465 O  O   . HOH   H 4 .   ? 178.523 -37.984 38.214 1.00 32.64 ? 506 HOH   B O   1 
HETATM 3466 O  O   . HOH   H 4 .   ? 172.447 -40.542 37.996 1.00 20.43 ? 507 HOH   B O   1 
HETATM 3467 O  O   . HOH   H 4 .   ? 148.095 -44.363 40.616 1.00 33.23 ? 508 HOH   B O   1 
HETATM 3468 O  O   . HOH   H 4 .   ? 155.121 -42.837 16.553 1.00 15.53 ? 509 HOH   B O   1 
HETATM 3469 O  O   . HOH   H 4 .   ? 165.826 -50.164 12.624 1.00 27.85 ? 510 HOH   B O   1 
HETATM 3470 O  O   . HOH   H 4 .   ? 170.073 -53.657 16.263 1.00 35.30 ? 511 HOH   B O   1 
HETATM 3471 O  O   . HOH   H 4 .   ? 153.849 -39.620 35.313 1.00 15.21 ? 512 HOH   B O   1 
HETATM 3472 O  O   . HOH   H 4 .   ? 167.402 -56.629 51.371 1.00 29.50 ? 513 HOH   B O   1 
HETATM 3473 O  O   . HOH   H 4 .   ? 166.886 -66.244 39.697 1.00 25.57 ? 514 HOH   B O   1 
HETATM 3474 O  O   . HOH   H 4 .   ? 165.452 -64.998 46.200 1.00 17.88 ? 515 HOH   B O   1 
HETATM 3475 O  O   . HOH   H 4 .   ? 164.386 -61.692 32.036 1.00 9.08  ? 516 HOH   B O   1 
HETATM 3476 O  O   . HOH   H 4 .   ? 167.163 -32.129 41.959 1.00 36.11 ? 517 HOH   B O   1 
HETATM 3477 O  O   . HOH   H 4 .   ? 163.051 -51.318 8.993  1.00 21.91 ? 518 HOH   B O   1 
HETATM 3478 O  O   . HOH   H 4 .   ? 174.077 -41.252 28.415 1.00 9.05  ? 519 HOH   B O   1 
HETATM 3479 O  O   . HOH   H 4 .   ? 167.427 -43.765 20.657 1.00 14.56 ? 520 HOH   B O   1 
HETATM 3480 O  O   . HOH   H 4 .   ? 153.706 -39.000 42.771 1.00 28.00 ? 521 HOH   B O   1 
HETATM 3481 O  O   . HOH   H 4 .   ? 153.572 -48.537 42.527 1.00 26.18 ? 522 HOH   B O   1 
HETATM 3482 O  O   . HOH   H 4 .   ? 168.838 -44.685 15.725 1.00 47.87 ? 523 HOH   B O   1 
HETATM 3483 O  O   . HOH   H 4 .   ? 169.980 -32.112 37.766 1.00 23.76 ? 524 HOH   B O   1 
HETATM 3484 O  O   . HOH   H 4 .   ? 156.218 -42.535 45.552 1.00 38.04 ? 525 HOH   B O   1 
HETATM 3485 O  O   . HOH   H 4 .   ? 157.207 -58.570 22.098 1.00 18.60 ? 526 HOH   B O   1 
HETATM 3486 O  O   . HOH   H 4 .   ? 151.387 -58.227 35.511 1.00 29.28 ? 527 HOH   B O   1 
HETATM 3487 O  O   . HOH   H 4 .   ? 159.051 -60.700 22.426 1.00 15.35 ? 528 HOH   B O   1 
HETATM 3488 O  O   . HOH   H 4 .   ? 178.896 -52.212 37.970 1.00 31.37 ? 529 HOH   B O   1 
HETATM 3489 O  O   . HOH   H 4 .   ? 154.888 -51.234 13.946 1.00 17.67 ? 530 HOH   B O   1 
HETATM 3490 O  O   . HOH   H 4 .   ? 161.009 -67.368 39.668 1.00 16.44 ? 531 HOH   B O   1 
HETATM 3491 O  O   . HOH   H 4 .   ? 170.787 -62.963 20.124 1.00 33.60 ? 532 HOH   B O   1 
HETATM 3492 O  O   . HOH   H 4 .   ? 170.992 -39.945 30.797 1.00 7.57  ? 533 HOH   B O   1 
HETATM 3493 O  O   . HOH   H 4 .   ? 165.429 -25.616 27.540 1.00 12.11 ? 534 HOH   B O   1 
HETATM 3494 O  O   . HOH   H 4 .   ? 164.247 -45.670 54.624 1.00 11.53 ? 535 HOH   B O   1 
HETATM 3495 O  O   . HOH   H 4 .   ? 167.453 -58.601 44.174 1.00 12.99 ? 536 HOH   B O   1 
HETATM 3496 O  O   . HOH   H 4 .   ? 160.329 -46.366 49.713 1.00 13.44 ? 537 HOH   B O   1 
HETATM 3497 O  O   . HOH   H 4 .   ? 163.178 -42.839 15.411 1.00 18.40 ? 538 HOH   B O   1 
HETATM 3498 O  O   . HOH   H 4 .   ? 170.223 -36.140 25.076 1.00 12.52 ? 539 HOH   B O   1 
HETATM 3499 O  O   . HOH   H 4 .   ? 163.966 -31.145 17.439 1.00 15.36 ? 540 HOH   B O   1 
HETATM 3500 O  O   . HOH   H 4 .   ? 163.957 -52.794 50.233 1.00 11.52 ? 541 HOH   B O   1 
HETATM 3501 O  O   . HOH   H 4 .   ? 163.643 -25.880 23.753 1.00 9.65  ? 542 HOH   B O   1 
HETATM 3502 O  O   . HOH   H 4 .   ? 166.628 -40.967 31.925 1.00 8.60  ? 543 HOH   B O   1 
HETATM 3503 O  O   . HOH   H 4 .   ? 158.244 -35.697 29.977 1.00 10.25 ? 544 HOH   B O   1 
HETATM 3504 O  O   . HOH   H 4 .   ? 157.424 -50.722 48.038 1.00 23.83 ? 545 HOH   B O   1 
HETATM 3505 O  O   . HOH   H 4 .   ? 161.899 -35.997 42.904 1.00 44.99 ? 546 HOH   B O   1 
HETATM 3506 O  O   . HOH   H 4 .   ? 173.726 -37.436 43.365 1.00 38.13 ? 547 HOH   B O   1 
HETATM 3507 O  O   . HOH   H 4 .   ? 171.613 -54.882 28.439 1.00 32.85 ? 548 HOH   B O   1 
HETATM 3508 O  O   . HOH   H 4 .   ? 156.718 -62.283 29.553 1.00 19.91 ? 549 HOH   B O   1 
HETATM 3509 O  O   . HOH   H 4 .   ? 152.835 -42.128 18.518 1.00 20.78 ? 550 HOH   B O   1 
HETATM 3510 O  O   . HOH   H 4 .   ? 160.116 -51.874 55.053 1.00 12.24 ? 551 HOH   B O   1 
HETATM 3511 O  O   . HOH   H 4 .   ? 152.197 -54.287 21.737 1.00 15.41 ? 552 HOH   B O   1 
HETATM 3512 O  O   . HOH   H 4 .   ? 171.760 -33.565 27.441 1.00 14.66 ? 553 HOH   B O   1 
HETATM 3513 O  O   . HOH   H 4 .   ? 168.429 -58.892 36.378 1.00 8.69  ? 554 HOH   B O   1 
HETATM 3514 O  O   . HOH   H 4 .   ? 153.315 -67.912 35.387 1.00 44.98 ? 555 HOH   B O   1 
HETATM 3515 O  O   . HOH   H 4 .   ? 155.395 -32.370 28.946 1.00 31.50 ? 556 HOH   B O   1 
HETATM 3516 O  O   . HOH   H 4 .   ? 168.112 -39.448 38.074 1.00 11.23 ? 557 HOH   B O   1 
HETATM 3517 O  O   . HOH   H 4 .   ? 155.483 -24.523 25.031 1.00 25.91 ? 558 HOH   B O   1 
HETATM 3518 O  O   . HOH   H 4 .   ? 164.479 -45.958 46.488 1.00 10.64 ? 559 HOH   B O   1 
HETATM 3519 O  O   . HOH   H 4 .   ? 175.703 -40.869 35.670 1.00 26.91 ? 560 HOH   B O   1 
HETATM 3520 O  O   . HOH   H 4 .   ? 154.867 -55.411 24.324 1.00 17.46 ? 561 HOH   B O   1 
HETATM 3521 O  O   . HOH   H 4 .   ? 169.720 -64.414 43.230 1.00 44.30 ? 562 HOH   B O   1 
HETATM 3522 O  O   . HOH   H 4 .   ? 160.849 -62.675 50.827 1.00 31.17 ? 563 HOH   B O   1 
HETATM 3523 O  O   . HOH   H 4 .   ? 152.168 -57.847 16.005 1.00 15.18 ? 564 HOH   B O   1 
HETATM 3524 O  O   . HOH   H 4 .   ? 160.112 -46.887 11.948 1.00 18.94 ? 565 HOH   B O   1 
HETATM 3525 O  O   . HOH   H 4 .   ? 172.368 -55.852 46.829 1.00 31.72 ? 566 HOH   B O   1 
HETATM 3526 O  O   . HOH   H 4 .   ? 156.478 -45.070 24.241 1.00 6.91  ? 567 HOH   B O   1 
HETATM 3527 O  O   . HOH   H 4 .   ? 169.573 -59.022 31.511 1.00 19.28 ? 568 HOH   B O   1 
HETATM 3528 O  O   . HOH   H 4 .   ? 151.958 -42.035 36.286 1.00 28.52 ? 569 HOH   B O   1 
HETATM 3529 O  O   . HOH   H 4 .   ? 178.292 -32.796 40.101 1.00 38.15 ? 570 HOH   B O   1 
HETATM 3530 O  O   . HOH   H 4 .   ? 167.756 -37.424 12.863 1.00 32.38 ? 571 HOH   B O   1 
HETATM 3531 O  O   . HOH   H 4 .   ? 164.940 -31.640 27.534 1.00 8.60  ? 572 HOH   B O   1 
HETATM 3532 O  O   . HOH   H 4 .   ? 163.188 -60.573 10.692 1.00 28.97 ? 573 HOH   B O   1 
HETATM 3533 O  O   . HOH   H 4 .   ? 168.692 -43.894 43.791 1.00 36.39 ? 574 HOH   B O   1 
HETATM 3534 O  O   . HOH   H 4 .   ? 171.573 -55.024 32.843 1.00 14.46 ? 575 HOH   B O   1 
HETATM 3535 O  O   . HOH   H 4 .   ? 177.832 -34.528 36.599 1.00 24.56 ? 576 HOH   B O   1 
HETATM 3536 O  O   . HOH   H 4 .   ? 170.117 -40.354 39.553 1.00 21.35 ? 577 HOH   B O   1 
HETATM 3537 O  O   . HOH   H 4 .   ? 176.708 -49.814 26.034 1.00 28.30 ? 578 HOH   B O   1 
HETATM 3538 O  O   . HOH   H 4 .   ? 156.270 -56.137 26.789 1.00 12.70 ? 579 HOH   B O   1 
HETATM 3539 O  O   . HOH   H 4 .   ? 177.113 -42.421 38.672 1.00 35.35 ? 580 HOH   B O   1 
HETATM 3540 O  O   . HOH   H 4 .   ? 169.319 -32.590 34.936 1.00 42.22 ? 581 HOH   B O   1 
HETATM 3541 O  O   . HOH   H 4 .   ? 156.218 -65.275 40.811 1.00 20.86 ? 582 HOH   B O   1 
HETATM 3542 O  O   . HOH   H 4 .   ? 158.493 -41.579 48.455 1.00 18.34 ? 583 HOH   B O   1 
HETATM 3543 O  O   . HOH   H 4 .   ? 151.291 -57.983 23.419 1.00 23.80 ? 584 HOH   B O   1 
HETATM 3544 O  O   . HOH   H 4 .   ? 152.411 -48.295 35.353 1.00 15.17 ? 585 HOH   B O   1 
HETATM 3545 O  O   . HOH   H 4 .   ? 152.163 -57.949 31.838 1.00 32.16 ? 586 HOH   B O   1 
HETATM 3546 O  O   . HOH   H 4 .   ? 168.484 -38.774 31.604 1.00 10.75 ? 587 HOH   B O   1 
HETATM 3547 O  O   . HOH   H 4 .   ? 154.701 -62.098 48.890 1.00 32.86 ? 588 HOH   B O   1 
HETATM 3548 O  O   . HOH   H 4 .   ? 182.815 -46.730 27.241 1.00 44.56 ? 589 HOH   B O   1 
HETATM 3549 O  O   . HOH   H 4 .   ? 161.836 -61.049 12.931 1.00 39.70 ? 590 HOH   B O   1 
HETATM 3550 O  O   . HOH   H 4 .   ? 165.244 -37.762 30.148 1.00 7.94  ? 591 HOH   B O   1 
HETATM 3551 O  O   . HOH   H 4 .   ? 158.733 -65.951 41.022 1.00 15.63 ? 592 HOH   B O   1 
HETATM 3552 O  O   . HOH   H 4 .   ? 155.777 -25.788 21.301 1.00 32.66 ? 593 HOH   B O   1 
HETATM 3553 O  O   . HOH   H 4 .   ? 172.621 -48.073 37.180 1.00 14.40 ? 594 HOH   B O   1 
HETATM 3554 O  O   . HOH   H 4 .   ? 152.440 -48.751 38.066 1.00 36.11 ? 595 HOH   B O   1 
HETATM 3555 O  O   . HOH   H 4 .   ? 165.374 -36.915 22.536 1.00 13.36 ? 596 HOH   B O   1 
HETATM 3556 O  O   . HOH   H 4 .   ? 180.732 -40.715 26.551 1.00 18.74 ? 597 HOH   B O   1 
HETATM 3557 O  O   . HOH   H 4 .   ? 178.080 -37.123 23.096 1.00 23.74 ? 598 HOH   B O   1 
HETATM 3558 O  O   . HOH   H 4 .   ? 149.529 -46.508 16.292 1.00 31.03 ? 599 HOH   B O   1 
HETATM 3559 O  O   . HOH   H 4 .   ? 166.970 -30.767 24.233 1.00 20.74 ? 600 HOH   B O   1 
HETATM 3560 O  O   . HOH   H 4 .   ? 170.591 -54.478 19.737 1.00 47.12 ? 601 HOH   B O   1 
HETATM 3561 O  O   . HOH   H 4 .   ? 160.406 -46.729 37.290 1.00 6.97  ? 602 HOH   B O   1 
HETATM 3562 O  O   . HOH   H 4 .   ? 154.080 -34.823 22.039 1.00 38.74 ? 603 HOH   B O   1 
HETATM 3563 O  O   . HOH   H 4 .   ? 154.783 -32.901 18.453 1.00 32.32 ? 604 HOH   B O   1 
HETATM 3564 O  O   . HOH   H 4 .   ? 151.060 -50.587 35.958 1.00 38.60 ? 605 HOH   B O   1 
HETATM 3565 O  O   . HOH   H 4 .   ? 179.644 -47.242 34.571 1.00 24.72 ? 606 HOH   B O   1 
HETATM 3566 O  O   . HOH   H 4 .   ? 164.453 -33.651 41.100 1.00 18.35 ? 607 HOH   B O   1 
HETATM 3567 O  O   . HOH   H 4 .   ? 160.919 -68.728 43.982 1.00 38.54 ? 608 HOH   B O   1 
HETATM 3568 O  O   . HOH   H 4 .   ? 171.606 -33.949 20.071 1.00 27.42 ? 609 HOH   B O   1 
HETATM 3569 O  O   . HOH   H 4 .   ? 174.550 -44.146 21.547 1.00 12.03 ? 610 HOH   B O   1 
HETATM 3570 O  O   . HOH   H 4 .   ? 176.068 -59.709 35.038 1.00 29.69 ? 611 HOH   B O   1 
HETATM 3571 O  O   . HOH   H 4 .   ? 164.124 -32.009 33.908 1.00 16.64 ? 612 HOH   B O   1 
HETATM 3572 O  O   . HOH   H 4 .   ? 162.510 -39.952 33.551 1.00 5.89  ? 613 HOH   B O   1 
HETATM 3573 O  O   . HOH   H 4 .   ? 150.633 -52.740 19.819 1.00 21.36 ? 614 HOH   B O   1 
HETATM 3574 O  O   . HOH   H 4 .   ? 164.086 -62.135 19.037 1.00 10.22 ? 615 HOH   B O   1 
HETATM 3575 O  O   . HOH   H 4 .   ? 162.143 -44.328 49.105 1.00 10.80 ? 616 HOH   B O   1 
HETATM 3576 O  O   . HOH   H 4 .   ? 167.792 -47.096 36.955 1.00 9.53  ? 617 HOH   B O   1 
HETATM 3577 O  O   . HOH   H 4 .   ? 170.189 -57.734 46.425 1.00 21.45 ? 618 HOH   B O   1 
HETATM 3578 O  O   . HOH   H 4 .   ? 162.569 -47.315 9.812  1.00 39.49 ? 619 HOH   B O   1 
HETATM 3579 O  O   . HOH   H 4 .   ? 162.678 -30.237 35.858 1.00 21.81 ? 620 HOH   B O   1 
HETATM 3580 O  O   . HOH   H 4 .   ? 154.052 -61.057 14.326 1.00 28.35 ? 621 HOH   B O   1 
HETATM 3581 O  O   . HOH   H 4 .   ? 153.939 -66.362 42.092 1.00 27.51 ? 622 HOH   B O   1 
HETATM 3582 O  O   . HOH   H 4 .   ? 172.791 -29.336 40.491 1.00 34.91 ? 623 HOH   B O   1 
HETATM 3583 O  O   . HOH   H 4 .   ? 176.186 -46.972 38.765 1.00 19.78 ? 624 HOH   B O   1 
HETATM 3584 O  O   . HOH   H 4 .   ? 164.355 -40.461 43.533 1.00 13.46 ? 625 HOH   B O   1 
HETATM 3585 O  O   . HOH   H 4 .   ? 172.827 -50.505 18.692 1.00 33.63 ? 626 HOH   B O   1 
HETATM 3586 O  O   . HOH   H 4 .   ? 157.772 -34.156 39.221 1.00 45.50 ? 627 HOH   B O   1 
HETATM 3587 O  O   . HOH   H 4 .   ? 153.306 -51.201 38.730 1.00 36.74 ? 628 HOH   B O   1 
HETATM 3588 O  O   . HOH   H 4 .   ? 149.990 -43.814 26.170 1.00 23.39 ? 629 HOH   B O   1 
HETATM 3589 O  O   . HOH   H 4 .   ? 169.850 -35.226 43.487 1.00 26.02 ? 630 HOH   B O   1 
HETATM 3590 O  O   . HOH   H 4 .   ? 168.008 -47.606 19.297 1.00 25.11 ? 631 HOH   B O   1 
HETATM 3591 O  O   . HOH   H 4 .   ? 163.767 -34.127 14.458 1.00 20.37 ? 632 HOH   B O   1 
HETATM 3592 O  O   . HOH   H 4 .   ? 149.439 -48.768 14.688 1.00 30.48 ? 633 HOH   B O   1 
HETATM 3593 O  O   . HOH   H 4 .   ? 173.787 -48.966 46.257 1.00 21.45 ? 634 HOH   B O   1 
HETATM 3594 O  O   . HOH   H 4 .   ? 170.774 -55.596 14.090 1.00 21.78 ? 635 HOH   B O   1 
HETATM 3595 O  O   . HOH   H 4 .   ? 150.161 -57.617 19.363 1.00 29.68 ? 636 HOH   B O   1 
HETATM 3596 O  O   . HOH   H 4 .   ? 173.033 -61.518 41.741 1.00 19.74 ? 637 HOH   B O   1 
HETATM 3597 O  O   . HOH   H 4 .   ? 152.407 -39.449 29.396 1.00 38.42 ? 638 HOH   B O   1 
HETATM 3598 O  O   . HOH   H 4 .   ? 156.201 -28.545 27.488 1.00 22.92 ? 639 HOH   B O   1 
HETATM 3599 O  O   . HOH   H 4 .   ? 160.738 -43.805 12.718 1.00 27.67 ? 640 HOH   B O   1 
HETATM 3600 O  O   . HOH   H 4 .   ? 155.014 -59.907 11.046 1.00 41.89 ? 641 HOH   B O   1 
HETATM 3601 O  O   . HOH   H 4 .   ? 159.255 -61.190 12.923 1.00 35.48 ? 642 HOH   B O   1 
HETATM 3602 O  O   . HOH   H 4 .   ? 151.330 -69.816 38.993 1.00 35.23 ? 643 HOH   B O   1 
HETATM 3603 O  O   . HOH   H 4 .   ? 165.377 -27.175 31.371 1.00 29.14 ? 644 HOH   B O   1 
HETATM 3604 O  O   . HOH   H 4 .   ? 153.138 -26.205 23.179 1.00 41.99 ? 645 HOH   B O   1 
HETATM 3605 O  O   . HOH   H 4 .   ? 180.385 -48.456 22.372 1.00 41.46 ? 646 HOH   B O   1 
HETATM 3606 O  O   . HOH   H 4 .   ? 171.962 -55.860 25.911 1.00 21.47 ? 647 HOH   B O   1 
HETATM 3607 O  O   . HOH   H 4 .   ? 155.354 -53.719 41.438 1.00 21.09 ? 648 HOH   B O   1 
HETATM 3608 O  O   . HOH   H 4 .   ? 154.007 -44.183 14.520 1.00 26.29 ? 649 HOH   B O   1 
HETATM 3609 O  O   . HOH   H 4 .   ? 157.997 -26.687 19.425 1.00 10.82 ? 650 HOH   B O   1 
HETATM 3610 O  O   . HOH   H 4 .   ? 158.099 -43.543 44.349 1.00 19.77 ? 651 HOH   B O   1 
HETATM 3611 O  O   . HOH   H 4 .   ? 174.606 -54.588 29.629 1.00 47.56 ? 652 HOH   B O   1 
HETATM 3612 O  O   . HOH   H 4 .   ? 155.714 -51.314 40.682 1.00 21.79 ? 653 HOH   B O   1 
HETATM 3613 O  O   . HOH   H 4 .   ? 178.523 -44.769 38.158 1.00 34.96 ? 654 HOH   B O   1 
HETATM 3614 O  O   . HOH   H 4 .   ? 170.110 -65.228 40.815 1.00 27.62 ? 655 HOH   B O   1 
HETATM 3615 O  O   . HOH   H 4 .   ? 158.192 -36.060 41.093 1.00 14.51 ? 656 HOH   B O   1 
HETATM 3616 O  O   . HOH   H 4 .   ? 171.977 -31.805 30.141 1.00 39.92 ? 657 HOH   B O   1 
HETATM 3617 O  O   . HOH   H 4 .   ? 161.566 -63.066 16.690 1.00 24.63 ? 658 HOH   B O   1 
HETATM 3618 O  O   . HOH   H 4 .   ? 165.226 -42.461 49.179 1.00 32.35 ? 659 HOH   B O   1 
HETATM 3619 O  O   . HOH   H 4 .   ? 165.560 -43.305 46.954 1.00 22.56 ? 660 HOH   B O   1 
HETATM 3620 O  O   . HOH   H 4 .   ? 152.722 -62.193 25.655 1.00 25.38 ? 661 HOH   B O   1 
HETATM 3621 O  O   . HOH   H 4 .   ? 152.040 -56.651 8.987  1.00 24.73 ? 662 HOH   B O   1 
HETATM 3622 O  O   . HOH   H 4 .   ? 156.013 -54.027 7.445  1.00 48.91 ? 663 HOH   B O   1 
HETATM 3623 O  O   A HOH   H 4 .   ? 163.774 -59.605 52.739 0.52 15.50 ? 664 HOH   B O   1 
HETATM 3624 O  O   B HOH   H 4 .   ? 161.978 -59.391 51.913 0.48 10.83 ? 664 HOH   B O   1 
HETATM 3625 O  O   . HOH   H 4 .   ? 177.151 -48.398 31.565 1.00 16.13 ? 665 HOH   B O   1 
HETATM 3626 O  O   . HOH   H 4 .   ? 162.090 -33.435 39.284 1.00 32.38 ? 666 HOH   B O   1 
HETATM 3627 O  O   . HOH   H 4 .   ? 161.013 -64.074 34.676 1.00 14.66 ? 667 HOH   B O   1 
HETATM 3628 O  O   . HOH   H 4 .   ? 160.286 -29.061 34.485 1.00 25.20 ? 668 HOH   B O   1 
HETATM 3629 O  O   . HOH   H 4 .   ? 173.054 -61.538 38.415 1.00 17.32 ? 669 HOH   B O   1 
HETATM 3630 O  O   . HOH   H 4 .   ? 147.431 -42.214 30.288 1.00 34.62 ? 670 HOH   B O   1 
HETATM 3631 O  O   . HOH   H 4 .   ? 151.067 -54.948 38.135 1.00 19.58 ? 671 HOH   B O   1 
HETATM 3632 O  O   . HOH   H 4 .   ? 166.113 -30.861 32.381 1.00 16.81 ? 672 HOH   B O   1 
HETATM 3633 O  O   . HOH   H 4 .   ? 166.144 -28.092 24.375 1.00 23.23 ? 673 HOH   B O   1 
HETATM 3634 O  O   . HOH   H 4 .   ? 168.087 -62.286 15.021 1.00 33.83 ? 674 HOH   B O   1 
HETATM 3635 O  O   . HOH   H 4 .   ? 170.654 -48.097 43.345 1.00 26.15 ? 675 HOH   B O   1 
HETATM 3636 O  O   . HOH   H 4 .   ? 172.450 -32.983 22.040 1.00 38.79 ? 676 HOH   B O   1 
HETATM 3637 O  O   . HOH   H 4 .   ? 155.683 -35.351 17.303 1.00 28.69 ? 677 HOH   B O   1 
HETATM 3638 O  O   . HOH   H 4 .   ? 179.277 -37.402 25.528 1.00 43.44 ? 678 HOH   B O   1 
HETATM 3639 O  O   . HOH   H 4 .   ? 149.655 -58.412 39.540 1.00 32.86 ? 679 HOH   B O   1 
HETATM 3640 O  O   . HOH   H 4 .   ? 173.240 -48.318 40.250 1.00 40.24 ? 680 HOH   B O   1 
HETATM 3641 O  O   . HOH   H 4 .   ? 170.657 -53.179 12.454 1.00 41.52 ? 681 HOH   B O   1 
HETATM 3642 O  O   . HOH   H 4 .   ? 151.294 -63.542 22.628 1.00 55.11 ? 682 HOH   B O   1 
HETATM 3643 O  O   . HOH   H 4 .   ? 175.413 -57.377 32.187 1.00 17.14 ? 683 HOH   B O   1 
HETATM 3644 O  O   . HOH   H 4 .   ? 176.697 -53.522 40.240 1.00 32.80 ? 684 HOH   B O   1 
HETATM 3645 O  O   . HOH   H 4 .   ? 168.080 -31.350 33.535 1.00 26.75 ? 685 HOH   B O   1 
HETATM 3646 O  O   . HOH   H 4 .   ? 178.343 -51.437 33.267 1.00 24.74 ? 686 HOH   B O   1 
HETATM 3647 O  O   . HOH   H 4 .   ? 164.132 -40.049 31.327 1.00 6.50  ? 687 HOH   B O   1 
HETATM 3648 O  O   . HOH   H 4 .   ? 169.752 -57.526 49.430 1.00 28.83 ? 688 HOH   B O   1 
HETATM 3649 O  O   . HOH   H 4 .   ? 166.225 -66.043 37.374 1.00 41.15 ? 689 HOH   B O   1 
HETATM 3650 O  O   . HOH   H 4 .   ? 172.148 -29.197 27.500 1.00 39.95 ? 690 HOH   B O   1 
HETATM 3651 O  O   . HOH   H 4 .   ? 184.117 -37.003 34.474 1.00 49.32 ? 691 HOH   B O   1 
HETATM 3652 O  O   . HOH   H 4 .   ? 174.760 -43.157 16.259 1.00 36.82 ? 692 HOH   B O   1 
HETATM 3653 O  O   . HOH   H 4 .   ? 167.128 -65.857 44.007 1.00 21.61 ? 693 HOH   B O   1 
HETATM 3654 O  O   . HOH   H 4 .   ? 149.350 -54.860 10.657 1.00 31.06 ? 694 HOH   B O   1 
HETATM 3655 O  O   . HOH   H 4 .   ? 162.405 -39.865 47.217 1.00 31.71 ? 695 HOH   B O   1 
HETATM 3656 O  O   . HOH   H 4 .   ? 151.799 -62.289 45.287 1.00 41.10 ? 696 HOH   B O   1 
HETATM 3657 O  O   . HOH   H 4 .   ? 153.747 -47.361 11.126 1.00 42.67 ? 697 HOH   B O   1 
HETATM 3658 O  O   . HOH   H 4 .   ? 160.989 -41.001 13.015 1.00 44.43 ? 698 HOH   B O   1 
HETATM 3659 O  O   . HOH   H 4 .   ? 177.325 -41.302 16.501 1.00 36.78 ? 699 HOH   B O   1 
HETATM 3660 O  O   . HOH   H 4 .   ? 167.783 -46.965 17.081 1.00 33.43 ? 700 HOH   B O   1 
HETATM 3661 O  O   . HOH   H 4 .   ? 149.850 -55.823 15.817 1.00 39.88 ? 701 HOH   B O   1 
HETATM 3662 O  O   . HOH   H 4 .   ? 168.221 -30.724 40.266 1.00 56.44 ? 702 HOH   B O   1 
HETATM 3663 O  O   . HOH   H 4 .   ? 158.447 -64.819 48.488 1.00 24.80 ? 703 HOH   B O   1 
HETATM 3664 O  O   . HOH   H 4 .   ? 168.531 -61.125 34.904 1.00 17.76 ? 704 HOH   B O   1 
HETATM 3665 O  O   . HOH   H 4 .   ? 152.194 -64.732 43.653 1.00 34.69 ? 705 HOH   B O   1 
HETATM 3666 O  O   . HOH   H 4 .   ? 156.954 -61.702 19.663 1.00 5.29  ? 706 HOH   B O   1 
HETATM 3667 O  O   . HOH   H 4 .   ? 170.984 -54.673 23.951 1.00 40.07 ? 707 HOH   B O   1 
HETATM 3668 O  O   . HOH   H 4 .   ? 151.232 -63.342 35.666 1.00 31.44 ? 708 HOH   B O   1 
HETATM 3669 O  O   . HOH   H 4 .   ? 151.055 -40.979 26.928 1.00 51.37 ? 709 HOH   B O   1 
HETATM 3670 O  O   . HOH   H 4 .   ? 166.562 -43.049 14.390 1.00 24.85 ? 710 HOH   B O   1 
HETATM 3671 O  O   . HOH   H 4 .   ? 163.355 -43.265 12.298 1.00 56.51 ? 711 HOH   B O   1 
HETATM 3672 O  O   . HOH   H 4 .   ? 164.764 -63.390 50.453 1.00 31.10 ? 712 HOH   B O   1 
HETATM 3673 O  O   . HOH   H 4 .   ? 171.269 -57.525 29.258 1.00 41.14 ? 713 HOH   B O   1 
HETATM 3674 O  O   . HOH   H 4 .   ? 149.809 -41.033 33.240 1.00 42.26 ? 714 HOH   B O   1 
HETATM 3675 O  O   . HOH   H 4 .   ? 170.221 -33.724 23.864 1.00 22.53 ? 715 HOH   B O   1 
HETATM 3676 O  O   . HOH   H 4 .   ? 174.555 -39.284 15.525 1.00 38.05 ? 716 HOH   B O   1 
HETATM 3677 O  O   . HOH   H 4 .   ? 156.346 -64.400 49.363 1.00 40.11 ? 717 HOH   B O   1 
HETATM 3678 O  O   . HOH   H 4 .   ? 154.733 -58.861 8.942  1.00 43.24 ? 718 HOH   B O   1 
HETATM 3679 O  O   . HOH   H 4 .   ? 149.596 -53.054 36.388 1.00 40.15 ? 719 HOH   B O   1 
HETATM 3680 O  O   . HOH   H 4 .   ? 147.863 -56.800 11.735 1.00 41.27 ? 720 HOH   B O   1 
HETATM 3681 O  O   . HOH   H 4 .   ? 170.713 -62.803 34.829 1.00 25.03 ? 721 HOH   B O   1 
HETATM 3682 O  O   . HOH   H 4 .   ? 167.565 -42.429 45.826 1.00 25.37 ? 722 HOH   B O   1 
HETATM 3683 O  O   . HOH   H 4 .   ? 153.954 -53.991 56.434 1.00 48.00 ? 723 HOH   B O   1 
HETATM 3684 O  O   . HOH   H 4 .   ? 169.438 -42.572 40.676 1.00 29.35 ? 724 HOH   B O   1 
HETATM 3685 O  O   . HOH   H 4 .   ? 156.581 -57.904 54.437 1.00 35.30 ? 725 HOH   B O   1 
HETATM 3686 O  O   . HOH   H 4 .   ? 151.476 -47.575 44.104 1.00 44.68 ? 726 HOH   B O   1 
HETATM 3687 O  O   . HOH   H 4 .   ? 159.332 -62.800 15.506 1.00 33.01 ? 727 HOH   B O   1 
HETATM 3688 O  O   . HOH   H 4 .   ? 166.944 -62.637 50.740 1.00 48.23 ? 728 HOH   B O   1 
HETATM 3689 O  O   . HOH   H 4 .   ? 156.500 -48.158 49.162 1.00 41.14 ? 729 HOH   B O   1 
HETATM 3690 O  O   . HOH   H 4 .   ? 149.508 -47.445 41.998 1.00 38.52 ? 730 HOH   B O   1 
HETATM 3691 O  O   . HOH   H 4 .   ? 176.691 -55.286 30.593 1.00 40.60 ? 731 HOH   B O   1 
HETATM 3692 O  O   . HOH   H 4 .   ? 161.091 -41.711 49.259 1.00 15.29 ? 732 HOH   B O   1 
HETATM 3693 O  O   . HOH   H 4 .   ? 158.553 -35.530 15.788 1.00 29.85 ? 733 HOH   B O   1 
HETATM 3694 O  O   . HOH   H 4 .   ? 166.087 -39.842 45.093 1.00 23.54 ? 734 HOH   B O   1 
HETATM 3695 O  O   . HOH   H 4 .   ? 170.771 -29.058 20.357 1.00 35.60 ? 735 HOH   B O   1 
HETATM 3696 O  O   . HOH   H 4 .   ? 154.922 -63.429 28.885 1.00 42.26 ? 736 HOH   B O   1 
HETATM 3697 O  O   . HOH   H 4 .   ? 184.499 -35.936 37.355 1.00 43.09 ? 737 HOH   B O   1 
HETATM 3698 O  O   . HOH   H 4 .   ? 159.114 -68.589 42.370 1.00 25.07 ? 738 HOH   B O   1 
HETATM 3699 O  O   A HOH   H 4 .   ? 163.044 -68.978 35.868 0.47 5.84  ? 739 HOH   B O   1 
HETATM 3700 O  O   B HOH   H 4 .   ? 164.920 -68.772 36.714 0.53 12.42 ? 739 HOH   B O   1 
HETATM 3701 O  O   . HOH   H 4 .   ? 173.309 -62.151 36.123 1.00 30.65 ? 740 HOH   B O   1 
HETATM 3702 O  O   . HOH   H 4 .   ? 155.195 -29.400 32.369 1.00 34.01 ? 741 HOH   B O   1 
HETATM 3703 O  O   . HOH   H 4 .   ? 151.268 -60.099 15.098 1.00 45.82 ? 742 HOH   B O   1 
HETATM 3704 O  O   . HOH   H 4 .   ? 157.148 -43.805 47.669 1.00 28.98 ? 743 HOH   B O   1 
HETATM 3705 O  O   . HOH   H 4 .   ? 174.537 -42.434 38.023 1.00 31.60 ? 744 HOH   B O   1 
HETATM 3706 O  O   . HOH   H 4 .   ? 149.589 -40.236 35.861 1.00 38.79 ? 745 HOH   B O   1 
HETATM 3707 O  O   . HOH   H 4 .   ? 154.526 -68.695 43.165 1.00 34.84 ? 746 HOH   B O   1 
HETATM 3708 O  O   . HOH   H 4 .   ? 150.115 -55.764 21.153 1.00 22.28 ? 747 HOH   B O   1 
HETATM 3709 O  O   . HOH   H 4 .   ? 160.296 -58.780 53.588 1.00 40.45 ? 748 HOH   B O   1 
HETATM 3710 O  O   A HOH   H 4 .   ? 150.567 -56.321 30.520 0.46 14.77 ? 749 HOH   B O   1 
HETATM 3711 O  O   B HOH   H 4 .   ? 149.693 -54.580 30.963 0.54 16.43 ? 749 HOH   B O   1 
HETATM 3712 O  O   . HOH   H 4 .   ? 152.781 -26.789 20.614 1.00 45.69 ? 750 HOH   B O   1 
HETATM 3713 O  O   . HOH   H 4 .   ? 152.820 -65.313 34.093 1.00 36.56 ? 751 HOH   B O   1 
HETATM 3714 O  O   . HOH   H 4 .   ? 157.739 -46.283 48.373 1.00 15.65 ? 752 HOH   B O   1 
HETATM 3715 O  O   . HOH   H 4 .   ? 159.627 -46.936 9.076  1.00 43.77 ? 753 HOH   B O   1 
HETATM 3716 O  O   . HOH   H 4 .   ? 158.682 -40.256 12.546 1.00 41.82 ? 754 HOH   B O   1 
HETATM 3717 O  O   . HOH   H 4 .   ? 170.501 -45.221 39.654 1.00 30.30 ? 755 HOH   B O   1 
HETATM 3718 O  O   . HOH   H 4 .   ? 155.105 -63.053 15.140 1.00 35.28 ? 756 HOH   B O   1 
HETATM 3719 O  O   . HOH   H 4 .   ? 160.275 -36.667 14.162 1.00 38.24 ? 757 HOH   B O   1 
HETATM 3720 O  O   . HOH   H 4 .   ? 177.114 -55.815 27.224 1.00 41.01 ? 758 HOH   B O   1 
HETATM 3721 O  O   . HOH   H 4 .   ? 170.504 -46.363 36.719 1.00 17.56 ? 759 HOH   B O   1 
HETATM 3722 O  O   . HOH   H 4 .   ? 179.976 -47.740 31.855 1.00 20.25 ? 760 HOH   B O   1 
HETATM 3723 O  O   . HOH   H 4 .   ? 160.276 -30.326 37.095 1.00 34.28 ? 761 HOH   B O   1 
HETATM 3724 O  O   . HOH   H 4 .   ? 153.615 -36.011 43.326 1.00 33.66 ? 762 HOH   B O   1 
HETATM 3725 O  O   . HOH   H 4 .   ? 158.970 -42.094 10.382 1.00 44.41 ? 763 HOH   B O   1 
HETATM 3726 O  O   . HOH   H 4 .   ? 175.805 -49.608 44.158 1.00 32.62 ? 764 HOH   B O   1 
# 
loop_
_atom_site_anisotrop.id 
_atom_site_anisotrop.type_symbol 
_atom_site_anisotrop.pdbx_label_atom_id 
_atom_site_anisotrop.pdbx_label_alt_id 
_atom_site_anisotrop.pdbx_label_comp_id 
_atom_site_anisotrop.pdbx_label_asym_id 
_atom_site_anisotrop.pdbx_label_seq_id 
_atom_site_anisotrop.pdbx_PDB_ins_code 
_atom_site_anisotrop.U[1][1] 
_atom_site_anisotrop.U[2][2] 
_atom_site_anisotrop.U[3][3] 
_atom_site_anisotrop.U[1][2] 
_atom_site_anisotrop.U[1][3] 
_atom_site_anisotrop.U[2][3] 
_atom_site_anisotrop.pdbx_auth_seq_id 
_atom_site_anisotrop.pdbx_auth_comp_id 
_atom_site_anisotrop.pdbx_auth_asym_id 
_atom_site_anisotrop.pdbx_auth_atom_id 
1    N N   . SER A 4   ? 0.8673 0.5737 0.8249 -0.1500 0.0788  0.1888  95  SER A N   
2    C CA  . SER A 4   ? 0.8967 0.6044 0.8680 -0.1436 0.0636  0.1677  95  SER A CA  
3    C C   . SER A 4   ? 0.8758 0.6313 0.8624 -0.1424 0.0719  0.1550  95  SER A C   
4    O O   . SER A 4   ? 0.9060 0.7125 0.9047 -0.1391 0.0742  0.1696  95  SER A O   
5    C CB  . SER A 4   ? 0.8682 0.5525 0.8302 -0.1090 0.0614  0.1664  95  SER A CB  
6    O OG  . SER A 4   ? 0.9087 0.5455 0.8649 -0.1044 0.0627  0.1737  95  SER A OG  
7    N N   . SER A 5   ? 0.7581 0.5180 0.7640 -0.1430 0.0620  0.1350  96  SER A N   
8    C CA  A SER A 5   ? 0.7059 0.5179 0.7207 -0.1479 0.0489  0.1257  96  SER A CA  
9    C CA  B SER A 5   ? 0.7084 0.5205 0.7233 -0.1479 0.0489  0.1257  96  SER A CA  
10   C C   . SER A 5   ? 0.7085 0.5522 0.7189 -0.1175 0.0473  0.1334  96  SER A C   
11   O O   . SER A 5   ? 0.6937 0.5130 0.6878 -0.0932 0.0513  0.1395  96  SER A O   
12   C CB  A SER A 5   ? 0.6742 0.4721 0.6849 -0.1557 0.0357  0.0983  96  SER A CB  
13   C CB  B SER A 5   ? 0.6751 0.4732 0.6858 -0.1558 0.0356  0.0982  96  SER A CB  
14   O OG  A SER A 5   ? 0.6061 0.4095 0.6045 -0.1353 0.0293  0.0892  96  SER A OG  
15   O OG  B SER A 5   ? 0.6074 0.4558 0.6286 -0.1583 0.0225  0.0921  96  SER A OG  
16   N N   . VAL A 6   ? 0.6578 0.5597 0.6843 -0.1142 0.0417  0.1289  97  VAL A N   
17   C CA  . VAL A 6   ? 0.5708 0.5074 0.5918 -0.0842 0.0420  0.1293  97  VAL A CA  
18   C C   . VAL A 6   ? 0.4658 0.4071 0.4846 -0.0717 0.0288  0.1057  97  VAL A C   
19   O O   . VAL A 6   ? 0.4873 0.4541 0.5217 -0.0833 0.0205  0.0954  97  VAL A O   
20   C CB  . VAL A 6   ? 0.5430 0.5360 0.5826 -0.0859 0.0501  0.1410  97  VAL A CB  
21   N N   . PRO A 7   ? 0.3894 0.3096 0.3919 -0.0493 0.0260  0.0992  98  PRO A N   
22   C CA  . PRO A 7   ? 0.3418 0.2730 0.3443 -0.0373 0.0158  0.0796  98  PRO A CA  
23   C C   . PRO A 7   ? 0.2842 0.2621 0.2919 -0.0244 0.0137  0.0790  98  PRO A C   
24   O O   . PRO A 7   ? 0.3000 0.2926 0.2999 -0.0140 0.0204  0.0911  98  PRO A O   
25   C CB  . PRO A 7   ? 0.3801 0.2807 0.3709 -0.0176 0.0156  0.0780  98  PRO A CB  
26   C CG  . PRO A 7   ? 0.4651 0.3556 0.4477 -0.0111 0.0226  0.1004  98  PRO A CG  
27   C CD  . PRO A 7   ? 0.4823 0.3683 0.4697 -0.0351 0.0312  0.1117  98  PRO A CD  
28   N N   . SER A 8   ? 0.2093 0.2069 0.2266 -0.0251 0.0055  0.0651  99  SER A N   
29   C CA  . SER A 8   ? 0.2428 0.2776 0.2654 -0.0111 0.0055  0.0632  99  SER A CA  
30   C C   . SER A 8   ? 0.2373 0.2657 0.2405 0.0108  0.0038  0.0589  99  SER A C   
31   O O   . SER A 8   ? 0.2200 0.2248 0.2158 0.0164  -0.0023 0.0527  99  SER A O   
32   C CB  . SER A 8   ? 0.2838 0.3354 0.3204 -0.0148 -0.0042 0.0514  99  SER A CB  
33   O OG  . SER A 8   ? 0.2570 0.3336 0.2962 0.0031  -0.0030 0.0479  99  SER A OG  
34   N N   . GLN A 9   ? 0.2012 0.2511 0.1961 0.0227  0.0098  0.0621  100 GLN A N   
35   C CA  . GLN A 9   ? 0.2583 0.3037 0.2309 0.0398  0.0047  0.0552  100 GLN A CA  
36   C C   . GLN A 9   ? 0.2475 0.3090 0.2218 0.0492  0.0033  0.0412  100 GLN A C   
37   O O   . GLN A 9   ? 0.2728 0.3310 0.2250 0.0609  0.0007  0.0341  100 GLN A O   
38   C CB  . GLN A 9   ? 0.3005 0.3453 0.2469 0.0458  0.0122  0.0687  100 GLN A CB  
39   C CG  . GLN A 9   ? 0.3569 0.4258 0.3006 0.0469  0.0296  0.0749  100 GLN A CG  
40   C CD  . GLN A 9   ? 0.4429 0.5079 0.3486 0.0540  0.0381  0.0862  100 GLN A CD  
41   O OE1 . GLN A 9   ? 0.3929 0.4529 0.2937 0.0465  0.0467  0.1055  100 GLN A OE1 
42   N NE2 . GLN A 9   ? 0.4294 0.4929 0.3036 0.0670  0.0353  0.0744  100 GLN A NE2 
43   N N   . LYS A 10  ? 0.1977 0.2740 0.1964 0.0437  0.0037  0.0378  101 LYS A N   
44   C CA  . LYS A 10  ? 0.1629 0.2534 0.1670 0.0548  0.0052  0.0287  101 LYS A CA  
45   C C   . LYS A 10  ? 0.1500 0.2224 0.1470 0.0595  -0.0077 0.0141  101 LYS A C   
46   O O   . LYS A 10  ? 0.1476 0.2092 0.1530 0.0505  -0.0166 0.0115  101 LYS A O   
47   C CB  . LYS A 10  ? 0.1861 0.3029 0.2234 0.0478  0.0074  0.0351  101 LYS A CB  
48   C CG  . LYS A 10  ? 0.2748 0.4062 0.3244 0.0621  0.0096  0.0295  101 LYS A CG  
49   C CD  . LYS A 10  ? 0.3373 0.5078 0.4228 0.0611  0.0192  0.0436  101 LYS A CD  
50   C CE  . LYS A 10  ? 0.3338 0.5200 0.4416 0.0756  0.0188  0.0422  101 LYS A CE  
51   N NZ  . LYS A 10  ? 0.4244 0.5821 0.5043 0.0941  0.0220  0.0262  101 LYS A NZ  
52   N N   . THR A 11  ? 0.1489 0.2153 0.1279 0.0720  -0.0072 0.0041  102 THR A N   
53   C CA  . THR A 11  ? 0.1367 0.1867 0.1116 0.0742  -0.0188 -0.0089 102 THR A CA  
54   C C   . THR A 11  ? 0.1270 0.1809 0.1244 0.0714  -0.0219 -0.0105 102 THR A C   
55   O O   . THR A 11  ? 0.1179 0.1877 0.1297 0.0764  -0.0153 -0.0064 102 THR A O   
56   C CB  . THR A 11  ? 0.2039 0.2434 0.1532 0.0851  -0.0171 -0.0205 102 THR A CB  
57   O OG1 . THR A 11  ? 0.2688 0.3040 0.1899 0.0855  -0.0181 -0.0179 102 THR A OG1 
58   C CG2 . THR A 11  ? 0.2206 0.2430 0.1693 0.0839  -0.0291 -0.0330 102 THR A CG2 
59   N N   . TYR A 12  ? 0.1173 0.1585 0.1186 0.0641  -0.0314 -0.0146 103 TYR A N   
60   C CA  . TYR A 12  ? 0.1044 0.1453 0.1187 0.0580  -0.0349 -0.0141 103 TYR A CA  
61   C C   . TYR A 12  ? 0.0956 0.1163 0.1037 0.0532  -0.0389 -0.0221 103 TYR A C   
62   O O   . TYR A 12  ? 0.1037 0.1168 0.1116 0.0478  -0.0410 -0.0231 103 TYR A O   
63   C CB  . TYR A 12  ? 0.0909 0.1385 0.1140 0.0451  -0.0369 -0.0064 103 TYR A CB  
64   C CG  . TYR A 12  ? 0.1143 0.1603 0.1419 0.0368  -0.0440 -0.0057 103 TYR A CG  
65   C CD1 . TYR A 12  ? 0.1400 0.2017 0.1802 0.0416  -0.0468 0.0002  103 TYR A CD1 
66   C CD2 . TYR A 12  ? 0.1737 0.2012 0.1909 0.0248  -0.0464 -0.0095 103 TYR A CD2 
67   C CE1 . TYR A 12  ? 0.1963 0.2566 0.2361 0.0330  -0.0555 0.0042  103 TYR A CE1 
68   C CE2 . TYR A 12  ? 0.2204 0.2438 0.2321 0.0156  -0.0529 -0.0087 103 TYR A CE2 
69   C CZ  . TYR A 12  ? 0.2884 0.3293 0.3105 0.0194  -0.0599 -0.0011 103 TYR A CZ  
70   O OH  . TYR A 12  ? 0.4212 0.4581 0.4336 0.0097  -0.0691 0.0026  103 TYR A OH  
71   N N   . GLN A 13  ? 0.1021 0.1150 0.1082 0.0571  -0.0394 -0.0269 104 GLN A N   
72   C CA  . GLN A 13  ? 0.1276 0.1252 0.1318 0.0525  -0.0441 -0.0331 104 GLN A CA  
73   C C   . GLN A 13  ? 0.1310 0.1252 0.1409 0.0455  -0.0458 -0.0292 104 GLN A C   
74   O O   . GLN A 13  ? 0.1742 0.1600 0.1865 0.0417  -0.0475 -0.0325 104 GLN A O   
75   C CB  . GLN A 13  ? 0.1300 0.1157 0.1296 0.0584  -0.0457 -0.0391 104 GLN A CB  
76   C CG  . GLN A 13  ? 0.1636 0.1440 0.1495 0.0658  -0.0479 -0.0483 104 GLN A CG  
77   C CD  . GLN A 13  ? 0.3271 0.2874 0.3070 0.0635  -0.0522 -0.0568 104 GLN A CD  
78   O OE1 . GLN A 13  ? 0.3511 0.3022 0.3400 0.0575  -0.0528 -0.0547 104 GLN A OE1 
79   N NE2 . GLN A 13  ? 0.3419 0.2932 0.3036 0.0658  -0.0541 -0.0655 104 GLN A NE2 
80   N N   . GLY A 14  ? 0.1593 0.1619 0.1724 0.0445  -0.0471 -0.0217 105 GLY A N   
81   C CA  . GLY A 14  ? 0.1304 0.1278 0.1390 0.0361  -0.0525 -0.0184 105 GLY A CA  
82   C C   . GLY A 14  ? 0.1510 0.1332 0.1554 0.0361  -0.0537 -0.0180 105 GLY A C   
83   O O   . GLY A 14  ? 0.1946 0.1692 0.2037 0.0444  -0.0535 -0.0209 105 GLY A O   
84   N N   . SER A 15  ? 0.1454 0.1186 0.1364 0.0250  -0.0537 -0.0149 106 SER A N   
85   C CA  A SER A 15  ? 0.2136 0.1716 0.1967 0.0228  -0.0538 -0.0105 106 SER A CA  
86   C CA  B SER A 15  ? 0.2122 0.1704 0.1958 0.0233  -0.0539 -0.0104 106 SER A CA  
87   C C   . SER A 15  ? 0.2439 0.1890 0.2337 0.0228  -0.0462 -0.0174 106 SER A C   
88   O O   . SER A 15  ? 0.2207 0.1520 0.2100 0.0226  -0.0459 -0.0137 106 SER A O   
89   C CB  A SER A 15  ? 0.2403 0.1899 0.1987 0.0091  -0.0539 -0.0059 106 SER A CB  
90   C CB  B SER A 15  ? 0.2437 0.1942 0.2029 0.0099  -0.0551 -0.0048 106 SER A CB  
91   O OG  A SER A 15  ? 0.2062 0.1702 0.1591 0.0043  -0.0650 0.0006  106 SER A OG  
92   O OG  B SER A 15  ? 0.2620 0.2041 0.2095 0.0010  -0.0450 -0.0137 106 SER A OG  
93   N N   . TYR A 16  ? 0.1769 0.1268 0.1755 0.0219  -0.0408 -0.0253 107 TYR A N   
94   C CA  . TYR A 16  ? 0.1243 0.0702 0.1367 0.0195  -0.0359 -0.0296 107 TYR A CA  
95   C C   . TYR A 16  ? 0.1190 0.0689 0.1437 0.0255  -0.0437 -0.0357 107 TYR A C   
96   O O   . TYR A 16  ? 0.1684 0.1182 0.2072 0.0208  -0.0443 -0.0390 107 TYR A O   
97   C CB  . TYR A 16  ? 0.1206 0.0714 0.1399 0.0161  -0.0253 -0.0319 107 TYR A CB  
98   C CG  . TYR A 16  ? 0.2215 0.1598 0.2188 0.0087  -0.0147 -0.0296 107 TYR A CG  
99   C CD1 . TYR A 16  ? 0.2483 0.1749 0.2375 0.0015  -0.0056 -0.0257 107 TYR A CD1 
100  C CD2 . TYR A 16  ? 0.2447 0.1793 0.2241 0.0066  -0.0139 -0.0314 107 TYR A CD2 
101  C CE1 . TYR A 16  ? 0.2260 0.1374 0.1848 -0.0064 0.0045  -0.0244 107 TYR A CE1 
102  C CE2 . TYR A 16  ? 0.2492 0.1667 0.1989 -0.0031 -0.0058 -0.0319 107 TYR A CE2 
103  C CZ  . TYR A 16  ? 0.2835 0.1893 0.2203 -0.0090 0.0036  -0.0287 107 TYR A CZ  
104  O OH  . TYR A 16  ? 0.3922 0.2776 0.2899 -0.0195 0.0127  -0.0299 107 TYR A OH  
105  N N   . GLY A 17  ? 0.1593 0.1130 0.1781 0.0345  -0.0493 -0.0372 108 GLY A N   
106  C CA  . GLY A 17  ? 0.1623 0.1174 0.1807 0.0378  -0.0535 -0.0431 108 GLY A CA  
107  C C   . GLY A 17  ? 0.1398 0.1061 0.1655 0.0373  -0.0580 -0.0478 108 GLY A C   
108  O O   . GLY A 17  ? 0.1251 0.0890 0.1554 0.0335  -0.0652 -0.0539 108 GLY A O   
109  N N   . PHE A 18  ? 0.1175 0.0956 0.1436 0.0396  -0.0547 -0.0437 109 PHE A N   
110  C CA  . PHE A 18  ? 0.1135 0.1031 0.1475 0.0401  -0.0571 -0.0425 109 PHE A CA  
111  C C   . PHE A 18  ? 0.1093 0.1011 0.1282 0.0448  -0.0625 -0.0451 109 PHE A C   
112  O O   . PHE A 18  ? 0.1336 0.1247 0.1382 0.0503  -0.0589 -0.0451 109 PHE A O   
113  C CB  . PHE A 18  ? 0.1107 0.1033 0.1453 0.0394  -0.0477 -0.0356 109 PHE A CB  
114  C CG  . PHE A 18  ? 0.1193 0.1201 0.1607 0.0418  -0.0475 -0.0301 109 PHE A CG  
115  C CD1 . PHE A 18  ? 0.0920 0.1006 0.1557 0.0419  -0.0477 -0.0272 109 PHE A CD1 
116  C CD2 . PHE A 18  ? 0.0950 0.0979 0.1248 0.0450  -0.0468 -0.0253 109 PHE A CD2 
117  C CE1 . PHE A 18  ? 0.1303 0.1479 0.2027 0.0461  -0.0480 -0.0183 109 PHE A CE1 
118  C CE2 . PHE A 18  ? 0.1234 0.1318 0.1595 0.0488  -0.0477 -0.0171 109 PHE A CE2 
119  C CZ  . PHE A 18  ? 0.1472 0.1629 0.2041 0.0498  -0.0486 -0.0129 109 PHE A CZ  
120  N N   . ARG A 19  ? 0.0982 0.0802 0.0989 0.0201  -0.0217 -0.0132 110 ARG A N   
121  C CA  . ARG A 19  ? 0.1203 0.1113 0.1283 0.0188  -0.0199 -0.0158 110 ARG A CA  
122  C C   . ARG A 19  ? 0.1282 0.1222 0.1360 0.0142  -0.0168 -0.0147 110 ARG A C   
123  O O   . ARG A 19  ? 0.1341 0.1236 0.1385 0.0123  -0.0154 -0.0123 110 ARG A O   
124  C CB  . ARG A 19  ? 0.1147 0.1027 0.1244 0.0206  -0.0199 -0.0186 110 ARG A CB  
125  C CG  . ARG A 19  ? 0.1022 0.0820 0.1064 0.0183  -0.0184 -0.0180 110 ARG A CG  
126  C CD  . ARG A 19  ? 0.1675 0.1358 0.1649 0.0202  -0.0201 -0.0155 110 ARG A CD  
127  N NE  . ARG A 19  ? 0.1328 0.0929 0.1263 0.0181  -0.0183 -0.0155 110 ARG A NE  
128  C CZ  . ARG A 19  ? 0.2273 0.1756 0.2137 0.0186  -0.0187 -0.0132 110 ARG A CZ  
129  N NH1 . ARG A 19  ? 0.1955 0.1378 0.1759 0.0213  -0.0212 -0.0106 110 ARG A NH1 
130  N NH2 . ARG A 19  ? 0.1808 0.1220 0.1648 0.0161  -0.0167 -0.0134 110 ARG A NH2 
131  N N   . LEU A 20  ? 0.1412 0.1427 0.1531 0.0125  -0.0158 -0.0163 111 LEU A N   
132  C CA  . LEU A 20  ? 0.0861 0.0911 0.0988 0.0084  -0.0146 -0.0151 111 LEU A CA  
133  C C   . LEU A 20  ? 0.1229 0.1243 0.1335 0.0059  -0.0145 -0.0165 111 LEU A C   
134  O O   . LEU A 20  ? 0.1462 0.1432 0.1547 0.0074  -0.0145 -0.0192 111 LEU A O   
135  C CB  . LEU A 20  ? 0.0993 0.1124 0.1150 0.0075  -0.0144 -0.0155 111 LEU A CB  
136  C CG  . LEU A 20  ? 0.0673 0.0843 0.0857 0.0091  -0.0146 -0.0144 111 LEU A CG  
137  C CD1 . LEU A 20  ? 0.0872 0.1112 0.1082 0.0077  -0.0137 -0.0149 111 LEU A CD1 
138  C CD2 . LEU A 20  ? 0.0661 0.0815 0.0841 0.0083  -0.0141 -0.0112 111 LEU A CD2 
139  N N   . GLY A 21  ? 0.0821 0.0851 0.0941 0.0020  -0.0148 -0.0148 112 GLY A N   
140  C CA  . GLY A 21  ? 0.0873 0.0879 0.0977 -0.0014 -0.0159 -0.0163 112 GLY A CA  
141  C C   . GLY A 21  ? 0.1094 0.1159 0.1224 -0.0050 -0.0180 -0.0149 112 GLY A C   
142  O O   . GLY A 21  ? 0.0932 0.1050 0.1110 -0.0049 -0.0180 -0.0121 112 GLY A O   
143  N N   . PHE A 22  ? 0.1025 0.1070 0.1115 -0.0082 -0.0203 -0.0168 113 PHE A N   
144  C CA  . PHE A 22  ? 0.0911 0.0995 0.1010 -0.0119 -0.0240 -0.0152 113 PHE A CA  
145  C C   . PHE A 22  ? 0.1381 0.1426 0.1478 -0.0164 -0.0277 -0.0159 113 PHE A C   
146  O O   . PHE A 22  ? 0.1574 0.1549 0.1621 -0.0169 -0.0270 -0.0189 113 PHE A O   
147  C CB  . PHE A 22  ? 0.0941 0.1033 0.0963 -0.0119 -0.0240 -0.0169 113 PHE A CB  
148  C CG  . PHE A 22  ? 0.1148 0.1285 0.1192 -0.0082 -0.0206 -0.0163 113 PHE A CG  
149  C CD1 . PHE A 22  ? 0.0982 0.1100 0.1016 -0.0045 -0.0170 -0.0191 113 PHE A CD1 
150  C CD2 . PHE A 22  ? 0.1382 0.1576 0.1467 -0.0082 -0.0215 -0.0130 113 PHE A CD2 
151  C CE1 . PHE A 22  ? 0.0806 0.0969 0.0876 -0.0014 -0.0148 -0.0187 113 PHE A CE1 
152  C CE2 . PHE A 22  ? 0.1092 0.1323 0.1200 -0.0053 -0.0186 -0.0128 113 PHE A CE2 
153  C CZ  . PHE A 22  ? 0.1021 0.1238 0.1122 -0.0021 -0.0155 -0.0157 113 PHE A CZ  
154  N N   . LEU A 23  ? 0.1029 0.1119 0.1191 -0.0196 -0.0320 -0.0130 114 LEU A N   
155  C CA  . LEU A 23  ? 0.1255 0.1316 0.1427 -0.0246 -0.0372 -0.0136 114 LEU A CA  
156  C C   . LEU A 23  ? 0.1664 0.1662 0.1692 -0.0270 -0.0404 -0.0171 114 LEU A C   
157  O O   . LEU A 23  ? 0.1727 0.1719 0.1664 -0.0253 -0.0387 -0.0182 114 LEU A O   
158  C CB  . LEU A 23  ? 0.1020 0.1153 0.1316 -0.0271 -0.0422 -0.0095 114 LEU A CB  
159  C CG  . LEU A 23  ? 0.1773 0.1962 0.2220 -0.0253 -0.0381 -0.0062 114 LEU A CG  
160  C CD1 . LEU A 23  ? 0.2284 0.2548 0.2874 -0.0276 -0.0432 -0.0025 114 LEU A CD1 
161  C CD2 . LEU A 23  ? 0.1720 0.1861 0.2199 -0.0262 -0.0343 -0.0075 114 LEU A CD2 
162  N N   . HIS A 24  ? 0.1276 0.1217 0.1277 -0.0314 -0.0447 -0.0190 115 HIS A N   
163  C CA  . HIS A 24  ? 0.1432 0.1291 0.1273 -0.0346 -0.0480 -0.0227 115 HIS A CA  
164  C C   . HIS A 24  ? 0.1806 0.1684 0.1660 -0.0395 -0.0576 -0.0201 115 HIS A C   
165  O O   . HIS A 24  ? 0.2476 0.2335 0.2377 -0.0440 -0.0636 -0.0204 115 HIS A O   
166  C CB  . HIS A 24  ? 0.1782 0.1542 0.1560 -0.0360 -0.0464 -0.0274 115 HIS A CB  
167  C CG  . HIS A 24  ? 0.2044 0.1779 0.1810 -0.0306 -0.0380 -0.0296 115 HIS A CG  
168  N ND1 . HIS A 24  ? 0.2213 0.1976 0.2088 -0.0276 -0.0344 -0.0275 115 HIS A ND1 
169  C CD2 . HIS A 24  ? 0.2157 0.1843 0.1822 -0.0274 -0.0328 -0.0334 115 HIS A CD2 
170  C CE1 . HIS A 24  ? 0.2347 0.2077 0.2186 -0.0227 -0.0287 -0.0297 115 HIS A CE1 
171  N NE2 . HIS A 24  ? 0.1993 0.1685 0.1721 -0.0224 -0.0274 -0.0334 115 HIS A NE2 
172  N N   . SER A 25  ? 0.1777 0.1689 0.1594 -0.0388 -0.0597 -0.0175 116 SER A N   
173  C CA  . SER A 25  ? 0.2122 0.2066 0.1979 -0.0424 -0.0694 -0.0137 116 SER A CA  
174  C C   . SER A 25  ? 0.2419 0.2267 0.2085 -0.0460 -0.0747 -0.0154 116 SER A C   
175  O O   . SER A 25  ? 0.2399 0.2265 0.2096 -0.0473 -0.0810 -0.0119 116 SER A O   
176  C CB  . SER A 25  ? 0.2059 0.2089 0.1995 -0.0389 -0.0682 -0.0089 116 SER A CB  
177  O OG  . SER A 25  ? 0.2443 0.2554 0.2554 -0.0352 -0.0624 -0.0072 116 SER A OG  
178  N N   . GLY A 26  ? 0.1950 0.1693 0.1423 -0.0468 -0.0707 -0.0206 117 GLY A N   
179  C CA  . GLY A 26  ? 0.2179 0.1820 0.1459 -0.0496 -0.0732 -0.0223 117 GLY A CA  
180  C C   . GLY A 26  ? 0.2084 0.1717 0.1259 -0.0488 -0.0734 -0.0193 117 GLY A C   
181  O O   . GLY A 26  ? 0.1993 0.1699 0.1238 -0.0461 -0.0710 -0.0163 117 GLY A O   
182  N N   . THR A 27  ? 0.2293 0.1823 0.1288 -0.0516 -0.0760 -0.0200 118 THR A N   
183  C CA  . THR A 27  ? 0.3011 0.2500 0.1868 -0.0516 -0.0754 -0.0174 118 THR A CA  
184  C C   . THR A 27  ? 0.3430 0.2880 0.2241 -0.0543 -0.0850 -0.0131 118 THR A C   
185  O O   . THR A 27  ? 0.3443 0.2804 0.2072 -0.0557 -0.0848 -0.0121 118 THR A O   
186  C CB  . THR A 27  ? 0.2997 0.2369 0.1630 -0.0522 -0.0664 -0.0227 118 THR A CB  
187  O OG1 . THR A 27  ? 0.3699 0.2961 0.2205 -0.0553 -0.0680 -0.0265 118 THR A OG1 
188  C CG2 . THR A 27  ? 0.3233 0.2643 0.1922 -0.0491 -0.0569 -0.0270 118 THR A CG2 
189  N N   . ALA A 28  ? 0.3096 0.2607 0.2071 -0.0550 -0.0930 -0.0106 119 ALA A N   
190  C CA  . ALA A 28  ? 0.3579 0.3063 0.2540 -0.0572 -0.1030 -0.0062 119 ALA A CA  
191  C C   . ALA A 28  ? 0.3881 0.3389 0.2843 -0.0552 -0.1041 -0.0007 119 ALA A C   
192  O O   . ALA A 28  ? 0.3396 0.2987 0.2457 -0.0517 -0.0987 0.0008  119 ALA A O   
193  C CB  . ALA A 28  ? 0.3053 0.2624 0.2240 -0.0576 -0.1101 -0.0042 119 ALA A CB  
194  N N   . LYS A 29  ? 0.3796 0.3219 0.2638 -0.0576 -0.1115 0.0025  120 LYS A N   
195  C CA  . LYS A 29  ? 0.3986 0.3403 0.2796 -0.0562 -0.1129 0.0077  120 LYS A CA  
196  C C   . LYS A 29  ? 0.4143 0.3707 0.3223 -0.0523 -0.1146 0.0123  120 LYS A C   
197  O O   . LYS A 29  ? 0.4241 0.3833 0.3337 -0.0498 -0.1115 0.0153  120 LYS A O   
198  C CB  . LYS A 29  ? 0.4065 0.3363 0.2721 -0.0597 -0.1224 0.0106  120 LYS A CB  
199  N N   . SER A 30  ? 0.3800 0.3452 0.3093 -0.0518 -0.1187 0.0126  121 SER A N   
200  C CA  . SER A 30  ? 0.4288 0.4070 0.3845 -0.0481 -0.1195 0.0166  121 SER A CA  
201  C C   . SER A 30  ? 0.4093 0.3978 0.3786 -0.0446 -0.1099 0.0148  121 SER A C   
202  O O   . SER A 30  ? 0.3673 0.3655 0.3566 -0.0413 -0.1087 0.0179  121 SER A O   
203  C CB  . SER A 30  ? 0.4218 0.4045 0.3950 -0.0493 -0.1272 0.0178  121 SER A CB  
204  O OG  . SER A 30  ? 0.4917 0.4752 0.4670 -0.0512 -0.1249 0.0130  121 SER A OG  
205  N N   . VAL A 31  ? 0.3516 0.3375 0.3107 -0.0452 -0.1030 0.0097  122 VAL A N   
206  C CA  . VAL A 31  ? 0.2705 0.2654 0.2429 -0.0422 -0.0951 0.0080  122 VAL A CA  
207  C C   . VAL A 31  ? 0.2480 0.2482 0.2253 -0.0387 -0.0914 0.0115  122 VAL A C   
208  O O   . VAL A 31  ? 0.3327 0.3267 0.2947 -0.0391 -0.0915 0.0130  122 VAL A O   
209  C CB  . VAL A 31  ? 0.2726 0.2621 0.2315 -0.0435 -0.0890 0.0020  122 VAL A CB  
210  C CG1 . VAL A 31  ? 0.3068 0.2894 0.2455 -0.0435 -0.0838 0.0005  122 VAL A CG1 
211  C CG2 . VAL A 31  ? 0.3359 0.3339 0.3113 -0.0414 -0.0834 0.0001  122 VAL A CG2 
212  N N   . THR A 32  ? 0.2625 0.2733 0.2608 -0.0353 -0.0878 0.0129  123 THR A N   
213  C CA  . THR A 32  ? 0.2411 0.2568 0.2456 -0.0319 -0.0841 0.0160  123 THR A CA  
214  C C   . THR A 32  ? 0.1903 0.2084 0.1918 -0.0304 -0.0761 0.0132  123 THR A C   
215  O O   . THR A 32  ? 0.2024 0.2225 0.2033 -0.0284 -0.0732 0.0153  123 THR A O   
216  C CB  . THR A 32  ? 0.2839 0.3088 0.3129 -0.0288 -0.0840 0.0193  123 THR A CB  
217  O OG1 . THR A 32  ? 0.2224 0.2527 0.2644 -0.0285 -0.0801 0.0167  123 THR A OG1 
218  C CG2 . THR A 32  ? 0.2883 0.3113 0.3219 -0.0300 -0.0925 0.0228  123 THR A CG2 
219  N N   . CYS A 33  ? 0.1780 0.1956 0.1778 -0.0314 -0.0730 0.0087  124 CYS A N   
220  C CA  . CYS A 33  ? 0.1426 0.1612 0.1400 -0.0286 -0.0631 0.0053  124 CYS A CA  
221  C C   . CYS A 33  ? 0.1637 0.1759 0.1504 -0.0305 -0.0609 -0.0001 124 CYS A C   
222  O O   . CYS A 33  ? 0.1477 0.1592 0.1392 -0.0329 -0.0654 -0.0011 124 CYS A O   
223  C CB  . CYS A 33  ? 0.1511 0.1785 0.1681 -0.0247 -0.0580 0.0064  124 CYS A CB  
224  S SG  . CYS A 33  ? 0.2167 0.2447 0.2315 -0.0206 -0.0465 0.0026  124 CYS A SG  
225  N N   . THR A 34  ? 0.1466 0.1538 0.1198 -0.0295 -0.0540 -0.0037 125 THR A N   
226  C CA  . THR A 34  ? 0.1651 0.1655 0.1289 -0.0308 -0.0512 -0.0092 125 THR A CA  
227  C C   . THR A 34  ? 0.1459 0.1459 0.1058 -0.0272 -0.0411 -0.0127 125 THR A C   
228  O O   . THR A 34  ? 0.1566 0.1576 0.1126 -0.0260 -0.0374 -0.0116 125 THR A O   
229  C CB  . THR A 34  ? 0.2489 0.2386 0.1940 -0.0360 -0.0572 -0.0108 125 THR A CB  
230  O OG1 . THR A 34  ? 0.2378 0.2205 0.1755 -0.0370 -0.0541 -0.0165 125 THR A OG1 
231  C CG2 . THR A 34  ? 0.2125 0.1961 0.1403 -0.0369 -0.0547 -0.0105 125 THR A CG2 
232  N N   . TYR A 35  ? 0.1326 0.1310 0.0948 -0.0256 -0.0369 -0.0166 126 TYR A N   
233  C CA  . TYR A 35  ? 0.1271 0.1266 0.0905 -0.0214 -0.0284 -0.0196 126 TYR A CA  
234  C C   . TYR A 35  ? 0.1475 0.1379 0.0982 -0.0223 -0.0245 -0.0252 126 TYR A C   
235  O O   . TYR A 35  ? 0.1483 0.1325 0.0948 -0.0246 -0.0273 -0.0276 126 TYR A O   
236  C CB  . TYR A 35  ? 0.1136 0.1184 0.0915 -0.0177 -0.0266 -0.0191 126 TYR A CB  
237  C CG  . TYR A 35  ? 0.1160 0.1209 0.0953 -0.0133 -0.0197 -0.0223 126 TYR A CG  
238  C CD1 . TYR A 35  ? 0.1039 0.1139 0.0866 -0.0108 -0.0159 -0.0216 126 TYR A CD1 
239  C CD2 . TYR A 35  ? 0.1142 0.1139 0.0924 -0.0119 -0.0175 -0.0261 126 TYR A CD2 
240  C CE1 . TYR A 35  ? 0.1143 0.1253 0.1007 -0.0069 -0.0107 -0.0245 126 TYR A CE1 
241  C CE2 . TYR A 35  ? 0.1120 0.1119 0.0933 -0.0076 -0.0121 -0.0288 126 TYR A CE2 
242  C CZ  . TYR A 35  ? 0.1053 0.1114 0.0914 -0.0051 -0.0091 -0.0281 126 TYR A CZ  
243  O OH  . TYR A 35  ? 0.1209 0.1283 0.1128 -0.0008 -0.0048 -0.0307 126 TYR A OH  
244  N N   . SER A 36  ? 0.1701 0.1593 0.1155 -0.0206 -0.0175 -0.0277 127 SER A N   
245  C CA  . SER A 36  ? 0.1564 0.1371 0.0914 -0.0207 -0.0116 -0.0335 127 SER A CA  
246  C C   . SER A 36  ? 0.1473 0.1317 0.0942 -0.0153 -0.0056 -0.0362 127 SER A C   
247  O O   . SER A 36  ? 0.1391 0.1301 0.0940 -0.0121 -0.0011 -0.0358 127 SER A O   
248  C CB  . SER A 36  ? 0.1688 0.1448 0.0902 -0.0228 -0.0066 -0.0347 127 SER A CB  
249  O OG  . SER A 36  ? 0.2158 0.1845 0.1300 -0.0220 0.0015  -0.0409 127 SER A OG  
250  N N   . PRO A 37  ? 0.1581 0.1381 0.1067 -0.0141 -0.0060 -0.0390 128 PRO A N   
251  C CA  . PRO A 37  ? 0.1756 0.1572 0.1342 -0.0087 -0.0007 -0.0417 128 PRO A CA  
252  C C   . PRO A 37  ? 0.1796 0.1591 0.1353 -0.0069 0.0079  -0.0462 128 PRO A C   
253  O O   . PRO A 37  ? 0.1995 0.1851 0.1674 -0.0023 0.0118  -0.0468 128 PRO A O   
254  C CB  . PRO A 37  ? 0.2016 0.1757 0.1587 -0.0089 -0.0029 -0.0438 128 PRO A CB  
255  C CG  . PRO A 37  ? 0.2216 0.1947 0.1748 -0.0139 -0.0105 -0.0406 128 PRO A CG  
256  C CD  . PRO A 37  ? 0.1564 0.1300 0.1000 -0.0177 -0.0119 -0.0392 128 PRO A CD  
257  N N   . ALA A 38  ? 0.2072 0.1775 0.1470 -0.0107 0.0110  -0.0496 129 ALA A N   
258  C CA  . ALA A 38  ? 0.1784 0.1456 0.1154 -0.0093 0.0210  -0.0544 129 ALA A CA  
259  C C   . ALA A 38  ? 0.2642 0.2403 0.2081 -0.0083 0.0250  -0.0521 129 ALA A C   
260  O O   . ALA A 38  ? 0.2608 0.2406 0.2146 -0.0048 0.0327  -0.0550 129 ALA A O   
261  C CB  . ALA A 38  ? 0.2012 0.1545 0.1160 -0.0143 0.0239  -0.0584 129 ALA A CB  
262  N N   . LEU A 39  ? 0.2442 0.2242 0.1849 -0.0114 0.0196  -0.0470 130 LEU A N   
263  C CA  . LEU A 39  ? 0.2300 0.2175 0.1764 -0.0111 0.0229  -0.0445 130 LEU A CA  
264  C C   . LEU A 39  ? 0.2408 0.2402 0.2058 -0.0073 0.0187  -0.0406 130 LEU A C   
265  O O   . LEU A 39  ? 0.2186 0.2247 0.1907 -0.0068 0.0213  -0.0389 130 LEU A O   
266  C CB  . LEU A 39  ? 0.2025 0.1854 0.1328 -0.0166 0.0199  -0.0409 130 LEU A CB  
267  C CG  . LEU A 39  ? 0.2408 0.2095 0.1481 -0.0213 0.0232  -0.0443 130 LEU A CG  
268  C CD1 . LEU A 39  ? 0.3100 0.2733 0.2011 -0.0267 0.0165  -0.0397 130 LEU A CD1 
269  C CD2 . LEU A 39  ? 0.2935 0.2593 0.1985 -0.0207 0.0362  -0.0489 130 LEU A CD2 
270  N N   . ASN A 40  ? 0.1533 0.1543 0.1254 -0.0050 0.0129  -0.0395 131 ASN A N   
271  C CA  . ASN A 40  ? 0.1207 0.1301 0.1052 -0.0027 0.0076  -0.0352 131 ASN A CA  
272  C C   . ASN A 40  ? 0.1225 0.1357 0.1048 -0.0055 0.0050  -0.0306 131 ASN A C   
273  O O   . ASN A 40  ? 0.1431 0.1633 0.1345 -0.0040 0.0057  -0.0287 131 ASN A O   
274  C CB  . ASN A 40  ? 0.1323 0.1481 0.1320 0.0024  0.0104  -0.0367 131 ASN A CB  
275  C CG  . ASN A 40  ? 0.1622 0.1836 0.1712 0.0047  0.0047  -0.0328 131 ASN A CG  
276  O OD1 . ASN A 40  ? 0.1192 0.1386 0.1250 0.0035  -0.0002 -0.0301 131 ASN A OD1 
277  N ND2 . ASN A 40  ? 0.0865 0.1145 0.1068 0.0075  0.0056  -0.0326 131 ASN A ND2 
278  N N   . LYS A 41  ? 0.1227 0.1308 0.0931 -0.0098 0.0013  -0.0288 132 LYS A N   
279  C CA  . LYS A 41  ? 0.1623 0.1720 0.1286 -0.0126 -0.0010 -0.0245 132 LYS A CA  
280  C C   . LYS A 41  ? 0.1815 0.1899 0.1452 -0.0151 -0.0095 -0.0207 132 LYS A C   
281  O O   . LYS A 41  ? 0.1390 0.1409 0.0940 -0.0177 -0.0127 -0.0220 132 LYS A O   
282  C CB  . LYS A 41  ? 0.1376 0.1407 0.0895 -0.0160 0.0041  -0.0262 132 LYS A CB  
283  C CG  . LYS A 41  ? 0.1367 0.1401 0.0836 -0.0187 0.0024  -0.0215 132 LYS A CG  
284  C CD  . LYS A 41  ? 0.1534 0.1493 0.0857 -0.0218 0.0097  -0.0235 132 LYS A CD  
285  C CE  . LYS A 41  ? 0.2076 0.2028 0.1348 -0.0244 0.0086  -0.0186 132 LYS A CE  
286  N NZ  . LYS A 41  ? 0.2483 0.2374 0.1646 -0.0269 0.0184  -0.0207 132 LYS A NZ  
287  N N   . LEU A 42  ? 0.1476 0.1621 0.1200 -0.0144 -0.0129 -0.0162 133 LEU A N   
288  C CA  . LEU A 42  ? 0.1285 0.1434 0.1023 -0.0164 -0.0204 -0.0122 133 LEU A CA  
289  C C   . LEU A 42  ? 0.1480 0.1600 0.1125 -0.0196 -0.0233 -0.0088 133 LEU A C   
290  O O   . LEU A 42  ? 0.1495 0.1631 0.1139 -0.0191 -0.0198 -0.0075 133 LEU A O   
291  C CB  . LEU A 42  ? 0.1204 0.1427 0.1092 -0.0134 -0.0216 -0.0093 133 LEU A CB  
292  C CG  . LEU A 42  ? 0.1598 0.1840 0.1549 -0.0148 -0.0281 -0.0054 133 LEU A CG  
293  C CD1 . LEU A 42  ? 0.1656 0.1874 0.1621 -0.0158 -0.0305 -0.0071 133 LEU A CD1 
294  C CD2 . LEU A 42  ? 0.1915 0.2218 0.1992 -0.0119 -0.0270 -0.0025 133 LEU A CD2 
295  N N   . PHE A 43  ? 0.1376 0.1444 0.0942 -0.0231 -0.0302 -0.0074 134 PHE A N   
296  C CA  . PHE A 43  ? 0.1414 0.1436 0.0877 -0.0264 -0.0353 -0.0035 134 PHE A CA  
297  C C   . PHE A 43  ? 0.1877 0.1947 0.1458 -0.0265 -0.0441 0.0015  134 PHE A C   
298  O O   . PHE A 43  ? 0.1785 0.1866 0.1427 -0.0272 -0.0487 0.0009  134 PHE A O   
299  C CB  . PHE A 43  ? 0.1685 0.1590 0.0943 -0.0309 -0.0378 -0.0058 134 PHE A CB  
300  C CG  . PHE A 43  ? 0.2133 0.1978 0.1270 -0.0311 -0.0283 -0.0111 134 PHE A CG  
301  C CD1 . PHE A 43  ? 0.1635 0.1492 0.0824 -0.0288 -0.0229 -0.0163 134 PHE A CD1 
302  C CD2 . PHE A 43  ? 0.1955 0.1722 0.0926 -0.0337 -0.0242 -0.0108 134 PHE A CD2 
303  C CE1 . PHE A 43  ? 0.2172 0.1977 0.1274 -0.0286 -0.0136 -0.0214 134 PHE A CE1 
304  C CE2 . PHE A 43  ? 0.1928 0.1640 0.0803 -0.0340 -0.0140 -0.0160 134 PHE A CE2 
305  C CZ  . PHE A 43  ? 0.2661 0.2397 0.1612 -0.0312 -0.0087 -0.0214 134 PHE A CZ  
306  N N   . CYS A 44  ? 0.1473 0.1569 0.1098 -0.0258 -0.0460 0.0062  135 CYS A N   
307  C CA  . CYS A 44  ? 0.1552 0.1703 0.1325 -0.0250 -0.0532 0.0106  135 CYS A CA  
308  C C   . CYS A 44  ? 0.1935 0.2061 0.1673 -0.0260 -0.0588 0.0162  135 CYS A C   
309  O O   . CYS A 44  ? 0.1701 0.1777 0.1320 -0.0268 -0.0553 0.0169  135 CYS A O   
310  C CB  . CYS A 44  ? 0.1574 0.1816 0.1533 -0.0208 -0.0483 0.0106  135 CYS A CB  
311  S SG  . CYS A 44  ? 0.1898 0.2161 0.1866 -0.0179 -0.0403 0.0109  135 CYS A SG  
312  N N   . GLN A 45  ? 0.2010 0.2169 0.1868 -0.0260 -0.0672 0.0202  136 GLN A N   
313  C CA  . GLN A 45  ? 0.2355 0.2498 0.2222 -0.0261 -0.0738 0.0262  136 GLN A CA  
314  C C   . GLN A 45  ? 0.2327 0.2542 0.2361 -0.0218 -0.0688 0.0285  136 GLN A C   
315  O O   . GLN A 45  ? 0.2093 0.2376 0.2257 -0.0190 -0.0625 0.0259  136 GLN A O   
316  C CB  . GLN A 45  ? 0.2043 0.2176 0.1984 -0.0266 -0.0814 0.0281  136 GLN A CB  
317  C CG  . GLN A 45  ? 0.2752 0.2787 0.2506 -0.0308 -0.0862 0.0262  136 GLN A CG  
318  C CD  . GLN A 45  ? 0.3695 0.3729 0.3539 -0.0315 -0.0940 0.0279  136 GLN A CD  
319  O OE1 . GLN A 45  ? 0.3592 0.3704 0.3648 -0.0289 -0.0950 0.0300  136 GLN A OE1 
320  N NE2 . GLN A 45  ? 0.4043 0.3982 0.3722 -0.0353 -0.0993 0.0269  136 GLN A NE2 
321  N N   . LEU A 46  ? 0.2114 0.2296 0.2126 -0.0215 -0.0721 0.0335  137 LEU A N   
322  C CA  . LEU A 46  ? 0.1192 0.1420 0.1337 -0.0177 -0.0676 0.0357  137 LEU A CA  
323  C C   . LEU A 46  ? 0.1131 0.1442 0.1513 -0.0145 -0.0686 0.0365  137 LEU A C   
324  O O   . LEU A 46  ? 0.1428 0.1731 0.1873 -0.0147 -0.0736 0.0379  137 LEU A O   
325  C CB  . LEU A 46  ? 0.1926 0.2084 0.1992 -0.0184 -0.0723 0.0414  137 LEU A CB  
326  C CG  . LEU A 46  ? 0.2385 0.2565 0.2565 -0.0149 -0.0683 0.0441  137 LEU A CG  
327  C CD1 . LEU A 46  ? 0.2586 0.2763 0.2701 -0.0148 -0.0573 0.0402  137 LEU A CD1 
328  C CD2 . LEU A 46  ? 0.2284 0.2387 0.2404 -0.0156 -0.0757 0.0509  137 LEU A CD2 
329  N N   . ALA A 47  ? 0.0936 0.1305 0.1430 -0.0115 -0.0606 0.0343  138 ALA A N   
330  C CA  . ALA A 47  ? 0.1471 0.1896 0.2167 -0.0083 -0.0579 0.0345  138 ALA A CA  
331  C C   . ALA A 47  ? 0.2242 0.2689 0.3005 -0.0092 -0.0592 0.0322  138 ALA A C   
332  O O   . ALA A 47  ? 0.2878 0.3349 0.3788 -0.0077 -0.0588 0.0332  138 ALA A O   
333  C CB  . ALA A 47  ? 0.1328 0.1736 0.2110 -0.0063 -0.0606 0.0389  138 ALA A CB  
334  N N   . LYS A 48  ? 0.1714 0.2148 0.2373 -0.0120 -0.0605 0.0293  139 LYS A N   
335  C CA  . LYS A 48  ? 0.1720 0.2169 0.2436 -0.0134 -0.0618 0.0271  139 LYS A CA  
336  C C   . LYS A 48  ? 0.1357 0.1839 0.2102 -0.0128 -0.0550 0.0232  139 LYS A C   
337  O O   . LYS A 48  ? 0.1431 0.1914 0.2111 -0.0120 -0.0506 0.0216  139 LYS A O   
338  C CB  . LYS A 48  ? 0.1835 0.2228 0.2407 -0.0174 -0.0691 0.0265  139 LYS A CB  
339  C CG  . LYS A 48  ? 0.3405 0.3752 0.3943 -0.0185 -0.0770 0.0305  139 LYS A CG  
340  C CD  . LYS A 48  ? 0.4164 0.4552 0.4900 -0.0167 -0.0789 0.0328  139 LYS A CD  
341  C CE  . LYS A 48  ? 0.5408 0.5746 0.6112 -0.0181 -0.0883 0.0367  139 LYS A CE  
342  N NZ  . LYS A 48  ? 0.6277 0.6551 0.6822 -0.0223 -0.0947 0.0352  139 LYS A NZ  
343  N N   . THR A 49  ? 0.1231 0.1736 0.2074 -0.0133 -0.0541 0.0219  140 THR A N   
344  C CA  . THR A 49  ? 0.1175 0.1700 0.2052 -0.0129 -0.0478 0.0188  140 THR A CA  
345  C C   . THR A 49  ? 0.1486 0.1974 0.2207 -0.0149 -0.0482 0.0154  140 THR A C   
346  O O   . THR A 49  ? 0.1606 0.2063 0.2249 -0.0182 -0.0541 0.0145  140 THR A O   
347  C CB  . THR A 49  ? 0.1036 0.1581 0.2042 -0.0139 -0.0473 0.0185  140 THR A CB  
348  O OG1 . THR A 49  ? 0.0987 0.1557 0.2135 -0.0119 -0.0461 0.0213  140 THR A OG1 
349  C CG2 . THR A 49  ? 0.1347 0.1902 0.2389 -0.0136 -0.0403 0.0159  140 THR A CG2 
350  N N   . CYS A 50  ? 0.0946 0.1416 0.1600 -0.0125 -0.0405 0.0127  141 CYS A N   
351  C CA  . CYS A 50  ? 0.1165 0.1589 0.1680 -0.0130 -0.0379 0.0085  141 CYS A CA  
352  C C   . CYS A 50  ? 0.1160 0.1578 0.1712 -0.0115 -0.0321 0.0062  141 CYS A C   
353  O O   . CYS A 50  ? 0.1056 0.1473 0.1613 -0.0086 -0.0266 0.0058  141 CYS A O   
354  C CB  . CYS A 50  ? 0.1302 0.1708 0.1710 -0.0114 -0.0348 0.0075  141 CYS A CB  
355  S SG  . CYS A 50  ? 0.1798 0.2186 0.2129 -0.0134 -0.0402 0.0105  141 CYS A SG  
356  N N   . PRO A 51  ? 0.1003 0.1403 0.1571 -0.0137 -0.0335 0.0049  142 PRO A N   
357  C CA  . PRO A 51  ? 0.1239 0.1614 0.1822 -0.0125 -0.0278 0.0031  142 PRO A CA  
358  C C   . PRO A 51  ? 0.1381 0.1708 0.1836 -0.0105 -0.0248 -0.0003 142 PRO A C   
359  O O   . PRO A 51  ? 0.1221 0.1520 0.1585 -0.0117 -0.0271 -0.0026 142 PRO A O   
360  C CB  . PRO A 51  ? 0.1091 0.1455 0.1725 -0.0161 -0.0310 0.0027  142 PRO A CB  
361  C CG  . PRO A 51  ? 0.1249 0.1642 0.1909 -0.0191 -0.0394 0.0045  142 PRO A CG  
362  C CD  . PRO A 51  ? 0.1237 0.1626 0.1793 -0.0177 -0.0406 0.0048  142 PRO A CD  
363  N N   . VAL A 52  ? 0.0963 0.1273 0.1413 -0.0076 -0.0197 -0.0007 143 VAL A N   
364  C CA  . VAL A 52  ? 0.0666 0.0933 0.1024 -0.0053 -0.0175 -0.0035 143 VAL A CA  
365  C C   . VAL A 52  ? 0.1295 0.1509 0.1653 -0.0043 -0.0141 -0.0037 143 VAL A C   
366  O O   . VAL A 52  ? 0.1004 0.1213 0.1400 -0.0035 -0.0107 -0.0019 143 VAL A O   
367  C CB  . VAL A 52  ? 0.1168 0.1455 0.1500 -0.0026 -0.0161 -0.0037 143 VAL A CB  
368  C CG1 . VAL A 52  ? 0.1034 0.1284 0.1302 0.0000  -0.0148 -0.0066 143 VAL A CG1 
369  C CG2 . VAL A 52  ? 0.0976 0.1301 0.1296 -0.0040 -0.0188 -0.0032 143 VAL A CG2 
370  N N   . GLN A 53  ? 0.0896 0.1056 0.1200 -0.0045 -0.0144 -0.0059 144 GLN A N   
371  C CA  . GLN A 53  ? 0.0745 0.0835 0.1027 -0.0038 -0.0114 -0.0058 144 GLN A CA  
372  C C   . GLN A 53  ? 0.1031 0.1078 0.1241 0.0002  -0.0101 -0.0066 144 GLN A C   
373  O O   . GLN A 53  ? 0.1349 0.1413 0.1529 0.0022  -0.0120 -0.0085 144 GLN A O   
374  C CB  . GLN A 53  ? 0.0810 0.0847 0.1064 -0.0057 -0.0127 -0.0076 144 GLN A CB  
375  C CG  . GLN A 53  ? 0.1563 0.1630 0.1887 -0.0103 -0.0151 -0.0071 144 GLN A CG  
376  C CD  . GLN A 53  ? 0.1788 0.1794 0.2070 -0.0125 -0.0169 -0.0096 144 GLN A CD  
377  O OE1 . GLN A 53  ? 0.1225 0.1178 0.1423 -0.0102 -0.0167 -0.0123 144 GLN A OE1 
378  N NE2 . GLN A 53  ? 0.2034 0.2044 0.2382 -0.0169 -0.0187 -0.0090 144 GLN A NE2 
379  N N   . LEU A 54  ? 0.0863 0.0845 0.1043 0.0009  -0.0070 -0.0051 145 LEU A N   
380  C CA  . LEU A 54  ? 0.0850 0.0767 0.0946 0.0043  -0.0070 -0.0055 145 LEU A CA  
381  C C   . LEU A 54  ? 0.1106 0.0919 0.1136 0.0045  -0.0063 -0.0054 145 LEU A C   
382  O O   . LEU A 54  ? 0.1197 0.0963 0.1230 0.0020  -0.0026 -0.0037 145 LEU A O   
383  C CB  . LEU A 54  ? 0.0893 0.0793 0.0969 0.0049  -0.0039 -0.0036 145 LEU A CB  
384  C CG  . LEU A 54  ? 0.1208 0.1199 0.1358 0.0044  -0.0039 -0.0032 145 LEU A CG  
385  C CD1 . LEU A 54  ? 0.1435 0.1385 0.1556 0.0049  0.0002  -0.0019 145 LEU A CD1 
386  C CD2 . LEU A 54  ? 0.1202 0.1249 0.1354 0.0062  -0.0080 -0.0051 145 LEU A CD2 
387  N N   . TRP A 55  ? 0.1220 0.0996 0.1204 0.0074  -0.0095 -0.0071 146 TRP A N   
388  C CA  . TRP A 55  ? 0.1317 0.0982 0.1234 0.0083  -0.0097 -0.0070 146 TRP A CA  
389  C C   . TRP A 55  ? 0.1389 0.0979 0.1222 0.0124  -0.0124 -0.0063 146 TRP A C   
390  O O   . TRP A 55  ? 0.1120 0.0763 0.0975 0.0152  -0.0159 -0.0076 146 TRP A O   
391  C CB  . TRP A 55  ? 0.1153 0.0826 0.1096 0.0085  -0.0118 -0.0098 146 TRP A CB  
392  C CG  . TRP A 55  ? 0.1062 0.0779 0.1062 0.0041  -0.0105 -0.0105 146 TRP A CG  
393  C CD1 . TRP A 55  ? 0.1570 0.1386 0.1628 0.0022  -0.0116 -0.0116 146 TRP A CD1 
394  C CD2 . TRP A 55  ? 0.1772 0.1431 0.1774 0.0005  -0.0087 -0.0099 146 TRP A CD2 
395  N NE1 . TRP A 55  ? 0.1273 0.1095 0.1367 -0.0021 -0.0116 -0.0118 146 TRP A NE1 
396  C CE2 . TRP A 55  ? 0.1186 0.0918 0.1257 -0.0034 -0.0097 -0.0109 146 TRP A CE2 
397  C CE3 . TRP A 55  ? 0.1239 0.0782 0.1188 -0.0001 -0.0065 -0.0084 146 TRP A CE3 
398  C CZ2 . TRP A 55  ? 0.1138 0.0843 0.1244 -0.0080 -0.0092 -0.0108 146 TRP A CZ2 
399  C CZ3 . TRP A 55  ? 0.1272 0.0788 0.1257 -0.0048 -0.0048 -0.0083 146 TRP A CZ3 
400  C CH2 . TRP A 55  ? 0.1213 0.0814 0.1283 -0.0087 -0.0063 -0.0097 146 TRP A CH2 
401  N N   . VAL A 56  ? 0.1661 0.1122 0.1394 0.0124  -0.0111 -0.0041 147 VAL A N   
402  C CA  . VAL A 56  ? 0.1808 0.1169 0.1441 0.0162  -0.0154 -0.0031 147 VAL A CA  
403  C C   . VAL A 56  ? 0.2122 0.1349 0.1680 0.0165  -0.0152 -0.0018 147 VAL A C   
404  O O   . VAL A 56  ? 0.1786 0.0981 0.1348 0.0128  -0.0103 -0.0010 147 VAL A O   
405  C CB  . VAL A 56  ? 0.1892 0.1191 0.1422 0.0160  -0.0144 -0.0009 147 VAL A CB  
406  C CG1 . VAL A 56  ? 0.1814 0.1227 0.1410 0.0168  -0.0162 -0.0025 147 VAL A CG1 
407  C CG2 . VAL A 56  ? 0.1524 0.0764 0.1010 0.0118  -0.0063 0.0013  147 VAL A CG2 
408  N N   . ASP A 57  ? 0.1988 0.1139 0.1492 0.0208  -0.0211 -0.0015 148 ASP A N   
409  C CA  . ASP A 57  ? 0.2097 0.1091 0.1504 0.0217  -0.0218 0.0005  148 ASP A CA  
410  C C   . ASP A 57  ? 0.3019 0.1860 0.2254 0.0202  -0.0196 0.0045  148 ASP A C   
411  O O   . ASP A 57  ? 0.2682 0.1385 0.1826 0.0188  -0.0171 0.0068  148 ASP A O   
412  C CB  . ASP A 57  ? 0.2245 0.1210 0.1668 0.0276  -0.0297 -0.0004 148 ASP A CB  
413  C CG  . ASP A 57  ? 0.2757 0.1841 0.2333 0.0291  -0.0302 -0.0046 148 ASP A CG  
414  O OD1 . ASP A 57  ? 0.2730 0.1853 0.2354 0.0256  -0.0252 -0.0063 148 ASP A OD1 
415  O OD2 . ASP A 57  ? 0.2361 0.1494 0.2010 0.0338  -0.0355 -0.0064 148 ASP A OD2 
416  N N   . SER A 58  ? 0.2455 0.1301 0.1631 0.0202  -0.0202 0.0053  149 SER A N   
417  C CA  . SER A 58  ? 0.2936 0.1623 0.1927 0.0181  -0.0166 0.0086  149 SER A CA  
418  C C   . SER A 58  ? 0.2589 0.1342 0.1582 0.0160  -0.0127 0.0080  149 SER A C   
419  O O   . SER A 58  ? 0.2115 0.0996 0.1203 0.0177  -0.0166 0.0056  149 SER A O   
420  C CB  . SER A 58  ? 0.3985 0.2504 0.2804 0.0218  -0.0246 0.0112  149 SER A CB  
421  O OG  . SER A 58  ? 0.4471 0.3063 0.3339 0.0259  -0.0339 0.0095  149 SER A OG  
422  N N   . THR A 59  ? 0.2453 0.1113 0.1346 0.0122  -0.0041 0.0099  150 THR A N   
423  C CA  . THR A 59  ? 0.2223 0.0934 0.1130 0.0099  0.0020  0.0092  150 THR A CA  
424  C C   . THR A 59  ? 0.2677 0.1344 0.1469 0.0122  -0.0037 0.0088  150 THR A C   
425  O O   . THR A 59  ? 0.2399 0.0891 0.0988 0.0132  -0.0071 0.0108  150 THR A O   
426  C CB  . THR A 59  ? 0.2776 0.1370 0.1594 0.0056  0.0133  0.0114  150 THR A CB  
427  O OG1 . THR A 59  ? 0.2701 0.1363 0.1664 0.0029  0.0180  0.0114  150 THR A OG1 
428  C CG2 . THR A 59  ? 0.2404 0.1029 0.1228 0.0036  0.0206  0.0106  150 THR A CG2 
429  N N   . PRO A 60  ? 0.2402 0.1210 0.1307 0.0128  -0.0053 0.0064  151 PRO A N   
430  C CA  . PRO A 60  ? 0.2111 0.0872 0.0909 0.0142  -0.0104 0.0056  151 PRO A CA  
431  C C   . PRO A 60  ? 0.2417 0.1060 0.1067 0.0111  -0.0016 0.0064  151 PRO A C   
432  O O   . PRO A 60  ? 0.2598 0.1220 0.1264 0.0081  0.0092  0.0073  151 PRO A O   
433  C CB  . PRO A 60  ? 0.1947 0.0910 0.0944 0.0153  -0.0137 0.0027  151 PRO A CB  
434  C CG  . PRO A 60  ? 0.1917 0.1002 0.1078 0.0130  -0.0061 0.0024  151 PRO A CG  
435  C CD  . PRO A 60  ? 0.1924 0.0935 0.1055 0.0123  -0.0040 0.0041  151 PRO A CD  
436  N N   . PRO A 61  ? 0.2846 0.1404 0.1353 0.0117  -0.0055 0.0057  152 PRO A N   
437  C CA  . PRO A 61  ? 0.2553 0.0958 0.0875 0.0088  0.0034  0.0061  152 PRO A CA  
438  C C   . PRO A 61  ? 0.2528 0.1048 0.1000 0.0067  0.0143  0.0044  152 PRO A C   
439  O O   . PRO A 61  ? 0.2420 0.1131 0.1104 0.0076  0.0119  0.0027  152 PRO A O   
440  C CB  . PRO A 61  ? 0.2846 0.1154 0.1002 0.0101  -0.0060 0.0050  152 PRO A CB  
441  C CG  . PRO A 61  ? 0.2680 0.1008 0.0862 0.0136  -0.0197 0.0058  152 PRO A CG  
442  C CD  . PRO A 61  ? 0.2411 0.0953 0.0870 0.0148  -0.0190 0.0050  152 PRO A CD  
443  N N   . PRO A 62  ? 0.2914 0.1318 0.1282 0.0037  0.0266  0.0050  153 PRO A N   
444  C CA  . PRO A 62  ? 0.2598 0.1082 0.1084 0.0023  0.0362  0.0032  153 PRO A CA  
445  C C   . PRO A 62  ? 0.2666 0.1183 0.1136 0.0038  0.0300  0.0006  153 PRO A C   
446  O O   . PRO A 62  ? 0.2606 0.0987 0.0870 0.0043  0.0231  0.0000  153 PRO A O   
447  C CB  . PRO A 62  ? 0.3032 0.1323 0.1336 -0.0007 0.0497  0.0040  153 PRO A CB  
448  C CG  . PRO A 62  ? 0.3562 0.1700 0.1695 -0.0015 0.0483  0.0070  153 PRO A CG  
449  C CD  . PRO A 62  ? 0.3506 0.1674 0.1617 0.0018  0.0319  0.0074  153 PRO A CD  
450  N N   . GLY A 63  ? 0.2236 0.0923 0.0920 0.0041  0.0321  -0.0010 154 GLY A N   
451  C CA  . GLY A 63  ? 0.2178 0.0919 0.0885 0.0053  0.0262  -0.0034 154 GLY A CA  
452  C C   . GLY A 63  ? 0.2067 0.0975 0.0933 0.0074  0.0145  -0.0038 154 GLY A C   
453  O O   . GLY A 63  ? 0.1898 0.0881 0.0829 0.0080  0.0102  -0.0057 154 GLY A O   
454  N N   . THR A 64  ? 0.2050 0.1008 0.0974 0.0084  0.0101  -0.0023 155 THR A N   
455  C CA  . THR A 64  ? 0.1719 0.0846 0.0819 0.0102  0.0019  -0.0029 155 THR A CA  
456  C C   . THR A 64  ? 0.1830 0.1119 0.1136 0.0095  0.0065  -0.0034 155 THR A C   
457  O O   . THR A 64  ? 0.1512 0.0811 0.0876 0.0079  0.0153  -0.0024 155 THR A O   
458  C CB  . THR A 64  ? 0.1807 0.0938 0.0927 0.0112  -0.0013 -0.0014 155 THR A CB  
459  O OG1 . THR A 64  ? 0.1907 0.0871 0.0826 0.0121  -0.0062 -0.0004 155 THR A OG1 
460  C CG2 . THR A 64  ? 0.1532 0.0820 0.0818 0.0131  -0.0088 -0.0025 155 THR A CG2 
461  N N   . ARG A 65  ? 0.1485 0.0898 0.0906 0.0106  0.0005  -0.0048 156 ARG A N   
462  C CA  . ARG A 65  ? 0.1230 0.0784 0.0827 0.0099  0.0033  -0.0048 156 ARG A CA  
463  C C   . ARG A 65  ? 0.1284 0.0971 0.1008 0.0109  -0.0028 -0.0052 156 ARG A C   
464  O O   . ARG A 65  ? 0.1208 0.0887 0.0902 0.0123  -0.0093 -0.0060 156 ARG A O   
465  C CB  . ARG A 65  ? 0.1433 0.0984 0.1026 0.0096  0.0043  -0.0062 156 ARG A CB  
466  C CG  . ARG A 65  ? 0.1566 0.0972 0.1021 0.0087  0.0114  -0.0066 156 ARG A CG  
467  C CD  . ARG A 65  ? 0.1645 0.1084 0.1169 0.0083  0.0155  -0.0076 156 ARG A CD  
468  N NE  . ARG A 65  ? 0.1466 0.0918 0.0970 0.0085  0.0084  -0.0095 156 ARG A NE  
469  C CZ  . ARG A 65  ? 0.1651 0.1121 0.1201 0.0081  0.0103  -0.0106 156 ARG A CZ  
470  N NH1 . ARG A 65  ? 0.1570 0.1048 0.1194 0.0080  0.0188  -0.0099 156 ARG A NH1 
471  N NH2 . ARG A 65  ? 0.1420 0.0900 0.0957 0.0077  0.0035  -0.0125 156 ARG A NH2 
472  N N   . VAL A 66  ? 0.1207 0.1008 0.1071 0.0100  -0.0007 -0.0046 157 VAL A N   
473  C CA  A VAL A 66  ? 0.1115 0.1029 0.1082 0.0103  -0.0050 -0.0051 157 VAL A CA  
474  C CA  B VAL A 66  ? 0.1107 0.1021 0.1075 0.0103  -0.0049 -0.0050 157 VAL A CA  
475  C C   . VAL A 66  ? 0.1033 0.1033 0.1089 0.0097  -0.0051 -0.0052 157 VAL A C   
476  O O   . VAL A 66  ? 0.0912 0.0932 0.1023 0.0087  -0.0009 -0.0038 157 VAL A O   
477  C CB  A VAL A 66  ? 0.1127 0.1075 0.1151 0.0093  -0.0033 -0.0039 157 VAL A CB  
478  C CB  B VAL A 66  ? 0.1115 0.1065 0.1144 0.0092  -0.0030 -0.0038 157 VAL A CB  
479  C CG1 A VAL A 66  ? 0.1103 0.1040 0.1167 0.0077  0.0030  -0.0022 157 VAL A CG1 
480  C CG1 B VAL A 66  ? 0.0711 0.0756 0.0816 0.0092  -0.0069 -0.0047 157 VAL A CG1 
481  C CG2 A VAL A 66  ? 0.1051 0.1108 0.1171 0.0089  -0.0063 -0.0045 157 VAL A CG2 
482  C CG2 B VAL A 66  ? 0.1366 0.1218 0.1306 0.0094  -0.0020 -0.0034 157 VAL A CG2 
483  N N   . ARG A 67  ? 0.0792 0.0841 0.0873 0.0102  -0.0097 -0.0067 158 ARG A N   
484  C CA  . ARG A 67  ? 0.0654 0.0771 0.0805 0.0094  -0.0098 -0.0068 158 ARG A CA  
485  C C   . ARG A 67  ? 0.0824 0.1033 0.1052 0.0087  -0.0112 -0.0068 158 ARG A C   
486  O O   . ARG A 67  ? 0.0784 0.1007 0.1011 0.0096  -0.0135 -0.0081 158 ARG A O   
487  C CB  . ARG A 67  ? 0.0693 0.0786 0.0812 0.0098  -0.0132 -0.0087 158 ARG A CB  
488  C CG  . ARG A 67  ? 0.0648 0.0793 0.0831 0.0084  -0.0129 -0.0089 158 ARG A CG  
489  C CD  . ARG A 67  ? 0.0825 0.0941 0.0983 0.0083  -0.0170 -0.0112 158 ARG A CD  
490  N NE  . ARG A 67  ? 0.0968 0.0967 0.1005 0.0088  -0.0171 -0.0118 158 ARG A NE  
491  C CZ  . ARG A 67  ? 0.1581 0.1516 0.1570 0.0079  -0.0134 -0.0117 158 ARG A CZ  
492  N NH1 . ARG A 67  ? 0.1365 0.1347 0.1432 0.0069  -0.0100 -0.0107 158 ARG A NH1 
493  N NH2 . ARG A 67  ? 0.1382 0.1192 0.1237 0.0081  -0.0126 -0.0125 158 ARG A NH2 
494  N N   . ALA A 68  ? 0.0526 0.0785 0.0811 0.0073  -0.0097 -0.0053 159 ALA A N   
495  C CA  . ALA A 68  ? 0.0481 0.0807 0.0809 0.0062  -0.0107 -0.0052 159 ALA A CA  
496  C C   . ALA A 68  ? 0.0712 0.1068 0.1070 0.0052  -0.0107 -0.0053 159 ALA A C   
497  O O   . ALA A 68  ? 0.0631 0.0967 0.0997 0.0049  -0.0095 -0.0042 159 ALA A O   
498  C CB  . ALA A 68  ? 0.0506 0.0854 0.0862 0.0048  -0.0100 -0.0027 159 ALA A CB  
499  N N   . MET A 69  ? 0.0589 0.0986 0.0967 0.0046  -0.0113 -0.0069 160 MET A N   
500  C CA  . MET A 69  ? 0.0777 0.1204 0.1191 0.0030  -0.0105 -0.0071 160 MET A CA  
501  C C   . MET A 69  ? 0.0763 0.1230 0.1185 0.0015  -0.0090 -0.0074 160 MET A C   
502  O O   . MET A 69  ? 0.0715 0.1192 0.1132 0.0024  -0.0091 -0.0094 160 MET A O   
503  C CB  . MET A 69  ? 0.0652 0.1077 0.1091 0.0038  -0.0124 -0.0097 160 MET A CB  
504  C CG  . MET A 69  ? 0.1082 0.1543 0.1578 0.0016  -0.0113 -0.0103 160 MET A CG  
505  S SD  . MET A 69  ? 0.1321 0.1791 0.1874 0.0023  -0.0152 -0.0139 160 MET A SD  
506  C CE  . MET A 69  ? 0.1410 0.1788 0.1878 0.0031  -0.0178 -0.0134 160 MET A CE  
507  N N   . ALA A 70  ? 0.0605 0.1082 0.1028 -0.0008 -0.0072 -0.0056 161 ALA A N   
508  C CA  . ALA A 70  ? 0.0693 0.1186 0.1097 -0.0028 -0.0046 -0.0060 161 ALA A CA  
509  C C   . ALA A 70  ? 0.0640 0.1166 0.1103 -0.0039 -0.0020 -0.0083 161 ALA A C   
510  O O   . ALA A 70  ? 0.0892 0.1420 0.1398 -0.0045 -0.0023 -0.0079 161 ALA A O   
511  C CB  . ALA A 70  ? 0.0814 0.1281 0.1165 -0.0051 -0.0045 -0.0020 161 ALA A CB  
512  N N   . ILE A 71  ? 0.0521 0.1070 0.0996 -0.0043 0.0011  -0.0108 162 ILE A N   
513  C CA  . ILE A 71  ? 0.0537 0.1124 0.1086 -0.0060 0.0052  -0.0129 162 ILE A CA  
514  C C   . ILE A 71  ? 0.0649 0.1222 0.1139 -0.0084 0.0111  -0.0132 162 ILE A C   
515  O O   . ILE A 71  ? 0.0819 0.1364 0.1231 -0.0079 0.0111  -0.0136 162 ILE A O   
516  C CB  . ILE A 71  ? 0.0976 0.1614 0.1641 -0.0035 0.0038  -0.0169 162 ILE A CB  
517  C CG1 . ILE A 71  ? 0.1756 0.2396 0.2415 -0.0011 0.0046  -0.0193 162 ILE A CG1 
518  C CG2 . ILE A 71  ? 0.2125 0.2750 0.2809 -0.0013 -0.0025 -0.0166 162 ILE A CG2 
519  C CD1 . ILE A 71  ? 0.2565 0.3259 0.3361 0.0013  0.0040  -0.0231 162 ILE A CD1 
520  N N   . TYR A 72  ? 0.0790 0.1373 0.1307 -0.0115 0.0163  -0.0133 163 TYR A N   
521  C CA  . TYR A 72  ? 0.0892 0.1448 0.1341 -0.0141 0.0234  -0.0141 163 TYR A CA  
522  C C   . TYR A 72  ? 0.0752 0.1348 0.1279 -0.0120 0.0270  -0.0191 163 TYR A C   
523  O O   . TYR A 72  ? 0.0774 0.1437 0.1454 -0.0099 0.0260  -0.0218 163 TYR A O   
524  C CB  . TYR A 72  ? 0.0819 0.1364 0.1276 -0.0183 0.0294  -0.0128 163 TYR A CB  
525  C CG  . TYR A 72  ? 0.0880 0.1361 0.1230 -0.0204 0.0265  -0.0074 163 TYR A CG  
526  C CD1 . TYR A 72  ? 0.0948 0.1352 0.1132 -0.0217 0.0253  -0.0044 163 TYR A CD1 
527  C CD2 . TYR A 72  ? 0.0818 0.1309 0.1234 -0.0211 0.0243  -0.0055 163 TYR A CD2 
528  C CE1 . TYR A 72  ? 0.0991 0.1336 0.1092 -0.0231 0.0216  0.0009  163 TYR A CE1 
529  C CE2 . TYR A 72  ? 0.0860 0.1286 0.1189 -0.0224 0.0216  -0.0004 163 TYR A CE2 
530  C CZ  . TYR A 72  ? 0.0944 0.1302 0.1123 -0.0232 0.0201  0.0029  163 TYR A CZ  
531  O OH  . TYR A 72  ? 0.1365 0.1659 0.1470 -0.0241 0.0163  0.0083  163 TYR A OH  
532  N N   . LYS A 73  ? 0.1163 0.1711 0.1582 -0.0127 0.0307  -0.0203 164 LYS A N   
533  C CA  . LYS A 73  ? 0.1241 0.1811 0.1721 -0.0102 0.0344  -0.0251 164 LYS A CA  
534  C C   . LYS A 73  ? 0.1672 0.2284 0.2265 -0.0116 0.0440  -0.0285 164 LYS A C   
535  O O   . LYS A 73  ? 0.1426 0.2100 0.2174 -0.0085 0.0455  -0.0325 164 LYS A O   
536  C CB  . LYS A 73  ? 0.1529 0.2017 0.1840 -0.0109 0.0354  -0.0256 164 LYS A CB  
537  C CG  . LYS A 73  ? 0.2269 0.2759 0.2622 -0.0086 0.0407  -0.0309 164 LYS A CG  
538  C CD  . LYS A 73  ? 0.3110 0.3499 0.3269 -0.0104 0.0424  -0.0316 164 LYS A CD  
539  C CE  . LYS A 73  ? 0.3473 0.3849 0.3667 -0.0081 0.0486  -0.0373 164 LYS A CE  
540  N NZ  . LYS A 73  ? 0.3685 0.3946 0.3668 -0.0106 0.0499  -0.0383 164 LYS A NZ  
541  N N   . GLN A 74  ? 0.1413 0.1989 0.1939 -0.0163 0.0506  -0.0269 165 GLN A N   
542  C CA  . GLN A 74  ? 0.1221 0.1828 0.1848 -0.0183 0.0616  -0.0301 165 GLN A CA  
543  C C   . GLN A 74  ? 0.1457 0.2169 0.2315 -0.0179 0.0604  -0.0309 165 GLN A C   
544  O O   . GLN A 74  ? 0.1529 0.2252 0.2400 -0.0186 0.0538  -0.0277 165 GLN A O   
545  C CB  . GLN A 74  ? 0.1475 0.1989 0.1931 -0.0240 0.0699  -0.0279 165 GLN A CB  
546  C CG  . GLN A 74  ? 0.2142 0.2538 0.2359 -0.0254 0.0722  -0.0279 165 GLN A CG  
547  C CD  . GLN A 74  ? 0.2627 0.2912 0.2633 -0.0309 0.0750  -0.0234 165 GLN A CD  
548  O OE1 . GLN A 74  ? 0.2700 0.2966 0.2651 -0.0317 0.0671  -0.0182 165 GLN A OE1 
549  N NE2 . GLN A 74  ? 0.3419 0.3622 0.3306 -0.0347 0.0867  -0.0252 165 GLN A NE2 
550  N N   . SER A 75  ? 0.1278 0.2059 0.2320 -0.0168 0.0670  -0.0354 166 SER A N   
551  C CA  . SER A 75  ? 0.1450 0.2302 0.2688 -0.0155 0.0621  -0.0354 166 SER A CA  
552  C C   . SER A 75  ? 0.1639 0.2486 0.2876 -0.0202 0.0627  -0.0322 166 SER A C   
553  O O   . SER A 75  ? 0.1125 0.2013 0.2455 -0.0195 0.0545  -0.0311 166 SER A O   
554  C CB  . SER A 75  ? 0.1908 0.2778 0.3270 -0.0141 0.0681  -0.0386 166 SER A CB  
555  O OG  . SER A 75  ? 0.2238 0.3170 0.3778 -0.0143 0.0647  -0.0386 166 SER A OG  
556  N N   . GLN A 76  ? 0.1225 0.2006 0.2342 -0.0251 0.0722  -0.0307 167 GLN A N   
557  C CA  . GLN A 76  ? 0.1264 0.2031 0.2389 -0.0296 0.0736  -0.0277 167 GLN A CA  
558  C C   . GLN A 76  ? 0.1261 0.2005 0.2297 -0.0313 0.0674  -0.0239 167 GLN A C   
559  O O   . GLN A 76  ? 0.1479 0.2208 0.2531 -0.0346 0.0672  -0.0213 167 GLN A O   
560  C CB  . GLN A 76  ? 0.1519 0.2201 0.2525 -0.0343 0.0856  -0.0268 167 GLN A CB  
561  C CG  . GLN A 76  ? 0.2134 0.2703 0.2874 -0.0370 0.0898  -0.0243 167 GLN A CG  
562  C CD  . GLN A 76  ? 0.2729 0.3258 0.3382 -0.0350 0.0948  -0.0277 167 GLN A CD  
563  O OE1 . GLN A 76  ? 0.2612 0.3210 0.3389 -0.0302 0.0913  -0.0314 167 GLN A OE1 
564  N NE2 . GLN A 76  ? 0.2152 0.2554 0.2577 -0.0387 0.1024  -0.0264 167 GLN A NE2 
565  N N   . HIS A 77  ? 0.1142 0.1849 0.2048 -0.0278 0.0598  -0.0224 168 HIS A N   
566  C CA  . HIS A 77  ? 0.1453 0.2105 0.2240 -0.0276 0.0512  -0.0177 168 HIS A CA  
567  C C   . HIS A 77  ? 0.1114 0.1812 0.1972 -0.0229 0.0403  -0.0183 168 HIS A C   
568  O O   . HIS A 77  ? 0.0758 0.1419 0.1551 -0.0226 0.0339  -0.0150 168 HIS A O   
569  C CB  . HIS A 77  ? 0.1479 0.2026 0.2028 -0.0283 0.0511  -0.0143 168 HIS A CB  
570  C CG  . HIS A 77  ? 0.1699 0.2165 0.2121 -0.0334 0.0610  -0.0129 168 HIS A CG  
571  N ND1 . HIS A 77  ? 0.1909 0.2344 0.2332 -0.0378 0.0653  -0.0101 168 HIS A ND1 
572  C CD2 . HIS A 77  ? 0.1848 0.2242 0.2119 -0.0350 0.0676  -0.0138 168 HIS A CD2 
573  C CE1 . HIS A 77  ? 0.2491 0.2836 0.2764 -0.0420 0.0744  -0.0090 168 HIS A CE1 
574  N NE2 . HIS A 77  ? 0.2167 0.2482 0.2339 -0.0404 0.0760  -0.0114 168 HIS A NE2 
575  N N   . MET A 78  ? 0.0726 0.1495 0.1713 -0.0193 0.0384  -0.0224 169 MET A N   
576  C CA  A MET A 78  ? 0.1115 0.1900 0.2122 -0.0149 0.0283  -0.0227 169 MET A CA  
577  C CA  B MET A 78  ? 0.1104 0.1889 0.2112 -0.0149 0.0283  -0.0227 169 MET A CA  
578  C C   . MET A 78  ? 0.0889 0.1686 0.1960 -0.0155 0.0220  -0.0216 169 MET A C   
579  O O   . MET A 78  ? 0.0769 0.1538 0.1786 -0.0130 0.0146  -0.0203 169 MET A O   
580  C CB  A MET A 78  ? 0.1068 0.1915 0.2202 -0.0110 0.0272  -0.0270 169 MET A CB  
581  C CB  B MET A 78  ? 0.1169 0.2017 0.2305 -0.0110 0.0273  -0.0270 169 MET A CB  
582  C CG  A MET A 78  ? 0.1796 0.2715 0.3125 -0.0116 0.0305  -0.0300 169 MET A CG  
583  C CG  B MET A 78  ? 0.1924 0.2842 0.3253 -0.0100 0.0234  -0.0293 169 MET A CG  
584  S SD  A MET A 78  ? 0.2741 0.3685 0.4164 -0.0058 0.0273  -0.0332 169 MET A SD  
585  S SD  B MET A 78  ? 0.2098 0.2999 0.3416 -0.0067 0.0100  -0.0283 169 MET A SD  
586  C CE  A MET A 78  ? 0.1053 0.2040 0.2646 -0.0074 0.0320  -0.0349 169 MET A CE  
587  C CE  B MET A 78  ? 0.2170 0.3054 0.3427 -0.0016 0.0067  -0.0293 169 MET A CE  
588  N N   . THR A 79  ? 0.0993 0.1824 0.2178 -0.0191 0.0254  -0.0223 170 THR A N   
589  C CA  . THR A 79  ? 0.0848 0.1676 0.2080 -0.0200 0.0190  -0.0217 170 THR A CA  
590  C C   . THR A 79  ? 0.1333 0.2076 0.2423 -0.0222 0.0190  -0.0173 170 THR A C   
591  O O   . THR A 79  ? 0.1178 0.1899 0.2280 -0.0227 0.0140  -0.0168 170 THR A O   
592  C CB  . THR A 79  ? 0.1094 0.1972 0.2488 -0.0225 0.0206  -0.0238 170 THR A CB  
593  O OG1 . THR A 79  ? 0.0912 0.1778 0.2303 -0.0271 0.0305  -0.0227 170 THR A OG1 
594  C CG2 . THR A 79  ? 0.1237 0.2162 0.2734 -0.0188 0.0180  -0.0268 170 THR A CG2 
595  N N   . GLU A 80  ? 0.0879 0.1567 0.1833 -0.0234 0.0238  -0.0142 171 GLU A N   
596  C CA  . GLU A 80  ? 0.1277 0.1883 0.2106 -0.0248 0.0228  -0.0095 171 GLU A CA  
597  C C   . GLU A 80  ? 0.1194 0.1766 0.1933 -0.0208 0.0161  -0.0078 171 GLU A C   
598  O O   . GLU A 80  ? 0.1332 0.1910 0.2020 -0.0183 0.0152  -0.0083 171 GLU A O   
599  C CB  . GLU A 80  ? 0.1090 0.1638 0.1801 -0.0280 0.0297  -0.0063 171 GLU A CB  
600  C CG  . GLU A 80  ? 0.1856 0.2315 0.2452 -0.0295 0.0283  -0.0009 171 GLU A CG  
601  C CD  . GLU A 80  ? 0.2440 0.2824 0.2896 -0.0329 0.0341  0.0026  171 GLU A CD  
602  O OE1 . GLU A 80  ? 0.2746 0.3055 0.3075 -0.0326 0.0307  0.0073  171 GLU A OE1 
603  O OE2 . GLU A 80  ? 0.2421 0.2816 0.2893 -0.0360 0.0420  0.0007  171 GLU A OE2 
604  N N   . VAL A 81  ? 0.0648 0.1178 0.1369 -0.0204 0.0121  -0.0059 172 VAL A N   
605  C CA  . VAL A 81  ? 0.0618 0.1111 0.1263 -0.0169 0.0073  -0.0041 172 VAL A CA  
606  C C   . VAL A 81  ? 0.0884 0.1341 0.1422 -0.0170 0.0086  -0.0003 172 VAL A C   
607  O O   . VAL A 81  ? 0.0763 0.1176 0.1248 -0.0198 0.0114  0.0030  172 VAL A O   
608  C CB  . VAL A 81  ? 0.0625 0.1068 0.1272 -0.0168 0.0047  -0.0028 172 VAL A CB  
609  C CG1 . VAL A 81  ? 0.0606 0.1010 0.1187 -0.0134 0.0016  -0.0006 172 VAL A CG1 
610  C CG2 . VAL A 81  ? 0.1875 0.2341 0.2607 -0.0170 0.0019  -0.0070 172 VAL A CG2 
611  N N   . VAL A 82  ? 0.0624 0.1089 0.1122 -0.0142 0.0059  -0.0006 173 VAL A N   
612  C CA  . VAL A 82  ? 0.0672 0.1099 0.1073 -0.0141 0.0050  0.0030  173 VAL A CA  
613  C C   . VAL A 82  ? 0.0660 0.1046 0.1053 -0.0128 0.0015  0.0066  173 VAL A C   
614  O O   . VAL A 82  ? 0.0731 0.1124 0.1164 -0.0101 -0.0009 0.0055  173 VAL A O   
615  C CB  . VAL A 82  ? 0.0678 0.1127 0.1053 -0.0120 0.0033  0.0010  173 VAL A CB  
616  C CG1 . VAL A 82  ? 0.0971 0.1378 0.1252 -0.0124 0.0009  0.0047  173 VAL A CG1 
617  C CG2 . VAL A 82  ? 0.0649 0.1133 0.1042 -0.0128 0.0074  -0.0027 173 VAL A CG2 
618  N N   . ARG A 83  ? 0.0768 0.1104 0.1106 -0.0145 0.0015  0.0111  174 ARG A N   
619  C CA  . ARG A 83  ? 0.1394 0.1690 0.1744 -0.0130 -0.0015 0.0149  174 ARG A CA  
620  C C   . ARG A 83  ? 0.1610 0.1861 0.1884 -0.0138 -0.0044 0.0200  174 ARG A C   
621  O O   . ARG A 83  ? 0.1167 0.1397 0.1350 -0.0165 -0.0033 0.0207  174 ARG A O   
622  C CB  . ARG A 83  ? 0.1204 0.1468 0.1596 -0.0141 0.0005  0.0154  174 ARG A CB  
623  C CG  . ARG A 83  ? 0.0855 0.1085 0.1200 -0.0183 0.0041  0.0172  174 ARG A CG  
624  C CD  . ARG A 83  ? 0.1448 0.1631 0.1832 -0.0197 0.0058  0.0184  174 ARG A CD  
625  N NE  . ARG A 83  ? 0.1682 0.1900 0.2151 -0.0195 0.0067  0.0135  174 ARG A NE  
626  C CZ  . ARG A 83  ? 0.1696 0.1901 0.2206 -0.0168 0.0045  0.0121  174 ARG A CZ  
627  N NH1 . ARG A 83  ? 0.1358 0.1582 0.1920 -0.0172 0.0045  0.0075  174 ARG A NH1 
628  N NH2 . ARG A 83  ? 0.0795 0.0965 0.1295 -0.0137 0.0023  0.0150  174 ARG A NH2 
629  N N   . ARG A 84  ? 0.0824 0.1052 0.1134 -0.0116 -0.0081 0.0235  175 ARG A N   
630  C CA  . ARG A 84  ? 0.0970 0.1151 0.1222 -0.0122 -0.0126 0.0289  175 ARG A CA  
631  C C   . ARG A 84  ? 0.1630 0.1738 0.1813 -0.0151 -0.0110 0.0326  175 ARG A C   
632  O O   . ARG A 84  ? 0.1025 0.1119 0.1246 -0.0159 -0.0070 0.0316  175 ARG A O   
633  C CB  . ARG A 84  ? 0.0886 0.1070 0.1230 -0.0087 -0.0170 0.0318  175 ARG A CB  
634  C CG  . ARG A 84  ? 0.0805 0.1048 0.1200 -0.0066 -0.0188 0.0293  175 ARG A CG  
635  C CD  . ARG A 84  ? 0.1072 0.1321 0.1582 -0.0033 -0.0220 0.0323  175 ARG A CD  
636  N NE  . ARG A 84  ? 0.0855 0.1092 0.1360 -0.0036 -0.0291 0.0371  175 ARG A NE  
637  C CZ  . ARG A 84  ? 0.1361 0.1601 0.1984 -0.0010 -0.0330 0.0407  175 ARG A CZ  
638  N NH1 . ARG A 84  ? 0.0879 0.1124 0.1618 0.0021  -0.0288 0.0399  175 ARG A NH1 
639  N NH2 . ARG A 84  ? 0.0931 0.1165 0.1558 -0.0014 -0.0410 0.0450  175 ARG A NH2 
640  N N   . CYS A 85  ? 0.1153 0.1202 0.1223 -0.0171 -0.0145 0.0369  176 CYS A N   
641  C CA  . CYS A 85  ? 0.1300 0.1258 0.1261 -0.0206 -0.0128 0.0409  176 CYS A CA  
642  C C   . CYS A 85  ? 0.1587 0.1490 0.1605 -0.0189 -0.0154 0.0458  176 CYS A C   
643  O O   . CYS A 85  ? 0.1680 0.1616 0.1819 -0.0149 -0.0190 0.0464  176 CYS A O   
644  C CB  . CYS A 85  ? 0.1446 0.1338 0.1241 -0.0232 -0.0168 0.0441  176 CYS A CB  
645  S SG  . CYS A 85  ? 0.1667 0.1525 0.1474 -0.0205 -0.0291 0.0507  176 CYS A SG  
646  N N   . PRO A 86  ? 0.1725 0.1404 0.1732 -0.0367 -0.0054 0.0604  177 PRO A N   
647  C CA  . PRO A 86  ? 0.2346 0.1931 0.2409 -0.0365 -0.0102 0.0637  177 PRO A CA  
648  C C   . PRO A 86  ? 0.2960 0.2484 0.2990 -0.0314 -0.0205 0.0653  177 PRO A C   
649  O O   . PRO A 86  ? 0.3460 0.2956 0.3603 -0.0290 -0.0252 0.0648  177 PRO A O   
650  C CB  . PRO A 86  ? 0.2542 0.2014 0.2497 -0.0413 -0.0046 0.0714  177 PRO A CB  
651  C CG  . PRO A 86  ? 0.1981 0.1538 0.1919 -0.0449 0.0056  0.0702  177 PRO A CG  
652  C CD  . PRO A 86  ? 0.1848 0.1499 0.1752 -0.0410 0.0040  0.0646  177 PRO A CD  
653  N N   . HIS A 87  ? 0.2335 0.1833 0.2220 -0.0296 -0.0245 0.0669  178 HIS A N   
654  C CA  . HIS A 87  ? 0.1971 0.1425 0.1855 -0.0249 -0.0359 0.0684  178 HIS A CA  
655  C C   . HIS A 87  ? 0.1910 0.1495 0.1980 -0.0214 -0.0392 0.0614  178 HIS A C   
656  O O   . HIS A 87  ? 0.2071 0.1656 0.2273 -0.0177 -0.0450 0.0613  178 HIS A O   
657  C CB  . HIS A 87  ? 0.2655 0.2030 0.2319 -0.0245 -0.0409 0.0720  178 HIS A CB  
658  C CG  . HIS A 87  ? 0.2163 0.1532 0.1862 -0.0200 -0.0539 0.0722  178 HIS A CG  
659  N ND1 . HIS A 87  ? 0.2532 0.1817 0.2273 -0.0170 -0.0629 0.0773  178 HIS A ND1 
660  C CD2 . HIS A 87  ? 0.2440 0.1887 0.2171 -0.0182 -0.0596 0.0678  178 HIS A CD2 
661  C CE1 . HIS A 87  ? 0.2490 0.1813 0.2297 -0.0134 -0.0738 0.0762  178 HIS A CE1 
662  N NE2 . HIS A 87  ? 0.2309 0.1729 0.2113 -0.0145 -0.0720 0.0705  178 HIS A NE2 
663  N N   . HIS A 88  ? 0.1630 0.1323 0.1712 -0.0221 -0.0351 0.0558  179 HIS A N   
664  C CA  . HIS A 88  ? 0.1555 0.1354 0.1784 -0.0190 -0.0385 0.0501  179 HIS A CA  
665  C C   . HIS A 88  ? 0.1791 0.1651 0.2199 -0.0181 -0.0344 0.0458  179 HIS A C   
666  O O   . HIS A 88  ? 0.1247 0.1157 0.1791 -0.0146 -0.0375 0.0430  179 HIS A O   
667  C CB  . HIS A 88  ? 0.1398 0.1270 0.1568 -0.0198 -0.0362 0.0458  179 HIS A CB  
668  C CG  . HIS A 88  ? 0.1528 0.1343 0.1556 -0.0192 -0.0437 0.0481  179 HIS A CG  
669  N ND1 . HIS A 88  ? 0.1662 0.1409 0.1476 -0.0213 -0.0410 0.0497  179 HIS A ND1 
670  C CD2 . HIS A 88  ? 0.1955 0.1760 0.2019 -0.0168 -0.0543 0.0492  179 HIS A CD2 
671  C CE1 . HIS A 88  ? 0.2170 0.1853 0.1870 -0.0204 -0.0502 0.0511  179 HIS A CE1 
672  N NE2 . HIS A 88  ? 0.2102 0.1825 0.1963 -0.0179 -0.0591 0.0511  179 HIS A NE2 
673  N N   . GLU A 89  ? 0.1506 0.1354 0.1916 -0.0213 -0.0275 0.0454  180 GLU A N   
674  C CA  . GLU A 89  ? 0.1784 0.1665 0.2335 -0.0206 -0.0248 0.0408  180 GLU A CA  
675  C C   . GLU A 89  ? 0.1297 0.1095 0.1922 -0.0175 -0.0290 0.0431  180 GLU A C   
676  O O   . GLU A 89  ? 0.1609 0.1421 0.2346 -0.0152 -0.0277 0.0387  180 GLU A O   
677  C CB  . GLU A 89  ? 0.1207 0.1095 0.1755 -0.0254 -0.0181 0.0395  180 GLU A CB  
678  C CG  . GLU A 89  ? 0.1355 0.1134 0.1857 -0.0289 -0.0171 0.0454  180 GLU A CG  
679  C CD  . GLU A 89  ? 0.1766 0.1560 0.2324 -0.0339 -0.0116 0.0436  180 GLU A CD  
680  O OE1 . GLU A 89  ? 0.1854 0.1746 0.2469 -0.0347 -0.0090 0.0380  180 GLU A OE1 
681  O OE2 . GLU A 89  ? 0.2200 0.1902 0.2746 -0.0374 -0.0105 0.0480  180 GLU A OE2 
682  N N   . ARG A 90  ? 0.1448 0.1147 0.2001 -0.0169 -0.0340 0.0498  181 ARG A N   
683  C CA  . ARG A 90  ? 0.1543 0.1150 0.2165 -0.0133 -0.0387 0.0529  181 ARG A CA  
684  C C   . ARG A 90  ? 0.1560 0.1186 0.2244 -0.0077 -0.0471 0.0546  181 ARG A C   
685  O O   . ARG A 90  ? 0.1679 0.1231 0.2430 -0.0037 -0.0520 0.0579  181 ARG A O   
686  C CB  . ARG A 90  ? 0.1730 0.1194 0.2238 -0.0164 -0.0391 0.0601  181 ARG A CB  
687  C CG  . ARG A 90  ? 0.1730 0.1175 0.2218 -0.0224 -0.0312 0.0591  181 ARG A CG  
688  C CD  . ARG A 90  ? 0.1935 0.1230 0.2314 -0.0260 -0.0309 0.0672  181 ARG A CD  
689  N NE  . ARG A 90  ? 0.2055 0.1223 0.2482 -0.0225 -0.0360 0.0704  181 ARG A NE  
690  C CZ  . ARG A 90  ? 0.2234 0.1281 0.2573 -0.0201 -0.0424 0.0780  181 ARG A CZ  
691  N NH1 . ARG A 90  ? 0.2327 0.1355 0.2504 -0.0211 -0.0447 0.0831  181 ARG A NH1 
692  N NH2 . ARG A 90  ? 0.2343 0.1274 0.2745 -0.0163 -0.0468 0.0805  181 ARG A NH2 
693  N N   . CYS A 91  ? 0.1481 0.1203 0.2159 -0.0073 -0.0494 0.0526  182 CYS A N   
694  C CA  A CYS A 91  ? 0.2159 0.1898 0.2906 -0.0030 -0.0589 0.0550  182 CYS A CA  
695  C CA  B CYS A 91  ? 0.2202 0.1953 0.2948 -0.0033 -0.0587 0.0545  182 CYS A CA  
696  C C   . CYS A 91  ? 0.2200 0.2040 0.3175 0.0018  -0.0584 0.0504  182 CYS A C   
697  O O   . CYS A 91  ? 0.1872 0.1755 0.2954 0.0053  -0.0660 0.0521  182 CYS A O   
698  C CB  A CYS A 91  ? 0.2244 0.2013 0.2867 -0.0053 -0.0635 0.0558  182 CYS A CB  
699  C CB  B CYS A 91  ? 0.2254 0.2060 0.2900 -0.0057 -0.0613 0.0536  182 CYS A CB  
700  S SG  A CYS A 91  ? 0.2048 0.1968 0.2737 -0.0066 -0.0588 0.0481  182 CYS A SG  
701  S SG  B CYS A 91  ? 0.2528 0.2205 0.2892 -0.0093 -0.0652 0.0600  182 CYS A SG  
702  N N   . SER A 92  ? 0.2049 0.1919 0.3099 0.0021  -0.0497 0.0449  183 SER A N   
703  C CA  A SER A 92  ? 0.1942 0.1875 0.3188 0.0072  -0.0471 0.0409  183 SER A CA  
704  C CA  B SER A 92  ? 0.2010 0.1943 0.3255 0.0072  -0.0470 0.0408  183 SER A CA  
705  C C   . SER A 92  ? 0.1796 0.1859 0.3143 0.0082  -0.0490 0.0388  183 SER A C   
706  O O   . SER A 92  ? 0.2118 0.2232 0.3640 0.0128  -0.0530 0.0400  183 SER A O   
707  C CB  A SER A 92  ? 0.2518 0.2377 0.3877 0.0130  -0.0517 0.0447  183 SER A CB  
708  C CB  B SER A 92  ? 0.2462 0.2319 0.3818 0.0129  -0.0513 0.0445  183 SER A CB  
709  O OG  A SER A 92  ? 0.2516 0.2242 0.3794 0.0120  -0.0492 0.0460  183 SER A OG  
710  O OG  B SER A 92  ? 0.2614 0.2527 0.4161 0.0184  -0.0468 0.0403  183 SER A OG  
711  N N   . ASP A 93  ? 0.1361 0.1480 0.2612 0.0038  -0.0460 0.0359  184 ASP A N   
712  C CA  . ASP A 93  ? 0.1058 0.1285 0.2389 0.0037  -0.0478 0.0340  184 ASP A CA  
713  C C   . ASP A 93  ? 0.0988 0.1285 0.2348 0.0028  -0.0382 0.0277  184 ASP A C   
714  O O   . ASP A 93  ? 0.0990 0.1358 0.2358 0.0009  -0.0384 0.0260  184 ASP A O   
715  C CB  . ASP A 93  ? 0.1216 0.1430 0.2397 -0.0003 -0.0546 0.0366  184 ASP A CB  
716  C CG  . ASP A 93  ? 0.1741 0.1921 0.2726 -0.0048 -0.0489 0.0348  184 ASP A CG  
717  O OD1 . ASP A 93  ? 0.1420 0.1598 0.2396 -0.0055 -0.0408 0.0316  184 ASP A OD1 
718  O OD2 . ASP A 93  ? 0.1490 0.1643 0.2330 -0.0076 -0.0527 0.0364  184 ASP A OD2 
719  N N   . SER A 94  ? 0.0855 0.1118 0.2218 0.0040  -0.0305 0.0243  185 SER A N   
720  C CA  . SER A 94  ? 0.1227 0.1536 0.2592 0.0035  -0.0221 0.0186  185 SER A CA  
721  C C   . SER A 94  ? 0.1281 0.1675 0.2822 0.0068  -0.0197 0.0173  185 SER A C   
722  O O   . SER A 94  ? 0.1032 0.1437 0.2730 0.0112  -0.0214 0.0193  185 SER A O   
723  C CB  . SER A 94  ? 0.1549 0.1782 0.2867 0.0043  -0.0157 0.0151  185 SER A CB  
724  O OG  . SER A 94  ? 0.0973 0.1233 0.2271 0.0042  -0.0084 0.0097  185 SER A OG  
725  N N   . ASP A 95  ? 0.1022 0.1474 0.2547 0.0047  -0.0155 0.0143  186 ASP A N   
726  C CA  . ASP A 95  ? 0.1268 0.1796 0.2948 0.0069  -0.0108 0.0129  186 ASP A CA  
727  C C   . ASP A 95  ? 0.1639 0.2135 0.3357 0.0108  -0.0003 0.0090  186 ASP A C   
728  O O   . ASP A 95  ? 0.1087 0.1613 0.2877 0.0124  0.0060  0.0077  186 ASP A O   
729  C CB  . ASP A 95  ? 0.1289 0.1852 0.2884 0.0028  -0.0095 0.0113  186 ASP A CB  
730  C CG  . ASP A 95  ? 0.1705 0.2242 0.3164 0.0007  -0.0038 0.0076  186 ASP A CG  
731  O OD1 . ASP A 95  ? 0.0955 0.1419 0.2309 0.0011  -0.0021 0.0061  186 ASP A OD1 
732  O OD2 . ASP A 95  ? 0.1309 0.1873 0.2728 -0.0015 -0.0012 0.0062  186 ASP A OD2 
733  N N   . GLY A 96  ? 0.1584 0.1981 0.3183 0.0115  0.0019  0.0069  187 GLY A N   
734  C CA  . GLY A 96  ? 0.1993 0.2324 0.3568 0.0147  0.0112  0.0023  187 GLY A CA  
735  C C   . GLY A 96  ? 0.1977 0.2259 0.3365 0.0116  0.0155  -0.0020 187 GLY A C   
736  O O   . GLY A 96  ? 0.1981 0.2172 0.3289 0.0136  0.0211  -0.0062 187 GLY A O   
737  N N   . LEU A 97  ? 0.1294 0.1626 0.2607 0.0072  0.0125  -0.0013 188 LEU A N   
738  C CA  . LEU A 97  ? 0.1022 0.1312 0.2165 0.0044  0.0147  -0.0048 188 LEU A CA  
739  C C   . LEU A 97  ? 0.0996 0.1270 0.2040 0.0005  0.0081  -0.0036 188 LEU A C   
740  O O   . LEU A 97  ? 0.0872 0.1082 0.1810 -0.0008 0.0083  -0.0063 188 LEU A O   
741  C CB  . LEU A 97  ? 0.0976 0.1324 0.2107 0.0029  0.0177  -0.0052 188 LEU A CB  
742  C CG  . LEU A 97  ? 0.1564 0.1938 0.2799 0.0059  0.0259  -0.0059 188 LEU A CG  
743  C CD1 . LEU A 97  ? 0.1626 0.2050 0.2846 0.0031  0.0278  -0.0053 188 LEU A CD1 
744  C CD2 . LEU A 97  ? 0.2108 0.2380 0.3259 0.0093  0.0342  -0.0102 188 LEU A CD2 
745  N N   . ALA A 98  ? 0.0867 0.1195 0.1942 -0.0015 0.0022  0.0005  189 ALA A N   
746  C CA  . ALA A 98  ? 0.1032 0.1350 0.2010 -0.0052 -0.0021 0.0018  189 ALA A CA  
747  C C   . ALA A 98  ? 0.1183 0.1434 0.2160 -0.0054 -0.0044 0.0035  189 ALA A C   
748  O O   . ALA A 98  ? 0.1114 0.1350 0.2171 -0.0032 -0.0068 0.0065  189 ALA A O   
749  C CB  . ALA A 98  ? 0.0532 0.0905 0.1509 -0.0070 -0.0067 0.0053  189 ALA A CB  
750  N N   . PRO A 99  ? 0.1037 0.1246 0.1936 -0.0081 -0.0044 0.0021  190 PRO A N   
751  C CA  . PRO A 99  ? 0.0834 0.0979 0.1733 -0.0096 -0.0070 0.0047  190 PRO A CA  
752  C C   . PRO A 99  ? 0.0837 0.1005 0.1728 -0.0112 -0.0109 0.0103  190 PRO A C   
753  O O   . PRO A 99  ? 0.0953 0.1181 0.1802 -0.0127 -0.0116 0.0112  190 PRO A O   
754  C CB  . PRO A 99  ? 0.1235 0.1357 0.2067 -0.0134 -0.0064 0.0020  190 PRO A CB  
755  C CG  . PRO A 99  ? 0.1220 0.1361 0.2014 -0.0121 -0.0036 -0.0030 190 PRO A CG  
756  C CD  . PRO A 99  ? 0.0640 0.0856 0.1461 -0.0101 -0.0026 -0.0017 190 PRO A CD  
757  N N   . PRO A 100 ? 0.0927 0.1032 0.1841 -0.0107 -0.0138 0.0143  191 PRO A N   
758  C CA  . PRO A 100 ? 0.1079 0.1181 0.1953 -0.0119 -0.0180 0.0201  191 PRO A CA  
759  C C   . PRO A 100 ? 0.1199 0.1313 0.1972 -0.0166 -0.0168 0.0217  191 PRO A C   
760  O O   . PRO A 100 ? 0.0913 0.1026 0.1617 -0.0175 -0.0191 0.0256  191 PRO A O   
761  C CB  . PRO A 100 ? 0.1011 0.1016 0.1918 -0.0104 -0.0209 0.0239  191 PRO A CB  
762  C CG  . PRO A 100 ? 0.1040 0.0989 0.1973 -0.0104 -0.0173 0.0198  191 PRO A CG  
763  C CD  . PRO A 100 ? 0.1261 0.1275 0.2222 -0.0085 -0.0134 0.0137  191 PRO A CD  
764  N N   . GLN A 101 ? 0.0824 0.0946 0.1588 -0.0195 -0.0132 0.0189  192 GLN A N   
765  C CA  . GLN A 101 ? 0.0907 0.1059 0.1611 -0.0235 -0.0109 0.0205  192 GLN A CA  
766  C C   . GLN A 101 ? 0.1162 0.1399 0.1831 -0.0230 -0.0093 0.0182  192 GLN A C   
767  O O   . GLN A 101 ? 0.0758 0.1022 0.1374 -0.0252 -0.0069 0.0199  192 GLN A O   
768  C CB  . GLN A 101 ? 0.0837 0.0978 0.1576 -0.0271 -0.0088 0.0186  192 GLN A CB  
769  C CG  . GLN A 101 ? 0.0940 0.0977 0.1706 -0.0286 -0.0101 0.0208  192 GLN A CG  
770  C CD  . GLN A 101 ? 0.0948 0.0933 0.1759 -0.0258 -0.0113 0.0159  192 GLN A CD  
771  O OE1 . GLN A 101 ? 0.0921 0.0931 0.1745 -0.0214 -0.0113 0.0131  192 GLN A OE1 
772  N NE2 . GLN A 101 ? 0.1274 0.1179 0.2106 -0.0286 -0.0117 0.0148  192 GLN A NE2 
773  N N   . HIS A 102 ? 0.0852 0.1126 0.1550 -0.0201 -0.0098 0.0143  193 HIS A N   
774  C CA  . HIS A 102 ? 0.1119 0.1458 0.1786 -0.0197 -0.0082 0.0116  193 HIS A CA  
775  C C   . HIS A 102 ? 0.0656 0.1003 0.1260 -0.0191 -0.0099 0.0139  193 HIS A C   
776  O O   . HIS A 102 ? 0.0775 0.1106 0.1397 -0.0175 -0.0135 0.0152  193 HIS A O   
777  C CB  . HIS A 102 ? 0.0574 0.0930 0.1279 -0.0173 -0.0074 0.0070  193 HIS A CB  
778  C CG  . HIS A 102 ? 0.0549 0.0894 0.1265 -0.0180 -0.0059 0.0035  193 HIS A CG  
779  N ND1 . HIS A 102 ? 0.0518 0.0882 0.1212 -0.0168 -0.0047 -0.0005 193 HIS A ND1 
780  C CD2 . HIS A 102 ? 0.0598 0.0900 0.1333 -0.0201 -0.0064 0.0032  193 HIS A CD2 
781  C CE1 . HIS A 102 ? 0.0552 0.0884 0.1243 -0.0179 -0.0051 -0.0031 193 HIS A CE1 
782  N NE2 . HIS A 102 ? 0.0714 0.1010 0.1436 -0.0201 -0.0062 -0.0012 193 HIS A NE2 
783  N N   . LEU A 103 ? 0.0629 0.1001 0.1165 -0.0203 -0.0075 0.0139  194 LEU A N   
784  C CA  . LEU A 103 ? 0.0799 0.1156 0.1242 -0.0198 -0.0090 0.0152  194 LEU A CA  
785  C C   . LEU A 103 ? 0.0624 0.1005 0.1085 -0.0180 -0.0112 0.0122  194 LEU A C   
786  O O   . LEU A 103 ? 0.0671 0.1027 0.1105 -0.0177 -0.0157 0.0135  194 LEU A O   
787  C CB  . LEU A 103 ? 0.0711 0.1082 0.1078 -0.0207 -0.0042 0.0154  194 LEU A CB  
788  C CG  . LEU A 103 ? 0.1076 0.1408 0.1313 -0.0199 -0.0051 0.0158  194 LEU A CG  
789  C CD1 . LEU A 103 ? 0.0952 0.1199 0.1095 -0.0208 -0.0089 0.0204  194 LEU A CD1 
790  C CD2 . LEU A 103 ? 0.0936 0.1288 0.1113 -0.0196 0.0013  0.0148  194 LEU A CD2 
791  N N   . ILE A 104 ? 0.0547 0.0971 0.1048 -0.0172 -0.0085 0.0085  195 ILE A N   
792  C CA  . ILE A 104 ? 0.0627 0.1065 0.1133 -0.0160 -0.0092 0.0059  195 ILE A CA  
793  C C   . ILE A 104 ? 0.0579 0.1028 0.1184 -0.0150 -0.0095 0.0048  195 ILE A C   
794  O O   . ILE A 104 ? 0.0845 0.1296 0.1484 -0.0144 -0.0069 0.0032  195 ILE A O   
795  C CB  . ILE A 104 ? 0.0734 0.1196 0.1206 -0.0153 -0.0059 0.0030  195 ILE A CB  
796  C CG1 . ILE A 104 ? 0.0803 0.1260 0.1194 -0.0155 -0.0040 0.0040  195 ILE A CG1 
797  C CG2 . ILE A 104 ? 0.0466 0.0924 0.0933 -0.0145 -0.0065 0.0010  195 ILE A CG2 
798  C CD1 . ILE A 104 ? 0.0783 0.1270 0.1164 -0.0139 -0.0009 0.0014  195 ILE A CD1 
799  N N   . ARG A 105 ? 0.0476 0.0928 0.1126 -0.0147 -0.0123 0.0055  196 ARG A N   
800  C CA  . ARG A 105 ? 0.0460 0.0933 0.1217 -0.0134 -0.0107 0.0044  196 ARG A CA  
801  C C   . ARG A 105 ? 0.0523 0.1011 0.1283 -0.0139 -0.0097 0.0028  196 ARG A C   
802  O O   . ARG A 105 ? 0.0452 0.0929 0.1152 -0.0153 -0.0125 0.0030  196 ARG A O   
803  C CB  . ARG A 105 ? 0.0509 0.0987 0.1367 -0.0126 -0.0147 0.0072  196 ARG A CB  
804  C CG  . ARG A 105 ? 0.0510 0.0952 0.1354 -0.0123 -0.0166 0.0097  196 ARG A CG  
805  C CD  . ARG A 105 ? 0.0590 0.1035 0.1554 -0.0104 -0.0206 0.0124  196 ARG A CD  
806  N NE  . ARG A 105 ? 0.1078 0.1472 0.2028 -0.0097 -0.0220 0.0149  196 ARG A NE  
807  C CZ  . ARG A 105 ? 0.0665 0.1040 0.1698 -0.0077 -0.0264 0.0181  196 ARG A CZ  
808  N NH1 . ARG A 105 ? 0.0850 0.1273 0.2010 -0.0060 -0.0302 0.0192  196 ARG A NH1 
809  N NH2 . ARG A 105 ? 0.0956 0.1267 0.1959 -0.0073 -0.0272 0.0206  196 ARG A NH2 
810  N N   . VAL A 106 ? 0.0408 0.0908 0.1232 -0.0129 -0.0052 0.0012  197 VAL A N   
811  C CA  . VAL A 106 ? 0.0562 0.1075 0.1421 -0.0138 -0.0036 0.0006  197 VAL A CA  
812  C C   . VAL A 106 ? 0.0888 0.1445 0.1910 -0.0139 -0.0050 0.0026  197 VAL A C   
813  O O   . VAL A 106 ? 0.1010 0.1582 0.2122 -0.0117 -0.0028 0.0031  197 VAL A O   
814  C CB  . VAL A 106 ? 0.0553 0.1041 0.1366 -0.0127 0.0032  -0.0018 197 VAL A CB  
815  C CG1 . VAL A 106 ? 0.1035 0.1531 0.1907 -0.0140 0.0064  -0.0015 197 VAL A CG1 
816  C CG2 . VAL A 106 ? 0.0676 0.1131 0.1351 -0.0127 0.0027  -0.0033 197 VAL A CG2 
817  N N   . GLU A 107 ? 0.0423 0.0996 0.1485 -0.0163 -0.0091 0.0037  198 GLU A N   
818  C CA  . GLU A 107 ? 0.0716 0.1312 0.1890 -0.0161 -0.0113 0.0054  198 GLU A CA  
819  C C   . GLU A 107 ? 0.1329 0.1940 0.2569 -0.0165 -0.0044 0.0048  198 GLU A C   
820  O O   . GLU A 107 ? 0.1327 0.1921 0.2516 -0.0189 -0.0023 0.0037  198 GLU A O   
821  C CB  . GLU A 107 ? 0.0674 0.1260 0.1830 -0.0188 -0.0206 0.0067  198 GLU A CB  
822  C CG  . GLU A 107 ? 0.1344 0.1958 0.2630 -0.0189 -0.0241 0.0086  198 GLU A CG  
823  C CD  . GLU A 107 ? 0.2300 0.2886 0.3547 -0.0219 -0.0343 0.0094  198 GLU A CD  
824  O OE1 . GLU A 107 ? 0.1972 0.2509 0.3079 -0.0235 -0.0385 0.0087  198 GLU A OE1 
825  O OE2 . GLU A 107 ? 0.2927 0.3536 0.4283 -0.0227 -0.0383 0.0108  198 GLU A OE2 
826  N N   . GLY A 108 ? 0.0495 0.1133 0.1854 -0.0142 -0.0006 0.0056  199 GLY A N   
827  C CA  . GLY A 108 ? 0.1814 0.2470 0.3254 -0.0149 0.0058  0.0058  199 GLY A CA  
828  C C   . GLY A 108 ? 0.2291 0.2915 0.3666 -0.0144 0.0159  0.0041  199 GLY A C   
829  O O   . GLY A 108 ? 0.2701 0.3319 0.4090 -0.0166 0.0204  0.0045  199 GLY A O   
830  N N   . ASN A 109 ? 0.1475 0.2070 0.2777 -0.0118 0.0195  0.0023  200 ASN A N   
831  C CA  . ASN A 109 ? 0.1417 0.1966 0.2643 -0.0108 0.0293  0.0003  200 ASN A CA  
832  C C   . ASN A 109 ? 0.1700 0.2228 0.2930 -0.0067 0.0341  -0.0014 200 ASN A C   
833  O O   . ASN A 109 ? 0.1604 0.2114 0.2772 -0.0057 0.0300  -0.0028 200 ASN A O   
834  C CB  . ASN A 109 ? 0.1853 0.2354 0.2917 -0.0126 0.0277  -0.0012 200 ASN A CB  
835  C CG  . ASN A 109 ? 0.1844 0.2260 0.2765 -0.0115 0.0360  -0.0027 200 ASN A CG  
836  O OD1 . ASN A 109 ? 0.2051 0.2434 0.2963 -0.0089 0.0437  -0.0038 200 ASN A OD1 
837  N ND2 . ASN A 109 ? 0.1109 0.1475 0.1904 -0.0132 0.0344  -0.0027 200 ASN A ND2 
838  N N   . LEU A 110 ? 0.1801 0.2316 0.3087 -0.0043 0.0423  -0.0015 201 LEU A N   
839  C CA  . LEU A 110 ? 0.1856 0.2332 0.3141 0.0001  0.0478  -0.0037 201 LEU A CA  
840  C C   . LEU A 110 ? 0.1234 0.1611 0.2319 0.0013  0.0524  -0.0074 201 LEU A C   
841  O O   . LEU A 110 ? 0.1829 0.2141 0.2857 0.0045  0.0543  -0.0100 201 LEU A O   
842  C CB  . LEU A 110 ? 0.2870 0.3344 0.4247 0.0025  0.0560  -0.0029 201 LEU A CB  
843  C CG  . LEU A 110 ? 0.3848 0.4408 0.5417 0.0020  0.0504  0.0005  201 LEU A CG  
844  C CD1 . LEU A 110 ? 0.4685 0.5251 0.6359 0.0042  0.0597  0.0013  201 LEU A CD1 
845  C CD2 . LEU A 110 ? 0.3862 0.4448 0.5503 0.0038  0.0420  0.0012  201 LEU A CD2 
846  N N   . ARG A 111 ? 0.1183 0.1515 0.2116 -0.0013 0.0517  -0.0077 202 ARG A N   
847  C CA  . ARG A 111 ? 0.1535 0.1751 0.2232 -0.0004 0.0517  -0.0107 202 ARG A CA  
848  C C   . ARG A 111 ? 0.1471 0.1693 0.2097 -0.0019 0.0409  -0.0114 202 ARG A C   
849  O O   . ARG A 111 ? 0.1418 0.1563 0.1874 -0.0017 0.0387  -0.0135 202 ARG A O   
850  C CB  . ARG A 111 ? 0.2079 0.2232 0.2645 -0.0017 0.0570  -0.0103 202 ARG A CB  
851  N N   . ALA A 112 ? 0.1180 0.1488 0.1931 -0.0033 0.0340  -0.0093 203 ALA A N   
852  C CA  . ALA A 112 ? 0.1070 0.1384 0.1763 -0.0045 0.0256  -0.0096 203 ALA A CA  
853  C C   . ALA A 112 ? 0.1554 0.1808 0.2188 -0.0029 0.0248  -0.0121 203 ALA A C   
854  O O   . ALA A 112 ? 0.1360 0.1598 0.2063 -0.0007 0.0279  -0.0127 203 ALA A O   
855  C CB  . ALA A 112 ? 0.1301 0.1697 0.2116 -0.0062 0.0194  -0.0066 203 ALA A CB  
856  N N   . GLU A 113 ? 0.0743 0.0962 0.1261 -0.0040 0.0203  -0.0136 204 GLU A N   
857  C CA  . GLU A 113 ? 0.0737 0.0898 0.1202 -0.0037 0.0178  -0.0160 204 GLU A CA  
858  C C   . GLU A 113 ? 0.1096 0.1308 0.1591 -0.0063 0.0107  -0.0145 204 GLU A C   
859  O O   . GLU A 113 ? 0.0917 0.1180 0.1400 -0.0076 0.0080  -0.0131 204 GLU A O   
860  C CB  . GLU A 113 ? 0.1539 0.1600 0.1837 -0.0030 0.0187  -0.0195 204 GLU A CB  
861  C CG  . GLU A 113 ? 0.2399 0.2384 0.2634 -0.0003 0.0274  -0.0211 204 GLU A CG  
862  C CD  . GLU A 113 ? 0.3514 0.3370 0.3540 0.0006  0.0279  -0.0244 204 GLU A CD  
863  O OE1 . GLU A 113 ? 0.3464 0.3240 0.3404 0.0028  0.0362  -0.0256 204 GLU A OE1 
864  O OE2 . GLU A 113 ? 0.2999 0.2833 0.2947 -0.0009 0.0200  -0.0257 204 GLU A OE2 
865  N N   . TYR A 114 ? 0.0881 0.1072 0.1412 -0.0068 0.0085  -0.0147 205 TYR A N   
866  C CA  . TYR A 114 ? 0.0801 0.1035 0.1371 -0.0095 0.0034  -0.0126 205 TYR A CA  
867  C C   . TYR A 114 ? 0.1154 0.1335 0.1671 -0.0113 0.0001  -0.0152 205 TYR A C   
868  O O   . TYR A 114 ? 0.1351 0.1443 0.1831 -0.0104 0.0009  -0.0180 205 TYR A O   
869  C CB  . TYR A 114 ? 0.0604 0.0852 0.1272 -0.0093 0.0029  -0.0095 205 TYR A CB  
870  C CG  . TYR A 114 ? 0.0543 0.0854 0.1273 -0.0085 0.0035  -0.0066 205 TYR A CG  
871  C CD1 . TYR A 114 ? 0.0742 0.1056 0.1523 -0.0060 0.0076  -0.0072 205 TYR A CD1 
872  C CD2 . TYR A 114 ? 0.0753 0.1117 0.1489 -0.0104 0.0001  -0.0036 205 TYR A CD2 
873  C CE1 . TYR A 114 ? 0.0568 0.0944 0.1426 -0.0060 0.0069  -0.0045 205 TYR A CE1 
874  C CE2 . TYR A 114 ? 0.0459 0.0864 0.1237 -0.0101 -0.0009 -0.0014 205 TYR A CE2 
875  C CZ  . TYR A 114 ? 0.0526 0.0942 0.1374 -0.0083 0.0018  -0.0019 205 TYR A CZ  
876  O OH  . TYR A 114 ? 0.0632 0.1093 0.1541 -0.0088 -0.0003 0.0003  205 TYR A OH  
877  N N   . LEU A 115 ? 0.0653 0.0885 0.1172 -0.0137 -0.0037 -0.0143 206 LEU A N   
878  C CA  . LEU A 115 ? 0.1090 0.1291 0.1588 -0.0161 -0.0082 -0.0165 206 LEU A CA  
879  C C   . LEU A 115 ? 0.1287 0.1536 0.1879 -0.0197 -0.0103 -0.0135 206 LEU A C   
880  O O   . LEU A 115 ? 0.0847 0.1177 0.1487 -0.0204 -0.0094 -0.0101 206 LEU A O   
881  C CB  . LEU A 115 ? 0.0914 0.1142 0.1360 -0.0159 -0.0110 -0.0179 206 LEU A CB  
882  C CG  . LEU A 115 ? 0.0787 0.0995 0.1230 -0.0185 -0.0176 -0.0201 206 LEU A CG  
883  C CD1 . LEU A 115 ? 0.1069 0.1141 0.1411 -0.0185 -0.0194 -0.0245 206 LEU A CD1 
884  C CD2 . LEU A 115 ? 0.1271 0.1527 0.1695 -0.0176 -0.0212 -0.0203 206 LEU A CD2 
885  N N   . ASP A 116 ? 0.0979 0.1161 0.1584 -0.0221 -0.0128 -0.0149 207 ASP A N   
886  C CA  . ASP A 116 ? 0.0906 0.1123 0.1596 -0.0268 -0.0155 -0.0126 207 ASP A CA  
887  C C   . ASP A 116 ? 0.1373 0.1592 0.2060 -0.0291 -0.0211 -0.0157 207 ASP A C   
888  O O   . ASP A 116 ? 0.1154 0.1270 0.1775 -0.0296 -0.0246 -0.0199 207 ASP A O   
889  C CB  . ASP A 116 ? 0.1842 0.1970 0.2556 -0.0288 -0.0157 -0.0119 207 ASP A CB  
890  C CG  . ASP A 116 ? 0.2542 0.2663 0.3273 -0.0264 -0.0120 -0.0082 207 ASP A CG  
891  O OD1 . ASP A 116 ? 0.2319 0.2519 0.3067 -0.0255 -0.0099 -0.0046 207 ASP A OD1 
892  O OD2 . ASP A 116 ? 0.3321 0.3346 0.4048 -0.0254 -0.0117 -0.0088 207 ASP A OD2 
893  N N   . ASP A 117 ? 0.0867 0.1196 0.1623 -0.0303 -0.0223 -0.0139 208 ASP A N   
894  C CA  . ASP A 117 ? 0.1280 0.1627 0.2057 -0.0321 -0.0289 -0.0165 208 ASP A CA  
895  C C   . ASP A 117 ? 0.1686 0.1993 0.2534 -0.0378 -0.0340 -0.0174 208 ASP A C   
896  O O   . ASP A 117 ? 0.1028 0.1380 0.1989 -0.0417 -0.0318 -0.0137 208 ASP A O   
897  C CB  . ASP A 117 ? 0.1308 0.1793 0.2179 -0.0316 -0.0285 -0.0139 208 ASP A CB  
898  C CG  . ASP A 117 ? 0.2005 0.2514 0.2894 -0.0316 -0.0363 -0.0165 208 ASP A CG  
899  O OD1 . ASP A 117 ? 0.1760 0.2274 0.2718 -0.0355 -0.0413 -0.0168 208 ASP A OD1 
900  O OD2 . ASP A 117 ? 0.1743 0.2248 0.2550 -0.0273 -0.0371 -0.0177 208 ASP A OD2 
901  N N   . ARG A 118 ? 0.1550 0.1756 0.2319 -0.0385 -0.0408 -0.0223 209 ARG A N   
902  C CA  . ARG A 118 ? 0.1676 0.1812 0.2492 -0.0443 -0.0465 -0.0240 209 ARG A CA  
903  C C   . ARG A 118 ? 0.2491 0.2747 0.3439 -0.0477 -0.0478 -0.0204 209 ARG A C   
904  O O   . ARG A 118 ? 0.2452 0.2683 0.3458 -0.0522 -0.0483 -0.0192 209 ARG A O   
905  C CB  . ARG A 118 ? 0.2349 0.2328 0.3005 -0.0437 -0.0535 -0.0305 209 ARG A CB  
906  N N   . ASN A 119 ? 0.2276 0.2655 0.3274 -0.0453 -0.0477 -0.0186 210 ASN A N   
907  C CA  . ASN A 119 ? 0.2165 0.2662 0.3300 -0.0477 -0.0481 -0.0157 210 ASN A CA  
908  C C   . ASN A 119 ? 0.1865 0.2479 0.3099 -0.0474 -0.0388 -0.0104 210 ASN A C   
909  O O   . ASN A 119 ? 0.1947 0.2614 0.3289 -0.0513 -0.0365 -0.0077 210 ASN A O   
910  C CB  . ASN A 119 ? 0.2339 0.2889 0.3476 -0.0449 -0.0543 -0.0173 210 ASN A CB  
911  C CG  . ASN A 119 ? 0.3564 0.3989 0.4590 -0.0457 -0.0644 -0.0223 210 ASN A CG  
912  O OD1 . ASN A 119 ? 0.4010 0.4345 0.5019 -0.0499 -0.0676 -0.0242 210 ASN A OD1 
913  N ND2 . ASN A 119 ? 0.4907 0.5310 0.5839 -0.0416 -0.0694 -0.0244 210 ASN A ND2 
914  N N   . THR A 120 ? 0.1032 0.1679 0.2223 -0.0431 -0.0333 -0.0090 211 THR A N   
915  C CA  . THR A 120 ? 0.1562 0.2303 0.2814 -0.0423 -0.0247 -0.0045 211 THR A CA  
916  C C   . THR A 120 ? 0.1444 0.2130 0.2651 -0.0432 -0.0188 -0.0019 211 THR A C   
917  O O   . THR A 120 ? 0.1329 0.2068 0.2568 -0.0435 -0.0119 0.0019  211 THR A O   
918  C CB  . THR A 120 ? 0.1575 0.2387 0.2809 -0.0369 -0.0226 -0.0044 211 THR A CB  
919  O OG1 . THR A 120 ? 0.2024 0.2768 0.3146 -0.0339 -0.0224 -0.0061 211 THR A OG1 
920  C CG2 . THR A 120 ? 0.1992 0.2848 0.3265 -0.0352 -0.0295 -0.0066 211 THR A CG2 
921  N N   . PHE A 121 ? 0.1222 0.1797 0.2353 -0.0435 -0.0213 -0.0040 212 PHE A N   
922  C CA  . PHE A 121 ? 0.0949 0.1463 0.2042 -0.0436 -0.0171 -0.0014 212 PHE A CA  
923  C C   . PHE A 121 ? 0.1016 0.1577 0.2070 -0.0395 -0.0120 0.0006  212 PHE A C   
924  O O   . PHE A 121 ? 0.1020 0.1540 0.2034 -0.0392 -0.0086 0.0036  212 PHE A O   
925  C CB  . PHE A 121 ? 0.1344 0.1843 0.2492 -0.0482 -0.0138 0.0028  212 PHE A CB  
926  C CG  . PHE A 121 ? 0.1880 0.2345 0.3081 -0.0528 -0.0186 0.0010  212 PHE A CG  
927  C CD1 . PHE A 121 ? 0.1695 0.2036 0.2849 -0.0540 -0.0243 -0.0028 212 PHE A CD1 
928  C CD2 . PHE A 121 ? 0.3048 0.3599 0.4348 -0.0559 -0.0176 0.0026  212 PHE A CD2 
929  C CE1 . PHE A 121 ? 0.2202 0.2497 0.3391 -0.0585 -0.0294 -0.0048 212 PHE A CE1 
930  C CE2 . PHE A 121 ? 0.3061 0.3583 0.4420 -0.0606 -0.0228 0.0010  212 PHE A CE2 
931  C CZ  . PHE A 121 ? 0.2555 0.2945 0.3851 -0.0620 -0.0290 -0.0028 212 PHE A CZ  
932  N N   . ARG A 122 ? 0.0586 0.1215 0.1629 -0.0360 -0.0121 -0.0009 213 ARG A N   
933  C CA  . ARG A 122 ? 0.0990 0.1641 0.1968 -0.0320 -0.0077 0.0004  213 ARG A CA  
934  C C   . ARG A 122 ? 0.1071 0.1638 0.1935 -0.0286 -0.0089 -0.0021 213 ARG A C   
935  O O   . ARG A 122 ? 0.1241 0.1747 0.2070 -0.0281 -0.0126 -0.0057 213 ARG A O   
936  C CB  . ARG A 122 ? 0.1267 0.2008 0.2276 -0.0292 -0.0071 -0.0004 213 ARG A CB  
937  C CG  . ARG A 122 ? 0.0888 0.1710 0.1981 -0.0307 -0.0030 0.0024  213 ARG A CG  
938  C CD  . ARG A 122 ? 0.1187 0.2087 0.2302 -0.0266 -0.0012 0.0018  213 ARG A CD  
939  N NE  . ARG A 122 ? 0.0689 0.1671 0.1901 -0.0276 0.0027  0.0037  213 ARG A NE  
940  C CZ  . ARG A 122 ? 0.0818 0.1833 0.2038 -0.0273 0.0109  0.0067  213 ARG A CZ  
941  N NH1 . ARG A 122 ? 0.0644 0.1611 0.1771 -0.0263 0.0151  0.0085  213 ARG A NH1 
942  N NH2 . ARG A 122 ? 0.0950 0.2043 0.2269 -0.0280 0.0151  0.0082  213 ARG A NH2 
943  N N   . HIS A 123 ? 0.0711 0.1270 0.1516 -0.0262 -0.0055 -0.0001 214 HIS A N   
944  C CA  . HIS A 123 ? 0.0530 0.1029 0.1263 -0.0233 -0.0057 -0.0015 214 HIS A CA  
945  C C   . HIS A 123 ? 0.0457 0.0980 0.1138 -0.0199 -0.0051 -0.0033 214 HIS A C   
946  O O   . HIS A 123 ? 0.1088 0.1665 0.1769 -0.0192 -0.0035 -0.0023 214 HIS A O   
947  C CB  . HIS A 123 ? 0.0728 0.1197 0.1441 -0.0233 -0.0041 0.0021  214 HIS A CB  
948  C CG  . HIS A 123 ? 0.1164 0.1595 0.1915 -0.0265 -0.0043 0.0050  214 HIS A CG  
949  N ND1 . HIS A 123 ? 0.0974 0.1376 0.1700 -0.0272 -0.0032 0.0095  214 HIS A ND1 
950  C CD2 . HIS A 123 ? 0.0855 0.1257 0.1658 -0.0296 -0.0059 0.0042  214 HIS A CD2 
951  C CE1 . HIS A 123 ? 0.0983 0.1340 0.1744 -0.0303 -0.0035 0.0118  214 HIS A CE1 
952  N NE2 . HIS A 123 ? 0.1122 0.1479 0.1937 -0.0321 -0.0051 0.0084  214 HIS A NE2 
953  N N   . SER A 124 ? 0.0514 0.0989 0.1148 -0.0178 -0.0056 -0.0058 215 SER A N   
954  C CA  . SER A 124 ? 0.0460 0.0941 0.1041 -0.0151 -0.0045 -0.0068 215 SER A CA  
955  C C   . SER A 124 ? 0.0699 0.1127 0.1254 -0.0136 -0.0030 -0.0078 215 SER A C   
956  O O   . SER A 124 ? 0.0581 0.0963 0.1149 -0.0137 -0.0028 -0.0087 215 SER A O   
957  C CB  . SER A 124 ? 0.0571 0.1064 0.1127 -0.0140 -0.0064 -0.0090 215 SER A CB  
958  O OG  . SER A 124 ? 0.0679 0.1117 0.1208 -0.0144 -0.0090 -0.0118 215 SER A OG  
959  N N   . VAL A 125 ? 0.0442 0.0875 0.0968 -0.0121 -0.0014 -0.0076 216 VAL A N   
960  C CA  . VAL A 125 ? 0.0457 0.0858 0.0983 -0.0108 0.0011  -0.0083 216 VAL A CA  
961  C C   . VAL A 125 ? 0.0639 0.1018 0.1095 -0.0096 0.0026  -0.0096 216 VAL A C   
962  O O   . VAL A 125 ? 0.0607 0.1009 0.1039 -0.0094 0.0015  -0.0090 216 VAL A O   
963  C CB  . VAL A 125 ? 0.0470 0.0895 0.1058 -0.0112 0.0010  -0.0056 216 VAL A CB  
964  C CG1 . VAL A 125 ? 0.0807 0.1261 0.1368 -0.0120 -0.0007 -0.0042 216 VAL A CG1 
965  C CG2 . VAL A 125 ? 0.0577 0.0989 0.1207 -0.0100 0.0042  -0.0060 216 VAL A CG2 
966  N N   . VAL A 126 ? 0.0540 0.0863 0.0954 -0.0084 0.0056  -0.0113 217 VAL A N   
967  C CA  . VAL A 126 ? 0.0596 0.0874 0.0917 -0.0072 0.0072  -0.0123 217 VAL A CA  
968  C C   . VAL A 126 ? 0.0660 0.0902 0.0984 -0.0066 0.0133  -0.0121 217 VAL A C   
969  O O   . VAL A 126 ? 0.0910 0.1139 0.1279 -0.0060 0.0165  -0.0126 217 VAL A O   
970  C CB  . VAL A 126 ? 0.0676 0.0898 0.0899 -0.0063 0.0044  -0.0147 217 VAL A CB  
971  C CG1 . VAL A 126 ? 0.0926 0.1090 0.1128 -0.0062 0.0053  -0.0170 217 VAL A CG1 
972  C CG2 . VAL A 126 ? 0.1379 0.1533 0.1481 -0.0047 0.0053  -0.0151 217 VAL A CG2 
973  N N   . VAL A 127 ? 0.0963 0.1189 0.1252 -0.0068 0.0155  -0.0110 218 VAL A N   
974  C CA  . VAL A 127 ? 0.0712 0.0908 0.1015 -0.0069 0.0223  -0.0102 218 VAL A CA  
975  C C   . VAL A 127 ? 0.0984 0.1092 0.1143 -0.0062 0.0248  -0.0102 218 VAL A C   
976  O O   . VAL A 127 ? 0.1015 0.1105 0.1097 -0.0057 0.0201  -0.0103 218 VAL A O   
977  C CB  . VAL A 127 ? 0.1405 0.1670 0.1841 -0.0091 0.0224  -0.0077 218 VAL A CB  
978  C CG1 . VAL A 127 ? 0.1289 0.1625 0.1867 -0.0094 0.0205  -0.0070 218 VAL A CG1 
979  C CG2 . VAL A 127 ? 0.1619 0.1894 0.2024 -0.0103 0.0175  -0.0070 218 VAL A CG2 
980  N N   . PRO A 128 ? 0.1272 0.1321 0.1394 -0.0059 0.0327  -0.0099 219 PRO A N   
981  C CA  . PRO A 128 ? 0.1552 0.1506 0.1533 -0.0057 0.0358  -0.0088 219 PRO A CA  
982  C C   . PRO A 128 ? 0.1639 0.1626 0.1680 -0.0080 0.0343  -0.0063 219 PRO A C   
983  O O   . PRO A 128 ? 0.1438 0.1511 0.1635 -0.0102 0.0335  -0.0053 219 PRO A O   
984  C CB  . PRO A 128 ? 0.1497 0.1393 0.1457 -0.0053 0.0467  -0.0085 219 PRO A CB  
985  C CG  . PRO A 128 ? 0.1335 0.1277 0.1391 -0.0040 0.0482  -0.0105 219 PRO A CG  
986  C CD  . PRO A 128 ? 0.0940 0.0999 0.1146 -0.0053 0.0399  -0.0102 219 PRO A CD  
987  N N   . CYS A 129 ? 0.2508 0.2413 0.2416 -0.0074 0.0329  -0.0054 220 CYS A N   
988  C CA  A CYS A 129 ? 0.2432 0.2327 0.2362 -0.0095 0.0323  -0.0032 220 CYS A CA  
989  C CA  B CYS A 129 ? 0.2479 0.2385 0.2430 -0.0098 0.0329  -0.0031 220 CYS A CA  
990  C C   . CYS A 129 ? 0.2411 0.2212 0.2274 -0.0110 0.0408  -0.0006 220 CYS A C   
991  O O   . CYS A 129 ? 0.2142 0.1843 0.1850 -0.0091 0.0448  -0.0006 220 CYS A O   
992  C CB  A CYS A 129 ? 0.2333 0.2190 0.2166 -0.0072 0.0251  -0.0035 220 CYS A CB  
993  C CB  B CYS A 129 ? 0.2424 0.2326 0.2330 -0.0084 0.0249  -0.0036 220 CYS A CB  
994  S SG  A CYS A 129 ? 0.2041 0.1980 0.1904 -0.0045 0.0166  -0.0062 220 CYS A SG  
995  S SG  B CYS A 129 ? 0.2453 0.2243 0.2161 -0.0044 0.0213  -0.0036 220 CYS A SG  
996  N N   . GLU A 130 ? 0.3206 0.3025 0.3170 -0.0148 0.0432  0.0016  221 GLU A N   
997  C CA  . GLU A 130 ? 0.4271 0.4011 0.4206 -0.0174 0.0519  0.0048  221 GLU A CA  
998  C C   . GLU A 130 ? 0.3495 0.3188 0.3421 -0.0200 0.0482  0.0066  221 GLU A C   
999  O O   . GLU A 130 ? 0.3404 0.3151 0.3392 -0.0201 0.0401  0.0050  221 GLU A O   
1000 C CB  . GLU A 130 ? 0.5360 0.5186 0.5491 -0.0206 0.0597  0.0060  221 GLU A CB  
1001 C CG  . GLU A 130 ? 0.6004 0.5955 0.6277 -0.0191 0.0567  0.0035  221 GLU A CG  
1002 C CD  . GLU A 130 ? 0.7102 0.7059 0.7409 -0.0175 0.0666  0.0034  221 GLU A CD  
1003 O OE1 . GLU A 130 ? 0.7332 0.7328 0.7785 -0.0202 0.0750  0.0058  221 GLU A OE1 
1004 O OE2 . GLU A 130 ? 0.7779 0.7698 0.7970 -0.0136 0.0664  0.0007  221 GLU A OE2 
1005 N N   . PRO A 131 ? 0.3456 0.3034 0.3293 -0.0219 0.0542  0.0098  222 PRO A N   
1006 C CA  . PRO A 131 ? 0.3267 0.2784 0.3103 -0.0249 0.0511  0.0115  222 PRO A CA  
1007 C C   . PRO A 131 ? 0.3812 0.3431 0.3876 -0.0305 0.0503  0.0117  222 PRO A C   
1008 O O   . PRO A 131 ? 0.3578 0.3307 0.3805 -0.0323 0.0542  0.0116  222 PRO A O   
1009 C CB  . PRO A 131 ? 0.3593 0.2955 0.3282 -0.0261 0.0596  0.0157  222 PRO A CB  
1010 C CG  . PRO A 131 ? 0.3594 0.2914 0.3139 -0.0220 0.0645  0.0153  222 PRO A CG  
1011 C CD  . PRO A 131 ? 0.3056 0.2530 0.2761 -0.0214 0.0646  0.0122  222 PRO A CD  
1012 N N   . PRO A 132 ? 0.3619 0.3198 0.3698 -0.0332 0.0445  0.0117  223 PRO A N   
1013 C CA  . PRO A 132 ? 0.2448 0.2111 0.2732 -0.0390 0.0414  0.0114  223 PRO A CA  
1014 C C   . PRO A 132 ? 0.3095 0.2783 0.3532 -0.0450 0.0505  0.0152  223 PRO A C   
1015 O O   . PRO A 132 ? 0.3406 0.2997 0.3757 -0.0459 0.0596  0.0185  223 PRO A O   
1016 C CB  . PRO A 132 ? 0.2380 0.1937 0.2586 -0.0404 0.0344  0.0106  223 PRO A CB  
1017 C CG  . PRO A 132 ? 0.3260 0.2732 0.3257 -0.0334 0.0319  0.0093  223 PRO A CG  
1018 C CD  . PRO A 132 ? 0.3405 0.2854 0.3314 -0.0306 0.0396  0.0115  223 PRO A CD  
1019 N N   . GLU A 133 ? 0.3679 0.3497 0.4350 -0.0491 0.0480  0.0149  224 GLU A N   
1020 C CA  . GLU A 133 ? 0.4530 0.4400 0.5389 -0.0548 0.0544  0.0183  224 GLU A CA  
1021 C C   . GLU A 133 ? 0.4932 0.4681 0.5747 -0.0601 0.0544  0.0207  224 GLU A C   
1022 O O   . GLU A 133 ? 0.4612 0.4242 0.5308 -0.0611 0.0485  0.0194  224 GLU A O   
1023 C CB  . GLU A 133 ? 0.4453 0.4483 0.5530 -0.0561 0.0462  0.0169  224 GLU A CB  
1024 N N   . VAL A 134 ? 0.5397 0.5172 0.6299 -0.0629 0.0607  0.0241  225 VAL A N   
1025 C CA  . VAL A 134 ? 0.5634 0.5297 0.6504 -0.0685 0.0614  0.0270  225 VAL A CA  
1026 C C   . VAL A 134 ? 0.5169 0.4830 0.6122 -0.0738 0.0488  0.0248  225 VAL A C   
1027 O O   . VAL A 134 ? 0.5407 0.5203 0.6531 -0.0755 0.0418  0.0230  225 VAL A O   
1028 C CB  . VAL A 134 ? 0.5494 0.5213 0.6482 -0.0711 0.0705  0.0307  225 VAL A CB  
1029 C CG1 . VAL A 134 ? 0.5052 0.4611 0.5919 -0.0748 0.0754  0.0346  225 VAL A CG1 
1030 C CG2 . VAL A 134 ? 0.5447 0.5226 0.6417 -0.0649 0.0806  0.0307  225 VAL A CG2 
1031 N N   . GLY A 135 ? 0.5074 0.4563 0.5883 -0.0759 0.0454  0.0248  226 GLY A N   
1032 C CA  . GLY A 135 ? 0.5062 0.4504 0.5896 -0.0804 0.0334  0.0218  226 GLY A CA  
1033 C C   . GLY A 135 ? 0.4833 0.4266 0.5604 -0.0766 0.0249  0.0165  226 GLY A C   
1034 O O   . GLY A 135 ? 0.5143 0.4521 0.5907 -0.0795 0.0144  0.0132  226 GLY A O   
1035 N N   . SER A 136 ? 0.3380 0.2870 0.4067 -0.0689 0.0277  0.0152  227 SER A N   
1036 C CA  . SER A 136 ? 0.2792 0.2295 0.3360 -0.0625 0.0189  0.0104  227 SER A CA  
1037 C C   . SER A 136 ? 0.2578 0.1955 0.2896 -0.0552 0.0206  0.0096  227 SER A C   
1038 O O   . SER A 136 ? 0.2826 0.2140 0.3058 -0.0536 0.0288  0.0129  227 SER A O   
1039 C CB  . SER A 136 ? 0.3394 0.3071 0.4067 -0.0590 0.0188  0.0093  227 SER A CB  
1040 O OG  . SER A 136 ? 0.4688 0.4377 0.5257 -0.0537 0.0108  0.0052  227 SER A OG  
1041 N N   . ASP A 137 ? 0.2314 0.1651 0.2513 -0.0506 0.0128  0.0054  228 ASP A N   
1042 C CA  . ASP A 137 ? 0.2398 0.1632 0.2393 -0.0431 0.0133  0.0046  228 ASP A CA  
1043 C C   . ASP A 137 ? 0.2070 0.1403 0.2020 -0.0356 0.0122  0.0024  228 ASP A C   
1044 O O   . ASP A 137 ? 0.1622 0.0896 0.1435 -0.0291 0.0123  0.0019  228 ASP A O   
1045 C CB  . ASP A 137 ? 0.2006 0.1094 0.1891 -0.0426 0.0069  0.0016  228 ASP A CB  
1046 C CG  . ASP A 137 ? 0.2707 0.1658 0.2605 -0.0497 0.0078  0.0040  228 ASP A CG  
1047 O OD1 . ASP A 137 ? 0.3310 0.2202 0.3184 -0.0511 0.0150  0.0085  228 ASP A OD1 
1048 O OD2 . ASP A 137 ? 0.3365 0.2253 0.3282 -0.0542 0.0012  0.0013  228 ASP A OD2 
1049 N N   . CYS A 138 ? 0.1568 0.1050 0.1642 -0.0364 0.0109  0.0013  229 CYS A N   
1050 C CA  . CYS A 138 ? 0.1328 0.0904 0.1375 -0.0304 0.0101  -0.0004 229 CYS A CA  
1051 C C   . CYS A 138 ? 0.1572 0.1288 0.1772 -0.0326 0.0125  0.0006  229 CYS A C   
1052 O O   . CYS A 138 ? 0.2264 0.2019 0.2606 -0.0383 0.0136  0.0022  229 CYS A O   
1053 C CB  . CYS A 138 ? 0.1629 0.1208 0.1623 -0.0273 0.0033  -0.0043 229 CYS A CB  
1054 S SG  . CYS A 138 ? 0.1945 0.1580 0.2052 -0.0331 -0.0035 -0.0060 229 CYS A SG  
1055 N N   . THR A 139 ? 0.1470 0.1261 0.1653 -0.0279 0.0134  -0.0002 230 THR A N   
1056 C CA  . THR A 139 ? 0.1298 0.1213 0.1618 -0.0290 0.0147  0.0002  230 THR A CA  
1057 C C   . THR A 139 ? 0.1710 0.1693 0.2052 -0.0276 0.0078  -0.0022 230 THR A C   
1058 O O   . THR A 139 ? 0.1727 0.1668 0.1964 -0.0247 0.0040  -0.0043 230 THR A O   
1059 C CB  . THR A 139 ? 0.2513 0.2448 0.2794 -0.0254 0.0209  0.0009  230 THR A CB  
1060 O OG1 . THR A 139 ? 0.2791 0.2717 0.2957 -0.0201 0.0178  -0.0010 230 THR A OG1 
1061 C CG2 . THR A 139 ? 0.1908 0.1748 0.2119 -0.0264 0.0281  0.0035  230 THR A CG2 
1062 N N   . THR A 140 ? 0.0965 0.1048 0.1447 -0.0294 0.0067  -0.0017 231 THR A N   
1063 C CA  . THR A 140 ? 0.0922 0.1057 0.1422 -0.0287 0.0000  -0.0031 231 THR A CA  
1064 C C   . THR A 140 ? 0.1459 0.1688 0.2037 -0.0266 0.0020  -0.0025 231 THR A C   
1065 O O   . THR A 140 ? 0.1072 0.1351 0.1771 -0.0277 0.0064  -0.0008 231 THR A O   
1066 C CB  . THR A 140 ? 0.1639 0.1776 0.2229 -0.0339 -0.0066 -0.0029 231 THR A CB  
1067 O OG1 . THR A 140 ? 0.2297 0.2323 0.2793 -0.0360 -0.0087 -0.0041 231 THR A OG1 
1068 C CG2 . THR A 140 ? 0.1600 0.1770 0.2179 -0.0332 -0.0139 -0.0039 231 THR A CG2 
1069 N N   . ILE A 141 ? 0.0764 0.1011 0.1276 -0.0233 -0.0004 -0.0037 232 ILE A N   
1070 C CA  . ILE A 141 ? 0.0681 0.1002 0.1262 -0.0217 -0.0002 -0.0032 232 ILE A CA  
1071 C C   . ILE A 141 ? 0.0946 0.1293 0.1560 -0.0231 -0.0074 -0.0028 232 ILE A C   
1072 O O   . ILE A 141 ? 0.1137 0.1434 0.1652 -0.0235 -0.0116 -0.0039 232 ILE A O   
1073 C CB  . ILE A 141 ? 0.1094 0.1413 0.1584 -0.0178 0.0020  -0.0043 232 ILE A CB  
1074 C CG1 . ILE A 141 ? 0.2202 0.2474 0.2630 -0.0163 0.0073  -0.0047 232 ILE A CG1 
1075 C CG2 . ILE A 141 ? 0.0965 0.1343 0.1525 -0.0166 0.0021  -0.0038 232 ILE A CG2 
1076 C CD1 . ILE A 141 ? 0.1995 0.2263 0.2345 -0.0129 0.0075  -0.0059 232 ILE A CD1 
1077 N N   . HIS A 142 ? 0.0890 0.1301 0.1631 -0.0236 -0.0087 -0.0011 233 HIS A N   
1078 C CA  A HIS A 142 ? 0.0870 0.1297 0.1632 -0.0245 -0.0164 -0.0001 233 HIS A CA  
1079 C CA  B HIS A 142 ? 0.0871 0.1298 0.1635 -0.0245 -0.0164 -0.0001 233 HIS A CA  
1080 C C   . HIS A 142 ? 0.0703 0.1150 0.1434 -0.0215 -0.0156 0.0004  233 HIS A C   
1081 O O   . HIS A 142 ? 0.0750 0.1240 0.1570 -0.0199 -0.0120 0.0011  233 HIS A O   
1082 C CB  A HIS A 142 ? 0.1004 0.1485 0.1948 -0.0272 -0.0202 0.0019  233 HIS A CB  
1083 C CB  B HIS A 142 ? 0.0935 0.1422 0.1888 -0.0270 -0.0199 0.0021  233 HIS A CB  
1084 C CG  A HIS A 142 ? 0.1164 0.1628 0.2161 -0.0312 -0.0207 0.0017  233 HIS A CG  
1085 C CG  B HIS A 142 ? 0.1252 0.1720 0.2256 -0.0314 -0.0233 0.0020  233 HIS A CG  
1086 N ND1 A HIS A 142 ? 0.1191 0.1672 0.2266 -0.0319 -0.0127 0.0021  233 HIS A ND1 
1087 N ND1 B HIS A 142 ? 0.1217 0.1722 0.2346 -0.0323 -0.0243 0.0036  233 HIS A ND1 
1088 C CD2 A HIS A 142 ? 0.1362 0.1777 0.2330 -0.0350 -0.0282 0.0012  233 HIS A CD2 
1089 C CD2 B HIS A 142 ? 0.1310 0.1697 0.2196 -0.0335 -0.0246 0.0002  233 HIS A CD2 
1090 C CE1 A HIS A 142 ? 0.1334 0.1782 0.2433 -0.0360 -0.0147 0.0022  233 HIS A CE1 
1091 C CE1 B HIS A 142 ? 0.1501 0.1968 0.2632 -0.0364 -0.0271 0.0030  233 HIS A CE1 
1092 N NE2 A HIS A 142 ? 0.1307 0.1714 0.2345 -0.0380 -0.0245 0.0014  233 HIS A NE2 
1093 N NE2 B HIS A 142 ? 0.1359 0.1753 0.2362 -0.0380 -0.0281 0.0010  233 HIS A NE2 
1094 N N   . TYR A 143 ? 0.0866 0.1273 0.1468 -0.0208 -0.0184 0.0000  234 TYR A N   
1095 C CA  . TYR A 143 ? 0.0759 0.1177 0.1328 -0.0189 -0.0178 0.0010  234 TYR A CA  
1096 C C   . TYR A 143 ? 0.0880 0.1285 0.1448 -0.0199 -0.0248 0.0035  234 TYR A C   
1097 O O   . TYR A 143 ? 0.0675 0.1046 0.1213 -0.0220 -0.0310 0.0037  234 TYR A O   
1098 C CB  . TYR A 143 ? 0.0626 0.1014 0.1061 -0.0174 -0.0147 -0.0005 234 TYR A CB  
1099 C CG  . TYR A 143 ? 0.0726 0.1124 0.1159 -0.0157 -0.0092 -0.0025 234 TYR A CG  
1100 C CD1 . TYR A 143 ? 0.0689 0.1119 0.1173 -0.0145 -0.0060 -0.0025 234 TYR A CD1 
1101 C CD2 . TYR A 143 ? 0.1264 0.1623 0.1626 -0.0152 -0.0079 -0.0043 234 TYR A CD2 
1102 C CE1 . TYR A 143 ? 0.0729 0.1152 0.1186 -0.0130 -0.0024 -0.0043 234 TYR A CE1 
1103 C CE2 . TYR A 143 ? 0.1003 0.1360 0.1351 -0.0133 -0.0041 -0.0055 234 TYR A CE2 
1104 C CZ  . TYR A 143 ? 0.0480 0.0869 0.0870 -0.0123 -0.0017 -0.0055 234 TYR A CZ  
1105 O OH  . TYR A 143 ? 0.0600 0.0972 0.0954 -0.0105 0.0007  -0.0067 234 TYR A OH  
1106 N N   . ASN A 144 ? 0.0992 0.1413 0.1586 -0.0186 -0.0245 0.0055  235 ASN A N   
1107 C CA  . ASN A 144 ? 0.1129 0.1519 0.1690 -0.0190 -0.0308 0.0085  235 ASN A CA  
1108 C C   . ASN A 144 ? 0.0763 0.1124 0.1219 -0.0181 -0.0273 0.0095  235 ASN A C   
1109 O O   . ASN A 144 ? 0.1162 0.1554 0.1663 -0.0171 -0.0218 0.0088  235 ASN A O   
1110 C CB  . ASN A 144 ? 0.1147 0.1576 0.1867 -0.0182 -0.0343 0.0111  235 ASN A CB  
1111 C CG  . ASN A 144 ? 0.1584 0.2065 0.2460 -0.0191 -0.0371 0.0108  235 ASN A CG  
1112 O OD1 . ASN A 144 ? 0.2362 0.2893 0.3394 -0.0174 -0.0354 0.0117  235 ASN A OD1 
1113 N ND2 . ASN A 144 ? 0.1483 0.1943 0.2317 -0.0217 -0.0406 0.0095  235 ASN A ND2 
1114 N N   . TYR A 145 ? 0.0799 0.1094 0.1113 -0.0189 -0.0302 0.0112  236 TYR A N   
1115 C CA  . TYR A 145 ? 0.0901 0.1166 0.1122 -0.0186 -0.0262 0.0130  236 TYR A CA  
1116 C C   . TYR A 145 ? 0.1069 0.1292 0.1285 -0.0189 -0.0314 0.0176  236 TYR A C   
1117 O O   . TYR A 145 ? 0.1031 0.1201 0.1190 -0.0194 -0.0392 0.0194  236 TYR A O   
1118 C CB  . TYR A 145 ? 0.0946 0.1153 0.0991 -0.0187 -0.0235 0.0120  236 TYR A CB  
1119 C CG  . TYR A 145 ? 0.0872 0.1118 0.0929 -0.0176 -0.0178 0.0079  236 TYR A CG  
1120 C CD1 . TYR A 145 ? 0.0865 0.1101 0.0925 -0.0177 -0.0203 0.0050  236 TYR A CD1 
1121 C CD2 . TYR A 145 ? 0.1414 0.1703 0.1492 -0.0166 -0.0106 0.0073  236 TYR A CD2 
1122 C CE1 . TYR A 145 ? 0.0998 0.1254 0.1060 -0.0163 -0.0155 0.0018  236 TYR A CE1 
1123 C CE2 . TYR A 145 ? 0.0763 0.1086 0.0859 -0.0150 -0.0066 0.0040  236 TYR A CE2 
1124 C CZ  . TYR A 145 ? 0.1545 0.1844 0.1624 -0.0146 -0.0090 0.0014  236 TYR A CZ  
1125 O OH  . TYR A 145 ? 0.1137 0.1454 0.1223 -0.0126 -0.0054 -0.0014 236 TYR A OH  
1126 N N   . MET A 146 ? 0.0926 0.1162 0.1197 -0.0185 -0.0280 0.0195  237 MET A N   
1127 C CA  . MET A 146 ? 0.0951 0.1152 0.1263 -0.0181 -0.0331 0.0237  237 MET A CA  
1128 C C   . MET A 146 ? 0.1096 0.1209 0.1264 -0.0192 -0.0326 0.0283  237 MET A C   
1129 O O   . MET A 146 ? 0.1277 0.1347 0.1470 -0.0188 -0.0363 0.0323  237 MET A O   
1130 C CB  . MET A 146 ? 0.0845 0.1097 0.1324 -0.0167 -0.0304 0.0228  237 MET A CB  
1131 C CG  . MET A 146 ? 0.0733 0.1059 0.1347 -0.0154 -0.0297 0.0190  237 MET A CG  
1132 S SD  . MET A 146 ? 0.1101 0.1445 0.1793 -0.0150 -0.0385 0.0200  237 MET A SD  
1133 C CE  . MET A 146 ? 0.1422 0.1731 0.2192 -0.0129 -0.0452 0.0252  237 MET A CE  
1134 N N   . CYS A 147 ? 0.1162 0.1243 0.1180 -0.0204 -0.0276 0.0279  238 CYS A N   
1135 C CA  . CYS A 147 ? 0.1340 0.1321 0.1184 -0.0217 -0.0263 0.0325  238 CYS A CA  
1136 C C   . CYS A 147 ? 0.1571 0.1490 0.1223 -0.0217 -0.0257 0.0311  238 CYS A C   
1137 O O   . CYS A 147 ? 0.1404 0.1373 0.1073 -0.0211 -0.0229 0.0263  238 CYS A O   
1138 C CB  . CYS A 147 ? 0.1850 0.1849 0.1711 -0.0233 -0.0168 0.0340  238 CYS A CB  
1139 S SG  . CYS A 147 ? 0.1512 0.1489 0.1482 -0.0243 -0.0178 0.0383  238 CYS A SG  
1140 N N   . TYR A 148 ? 0.1766 0.1558 0.1214 -0.0223 -0.0282 0.0352  239 TYR A N   
1141 C CA  . TYR A 148 ? 0.1843 0.1549 0.1066 -0.0222 -0.0249 0.0338  239 TYR A CA  
1142 C C   . TYR A 148 ? 0.1826 0.1570 0.1034 -0.0224 -0.0109 0.0332  239 TYR A C   
1143 O O   . TYR A 148 ? 0.1778 0.1562 0.1078 -0.0237 -0.0051 0.0363  239 TYR A O   
1144 C CB  . TYR A 148 ? 0.2416 0.1955 0.1393 -0.0228 -0.0309 0.0386  239 TYR A CB  
1145 C CG  . TYR A 148 ? 0.2659 0.2150 0.1624 -0.0226 -0.0461 0.0387  239 TYR A CG  
1146 C CD1 . TYR A 148 ? 0.2844 0.2325 0.1768 -0.0225 -0.0517 0.0338  239 TYR A CD1 
1147 C CD2 . TYR A 148 ? 0.2920 0.2374 0.1928 -0.0225 -0.0554 0.0440  239 TYR A CD2 
1148 C CE1 . TYR A 148 ? 0.3661 0.3106 0.2598 -0.0230 -0.0666 0.0341  239 TYR A CE1 
1149 C CE2 . TYR A 148 ? 0.3058 0.2483 0.2086 -0.0221 -0.0704 0.0445  239 TYR A CE2 
1150 C CZ  . TYR A 148 ? 0.3349 0.2775 0.2348 -0.0227 -0.0760 0.0395  239 TYR A CZ  
1151 O OH  . TYR A 148 ? 0.4140 0.3546 0.3184 -0.0230 -0.0916 0.0400  239 TYR A OH  
1152 N N   . SER A 149 ? 0.1988 0.1710 0.1082 -0.0211 -0.0057 0.0294  240 SER A N   
1153 C CA  . SER A 149 ? 0.1917 0.1663 0.0982 -0.0206 0.0080  0.0295  240 SER A CA  
1154 C C   . SER A 149 ? 0.2181 0.1835 0.1108 -0.0225 0.0138  0.0360  240 SER A C   
1155 O O   . SER A 149 ? 0.2079 0.1796 0.1089 -0.0235 0.0247  0.0380  240 SER A O   
1156 C CB  . SER A 149 ? 0.2017 0.1712 0.0933 -0.0180 0.0124  0.0248  240 SER A CB  
1157 O OG  . SER A 149 ? 0.1827 0.1624 0.0900 -0.0164 0.0105  0.0193  240 SER A OG  
1158 N N   . SER A 150 ? 0.2315 0.1820 0.1040 -0.0231 0.0063  0.0396  241 SER A N   
1159 C CA  . SER A 150 ? 0.2761 0.2143 0.1306 -0.0248 0.0112  0.0465  241 SER A CA  
1160 C C   . SER A 150 ? 0.2480 0.1888 0.1168 -0.0273 0.0085  0.0521  241 SER A C   
1161 O O   . SER A 150 ? 0.2681 0.1976 0.1224 -0.0292 0.0122  0.0586  241 SER A O   
1162 C CB  . SER A 150 ? 0.3268 0.2449 0.1497 -0.0242 0.0028  0.0482  241 SER A CB  
1163 O OG  . SER A 150 ? 0.3535 0.2708 0.1833 -0.0243 -0.0134 0.0489  241 SER A OG  
1164 N N   . CYS A 151 ? 0.2234 0.1768 0.1182 -0.0274 0.0027  0.0500  242 CYS A N   
1165 C CA  . CYS A 151 ? 0.2197 0.1730 0.1264 -0.0291 -0.0010 0.0547  242 CYS A CA  
1166 C C   . CYS A 151 ? 0.2429 0.1980 0.1544 -0.0323 0.0112  0.0587  242 CYS A C   
1167 O O   . CYS A 151 ? 0.2227 0.1911 0.1516 -0.0332 0.0189  0.0554  242 CYS A O   
1168 C CB  . CYS A 151 ? 0.1962 0.1624 0.1290 -0.0280 -0.0076 0.0506  242 CYS A CB  
1169 S SG  . CYS A 151 ? 0.2375 0.2010 0.1725 -0.0253 -0.0240 0.0495  242 CYS A SG  
1170 N N   . MET A 152 ? 0.2433 0.1850 0.1408 -0.0344 0.0121  0.0660  243 MET A N   
1171 C CA  . MET A 152 ? 0.2492 0.1911 0.1504 -0.0384 0.0242  0.0707  243 MET A CA  
1172 C C   . MET A 152 ? 0.2294 0.1814 0.1582 -0.0406 0.0227  0.0702  243 MET A C   
1173 O O   . MET A 152 ? 0.2277 0.1780 0.1643 -0.0393 0.0122  0.0701  243 MET A O   
1174 C CB  . MET A 152 ? 0.3188 0.2410 0.1947 -0.0401 0.0256  0.0794  243 MET A CB  
1175 C CG  . MET A 152 ? 0.3884 0.2979 0.2327 -0.0382 0.0285  0.0799  243 MET A CG  
1176 S SD  . MET A 152 ? 0.4402 0.3616 0.2876 -0.0375 0.0451  0.0744  243 MET A SD  
1177 C CE  . MET A 152 ? 0.4662 0.3866 0.3169 -0.0425 0.0618  0.0821  243 MET A CE  
1178 N N   . GLY A 153 ? 0.2405 0.2027 0.1845 -0.0439 0.0332  0.0697  244 GLY A N   
1179 C CA  . GLY A 153 ? 0.2183 0.1902 0.1879 -0.0463 0.0315  0.0678  244 GLY A CA  
1180 C C   . GLY A 153 ? 0.3163 0.3023 0.3029 -0.0433 0.0265  0.0595  244 GLY A C   
1181 O O   . GLY A 153 ? 0.2780 0.2716 0.2840 -0.0451 0.0252  0.0569  244 GLY A O   
1182 N N   . GLY A 154 ? 0.2302 0.2181 0.2085 -0.0391 0.0232  0.0553  245 GLY A N   
1183 C CA  . GLY A 154 ? 0.1807 0.1813 0.1727 -0.0366 0.0208  0.0479  245 GLY A CA  
1184 C C   . GLY A 154 ? 0.1875 0.1943 0.1753 -0.0352 0.0289  0.0453  245 GLY A C   
1185 O O   . GLY A 154 ? 0.1783 0.1891 0.1702 -0.0376 0.0387  0.0474  245 GLY A O   
1186 N N   . MET A 155 ? 0.1507 0.1577 0.1308 -0.0314 0.0252  0.0410  246 MET A N   
1187 C CA  . MET A 155 ? 0.1527 0.1637 0.1278 -0.0293 0.0329  0.0380  246 MET A CA  
1188 C C   . MET A 155 ? 0.1759 0.1780 0.1328 -0.0301 0.0426  0.0426  246 MET A C   
1189 O O   . MET A 155 ? 0.1852 0.1929 0.1443 -0.0293 0.0531  0.0417  246 MET A O   
1190 C CB  . MET A 155 ? 0.2129 0.2223 0.1804 -0.0255 0.0263  0.0330  246 MET A CB  
1191 C CG  . MET A 155 ? 0.1377 0.1581 0.1241 -0.0243 0.0211  0.0280  246 MET A CG  
1192 S SD  . MET A 155 ? 0.1594 0.1775 0.1385 -0.0209 0.0143  0.0227  246 MET A SD  
1193 C CE  . MET A 155 ? 0.1383 0.1474 0.1115 -0.0218 0.0028  0.0254  246 MET A CE  
1194 N N   . ASN A 156 ? 0.1941 0.1817 0.1328 -0.0315 0.0397  0.0479  247 ASN A N   
1195 C CA  . ASN A 156 ? 0.2220 0.1997 0.1436 -0.0334 0.0502  0.0537  247 ASN A CA  
1196 C C   . ASN A 156 ? 0.2567 0.2304 0.1606 -0.0300 0.0585  0.0510  247 ASN A C   
1197 O O   . ASN A 156 ? 0.2677 0.2418 0.1683 -0.0306 0.0724  0.0533  247 ASN A O   
1198 C CB  . ASN A 156 ? 0.2705 0.2574 0.2115 -0.0376 0.0599  0.0572  247 ASN A CB  
1199 C CG  . ASN A 156 ? 0.3380 0.3118 0.2660 -0.0417 0.0647  0.0657  247 ASN A CG  
1200 O OD1 . ASN A 156 ? 0.3527 0.3195 0.2809 -0.0437 0.0564  0.0692  247 ASN A OD1 
1201 N ND2 . ASN A 156 ? 0.3535 0.3237 0.2707 -0.0427 0.0790  0.0693  247 ASN A ND2 
1202 N N   . ARG A 157 ? 0.2639 0.2335 0.1570 -0.0264 0.0505  0.0458  248 ARG A N   
1203 C CA  . ARG A 157 ? 0.2444 0.2081 0.1196 -0.0226 0.0559  0.0417  248 ARG A CA  
1204 C C   . ARG A 157 ? 0.3000 0.2791 0.1943 -0.0201 0.0652  0.0371  248 ARG A C   
1205 O O   . ARG A 157 ? 0.3335 0.3083 0.2149 -0.0164 0.0727  0.0339  248 ARG A O   
1206 C CB  . ARG A 157 ? 0.3429 0.2889 0.1873 -0.0227 0.0651  0.0462  248 ARG A CB  
1207 C CG  . ARG A 157 ? 0.3748 0.3050 0.2006 -0.0255 0.0565  0.0525  248 ARG A CG  
1208 C CD  . ARG A 157 ? 0.5465 0.4604 0.3438 -0.0244 0.0622  0.0555  248 ARG A CD  
1209 N NE  . ARG A 157 ? 0.6797 0.5810 0.4538 -0.0209 0.0542  0.0504  248 ARG A NE  
1210 C CZ  . ARG A 157 ? 0.7860 0.6740 0.5437 -0.0211 0.0391  0.0513  248 ARG A CZ  
1211 N NH1 . ARG A 157 ? 0.8720 0.7497 0.6118 -0.0185 0.0319  0.0459  248 ARG A NH1 
1212 N NH2 . ARG A 157 ? 0.7571 0.6421 0.5180 -0.0239 0.0305  0.0573  248 ARG A NH2 
1213 N N   . ARG A 158 ? 0.2040 0.2002 0.1283 -0.0216 0.0643  0.0363  249 ARG A N   
1214 C CA  . ARG A 158 ? 0.1900 0.2010 0.1334 -0.0188 0.0710  0.0321  249 ARG A CA  
1215 C C   . ARG A 158 ? 0.1780 0.1917 0.1247 -0.0154 0.0616  0.0256  249 ARG A C   
1216 O O   . ARG A 158 ? 0.1728 0.1867 0.1244 -0.0168 0.0500  0.0247  249 ARG A O   
1217 C CB  . ARG A 158 ? 0.1728 0.1996 0.1454 -0.0223 0.0733  0.0343  249 ARG A CB  
1218 C CG  . ARG A 158 ? 0.2005 0.2257 0.1730 -0.0264 0.0844  0.0411  249 ARG A CG  
1219 C CD  . ARG A 158 ? 0.2243 0.2626 0.2251 -0.0313 0.0835  0.0434  249 ARG A CD  
1220 N NE  . ARG A 158 ? 0.1906 0.2252 0.1940 -0.0341 0.0708  0.0438  249 ARG A NE  
1221 C CZ  . ARG A 158 ? 0.2025 0.2451 0.2272 -0.0382 0.0671  0.0446  249 ARG A CZ  
1222 N NH1 . ARG A 158 ? 0.1443 0.2002 0.1909 -0.0406 0.0740  0.0452  249 ARG A NH1 
1223 N NH2 . ARG A 158 ? 0.1442 0.1814 0.1690 -0.0397 0.0564  0.0446  249 ARG A NH2 
1224 N N   . PRO A 159 ? 0.1781 0.1934 0.1227 -0.0108 0.0669  0.0212  250 PRO A N   
1225 C CA  . PRO A 159 ? 0.1894 0.2065 0.1376 -0.0079 0.0585  0.0155  250 PRO A CA  
1226 C C   . PRO A 159 ? 0.1411 0.1737 0.1165 -0.0088 0.0537  0.0143  250 PRO A C   
1227 O O   . PRO A 159 ? 0.1335 0.1779 0.1274 -0.0098 0.0592  0.0161  250 PRO A O   
1228 C CB  . PRO A 159 ? 0.2286 0.2429 0.1685 -0.0025 0.0674  0.0118  250 PRO A CB  
1229 C CG  . PRO A 159 ? 0.2586 0.2778 0.2030 -0.0023 0.0819  0.0155  250 PRO A CG  
1230 C CD  . PRO A 159 ? 0.2239 0.2376 0.1612 -0.0077 0.0815  0.0215  250 PRO A CD  
1231 N N   . ILE A 160 ? 0.1303 0.1621 0.1074 -0.0086 0.0433  0.0113  251 ILE A N   
1232 C CA  . ILE A 160 ? 0.1102 0.1535 0.1081 -0.0089 0.0384  0.0096  251 ILE A CA  
1233 C C   . ILE A 160 ? 0.1059 0.1489 0.1032 -0.0050 0.0356  0.0048  251 ILE A C   
1234 O O   . ILE A 160 ? 0.1164 0.1490 0.0975 -0.0032 0.0343  0.0026  251 ILE A O   
1235 C CB  . ILE A 160 ? 0.1015 0.1441 0.1039 -0.0126 0.0295  0.0110  251 ILE A CB  
1236 C CG1 . ILE A 160 ? 0.1579 0.1904 0.1466 -0.0125 0.0219  0.0097  251 ILE A CG1 
1237 C CG2 . ILE A 160 ? 0.1063 0.1484 0.1105 -0.0165 0.0319  0.0161  251 ILE A CG2 
1238 C CD1 . ILE A 160 ? 0.1200 0.1547 0.1183 -0.0143 0.0136  0.0095  251 ILE A CD1 
1239 N N   . LEU A 161 ? 0.0923 0.1454 0.1065 -0.0039 0.0340  0.0032  252 LEU A N   
1240 C CA  . LEU A 161 ? 0.0971 0.1496 0.1125 -0.0012 0.0292  -0.0005 252 LEU A CA  
1241 C C   . LEU A 161 ? 0.0896 0.1436 0.1115 -0.0041 0.0212  -0.0005 252 LEU A C   
1242 O O   . LEU A 161 ? 0.1179 0.1770 0.1492 -0.0070 0.0200  0.0014  252 LEU A O   
1243 C CB  . LEU A 161 ? 0.1236 0.1852 0.1521 0.0028  0.0327  -0.0019 252 LEU A CB  
1244 C CG  . LEU A 161 ? 0.2684 0.3322 0.2969 0.0061  0.0427  -0.0014 252 LEU A CG  
1245 C CD1 . LEU A 161 ? 0.3246 0.3986 0.3697 0.0106  0.0442  -0.0027 252 LEU A CD1 
1246 C CD2 . LEU A 161 ? 0.2856 0.3356 0.2924 0.0087  0.0456  -0.0034 252 LEU A CD2 
1247 N N   . THR A 162 ? 0.0756 0.1241 0.0920 -0.0033 0.0165  -0.0029 253 THR A N   
1248 C CA  . THR A 162 ? 0.0637 0.1142 0.0873 -0.0047 0.0111  -0.0035 253 THR A CA  
1249 C C   . THR A 162 ? 0.1171 0.1703 0.1455 -0.0013 0.0109  -0.0057 253 THR A C   
1250 O O   . THR A 162 ? 0.0942 0.1431 0.1162 0.0018  0.0122  -0.0074 253 THR A O   
1251 C CB  . THR A 162 ? 0.0892 0.1325 0.1059 -0.0065 0.0064  -0.0039 253 THR A CB  
1252 O OG1 . THR A 162 ? 0.1204 0.1611 0.1333 -0.0091 0.0051  -0.0014 253 THR A OG1 
1253 C CG2 . THR A 162 ? 0.0928 0.1380 0.1169 -0.0074 0.0030  -0.0046 253 THR A CG2 
1254 N N   . ILE A 163 ? 0.0625 0.1219 0.1011 -0.0018 0.0089  -0.0056 254 ILE A N   
1255 C CA  . ILE A 163 ? 0.0520 0.1128 0.0940 0.0012  0.0068  -0.0072 254 ILE A CA  
1256 C C   . ILE A 163 ? 0.0501 0.1054 0.0880 -0.0001 0.0029  -0.0080 254 ILE A C   
1257 O O   . ILE A 163 ? 0.0466 0.1024 0.0872 -0.0029 0.0012  -0.0075 254 ILE A O   
1258 C CB  . ILE A 163 ? 0.0565 0.1265 0.1114 0.0014  0.0060  -0.0066 254 ILE A CB  
1259 C CG1 . ILE A 163 ? 0.1027 0.1795 0.1645 0.0022  0.0117  -0.0052 254 ILE A CG1 
1260 C CG2 . ILE A 163 ? 0.0495 0.1197 0.1065 0.0049  0.0021  -0.0080 254 ILE A CG2 
1261 C CD1 . ILE A 163 ? 0.1899 0.2770 0.2677 0.0006  0.0108  -0.0040 254 ILE A CD1 
1262 N N   . ILE A 164 ? 0.0540 0.1033 0.0854 0.0022  0.0022  -0.0092 255 ILE A N   
1263 C CA  . ILE A 164 ? 0.0544 0.0980 0.0817 0.0011  0.0001  -0.0096 255 ILE A CA  
1264 C C   . ILE A 164 ? 0.1159 0.1586 0.1427 0.0040  -0.0023 -0.0101 255 ILE A C   
1265 O O   . ILE A 164 ? 0.0615 0.1033 0.0873 0.0078  -0.0025 -0.0104 255 ILE A O   
1266 C CB  . ILE A 164 ? 0.0643 0.1002 0.0841 0.0005  0.0008  -0.0099 255 ILE A CB  
1267 C CG1 . ILE A 164 ? 0.0585 0.0945 0.0778 -0.0023 0.0012  -0.0093 255 ILE A CG1 
1268 C CG2 . ILE A 164 ? 0.0673 0.0984 0.0849 -0.0010 0.0002  -0.0096 255 ILE A CG2 
1269 C CD1 . ILE A 164 ? 0.0529 0.0924 0.0780 -0.0055 0.0003  -0.0080 255 ILE A CD1 
1270 N N   . THR A 165 ? 0.0768 0.1184 0.1032 0.0028  -0.0045 -0.0103 256 THR A N   
1271 C CA  A THR A 165 ? 0.0713 0.1099 0.0944 0.0054  -0.0082 -0.0107 256 THR A CA  
1272 C CA  B THR A 165 ? 0.0801 0.1189 0.1034 0.0053  -0.0083 -0.0107 256 THR A CA  
1273 C C   . THR A 165 ? 0.0899 0.1186 0.1022 0.0046  -0.0078 -0.0107 256 THR A C   
1274 O O   . THR A 165 ? 0.0822 0.1093 0.0936 0.0018  -0.0054 -0.0109 256 THR A O   
1275 C CB  A THR A 165 ? 0.1140 0.1586 0.1442 0.0048  -0.0123 -0.0112 256 THR A CB  
1276 C CB  B THR A 165 ? 0.1051 0.1498 0.1356 0.0042  -0.0121 -0.0112 256 THR A CB  
1277 O OG1 A THR A 165 ? 0.0983 0.1430 0.1297 0.0010  -0.0113 -0.0116 256 THR A OG1 
1278 O OG1 B THR A 165 ? 0.1390 0.1937 0.1813 0.0047  -0.0115 -0.0107 256 THR A OG1 
1279 C CG2 A THR A 165 ? 0.1236 0.1786 0.1662 0.0061  -0.0122 -0.0106 256 THR A CG2 
1280 C CG2 B THR A 165 ? 0.0996 0.1397 0.1246 0.0065  -0.0179 -0.0118 256 THR A CG2 
1281 N N   . LEU A 166 ? 0.0875 0.1092 0.0918 0.0076  -0.0094 -0.0103 257 LEU A N   
1282 C CA  . LEU A 166 ? 0.1470 0.1576 0.1388 0.0073  -0.0087 -0.0097 257 LEU A CA  
1283 C C   . LEU A 166 ? 0.1427 0.1511 0.1297 0.0086  -0.0141 -0.0105 257 LEU A C   
1284 O O   . LEU A 166 ? 0.1618 0.1738 0.1527 0.0114  -0.0200 -0.0106 257 LEU A O   
1285 C CB  . LEU A 166 ? 0.0975 0.0995 0.0812 0.0097  -0.0081 -0.0083 257 LEU A CB  
1286 C CG  . LEU A 166 ? 0.1428 0.1321 0.1130 0.0087  -0.0051 -0.0068 257 LEU A CG  
1287 C CD1 . LEU A 166 ? 0.1222 0.1120 0.0961 0.0042  0.0015  -0.0065 257 LEU A CD1 
1288 C CD2 . LEU A 166 ? 0.1419 0.1217 0.1040 0.0118  -0.0063 -0.0051 257 LEU A CD2 
1289 N N   . GLU A 167 ? 0.1199 0.1221 0.0990 0.0065  -0.0125 -0.0113 258 GLU A N   
1290 C CA  . GLU A 167 ? 0.1171 0.1155 0.0898 0.0069  -0.0181 -0.0129 258 GLU A CA  
1291 C C   . GLU A 167 ? 0.1282 0.1112 0.0811 0.0074  -0.0158 -0.0127 258 GLU A C   
1292 O O   . GLU A 167 ? 0.1366 0.1151 0.0856 0.0059  -0.0077 -0.0119 258 GLU A O   
1293 C CB  . GLU A 167 ? 0.1250 0.1291 0.1058 0.0039  -0.0179 -0.0149 258 GLU A CB  
1294 C CG  . GLU A 167 ? 0.1752 0.1930 0.1739 0.0025  -0.0188 -0.0148 258 GLU A CG  
1295 C CD  . GLU A 167 ? 0.2201 0.2405 0.2245 -0.0007 -0.0179 -0.0163 258 GLU A CD  
1296 O OE1 . GLU A 167 ? 0.2105 0.2227 0.2063 -0.0016 -0.0149 -0.0176 258 GLU A OE1 
1297 O OE2 . GLU A 167 ? 0.1994 0.2294 0.2169 -0.0023 -0.0198 -0.0160 258 GLU A OE2 
1298 N N   . ASP A 168 ? 0.1430 0.1178 0.0837 0.0092  -0.0230 -0.0134 259 ASP A N   
1299 C CA  . ASP A 168 ? 0.1628 0.1211 0.0815 0.0094  -0.0201 -0.0136 259 ASP A CA  
1300 C C   . ASP A 168 ? 0.1640 0.1204 0.0811 0.0069  -0.0162 -0.0167 259 ASP A C   
1301 O O   . ASP A 168 ? 0.1633 0.1310 0.0966 0.0049  -0.0165 -0.0182 259 ASP A O   
1302 C CB  . ASP A 168 ? 0.1827 0.1296 0.0846 0.0124  -0.0298 -0.0132 259 ASP A CB  
1303 C CG  . ASP A 168 ? 0.2446 0.1949 0.1502 0.0122  -0.0411 -0.0160 259 ASP A CG  
1304 O OD1 . ASP A 168 ? 0.2119 0.1689 0.1274 0.0092  -0.0404 -0.0188 259 ASP A OD1 
1305 O OD2 . ASP A 168 ? 0.2849 0.2303 0.1834 0.0148  -0.0516 -0.0153 259 ASP A OD2 
1306 N N   . SER A 169 ? 0.1837 0.1245 0.0800 0.0073  -0.0119 -0.0175 260 SER A N   
1307 C CA  . SER A 169 ? 0.1873 0.1244 0.0810 0.0058  -0.0064 -0.0206 260 SER A CA  
1308 C C   . SER A 169 ? 0.2163 0.1551 0.1127 0.0048  -0.0159 -0.0243 260 SER A C   
1309 O O   . SER A 169 ? 0.2283 0.1677 0.1293 0.0033  -0.0123 -0.0269 260 SER A O   
1310 C CB  . SER A 169 ? 0.2120 0.1302 0.0805 0.0070  0.0013  -0.0208 260 SER A CB  
1311 O OG  . SER A 169 ? 0.2629 0.1660 0.1080 0.0089  -0.0071 -0.0213 260 SER A OG  
1312 N N   . SER A 170 ? 0.2004 0.1396 0.0952 0.0055  -0.0282 -0.0245 261 SER A N   
1313 C CA  . SER A 170 ? 0.1928 0.1355 0.0944 0.0036  -0.0384 -0.0276 261 SER A CA  
1314 C C   . SER A 170 ? 0.2216 0.1847 0.1520 0.0016  -0.0402 -0.0265 261 SER A C   
1315 O O   . SER A 170 ? 0.2132 0.1808 0.1528 -0.0009 -0.0471 -0.0286 261 SER A O   
1316 C CB  . SER A 170 ? 0.2288 0.1635 0.1180 0.0051  -0.0520 -0.0281 261 SER A CB  
1317 O OG  . SER A 170 ? 0.2710 0.1837 0.1296 0.0064  -0.0521 -0.0299 261 SER A OG  
1318 N N   . GLY A 171 ? 0.2091 0.1831 0.1524 0.0024  -0.0343 -0.0233 262 GLY A N   
1319 C CA  . GLY A 171 ? 0.1928 0.1842 0.1598 0.0010  -0.0353 -0.0220 262 GLY A CA  
1320 C C   . GLY A 171 ? 0.1964 0.1960 0.1725 0.0031  -0.0427 -0.0202 262 GLY A C   
1321 O O   . GLY A 171 ? 0.1922 0.2060 0.1877 0.0022  -0.0430 -0.0192 262 GLY A O   
1322 N N   . ASN A 172 ? 0.1419 0.1325 0.1045 0.0062  -0.0483 -0.0195 263 ASN A N   
1323 C CA  . ASN A 172 ? 0.1441 0.1423 0.1165 0.0094  -0.0553 -0.0175 263 ASN A CA  
1324 C C   . ASN A 172 ? 0.1494 0.1543 0.1298 0.0116  -0.0478 -0.0149 263 ASN A C   
1325 O O   . ASN A 172 ? 0.1282 0.1262 0.0989 0.0115  -0.0397 -0.0140 263 ASN A O   
1326 C CB  . ASN A 172 ? 0.1615 0.1461 0.1153 0.0127  -0.0641 -0.0171 263 ASN A CB  
1327 C CG  . ASN A 172 ? 0.2803 0.2562 0.2235 0.0106  -0.0735 -0.0201 263 ASN A CG  
1328 O OD1 . ASN A 172 ? 0.2968 0.2822 0.2555 0.0076  -0.0792 -0.0219 263 ASN A OD1 
1329 N ND2 . ASN A 172 ? 0.3455 0.3019 0.2611 0.0118  -0.0749 -0.0207 263 ASN A ND2 
1330 N N   . LEU A 173 ? 0.1220 0.1396 0.1201 0.0136  -0.0507 -0.0137 264 LEU A N   
1331 C CA  . LEU A 173 ? 0.1777 0.2012 0.1835 0.0158  -0.0437 -0.0120 264 LEU A CA  
1332 C C   . LEU A 173 ? 0.1594 0.1712 0.1508 0.0199  -0.0436 -0.0102 264 LEU A C   
1333 O O   . LEU A 173 ? 0.1403 0.1470 0.1264 0.0236  -0.0516 -0.0093 264 LEU A O   
1334 C CB  . LEU A 173 ? 0.1825 0.2215 0.2101 0.0177  -0.0460 -0.0114 264 LEU A CB  
1335 C CG  . LEU A 173 ? 0.1979 0.2410 0.2312 0.0209  -0.0389 -0.0101 264 LEU A CG  
1336 C CD1 . LEU A 173 ? 0.1529 0.1994 0.1886 0.0171  -0.0300 -0.0106 264 LEU A CD1 
1337 C CD2 . LEU A 173 ? 0.2447 0.3003 0.2968 0.0250  -0.0416 -0.0093 264 LEU A CD2 
1338 N N   . LEU A 174 ? 0.1168 0.1238 0.1022 0.0191  -0.0350 -0.0095 265 LEU A N   
1339 C CA  . LEU A 174 ? 0.1262 0.1228 0.1009 0.0224  -0.0335 -0.0075 265 LEU A CA  
1340 C C   . LEU A 174 ? 0.1345 0.1370 0.1193 0.0244  -0.0291 -0.0071 265 LEU A C   
1341 O O   . LEU A 174 ? 0.1266 0.1223 0.1066 0.0285  -0.0301 -0.0056 265 LEU A O   
1342 C CB  . LEU A 174 ? 0.1338 0.1175 0.0920 0.0195  -0.0271 -0.0067 265 LEU A CB  
1343 C CG  . LEU A 174 ? 0.1681 0.1419 0.1111 0.0179  -0.0292 -0.0074 265 LEU A CG  
1344 C CD1 . LEU A 174 ? 0.2053 0.1682 0.1352 0.0151  -0.0200 -0.0064 265 LEU A CD1 
1345 C CD2 . LEU A 174 ? 0.1792 0.1438 0.1103 0.0220  -0.0386 -0.0062 265 LEU A CD2 
1346 N N   . GLY A 175 ? 0.1037 0.1169 0.1006 0.0217  -0.0243 -0.0083 266 GLY A N   
1347 C CA  . GLY A 175 ? 0.1098 0.1262 0.1127 0.0233  -0.0196 -0.0085 266 GLY A CA  
1348 C C   . GLY A 175 ? 0.1099 0.1373 0.1238 0.0200  -0.0155 -0.0096 266 GLY A C   
1349 O O   . GLY A 175 ? 0.1414 0.1719 0.1568 0.0158  -0.0152 -0.0100 266 GLY A O   
1350 N N   . ARG A 176 ? 0.0833 0.1153 0.1036 0.0223  -0.0121 -0.0100 267 ARG A N   
1351 C CA  . ARG A 176 ? 0.0743 0.1155 0.1031 0.0196  -0.0080 -0.0106 267 ARG A CA  
1352 C C   . ARG A 176 ? 0.1166 0.1550 0.1426 0.0214  -0.0028 -0.0113 267 ARG A C   
1353 O O   . ARG A 176 ? 0.0840 0.1188 0.1088 0.0265  -0.0024 -0.0118 267 ARG A O   
1354 C CB  . ARG A 176 ? 0.0919 0.1458 0.1359 0.0206  -0.0098 -0.0103 267 ARG A CB  
1355 C CG  . ARG A 176 ? 0.0994 0.1615 0.1510 0.0172  -0.0049 -0.0101 267 ARG A CG  
1356 C CD  . ARG A 176 ? 0.1230 0.1981 0.1917 0.0181  -0.0052 -0.0093 267 ARG A CD  
1357 N NE  . ARG A 176 ? 0.1787 0.2573 0.2537 0.0163  -0.0127 -0.0092 267 ARG A NE  
1358 C CZ  . ARG A 176 ? 0.2368 0.3193 0.3199 0.0198  -0.0189 -0.0090 267 ARG A CZ  
1359 N NH1 . ARG A 176 ? 0.1813 0.2655 0.2688 0.0260  -0.0178 -0.0087 267 ARG A NH1 
1360 N NH2 . ARG A 176 ? 0.2505 0.3343 0.3368 0.0174  -0.0267 -0.0092 267 ARG A NH2 
1361 N N   . ASP A 177 ? 0.0730 0.1120 0.0972 0.0174  0.0007  -0.0116 268 ASP A N   
1362 C CA  . ASP A 177 ? 0.0779 0.1129 0.0967 0.0182  0.0051  -0.0127 268 ASP A CA  
1363 C C   . ASP A 177 ? 0.0729 0.1139 0.0947 0.0145  0.0078  -0.0121 268 ASP A C   
1364 O O   . ASP A 177 ? 0.0769 0.1241 0.1051 0.0112  0.0061  -0.0109 268 ASP A O   
1365 C CB  . ASP A 177 ? 0.0844 0.1068 0.0911 0.0165  0.0043  -0.0135 268 ASP A CB  
1366 C CG  . ASP A 177 ? 0.1533 0.1673 0.1517 0.0194  0.0072  -0.0155 268 ASP A CG  
1367 O OD1 . ASP A 177 ? 0.1473 0.1650 0.1474 0.0222  0.0113  -0.0163 268 ASP A OD1 
1368 O OD2 . ASP A 177 ? 0.1680 0.1708 0.1576 0.0185  0.0057  -0.0162 268 ASP A OD2 
1369 N N   . SER A 178 ? 0.1026 0.1400 0.1181 0.0152  0.0119  -0.0130 269 SER A N   
1370 C CA  . SER A 178 ? 0.0963 0.1377 0.1123 0.0119  0.0146  -0.0118 269 SER A CA  
1371 C C   . SER A 178 ? 0.0928 0.1247 0.0949 0.0122  0.0174  -0.0131 269 SER A C   
1372 O O   . SER A 178 ? 0.1389 0.1625 0.1329 0.0157  0.0187  -0.0154 269 SER A O   
1373 C CB  . SER A 178 ? 0.0833 0.1363 0.1120 0.0134  0.0184  -0.0104 269 SER A CB  
1374 O OG  . SER A 178 ? 0.0819 0.1355 0.1117 0.0191  0.0237  -0.0115 269 SER A OG  
1375 N N   . PHE A 179 ? 0.1031 0.1347 0.1011 0.0085  0.0180  -0.0117 270 PHE A N   
1376 C CA  . PHE A 179 ? 0.1100 0.1312 0.0922 0.0081  0.0196  -0.0127 270 PHE A CA  
1377 C C   . PHE A 179 ? 0.1197 0.1439 0.1007 0.0054  0.0221  -0.0099 270 PHE A C   
1378 O O   . PHE A 179 ? 0.1243 0.1559 0.1153 0.0022  0.0198  -0.0073 270 PHE A O   
1379 C CB  . PHE A 179 ? 0.1087 0.1199 0.0818 0.0049  0.0129  -0.0139 270 PHE A CB  
1380 C CG  . PHE A 179 ? 0.0970 0.1132 0.0788 0.0001  0.0072  -0.0118 270 PHE A CG  
1381 C CD1 . PHE A 179 ? 0.0942 0.1151 0.0863 -0.0002 0.0052  -0.0116 270 PHE A CD1 
1382 C CD2 . PHE A 179 ? 0.1041 0.1189 0.0827 -0.0036 0.0041  -0.0098 270 PHE A CD2 
1383 C CE1 . PHE A 179 ? 0.0829 0.1076 0.0826 -0.0038 0.0016  -0.0099 270 PHE A CE1 
1384 C CE2 . PHE A 179 ? 0.1254 0.1449 0.1137 -0.0071 -0.0005 -0.0079 270 PHE A CE2 
1385 C CZ  . PHE A 179 ? 0.1283 0.1528 0.1272 -0.0071 -0.0010 -0.0082 270 PHE A CZ  
1386 N N   . GLU A 180 ? 0.1219 0.1384 0.0887 0.0067  0.0270  -0.0103 271 GLU A N   
1387 C CA  . GLU A 180 ? 0.1282 0.1438 0.0890 0.0039  0.0294  -0.0072 271 GLU A CA  
1388 C C   . GLU A 180 ? 0.1312 0.1390 0.0829 -0.0006 0.0205  -0.0062 271 GLU A C   
1389 O O   . GLU A 180 ? 0.1341 0.1346 0.0798 -0.0013 0.0142  -0.0087 271 GLU A O   
1390 C CB  . GLU A 180 ? 0.1476 0.1556 0.0934 0.0074  0.0386  -0.0080 271 GLU A CB  
1391 C CG  . GLU A 180 ? 0.1725 0.1781 0.1099 0.0048  0.0429  -0.0041 271 GLU A CG  
1392 C CD  . GLU A 180 ? 0.2729 0.2720 0.1966 0.0086  0.0548  -0.0045 271 GLU A CD  
1393 O OE1 . GLU A 180 ? 0.2593 0.2598 0.1861 0.0140  0.0611  -0.0077 271 GLU A OE1 
1394 O OE2 . GLU A 180 ? 0.2872 0.2789 0.1963 0.0066  0.0582  -0.0016 271 GLU A OE2 
1395 N N   . VAL A 181 ? 0.1310 0.1405 0.0832 -0.0038 0.0196  -0.0024 272 VAL A N   
1396 C CA  . VAL A 181 ? 0.1337 0.1373 0.0803 -0.0076 0.0106  -0.0008 272 VAL A CA  
1397 C C   . VAL A 181 ? 0.1623 0.1575 0.0931 -0.0089 0.0120  0.0025  272 VAL A C   
1398 O O   . VAL A 181 ? 0.1731 0.1726 0.1070 -0.0090 0.0191  0.0056  272 VAL A O   
1399 C CB  . VAL A 181 ? 0.2061 0.2196 0.1715 -0.0101 0.0057  0.0011  272 VAL A CB  
1400 C CG1 . VAL A 181 ? 0.1769 0.1850 0.1388 -0.0132 -0.0034 0.0031  272 VAL A CG1 
1401 C CG2 . VAL A 181 ? 0.2103 0.2299 0.1880 -0.0089 0.0046  -0.0018 272 VAL A CG2 
1402 N N   . ARG A 182 ? 0.1684 0.1508 0.0820 -0.0103 0.0049  0.0021  273 ARG A N   
1403 C CA  . ARG A 182 ? 0.2019 0.1748 0.0997 -0.0121 0.0028  0.0061  273 ARG A CA  
1404 C C   . ARG A 182 ? 0.2239 0.1952 0.1256 -0.0152 -0.0103 0.0078  273 ARG A C   
1405 O O   . ARG A 182 ? 0.2327 0.1991 0.1315 -0.0161 -0.0186 0.0050  273 ARG A O   
1406 C CB  . ARG A 182 ? 0.2285 0.1847 0.0977 -0.0104 0.0060  0.0043  273 ARG A CB  
1407 C CG  . ARG A 182 ? 0.2844 0.2274 0.1323 -0.0123 0.0028  0.0085  273 ARG A CG  
1408 C CD  . ARG A 182 ? 0.2832 0.2084 0.1001 -0.0100 0.0081  0.0064  273 ARG A CD  
1409 N NE  . ARG A 182 ? 0.3558 0.2642 0.1473 -0.0121 0.0011  0.0098  273 ARG A NE  
1410 C CZ  . ARG A 182 ? 0.5279 0.4328 0.3112 -0.0131 0.0059  0.0157  273 ARG A CZ  
1411 N NH1 . ARG A 182 ? 0.5616 0.4796 0.3618 -0.0127 0.0180  0.0188  273 ARG A NH1 
1412 N NH2 . ARG A 182 ? 0.6058 0.4941 0.3650 -0.0145 -0.0020 0.0188  273 ARG A NH2 
1413 N N   . VAL A 183 ? 0.2017 0.1771 0.1117 -0.0169 -0.0122 0.0126  274 VAL A N   
1414 C CA  . VAL A 183 ? 0.1875 0.1616 0.1025 -0.0190 -0.0242 0.0149  274 VAL A CA  
1415 C C   . VAL A 183 ? 0.2078 0.1666 0.0989 -0.0199 -0.0288 0.0186  274 VAL A C   
1416 O O   . VAL A 183 ? 0.2423 0.1976 0.1252 -0.0199 -0.0225 0.0226  274 VAL A O   
1417 C CB  . VAL A 183 ? 0.1913 0.1773 0.1291 -0.0196 -0.0240 0.0178  274 VAL A CB  
1418 C CG1 . VAL A 183 ? 0.1525 0.1398 0.1010 -0.0207 -0.0358 0.0191  274 VAL A CG1 
1419 C CG2 . VAL A 183 ? 0.1355 0.1342 0.0910 -0.0185 -0.0168 0.0145  274 VAL A CG2 
1420 N N   . CYS A 184 ? 0.2152 0.1639 0.0944 -0.0209 -0.0400 0.0173  275 CYS A N   
1421 C CA  . CYS A 184 ? 0.2453 0.1759 0.0955 -0.0214 -0.0451 0.0197  275 CYS A CA  
1422 C C   . CYS A 184 ? 0.3428 0.2678 0.1924 -0.0234 -0.0625 0.0201  275 CYS A C   
1423 O O   . CYS A 184 ? 0.3293 0.2643 0.2003 -0.0245 -0.0689 0.0177  275 CYS A O   
1424 C CB  . CYS A 184 ? 0.2853 0.2032 0.1094 -0.0198 -0.0375 0.0158  275 CYS A CB  
1425 S SG  . CYS A 184 ? 0.3246 0.2427 0.1523 -0.0196 -0.0411 0.0078  275 CYS A SG  
1426 N N   . ALA A 185 ? 0.2818 0.1901 0.1064 -0.0240 -0.0702 0.0234  276 ALA A N   
1427 C CA  . ALA A 185 ? 0.3211 0.2266 0.1517 -0.0252 -0.0855 0.0236  276 ALA A CA  
1428 C C   . ALA A 185 ? 0.3559 0.2568 0.1837 -0.0263 -0.0904 0.0172  276 ALA A C   
1429 O O   . ALA A 185 ? 0.3273 0.2342 0.1740 -0.0280 -0.1009 0.0164  276 ALA A O   
1430 C CB  . ALA A 185 ? 0.3807 0.2724 0.1924 -0.0246 -0.0891 0.0280  276 ALA A CB  
1431 N N   . CYS A 186 ? 0.3170 0.2075 0.1233 -0.0252 -0.0824 0.0129  277 CYS A N   
1432 C CA  A CYS A 186 ? 0.3760 0.2592 0.1771 -0.0262 -0.0869 0.0070  277 CYS A CA  
1433 C CA  B CYS A 186 ? 0.3787 0.2618 0.1796 -0.0262 -0.0868 0.0070  277 CYS A CA  
1434 C C   . CYS A 186 ? 0.3744 0.2594 0.1729 -0.0247 -0.0757 0.0019  277 CYS A C   
1435 O O   . CYS A 186 ? 0.3312 0.2045 0.1076 -0.0223 -0.0668 -0.0009 277 CYS A O   
1436 C CB  A CYS A 186 ? 0.4553 0.3187 0.2289 -0.0258 -0.0906 0.0064  277 CYS A CB  
1437 C CB  B CYS A 186 ? 0.4482 0.3114 0.2211 -0.0257 -0.0901 0.0065  277 CYS A CB  
1438 S SG  A CYS A 186 ? 0.4585 0.3118 0.2280 -0.0280 -0.0999 0.0003  277 CYS A SG  
1439 S SG  B CYS A 186 ? 0.4837 0.3421 0.2568 -0.0271 -0.1043 0.0123  277 CYS A SG  
1440 N N   . PRO A 187 ? 0.3150 0.2145 0.1369 -0.0259 -0.0757 0.0005  278 PRO A N   
1441 C CA  . PRO A 187 ? 0.3521 0.2531 0.1723 -0.0242 -0.0654 -0.0044 278 PRO A CA  
1442 C C   . PRO A 187 ? 0.3552 0.2422 0.1595 -0.0233 -0.0648 -0.0100 278 PRO A C   
1443 O O   . PRO A 187 ? 0.3032 0.1853 0.0953 -0.0198 -0.0532 -0.0133 278 PRO A O   
1444 C CB  . PRO A 187 ? 0.2809 0.2000 0.1340 -0.0260 -0.0677 -0.0045 278 PRO A CB  
1445 C CG  . PRO A 187 ? 0.3191 0.2482 0.1894 -0.0275 -0.0745 0.0011  278 PRO A CG  
1446 C CD  . PRO A 187 ? 0.3109 0.2262 0.1623 -0.0282 -0.0835 0.0035  278 PRO A CD  
1447 N N   . GLY A 188 ? 0.3356 0.2163 0.1411 -0.0262 -0.0767 -0.0111 279 GLY A N   
1448 C CA  . GLY A 188 ? 0.3295 0.1958 0.1199 -0.0259 -0.0770 -0.0163 279 GLY A CA  
1449 C C   . GLY A 188 ? 0.4849 0.3348 0.2453 -0.0223 -0.0693 -0.0175 279 GLY A C   
1450 O O   . GLY A 188 ? 0.3661 0.2085 0.1147 -0.0191 -0.0602 -0.0218 279 GLY A O   
1451 N N   . ARG A 189 ? 0.3727 0.2165 0.1209 -0.0224 -0.0725 -0.0136 280 ARG A N   
1452 C CA  . ARG A 189 ? 0.4009 0.2291 0.1207 -0.0191 -0.0642 -0.0142 280 ARG A CA  
1453 C C   . ARG A 189 ? 0.4121 0.2467 0.1304 -0.0147 -0.0464 -0.0141 280 ARG A C   
1454 O O   . ARG A 189 ? 0.4138 0.2392 0.1167 -0.0109 -0.0358 -0.0174 280 ARG A O   
1455 C CB  . ARG A 189 ? 0.5305 0.3510 0.2383 -0.0203 -0.0712 -0.0093 280 ARG A CB  
1456 N N   . ASP A 190 ? 0.3652 0.2160 0.1013 -0.0150 -0.0429 -0.0103 281 ASP A N   
1457 C CA  . ASP A 190 ? 0.3696 0.2277 0.1068 -0.0112 -0.0262 -0.0094 281 ASP A CA  
1458 C C   . ASP A 190 ? 0.3472 0.2085 0.0904 -0.0082 -0.0179 -0.0149 281 ASP A C   
1459 O O   . ASP A 190 ? 0.3819 0.2416 0.1183 -0.0037 -0.0038 -0.0163 281 ASP A O   
1460 C CB  . ASP A 190 ? 0.3438 0.2172 0.0985 -0.0129 -0.0255 -0.0038 281 ASP A CB  
1461 C CG  . ASP A 190 ? 0.4336 0.3022 0.1792 -0.0143 -0.0288 0.0024  281 ASP A CG  
1462 O OD1 . ASP A 190 ? 0.4564 0.3096 0.1812 -0.0139 -0.0312 0.0020  281 ASP A OD1 
1463 O OD2 . ASP A 190 ? 0.4198 0.2983 0.1777 -0.0159 -0.0292 0.0077  281 ASP A OD2 
1464 N N   . ARG A 191 ? 0.3429 0.2090 0.1004 -0.0104 -0.0263 -0.0179 282 ARG A N   
1465 C CA  . ARG A 191 ? 0.3274 0.1938 0.0889 -0.0072 -0.0196 -0.0231 282 ARG A CA  
1466 C C   . ARG A 191 ? 0.3801 0.2292 0.1210 -0.0044 -0.0164 -0.0273 282 ARG A C   
1467 O O   . ARG A 191 ? 0.3804 0.2283 0.1182 0.0008  -0.0041 -0.0301 282 ARG A O   
1468 C CB  . ARG A 191 ? 0.3098 0.1823 0.0892 -0.0109 -0.0299 -0.0251 282 ARG A CB  
1469 C CG  . ARG A 191 ? 0.3102 0.1789 0.0906 -0.0078 -0.0244 -0.0305 282 ARG A CG  
1470 C CD  . ARG A 191 ? 0.3110 0.1864 0.1104 -0.0114 -0.0323 -0.0319 282 ARG A CD  
1471 N NE  . ARG A 191 ? 0.2989 0.1662 0.0953 -0.0086 -0.0284 -0.0368 282 ARG A NE  
1472 C CZ  . ARG A 191 ? 0.3476 0.2132 0.1537 -0.0120 -0.0355 -0.0388 282 ARG A CZ  
1473 N NH1 . ARG A 191 ? 0.2819 0.1553 0.1042 -0.0184 -0.0463 -0.0364 282 ARG A NH1 
1474 N NH2 . ARG A 191 ? 0.3038 0.1602 0.1049 -0.0088 -0.0313 -0.0428 282 ARG A NH2 
1475 N N   . ARG A 192 ? 0.3772 0.2127 0.1047 -0.0076 -0.0278 -0.0278 283 ARG A N   
1476 C CA  . ARG A 192 ? 0.4699 0.2866 0.1749 -0.0053 -0.0258 -0.0318 283 ARG A CA  
1477 C C   . ARG A 192 ? 0.5408 0.3527 0.2300 -0.0003 -0.0111 -0.0308 283 ARG A C   
1478 O O   . ARG A 192 ? 0.5222 0.3272 0.2028 0.0045  -0.0009 -0.0344 283 ARG A O   
1479 C CB  . ARG A 192 ? 0.5226 0.3256 0.2154 -0.0099 -0.0412 -0.0316 283 ARG A CB  
1480 C CG  . ARG A 192 ? 0.6233 0.4198 0.3199 -0.0128 -0.0513 -0.0357 283 ARG A CG  
1481 C CD  . ARG A 192 ? 0.6806 0.4629 0.3647 -0.0172 -0.0663 -0.0354 283 ARG A CD  
1482 N NE  . ARG A 192 ? 0.7089 0.5025 0.4098 -0.0218 -0.0781 -0.0306 283 ARG A NE  
1483 C CZ  . ARG A 192 ? 0.7122 0.5016 0.4038 -0.0229 -0.0838 -0.0267 283 ARG A CZ  
1484 N NH1 . ARG A 192 ? 0.7911 0.5642 0.4547 -0.0201 -0.0789 -0.0269 283 ARG A NH1 
1485 N NH2 . ARG A 192 ? 0.6506 0.4515 0.3611 -0.0266 -0.0944 -0.0223 283 ARG A NH2 
1486 N N   . THR A 193 ? 0.5682 0.3841 0.2549 -0.0013 -0.0095 -0.0255 284 THR A N   
1487 C CA  . THR A 193 ? 0.5773 0.3899 0.2512 0.0027  0.0051  -0.0236 284 THR A CA  
1488 C C   . THR A 193 ? 0.5585 0.3847 0.2475 0.0076  0.0211  -0.0245 284 THR A C   
1489 O O   . THR A 193 ? 0.5377 0.3580 0.2177 0.0123  0.0331  -0.0267 284 THR A O   
1490 C CB  . THR A 193 ? 0.5682 0.3843 0.2403 0.0001  0.0034  -0.0169 284 THR A CB  
1491 O OG1 . THR A 193 ? 0.5515 0.3527 0.2069 -0.0034 -0.0107 -0.0161 284 THR A OG1 
1492 C CG2 . THR A 193 ? 0.5849 0.4008 0.2486 0.0036  0.0201  -0.0143 284 THR A CG2 
1493 N N   . GLU A 194 ? 0.5061 0.3509 0.2192 0.0066  0.0216  -0.0226 285 GLU A N   
1494 C CA  . GLU A 194 ? 0.4609 0.3198 0.1907 0.0113  0.0363  -0.0229 285 GLU A CA  
1495 C C   . GLU A 194 ? 0.4447 0.2991 0.1755 0.0156  0.0393  -0.0290 285 GLU A C   
1496 O O   . GLU A 194 ? 0.4820 0.3404 0.2174 0.0211  0.0526  -0.0301 285 GLU A O   
1497 C CB  . GLU A 194 ? 0.3872 0.2651 0.1409 0.0092  0.0352  -0.0196 285 GLU A CB  
1498 C CG  . GLU A 194 ? 0.4082 0.2905 0.1616 0.0055  0.0341  -0.0130 285 GLU A CG  
1499 C CD  . GLU A 194 ? 0.4369 0.3382 0.2138 0.0045  0.0385  -0.0093 285 GLU A CD  
1500 O OE1 . GLU A 194 ? 0.4574 0.3696 0.2511 0.0075  0.0446  -0.0117 285 GLU A OE1 
1501 O OE2 . GLU A 194 ? 0.4866 0.3910 0.2648 0.0008  0.0356  -0.0037 285 GLU A OE2 
1502 N N   . GLU A 195 ? 0.4230 0.2690 0.1507 0.0132  0.0270  -0.0326 286 GLU A N   
1503 C CA  . GLU A 195 ? 0.3873 0.2259 0.1134 0.0171  0.0294  -0.0381 286 GLU A CA  
1504 C C   . GLU A 195 ? 0.5257 0.3464 0.2280 0.0203  0.0349  -0.0407 286 GLU A C   
1505 O O   . GLU A 195 ? 0.5314 0.3491 0.2333 0.0260  0.0443  -0.0440 286 GLU A O   
1506 C CB  . GLU A 195 ? 0.3815 0.2152 0.1111 0.0129  0.0151  -0.0409 286 GLU A CB  
1507 C CG  . GLU A 195 ? 0.3726 0.2230 0.1263 0.0110  0.0120  -0.0396 286 GLU A CG  
1508 C CD  . GLU A 195 ? 0.4320 0.2779 0.1917 0.0076  0.0008  -0.0427 286 GLU A CD  
1509 O OE1 . GLU A 195 ? 0.4452 0.2754 0.1915 0.0064  -0.0052 -0.0458 286 GLU A OE1 
1510 O OE2 . GLU A 195 ? 0.3605 0.2184 0.1385 0.0059  -0.0018 -0.0418 286 GLU A OE2 
1511 N N   . GLU A 196 ? 0.5925 0.4003 0.2745 0.0171  0.0292  -0.0391 287 GLU A N   
1512 C CA  . GLU A 196 ? 0.7231 0.5128 0.3802 0.0205  0.0357  -0.0413 287 GLU A CA  
1513 C C   . GLU A 196 ? 0.6806 0.4785 0.3414 0.0258  0.0540  -0.0392 287 GLU A C   
1514 O O   . GLU A 196 ? 0.7949 0.5855 0.4480 0.0313  0.0643  -0.0424 287 GLU A O   
1515 C CB  . GLU A 196 ? 0.8507 0.6246 0.4850 0.0159  0.0253  -0.0396 287 GLU A CB  
1516 C CG  . GLU A 196 ? 0.9956 0.7477 0.6004 0.0191  0.0310  -0.0421 287 GLU A CG  
1517 C CD  . GLU A 196 ? 1.1013 0.8408 0.6986 0.0224  0.0317  -0.0485 287 GLU A CD  
1518 O OE1 . GLU A 196 ? 1.1217 0.8611 0.7276 0.0194  0.0202  -0.0510 287 GLU A OE1 
1519 O OE2 . GLU A 196 ? 1.1621 0.8917 0.7455 0.0279  0.0440  -0.0509 287 GLU A OE2 
1520 N N   . ASN A 197 ? 0.6412 0.4547 0.3151 0.0242  0.0582  -0.0337 288 ASN A N   
1521 C CA  . ASN A 197 ? 0.6602 0.4848 0.3433 0.0285  0.0754  -0.0312 288 ASN A CA  
1522 C C   . ASN A 197 ? 0.6303 0.4662 0.3334 0.0342  0.0844  -0.0343 288 ASN A C   
1523 O O   . ASN A 197 ? 0.6489 0.4845 0.3514 0.0396  0.0978  -0.0352 288 ASN A O   
1524 C CB  . ASN A 197 ? 0.6468 0.4881 0.3453 0.0250  0.0769  -0.0246 288 ASN A CB  
1525 C CG  . ASN A 197 ? 0.7211 0.5509 0.3991 0.0208  0.0722  -0.0206 288 ASN A CG  
1526 O OD1 . ASN A 197 ? 0.7553 0.5652 0.4070 0.0213  0.0706  -0.0224 288 ASN A OD1 
1527 N ND2 . ASN A 197 ? 0.7440 0.5855 0.4334 0.0168  0.0696  -0.0149 288 ASN A ND2 
1528 N N   . LEU A 198 ? 0.5477 0.3932 0.2688 0.0334  0.0771  -0.0358 289 LEU A N   
1529 C CA  . LEU A 198 ? 0.5350 0.3904 0.2752 0.0391  0.0840  -0.0385 289 LEU A CA  
1530 C C   . LEU A 198 ? 0.6165 0.4548 0.3406 0.0441  0.0877  -0.0438 289 LEU A C   
1531 O O   . LEU A 198 ? 0.6719 0.5159 0.4062 0.0505  0.0991  -0.0452 289 LEU A O   
1532 C CB  . LEU A 198 ? 0.5485 0.4126 0.3056 0.0369  0.0739  -0.0394 289 LEU A CB  
1533 C CG  . LEU A 198 ? 0.5455 0.4232 0.3265 0.0425  0.0802  -0.0408 289 LEU A CG  
1534 C CD1 . LEU A 198 ? 0.5072 0.4056 0.3101 0.0448  0.0918  -0.0365 289 LEU A CD1 
1535 C CD2 . LEU A 198 ? 0.5072 0.3892 0.2999 0.0400  0.0694  -0.0418 289 LEU A CD2 
1536 N N   . ARG A 199 ? 0.7030 0.5203 0.4024 0.0413  0.0779  -0.0468 290 ARG A N   
1537 C CA  . ARG A 199 ? 0.8585 0.6570 0.5406 0.0454  0.0798  -0.0522 290 ARG A CA  
1538 C C   . ARG A 199 ? 0.8831 0.6751 0.5520 0.0505  0.0946  -0.0522 290 ARG A C   
1539 O O   . ARG A 199 ? 0.9547 0.7314 0.6091 0.0551  0.0991  -0.0566 290 ARG A O   
1540 C CB  . ARG A 199 ? 0.9257 0.7034 0.5850 0.0402  0.0648  -0.0549 290 ARG A CB  
1541 N N   . LYS A 200 ? 0.8440 0.6467 0.5178 0.0497  0.1026  -0.0472 291 LYS A N   
1542 C CA  . LYS A 200 ? 0.8503 0.6483 0.5136 0.0541  0.1178  -0.0465 291 LYS A CA  
1543 C C   . LYS A 200 ? 0.8402 0.6614 0.5333 0.0588  0.1320  -0.0441 291 LYS A C   
1544 O O   . LYS A 200 ? 0.8096 0.6517 0.5283 0.0565  0.1304  -0.0404 291 LYS A O   
1545 C CB  . LYS A 200 ? 0.8052 0.5948 0.4486 0.0495  0.1169  -0.0424 291 LYS A CB  
1546 N N   . GLY B 1   ? 0.6878 0.5073 0.7437 -0.0994 -0.1090 0.1092  92  GLY B N   
1547 C CA  . GLY B 1   ? 0.6368 0.4639 0.7043 -0.1000 -0.1005 0.0937  92  GLY B CA  
1548 C C   . GLY B 1   ? 0.5456 0.3928 0.6031 -0.1019 -0.0978 0.0878  92  GLY B C   
1549 O O   . GLY B 1   ? 0.3550 0.2097 0.4047 -0.0968 -0.1030 0.0910  92  GLY B O   
1550 N N   . SER B 2   ? 0.6536 0.5103 0.7130 -0.1097 -0.0895 0.0793  93  SER B N   
1551 C CA  . SER B 2   ? 0.5871 0.4649 0.6408 -0.1125 -0.0857 0.0755  93  SER B CA  
1552 C C   . SER B 2   ? 0.5194 0.4118 0.5871 -0.1112 -0.0838 0.0610  93  SER B C   
1553 O O   . SER B 2   ? 0.5422 0.4326 0.6187 -0.1167 -0.0802 0.0532  93  SER B O   
1554 C CB  . SER B 2   ? 0.5638 0.4462 0.6085 -0.1240 -0.0771 0.0801  93  SER B CB  
1555 O OG  . SER B 2   ? 0.6074 0.5003 0.6658 -0.1309 -0.0714 0.0712  93  SER B OG  
1556 N N   . SER B 3   ? 0.3736 0.2808 0.4407 -0.1051 -0.0860 0.0574  94  SER B N   
1557 C CA  . SER B 3   ? 0.2675 0.1912 0.3429 -0.1032 -0.0852 0.0448  94  SER B CA  
1558 C C   . SER B 3   ? 0.3081 0.2531 0.3876 -0.1117 -0.0804 0.0427  94  SER B C   
1559 O O   . SER B 3   ? 0.3304 0.2814 0.4077 -0.1169 -0.0761 0.0509  94  SER B O   
1560 C CB  . SER B 3   ? 0.2355 0.1679 0.3077 -0.0936 -0.0888 0.0437  94  SER B CB  
1561 O OG  . SER B 3   ? 0.2921 0.2423 0.3682 -0.0916 -0.0877 0.0331  94  SER B OG  
1562 N N   . SER B 4   ? 0.2540 0.2112 0.3398 -0.1135 -0.0802 0.0317  95  SER B N   
1563 C CA  . SER B 4   ? 0.2392 0.2210 0.3324 -0.1198 -0.0780 0.0307  95  SER B CA  
1564 C C   . SER B 4   ? 0.3061 0.3104 0.4016 -0.1129 -0.0789 0.0335  95  SER B C   
1565 O O   . SER B 4   ? 0.3267 0.3538 0.4327 -0.1157 -0.0777 0.0344  95  SER B O   
1566 C CB  . SER B 4   ? 0.2866 0.2728 0.3829 -0.1263 -0.0786 0.0188  95  SER B CB  
1567 O OG  . SER B 4   ? 0.3536 0.3382 0.4436 -0.1204 -0.0810 0.0096  95  SER B OG  
1568 N N   . SER B 5   ? 0.2256 0.2243 0.3137 -0.1036 -0.0808 0.0353  96  SER B N   
1569 C CA  . SER B 5   ? 0.2051 0.2230 0.2954 -0.0966 -0.0804 0.0374  96  SER B CA  
1570 C C   . SER B 5   ? 0.2107 0.2177 0.2918 -0.0909 -0.0804 0.0429  96  SER B C   
1571 O O   . SER B 5   ? 0.2475 0.2327 0.3202 -0.0919 -0.0823 0.0459  96  SER B O   
1572 C CB  . SER B 5   ? 0.2392 0.2662 0.3271 -0.0913 -0.0836 0.0281  96  SER B CB  
1573 O OG  . SER B 5   ? 0.2380 0.2468 0.3164 -0.0864 -0.0856 0.0212  96  SER B OG  
1574 N N   . VAL B 6   ? 0.1687 0.1904 0.2503 -0.0838 -0.0773 0.0446  97  VAL B N   
1575 C CA  . VAL B 6   ? 0.1661 0.1782 0.2332 -0.0753 -0.0740 0.0469  97  VAL B CA  
1576 C C   . VAL B 6   ? 0.1502 0.1730 0.2178 -0.0657 -0.0761 0.0414  97  VAL B C   
1577 O O   . VAL B 6   ? 0.1406 0.1835 0.2192 -0.0643 -0.0744 0.0418  97  VAL B O   
1578 C CB  . VAL B 6   ? 0.1707 0.1856 0.2336 -0.0772 -0.0621 0.0541  97  VAL B CB  
1579 C CG1 . VAL B 6   ? 0.1721 0.1758 0.2157 -0.0712 -0.0590 0.0553  97  VAL B CG1 
1580 C CG2 . VAL B 6   ? 0.2209 0.2249 0.2814 -0.0888 -0.0586 0.0598  97  VAL B CG2 
1581 N N   . PRO B 7   ? 0.1528 0.1635 0.2108 -0.0592 -0.0801 0.0374  98  PRO B N   
1582 C CA  . PRO B 7   ? 0.1351 0.1549 0.1918 -0.0508 -0.0804 0.0323  98  PRO B CA  
1583 C C   . PRO B 7   ? 0.2029 0.2329 0.2576 -0.0457 -0.0718 0.0370  98  PRO B C   
1584 O O   . PRO B 7   ? 0.1744 0.1968 0.2206 -0.0469 -0.0651 0.0419  98  PRO B O   
1585 C CB  . PRO B 7   ? 0.1700 0.1730 0.2193 -0.0458 -0.0844 0.0280  98  PRO B CB  
1586 C CG  . PRO B 7   ? 0.2119 0.1990 0.2569 -0.0500 -0.0863 0.0347  98  PRO B CG  
1587 C CD  . PRO B 7   ? 0.1907 0.1797 0.2415 -0.0593 -0.0848 0.0384  98  PRO B CD  
1588 N N   . SER B 8   ? 0.1501 0.1955 0.2112 -0.0408 -0.0712 0.0357  99  SER B N   
1589 C CA  . SER B 8   ? 0.1771 0.2300 0.2392 -0.0344 -0.0615 0.0397  99  SER B CA  
1590 C C   . SER B 8   ? 0.1598 0.1972 0.2042 -0.0300 -0.0579 0.0372  99  SER B C   
1591 O O   . SER B 8   ? 0.1607 0.1885 0.1972 -0.0282 -0.0648 0.0320  99  SER B O   
1592 C CB  . SER B 8   ? 0.1926 0.2625 0.2647 -0.0294 -0.0638 0.0402  99  SER B CB  
1593 O OG  . SER B 8   ? 0.2997 0.3738 0.3750 -0.0221 -0.0529 0.0443  99  SER B OG  
1594 N N   . GLN B 9   ? 0.1516 0.1863 0.1905 -0.0294 -0.0460 0.0406  100 GLN B N   
1595 C CA  . GLN B 9   ? 0.1610 0.1827 0.1815 -0.0271 -0.0421 0.0382  100 GLN B CA  
1596 C C   . GLN B 9   ? 0.1744 0.2025 0.1977 -0.0199 -0.0312 0.0374  100 GLN B C   
1597 O O   . GLN B 9   ? 0.1796 0.1968 0.1873 -0.0199 -0.0236 0.0353  100 GLN B O   
1598 C CB  . GLN B 9   ? 0.2406 0.2474 0.2441 -0.0358 -0.0369 0.0415  100 GLN B CB  
1599 C CG  . GLN B 9   ? 0.3171 0.3265 0.3229 -0.0394 -0.0198 0.0446  100 GLN B CG  
1600 C CD  . GLN B 9   ? 0.4138 0.4059 0.3972 -0.0514 -0.0148 0.0475  100 GLN B CD  
1601 O OE1 . GLN B 9   ? 0.4492 0.4376 0.4328 -0.0584 -0.0203 0.0515  100 GLN B OE1 
1602 N NE2 . GLN B 9   ? 0.3014 0.2809 0.2627 -0.0554 -0.0043 0.0454  100 GLN B NE2 
1603 N N   . LYS B 10  ? 0.1579 0.2026 0.2005 -0.0147 -0.0310 0.0398  101 LYS B N   
1604 C CA  . LYS B 10  ? 0.1187 0.1693 0.1688 -0.0072 -0.0202 0.0416  101 LYS B CA  
1605 C C   . LYS B 10  ? 0.1180 0.1617 0.1547 -0.0021 -0.0236 0.0361  101 LYS B C   
1606 O O   . LYS B 10  ? 0.1449 0.1920 0.1810 -0.0011 -0.0354 0.0333  101 LYS B O   
1607 C CB  . LYS B 10  ? 0.1103 0.1823 0.1875 -0.0037 -0.0227 0.0489  101 LYS B CB  
1608 C CG  . LYS B 10  ? 0.1927 0.2719 0.2846 0.0054  -0.0122 0.0539  101 LYS B CG  
1609 C CD  . LYS B 10  ? 0.2912 0.3940 0.4113 0.0080  -0.0207 0.0639  101 LYS B CD  
1610 C CE  . LYS B 10  ? 0.4029 0.5128 0.5420 0.0181  -0.0116 0.0719  101 LYS B CE  
1611 N NZ  . LYS B 10  ? 0.5146 0.6153 0.6615 0.0211  0.0116  0.0712  101 LYS B NZ  
1612 N N   . THR B 11  ? 0.1574 0.1904 0.1829 -0.0001 -0.0115 0.0338  102 THR B N   
1613 C CA  . THR B 11  ? 0.1028 0.1300 0.1178 0.0043  -0.0125 0.0288  102 THR B CA  
1614 C C   . THR B 11  ? 0.1352 0.1752 0.1646 0.0117  -0.0152 0.0325  102 THR B C   
1615 O O   . THR B 11  ? 0.0989 0.1490 0.1468 0.0161  -0.0084 0.0400  102 THR B O   
1616 C CB  . THR B 11  ? 0.1890 0.2026 0.1906 0.0036  0.0033  0.0259  102 THR B CB  
1617 O OG1 . THR B 11  ? 0.1966 0.1975 0.1796 -0.0062 0.0039  0.0236  102 THR B OG1 
1618 C CG2 . THR B 11  ? 0.1650 0.1728 0.1568 0.0073  0.0027  0.0206  102 THR B CG2 
1619 N N   . TYR B 12  ? 0.1220 0.1612 0.1438 0.0126  -0.0248 0.0278  103 TYR B N   
1620 C CA  . TYR B 12  ? 0.0859 0.1354 0.1147 0.0165  -0.0299 0.0314  103 TYR B CA  
1621 C C   . TYR B 12  ? 0.1033 0.1436 0.1170 0.0178  -0.0305 0.0238  103 TYR B C   
1622 O O   . TYR B 12  ? 0.1090 0.1446 0.1147 0.0140  -0.0378 0.0160  103 TYR B O   
1623 C CB  . TYR B 12  ? 0.1136 0.1746 0.1496 0.0114  -0.0433 0.0333  103 TYR B CB  
1624 C CG  . TYR B 12  ? 0.1460 0.2123 0.1797 0.0110  -0.0493 0.0340  103 TYR B CG  
1625 C CD1 . TYR B 12  ? 0.2353 0.3091 0.2787 0.0158  -0.0464 0.0436  103 TYR B CD1 
1626 C CD2 . TYR B 12  ? 0.1570 0.2182 0.1781 0.0052  -0.0556 0.0246  103 TYR B CD2 
1627 C CE1 . TYR B 12  ? 0.2727 0.3483 0.3096 0.0133  -0.0526 0.0446  103 TYR B CE1 
1628 C CE2 . TYR B 12  ? 0.2163 0.2800 0.2307 0.0026  -0.0597 0.0248  103 TYR B CE2 
1629 C CZ  . TYR B 12  ? 0.2634 0.3340 0.2839 0.0061  -0.0594 0.0353  103 TYR B CZ  
1630 O OH  . TYR B 12  ? 0.3226 0.3949 0.3339 0.0019  -0.0651 0.0371  103 TYR B OH  
1631 N N   . GLN B 13  ? 0.0961 0.1326 0.1081 0.0231  -0.0213 0.0258  104 GLN B N   
1632 C CA  . GLN B 13  ? 0.1012 0.1290 0.0993 0.0235  -0.0207 0.0185  104 GLN B CA  
1633 C C   . GLN B 13  ? 0.1212 0.1549 0.1159 0.0215  -0.0301 0.0184  104 GLN B C   
1634 O O   . GLN B 13  ? 0.1249 0.1520 0.1087 0.0187  -0.0317 0.0091  104 GLN B O   
1635 C CB  . GLN B 13  ? 0.0993 0.1191 0.0951 0.0285  -0.0071 0.0203  104 GLN B CB  
1636 C CG  . GLN B 13  ? 0.1653 0.1736 0.1549 0.0265  0.0040  0.0158  104 GLN B CG  
1637 C CD  . GLN B 13  ? 0.2621 0.2571 0.2402 0.0272  0.0153  0.0106  104 GLN B CD  
1638 O OE1 . GLN B 13  ? 0.2707 0.2650 0.2485 0.0311  0.0171  0.0121  104 GLN B OE1 
1639 N NE2 . GLN B 13  ? 0.2560 0.2397 0.2225 0.0218  0.0228  0.0047  104 GLN B NE2 
1640 N N   . GLY B 14  ? 0.1158 0.1618 0.1197 0.0218  -0.0360 0.0285  105 GLY B N   
1641 C CA  . GLY B 14  ? 0.1671 0.2177 0.1622 0.0163  -0.0460 0.0288  105 GLY B CA  
1642 C C   . GLY B 14  ? 0.1571 0.2007 0.1395 0.0181  -0.0417 0.0293  105 GLY B C   
1643 O O   . GLY B 14  ? 0.1290 0.1649 0.1122 0.0244  -0.0308 0.0301  105 GLY B O   
1644 N N   . SER B 15  ? 0.1336 0.1780 0.1015 0.0106  -0.0493 0.0279  106 SER B N   
1645 C CA  A SER B 15  ? 0.1594 0.1971 0.1124 0.0101  -0.0463 0.0305  106 SER B CA  
1646 C CA  B SER B 15  ? 0.1596 0.1974 0.1134 0.0106  -0.0460 0.0309  106 SER B CA  
1647 C C   . SER B 15  ? 0.1858 0.2085 0.1295 0.0122  -0.0340 0.0176  106 SER B C   
1648 O O   . SER B 15  ? 0.1741 0.1896 0.1094 0.0142  -0.0275 0.0205  106 SER B O   
1649 C CB  A SER B 15  ? 0.1787 0.2170 0.1128 -0.0016 -0.0555 0.0290  106 SER B CB  
1650 C CB  B SER B 15  ? 0.1802 0.2193 0.1159 -0.0006 -0.0556 0.0312  106 SER B CB  
1651 O OG  A SER B 15  ? 0.1891 0.2370 0.1351 -0.0041 -0.0634 0.0352  106 SER B OG  
1652 O OG  B SER B 15  ? 0.1946 0.2252 0.1152 -0.0093 -0.0539 0.0142  106 SER B OG  
1653 N N   . TYR B 16  ? 0.1223 0.1407 0.0689 0.0111  -0.0313 0.0046  107 TYR B N   
1654 C CA  . TYR B 16  ? 0.1297 0.1369 0.0713 0.0116  -0.0220 -0.0073 107 TYR B CA  
1655 C C   . TYR B 16  ? 0.1399 0.1436 0.0906 0.0178  -0.0148 -0.0070 107 TYR B C   
1656 O O   . TYR B 16  ? 0.1492 0.1452 0.0970 0.0174  -0.0082 -0.0154 107 TYR B O   
1657 C CB  . TYR B 16  ? 0.1585 0.1629 0.1005 0.0057  -0.0239 -0.0211 107 TYR B CB  
1658 C CG  . TYR B 16  ? 0.1372 0.1411 0.0650 -0.0032 -0.0277 -0.0241 107 TYR B CG  
1659 C CD1 . TYR B 16  ? 0.1509 0.1471 0.0608 -0.0082 -0.0215 -0.0279 107 TYR B CD1 
1660 C CD2 . TYR B 16  ? 0.1930 0.2030 0.1222 -0.0086 -0.0369 -0.0229 107 TYR B CD2 
1661 C CE1 . TYR B 16  ? 0.1918 0.1854 0.0826 -0.0195 -0.0244 -0.0308 107 TYR B CE1 
1662 C CE2 . TYR B 16  ? 0.2121 0.2201 0.1240 -0.0196 -0.0401 -0.0262 107 TYR B CE2 
1663 C CZ  . TYR B 16  ? 0.2866 0.2862 0.1817 -0.0239 -0.0330 -0.0295 107 TYR B CZ  
1664 O OH  . TYR B 16  ? 0.3535 0.3498 0.2355 -0.0335 -0.0336 -0.0315 107 TYR B OH  
1665 N N   . GLY B 17  ? 0.1235 0.1323 0.0842 0.0220  -0.0152 0.0022  108 GLY B N   
1666 C CA  . GLY B 17  ? 0.1393 0.1421 0.1034 0.0250  -0.0067 0.0013  108 GLY B CA  
1667 C C   . GLY B 17  ? 0.1733 0.1739 0.1383 0.0211  -0.0103 -0.0074 108 GLY B C   
1668 O O   . GLY B 17  ? 0.1417 0.1347 0.1022 0.0195  -0.0050 -0.0129 108 GLY B O   
1669 N N   . PHE B 18  ? 0.1238 0.1306 0.0949 0.0186  -0.0199 -0.0077 109 PHE B N   
1670 C CA  . PHE B 18  ? 0.1219 0.1265 0.0968 0.0152  -0.0254 -0.0135 109 PHE B CA  
1671 C C   . PHE B 18  ? 0.1673 0.1687 0.1409 0.0139  -0.0234 -0.0094 109 PHE B C   
1672 O O   . PHE B 18  ? 0.1465 0.1509 0.1223 0.0151  -0.0206 -0.0024 109 PHE B O   
1673 C CB  . PHE B 18  ? 0.1296 0.1391 0.1116 0.0126  -0.0348 -0.0147 109 PHE B CB  
1674 C CG  . PHE B 18  ? 0.1118 0.1186 0.1018 0.0101  -0.0413 -0.0174 109 PHE B CG  
1675 C CD1 . PHE B 18  ? 0.1883 0.1913 0.1849 0.0093  -0.0426 -0.0249 109 PHE B CD1 
1676 C CD2 . PHE B 18  ? 0.1011 0.1096 0.0948 0.0083  -0.0463 -0.0112 109 PHE B CD2 
1677 C CE1 . PHE B 18  ? 0.2017 0.2025 0.2098 0.0076  -0.0490 -0.0240 109 PHE B CE1 
1678 C CE2 . PHE B 18  ? 0.1416 0.1460 0.1420 0.0054  -0.0507 -0.0109 109 PHE B CE2 
1679 C CZ  . PHE B 18  ? 0.1664 0.1669 0.1745 0.0055  -0.0523 -0.0160 109 PHE B CZ  
1680 N N   . ARG B 19  ? 0.0924 0.0881 0.0628 0.0102  -0.0249 -0.0137 110 ARG B N   
1681 C CA  . ARG B 19  ? 0.1079 0.0987 0.0716 0.0052  -0.0252 -0.0103 110 ARG B CA  
1682 C C   . ARG B 19  ? 0.1402 0.1282 0.1043 -0.0002 -0.0343 -0.0133 110 ARG B C   
1683 O O   . ARG B 19  ? 0.1217 0.1115 0.0931 0.0008  -0.0364 -0.0189 110 ARG B O   
1684 C CB  . ARG B 19  ? 0.1342 0.1174 0.0857 0.0043  -0.0111 -0.0092 110 ARG B CB  
1685 C CG  . ARG B 19  ? 0.1363 0.1122 0.0787 0.0019  -0.0049 -0.0155 110 ARG B CG  
1686 C CD  . ARG B 19  ? 0.1172 0.0952 0.0644 0.0086  0.0005  -0.0177 110 ARG B CD  
1687 N NE  . ARG B 19  ? 0.1407 0.1100 0.0786 0.0056  0.0089  -0.0235 110 ARG B NE  
1688 C CZ  . ARG B 19  ? 0.2502 0.2177 0.1883 0.0092  0.0154  -0.0259 110 ARG B CZ  
1689 N NH1 . ARG B 19  ? 0.1652 0.1387 0.1097 0.0151  0.0133  -0.0226 110 ARG B NH1 
1690 N NH2 . ARG B 19  ? 0.2087 0.1701 0.1418 0.0051  0.0224  -0.0304 110 ARG B NH2 
1691 N N   . LEU B 20  ? 0.1243 0.1082 0.0811 -0.0069 -0.0393 -0.0086 111 LEU B N   
1692 C CA  . LEU B 20  ? 0.1183 0.1007 0.0766 -0.0133 -0.0514 -0.0076 111 LEU B CA  
1693 C C   . LEU B 20  ? 0.1316 0.1074 0.0725 -0.0212 -0.0471 -0.0100 111 LEU B C   
1694 O O   . LEU B 20  ? 0.2320 0.2011 0.1574 -0.0225 -0.0327 -0.0126 111 LEU B O   
1695 C CB  . LEU B 20  ? 0.1253 0.1063 0.0840 -0.0175 -0.0573 0.0006  111 LEU B CB  
1696 C CG  . LEU B 20  ? 0.1153 0.1011 0.0903 -0.0116 -0.0596 0.0025  111 LEU B CG  
1697 C CD1 . LEU B 20  ? 0.1263 0.1071 0.0971 -0.0172 -0.0642 0.0104  111 LEU B CD1 
1698 C CD2 . LEU B 20  ? 0.1062 0.0963 0.1028 -0.0061 -0.0622 -0.0013 111 LEU B CD2 
1699 N N   . GLY B 21  ? 0.1346 0.1147 0.0849 -0.0248 -0.0546 -0.0085 112 GLY B N   
1700 C CA  . GLY B 21  ? 0.1508 0.1260 0.0858 -0.0345 -0.0529 -0.0090 112 GLY B CA  
1701 C C   . GLY B 21  ? 0.1617 0.1395 0.1029 -0.0399 -0.0650 -0.0008 112 GLY B C   
1702 O O   . GLY B 21  ? 0.1728 0.1572 0.1359 -0.0344 -0.0735 0.0034  112 GLY B O   
1703 N N   . PHE B 22  ? 0.0991 0.0866 0.0976 -0.0125 -0.0143 -0.0034 113 PHE B N   
1704 C CA  . PHE B 22  ? 0.1158 0.1075 0.1178 -0.0138 -0.0169 -0.0039 113 PHE B CA  
1705 C C   . PHE B 22  ? 0.1739 0.1565 0.1688 -0.0199 -0.0227 -0.0046 113 PHE B C   
1706 O O   . PHE B 22  ? 0.1431 0.1101 0.1245 -0.0213 -0.0243 -0.0051 113 PHE B O   
1707 C CB  . PHE B 22  ? 0.1029 0.0916 0.0992 -0.0070 -0.0151 -0.0046 113 PHE B CB  
1708 C CG  . PHE B 22  ? 0.1164 0.1157 0.1207 -0.0032 -0.0100 -0.0038 113 PHE B CG  
1709 C CD1 . PHE B 22  ? 0.1622 0.1703 0.1741 -0.0036 -0.0086 -0.0035 113 PHE B CD1 
1710 C CD2 . PHE B 22  ? 0.1206 0.1205 0.1235 0.0007  -0.0069 -0.0033 113 PHE B CD2 
1711 C CE1 . PHE B 22  ? 0.1453 0.1611 0.1626 -0.0021 -0.0042 -0.0030 113 PHE B CE1 
1712 C CE2 . PHE B 22  ? 0.1742 0.1854 0.1852 0.0024  -0.0032 -0.0026 113 PHE B CE2 
1713 C CZ  . PHE B 22  ? 0.0698 0.0881 0.0875 0.0001  -0.0019 -0.0025 113 PHE B CZ  
1714 N N   . LEU B 23  ? 0.1476 0.1394 0.1507 -0.0234 -0.0263 -0.0044 114 LEU B N   
1715 C CA  . LEU B 23  ? 0.1954 0.1815 0.1934 -0.0304 -0.0334 -0.0050 114 LEU B CA  
1716 C C   . LEU B 23  ? 0.1859 0.1547 0.1659 -0.0267 -0.0366 -0.0068 114 LEU B C   
1717 O O   . LEU B 23  ? 0.2139 0.1791 0.1887 -0.0184 -0.0327 -0.0072 114 LEU B O   
1718 C CB  . LEU B 23  ? 0.1584 0.1629 0.1720 -0.0338 -0.0369 -0.0040 114 LEU B CB  
1719 C CG  . LEU B 23  ? 0.2270 0.2490 0.2579 -0.0358 -0.0324 -0.0019 114 LEU B CG  
1720 C CD1 . LEU B 23  ? 0.2881 0.3289 0.3340 -0.0373 -0.0358 -0.0006 114 LEU B CD1 
1721 C CD2 . LEU B 23  ? 0.2681 0.2850 0.2970 -0.0436 -0.0314 -0.0013 114 LEU B CD2 
1722 N N   . HIS B 24  ? 0.1778 0.1350 0.1471 -0.0336 -0.0437 -0.0078 115 HIS B N   
1723 C CA  . HIS B 24  ? 0.1873 0.1247 0.1360 -0.0309 -0.0478 -0.0096 115 HIS B CA  
1724 C C   . HIS B 24  ? 0.2503 0.1967 0.2045 -0.0343 -0.0555 -0.0099 115 HIS B C   
1725 O O   . HIS B 24  ? 0.2646 0.2117 0.2191 -0.0441 -0.0635 -0.0101 115 HIS B O   
1726 C CB  . HIS B 24  ? 0.2380 0.1511 0.1656 -0.0361 -0.0507 -0.0108 115 HIS B CB  
1727 C CG  . HIS B 24  ? 0.2858 0.1903 0.2075 -0.0313 -0.0436 -0.0103 115 HIS B CG  
1728 N ND1 . HIS B 24  ? 0.2990 0.2069 0.2269 -0.0377 -0.0422 -0.0091 115 HIS B ND1 
1729 C CD2 . HIS B 24  ? 0.2863 0.1808 0.1972 -0.0200 -0.0374 -0.0104 115 HIS B CD2 
1730 C CE1 . HIS B 24  ? 0.3101 0.2089 0.2298 -0.0301 -0.0362 -0.0087 115 HIS B CE1 
1731 N NE2 . HIS B 24  ? 0.2570 0.1492 0.1676 -0.0191 -0.0334 -0.0094 115 HIS B NE2 
1732 N N   . SER B 25  ? 0.2142 0.1671 0.1719 -0.0262 -0.0532 -0.0096 116 SER B N   
1733 C CA  . SER B 25  ? 0.2123 0.1767 0.1774 -0.0267 -0.0595 -0.0092 116 SER B CA  
1734 C C   . SER B 25  ? 0.2798 0.2260 0.2242 -0.0243 -0.0657 -0.0109 116 SER B C   
1735 O O   . SER B 25  ? 0.2367 0.1900 0.1841 -0.0253 -0.0733 -0.0108 116 SER B O   
1736 C CB  . SER B 25  ? 0.1864 0.1668 0.1657 -0.0192 -0.0532 -0.0077 116 SER B CB  
1737 O OG  . SER B 25  ? 0.1910 0.1870 0.1877 -0.0215 -0.0481 -0.0062 116 SER B OG  
1738 N N   . GLY B 26  ? 0.2257 0.1483 0.1482 -0.0202 -0.0625 -0.0124 117 GLY B N   
1739 C CA  . GLY B 26  ? 0.2220 0.1234 0.1209 -0.0174 -0.0676 -0.0141 117 GLY B CA  
1740 C C   . GLY B 26  ? 0.2946 0.1968 0.1911 -0.0073 -0.0627 -0.0135 117 GLY B C   
1741 O O   . GLY B 26  ? 0.2549 0.1727 0.1670 -0.0030 -0.0552 -0.0119 117 GLY B O   
1742 N N   . THR B 27  ? 0.2672 0.1498 0.1413 -0.0042 -0.0671 -0.0148 118 THR B N   
1743 C CA  . THR B 27  ? 0.2977 0.1751 0.1636 0.0052  -0.0616 -0.0142 118 THR B CA  
1744 C C   . THR B 27  ? 0.3590 0.2313 0.2151 0.0055  -0.0719 -0.0147 118 THR B C   
1745 O O   . THR B 27  ? 0.2890 0.1453 0.1264 0.0126  -0.0695 -0.0149 118 THR B O   
1746 C CB  . THR B 27  ? 0.3639 0.2190 0.2078 0.0126  -0.0529 -0.0148 118 THR B CB  
1747 O OG1 . THR B 27  ? 0.3613 0.1906 0.1792 0.0105  -0.0600 -0.0170 118 THR B OG1 
1748 C CG2 . THR B 27  ? 0.3166 0.1795 0.1715 0.0141  -0.0430 -0.0139 118 THR B CG2 
1749 N N   . ALA B 28  ? 0.3388 0.2251 0.2071 -0.0021 -0.0834 -0.0147 119 ALA B N   
1750 C CA  . ALA B 28  ? 0.3669 0.2526 0.2286 -0.0010 -0.0943 -0.0148 119 ALA B CA  
1751 C C   . ALA B 28  ? 0.3654 0.2577 0.2313 0.0089  -0.0882 -0.0129 119 ALA B C   
1752 O O   . ALA B 28  ? 0.2516 0.1584 0.1345 0.0115  -0.0785 -0.0113 119 ALA B O   
1753 C CB  . ALA B 28  ? 0.3889 0.2982 0.2726 -0.0101 -0.1040 -0.0138 119 ALA B CB  
1754 N N   . LYS B 29  ? 0.3682 0.2477 0.2165 0.0139  -0.0941 -0.0131 120 LYS B N   
1755 C CA  . LYS B 29  ? 0.3561 0.2366 0.2024 0.0234  -0.0896 -0.0114 120 LYS B CA  
1756 C C   . LYS B 29  ? 0.3800 0.2891 0.2541 0.0241  -0.0894 -0.0091 120 LYS B C   
1757 O O   . LYS B 29  ? 0.3230 0.2344 0.2002 0.0306  -0.0803 -0.0075 120 LYS B O   
1758 C CB  . LYS B 29  ? 0.3827 0.2489 0.2119 0.0274  -0.0957 -0.0116 120 LYS B CB  
1759 N N   . SER B 30  ? 0.3242 0.2547 0.2180 0.0171  -0.0986 -0.0088 121 SER B N   
1760 C CA  . SER B 30  ? 0.3449 0.3033 0.2644 0.0190  -0.0988 -0.0064 121 SER B CA  
1761 C C   . SER B 30  ? 0.3175 0.2902 0.2572 0.0156  -0.0880 -0.0056 121 SER B C   
1762 O O   . SER B 30  ? 0.2934 0.2868 0.2523 0.0182  -0.0861 -0.0035 121 SER B O   
1763 C CB  . SER B 30  ? 0.3825 0.3612 0.3166 0.0129  -0.1118 -0.0058 121 SER B CB  
1764 O OG  . SER B 30  ? 0.4077 0.3877 0.3465 0.0007  -0.1138 -0.0072 121 SER B OG  
1765 N N   . VAL B 31  ? 0.2332 0.1952 0.1682 0.0110  -0.0809 -0.0070 122 VAL B N   
1766 C CA  . VAL B 31  ? 0.2176 0.1928 0.1707 0.0075  -0.0723 -0.0063 122 VAL B CA  
1767 C C   . VAL B 31  ? 0.2590 0.2365 0.2157 0.0147  -0.0615 -0.0049 122 VAL B C   
1768 O O   . VAL B 31  ? 0.2594 0.2212 0.2000 0.0206  -0.0569 -0.0050 122 VAL B O   
1769 C CB  . VAL B 31  ? 0.2503 0.2121 0.1950 0.0022  -0.0684 -0.0081 122 VAL B CB  
1770 C CG1 . VAL B 31  ? 0.2748 0.2193 0.2043 0.0085  -0.0581 -0.0086 122 VAL B CG1 
1771 C CG2 . VAL B 31  ? 0.2100 0.1870 0.1737 -0.0040 -0.0647 -0.0074 122 VAL B CG2 
1772 N N   . THR B 32  ? 0.1551 0.1507 0.1313 0.0137  -0.0573 -0.0034 123 THR B N   
1773 C CA  . THR B 32  ? 0.2063 0.2032 0.1848 0.0194  -0.0483 -0.0021 123 THR B CA  
1774 C C   . THR B 32  ? 0.1849 0.1815 0.1682 0.0160  -0.0385 -0.0025 123 THR B C   
1775 O O   . THR B 32  ? 0.1785 0.1721 0.1600 0.0191  -0.0308 -0.0018 123 THR B O   
1776 C CB  . THR B 32  ? 0.1658 0.1815 0.1598 0.0229  -0.0503 0.0000  123 THR B CB  
1777 O OG1 . THR B 32  ? 0.1317 0.1645 0.1444 0.0165  -0.0496 0.0005  123 THR B OG1 
1778 C CG2 . THR B 32  ? 0.1798 0.2004 0.1720 0.0264  -0.0617 0.0007  123 THR B CG2 
1779 N N   . CYS B 33  ? 0.1463 0.1446 0.1340 0.0096  -0.0392 -0.0035 124 CYS B N   
1780 C CA  . CYS B 33  ? 0.1417 0.1400 0.1332 0.0071  -0.0313 -0.0037 124 CYS B CA  
1781 C C   . CYS B 33  ? 0.1777 0.1680 0.1630 0.0028  -0.0338 -0.0051 124 CYS B C   
1782 O O   . CYS B 33  ? 0.1458 0.1397 0.1346 -0.0023 -0.0407 -0.0055 124 CYS B O   
1783 C CB  . CYS B 33  ? 0.1285 0.1425 0.1370 0.0048  -0.0286 -0.0025 124 CYS B CB  
1784 S SG  . CYS B 33  ? 0.1802 0.1950 0.1931 0.0015  -0.0210 -0.0027 124 CYS B SG  
1785 N N   . THR B 34  ? 0.1285 0.1077 0.1037 0.0049  -0.0283 -0.0058 125 THR B N   
1786 C CA  . THR B 34  ? 0.1544 0.1231 0.1206 0.0029  -0.0297 -0.0070 125 THR B CA  
1787 C C   . THR B 34  ? 0.1290 0.0959 0.0941 0.0059  -0.0211 -0.0067 125 THR B C   
1788 O O   . THR B 34  ? 0.1668 0.1346 0.1310 0.0097  -0.0149 -0.0061 125 THR B O   
1789 C CB  . THR B 34  ? 0.1963 0.1476 0.1432 0.0047  -0.0351 -0.0083 125 THR B CB  
1790 O OG1 . THR B 34  ? 0.2120 0.1499 0.1472 0.0027  -0.0368 -0.0096 125 THR B OG1 
1791 C CG2 . THR B 34  ? 0.1739 0.1156 0.1088 0.0117  -0.0291 -0.0080 125 THR B CG2 
1792 N N   . TYR B 35  ? 0.1287 0.0933 0.0934 0.0041  -0.0209 -0.0071 126 TYR B N   
1793 C CA  . TYR B 35  ? 0.1249 0.0914 0.0910 0.0076  -0.0139 -0.0065 126 TYR B CA  
1794 C C   . TYR B 35  ? 0.1530 0.1028 0.1016 0.0124  -0.0128 -0.0072 126 TYR B C   
1795 O O   . TYR B 35  ? 0.1573 0.0940 0.0949 0.0099  -0.0182 -0.0083 126 TYR B O   
1796 C CB  . TYR B 35  ? 0.1160 0.0925 0.0943 0.0037  -0.0137 -0.0059 126 TYR B CB  
1797 C CG  . TYR B 35  ? 0.1171 0.0955 0.0957 0.0080  -0.0082 -0.0052 126 TYR B CG  
1798 C CD1 . TYR B 35  ? 0.1004 0.0910 0.0883 0.0101  -0.0026 -0.0042 126 TYR B CD1 
1799 C CD2 . TYR B 35  ? 0.1259 0.0935 0.0947 0.0101  -0.0089 -0.0055 126 TYR B CD2 
1800 C CE1 . TYR B 35  ? 0.1186 0.1146 0.1089 0.0141  0.0015  -0.0032 126 TYR B CE1 
1801 C CE2 . TYR B 35  ? 0.1216 0.0924 0.0909 0.0158  -0.0044 -0.0045 126 TYR B CE2 
1802 C CZ  . TYR B 35  ? 0.1432 0.1302 0.1247 0.0178  0.0005  -0.0033 126 TYR B CZ  
1803 O OH  . TYR B 35  ? 0.1520 0.1455 0.1358 0.0236  0.0040  -0.0021 126 TYR B OH  
1804 N N   . SER B 36  ? 0.2105 0.1606 0.1560 0.0190  -0.0055 -0.0064 127 SER B N   
1805 C CA  . SER B 36  ? 0.1719 0.1076 0.1010 0.0262  -0.0022 -0.0065 127 SER B CA  
1806 C C   . SER B 36  ? 0.1930 0.1363 0.1284 0.0299  0.0018  -0.0054 127 SER B C   
1807 O O   . SER B 36  ? 0.1442 0.1041 0.0925 0.0323  0.0076  -0.0038 127 SER B O   
1808 C CB  . SER B 36  ? 0.1854 0.1183 0.1072 0.0324  0.0045  -0.0058 127 SER B CB  
1809 O OG  . SER B 36  ? 0.2085 0.1300 0.1158 0.0412  0.0094  -0.0054 127 SER B OG  
1810 N N   . PRO B 37  ? 0.2223 0.1531 0.1477 0.0304  -0.0014 -0.0060 128 PRO B N   
1811 C CA  . PRO B 37  ? 0.1671 0.1024 0.0946 0.0367  0.0025  -0.0047 128 PRO B CA  
1812 C C   . PRO B 37  ? 0.1914 0.1259 0.1118 0.0485  0.0102  -0.0034 128 PRO B C   
1813 O O   . PRO B 37  ? 0.1693 0.1198 0.1009 0.0538  0.0147  -0.0015 128 PRO B O   
1814 C CB  . PRO B 37  ? 0.2250 0.1402 0.1371 0.0345  -0.0027 -0.0058 128 PRO B CB  
1815 C CG  . PRO B 37  ? 0.2667 0.1773 0.1790 0.0233  -0.0100 -0.0074 128 PRO B CG  
1816 C CD  . PRO B 37  ? 0.2307 0.1441 0.1435 0.0241  -0.0093 -0.0078 128 PRO B CD  
1817 N N   . ALA B 38  ? 0.1957 0.1132 0.0980 0.0530  0.0119  -0.0040 129 ALA B N   
1818 C CA  . ALA B 38  ? 0.2349 0.1517 0.1298 0.0653  0.0208  -0.0024 129 ALA B CA  
1819 C C   . ALA B 38  ? 0.2673 0.2113 0.1836 0.0654  0.0276  -0.0002 129 ALA B C   
1820 O O   . ALA B 38  ? 0.2171 0.1746 0.1398 0.0740  0.0349  0.0022  129 ALA B O   
1821 C CB  . ALA B 38  ? 0.2794 0.1698 0.1480 0.0696  0.0215  -0.0036 129 ALA B CB  
1822 N N   . LEU B 39  ? 0.1748 0.1271 0.1018 0.0560  0.0254  -0.0008 130 LEU B N   
1823 C CA  . LEU B 39  ? 0.1713 0.1453 0.1154 0.0537  0.0315  0.0010  130 LEU B CA  
1824 C C   . LEU B 39  ? 0.2036 0.1990 0.1698 0.0464  0.0288  0.0016  130 LEU B C   
1825 O O   . LEU B 39  ? 0.1700 0.1835 0.1503 0.0431  0.0333  0.0031  130 LEU B O   
1826 C CB  . LEU B 39  ? 0.1632 0.1292 0.1014 0.0487  0.0314  0.0003  130 LEU B CB  
1827 C CG  . LEU B 39  ? 0.1868 0.1305 0.1013 0.0551  0.0341  -0.0002 130 LEU B CG  
1828 C CD1 . LEU B 39  ? 0.1896 0.1231 0.0970 0.0493  0.0303  -0.0015 130 LEU B CD1 
1829 C CD2 . LEU B 39  ? 0.2360 0.1872 0.1500 0.0635  0.0459  0.0024  130 LEU B CD2 
1830 N N   . ASN B 40  ? 0.1575 0.1494 0.1250 0.0431  0.0219  0.0004  131 ASN B N   
1831 C CA  . ASN B 40  ? 0.1488 0.1549 0.1327 0.0351  0.0183  0.0003  131 ASN B CA  
1832 C C   . ASN B 40  ? 0.1467 0.1588 0.1379 0.0275  0.0188  0.0001  131 ASN B C   
1833 O O   . ASN B 40  ? 0.1569 0.1847 0.1610 0.0235  0.0214  0.0012  131 ASN B O   
1834 C CB  . ASN B 40  ? 0.1082 0.1330 0.1050 0.0381  0.0206  0.0021  131 ASN B CB  
1835 C CG  . ASN B 40  ? 0.0930 0.1288 0.1030 0.0300  0.0164  0.0019  131 ASN B CG  
1836 O OD1 . ASN B 40  ? 0.0916 0.1184 0.0988 0.0248  0.0115  0.0005  131 ASN B OD1 
1837 N ND2 . ASN B 40  ? 0.1605 0.2160 0.1843 0.0286  0.0184  0.0034  131 ASN B ND2 
1838 N N   . LYS B 41  ? 0.1124 0.1104 0.0936 0.0254  0.0158  -0.0013 132 LYS B N   
1839 C CA  . LYS B 41  ? 0.1093 0.1084 0.0921 0.0209  0.0170  -0.0012 132 LYS B CA  
1840 C C   . LYS B 41  ? 0.1098 0.0996 0.0885 0.0172  0.0100  -0.0027 132 LYS B C   
1841 O O   . LYS B 41  ? 0.1278 0.1046 0.0952 0.0188  0.0055  -0.0039 132 LYS B O   
1842 C CB  . LYS B 41  ? 0.1219 0.1145 0.0944 0.0254  0.0233  -0.0004 132 LYS B CB  
1843 C CG  . LYS B 41  ? 0.1224 0.1134 0.0935 0.0211  0.0255  -0.0001 132 LYS B CG  
1844 C CD  . LYS B 41  ? 0.1557 0.1428 0.1179 0.0250  0.0340  0.0014  132 LYS B CD  
1845 C CE  . LYS B 41  ? 0.1481 0.1300 0.1055 0.0207  0.0367  0.0019  132 LYS B CE  
1846 N NZ  . LYS B 41  ? 0.1863 0.1672 0.1374 0.0228  0.0468  0.0039  132 LYS B NZ  
1847 N N   . LEU B 42  ? 0.0999 0.0968 0.0873 0.0122  0.0089  -0.0026 133 LEU B N   
1848 C CA  . LEU B 42  ? 0.1485 0.1412 0.1349 0.0097  0.0031  -0.0034 133 LEU B CA  
1849 C C   . LEU B 42  ? 0.1790 0.1635 0.1561 0.0114  0.0043  -0.0032 133 LEU B C   
1850 O O   . LEU B 42  ? 0.1675 0.1536 0.1444 0.0108  0.0101  -0.0022 133 LEU B O   
1851 C CB  . LEU B 42  ? 0.0935 0.0968 0.0923 0.0054  0.0024  -0.0030 133 LEU B CB  
1852 C CG  . LEU B 42  ? 0.1365 0.1393 0.1368 0.0042  -0.0024 -0.0032 133 LEU B CG  
1853 C CD1 . LEU B 42  ? 0.1573 0.1582 0.1573 0.0031  -0.0086 -0.0039 133 LEU B CD1 
1854 C CD2 . LEU B 42  ? 0.1220 0.1331 0.1317 0.0016  -0.0009 -0.0025 133 LEU B CD2 
1855 N N   . PHE B 43  ? 0.1176 0.0927 0.0860 0.0129  -0.0017 -0.0040 134 PHE B N   
1856 C CA  . PHE B 43  ? 0.1437 0.1096 0.1014 0.0154  -0.0020 -0.0038 134 PHE B CA  
1857 C C   . PHE B 43  ? 0.1521 0.1226 0.1154 0.0145  -0.0086 -0.0037 134 PHE B C   
1858 O O   . PHE B 43  ? 0.1558 0.1298 0.1235 0.0127  -0.0155 -0.0044 134 PHE B O   
1859 C CB  . PHE B 43  ? 0.1833 0.1334 0.1234 0.0193  -0.0042 -0.0046 134 PHE B CB  
1860 C CG  . PHE B 43  ? 0.2110 0.1560 0.1440 0.0222  0.0030  -0.0043 134 PHE B CG  
1861 C CD1 . PHE B 43  ? 0.1684 0.1165 0.1051 0.0225  0.0032  -0.0047 134 PHE B CD1 
1862 C CD2 . PHE B 43  ? 0.1961 0.1328 0.1178 0.0255  0.0101  -0.0033 134 PHE B CD2 
1863 C CE1 . PHE B 43  ? 0.1820 0.1269 0.1125 0.0273  0.0103  -0.0040 134 PHE B CE1 
1864 C CE2 . PHE B 43  ? 0.1712 0.1057 0.0876 0.0292  0.0178  -0.0025 134 PHE B CE2 
1865 C CZ  . PHE B 43  ? 0.1674 0.1068 0.0887 0.0308  0.0178  -0.0029 134 PHE B CZ  
1866 N N   . CYS B 44  ? 0.1377 0.1074 0.0997 0.0159  -0.0062 -0.0028 135 CYS B N   
1867 C CA  . CYS B 44  ? 0.1664 0.1424 0.1346 0.0171  -0.0111 -0.0022 135 CYS B CA  
1868 C C   . CYS B 44  ? 0.2237 0.1895 0.1798 0.0220  -0.0100 -0.0013 135 CYS B C   
1869 O O   . CYS B 44  ? 0.2080 0.1634 0.1537 0.0222  -0.0032 -0.0009 135 CYS B O   
1870 C CB  . CYS B 44  ? 0.1469 0.1354 0.1296 0.0139  -0.0084 -0.0017 135 CYS B CB  
1871 S SG  . CYS B 44  ? 0.1931 0.1777 0.1728 0.0119  0.0011  -0.0010 135 CYS B SG  
1872 N N   . GLN B 45  ? 0.1641 0.1332 0.1216 0.0261  -0.0165 -0.0007 136 GLN B N   
1873 C CA  . GLN B 45  ? 0.1671 0.1261 0.1123 0.0326  -0.0160 0.0005  136 GLN B CA  
1874 C C   . GLN B 45  ? 0.1537 0.1143 0.1023 0.0331  -0.0098 0.0016  136 GLN B C   
1875 O O   . GLN B 45  ? 0.1604 0.1331 0.1231 0.0292  -0.0080 0.0015  136 GLN B O   
1876 C CB  . GLN B 45  ? 0.1677 0.1320 0.1139 0.0382  -0.0261 0.0010  136 GLN B CB  
1877 C CG  . GLN B 45  ? 0.2270 0.1837 0.1632 0.0381  -0.0333 -0.0001 136 GLN B CG  
1878 C CD  . GLN B 45  ? 0.2844 0.2494 0.2235 0.0422  -0.0450 0.0004  136 GLN B CD  
1879 O OE1 . GLN B 45  ? 0.2638 0.2459 0.2180 0.0443  -0.0476 0.0018  136 GLN B OE1 
1880 N NE2 . GLN B 45  ? 0.3085 0.2619 0.2329 0.0435  -0.0520 -0.0005 136 GLN B NE2 
1881 N N   . LEU B 46  ? 0.2246 0.1701 0.1571 0.0381  -0.0067 0.0026  137 LEU B N   
1882 C CA  . LEU B 46  ? 0.2274 0.1678 0.1565 0.0391  -0.0008 0.0035  137 LEU B CA  
1883 C C   . LEU B 46  ? 0.1820 0.1375 0.1251 0.0433  -0.0038 0.0044  137 LEU B C   
1884 O O   . LEU B 46  ? 0.2037 0.1661 0.1496 0.0509  -0.0103 0.0054  137 LEU B O   
1885 C CB  . LEU B 46  ? 0.1906 0.1088 0.0962 0.0455  0.0016  0.0047  137 LEU B CB  
1886 C CG  . LEU B 46  ? 0.2823 0.1884 0.1776 0.0472  0.0078  0.0057  137 LEU B CG  
1887 C CD1 . LEU B 46  ? 0.2435 0.1455 0.1386 0.0359  0.0155  0.0048  137 LEU B CD1 
1888 C CD2 . LEU B 46  ? 0.3004 0.1824 0.1698 0.0555  0.0089  0.0071  137 LEU B CD2 
1889 N N   . ALA B 47  ? 0.1598 0.1208 0.1111 0.0386  0.0009  0.0042  138 ALA B N   
1890 C CA  . ALA B 47  ? 0.1567 0.1287 0.1182 0.0424  0.0011  0.0052  138 ALA B CA  
1891 C C   . ALA B 47  ? 0.2304 0.2253 0.2123 0.0427  -0.0054 0.0056  138 ALA B C   
1892 O O   . ALA B 47  ? 0.3117 0.3185 0.3033 0.0475  -0.0054 0.0071  138 ALA B O   
1893 C CB  . ALA B 47  ? 0.2318 0.1924 0.1794 0.0535  0.0027  0.0071  138 ALA B CB  
1894 N N   . LYS B 48  ? 0.1298 0.1305 0.1176 0.0375  -0.0104 0.0044  139 LYS B N   
1895 C CA  . LYS B 48  ? 0.1193 0.1395 0.1245 0.0356  -0.0169 0.0047  139 LYS B CA  
1896 C C   . LYS B 48  ? 0.1474 0.1766 0.1650 0.0275  -0.0138 0.0040  139 LYS B C   
1897 O O   . LYS B 48  ? 0.1093 0.1301 0.1222 0.0229  -0.0087 0.0029  139 LYS B O   
1898 C CB  . LYS B 48  ? 0.1365 0.1549 0.1382 0.0338  -0.0246 0.0036  139 LYS B CB  
1899 C CG  . LYS B 48  ? 0.1484 0.1576 0.1365 0.0424  -0.0291 0.0044  139 LYS B CG  
1900 C CD  . LYS B 48  ? 0.2888 0.3109 0.2843 0.0512  -0.0321 0.0068  139 LYS B CD  
1901 C CE  . LYS B 48  ? 0.4188 0.4292 0.3979 0.0614  -0.0364 0.0078  139 LYS B CE  
1902 N NZ  . LYS B 48  ? 0.4679 0.4711 0.4382 0.0587  -0.0440 0.0063  139 LYS B NZ  
1903 N N   . THR B 49  ? 0.0895 0.1363 0.1229 0.0257  -0.0173 0.0049  140 THR B N   
1904 C CA  . THR B 49  ? 0.0784 0.1325 0.1221 0.0187  -0.0143 0.0047  140 THR B CA  
1905 C C   . THR B 49  ? 0.1222 0.1697 0.1628 0.0111  -0.0158 0.0026  140 THR B C   
1906 O O   . THR B 49  ? 0.1597 0.2063 0.1985 0.0091  -0.0220 0.0019  140 THR B O   
1907 C CB  . THR B 49  ? 0.1090 0.1835 0.1698 0.0177  -0.0173 0.0065  140 THR B CB  
1908 O OG1 . THR B 49  ? 0.0869 0.1690 0.1508 0.0270  -0.0155 0.0088  140 THR B OG1 
1909 C CG2 . THR B 49  ? 0.1357 0.2151 0.2044 0.0110  -0.0130 0.0065  140 THR B CG2 
1910 N N   . CYS B 50  ? 0.0867 0.1292 0.1255 0.0076  -0.0105 0.0019  141 CYS B N   
1911 C CA  . CYS B 50  ? 0.0891 0.1261 0.1249 0.0025  -0.0109 0.0004  141 CYS B CA  
1912 C C   . CYS B 50  ? 0.1083 0.1515 0.1521 -0.0024 -0.0093 0.0007  141 CYS B C   
1913 O O   . CYS B 50  ? 0.0952 0.1373 0.1390 -0.0028 -0.0044 0.0008  141 CYS B O   
1914 C CB  . CYS B 50  ? 0.1177 0.1443 0.1439 0.0031  -0.0063 -0.0005 141 CYS B CB  
1915 S SG  . CYS B 50  ? 0.1292 0.1446 0.1422 0.0079  -0.0066 -0.0006 141 CYS B SG  
1916 N N   . PRO B 51  ? 0.0861 0.1340 0.1350 -0.0067 -0.0135 0.0007  142 PRO B N   
1917 C CA  . PRO B 51  ? 0.0797 0.1310 0.1339 -0.0116 -0.0115 0.0012  142 PRO B CA  
1918 C C   . PRO B 51  ? 0.1491 0.1902 0.1954 -0.0130 -0.0100 -0.0000 142 PRO B C   
1919 O O   . PRO B 51  ? 0.1214 0.1544 0.1600 -0.0129 -0.0128 -0.0012 142 PRO B O   
1920 C CB  . PRO B 51  ? 0.0895 0.1475 0.1499 -0.0169 -0.0168 0.0018  142 PRO B CB  
1921 C CG  . PRO B 51  ? 0.1450 0.2048 0.2043 -0.0142 -0.0226 0.0015  142 PRO B CG  
1922 C CD  . PRO B 51  ? 0.1371 0.1858 0.1854 -0.0081 -0.0206 0.0004  142 PRO B CD  
1923 N N   . VAL B 52  ? 0.1177 0.1589 0.1649 -0.0135 -0.0058 0.0003  143 VAL B N   
1924 C CA  . VAL B 52  ? 0.0839 0.1182 0.1250 -0.0138 -0.0048 -0.0004 143 VAL B CA  
1925 C C   . VAL B 52  ? 0.1201 0.1543 0.1625 -0.0173 -0.0036 0.0004  143 VAL B C   
1926 O O   . VAL B 52  ? 0.0956 0.1344 0.1423 -0.0179 -0.0004 0.0015  143 VAL B O   
1927 C CB  . VAL B 52  ? 0.1064 0.1402 0.1451 -0.0111 -0.0017 -0.0008 143 VAL B CB  
1928 C CG1 . VAL B 52  ? 0.0862 0.1171 0.1211 -0.0106 -0.0013 -0.0011 143 VAL B CG1 
1929 C CG2 . VAL B 52  ? 0.1325 0.1645 0.1682 -0.0083 -0.0019 -0.0013 143 VAL B CG2 
1930 N N   . GLN B 53  ? 0.0634 0.0901 0.0998 -0.0192 -0.0056 0.0001  144 GLN B N   
1931 C CA  . GLN B 53  ? 0.0784 0.1017 0.1129 -0.0227 -0.0042 0.0011  144 GLN B CA  
1932 C C   . GLN B 53  ? 0.1093 0.1292 0.1391 -0.0195 -0.0021 0.0011  144 GLN B C   
1933 O O   . GLN B 53  ? 0.0999 0.1186 0.1265 -0.0153 -0.0028 0.0003  144 GLN B O   
1934 C CB  . GLN B 53  ? 0.1008 0.1133 0.1270 -0.0264 -0.0074 0.0008  144 GLN B CB  
1935 C CG  . GLN B 53  ? 0.1347 0.1504 0.1647 -0.0313 -0.0112 0.0007  144 GLN B CG  
1936 C CD  . GLN B 53  ? 0.1822 0.1833 0.2003 -0.0360 -0.0148 0.0002  144 GLN B CD  
1937 O OE1 . GLN B 53  ? 0.1660 0.1529 0.1707 -0.0324 -0.0148 -0.0006 144 GLN B OE1 
1938 N NE2 . GLN B 53  ? 0.2499 0.2544 0.2720 -0.0443 -0.0181 0.0007  144 GLN B NE2 
1939 N N   . LEU B 54  ? 0.0873 0.1062 0.1165 -0.0217 0.0005  0.0022  145 LEU B N   
1940 C CA  . LEU B 54  ? 0.1099 0.1242 0.1327 -0.0192 0.0013  0.0023  145 LEU B CA  
1941 C C   . LEU B 54  ? 0.1001 0.1030 0.1133 -0.0210 0.0012  0.0031  145 LEU B C   
1942 O O   . LEU B 54  ? 0.1218 0.1227 0.1353 -0.0261 0.0034  0.0043  145 LEU B O   
1943 C CB  . LEU B 54  ? 0.1577 0.1761 0.1831 -0.0194 0.0046  0.0028  145 LEU B CB  
1944 C CG  . LEU B 54  ? 0.1135 0.1393 0.1450 -0.0181 0.0056  0.0022  145 LEU B CG  
1945 C CD1 . LEU B 54  ? 0.1665 0.1913 0.1960 -0.0183 0.0094  0.0028  145 LEU B CD1 
1946 C CD2 . LEU B 54  ? 0.0855 0.1131 0.1163 -0.0157 0.0032  0.0010  145 LEU B CD2 
1947 N N   . TRP B 55  ? 0.0919 0.0875 0.0963 -0.0164 -0.0011 0.0028  146 TRP B N   
1948 C CA  . TRP B 55  ? 0.1274 0.1080 0.1183 -0.0164 -0.0015 0.0036  146 TRP B CA  
1949 C C   . TRP B 55  ? 0.1108 0.0883 0.0947 -0.0111 -0.0022 0.0041  146 TRP B C   
1950 O O   . TRP B 55  ? 0.1486 0.1346 0.1363 -0.0057 -0.0042 0.0036  146 TRP B O   
1951 C CB  . TRP B 55  ? 0.1154 0.0861 0.0977 -0.0135 -0.0042 0.0029  146 TRP B CB  
1952 C CG  . TRP B 55  ? 0.1263 0.0957 0.1109 -0.0196 -0.0051 0.0023  146 TRP B CG  
1953 C CD1 . TRP B 55  ? 0.1563 0.1348 0.1494 -0.0193 -0.0065 0.0012  146 TRP B CD1 
1954 C CD2 . TRP B 55  ? 0.1595 0.1169 0.1365 -0.0274 -0.0054 0.0028  146 TRP B CD2 
1955 N NE1 . TRP B 55  ? 0.1532 0.1271 0.1449 -0.0259 -0.0086 0.0009  146 TRP B NE1 
1956 C CE2 . TRP B 55  ? 0.1486 0.1104 0.1313 -0.0318 -0.0080 0.0019  146 TRP B CE2 
1957 C CE3 . TRP B 55  ? 0.1804 0.1230 0.1452 -0.0318 -0.0039 0.0041  146 TRP B CE3 
1958 C CZ2 . TRP B 55  ? 0.1924 0.1464 0.1705 -0.0413 -0.0099 0.0021  146 TRP B CZ2 
1959 C CZ3 . TRP B 55  ? 0.2123 0.1461 0.1722 -0.0417 -0.0046 0.0044  146 TRP B CZ3 
1960 C CH2 . TRP B 55  ? 0.1996 0.1401 0.1669 -0.0469 -0.0080 0.0034  146 TRP B CH2 
1961 N N   . VAL B 56  ? 0.1234 0.0888 0.0965 -0.0129 -0.0007 0.0054  147 VAL B N   
1962 C CA  . VAL B 56  ? 0.1362 0.0943 0.0980 -0.0070 -0.0025 0.0061  147 VAL B CA  
1963 C C   . VAL B 56  ? 0.1547 0.0914 0.0981 -0.0071 -0.0019 0.0073  147 VAL B C   
1964 O O   . VAL B 56  ? 0.1807 0.1092 0.1212 -0.0147 0.0011  0.0078  147 VAL B O   
1965 C CB  . VAL B 56  ? 0.1650 0.1268 0.1279 -0.0086 -0.0012 0.0065  147 VAL B CB  
1966 C CG1 . VAL B 56  ? 0.1395 0.1182 0.1154 -0.0077 -0.0028 0.0053  147 VAL B CG1 
1967 C CG2 . VAL B 56  ? 0.1390 0.0966 0.1021 -0.0161 0.0045  0.0075  147 VAL B CG2 
1968 N N   . ASP B 57  ? 0.1965 0.1242 0.1269 0.0013  -0.0049 0.0079  148 ASP B N   
1969 C CA  . ASP B 57  ? 0.2037 0.1071 0.1123 0.0022  -0.0041 0.0093  148 ASP B CA  
1970 C C   . ASP B 57  ? 0.2795 0.1742 0.1801 -0.0024 -0.0009 0.0107  148 ASP B C   
1971 O O   . ASP B 57  ? 0.2383 0.1128 0.1229 -0.0067 0.0023  0.0121  148 ASP B O   
1972 C CB  . ASP B 57  ? 0.2200 0.1160 0.1157 0.0151  -0.0084 0.0099  148 ASP B CB  
1973 C CG  . ASP B 57  ? 0.2693 0.1686 0.1678 0.0210  -0.0099 0.0090  148 ASP B CG  
1974 O OD1 . ASP B 57  ? 0.2929 0.1866 0.1917 0.0143  -0.0080 0.0081  148 ASP B OD1 
1975 O OD2 . ASP B 57  ? 0.3261 0.2344 0.2265 0.0322  -0.0131 0.0093  148 ASP B OD2 
1976 N N   . SER B 58  ? 0.1923 0.0995 0.1010 -0.0018 -0.0014 0.0105  149 SER B N   
1977 C CA  . SER B 58  ? 0.2428 0.1409 0.1424 -0.0053 0.0022  0.0118  149 SER B CA  
1978 C C   . SER B 58  ? 0.2047 0.1195 0.1196 -0.0092 0.0042  0.0109  149 SER B C   
1979 O O   . SER B 58  ? 0.1704 0.1018 0.0986 -0.0068 0.0006  0.0094  149 SER B O   
1980 C CB  . SER B 58  ? 0.3422 0.2273 0.2231 0.0031  -0.0021 0.0127  149 SER B CB  
1981 O OG  . SER B 58  ? 0.4240 0.3244 0.3129 0.0110  -0.0091 0.0117  149 SER B OG  
1982 N N   . THR B 59  ? 0.2323 0.1414 0.1438 -0.0151 0.0107  0.0121  150 THR B N   
1983 C CA  . THR B 59  ? 0.2320 0.1539 0.1557 -0.0183 0.0144  0.0116  150 THR B CA  
1984 C C   . THR B 59  ? 0.2083 0.1313 0.1271 -0.0138 0.0102  0.0106  150 THR B C   
1985 O O   . THR B 59  ? 0.1940 0.1026 0.0953 -0.0111 0.0089  0.0114  150 THR B O   
1986 C CB  . THR B 59  ? 0.2565 0.1716 0.1764 -0.0244 0.0235  0.0137  150 THR B CB  
1987 O OG1 . THR B 59  ? 0.2183 0.1368 0.1465 -0.0308 0.0266  0.0146  150 THR B OG1 
1988 C CG2 . THR B 59  ? 0.2175 0.1422 0.1453 -0.0250 0.0281  0.0136  150 THR B CG2 
1989 N N   . PRO B 60  ? 0.1754 0.1135 0.1072 -0.0134 0.0075  0.0089  151 PRO B N   
1990 C CA  . PRO B 60  ? 0.1637 0.1022 0.0901 -0.0114 0.0030  0.0078  151 PRO B CA  
1991 C C   . PRO B 60  ? 0.1727 0.1021 0.0903 -0.0140 0.0092  0.0082  151 PRO B C   
1992 O O   . PRO B 60  ? 0.1977 0.1245 0.1168 -0.0166 0.0176  0.0097  151 PRO B O   
1993 C CB  . PRO B 60  ? 0.1455 0.1021 0.0888 -0.0119 -0.0005 0.0060  151 PRO B CB  
1994 C CG  . PRO B 60  ? 0.2338 0.1971 0.1898 -0.0148 0.0052  0.0062  151 PRO B CG  
1995 C CD  . PRO B 60  ? 0.1419 0.0961 0.0923 -0.0151 0.0077  0.0078  151 PRO B CD  
1996 N N   . PRO B 61  ? 0.2209 0.1450 0.1281 -0.0132 0.0053  0.0072  152 PRO B N   
1997 C CA  . PRO B 61  ? 0.2380 0.1481 0.1309 -0.0143 0.0115  0.0077  152 PRO B CA  
1998 C C   . PRO B 61  ? 0.1912 0.1079 0.0941 -0.0161 0.0190  0.0076  152 PRO B C   
1999 O O   . PRO B 61  ? 0.1893 0.1202 0.1073 -0.0171 0.0167  0.0063  152 PRO B O   
2000 C CB  . PRO B 61  ? 0.2681 0.1714 0.1475 -0.0137 0.0031  0.0061  152 PRO B CB  
2001 C CG  . PRO B 61  ? 0.2268 0.1367 0.1088 -0.0107 -0.0065 0.0061  152 PRO B CG  
2002 C CD  . PRO B 61  ? 0.1849 0.1119 0.0882 -0.0107 -0.0052 0.0061  152 PRO B CD  
2003 N N   . PRO B 62  ? 0.2105 0.1174 0.1049 -0.0159 0.0286  0.0092  153 PRO B N   
2004 C CA  . PRO B 62  ? 0.1954 0.1054 0.0939 -0.0152 0.0353  0.0091  153 PRO B CA  
2005 C C   . PRO B 62  ? 0.1975 0.1044 0.0900 -0.0155 0.0290  0.0064  153 PRO B C   
2006 O O   . PRO B 62  ? 0.2488 0.1442 0.1257 -0.0163 0.0223  0.0052  153 PRO B O   
2007 C CB  . PRO B 62  ? 0.2339 0.1284 0.1161 -0.0133 0.0454  0.0112  153 PRO B CB  
2008 C CG  . PRO B 62  ? 0.2288 0.1172 0.1056 -0.0148 0.0463  0.0131  153 PRO B CG  
2009 C CD  . PRO B 62  ? 0.2172 0.1077 0.0949 -0.0153 0.0340  0.0114  153 PRO B CD  
2010 N N   . GLY B 63  ? 0.1863 0.1028 0.0902 -0.0153 0.0306  0.0056  154 GLY B N   
2011 C CA  . GLY B 63  ? 0.2420 0.1549 0.1402 -0.0172 0.0251  0.0032  154 GLY B CA  
2012 C C   . GLY B 63  ? 0.2073 0.1356 0.1204 -0.0205 0.0162  0.0017  154 GLY B C   
2013 O O   . GLY B 63  ? 0.1775 0.1056 0.0891 -0.0234 0.0124  -0.0001 154 GLY B O   
2014 N N   . THR B 64  ? 0.1603 0.1004 0.0860 -0.0201 0.0134  0.0025  155 THR B N   
2015 C CA  . THR B 64  ? 0.1537 0.1102 0.0956 -0.0215 0.0075  0.0016  155 THR B CA  
2016 C C   . THR B 64  ? 0.1869 0.1515 0.1404 -0.0214 0.0116  0.0013  155 THR B C   
2017 O O   . THR B 64  ? 0.1308 0.0952 0.0873 -0.0190 0.0188  0.0026  155 THR B O   
2018 C CB  . THR B 64  ? 0.1395 0.1028 0.0892 -0.0195 0.0059  0.0028  155 THR B CB  
2019 O OG1 . THR B 64  ? 0.1575 0.1111 0.0939 -0.0182 0.0020  0.0032  155 THR B OG1 
2020 C CG2 . THR B 64  ? 0.1216 0.1003 0.0861 -0.0194 0.0006  0.0020  155 THR B CG2 
2021 N N   . ARG B 65  ? 0.1658 0.1317 0.0876 -0.0439 -0.0327 0.0059  156 ARG B N   
2022 C CA  . ARG B 65  ? 0.1521 0.1300 0.0895 -0.0423 -0.0296 0.0062  156 ARG B CA  
2023 C C   . ARG B 65  ? 0.1967 0.1810 0.1465 -0.0457 -0.0390 0.0030  156 ARG B C   
2024 O O   . ARG B 65  ? 0.1358 0.1151 0.0833 -0.0468 -0.0458 0.0001  156 ARG B O   
2025 C CB  . ARG B 65  ? 0.1593 0.1294 0.0873 -0.0372 -0.0249 0.0020  156 ARG B CB  
2026 C CG  . ARG B 65  ? 0.1810 0.1397 0.0911 -0.0317 -0.0139 0.0048  156 ARG B CG  
2027 C CD  . ARG B 65  ? 0.1865 0.1410 0.0923 -0.0256 -0.0069 0.0028  156 ARG B CD  
2028 N NE  . ARG B 65  ? 0.2036 0.1439 0.0974 -0.0265 -0.0154 -0.0052 156 ARG B NE  
2029 C CZ  . ARG B 65  ? 0.2391 0.1724 0.1272 -0.0226 -0.0128 -0.0082 156 ARG B CZ  
2030 N NH1 . ARG B 65  ? 0.1988 0.1382 0.0919 -0.0165 -0.0010 -0.0042 156 ARG B NH1 
2031 N NH2 . ARG B 65  ? 0.2058 0.1261 0.0845 -0.0250 -0.0224 -0.0142 156 ARG B NH2 
2032 N N   . VAL B 66  ? 0.1248 0.1195 0.0884 -0.0453 -0.0375 0.0044  157 VAL B N   
2033 C CA  A VAL B 66  ? 0.1208 0.1187 0.0934 -0.0456 -0.0431 0.0018  157 VAL B CA  
2034 C CA  B VAL B 66  ? 0.1161 0.1143 0.0889 -0.0458 -0.0431 0.0020  157 VAL B CA  
2035 C C   . VAL B 66  ? 0.1072 0.1085 0.0847 -0.0431 -0.0409 -0.0011 157 VAL B C   
2036 O O   . VAL B 66  ? 0.1274 0.1347 0.1101 -0.0423 -0.0359 0.0020  157 VAL B O   
2037 C CB  A VAL B 66  ? 0.1181 0.1211 0.0997 -0.0476 -0.0449 0.0073  157 VAL B CB  
2038 C CB  B VAL B 66  ? 0.1152 0.1190 0.0974 -0.0480 -0.0448 0.0077  157 VAL B CB  
2039 C CG1 A VAL B 66  ? 0.1106 0.1240 0.1012 -0.0513 -0.0421 0.0152  157 VAL B CG1 
2040 C CG1 B VAL B 66  ? 0.1047 0.1061 0.0908 -0.0425 -0.0446 0.0045  157 VAL B CG1 
2041 C CG2 A VAL B 66  ? 0.1103 0.1123 0.0969 -0.0425 -0.0444 0.0044  157 VAL B CG2 
2042 C CG2 B VAL B 66  ? 0.1179 0.1178 0.0955 -0.0512 -0.0477 0.0114  157 VAL B CG2 
2043 N N   . ARG B 67  ? 0.1027 0.1012 0.0823 -0.0377 -0.0401 -0.0057 158 ARG B N   
2044 C CA  . ARG B 67  ? 0.1035 0.1040 0.0869 -0.0356 -0.0384 -0.0083 158 ARG B CA  
2045 C C   . ARG B 67  ? 0.1533 0.1572 0.1442 -0.0325 -0.0377 -0.0089 158 ARG B C   
2046 O O   . ARG B 67  ? 0.0953 0.0974 0.0860 -0.0309 -0.0386 -0.0091 158 ARG B O   
2047 C CB  . ARG B 67  ? 0.1026 0.0973 0.0816 -0.0339 -0.0390 -0.0116 158 ARG B CB  
2048 C CG  . ARG B 67  ? 0.0986 0.0946 0.0820 -0.0325 -0.0381 -0.0137 158 ARG B CG  
2049 C CD  . ARG B 67  ? 0.1218 0.1114 0.1018 -0.0322 -0.0404 -0.0151 158 ARG B CD  
2050 N NE  . ARG B 67  ? 0.1527 0.1308 0.1174 -0.0338 -0.0422 -0.0155 158 ARG B NE  
2051 C CZ  . ARG B 67  ? 0.1335 0.1008 0.0839 -0.0347 -0.0418 -0.0171 158 ARG B CZ  
2052 N NH1 . ARG B 67  ? 0.1315 0.0995 0.0835 -0.0347 -0.0403 -0.0183 158 ARG B NH1 
2053 N NH2 . ARG B 67  ? 0.1589 0.1113 0.0894 -0.0351 -0.0424 -0.0178 158 ARG B NH2 
2054 N N   . ALA B 68  ? 0.0926 0.0997 0.0876 -0.0323 -0.0365 -0.0090 159 ALA B N   
2055 C CA  . ALA B 68  ? 0.0829 0.0904 0.0805 -0.0302 -0.0362 -0.0096 159 ALA B CA  
2056 C C   . ALA B 68  ? 0.1072 0.1158 0.1075 -0.0291 -0.0349 -0.0118 159 ALA B C   
2057 O O   . ALA B 68  ? 0.1012 0.1107 0.1022 -0.0302 -0.0342 -0.0123 159 ALA B O   
2058 C CB  . ALA B 68  ? 0.1077 0.1165 0.1070 -0.0316 -0.0373 -0.0064 159 ALA B CB  
2059 N N   . MET B 69  ? 0.1349 0.1426 0.1362 -0.0278 -0.0354 -0.0125 160 MET B N   
2060 C CA  . MET B 69  ? 0.1260 0.1353 0.1318 -0.0280 -0.0351 -0.0132 160 MET B CA  
2061 C C   . MET B 69  ? 0.1099 0.1168 0.1148 -0.0276 -0.0368 -0.0124 160 MET B C   
2062 O O   . MET B 69  ? 0.1306 0.1326 0.1302 -0.0267 -0.0391 -0.0122 160 MET B O   
2063 C CB  . MET B 69  ? 0.1101 0.1199 0.1193 -0.0285 -0.0363 -0.0133 160 MET B CB  
2064 C CG  . MET B 69  ? 0.2181 0.2302 0.2354 -0.0296 -0.0372 -0.0120 160 MET B CG  
2065 S SD  . MET B 69  ? 0.1870 0.1989 0.2098 -0.0306 -0.0410 -0.0100 160 MET B SD  
2066 C CE  . MET B 69  ? 0.2152 0.2196 0.2264 -0.0314 -0.0412 -0.0126 160 MET B CE  
2067 N N   . ALA B 70  ? 0.0792 0.0870 0.0870 -0.0277 -0.0356 -0.0118 161 ALA B N   
2068 C CA  . ALA B 70  ? 0.1119 0.1156 0.1163 -0.0232 -0.0318 -0.0104 161 ALA B CA  
2069 C C   . ALA B 70  ? 0.0831 0.0923 0.0990 -0.0208 -0.0276 -0.0076 161 ALA B C   
2070 O O   . ALA B 70  ? 0.1131 0.1280 0.1384 -0.0237 -0.0283 -0.0069 161 ALA B O   
2071 C CB  . ALA B 70  ? 0.1215 0.1214 0.1200 -0.0229 -0.0305 -0.0103 161 ALA B CB  
2072 N N   . ILE B 71  ? 0.1494 0.1559 0.1641 -0.0152 -0.0232 -0.0052 162 ILE B N   
2073 C CA  . ILE B 71  ? 0.0899 0.1031 0.1182 -0.0117 -0.0172 -0.0000 162 ILE B CA  
2074 C C   . ILE B 71  ? 0.1025 0.1071 0.1199 -0.0039 -0.0087 0.0020  162 ILE B C   
2075 O O   . ILE B 71  ? 0.1134 0.1047 0.1116 -0.0011 -0.0093 -0.0009 162 ILE B O   
2076 C CB  . ILE B 71  ? 0.1189 0.1390 0.1607 -0.0109 -0.0188 0.0033  162 ILE B CB  
2077 C CG1 . ILE B 71  ? 0.1304 0.1420 0.1608 -0.0054 -0.0176 0.0024  162 ILE B CG1 
2078 C CG2 . ILE B 71  ? 0.1493 0.1736 0.1975 -0.0185 -0.0279 0.0014  162 ILE B CG2 
2079 C CD1 . ILE B 71  ? 0.1420 0.1609 0.1881 -0.0019 -0.0166 0.0078  162 ILE B CD1 
2080 N N   . TYR B 72  ? 0.1284 0.1391 0.1570 -0.0004 -0.0009 0.0077  163 TYR B N   
2081 C CA  . TYR B 72  ? 0.1195 0.1209 0.1368 0.0089  0.0098  0.0110  163 TYR B CA  
2082 C C   . TYR B 72  ? 0.1392 0.1376 0.1558 0.0169  0.0146  0.0138  163 TYR B C   
2083 O O   . TYR B 72  ? 0.1459 0.1572 0.1829 0.0158  0.0130  0.0175  163 TYR B O   
2084 C CB  . TYR B 72  ? 0.1190 0.1288 0.1501 0.0107  0.0182  0.0178  163 TYR B CB  
2085 C CG  . TYR B 72  ? 0.1157 0.1227 0.1406 0.0052  0.0148  0.0147  163 TYR B CG  
2086 C CD1 . TYR B 72  ? 0.1286 0.1189 0.1285 0.0077  0.0154  0.0109  163 TYR B CD1 
2087 C CD2 . TYR B 72  ? 0.1023 0.1209 0.1445 -0.0025 0.0097  0.0157  163 TYR B CD2 
2088 C CE1 . TYR B 72  ? 0.1258 0.1141 0.1215 0.0029  0.0117  0.0087  163 TYR B CE1 
2089 C CE2 . TYR B 72  ? 0.1006 0.1157 0.1366 -0.0065 0.0069  0.0129  163 TYR B CE2 
2090 C CZ  . TYR B 72  ? 0.1992 0.2005 0.2135 -0.0037 0.0082  0.0097  163 TYR B CZ  
2091 O OH  . TYR B 72  ? 0.1797 0.1782 0.1895 -0.0074 0.0050  0.0077  163 TYR B OH  
2092 N N   . LYS B 73  ? 0.1495 0.1287 0.1408 0.0251  0.0200  0.0123  164 LYS B N   
2093 C CA  . LYS B 73  ? 0.1645 0.1355 0.1488 0.0340  0.0247  0.0139  164 LYS B CA  
2094 C C   . LYS B 73  ? 0.2344 0.2144 0.2351 0.0443  0.0394  0.0238  164 LYS B C   
2095 O O   . LYS B 73  ? 0.1689 0.1560 0.1833 0.0491  0.0420  0.0283  164 LYS B O   
2096 C CB  . LYS B 73  ? 0.2137 0.1559 0.1605 0.0392  0.0241  0.0087  164 LYS B CB  
2097 C CG  . LYS B 73  ? 0.2771 0.2046 0.2099 0.0499  0.0293  0.0098  164 LYS B CG  
2098 C CD  . LYS B 73  ? 0.4031 0.2964 0.2937 0.0551  0.0280  0.0050  164 LYS B CD  
2099 C CE  . LYS B 73  ? 0.5108 0.3852 0.3832 0.0670  0.0336  0.0058  164 LYS B CE  
2100 N NZ  . LYS B 73  ? 0.6027 0.4385 0.4294 0.0740  0.0341  0.0022  164 LYS B NZ  
2101 N N   . GLN B 74  ? 0.1755 0.1557 0.1762 0.0481  0.0494  0.0285  165 GLN B N   
2102 C CA  . GLN B 74  ? 0.2209 0.2099 0.2378 0.0589  0.0656  0.0398  165 GLN B CA  
2103 C C   . GLN B 74  ? 0.2815 0.3004 0.3419 0.0526  0.0629  0.0483  165 GLN B C   
2104 O O   . GLN B 74  ? 0.1419 0.1726 0.2170 0.0404  0.0524  0.0466  165 GLN B O   
2105 C CB  . GLN B 74  ? 0.2471 0.2274 0.2510 0.0637  0.0768  0.0430  165 GLN B CB  
2106 C CG  . GLN B 74  ? 0.3082 0.2547 0.2662 0.0715  0.0799  0.0364  165 GLN B CG  
2107 C CD  . GLN B 74  ? 0.3460 0.2822 0.2883 0.0725  0.0858  0.0373  165 GLN B CD  
2108 O OE1 . GLN B 74  ? 0.3104 0.2539 0.2592 0.0613  0.0763  0.0340  165 GLN B OE1 
2109 N NE2 . GLN B 74  ? 0.5143 0.4319 0.4343 0.0869  0.1025  0.0423  165 GLN B NE2 
2110 N N   . SER B 75  ? 0.2656 0.2948 0.3458 0.0616  0.0723  0.0583  166 SER B N   
2111 C CA  . SER B 75  ? 0.1991 0.2554 0.3218 0.0555  0.0674  0.0679  166 SER B CA  
2112 C C   . SER B 75  ? 0.1918 0.2641 0.3377 0.0470  0.0663  0.0744  166 SER B C   
2113 O O   . SER B 75  ? 0.1182 0.2041 0.2858 0.0344  0.0523  0.0751  166 SER B O   
2114 C CB  . SER B 75  ? 0.2115 0.2761 0.3525 0.0692  0.0811  0.0803  166 SER B CB  
2115 O OG  . SER B 75  ? 0.2980 0.3887 0.4820 0.0642  0.0794  0.0937  166 SER B OG  
2116 N N   . GLN B 76  ? 0.1862 0.2542 0.3248 0.0536  0.0802  0.0790  167 GLN B N   
2117 C CA  . GLN B 76  ? 0.1974 0.2803 0.3590 0.0460  0.0799  0.0866  167 GLN B CA  
2118 C C   . GLN B 76  ? 0.1437 0.2201 0.2921 0.0326  0.0651  0.0755  167 GLN B C   
2119 O O   . GLN B 76  ? 0.1175 0.2045 0.2840 0.0245  0.0616  0.0806  167 GLN B O   
2120 C CB  . GLN B 76  ? 0.2551 0.3327 0.4093 0.0570  0.0993  0.0949  167 GLN B CB  
2121 C CG  . GLN B 76  ? 0.3301 0.3807 0.4398 0.0624  0.1046  0.0841  167 GLN B CG  
2122 C CD  . GLN B 76  ? 0.4018 0.4313 0.4820 0.0783  0.1168  0.0821  167 GLN B CD  
2123 O OE1 . GLN B 76  ? 0.3692 0.3996 0.4530 0.0819  0.1144  0.0812  167 GLN B OE1 
2124 N NE2 . GLN B 76  ? 0.4743 0.4818 0.5226 0.0882  0.1299  0.0816  167 GLN B NE2 
2125 N N   . HIS B 77  ? 0.1259 0.1850 0.2443 0.0303  0.0568  0.0615  168 HIS B N   
2126 C CA  . HIS B 77  ? 0.1163 0.1698 0.2233 0.0192  0.0441  0.0518  168 HIS B CA  
2127 C C   . HIS B 77  ? 0.1035 0.1586 0.2122 0.0101  0.0282  0.0443  168 HIS B C   
2128 O O   . HIS B 77  ? 0.0977 0.1486 0.1982 0.0018  0.0185  0.0370  168 HIS B O   
2129 C CB  . HIS B 77  ? 0.1494 0.1812 0.2204 0.0233  0.0474  0.0433  168 HIS B CB  
2130 C CG  . HIS B 77  ? 0.1455 0.1714 0.2088 0.0314  0.0621  0.0497  168 HIS B CG  
2131 N ND1 . HIS B 77  ? 0.1738 0.2090 0.2520 0.0271  0.0645  0.0558  168 HIS B ND1 
2132 C CD2 . HIS B 77  ? 0.2013 0.2106 0.2413 0.0440  0.0755  0.0513  168 HIS B CD2 
2133 C CE1 . HIS B 77  ? 0.2251 0.2513 0.2908 0.0366  0.0793  0.0613  168 HIS B CE1 
2134 N NE2 . HIS B 77  ? 0.1823 0.1918 0.2234 0.0474  0.0865  0.0585  168 HIS B NE2 
2135 N N   . MET B 78  ? 0.1020 0.1624 0.2208 0.0122  0.0260  0.0465  169 MET B N   
2136 C CA  . MET B 78  ? 0.0939 0.1516 0.2077 0.0050  0.0121  0.0386  169 MET B CA  
2137 C C   . MET B 78  ? 0.0930 0.1573 0.2194 -0.0071 -0.0005 0.0379  169 MET B C   
2138 O O   . MET B 78  ? 0.0867 0.1437 0.1999 -0.0131 -0.0103 0.0293  169 MET B O   
2139 C CB  . MET B 78  ? 0.0956 0.1580 0.2198 0.0094  0.0118  0.0425  169 MET B CB  
2140 C CG  . MET B 78  ? 0.2678 0.3160 0.3692 0.0204  0.0204  0.0391  169 MET B CG  
2141 S SD  . MET B 78  ? 0.2183 0.2714 0.3324 0.0268  0.0205  0.0443  169 MET B SD  
2142 C CE  . MET B 78  ? 0.3024 0.3364 0.3848 0.0237  0.0104  0.0309  169 MET B CE  
2143 N N   . THR B 79  ? 0.0973 0.1736 0.2479 -0.0106 -0.0005 0.0473  170 THR B N   
2144 C CA  . THR B 79  ? 0.0760 0.1538 0.2351 -0.0222 -0.0143 0.0468  170 THR B CA  
2145 C C   . THR B 79  ? 0.0753 0.1441 0.2188 -0.0264 -0.0157 0.0404  170 THR B C   
2146 O O   . THR B 79  ? 0.1045 0.1686 0.2468 -0.0343 -0.0263 0.0382  170 THR B O   
2147 C CB  . THR B 79  ? 0.0799 0.1668 0.2627 -0.0247 -0.0165 0.0584  170 THR B CB  
2148 O OG1 . THR B 79  ? 0.0821 0.1759 0.2751 -0.0206 -0.0048 0.0663  170 THR B OG1 
2149 C CG2 . THR B 79  ? 0.1036 0.1975 0.3007 -0.0207 -0.0164 0.0650  170 THR B CG2 
2150 N N   . GLU B 80  ? 0.0963 0.1591 0.2241 -0.0203 -0.0056 0.0373  171 GLU B N   
2151 C CA  . GLU B 80  ? 0.1077 0.1624 0.2219 -0.0236 -0.0070 0.0318  171 GLU B CA  
2152 C C   . GLU B 80  ? 0.1023 0.1462 0.1946 -0.0251 -0.0130 0.0207  171 GLU B C   
2153 O O   . GLU B 80  ? 0.1213 0.1606 0.2009 -0.0203 -0.0102 0.0168  171 GLU B O   
2154 C CB  . GLU B 80  ? 0.1544 0.2062 0.2608 -0.0169 0.0052  0.0343  171 GLU B CB  
2155 C CG  . GLU B 80  ? 0.1929 0.2377 0.2891 -0.0206 0.0033  0.0306  171 GLU B CG  
2156 C CD  . GLU B 80  ? 0.3185 0.3580 0.4044 -0.0141 0.0147  0.0332  171 GLU B CD  
2157 O OE1 . GLU B 80  ? 0.2785 0.3075 0.3461 -0.0141 0.0135  0.0273  171 GLU B OE1 
2158 O OE2 . GLU B 80  ? 0.3247 0.3701 0.4209 -0.0085 0.0250  0.0420  171 GLU B OE2 
2159 N N   . VAL B 81  ? 0.0761 0.1150 0.1638 -0.0314 -0.0209 0.0165  172 VAL B N   
2160 C CA  . VAL B 81  ? 0.0899 0.1203 0.1599 -0.0322 -0.0250 0.0079  172 VAL B CA  
2161 C C   . VAL B 81  ? 0.1217 0.1472 0.1774 -0.0276 -0.0189 0.0047  172 VAL B C   
2162 O O   . VAL B 81  ? 0.1060 0.1301 0.1609 -0.0267 -0.0150 0.0065  172 VAL B O   
2163 C CB  . VAL B 81  ? 0.0964 0.1202 0.1627 -0.0379 -0.0327 0.0051  172 VAL B CB  
2164 C CG1 . VAL B 81  ? 0.0888 0.1050 0.1378 -0.0369 -0.0338 -0.0022 172 VAL B CG1 
2165 C CG2 . VAL B 81  ? 0.1458 0.1687 0.2178 -0.0411 -0.0393 0.0076  172 VAL B CG2 
2166 N N   . VAL B 82  ? 0.0765 0.0982 0.1209 -0.0255 -0.0194 0.0005  173 VAL B N   
2167 C CA  . VAL B 82  ? 0.1042 0.1194 0.1347 -0.0227 -0.0171 -0.0021 173 VAL B CA  
2168 C C   . VAL B 82  ? 0.1064 0.1195 0.1329 -0.0257 -0.0207 -0.0052 173 VAL B C   
2169 O O   . VAL B 82  ? 0.0783 0.0917 0.1042 -0.0282 -0.0248 -0.0078 173 VAL B O   
2170 C CB  . VAL B 82  ? 0.1175 0.1282 0.1380 -0.0203 -0.0181 -0.0041 173 VAL B CB  
2171 C CG1 . VAL B 82  ? 0.1539 0.1560 0.1600 -0.0193 -0.0189 -0.0058 173 VAL B CG1 
2172 C CG2 . VAL B 82  ? 0.0942 0.1048 0.1165 -0.0152 -0.0129 -0.0008 173 VAL B CG2 
2173 N N   . ARG B 83  ? 0.1052 0.1152 0.1279 -0.0248 -0.0186 -0.0045 174 ARG B N   
2174 C CA  . ARG B 83  ? 0.1282 0.1366 0.1489 -0.0263 -0.0210 -0.0064 174 ARG B CA  
2175 C C   . ARG B 83  ? 0.1402 0.1441 0.1538 -0.0244 -0.0201 -0.0054 174 ARG B C   
2176 O O   . ARG B 83  ? 0.0902 0.0896 0.0979 -0.0221 -0.0173 -0.0036 174 ARG B O   
2177 C CB  . ARG B 83  ? 0.1106 0.1188 0.1373 -0.0286 -0.0217 -0.0058 174 ARG B CB  
2178 C CG  . ARG B 83  ? 0.0935 0.1023 0.1256 -0.0285 -0.0183 -0.0017 174 ARG B CG  
2179 C CD  . ARG B 83  ? 0.1602 0.1659 0.1958 -0.0313 -0.0204 -0.0008 174 ARG B CD  
2180 N NE  . ARG B 83  ? 0.1648 0.1694 0.2053 -0.0353 -0.0258 -0.0010 174 ARG B NE  
2181 C CZ  . ARG B 83  ? 0.1752 0.1726 0.2080 -0.0363 -0.0301 -0.0050 174 ARG B CZ  
2182 N NH1 . ARG B 83  ? 0.2002 0.1928 0.2338 -0.0403 -0.0364 -0.0049 174 ARG B NH1 
2183 N NH2 . ARG B 83  ? 0.1369 0.1308 0.1606 -0.0330 -0.0281 -0.0082 174 ARG B NH2 
2184 N N   . ARG B 84  ? 0.1303 0.1340 0.1435 -0.0248 -0.0223 -0.0060 175 ARG B N   
2185 C CA  . ARG B 84  ? 0.1114 0.1108 0.1196 -0.0238 -0.0233 -0.0041 175 ARG B CA  
2186 C C   . ARG B 84  ? 0.1136 0.1094 0.1213 -0.0231 -0.0201 -0.0025 175 ARG B C   
2187 O O   . ARG B 84  ? 0.1258 0.1236 0.1397 -0.0241 -0.0183 -0.0026 175 ARG B O   
2188 C CB  . ARG B 84  ? 0.1148 0.1172 0.1272 -0.0239 -0.0259 -0.0033 175 ARG B CB  
2189 C CG  . ARG B 84  ? 0.1513 0.1578 0.1654 -0.0250 -0.0289 -0.0029 175 ARG B CG  
2190 C CD  . ARG B 84  ? 0.1546 0.1666 0.1767 -0.0241 -0.0295 0.0001  175 ARG B CD  
2191 N NE  . ARG B 84  ? 0.1657 0.1766 0.1889 -0.0250 -0.0348 0.0046  175 ARG B NE  
2192 C CZ  . ARG B 84  ? 0.0856 0.1022 0.1189 -0.0238 -0.0358 0.0094  175 ARG B CZ  
2193 N NH1 . ARG B 84  ? 0.0881 0.1105 0.1288 -0.0203 -0.0297 0.0098  175 ARG B NH1 
2194 N NH2 . ARG B 84  ? 0.1008 0.1157 0.1359 -0.0258 -0.0430 0.0144  175 ARG B NH2 
2195 N N   . CYS B 85  ? 0.1364 0.1250 0.1353 -0.0217 -0.0205 -0.0006 176 CYS B N   
2196 C CA  . CYS B 85  ? 0.1908 0.1745 0.1868 -0.0207 -0.0168 0.0017  176 CYS B CA  
2197 C C   . CYS B 85  ? 0.1835 0.1682 0.1852 -0.0216 -0.0184 0.0021  176 CYS B C   
2198 O O   . CYS B 85  ? 0.1419 0.1303 0.1484 -0.0218 -0.0214 0.0009  176 CYS B O   
2199 C CB  . CYS B 85  ? 0.1217 0.0934 0.1016 -0.0185 -0.0172 0.0034  176 CYS B CB  
2200 S SG  . CYS B 85  ? 0.1322 0.0982 0.1071 -0.0199 -0.0263 0.0045  176 CYS B SG  
2201 N N   . PRO B 86  ? 0.1203 0.1012 0.1214 -0.0216 -0.0154 0.0044  177 PRO B N   
2202 C CA  . PRO B 86  ? 0.1367 0.1162 0.1417 -0.0221 -0.0171 0.0046  177 PRO B CA  
2203 C C   . PRO B 86  ? 0.1818 0.1587 0.1839 -0.0205 -0.0213 0.0052  177 PRO B C   
2204 O O   . PRO B 86  ? 0.1671 0.1441 0.1737 -0.0194 -0.0224 0.0052  177 PRO B O   
2205 C CB  . PRO B 86  ? 0.1187 0.0937 0.1224 -0.0228 -0.0133 0.0081  177 PRO B CB  
2206 C CG  . PRO B 86  ? 0.1688 0.1477 0.1750 -0.0230 -0.0084 0.0099  177 PRO B CG  
2207 C CD  . PRO B 86  ? 0.1236 0.1019 0.1222 -0.0208 -0.0094 0.0076  177 PRO B CD  
2208 N N   . HIS B 87  ? 0.1245 0.0975 0.1187 -0.0200 -0.0243 0.0066  178 HIS B N   
2209 C CA  . HIS B 87  ? 0.1815 0.1530 0.1761 -0.0196 -0.0306 0.0089  178 HIS B CA  
2210 C C   . HIS B 87  ? 0.1736 0.1548 0.1784 -0.0197 -0.0333 0.0088  178 HIS B C   
2211 O O   . HIS B 87  ? 0.1458 0.1325 0.1606 -0.0180 -0.0343 0.0109  178 HIS B O   
2212 C CB  . HIS B 87  ? 0.2050 0.1645 0.1843 -0.0201 -0.0353 0.0112  178 HIS B CB  
2213 C CG  . HIS B 87  ? 0.1893 0.1481 0.1710 -0.0214 -0.0449 0.0148  178 HIS B CG  
2214 N ND1 . HIS B 87  ? 0.1944 0.1560 0.1854 -0.0206 -0.0482 0.0183  178 HIS B ND1 
2215 C CD2 . HIS B 87  ? 0.2160 0.1724 0.1945 -0.0237 -0.0526 0.0164  178 HIS B CD2 
2216 C CE1 . HIS B 87  ? 0.2063 0.1691 0.2021 -0.0224 -0.0576 0.0229  178 HIS B CE1 
2217 N NE2 . HIS B 87  ? 0.2089 0.1681 0.1969 -0.0250 -0.0611 0.0219  178 HIS B NE2 
2218 N N   . HIS B 88  ? 0.1111 0.0945 0.1138 -0.0211 -0.0337 0.0071  179 HIS B N   
2219 C CA  . HIS B 88  ? 0.1049 0.0968 0.1169 -0.0218 -0.0368 0.0085  179 HIS B CA  
2220 C C   . HIS B 88  ? 0.1181 0.1184 0.1400 -0.0197 -0.0313 0.0066  179 HIS B C   
2221 O O   . HIS B 88  ? 0.1254 0.1333 0.1572 -0.0184 -0.0316 0.0096  179 HIS B O   
2222 C CB  . HIS B 88  ? 0.1064 0.0959 0.1115 -0.0241 -0.0398 0.0075  179 HIS B CB  
2223 C CG  . HIS B 88  ? 0.1868 0.1653 0.1809 -0.0262 -0.0484 0.0106  179 HIS B CG  
2224 N ND1 . HIS B 88  ? 0.1725 0.1363 0.1473 -0.0258 -0.0488 0.0088  179 HIS B ND1 
2225 C CD2 . HIS B 88  ? 0.1951 0.1731 0.1936 -0.0285 -0.0576 0.0161  179 HIS B CD2 
2226 C CE1 . HIS B 88  ? 0.2117 0.1630 0.1752 -0.0280 -0.0586 0.0121  179 HIS B CE1 
2227 N NE2 . HIS B 88  ? 0.1570 0.1176 0.1363 -0.0304 -0.0652 0.0169  179 HIS B NE2 
2228 N N   . GLU B 89  ? 0.1017 0.0997 0.1207 -0.0193 -0.0265 0.0028  180 GLU B N   
2229 C CA  . GLU B 89  ? 0.1540 0.1543 0.1768 -0.0173 -0.0227 0.0008  180 GLU B CA  
2230 C C   . GLU B 89  ? 0.1784 0.1773 0.2048 -0.0132 -0.0210 0.0030  180 GLU B C   
2231 O O   . GLU B 89  ? 0.2124 0.2105 0.2391 -0.0097 -0.0171 0.0019  180 GLU B O   
2232 C CB  . GLU B 89  ? 0.0942 0.0898 0.1127 -0.0191 -0.0208 -0.0029 180 GLU B CB  
2233 C CG  . GLU B 89  ? 0.1291 0.1177 0.1452 -0.0195 -0.0203 -0.0025 180 GLU B CG  
2234 C CD  . GLU B 89  ? 0.2272 0.2113 0.2423 -0.0223 -0.0204 -0.0043 180 GLU B CD  
2235 O OE1 . GLU B 89  ? 0.2176 0.2041 0.2334 -0.0241 -0.0212 -0.0061 180 GLU B OE1 
2236 O OE2 . GLU B 89  ? 0.2502 0.2275 0.2640 -0.0232 -0.0210 -0.0035 180 GLU B OE2 
2237 N N   . ARG B 90  ? 0.1354 0.1322 0.1628 -0.0128 -0.0236 0.0061  181 ARG B N   
2238 C CA  . ARG B 90  ? 0.1491 0.1444 0.1808 -0.0081 -0.0220 0.0088  181 ARG B CA  
2239 C C   . ARG B 90  ? 0.1263 0.1291 0.1692 -0.0067 -0.0257 0.0157  181 ARG B C   
2240 O O   . ARG B 90  ? 0.1570 0.1587 0.2046 -0.0031 -0.0258 0.0193  181 ARG B O   
2241 C CB  . ARG B 90  ? 0.1397 0.1251 0.1645 -0.0088 -0.0227 0.0079  181 ARG B CB  
2242 C CG  . ARG B 90  ? 0.1564 0.1345 0.1738 -0.0108 -0.0205 0.0034  181 ARG B CG  
2243 C CD  . ARG B 90  ? 0.1414 0.1103 0.1542 -0.0119 -0.0214 0.0043  181 ARG B CD  
2244 N NE  . ARG B 90  ? 0.1323 0.0954 0.1452 -0.0071 -0.0209 0.0058  181 ARG B NE  
2245 C CZ  . ARG B 90  ? 0.1362 0.0977 0.1506 -0.0057 -0.0231 0.0096  181 ARG B CZ  
2246 N NH1 . ARG B 90  ? 0.1344 0.0976 0.1475 -0.0090 -0.0264 0.0119  181 ARG B NH1 
2247 N NH2 . ARG B 90  ? 0.1446 0.1005 0.1597 -0.0005 -0.0223 0.0112  181 ARG B NH2 
2248 N N   A CYS B 91  ? 0.3172 0.1739 0.2683 0.0665  -0.0184 0.0572  182 CYS B N   
2249 N N   B CYS B 91  ? 0.2870 0.1419 0.2337 0.0652  -0.0190 0.0589  182 CYS B N   
2250 C CA  A CYS B 91  ? 0.3417 0.2226 0.3017 0.0809  -0.0313 0.0616  182 CYS B CA  
2251 C CA  B CYS B 91  ? 0.3436 0.2230 0.3038 0.0817  -0.0309 0.0616  182 CYS B CA  
2252 C C   A CYS B 91  ? 0.3445 0.2431 0.3299 0.0976  -0.0344 0.0586  182 CYS B C   
2253 C C   B CYS B 91  ? 0.3297 0.2319 0.3191 0.0851  -0.0282 0.0514  182 CYS B C   
2254 O O   A CYS B 91  ? 0.3339 0.2580 0.3320 0.1090  -0.0464 0.0618  182 CYS B O   
2255 O O   B CYS B 91  ? 0.3729 0.3002 0.3776 0.0744  -0.0275 0.0429  182 CYS B O   
2256 C CB  A CYS B 91  ? 0.2809 0.1943 0.2496 0.0699  -0.0373 0.0561  182 CYS B CB  
2257 C CB  B CYS B 91  ? 0.3217 0.2252 0.2792 0.0769  -0.0411 0.0629  182 CYS B CB  
2258 S SG  A CYS B 91  ? 0.2889 0.1939 0.2276 0.0654  -0.0430 0.0648  182 CYS B SG  
2259 S SG  B CYS B 91  ? 0.2410 0.1749 0.2159 0.0590  -0.0389 0.0501  182 CYS B SG  
2260 N N   . SER B 92  ? 0.4940 0.3815 0.4875 0.0996  -0.0240 0.0523  183 SER B N   
2261 C CA  . SER B 92  ? 0.6088 0.5203 0.6304 0.1112  -0.0227 0.0461  183 SER B CA  
2262 C C   . SER B 92  ? 0.5117 0.4698 0.5594 0.1073  -0.0306 0.0416  183 SER B C   
2263 O O   . SER B 92  ? 0.5167 0.5012 0.5854 0.1210  -0.0390 0.0439  183 SER B O   
2264 C CB  . SER B 92  ? 0.6965 0.6026 0.7238 0.1284  -0.0257 0.0514  183 SER B CB  
2265 O OG  . SER B 92  ? 0.7441 0.6082 0.7457 0.1274  -0.0205 0.0563  183 SER B OG  
2266 N N   . ASP B 93  ? 0.4246 0.3930 0.4722 0.0884  -0.0283 0.0350  184 ASP B N   
2267 C CA  . ASP B 93  ? 0.3053 0.3110 0.3755 0.0816  -0.0329 0.0292  184 ASP B CA  
2268 C C   . ASP B 93  ? 0.2645 0.2753 0.3446 0.0719  -0.0215 0.0199  184 ASP B C   
2269 O O   . ASP B 93  ? 0.2704 0.3005 0.3599 0.0602  -0.0224 0.0151  184 ASP B O   
2270 C CB  . ASP B 93  ? 0.2296 0.2419 0.2886 0.0695  -0.0414 0.0301  184 ASP B CB  
2271 C CG  . ASP B 93  ? 0.2630 0.2541 0.3022 0.0545  -0.0338 0.0279  184 ASP B CG  
2272 O OD1 . ASP B 93  ? 0.2859 0.2582 0.3198 0.0513  -0.0239 0.0255  184 ASP B OD1 
2273 O OD2 . ASP B 93  ? 0.2386 0.2334 0.2681 0.0457  -0.0381 0.0280  184 ASP B OD2 
2274 N N   . SER B 94  ? 0.2929 0.2830 0.3674 0.0766  -0.0107 0.0175  185 SER B N   
2275 C CA  . SER B 94  ? 0.3225 0.3126 0.3994 0.0683  0.0001  0.0093  185 SER B CA  
2276 C C   . SER B 94  ? 0.3623 0.3859 0.4668 0.0707  0.0028  0.0055  185 SER B C   
2277 O O   . SER B 94  ? 0.3534 0.3974 0.4790 0.0838  -0.0003 0.0078  185 SER B O   
2278 C CB  . SER B 94  ? 0.4206 0.3797 0.4830 0.0745  0.0105  0.0065  185 SER B CB  
2279 O OG  . SER B 94  ? 0.4107 0.3780 0.4825 0.0767  0.0213  -0.0007 185 SER B OG  
2280 N N   . ASP B 95  ? 0.3450 0.3746 0.4499 0.0577  0.0087  0.0000  186 ASP B N   
2281 C CA  . ASP B 95  ? 0.2858 0.3422 0.4133 0.0564  0.0152  -0.0037 186 ASP B CA  
2282 C C   . ASP B 95  ? 0.3360 0.3813 0.4587 0.0608  0.0309  -0.0088 186 ASP B C   
2283 O O   . ASP B 95  ? 0.3758 0.4386 0.5117 0.0572  0.0402  -0.0121 186 ASP B O   
2284 C CB  . ASP B 95  ? 0.2855 0.3517 0.4129 0.0396  0.0125  -0.0053 186 ASP B CB  
2285 C CG  . ASP B 95  ? 0.2542 0.2962 0.3568 0.0295  0.0172  -0.0077 186 ASP B CG  
2286 O OD1 . ASP B 95  ? 0.2659 0.3128 0.3675 0.0181  0.0168  -0.0087 186 ASP B OD1 
2287 O OD2 . ASP B 95  ? 0.2352 0.2528 0.3193 0.0327  0.0206  -0.0087 186 ASP B OD2 
2288 N N   . GLY B 96  ? 0.2990 0.3133 0.4006 0.0671  0.0349  -0.0099 187 GLY B N   
2289 C CA  . GLY B 96  ? 0.3423 0.3399 0.4323 0.0711  0.0496  -0.0163 187 GLY B CA  
2290 C C   . GLY B 96  ? 0.3733 0.3501 0.4361 0.0564  0.0528  -0.0210 187 GLY B C   
2291 O O   . GLY B 96  ? 0.4111 0.3676 0.4561 0.0586  0.0635  -0.0272 187 GLY B O   
2292 N N   . LEU B 97  ? 0.2890 0.2697 0.3468 0.0425  0.0435  -0.0186 188 LEU B N   
2293 C CA  . LEU B 97  ? 0.2364 0.2025 0.2716 0.0302  0.0446  -0.0221 188 LEU B CA  
2294 C C   . LEU B 97  ? 0.1971 0.1519 0.2208 0.0209  0.0328  -0.0200 188 LEU B C   
2295 O O   . LEU B 97  ? 0.2106 0.1443 0.2137 0.0150  0.0317  -0.0237 188 LEU B O   
2296 C CB  . LEU B 97  ? 0.2723 0.2574 0.3151 0.0227  0.0483  -0.0214 188 LEU B CB  
2297 C CG  . LEU B 97  ? 0.3692 0.3404 0.3876 0.0131  0.0512  -0.0238 188 LEU B CG  
2298 C CD1 . LEU B 97  ? 0.4414 0.3906 0.4372 0.0174  0.0615  -0.0305 188 LEU B CD1 
2299 C CD2 . LEU B 97  ? 0.4442 0.4325 0.4719 0.0073  0.0568  -0.0211 188 LEU B CD2 
2300 N N   . ALA B 98  ? 0.1372 0.1072 0.1745 0.0188  0.0241  -0.0148 189 ALA B N   
2301 C CA  . ALA B 98  ? 0.1470 0.1101 0.1764 0.0105  0.0153  -0.0128 189 ALA B CA  
2302 C C   . ALA B 98  ? 0.2200 0.1609 0.2383 0.0129  0.0146  -0.0123 189 ALA B C   
2303 O O   . ALA B 98  ? 0.1935 0.1312 0.2166 0.0232  0.0156  -0.0093 189 ALA B O   
2304 C CB  . ALA B 98  ? 0.1113 0.0936 0.1550 0.0091  0.0083  -0.0083 189 ALA B CB  
2305 N N   . PRO B 99  ? 0.1683 0.0937 0.1726 0.0034  0.0124  -0.0149 190 PRO B N   
2306 C CA  . PRO B 99  ? 0.1747 0.0790 0.1698 0.0018  0.0117  -0.0135 190 PRO B CA  
2307 C C   . PRO B 99  ? 0.1642 0.0771 0.1673 0.0041  0.0075  -0.0057 190 PRO B C   
2308 O O   . PRO B 99  ? 0.1431 0.0764 0.1558 0.0007  0.0031  -0.0036 190 PRO B O   
2309 C CB  . PRO B 99  ? 0.2062 0.1037 0.1920 -0.0126 0.0082  -0.0178 190 PRO B CB  
2310 C CG  . PRO B 99  ? 0.2547 0.1607 0.2372 -0.0143 0.0082  -0.0227 190 PRO B CG  
2311 C CD  . PRO B 99  ? 0.1551 0.0833 0.1528 -0.0071 0.0093  -0.0184 190 PRO B CD  
2312 N N   . PRO B 100 ? 0.1847 0.0794 0.1811 0.0102  0.0088  -0.0012 191 PRO B N   
2313 C CA  . PRO B 100 ? 0.1812 0.0818 0.1797 0.0133  0.0045  0.0071  191 PRO B CA  
2314 C C   . PRO B 100 ? 0.1747 0.0777 0.1697 0.0002  0.0028  0.0088  191 PRO B C   
2315 O O   . PRO B 100 ? 0.1707 0.0822 0.1657 0.0015  -0.0001 0.0144  191 PRO B O   
2316 C CB  . PRO B 100 ? 0.2126 0.0859 0.1994 0.0235  0.0071  0.0123  191 PRO B CB  
2317 C CG  . PRO B 100 ? 0.2987 0.1462 0.2745 0.0194  0.0136  0.0054  191 PRO B CG  
2318 C CD  . PRO B 100 ? 0.2288 0.0935 0.2123 0.0158  0.0147  -0.0033 191 PRO B CD  
2319 N N   . GLN B 101 ? 0.1941 0.0918 0.1867 -0.0123 0.0046  0.0037  192 GLN B N   
2320 C CA  . GLN B 101 ? 0.1714 0.0772 0.1668 -0.0244 0.0041  0.0046  192 GLN B CA  
2321 C C   . GLN B 101 ? 0.1487 0.0824 0.1573 -0.0257 0.0003  0.0025  192 GLN B C   
2322 O O   . GLN B 101 ? 0.1345 0.0784 0.1474 -0.0314 0.0008  0.0041  192 GLN B O   
2323 C CB  . GLN B 101 ? 0.1819 0.0752 0.1737 -0.0376 0.0058  -0.0006 192 GLN B CB  
2324 C CG  . GLN B 101 ? 0.2161 0.0750 0.1923 -0.0393 0.0108  0.0005  192 GLN B CG  
2325 C CD  . GLN B 101 ? 0.2302 0.0723 0.1979 -0.0334 0.0116  -0.0062 192 GLN B CD  
2326 O OE1 . GLN B 101 ? 0.2427 0.0974 0.2151 -0.0227 0.0104  -0.0080 192 GLN B OE1 
2327 N NE2 . GLN B 101 ? 0.2578 0.0765 0.2148 -0.0401 0.0140  -0.0103 192 GLN B NE2 
2328 N N   . HIS B 102 ? 0.1282 0.0724 0.1424 -0.0204 -0.0021 -0.0009 193 HIS B N   
2329 C CA  . HIS B 102 ? 0.1082 0.0722 0.1323 -0.0225 -0.0053 -0.0030 193 HIS B CA  
2330 C C   . HIS B 102 ? 0.1232 0.0997 0.1521 -0.0183 -0.0068 -0.0000 193 HIS B C   
2331 O O   . HIS B 102 ? 0.1034 0.0818 0.1328 -0.0112 -0.0080 0.0018  193 HIS B O   
2332 C CB  . HIS B 102 ? 0.1082 0.0748 0.1327 -0.0200 -0.0058 -0.0067 193 HIS B CB  
2333 C CG  . HIS B 102 ? 0.1677 0.1258 0.1849 -0.0262 -0.0067 -0.0113 193 HIS B CG  
2334 N ND1 . HIS B 102 ? 0.1185 0.0822 0.1339 -0.0276 -0.0094 -0.0138 193 HIS B ND1 
2335 C CD2 . HIS B 102 ? 0.1853 0.1282 0.1943 -0.0323 -0.0063 -0.0140 193 HIS B CD2 
2336 C CE1 . HIS B 102 ? 0.1261 0.0803 0.1318 -0.0335 -0.0119 -0.0180 193 HIS B CE1 
2337 N NE2 . HIS B 102 ? 0.1499 0.0917 0.1527 -0.0374 -0.0100 -0.0190 193 HIS B NE2 
2338 N N   . LEU B 103 ? 0.0901 0.0764 0.1233 -0.0225 -0.0071 -0.0005 194 LEU B N   
2339 C CA  . LEU B 103 ? 0.0846 0.0799 0.1189 -0.0196 -0.0083 0.0002  194 LEU B CA  
2340 C C   . LEU B 103 ? 0.0864 0.0897 0.1269 -0.0167 -0.0114 -0.0024 194 LEU B C   
2341 O O   . LEU B 103 ? 0.0784 0.0862 0.1191 -0.0136 -0.0140 -0.0021 194 LEU B O   
2342 C CB  . LEU B 103 ? 0.0823 0.0844 0.1198 -0.0237 -0.0057 -0.0010 194 LEU B CB  
2343 C CG  . LEU B 103 ? 0.1247 0.1326 0.1600 -0.0209 -0.0060 -0.0025 194 LEU B CG  
2344 C CD1 . LEU B 103 ? 0.1386 0.1402 0.1599 -0.0190 -0.0057 0.0011  194 LEU B CD1 
2345 C CD2 . LEU B 103 ? 0.0848 0.1003 0.1266 -0.0224 -0.0020 -0.0052 194 LEU B CD2 
2346 N N   . ILE B 104 ? 0.0693 0.0741 0.1140 -0.0185 -0.0115 -0.0047 195 ILE B N   
2347 C CA  . ILE B 104 ? 0.0643 0.0736 0.1132 -0.0178 -0.0124 -0.0062 195 ILE B CA  
2348 C C   . ILE B 104 ? 0.0881 0.0956 0.1374 -0.0161 -0.0104 -0.0062 195 ILE B C   
2349 O O   . ILE B 104 ? 0.0976 0.0980 0.1413 -0.0167 -0.0088 -0.0067 195 ILE B O   
2350 C CB  . ILE B 104 ? 0.0625 0.0720 0.1126 -0.0194 -0.0132 -0.0072 195 ILE B CB  
2351 C CG1 . ILE B 104 ? 0.0944 0.1076 0.1470 -0.0192 -0.0130 -0.0080 195 ILE B CG1 
2352 C CG2 . ILE B 104 ? 0.1008 0.1092 0.1519 -0.0198 -0.0127 -0.0076 195 ILE B CG2 
2353 C CD1 . ILE B 104 ? 0.0987 0.1132 0.1555 -0.0175 -0.0144 -0.0084 195 ILE B CD1 
2354 N N   . ARG B 105 ? 0.0650 0.0802 0.1213 -0.0146 -0.0102 -0.0065 196 ARG B N   
2355 C CA  . ARG B 105 ? 0.0680 0.0853 0.1283 -0.0130 -0.0056 -0.0069 196 ARG B CA  
2356 C C   . ARG B 105 ? 0.0667 0.0889 0.1322 -0.0179 -0.0035 -0.0077 196 ARG B C   
2357 O O   . ARG B 105 ? 0.0817 0.1066 0.1502 -0.0214 -0.0068 -0.0086 196 ARG B O   
2358 C CB  . ARG B 105 ? 0.0827 0.1087 0.1522 -0.0068 -0.0059 -0.0061 196 ARG B CB  
2359 C CG  . ARG B 105 ? 0.1070 0.1231 0.1688 -0.0014 -0.0075 -0.0039 196 ARG B CG  
2360 C CD  . ARG B 105 ? 0.1302 0.1539 0.2014 0.0078  -0.0080 -0.0022 196 ARG B CD  
2361 N NE  . ARG B 105 ? 0.1667 0.1757 0.2275 0.0139  -0.0093 0.0013  196 ARG B NE  
2362 C CZ  . ARG B 105 ? 0.1822 0.1936 0.2476 0.0246  -0.0119 0.0048  196 ARG B CZ  
2363 N NH1 . ARG B 105 ? 0.1607 0.1943 0.2451 0.0299  -0.0144 0.0043  196 ARG B NH1 
2364 N NH2 . ARG B 105 ? 0.1811 0.1731 0.2331 0.0298  -0.0123 0.0092  196 ARG B NH2 
2365 N N   . VAL B 106 ? 0.0729 0.0936 0.1374 -0.0186 0.0034  -0.0076 197 VAL B N   
2366 C CA  . VAL B 106 ? 0.1018 0.1277 0.1732 -0.0243 0.0082  -0.0075 197 VAL B CA  
2367 C C   . VAL B 106 ? 0.1184 0.1630 0.2090 -0.0225 0.0118  -0.0088 197 VAL B C   
2368 O O   . VAL B 106 ? 0.1456 0.1926 0.2379 -0.0155 0.0161  -0.0091 197 VAL B O   
2369 C CB  . VAL B 106 ? 0.1258 0.1388 0.1824 -0.0268 0.0152  -0.0056 197 VAL B CB  
2370 C CG1 . VAL B 106 ? 0.1421 0.1598 0.2061 -0.0336 0.0236  -0.0046 197 VAL B CG1 
2371 C CG2 . VAL B 106 ? 0.0926 0.0914 0.1347 -0.0277 0.0094  -0.0036 197 VAL B CG2 
2372 N N   . GLU B 107 ? 0.0712 0.1291 0.1769 -0.0285 0.0097  -0.0101 198 GLU B N   
2373 C CA  . GLU B 107 ? 0.1458 0.2280 0.2757 -0.0278 0.0110  -0.0116 198 GLU B CA  
2374 C C   . GLU B 107 ? 0.1123 0.2011 0.2516 -0.0351 0.0236  -0.0115 198 GLU B C   
2375 O O   . GLU B 107 ? 0.1758 0.2534 0.3077 -0.0453 0.0271  -0.0108 198 GLU B O   
2376 C CB  . GLU B 107 ? 0.0824 0.1779 0.2241 -0.0324 -0.0002 -0.0142 198 GLU B CB  
2377 C CG  . GLU B 107 ? 0.1638 0.2865 0.3280 -0.0289 -0.0040 -0.0149 198 GLU B CG  
2378 C CD  . GLU B 107 ? 0.1389 0.2679 0.3005 -0.0307 -0.0181 -0.0161 198 GLU B CD  
2379 O OE1 . GLU B 107 ? 0.1166 0.2298 0.2622 -0.0375 -0.0220 -0.0181 198 GLU B OE1 
2380 O OE2 . GLU B 107 ? 0.2080 0.3571 0.3827 -0.0244 -0.0249 -0.0151 198 GLU B OE2 
2381 N N   . GLY B 108 ? 0.2100 0.3154 0.3652 -0.0293 0.0318  -0.0120 199 GLY B N   
2382 C CA  . GLY B 108 ? 0.2020 0.3189 0.3702 -0.0367 0.0459  -0.0121 199 GLY B CA  
2383 C C   . GLY B 108 ? 0.2917 0.3840 0.4343 -0.0419 0.0582  -0.0093 199 GLY B C   
2384 O O   . GLY B 108 ? 0.3865 0.4758 0.5280 -0.0534 0.0654  -0.0074 199 GLY B O   
2385 N N   . ASN B 109 ? 0.2449 0.3165 0.3618 -0.0335 0.0589  -0.0086 200 ASN B N   
2386 C CA  . ASN B 109 ? 0.1985 0.2478 0.2876 -0.0361 0.0696  -0.0061 200 ASN B CA  
2387 C C   . ASN B 109 ? 0.1703 0.2128 0.2469 -0.0248 0.0750  -0.0090 200 ASN B C   
2388 O O   . ASN B 109 ? 0.2050 0.2358 0.2695 -0.0182 0.0649  -0.0104 200 ASN B O   
2389 C CB  . ASN B 109 ? 0.2129 0.2371 0.2761 -0.0400 0.0602  -0.0027 200 ASN B CB  
2390 C CG  . ASN B 109 ? 0.2829 0.2850 0.3171 -0.0442 0.0696  0.0017  200 ASN B CG  
2391 O OD1 . ASN B 109 ? 0.2348 0.2305 0.2535 -0.0403 0.0792  0.0006  200 ASN B OD1 
2392 N ND2 . ASN B 109 ? 0.2520 0.2395 0.2759 -0.0516 0.0669  0.0066  200 ASN B ND2 
2393 N N   . LEU B 110 ? 0.2538 0.3021 0.3325 -0.0231 0.0921  -0.0105 201 LEU B N   
2394 C CA  . LEU B 110 ? 0.3552 0.3939 0.4203 -0.0117 0.0990  -0.0148 201 LEU B CA  
2395 C C   . LEU B 110 ? 0.3642 0.3702 0.3864 -0.0130 0.0973  -0.0150 201 LEU B C   
2396 O O   . LEU B 110 ? 0.3862 0.3784 0.3925 -0.0050 0.0983  -0.0200 201 LEU B O   
2397 C CB  . LEU B 110 ? 0.4545 0.5101 0.5351 -0.0084 0.1199  -0.0173 201 LEU B CB  
2398 C CG  . LEU B 110 ? 0.4764 0.5693 0.6038 -0.0030 0.1199  -0.0186 201 LEU B CG  
2399 C CD1 . LEU B 110 ? 0.4492 0.5593 0.5881 -0.0005 0.1338  -0.0193 201 LEU B CD1 
2400 C CD2 . LEU B 110 ? 0.4864 0.5792 0.6207 0.0121  0.1078  -0.0210 201 LEU B CD2 
2401 N N   . ARG B 111 ? 0.2672 0.2596 0.2700 -0.0224 0.0938  -0.0099 202 ARG B N   
2402 C CA  . ARG B 111 ? 0.2348 0.1996 0.1984 -0.0232 0.0881  -0.0094 202 ARG B CA  
2403 C C   . ARG B 111 ? 0.2402 0.1993 0.2018 -0.0227 0.0677  -0.0088 202 ARG B C   
2404 O O   . ARG B 111 ? 0.2398 0.1814 0.1747 -0.0245 0.0594  -0.0073 202 ARG B O   
2405 C CB  . ARG B 111 ? 0.2629 0.2141 0.2031 -0.0315 0.0956  -0.0029 202 ARG B CB  
2406 N N   . ALA B 112 ? 0.1814 0.1561 0.1703 -0.0202 0.0595  -0.0098 203 ALA B N   
2407 C CA  . ALA B 112 ? 0.1940 0.1647 0.1821 -0.0196 0.0433  -0.0097 203 ALA B CA  
2408 C C   . ALA B 112 ? 0.2795 0.2357 0.2492 -0.0160 0.0399  -0.0148 203 ALA B C   
2409 O O   . ALA B 112 ? 0.2159 0.1692 0.1847 -0.0107 0.0481  -0.0196 203 ALA B O   
2410 C CB  . ALA B 112 ? 0.2051 0.1936 0.2218 -0.0174 0.0375  -0.0098 203 ALA B CB  
2411 N N   . GLU B 113 ? 0.1721 0.1193 0.1286 -0.0191 0.0276  -0.0143 204 GLU B N   
2412 C CA  . GLU B 113 ? 0.1837 0.1186 0.1258 -0.0192 0.0216  -0.0197 204 GLU B CA  
2413 C C   . GLU B 113 ? 0.1646 0.1065 0.1211 -0.0211 0.0092  -0.0189 204 GLU B C   
2414 O O   . GLU B 113 ? 0.1507 0.1018 0.1167 -0.0228 0.0024  -0.0143 204 GLU B O   
2415 C CB  . GLU B 113 ? 0.2971 0.2161 0.2075 -0.0228 0.0179  -0.0212 204 GLU B CB  
2416 C CG  . GLU B 113 ? 0.3703 0.2795 0.2602 -0.0217 0.0319  -0.0215 204 GLU B CG  
2417 C CD  . GLU B 113 ? 0.4431 0.3335 0.2945 -0.0251 0.0269  -0.0230 204 GLU B CD  
2418 O OE1 . GLU B 113 ? 0.4074 0.2955 0.2519 -0.0284 0.0105  -0.0241 204 GLU B OE1 
2419 O OE2 . GLU B 113 ? 0.4614 0.3407 0.2897 -0.0247 0.0395  -0.0231 204 GLU B OE2 
2420 N N   . TYR B 114 ? 0.1677 0.1031 0.1248 -0.0209 0.0078  -0.0233 205 TYR B N   
2421 C CA  . TYR B 114 ? 0.1539 0.0948 0.1238 -0.0239 -0.0007 -0.0225 205 TYR B CA  
2422 C C   . TYR B 114 ? 0.2258 0.1557 0.1813 -0.0309 -0.0084 -0.0276 205 TYR B C   
2423 O O   . TYR B 114 ? 0.2257 0.1378 0.1631 -0.0318 -0.0048 -0.0338 205 TYR B O   
2424 C CB  . TYR B 114 ? 0.1470 0.0881 0.1298 -0.0190 0.0041  -0.0220 205 TYR B CB  
2425 C CG  . TYR B 114 ? 0.1292 0.0862 0.1295 -0.0136 0.0076  -0.0175 205 TYR B CG  
2426 C CD1 . TYR B 114 ? 0.1185 0.0881 0.1329 -0.0148 0.0022  -0.0136 205 TYR B CD1 
2427 C CD2 . TYR B 114 ? 0.1333 0.0940 0.1365 -0.0083 0.0167  -0.0179 205 TYR B CD2 
2428 C CE1 . TYR B 114 ? 0.1404 0.1238 0.1690 -0.0117 0.0036  -0.0110 205 TYR B CE1 
2429 C CE2 . TYR B 114 ? 0.1182 0.0968 0.1405 -0.0058 0.0184  -0.0146 205 TYR B CE2 
2430 C CZ  . TYR B 114 ? 0.1412 0.1300 0.1749 -0.0080 0.0108  -0.0115 205 TYR B CZ  
2431 O OH  . TYR B 114 ? 0.1196 0.1250 0.1703 -0.0071 0.0109  -0.0097 205 TYR B OH  
2432 N N   . LEU B 115 ? 0.1621 0.1031 0.1263 -0.0361 -0.0187 -0.0258 206 LEU B N   
2433 C CA  . LEU B 115 ? 0.1916 0.1289 0.1476 -0.0446 -0.0285 -0.0308 206 LEU B CA  
2434 C C   . LEU B 115 ? 0.1883 0.1323 0.1624 -0.0507 -0.0309 -0.0311 206 LEU B C   
2435 O O   . LEU B 115 ? 0.1468 0.1068 0.1404 -0.0485 -0.0307 -0.0259 206 LEU B O   
2436 C CB  . LEU B 115 ? 0.1799 0.1283 0.1328 -0.0453 -0.0397 -0.0282 206 LEU B CB  
2437 C CG  . LEU B 115 ? 0.1951 0.1476 0.1448 -0.0542 -0.0536 -0.0330 206 LEU B CG  
2438 C CD1 . LEU B 115 ? 0.2285 0.1584 0.1482 -0.0596 -0.0542 -0.0415 206 LEU B CD1 
2439 C CD2 . LEU B 115 ? 0.2778 0.2466 0.2313 -0.0511 -0.0661 -0.0280 206 LEU B CD2 
2440 N N   . ASP B 116 ? 0.2141 0.1434 0.1795 -0.0591 -0.0319 -0.0375 207 ASP B N   
2441 C CA  . ASP B 116 ? 0.2558 0.1940 0.2375 -0.0676 -0.0351 -0.0381 207 ASP B CA  
2442 C C   . ASP B 116 ? 0.2530 0.2043 0.2357 -0.0730 -0.0464 -0.0422 207 ASP B C   
2443 O O   . ASP B 116 ? 0.2228 0.1601 0.1877 -0.0768 -0.0491 -0.0487 207 ASP B O   
2444 C CB  . ASP B 116 ? 0.3003 0.2169 0.2757 -0.0705 -0.0277 -0.0411 207 ASP B CB  
2445 C CG  . ASP B 116 ? 0.3584 0.2600 0.3309 -0.0632 -0.0174 -0.0368 207 ASP B CG  
2446 O OD1 . ASP B 116 ? 0.3966 0.2738 0.3547 -0.0600 -0.0110 -0.0398 207 ASP B OD1 
2447 O OD2 . ASP B 116 ? 0.3160 0.2322 0.3021 -0.0580 -0.0156 -0.0301 207 ASP B OD2 
2448 N N   . ASP B 117 ? 0.1806 0.1584 0.1836 -0.0725 -0.0530 -0.0387 208 ASP B N   
2449 C CA  . ASP B 117 ? 0.1919 0.1851 0.1977 -0.0758 -0.0651 -0.0421 208 ASP B CA  
2450 C C   . ASP B 117 ? 0.2174 0.2098 0.2299 -0.0862 -0.0663 -0.0493 208 ASP B C   
2451 O O   . ASP B 117 ? 0.2018 0.2003 0.2344 -0.0906 -0.0604 -0.0484 208 ASP B O   
2452 C CB  . ASP B 117 ? 0.1723 0.1946 0.2013 -0.0708 -0.0704 -0.0367 208 ASP B CB  
2453 C CG  . ASP B 117 ? 0.1860 0.2243 0.2148 -0.0702 -0.0847 -0.0384 208 ASP B CG  
2454 O OD1 . ASP B 117 ? 0.1995 0.2484 0.2372 -0.0780 -0.0900 -0.0450 208 ASP B OD1 
2455 O OD2 . ASP B 117 ? 0.2292 0.2686 0.2488 -0.0616 -0.0914 -0.0327 208 ASP B OD2 
2456 N N   . ARG B 118 ? 0.2370 0.2202 0.2317 -0.0908 -0.0740 -0.0563 209 ARG B N   
2457 C CA  . ARG B 118 ? 0.2588 0.2370 0.2582 -0.1019 -0.0756 -0.0640 209 ARG B CA  
2458 C C   . ARG B 118 ? 0.3055 0.3152 0.3362 -0.1077 -0.0839 -0.0659 209 ARG B C   
2459 O O   . ARG B 118 ? 0.3065 0.3148 0.3496 -0.1183 -0.0839 -0.0706 209 ARG B O   
2460 C CB  . ARG B 118 ? 0.3029 0.2610 0.2725 -0.1054 -0.0814 -0.0723 209 ARG B CB  
2461 N N   . ASN B 119 ? 0.2377 0.2750 0.2820 -0.1010 -0.0907 -0.0620 210 ASN B N   
2462 C CA  . ASN B 119 ? 0.2887 0.3594 0.3650 -0.1048 -0.0983 -0.0648 210 ASN B CA  
2463 C C   . ASN B 119 ? 0.2849 0.3750 0.3896 -0.1005 -0.0890 -0.0586 210 ASN B C   
2464 O O   . ASN B 119 ? 0.2092 0.3112 0.3401 -0.1067 -0.0865 -0.0594 210 ASN B O   
2465 C CB  . ASN B 119 ? 0.3277 0.4192 0.3991 -0.0994 -0.1139 -0.0654 210 ASN B CB  
2466 C CG  . ASN B 119 ? 0.4011 0.4763 0.4453 -0.1049 -0.1243 -0.0730 210 ASN B CG  
2467 O OD1 . ASN B 119 ? 0.4775 0.5470 0.5254 -0.1166 -0.1267 -0.0821 210 ASN B OD1 
2468 N ND2 . ASN B 119 ? 0.4349 0.4996 0.4496 -0.0969 -0.1301 -0.0690 210 ASN B ND2 
2469 N N   . THR B 120 ? 0.1861 0.2763 0.2842 -0.0901 -0.0834 -0.0508 211 THR B N   
2470 C CA  . THR B 120 ? 0.2156 0.3220 0.3336 -0.0854 -0.0733 -0.0445 211 THR B CA  
2471 C C   . THR B 120 ? 0.2146 0.2987 0.3302 -0.0870 -0.0591 -0.0413 211 THR B C   
2472 O O   . THR B 120 ? 0.1867 0.2812 0.3179 -0.0848 -0.0499 -0.0371 211 THR B O   
2473 C CB  . THR B 120 ? 0.1490 0.2659 0.2632 -0.0730 -0.0769 -0.0361 211 THR B CB  
2474 O OG1 . THR B 120 ? 0.1484 0.2367 0.2398 -0.0677 -0.0725 -0.0321 211 THR B OG1 
2475 C CG2 . THR B 120 ? 0.2241 0.3548 0.3357 -0.0679 -0.0932 -0.0359 211 THR B CG2 
2476 N N   . PHE B 121 ? 0.1659 0.2199 0.2600 -0.0902 -0.0572 -0.0426 212 PHE B N   
2477 C CA  . PHE B 121 ? 0.1639 0.1945 0.2495 -0.0908 -0.0456 -0.0377 212 PHE B CA  
2478 C C   . PHE B 121 ? 0.1512 0.1812 0.2317 -0.0809 -0.0389 -0.0316 212 PHE B C   
2479 O O   . PHE B 121 ? 0.2115 0.2249 0.2848 -0.0803 -0.0304 -0.0270 212 PHE B O   
2480 C CB  . PHE B 121 ? 0.2336 0.2662 0.3370 -0.0995 -0.0400 -0.0339 212 PHE B CB  
2481 C CG  . PHE B 121 ? 0.3106 0.3452 0.4222 -0.1113 -0.0465 -0.0399 212 PHE B CG  
2482 C CD1 . PHE B 121 ? 0.3625 0.4192 0.5012 -0.1184 -0.0480 -0.0374 212 PHE B CD1 
2483 C CD2 . PHE B 121 ? 0.3959 0.4102 0.4864 -0.1156 -0.0510 -0.0473 212 PHE B CD2 
2484 C CE1 . PHE B 121 ? 0.4206 0.4806 0.5694 -0.1309 -0.0552 -0.0436 212 PHE B CE1 
2485 C CE2 . PHE B 121 ? 0.3963 0.4116 0.4934 -0.1276 -0.0580 -0.0541 212 PHE B CE2 
2486 C CZ  . PHE B 121 ? 0.4127 0.4517 0.5407 -0.1358 -0.0608 -0.0528 212 PHE B CZ  
2487 N N   . ARG B 122 ? 0.1303 0.1760 0.2114 -0.0736 -0.0436 -0.0298 213 ARG B N   
2488 C CA  . ARG B 122 ? 0.1135 0.1572 0.1918 -0.0651 -0.0388 -0.0231 213 ARG B CA  
2489 C C   . ARG B 122 ? 0.1163 0.1362 0.1734 -0.0608 -0.0388 -0.0221 213 ARG B C   
2490 O O   . ARG B 122 ? 0.1577 0.1657 0.1987 -0.0624 -0.0442 -0.0256 213 ARG B O   
2491 C CB  . ARG B 122 ? 0.2256 0.2902 0.3168 -0.0565 -0.0448 -0.0197 213 ARG B CB  
2492 C CG  . ARG B 122 ? 0.2262 0.3171 0.3391 -0.0602 -0.0447 -0.0201 213 ARG B CG  
2493 C CD  . ARG B 122 ? 0.1678 0.2740 0.2968 -0.0495 -0.0425 -0.0157 213 ARG B CD  
2494 N NE  . ARG B 122 ? 0.0919 0.2250 0.2441 -0.0517 -0.0410 -0.0150 213 ARG B NE  
2495 C CZ  . ARG B 122 ? 0.0870 0.2279 0.2518 -0.0517 -0.0296 -0.0128 213 ARG B CZ  
2496 N NH1 . ARG B 122 ? 0.0805 0.2042 0.2352 -0.0501 -0.0199 -0.0120 213 ARG B NH1 
2497 N NH2 . ARG B 122 ? 0.0909 0.2577 0.2787 -0.0531 -0.0279 -0.0117 213 ARG B NH2 
2498 N N   . HIS B 123 ? 0.1883 0.1149 0.1332 0.0147  0.0018  0.0103  214 HIS B N   
2499 C CA  . HIS B 123 ? 0.1441 0.0900 0.0929 0.0168  -0.0170 0.0178  214 HIS B CA  
2500 C C   . HIS B 123 ? 0.1401 0.0900 0.0863 0.0128  -0.0099 0.0105  214 HIS B C   
2501 O O   . HIS B 123 ? 0.1583 0.0916 0.0878 0.0001  0.0061  0.0020  214 HIS B O   
2502 C CB  . HIS B 123 ? 0.1766 0.1152 0.0977 0.0002  -0.0347 0.0306  214 HIS B CB  
2503 C CG  . HIS B 123 ? 0.1896 0.1198 0.1101 -0.0008 -0.0454 0.0418  214 HIS B CG  
2504 N ND1 . HIS B 123 ? 0.2318 0.1463 0.1193 -0.0230 -0.0601 0.0549  214 HIS B ND1 
2505 C CD2 . HIS B 123 ? 0.1683 0.1043 0.1188 0.0157  -0.0445 0.0421  214 HIS B CD2 
2506 C CE1 . HIS B 123 ? 0.2332 0.1471 0.1357 -0.0191 -0.0657 0.0612  214 HIS B CE1 
2507 N NE2 . HIS B 123 ? 0.2011 0.1270 0.1405 0.0049  -0.0566 0.0544  214 HIS B NE2 
2508 N N   . SER B 124 ? 0.1195 0.0909 0.0846 0.0213  -0.0202 0.0123  215 SER B N   
2509 C CA  . SER B 124 ? 0.1226 0.0984 0.0834 0.0159  -0.0168 0.0079  215 SER B CA  
2510 C C   . SER B 124 ? 0.1238 0.1216 0.0981 0.0189  -0.0309 0.0114  215 SER B C   
2511 O O   . SER B 124 ? 0.1237 0.1349 0.1212 0.0276  -0.0399 0.0141  215 SER B O   
2512 C CB  . SER B 124 ? 0.1385 0.1127 0.1171 0.0220  -0.0057 0.0017  215 SER B CB  
2513 O OG  . SER B 124 ? 0.1015 0.0893 0.1008 0.0338  -0.0114 0.0035  215 SER B OG  
2514 N N   . VAL B 125 ? 0.1271 0.1282 0.0925 0.0109  -0.0309 0.0093  216 VAL B N   
2515 C CA  . VAL B 125 ? 0.1040 0.1257 0.0873 0.0124  -0.0402 0.0094  216 VAL B CA  
2516 C C   . VAL B 125 ? 0.1159 0.1418 0.0984 0.0105  -0.0307 0.0033  216 VAL B C   
2517 O O   . VAL B 125 ? 0.1061 0.1186 0.0726 0.0032  -0.0231 0.0015  216 VAL B O   
2518 C CB  . VAL B 125 ? 0.1240 0.1457 0.0992 0.0014  -0.0561 0.0167  216 VAL B CB  
2519 C CG1 . VAL B 125 ? 0.1510 0.1532 0.0857 -0.0158 -0.0505 0.0158  216 VAL B CG1 
2520 C CG2 . VAL B 125 ? 0.1126 0.1565 0.1187 0.0037  -0.0638 0.0144  216 VAL B CG2 
2521 N N   . VAL B 126 ? 0.0829 0.1258 0.0838 0.0141  -0.0299 -0.0009 217 VAL B N   
2522 C CA  . VAL B 126 ? 0.0814 0.1259 0.0770 0.0087  -0.0233 -0.0038 217 VAL B CA  
2523 C C   . VAL B 126 ? 0.0977 0.1609 0.1054 0.0037  -0.0232 -0.0099 217 VAL B C   
2524 O O   . VAL B 126 ? 0.0928 0.1704 0.1251 0.0072  -0.0242 -0.0153 217 VAL B O   
2525 C CB  . VAL B 126 ? 0.0769 0.1165 0.0734 0.0111  -0.0197 -0.0031 217 VAL B CB  
2526 C CG1 . VAL B 126 ? 0.0714 0.1241 0.0827 0.0157  -0.0185 -0.0089 217 VAL B CG1 
2527 C CG2 . VAL B 126 ? 0.1032 0.1405 0.0906 0.0005  -0.0190 -0.0009 217 VAL B CG2 
2528 N N   . VAL B 127 ? 0.0860 0.1488 0.0833 -0.0051 -0.0207 -0.0103 218 VAL B N   
2529 C CA  . VAL B 127 ? 0.0873 0.1664 0.0956 -0.0123 -0.0174 -0.0178 218 VAL B CA  
2530 C C   . VAL B 127 ? 0.0962 0.1707 0.0862 -0.0240 -0.0113 -0.0172 218 VAL B C   
2531 O O   . VAL B 127 ? 0.1006 0.1590 0.0766 -0.0254 -0.0142 -0.0084 218 VAL B O   
2532 C CB  . VAL B 127 ? 0.1134 0.1965 0.1275 -0.0148 -0.0248 -0.0168 218 VAL B CB  
2533 C CG1 . VAL B 127 ? 0.1261 0.2116 0.1575 -0.0087 -0.0379 -0.0126 218 VAL B CG1 
2534 C CG2 . VAL B 127 ? 0.1847 0.2516 0.1735 -0.0201 -0.0246 -0.0114 218 VAL B CG2 
2535 N N   . PRO B 128 ? 0.1116 0.1985 0.1050 -0.0348 -0.0028 -0.0265 219 PRO B N   
2536 C CA  . PRO B 128 ? 0.1198 0.2002 0.0894 -0.0515 0.0004  -0.0234 219 PRO B CA  
2537 C C   . PRO B 128 ? 0.1844 0.2602 0.1517 -0.0528 -0.0041 -0.0176 219 PRO B C   
2538 O O   . PRO B 128 ? 0.1678 0.2509 0.1500 -0.0460 -0.0061 -0.0212 219 PRO B O   
2539 C CB  . PRO B 128 ? 0.1811 0.2769 0.1564 -0.0657 0.0156  -0.0399 219 PRO B CB  
2540 C CG  . PRO B 128 ? 0.2128 0.3221 0.2217 -0.0545 0.0207  -0.0519 219 PRO B CG  
2541 C CD  . PRO B 128 ? 0.1192 0.2255 0.1434 -0.0350 0.0053  -0.0414 219 PRO B CD  
2542 N N   . CYS B 129 ? 0.2268 0.2892 0.1771 -0.0635 -0.0078 -0.0076 220 CYS B N   
2543 C CA  A CYS B 129 ? 0.2304 0.2880 0.1815 -0.0678 -0.0099 -0.0034 220 CYS B CA  
2544 C CA  B CYS B 129 ? 0.2354 0.2958 0.1879 -0.0672 -0.0088 -0.0054 220 CYS B CA  
2545 C C   . CYS B 129 ? 0.2276 0.2899 0.1653 -0.0869 -0.0047 -0.0053 220 CYS B C   
2546 O O   . CYS B 129 ? 0.1749 0.2336 0.0923 -0.1023 -0.0031 -0.0034 220 CYS B O   
2547 C CB  A CYS B 129 ? 0.2109 0.2480 0.1657 -0.0670 -0.0186 0.0101  220 CYS B CB  
2548 C CB  B CYS B 129 ? 0.2295 0.2717 0.1881 -0.0624 -0.0157 0.0050  220 CYS B CB  
2549 S SG  A CYS B 129 ? 0.1943 0.2190 0.1618 -0.0524 -0.0224 0.0140  220 CYS B SG  
2550 S SG  B CYS B 129 ? 0.2156 0.2376 0.1734 -0.0705 -0.0272 0.0221  220 CYS B SG  
2551 N N   . GLU B 130 ? 0.2820 0.3497 0.2265 -0.0895 -0.0020 -0.0088 221 GLU B N   
2552 C CA  . GLU B 130 ? 0.3731 0.4438 0.3056 -0.1087 0.0042  -0.0109 221 GLU B CA  
2553 C C   . GLU B 130 ? 0.3136 0.3774 0.2527 -0.1095 -0.0009 -0.0040 221 GLU B C   
2554 O O   . GLU B 130 ? 0.2637 0.3244 0.2178 -0.0960 -0.0047 -0.0037 221 GLU B O   
2555 C CB  . GLU B 130 ? 0.5020 0.5941 0.4487 -0.1116 0.0191  -0.0306 221 GLU B CB  
2556 C CG  . GLU B 130 ? 0.5859 0.6909 0.5642 -0.0917 0.0165  -0.0384 221 GLU B CG  
2557 C CD  . GLU B 130 ? 0.6852 0.8068 0.6871 -0.0926 0.0285  -0.0553 221 GLU B CD  
2558 O OE1 . GLU B 130 ? 0.7079 0.8457 0.7466 -0.0896 0.0320  -0.0670 221 GLU B OE1 
2559 O OE2 . GLU B 130 ? 0.7104 0.8283 0.6992 -0.0975 0.0345  -0.0575 221 GLU B OE2 
2560 N N   . PRO B 131 ? 0.2925 0.3519 0.2188 -0.1280 0.0001  0.0010  222 PRO B N   
2561 C CA  . PRO B 131 ? 0.3076 0.3601 0.2451 -0.1294 -0.0042 0.0071  222 PRO B CA  
2562 C C   . PRO B 131 ? 0.3005 0.3693 0.2545 -0.1216 0.0039  -0.0079 222 PRO B C   
2563 O O   . PRO B 131 ? 0.2288 0.3146 0.1892 -0.1186 0.0114  -0.0213 222 PRO B O   
2564 C CB  . PRO B 131 ? 0.3489 0.3905 0.2631 -0.1466 -0.0065 0.0160  222 PRO B CB  
2565 C CG  . PRO B 131 ? 0.3817 0.4189 0.2669 -0.1572 -0.0075 0.0175  222 PRO B CG  
2566 C CD  . PRO B 131 ? 0.2838 0.3396 0.1804 -0.1482 0.0054  0.0004  222 PRO B CD  
2567 N N   . PRO B 132 ? 0.2520 0.3156 0.2184 -0.1197 0.0016  -0.0064 223 PRO B N   
2568 C CA  . PRO B 132 ? 0.2317 0.3087 0.2100 -0.1158 0.0057  -0.0190 223 PRO B CA  
2569 C C   . PRO B 132 ? 0.3162 0.4058 0.2954 -0.1251 0.0135  -0.0264 223 PRO B C   
2570 O O   . PRO B 132 ? 0.3617 0.4433 0.3263 -0.1361 0.0169  -0.0207 223 PRO B O   
2571 C CB  . PRO B 132 ? 0.2694 0.3338 0.2570 -0.1167 0.0042  -0.0163 223 PRO B CB  
2572 C CG  . PRO B 132 ? 0.3013 0.3470 0.2938 -0.1148 -0.0004 -0.0046 223 PRO B CG  
2573 C CD  . PRO B 132 ? 0.2550 0.2993 0.2320 -0.1217 -0.0053 0.0060  223 PRO B CD  
2574 N N   . GLU B 133 ? 0.3258 0.4317 0.3231 -0.1198 0.0149  -0.0384 224 GLU B N   
2575 C CA  . GLU B 133 ? 0.4304 0.5466 0.4401 -0.1252 0.0231  -0.0478 224 GLU B CA  
2576 C C   . GLU B 133 ? 0.3983 0.5042 0.3993 -0.1331 0.0246  -0.0424 224 GLU B C   
2577 O O   . GLU B 133 ? 0.3529 0.4480 0.3520 -0.1309 0.0182  -0.0354 224 GLU B O   
2578 C CB  . GLU B 133 ? 0.4712 0.6021 0.5112 -0.1168 0.0162  -0.0564 224 GLU B CB  
2579 C CG  . GLU B 133 ? 0.5686 0.7085 0.6309 -0.1209 0.0214  -0.0651 224 GLU B CG  
2580 C CD  . GLU B 133 ? 0.6073 0.7517 0.6888 -0.1164 0.0059  -0.0647 224 GLU B CD  
2581 O OE1 . GLU B 133 ? 0.6131 0.7503 0.6831 -0.1207 0.0038  -0.0621 224 GLU B OE1 
2582 O OE2 . GLU B 133 ? 0.6308 0.7837 0.7387 -0.1099 -0.0062 -0.0657 224 GLU B OE2 
2583 N N   . VAL B 134 ? 0.3817 0.4894 0.3793 -0.1431 0.0348  -0.0472 225 VAL B N   
2584 C CA  . VAL B 134 ? 0.3687 0.4681 0.3616 -0.1508 0.0355  -0.0423 225 VAL B CA  
2585 C C   . VAL B 134 ? 0.3520 0.4561 0.3654 -0.1431 0.0296  -0.0455 225 VAL B C   
2586 O O   . VAL B 134 ? 0.3854 0.5033 0.4187 -0.1370 0.0272  -0.0551 225 VAL B O   
2587 C CB  . VAL B 134 ? 0.4148 0.5179 0.4030 -0.1631 0.0492  -0.0518 225 VAL B CB  
2588 C CG1 . VAL B 134 ? 0.3802 0.5027 0.4031 -0.1568 0.0568  -0.0701 225 VAL B CG1 
2589 C CG2 . VAL B 134 ? 0.4183 0.5109 0.3979 -0.1726 0.0486  -0.0441 225 VAL B CG2 
2590 N N   . GLY B 135 ? 0.3131 0.4038 0.3241 -0.1444 0.0254  -0.0371 226 GLY B N   
2591 C CA  . GLY B 135 ? 0.4106 0.5016 0.4342 -0.1406 0.0221  -0.0420 226 GLY B CA  
2592 C C   . GLY B 135 ? 0.4487 0.5326 0.4694 -0.1345 0.0170  -0.0423 226 GLY B C   
2593 O O   . GLY B 135 ? 0.4494 0.5291 0.4728 -0.1354 0.0168  -0.0480 226 GLY B O   
2594 N N   . SER B 136 ? 0.3936 0.4747 0.4063 -0.1304 0.0146  -0.0378 227 SER B N   
2595 C CA  A SER B 136 ? 0.3564 0.4289 0.3649 -0.1262 0.0122  -0.0393 227 SER B CA  
2596 C CA  B SER B 136 ? 0.3552 0.4280 0.3634 -0.1261 0.0121  -0.0392 227 SER B CA  
2597 C C   . SER B 136 ? 0.3126 0.3689 0.3257 -0.1249 0.0131  -0.0296 227 SER B C   
2598 O O   . SER B 136 ? 0.2774 0.3308 0.2895 -0.1273 0.0104  -0.0185 227 SER B O   
2599 C CB  A SER B 136 ? 0.3486 0.4317 0.3500 -0.1210 0.0056  -0.0424 227 SER B CB  
2600 C CB  B SER B 136 ? 0.3472 0.4308 0.3487 -0.1207 0.0056  -0.0418 227 SER B CB  
2601 O OG  A SER B 136 ? 0.3395 0.4348 0.3477 -0.1216 -0.0004 -0.0481 227 SER B OG  
2602 O OG  B SER B 136 ? 0.3372 0.4097 0.3285 -0.1185 0.0042  -0.0423 227 SER B OG  
2603 N N   . ASP B 137 ? 0.2003 0.2438 0.2192 -0.1228 0.0168  -0.0339 228 ASP B N   
2604 C CA  . ASP B 137 ? 0.2358 0.2622 0.2760 -0.1200 0.0176  -0.0262 228 ASP B CA  
2605 C C   . ASP B 137 ? 0.2661 0.2872 0.3017 -0.1148 0.0172  -0.0258 228 ASP B C   
2606 O O   . ASP B 137 ? 0.1854 0.1924 0.2453 -0.1114 0.0159  -0.0183 228 ASP B O   
2607 C CB  . ASP B 137 ? 0.2022 0.2156 0.2663 -0.1207 0.0266  -0.0339 228 ASP B CB  
2608 C CG  . ASP B 137 ? 0.3444 0.3602 0.4211 -0.1255 0.0254  -0.0310 228 ASP B CG  
2609 O OD1 . ASP B 137 ? 0.3250 0.3427 0.4064 -0.1281 0.0165  -0.0167 228 ASP B OD1 
2610 O OD2 . ASP B 137 ? 0.3097 0.3243 0.3878 -0.1285 0.0341  -0.0434 228 ASP B OD2 
2611 N N   . CYS B 138 ? 0.1803 0.2117 0.1914 -0.1140 0.0161  -0.0324 229 CYS B N   
2612 C CA  . CYS B 138 ? 0.1754 0.2010 0.1801 -0.1054 0.0150  -0.0306 229 CYS B CA  
2613 C C   . CYS B 138 ? 0.1684 0.2100 0.1519 -0.0996 0.0067  -0.0298 229 CYS B C   
2614 O O   . CYS B 138 ? 0.1870 0.2428 0.1662 -0.1029 0.0027  -0.0330 229 CYS B O   
2615 C CB  . CYS B 138 ? 0.2236 0.2341 0.2291 -0.1094 0.0271  -0.0434 229 CYS B CB  
2616 S SG  . CYS B 138 ? 0.2500 0.2639 0.2190 -0.1203 0.0281  -0.0562 229 CYS B SG  
2617 N N   . THR B 139 ? 0.1745 0.2123 0.2406 -0.0544 0.0131  0.1014  230 THR B N   
2618 C CA  . THR B 139 ? 0.1672 0.2114 0.2233 -0.0527 0.0203  0.0856  230 THR B CA  
2619 C C   . THR B 139 ? 0.1938 0.2344 0.2562 -0.0459 0.0095  0.0691  230 THR B C   
2620 O O   . THR B 139 ? 0.1931 0.2264 0.2590 -0.0426 -0.0013 0.0694  230 THR B O   
2621 C CB  . THR B 139 ? 0.2158 0.2629 0.2310 -0.0563 0.0274  0.0865  230 THR B CB  
2622 O OG1 . THR B 139 ? 0.2155 0.2600 0.2100 -0.0560 0.0132  0.0878  230 THR B OG1 
2623 C CG2 . THR B 139 ? 0.2182 0.2674 0.2207 -0.0642 0.0387  0.1042  230 THR B CG2 
2624 N N   . THR B 140 ? 0.1351 0.1805 0.2006 -0.0433 0.0144  0.0563  231 THR B N   
2625 C CA  . THR B 140 ? 0.1168 0.1593 0.1872 -0.0376 0.0051  0.0425  231 THR B CA  
2626 C C   . THR B 140 ? 0.1639 0.2089 0.2150 -0.0346 0.0107  0.0327  231 THR B C   
2627 O O   . THR B 140 ? 0.1893 0.2388 0.2375 -0.0354 0.0249  0.0321  231 THR B O   
2628 C CB  . THR B 140 ? 0.1428 0.1876 0.2444 -0.0381 0.0017  0.0382  231 THR B CB  
2629 O OG1 . THR B 140 ? 0.1782 0.2155 0.2957 -0.0428 -0.0032 0.0452  231 THR B OG1 
2630 C CG2 . THR B 140 ? 0.1534 0.1945 0.2541 -0.0334 -0.0089 0.0256  231 THR B CG2 
2631 N N   . ILE B 141 ? 0.1091 0.1492 0.1479 -0.0310 0.0017  0.0252  232 ILE B N   
2632 C CA  A ILE B 141 ? 0.1094 0.1481 0.1340 -0.0282 0.0052  0.0146  232 ILE B CA  
2633 C CA  B ILE B 141 ? 0.1095 0.1482 0.1341 -0.0282 0.0053  0.0146  232 ILE B CA  
2634 C C   . ILE B 141 ? 0.0959 0.1341 0.1377 -0.0225 -0.0023 0.0068  232 ILE B C   
2635 O O   . ILE B 141 ? 0.1332 0.1679 0.1819 -0.0215 -0.0128 0.0070  232 ILE B O   
2636 C CB  A ILE B 141 ? 0.1460 0.1800 0.1415 -0.0311 -0.0001 0.0137  232 ILE B CB  
2637 C CB  B ILE B 141 ? 0.1443 0.1784 0.1393 -0.0315 0.0002  0.0145  232 ILE B CB  
2638 C CG1 A ILE B 141 ? 0.2049 0.2392 0.1761 -0.0392 0.0046  0.0223  232 ILE B CG1 
2639 C CG1 B ILE B 141 ? 0.1440 0.1724 0.1240 -0.0302 0.0042  0.0024  232 ILE B CG1 
2640 C CG2 A ILE B 141 ? 0.1333 0.1618 0.1167 -0.0290 0.0031  0.0014  232 ILE B CG2 
2641 C CG2 B ILE B 141 ? 0.1079 0.1416 0.1098 -0.0298 -0.0132 0.0196  232 ILE B CG2 
2642 C CD1 A ILE B 141 ? 0.2648 0.2961 0.2078 -0.0449 -0.0038 0.0216  232 ILE B CD1 
2643 C CD1 B ILE B 141 ? 0.2038 0.2274 0.1638 -0.0341 0.0203  -0.0018 232 ILE B CD1 
2644 N N   . HIS B 142 ? 0.0955 0.1355 0.1431 -0.0186 0.0040  0.0007  233 HIS B N   
2645 C CA  A HIS B 142 ? 0.0952 0.1359 0.1577 -0.0139 -0.0044 -0.0035 233 HIS B CA  
2646 C CA  B HIS B 142 ? 0.0952 0.1362 0.1583 -0.0138 -0.0040 -0.0035 233 HIS B CA  
2647 C C   . HIS B 142 ? 0.1152 0.1482 0.1597 -0.0108 -0.0050 -0.0104 233 HIS B C   
2648 O O   . HIS B 142 ? 0.1202 0.1493 0.1565 -0.0096 0.0060  -0.0146 233 HIS B O   
2649 C CB  A HIS B 142 ? 0.0927 0.1441 0.1856 -0.0115 0.0007  -0.0006 233 HIS B CB  
2650 C CB  B HIS B 142 ? 0.1001 0.1512 0.1921 -0.0107 0.0026  -0.0012 233 HIS B CB  
2651 C CG  A HIS B 142 ? 0.0939 0.1538 0.2085 -0.0167 0.0000  0.0072  233 HIS B CG  
2652 C CG  B HIS B 142 ? 0.1087 0.1699 0.2270 -0.0152 0.0001  0.0065  233 HIS B CG  
2653 N ND1 A HIS B 142 ? 0.1173 0.1796 0.2298 -0.0203 0.0128  0.0128  233 HIS B ND1 
2654 N ND1 B HIS B 142 ? 0.0762 0.1331 0.1920 -0.0211 -0.0098 0.0088  233 HIS B ND1 
2655 C CD2 A HIS B 142 ? 0.0736 0.1385 0.2105 -0.0207 -0.0125 0.0105  233 HIS B CD2 
2656 C CD2 B HIS B 142 ? 0.0784 0.1536 0.2301 -0.0150 0.0067  0.0131  233 HIS B CD2 
2657 C CE1 A HIS B 142 ? 0.0968 0.1661 0.2341 -0.0255 0.0092  0.0202  233 HIS B CE1 
2658 C CE1 B HIS B 142 ? 0.0945 0.1605 0.2381 -0.0259 -0.0104 0.0155  233 HIS B CE1 
2659 N NE2 A HIS B 142 ? 0.0787 0.1492 0.2311 -0.0264 -0.0069 0.0181  233 HIS B NE2 
2660 N NE2 B HIS B 142 ? 0.0951 0.1746 0.2625 -0.0226 -0.0011 0.0191  233 HIS B NE2 
2661 N N   . TYR B 143 ? 0.0824 0.1110 0.1203 -0.0100 -0.0161 -0.0119 234 TYR B N   
2662 C CA  . TYR B 143 ? 0.1035 0.1256 0.1282 -0.0080 -0.0174 -0.0166 234 TYR B CA  
2663 C C   . TYR B 143 ? 0.0739 0.0955 0.1097 -0.0031 -0.0229 -0.0175 234 TYR B C   
2664 O O   . TYR B 143 ? 0.0891 0.1148 0.1370 -0.0030 -0.0304 -0.0149 234 TYR B O   
2665 C CB  . TYR B 143 ? 0.1213 0.1405 0.1326 -0.0103 -0.0237 -0.0151 234 TYR B CB  
2666 C CG  . TYR B 143 ? 0.1071 0.1282 0.1060 -0.0162 -0.0218 -0.0110 234 TYR B CG  
2667 C CD1 . TYR B 143 ? 0.1095 0.1341 0.1130 -0.0179 -0.0250 -0.0031 234 TYR B CD1 
2668 C CD2 . TYR B 143 ? 0.0948 0.1121 0.0757 -0.0211 -0.0176 -0.0145 234 TYR B CD2 
2669 C CE1 . TYR B 143 ? 0.0909 0.1190 0.0829 -0.0239 -0.0259 0.0044  234 TYR B CE1 
2670 C CE2 . TYR B 143 ? 0.1094 0.1285 0.0729 -0.0292 -0.0190 -0.0095 234 TYR B CE2 
2671 C CZ  . TYR B 143 ? 0.1063 0.1326 0.0765 -0.0303 -0.0240 0.0014  234 TYR B CZ  
2672 O OH  . TYR B 143 ? 0.1237 0.1534 0.0768 -0.0388 -0.0278 0.0099  234 TYR B OH  
2673 N N   . ASN B 144 ? 0.0774 0.0930 0.1082 -0.0003 -0.0198 -0.0204 235 ASN B N   
2674 C CA  . ASN B 144 ? 0.1122 0.1260 0.1492 0.0039  -0.0260 -0.0185 235 ASN B CA  
2675 C C   . ASN B 144 ? 0.1442 0.1495 0.1642 0.0028  -0.0274 -0.0204 235 ASN B C   
2676 O O   . ASN B 144 ? 0.1497 0.1495 0.1593 -0.0004 -0.0218 -0.0242 235 ASN B O   
2677 C CB  . ASN B 144 ? 0.1249 0.1388 0.1802 0.0097  -0.0194 -0.0166 235 ASN B CB  
2678 C CG  . ASN B 144 ? 0.1586 0.1838 0.2387 0.0116  -0.0148 -0.0127 235 ASN B CG  
2679 O OD1 . ASN B 144 ? 0.1752 0.1993 0.2699 0.0164  -0.0014 -0.0130 235 ASN B OD1 
2680 N ND2 . ASN B 144 ? 0.1651 0.2000 0.2527 0.0077  -0.0242 -0.0090 235 ASN B ND2 
2681 N N   . TYR B 145 ? 0.0745 0.0781 0.0905 0.0042  -0.0348 -0.0175 236 TYR B N   
2682 C CA  . TYR B 145 ? 0.0850 0.0821 0.0896 0.0036  -0.0343 -0.0170 236 TYR B CA  
2683 C C   . TYR B 145 ? 0.1220 0.1144 0.1316 0.0075  -0.0358 -0.0125 236 TYR B C   
2684 O O   . TYR B 145 ? 0.1168 0.1122 0.1290 0.0095  -0.0435 -0.0074 236 TYR B O   
2685 C CB  . TYR B 145 ? 0.0790 0.0758 0.0731 0.0026  -0.0372 -0.0161 236 TYR B CB  
2686 C CG  . TYR B 145 ? 0.1006 0.1015 0.0952 0.0000  -0.0351 -0.0173 236 TYR B CG  
2687 C CD1 . TYR B 145 ? 0.1437 0.1473 0.1429 -0.0006 -0.0368 -0.0183 236 TYR B CD1 
2688 C CD2 . TYR B 145 ? 0.1325 0.1356 0.1262 -0.0026 -0.0326 -0.0153 236 TYR B CD2 
2689 C CE1 . TYR B 145 ? 0.0921 0.0987 0.0938 -0.0024 -0.0350 -0.0165 236 TYR B CE1 
2690 C CE2 . TYR B 145 ? 0.0889 0.0981 0.0867 -0.0047 -0.0328 -0.0124 236 TYR B CE2 
2691 C CZ  . TYR B 145 ? 0.0664 0.0764 0.0675 -0.0040 -0.0334 -0.0128 236 TYR B CZ  
2692 O OH  . TYR B 145 ? 0.1157 0.1306 0.1226 -0.0055 -0.0337 -0.0074 236 TYR B OH  
2693 N N   . MET B 146 ? 0.1161 0.1003 0.1265 0.0074  -0.0298 -0.0134 237 MET B N   
2694 C CA  . MET B 146 ? 0.1010 0.0789 0.1232 0.0124  -0.0284 -0.0082 237 MET B CA  
2695 C C   . MET B 146 ? 0.1092 0.0805 0.1240 0.0122  -0.0311 -0.0012 237 MET B C   
2696 O O   . MET B 146 ? 0.1305 0.0931 0.1553 0.0156  -0.0285 0.0041  237 MET B O   
2697 C CB  . MET B 146 ? 0.1225 0.0896 0.1515 0.0127  -0.0168 -0.0150 237 MET B CB  
2698 C CG  . MET B 146 ? 0.1999 0.1723 0.2328 0.0126  -0.0106 -0.0212 237 MET B CG  
2699 S SD  . MET B 146 ? 0.1732 0.1609 0.2339 0.0203  -0.0142 -0.0124 237 MET B SD  
2700 C CE  . MET B 146 ? 0.1706 0.1505 0.2549 0.0295  -0.0113 -0.0030 237 MET B CE  
2701 N N   . CYS B 147 ? 0.1134 0.0876 0.1128 0.0089  -0.0340 -0.0003 238 CYS B N   
2702 C CA  . CYS B 147 ? 0.1599 0.1291 0.1495 0.0086  -0.0345 0.0077  238 CYS B CA  
2703 C C   . CYS B 147 ? 0.1727 0.1457 0.1443 0.0078  -0.0377 0.0081  238 CYS B C   
2704 O O   . CYS B 147 ? 0.2015 0.1793 0.1707 0.0065  -0.0369 0.0012  238 CYS B O   
2705 C CB  . CYS B 147 ? 0.2650 0.2294 0.2546 0.0037  -0.0275 0.0069  238 CYS B CB  
2706 S SG  . CYS B 147 ? 0.2041 0.1537 0.2042 0.0032  -0.0234 0.0123  238 CYS B SG  
2707 N N   . TYR B 148 ? 0.1551 0.1235 0.1118 0.0081  -0.0399 0.0163  239 TYR B N   
2708 C CA  . TYR B 148 ? 0.1652 0.1310 0.0973 0.0062  -0.0383 0.0144  239 TYR B CA  
2709 C C   . TYR B 148 ? 0.1749 0.1404 0.1067 0.0055  -0.0250 0.0128  239 TYR B C   
2710 O O   . TYR B 148 ? 0.1728 0.1390 0.1176 0.0045  -0.0200 0.0175  239 TYR B O   
2711 C CB  . TYR B 148 ? 0.2107 0.1698 0.1198 0.0051  -0.0442 0.0241  239 TYR B CB  
2712 C CG  . TYR B 148 ? 0.2415 0.2041 0.1497 0.0040  -0.0610 0.0281  239 TYR B CG  
2713 C CD1 . TYR B 148 ? 0.2520 0.2177 0.1536 0.0003  -0.0657 0.0190  239 TYR B CD1 
2714 C CD2 . TYR B 148 ? 0.2181 0.1833 0.1394 0.0063  -0.0697 0.0421  239 TYR B CD2 
2715 C CE1 . TYR B 148 ? 0.2956 0.2707 0.2073 -0.0022 -0.0763 0.0224  239 TYR B CE1 
2716 C CE2 . TYR B 148 ? 0.3061 0.2824 0.2391 0.0054  -0.0798 0.0457  239 TYR B CE2 
2717 C CZ  . TYR B 148 ? 0.2841 0.2656 0.2113 0.0005  -0.0838 0.0358  239 TYR B CZ  
2718 O OH  . TYR B 148 ? 0.3010 0.2928 0.2401 -0.0019 -0.0948 0.0404  239 TYR B OH  
2719 N N   . SER B 149 ? 0.1947 0.1585 0.1143 0.0058  -0.0188 0.0070  240 SER B N   
2720 C CA  . SER B 149 ? 0.1951 0.1607 0.1195 0.0067  -0.0043 0.0088  240 SER B CA  
2721 C C   . SER B 149 ? 0.1758 0.1365 0.0901 0.0060  0.0035  0.0187  240 SER B C   
2722 O O   . SER B 149 ? 0.1806 0.1473 0.1114 0.0054  0.0138  0.0245  240 SER B O   
2723 C CB  . SER B 149 ? 0.2239 0.1839 0.1364 0.0091  0.0045  0.0015  240 SER B CB  
2724 O OG  . SER B 149 ? 0.1742 0.1410 0.1051 0.0098  0.0002  -0.0042 240 SER B OG  
2725 N N   . SER B 150 ? 0.1978 0.1494 0.0876 0.0050  -0.0024 0.0231  241 SER B N   
2726 C CA  . SER B 150 ? 0.2229 0.1679 0.0965 0.0038  0.0051  0.0346  241 SER B CA  
2727 C C   . SER B 150 ? 0.2256 0.1725 0.1195 0.0026  0.0004  0.0459  241 SER B C   
2728 O O   . SER B 150 ? 0.2575 0.1993 0.1430 0.0012  0.0075  0.0578  241 SER B O   
2729 C CB  . SER B 150 ? 0.2967 0.2294 0.1284 0.0015  -0.0012 0.0360  241 SER B CB  
2730 O OG  . SER B 150 ? 0.3367 0.2723 0.1733 0.0004  -0.0215 0.0392  241 SER B OG  
2731 N N   . CYS B 151 ? 0.1920 0.1437 0.1115 0.0029  -0.0089 0.0423  242 CYS B N   
2732 C CA  . CYS B 151 ? 0.2391 0.1860 0.1751 0.0023  -0.0124 0.0513  242 CYS B CA  
2733 C C   . CYS B 151 ? 0.1981 0.1434 0.1458 -0.0019 -0.0010 0.0589  242 CYS B C   
2734 O O   . CYS B 151 ? 0.2057 0.1586 0.1694 -0.0054 0.0048  0.0537  242 CYS B O   
2735 C CB  . CYS B 151 ? 0.2551 0.2039 0.2143 0.0031  -0.0189 0.0427  242 CYS B CB  
2736 S SG  . CYS B 151 ? 0.1971 0.1476 0.1568 0.0085  -0.0326 0.0424  242 CYS B SG  
2737 N N   . MET B 152 ? 0.2198 0.1563 0.1621 -0.0025 0.0007  0.0734  243 MET B N   
2738 C CA  . MET B 152 ? 0.2285 0.1624 0.1837 -0.0076 0.0116  0.0832  243 MET B CA  
2739 C C   . MET B 152 ? 0.2229 0.1531 0.2087 -0.0127 0.0090  0.0781  243 MET B C   
2740 O O   . MET B 152 ? 0.2124 0.1338 0.2060 -0.0103 0.0012  0.0740  243 MET B O   
2741 C CB  . MET B 152 ? 0.3125 0.2357 0.2532 -0.0072 0.0133  0.1019  243 MET B CB  
2742 C CG  . MET B 152 ? 0.5227 0.4458 0.4239 -0.0055 0.0172  0.1071  243 MET B CG  
2743 S SD  . MET B 152 ? 0.5777 0.5085 0.4748 -0.0077 0.0401  0.1048  243 MET B SD  
2744 C CE  . MET B 152 ? 0.4787 0.4065 0.3993 -0.0138 0.0513  0.1242  243 MET B CE  
2745 N N   . GLY B 153 ? 0.2112 0.1472 0.2146 -0.0205 0.0161  0.0789  244 GLY B N   
2746 C CA  . GLY B 153 ? 0.2317 0.1630 0.2580 -0.0291 0.0117  0.0714  244 GLY B CA  
2747 C C   . GLY B 153 ? 0.2734 0.2116 0.3009 -0.0298 0.0038  0.0546  244 GLY B C   
2748 O O   . GLY B 153 ? 0.2703 0.2025 0.3089 -0.0387 -0.0006 0.0464  244 GLY B O   
2749 N N   . GLY B 154 ? 0.2019 0.1501 0.2153 -0.0219 0.0019  0.0493  245 GLY B N   
2750 C CA  . GLY B 154 ? 0.1542 0.1112 0.1687 -0.0224 -0.0042 0.0364  245 GLY B CA  
2751 C C   . GLY B 154 ? 0.2367 0.2112 0.2526 -0.0206 0.0002  0.0381  245 GLY B C   
2752 O O   . GLY B 154 ? 0.2007 0.1844 0.2316 -0.0253 0.0065  0.0463  245 GLY B O   
2753 N N   . MET B 155 ? 0.1952 0.1740 0.1992 -0.0138 -0.0017 0.0315  246 MET B N   
2754 C CA  . MET B 155 ? 0.1522 0.1433 0.1594 -0.0106 0.0050  0.0326  246 MET B CA  
2755 C C   . MET B 155 ? 0.1725 0.1623 0.1728 -0.0072 0.0193  0.0419  246 MET B C   
2756 O O   . MET B 155 ? 0.2418 0.2424 0.2565 -0.0060 0.0301  0.0468  246 MET B O   
2757 C CB  . MET B 155 ? 0.1507 0.1411 0.1447 -0.0046 0.0009  0.0232  246 MET B CB  
2758 C CG  . MET B 155 ? 0.1622 0.1574 0.1652 -0.0085 -0.0094 0.0160  246 MET B CG  
2759 S SD  . MET B 155 ? 0.1674 0.1631 0.1609 -0.0030 -0.0136 0.0073  246 MET B SD  
2760 C CE  . MET B 155 ? 0.2165 0.2005 0.1953 -0.0002 -0.0195 0.0038  246 MET B CE  
2761 N N   . ASN B 156 ? 0.1718 0.1486 0.1515 -0.0057 0.0206  0.0463  247 ASN B N   
2762 C CA  . ASN B 156 ? 0.1892 0.1621 0.1565 -0.0044 0.0352  0.0568  247 ASN B CA  
2763 C C   . ASN B 156 ? 0.2439 0.2196 0.2011 0.0013  0.0498  0.0534  247 ASN B C   
2764 O O   . ASN B 156 ? 0.2073 0.1896 0.1770 0.0022  0.0671  0.0612  247 ASN B O   
2765 C CB  . ASN B 156 ? 0.2878 0.2665 0.2816 -0.0112 0.0415  0.0687  247 ASN B CB  
2766 C CG  . ASN B 156 ? 0.4042 0.3772 0.3841 -0.0105 0.0575  0.0821  247 ASN B CG  
2767 O OD1 . ASN B 156 ? 0.4825 0.4430 0.4267 -0.0066 0.0593  0.0833  247 ASN B OD1 
2768 N ND2 . ASN B 156 ? 0.4013 0.3843 0.4087 -0.0155 0.0688  0.0934  247 ASN B ND2 
2769 N N   . ARG B 157 ? 0.1983 0.1678 0.1356 0.0053  0.0443  0.0418  248 ARG B N   
2770 C CA  . ARG B 157 ? 0.2738 0.2374 0.1944 0.0107  0.0577  0.0348  248 ARG B CA  
2771 C C   . ARG B 157 ? 0.2672 0.2450 0.2228 0.0144  0.0663  0.0342  248 ARG B C   
2772 O O   . ARG B 157 ? 0.3184 0.2900 0.2674 0.0205  0.0818  0.0295  248 ARG B O   
2773 C CB  . ARG B 157 ? 0.2536 0.2050 0.1445 0.0120  0.0770  0.0403  248 ARG B CB  
2774 C CG  . ARG B 157 ? 0.3026 0.2410 0.1570 0.0076  0.0667  0.0448  248 ARG B CG  
2775 C CD  . ARG B 157 ? 0.5231 0.4451 0.3337 0.0073  0.0846  0.0482  248 ARG B CD  
2776 N NE  . ARG B 157 ? 0.7231 0.6366 0.5012 0.0018  0.0676  0.0530  248 ARG B NE  
2777 C CZ  . ARG B 157 ? 0.7625 0.6692 0.5139 -0.0014 0.0511  0.0434  248 ARG B CZ  
2778 N NH1 . ARG B 157 ? 0.7375 0.6396 0.4853 0.0001  0.0508  0.0271  248 ARG B NH1 
2779 N NH2 . ARG B 157 ? 0.7666 0.6736 0.5010 -0.0062 0.0345  0.0519  248 ARG B NH2 
2780 N N   . ARG B 158 ? 0.1690 0.1640 0.1606 0.0104  0.0566  0.0394  249 ARG B N   
2781 C CA  . ARG B 158 ? 0.1834 0.1951 0.2106 0.0128  0.0605  0.0425  249 ARG B CA  
2782 C C   . ARG B 158 ? 0.1701 0.1796 0.1936 0.0150  0.0490  0.0323  249 ARG B C   
2783 O O   . ARG B 158 ? 0.1762 0.1824 0.1887 0.0104  0.0322  0.0261  249 ARG B O   
2784 C CB  . ARG B 158 ? 0.1365 0.1679 0.2004 0.0042  0.0516  0.0535  249 ARG B CB  
2785 C CG  . ARG B 158 ? 0.1631 0.1989 0.2391 0.0014  0.0648  0.0661  249 ARG B CG  
2786 C CD  . ARG B 158 ? 0.2149 0.2652 0.3219 -0.0111 0.0522  0.0751  249 ARG B CD  
2787 N NE  . ARG B 158 ? 0.1811 0.2180 0.2688 -0.0187 0.0349  0.0669  249 ARG B NE  
2788 C CZ  . ARG B 158 ? 0.2120 0.2522 0.3159 -0.0314 0.0226  0.0696  249 ARG B CZ  
2789 N NH1 . ARG B 158 ? 0.1734 0.2334 0.3140 -0.0399 0.0220  0.0814  249 ARG B NH1 
2790 N NH2 . ARG B 158 ? 0.1940 0.2172 0.2791 -0.0362 0.0114  0.0604  249 ARG B NH2 
2791 N N   . PRO B 159 ? 0.1552 0.1655 0.1899 0.0222  0.0595  0.0312  250 PRO B N   
2792 C CA  . PRO B 159 ? 0.1554 0.1639 0.1903 0.0234  0.0486  0.0239  250 PRO B CA  
2793 C C   . PRO B 159 ? 0.1293 0.1577 0.1917 0.0169  0.0316  0.0309  250 PRO B C   
2794 O O   . PRO B 159 ? 0.1004 0.1471 0.1925 0.0132  0.0306  0.0431  250 PRO B O   
2795 C CB  . PRO B 159 ? 0.1761 0.1787 0.2216 0.0334  0.0678  0.0236  250 PRO B CB  
2796 C CG  . PRO B 159 ? 0.2597 0.2722 0.3280 0.0374  0.0866  0.0353  250 PRO B CG  
2797 C CD  . PRO B 159 ? 0.1882 0.1972 0.2339 0.0308  0.0847  0.0359  250 PRO B CD  
2798 N N   . ILE B 160 ? 0.1212 0.1954 0.1358 -0.0297 0.0149  0.0277  251 ILE B N   
2799 C CA  . ILE B 160 ? 0.0839 0.1561 0.1075 -0.0364 0.0119  0.0248  251 ILE B CA  
2800 C C   . ILE B 160 ? 0.0787 0.1491 0.1016 -0.0284 0.0089  0.0179  251 ILE B C   
2801 O O   . ILE B 160 ? 0.0971 0.1612 0.1114 -0.0194 0.0077  0.0146  251 ILE B O   
2802 C CB  . ILE B 160 ? 0.0857 0.1380 0.1084 -0.0433 0.0090  0.0239  251 ILE B CB  
2803 C CG1 . ILE B 160 ? 0.1673 0.2052 0.1833 -0.0361 0.0060  0.0204  251 ILE B CG1 
2804 C CG2 . ILE B 160 ? 0.0967 0.1462 0.1181 -0.0527 0.0116  0.0311  251 ILE B CG2 
2805 C CD1 . ILE B 160 ? 0.1273 0.1496 0.1445 -0.0387 0.0032  0.0183  251 ILE B CD1 
2806 N N   . LEU B 161 ? 0.0709 0.1447 0.1013 -0.0325 0.0072  0.0160  252 LEU B N   
2807 C CA  . LEU B 161 ? 0.1240 0.1925 0.1538 -0.0270 0.0041  0.0103  252 LEU B CA  
2808 C C   . LEU B 161 ? 0.1511 0.2058 0.1835 -0.0334 0.0010  0.0079  252 LEU B C   
2809 O O   . LEU B 161 ? 0.1178 0.1716 0.1534 -0.0420 0.0011  0.0100  252 LEU B O   
2810 C CB  . LEU B 161 ? 0.1727 0.2591 0.2078 -0.0241 0.0051  0.0109  252 LEU B CB  
2811 C CG  . LEU B 161 ? 0.3384 0.4466 0.3745 -0.0185 0.0098  0.0157  252 LEU B CG  
2812 C CD1 . LEU B 161 ? 0.3593 0.4883 0.4032 -0.0159 0.0101  0.0172  252 LEU B CD1 
2813 C CD2 . LEU B 161 ? 0.4117 0.5114 0.4344 -0.0057 0.0111  0.0131  252 LEU B CD2 
2814 N N   . THR B 162 ? 0.0673 0.1107 0.0971 -0.0293 -0.0017 0.0039  253 THR B N   
2815 C CA  . THR B 162 ? 0.0865 0.1208 0.1189 -0.0330 -0.0034 0.0020  253 THR B CA  
2816 C C   . THR B 162 ? 0.1021 0.1418 0.1363 -0.0308 -0.0044 -0.0003 253 THR B C   
2817 O O   . THR B 162 ? 0.1114 0.1526 0.1425 -0.0240 -0.0049 -0.0017 253 THR B O   
2818 C CB  . THR B 162 ? 0.0875 0.1098 0.1182 -0.0308 -0.0052 0.0009  253 THR B CB  
2819 O OG1 . THR B 162 ? 0.1159 0.1342 0.1446 -0.0319 -0.0046 0.0036  253 THR B OG1 
2820 C CG2 . THR B 162 ? 0.0554 0.0710 0.0885 -0.0326 -0.0055 -0.0002 253 THR B CG2 
2821 N N   . ILE B 163 ? 0.0538 0.0946 0.0906 -0.0360 -0.0049 -0.0006 254 ILE B N   
2822 C CA  . ILE B 163 ? 0.0574 0.1030 0.0948 -0.0338 -0.0064 -0.0024 254 ILE B CA  
2823 C C   . ILE B 163 ? 0.0528 0.0849 0.0877 -0.0341 -0.0071 -0.0044 254 ILE B C   
2824 O O   . ILE B 163 ? 0.0999 0.1237 0.1329 -0.0385 -0.0068 -0.0046 254 ILE B O   
2825 C CB  . ILE B 163 ? 0.0827 0.1425 0.1241 -0.0395 -0.0074 -0.0008 254 ILE B CB  
2826 C CG1 . ILE B 163 ? 0.0533 0.1313 0.0992 -0.0389 -0.0055 0.0031  254 ILE B CG1 
2827 C CG2 . ILE B 163 ? 0.0593 0.1247 0.1006 -0.0362 -0.0097 -0.0024 254 ILE B CG2 
2828 C CD1 . ILE B 163 ? 0.0605 0.1464 0.1086 -0.0443 -0.0062 0.0060  254 ILE B CD1 
2829 N N   . ILE B 164 ? 0.0519 0.0803 0.0850 -0.0287 -0.0076 -0.0055 255 ILE B N   
2830 C CA  . ILE B 164 ? 0.0906 0.1096 0.1221 -0.0283 -0.0074 -0.0060 255 ILE B CA  
2831 C C   . ILE B 164 ? 0.1237 0.1463 0.1526 -0.0266 -0.0084 -0.0068 255 ILE B C   
2832 O O   . ILE B 164 ? 0.0756 0.1029 0.1034 -0.0218 -0.0093 -0.0067 255 ILE B O   
2833 C CB  . ILE B 164 ? 0.1058 0.1180 0.1373 -0.0256 -0.0077 -0.0051 255 ILE B CB  
2834 C CG1 . ILE B 164 ? 0.1099 0.1205 0.1433 -0.0268 -0.0080 -0.0041 255 ILE B CG1 
2835 C CG2 . ILE B 164 ? 0.0748 0.0815 0.1067 -0.0258 -0.0063 -0.0037 255 ILE B CG2 
2836 C CD1 . ILE B 164 ? 0.1084 0.1168 0.1441 -0.0293 -0.0062 -0.0028 255 ILE B CD1 
2837 N N   . THR B 165 ? 0.0771 0.0960 0.1030 -0.0292 -0.0083 -0.0078 256 THR B N   
2838 C CA  A THR B 165 ? 0.0991 0.1210 0.1209 -0.0275 -0.0099 -0.0086 256 THR B CA  
2839 C CA  B THR B 165 ? 0.0973 0.1192 0.1191 -0.0276 -0.0099 -0.0086 256 THR B CA  
2840 C C   . THR B 165 ? 0.1325 0.1441 0.1491 -0.0248 -0.0077 -0.0081 256 THR B C   
2841 O O   . THR B 165 ? 0.1130 0.1166 0.1281 -0.0257 -0.0051 -0.0080 256 THR B O   
2842 C CB  A THR B 165 ? 0.1089 0.1362 0.1287 -0.0336 -0.0130 -0.0102 256 THR B CB  
2843 C CB  B THR B 165 ? 0.0971 0.1245 0.1169 -0.0337 -0.0130 -0.0102 256 THR B CB  
2844 O OG1 A THR B 165 ? 0.0849 0.1147 0.0992 -0.0318 -0.0154 -0.0111 256 THR B OG1 
2845 O OG1 B THR B 165 ? 0.1813 0.1971 0.1973 -0.0389 -0.0122 -0.0115 256 THR B OG1 
2846 C CG2 A THR B 165 ? 0.1520 0.1661 0.1668 -0.0385 -0.0121 -0.0117 256 THR B CG2 
2847 C CG2 B THR B 165 ? 0.0640 0.1086 0.0910 -0.0358 -0.0150 -0.0087 256 THR B CG2 
2848 N N   . LEU B 166 ? 0.1366 0.1489 0.1500 -0.0204 -0.0081 -0.0070 257 LEU B N   
2849 C CA  . LEU B 166 ? 0.1199 0.1251 0.1272 -0.0177 -0.0057 -0.0056 257 LEU B CA  
2850 C C   . LEU B 166 ? 0.0848 0.0912 0.0835 -0.0181 -0.0081 -0.0082 257 LEU B C   
2851 O O   . LEU B 166 ? 0.1010 0.1170 0.0998 -0.0180 -0.0122 -0.0090 257 LEU B O   
2852 C CB  . LEU B 166 ? 0.1111 0.1140 0.1173 -0.0133 -0.0053 -0.0024 257 LEU B CB  
2853 C CG  . LEU B 166 ? 0.1168 0.1129 0.1186 -0.0114 -0.0016 0.0015  257 LEU B CG  
2854 C CD1 . LEU B 166 ? 0.1086 0.1027 0.1173 -0.0144 0.0020  0.0043  257 LEU B CD1 
2855 C CD2 . LEU B 166 ? 0.1254 0.1165 0.1227 -0.0079 -0.0024 0.0048  257 LEU B CD2 
2856 N N   . GLU B 167 ? 0.1305 0.1282 0.1214 -0.0182 -0.0059 -0.0094 258 GLU B N   
2857 C CA  . GLU B 167 ? 0.1183 0.1128 0.0974 -0.0197 -0.0094 -0.0131 258 GLU B CA  
2858 C C   . GLU B 167 ? 0.1177 0.1039 0.0848 -0.0136 -0.0058 -0.0120 258 GLU B C   
2859 O O   . GLU B 167 ? 0.1173 0.0990 0.0855 -0.0097 0.0005  -0.0087 258 GLU B O   
2860 C CB  . GLU B 167 ? 0.1182 0.1032 0.0922 -0.0253 -0.0106 -0.0168 258 GLU B CB  
2861 C CG  . GLU B 167 ? 0.2562 0.2472 0.2400 -0.0322 -0.0132 -0.0171 258 GLU B CG  
2862 C CD  . GLU B 167 ? 0.2208 0.1968 0.1961 -0.0375 -0.0138 -0.0201 258 GLU B CD  
2863 O OE1 . GLU B 167 ? 0.2214 0.1810 0.1836 -0.0332 -0.0108 -0.0218 258 GLU B OE1 
2864 O OE2 . GLU B 167 ? 0.2670 0.2470 0.2474 -0.0454 -0.0171 -0.0202 258 GLU B OE2 
2865 N N   . ASP B 168 ? 0.1474 0.1330 0.1025 -0.0129 -0.0099 -0.0144 259 ASP B N   
2866 C CA  . ASP B 168 ? 0.1450 0.1207 0.0849 -0.0065 -0.0061 -0.0139 259 ASP B CA  
2867 C C   . ASP B 168 ? 0.2064 0.1665 0.1333 -0.0069 -0.0047 -0.0184 259 ASP B C   
2868 O O   . ASP B 168 ? 0.1648 0.1209 0.0954 -0.0126 -0.0066 -0.0212 259 ASP B O   
2869 C CB  . ASP B 168 ? 0.1554 0.1346 0.0844 -0.0041 -0.0110 -0.0144 259 ASP B CB  
2870 C CG  . ASP B 168 ? 0.2119 0.1925 0.1333 -0.0109 -0.0206 -0.0204 259 ASP B CG  
2871 O OD1 . ASP B 168 ? 0.1958 0.1681 0.1141 -0.0176 -0.0230 -0.0248 259 ASP B OD1 
2872 O OD2 . ASP B 168 ? 0.2416 0.2315 0.1592 -0.0098 -0.0263 -0.0200 259 ASP B OD2 
2873 N N   . SER B 169 ? 0.1793 0.1287 0.0884 0.0002  -0.0010 -0.0190 260 SER B N   
2874 C CA  . SER B 169 ? 0.1978 0.1288 0.0909 0.0036  0.0021  -0.0228 260 SER B CA  
2875 C C   . SER B 169 ? 0.2582 0.1754 0.1371 -0.0045 -0.0072 -0.0309 260 SER B C   
2876 O O   . SER B 169 ? 0.2602 0.1586 0.1269 -0.0038 -0.0059 -0.0346 260 SER B O   
2877 C CB  . SER B 169 ? 0.2162 0.1396 0.0915 0.0151  0.0091  -0.0210 260 SER B CB  
2878 O OG  . SER B 169 ? 0.2346 0.1564 0.0947 0.0156  0.0037  -0.0234 260 SER B OG  
2879 N N   . SER B 170 ? 0.2294 0.1553 0.1091 -0.0123 -0.0167 -0.0331 261 SER B N   
2880 C CA  . SER B 170 ? 0.2446 0.1624 0.1151 -0.0239 -0.0272 -0.0393 261 SER B CA  
2881 C C   . SER B 170 ? 0.2138 0.1422 0.1042 -0.0346 -0.0304 -0.0381 261 SER B C   
2882 O O   . SER B 170 ? 0.2268 0.1483 0.1112 -0.0462 -0.0385 -0.0419 261 SER B O   
2883 C CB  . SER B 170 ? 0.2706 0.1987 0.1350 -0.0277 -0.0368 -0.0410 261 SER B CB  
2884 O OG  . SER B 170 ? 0.3086 0.2231 0.1490 -0.0190 -0.0355 -0.0433 261 SER B OG  
2885 N N   . GLY B 171 ? 0.1862 0.1304 0.0985 -0.0318 -0.0246 -0.0325 262 GLY B N   
2886 C CA  . GLY B 171 ? 0.1992 0.1559 0.1298 -0.0402 -0.0269 -0.0306 262 GLY B CA  
2887 C C   . GLY B 171 ? 0.2443 0.2268 0.1901 -0.0432 -0.0317 -0.0276 262 GLY B C   
2888 O O   . GLY B 171 ? 0.2169 0.2123 0.1773 -0.0492 -0.0331 -0.0255 262 GLY B O   
2889 N N   . ASN B 172 ? 0.1791 0.1696 0.1208 -0.0379 -0.0336 -0.0268 263 ASN B N   
2890 C CA  . ASN B 172 ? 0.1654 0.1804 0.1199 -0.0377 -0.0378 -0.0234 263 ASN B CA  
2891 C C   . ASN B 172 ? 0.1242 0.1481 0.0940 -0.0309 -0.0313 -0.0187 263 ASN B C   
2892 O O   . ASN B 172 ? 0.1381 0.1510 0.1069 -0.0248 -0.0243 -0.0172 263 ASN B O   
2893 C CB  . ASN B 172 ? 0.1704 0.1893 0.1141 -0.0319 -0.0413 -0.0233 263 ASN B CB  
2894 C CG  . ASN B 172 ? 0.2593 0.2678 0.1846 -0.0385 -0.0491 -0.0287 263 ASN B CG  
2895 O OD1 . ASN B 172 ? 0.2693 0.2817 0.1964 -0.0504 -0.0566 -0.0310 263 ASN B OD1 
2896 N ND2 . ASN B 172 ? 0.2751 0.2692 0.1816 -0.0310 -0.0473 -0.0305 263 ASN B ND2 
2897 N N   . LEU B 173 ? 0.1136 0.1581 0.0966 -0.0318 -0.0340 -0.0160 264 LEU B N   
2898 C CA  . LEU B 173 ? 0.1070 0.1571 0.1013 -0.0258 -0.0289 -0.0125 264 LEU B CA  
2899 C C   . LEU B 173 ? 0.1151 0.1611 0.1051 -0.0150 -0.0257 -0.0098 264 LEU B C   
2900 O O   . LEU B 173 ? 0.1362 0.1899 0.1214 -0.0101 -0.0290 -0.0084 264 LEU B O   
2901 C CB  . LEU B 173 ? 0.1516 0.2253 0.1586 -0.0277 -0.0320 -0.0100 264 LEU B CB  
2902 C CG  . LEU B 173 ? 0.1920 0.2706 0.2069 -0.0197 -0.0273 -0.0070 264 LEU B CG  
2903 C CD1 . LEU B 173 ? 0.1310 0.1979 0.1494 -0.0235 -0.0229 -0.0079 264 LEU B CD1 
2904 C CD2 . LEU B 173 ? 0.2318 0.3372 0.2566 -0.0172 -0.0297 -0.0036 264 LEU B CD2 
2905 N N   . LEU B 174 ? 0.0997 0.1335 0.0911 -0.0117 -0.0198 -0.0083 265 LEU B N   
2906 C CA  . LEU B 174 ? 0.0973 0.1256 0.0852 -0.0033 -0.0172 -0.0047 265 LEU B CA  
2907 C C   . LEU B 174 ? 0.1267 0.1558 0.1210 0.0003  -0.0158 -0.0029 265 LEU B C   
2908 O O   . LEU B 174 ? 0.1225 0.1475 0.1118 0.0079  -0.0155 -0.0002 265 LEU B O   
2909 C CB  . LEU B 174 ? 0.1018 0.1144 0.0840 -0.0029 -0.0120 -0.0031 265 LEU B CB  
2910 C CG  . LEU B 174 ? 0.1354 0.1434 0.1066 -0.0035 -0.0120 -0.0048 265 LEU B CG  
2911 C CD1 . LEU B 174 ? 0.1163 0.1128 0.0841 -0.0016 -0.0051 -0.0015 265 LEU B CD1 
2912 C CD2 . LEU B 174 ? 0.1633 0.1771 0.1251 0.0012  -0.0165 -0.0043 265 LEU B CD2 
2913 N N   . GLY B 175 ? 0.0829 0.1145 0.0853 -0.0043 -0.0151 -0.0044 266 GLY B N   
2914 C CA  . GLY B 175 ? 0.0805 0.1096 0.0857 -0.0008 -0.0138 -0.0035 266 GLY B CA  
2915 C C   . GLY B 175 ? 0.1397 0.1748 0.1530 -0.0066 -0.0134 -0.0052 266 GLY B C   
2916 O O   . GLY B 175 ? 0.1174 0.1524 0.1334 -0.0139 -0.0133 -0.0066 266 GLY B O   
2917 N N   . ARG B 176 ? 0.0786 0.1169 0.0935 -0.0024 -0.0130 -0.0048 267 ARG B N   
2918 C CA  . ARG B 176 ? 0.0645 0.1091 0.0859 -0.0071 -0.0122 -0.0055 267 ARG B CA  
2919 C C   . ARG B 176 ? 0.1265 0.1645 0.1443 -0.0013 -0.0111 -0.0055 267 ARG B C   
2920 O O   . ARG B 176 ? 0.0766 0.1125 0.0876 0.0080  -0.0113 -0.0051 267 ARG B O   
2921 C CB  . ARG B 176 ? 0.0827 0.1491 0.1107 -0.0094 -0.0136 -0.0044 267 ARG B CB  
2922 C CG  . ARG B 176 ? 0.0567 0.1296 0.0909 -0.0151 -0.0122 -0.0038 267 ARG B CG  
2923 C CD  . ARG B 176 ? 0.1722 0.2705 0.2143 -0.0173 -0.0132 -0.0008 267 ARG B CD  
2924 N NE  . ARG B 176 ? 0.1312 0.2374 0.1759 -0.0254 -0.0174 -0.0008 267 ARG B NE  
2925 C CZ  . ARG B 176 ? 0.1599 0.2818 0.2060 -0.0221 -0.0206 0.0007  267 ARG B CZ  
2926 N NH1 . ARG B 176 ? 0.0865 0.2186 0.1321 -0.0092 -0.0192 0.0028  267 ARG B NH1 
2927 N NH2 . ARG B 176 ? 0.1198 0.2426 0.1648 -0.0304 -0.0249 -0.0000 267 ARG B NH2 
2928 N N   . ASP B 177 ? 0.0852 0.1181 0.1054 -0.0060 -0.0103 -0.0062 268 ASP B N   
2929 C CA  . ASP B 177 ? 0.0734 0.0995 0.0884 -0.0017 -0.0101 -0.0069 268 ASP B CA  
2930 C C   . ASP B 177 ? 0.0891 0.1224 0.1098 -0.0069 -0.0089 -0.0065 268 ASP B C   
2931 O O   . ASP B 177 ? 0.0791 0.1180 0.1066 -0.0143 -0.0084 -0.0058 268 ASP B O   
2932 C CB  . ASP B 177 ? 0.0770 0.0827 0.0858 -0.0028 -0.0119 -0.0077 268 ASP B CB  
2933 C CG  . ASP B 177 ? 0.1367 0.1297 0.1335 0.0037  -0.0135 -0.0093 268 ASP B CG  
2934 O OD1 . ASP B 177 ? 0.1383 0.1129 0.1273 0.0028  -0.0162 -0.0096 268 ASP B OD1 
2935 O OD2 . ASP B 177 ? 0.1475 0.1479 0.1413 0.0096  -0.0122 -0.0101 268 ASP B OD2 
2936 N N   . SER B 178 ? 0.1042 0.1352 0.1197 -0.0028 -0.0084 -0.0070 269 SER B N   
2937 C CA  . SER B 178 ? 0.0924 0.1306 0.1121 -0.0070 -0.0069 -0.0057 269 SER B CA  
2938 C C   . SER B 178 ? 0.0844 0.1137 0.0945 -0.0020 -0.0074 -0.0069 269 SER B C   
2939 O O   . SER B 178 ? 0.0857 0.1043 0.0846 0.0057  -0.0088 -0.0092 269 SER B O   
2940 C CB  . SER B 178 ? 0.0938 0.1537 0.1202 -0.0075 -0.0042 -0.0026 269 SER B CB  
2941 O OG  . SER B 178 ? 0.0954 0.1649 0.1170 0.0034  -0.0023 -0.0018 269 SER B OG  
2942 N N   . PHE B 179 ? 0.0716 0.1029 0.0837 -0.0061 -0.0066 -0.0056 270 PHE B N   
2943 C CA  . PHE B 179 ? 0.0844 0.1074 0.0864 -0.0023 -0.0078 -0.0067 270 PHE B CA  
2944 C C   . PHE B 179 ? 0.1033 0.1362 0.1089 -0.0056 -0.0049 -0.0032 270 PHE B C   
2945 O O   . PHE B 179 ? 0.0723 0.1095 0.0874 -0.0134 -0.0039 -0.0007 270 PHE B O   
2946 C CB  . PHE B 179 ? 0.0857 0.0911 0.0839 -0.0059 -0.0132 -0.0090 270 PHE B CB  
2947 C CG  . PHE B 179 ? 0.0747 0.0812 0.0845 -0.0146 -0.0139 -0.0068 270 PHE B CG  
2948 C CD1 . PHE B 179 ? 0.0749 0.0813 0.0917 -0.0179 -0.0136 -0.0065 270 PHE B CD1 
2949 C CD2 . PHE B 179 ? 0.0788 0.0856 0.0904 -0.0177 -0.0147 -0.0049 270 PHE B CD2 
2950 C CE1 . PHE B 179 ? 0.0613 0.0681 0.0863 -0.0232 -0.0132 -0.0044 270 PHE B CE1 
2951 C CE2 . PHE B 179 ? 0.0730 0.0804 0.0936 -0.0229 -0.0147 -0.0026 270 PHE B CE2 
2952 C CZ  . PHE B 179 ? 0.0609 0.0682 0.0878 -0.0252 -0.0137 -0.0025 270 PHE B CZ  
2953 N N   . GLU B 180 ? 0.1067 0.1412 0.1027 0.0010  -0.0032 -0.0028 271 GLU B N   
2954 C CA  . GLU B 180 ? 0.0886 0.1297 0.0854 -0.0018 -0.0006 0.0012  271 GLU B CA  
2955 C C   . GLU B 180 ? 0.0984 0.1261 0.0937 -0.0067 -0.0050 0.0005  271 GLU B C   
2956 O O   . GLU B 180 ? 0.0931 0.1080 0.0838 -0.0062 -0.0104 -0.0032 271 GLU B O   
2957 C CB  . GLU B 180 ? 0.1017 0.1484 0.0862 0.0084  0.0030  0.0021  271 GLU B CB  
2958 C CG  . GLU B 180 ? 0.1604 0.2171 0.1451 0.0063  0.0074  0.0080  271 GLU B CG  
2959 C CD  . GLU B 180 ? 0.2556 0.3216 0.2281 0.0181  0.0126  0.0099  271 GLU B CD  
2960 O OE1 . GLU B 180 ? 0.2245 0.2936 0.1911 0.0283  0.0142  0.0075  271 GLU B OE1 
2961 O OE2 . GLU B 180 ? 0.2234 0.2928 0.1906 0.0184  0.0156  0.0142  271 GLU B OE2 
2962 N N   . VAL B 181 ? 0.1073 0.1387 0.1064 -0.0115 -0.0030 0.0049  272 VAL B N   
2963 C CA  . VAL B 181 ? 0.0889 0.1107 0.0868 -0.0141 -0.0067 0.0055  272 VAL B CA  
2964 C C   . VAL B 181 ? 0.1629 0.1870 0.1535 -0.0123 -0.0043 0.0097  272 VAL B C   
2965 O O   . VAL B 181 ? 0.1370 0.1705 0.1296 -0.0141 0.0012  0.0143  272 VAL B O   
2966 C CB  . VAL B 181 ? 0.1344 0.1537 0.1430 -0.0208 -0.0067 0.0072  272 VAL B CB  
2967 C CG1 . VAL B 181 ? 0.0928 0.1054 0.1005 -0.0210 -0.0100 0.0090  272 VAL B CG1 
2968 C CG2 . VAL B 181 ? 0.1488 0.1662 0.1633 -0.0220 -0.0085 0.0036  272 VAL B CG2 
2969 N N   . ARG B 182 ? 0.1154 0.1317 0.0973 -0.0094 -0.0090 0.0088  273 ARG B N   
2970 C CA  . ARG B 182 ? 0.1185 0.1349 0.0931 -0.0079 -0.0077 0.0135  273 ARG B CA  
2971 C C   . ARG B 182 ? 0.1522 0.1622 0.1299 -0.0102 -0.0130 0.0147  273 ARG B C   
2972 O O   . ARG B 182 ? 0.1487 0.1544 0.1254 -0.0098 -0.0201 0.0111  273 ARG B O   
2973 C CB  . ARG B 182 ? 0.1308 0.1457 0.0881 0.0003  -0.0086 0.0117  273 ARG B CB  
2974 C CG  . ARG B 182 ? 0.1715 0.1855 0.1188 0.0027  -0.0081 0.0167  273 ARG B CG  
2975 C CD  . ARG B 182 ? 0.1690 0.1804 0.0959 0.0120  -0.0084 0.0143  273 ARG B CD  
2976 N NE  . ARG B 182 ? 0.2361 0.2446 0.1508 0.0151  -0.0098 0.0183  273 ARG B NE  
2977 C CZ  . ARG B 182 ? 0.3469 0.3625 0.2597 0.0156  -0.0024 0.0263  273 ARG B CZ  
2978 N NH1 . ARG B 182 ? 0.4138 0.4409 0.3378 0.0116  0.0063  0.0312  273 ARG B NH1 
2979 N NH2 . ARG B 182 ? 0.3780 0.3895 0.2777 0.0192  -0.0042 0.0300  273 ARG B NH2 
2980 N N   . VAL B 183 ? 0.1282 0.1375 0.1093 -0.0126 -0.0099 0.0204  274 VAL B N   
2981 C CA  . VAL B 183 ? 0.1598 0.1649 0.1427 -0.0118 -0.0140 0.0230  274 VAL B CA  
2982 C C   . VAL B 183 ? 0.1751 0.1789 0.1453 -0.0073 -0.0147 0.0272  274 VAL B C   
2983 O O   . VAL B 183 ? 0.1383 0.1417 0.1030 -0.0076 -0.0086 0.0320  274 VAL B O   
2984 C CB  . VAL B 183 ? 0.1136 0.1141 0.1044 -0.0149 -0.0101 0.0265  274 VAL B CB  
2985 C CG1 . VAL B 183 ? 0.1150 0.1139 0.1094 -0.0114 -0.0142 0.0287  274 VAL B CG1 
2986 C CG2 . VAL B 183 ? 0.1025 0.1042 0.1022 -0.0195 -0.0079 0.0226  274 VAL B CG2 
2987 N N   . CYS B 184 ? 0.1377 0.1414 0.1027 -0.0041 -0.0224 0.0258  275 CYS B N   
2988 C CA  . CYS B 184 ? 0.1774 0.1798 0.1271 0.0011  -0.0246 0.0284  275 CYS B CA  
2989 C C   . CYS B 184 ? 0.1871 0.1911 0.1366 0.0028  -0.0343 0.0291  275 CYS B C   
2990 O O   . CYS B 184 ? 0.1499 0.1579 0.1116 -0.0003 -0.0394 0.0272  275 CYS B O   
2991 C CB  . CYS B 184 ? 0.2035 0.2049 0.1392 0.0043  -0.0247 0.0234  275 CYS B CB  
2992 S SG  . CYS B 184 ? 0.2076 0.2047 0.1436 0.0023  -0.0332 0.0137  275 CYS B SG  
2993 N N   . ALA B 185 ? 0.2276 0.2305 0.1631 0.0079  -0.0370 0.0325  276 ALA B N   
2994 C CA  . ALA B 185 ? 0.2496 0.2569 0.1849 0.0098  -0.0472 0.0344  276 ALA B CA  
2995 C C   . ALA B 185 ? 0.2228 0.2309 0.1546 0.0063  -0.0585 0.0273  276 ALA B C   
2996 O O   . ALA B 185 ? 0.2025 0.2188 0.1437 0.0033  -0.0676 0.0282  276 ALA B O   
2997 C CB  . ALA B 185 ? 0.2851 0.2903 0.2042 0.0167  -0.0473 0.0404  276 ALA B CB  
2998 N N   . CYS B 186 ? 0.2037 0.2031 0.1211 0.0066  -0.0584 0.0207  277 CYS B N   
2999 C CA  A CYS B 186 ? 0.2074 0.2002 0.1142 0.0035  -0.0700 0.0133  277 CYS B CA  
3000 C CA  B CYS B 186 ? 0.2358 0.2284 0.1423 0.0036  -0.0699 0.0133  277 CYS B CA  
3001 C C   . CYS B 186 ? 0.2042 0.1882 0.1098 0.0014  -0.0664 0.0063  277 CYS B C   
3002 O O   . CYS B 186 ? 0.2565 0.2304 0.1430 0.0070  -0.0637 0.0018  277 CYS B O   
3003 C CB  A CYS B 186 ? 0.2874 0.2726 0.1679 0.0094  -0.0757 0.0118  277 CYS B CB  
3004 C CB  B CYS B 186 ? 0.2888 0.2733 0.1684 0.0098  -0.0750 0.0115  277 CYS B CB  
3005 S SG  A CYS B 186 ? 0.3135 0.2901 0.1822 0.0033  -0.0924 0.0037  277 CYS B SG  
3006 S SG  B CYS B 186 ? 0.3215 0.3151 0.1977 0.0141  -0.0801 0.0200  277 CYS B SG  
3007 N N   . PRO B 187 ? 0.2767 0.2053 0.1523 -0.0136 -0.0430 0.0070  278 PRO B N   
3008 C CA  . PRO B 187 ? 0.2323 0.1642 0.1117 -0.0125 -0.0371 0.0018  278 PRO B CA  
3009 C C   . PRO B 187 ? 0.2162 0.1412 0.0786 0.0025  -0.0394 -0.0126 278 PRO B C   
3010 O O   . PRO B 187 ? 0.2332 0.1655 0.0878 0.0111  -0.0315 -0.0118 278 PRO B O   
3011 C CB  . PRO B 187 ? 0.2080 0.1271 0.1128 -0.0287 -0.0396 -0.0033 278 PRO B CB  
3012 C CG  . PRO B 187 ? 0.2792 0.1943 0.2017 -0.0337 -0.0419 -0.0010 278 PRO B CG  
3013 C CD  . PRO B 187 ? 0.2760 0.1938 0.1776 -0.0291 -0.0460 0.0082  278 PRO B CD  
3014 N N   . GLY B 188 ? 0.2447 0.1626 0.1120 0.0051  -0.0456 -0.0237 279 GLY B N   
3015 C CA  . GLY B 188 ? 0.2837 0.1989 0.1435 0.0147  -0.0434 -0.0360 279 GLY B CA  
3016 C C   . GLY B 188 ? 0.3162 0.2405 0.1474 0.0272  -0.0378 -0.0339 279 GLY B C   
3017 O O   . GLY B 188 ? 0.3072 0.2295 0.1299 0.0362  -0.0296 -0.0381 279 GLY B O   
3018 N N   . ARG B 189 ? 0.2650 0.2004 0.0830 0.0285  -0.0398 -0.0259 280 ARG B N   
3019 C CA  . ARG B 189 ? 0.3135 0.2600 0.1085 0.0382  -0.0312 -0.0224 280 ARG B CA  
3020 C C   . ARG B 189 ? 0.2998 0.2584 0.0959 0.0419  -0.0177 -0.0108 280 ARG B C   
3021 O O   . ARG B 189 ? 0.3012 0.2653 0.0857 0.0522  -0.0071 -0.0128 280 ARG B O   
3022 C CB  . ARG B 189 ? 0.3425 0.2985 0.1247 0.0372  -0.0352 -0.0133 280 ARG B CB  
3023 N N   . ASP B 190 ? 0.2591 0.2239 0.0715 0.0328  -0.0167 0.0014  281 ASP B N   
3024 C CA  . ASP B 190 ? 0.3111 0.2954 0.1311 0.0335  -0.0033 0.0137  281 ASP B CA  
3025 C C   . ASP B 190 ? 0.2861 0.2700 0.1102 0.0422  0.0008  0.0077  281 ASP B C   
3026 O O   . ASP B 190 ? 0.2532 0.2552 0.0783 0.0518  0.0131  0.0127  281 ASP B O   
3027 C CB  . ASP B 190 ? 0.2279 0.2206 0.0661 0.0181  -0.0020 0.0279  281 ASP B CB  
3028 C CG  . ASP B 190 ? 0.3708 0.3670 0.2041 0.0128  0.0014  0.0387  281 ASP B CG  
3029 O OD1 . ASP B 190 ? 0.3626 0.3577 0.1771 0.0212  0.0015  0.0364  281 ASP B OD1 
3030 O OD2 . ASP B 190 ? 0.3502 0.3463 0.1975 0.0010  0.0055  0.0487  281 ASP B OD2 
3031 N N   . ARG B 191 ? 0.2357 0.1999 0.0702 0.0376  -0.0084 -0.0028 282 ARG B N   
3032 C CA  . ARG B 191 ? 0.2361 0.1959 0.0783 0.0461  -0.0039 -0.0080 282 ARG B CA  
3033 C C   . ARG B 191 ? 0.2677 0.2200 0.0878 0.0647  0.0039  -0.0187 282 ARG B C   
3034 O O   . ARG B 191 ? 0.2742 0.2368 0.0997 0.0771  0.0153  -0.0150 282 ARG B O   
3035 C CB  . ARG B 191 ? 0.2248 0.1594 0.0779 0.0373  -0.0135 -0.0182 282 ARG B CB  
3036 C CG  . ARG B 191 ? 0.2330 0.1570 0.0897 0.0483  -0.0077 -0.0229 282 ARG B CG  
3037 C CD  . ARG B 191 ? 0.2340 0.1322 0.1011 0.0385  -0.0144 -0.0307 282 ARG B CD  
3038 N NE  . ARG B 191 ? 0.2427 0.1227 0.1063 0.0524  -0.0071 -0.0368 282 ARG B NE  
3039 C CZ  . ARG B 191 ? 0.3005 0.1665 0.1797 0.0434  -0.0083 -0.0424 282 ARG B CZ  
3040 N NH1 . ARG B 191 ? 0.2121 0.0878 0.1144 0.0238  -0.0138 -0.0430 282 ARG B NH1 
3041 N NH2 . ARG B 191 ? 0.2558 0.1122 0.1370 0.0533  0.0003  -0.0439 282 ARG B NH2 
3042 N N   . ARG B 192 ? 0.3169 0.2549 0.1199 0.0648  -0.0014 -0.0310 283 ARG B N   
3043 C CA  . ARG B 192 ? 0.3474 0.2802 0.1370 0.0763  0.0070  -0.0411 283 ARG B CA  
3044 C C   . ARG B 192 ? 0.3497 0.3053 0.1306 0.0863  0.0210  -0.0306 283 ARG B C   
3045 O O   . ARG B 192 ? 0.3515 0.3084 0.1311 0.0997  0.0340  -0.0333 283 ARG B O   
3046 C CB  . ARG B 192 ? 0.4167 0.3402 0.1978 0.0685  -0.0023 -0.0529 283 ARG B CB  
3047 C CG  . ARG B 192 ? 0.4573 0.3620 0.2505 0.0626  -0.0064 -0.0679 283 ARG B CG  
3048 C CD  . ARG B 192 ? 0.5635 0.4683 0.3493 0.0543  -0.0137 -0.0787 283 ARG B CD  
3049 N NE  . ARG B 192 ? 0.6116 0.5217 0.4089 0.0435  -0.0271 -0.0740 283 ARG B NE  
3050 C CZ  . ARG B 192 ? 0.5804 0.5015 0.3646 0.0420  -0.0346 -0.0687 283 ARG B CZ  
3051 N NH1 . ARG B 192 ? 0.6006 0.5297 0.3586 0.0487  -0.0298 -0.0671 283 ARG B NH1 
3052 N NH2 . ARG B 192 ? 0.4496 0.3740 0.2479 0.0340  -0.0455 -0.0641 283 ARG B NH2 
3053 N N   . THR B 193 ? 0.3227 0.2961 0.1026 0.0787  0.0200  -0.0178 284 THR B N   
3054 C CA  . THR B 193 ? 0.3342 0.3296 0.1114 0.0840  0.0341  -0.0073 284 THR B CA  
3055 C C   . THR B 193 ? 0.3209 0.3373 0.1181 0.0925  0.0463  0.0021  284 THR B C   
3056 O O   . THR B 193 ? 0.3535 0.3796 0.1504 0.1050  0.0602  0.0017  284 THR B O   
3057 C CB  . THR B 193 ? 0.4142 0.4209 0.1921 0.0712  0.0312  0.0057  284 THR B CB  
3058 O OG1 . THR B 193 ? 0.4095 0.4012 0.1699 0.0662  0.0196  -0.0009 284 THR B OG1 
3059 C CG2 . THR B 193 ? 0.3847 0.4109 0.1607 0.0744  0.0466  0.0151  284 THR B CG2 
3060 N N   . GLU B 194 ? 0.2907 0.3171 0.1078 0.0849  0.0415  0.0111  285 GLU B N   
3061 C CA  . GLU B 194 ? 0.2936 0.3490 0.1359 0.0901  0.0509  0.0226  285 GLU B CA  
3062 C C   . GLU B 194 ? 0.3415 0.3863 0.1902 0.1066  0.0547  0.0155  285 GLU B C   
3063 O O   . GLU B 194 ? 0.3328 0.4018 0.1987 0.1188  0.0661  0.0233  285 GLU B O   
3064 C CB  . GLU B 194 ? 0.2729 0.3423 0.1412 0.0711  0.0421  0.0333  285 GLU B CB  
3065 C CG  . GLU B 194 ? 0.2787 0.3587 0.1484 0.0545  0.0429  0.0417  285 GLU B CG  
3066 C CD  . GLU B 194 ? 0.3210 0.4176 0.2178 0.0349  0.0389  0.0508  285 GLU B CD  
3067 O OE1 . GLU B 194 ? 0.2747 0.3631 0.1741 0.0188  0.0365  0.0530  285 GLU B OE1 
3068 O OE2 . GLU B 194 ? 0.2970 0.4131 0.2129 0.0355  0.0386  0.0553  285 GLU B OE2 
3069 N N   . GLU B 195 ? 0.2955 0.3046 0.1320 0.1079  0.0467  0.0009  286 GLU B N   
3070 C CA  . GLU B 195 ? 0.3128 0.3053 0.1521 0.1247  0.0540  -0.0064 286 GLU B CA  
3071 C C   . GLU B 195 ? 0.4908 0.4802 0.3137 0.1409  0.0699  -0.0145 286 GLU B C   
3072 O O   . GLU B 195 ? 0.3608 0.3535 0.1973 0.1560  0.0815  -0.0118 286 GLU B O   
3073 C CB  . GLU B 195 ? 0.3160 0.2689 0.1473 0.1192  0.0435  -0.0213 286 GLU B CB  
3074 C CG  . GLU B 195 ? 0.2849 0.2394 0.1380 0.1048  0.0311  -0.0124 286 GLU B CG  
3075 C CD  . GLU B 195 ? 0.3686 0.2839 0.2180 0.1012  0.0249  -0.0261 286 GLU B CD  
3076 O OE1 . GLU B 195 ? 0.3871 0.2765 0.2220 0.1050  0.0278  -0.0425 286 GLU B OE1 
3077 O OE2 . GLU B 195 ? 0.2917 0.2049 0.1564 0.0904  0.0171  -0.0196 286 GLU B OE2 
3078 N N   . GLU B 196 ? 0.3625 0.3465 0.1646 0.1324  0.0673  -0.0217 287 GLU B N   
3079 C CA  . GLU B 196 ? 0.4453 0.4283 0.2368 0.1402  0.0803  -0.0281 287 GLU B CA  
3080 C C   . GLU B 196 ? 0.4198 0.4377 0.2261 0.1478  0.0944  -0.0132 287 GLU B C   
3081 O O   . GLU B 196 ? 0.4675 0.4883 0.2794 0.1603  0.1090  -0.0151 287 GLU B O   
3082 C CB  . GLU B 196 ? 0.5324 0.5032 0.2969 0.1285  0.0734  -0.0389 287 GLU B CB  
3083 C CG  . GLU B 196 ? 0.6941 0.6620 0.4426 0.1342  0.0875  -0.0483 287 GLU B CG  
3084 C CD  . GLU B 196 ? 0.8515 0.7977 0.6042 0.1423  0.0962  -0.0626 287 GLU B CD  
3085 O OE1 . GLU B 196 ? 0.9046 0.8303 0.6629 0.1375  0.0870  -0.0709 287 GLU B OE1 
3086 O OE2 . GLU B 196 ? 0.9436 0.8931 0.6964 0.1520  0.1134  -0.0655 287 GLU B OE2 
3087 N N   . ASN B 197 ? 0.4110 0.4558 0.2274 0.1381  0.0907  0.0013  288 ASN B N   
3088 C CA  . ASN B 197 ? 0.4281 0.5093 0.2658 0.1414  0.1030  0.0150  288 ASN B CA  
3089 C C   . ASN B 197 ? 0.4406 0.5395 0.3082 0.1569  0.1100  0.0220  288 ASN B C   
3090 O O   . ASN B 197 ? 0.4113 0.5275 0.2929 0.1674  0.1234  0.0255  288 ASN B O   
3091 C CB  . ASN B 197 ? 0.4105 0.5150 0.2598 0.1236  0.0965  0.0283  288 ASN B CB  
3092 C CG  . ASN B 197 ? 0.5686 0.6581 0.3929 0.1101  0.0919  0.0253  288 ASN B CG  
3093 O OD1 . ASN B 197 ? 0.6240 0.6974 0.4237 0.1143  0.0966  0.0160  288 ASN B OD1 
3094 N ND2 . ASN B 197 ? 0.6195 0.7142 0.4513 0.0931  0.0831  0.0338  288 ASN B ND2 
3095 N N   . LEU B 198 ? 0.3361 0.4310 0.2150 0.1584  0.1009  0.0247  289 LEU B N   
3096 C CA  . LEU B 198 ? 0.3394 0.4494 0.2475 0.1737  0.1048  0.0336  289 LEU B CA  
3097 C C   . LEU B 198 ? 0.4257 0.5072 0.3276 0.1900  0.1151  0.0235  289 LEU B C   
3098 O O   . LEU B 198 ? 0.4104 0.5096 0.3351 0.2035  0.1245  0.0317  289 LEU B O   
3099 C CB  . LEU B 198 ? 0.3317 0.4345 0.2500 0.1673  0.0897  0.0379  289 LEU B CB  
3100 C CG  . LEU B 198 ? 0.3864 0.5006 0.3323 0.1828  0.0900  0.0492  289 LEU B CG  
3101 C CD1 . LEU B 198 ? 0.3501 0.5223 0.3303 0.1857  0.0932  0.0676  289 LEU B CD1 
3102 C CD2 . LEU B 198 ? 0.3931 0.4864 0.3397 0.1705  0.0727  0.0504  289 LEU B CD2 
3103 N N   . ARG B 199 ? 0.4432 0.4816 0.3164 0.1866  0.1130  0.0054  290 ARG B N   
3104 C CA  . ARG B 199 ? 0.5224 0.5332 0.3907 0.1969  0.1239  -0.0061 290 ARG B CA  
3105 C C   . ARG B 199 ? 0.6257 0.6527 0.4947 0.2037  0.1405  -0.0069 290 ARG B C   
3106 O O   . ARG B 199 ? 0.6865 0.7109 0.5692 0.2172  0.1534  -0.0071 290 ARG B O   
3107 C CB  . ARG B 199 ? 0.5351 0.5037 0.3756 0.1858  0.1172  -0.0270 290 ARG B CB  
3108 N N   . LYS B 200 ? 0.6382 0.6816 0.4936 0.1937  0.1409  -0.0065 291 LYS B N   
3109 C CA  . LYS B 200 ? 0.6888 0.7474 0.5434 0.1975  0.1572  -0.0075 291 LYS B CA  
3110 C C   . LYS B 200 ? 0.7479 0.8494 0.6388 0.2056  0.1649  0.0102  291 LYS B C   
3111 O O   . LYS B 200 ? 0.7868 0.9041 0.6810 0.2075  0.1792  0.0101  291 LYS B O   
3112 C CB  . LYS B 200 ? 0.6686 0.7266 0.4939 0.1820  0.1543  -0.0123 291 LYS B CB  
3113 N N   . LYS B 201 ? 0.7565 0.8788 0.6753 0.2089  0.1557  0.0247  292 LYS B N   
3114 C CA  . LYS B 201 ? 0.7406 0.9093 0.6967 0.2135  0.1596  0.0412  292 LYS B CA  
3115 C C   . LYS B 201 ? 0.7768 0.9481 0.7584 0.2334  0.1672  0.0462  292 LYS B C   
3116 O O   . LYS B 201 ? 0.8356 0.9708 0.8072 0.2424  0.1687  0.0382  292 LYS B O   
3117 C CB  . LYS B 201 ? 0.6437 0.8418 0.6172 0.2014  0.1435  0.0551  292 LYS B CB  
# 
